data_9KYR
# 
_entry.id   9KYR 
# 
_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   9KYR         pdb_00009kyr 10.2210/pdb9kyr/pdb 
WWPDB D_1300054538 ?            ?                   
# 
_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                        9KYR 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 zhuzhimin@sinap.ac.cn Zhimin Zhu  ? 'principal investigator/group leader' 0009-0004-3840-9685 
3 wangww@sari.ac.cn     Weiwei Wang ? 'principal investigator/group leader' 0000-0002-0699-3598 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhu, Z.M.'   1 ? 
'Wang, W.W.'  2 ? 
'Yu, F.'      3 ? 
'Li, M.J.'    4 ? 
'Xu, Q.'      5 ? 
'Zhou, H.'    6 ? 
'Huang, L.Q.' 7 ? 
'Wang, Q.S.'  8 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Struct.Biol. 
_citation.journal_id_ASTM           JSBIEM 
_citation.journal_id_CSD            0803 
_citation.journal_id_ISSN           1095-8657 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            217 
_citation.language                  ? 
_citation.page_first                108199 
_citation.page_last                 108199 
_citation.title                     
'Mechanistic insights into cyclodextrins as substrates and inhibitors of GH57 family amylopullulanase from Aquifex aeolicus.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jsb.2025.108199 
_citation.pdbx_database_id_PubMed   40120836 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhu, Z.'   1 ? 
primary 'Li, M.'    2 ? 
primary 'Xu, Q.'    3 ? 
primary 'Huang, L.' 4 ? 
primary 'Zhou, H.'  5 ? 
primary 'Wang, W.'  6 ? 
primary 'Wang, Q.'  7 ? 
primary 'Yu, F.'    8 ? 
# 
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 'Glycoside hydrolase family 57 N-terminal domain-containing protein' 57252.250 4   ? D352N ? ? 
2 branched    man 'Cyclooctakis-(1-4)-(alpha-D-glucopyranose)'                         1315.142  4   ? ?     ? ? 
3 non-polymer syn GLYCEROL                                                             92.094    6   ? ?     ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                              106.120   4   ? ?     ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                       62.068    7   ? ?     ? ? 
6 water       nat water                                                                18.015    645 ? ?     ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLNGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLNGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_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 GLYCEROL                GOL 
4 'DI(HYDROXYETHYL)ETHER' PEG 
5 1,2-ETHANEDIOL          EDO 
6 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   LYS n 
1 3   LYS n 
1 4   LEU n 
1 5   PHE n 
1 6   LEU n 
1 7   VAL n 
1 8   PHE n 
1 9   TRP n 
1 10  TRP n 
1 11  HIS n 
1 12  MET n 
1 13  HIS n 
1 14  GLN n 
1 15  PRO n 
1 16  LEU n 
1 17  TYR n 
1 18  ARG n 
1 19  GLU n 
1 20  PRO n 
1 21  TYR n 
1 22  THR n 
1 23  GLY n 
1 24  GLU n 
1 25  TYR n 
1 26  LEU n 
1 27  LEU n 
1 28  PRO n 
1 29  TRP n 
1 30  THR n 
1 31  PHE n 
1 32  PHE n 
1 33  HIS n 
1 34  ALA n 
1 35  VAL n 
1 36  LYS n 
1 37  ASP n 
1 38  TYR n 
1 39  TYR n 
1 40  ASP n 
1 41  MET n 
1 42  PRO n 
1 43  ALA n 
1 44  TYR n 
1 45  LEU n 
1 46  LYS n 
1 47  ASP n 
1 48  PHE n 
1 49  GLU n 
1 50  ILE n 
1 51  LYS n 
1 52  LEU n 
1 53  ASN n 
1 54  PHE n 
1 55  ASN n 
1 56  LEU n 
1 57  THR n 
1 58  PRO n 
1 59  VAL n 
1 60  LEU n 
1 61  ILE n 
1 62  ASP n 
1 63  GLN n 
1 64  ILE n 
1 65  GLN n 
1 66  GLU n 
1 67  TYR n 
1 68  ALA n 
1 69  GLN n 
1 70  GLY n 
1 71  LYS n 
1 72  ALA n 
1 73  LYS n 
1 74  ASP n 
1 75  VAL n 
1 76  PHE n 
1 77  LEU n 
1 78  GLU n 
1 79  ALA n 
1 80  ILE n 
1 81  ARG n 
1 82  LYS n 
1 83  ASP n 
1 84  PRO n 
1 85  ASP n 
1 86  ASP n 
1 87  LEU n 
1 88  GLU n 
1 89  LYS n 
1 90  GLU n 
1 91  GLU n 
1 92  VAL n 
1 93  GLU n 
1 94  LYS n 
1 95  LEU n 
1 96  ILE n 
1 97  GLU n 
1 98  PHE n 
1 99  THR n 
1 100 LYS n 
1 101 LEU n 
1 102 ASN n 
1 103 TYR n 
1 104 GLU n 
1 105 LYS n 
1 106 PRO n 
1 107 ILE n 
1 108 TYR n 
1 109 ARG n 
1 110 PHE n 
1 111 GLU n 
1 112 ARG n 
1 113 ILE n 
1 114 ARG n 
1 115 GLU n 
1 116 LEU n 
1 117 MET n 
1 118 ASN n 
1 119 LYS n 
1 120 GLU n 
1 121 LYS n 
1 122 LEU n 
1 123 ASN n 
1 124 ARG n 
1 125 GLU n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 ASP n 
1 130 LEU n 
1 131 GLN n 
1 132 THR n 
1 133 LEU n 
1 134 ASN n 
1 135 LEU n 
1 136 LEU n 
1 137 ALA n 
1 138 TRP n 
1 139 CYS n 
1 140 GLY n 
1 141 ARG n 
1 142 THR n 
1 143 LEU n 
1 144 ARG n 
1 145 LYS n 
1 146 ASP n 
1 147 LEU n 
1 148 LYS n 
1 149 ASP n 
1 150 LEU n 
1 151 LEU n 
1 152 ASN n 
1 153 LYS n 
1 154 GLY n 
1 155 ARG n 
1 156 ASN n 
1 157 TYR n 
1 158 THR n 
1 159 GLN n 
1 160 GLU n 
1 161 GLU n 
1 162 LYS n 
1 163 GLU n 
1 164 TYR n 
1 165 VAL n 
1 166 LEU n 
1 167 ASN n 
1 168 LYS n 
1 169 TYR n 
1 170 PHE n 
1 171 GLU n 
1 172 ILE n 
1 173 ILE n 
1 174 LYS n 
1 175 LYS n 
1 176 THR n 
1 177 LEU n 
1 178 SER n 
1 179 ILE n 
1 180 TYR n 
1 181 ARG n 
1 182 GLU n 
1 183 ILE n 
1 184 LYS n 
1 185 GLU n 
1 186 GLU n 
1 187 GLY n 
1 188 LYS n 
1 189 GLY n 
1 190 SER n 
1 191 VAL n 
1 192 SER n 
1 193 THR n 
1 194 SER n 
1 195 PRO n 
1 196 TYR n 
1 197 TYR n 
1 198 HIS n 
1 199 PRO n 
1 200 LEU n 
1 201 ILE n 
1 202 PRO n 
1 203 ILE n 
1 204 LEU n 
1 205 LEU n 
1 206 ASN n 
1 207 PRO n 
1 208 ASN n 
1 209 CYS n 
1 210 VAL n 
1 211 TYR n 
1 212 GLU n 
1 213 THR n 
1 214 THR n 
1 215 PRO n 
1 216 ASN n 
1 217 VAL n 
1 218 LYS n 
1 219 ILE n 
1 220 PRO n 
1 221 ASP n 
1 222 PHE n 
1 223 ALA n 
1 224 VAL n 
1 225 SER n 
1 226 PHE n 
1 227 ARG n 
1 228 GLU n 
1 229 ASP n 
1 230 ALA n 
1 231 SER n 
1 232 LYS n 
1 233 HIS n 
1 234 VAL n 
1 235 GLU n 
1 236 LEU n 
1 237 ALA n 
1 238 LYS n 
1 239 GLU n 
1 240 LYS n 
1 241 TYR n 
1 242 PHE n 
1 243 GLU n 
1 244 ILE n 
1 245 PHE n 
1 246 GLY n 
1 247 GLU n 
1 248 HIS n 
1 249 PRO n 
1 250 VAL n 
1 251 TYR n 
1 252 MET n 
1 253 TRP n 
1 254 PRO n 
1 255 PRO n 
1 256 GLU n 
1 257 ALA n 
1 258 SER n 
1 259 VAL n 
1 260 SER n 
1 261 ASN n 
1 262 GLU n 
1 263 ALA n 
1 264 LEU n 
1 265 GLU n 
1 266 LEU n 
1 267 TYR n 
1 268 TYR n 
1 269 GLU n 
1 270 LYS n 
1 271 GLY n 
1 272 ILE n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 ALA n 
1 277 THR n 
1 278 ASP n 
1 279 GLU n 
1 280 VAL n 
1 281 ILE n 
1 282 LEU n 
1 283 LYS n 
1 284 ASN n 
1 285 SER n 
1 286 VAL n 
1 287 GLU n 
1 288 ARG n 
1 289 ALA n 
1 290 SER n 
1 291 PRO n 
1 292 TYR n 
1 293 LEU n 
1 294 ARG n 
1 295 TYR n 
1 296 TYR n 
1 297 PHE n 
1 298 ARG n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 SER n 
1 303 VAL n 
1 304 PHE n 
1 305 PHE n 
1 306 ARG n 
1 307 ASP n 
1 308 LYS n 
1 309 THR n 
1 310 LEU n 
1 311 SER n 
1 312 ASP n 
1 313 LEU n 
1 314 ILE n 
1 315 GLY n 
1 316 PHE n 
1 317 SER n 
1 318 TYR n 
1 319 HIS n 
1 320 ALA n 
1 321 TRP n 
1 322 ASN n 
1 323 ALA n 
1 324 GLU n 
1 325 ASP n 
1 326 ALA n 
1 327 VAL n 
1 328 ARG n 
1 329 ASP n 
1 330 PHE n 
1 331 ILE n 
1 332 GLY n 
1 333 ARG n 
1 334 LEU n 
1 335 LYS n 
1 336 LYS n 
1 337 ILE n 
1 338 HIS n 
1 339 GLU n 
1 340 SER n 
1 341 VAL n 
1 342 ASP n 
1 343 PHE n 
1 344 GLN n 
1 345 PRO n 
1 346 VAL n 
1 347 VAL n 
1 348 PHE n 
1 349 VAL n 
1 350 VAL n 
1 351 LEU n 
1 352 ASN n 
1 353 GLY n 
1 354 GLU n 
1 355 ASN n 
1 356 CYS n 
1 357 TRP n 
1 358 GLU n 
1 359 TYR n 
1 360 TYR n 
1 361 GLU n 
1 362 GLU n 
1 363 ASN n 
1 364 GLY n 
1 365 ILE n 
1 366 PRO n 
1 367 PHE n 
1 368 LEU n 
1 369 GLU n 
1 370 LYS n 
1 371 LEU n 
1 372 TYR n 
1 373 SER n 
1 374 THR n 
1 375 LEU n 
1 376 GLU n 
1 377 LYS n 
1 378 GLU n 
1 379 GLU n 
1 380 TRP n 
1 381 ILE n 
1 382 GLU n 
1 383 THR n 
1 384 LEU n 
1 385 THR n 
1 386 LEU n 
1 387 GLU n 
1 388 GLU n 
1 389 ALA n 
1 390 MET n 
1 391 ARG n 
1 392 LYS n 
1 393 GLU n 
1 394 ASP n 
1 395 VAL n 
1 396 LYS n 
1 397 THR n 
1 398 GLU n 
1 399 VAL n 
1 400 ILE n 
1 401 GLU n 
1 402 SER n 
1 403 VAL n 
1 404 LYS n 
1 405 ALA n 
1 406 GLY n 
1 407 THR n 
1 408 TRP n 
1 409 PHE n 
1 410 ASP n 
1 411 GLY n 
1 412 ASN n 
1 413 PHE n 
1 414 LEU n 
1 415 LYS n 
1 416 TRP n 
1 417 ILE n 
1 418 GLY n 
1 419 ASN n 
1 420 LYS n 
1 421 GLU n 
1 422 LYS n 
1 423 ASN n 
1 424 GLU n 
1 425 TYR n 
1 426 TRP n 
1 427 LYS n 
1 428 ILE n 
1 429 LEU n 
1 430 ILE n 
1 431 GLU n 
1 432 ALA n 
1 433 LYS n 
1 434 LYS n 
1 435 LYS n 
1 436 ALA n 
1 437 LYS n 
1 438 ASN n 
1 439 ASP n 
1 440 TYR n 
1 441 ILE n 
1 442 LEU n 
1 443 VAL n 
1 444 ALA n 
1 445 GLU n 
1 446 GLY n 
1 447 SER n 
1 448 ASP n 
1 449 TRP n 
1 450 PHE n 
1 451 TRP n 
1 452 TRP n 
1 453 GLN n 
1 454 GLY n 
1 455 GLU n 
1 456 GLU n 
1 457 LYS n 
1 458 ALA n 
1 459 PRO n 
1 460 PHE n 
1 461 VAL n 
1 462 GLU n 
1 463 VAL n 
1 464 PHE n 
1 465 ASP n 
1 466 LYS n 
1 467 LEU n 
1 468 PHE n 
1 469 ARG n 
1 470 SER n 
1 471 PHE n 
1 472 VAL n 
1 473 ARG n 
1 474 ARG n 
1 475 ALA n 
1 476 GLN n 
1 477 GLU 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                   477 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 aq_720 
_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      'Aquifex aeolicus VF5' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     224324 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_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=2.0/1,8,8/[a2122h-1a_1-5]/1-1-1-1-1-1-1-1/a1-h4_a4-b1_b4-c1_c4-d1_d4-e1_e4-f1_f4-g1_g4-h1' 
_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 1 GLC C1 O1 8 GLC O4 HO4 sing ? 
2 2 2 GLC C1 O1 1 GLC O4 HO4 sing ? 
3 2 3 GLC C1 O1 2 GLC O4 HO4 sing ? 
4 2 4 GLC C1 O1 3 GLC O4 HO4 sing ? 
5 2 5 GLC C1 O1 4 GLC O4 HO4 sing ? 
6 2 6 GLC C1 O1 5 GLC O4 HO4 sing ? 
7 2 7 GLC C1 O1 6 GLC O4 HO4 sing ? 
8 2 8 GLC C1 O1 7 GLC O4 HO4 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 
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 
CYS 'L-peptide linking'           y CYSTEINE                ?                                     'C3 H7 N O2 S'   121.158 
EDO non-polymer                   . 1,2-ETHANEDIOL          'ETHYLENE GLYCOL'                     'C2 H6 O2'       62.068  
GLC 'D-saccharide, alpha linking' . alpha-D-glucopyranose   'alpha-D-glucose; D-glucose; glucose' '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 
PEG non-polymer                   . 'DI(HYDROXYETHYL)ETHER' ?                                     'C4 H10 O3'      106.120 
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 
GLC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpa            
GLC 'COMMON NAME'                         GMML     1.0 a-D-glucopyranose 
GLC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Glcp          
GLC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
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   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  HIS 11  11  11  HIS HIS A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  HIS 13  13  13  HIS HIS A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  MET 41  41  41  MET MET A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 HIS 198 198 198 HIS HIS A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 HIS 248 248 248 HIS HIS A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 TRP 253 253 253 TRP TRP A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 ASN 261 261 261 ASN ASN A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 TYR 267 267 267 TYR TYR A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 MET 274 274 274 MET MET A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 PRO 291 291 291 PRO PRO A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 SER 302 302 302 SER SER A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 PHE 304 304 304 PHE PHE A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 ARG 306 306 306 ARG ARG A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ILE 314 314 314 ILE ILE A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 PHE 316 316 316 PHE PHE A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 TYR 318 318 318 TYR TYR A . n 
A 1 319 HIS 319 319 319 HIS HIS A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 GLU 324 324 324 GLU GLU A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 PHE 330 330 330 PHE PHE A . n 
A 1 331 ILE 331 331 331 ILE ILE A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 GLN 344 344 344 GLN GLN A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 ASN 352 352 352 ASN ASN A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 GLU 354 354 354 GLU GLU A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 CYS 356 356 356 CYS CYS A . n 
A 1 357 TRP 357 357 357 TRP TRP A . n 
A 1 358 GLU 358 358 358 GLU GLU A . n 
A 1 359 TYR 359 359 359 TYR TYR A . n 
A 1 360 TYR 360 360 360 TYR TYR A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 PRO 366 366 366 PRO PRO A . n 
A 1 367 PHE 367 367 367 PHE PHE A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 GLU 369 369 369 GLU GLU A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 TYR 372 372 372 TYR TYR A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 GLU 378 378 378 GLU GLU A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 TRP 380 380 380 TRP TRP A . n 
A 1 381 ILE 381 381 381 ILE ILE A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 MET 390 390 390 MET MET A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 LYS 392 392 392 LYS LYS A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 ASP 394 394 394 ASP ASP A . n 
A 1 395 VAL 395 395 395 VAL VAL A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 ILE 400 400 400 ILE ILE A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 SER 402 402 402 SER SER A . n 
A 1 403 VAL 403 403 403 VAL VAL A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 ALA 405 405 405 ALA ALA A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 TRP 408 408 408 TRP TRP A . n 
A 1 409 PHE 409 409 409 PHE PHE A . n 
A 1 410 ASP 410 410 410 ASP ASP A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 ASN 412 412 412 ASN ASN A . n 
A 1 413 PHE 413 413 413 PHE PHE A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 TRP 416 416 416 TRP TRP A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 GLY 418 418 418 GLY GLY A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 LYS 422 422 422 LYS LYS A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 TYR 425 425 425 TYR TYR A . n 
A 1 426 TRP 426 426 426 TRP TRP A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 LYS 435 435 435 LYS LYS A . n 
A 1 436 ALA 436 436 436 ALA ALA A . n 
A 1 437 LYS 437 437 437 LYS LYS A . n 
A 1 438 ASN 438 438 438 ASN ASN A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 TYR 440 440 440 TYR TYR A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 LEU 442 442 442 LEU LEU A . n 
A 1 443 VAL 443 443 443 VAL VAL A . n 
A 1 444 ALA 444 444 444 ALA ALA A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 SER 447 447 447 SER SER A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 TRP 449 449 449 TRP TRP A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 TRP 451 451 451 TRP TRP A . n 
A 1 452 TRP 452 452 452 TRP TRP A . n 
A 1 453 GLN 453 453 453 GLN GLN A . n 
A 1 454 GLY 454 454 454 GLY GLY A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 GLU 456 456 456 GLU GLU A . n 
A 1 457 LYS 457 457 457 LYS LYS A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 PRO 459 459 459 PRO PRO A . n 
A 1 460 PHE 460 460 460 PHE PHE A . n 
A 1 461 VAL 461 461 461 VAL VAL A . n 
A 1 462 GLU 462 462 462 GLU GLU A . n 
A 1 463 VAL 463 463 463 VAL VAL A . n 
A 1 464 PHE 464 464 464 PHE PHE A . n 
A 1 465 ASP 465 465 465 ASP ASP A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 LEU 467 467 467 LEU LEU A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 PHE 471 471 471 PHE PHE A . n 
A 1 472 VAL 472 472 472 VAL VAL A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 ARG 474 474 474 ARG ARG A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 GLN 476 476 476 GLN GLN A . n 
A 1 477 GLU 477 477 477 GLU GLU A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LYS 2   2   2   LYS LYS B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   PHE 5   5   5   PHE PHE B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  TRP 10  10  10  TRP TRP B . n 
B 1 11  HIS 11  11  11  HIS HIS B . n 
B 1 12  MET 12  12  12  MET MET B . n 
B 1 13  HIS 13  13  13  HIS HIS B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ARG 18  18  18  ARG ARG B . n 
B 1 19  GLU 19  19  19  GLU GLU B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  TYR 25  25  25  TYR TYR B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  THR 30  30  30  THR THR B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  ASP 37  37  37  ASP ASP B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  MET 41  41  41  MET MET B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  PHE 54  54  54  PHE PHE B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  TYR 67  67  67  TYR TYR B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  GLU 90  90  90  GLU GLU B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 LYS 105 105 105 LYS LYS B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 TYR 108 108 108 TYR TYR B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 PHE 110 110 110 PHE PHE B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 MET 117 117 117 MET MET B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 ASN 123 123 123 ASN ASN B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 TRP 138 138 138 TRP TRP B . n 
B 1 139 CYS 139 139 139 CYS CYS B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 ASP 149 149 149 ASP ASP B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 ARG 155 155 155 ARG ARG B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 TYR 157 157 157 TYR TYR B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 GLN 159 159 159 GLN GLN B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 GLU 163 163 163 GLU GLU B . n 
B 1 164 TYR 164 164 164 TYR TYR B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 ILE 173 173 173 ILE ILE B . n 
B 1 174 LYS 174 174 174 LYS LYS B . n 
B 1 175 LYS 175 175 175 LYS LYS B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 TYR 180 180 180 TYR TYR B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 ILE 183 183 183 ILE ILE B . n 
B 1 184 LYS 184 184 184 LYS LYS B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 LYS 188 188 188 LYS LYS B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 SER 192 192 192 SER SER B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 SER 194 194 194 SER SER B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 TYR 196 196 196 TYR TYR B . n 
B 1 197 TYR 197 197 197 TYR TYR B . n 
B 1 198 HIS 198 198 198 HIS HIS B . n 
B 1 199 PRO 199 199 199 PRO PRO B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 ILE 201 201 201 ILE ILE B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ASN 206 206 206 ASN ASN B . n 
B 1 207 PRO 207 207 207 PRO PRO B . n 
B 1 208 ASN 208 208 208 ASN ASN B . n 
B 1 209 CYS 209 209 209 CYS CYS B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 PRO 215 215 215 PRO PRO B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 PRO 220 220 220 PRO PRO B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 PHE 226 226 226 PHE PHE B . n 
B 1 227 ARG 227 227 227 ARG ARG B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 LYS 232 232 232 LYS LYS B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 VAL 234 234 234 VAL VAL B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 LYS 238 238 238 LYS LYS B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 PHE 242 242 242 PHE PHE B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 PHE 245 245 245 PHE PHE B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 HIS 248 248 248 HIS HIS B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 TYR 251 251 251 TYR TYR B . n 
B 1 252 MET 252 252 252 MET MET B . n 
B 1 253 TRP 253 253 253 TRP TRP B . n 
B 1 254 PRO 254 254 254 PRO PRO B . n 
B 1 255 PRO 255 255 255 PRO PRO B . n 
B 1 256 GLU 256 256 256 GLU GLU B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 SER 258 258 258 SER SER B . n 
B 1 259 VAL 259 259 259 VAL VAL B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 ASN 261 261 261 ASN ASN B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 GLU 265 265 265 GLU GLU B . n 
B 1 266 LEU 266 266 266 LEU LEU B . n 
B 1 267 TYR 267 267 267 TYR TYR B . n 
B 1 268 TYR 268 268 268 TYR TYR B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 LYS 270 270 270 LYS LYS B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 ILE 272 272 272 ILE ILE B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 MET 274 274 274 MET MET B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 ASP 278 278 278 ASP ASP B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 VAL 280 280 280 VAL VAL B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 ASN 284 284 284 ASN ASN B . n 
B 1 285 SER 285 285 285 SER SER B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 GLU 287 287 287 GLU GLU B . n 
B 1 288 ARG 288 288 288 ARG ARG B . n 
B 1 289 ALA 289 289 289 ALA ALA B . n 
B 1 290 SER 290 290 290 SER SER B . n 
B 1 291 PRO 291 291 291 PRO PRO B . n 
B 1 292 TYR 292 292 292 TYR TYR B . n 
B 1 293 LEU 293 293 293 LEU LEU B . n 
B 1 294 ARG 294 294 294 ARG ARG B . n 
B 1 295 TYR 295 295 295 TYR TYR B . n 
B 1 296 TYR 296 296 296 TYR TYR B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 ILE 301 301 301 ILE ILE B . n 
B 1 302 SER 302 302 302 SER SER B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 PHE 304 304 304 PHE PHE B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 ARG 306 306 306 ARG ARG B . n 
B 1 307 ASP 307 307 307 ASP ASP B . n 
B 1 308 LYS 308 308 308 LYS LYS B . n 
B 1 309 THR 309 309 309 THR THR B . n 
B 1 310 LEU 310 310 310 LEU LEU B . n 
B 1 311 SER 311 311 311 SER SER B . n 
B 1 312 ASP 312 312 312 ASP ASP B . n 
B 1 313 LEU 313 313 313 LEU LEU B . n 
B 1 314 ILE 314 314 314 ILE ILE B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 PHE 316 316 316 PHE PHE B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 TYR 318 318 318 TYR TYR B . n 
B 1 319 HIS 319 319 319 HIS HIS B . n 
B 1 320 ALA 320 320 320 ALA ALA B . n 
B 1 321 TRP 321 321 321 TRP TRP B . n 
B 1 322 ASN 322 322 322 ASN ASN B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 GLU 324 324 324 GLU GLU B . n 
B 1 325 ASP 325 325 325 ASP ASP B . n 
B 1 326 ALA 326 326 326 ALA ALA B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ARG 328 328 328 ARG ARG B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 PHE 330 330 330 PHE PHE B . n 
B 1 331 ILE 331 331 331 ILE ILE B . n 
B 1 332 GLY 332 332 332 GLY GLY B . n 
B 1 333 ARG 333 333 333 ARG ARG B . n 
B 1 334 LEU 334 334 334 LEU LEU B . n 
B 1 335 LYS 335 335 335 LYS LYS B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 HIS 338 338 338 HIS HIS B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 SER 340 340 340 SER SER B . n 
B 1 341 VAL 341 341 341 VAL VAL B . n 
B 1 342 ASP 342 342 342 ASP ASP B . n 
B 1 343 PHE 343 343 343 PHE PHE B . n 
B 1 344 GLN 344 344 344 GLN GLN B . n 
B 1 345 PRO 345 345 345 PRO PRO B . n 
B 1 346 VAL 346 346 346 VAL VAL B . n 
B 1 347 VAL 347 347 347 VAL VAL B . n 
B 1 348 PHE 348 348 348 PHE PHE B . n 
B 1 349 VAL 349 349 349 VAL VAL B . n 
B 1 350 VAL 350 350 350 VAL VAL B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 ASN 352 352 352 ASN ASN B . n 
B 1 353 GLY 353 353 353 GLY GLY B . n 
B 1 354 GLU 354 354 354 GLU GLU B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 CYS 356 356 356 CYS CYS B . n 
B 1 357 TRP 357 357 357 TRP TRP B . n 
B 1 358 GLU 358 358 358 GLU GLU B . n 
B 1 359 TYR 359 359 359 TYR TYR B . n 
B 1 360 TYR 360 360 360 TYR TYR B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 GLU 362 362 362 GLU GLU B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 ILE 365 365 365 ILE ILE B . n 
B 1 366 PRO 366 366 366 PRO PRO B . n 
B 1 367 PHE 367 367 367 PHE PHE B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 GLU 369 369 369 GLU GLU B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 LEU 371 371 371 LEU LEU B . n 
B 1 372 TYR 372 372 372 TYR TYR B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 THR 374 374 374 THR THR B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 GLU 378 378 378 GLU GLU B . n 
B 1 379 GLU 379 379 379 GLU GLU B . n 
B 1 380 TRP 380 380 380 TRP TRP B . n 
B 1 381 ILE 381 381 381 ILE ILE B . n 
B 1 382 GLU 382 382 382 GLU GLU B . n 
B 1 383 THR 383 383 383 THR THR B . n 
B 1 384 LEU 384 384 384 LEU LEU B . n 
B 1 385 THR 385 385 385 THR THR B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLU 387 387 387 GLU GLU B . n 
B 1 388 GLU 388 388 388 GLU GLU B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 MET 390 390 390 MET MET B . n 
B 1 391 ARG 391 391 391 ARG ARG B . n 
B 1 392 LYS 392 392 392 LYS LYS B . n 
B 1 393 GLU 393 393 393 GLU GLU B . n 
B 1 394 ASP 394 394 394 ASP ASP B . n 
B 1 395 VAL 395 395 395 VAL VAL B . n 
B 1 396 LYS 396 396 396 LYS LYS B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 GLU 398 398 398 GLU GLU B . n 
B 1 399 VAL 399 399 399 VAL VAL B . n 
B 1 400 ILE 400 400 400 ILE ILE B . n 
B 1 401 GLU 401 401 401 GLU GLU B . n 
B 1 402 SER 402 402 402 SER SER B . n 
B 1 403 VAL 403 403 403 VAL VAL B . n 
B 1 404 LYS 404 404 404 LYS LYS B . n 
B 1 405 ALA 405 405 405 ALA ALA B . n 
B 1 406 GLY 406 406 406 GLY GLY B . n 
B 1 407 THR 407 407 407 THR THR B . n 
B 1 408 TRP 408 408 408 TRP TRP B . n 
B 1 409 PHE 409 409 409 PHE PHE B . n 
B 1 410 ASP 410 410 410 ASP ASP B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 ASN 412 412 412 ASN ASN B . n 
B 1 413 PHE 413 413 413 PHE PHE B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 LYS 415 415 415 LYS LYS B . n 
B 1 416 TRP 416 416 416 TRP TRP B . n 
B 1 417 ILE 417 417 417 ILE ILE B . n 
B 1 418 GLY 418 418 418 GLY GLY B . n 
B 1 419 ASN 419 419 419 ASN ASN B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 LYS 422 422 422 LYS LYS B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 GLU 424 424 424 GLU GLU B . n 
B 1 425 TYR 425 425 425 TYR TYR B . n 
B 1 426 TRP 426 426 426 TRP TRP B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 ILE 428 428 428 ILE ILE B . n 
B 1 429 LEU 429 429 429 LEU LEU B . n 
B 1 430 ILE 430 430 430 ILE ILE B . n 
B 1 431 GLU 431 431 431 GLU GLU B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 LYS 433 433 433 LYS LYS B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 LYS 435 435 435 LYS LYS B . n 
B 1 436 ALA 436 436 436 ALA ALA B . n 
B 1 437 LYS 437 437 437 LYS LYS B . n 
B 1 438 ASN 438 438 438 ASN ASN B . n 
B 1 439 ASP 439 439 439 ASP ASP B . n 
B 1 440 TYR 440 440 440 TYR TYR B . n 
B 1 441 ILE 441 441 441 ILE ILE B . n 
B 1 442 LEU 442 442 442 LEU LEU B . n 
B 1 443 VAL 443 443 443 VAL VAL B . n 
B 1 444 ALA 444 444 444 ALA ALA B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 GLY 446 446 446 GLY GLY B . n 
B 1 447 SER 447 447 447 SER SER B . n 
B 1 448 ASP 448 448 448 ASP ASP B . n 
B 1 449 TRP 449 449 449 TRP TRP B . n 
B 1 450 PHE 450 450 450 PHE PHE B . n 
B 1 451 TRP 451 451 451 TRP TRP B . n 
B 1 452 TRP 452 452 452 TRP TRP B . n 
B 1 453 GLN 453 453 453 GLN GLN B . n 
B 1 454 GLY 454 454 454 GLY GLY B . n 
B 1 455 GLU 455 455 455 GLU GLU B . n 
B 1 456 GLU 456 456 456 GLU GLU B . n 
B 1 457 LYS 457 457 457 LYS LYS B . n 
B 1 458 ALA 458 458 458 ALA ALA B . n 
B 1 459 PRO 459 459 459 PRO PRO B . n 
B 1 460 PHE 460 460 460 PHE PHE B . n 
B 1 461 VAL 461 461 461 VAL VAL B . n 
B 1 462 GLU 462 462 462 GLU GLU B . n 
B 1 463 VAL 463 463 463 VAL VAL B . n 
B 1 464 PHE 464 464 464 PHE PHE B . n 
B 1 465 ASP 465 465 465 ASP ASP B . n 
B 1 466 LYS 466 466 466 LYS LYS B . n 
B 1 467 LEU 467 467 467 LEU LEU B . n 
B 1 468 PHE 468 468 468 PHE PHE B . n 
B 1 469 ARG 469 469 469 ARG ARG B . n 
B 1 470 SER 470 470 470 SER SER B . n 
B 1 471 PHE 471 471 471 PHE PHE B . n 
B 1 472 VAL 472 472 472 VAL VAL B . n 
B 1 473 ARG 473 473 473 ARG ARG B . n 
B 1 474 ARG 474 474 474 ARG ARG B . n 
B 1 475 ALA 475 475 475 ALA ALA B . n 
B 1 476 GLN 476 476 476 GLN GLN B . n 
B 1 477 GLU 477 477 477 GLU GLU B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   LYS 2   2   2   LYS LYS C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   LEU 4   4   4   LEU LEU C . n 
C 1 5   PHE 5   5   5   PHE PHE C . n 
C 1 6   LEU 6   6   6   LEU LEU C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   PHE 8   8   8   PHE PHE C . n 
C 1 9   TRP 9   9   9   TRP TRP C . n 
C 1 10  TRP 10  10  10  TRP TRP C . n 
C 1 11  HIS 11  11  11  HIS HIS C . n 
C 1 12  MET 12  12  12  MET MET C . n 
C 1 13  HIS 13  13  13  HIS HIS C . n 
C 1 14  GLN 14  14  14  GLN GLN C . n 
C 1 15  PRO 15  15  15  PRO PRO C . n 
C 1 16  LEU 16  16  16  LEU LEU C . n 
C 1 17  TYR 17  17  17  TYR TYR C . n 
C 1 18  ARG 18  18  18  ARG ARG C . n 
C 1 19  GLU 19  19  19  GLU GLU C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  TYR 21  21  21  TYR TYR C . n 
C 1 22  THR 22  22  22  THR THR C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  TYR 25  25  25  TYR TYR C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  LEU 27  27  27  LEU LEU C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  TRP 29  29  29  TRP TRP C . n 
C 1 30  THR 30  30  30  THR THR C . n 
C 1 31  PHE 31  31  31  PHE PHE C . n 
C 1 32  PHE 32  32  32  PHE PHE C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  ALA 34  34  34  ALA ALA C . n 
C 1 35  VAL 35  35  35  VAL VAL C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  ASP 37  37  37  ASP ASP C . n 
C 1 38  TYR 38  38  38  TYR TYR C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  MET 41  41  41  MET MET C . n 
C 1 42  PRO 42  42  42  PRO PRO C . n 
C 1 43  ALA 43  43  43  ALA ALA C . n 
C 1 44  TYR 44  44  44  TYR TYR C . n 
C 1 45  LEU 45  45  45  LEU LEU C . n 
C 1 46  LYS 46  46  46  LYS LYS C . n 
C 1 47  ASP 47  47  47  ASP ASP C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  ILE 50  50  50  ILE ILE C . n 
C 1 51  LYS 51  51  51  LYS LYS C . n 
C 1 52  LEU 52  52  52  LEU LEU C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  PHE 54  54  54  PHE PHE C . n 
C 1 55  ASN 55  55  55  ASN ASN C . n 
C 1 56  LEU 56  56  56  LEU LEU C . n 
C 1 57  THR 57  57  57  THR THR C . n 
C 1 58  PRO 58  58  58  PRO PRO C . n 
C 1 59  VAL 59  59  59  VAL VAL C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  ILE 61  61  61  ILE ILE C . n 
C 1 62  ASP 62  62  62  ASP ASP C . n 
C 1 63  GLN 63  63  63  GLN GLN C . n 
C 1 64  ILE 64  64  64  ILE ILE C . n 
C 1 65  GLN 65  65  65  GLN GLN C . n 
C 1 66  GLU 66  66  66  GLU GLU C . n 
C 1 67  TYR 67  67  67  TYR TYR C . n 
C 1 68  ALA 68  68  68  ALA ALA C . n 
C 1 69  GLN 69  69  69  GLN GLN C . n 
C 1 70  GLY 70  70  70  GLY GLY C . n 
C 1 71  LYS 71  71  71  LYS LYS C . n 
C 1 72  ALA 72  72  72  ALA ALA C . n 
C 1 73  LYS 73  73  73  LYS LYS C . n 
C 1 74  ASP 74  74  74  ASP ASP C . n 
C 1 75  VAL 75  75  75  VAL VAL C . n 
C 1 76  PHE 76  76  76  PHE PHE C . n 
C 1 77  LEU 77  77  77  LEU LEU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ALA 79  79  79  ALA ALA C . n 
C 1 80  ILE 80  80  80  ILE ILE C . n 
C 1 81  ARG 81  81  81  ARG ARG C . n 
C 1 82  LYS 82  82  82  LYS LYS C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  PRO 84  84  84  PRO PRO C . n 
C 1 85  ASP 85  85  85  ASP ASP C . n 
C 1 86  ASP 86  86  86  ASP ASP C . n 
C 1 87  LEU 87  87  87  LEU LEU C . n 
C 1 88  GLU 88  88  88  GLU GLU C . n 
C 1 89  LYS 89  89  89  LYS LYS C . n 
C 1 90  GLU 90  90  90  GLU GLU C . n 
C 1 91  GLU 91  91  91  GLU GLU C . n 
C 1 92  VAL 92  92  92  VAL VAL C . n 
C 1 93  GLU 93  93  93  GLU GLU C . n 
C 1 94  LYS 94  94  94  LYS LYS C . n 
C 1 95  LEU 95  95  95  LEU LEU C . n 
C 1 96  ILE 96  96  96  ILE ILE C . n 
C 1 97  GLU 97  97  97  GLU GLU C . n 
C 1 98  PHE 98  98  98  PHE PHE C . n 
C 1 99  THR 99  99  99  THR THR C . n 
C 1 100 LYS 100 100 100 LYS LYS C . n 
C 1 101 LEU 101 101 101 LEU LEU C . n 
C 1 102 ASN 102 102 102 ASN ASN C . n 
C 1 103 TYR 103 103 103 TYR TYR C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 LYS 105 105 105 LYS LYS C . n 
C 1 106 PRO 106 106 106 PRO PRO C . n 
C 1 107 ILE 107 107 107 ILE ILE C . n 
C 1 108 TYR 108 108 108 TYR TYR C . n 
C 1 109 ARG 109 109 109 ARG ARG C . n 
C 1 110 PHE 110 110 110 PHE PHE C . n 
C 1 111 GLU 111 111 111 GLU GLU C . n 
C 1 112 ARG 112 112 112 ARG ARG C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 ARG 114 114 114 ARG ARG C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 MET 117 117 117 MET MET C . n 
C 1 118 ASN 118 118 118 ASN ASN C . n 
C 1 119 LYS 119 119 119 LYS LYS C . n 
C 1 120 GLU 120 120 120 GLU GLU C . n 
C 1 121 LYS 121 121 121 LYS LYS C . n 
C 1 122 LEU 122 122 122 LEU LEU C . n 
C 1 123 ASN 123 123 123 ASN ASN C . n 
C 1 124 ARG 124 124 124 ARG ARG C . n 
C 1 125 GLU 125 125 125 GLU GLU C . n 
C 1 126 GLU 126 126 126 GLU GLU C . n 
C 1 127 LEU 127 127 127 LEU LEU C . n 
C 1 128 LEU 128 128 128 LEU LEU C . n 
C 1 129 ASP 129 129 129 ASP ASP C . n 
C 1 130 LEU 130 130 130 LEU LEU C . n 
C 1 131 GLN 131 131 131 GLN GLN C . n 
C 1 132 THR 132 132 132 THR THR C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LEU 135 135 135 LEU LEU C . n 
C 1 136 LEU 136 136 136 LEU LEU C . n 
C 1 137 ALA 137 137 137 ALA ALA C . n 
C 1 138 TRP 138 138 138 TRP TRP C . n 
C 1 139 CYS 139 139 139 CYS CYS C . n 
C 1 140 GLY 140 140 140 GLY GLY C . n 
C 1 141 ARG 141 141 141 ARG ARG C . n 
C 1 142 THR 142 142 142 THR THR C . n 
C 1 143 LEU 143 143 143 LEU LEU C . n 
C 1 144 ARG 144 144 144 ARG ARG C . n 
C 1 145 LYS 145 145 145 LYS LYS C . n 
C 1 146 ASP 146 146 146 ASP ASP C . n 
C 1 147 LEU 147 147 147 LEU LEU C . n 
C 1 148 LYS 148 148 148 LYS LYS C . n 
C 1 149 ASP 149 149 149 ASP ASP C . n 
C 1 150 LEU 150 150 150 LEU LEU C . n 
C 1 151 LEU 151 151 151 LEU LEU C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 LYS 153 153 153 LYS LYS C . n 
C 1 154 GLY 154 154 154 GLY GLY C . n 
C 1 155 ARG 155 155 155 ARG ARG C . n 
C 1 156 ASN 156 156 156 ASN ASN C . n 
C 1 157 TYR 157 157 157 TYR TYR C . n 
C 1 158 THR 158 158 158 THR THR C . n 
C 1 159 GLN 159 159 159 GLN GLN C . n 
C 1 160 GLU 160 160 160 GLU GLU C . n 
C 1 161 GLU 161 161 161 GLU GLU C . n 
C 1 162 LYS 162 162 162 LYS LYS C . n 
C 1 163 GLU 163 163 163 GLU GLU C . n 
C 1 164 TYR 164 164 164 TYR TYR C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LEU 166 166 166 LEU LEU C . n 
C 1 167 ASN 167 167 167 ASN ASN C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 TYR 169 169 169 TYR TYR C . n 
C 1 170 PHE 170 170 170 PHE PHE C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ILE 172 172 172 ILE ILE C . n 
C 1 173 ILE 173 173 173 ILE ILE C . n 
C 1 174 LYS 174 174 174 LYS LYS C . n 
C 1 175 LYS 175 175 175 LYS LYS C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 LEU 177 177 177 LEU LEU C . n 
C 1 178 SER 178 178 178 SER SER C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 TYR 180 180 180 TYR TYR C . n 
C 1 181 ARG 181 181 181 ARG ARG C . n 
C 1 182 GLU 182 182 182 GLU GLU C . n 
C 1 183 ILE 183 183 183 ILE ILE C . n 
C 1 184 LYS 184 184 184 LYS LYS C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 GLU 186 186 186 GLU GLU C . n 
C 1 187 GLY 187 187 187 GLY GLY C . n 
C 1 188 LYS 188 188 188 LYS LYS C . n 
C 1 189 GLY 189 189 189 GLY GLY C . n 
C 1 190 SER 190 190 190 SER SER C . n 
C 1 191 VAL 191 191 191 VAL VAL C . n 
C 1 192 SER 192 192 192 SER SER C . n 
C 1 193 THR 193 193 193 THR THR C . n 
C 1 194 SER 194 194 194 SER SER C . n 
C 1 195 PRO 195 195 195 PRO PRO C . n 
C 1 196 TYR 196 196 196 TYR TYR C . n 
C 1 197 TYR 197 197 197 TYR TYR C . n 
C 1 198 HIS 198 198 198 HIS HIS C . n 
C 1 199 PRO 199 199 199 PRO PRO C . n 
C 1 200 LEU 200 200 200 LEU LEU C . n 
C 1 201 ILE 201 201 201 ILE ILE C . n 
C 1 202 PRO 202 202 202 PRO PRO C . n 
C 1 203 ILE 203 203 203 ILE ILE C . n 
C 1 204 LEU 204 204 204 LEU LEU C . n 
C 1 205 LEU 205 205 205 LEU LEU C . n 
C 1 206 ASN 206 206 206 ASN ASN C . n 
C 1 207 PRO 207 207 207 PRO PRO C . n 
C 1 208 ASN 208 208 208 ASN ASN C . n 
C 1 209 CYS 209 209 209 CYS CYS C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 TYR 211 211 211 TYR TYR C . n 
C 1 212 GLU 212 212 212 GLU GLU C . n 
C 1 213 THR 213 213 213 THR THR C . n 
C 1 214 THR 214 214 214 THR THR C . n 
C 1 215 PRO 215 215 215 PRO PRO C . n 
C 1 216 ASN 216 216 216 ASN ASN C . n 
C 1 217 VAL 217 217 217 VAL VAL C . n 
C 1 218 LYS 218 218 218 LYS LYS C . n 
C 1 219 ILE 219 219 219 ILE ILE C . n 
C 1 220 PRO 220 220 220 PRO PRO C . n 
C 1 221 ASP 221 221 221 ASP ASP C . n 
C 1 222 PHE 222 222 222 PHE PHE C . n 
C 1 223 ALA 223 223 223 ALA ALA C . n 
C 1 224 VAL 224 224 224 VAL VAL C . n 
C 1 225 SER 225 225 225 SER SER C . n 
C 1 226 PHE 226 226 226 PHE PHE C . n 
C 1 227 ARG 227 227 227 ARG ARG C . n 
C 1 228 GLU 228 228 228 GLU GLU C . n 
C 1 229 ASP 229 229 229 ASP ASP C . n 
C 1 230 ALA 230 230 230 ALA ALA C . n 
C 1 231 SER 231 231 231 SER SER C . n 
C 1 232 LYS 232 232 232 LYS LYS C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 VAL 234 234 234 VAL VAL C . n 
C 1 235 GLU 235 235 235 GLU GLU C . n 
C 1 236 LEU 236 236 236 LEU LEU C . n 
C 1 237 ALA 237 237 237 ALA ALA C . n 
C 1 238 LYS 238 238 238 LYS LYS C . n 
C 1 239 GLU 239 239 239 GLU GLU C . n 
C 1 240 LYS 240 240 240 LYS LYS C . n 
C 1 241 TYR 241 241 241 TYR TYR C . n 
C 1 242 PHE 242 242 242 PHE PHE C . n 
C 1 243 GLU 243 243 243 GLU GLU C . n 
C 1 244 ILE 244 244 244 ILE ILE C . n 
C 1 245 PHE 245 245 245 PHE PHE C . n 
C 1 246 GLY 246 246 246 GLY GLY C . n 
C 1 247 GLU 247 247 247 GLU GLU C . n 
C 1 248 HIS 248 248 248 HIS HIS C . n 
C 1 249 PRO 249 249 249 PRO PRO C . n 
C 1 250 VAL 250 250 250 VAL VAL C . n 
C 1 251 TYR 251 251 251 TYR TYR C . n 
C 1 252 MET 252 252 252 MET MET C . n 
C 1 253 TRP 253 253 253 TRP TRP C . n 
C 1 254 PRO 254 254 254 PRO PRO C . n 
C 1 255 PRO 255 255 255 PRO PRO C . n 
C 1 256 GLU 256 256 256 GLU GLU C . n 
C 1 257 ALA 257 257 257 ALA ALA C . n 
C 1 258 SER 258 258 258 SER SER C . n 
C 1 259 VAL 259 259 259 VAL VAL C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 ASN 261 261 261 ASN ASN C . n 
C 1 262 GLU 262 262 262 GLU GLU C . n 
C 1 263 ALA 263 263 263 ALA ALA C . n 
C 1 264 LEU 264 264 264 LEU LEU C . n 
C 1 265 GLU 265 265 265 GLU GLU C . n 
C 1 266 LEU 266 266 266 LEU LEU C . n 
C 1 267 TYR 267 267 267 TYR TYR C . n 
C 1 268 TYR 268 268 268 TYR TYR C . n 
C 1 269 GLU 269 269 269 GLU GLU C . n 
C 1 270 LYS 270 270 270 LYS LYS C . n 
C 1 271 GLY 271 271 271 GLY GLY C . n 
C 1 272 ILE 272 272 272 ILE ILE C . n 
C 1 273 ASN 273 273 273 ASN ASN C . n 
C 1 274 MET 274 274 274 MET MET C . n 
C 1 275 LEU 275 275 275 LEU LEU C . n 
C 1 276 ALA 276 276 276 ALA ALA C . n 
C 1 277 THR 277 277 277 THR THR C . n 
C 1 278 ASP 278 278 278 ASP ASP C . n 
C 1 279 GLU 279 279 279 GLU GLU C . n 
C 1 280 VAL 280 280 280 VAL VAL C . n 
C 1 281 ILE 281 281 281 ILE ILE C . n 
C 1 282 LEU 282 282 282 LEU LEU C . n 
C 1 283 LYS 283 283 283 LYS LYS C . n 
C 1 284 ASN 284 284 284 ASN ASN C . n 
C 1 285 SER 285 285 285 SER SER C . n 
C 1 286 VAL 286 286 286 VAL VAL C . n 
C 1 287 GLU 287 287 287 GLU GLU C . n 
C 1 288 ARG 288 288 288 ARG ARG C . n 
C 1 289 ALA 289 289 289 ALA ALA C . n 
C 1 290 SER 290 290 290 SER SER C . n 
C 1 291 PRO 291 291 291 PRO PRO C . n 
C 1 292 TYR 292 292 292 TYR TYR C . n 
C 1 293 LEU 293 293 293 LEU LEU C . n 
C 1 294 ARG 294 294 294 ARG ARG C . n 
C 1 295 TYR 295 295 295 TYR TYR C . n 
C 1 296 TYR 296 296 296 TYR TYR C . n 
C 1 297 PHE 297 297 297 PHE PHE C . n 
C 1 298 ARG 298 298 298 ARG ARG C . n 
C 1 299 GLU 299 299 299 GLU GLU C . n 
C 1 300 LEU 300 300 300 LEU LEU C . n 
C 1 301 ILE 301 301 301 ILE ILE C . n 
C 1 302 SER 302 302 302 SER SER C . n 
C 1 303 VAL 303 303 303 VAL VAL C . n 
C 1 304 PHE 304 304 304 PHE PHE C . n 
C 1 305 PHE 305 305 305 PHE PHE C . n 
C 1 306 ARG 306 306 306 ARG ARG C . n 
C 1 307 ASP 307 307 307 ASP ASP C . n 
C 1 308 LYS 308 308 308 LYS LYS C . n 
C 1 309 THR 309 309 309 THR THR C . n 
C 1 310 LEU 310 310 310 LEU LEU C . n 
C 1 311 SER 311 311 311 SER SER C . n 
C 1 312 ASP 312 312 312 ASP ASP C . n 
C 1 313 LEU 313 313 313 LEU LEU C . n 
C 1 314 ILE 314 314 314 ILE ILE C . n 
C 1 315 GLY 315 315 315 GLY GLY C . n 
C 1 316 PHE 316 316 316 PHE PHE C . n 
C 1 317 SER 317 317 317 SER SER C . n 
C 1 318 TYR 318 318 318 TYR TYR C . n 
C 1 319 HIS 319 319 319 HIS HIS C . n 
C 1 320 ALA 320 320 320 ALA ALA C . n 
C 1 321 TRP 321 321 321 TRP TRP C . n 
C 1 322 ASN 322 322 322 ASN ASN C . n 
C 1 323 ALA 323 323 323 ALA ALA C . n 
C 1 324 GLU 324 324 324 GLU GLU C . n 
C 1 325 ASP 325 325 325 ASP ASP C . n 
C 1 326 ALA 326 326 326 ALA ALA C . n 
C 1 327 VAL 327 327 327 VAL VAL C . n 
C 1 328 ARG 328 328 328 ARG ARG C . n 
C 1 329 ASP 329 329 329 ASP ASP C . n 
C 1 330 PHE 330 330 330 PHE PHE C . n 
C 1 331 ILE 331 331 331 ILE ILE C . n 
C 1 332 GLY 332 332 332 GLY GLY C . n 
C 1 333 ARG 333 333 333 ARG ARG C . n 
C 1 334 LEU 334 334 334 LEU LEU C . n 
C 1 335 LYS 335 335 335 LYS LYS C . n 
C 1 336 LYS 336 336 336 LYS LYS C . n 
C 1 337 ILE 337 337 337 ILE ILE C . n 
C 1 338 HIS 338 338 338 HIS HIS C . n 
C 1 339 GLU 339 339 339 GLU GLU C . n 
C 1 340 SER 340 340 340 SER SER C . n 
C 1 341 VAL 341 341 341 VAL VAL C . n 
C 1 342 ASP 342 342 342 ASP ASP C . n 
C 1 343 PHE 343 343 343 PHE PHE C . n 
C 1 344 GLN 344 344 344 GLN GLN C . n 
C 1 345 PRO 345 345 345 PRO PRO C . n 
C 1 346 VAL 346 346 346 VAL VAL C . n 
C 1 347 VAL 347 347 347 VAL VAL C . n 
C 1 348 PHE 348 348 348 PHE PHE C . n 
C 1 349 VAL 349 349 349 VAL VAL C . n 
C 1 350 VAL 350 350 350 VAL VAL C . n 
C 1 351 LEU 351 351 351 LEU LEU C . n 
C 1 352 ASN 352 352 352 ASN ASN C . n 
C 1 353 GLY 353 353 353 GLY GLY C . n 
C 1 354 GLU 354 354 354 GLU GLU C . n 
C 1 355 ASN 355 355 355 ASN ASN C . n 
C 1 356 CYS 356 356 356 CYS CYS C . n 
C 1 357 TRP 357 357 357 TRP TRP C . n 
C 1 358 GLU 358 358 358 GLU GLU C . n 
C 1 359 TYR 359 359 359 TYR TYR C . n 
C 1 360 TYR 360 360 360 TYR TYR C . n 
C 1 361 GLU 361 361 361 GLU GLU C . n 
C 1 362 GLU 362 362 362 GLU GLU C . n 
C 1 363 ASN 363 363 363 ASN ASN C . n 
C 1 364 GLY 364 364 364 GLY GLY C . n 
C 1 365 ILE 365 365 365 ILE ILE C . n 
C 1 366 PRO 366 366 366 PRO PRO C . n 
C 1 367 PHE 367 367 367 PHE PHE C . n 
C 1 368 LEU 368 368 368 LEU LEU C . n 
C 1 369 GLU 369 369 369 GLU GLU C . n 
C 1 370 LYS 370 370 370 LYS LYS C . n 
C 1 371 LEU 371 371 371 LEU LEU C . n 
C 1 372 TYR 372 372 372 TYR TYR C . n 
C 1 373 SER 373 373 373 SER SER C . n 
C 1 374 THR 374 374 374 THR THR C . n 
C 1 375 LEU 375 375 375 LEU LEU C . n 
C 1 376 GLU 376 376 376 GLU GLU C . n 
C 1 377 LYS 377 377 377 LYS LYS C . n 
C 1 378 GLU 378 378 378 GLU GLU C . n 
C 1 379 GLU 379 379 379 GLU GLU C . n 
C 1 380 TRP 380 380 380 TRP TRP C . n 
C 1 381 ILE 381 381 381 ILE ILE C . n 
C 1 382 GLU 382 382 382 GLU GLU C . n 
C 1 383 THR 383 383 383 THR THR C . n 
C 1 384 LEU 384 384 384 LEU LEU C . n 
C 1 385 THR 385 385 385 THR THR C . n 
C 1 386 LEU 386 386 386 LEU LEU C . n 
C 1 387 GLU 387 387 387 GLU GLU C . n 
C 1 388 GLU 388 388 388 GLU GLU C . n 
C 1 389 ALA 389 389 389 ALA ALA C . n 
C 1 390 MET 390 390 390 MET MET C . n 
C 1 391 ARG 391 391 391 ARG ARG C . n 
C 1 392 LYS 392 392 392 LYS LYS C . n 
C 1 393 GLU 393 393 393 GLU GLU C . n 
C 1 394 ASP 394 394 394 ASP ASP C . n 
C 1 395 VAL 395 395 395 VAL VAL C . n 
C 1 396 LYS 396 396 396 LYS LYS C . n 
C 1 397 THR 397 397 397 THR THR C . n 
C 1 398 GLU 398 398 398 GLU GLU C . n 
C 1 399 VAL 399 399 399 VAL VAL C . n 
C 1 400 ILE 400 400 400 ILE ILE C . n 
C 1 401 GLU 401 401 401 GLU GLU C . n 
C 1 402 SER 402 402 402 SER SER C . n 
C 1 403 VAL 403 403 403 VAL VAL C . n 
C 1 404 LYS 404 404 404 LYS LYS C . n 
C 1 405 ALA 405 405 405 ALA ALA C . n 
C 1 406 GLY 406 406 406 GLY GLY C . n 
C 1 407 THR 407 407 407 THR THR C . n 
C 1 408 TRP 408 408 408 TRP TRP C . n 
C 1 409 PHE 409 409 409 PHE PHE C . n 
C 1 410 ASP 410 410 410 ASP ASP C . n 
C 1 411 GLY 411 411 411 GLY GLY C . n 
C 1 412 ASN 412 412 412 ASN ASN C . n 
C 1 413 PHE 413 413 413 PHE PHE C . n 
C 1 414 LEU 414 414 414 LEU LEU C . n 
C 1 415 LYS 415 415 415 LYS LYS C . n 
C 1 416 TRP 416 416 416 TRP TRP C . n 
C 1 417 ILE 417 417 417 ILE ILE C . n 
C 1 418 GLY 418 418 418 GLY GLY C . n 
C 1 419 ASN 419 419 419 ASN ASN C . n 
C 1 420 LYS 420 420 420 LYS LYS C . n 
C 1 421 GLU 421 421 421 GLU GLU C . n 
C 1 422 LYS 422 422 422 LYS LYS C . n 
C 1 423 ASN 423 423 423 ASN ASN C . n 
C 1 424 GLU 424 424 424 GLU GLU C . n 
C 1 425 TYR 425 425 425 TYR TYR C . n 
C 1 426 TRP 426 426 426 TRP TRP C . n 
C 1 427 LYS 427 427 427 LYS LYS C . n 
C 1 428 ILE 428 428 428 ILE ILE C . n 
C 1 429 LEU 429 429 429 LEU LEU C . n 
C 1 430 ILE 430 430 430 ILE ILE C . n 
C 1 431 GLU 431 431 431 GLU GLU C . n 
C 1 432 ALA 432 432 432 ALA ALA C . n 
C 1 433 LYS 433 433 433 LYS LYS C . n 
C 1 434 LYS 434 434 434 LYS LYS C . n 
C 1 435 LYS 435 435 435 LYS LYS C . n 
C 1 436 ALA 436 436 436 ALA ALA C . n 
C 1 437 LYS 437 437 437 LYS LYS C . n 
C 1 438 ASN 438 438 438 ASN ASN C . n 
C 1 439 ASP 439 439 439 ASP ASP C . n 
C 1 440 TYR 440 440 440 TYR TYR C . n 
C 1 441 ILE 441 441 441 ILE ILE C . n 
C 1 442 LEU 442 442 442 LEU LEU C . n 
C 1 443 VAL 443 443 443 VAL VAL C . n 
C 1 444 ALA 444 444 444 ALA ALA C . n 
C 1 445 GLU 445 445 445 GLU GLU C . n 
C 1 446 GLY 446 446 446 GLY GLY C . n 
C 1 447 SER 447 447 447 SER SER C . n 
C 1 448 ASP 448 448 448 ASP ASP C . n 
C 1 449 TRP 449 449 449 TRP TRP C . n 
C 1 450 PHE 450 450 450 PHE PHE C . n 
C 1 451 TRP 451 451 451 TRP TRP C . n 
C 1 452 TRP 452 452 452 TRP TRP C . n 
C 1 453 GLN 453 453 453 GLN GLN C . n 
C 1 454 GLY 454 454 454 GLY GLY C . n 
C 1 455 GLU 455 455 455 GLU GLU C . n 
C 1 456 GLU 456 456 456 GLU GLU C . n 
C 1 457 LYS 457 457 457 LYS LYS C . n 
C 1 458 ALA 458 458 458 ALA ALA C . n 
C 1 459 PRO 459 459 459 PRO PRO C . n 
C 1 460 PHE 460 460 460 PHE PHE C . n 
C 1 461 VAL 461 461 461 VAL VAL C . n 
C 1 462 GLU 462 462 462 GLU GLU C . n 
C 1 463 VAL 463 463 463 VAL VAL C . n 
C 1 464 PHE 464 464 464 PHE PHE C . n 
C 1 465 ASP 465 465 465 ASP ASP C . n 
C 1 466 LYS 466 466 466 LYS LYS C . n 
C 1 467 LEU 467 467 467 LEU LEU C . n 
C 1 468 PHE 468 468 468 PHE PHE C . n 
C 1 469 ARG 469 469 469 ARG ARG C . n 
C 1 470 SER 470 470 470 SER SER C . n 
C 1 471 PHE 471 471 471 PHE PHE C . n 
C 1 472 VAL 472 472 472 VAL VAL C . n 
C 1 473 ARG 473 473 473 ARG ARG C . n 
C 1 474 ARG 474 474 474 ARG ARG C . n 
C 1 475 ALA 475 475 475 ALA ALA C . n 
C 1 476 GLN 476 476 476 GLN GLN C . n 
C 1 477 GLU 477 477 477 GLU GLU C . n 
D 1 1   MET 1   1   1   MET MET D . n 
D 1 2   LYS 2   2   2   LYS LYS D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   LEU 4   4   4   LEU LEU D . n 
D 1 5   PHE 5   5   5   PHE PHE D . n 
D 1 6   LEU 6   6   6   LEU LEU D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   PHE 8   8   8   PHE PHE D . n 
D 1 9   TRP 9   9   9   TRP TRP D . n 
D 1 10  TRP 10  10  10  TRP TRP D . n 
D 1 11  HIS 11  11  11  HIS HIS D . n 
D 1 12  MET 12  12  12  MET MET D . n 
D 1 13  HIS 13  13  13  HIS HIS D . n 
D 1 14  GLN 14  14  14  GLN GLN D . n 
D 1 15  PRO 15  15  15  PRO PRO D . n 
D 1 16  LEU 16  16  16  LEU LEU D . n 
D 1 17  TYR 17  17  17  TYR TYR D . n 
D 1 18  ARG 18  18  18  ARG ARG D . n 
D 1 19  GLU 19  19  19  GLU GLU D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  TYR 21  21  21  TYR TYR D . n 
D 1 22  THR 22  22  22  THR THR D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  TYR 25  25  25  TYR TYR D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  LEU 27  27  27  LEU LEU D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  TRP 29  29  29  TRP TRP D . n 
D 1 30  THR 30  30  30  THR THR D . n 
D 1 31  PHE 31  31  31  PHE PHE D . n 
D 1 32  PHE 32  32  32  PHE PHE D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  ALA 34  34  34  ALA ALA D . n 
D 1 35  VAL 35  35  35  VAL VAL D . n 
D 1 36  LYS 36  36  36  LYS LYS D . n 
D 1 37  ASP 37  37  37  ASP ASP D . n 
D 1 38  TYR 38  38  38  TYR TYR D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  MET 41  41  41  MET MET D . n 
D 1 42  PRO 42  42  42  PRO PRO D . n 
D 1 43  ALA 43  43  43  ALA ALA D . n 
D 1 44  TYR 44  44  44  TYR TYR D . n 
D 1 45  LEU 45  45  45  LEU LEU D . n 
D 1 46  LYS 46  46  46  LYS LYS D . n 
D 1 47  ASP 47  47  47  ASP ASP D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  ILE 50  50  50  ILE ILE D . n 
D 1 51  LYS 51  51  51  LYS LYS D . n 
D 1 52  LEU 52  52  52  LEU LEU D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  PHE 54  54  54  PHE PHE D . n 
D 1 55  ASN 55  55  55  ASN ASN D . n 
D 1 56  LEU 56  56  56  LEU LEU D . n 
D 1 57  THR 57  57  57  THR THR D . n 
D 1 58  PRO 58  58  58  PRO PRO D . n 
D 1 59  VAL 59  59  59  VAL VAL D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  ILE 61  61  61  ILE ILE D . n 
D 1 62  ASP 62  62  62  ASP ASP D . n 
D 1 63  GLN 63  63  63  GLN GLN D . n 
D 1 64  ILE 64  64  64  ILE ILE D . n 
D 1 65  GLN 65  65  65  GLN GLN D . n 
D 1 66  GLU 66  66  66  GLU GLU D . n 
D 1 67  TYR 67  67  67  TYR TYR D . n 
D 1 68  ALA 68  68  68  ALA ALA D . n 
D 1 69  GLN 69  69  69  GLN GLN D . n 
D 1 70  GLY 70  70  70  GLY GLY D . n 
D 1 71  LYS 71  71  71  LYS LYS D . n 
D 1 72  ALA 72  72  72  ALA ALA D . n 
D 1 73  LYS 73  73  73  LYS LYS D . n 
D 1 74  ASP 74  74  74  ASP ASP D . n 
D 1 75  VAL 75  75  75  VAL VAL D . n 
D 1 76  PHE 76  76  76  PHE PHE D . n 
D 1 77  LEU 77  77  77  LEU LEU D . n 
D 1 78  GLU 78  78  78  GLU GLU D . n 
D 1 79  ALA 79  79  79  ALA ALA D . n 
D 1 80  ILE 80  80  80  ILE ILE D . n 
D 1 81  ARG 81  81  81  ARG ARG D . n 
D 1 82  LYS 82  82  82  LYS LYS D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  PRO 84  84  84  PRO PRO D . n 
D 1 85  ASP 85  85  85  ASP ASP D . n 
D 1 86  ASP 86  86  86  ASP ASP D . n 
D 1 87  LEU 87  87  87  LEU LEU D . n 
D 1 88  GLU 88  88  88  GLU GLU D . n 
D 1 89  LYS 89  89  89  LYS LYS D . n 
D 1 90  GLU 90  90  90  GLU GLU D . n 
D 1 91  GLU 91  91  91  GLU GLU D . n 
D 1 92  VAL 92  92  92  VAL VAL D . n 
D 1 93  GLU 93  93  93  GLU GLU D . n 
D 1 94  LYS 94  94  94  LYS LYS D . n 
D 1 95  LEU 95  95  95  LEU LEU D . n 
D 1 96  ILE 96  96  96  ILE ILE D . n 
D 1 97  GLU 97  97  97  GLU GLU D . n 
D 1 98  PHE 98  98  98  PHE PHE D . n 
D 1 99  THR 99  99  99  THR THR D . n 
D 1 100 LYS 100 100 100 LYS LYS D . n 
D 1 101 LEU 101 101 101 LEU LEU D . n 
D 1 102 ASN 102 102 102 ASN ASN D . n 
D 1 103 TYR 103 103 103 TYR TYR D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 LYS 105 105 105 LYS LYS D . n 
D 1 106 PRO 106 106 106 PRO PRO D . n 
D 1 107 ILE 107 107 107 ILE ILE D . n 
D 1 108 TYR 108 108 108 TYR TYR D . n 
D 1 109 ARG 109 109 109 ARG ARG D . n 
D 1 110 PHE 110 110 110 PHE PHE D . n 
D 1 111 GLU 111 111 111 GLU GLU D . n 
D 1 112 ARG 112 112 112 ARG ARG D . n 
D 1 113 ILE 113 113 113 ILE ILE D . n 
D 1 114 ARG 114 114 114 ARG ARG D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 MET 117 117 117 MET MET D . n 
D 1 118 ASN 118 118 118 ASN ASN D . n 
D 1 119 LYS 119 119 119 LYS LYS D . n 
D 1 120 GLU 120 120 120 GLU GLU D . n 
D 1 121 LYS 121 121 121 LYS LYS D . n 
D 1 122 LEU 122 122 122 LEU LEU D . n 
D 1 123 ASN 123 123 123 ASN ASN D . n 
D 1 124 ARG 124 124 124 ARG ARG D . n 
D 1 125 GLU 125 125 125 GLU GLU D . n 
D 1 126 GLU 126 126 126 GLU GLU D . n 
D 1 127 LEU 127 127 127 LEU LEU D . n 
D 1 128 LEU 128 128 128 LEU LEU D . n 
D 1 129 ASP 129 129 129 ASP ASP D . n 
D 1 130 LEU 130 130 130 LEU LEU D . n 
D 1 131 GLN 131 131 131 GLN GLN D . n 
D 1 132 THR 132 132 132 THR THR D . n 
D 1 133 LEU 133 133 133 LEU LEU D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LEU 135 135 135 LEU LEU D . n 
D 1 136 LEU 136 136 136 LEU LEU D . n 
D 1 137 ALA 137 137 137 ALA ALA D . n 
D 1 138 TRP 138 138 138 TRP TRP D . n 
D 1 139 CYS 139 139 139 CYS CYS D . n 
D 1 140 GLY 140 140 140 GLY GLY D . n 
D 1 141 ARG 141 141 141 ARG ARG D . n 
D 1 142 THR 142 142 142 THR THR D . n 
D 1 143 LEU 143 143 143 LEU LEU D . n 
D 1 144 ARG 144 144 144 ARG ARG D . n 
D 1 145 LYS 145 145 145 LYS LYS D . n 
D 1 146 ASP 146 146 146 ASP ASP D . n 
D 1 147 LEU 147 147 147 LEU LEU D . n 
D 1 148 LYS 148 148 148 LYS LYS D . n 
D 1 149 ASP 149 149 149 ASP ASP D . n 
D 1 150 LEU 150 150 150 LEU LEU D . n 
D 1 151 LEU 151 151 151 LEU LEU D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 LYS 153 153 153 LYS LYS D . n 
D 1 154 GLY 154 154 154 GLY GLY D . n 
D 1 155 ARG 155 155 155 ARG ARG D . n 
D 1 156 ASN 156 156 156 ASN ASN D . n 
D 1 157 TYR 157 157 157 TYR TYR D . n 
D 1 158 THR 158 158 158 THR THR D . n 
D 1 159 GLN 159 159 159 GLN GLN D . n 
D 1 160 GLU 160 160 160 GLU GLU D . n 
D 1 161 GLU 161 161 161 GLU GLU D . n 
D 1 162 LYS 162 162 162 LYS LYS D . n 
D 1 163 GLU 163 163 163 GLU GLU D . n 
D 1 164 TYR 164 164 164 TYR TYR D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LEU 166 166 166 LEU LEU D . n 
D 1 167 ASN 167 167 167 ASN ASN D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 TYR 169 169 169 TYR TYR D . n 
D 1 170 PHE 170 170 170 PHE PHE D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ILE 172 172 172 ILE ILE D . n 
D 1 173 ILE 173 173 173 ILE ILE D . n 
D 1 174 LYS 174 174 174 LYS LYS D . n 
D 1 175 LYS 175 175 175 LYS LYS D . n 
D 1 176 THR 176 176 176 THR THR D . n 
D 1 177 LEU 177 177 177 LEU LEU D . n 
D 1 178 SER 178 178 178 SER SER D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 TYR 180 180 180 TYR TYR D . n 
D 1 181 ARG 181 181 181 ARG ARG D . n 
D 1 182 GLU 182 182 182 GLU GLU D . n 
D 1 183 ILE 183 183 183 ILE ILE D . n 
D 1 184 LYS 184 184 184 LYS LYS D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 GLU 186 186 186 GLU GLU D . n 
D 1 187 GLY 187 187 187 GLY GLY D . n 
D 1 188 LYS 188 188 188 LYS LYS D . n 
D 1 189 GLY 189 189 189 GLY GLY D . n 
D 1 190 SER 190 190 190 SER SER D . n 
D 1 191 VAL 191 191 191 VAL VAL D . n 
D 1 192 SER 192 192 192 SER SER D . n 
D 1 193 THR 193 193 193 THR THR D . n 
D 1 194 SER 194 194 194 SER SER D . n 
D 1 195 PRO 195 195 195 PRO PRO D . n 
D 1 196 TYR 196 196 196 TYR TYR D . n 
D 1 197 TYR 197 197 197 TYR TYR D . n 
D 1 198 HIS 198 198 198 HIS HIS D . n 
D 1 199 PRO 199 199 199 PRO PRO D . n 
D 1 200 LEU 200 200 200 LEU LEU D . n 
D 1 201 ILE 201 201 201 ILE ILE D . n 
D 1 202 PRO 202 202 202 PRO PRO D . n 
D 1 203 ILE 203 203 203 ILE ILE D . n 
D 1 204 LEU 204 204 204 LEU LEU D . n 
D 1 205 LEU 205 205 205 LEU LEU D . n 
D 1 206 ASN 206 206 206 ASN ASN D . n 
D 1 207 PRO 207 207 207 PRO PRO D . n 
D 1 208 ASN 208 208 208 ASN ASN D . n 
D 1 209 CYS 209 209 209 CYS CYS D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 TYR 211 211 211 TYR TYR D . n 
D 1 212 GLU 212 212 212 GLU GLU D . n 
D 1 213 THR 213 213 213 THR THR D . n 
D 1 214 THR 214 214 214 THR THR D . n 
D 1 215 PRO 215 215 215 PRO PRO D . n 
D 1 216 ASN 216 216 216 ASN ASN D . n 
D 1 217 VAL 217 217 217 VAL VAL D . n 
D 1 218 LYS 218 218 218 LYS LYS D . n 
D 1 219 ILE 219 219 219 ILE ILE D . n 
D 1 220 PRO 220 220 220 PRO PRO D . n 
D 1 221 ASP 221 221 221 ASP ASP D . n 
D 1 222 PHE 222 222 222 PHE PHE D . n 
D 1 223 ALA 223 223 223 ALA ALA D . n 
D 1 224 VAL 224 224 224 VAL VAL D . n 
D 1 225 SER 225 225 225 SER SER D . n 
D 1 226 PHE 226 226 226 PHE PHE D . n 
D 1 227 ARG 227 227 227 ARG ARG D . n 
D 1 228 GLU 228 228 228 GLU GLU D . n 
D 1 229 ASP 229 229 229 ASP ASP D . n 
D 1 230 ALA 230 230 230 ALA ALA D . n 
D 1 231 SER 231 231 231 SER SER D . n 
D 1 232 LYS 232 232 232 LYS LYS D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 VAL 234 234 234 VAL VAL D . n 
D 1 235 GLU 235 235 235 GLU GLU D . n 
D 1 236 LEU 236 236 236 LEU LEU D . n 
D 1 237 ALA 237 237 237 ALA ALA D . n 
D 1 238 LYS 238 238 238 LYS LYS D . n 
D 1 239 GLU 239 239 239 GLU GLU D . n 
D 1 240 LYS 240 240 240 LYS LYS D . n 
D 1 241 TYR 241 241 241 TYR TYR D . n 
D 1 242 PHE 242 242 242 PHE PHE D . n 
D 1 243 GLU 243 243 243 GLU GLU D . n 
D 1 244 ILE 244 244 244 ILE ILE D . n 
D 1 245 PHE 245 245 245 PHE PHE D . n 
D 1 246 GLY 246 246 246 GLY GLY D . n 
D 1 247 GLU 247 247 247 GLU GLU D . n 
D 1 248 HIS 248 248 248 HIS HIS D . n 
D 1 249 PRO 249 249 249 PRO PRO D . n 
D 1 250 VAL 250 250 250 VAL VAL D . n 
D 1 251 TYR 251 251 251 TYR TYR D . n 
D 1 252 MET 252 252 252 MET MET D . n 
D 1 253 TRP 253 253 253 TRP TRP D . n 
D 1 254 PRO 254 254 254 PRO PRO D . n 
D 1 255 PRO 255 255 255 PRO PRO D . n 
D 1 256 GLU 256 256 256 GLU GLU D . n 
D 1 257 ALA 257 257 257 ALA ALA D . n 
D 1 258 SER 258 258 258 SER SER D . n 
D 1 259 VAL 259 259 259 VAL VAL D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 ASN 261 261 261 ASN ASN D . n 
D 1 262 GLU 262 262 262 GLU GLU D . n 
D 1 263 ALA 263 263 263 ALA ALA D . n 
D 1 264 LEU 264 264 264 LEU LEU D . n 
D 1 265 GLU 265 265 265 GLU GLU D . n 
D 1 266 LEU 266 266 266 LEU LEU D . n 
D 1 267 TYR 267 267 267 TYR TYR D . n 
D 1 268 TYR 268 268 268 TYR TYR D . n 
D 1 269 GLU 269 269 269 GLU GLU D . n 
D 1 270 LYS 270 270 270 LYS LYS D . n 
D 1 271 GLY 271 271 271 GLY GLY D . n 
D 1 272 ILE 272 272 272 ILE ILE D . n 
D 1 273 ASN 273 273 273 ASN ASN D . n 
D 1 274 MET 274 274 274 MET MET D . n 
D 1 275 LEU 275 275 275 LEU LEU D . n 
D 1 276 ALA 276 276 276 ALA ALA D . n 
D 1 277 THR 277 277 277 THR THR D . n 
D 1 278 ASP 278 278 278 ASP ASP D . n 
D 1 279 GLU 279 279 279 GLU GLU D . n 
D 1 280 VAL 280 280 280 VAL VAL D . n 
D 1 281 ILE 281 281 281 ILE ILE D . n 
D 1 282 LEU 282 282 282 LEU LEU D . n 
D 1 283 LYS 283 283 283 LYS LYS D . n 
D 1 284 ASN 284 284 284 ASN ASN D . n 
D 1 285 SER 285 285 285 SER SER D . n 
D 1 286 VAL 286 286 286 VAL VAL D . n 
D 1 287 GLU 287 287 287 GLU GLU D . n 
D 1 288 ARG 288 288 288 ARG ARG D . n 
D 1 289 ALA 289 289 289 ALA ALA D . n 
D 1 290 SER 290 290 290 SER SER D . n 
D 1 291 PRO 291 291 291 PRO PRO D . n 
D 1 292 TYR 292 292 292 TYR TYR D . n 
D 1 293 LEU 293 293 293 LEU LEU D . n 
D 1 294 ARG 294 294 294 ARG ARG D . n 
D 1 295 TYR 295 295 295 TYR TYR D . n 
D 1 296 TYR 296 296 296 TYR TYR D . n 
D 1 297 PHE 297 297 297 PHE PHE D . n 
D 1 298 ARG 298 298 298 ARG ARG D . n 
D 1 299 GLU 299 299 299 GLU GLU D . n 
D 1 300 LEU 300 300 300 LEU LEU D . n 
D 1 301 ILE 301 301 301 ILE ILE D . n 
D 1 302 SER 302 302 302 SER SER D . n 
D 1 303 VAL 303 303 303 VAL VAL D . n 
D 1 304 PHE 304 304 304 PHE PHE D . n 
D 1 305 PHE 305 305 305 PHE PHE D . n 
D 1 306 ARG 306 306 306 ARG ARG D . n 
D 1 307 ASP 307 307 307 ASP ASP D . n 
D 1 308 LYS 308 308 308 LYS LYS D . n 
D 1 309 THR 309 309 309 THR THR D . n 
D 1 310 LEU 310 310 310 LEU LEU D . n 
D 1 311 SER 311 311 311 SER SER D . n 
D 1 312 ASP 312 312 312 ASP ASP D . n 
D 1 313 LEU 313 313 313 LEU LEU D . n 
D 1 314 ILE 314 314 314 ILE ILE D . n 
D 1 315 GLY 315 315 315 GLY GLY D . n 
D 1 316 PHE 316 316 316 PHE PHE D . n 
D 1 317 SER 317 317 317 SER SER D . n 
D 1 318 TYR 318 318 318 TYR TYR D . n 
D 1 319 HIS 319 319 319 HIS HIS D . n 
D 1 320 ALA 320 320 320 ALA ALA D . n 
D 1 321 TRP 321 321 321 TRP TRP D . n 
D 1 322 ASN 322 322 322 ASN ASN D . n 
D 1 323 ALA 323 323 323 ALA ALA D . n 
D 1 324 GLU 324 324 324 GLU GLU D . n 
D 1 325 ASP 325 325 325 ASP ASP D . n 
D 1 326 ALA 326 326 326 ALA ALA D . n 
D 1 327 VAL 327 327 327 VAL VAL D . n 
D 1 328 ARG 328 328 328 ARG ARG D . n 
D 1 329 ASP 329 329 329 ASP ASP D . n 
D 1 330 PHE 330 330 330 PHE PHE D . n 
D 1 331 ILE 331 331 331 ILE ILE D . n 
D 1 332 GLY 332 332 332 GLY GLY D . n 
D 1 333 ARG 333 333 333 ARG ARG D . n 
D 1 334 LEU 334 334 334 LEU LEU D . n 
D 1 335 LYS 335 335 335 LYS LYS D . n 
D 1 336 LYS 336 336 336 LYS LYS D . n 
D 1 337 ILE 337 337 337 ILE ILE D . n 
D 1 338 HIS 338 338 338 HIS HIS D . n 
D 1 339 GLU 339 339 339 GLU GLU D . n 
D 1 340 SER 340 340 340 SER SER D . n 
D 1 341 VAL 341 341 341 VAL VAL D . n 
D 1 342 ASP 342 342 342 ASP ASP D . n 
D 1 343 PHE 343 343 343 PHE PHE D . n 
D 1 344 GLN 344 344 344 GLN GLN D . n 
D 1 345 PRO 345 345 345 PRO PRO D . n 
D 1 346 VAL 346 346 346 VAL VAL D . n 
D 1 347 VAL 347 347 347 VAL VAL D . n 
D 1 348 PHE 348 348 348 PHE PHE D . n 
D 1 349 VAL 349 349 349 VAL VAL D . n 
D 1 350 VAL 350 350 350 VAL VAL D . n 
D 1 351 LEU 351 351 351 LEU LEU D . n 
D 1 352 ASN 352 352 352 ASN ASN D . n 
D 1 353 GLY 353 353 353 GLY GLY D . n 
D 1 354 GLU 354 354 354 GLU GLU D . n 
D 1 355 ASN 355 355 355 ASN ASN D . n 
D 1 356 CYS 356 356 356 CYS CYS D . n 
D 1 357 TRP 357 357 357 TRP TRP D . n 
D 1 358 GLU 358 358 358 GLU GLU D . n 
D 1 359 TYR 359 359 359 TYR TYR D . n 
D 1 360 TYR 360 360 360 TYR TYR D . n 
D 1 361 GLU 361 361 361 GLU GLU D . n 
D 1 362 GLU 362 362 362 GLU GLU D . n 
D 1 363 ASN 363 363 363 ASN ASN D . n 
D 1 364 GLY 364 364 364 GLY GLY D . n 
D 1 365 ILE 365 365 365 ILE ILE D . n 
D 1 366 PRO 366 366 366 PRO PRO D . n 
D 1 367 PHE 367 367 367 PHE PHE D . n 
D 1 368 LEU 368 368 368 LEU LEU D . n 
D 1 369 GLU 369 369 369 GLU GLU D . n 
D 1 370 LYS 370 370 370 LYS LYS D . n 
D 1 371 LEU 371 371 371 LEU LEU D . n 
D 1 372 TYR 372 372 372 TYR TYR D . n 
D 1 373 SER 373 373 373 SER SER D . n 
D 1 374 THR 374 374 374 THR THR D . n 
D 1 375 LEU 375 375 375 LEU LEU D . n 
D 1 376 GLU 376 376 376 GLU GLU D . n 
D 1 377 LYS 377 377 377 LYS LYS D . n 
D 1 378 GLU 378 378 378 GLU GLU D . n 
D 1 379 GLU 379 379 379 GLU GLU D . n 
D 1 380 TRP 380 380 380 TRP TRP D . n 
D 1 381 ILE 381 381 381 ILE ILE D . n 
D 1 382 GLU 382 382 382 GLU GLU D . n 
D 1 383 THR 383 383 383 THR THR D . n 
D 1 384 LEU 384 384 384 LEU LEU D . n 
D 1 385 THR 385 385 385 THR THR D . n 
D 1 386 LEU 386 386 386 LEU LEU D . n 
D 1 387 GLU 387 387 387 GLU GLU D . n 
D 1 388 GLU 388 388 388 GLU GLU D . n 
D 1 389 ALA 389 389 389 ALA ALA D . n 
D 1 390 MET 390 390 390 MET MET D . n 
D 1 391 ARG 391 391 391 ARG ARG D . n 
D 1 392 LYS 392 392 392 LYS LYS D . n 
D 1 393 GLU 393 393 393 GLU GLU D . n 
D 1 394 ASP 394 394 394 ASP ASP D . n 
D 1 395 VAL 395 395 395 VAL VAL D . n 
D 1 396 LYS 396 396 396 LYS LYS D . n 
D 1 397 THR 397 397 397 THR THR D . n 
D 1 398 GLU 398 398 398 GLU GLU D . n 
D 1 399 VAL 399 399 399 VAL VAL D . n 
D 1 400 ILE 400 400 400 ILE ILE D . n 
D 1 401 GLU 401 401 401 GLU GLU D . n 
D 1 402 SER 402 402 402 SER SER D . n 
D 1 403 VAL 403 403 403 VAL VAL D . n 
D 1 404 LYS 404 404 404 LYS LYS D . n 
D 1 405 ALA 405 405 405 ALA ALA D . n 
D 1 406 GLY 406 406 406 GLY GLY D . n 
D 1 407 THR 407 407 407 THR THR D . n 
D 1 408 TRP 408 408 408 TRP TRP D . n 
D 1 409 PHE 409 409 409 PHE PHE D . n 
D 1 410 ASP 410 410 410 ASP ASP D . n 
D 1 411 GLY 411 411 411 GLY GLY D . n 
D 1 412 ASN 412 412 412 ASN ASN D . n 
D 1 413 PHE 413 413 413 PHE PHE D . n 
D 1 414 LEU 414 414 414 LEU LEU D . n 
D 1 415 LYS 415 415 415 LYS LYS D . n 
D 1 416 TRP 416 416 416 TRP TRP D . n 
D 1 417 ILE 417 417 417 ILE ILE D . n 
D 1 418 GLY 418 418 418 GLY GLY D . n 
D 1 419 ASN 419 419 419 ASN ASN D . n 
D 1 420 LYS 420 420 420 LYS LYS D . n 
D 1 421 GLU 421 421 421 GLU GLU D . n 
D 1 422 LYS 422 422 422 LYS LYS D . n 
D 1 423 ASN 423 423 423 ASN ASN D . n 
D 1 424 GLU 424 424 424 GLU GLU D . n 
D 1 425 TYR 425 425 425 TYR TYR D . n 
D 1 426 TRP 426 426 426 TRP TRP D . n 
D 1 427 LYS 427 427 427 LYS LYS D . n 
D 1 428 ILE 428 428 428 ILE ILE D . n 
D 1 429 LEU 429 429 429 LEU LEU D . n 
D 1 430 ILE 430 430 430 ILE ILE D . n 
D 1 431 GLU 431 431 431 GLU GLU D . n 
D 1 432 ALA 432 432 432 ALA ALA D . n 
D 1 433 LYS 433 433 433 LYS LYS D . n 
D 1 434 LYS 434 434 434 LYS LYS D . n 
D 1 435 LYS 435 435 435 LYS LYS D . n 
D 1 436 ALA 436 436 436 ALA ALA D . n 
D 1 437 LYS 437 437 437 LYS LYS D . n 
D 1 438 ASN 438 438 438 ASN ASN D . n 
D 1 439 ASP 439 439 439 ASP ASP D . n 
D 1 440 TYR 440 440 440 TYR TYR D . n 
D 1 441 ILE 441 441 441 ILE ILE D . n 
D 1 442 LEU 442 442 442 LEU LEU D . n 
D 1 443 VAL 443 443 443 VAL VAL D . n 
D 1 444 ALA 444 444 444 ALA ALA D . n 
D 1 445 GLU 445 445 445 GLU GLU D . n 
D 1 446 GLY 446 446 446 GLY GLY D . n 
D 1 447 SER 447 447 447 SER SER D . n 
D 1 448 ASP 448 448 448 ASP ASP D . n 
D 1 449 TRP 449 449 449 TRP TRP D . n 
D 1 450 PHE 450 450 450 PHE PHE D . n 
D 1 451 TRP 451 451 451 TRP TRP D . n 
D 1 452 TRP 452 452 452 TRP TRP D . n 
D 1 453 GLN 453 453 453 GLN GLN D . n 
D 1 454 GLY 454 454 454 GLY GLY D . n 
D 1 455 GLU 455 455 455 GLU GLU D . n 
D 1 456 GLU 456 456 456 GLU GLU D . n 
D 1 457 LYS 457 457 457 LYS LYS D . n 
D 1 458 ALA 458 458 458 ALA ALA D . n 
D 1 459 PRO 459 459 459 PRO PRO D . n 
D 1 460 PHE 460 460 460 PHE PHE D . n 
D 1 461 VAL 461 461 461 VAL VAL D . n 
D 1 462 GLU 462 462 462 GLU GLU D . n 
D 1 463 VAL 463 463 463 VAL VAL D . n 
D 1 464 PHE 464 464 464 PHE PHE D . n 
D 1 465 ASP 465 465 465 ASP ASP D . n 
D 1 466 LYS 466 466 466 LYS LYS D . n 
D 1 467 LEU 467 467 467 LEU LEU D . n 
D 1 468 PHE 468 468 468 PHE PHE D . n 
D 1 469 ARG 469 469 469 ARG ARG D . n 
D 1 470 SER 470 470 470 SER SER D . n 
D 1 471 PHE 471 471 471 PHE PHE D . n 
D 1 472 VAL 472 472 472 VAL VAL D . n 
D 1 473 ARG 473 473 473 ARG ARG D . n 
D 1 474 ARG 474 474 474 ARG ARG D . n 
D 1 475 ALA 475 475 475 ALA ALA D . n 
D 1 476 GLN 476 476 476 GLN GLN D . n 
D 1 477 GLU 477 477 477 GLU GLU 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 GLC 1 E GLC 6 E GLC 1 n 
E 2 GLC 2 E GLC 7 E GLC 2 n 
E 2 GLC 3 E GLC 8 E GLC 3 n 
E 2 GLC 4 E GLC 1 E GLC 4 n 
E 2 GLC 5 E GLC 2 E GLC 5 n 
E 2 GLC 6 E GLC 3 E GLC 6 n 
E 2 GLC 7 E GLC 4 E GLC 7 n 
E 2 GLC 8 E GLC 5 E GLC 8 n 
F 2 GLC 1 F GLC 6 F GLC 1 n 
F 2 GLC 2 F GLC 7 F GLC 2 n 
F 2 GLC 3 F GLC 8 F GLC 3 n 
F 2 GLC 4 F GLC 1 F GLC 4 n 
F 2 GLC 5 F GLC 2 F GLC 5 n 
F 2 GLC 6 F GLC 3 F GLC 6 n 
F 2 GLC 7 F GLC 4 F GLC 7 n 
F 2 GLC 8 F GLC 5 F GLC 8 n 
G 2 GLC 1 G GLC 6 G GLC 1 n 
G 2 GLC 2 G GLC 7 G GLC 2 n 
G 2 GLC 3 G GLC 8 G GLC 3 n 
G 2 GLC 4 G GLC 1 G GLC 4 n 
G 2 GLC 5 G GLC 2 G GLC 5 n 
G 2 GLC 6 G GLC 3 G GLC 6 n 
G 2 GLC 7 G GLC 4 G GLC 7 n 
G 2 GLC 8 G GLC 5 G GLC 8 n 
H 2 GLC 1 H GLC 6 H GLC 1 n 
H 2 GLC 2 H GLC 7 H GLC 2 n 
H 2 GLC 3 H GLC 8 H GLC 3 n 
H 2 GLC 4 H GLC 1 H GLC 4 n 
H 2 GLC 5 H GLC 2 H GLC 5 n 
H 2 GLC 6 H GLC 3 H GLC 6 n 
H 2 GLC 7 H GLC 4 H GLC 7 n 
H 2 GLC 8 H GLC 5 H GLC 8 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GLC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GLC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 GOL 1   501 501 GOL GOL A . 
J  3 GOL 1   502 505 GOL GOL A . 
K  3 GOL 1   503 506 GOL GOL A . 
L  4 PEG 1   504 511 PEG PEG A . 
M  4 PEG 1   505 512 PEG PEG A . 
N  5 EDO 1   506 521 EDO EDO A . 
O  5 EDO 1   507 522 EDO EDO A . 
P  5 EDO 1   508 523 EDO EDO A . 
Q  3 GOL 1   501 501 GOL GOL B . 
R  3 GOL 1   502 502 GOL GOL B . 
S  4 PEG 1   503 511 PEG PEG B . 
T  5 EDO 1   504 516 EDO EDO B . 
U  5 EDO 1   505 517 EDO EDO B . 
V  5 EDO 1   506 518 EDO EDO B . 
W  5 EDO 1   501 524 EDO EDO C . 
X  4 PEG 1   502 511 PEG PEG C . 
Y  3 GOL 1   501 501 GOL GOL D . 
Z  6 HOH 1   601 265 HOH HOH A . 
Z  6 HOH 2   602 626 HOH HOH A . 
Z  6 HOH 3   603 658 HOH HOH A . 
Z  6 HOH 4   604 474 HOH HOH A . 
Z  6 HOH 5   605 556 HOH HOH A . 
Z  6 HOH 6   606 558 HOH HOH A . 
Z  6 HOH 7   607 410 HOH HOH A . 
Z  6 HOH 8   608 255 HOH HOH A . 
Z  6 HOH 9   609 498 HOH HOH A . 
Z  6 HOH 10  610 197 HOH HOH A . 
Z  6 HOH 11  611 124 HOH HOH A . 
Z  6 HOH 12  612 642 HOH HOH A . 
Z  6 HOH 13  613 465 HOH HOH A . 
Z  6 HOH 14  614 141 HOH HOH A . 
Z  6 HOH 15  615 64  HOH HOH A . 
Z  6 HOH 16  616 224 HOH HOH A . 
Z  6 HOH 17  617 94  HOH HOH A . 
Z  6 HOH 18  618 572 HOH HOH A . 
Z  6 HOH 19  619 376 HOH HOH A . 
Z  6 HOH 20  620 298 HOH HOH A . 
Z  6 HOH 21  621 458 HOH HOH A . 
Z  6 HOH 22  622 42  HOH HOH A . 
Z  6 HOH 23  623 59  HOH HOH A . 
Z  6 HOH 24  624 413 HOH HOH A . 
Z  6 HOH 25  625 660 HOH HOH A . 
Z  6 HOH 26  626 32  HOH HOH A . 
Z  6 HOH 27  627 528 HOH HOH A . 
Z  6 HOH 28  628 66  HOH HOH A . 
Z  6 HOH 29  629 5   HOH HOH A . 
Z  6 HOH 30  630 24  HOH HOH A . 
Z  6 HOH 31  631 531 HOH HOH A . 
Z  6 HOH 32  632 25  HOH HOH A . 
Z  6 HOH 33  633 221 HOH HOH A . 
Z  6 HOH 34  634 17  HOH HOH A . 
Z  6 HOH 35  635 291 HOH HOH A . 
Z  6 HOH 36  636 136 HOH HOH A . 
Z  6 HOH 37  637 23  HOH HOH A . 
Z  6 HOH 38  638 29  HOH HOH A . 
Z  6 HOH 39  639 311 HOH HOH A . 
Z  6 HOH 40  640 22  HOH HOH A . 
Z  6 HOH 41  641 547 HOH HOH A . 
Z  6 HOH 42  642 125 HOH HOH A . 
Z  6 HOH 43  643 661 HOH HOH A . 
Z  6 HOH 44  644 68  HOH HOH A . 
Z  6 HOH 45  645 421 HOH HOH A . 
Z  6 HOH 46  646 243 HOH HOH A . 
Z  6 HOH 47  647 361 HOH HOH A . 
Z  6 HOH 48  648 183 HOH HOH A . 
Z  6 HOH 49  649 326 HOH HOH A . 
Z  6 HOH 50  650 88  HOH HOH A . 
Z  6 HOH 51  651 91  HOH HOH A . 
Z  6 HOH 52  652 581 HOH HOH A . 
Z  6 HOH 53  653 109 HOH HOH A . 
Z  6 HOH 54  654 4   HOH HOH A . 
Z  6 HOH 55  655 181 HOH HOH A . 
Z  6 HOH 56  656 132 HOH HOH A . 
Z  6 HOH 57  657 194 HOH HOH A . 
Z  6 HOH 58  658 510 HOH HOH A . 
Z  6 HOH 59  659 391 HOH HOH A . 
Z  6 HOH 60  660 592 HOH HOH A . 
Z  6 HOH 61  661 13  HOH HOH A . 
Z  6 HOH 62  662 476 HOH HOH A . 
Z  6 HOH 63  663 143 HOH HOH A . 
Z  6 HOH 64  664 62  HOH HOH A . 
Z  6 HOH 65  665 381 HOH HOH A . 
Z  6 HOH 66  666 216 HOH HOH A . 
Z  6 HOH 67  667 14  HOH HOH A . 
Z  6 HOH 68  668 215 HOH HOH A . 
Z  6 HOH 69  669 562 HOH HOH A . 
Z  6 HOH 70  670 240 HOH HOH A . 
Z  6 HOH 71  671 126 HOH HOH A . 
Z  6 HOH 72  672 622 HOH HOH A . 
Z  6 HOH 73  673 436 HOH HOH A . 
Z  6 HOH 74  674 307 HOH HOH A . 
Z  6 HOH 75  675 418 HOH HOH A . 
Z  6 HOH 76  676 317 HOH HOH A . 
Z  6 HOH 77  677 244 HOH HOH A . 
Z  6 HOH 78  678 460 HOH HOH A . 
Z  6 HOH 79  679 43  HOH HOH A . 
Z  6 HOH 80  680 122 HOH HOH A . 
Z  6 HOH 81  681 26  HOH HOH A . 
Z  6 HOH 82  682 3   HOH HOH A . 
Z  6 HOH 83  683 82  HOH HOH A . 
Z  6 HOH 84  684 248 HOH HOH A . 
Z  6 HOH 85  685 448 HOH HOH A . 
Z  6 HOH 86  686 568 HOH HOH A . 
Z  6 HOH 87  687 272 HOH HOH A . 
Z  6 HOH 88  688 233 HOH HOH A . 
Z  6 HOH 89  689 69  HOH HOH A . 
Z  6 HOH 90  690 6   HOH HOH A . 
Z  6 HOH 91  691 21  HOH HOH A . 
Z  6 HOH 92  692 550 HOH HOH A . 
Z  6 HOH 93  693 117 HOH HOH A . 
Z  6 HOH 94  694 617 HOH HOH A . 
Z  6 HOH 95  695 401 HOH HOH A . 
Z  6 HOH 96  696 8   HOH HOH A . 
Z  6 HOH 97  697 327 HOH HOH A . 
Z  6 HOH 98  698 543 HOH HOH A . 
Z  6 HOH 99  699 499 HOH HOH A . 
Z  6 HOH 100 700 589 HOH HOH A . 
Z  6 HOH 101 701 292 HOH HOH A . 
Z  6 HOH 102 702 345 HOH HOH A . 
Z  6 HOH 103 703 18  HOH HOH A . 
Z  6 HOH 104 704 99  HOH HOH A . 
Z  6 HOH 105 705 387 HOH HOH A . 
Z  6 HOH 106 706 28  HOH HOH A . 
Z  6 HOH 107 707 582 HOH HOH A . 
Z  6 HOH 108 708 526 HOH HOH A . 
Z  6 HOH 109 709 437 HOH HOH A . 
Z  6 HOH 110 710 315 HOH HOH A . 
Z  6 HOH 111 711 159 HOH HOH A . 
Z  6 HOH 112 712 420 HOH HOH A . 
Z  6 HOH 113 713 65  HOH HOH A . 
Z  6 HOH 114 714 110 HOH HOH A . 
Z  6 HOH 115 715 360 HOH HOH A . 
Z  6 HOH 116 716 2   HOH HOH A . 
Z  6 HOH 117 717 290 HOH HOH A . 
Z  6 HOH 118 718 250 HOH HOH A . 
Z  6 HOH 119 719 443 HOH HOH A . 
Z  6 HOH 120 720 296 HOH HOH A . 
Z  6 HOH 121 721 253 HOH HOH A . 
Z  6 HOH 122 722 103 HOH HOH A . 
Z  6 HOH 123 723 79  HOH HOH A . 
Z  6 HOH 124 724 336 HOH HOH A . 
Z  6 HOH 125 725 284 HOH HOH A . 
Z  6 HOH 126 726 633 HOH HOH A . 
Z  6 HOH 127 727 238 HOH HOH A . 
Z  6 HOH 128 728 78  HOH HOH A . 
Z  6 HOH 129 729 140 HOH HOH A . 
Z  6 HOH 130 730 512 HOH HOH A . 
Z  6 HOH 131 731 93  HOH HOH A . 
Z  6 HOH 132 732 409 HOH HOH A . 
Z  6 HOH 133 733 175 HOH HOH A . 
Z  6 HOH 134 734 485 HOH HOH A . 
Z  6 HOH 135 735 210 HOH HOH A . 
Z  6 HOH 136 736 350 HOH HOH A . 
Z  6 HOH 137 737 306 HOH HOH A . 
Z  6 HOH 138 738 218 HOH HOH A . 
Z  6 HOH 139 739 527 HOH HOH A . 
Z  6 HOH 140 740 31  HOH HOH A . 
Z  6 HOH 141 741 201 HOH HOH A . 
Z  6 HOH 142 742 507 HOH HOH A . 
Z  6 HOH 143 743 319 HOH HOH A . 
Z  6 HOH 144 744 515 HOH HOH A . 
Z  6 HOH 145 745 189 HOH HOH A . 
Z  6 HOH 146 746 289 HOH HOH A . 
Z  6 HOH 147 747 405 HOH HOH A . 
Z  6 HOH 148 748 591 HOH HOH A . 
Z  6 HOH 149 749 567 HOH HOH A . 
Z  6 HOH 150 750 637 HOH HOH A . 
Z  6 HOH 151 751 429 HOH HOH A . 
Z  6 HOH 152 752 417 HOH HOH A . 
Z  6 HOH 153 753 619 HOH HOH A . 
Z  6 HOH 154 754 480 HOH HOH A . 
Z  6 HOH 155 755 625 HOH HOH A . 
Z  6 HOH 156 756 277 HOH HOH A . 
Z  6 HOH 157 757 259 HOH HOH A . 
Z  6 HOH 158 758 308 HOH HOH A . 
Z  6 HOH 159 759 561 HOH HOH A . 
Z  6 HOH 160 760 332 HOH HOH A . 
Z  6 HOH 161 761 481 HOH HOH A . 
Z  6 HOH 162 762 286 HOH HOH A . 
Z  6 HOH 163 763 129 HOH HOH A . 
Z  6 HOH 164 764 587 HOH HOH A . 
Z  6 HOH 165 765 228 HOH HOH A . 
Z  6 HOH 166 766 341 HOH HOH A . 
Z  6 HOH 167 767 539 HOH HOH A . 
Z  6 HOH 168 768 139 HOH HOH A . 
Z  6 HOH 169 769 349 HOH HOH A . 
Z  6 HOH 170 770 338 HOH HOH A . 
Z  6 HOH 171 771 412 HOH HOH A . 
Z  6 HOH 172 772 440 HOH HOH A . 
Z  6 HOH 173 773 239 HOH HOH A . 
Z  6 HOH 174 774 333 HOH HOH A . 
Z  6 HOH 175 775 295 HOH HOH A . 
Z  6 HOH 176 776 262 HOH HOH A . 
Z  6 HOH 177 777 580 HOH HOH A . 
Z  6 HOH 178 778 397 HOH HOH A . 
Z  6 HOH 179 779 247 HOH HOH A . 
Z  6 HOH 180 780 623 HOH HOH A . 
Z  6 HOH 181 781 537 HOH HOH A . 
Z  6 HOH 182 782 631 HOH HOH A . 
Z  6 HOH 183 783 484 HOH HOH A . 
Z  6 HOH 184 784 365 HOH HOH A . 
Z  6 HOH 185 785 652 HOH HOH A . 
Z  6 HOH 186 786 644 HOH HOH A . 
Z  6 HOH 187 787 497 HOH HOH A . 
Z  6 HOH 188 788 508 HOH HOH A . 
Z  6 HOH 189 789 457 HOH HOH A . 
Z  6 HOH 190 790 487 HOH HOH A . 
Z  6 HOH 191 791 548 HOH HOH A . 
Z  6 HOH 192 792 278 HOH HOH A . 
Z  6 HOH 193 793 621 HOH HOH A . 
AA 6 HOH 1   601 533 HOH HOH B . 
AA 6 HOH 2   602 203 HOH HOH B . 
AA 6 HOH 3   603 371 HOH HOH B . 
AA 6 HOH 4   604 473 HOH HOH B . 
AA 6 HOH 5   605 597 HOH HOH B . 
AA 6 HOH 6   606 256 HOH HOH B . 
AA 6 HOH 7   607 557 HOH HOH B . 
AA 6 HOH 8   608 358 HOH HOH B . 
AA 6 HOH 9   609 80  HOH HOH B . 
AA 6 HOH 10  610 30  HOH HOH B . 
AA 6 HOH 11  611 70  HOH HOH B . 
AA 6 HOH 12  612 450 HOH HOH B . 
AA 6 HOH 13  613 225 HOH HOH B . 
AA 6 HOH 14  614 586 HOH HOH B . 
AA 6 HOH 15  615 85  HOH HOH B . 
AA 6 HOH 16  616 50  HOH HOH B . 
AA 6 HOH 17  617 193 HOH HOH B . 
AA 6 HOH 18  618 662 HOH HOH B . 
AA 6 HOH 19  619 583 HOH HOH B . 
AA 6 HOH 20  620 172 HOH HOH B . 
AA 6 HOH 21  621 102 HOH HOH B . 
AA 6 HOH 22  622 81  HOH HOH B . 
AA 6 HOH 23  623 276 HOH HOH B . 
AA 6 HOH 24  624 196 HOH HOH B . 
AA 6 HOH 25  625 185 HOH HOH B . 
AA 6 HOH 26  626 380 HOH HOH B . 
AA 6 HOH 27  627 97  HOH HOH B . 
AA 6 HOH 28  628 127 HOH HOH B . 
AA 6 HOH 29  629 166 HOH HOH B . 
AA 6 HOH 30  630 513 HOH HOH B . 
AA 6 HOH 31  631 135 HOH HOH B . 
AA 6 HOH 32  632 607 HOH HOH B . 
AA 6 HOH 33  633 9   HOH HOH B . 
AA 6 HOH 34  634 200 HOH HOH B . 
AA 6 HOH 35  635 399 HOH HOH B . 
AA 6 HOH 36  636 180 HOH HOH B . 
AA 6 HOH 37  637 137 HOH HOH B . 
AA 6 HOH 38  638 10  HOH HOH B . 
AA 6 HOH 39  639 223 HOH HOH B . 
AA 6 HOH 40  640 227 HOH HOH B . 
AA 6 HOH 41  641 525 HOH HOH B . 
AA 6 HOH 42  642 395 HOH HOH B . 
AA 6 HOH 43  643 636 HOH HOH B . 
AA 6 HOH 44  644 7   HOH HOH B . 
AA 6 HOH 45  645 343 HOH HOH B . 
AA 6 HOH 46  646 552 HOH HOH B . 
AA 6 HOH 47  647 232 HOH HOH B . 
AA 6 HOH 48  648 518 HOH HOH B . 
AA 6 HOH 49  649 41  HOH HOH B . 
AA 6 HOH 50  650 11  HOH HOH B . 
AA 6 HOH 51  651 77  HOH HOH B . 
AA 6 HOH 52  652 74  HOH HOH B . 
AA 6 HOH 53  653 431 HOH HOH B . 
AA 6 HOH 54  654 35  HOH HOH B . 
AA 6 HOH 55  655 164 HOH HOH B . 
AA 6 HOH 56  656 639 HOH HOH B . 
AA 6 HOH 57  657 640 HOH HOH B . 
AA 6 HOH 58  658 406 HOH HOH B . 
AA 6 HOH 59  659 53  HOH HOH B . 
AA 6 HOH 60  660 33  HOH HOH B . 
AA 6 HOH 61  661 163 HOH HOH B . 
AA 6 HOH 62  662 177 HOH HOH B . 
AA 6 HOH 63  663 456 HOH HOH B . 
AA 6 HOH 64  664 269 HOH HOH B . 
AA 6 HOH 65  665 309 HOH HOH B . 
AA 6 HOH 66  666 220 HOH HOH B . 
AA 6 HOH 67  667 54  HOH HOH B . 
AA 6 HOH 68  668 340 HOH HOH B . 
AA 6 HOH 69  669 104 HOH HOH B . 
AA 6 HOH 70  670 151 HOH HOH B . 
AA 6 HOH 71  671 388 HOH HOH B . 
AA 6 HOH 72  672 500 HOH HOH B . 
AA 6 HOH 73  673 106 HOH HOH B . 
AA 6 HOH 74  674 39  HOH HOH B . 
AA 6 HOH 75  675 347 HOH HOH B . 
AA 6 HOH 76  676 187 HOH HOH B . 
AA 6 HOH 77  677 115 HOH HOH B . 
AA 6 HOH 78  678 45  HOH HOH B . 
AA 6 HOH 79  679 263 HOH HOH B . 
AA 6 HOH 80  680 491 HOH HOH B . 
AA 6 HOH 81  681 101 HOH HOH B . 
AA 6 HOH 82  682 297 HOH HOH B . 
AA 6 HOH 83  683 207 HOH HOH B . 
AA 6 HOH 84  684 569 HOH HOH B . 
AA 6 HOH 85  685 202 HOH HOH B . 
AA 6 HOH 86  686 300 HOH HOH B . 
AA 6 HOH 87  687 392 HOH HOH B . 
AA 6 HOH 88  688 461 HOH HOH B . 
AA 6 HOH 89  689 246 HOH HOH B . 
AA 6 HOH 90  690 294 HOH HOH B . 
AA 6 HOH 91  691 258 HOH HOH B . 
AA 6 HOH 92  692 305 HOH HOH B . 
AA 6 HOH 93  693 226 HOH HOH B . 
AA 6 HOH 94  694 205 HOH HOH B . 
AA 6 HOH 95  695 463 HOH HOH B . 
AA 6 HOH 96  696 86  HOH HOH B . 
AA 6 HOH 97  697 199 HOH HOH B . 
AA 6 HOH 98  698 425 HOH HOH B . 
AA 6 HOH 99  699 575 HOH HOH B . 
AA 6 HOH 100 700 449 HOH HOH B . 
AA 6 HOH 101 701 605 HOH HOH B . 
AA 6 HOH 102 702 439 HOH HOH B . 
AA 6 HOH 103 703 134 HOH HOH B . 
AA 6 HOH 104 704 363 HOH HOH B . 
AA 6 HOH 105 705 482 HOH HOH B . 
AA 6 HOH 106 706 58  HOH HOH B . 
AA 6 HOH 107 707 128 HOH HOH B . 
AA 6 HOH 108 708 19  HOH HOH B . 
AA 6 HOH 109 709 432 HOH HOH B . 
AA 6 HOH 110 710 452 HOH HOH B . 
AA 6 HOH 111 711 468 HOH HOH B . 
AA 6 HOH 112 712 145 HOH HOH B . 
AA 6 HOH 113 713 344 HOH HOH B . 
AA 6 HOH 114 714 608 HOH HOH B . 
AA 6 HOH 115 715 469 HOH HOH B . 
AA 6 HOH 116 716 657 HOH HOH B . 
AA 6 HOH 117 717 274 HOH HOH B . 
AA 6 HOH 118 718 374 HOH HOH B . 
AA 6 HOH 119 719 540 HOH HOH B . 
AA 6 HOH 120 720 595 HOH HOH B . 
AA 6 HOH 121 721 179 HOH HOH B . 
AA 6 HOH 122 722 123 HOH HOH B . 
AA 6 HOH 123 723 516 HOH HOH B . 
AA 6 HOH 124 724 495 HOH HOH B . 
AA 6 HOH 125 725 362 HOH HOH B . 
AA 6 HOH 126 726 604 HOH HOH B . 
AA 6 HOH 127 727 546 HOH HOH B . 
AA 6 HOH 128 728 641 HOH HOH B . 
AA 6 HOH 129 729 650 HOH HOH B . 
AA 6 HOH 130 730 113 HOH HOH B . 
AA 6 HOH 131 731 496 HOH HOH B . 
AA 6 HOH 132 732 184 HOH HOH B . 
AA 6 HOH 133 733 612 HOH HOH B . 
AA 6 HOH 134 734 377 HOH HOH B . 
AA 6 HOH 135 735 459 HOH HOH B . 
AA 6 HOH 136 736 375 HOH HOH B . 
AA 6 HOH 137 737 649 HOH HOH B . 
AA 6 HOH 138 738 519 HOH HOH B . 
AA 6 HOH 139 739 603 HOH HOH B . 
AA 6 HOH 140 740 447 HOH HOH B . 
AA 6 HOH 141 741 150 HOH HOH B . 
AA 6 HOH 142 742 182 HOH HOH B . 
AA 6 HOH 143 743 160 HOH HOH B . 
AA 6 HOH 144 744 544 HOH HOH B . 
AA 6 HOH 145 745 407 HOH HOH B . 
AA 6 HOH 146 746 466 HOH HOH B . 
AA 6 HOH 147 747 651 HOH HOH B . 
AA 6 HOH 148 748 521 HOH HOH B . 
AA 6 HOH 149 749 478 HOH HOH B . 
AA 6 HOH 150 750 635 HOH HOH B . 
AA 6 HOH 151 751 455 HOH HOH B . 
AA 6 HOH 152 752 534 HOH HOH B . 
AA 6 HOH 153 753 275 HOH HOH B . 
AA 6 HOH 154 754 663 HOH HOH B . 
AA 6 HOH 155 755 467 HOH HOH B . 
AA 6 HOH 156 756 337 HOH HOH B . 
AA 6 HOH 157 757 370 HOH HOH B . 
AA 6 HOH 158 758 511 HOH HOH B . 
AA 6 HOH 159 759 599 HOH HOH B . 
AA 6 HOH 160 760 588 HOH HOH B . 
AA 6 HOH 161 761 609 HOH HOH B . 
AA 6 HOH 162 762 400 HOH HOH B . 
AA 6 HOH 163 763 280 HOH HOH B . 
AA 6 HOH 164 764 268 HOH HOH B . 
AA 6 HOH 165 765 357 HOH HOH B . 
AA 6 HOH 166 766 520 HOH HOH B . 
AA 6 HOH 167 767 169 HOH HOH B . 
AA 6 HOH 168 768 270 HOH HOH B . 
AA 6 HOH 169 769 541 HOH HOH B . 
AA 6 HOH 170 770 632 HOH HOH B . 
BA 6 HOH 1   601 378 HOH HOH C . 
BA 6 HOH 2   602 606 HOH HOH C . 
BA 6 HOH 3   603 394 HOH HOH C . 
BA 6 HOH 4   604 488 HOH HOH C . 
BA 6 HOH 5   605 67  HOH HOH C . 
BA 6 HOH 6   606 271 HOH HOH C . 
BA 6 HOH 7   607 282 HOH HOH C . 
BA 6 HOH 8   608 382 HOH HOH C . 
BA 6 HOH 9   609 211 HOH HOH C . 
BA 6 HOH 10  610 630 HOH HOH C . 
BA 6 HOH 11  611 523 HOH HOH C . 
BA 6 HOH 12  612 236 HOH HOH C . 
BA 6 HOH 13  613 89  HOH HOH C . 
BA 6 HOH 14  614 237 HOH HOH C . 
BA 6 HOH 15  615 334 HOH HOH C . 
BA 6 HOH 16  616 142 HOH HOH C . 
BA 6 HOH 17  617 368 HOH HOH C . 
BA 6 HOH 18  618 261 HOH HOH C . 
BA 6 HOH 19  619 426 HOH HOH C . 
BA 6 HOH 20  620 505 HOH HOH C . 
BA 6 HOH 21  621 47  HOH HOH C . 
BA 6 HOH 22  622 195 HOH HOH C . 
BA 6 HOH 23  623 339 HOH HOH C . 
BA 6 HOH 24  624 628 HOH HOH C . 
BA 6 HOH 25  625 108 HOH HOH C . 
BA 6 HOH 26  626 423 HOH HOH C . 
BA 6 HOH 27  627 312 HOH HOH C . 
BA 6 HOH 28  628 71  HOH HOH C . 
BA 6 HOH 29  629 107 HOH HOH C . 
BA 6 HOH 30  630 156 HOH HOH C . 
BA 6 HOH 31  631 167 HOH HOH C . 
BA 6 HOH 32  632 61  HOH HOH C . 
BA 6 HOH 33  633 112 HOH HOH C . 
BA 6 HOH 34  634 213 HOH HOH C . 
BA 6 HOH 35  635 146 HOH HOH C . 
BA 6 HOH 36  636 83  HOH HOH C . 
BA 6 HOH 37  637 170 HOH HOH C . 
BA 6 HOH 38  638 408 HOH HOH C . 
BA 6 HOH 39  639 173 HOH HOH C . 
BA 6 HOH 40  640 545 HOH HOH C . 
BA 6 HOH 41  641 34  HOH HOH C . 
BA 6 HOH 42  642 314 HOH HOH C . 
BA 6 HOH 43  643 98  HOH HOH C . 
BA 6 HOH 44  644 155 HOH HOH C . 
BA 6 HOH 45  645 489 HOH HOH C . 
BA 6 HOH 46  646 165 HOH HOH C . 
BA 6 HOH 47  647 551 HOH HOH C . 
BA 6 HOH 48  648 36  HOH HOH C . 
BA 6 HOH 49  649 486 HOH HOH C . 
BA 6 HOH 50  650 313 HOH HOH C . 
BA 6 HOH 51  651 27  HOH HOH C . 
BA 6 HOH 52  652 147 HOH HOH C . 
BA 6 HOH 53  653 171 HOH HOH C . 
BA 6 HOH 54  654 234 HOH HOH C . 
BA 6 HOH 55  655 161 HOH HOH C . 
BA 6 HOH 56  656 288 HOH HOH C . 
BA 6 HOH 57  657 446 HOH HOH C . 
BA 6 HOH 58  658 84  HOH HOH C . 
BA 6 HOH 59  659 178 HOH HOH C . 
BA 6 HOH 60  660 492 HOH HOH C . 
BA 6 HOH 61  661 442 HOH HOH C . 
BA 6 HOH 62  662 404 HOH HOH C . 
BA 6 HOH 63  663 464 HOH HOH C . 
BA 6 HOH 64  664 542 HOH HOH C . 
BA 6 HOH 65  665 48  HOH HOH C . 
BA 6 HOH 66  666 114 HOH HOH C . 
BA 6 HOH 67  667 416 HOH HOH C . 
BA 6 HOH 68  668 279 HOH HOH C . 
BA 6 HOH 69  669 411 HOH HOH C . 
BA 6 HOH 70  670 509 HOH HOH C . 
BA 6 HOH 71  671 656 HOH HOH C . 
BA 6 HOH 72  672 571 HOH HOH C . 
BA 6 HOH 73  673 230 HOH HOH C . 
BA 6 HOH 74  674 590 HOH HOH C . 
BA 6 HOH 75  675 643 HOH HOH C . 
BA 6 HOH 76  676 573 HOH HOH C . 
BA 6 HOH 77  677 252 HOH HOH C . 
BA 6 HOH 78  678 120 HOH HOH C . 
BA 6 HOH 79  679 445 HOH HOH C . 
BA 6 HOH 80  680 602 HOH HOH C . 
BA 6 HOH 81  681 283 HOH HOH C . 
BA 6 HOH 82  682 251 HOH HOH C . 
BA 6 HOH 83  683 254 HOH HOH C . 
BA 6 HOH 84  684 346 HOH HOH C . 
BA 6 HOH 85  685 287 HOH HOH C . 
BA 6 HOH 86  686 506 HOH HOH C . 
BA 6 HOH 87  687 655 HOH HOH C . 
BA 6 HOH 88  688 273 HOH HOH C . 
BA 6 HOH 89  689 616 HOH HOH C . 
BA 6 HOH 90  690 593 HOH HOH C . 
BA 6 HOH 91  691 435 HOH HOH C . 
BA 6 HOH 92  692 162 HOH HOH C . 
BA 6 HOH 93  693 601 HOH HOH C . 
BA 6 HOH 94  694 281 HOH HOH C . 
BA 6 HOH 95  695 594 HOH HOH C . 
BA 6 HOH 96  696 323 HOH HOH C . 
BA 6 HOH 97  697 462 HOH HOH C . 
BA 6 HOH 98  698 454 HOH HOH C . 
BA 6 HOH 99  699 549 HOH HOH C . 
BA 6 HOH 100 700 502 HOH HOH C . 
BA 6 HOH 101 701 600 HOH HOH C . 
BA 6 HOH 102 702 219 HOH HOH C . 
BA 6 HOH 103 703 372 HOH HOH C . 
BA 6 HOH 104 704 564 HOH HOH C . 
BA 6 HOH 105 705 398 HOH HOH C . 
BA 6 HOH 106 706 585 HOH HOH C . 
BA 6 HOH 107 707 356 HOH HOH C . 
CA 6 HOH 1   601 638 HOH HOH D . 
CA 6 HOH 2   602 532 HOH HOH D . 
CA 6 HOH 3   603 198 HOH HOH D . 
CA 6 HOH 4   604 49  HOH HOH D . 
CA 6 HOH 5   605 352 HOH HOH D . 
CA 6 HOH 6   606 438 HOH HOH D . 
CA 6 HOH 7   607 55  HOH HOH D . 
CA 6 HOH 8   608 318 HOH HOH D . 
CA 6 HOH 9   609 168 HOH HOH D . 
CA 6 HOH 10  610 95  HOH HOH D . 
CA 6 HOH 11  611 324 HOH HOH D . 
CA 6 HOH 12  612 40  HOH HOH D . 
CA 6 HOH 13  613 596 HOH HOH D . 
CA 6 HOH 14  614 302 HOH HOH D . 
CA 6 HOH 15  615 559 HOH HOH D . 
CA 6 HOH 16  616 316 HOH HOH D . 
CA 6 HOH 17  617 15  HOH HOH D . 
CA 6 HOH 18  618 260 HOH HOH D . 
CA 6 HOH 19  619 624 HOH HOH D . 
CA 6 HOH 20  620 422 HOH HOH D . 
CA 6 HOH 21  621 176 HOH HOH D . 
CA 6 HOH 22  622 330 HOH HOH D . 
CA 6 HOH 23  623 373 HOH HOH D . 
CA 6 HOH 24  624 659 HOH HOH D . 
CA 6 HOH 25  625 52  HOH HOH D . 
CA 6 HOH 26  626 353 HOH HOH D . 
CA 6 HOH 27  627 217 HOH HOH D . 
CA 6 HOH 28  628 529 HOH HOH D . 
CA 6 HOH 29  629 119 HOH HOH D . 
CA 6 HOH 30  630 212 HOH HOH D . 
CA 6 HOH 31  631 427 HOH HOH D . 
CA 6 HOH 32  632 257 HOH HOH D . 
CA 6 HOH 33  633 133 HOH HOH D . 
CA 6 HOH 34  634 229 HOH HOH D . 
CA 6 HOH 35  635 331 HOH HOH D . 
CA 6 HOH 36  636 111 HOH HOH D . 
CA 6 HOH 37  637 304 HOH HOH D . 
CA 6 HOH 38  638 647 HOH HOH D . 
CA 6 HOH 39  639 118 HOH HOH D . 
CA 6 HOH 40  640 214 HOH HOH D . 
CA 6 HOH 41  641 57  HOH HOH D . 
CA 6 HOH 42  642 96  HOH HOH D . 
CA 6 HOH 43  643 266 HOH HOH D . 
CA 6 HOH 44  644 51  HOH HOH D . 
CA 6 HOH 45  645 451 HOH HOH D . 
CA 6 HOH 46  646 56  HOH HOH D . 
CA 6 HOH 47  647 472 HOH HOH D . 
CA 6 HOH 48  648 242 HOH HOH D . 
CA 6 HOH 49  649 174 HOH HOH D . 
CA 6 HOH 50  650 191 HOH HOH D . 
CA 6 HOH 51  651 192 HOH HOH D . 
CA 6 HOH 52  652 12  HOH HOH D . 
CA 6 HOH 53  653 73  HOH HOH D . 
CA 6 HOH 54  654 190 HOH HOH D . 
CA 6 HOH 55  655 46  HOH HOH D . 
CA 6 HOH 56  656 348 HOH HOH D . 
CA 6 HOH 57  657 149 HOH HOH D . 
CA 6 HOH 58  658 38  HOH HOH D . 
CA 6 HOH 59  659 501 HOH HOH D . 
CA 6 HOH 60  660 76  HOH HOH D . 
CA 6 HOH 61  661 477 HOH HOH D . 
CA 6 HOH 62  662 614 HOH HOH D . 
CA 6 HOH 63  663 188 HOH HOH D . 
CA 6 HOH 64  664 301 HOH HOH D . 
CA 6 HOH 65  665 144 HOH HOH D . 
CA 6 HOH 66  666 16  HOH HOH D . 
CA 6 HOH 67  667 154 HOH HOH D . 
CA 6 HOH 68  668 116 HOH HOH D . 
CA 6 HOH 69  669 629 HOH HOH D . 
CA 6 HOH 70  670 158 HOH HOH D . 
CA 6 HOH 71  671 37  HOH HOH D . 
CA 6 HOH 72  672 354 HOH HOH D . 
CA 6 HOH 73  673 646 HOH HOH D . 
CA 6 HOH 74  674 20  HOH HOH D . 
CA 6 HOH 75  675 367 HOH HOH D . 
CA 6 HOH 76  676 503 HOH HOH D . 
CA 6 HOH 77  677 44  HOH HOH D . 
CA 6 HOH 78  678 209 HOH HOH D . 
CA 6 HOH 79  679 574 HOH HOH D . 
CA 6 HOH 80  680 208 HOH HOH D . 
CA 6 HOH 81  681 130 HOH HOH D . 
CA 6 HOH 82  682 235 HOH HOH D . 
CA 6 HOH 83  683 355 HOH HOH D . 
CA 6 HOH 84  684 186 HOH HOH D . 
CA 6 HOH 85  685 328 HOH HOH D . 
CA 6 HOH 86  686 138 HOH HOH D . 
CA 6 HOH 87  687 267 HOH HOH D . 
CA 6 HOH 88  688 321 HOH HOH D . 
CA 6 HOH 89  689 1   HOH HOH D . 
CA 6 HOH 90  690 415 HOH HOH D . 
CA 6 HOH 91  691 584 HOH HOH D . 
CA 6 HOH 92  692 153 HOH HOH D . 
CA 6 HOH 93  693 653 HOH HOH D . 
CA 6 HOH 94  694 90  HOH HOH D . 
CA 6 HOH 95  695 402 HOH HOH D . 
CA 6 HOH 96  696 204 HOH HOH D . 
CA 6 HOH 97  697 222 HOH HOH D . 
CA 6 HOH 98  698 63  HOH HOH D . 
CA 6 HOH 99  699 75  HOH HOH D . 
CA 6 HOH 100 700 148 HOH HOH D . 
CA 6 HOH 101 701 393 HOH HOH D . 
CA 6 HOH 102 702 87  HOH HOH D . 
CA 6 HOH 103 703 285 HOH HOH D . 
CA 6 HOH 104 704 579 HOH HOH D . 
CA 6 HOH 105 705 389 HOH HOH D . 
CA 6 HOH 106 706 553 HOH HOH D . 
CA 6 HOH 107 707 60  HOH HOH D . 
CA 6 HOH 108 708 483 HOH HOH D . 
CA 6 HOH 109 709 325 HOH HOH D . 
CA 6 HOH 110 710 366 HOH HOH D . 
CA 6 HOH 111 711 157 HOH HOH D . 
CA 6 HOH 112 712 121 HOH HOH D . 
CA 6 HOH 113 713 72  HOH HOH D . 
CA 6 HOH 114 714 92  HOH HOH D . 
CA 6 HOH 115 715 419 HOH HOH D . 
CA 6 HOH 116 716 322 HOH HOH D . 
CA 6 HOH 117 717 264 HOH HOH D . 
CA 6 HOH 118 718 555 HOH HOH D . 
CA 6 HOH 119 719 554 HOH HOH D . 
CA 6 HOH 120 720 206 HOH HOH D . 
CA 6 HOH 121 721 131 HOH HOH D . 
CA 6 HOH 122 722 414 HOH HOH D . 
CA 6 HOH 123 723 335 HOH HOH D . 
CA 6 HOH 124 724 610 HOH HOH D . 
CA 6 HOH 125 725 479 HOH HOH D . 
CA 6 HOH 126 726 329 HOH HOH D . 
CA 6 HOH 127 727 504 HOH HOH D . 
CA 6 HOH 128 728 100 HOH HOH D . 
CA 6 HOH 129 729 396 HOH HOH D . 
CA 6 HOH 130 730 249 HOH HOH D . 
CA 6 HOH 131 731 538 HOH HOH D . 
CA 6 HOH 132 732 611 HOH HOH D . 
CA 6 HOH 133 733 385 HOH HOH D . 
CA 6 HOH 134 734 535 HOH HOH D . 
CA 6 HOH 135 735 299 HOH HOH D . 
CA 6 HOH 136 736 471 HOH HOH D . 
CA 6 HOH 137 737 383 HOH HOH D . 
CA 6 HOH 138 738 241 HOH HOH D . 
CA 6 HOH 139 739 384 HOH HOH D . 
CA 6 HOH 140 740 620 HOH HOH D . 
CA 6 HOH 141 741 524 HOH HOH D . 
CA 6 HOH 142 742 654 HOH HOH D . 
CA 6 HOH 143 743 379 HOH HOH D . 
CA 6 HOH 144 744 578 HOH HOH D . 
CA 6 HOH 145 745 470 HOH HOH D . 
CA 6 HOH 146 746 105 HOH HOH D . 
CA 6 HOH 147 747 615 HOH HOH D . 
CA 6 HOH 148 748 152 HOH HOH D . 
CA 6 HOH 149 749 364 HOH HOH D . 
CA 6 HOH 150 750 390 HOH HOH D . 
CA 6 HOH 151 751 369 HOH HOH D . 
CA 6 HOH 152 752 627 HOH HOH D . 
CA 6 HOH 153 753 494 HOH HOH D . 
CA 6 HOH 154 754 536 HOH HOH D . 
CA 6 HOH 155 755 293 HOH HOH D . 
CA 6 HOH 156 756 563 HOH HOH D . 
CA 6 HOH 157 757 403 HOH HOH D . 
CA 6 HOH 158 758 645 HOH HOH D . 
CA 6 HOH 159 759 359 HOH HOH D . 
CA 6 HOH 160 760 434 HOH HOH D . 
CA 6 HOH 161 761 598 HOH HOH D . 
CA 6 HOH 162 762 522 HOH HOH D . 
CA 6 HOH 163 763 576 HOH HOH D . 
CA 6 HOH 164 764 433 HOH HOH D . 
CA 6 HOH 165 765 514 HOH HOH D . 
CA 6 HOH 166 766 577 HOH HOH D . 
CA 6 HOH 167 767 618 HOH HOH D . 
CA 6 HOH 168 768 475 HOH HOH D . 
CA 6 HOH 169 769 444 HOH HOH D . 
CA 6 HOH 170 770 386 HOH HOH D . 
CA 6 HOH 171 771 342 HOH HOH D . 
CA 6 HOH 172 772 566 HOH HOH D . 
CA 6 HOH 173 773 245 HOH HOH D . 
CA 6 HOH 174 774 490 HOH HOH D . 
CA 6 HOH 175 775 565 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 71  ? CG  ? A LYS 71  CG  
2  1 Y 1 A LYS 71  ? CD  ? A LYS 71  CD  
3  1 Y 1 A LYS 71  ? CE  ? A LYS 71  CE  
4  1 Y 1 A LYS 71  ? NZ  ? A LYS 71  NZ  
5  1 Y 1 A GLU 120 ? CG  ? A GLU 120 CG  
6  1 Y 1 A GLU 120 ? CD  ? A GLU 120 CD  
7  1 Y 1 A GLU 120 ? OE1 ? A GLU 120 OE1 
8  1 Y 1 A GLU 120 ? OE2 ? A GLU 120 OE2 
9  1 Y 1 A LYS 121 ? CG  ? A LYS 121 CG  
10 1 Y 1 A LYS 121 ? CD  ? A LYS 121 CD  
11 1 Y 1 A LYS 121 ? CE  ? A LYS 121 CE  
12 1 Y 1 A LYS 121 ? NZ  ? A LYS 121 NZ  
13 1 Y 1 A GLU 379 ? CG  ? A GLU 379 CG  
14 1 Y 1 A GLU 379 ? CD  ? A GLU 379 CD  
15 1 Y 1 A GLU 379 ? OE1 ? A GLU 379 OE1 
16 1 Y 1 A GLU 379 ? OE2 ? A GLU 379 OE2 
17 1 Y 1 A GLU 456 ? CG  ? A GLU 456 CG  
18 1 Y 1 A GLU 456 ? CD  ? A GLU 456 CD  
19 1 Y 1 A GLU 456 ? OE1 ? A GLU 456 OE1 
20 1 Y 1 A GLU 456 ? OE2 ? A GLU 456 OE2 
21 1 Y 1 A LYS 457 ? CG  ? A LYS 457 CG  
22 1 Y 1 A LYS 457 ? CD  ? A LYS 457 CD  
23 1 Y 1 A LYS 457 ? CE  ? A LYS 457 CE  
24 1 Y 1 A LYS 457 ? NZ  ? A LYS 457 NZ  
25 1 Y 1 B LYS 71  ? CG  ? B LYS 71  CG  
26 1 Y 1 B LYS 71  ? CD  ? B LYS 71  CD  
27 1 Y 1 B LYS 71  ? CE  ? B LYS 71  CE  
28 1 Y 1 B LYS 71  ? NZ  ? B LYS 71  NZ  
29 1 Y 1 B GLU 120 ? CG  ? B GLU 120 CG  
30 1 Y 1 B GLU 120 ? CD  ? B GLU 120 CD  
31 1 Y 1 B GLU 120 ? OE1 ? B GLU 120 OE1 
32 1 Y 1 B GLU 120 ? OE2 ? B GLU 120 OE2 
33 1 Y 1 B LYS 121 ? CG  ? B LYS 121 CG  
34 1 Y 1 B LYS 121 ? CD  ? B LYS 121 CD  
35 1 Y 1 B LYS 121 ? CE  ? B LYS 121 CE  
36 1 Y 1 B LYS 121 ? NZ  ? B LYS 121 NZ  
37 1 Y 1 B GLU 379 ? CG  ? B GLU 379 CG  
38 1 Y 1 B GLU 379 ? CD  ? B GLU 379 CD  
39 1 Y 1 B GLU 379 ? OE1 ? B GLU 379 OE1 
40 1 Y 1 B GLU 379 ? OE2 ? B GLU 379 OE2 
41 1 Y 1 B GLU 456 ? CG  ? B GLU 456 CG  
42 1 Y 1 B GLU 456 ? CD  ? B GLU 456 CD  
43 1 Y 1 B GLU 456 ? OE1 ? B GLU 456 OE1 
44 1 Y 1 B GLU 456 ? OE2 ? B GLU 456 OE2 
45 1 Y 1 B LYS 457 ? CG  ? B LYS 457 CG  
46 1 Y 1 B LYS 457 ? CD  ? B LYS 457 CD  
47 1 Y 1 B LYS 457 ? CE  ? B LYS 457 CE  
48 1 Y 1 B LYS 457 ? NZ  ? B LYS 457 NZ  
49 1 Y 1 C LYS 71  ? CG  ? C LYS 71  CG  
50 1 Y 1 C LYS 71  ? CD  ? C LYS 71  CD  
51 1 Y 1 C LYS 71  ? CE  ? C LYS 71  CE  
52 1 Y 1 C LYS 71  ? NZ  ? C LYS 71  NZ  
53 1 Y 1 C GLU 120 ? CG  ? C GLU 120 CG  
54 1 Y 1 C GLU 120 ? CD  ? C GLU 120 CD  
55 1 Y 1 C GLU 120 ? OE1 ? C GLU 120 OE1 
56 1 Y 1 C GLU 120 ? OE2 ? C GLU 120 OE2 
57 1 Y 1 C LYS 121 ? CG  ? C LYS 121 CG  
58 1 Y 1 C LYS 121 ? CD  ? C LYS 121 CD  
59 1 Y 1 C LYS 121 ? CE  ? C LYS 121 CE  
60 1 Y 1 C LYS 121 ? NZ  ? C LYS 121 NZ  
61 1 Y 1 C GLU 379 ? CG  ? C GLU 379 CG  
62 1 Y 1 C GLU 379 ? CD  ? C GLU 379 CD  
63 1 Y 1 C GLU 379 ? OE1 ? C GLU 379 OE1 
64 1 Y 1 C GLU 379 ? OE2 ? C GLU 379 OE2 
65 1 Y 1 C GLU 456 ? CG  ? C GLU 456 CG  
66 1 Y 1 C GLU 456 ? CD  ? C GLU 456 CD  
67 1 Y 1 C GLU 456 ? OE1 ? C GLU 456 OE1 
68 1 Y 1 C GLU 456 ? OE2 ? C GLU 456 OE2 
69 1 Y 1 C LYS 457 ? CG  ? C LYS 457 CG  
70 1 Y 1 C LYS 457 ? CD  ? C LYS 457 CD  
71 1 Y 1 C LYS 457 ? CE  ? C LYS 457 CE  
72 1 Y 1 C LYS 457 ? NZ  ? C LYS 457 NZ  
73 1 Y 1 D LYS 71  ? CG  ? D LYS 71  CG  
74 1 Y 1 D LYS 71  ? CD  ? D LYS 71  CD  
75 1 Y 1 D LYS 71  ? CE  ? D LYS 71  CE  
76 1 Y 1 D LYS 71  ? NZ  ? D LYS 71  NZ  
77 1 Y 1 D GLU 120 ? CG  ? D GLU 120 CG  
78 1 Y 1 D GLU 120 ? CD  ? D GLU 120 CD  
79 1 Y 1 D GLU 120 ? OE1 ? D GLU 120 OE1 
80 1 Y 1 D GLU 120 ? OE2 ? D GLU 120 OE2 
81 1 Y 1 D LYS 121 ? CG  ? D LYS 121 CG  
82 1 Y 1 D LYS 121 ? CD  ? D LYS 121 CD  
83 1 Y 1 D LYS 121 ? CE  ? D LYS 121 CE  
84 1 Y 1 D LYS 121 ? NZ  ? D LYS 121 NZ  
85 1 Y 1 D GLU 379 ? CG  ? D GLU 379 CG  
86 1 Y 1 D GLU 379 ? CD  ? D GLU 379 CD  
87 1 Y 1 D GLU 379 ? OE1 ? D GLU 379 OE1 
88 1 Y 1 D GLU 379 ? OE2 ? D GLU 379 OE2 
89 1 Y 1 D GLU 456 ? CG  ? D GLU 456 CG  
90 1 Y 1 D GLU 456 ? CD  ? D GLU 456 CD  
91 1 Y 1 D GLU 456 ? OE1 ? D GLU 456 OE1 
92 1 Y 1 D GLU 456 ? OE2 ? D GLU 456 OE2 
93 1 Y 1 D LYS 457 ? CG  ? D LYS 457 CG  
94 1 Y 1 D LYS 457 ? CD  ? D LYS 457 CD  
95 1 Y 1 D LYS 457 ? CE  ? D LYS 457 CE  
96 1 Y 1 D LYS 457 ? NZ  ? D LYS 457 NZ  
# 
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  ? ? ? '(1.13_2998: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  4 
# 
_cell.angle_alpha                  83.94 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   88.85 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  89.09 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KYR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     40.830 
_cell.length_a_esd                 ? 
_cell.length_b                     61.530 
_cell.length_b_esd                 ? 
_cell.length_c                     195.400 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9KYR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   9KYR 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.28 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Sodium citrate, pH 4.2, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            338 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_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         2024-11-10 
_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   0.97918 
_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                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KYR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.89 
_reflns.d_resolution_low                               64.76 
_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                                     143351 
_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                           94.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.92 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.217 
_reflns.pdbx_Rpim_I_all                                0.116 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       492924 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.989 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.182 
_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                                    1.89 
_reflns_shell.d_res_low                                     1.94 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           35725 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10495 
_reflns_shell.percent_possible_obs                          92.8 
_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                               3.4 
_reflns_shell.pdbx_chi_squared                              0.96 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               2.622 
_reflns_shell.pdbx_Rpim_I_all                               1.396 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.320 
_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                                  2.210 
_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                                 9KYR 
_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                            1.890 
_refine.ls_d_res_low                             24.329 
_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                     143024 
_refine.ls_number_reflns_R_free                  7281 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.48 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1948 
_refine.ls_R_factor_R_free                       0.2346 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1926 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.96 
_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             1.11 
_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                 28.07 
_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                            0.27 
_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                       1.890 
_refine_hist.d_res_low                        24.329 
_refine_hist.number_atoms_solvent             645 
_refine_hist.number_atoms_total               17177 
_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        16088 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         444 
_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' ? 0.008 ? 17040 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.955 ? 23086 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.698 ? 14169 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053 ? 2500  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 2846  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 1.8900 1.9115 . . 225 4428 91.00 . . . . 0.3741 . . . . . . . . . . . . . . . 0.4012 
'X-RAY DIFFRACTION' 1.9115 1.9340 . . 212 4400 91.00 . . . . 0.3569 . . . . . . . . . . . . . . . 0.4238 
'X-RAY DIFFRACTION' 1.9340 1.9575 . . 228 4516 94.00 . . . . 0.3156 . . . . . . . . . . . . . . . 0.3297 
'X-RAY DIFFRACTION' 1.9575 1.9823 . . 232 4624 96.00 . . . . 0.2929 . . . . . . . . . . . . . . . 0.3316 
'X-RAY DIFFRACTION' 1.9823 2.0084 . . 237 4531 95.00 . . . . 0.2815 . . . . . . . . . . . . . . . 0.3090 
'X-RAY DIFFRACTION' 2.0084 2.0359 . . 242 4579 94.00 . . . . 0.2780 . . . . . . . . . . . . . . . 0.3279 
'X-RAY DIFFRACTION' 2.0359 2.0649 . . 225 4438 94.00 . . . . 0.2897 . . . . . . . . . . . . . . . 0.3486 
'X-RAY DIFFRACTION' 2.0649 2.0957 . . 257 4486 95.00 . . . . 0.2632 . . . . . . . . . . . . . . . 0.3319 
'X-RAY DIFFRACTION' 2.0957 2.1285 . . 230 4653 96.00 . . . . 0.2358 . . . . . . . . . . . . . . . 0.2604 
'X-RAY DIFFRACTION' 2.1285 2.1633 . . 225 4584 95.00 . . . . 0.2359 . . . . . . . . . . . . . . . 0.2767 
'X-RAY DIFFRACTION' 2.1633 2.2006 . . 251 4586 97.00 . . . . 0.2408 . . . . . . . . . . . . . . . 0.2697 
'X-RAY DIFFRACTION' 2.2006 2.2406 . . 220 4497 94.00 . . . . 0.2521 . . . . . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 2.2406 2.2837 . . 228 4468 92.00 . . . . 0.2404 . . . . . . . . . . . . . . . 0.3249 
'X-RAY DIFFRACTION' 2.2837 2.3303 . . 213 4583 97.00 . . . . 0.2210 . . . . . . . . . . . . . . . 0.2513 
'X-RAY DIFFRACTION' 2.3303 2.3809 . . 263 4613 96.00 . . . . 0.2165 . . . . . . . . . . . . . . . 0.2871 
'X-RAY DIFFRACTION' 2.3809 2.4362 . . 229 4551 96.00 . . . . 0.2233 . . . . . . . . . . . . . . . 0.2937 
'X-RAY DIFFRACTION' 2.4362 2.4971 . . 254 4615 97.00 . . . . 0.2067 . . . . . . . . . . . . . . . 0.2706 
'X-RAY DIFFRACTION' 2.4971 2.5645 . . 239 4630 95.00 . . . . 0.2044 . . . . . . . . . . . . . . . 0.2563 
'X-RAY DIFFRACTION' 2.5645 2.6399 . . 256 4538 96.00 . . . . 0.1982 . . . . . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 2.6399 2.7250 . . 288 4528 95.00 . . . . 0.1937 . . . . . . . . . . . . . . . 0.2433 
'X-RAY DIFFRACTION' 2.7250 2.8223 . . 231 4608 97.00 . . . . 0.2011 . . . . . . . . . . . . . . . 0.2424 
'X-RAY DIFFRACTION' 2.8223 2.9351 . . 254 4583 95.00 . . . . 0.1958 . . . . . . . . . . . . . . . 0.2536 
'X-RAY DIFFRACTION' 2.9351 3.0684 . . 288 4491 96.00 . . . . 0.1935 . . . . . . . . . . . . . . . 0.2604 
'X-RAY DIFFRACTION' 3.0684 3.2298 . . 234 4506 94.00 . . . . 0.1861 . . . . . . . . . . . . . . . 0.2509 
'X-RAY DIFFRACTION' 3.2298 3.4317 . . 226 4446 92.00 . . . . 0.1754 . . . . . . . . . . . . . . . 0.2304 
'X-RAY DIFFRACTION' 3.4317 3.6958 . . 260 4324 91.00 . . . . 0.1638 . . . . . . . . . . . . . . . 0.1917 
'X-RAY DIFFRACTION' 3.6958 4.0662 . . 272 4378 92.00 . . . . 0.1438 . . . . . . . . . . . . . . . 0.1871 
'X-RAY DIFFRACTION' 4.0662 4.6510 . . 289 4417 94.00 . . . . 0.1344 . . . . . . . . . . . . . . . 0.1639 
'X-RAY DIFFRACTION' 4.6510 5.8463 . . 238 4589 96.00 . . . . 0.1444 . . . . . . . . . . . . . . . 0.1706 
'X-RAY DIFFRACTION' 5.8463 24.329 . . 235 4553 95.00 . . . . 0.1595 . . . . . . . . . . . . . . . 0.1921 
# 
_struct.entry_id                     9KYR 
_struct.title                        
'GH57 family amylopullulanase from Aquifex aeolicus D352N mutant complex with gama-cyclodextrin' 
_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        9KYR 
_struct_keywords.text            'GH57 family, amylopullulanase, Aquifex aeolicus, cyclodextrin, 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 3 ? 
K  N N 3 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 5 ? 
O  N N 5 ? 
P  N N 5 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 4 ? 
T  N N 5 ? 
U  N N 5 ? 
V  N N 5 ? 
W  N N 5 ? 
X  N N 4 ? 
Y  N N 3 ? 
Z  N N 6 ? 
AA N N 6 ? 
BA N N 6 ? 
CA N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    O66934_AQUAE 
_struct_ref.pdbx_db_accession          O66934 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9KYR A 1 ? 477 ? O66934 1 ? 477 ? 1 477 
2 1 9KYR B 1 ? 477 ? O66934 1 ? 477 ? 1 477 
3 1 9KYR C 1 ? 477 ? O66934 1 ? 477 ? 1 477 
4 1 9KYR D 1 ? 477 ? O66934 1 ? 477 ? 1 477 
# 
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 9KYR ASN A 352 ? UNP O66934 ASP 352 'engineered mutation' 352 1 
2 9KYR ASN B 352 ? UNP O66934 ASP 352 'engineered mutation' 352 2 
3 9KYR ASN C 352 ? UNP O66934 ASP 352 'engineered mutation' 352 3 
4 9KYR ASN D 352 ? UNP O66934 ASP 352 'engineered mutation' 352 4 
# 
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 
# 
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,Z 
2 1 B,F,Q,R,S,T,U,V,AA    
3 1 C,G,W,X,BA            
4 1 D,H,Y,CA              
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'native gel electrophoresis' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 PRO A 28  ? ASP A 37  ? PRO A 28  ASP A 37  1 ? 10 
HELX_P HELX_P2   AA2 TYR A 39  ? TYR A 44  ? TYR A 39  TYR A 44  1 ? 6  
HELX_P HELX_P3   AA3 LEU A 45  ? ASP A 47  ? LEU A 45  ASP A 47  5 ? 3  
HELX_P HELX_P4   AA4 THR A 57  ? GLN A 69  ? THR A 57  GLN A 69  1 ? 13 
HELX_P HELX_P5   AA5 VAL A 75  ? LYS A 82  ? VAL A 75  LYS A 82  1 ? 8  
HELX_P HELX_P6   AA6 ASP A 83  ? LEU A 87  ? ASP A 83  LEU A 87  5 ? 5  
HELX_P HELX_P7   AA7 GLU A 88  ? TYR A 103 ? GLU A 88  TYR A 103 1 ? 16 
HELX_P HELX_P8   AA8 LYS A 105 ? ARG A 109 ? LYS A 105 ARG A 109 5 ? 5  
HELX_P HELX_P9   AA9 PHE A 110 ? ASN A 118 ? PHE A 110 ASN A 118 1 ? 9  
HELX_P HELX_P10  AB1 ASN A 123 ? TRP A 138 ? ASN A 123 TRP A 138 1 ? 16 
HELX_P HELX_P11  AB2 GLY A 140 ? LEU A 147 ? GLY A 140 LEU A 147 1 ? 8  
HELX_P HELX_P12  AB3 LEU A 147 ? GLY A 154 ? LEU A 147 GLY A 154 1 ? 8  
HELX_P HELX_P13  AB4 THR A 158 ? LYS A 175 ? THR A 158 LYS A 175 1 ? 18 
HELX_P HELX_P14  AB5 LYS A 175 ? GLU A 186 ? LYS A 175 GLU A 186 1 ? 12 
HELX_P HELX_P15  AB6 LEU A 200 ? ASN A 206 ? LEU A 200 ASN A 206 1 ? 7  
HELX_P HELX_P16  AB7 PRO A 207 ? THR A 213 ? PRO A 207 THR A 213 5 ? 7  
HELX_P HELX_P17  AB8 PHE A 226 ? GLY A 246 ? PHE A 226 GLY A 246 1 ? 21 
HELX_P HELX_P18  AB9 PRO A 254 ? SER A 258 ? PRO A 254 SER A 258 5 ? 5  
HELX_P HELX_P19  AC1 SER A 260 ? LYS A 270 ? SER A 260 LYS A 270 1 ? 11 
HELX_P HELX_P20  AC2 ASP A 278 ? VAL A 286 ? ASP A 278 VAL A 286 1 ? 9  
HELX_P HELX_P21  AC3 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P22  AC4 TYR A 318 ? TRP A 321 ? TYR A 318 TRP A 321 5 ? 4  
HELX_P HELX_P23  AC5 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P24  AC6 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P25  AC7 GLY A 364 ? GLU A 376 ? GLY A 364 GLU A 376 1 ? 13 
HELX_P HELX_P26  AC8 THR A 385 ? LYS A 392 ? THR A 385 LYS A 392 1 ? 8  
HELX_P HELX_P27  AC9 ASN A 419 ? LYS A 435 ? ASN A 419 LYS A 435 1 ? 17 
HELX_P HELX_P28  AD1 ASP A 439 ? ALA A 444 ? ASP A 439 ALA A 444 1 ? 6  
HELX_P HELX_P29  AD2 GLY A 446 ? GLN A 453 ? GLY A 446 GLN A 453 1 ? 8  
HELX_P HELX_P30  AD3 PHE A 460 ? ALA A 475 ? PHE A 460 ALA A 475 1 ? 16 
HELX_P HELX_P31  AD4 PRO B 28  ? ASP B 37  ? PRO B 28  ASP B 37  1 ? 10 
HELX_P HELX_P32  AD5 TYR B 39  ? TYR B 44  ? TYR B 39  TYR B 44  1 ? 6  
HELX_P HELX_P33  AD6 LEU B 45  ? ASP B 47  ? LEU B 45  ASP B 47  5 ? 3  
HELX_P HELX_P34  AD7 THR B 57  ? GLN B 69  ? THR B 57  GLN B 69  1 ? 13 
HELX_P HELX_P35  AD8 VAL B 75  ? LYS B 82  ? VAL B 75  LYS B 82  1 ? 8  
HELX_P HELX_P36  AD9 ASP B 83  ? LEU B 87  ? ASP B 83  LEU B 87  5 ? 5  
HELX_P HELX_P37  AE1 GLU B 88  ? TYR B 103 ? GLU B 88  TYR B 103 1 ? 16 
HELX_P HELX_P38  AE2 LYS B 105 ? ARG B 109 ? LYS B 105 ARG B 109 5 ? 5  
HELX_P HELX_P39  AE3 PHE B 110 ? MET B 117 ? PHE B 110 MET B 117 1 ? 8  
HELX_P HELX_P40  AE4 ASN B 123 ? TRP B 138 ? ASN B 123 TRP B 138 1 ? 16 
HELX_P HELX_P41  AE5 GLY B 140 ? LEU B 147 ? GLY B 140 LEU B 147 1 ? 8  
HELX_P HELX_P42  AE6 LEU B 147 ? GLY B 154 ? LEU B 147 GLY B 154 1 ? 8  
HELX_P HELX_P43  AE7 THR B 158 ? LYS B 175 ? THR B 158 LYS B 175 1 ? 18 
HELX_P HELX_P44  AE8 LYS B 175 ? GLU B 186 ? LYS B 175 GLU B 186 1 ? 12 
HELX_P HELX_P45  AE9 LEU B 200 ? ASN B 206 ? LEU B 200 ASN B 206 1 ? 7  
HELX_P HELX_P46  AF1 PRO B 207 ? THR B 213 ? PRO B 207 THR B 213 5 ? 7  
HELX_P HELX_P47  AF2 PHE B 226 ? GLY B 246 ? PHE B 226 GLY B 246 1 ? 21 
HELX_P HELX_P48  AF3 PRO B 254 ? SER B 258 ? PRO B 254 SER B 258 5 ? 5  
HELX_P HELX_P49  AF4 SER B 260 ? LYS B 270 ? SER B 260 LYS B 270 1 ? 11 
HELX_P HELX_P50  AF5 ASP B 278 ? VAL B 286 ? ASP B 278 VAL B 286 1 ? 9  
HELX_P HELX_P51  AF6 ASP B 307 ? SER B 317 ? ASP B 307 SER B 317 1 ? 11 
HELX_P HELX_P52  AF7 TYR B 318 ? TRP B 321 ? TYR B 318 TRP B 321 5 ? 4  
HELX_P HELX_P53  AF8 ASN B 322 ? VAL B 341 ? ASN B 322 VAL B 341 1 ? 20 
HELX_P HELX_P54  AF9 CYS B 356 ? ASN B 363 ? CYS B 356 ASN B 363 5 ? 8  
HELX_P HELX_P55  AG1 GLY B 364 ? GLU B 376 ? GLY B 364 GLU B 376 1 ? 13 
HELX_P HELX_P56  AG2 THR B 385 ? LYS B 392 ? THR B 385 LYS B 392 1 ? 8  
HELX_P HELX_P57  AG3 ASN B 419 ? LYS B 435 ? ASN B 419 LYS B 435 1 ? 17 
HELX_P HELX_P58  AG4 ASP B 439 ? GLU B 445 ? ASP B 439 GLU B 445 1 ? 7  
HELX_P HELX_P59  AG5 GLY B 446 ? GLN B 453 ? GLY B 446 GLN B 453 1 ? 8  
HELX_P HELX_P60  AG6 PHE B 460 ? ALA B 475 ? PHE B 460 ALA B 475 1 ? 16 
HELX_P HELX_P61  AG7 PRO C 28  ? ASP C 37  ? PRO C 28  ASP C 37  1 ? 10 
HELX_P HELX_P62  AG8 TYR C 39  ? TYR C 44  ? TYR C 39  TYR C 44  1 ? 6  
HELX_P HELX_P63  AG9 LEU C 45  ? ASP C 47  ? LEU C 45  ASP C 47  5 ? 3  
HELX_P HELX_P64  AH1 THR C 57  ? GLN C 69  ? THR C 57  GLN C 69  1 ? 13 
HELX_P HELX_P65  AH2 VAL C 75  ? LYS C 82  ? VAL C 75  LYS C 82  1 ? 8  
HELX_P HELX_P66  AH3 ASP C 83  ? LEU C 87  ? ASP C 83  LEU C 87  5 ? 5  
HELX_P HELX_P67  AH4 GLU C 88  ? TYR C 103 ? GLU C 88  TYR C 103 1 ? 16 
HELX_P HELX_P68  AH5 LYS C 105 ? ARG C 109 ? LYS C 105 ARG C 109 5 ? 5  
HELX_P HELX_P69  AH6 PHE C 110 ? MET C 117 ? PHE C 110 MET C 117 1 ? 8  
HELX_P HELX_P70  AH7 ASN C 123 ? TRP C 138 ? ASN C 123 TRP C 138 1 ? 16 
HELX_P HELX_P71  AH8 ARG C 141 ? LYS C 145 ? ARG C 141 LYS C 145 5 ? 5  
HELX_P HELX_P72  AH9 LEU C 147 ? GLY C 154 ? LEU C 147 GLY C 154 1 ? 8  
HELX_P HELX_P73  AI1 THR C 158 ? LYS C 174 ? THR C 158 LYS C 174 1 ? 17 
HELX_P HELX_P74  AI2 LYS C 175 ? GLU C 186 ? LYS C 175 GLU C 186 1 ? 12 
HELX_P HELX_P75  AI3 LEU C 200 ? ASN C 206 ? LEU C 200 ASN C 206 1 ? 7  
HELX_P HELX_P76  AI4 PRO C 207 ? THR C 213 ? PRO C 207 THR C 213 5 ? 7  
HELX_P HELX_P77  AI5 PHE C 226 ? GLY C 246 ? PHE C 226 GLY C 246 1 ? 21 
HELX_P HELX_P78  AI6 PRO C 254 ? SER C 258 ? PRO C 254 SER C 258 5 ? 5  
HELX_P HELX_P79  AI7 SER C 260 ? LYS C 270 ? SER C 260 LYS C 270 1 ? 11 
HELX_P HELX_P80  AI8 ASP C 278 ? VAL C 286 ? ASP C 278 VAL C 286 1 ? 9  
HELX_P HELX_P81  AI9 ASP C 307 ? SER C 317 ? ASP C 307 SER C 317 1 ? 11 
HELX_P HELX_P82  AJ1 TYR C 318 ? TRP C 321 ? TYR C 318 TRP C 321 5 ? 4  
HELX_P HELX_P83  AJ2 ASN C 322 ? VAL C 341 ? ASN C 322 VAL C 341 1 ? 20 
HELX_P HELX_P84  AJ3 CYS C 356 ? ASN C 363 ? CYS C 356 ASN C 363 5 ? 8  
HELX_P HELX_P85  AJ4 GLY C 364 ? LYS C 377 ? GLY C 364 LYS C 377 1 ? 14 
HELX_P HELX_P86  AJ5 THR C 385 ? LYS C 392 ? THR C 385 LYS C 392 1 ? 8  
HELX_P HELX_P87  AJ6 ASN C 419 ? LYS C 435 ? ASN C 419 LYS C 435 1 ? 17 
HELX_P HELX_P88  AJ7 ASP C 439 ? ALA C 444 ? ASP C 439 ALA C 444 1 ? 6  
HELX_P HELX_P89  AJ8 GLY C 446 ? GLN C 453 ? GLY C 446 GLN C 453 1 ? 8  
HELX_P HELX_P90  AJ9 PHE C 460 ? ALA C 475 ? PHE C 460 ALA C 475 1 ? 16 
HELX_P HELX_P91  AK1 PRO D 28  ? ASP D 37  ? PRO D 28  ASP D 37  1 ? 10 
HELX_P HELX_P92  AK2 TYR D 39  ? TYR D 44  ? TYR D 39  TYR D 44  1 ? 6  
HELX_P HELX_P93  AK3 LEU D 45  ? ASP D 47  ? LEU D 45  ASP D 47  5 ? 3  
HELX_P HELX_P94  AK4 THR D 57  ? GLN D 69  ? THR D 57  GLN D 69  1 ? 13 
HELX_P HELX_P95  AK5 VAL D 75  ? LYS D 82  ? VAL D 75  LYS D 82  1 ? 8  
HELX_P HELX_P96  AK6 ASP D 83  ? LEU D 87  ? ASP D 83  LEU D 87  5 ? 5  
HELX_P HELX_P97  AK7 GLU D 88  ? TYR D 103 ? GLU D 88  TYR D 103 1 ? 16 
HELX_P HELX_P98  AK8 LYS D 105 ? ARG D 109 ? LYS D 105 ARG D 109 5 ? 5  
HELX_P HELX_P99  AK9 PHE D 110 ? MET D 117 ? PHE D 110 MET D 117 1 ? 8  
HELX_P HELX_P100 AL1 ASN D 123 ? TRP D 138 ? ASN D 123 TRP D 138 1 ? 16 
HELX_P HELX_P101 AL2 THR D 142 ? LEU D 147 ? THR D 142 LEU D 147 1 ? 6  
HELX_P HELX_P102 AL3 LEU D 147 ? GLY D 154 ? LEU D 147 GLY D 154 1 ? 8  
HELX_P HELX_P103 AL4 THR D 158 ? LYS D 175 ? THR D 158 LYS D 175 1 ? 18 
HELX_P HELX_P104 AL5 LYS D 175 ? GLU D 186 ? LYS D 175 GLU D 186 1 ? 12 
HELX_P HELX_P105 AL6 LEU D 200 ? ASN D 206 ? LEU D 200 ASN D 206 1 ? 7  
HELX_P HELX_P106 AL7 PRO D 207 ? THR D 213 ? PRO D 207 THR D 213 5 ? 7  
HELX_P HELX_P107 AL8 PHE D 226 ? GLY D 246 ? PHE D 226 GLY D 246 1 ? 21 
HELX_P HELX_P108 AL9 PRO D 254 ? SER D 258 ? PRO D 254 SER D 258 5 ? 5  
HELX_P HELX_P109 AM1 SER D 260 ? LYS D 270 ? SER D 260 LYS D 270 1 ? 11 
HELX_P HELX_P110 AM2 ASP D 278 ? VAL D 286 ? ASP D 278 VAL D 286 1 ? 9  
HELX_P HELX_P111 AM3 ASP D 307 ? SER D 317 ? ASP D 307 SER D 317 1 ? 11 
HELX_P HELX_P112 AM4 TYR D 318 ? TRP D 321 ? TYR D 318 TRP D 321 5 ? 4  
HELX_P HELX_P113 AM5 ASN D 322 ? VAL D 341 ? ASN D 322 VAL D 341 1 ? 20 
HELX_P HELX_P114 AM6 CYS D 356 ? ASN D 363 ? CYS D 356 ASN D 363 5 ? 8  
HELX_P HELX_P115 AM7 GLY D 364 ? GLU D 378 ? GLY D 364 GLU D 378 1 ? 15 
HELX_P HELX_P116 AM8 THR D 385 ? LYS D 392 ? THR D 385 LYS D 392 1 ? 8  
HELX_P HELX_P117 AM9 ASN D 419 ? LYS D 435 ? ASN D 419 LYS D 435 1 ? 17 
HELX_P HELX_P118 AN1 ASP D 439 ? GLU D 445 ? ASP D 439 GLU D 445 1 ? 7  
HELX_P HELX_P119 AN2 GLY D 446 ? GLN D 453 ? GLY D 446 GLN D 453 1 ? 8  
HELX_P HELX_P120 AN3 PHE D 460 ? GLN D 476 ? PHE D 460 GLN D 476 1 ? 17 
# 
_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 ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 1 E GLC 2 1_555 ? ? ? ? ? ? ? 1.388 ? ? 
covale2  covale both ? E GLC . C1 ? ? ? 1_555 E GLC . O4 ? ? E GLC 1 E GLC 8 1_555 ? ? ? ? ? ? ? 1.371 ? ? 
covale3  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 2 E GLC 3 1_555 ? ? ? ? ? ? ? 1.423 ? ? 
covale4  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 3 E GLC 4 1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale5  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 4 E GLC 5 1_555 ? ? ? ? ? ? ? 1.452 ? ? 
covale6  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 5 E GLC 6 1_555 ? ? ? ? ? ? ? 1.281 ? ? 
covale7  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 6 E GLC 7 1_555 ? ? ? ? ? ? ? 1.288 ? ? 
covale8  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 7 E GLC 8 1_555 ? ? ? ? ? ? ? 1.359 ? ? 
covale9  covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 1 F GLC 2 1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale10 covale both ? F GLC . C1 ? ? ? 1_555 F GLC . O4 ? ? F GLC 1 F GLC 8 1_555 ? ? ? ? ? ? ? 1.426 ? ? 
covale11 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 2 F GLC 3 1_555 ? ? ? ? ? ? ? 1.443 ? ? 
covale12 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 3 F GLC 4 1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale13 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 4 F GLC 5 1_555 ? ? ? ? ? ? ? 1.458 ? ? 
covale14 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 5 F GLC 6 1_555 ? ? ? ? ? ? ? 1.453 ? ? 
covale15 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 6 F GLC 7 1_555 ? ? ? ? ? ? ? 1.446 ? ? 
covale16 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 7 F GLC 8 1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale17 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 1 G GLC 2 1_555 ? ? ? ? ? ? ? 1.455 ? ? 
covale18 covale both ? G GLC . C1 ? ? ? 1_555 G GLC . O4 ? ? G GLC 1 G GLC 8 1_555 ? ? ? ? ? ? ? 1.447 ? ? 
covale19 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 2 G GLC 3 1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale20 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 3 G GLC 4 1_555 ? ? ? ? ? ? ? 1.455 ? ? 
covale21 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 4 G GLC 5 1_555 ? ? ? ? ? ? ? 1.455 ? ? 
covale22 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 5 G GLC 6 1_555 ? ? ? ? ? ? ? 1.447 ? ? 
covale23 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 6 G GLC 7 1_555 ? ? ? ? ? ? ? 1.433 ? ? 
covale24 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 7 G GLC 8 1_555 ? ? ? ? ? ? ? 1.441 ? ? 
covale25 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 1 H GLC 2 1_555 ? ? ? ? ? ? ? 1.450 ? ? 
covale26 covale both ? H GLC . C1 ? ? ? 1_555 H GLC . O4 ? ? H GLC 1 H GLC 8 1_555 ? ? ? ? ? ? ? 1.460 ? ? 
covale27 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 2 H GLC 3 1_555 ? ? ? ? ? ? ? 1.446 ? ? 
covale28 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 3 H GLC 4 1_555 ? ? ? ? ? ? ? 1.452 ? ? 
covale29 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 4 H GLC 5 1_555 ? ? ? ? ? ? ? 1.457 ? ? 
covale30 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 5 H GLC 6 1_555 ? ? ? ? ? ? ? 1.450 ? ? 
covale31 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 6 H GLC 7 1_555 ? ? ? ? ? ? ? 1.451 ? ? 
covale32 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 7 H GLC 8 1_555 ? ? ? ? ? ? ? 1.449 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 5 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 2 ? 
AB3 ? 5 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
AB6 ? 2 ? 
AB7 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? parallel      
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB2 1 2 ? parallel      
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB3 4 5 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB6 1 2 ? parallel      
AB7 1 2 ? parallel      
AB7 2 3 ? parallel      
AB7 3 4 ? anti-parallel 
AB7 4 5 ? 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 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA1 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA1 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA1 4 VAL A 346 ? ASN A 352 ? VAL A 346 ASN A 352 
AA2 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA2 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA2 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA2 4 ILE A 381 ? THR A 383 ? ILE A 381 THR A 383 
AA3 1 GLU A 24  ? TYR A 25  ? GLU A 24  TYR A 25  
AA3 2 LYS A 73  ? ASP A 74  ? LYS A 73  ASP A 74  
AA4 1 TYR A 251 ? MET A 252 ? TYR A 251 MET A 252 
AA4 2 MET A 274 ? THR A 277 ? MET A 274 THR A 277 
AA4 3 ILE A 301 ? PHE A 305 ? ILE A 301 PHE A 305 
AA4 4 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 5 THR A 397 ? ILE A 400 ? THR A 397 ILE A 400 
AA5 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA5 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA5 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA5 4 VAL B 346 ? ASN B 352 ? VAL B 346 ASN B 352 
AA6 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA6 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA6 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA6 4 ILE B 381 ? THR B 383 ? ILE B 381 THR B 383 
AA7 1 GLU B 24  ? TYR B 25  ? GLU B 24  TYR B 25  
AA7 2 LYS B 73  ? ASP B 74  ? LYS B 73  ASP B 74  
AA8 1 TYR B 251 ? MET B 252 ? TYR B 251 MET B 252 
AA8 2 MET B 274 ? THR B 277 ? MET B 274 THR B 277 
AA8 3 ILE B 301 ? PHE B 305 ? ILE B 301 PHE B 305 
AA8 4 ARG B 294 ? PHE B 297 ? ARG B 294 PHE B 297 
AA8 5 THR B 397 ? ILE B 400 ? THR B 397 ILE B 400 
AA9 1 VAL C 191 ? SER C 192 ? VAL C 191 SER C 192 
AA9 2 ASN C 53  ? LEU C 56  ? ASN C 53  LEU C 56  
AA9 3 LEU C 4   ? MET C 12  ? LEU C 4   MET C 12  
AA9 4 VAL C 346 ? ASN C 352 ? VAL C 346 ASN C 352 
AB1 1 VAL C 191 ? SER C 192 ? VAL C 191 SER C 192 
AB1 2 ASN C 53  ? LEU C 56  ? ASN C 53  LEU C 56  
AB1 3 LEU C 4   ? MET C 12  ? LEU C 4   MET C 12  
AB1 4 ILE C 381 ? THR C 383 ? ILE C 381 THR C 383 
AB2 1 GLU C 24  ? TYR C 25  ? GLU C 24  TYR C 25  
AB2 2 LYS C 73  ? ASP C 74  ? LYS C 73  ASP C 74  
AB3 1 TYR C 251 ? MET C 252 ? TYR C 251 MET C 252 
AB3 2 MET C 274 ? THR C 277 ? MET C 274 THR C 277 
AB3 3 ILE C 301 ? PHE C 305 ? ILE C 301 PHE C 305 
AB3 4 ARG C 294 ? PHE C 297 ? ARG C 294 PHE C 297 
AB3 5 THR C 397 ? ILE C 400 ? THR C 397 ILE C 400 
AB4 1 VAL D 191 ? SER D 192 ? VAL D 191 SER D 192 
AB4 2 ASN D 53  ? LEU D 56  ? ASN D 53  LEU D 56  
AB4 3 LEU D 4   ? MET D 12  ? LEU D 4   MET D 12  
AB4 4 VAL D 346 ? ASN D 352 ? VAL D 346 ASN D 352 
AB5 1 VAL D 191 ? SER D 192 ? VAL D 191 SER D 192 
AB5 2 ASN D 53  ? LEU D 56  ? ASN D 53  LEU D 56  
AB5 3 LEU D 4   ? MET D 12  ? LEU D 4   MET D 12  
AB5 4 ILE D 381 ? THR D 383 ? ILE D 381 THR D 383 
AB6 1 GLU D 24  ? TYR D 25  ? GLU D 24  TYR D 25  
AB6 2 LYS D 73  ? ASP D 74  ? LYS D 73  ASP D 74  
AB7 1 TYR D 251 ? MET D 252 ? TYR D 251 MET D 252 
AB7 2 MET D 274 ? THR D 277 ? MET D 274 THR D 277 
AB7 3 ILE D 301 ? PHE D 305 ? ILE D 301 PHE D 305 
AB7 4 ARG D 294 ? PHE D 297 ? ARG D 294 PHE D 297 
AB7 5 THR D 397 ? ILE D 400 ? THR D 397 ILE D 400 
# 
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 SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA1 2 3 O ASN A 53  ? O ASN A 53  N TRP A 10  ? N TRP A 10  
AA1 3 4 N VAL A 7   ? N VAL A 7   O VAL A 349 ? O VAL A 349 
AA2 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA2 2 3 O ASN A 53  ? O ASN A 53  N TRP A 10  ? N TRP A 10  
AA2 3 4 N LEU A 4   ? N LEU A 4   O GLU A 382 ? O GLU A 382 
AA3 1 2 N TYR A 25  ? N TYR A 25  O LYS A 73  ? O LYS A 73  
AA4 1 2 N MET A 252 ? N MET A 252 O MET A 274 ? O MET A 274 
AA4 2 3 N LEU A 275 ? N LEU A 275 O PHE A 304 ? O PHE A 304 
AA4 3 4 O VAL A 303 ? O VAL A 303 N TYR A 295 ? N TYR A 295 
AA4 4 5 N TYR A 296 ? N TYR A 296 O ILE A 400 ? O ILE A 400 
AA5 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA5 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA5 3 4 N PHE B 5   ? N PHE B 5   O VAL B 347 ? O VAL B 347 
AA6 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA6 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA6 3 4 N LEU B 4   ? N LEU B 4   O GLU B 382 ? O GLU B 382 
AA7 1 2 N TYR B 25  ? N TYR B 25  O LYS B 73  ? O LYS B 73  
AA8 1 2 N MET B 252 ? N MET B 252 O MET B 274 ? O MET B 274 
AA8 2 3 N THR B 277 ? N THR B 277 O PHE B 304 ? O PHE B 304 
AA8 3 4 O VAL B 303 ? O VAL B 303 N TYR B 295 ? N TYR B 295 
AA8 4 5 N TYR B 296 ? N TYR B 296 O ILE B 400 ? O ILE B 400 
AA9 1 2 O SER C 192 ? O SER C 192 N PHE C 54  ? N PHE C 54  
AA9 2 3 O ASN C 55  ? O ASN C 55  N MET C 12  ? N MET C 12  
AA9 3 4 N PHE C 5   ? N PHE C 5   O VAL C 347 ? O VAL C 347 
AB1 1 2 O SER C 192 ? O SER C 192 N PHE C 54  ? N PHE C 54  
AB1 2 3 O ASN C 55  ? O ASN C 55  N MET C 12  ? N MET C 12  
AB1 3 4 N LEU C 4   ? N LEU C 4   O GLU C 382 ? O GLU C 382 
AB2 1 2 N TYR C 25  ? N TYR C 25  O LYS C 73  ? O LYS C 73  
AB3 1 2 N MET C 252 ? N MET C 252 O MET C 274 ? O MET C 274 
AB3 2 3 N LEU C 275 ? N LEU C 275 O PHE C 304 ? O PHE C 304 
AB3 3 4 O VAL C 303 ? O VAL C 303 N TYR C 295 ? N TYR C 295 
AB3 4 5 N TYR C 296 ? N TYR C 296 O GLU C 398 ? O GLU C 398 
AB4 1 2 O SER D 192 ? O SER D 192 N PHE D 54  ? N PHE D 54  
AB4 2 3 O ASN D 55  ? O ASN D 55  N TRP D 10  ? N TRP D 10  
AB4 3 4 N PHE D 5   ? N PHE D 5   O VAL D 347 ? O VAL D 347 
AB5 1 2 O SER D 192 ? O SER D 192 N PHE D 54  ? N PHE D 54  
AB5 2 3 O ASN D 55  ? O ASN D 55  N TRP D 10  ? N TRP D 10  
AB5 3 4 N LEU D 4   ? N LEU D 4   O GLU D 382 ? O GLU D 382 
AB6 1 2 N TYR D 25  ? N TYR D 25  O LYS D 73  ? O LYS D 73  
AB7 1 2 N MET D 252 ? N MET D 252 O MET D 274 ? O MET D 274 
AB7 2 3 N LEU D 275 ? N LEU D 275 O PHE D 304 ? O PHE D 304 
AB7 3 4 O ILE D 301 ? O ILE D 301 N PHE D 297 ? N PHE D 297 
AB7 4 5 N TYR D 296 ? N TYR D 296 O GLU D 398 ? O GLU D 398 
# 
_pdbx_entry_details.entry_id                   9KYR 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   C HOH 691 ? ? O C HOH 698 ? ? 1.96 
2  1 O   B HOH 747 ? ? O B HOH 768 ? ? 2.04 
3  1 N   D ARG 141 ? ? O D HOH 601 ? ? 2.05 
4  1 OH  C TYR 103 ? ? O C HOH 601 ? ? 2.06 
5  1 O   B HOH 602 ? ? O B HOH 753 ? ? 2.06 
6  1 O   B HOH 714 ? ? O B HOH 741 ? ? 2.08 
7  1 O   A GLU 287 ? ? O A HOH 601 ? ? 2.08 
8  1 NH2 B ARG 473 ? ? O B HOH 601 ? ? 2.08 
9  1 OE1 D GLU 299 ? ? O D HOH 602 ? ? 2.09 
10 1 OD1 A ASP 149 ? ? O A HOH 602 ? ? 2.09 
11 1 NZ  B LYS 232 ? ? O B HOH 602 ? ? 2.10 
12 1 O   B HOH 630 ? ? O B HOH 711 ? ? 2.10 
13 1 OH  C TYR 251 ? ? O C HOH 602 ? ? 2.11 
14 1 O   D HOH 606 ? ? O D HOH 725 ? ? 2.11 
15 1 O   D HOH 762 ? ? O D HOH 763 ? ? 2.11 
16 1 OE2 C GLU 49  ? ? O C HOH 603 ? ? 2.11 
17 1 O   C HOH 650 ? ? O C HOH 682 ? ? 2.12 
18 1 O   B HOH 738 ? ? O B HOH 770 ? ? 2.13 
19 1 O   C HOH 664 ? ? O C HOH 682 ? ? 2.14 
20 1 NH1 D ARG 81  ? ? O D HOH 603 ? ? 2.14 
21 1 OH  A TYR 268 ? ? O A HOH 603 ? ? 2.14 
22 1 OG  D SER 258 ? A O D HOH 604 ? ? 2.15 
23 1 NZ  A LYS 466 ? ? O A HOH 604 ? ? 2.15 
24 1 O   C HOH 602 ? ? O C HOH 611 ? ? 2.15 
25 1 NZ  C LYS 145 ? ? O C HOH 604 ? ? 2.16 
26 1 O   B HOH 706 ? ? O B HOH 767 ? ? 2.18 
27 1 O   D HOH 743 ? ? O D HOH 760 ? ? 2.18 
28 1 OG  C SER 258 ? A O C HOH 605 ? ? 2.19 
29 1 O2  A EDO 507 ? ? O A HOH 605 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 120 ? ? -77.78  -75.84  
2  1 ASN A 206 ? ? -165.02 93.44   
3  1 ALA A 257 ? ? 52.66   19.64   
4  1 ASP A 394 ? ? -90.85  46.89   
5  1 GLU A 455 ? ? 177.12  73.01   
6  1 GLU A 456 ? ? -84.34  -110.93 
7  1 PHE A 460 ? ? 81.68   -3.57   
8  1 ASN B 206 ? ? -169.41 92.09   
9  1 ALA B 289 ? ? -116.86 66.10   
10 1 ASP B 410 ? ? 57.53   17.14   
11 1 GLU B 455 ? ? -127.47 -157.11 
12 1 LYS B 457 ? ? -8.76   110.93  
13 1 PHE B 460 ? ? 65.96   -2.18   
14 1 GLU C 49  ? ? -90.49  59.10   
15 1 PRO C 195 ? ? -39.26  141.85  
16 1 ASN C 206 ? ? -162.03 98.91   
17 1 ALA C 257 ? ? 47.62   24.08   
18 1 ALA C 257 ? ? 47.62   24.69   
19 1 THR C 277 ? ? -147.40 -158.48 
20 1 ASP C 410 ? ? 59.70   11.92   
21 1 GLU C 456 ? ? 64.91   -18.98  
22 1 LYS C 457 ? ? -81.26  43.84   
23 1 ALA C 458 ? ? 177.61  158.23  
24 1 ASN D 206 ? ? -164.69 91.61   
25 1 ASP D 394 ? ? -88.45  48.61   
26 1 GLU D 456 ? ? 90.18   -77.81  
# 
_pdbx_molecule_features.prd_id    PRD_900042 
_pdbx_molecule_features.name      gamma-cyclodextrin 
_pdbx_molecule_features.type      Oligosaccharide 
_pdbx_molecule_features.class     'Drug delivery' 
_pdbx_molecule_features.details   'cyclic oligosaccharide' 
# 
loop_
_pdbx_molecule.instance_id 
_pdbx_molecule.prd_id 
_pdbx_molecule.asym_id 
1 PRD_900042 E 
2 PRD_900042 F 
3 PRD_900042 G 
4 PRD_900042 H 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -24.1182 -33.1032 26.7128  0.1353 ? -0.0503 ? 0.0075  ? 0.1681 ? -0.0003 ? 0.2231 ? 0.2879 ? 
-0.0185 ? -0.0313 ? 1.1847 ? 0.2919  ? 1.9064 ? -0.0026 ? 0.0211  ? -0.0274 ? -0.0806 ? -0.0339 ? 0.1473  ? 0.1681  ? -0.1480 ? 
0.0433  ? 
2  'X-RAY DIFFRACTION' ? refined -11.2650 -44.5070 10.3820  0.3333 ? -0.0280 ? 0.0576  ? 0.3199 ? -0.0034 ? 0.2961 ? 0.9787 ? 
0.0012  ? 0.1594  ? 1.9458 ? 0.9511  ? 2.4646 ? 0.0611  ? 0.1692  ? -0.0461 ? -0.5724 ? 0.0817  ? -0.2992 ? -0.0083 ? 0.3973  ? 
-0.1001 ? 
3  'X-RAY DIFFRACTION' ? refined -22.4322 -43.5145 25.1358  0.2040 ? -0.0414 ? -0.0051 ? 0.1835 ? 0.0135  ? 0.2242 ? 0.4753 ? 
0.0656  ? -0.1089 ? 1.9181 ? 0.6475  ? 0.9939 ? -0.0355 ? 0.0065  ? -0.1086 ? 0.1195  ? 0.0151  ? 0.0600  ? 0.3005  ? -0.0724 ? 
0.0124  ? 
4  'X-RAY DIFFRACTION' ? refined -26.2745 -9.9047  24.8383  0.1923 ? -0.0066 ? -0.0215 ? 0.2244 ? 0.0063  ? 0.2431 ? 0.6572 ? 
0.2701  ? -0.8850 ? 1.4566 ? -0.5020 ? 1.3476 ? 0.0107  ? 0.0712  ? 0.1541  ? -0.1888 ? -0.0180 ? 0.1415  ? -0.0880 ? -0.0002 ? 
-0.0373 ? 
5  'X-RAY DIFFRACTION' ? refined -26.3861 -13.7128 35.7028  0.1354 ? -0.0072 ? 0.0150  ? 0.2543 ? 0.0040  ? 0.2314 ? 1.6191 ? 
0.8390  ? 0.0885  ? 1.1417 ? 0.1674  ? 1.2094 ? -0.1013 ? -0.1645 ? 0.0235  ? 0.1554  ? -0.0094 ? 0.0219  ? -0.1684 ? -0.2529 ? 
0.1084  ? 
6  'X-RAY DIFFRACTION' ? refined -11.9123 -16.6046 40.5962  0.1420 ? -0.0495 ? 0.0103  ? 0.2308 ? 0.0162  ? 0.2224 ? 0.8259 ? 
-0.4780 ? 0.3738  ? 2.1235 ? -0.1907 ? 1.1589 ? -0.0325 ? 0.1204  ? 0.0524  ? 0.2306  ? -0.0231 ? -0.1752 ? -0.2916 ? 0.1250  ? 
0.0230  ? 
7  'X-RAY DIFFRACTION' ? refined -11.9163 -29.8613 44.4339  0.1705 ? -0.0197 ? -0.0156 ? 0.2005 ? 0.0234  ? 0.1991 ? 0.7488 ? 
0.5736  ? 0.0969  ? 2.5302 ? 1.6217  ? 3.1321 ? 0.1120  ? -0.0644 ? -0.0442 ? 0.3771  ? 0.0204  ? -0.1603 ? 0.1688  ? -0.0418 ? 
-0.1226 ? 
8  'X-RAY DIFFRACTION' ? refined -17.7845 -9.4958  22.0654  0.2301 ? -0.0211 ? 0.0008  ? 0.2000 ? 0.0208  ? 0.2537 ? 0.9981 ? 
0.0335  ? -0.1152 ? 1.3710 ? 0.1449  ? 2.2422 ? 0.0233  ? 0.0418  ? 0.0290  ? -0.2529 ? -0.0424 ? -0.1491 ? -0.2144 ? 0.0803  ? 
0.0300  ? 
9  'X-RAY DIFFRACTION' ? refined -23.7811 -19.6958 12.2803  0.2020 ? -0.0159 ? -0.0300 ? 0.2126 ? 0.0241  ? 0.1857 ? 1.4135 ? 
0.0696  ? -0.0244 ? 3.3575 ? 0.2808  ? 2.6870 ? -0.0103 ? -0.0632 ? -0.1464 ? -0.3289 ? -0.0290 ? 0.0551  ? -0.0888 ? -0.0356 ? 
0.0772  ? 
10 'X-RAY DIFFRACTION' ? refined -28.1418 -29.3430 -21.0009 0.2478 ? 0.0560  ? 0.0040  ? 0.2519 ? -0.0006 ? 0.1726 ? 0.5406 ? 
-0.1129 ? 0.2515  ? 1.7951 ? 0.1943  ? 0.5143 ? 0.0842  ? 0.0804  ? 0.0400  ? 0.0263  ? -0.0554 ? 0.0710  ? -0.1531 ? -0.0957 ? 
-0.0139 ? 
11 'X-RAY DIFFRACTION' ? refined -10.7156 -20.4573 -10.5920 0.2974 ? -0.0029 ? -0.0087 ? 0.3666 ? -0.0125 ? 0.3016 ? 0.4309 ? 
-0.4221 ? 0.3051  ? 1.7036 ? 1.2567  ? 2.9012 ? -0.0646 ? 0.0425  ? 0.0562  ? 0.1634  ? 0.1577  ? -0.4298 ? 0.3095  ? 0.6154  ? 
-0.1121 ? 
12 'X-RAY DIFFRACTION' ? refined -26.3040 -20.1874 -21.4420 0.3742 ? 0.0762  ? 0.0146  ? 0.2960 ? 0.0096  ? 0.2382 ? 0.5454 ? 
-0.0174 ? 0.3782  ? 1.3291 ? 0.7217  ? 1.0922 ? -0.0042 ? 0.0585  ? 0.1301  ? -0.2351 ? -0.0899 ? 0.1167  ? -0.3439 ? -0.0681 ? 
0.0802  ? 
13 'X-RAY DIFFRACTION' ? refined -31.1098 -53.7607 -20.3479 0.2843 ? 0.0116  ? 0.0135  ? 0.2464 ? -0.0371 ? 0.2341 ? 1.0721 ? 
-0.5446 ? 0.5630  ? 2.0678 ? -0.2103 ? 1.7112 ? 0.1397  ? 0.0839  ? -0.1837 ? -0.0440 ? -0.1669 ? 0.1959  ? 0.3393  ? -0.0154 ? 
0.0463  ? 
14 'X-RAY DIFFRACTION' ? refined -33.0979 -49.8042 -31.1110 0.2968 ? 0.0416  ? -0.0758 ? 0.3381 ? -0.0318 ? 0.2458 ? 1.6234 ? 
-0.3459 ? -0.0023 ? 1.6315 ? 0.6304  ? 1.6704 ? 0.0769  ? 0.1632  ? -0.0086 ? -0.1210 ? -0.1475 ? 0.2969  ? -0.0503 ? -0.3033 ? 
0.0879  ? 
15 'X-RAY DIFFRACTION' ? refined -19.6540 -47.3653 -38.4683 0.3481 ? 0.1065  ? -0.0301 ? 0.3460 ? -0.0153 ? 0.1835 ? 1.3770 ? 
0.6634  ? 0.0349  ? 2.0634 ? 0.3697  ? 1.2177 ? -0.0739 ? 0.2041  ? -0.0619 ? -0.4758 ? 0.0215  ? -0.0149 ? 0.0028  ? 0.0908  ? 
0.0086  ? 
16 'X-RAY DIFFRACTION' ? refined -16.0394 -35.9225 -41.1944 0.3926 ? 0.1259  ? 0.0184  ? 0.3987 ? 0.0154  ? 0.2385 ? 1.2611 ? 
-0.1587 ? 0.5122  ? 1.7119 ? 0.5978  ? 1.8048 ? 0.1092  ? 0.2574  ? 0.0075  ? -0.3977 ? -0.0451 ? -0.0153 ? -0.1460 ? 0.2030  ? 
-0.0857 ? 
17 'X-RAY DIFFRACTION' ? refined -24.0733 -32.4333 -43.6477 0.4201 ? 0.1466  ? 0.0007  ? 0.4230 ? 0.0333  ? 0.2237 ? 1.1952 ? 
-0.2936 ? 0.2482  ? 2.3098 ? 0.6418  ? 1.7311 ? 0.1143  ? 0.4809  ? 0.1422  ? -0.5038 ? -0.0704 ? 0.1509  ? -0.0326 ? 0.0482  ? 
-0.0531 ? 
18 'X-RAY DIFFRACTION' ? refined -22.2248 -54.3620 -19.2125 0.2743 ? 0.0421  ? -0.0230 ? 0.2471 ? -0.0323 ? 0.2368 ? 1.1728 ? 
0.1375  ? 0.0560  ? 2.2693 ? -0.6129 ? 1.6424 ? 0.0059  ? -0.0687 ? -0.1220 ? 0.1451  ? -0.1190 ? -0.1038 ? -0.0989 ? 0.2858  ? 
0.1361  ? 
19 'X-RAY DIFFRACTION' ? refined -25.9776 -44.0714 -8.5975  0.3226 ? 0.0354  ? -0.0123 ? 0.2531 ? -0.0028 ? 0.1788 ? 1.8576 ? 
0.5906  ? 0.3268  ? 3.4885 ? 0.0045  ? 1.8392 ? 0.0482  ? -0.0571 ? 0.0462  ? 0.4480  ? -0.0344 ? -0.0491 ? -0.0163 ? -0.0605 ? 
0.0268  ? 
20 'X-RAY DIFFRACTION' ? refined -9.5169  -15.8909 -68.3205 0.2347 ? 0.0006  ? -0.0245 ? 0.2630 ? 0.0064  ? 0.2159 ? 0.8570 ? 
-0.4733 ? -0.1200 ? 3.3333 ? 0.8877  ? 1.0224 ? -0.1164 ? -0.0232 ? -0.1344 ? -0.2106 ? 0.0302  ? 0.3199  ? -0.0252 ? -0.2652 ? 
0.0746  ? 
21 'X-RAY DIFFRACTION' ? refined -4.6034  -22.5323 -89.7856 0.6307 ? 0.0115  ? -0.0407 ? 0.3350 ? 0.0121  ? 0.2778 ? 0.5459 ? 
-0.4265 ? -0.1008 ? 1.3897 ? 0.8159  ? 1.9338 ? 0.1316  ? 0.2098  ? -0.0212 ? -0.8452 ? -0.0479 ? 0.1595  ? -0.1151 ? -0.1223 ? 
0.0323  ? 
22 'X-RAY DIFFRACTION' ? refined 8.9576   -28.4179 -83.1450 0.4785 ? 0.0279  ? 0.1065  ? 0.4402 ? -0.0377 ? 0.3507 ? 0.6096 ? 
-0.2365 ? -0.2332 ? 1.3336 ? 1.3113  ? 1.3740 ? -0.1795 ? 0.0110  ? -0.2879 ? -0.5940 ? 0.2317  ? -0.4685 ? 0.1476  ? 0.5525  ? 
-0.1348 ? 
23 'X-RAY DIFFRACTION' ? refined -6.9634  -30.8557 -76.2457 0.3728 ? -0.0229 ? -0.0631 ? 0.2551 ? 0.0137  ? 0.2916 ? 1.4365 ? 
0.0777  ? -0.1582 ? 2.9475 ? -0.0399 ? 2.1468 ? 0.0390  ? -0.0235 ? -0.1850 ? -0.2696 ? -0.0213 ? 0.2859  ? 0.5655  ? -0.2152 ? 
-0.0111 ? 
24 'X-RAY DIFFRACTION' ? refined -7.6104  5.6725   -68.4690 0.5425 ? 0.0874  ? -0.0464 ? 0.3255 ? -0.0058 ? 0.2743 ? 1.5872 ? 
-0.8907 ? -0.8174 ? 2.0887 ? 1.0617  ? 2.1259 ? 0.2325  ? 0.0531  ? 0.3308  ? -0.5635 ? -0.1041 ? 0.0112  ? -0.5931 ? -0.0654 ? 
-0.1439 ? 
25 'X-RAY DIFFRACTION' ? refined -15.9371 -0.0994  -62.0838 0.2973 ? 0.0975  ? -0.0757 ? 0.3574 ? -0.0351 ? 0.3913 ? 1.5946 ? 
-0.5659 ? -0.1359 ? 2.2268 ? 0.8952  ? 2.3423 ? -0.0210 ? -0.1882 ? -0.3314 ? -0.1817 ? -0.0986 ? 0.7264  ? -0.3588 ? -0.4355 ? 
0.0623  ? 
26 'X-RAY DIFFRACTION' ? refined 1.1431   -2.7689  -53.6263 0.2659 ? 0.0457  ? -0.0987 ? 0.3818 ? -0.0704 ? 0.3253 ? 0.4271 ? 
-0.5106 ? -0.5445 ? 1.2760 ? 0.0256  ? 1.2144 ? -0.0772 ? -0.0482 ? 0.1258  ? 0.2654  ? 0.1598  ? -0.3498 ? -0.0594 ? 0.1664  ? 
-0.1041 ? 
27 'X-RAY DIFFRACTION' ? refined 4.4693   -14.4216 -53.0434 0.4267 ? 0.1343  ? -0.1249 ? 0.4635 ? -0.0516 ? 0.3260 ? 0.8507 ? 
0.3238  ? -0.9087 ? 1.4643 ? 0.8021  ? 1.8766 ? -0.1362 ? -0.3356 ? -0.0727 ? 0.5146  ? 0.3469  ? -0.4588 ? 0.2526  ? 0.5068  ? 
-0.1616 ? 
28 'X-RAY DIFFRACTION' ? refined -3.3259  -18.0673 -50.3095 0.4814 ? 0.1032  ? -0.0343 ? 0.4210 ? 0.0183  ? 0.2711 ? 0.7997 ? 
0.4038  ? 0.0860  ? 2.2115 ? 0.4432  ? 1.7378 ? -0.1880 ? -0.2903 ? -0.1744 ? 0.7637  ? 0.2163  ? 0.0926  ? 0.2983  ? -0.0059 ? 
-0.0576 ? 
29 'X-RAY DIFFRACTION' ? refined -2.4310  7.1134   -70.7216 0.7255 ? 0.0415  ? 0.0397  ? 0.2419 ? -0.0046 ? 0.3209 ? 1.8380 ? 
-0.5361 ? -0.8703 ? 2.2959 ? -0.9798 ? 2.4235 ? 0.2821  ? 0.0329  ? 0.2233  ? -0.8345 ? -0.0113 ? -0.3339 ? -0.6808 ? 0.4335  ? 
-0.0626 ? 
30 'X-RAY DIFFRACTION' ? refined -8.2657  -0.9909  -83.0173 0.8658 ? 0.1479  ? -0.0692 ? 0.3503 ? -0.0099 ? 0.2604 ? 1.3717 ? 
-0.3797 ? -0.3817 ? 3.3049 ? -0.0897 ? 2.1443 ? 0.4028  ? 0.1347  ? 0.0478  ? -1.0999 ? -0.3082 ? 0.1117  ? -0.6080 ? -0.2220 ? 
-0.0211 ? 
31 'X-RAY DIFFRACTION' ? refined -4.7833  -46.9550 73.7067  0.1977 ? 0.0093  ? 0.0250  ? 0.2359 ? 0.0002  ? 0.2137 ? 0.6698 ? 
0.1247  ? 0.0413  ? 1.9688 ? -0.3791 ? 0.7086 ? -0.0267 ? -0.0625 ? 0.0470  ? 0.2664  ? 0.0553  ? 0.0839  ? -0.0466 ? -0.1922 ? 
-0.0316 ? 
32 'X-RAY DIFFRACTION' ? refined 8.2315   -37.9111 91.9932  0.6585 ? 0.0410  ? -0.1249 ? 0.4110 ? -0.0445 ? 0.3515 ? 0.2095 ? 
-0.4023 ? -0.1864 ? 1.3635 ? 0.5025  ? 2.5069 ? -0.0441 ? -0.4171 ? 0.0855  ? 0.8565  ? 0.1183  ? -0.4388 ? -0.0296 ? 0.4838  ? 
-0.0174 ? 
33 'X-RAY DIFFRACTION' ? refined -3.5075  -36.8324 77.5940  0.3056 ? 0.0280  ? 0.0283  ? 0.2516 ? 0.0034  ? 0.2631 ? 0.2299 ? 
-0.0837 ? -0.0400 ? 1.4867 ? -0.0604 ? 1.1956 ? -0.0210 ? -0.0508 ? 0.0634  ? 0.2846  ? 0.0539  ? 0.0110  ? -0.3794 ? -0.1793 ? 
-0.0490 ? 
34 'X-RAY DIFFRACTION' ? refined -6.7728  -70.1554 72.2158  0.2394 ? -0.0500 ? 0.0365  ? 0.2298 ? 0.0233  ? 0.2265 ? 1.3208 ? 
-1.0014 ? 0.4557  ? 2.6424 ? -0.2541 ? 1.8549 ? 0.0138  ? -0.0111 ? -0.2452 ? 0.0944  ? 0.0820  ? 0.3097  ? 0.3680  ? -0.1563 ? 
-0.0439 ? 
35 'X-RAY DIFFRACTION' ? refined -7.0399  -64.5787 62.1300  0.1865 ? -0.0573 ? 0.0117  ? 0.2785 ? 0.0096  ? 0.2601 ? 1.1441 ? 
-1.3150 ? -0.2630 ? 1.7067 ? -0.0947 ? 1.4775 ? 0.0638  ? 0.1572  ? 0.0225  ? 0.0301  ? -0.0825 ? 0.2295  ? 0.1987  ? -0.1187 ? 
0.0044  ? 
36 'X-RAY DIFFRACTION' ? refined 7.3688   -60.6416 57.6989  0.1713 ? -0.0205 ? 0.0329  ? 0.2770 ? -0.0107 ? 0.2868 ? 0.9067 ? 
0.7093  ? 0.1711  ? 2.0434 ? -0.0934 ? 0.8578 ? -0.0506 ? -0.1534 ? -0.0951 ? -0.2711 ? -0.0221 ? -0.3536 ? 0.0180  ? 0.0070  ? 
0.0142  ? 
37 'X-RAY DIFFRACTION' ? refined 10.7812  -48.8753 57.4625  0.1480 ? -0.0475 ? 0.0615  ? 0.2174 ? 0.0043  ? 0.3019 ? 0.8856 ? 
-0.6050 ? 0.8187  ? 1.4168 ? 0.0888  ? 2.4009 ? 0.0066  ? 0.0200  ? 0.1199  ? -0.2264 ? 0.0162  ? -0.3026 ? 0.0645  ? 0.2962  ? 
-0.0299 ? 
38 'X-RAY DIFFRACTION' ? refined 2.8791   -50.0845 54.2037  0.0845 ? -0.0161 ? 0.0462  ? 0.2287 ? 0.0161  ? 0.2172 ? 0.4066 ? 
-0.4472 ? 0.0433  ? 2.0489 ? -0.3946 ? 1.7909 ? -0.0515 ? 0.1125  ? 0.0419  ? -0.3872 ? 0.0901  ? -0.0167 ? -0.1100 ? -0.0305 ? 
-0.0656 ? 
39 'X-RAY DIFFRACTION' ? refined 2.0047   -70.5311 80.2166  0.3364 ? 0.0065  ? -0.0485 ? 0.2255 ? 0.0000  ? 0.2300 ? 2.1494 ? 
-0.1751 ? 0.0156  ? 2.2662 ? -0.2441 ? 2.6571 ? -0.0199 ? -0.3389 ? -0.1117 ? 0.6696  ? -0.0597 ? -0.3112 ? 0.0687  ? 0.3776  ? 
0.0606  ? 
40 'X-RAY DIFFRACTION' ? refined -4.0947  -62.4444 86.1883  0.3457 ? 0.0249  ? 0.0042  ? 0.1808 ? 0.0241  ? 0.1723 ? 1.4353 ? 
-0.0232 ? -0.4619 ? 3.4626 ? 0.5011  ? 2.6893 ? 0.0181  ? -0.0912 ? 0.1937  ? 0.6157  ? 0.0843  ? -0.0332 ? 0.1551  ? -0.0951 ? 
-0.0600 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 81 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 82 through 123 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 124 through 200 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 201 through 245 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 246 through 278 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 279 through 322 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 323 through 396 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 435 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 436 through 477 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 88 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 89 through 123 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 124 through 200 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 201 through 245 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 246 through 278 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 279 through 322 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 323 through 360 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 361 through 396 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 397 through 435 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 436 through 477 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 2 through 68 )
;
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 69 through 101 )
;
22 'X-RAY DIFFRACTION' 22 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 102 through 123 )
;
23 'X-RAY DIFFRACTION' 23 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 124 through 185 )
;
24 'X-RAY DIFFRACTION' 24 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 186 through 226 )
;
25 'X-RAY DIFFRACTION' 25 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 227 through 278 )
;
26 'X-RAY DIFFRACTION' 26 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 279 through 322 )
;
27 'X-RAY DIFFRACTION' 27 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 323 through 360 )
;
28 'X-RAY DIFFRACTION' 28 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 361 through 396 )
;
29 'X-RAY DIFFRACTION' 29 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 397 through 434 )
;
30 'X-RAY DIFFRACTION' 30 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 435 through 477 )
;
31 'X-RAY DIFFRACTION' 31 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 1 through 81 )
;
32 'X-RAY DIFFRACTION' 32 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 82 through 123 )
;
33 'X-RAY DIFFRACTION' 33 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 124 through 200 )
;
34 'X-RAY DIFFRACTION' 34 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 201 through 245 )
;
35 'X-RAY DIFFRACTION' 35 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 246 through 278 )
;
36 'X-RAY DIFFRACTION' 36 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 279 through 322 )
;
37 'X-RAY DIFFRACTION' 37 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 323 through 360 )
;
38 'X-RAY DIFFRACTION' 38 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 361 through 405 )
;
39 'X-RAY DIFFRACTION' 39 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 406 through 435 )
;
40 'X-RAY DIFFRACTION' 40 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 436 through 477 )
;
# 
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 1 ? A MET 1 
2 1 Y 1 B MET 1 ? B MET 1 
3 1 Y 1 C MET 1 ? C MET 1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLC C1   C N S 98  
GLC C2   C N R 99  
GLC C3   C N S 100 
GLC C4   C N S 101 
GLC C5   C N R 102 
GLC C6   C N N 103 
GLC O1   O N N 104 
GLC O2   O N N 105 
GLC O3   O N N 106 
GLC O4   O N N 107 
GLC O5   O N N 108 
GLC O6   O N N 109 
GLC H1   H N N 110 
GLC H2   H N N 111 
GLC H3   H N N 112 
GLC H4   H N N 113 
GLC H5   H N N 114 
GLC H61  H N N 115 
GLC H62  H N N 116 
GLC HO1  H N N 117 
GLC HO2  H N N 118 
GLC HO3  H N N 119 
GLC HO4  H N N 120 
GLC HO6  H N N 121 
GLN N    N N N 122 
GLN CA   C N S 123 
GLN C    C N N 124 
GLN O    O N N 125 
GLN CB   C N N 126 
GLN CG   C N N 127 
GLN CD   C N N 128 
GLN OE1  O N N 129 
GLN NE2  N N N 130 
GLN OXT  O N N 131 
GLN H    H N N 132 
GLN H2   H N N 133 
GLN HA   H N N 134 
GLN HB2  H N N 135 
GLN HB3  H N N 136 
GLN HG2  H N N 137 
GLN HG3  H N N 138 
GLN HE21 H N N 139 
GLN HE22 H N N 140 
GLN HXT  H N N 141 
GLU N    N N N 142 
GLU CA   C N S 143 
GLU C    C N N 144 
GLU O    O N N 145 
GLU CB   C N N 146 
GLU CG   C N N 147 
GLU CD   C N N 148 
GLU OE1  O N N 149 
GLU OE2  O N N 150 
GLU OXT  O N N 151 
GLU H    H N N 152 
GLU H2   H N N 153 
GLU HA   H N N 154 
GLU HB2  H N N 155 
GLU HB3  H N N 156 
GLU HG2  H N N 157 
GLU HG3  H N N 158 
GLU HE2  H N N 159 
GLU HXT  H N N 160 
GLY N    N N N 161 
GLY CA   C N N 162 
GLY C    C N N 163 
GLY O    O N N 164 
GLY OXT  O N N 165 
GLY H    H N N 166 
GLY H2   H N N 167 
GLY HA2  H N N 168 
GLY HA3  H N N 169 
GLY HXT  H N N 170 
GOL C1   C N N 171 
GOL O1   O N N 172 
GOL C2   C N N 173 
GOL O2   O N N 174 
GOL C3   C N N 175 
GOL O3   O N N 176 
GOL H11  H N N 177 
GOL H12  H N N 178 
GOL HO1  H N N 179 
GOL H2   H N N 180 
GOL HO2  H N N 181 
GOL H31  H N N 182 
GOL H32  H N N 183 
GOL HO3  H N N 184 
HIS N    N N N 185 
HIS CA   C N S 186 
HIS C    C N N 187 
HIS O    O N N 188 
HIS CB   C N N 189 
HIS CG   C Y N 190 
HIS ND1  N Y N 191 
HIS CD2  C Y N 192 
HIS CE1  C Y N 193 
HIS NE2  N Y N 194 
HIS OXT  O N N 195 
HIS H    H N N 196 
HIS H2   H N N 197 
HIS HA   H N N 198 
HIS HB2  H N N 199 
HIS HB3  H N N 200 
HIS HD1  H N N 201 
HIS HD2  H N N 202 
HIS HE1  H N N 203 
HIS HE2  H N N 204 
HIS HXT  H N N 205 
HOH O    O N N 206 
HOH H1   H N N 207 
HOH H2   H N N 208 
ILE N    N N N 209 
ILE CA   C N S 210 
ILE C    C N N 211 
ILE O    O N N 212 
ILE CB   C N S 213 
ILE CG1  C N N 214 
ILE CG2  C N N 215 
ILE CD1  C N N 216 
ILE OXT  O N N 217 
ILE H    H N N 218 
ILE H2   H N N 219 
ILE HA   H N N 220 
ILE HB   H N N 221 
ILE HG12 H N N 222 
ILE HG13 H N N 223 
ILE HG21 H N N 224 
ILE HG22 H N N 225 
ILE HG23 H N N 226 
ILE HD11 H N N 227 
ILE HD12 H N N 228 
ILE HD13 H N N 229 
ILE HXT  H N N 230 
LEU N    N N N 231 
LEU CA   C N S 232 
LEU C    C N N 233 
LEU O    O N N 234 
LEU CB   C N N 235 
LEU CG   C N N 236 
LEU CD1  C N N 237 
LEU CD2  C N N 238 
LEU OXT  O N N 239 
LEU H    H N N 240 
LEU H2   H N N 241 
LEU HA   H N N 242 
LEU HB2  H N N 243 
LEU HB3  H N N 244 
LEU HG   H N N 245 
LEU HD11 H N N 246 
LEU HD12 H N N 247 
LEU HD13 H N N 248 
LEU HD21 H N N 249 
LEU HD22 H N N 250 
LEU HD23 H N N 251 
LEU HXT  H N N 252 
LYS N    N N N 253 
LYS CA   C N S 254 
LYS C    C N N 255 
LYS O    O N N 256 
LYS CB   C N N 257 
LYS CG   C N N 258 
LYS CD   C N N 259 
LYS CE   C N N 260 
LYS NZ   N N N 261 
LYS OXT  O N N 262 
LYS H    H N N 263 
LYS H2   H N N 264 
LYS HA   H N N 265 
LYS HB2  H N N 266 
LYS HB3  H N N 267 
LYS HG2  H N N 268 
LYS HG3  H N N 269 
LYS HD2  H N N 270 
LYS HD3  H N N 271 
LYS HE2  H N N 272 
LYS HE3  H N N 273 
LYS HZ1  H N N 274 
LYS HZ2  H N N 275 
LYS HZ3  H N N 276 
LYS HXT  H N N 277 
MET N    N N N 278 
MET CA   C N S 279 
MET C    C N N 280 
MET O    O N N 281 
MET CB   C N N 282 
MET CG   C N N 283 
MET SD   S N N 284 
MET CE   C N N 285 
MET OXT  O N N 286 
MET H    H N N 287 
MET H2   H N N 288 
MET HA   H N N 289 
MET HB2  H N N 290 
MET HB3  H N N 291 
MET HG2  H N N 292 
MET HG3  H N N 293 
MET HE1  H N N 294 
MET HE2  H N N 295 
MET HE3  H N N 296 
MET HXT  H N N 297 
PEG C1   C N N 298 
PEG O1   O N N 299 
PEG C2   C N N 300 
PEG O2   O N N 301 
PEG C3   C N N 302 
PEG C4   C N N 303 
PEG O4   O N N 304 
PEG H11  H N N 305 
PEG H12  H N N 306 
PEG HO1  H N N 307 
PEG H21  H N N 308 
PEG H22  H N N 309 
PEG H31  H N N 310 
PEG H32  H N N 311 
PEG H41  H N N 312 
PEG H42  H N N 313 
PEG HO4  H N N 314 
PHE N    N N N 315 
PHE CA   C N S 316 
PHE C    C N N 317 
PHE O    O N N 318 
PHE CB   C N N 319 
PHE CG   C Y N 320 
PHE CD1  C Y N 321 
PHE CD2  C Y N 322 
PHE CE1  C Y N 323 
PHE CE2  C Y N 324 
PHE CZ   C Y N 325 
PHE OXT  O N N 326 
PHE H    H N N 327 
PHE H2   H N N 328 
PHE HA   H N N 329 
PHE HB2  H N N 330 
PHE HB3  H N N 331 
PHE HD1  H N N 332 
PHE HD2  H N N 333 
PHE HE1  H N N 334 
PHE HE2  H N N 335 
PHE HZ   H N N 336 
PHE HXT  H N N 337 
PRO N    N N N 338 
PRO CA   C N S 339 
PRO C    C N N 340 
PRO O    O N N 341 
PRO CB   C N N 342 
PRO CG   C N N 343 
PRO CD   C N N 344 
PRO OXT  O N N 345 
PRO H    H N N 346 
PRO HA   H N N 347 
PRO HB2  H N N 348 
PRO HB3  H N N 349 
PRO HG2  H N N 350 
PRO HG3  H N N 351 
PRO HD2  H N N 352 
PRO HD3  H N N 353 
PRO HXT  H N N 354 
SER N    N N N 355 
SER CA   C N S 356 
SER C    C N N 357 
SER O    O N N 358 
SER CB   C N N 359 
SER OG   O N N 360 
SER OXT  O N N 361 
SER H    H N N 362 
SER H2   H N N 363 
SER HA   H N N 364 
SER HB2  H N N 365 
SER HB3  H N N 366 
SER HG   H N N 367 
SER HXT  H N N 368 
THR N    N N N 369 
THR CA   C N S 370 
THR C    C N N 371 
THR O    O N N 372 
THR CB   C N R 373 
THR OG1  O N N 374 
THR CG2  C N N 375 
THR OXT  O N N 376 
THR H    H N N 377 
THR H2   H N N 378 
THR HA   H N N 379 
THR HB   H N N 380 
THR HG1  H N N 381 
THR HG21 H N N 382 
THR HG22 H N N 383 
THR HG23 H N N 384 
THR HXT  H N N 385 
TRP N    N N N 386 
TRP CA   C N S 387 
TRP C    C N N 388 
TRP O    O N N 389 
TRP CB   C N N 390 
TRP CG   C Y N 391 
TRP CD1  C Y N 392 
TRP CD2  C Y N 393 
TRP NE1  N Y N 394 
TRP CE2  C Y N 395 
TRP CE3  C Y N 396 
TRP CZ2  C Y N 397 
TRP CZ3  C Y N 398 
TRP CH2  C Y N 399 
TRP OXT  O N N 400 
TRP H    H N N 401 
TRP H2   H N N 402 
TRP HA   H N N 403 
TRP HB2  H N N 404 
TRP HB3  H N N 405 
TRP HD1  H N N 406 
TRP HE1  H N N 407 
TRP HE3  H N N 408 
TRP HZ2  H N N 409 
TRP HZ3  H N N 410 
TRP HH2  H N N 411 
TRP HXT  H N N 412 
TYR N    N N N 413 
TYR CA   C N S 414 
TYR C    C N N 415 
TYR O    O N N 416 
TYR CB   C N N 417 
TYR CG   C Y N 418 
TYR CD1  C Y N 419 
TYR CD2  C Y N 420 
TYR CE1  C Y N 421 
TYR CE2  C Y N 422 
TYR CZ   C Y N 423 
TYR OH   O N N 424 
TYR OXT  O N N 425 
TYR H    H N N 426 
TYR H2   H N N 427 
TYR HA   H N N 428 
TYR HB2  H N N 429 
TYR HB3  H N N 430 
TYR HD1  H N N 431 
TYR HD2  H N N 432 
TYR HE1  H N N 433 
TYR HE2  H N N 434 
TYR HH   H N N 435 
TYR HXT  H N N 436 
VAL N    N N N 437 
VAL CA   C N S 438 
VAL C    C N N 439 
VAL O    O N N 440 
VAL CB   C N N 441 
VAL CG1  C N N 442 
VAL CG2  C N N 443 
VAL OXT  O N N 444 
VAL H    H N N 445 
VAL H2   H N N 446 
VAL HA   H N N 447 
VAL HB   H N N 448 
VAL HG11 H N N 449 
VAL HG12 H N N 450 
VAL HG13 H N N 451 
VAL HG21 H N N 452 
VAL HG22 H N N 453 
VAL HG23 H N N 454 
VAL HXT  H N N 455 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLC C1  C2   sing N N 92  
GLC C1  O1   sing N N 93  
GLC C1  O5   sing N N 94  
GLC C1  H1   sing N N 95  
GLC C2  C3   sing N N 96  
GLC C2  O2   sing N N 97  
GLC C2  H2   sing N N 98  
GLC C3  C4   sing N N 99  
GLC C3  O3   sing N N 100 
GLC C3  H3   sing N N 101 
GLC C4  C5   sing N N 102 
GLC C4  O4   sing N N 103 
GLC C4  H4   sing N N 104 
GLC C5  C6   sing N N 105 
GLC C5  O5   sing N N 106 
GLC C5  H5   sing N N 107 
GLC C6  O6   sing N N 108 
GLC C6  H61  sing N N 109 
GLC C6  H62  sing N N 110 
GLC O1  HO1  sing N N 111 
GLC O2  HO2  sing N N 112 
GLC O3  HO3  sing N N 113 
GLC O4  HO4  sing N N 114 
GLC O6  HO6  sing N N 115 
GLN N   CA   sing N N 116 
GLN N   H    sing N N 117 
GLN N   H2   sing N N 118 
GLN CA  C    sing N N 119 
GLN CA  CB   sing N N 120 
GLN CA  HA   sing N N 121 
GLN C   O    doub N N 122 
GLN C   OXT  sing N N 123 
GLN CB  CG   sing N N 124 
GLN CB  HB2  sing N N 125 
GLN CB  HB3  sing N N 126 
GLN CG  CD   sing N N 127 
GLN CG  HG2  sing N N 128 
GLN CG  HG3  sing N N 129 
GLN CD  OE1  doub N N 130 
GLN CD  NE2  sing N N 131 
GLN NE2 HE21 sing N N 132 
GLN NE2 HE22 sing N N 133 
GLN OXT HXT  sing N N 134 
GLU N   CA   sing N N 135 
GLU N   H    sing N N 136 
GLU N   H2   sing N N 137 
GLU CA  C    sing N N 138 
GLU CA  CB   sing N N 139 
GLU CA  HA   sing N N 140 
GLU C   O    doub N N 141 
GLU C   OXT  sing N N 142 
GLU CB  CG   sing N N 143 
GLU CB  HB2  sing N N 144 
GLU CB  HB3  sing N N 145 
GLU CG  CD   sing N N 146 
GLU CG  HG2  sing N N 147 
GLU CG  HG3  sing N N 148 
GLU CD  OE1  doub N N 149 
GLU CD  OE2  sing N N 150 
GLU OE2 HE2  sing N N 151 
GLU OXT HXT  sing N N 152 
GLY N   CA   sing N N 153 
GLY N   H    sing N N 154 
GLY N   H2   sing N N 155 
GLY CA  C    sing N N 156 
GLY CA  HA2  sing N N 157 
GLY CA  HA3  sing N N 158 
GLY C   O    doub N N 159 
GLY C   OXT  sing N N 160 
GLY OXT HXT  sing N N 161 
GOL C1  O1   sing N N 162 
GOL C1  C2   sing N N 163 
GOL C1  H11  sing N N 164 
GOL C1  H12  sing N N 165 
GOL O1  HO1  sing N N 166 
GOL C2  O2   sing N N 167 
GOL C2  C3   sing N N 168 
GOL C2  H2   sing N N 169 
GOL O2  HO2  sing N N 170 
GOL C3  O3   sing N N 171 
GOL C3  H31  sing N N 172 
GOL C3  H32  sing N N 173 
GOL O3  HO3  sing N N 174 
HIS N   CA   sing N N 175 
HIS N   H    sing N N 176 
HIS N   H2   sing N N 177 
HIS CA  C    sing N N 178 
HIS CA  CB   sing N N 179 
HIS CA  HA   sing N N 180 
HIS C   O    doub N N 181 
HIS C   OXT  sing N N 182 
HIS CB  CG   sing N N 183 
HIS CB  HB2  sing N N 184 
HIS CB  HB3  sing N N 185 
HIS CG  ND1  sing Y N 186 
HIS CG  CD2  doub Y N 187 
HIS ND1 CE1  doub Y N 188 
HIS ND1 HD1  sing N N 189 
HIS CD2 NE2  sing Y N 190 
HIS CD2 HD2  sing N N 191 
HIS CE1 NE2  sing Y N 192 
HIS CE1 HE1  sing N N 193 
HIS NE2 HE2  sing N N 194 
HIS OXT HXT  sing N N 195 
HOH O   H1   sing N N 196 
HOH O   H2   sing N N 197 
ILE N   CA   sing N N 198 
ILE N   H    sing N N 199 
ILE N   H2   sing N N 200 
ILE CA  C    sing N N 201 
ILE CA  CB   sing N N 202 
ILE CA  HA   sing N N 203 
ILE C   O    doub N N 204 
ILE C   OXT  sing N N 205 
ILE CB  CG1  sing N N 206 
ILE CB  CG2  sing N N 207 
ILE CB  HB   sing N N 208 
ILE CG1 CD1  sing N N 209 
ILE CG1 HG12 sing N N 210 
ILE CG1 HG13 sing N N 211 
ILE CG2 HG21 sing N N 212 
ILE CG2 HG22 sing N N 213 
ILE CG2 HG23 sing N N 214 
ILE CD1 HD11 sing N N 215 
ILE CD1 HD12 sing N N 216 
ILE CD1 HD13 sing N N 217 
ILE OXT HXT  sing N N 218 
LEU N   CA   sing N N 219 
LEU N   H    sing N N 220 
LEU N   H2   sing N N 221 
LEU CA  C    sing N N 222 
LEU CA  CB   sing N N 223 
LEU CA  HA   sing N N 224 
LEU C   O    doub N N 225 
LEU C   OXT  sing N N 226 
LEU CB  CG   sing N N 227 
LEU CB  HB2  sing N N 228 
LEU CB  HB3  sing N N 229 
LEU CG  CD1  sing N N 230 
LEU CG  CD2  sing N N 231 
LEU CG  HG   sing N N 232 
LEU CD1 HD11 sing N N 233 
LEU CD1 HD12 sing N N 234 
LEU CD1 HD13 sing N N 235 
LEU CD2 HD21 sing N N 236 
LEU CD2 HD22 sing N N 237 
LEU CD2 HD23 sing N N 238 
LEU OXT HXT  sing N N 239 
LYS N   CA   sing N N 240 
LYS N   H    sing N N 241 
LYS N   H2   sing N N 242 
LYS CA  C    sing N N 243 
LYS CA  CB   sing N N 244 
LYS CA  HA   sing N N 245 
LYS C   O    doub N N 246 
LYS C   OXT  sing N N 247 
LYS CB  CG   sing N N 248 
LYS CB  HB2  sing N N 249 
LYS CB  HB3  sing N N 250 
LYS CG  CD   sing N N 251 
LYS CG  HG2  sing N N 252 
LYS CG  HG3  sing N N 253 
LYS CD  CE   sing N N 254 
LYS CD  HD2  sing N N 255 
LYS CD  HD3  sing N N 256 
LYS CE  NZ   sing N N 257 
LYS CE  HE2  sing N N 258 
LYS CE  HE3  sing N N 259 
LYS NZ  HZ1  sing N N 260 
LYS NZ  HZ2  sing N N 261 
LYS NZ  HZ3  sing N N 262 
LYS OXT HXT  sing N N 263 
MET N   CA   sing N N 264 
MET N   H    sing N N 265 
MET N   H2   sing N N 266 
MET CA  C    sing N N 267 
MET CA  CB   sing N N 268 
MET CA  HA   sing N N 269 
MET C   O    doub N N 270 
MET C   OXT  sing N N 271 
MET CB  CG   sing N N 272 
MET CB  HB2  sing N N 273 
MET CB  HB3  sing N N 274 
MET CG  SD   sing N N 275 
MET CG  HG2  sing N N 276 
MET CG  HG3  sing N N 277 
MET SD  CE   sing N N 278 
MET CE  HE1  sing N N 279 
MET CE  HE2  sing N N 280 
MET CE  HE3  sing N N 281 
MET OXT HXT  sing N N 282 
PEG C1  O1   sing N N 283 
PEG C1  C2   sing N N 284 
PEG C1  H11  sing N N 285 
PEG C1  H12  sing N N 286 
PEG O1  HO1  sing N N 287 
PEG C2  O2   sing N N 288 
PEG C2  H21  sing N N 289 
PEG C2  H22  sing N N 290 
PEG O2  C3   sing N N 291 
PEG C3  C4   sing N N 292 
PEG C3  H31  sing N N 293 
PEG C3  H32  sing N N 294 
PEG C4  O4   sing N N 295 
PEG C4  H41  sing N N 296 
PEG C4  H42  sing N N 297 
PEG O4  HO4  sing N N 298 
PHE N   CA   sing N N 299 
PHE N   H    sing N N 300 
PHE N   H2   sing N N 301 
PHE CA  C    sing N N 302 
PHE CA  CB   sing N N 303 
PHE CA  HA   sing N N 304 
PHE C   O    doub N N 305 
PHE C   OXT  sing N N 306 
PHE CB  CG   sing N N 307 
PHE CB  HB2  sing N N 308 
PHE CB  HB3  sing N N 309 
PHE CG  CD1  doub Y N 310 
PHE CG  CD2  sing Y N 311 
PHE CD1 CE1  sing Y N 312 
PHE CD1 HD1  sing N N 313 
PHE CD2 CE2  doub Y N 314 
PHE CD2 HD2  sing N N 315 
PHE CE1 CZ   doub Y N 316 
PHE CE1 HE1  sing N N 317 
PHE CE2 CZ   sing Y N 318 
PHE CE2 HE2  sing N N 319 
PHE CZ  HZ   sing N N 320 
PHE OXT HXT  sing N N 321 
PRO N   CA   sing N N 322 
PRO N   CD   sing N N 323 
PRO N   H    sing N N 324 
PRO CA  C    sing N N 325 
PRO CA  CB   sing N N 326 
PRO CA  HA   sing N N 327 
PRO C   O    doub N N 328 
PRO C   OXT  sing N N 329 
PRO CB  CG   sing N N 330 
PRO CB  HB2  sing N N 331 
PRO CB  HB3  sing N N 332 
PRO CG  CD   sing N N 333 
PRO CG  HG2  sing N N 334 
PRO CG  HG3  sing N N 335 
PRO CD  HD2  sing N N 336 
PRO CD  HD3  sing N N 337 
PRO OXT HXT  sing N N 338 
SER N   CA   sing N N 339 
SER N   H    sing N N 340 
SER N   H2   sing N N 341 
SER CA  C    sing N N 342 
SER CA  CB   sing N N 343 
SER CA  HA   sing N N 344 
SER C   O    doub N N 345 
SER C   OXT  sing N N 346 
SER CB  OG   sing N N 347 
SER CB  HB2  sing N N 348 
SER CB  HB3  sing N N 349 
SER OG  HG   sing N N 350 
SER OXT HXT  sing N N 351 
THR N   CA   sing N N 352 
THR N   H    sing N N 353 
THR N   H2   sing N N 354 
THR CA  C    sing N N 355 
THR CA  CB   sing N N 356 
THR CA  HA   sing N N 357 
THR C   O    doub N N 358 
THR C   OXT  sing N N 359 
THR CB  OG1  sing N N 360 
THR CB  CG2  sing N N 361 
THR CB  HB   sing N N 362 
THR OG1 HG1  sing N N 363 
THR CG2 HG21 sing N N 364 
THR CG2 HG22 sing N N 365 
THR CG2 HG23 sing N N 366 
THR OXT HXT  sing N N 367 
TRP N   CA   sing N N 368 
TRP N   H    sing N N 369 
TRP N   H2   sing N N 370 
TRP CA  C    sing N N 371 
TRP CA  CB   sing N N 372 
TRP CA  HA   sing N N 373 
TRP C   O    doub N N 374 
TRP C   OXT  sing N N 375 
TRP CB  CG   sing N N 376 
TRP CB  HB2  sing N N 377 
TRP CB  HB3  sing N N 378 
TRP CG  CD1  doub Y N 379 
TRP CG  CD2  sing Y N 380 
TRP CD1 NE1  sing Y N 381 
TRP CD1 HD1  sing N N 382 
TRP CD2 CE2  doub Y N 383 
TRP CD2 CE3  sing Y N 384 
TRP NE1 CE2  sing Y N 385 
TRP NE1 HE1  sing N N 386 
TRP CE2 CZ2  sing Y N 387 
TRP CE3 CZ3  doub Y N 388 
TRP CE3 HE3  sing N N 389 
TRP CZ2 CH2  doub Y N 390 
TRP CZ2 HZ2  sing N N 391 
TRP CZ3 CH2  sing Y N 392 
TRP CZ3 HZ3  sing N N 393 
TRP CH2 HH2  sing N N 394 
TRP OXT HXT  sing N N 395 
TYR N   CA   sing N N 396 
TYR N   H    sing N N 397 
TYR N   H2   sing N N 398 
TYR CA  C    sing N N 399 
TYR CA  CB   sing N N 400 
TYR CA  HA   sing N N 401 
TYR C   O    doub N N 402 
TYR C   OXT  sing N N 403 
TYR CB  CG   sing N N 404 
TYR CB  HB2  sing N N 405 
TYR CB  HB3  sing N N 406 
TYR CG  CD1  doub Y N 407 
TYR CG  CD2  sing Y N 408 
TYR CD1 CE1  sing Y N 409 
TYR CD1 HD1  sing N N 410 
TYR CD2 CE2  doub Y N 411 
TYR CD2 HD2  sing N N 412 
TYR CE1 CZ   doub Y N 413 
TYR CE1 HE1  sing N N 414 
TYR CE2 CZ   sing Y N 415 
TYR CE2 HE2  sing N N 416 
TYR CZ  OH   sing N N 417 
TYR OH  HH   sing N N 418 
TYR OXT HXT  sing N N 419 
VAL N   CA   sing N N 420 
VAL N   H    sing N N 421 
VAL N   H2   sing N N 422 
VAL CA  C    sing N N 423 
VAL CA  CB   sing N N 424 
VAL CA  HA   sing N N 425 
VAL C   O    doub N N 426 
VAL C   OXT  sing N N 427 
VAL CB  CG1  sing N N 428 
VAL CB  CG2  sing N N 429 
VAL CB  HB   sing N N 430 
VAL CG1 HG11 sing N N 431 
VAL CG1 HG12 sing N N 432 
VAL CG1 HG13 sing N N 433 
VAL CG2 HG21 sing N N 434 
VAL CG2 HG22 sing N N 435 
VAL CG2 HG23 sing N N 436 
VAL OXT HXT  sing N N 437 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_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 GLC 1 n 
2 GLC 2 n 
2 GLC 3 n 
2 GLC 4 n 
2 GLC 5 n 
2 GLC 6 n 
2 GLC 7 n 
2 GLC 8 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                    9KYR 
_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]   0.024492 
_atom_sites.fract_transf_matrix[1][2]   -0.000389 
_atom_sites.fract_transf_matrix[1][3]   -0.000453 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016254 
_atom_sites.fract_transf_matrix[2][3]   -0.001721 
_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]   0.005147 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . LYS A  1 2   ? -12.542 -25.356 61.103   1.00 33.64  ? 2   LYS A N   1 
ATOM   2     C CA  . LYS A  1 2   ? -12.300 -24.464 59.970   1.00 36.53  ? 2   LYS A CA  1 
ATOM   3     C C   . LYS A  1 2   ? -12.181 -25.252 58.659   1.00 35.81  ? 2   LYS A C   1 
ATOM   4     O O   . LYS A  1 2   ? -11.231 -26.009 58.436   1.00 41.74  ? 2   LYS A O   1 
ATOM   5     C CB  . LYS A  1 2   ? -11.046 -23.626 60.223   1.00 37.85  ? 2   LYS A CB  1 
ATOM   6     C CG  . LYS A  1 2   ? -10.511 -22.884 59.033   1.00 44.08  ? 2   LYS A CG  1 
ATOM   7     C CD  . LYS A  1 2   ? -9.341  -22.018 59.452   1.00 51.48  ? 2   LYS A CD  1 
ATOM   8     C CE  . LYS A  1 2   ? -8.207  -22.069 58.440   1.00 54.84  ? 2   LYS A CE  1 
ATOM   9     N NZ  . LYS A  1 2   ? -7.617  -23.425 58.334   1.00 54.31  ? 2   LYS A NZ  1 
ATOM   10    N N   . LYS A  1 3   ? -13.167 -25.077 57.795   1.00 30.06  ? 3   LYS A N   1 
ATOM   11    C CA  . LYS A  1 3   ? -13.271 -25.837 56.564   1.00 26.91  ? 3   LYS A CA  1 
ATOM   12    C C   . LYS A  1 3   ? -12.825 -25.003 55.367   1.00 26.72  ? 3   LYS A C   1 
ATOM   13    O O   . LYS A  1 3   ? -12.839 -23.769 55.388   1.00 27.57  ? 3   LYS A O   1 
ATOM   14    C CB  . LYS A  1 3   ? -14.710 -26.302 56.353   1.00 27.05  ? 3   LYS A CB  1 
ATOM   15    C CG  . LYS A  1 3   ? -15.232 -27.173 57.452   1.00 39.45  ? 3   LYS A CG  1 
ATOM   16    C CD  . LYS A  1 3   ? -15.306 -28.605 56.997   1.00 43.97  ? 3   LYS A CD  1 
ATOM   17    C CE  . LYS A  1 3   ? -16.020 -29.456 58.025   1.00 53.09  ? 3   LYS A CE  1 
ATOM   18    N NZ  . LYS A  1 3   ? -15.094 -29.842 59.122   1.00 57.05  ? 3   LYS A NZ  1 
ATOM   19    N N   . LEU A  1 4   ? -12.398 -25.699 54.327   1.00 26.61  ? 4   LEU A N   1 
ATOM   20    C CA  . LEU A  1 4   ? -12.253 -25.110 53.000   1.00 23.29  ? 4   LEU A CA  1 
ATOM   21    C C   . LEU A  1 4   ? -13.510 -25.484 52.236   1.00 22.98  ? 4   LEU A C   1 
ATOM   22    O O   . LEU A  1 4   ? -13.846 -26.668 52.158   1.00 24.99  ? 4   LEU A O   1 
ATOM   23    C CB  . LEU A  1 4   ? -11.013 -25.630 52.275   1.00 19.98  ? 4   LEU A CB  1 
ATOM   24    C CG  . LEU A  1 4   ? -10.832 -25.128 50.823   1.00 23.85  ? 4   LEU A CG  1 
ATOM   25    C CD1 . LEU A  1 4   ? -9.377  -24.877 50.543   1.00 28.98  ? 4   LEU A CD1 1 
ATOM   26    C CD2 . LEU A  1 4   ? -11.433 -26.050 49.743   1.00 23.18  ? 4   LEU A CD2 1 
ATOM   27    N N   . PHE A  1 5   ? -14.219 -24.483 51.700   1.00 17.60  ? 5   PHE A N   1 
ATOM   28    C CA  . PHE A  1 5   ? -15.448 -24.748 50.965   1.00 16.95  ? 5   PHE A CA  1 
ATOM   29    C C   . PHE A  1 5   ? -15.113 -24.842 49.478   1.00 21.14  ? 5   PHE A C   1 
ATOM   30    O O   . PHE A  1 5   ? -14.637 -23.876 48.893   1.00 22.55  ? 5   PHE A O   1 
ATOM   31    C CB  . PHE A  1 5   ? -16.487 -23.662 51.212   1.00 21.51  ? 5   PHE A CB  1 
ATOM   32    C CG  . PHE A  1 5   ? -17.022 -23.657 52.623   1.00 29.99  ? 5   PHE A CG  1 
ATOM   33    C CD1 . PHE A  1 5   ? -17.527 -24.810 53.183   1.00 28.99  ? 5   PHE A CD1 1 
ATOM   34    C CD2 . PHE A  1 5   ? -17.014 -22.499 53.377   1.00 29.25  ? 5   PHE A CD2 1 
ATOM   35    C CE1 . PHE A  1 5   ? -18.010 -24.806 54.489   1.00 30.33  ? 5   PHE A CE1 1 
ATOM   36    C CE2 . PHE A  1 5   ? -17.499 -22.496 54.673   1.00 29.01  ? 5   PHE A CE2 1 
ATOM   37    C CZ  . PHE A  1 5   ? -17.998 -23.653 55.220   1.00 29.65  ? 5   PHE A CZ  1 
ATOM   38    N N   . LEU A  1 6   ? -15.370 -26.001 48.882   1.00 18.91  ? 6   LEU A N   1 
ATOM   39    C CA  . LEU A  1 6   ? -14.965 -26.278 47.513   1.00 20.97  ? 6   LEU A CA  1 
ATOM   40    C C   . LEU A  1 6   ? -16.219 -26.407 46.658   1.00 21.53  ? 6   LEU A C   1 
ATOM   41    O O   . LEU A  1 6   ? -17.145 -27.145 47.010   1.00 21.34  ? 6   LEU A O   1 
ATOM   42    C CB  . LEU A  1 6   ? -14.113 -27.554 47.464   1.00 21.40  ? 6   LEU A CB  1 
ATOM   43    C CG  . LEU A  1 6   ? -13.541 -28.038 46.126   1.00 25.64  ? 6   LEU A CG  1 
ATOM   44    C CD1 . LEU A  1 6   ? -12.660 -26.995 45.481   1.00 26.00  ? 6   LEU A CD1 1 
ATOM   45    C CD2 . LEU A  1 6   ? -12.771 -29.336 46.316   1.00 24.19  ? 6   LEU A CD2 1 
ATOM   46    N N   . VAL A  1 7   ? -16.263 -25.693 45.538   1.00 18.34  ? 7   VAL A N   1 
ATOM   47    C CA  . VAL A  1 7   ? -17.458 -25.676 44.703   1.00 23.51  ? 7   VAL A CA  1 
ATOM   48    C C   . VAL A  1 7   ? -17.037 -26.027 43.269   1.00 20.40  ? 7   VAL A C   1 
ATOM   49    O O   . VAL A  1 7   ? -16.386 -25.220 42.600   1.00 21.90  ? 7   VAL A O   1 
ATOM   50    C CB  . VAL A  1 7   ? -18.175 -24.307 44.785   1.00 21.04  ? 7   VAL A CB  1 
ATOM   51    C CG1 . VAL A  1 7   ? -19.549 -24.356 44.150   1.00 28.01  ? 7   VAL A CG1 1 
ATOM   52    C CG2 . VAL A  1 7   ? -18.333 -23.885 46.267   1.00 24.38  ? 7   VAL A CG2 1 
ATOM   53    N N   . PHE A  1 8   ? -17.383 -27.237 42.806   1.00 16.13  ? 8   PHE A N   1 
ATOM   54    C CA  . PHE A  1 8   ? -17.217 -27.587 41.386   1.00 17.98  ? 8   PHE A CA  1 
ATOM   55    C C   . PHE A  1 8   ? -18.453 -27.154 40.612   1.00 20.95  ? 8   PHE A C   1 
ATOM   56    O O   . PHE A  1 8   ? -19.582 -27.391 41.039   1.00 20.98  ? 8   PHE A O   1 
ATOM   57    C CB  . PHE A  1 8   ? -17.022 -29.094 41.171   1.00 20.55  ? 8   PHE A CB  1 
ATOM   58    C CG  . PHE A  1 8   ? -15.686 -29.613 41.621   1.00 26.17  ? 8   PHE A CG  1 
ATOM   59    C CD1 . PHE A  1 8   ? -15.511 -30.057 42.919   1.00 27.35  ? 8   PHE A CD1 1 
ATOM   60    C CD2 . PHE A  1 8   ? -14.613 -29.681 40.742   1.00 29.08  ? 8   PHE A CD2 1 
ATOM   61    C CE1 . PHE A  1 8   ? -14.283 -30.543 43.345   1.00 24.33  ? 8   PHE A CE1 1 
ATOM   62    C CE2 . PHE A  1 8   ? -13.379 -30.164 41.161   1.00 22.57  ? 8   PHE A CE2 1 
ATOM   63    C CZ  . PHE A  1 8   ? -13.213 -30.581 42.464   1.00 26.96  ? 8   PHE A CZ  1 
ATOM   64    N N   . TRP A  1 9   ? -18.242 -26.555 39.446   1.00 22.10  ? 9   TRP A N   1 
ATOM   65    C CA  . TRP A  1 9   ? -19.357 -26.147 38.600   1.00 18.50  ? 9   TRP A CA  1 
ATOM   66    C C   . TRP A  1 9   ? -18.954 -26.524 37.178   1.00 14.40  ? 9   TRP A C   1 
ATOM   67    O O   . TRP A  1 9   ? -18.083 -25.890 36.588   1.00 15.10  ? 9   TRP A O   1 
ATOM   68    C CB  . TRP A  1 9   ? -19.620 -24.661 38.745   1.00 15.04  ? 9   TRP A CB  1 
ATOM   69    C CG  . TRP A  1 9   ? -20.914 -24.140 38.210   1.00 13.61  ? 9   TRP A CG  1 
ATOM   70    C CD1 . TRP A  1 9   ? -21.848 -24.796 37.461   1.00 20.01  ? 9   TRP A CD1 1 
ATOM   71    C CD2 . TRP A  1 9   ? -21.390 -22.813 38.372   1.00 18.80  ? 9   TRP A CD2 1 
ATOM   72    N NE1 . TRP A  1 9   ? -22.888 -23.944 37.148   1.00 16.03  ? 9   TRP A NE1 1 
ATOM   73    C CE2 . TRP A  1 9   ? -22.625 -22.719 37.698   1.00 17.86  ? 9   TRP A CE2 1 
ATOM   74    C CE3 . TRP A  1 9   ? -20.899 -21.692 39.039   1.00 18.24  ? 9   TRP A CE3 1 
ATOM   75    C CZ2 . TRP A  1 9   ? -23.374 -21.555 37.686   1.00 16.62  ? 9   TRP A CZ2 1 
ATOM   76    C CZ3 . TRP A  1 9   ? -21.647 -20.524 39.011   1.00 22.38  ? 9   TRP A CZ3 1 
ATOM   77    C CH2 . TRP A  1 9   ? -22.865 -20.466 38.337   1.00 24.33  ? 9   TRP A CH2 1 
ATOM   78    N N   . TRP A  1 10  ? -19.520 -27.594 36.673   1.00 18.80  ? 10  TRP A N   1 
ATOM   79    C CA  . TRP A  1 10  ? -19.087 -28.116 35.389   1.00 19.67  ? 10  TRP A CA  1 
ATOM   80    C C   . TRP A  1 10  ? -20.014 -27.548 34.322   1.00 16.70  ? 10  TRP A C   1 
ATOM   81    O O   . TRP A  1 10  ? -21.229 -27.754 34.381   1.00 16.76  ? 10  TRP A O   1 
ATOM   82    C CB  . TRP A  1 10  ? -19.124 -29.640 35.374   1.00 17.21  ? 10  TRP A CB  1 
ATOM   83    C CG  . TRP A  1 10  ? -18.213 -30.382 36.352   1.00 18.42  ? 10  TRP A CG  1 
ATOM   84    C CD1 . TRP A  1 10  ? -18.598 -31.117 37.439   1.00 21.49  ? 10  TRP A CD1 1 
ATOM   85    C CD2 . TRP A  1 10  ? -16.792 -30.498 36.273   1.00 18.36  ? 10  TRP A CD2 1 
ATOM   86    N NE1 . TRP A  1 10  ? -17.488 -31.675 38.058   1.00 19.78  ? 10  TRP A NE1 1 
ATOM   87    C CE2 . TRP A  1 10  ? -16.369 -31.304 37.361   1.00 19.27  ? 10  TRP A CE2 1 
ATOM   88    C CE3 . TRP A  1 10  ? -15.822 -29.985 35.394   1.00 24.23  ? 10  TRP A CE3 1 
ATOM   89    C CZ2 . TRP A  1 10  ? -15.030 -31.615 37.585   1.00 18.27  ? 10  TRP A CZ2 1 
ATOM   90    C CZ3 . TRP A  1 10  ? -14.473 -30.307 35.625   1.00 23.83  ? 10  TRP A CZ3 1 
ATOM   91    C CH2 . TRP A  1 10  ? -14.099 -31.112 36.717   1.00 19.99  ? 10  TRP A CH2 1 
ATOM   92    N N   . HIS A  1 11  ? -19.449 -26.868 33.341   1.00 15.04  ? 11  HIS A N   1 
ATOM   93    C CA  . HIS A  1 11  ? -20.252 -26.189 32.327   1.00 22.69  ? 11  HIS A CA  1 
ATOM   94    C C   . HIS A  1 11  ? -20.366 -27.063 31.083   1.00 21.26  ? 11  HIS A C   1 
ATOM   95    O O   . HIS A  1 11  ? -19.344 -27.485 30.537   1.00 21.57  ? 11  HIS A O   1 
ATOM   96    C CB  . HIS A  1 11  ? -19.624 -24.832 31.988   1.00 22.10  ? 11  HIS A CB  1 
ATOM   97    C CG  . HIS A  1 11  ? -20.116 -24.242 30.711   1.00 21.63  ? 11  HIS A CG  1 
ATOM   98    N ND1 . HIS A  1 11  ? -21.455 -24.046 30.447   1.00 20.86  ? 11  HIS A ND1 1 
ATOM   99    C CD2 . HIS A  1 11  ? -19.447 -23.825 29.609   1.00 23.28  ? 11  HIS A CD2 1 
ATOM   100   C CE1 . HIS A  1 11  ? -21.588 -23.535 29.236   1.00 22.55  ? 11  HIS A CE1 1 
ATOM   101   N NE2 . HIS A  1 11  ? -20.385 -23.384 28.712   1.00 21.88  ? 11  HIS A NE2 1 
ATOM   102   N N   . MET A  1 12  ? -21.610 -27.319 30.635   1.00 21.23  ? 12  MET A N   1 
ATOM   103   C CA  . MET A  1 12  ? -21.919 -28.197 29.502   1.00 19.66  ? 12  MET A CA  1 
ATOM   104   C C   . MET A  1 12  ? -22.630 -27.406 28.416   1.00 24.20  ? 12  MET A C   1 
ATOM   105   O O   . MET A  1 12  ? -23.695 -26.824 28.666   1.00 18.62  ? 12  MET A O   1 
ATOM   106   C CB  . MET A  1 12  ? -22.829 -29.370 29.916   1.00 18.19  ? 12  MET A CB  1 
ATOM   107   C CG  . MET A  1 12  ? -22.423 -30.103 31.177   1.00 21.99  ? 12  MET A CG  1 
ATOM   108   S SD  . MET A  1 12  ? -20.773 -30.759 30.994   1.00 20.18  ? 12  MET A SD  1 
ATOM   109   C CE  . MET A  1 12  ? -20.694 -31.872 32.412   1.00 34.58  ? 12  MET A CE  1 
ATOM   110   N N   . HIS A  1 13  ? -22.085 -27.425 27.197   1.00 21.62  ? 13  HIS A N   1 
ATOM   111   C CA  . HIS A  1 13  ? -22.704 -26.643 26.140   1.00 17.42  ? 13  HIS A CA  1 
ATOM   112   C C   . HIS A  1 13  ? -22.347 -27.253 24.782   1.00 17.97  ? 13  HIS A C   1 
ATOM   113   O O   . HIS A  1 13  ? -21.238 -27.752 24.601   1.00 14.57  ? 13  HIS A O   1 
ATOM   114   C CB  . HIS A  1 13  ? -22.254 -25.157 26.230   1.00 13.19  ? 13  HIS A CB  1 
ATOM   115   C CG  . HIS A  1 13  ? -22.562 -24.357 24.997   1.00 22.03  ? 13  HIS A CG  1 
ATOM   116   N ND1 . HIS A  1 13  ? -23.850 -24.165 24.538   1.00 16.79  ? 13  HIS A ND1 1 
ATOM   117   C CD2 . HIS A  1 13  ? -21.749 -23.732 24.109   1.00 19.06  ? 13  HIS A CD2 1 
ATOM   118   C CE1 . HIS A  1 13  ? -23.818 -23.471 23.414   1.00 17.18  ? 13  HIS A CE1 1 
ATOM   119   N NE2 . HIS A  1 13  ? -22.558 -23.190 23.132   1.00 21.76  ? 13  HIS A NE2 1 
ATOM   120   N N   . GLN A  1 14  ? -23.296 -27.207 23.831   1.00 16.43  ? 14  GLN A N   1 
ATOM   121   C CA  . GLN A  1 14  ? -23.015 -27.445 22.401   1.00 14.40  ? 14  GLN A CA  1 
ATOM   122   C C   . GLN A  1 14  ? -23.860 -26.442 21.629   1.00 19.04  ? 14  GLN A C   1 
ATOM   123   O O   . GLN A  1 14  ? -25.054 -26.274 21.941   1.00 17.08  ? 14  GLN A O   1 
ATOM   124   C CB  . GLN A  1 14  ? -23.356 -28.865 21.929   1.00 14.03  ? 14  GLN A CB  1 
ATOM   125   C CG  . GLN A  1 14  ? -22.507 -29.973 22.503   1.00 16.76  ? 14  GLN A CG  1 
ATOM   126   C CD  . GLN A  1 14  ? -21.063 -29.885 22.092   1.00 25.53  ? 14  GLN A CD  1 
ATOM   127   O OE1 . GLN A  1 14  ? -20.704 -29.240 21.082   1.00 21.70  ? 14  GLN A OE1 1 
ATOM   128   N NE2 . GLN A  1 14  ? -20.208 -30.541 22.869   1.00 22.99  ? 14  GLN A NE2 1 
ATOM   129   N N   . PRO A  1 15  ? -23.294 -25.762 20.631   1.00 21.46  ? 15  PRO A N   1 
ATOM   130   C CA  . PRO A  1 15  ? -24.125 -24.974 19.707   1.00 21.31  ? 15  PRO A CA  1 
ATOM   131   C C   . PRO A  1 15  ? -25.100 -25.867 18.948   1.00 17.39  ? 15  PRO A C   1 
ATOM   132   O O   . PRO A  1 15  ? -24.978 -27.088 18.922   1.00 21.87  ? 15  PRO A O   1 
ATOM   133   C CB  . PRO A  1 15  ? -23.102 -24.332 18.752   1.00 18.50  ? 15  PRO A CB  1 
ATOM   134   C CG  . PRO A  1 15  ? -21.871 -25.176 18.851   1.00 18.42  ? 15  PRO A CG  1 
ATOM   135   C CD  . PRO A  1 15  ? -21.857 -25.645 20.332   1.00 17.60  ? 15  PRO A CD  1 
ATOM   136   N N   . LEU A  1 16  ? -26.051 -25.242 18.254   1.00 18.56  ? 16  LEU A N   1 
ATOM   137   C CA  . LEU A  1 16  ? -27.060 -26.004 17.519   1.00 21.94  ? 16  LEU A CA  1 
ATOM   138   C C   . LEU A  1 16  ? -26.466 -26.510 16.205   1.00 24.78  ? 16  LEU A C   1 
ATOM   139   O O   . LEU A  1 16  ? -26.186 -25.723 15.292   1.00 18.69  ? 16  LEU A O   1 
ATOM   140   C CB  . LEU A  1 16  ? -28.300 -25.158 17.265   1.00 21.67  ? 16  LEU A CB  1 
ATOM   141   C CG  . LEU A  1 16  ? -29.468 -25.877 16.598   1.00 22.74  ? 16  LEU A CG  1 
ATOM   142   C CD1 . LEU A  1 16  ? -29.874 -27.094 17.437   1.00 24.34  ? 16  LEU A CD1 1 
ATOM   143   C CD2 . LEU A  1 16  ? -30.645 -24.883 16.394   1.00 19.03  ? 16  LEU A CD2 1 
ATOM   144   N N   . TYR A  1 17  ? -26.265 -27.822 16.116   1.00 23.50  ? 17  TYR A N   1 
ATOM   145   C CA  . TYR A  1 17  ? -25.694 -28.457 14.939   1.00 20.30  ? 17  TYR A CA  1 
ATOM   146   C C   . TYR A  1 17  ? -26.751 -28.844 13.922   1.00 24.61  ? 17  TYR A C   1 
ATOM   147   O O   . TYR A  1 17  ? -26.408 -29.385 12.868   1.00 26.09  ? 17  TYR A O   1 
ATOM   148   C CB  . TYR A  1 17  ? -24.915 -29.714 15.329   1.00 16.78  ? 17  TYR A CB  1 
ATOM   149   C CG  . TYR A  1 17  ? -23.710 -29.450 16.188   1.00 19.31  ? 17  TYR A CG  1 
ATOM   150   C CD1 . TYR A  1 17  ? -22.567 -28.888 15.648   1.00 20.61  ? 17  TYR A CD1 1 
ATOM   151   C CD2 . TYR A  1 17  ? -23.712 -29.785 17.545   1.00 21.24  ? 17  TYR A CD2 1 
ATOM   152   C CE1 . TYR A  1 17  ? -21.445 -28.650 16.430   1.00 21.03  ? 17  TYR A CE1 1 
ATOM   153   C CE2 . TYR A  1 17  ? -22.598 -29.563 18.333   1.00 23.95  ? 17  TYR A CE2 1 
ATOM   154   C CZ  . TYR A  1 17  ? -21.468 -28.984 17.775   1.00 22.82  ? 17  TYR A CZ  1 
ATOM   155   O OH  . TYR A  1 17  ? -20.358 -28.754 18.573   1.00 17.84  ? 17  TYR A OH  1 
ATOM   156   N N   . ARG A  1 18  ? -28.018 -28.612 14.241   1.00 23.40  ? 18  ARG A N   1 
ATOM   157   C CA  . ARG A  1 18  ? -29.133 -29.014 13.403   1.00 22.63  ? 18  ARG A CA  1 
ATOM   158   C C   . ARG A  1 18  ? -29.337 -27.932 12.355   1.00 27.85  ? 18  ARG A C   1 
ATOM   159   O O   . ARG A  1 18  ? -29.761 -26.812 12.676   1.00 26.31  ? 18  ARG A O   1 
ATOM   160   C CB  . ARG A  1 18  ? -30.385 -29.225 14.245   1.00 24.69  ? 18  ARG A CB  1 
ATOM   161   C CG  . ARG A  1 18  ? -31.551 -29.784 13.474   1.00 25.62  ? 18  ARG A CG  1 
ATOM   162   C CD  . ARG A  1 18  ? -32.814 -29.869 14.335   1.00 25.15  ? 18  ARG A CD  1 
ATOM   163   N NE  . ARG A  1 18  ? -33.885 -30.473 13.557   1.00 34.55  ? 18  ARG A NE  1 
ATOM   164   C CZ  . ARG A  1 18  ? -34.673 -29.805 12.718   1.00 33.41  ? 18  ARG A CZ  1 
ATOM   165   N NH1 . ARG A  1 18  ? -34.524 -28.493 12.548   1.00 36.12  ? 18  ARG A NH1 1 
ATOM   166   N NH2 . ARG A  1 18  ? -35.610 -30.450 12.054   1.00 34.97  ? 18  ARG A NH2 1 
ATOM   167   N N   . GLU A  1 19  ? -28.981 -28.254 11.125   1.00 26.01  ? 19  GLU A N   1 
ATOM   168   C CA  . GLU A  1 19  ? -29.210 -27.356 10.002   1.00 28.15  ? 19  GLU A CA  1 
ATOM   169   C C   . GLU A  1 19  ? -30.711 -27.163 9.826    1.00 28.90  ? 19  GLU A C   1 
ATOM   170   O O   . GLU A  1 19  ? -31.453 -28.152 9.804    1.00 31.52  ? 19  GLU A O   1 
ATOM   171   C CB  . GLU A  1 19  ? -28.600 -27.960 8.738    1.00 27.75  ? 19  GLU A CB  1 
ATOM   172   C CG  . GLU A  1 19  ? -28.124 -26.944 7.718    1.00 33.75  ? 19  GLU A CG  1 
ATOM   173   C CD  . GLU A  1 19  ? -29.218 -26.521 6.765    1.00 39.65  ? 19  GLU A CD  1 
ATOM   174   O OE1 . GLU A  1 19  ? -30.213 -27.258 6.632    1.00 39.02  ? 19  GLU A OE1 1 
ATOM   175   O OE2 . GLU A  1 19  ? -29.093 -25.424 6.184    1.00 44.24  ? 19  GLU A OE2 1 
ATOM   176   N N   . PRO A  1 20  ? -31.203 -25.923 9.722    1.00 31.00  ? 20  PRO A N   1 
ATOM   177   C CA  . PRO A  1 20  ? -32.650 -25.704 9.819    1.00 36.81  ? 20  PRO A CA  1 
ATOM   178   C C   . PRO A  1 20  ? -33.424 -26.031 8.550    1.00 41.56  ? 20  PRO A C   1 
ATOM   179   O O   . PRO A  1 20  ? -34.655 -26.143 8.613    1.00 45.08  ? 20  PRO A O   1 
ATOM   180   C CB  . PRO A  1 20  ? -32.747 -24.209 10.165   1.00 34.84  ? 20  PRO A CB  1 
ATOM   181   C CG  . PRO A  1 20  ? -31.540 -23.621 9.525    1.00 31.11  ? 20  PRO A CG  1 
ATOM   182   C CD  . PRO A  1 20  ? -30.459 -24.657 9.594    1.00 28.27  ? 20  PRO A CD  1 
ATOM   183   N N   . TYR A  1 21  ? -32.759 -26.210 7.412    1.00 41.18  ? 21  TYR A N   1 
ATOM   184   C CA  . TYR A  1 21  ? -33.466 -26.499 6.170    1.00 43.92  ? 21  TYR A CA  1 
ATOM   185   C C   . TYR A  1 21  ? -33.582 -27.987 5.876    1.00 44.37  ? 21  TYR A C   1 
ATOM   186   O O   . TYR A  1 21  ? -34.587 -28.416 5.303    1.00 50.47  ? 21  TYR A O   1 
ATOM   187   C CB  . TYR A  1 21  ? -32.777 -25.788 5.000    1.00 40.04  ? 21  TYR A CB  1 
ATOM   188   C CG  . TYR A  1 21  ? -32.989 -24.290 5.038    1.00 41.98  ? 21  TYR A CG  1 
ATOM   189   C CD1 . TYR A  1 21  ? -34.121 -23.717 4.472    1.00 44.26  ? 21  TYR A CD1 1 
ATOM   190   C CD2 . TYR A  1 21  ? -32.071 -23.449 5.660    1.00 40.48  ? 21  TYR A CD2 1 
ATOM   191   C CE1 . TYR A  1 21  ? -34.328 -22.353 4.508    1.00 47.96  ? 21  TYR A CE1 1 
ATOM   192   C CE2 . TYR A  1 21  ? -32.269 -22.072 5.704    1.00 43.60  ? 21  TYR A CE2 1 
ATOM   193   C CZ  . TYR A  1 21  ? -33.402 -21.533 5.125    1.00 46.03  ? 21  TYR A CZ  1 
ATOM   194   O OH  . TYR A  1 21  ? -33.629 -20.180 5.148    1.00 44.86  ? 21  TYR A OH  1 
ATOM   195   N N   . THR A  1 22  ? -32.580 -28.777 6.256    1.00 41.75  ? 22  THR A N   1 
ATOM   196   C CA  . THR A  1 22  ? -32.626 -30.232 6.162    1.00 38.89  ? 22  THR A CA  1 
ATOM   197   C C   . THR A  1 22  ? -33.063 -30.888 7.459    1.00 40.96  ? 22  THR A C   1 
ATOM   198   O O   . THR A  1 22  ? -33.601 -31.997 7.433    1.00 45.72  ? 22  THR A O   1 
ATOM   199   C CB  . THR A  1 22  ? -31.246 -30.784 5.794    1.00 32.10  ? 22  THR A CB  1 
ATOM   200   O OG1 . THR A  1 22  ? -30.271 -30.257 6.707    1.00 25.20  ? 22  THR A OG1 1 
ATOM   201   C CG2 . THR A  1 22  ? -30.875 -30.383 4.400    1.00 28.78  ? 22  THR A CG2 1 
ATOM   202   N N   . GLY A  1 23  ? -32.842 -30.232 8.593    1.00 39.45  ? 23  GLY A N   1 
ATOM   203   C CA  . GLY A  1 23  ? -33.046 -30.889 9.860    1.00 40.53  ? 23  GLY A CA  1 
ATOM   204   C C   . GLY A  1 23  ? -31.967 -31.883 10.220   1.00 40.87  ? 23  GLY A C   1 
ATOM   205   O O   . GLY A  1 23  ? -32.173 -32.705 11.120   1.00 41.79  ? 23  GLY A O   1 
ATOM   206   N N   . GLU A  1 24  ? -30.810 -31.831 9.559    1.00 33.96  ? 24  GLU A N   1 
ATOM   207   C CA  . GLU A  1 24  ? -29.722 -32.759 9.842    1.00 29.03  ? 24  GLU A CA  1 
ATOM   208   C C   . GLU A  1 24  ? -28.724 -32.144 10.813   1.00 26.03  ? 24  GLU A C   1 
ATOM   209   O O   . GLU A  1 24  ? -28.346 -30.971 10.674   1.00 22.42  ? 24  GLU A O   1 
ATOM   210   C CB  . GLU A  1 24  ? -29.017 -33.176 8.556    1.00 28.43  ? 24  GLU A CB  1 
ATOM   211   C CG  . GLU A  1 24  ? -29.884 -34.052 7.687    1.00 37.90  ? 24  GLU A CG  1 
ATOM   212   C CD  . GLU A  1 24  ? -29.146 -34.529 6.471    1.00 49.17  ? 24  GLU A CD  1 
ATOM   213   O OE1 . GLU A  1 24  ? -28.540 -33.671 5.791    1.00 49.00  ? 24  GLU A OE1 1 
ATOM   214   O OE2 . GLU A  1 24  ? -29.165 -35.751 6.206    1.00 57.72  ? 24  GLU A OE2 1 
ATOM   215   N N   . TYR A  1 25  ? -28.329 -32.931 11.818   1.00 27.90  ? 25  TYR A N   1 
ATOM   216   C CA  . TYR A  1 25  ? -27.189 -32.582 12.662   1.00 28.24  ? 25  TYR A CA  1 
ATOM   217   C C   . TYR A  1 25  ? -25.926 -32.817 11.852   1.00 26.45  ? 25  TYR A C   1 
ATOM   218   O O   . TYR A  1 25  ? -25.595 -33.964 11.524   1.00 29.44  ? 25  TYR A O   1 
ATOM   219   C CB  . TYR A  1 25  ? -27.170 -33.396 13.957   1.00 22.61  ? 25  TYR A CB  1 
ATOM   220   C CG  . TYR A  1 25  ? -28.192 -32.935 14.955   1.00 25.02  ? 25  TYR A CG  1 
ATOM   221   C CD1 . TYR A  1 25  ? -29.548 -33.100 14.708   1.00 28.59  ? 25  TYR A CD1 1 
ATOM   222   C CD2 . TYR A  1 25  ? -27.806 -32.318 16.142   1.00 27.50  ? 25  TYR A CD2 1 
ATOM   223   C CE1 . TYR A  1 25  ? -30.498 -32.662 15.614   1.00 27.25  ? 25  TYR A CE1 1 
ATOM   224   C CE2 . TYR A  1 25  ? -28.739 -31.884 17.047   1.00 29.38  ? 25  TYR A CE2 1 
ATOM   225   C CZ  . TYR A  1 25  ? -30.083 -32.059 16.777   1.00 29.73  ? 25  TYR A CZ  1 
ATOM   226   O OH  . TYR A  1 25  ? -31.009 -31.614 17.683   1.00 28.37  ? 25  TYR A OH  1 
ATOM   227   N N   . LEU A  1 26  ? -25.234 -31.729 11.519   1.00 26.68  ? 26  LEU A N   1 
ATOM   228   C CA  . LEU A  1 26  ? -24.146 -31.756 10.550   1.00 27.98  ? 26  LEU A CA  1 
ATOM   229   C C   . LEU A  1 26  ? -22.826 -32.198 11.153   1.00 31.25  ? 26  LEU A C   1 
ATOM   230   O O   . LEU A  1 26  ? -21.883 -32.495 10.399   1.00 27.02  ? 26  LEU A O   1 
ATOM   231   C CB  . LEU A  1 26  ? -23.990 -30.375 9.913    1.00 20.80  ? 26  LEU A CB  1 
ATOM   232   C CG  . LEU A  1 26  ? -25.192 -30.011 9.048    1.00 25.39  ? 26  LEU A CG  1 
ATOM   233   C CD1 . LEU A  1 26  ? -25.027 -28.605 8.468    1.00 27.51  ? 26  LEU A CD1 1 
ATOM   234   C CD2 . LEU A  1 26  ? -25.391 -31.045 7.952    1.00 24.77  ? 26  LEU A CD2 1 
ATOM   235   N N   . LEU A  1 27  ? -22.752 -32.233 12.483   1.00 25.49  ? 27  LEU A N   1 
ATOM   236   C CA  . LEU A  1 27  ? -21.598 -32.637 13.262   1.00 25.49  ? 27  LEU A CA  1 
ATOM   237   C C   . LEU A  1 27  ? -22.147 -33.452 14.422   1.00 27.29  ? 27  LEU A C   1 
ATOM   238   O O   . LEU A  1 27  ? -23.215 -33.110 14.958   1.00 25.97  ? 27  LEU A O   1 
ATOM   239   C CB  . LEU A  1 27  ? -20.811 -31.437 13.790   1.00 23.32  ? 27  LEU A CB  1 
ATOM   240   C CG  . LEU A  1 27  ? -19.954 -30.693 12.763   1.00 25.60  ? 27  LEU A CG  1 
ATOM   241   C CD1 . LEU A  1 27  ? -19.415 -29.409 13.394   1.00 24.50  ? 27  LEU A CD1 1 
ATOM   242   C CD2 . LEU A  1 27  ? -18.825 -31.606 12.288   1.00 30.09  ? 27  LEU A CD2 1 
ATOM   243   N N   . PRO A  1 28  ? -21.454 -34.521 14.818   1.00 21.90  ? 28  PRO A N   1 
ATOM   244   C CA  . PRO A  1 28  ? -21.982 -35.453 15.823   1.00 20.08  ? 28  PRO A CA  1 
ATOM   245   C C   . PRO A  1 28  ? -21.620 -35.102 17.264   1.00 23.73  ? 28  PRO A C   1 
ATOM   246   O O   . PRO A  1 28  ? -21.807 -35.952 18.144   1.00 21.31  ? 28  PRO A O   1 
ATOM   247   C CB  . PRO A  1 28  ? -21.310 -36.767 15.406   1.00 22.73  ? 28  PRO A CB  1 
ATOM   248   C CG  . PRO A  1 28  ? -19.923 -36.316 14.920   1.00 19.33  ? 28  PRO A CG  1 
ATOM   249   C CD  . PRO A  1 28  ? -20.108 -34.918 14.355   1.00 21.82  ? 28  PRO A CD  1 
ATOM   250   N N   . TRP A  1 29  ? -21.124 -33.878 17.520   1.00 16.98  ? 29  TRP A N   1 
ATOM   251   C CA  . TRP A  1 29  ? -20.468 -33.577 18.796   1.00 19.66  ? 29  TRP A CA  1 
ATOM   252   C C   . TRP A  1 29  ? -21.436 -33.607 19.970   1.00 22.83  ? 29  TRP A C   1 
ATOM   253   O O   . TRP A  1 29  ? -21.025 -33.894 21.102   1.00 20.57  ? 29  TRP A O   1 
ATOM   254   C CB  . TRP A  1 29  ? -19.788 -32.207 18.740   1.00 14.51  ? 29  TRP A CB  1 
ATOM   255   C CG  . TRP A  1 29  ? -18.621 -32.112 17.774   1.00 22.13  ? 29  TRP A CG  1 
ATOM   256   C CD1 . TRP A  1 29  ? -18.425 -31.153 16.839   1.00 20.18  ? 29  TRP A CD1 1 
ATOM   257   C CD2 . TRP A  1 29  ? -17.488 -32.993 17.690   1.00 29.00  ? 29  TRP A CD2 1 
ATOM   258   N NE1 . TRP A  1 29  ? -17.238 -31.360 16.181   1.00 23.82  ? 29  TRP A NE1 1 
ATOM   259   C CE2 . TRP A  1 29  ? -16.648 -32.492 16.677   1.00 26.80  ? 29  TRP A CE2 1 
ATOM   260   C CE3 . TRP A  1 29  ? -17.097 -34.142 18.384   1.00 29.52  ? 29  TRP A CE3 1 
ATOM   261   C CZ2 . TRP A  1 29  ? -15.446 -33.098 16.335   1.00 27.14  ? 29  TRP A CZ2 1 
ATOM   262   C CZ3 . TRP A  1 29  ? -15.899 -34.747 18.042   1.00 30.74  ? 29  TRP A CZ3 1 
ATOM   263   C CH2 . TRP A  1 29  ? -15.089 -34.224 17.020   1.00 30.17  ? 29  TRP A CH2 1 
ATOM   264   N N   . THR A  1 30  ? -22.706 -33.259 19.749   1.00 22.73  ? 30  THR A N   1 
ATOM   265   C CA  . THR A  1 30  ? -23.672 -33.381 20.840   1.00 23.83  ? 30  THR A CA  1 
ATOM   266   C C   . THR A  1 30  ? -23.876 -34.838 21.219   1.00 24.91  ? 30  THR A C   1 
ATOM   267   O O   . THR A  1 30  ? -23.858 -35.196 22.409   1.00 22.96  ? 30  THR A O   1 
ATOM   268   C CB  . THR A  1 30  ? -24.989 -32.745 20.437   1.00 20.13  ? 30  THR A CB  1 
ATOM   269   O OG1 . THR A  1 30  ? -24.787 -31.337 20.304   1.00 23.94  ? 30  THR A OG1 1 
ATOM   270   C CG2 . THR A  1 30  ? -26.042 -33.025 21.477   1.00 18.87  ? 30  THR A CG2 1 
ATOM   271   N N   . PHE A  1 31  ? -24.050 -35.697 20.213   1.00 22.17  ? 31  PHE A N   1 
ATOM   272   C CA  . PHE A  1 31  ? -24.180 -37.133 20.455   1.00 22.50  ? 31  PHE A CA  1 
ATOM   273   C C   . PHE A  1 31  ? -22.974 -37.685 21.207   1.00 22.31  ? 31  PHE A C   1 
ATOM   274   O O   . PHE A  1 31  ? -23.127 -38.354 22.235   1.00 21.70  ? 31  PHE A O   1 
ATOM   275   C CB  . PHE A  1 31  ? -24.359 -37.882 19.133   1.00 26.59  ? 31  PHE A CB  1 
ATOM   276   C CG  . PHE A  1 31  ? -24.389 -39.379 19.302   1.00 23.59  ? 31  PHE A CG  1 
ATOM   277   C CD1 . PHE A  1 31  ? -25.557 -40.021 19.695   1.00 22.00  ? 31  PHE A CD1 1 
ATOM   278   C CD2 . PHE A  1 31  ? -23.250 -40.139 19.102   1.00 23.90  ? 31  PHE A CD2 1 
ATOM   279   C CE1 . PHE A  1 31  ? -25.592 -41.388 19.869   1.00 25.52  ? 31  PHE A CE1 1 
ATOM   280   C CE2 . PHE A  1 31  ? -23.278 -41.519 19.283   1.00 27.93  ? 31  PHE A CE2 1 
ATOM   281   C CZ  . PHE A  1 31  ? -24.454 -42.142 19.672   1.00 28.79  ? 31  PHE A CZ  1 
ATOM   282   N N   . PHE A  1 32  ? -21.762 -37.411 20.715   1.00 22.41  ? 32  PHE A N   1 
ATOM   283   C CA  . PHE A  1 32  ? -20.569 -38.018 21.314   1.00 21.60  ? 32  PHE A CA  1 
ATOM   284   C C   . PHE A  1 32  ? -20.290 -37.483 22.724   1.00 20.14  ? 32  PHE A C   1 
ATOM   285   O O   . PHE A  1 32  ? -19.898 -38.251 23.598   1.00 18.32  ? 32  PHE A O   1 
ATOM   286   C CB  . PHE A  1 32  ? -19.359 -37.803 20.407   1.00 19.95  ? 32  PHE A CB  1 
ATOM   287   C CG  . PHE A  1 32  ? -19.279 -38.781 19.269   1.00 25.59  ? 32  PHE A CG  1 
ATOM   288   C CD1 . PHE A  1 32  ? -19.451 -40.138 19.490   1.00 22.64  ? 32  PHE A CD1 1 
ATOM   289   C CD2 . PHE A  1 32  ? -19.048 -38.339 17.968   1.00 22.15  ? 32  PHE A CD2 1 
ATOM   290   C CE1 . PHE A  1 32  ? -19.381 -41.036 18.449   1.00 24.94  ? 32  PHE A CE1 1 
ATOM   291   C CE2 . PHE A  1 32  ? -18.981 -39.228 16.922   1.00 24.80  ? 32  PHE A CE2 1 
ATOM   292   C CZ  . PHE A  1 32  ? -19.143 -40.576 17.145   1.00 21.15  ? 32  PHE A CZ  1 
ATOM   293   N N   . HIS A  1 33  ? -20.490 -36.180 22.986   1.00 17.82  ? 33  HIS A N   1 
ATOM   294   C CA  . HIS A  1 33  ? -20.309 -35.718 24.370   1.00 14.61  ? 33  HIS A CA  1 
ATOM   295   C C   . HIS A  1 33  ? -21.471 -36.126 25.270   1.00 16.16  ? 33  HIS A C   1 
ATOM   296   O O   . HIS A  1 33  ? -21.320 -36.172 26.504   1.00 14.14  ? 33  HIS A O   1 
ATOM   297   C CB  . HIS A  1 33  ? -20.094 -34.189 24.423   1.00 13.64  ? 33  HIS A CB  1 
ATOM   298   C CG  . HIS A  1 33  ? -18.723 -33.773 23.972   1.00 16.06  ? 33  HIS A CG  1 
ATOM   299   N ND1 . HIS A  1 33  ? -17.580 -34.082 24.675   1.00 20.01  ? 33  HIS A ND1 1 
ATOM   300   C CD2 . HIS A  1 33  ? -18.307 -33.180 22.827   1.00 18.92  ? 33  HIS A CD2 1 
ATOM   301   C CE1 . HIS A  1 33  ? -16.520 -33.646 24.014   1.00 20.52  ? 33  HIS A CE1 1 
ATOM   302   N NE2 . HIS A  1 33  ? -16.934 -33.102 22.885   1.00 20.25  ? 33  HIS A NE2 1 
ATOM   303   N N   . ALA A  1 34  ? -22.619 -36.470 24.695   1.00 18.63  ? 34  ALA A N   1 
ATOM   304   C CA  . ALA A  1 34  ? -23.688 -37.023 25.517   1.00 24.09  ? 34  ALA A CA  1 
ATOM   305   C C   . ALA A  1 34  ? -23.350 -38.445 25.969   1.00 29.36  ? 34  ALA A C   1 
ATOM   306   O O   . ALA A  1 34  ? -23.423 -38.760 27.165   1.00 28.54  ? 34  ALA A O   1 
ATOM   307   C CB  . ALA A  1 34  ? -25.011 -36.978 24.759   1.00 19.38  ? 34  ALA A CB  1 
ATOM   308   N N   . VAL A  1 35  ? -22.938 -39.314 25.039   1.00 22.65  ? 35  VAL A N   1 
ATOM   309   C CA  . VAL A  1 35  ? -22.671 -40.696 25.449   1.00 22.92  ? 35  VAL A CA  1 
ATOM   310   C C   . VAL A  1 35  ? -21.439 -40.773 26.343   1.00 18.39  ? 35  VAL A C   1 
ATOM   311   O O   . VAL A  1 35  ? -21.316 -41.704 27.141   1.00 21.25  ? 35  VAL A O   1 
ATOM   312   C CB  . VAL A  1 35  ? -22.519 -41.645 24.243   1.00 22.05  ? 35  VAL A CB  1 
ATOM   313   C CG1 . VAL A  1 35  ? -23.803 -41.655 23.387   1.00 20.66  ? 35  VAL A CG1 1 
ATOM   314   C CG2 . VAL A  1 35  ? -21.299 -41.255 23.407   1.00 16.47  ? 35  VAL A CG2 1 
ATOM   315   N N   . LYS A  1 36  ? -20.507 -39.831 26.203   1.00 23.15  ? 36  LYS A N   1 
ATOM   316   C CA  . LYS A  1 36  ? -19.247 -39.836 26.944   1.00 24.60  ? 36  LYS A CA  1 
ATOM   317   C C   . LYS A  1 36  ? -19.330 -39.059 28.252   1.00 22.50  ? 36  LYS A C   1 
ATOM   318   O O   . LYS A  1 36  ? -18.909 -39.568 29.299   1.00 20.47  ? 36  LYS A O   1 
ATOM   319   C CB  . LYS A  1 36  ? -18.113 -39.247 26.087   1.00 21.97  ? 36  LYS A CB  1 
ATOM   320   C CG  . LYS A  1 36  ? -16.742 -39.427 26.739   1.00 18.91  ? 36  LYS A CG  1 
ATOM   321   C CD  . LYS A  1 36  ? -15.582 -39.097 25.758   1.00 20.82  ? 36  LYS A CD  1 
ATOM   322   C CE  . LYS A  1 36  ? -15.350 -37.598 25.618   1.00 25.73  ? 36  LYS A CE  1 
ATOM   323   N NZ  . LYS A  1 36  ? -14.878 -36.982 26.899   1.00 25.80  ? 36  LYS A NZ  1 
ATOM   324   N N   . ASP A  1 37  ? -19.837 -37.813 28.214   1.00 22.90  ? 37  ASP A N   1 
ATOM   325   C CA  . ASP A  1 37  ? -19.699 -36.922 29.369   1.00 22.77  ? 37  ASP A CA  1 
ATOM   326   C C   . ASP A  1 37  ? -21.008 -36.465 30.000   1.00 25.38  ? 37  ASP A C   1 
ATOM   327   O O   . ASP A  1 37  ? -21.074 -36.345 31.229   1.00 23.52  ? 37  ASP A O   1 
ATOM   328   C CB  . ASP A  1 37  ? -18.868 -35.697 28.978   1.00 21.16  ? 37  ASP A CB  1 
ATOM   329   C CG  . ASP A  1 37  ? -17.662 -36.075 28.125   1.00 25.49  ? 37  ASP A CG  1 
ATOM   330   O OD1 . ASP A  1 37  ? -16.679 -36.659 28.667   1.00 22.84  ? 37  ASP A OD1 1 
ATOM   331   O OD2 . ASP A  1 37  ? -17.725 -35.821 26.899   1.00 18.37  ? 37  ASP A OD2 1 
ATOM   332   N N   . TYR A  1 38  ? -22.059 -36.191 29.223   1.00 17.58  ? 38  TYR A N   1 
ATOM   333   C CA  . TYR A  1 38  ? -23.150 -35.405 29.799   1.00 20.83  ? 38  TYR A CA  1 
ATOM   334   C C   . TYR A  1 38  ? -23.972 -36.213 30.796   1.00 23.48  ? 38  TYR A C   1 
ATOM   335   O O   . TYR A  1 38  ? -24.495 -35.642 31.759   1.00 22.97  ? 38  TYR A O   1 
ATOM   336   C CB  . TYR A  1 38  ? -24.042 -34.818 28.695   1.00 21.34  ? 38  TYR A CB  1 
ATOM   337   C CG  . TYR A  1 38  ? -23.370 -33.730 27.872   1.00 19.32  ? 38  TYR A CG  1 
ATOM   338   C CD1 . TYR A  1 38  ? -22.435 -32.875 28.444   1.00 15.76  ? 38  TYR A CD1 1 
ATOM   339   C CD2 . TYR A  1 38  ? -23.668 -33.564 26.516   1.00 23.53  ? 38  TYR A CD2 1 
ATOM   340   C CE1 . TYR A  1 38  ? -21.810 -31.864 27.699   1.00 23.45  ? 38  TYR A CE1 1 
ATOM   341   C CE2 . TYR A  1 38  ? -23.038 -32.563 25.746   1.00 20.41  ? 38  TYR A CE2 1 
ATOM   342   C CZ  . TYR A  1 38  ? -22.116 -31.722 26.335   1.00 25.75  ? 38  TYR A CZ  1 
ATOM   343   O OH  . TYR A  1 38  ? -21.505 -30.725 25.590   1.00 23.62  ? 38  TYR A OH  1 
ATOM   344   N N   . TYR A  1 39  ? -24.095 -37.533 30.605   1.00 22.35  ? 39  TYR A N   1 
ATOM   345   C CA  . TYR A  1 39  ? -24.715 -38.341 31.650   1.00 23.54  ? 39  TYR A CA  1 
ATOM   346   C C   . TYR A  1 39  ? -23.685 -38.727 32.702   1.00 22.52  ? 39  TYR A C   1 
ATOM   347   O O   . TYR A  1 39  ? -23.964 -38.708 33.911   1.00 17.21  ? 39  TYR A O   1 
ATOM   348   C CB  . TYR A  1 39  ? -25.352 -39.594 31.049   1.00 20.18  ? 39  TYR A CB  1 
ATOM   349   C CG  . TYR A  1 39  ? -25.793 -40.620 32.079   1.00 26.37  ? 39  TYR A CG  1 
ATOM   350   C CD1 . TYR A  1 39  ? -27.079 -40.588 32.618   1.00 24.69  ? 39  TYR A CD1 1 
ATOM   351   C CD2 . TYR A  1 39  ? -24.931 -41.642 32.498   1.00 23.94  ? 39  TYR A CD2 1 
ATOM   352   C CE1 . TYR A  1 39  ? -27.491 -41.532 33.562   1.00 25.97  ? 39  TYR A CE1 1 
ATOM   353   C CE2 . TYR A  1 39  ? -25.331 -42.575 33.433   1.00 26.91  ? 39  TYR A CE2 1 
ATOM   354   C CZ  . TYR A  1 39  ? -26.606 -42.516 33.963   1.00 26.49  ? 39  TYR A CZ  1 
ATOM   355   O OH  . TYR A  1 39  ? -26.985 -43.458 34.884   1.00 22.15  ? 39  TYR A OH  1 
ATOM   356   N N   . ASP A  1 40  ? -22.476 -39.033 32.249   1.00 20.00  ? 40  ASP A N   1 
ATOM   357   C CA  . ASP A  1 40  ? -21.493 -39.642 33.115   1.00 22.42  ? 40  ASP A CA  1 
ATOM   358   C C   . ASP A  1 40  ? -20.898 -38.678 34.124   1.00 24.98  ? 40  ASP A C   1 
ATOM   359   O O   . ASP A  1 40  ? -20.556 -39.113 35.226   1.00 27.35  ? 40  ASP A O   1 
ATOM   360   C CB  . ASP A  1 40  ? -20.419 -40.284 32.255   1.00 26.38  ? 40  ASP A CB  1 
ATOM   361   C CG  . ASP A  1 40  ? -20.770 -41.717 31.910   1.00 26.49  ? 40  ASP A CG  1 
ATOM   362   O OD1 . ASP A  1 40  ? -20.755 -42.503 32.859   1.00 28.73  ? 40  ASP A OD1 1 
ATOM   363   O OD2 . ASP A  1 40  ? -21.103 -42.046 30.733   1.00 20.77  ? 40  ASP A OD2 1 
ATOM   364   N N   . MET A  1 41  ? -20.803 -37.373 33.802   1.00 26.10  ? 41  MET A N   1 
ATOM   365   C CA  . MET A  1 41  ? -20.267 -36.424 34.775   1.00 26.94  ? 41  MET A CA  1 
ATOM   366   C C   . MET A  1 41  ? -21.151 -36.306 36.015   1.00 25.67  ? 41  MET A C   1 
ATOM   367   O O   . MET A  1 41  ? -20.625 -36.460 37.132   1.00 23.83  ? 41  MET A O   1 
ATOM   368   C CB  . MET A  1 41  ? -20.010 -35.070 34.095   1.00 19.42  ? 41  MET A CB  1 
ATOM   369   C CG  . MET A  1 41  ? -18.720 -35.074 33.223   1.00 21.50  ? 41  MET A CG  1 
ATOM   370   S SD  . MET A  1 41  ? -17.249 -35.191 34.272   1.00 22.52  ? 41  MET A SD  1 
ATOM   371   C CE  . MET A  1 41  ? -17.029 -33.500 34.794   1.00 27.36  ? 41  MET A CE  1 
ATOM   372   N N   . PRO A  1 42  ? -22.471 -36.075 35.915   1.00 25.05  ? 42  PRO A N   1 
ATOM   373   C CA  . PRO A  1 42  ? -23.305 -36.198 37.123   1.00 20.03  ? 42  PRO A CA  1 
ATOM   374   C C   . PRO A  1 42  ? -23.399 -37.614 37.672   1.00 22.22  ? 42  PRO A C   1 
ATOM   375   O O   . PRO A  1 42  ? -23.613 -37.767 38.887   1.00 26.57  ? 42  PRO A O   1 
ATOM   376   C CB  . PRO A  1 42  ? -24.676 -35.684 36.669   1.00 19.24  ? 42  PRO A CB  1 
ATOM   377   C CG  . PRO A  1 42  ? -24.660 -35.853 35.137   1.00 18.94  ? 42  PRO A CG  1 
ATOM   378   C CD  . PRO A  1 42  ? -23.254 -35.609 34.744   1.00 22.07  ? 42  PRO A CD  1 
ATOM   379   N N   . ALA A  1 43  ? -23.247 -38.655 36.852   1.00 18.07  ? 43  ALA A N   1 
ATOM   380   C CA  . ALA A  1 43  ? -23.377 -40.008 37.401   1.00 23.33  ? 43  ALA A CA  1 
ATOM   381   C C   . ALA A  1 43  ? -22.300 -40.333 38.428   1.00 26.21  ? 43  ALA A C   1 
ATOM   382   O O   . ALA A  1 43  ? -22.496 -41.249 39.233   1.00 22.25  ? 43  ALA A O   1 
ATOM   383   C CB  . ALA A  1 43  ? -23.352 -41.070 36.300   1.00 18.68  ? 43  ALA A CB  1 
ATOM   384   N N   . TYR A  1 44  ? -21.175 -39.606 38.442   1.00 26.22  ? 44  TYR A N   1 
ATOM   385   C CA  . TYR A  1 44  ? -20.205 -39.815 39.516   1.00 25.87  ? 44  TYR A CA  1 
ATOM   386   C C   . TYR A  1 44  ? -20.853 -39.646 40.896   1.00 25.19  ? 44  TYR A C   1 
ATOM   387   O O   . TYR A  1 44  ? -20.445 -40.297 41.865   1.00 25.99  ? 44  TYR A O   1 
ATOM   388   C CB  . TYR A  1 44  ? -19.051 -38.831 39.371   1.00 22.60  ? 44  TYR A CB  1 
ATOM   389   C CG  . TYR A  1 44  ? -18.006 -39.205 38.354   1.00 24.02  ? 44  TYR A CG  1 
ATOM   390   C CD1 . TYR A  1 44  ? -16.924 -40.012 38.708   1.00 23.33  ? 44  TYR A CD1 1 
ATOM   391   C CD2 . TYR A  1 44  ? -18.090 -38.742 37.043   1.00 23.36  ? 44  TYR A CD2 1 
ATOM   392   C CE1 . TYR A  1 44  ? -15.944 -40.333 37.800   1.00 23.31  ? 44  TYR A CE1 1 
ATOM   393   C CE2 . TYR A  1 44  ? -17.134 -39.067 36.116   1.00 20.62  ? 44  TYR A CE2 1 
ATOM   394   C CZ  . TYR A  1 44  ? -16.051 -39.869 36.496   1.00 22.99  ? 44  TYR A CZ  1 
ATOM   395   O OH  . TYR A  1 44  ? -15.073 -40.215 35.573   1.00 22.03  ? 44  TYR A OH  1 
ATOM   396   N N   . LEU A  1 45  ? -21.858 -38.773 40.999   1.00 27.79  ? 45  LEU A N   1 
ATOM   397   C CA  . LEU A  1 45  ? -22.525 -38.527 42.273   1.00 31.28  ? 45  LEU A CA  1 
ATOM   398   C C   . LEU A  1 45  ? -23.259 -39.764 42.805   1.00 28.66  ? 45  LEU A C   1 
ATOM   399   O O   . LEU A  1 45  ? -23.631 -39.794 43.990   1.00 22.24  ? 45  LEU A O   1 
ATOM   400   C CB  . LEU A  1 45  ? -23.481 -37.324 42.123   1.00 22.35  ? 45  LEU A CB  1 
ATOM   401   C CG  . LEU A  1 45  ? -22.827 -35.945 41.895   1.00 22.41  ? 45  LEU A CG  1 
ATOM   402   C CD1 . LEU A  1 45  ? -23.855 -34.887 41.534   1.00 20.53  ? 45  LEU A CD1 1 
ATOM   403   C CD2 . LEU A  1 45  ? -21.977 -35.457 43.095   1.00 19.37  ? 45  LEU A CD2 1 
ATOM   404   N N   . LYS A  1 46  ? -23.474 -40.781 41.972   1.00 29.55  ? 46  LYS A N   1 
ATOM   405   C CA  . LYS A  1 46  ? -24.009 -42.052 42.459   1.00 35.67  ? 46  LYS A CA  1 
ATOM   406   C C   . LYS A  1 46  ? -22.996 -42.818 43.299   1.00 37.44  ? 46  LYS A C   1 
ATOM   407   O O   . LYS A  1 46  ? -23.387 -43.651 44.120   1.00 34.71  ? 46  LYS A O   1 
ATOM   408   C CB  . LYS A  1 46  ? -24.434 -42.938 41.289   1.00 39.94  ? 46  LYS A CB  1 
ATOM   409   C CG  . LYS A  1 46  ? -25.542 -42.364 40.416   1.00 40.99  ? 46  LYS A CG  1 
ATOM   410   C CD  . LYS A  1 46  ? -25.656 -43.155 39.123   1.00 46.62  ? 46  LYS A CD  1 
ATOM   411   C CE  . LYS A  1 46  ? -27.106 -43.292 38.681   1.00 53.15  ? 46  LYS A CE  1 
ATOM   412   N NZ  . LYS A  1 46  ? -27.506 -44.727 38.525   1.00 56.42  ? 46  LYS A NZ  1 
ATOM   413   N N   . ASP A  1 47  ? -21.708 -42.573 43.101   1.00 39.65  ? 47  ASP A N   1 
ATOM   414   C CA  . ASP A  1 47  ? -20.678 -43.375 43.736   1.00 36.41  ? 47  ASP A CA  1 
ATOM   415   C C   . ASP A  1 47  ? -19.810 -42.609 44.709   1.00 30.25  ? 47  ASP A C   1 
ATOM   416   O O   . ASP A  1 47  ? -19.043 -43.243 45.443   1.00 32.12  ? 47  ASP A O   1 
ATOM   417   C CB  . ASP A  1 47  ? -19.768 -44.012 42.676   1.00 35.07  ? 47  ASP A CB  1 
ATOM   418   C CG  . ASP A  1 47  ? -20.534 -44.892 41.714   1.00 40.02  ? 47  ASP A CG  1 
ATOM   419   O OD1 . ASP A  1 47  ? -21.451 -45.604 42.178   1.00 33.93  ? 47  ASP A OD1 1 
ATOM   420   O OD2 . ASP A  1 47  ? -20.209 -44.885 40.502   1.00 39.58  ? 47  ASP A OD2 1 
ATOM   421   N N   . PHE A  1 48  ? -19.896 -41.277 44.734   1.00 29.59  ? 48  PHE A N   1 
ATOM   422   C CA  . PHE A  1 48  ? -19.035 -40.450 45.566   1.00 30.70  ? 48  PHE A CA  1 
ATOM   423   C C   . PHE A  1 48  ? -19.885 -39.458 46.328   1.00 31.41  ? 48  PHE A C   1 
ATOM   424   O O   . PHE A  1 48  ? -20.751 -38.796 45.746   1.00 37.15  ? 48  PHE A O   1 
ATOM   425   C CB  . PHE A  1 48  ? -17.966 -39.739 44.731   1.00 28.54  ? 48  PHE A CB  1 
ATOM   426   C CG  . PHE A  1 48  ? -17.041 -40.687 44.030   1.00 32.25  ? 48  PHE A CG  1 
ATOM   427   C CD1 . PHE A  1 48  ? -16.001 -41.294 44.722   1.00 31.98  ? 48  PHE A CD1 1 
ATOM   428   C CD2 . PHE A  1 48  ? -17.223 -40.997 42.684   1.00 28.45  ? 48  PHE A CD2 1 
ATOM   429   C CE1 . PHE A  1 48  ? -15.155 -42.189 44.099   1.00 29.19  ? 48  PHE A CE1 1 
ATOM   430   C CE2 . PHE A  1 48  ? -16.378 -41.897 42.046   1.00 29.61  ? 48  PHE A CE2 1 
ATOM   431   C CZ  . PHE A  1 48  ? -15.334 -42.487 42.751   1.00 28.54  ? 48  PHE A CZ  1 
ATOM   432   N N   . GLU A  1 49  ? -19.637 -39.373 47.632   1.00 32.74  ? 49  GLU A N   1 
ATOM   433   C CA  . GLU A  1 49  ? -20.416 -38.542 48.539   1.00 32.90  ? 49  GLU A CA  1 
ATOM   434   C C   . GLU A  1 49  ? -19.804 -37.147 48.624   1.00 30.72  ? 49  GLU A C   1 
ATOM   435   O O   . GLU A  1 49  ? -19.276 -36.714 49.648   1.00 28.85  ? 49  GLU A O   1 
ATOM   436   C CB  . GLU A  1 49  ? -20.497 -39.202 49.912   1.00 40.29  ? 49  GLU A CB  1 
ATOM   437   C CG  . GLU A  1 49  ? -21.507 -40.324 49.987   1.00 49.00  ? 49  GLU A CG  1 
ATOM   438   C CD  . GLU A  1 49  ? -20.864 -41.695 50.062   1.00 59.78  ? 49  GLU A CD  1 
ATOM   439   O OE1 . GLU A  1 49  ? -20.251 -42.123 49.057   1.00 58.12  ? 49  GLU A OE1 1 
ATOM   440   O OE2 . GLU A  1 49  ? -20.983 -42.346 51.131   1.00 62.55  ? 49  GLU A OE2 1 
ATOM   441   N N   . ILE A  1 50  ? -19.840 -36.466 47.488   1.00 23.89  ? 50  ILE A N   1 
ATOM   442   C CA  . ILE A  1 50  ? -19.450 -35.076 47.376   1.00 25.24  ? 50  ILE A CA  1 
ATOM   443   C C   . ILE A  1 50  ? -20.588 -34.356 46.681   1.00 23.32  ? 50  ILE A C   1 
ATOM   444   O O   . ILE A  1 50  ? -21.532 -34.969 46.193   1.00 27.73  ? 50  ILE A O   1 
ATOM   445   C CB  . ILE A  1 50  ? -18.134 -34.888 46.584   1.00 23.83  ? 50  ILE A CB  1 
ATOM   446   C CG1 . ILE A  1 50  ? -18.193 -35.710 45.298   1.00 26.43  ? 50  ILE A CG1 1 
ATOM   447   C CG2 . ILE A  1 50  ? -16.946 -35.307 47.452   1.00 27.58  ? 50  ILE A CG2 1 
ATOM   448   C CD1 . ILE A  1 50  ? -17.328 -35.187 44.168   1.00 19.61  ? 50  ILE A CD1 1 
ATOM   449   N N   . LYS A  1 51  ? -20.492 -33.038 46.656   1.00 25.17  ? 51  LYS A N   1 
ATOM   450   C CA  . LYS A  1 51  ? -21.417 -32.199 45.915   1.00 23.17  ? 51  LYS A CA  1 
ATOM   451   C C   . LYS A  1 51  ? -20.748 -31.755 44.618   1.00 19.92  ? 51  LYS A C   1 
ATOM   452   O O   . LYS A  1 51  ? -19.563 -31.400 44.611   1.00 20.28  ? 51  LYS A O   1 
ATOM   453   C CB  . LYS A  1 51  ? -21.830 -30.997 46.770   1.00 22.60  ? 51  LYS A CB  1 
ATOM   454   C CG  . LYS A  1 51  ? -22.304 -31.389 48.211   1.00 20.96  ? 51  LYS A CG  1 
ATOM   455   C CD  . LYS A  1 51  ? -23.733 -31.917 48.210   1.00 22.00  ? 51  LYS A CD  1 
ATOM   456   C CE  . LYS A  1 51  ? -24.148 -32.471 49.606   1.00 27.97  ? 51  LYS A CE  1 
ATOM   457   N NZ  . LYS A  1 51  ? -23.762 -31.538 50.695   1.00 35.21  ? 51  LYS A NZ  1 
ATOM   458   N N   . LEU A  1 52  ? -21.506 -31.787 43.517   1.00 16.78  ? 52  LEU A N   1 
ATOM   459   C CA  . LEU A  1 52  ? -21.011 -31.306 42.229   1.00 21.96  ? 52  LEU A CA  1 
ATOM   460   C C   . LEU A  1 52  ? -22.126 -30.549 41.516   1.00 22.50  ? 52  LEU A C   1 
ATOM   461   O O   . LEU A  1 52  ? -23.275 -30.996 41.506   1.00 23.48  ? 52  LEU A O   1 
ATOM   462   C CB  . LEU A  1 52  ? -20.522 -32.458 41.319   1.00 25.59  ? 52  LEU A CB  1 
ATOM   463   C CG  . LEU A  1 52  ? -19.291 -33.290 41.737   1.00 23.32  ? 52  LEU A CG  1 
ATOM   464   C CD1 . LEU A  1 52  ? -19.057 -34.475 40.797   1.00 21.23  ? 52  LEU A CD1 1 
ATOM   465   C CD2 . LEU A  1 52  ? -18.026 -32.404 41.796   1.00 20.22  ? 52  LEU A CD2 1 
ATOM   466   N N   . ASN A  1 53  ? -21.781 -29.425 40.895   1.00 15.15  ? 53  ASN A N   1 
ATOM   467   C CA  . ASN A  1 53  ? -22.760 -28.545 40.275   1.00 13.71  ? 53  ASN A CA  1 
ATOM   468   C C   . ASN A  1 53  ? -22.542 -28.506 38.777   1.00 23.81  ? 53  ASN A C   1 
ATOM   469   O O   . ASN A  1 53  ? -21.430 -28.723 38.290   1.00 21.96  ? 53  ASN A O   1 
ATOM   470   C CB  . ASN A  1 53  ? -22.661 -27.150 40.838   1.00 13.72  ? 53  ASN A CB  1 
ATOM   471   C CG  . ASN A  1 53  ? -22.753 -27.171 42.339   1.00 19.22  ? 53  ASN A CG  1 
ATOM   472   O OD1 . ASN A  1 53  ? -23.813 -27.474 42.890   1.00 19.31  ? 53  ASN A OD1 1 
ATOM   473   N ND2 . ASN A  1 53  ? -21.637 -26.928 43.005   1.00 15.41  ? 53  ASN A ND2 1 
ATOM   474   N N   . PHE A  1 54  ? -23.617 -28.228 38.060   1.00 22.38  ? 54  PHE A N   1 
ATOM   475   C CA  . PHE A  1 54  ? -23.596 -28.345 36.613   1.00 18.22  ? 54  PHE A CA  1 
ATOM   476   C C   . PHE A  1 54  ? -24.336 -27.178 36.001   1.00 23.18  ? 54  PHE A C   1 
ATOM   477   O O   . PHE A  1 54  ? -25.317 -26.684 36.552   1.00 21.38  ? 54  PHE A O   1 
ATOM   478   C CB  . PHE A  1 54  ? -24.222 -29.672 36.162   1.00 15.21  ? 54  PHE A CB  1 
ATOM   479   C CG  . PHE A  1 54  ? -23.487 -30.860 36.679   1.00 19.92  ? 54  PHE A CG  1 
ATOM   480   C CD1 . PHE A  1 54  ? -22.440 -31.399 35.959   1.00 22.26  ? 54  PHE A CD1 1 
ATOM   481   C CD2 . PHE A  1 54  ? -23.798 -31.405 37.934   1.00 19.43  ? 54  PHE A CD2 1 
ATOM   482   C CE1 . PHE A  1 54  ? -21.727 -32.492 36.461   1.00 22.46  ? 54  PHE A CE1 1 
ATOM   483   C CE2 . PHE A  1 54  ? -23.082 -32.492 38.429   1.00 19.51  ? 54  PHE A CE2 1 
ATOM   484   C CZ  . PHE A  1 54  ? -22.051 -33.023 37.687   1.00 22.61  ? 54  PHE A CZ  1 
ATOM   485   N N   . ASN A  1 55  ? -23.854 -26.749 34.840   1.00 19.53  ? 55  ASN A N   1 
ATOM   486   C CA  . ASN A  1 55  ? -24.575 -25.799 34.014   1.00 21.95  ? 55  ASN A CA  1 
ATOM   487   C C   . ASN A  1 55  ? -24.924 -26.509 32.715   1.00 24.77  ? 55  ASN A C   1 
ATOM   488   O O   . ASN A  1 55  ? -24.065 -27.178 32.129   1.00 22.66  ? 55  ASN A O   1 
ATOM   489   C CB  . ASN A  1 55  ? -23.733 -24.546 33.746   1.00 16.90  ? 55  ASN A CB  1 
ATOM   490   C CG  . ASN A  1 55  ? -24.500 -23.489 32.955   1.00 20.51  ? 55  ASN A CG  1 
ATOM   491   O OD1 . ASN A  1 55  ? -25.469 -22.923 33.460   1.00 18.81  ? 55  ASN A OD1 1 
ATOM   492   N ND2 . ASN A  1 55  ? -24.064 -23.214 31.716   1.00 17.93  ? 55  ASN A ND2 1 
ATOM   493   N N   . LEU A  1 56  ? -26.181 -26.386 32.283   1.00 23.42  ? 56  LEU A N   1 
ATOM   494   C CA  . LEU A  1 56  ? -26.646 -26.927 31.006   1.00 24.59  ? 56  LEU A CA  1 
ATOM   495   C C   . LEU A  1 56  ? -27.232 -25.790 30.177   1.00 25.28  ? 56  LEU A C   1 
ATOM   496   O O   . LEU A  1 56  ? -28.218 -25.174 30.591   1.00 21.22  ? 56  LEU A O   1 
ATOM   497   C CB  . LEU A  1 56  ? -27.710 -28.013 31.225   1.00 23.76  ? 56  LEU A CB  1 
ATOM   498   C CG  . LEU A  1 56  ? -27.357 -29.278 32.007   1.00 28.26  ? 56  LEU A CG  1 
ATOM   499   C CD1 . LEU A  1 56  ? -28.583 -30.203 32.170   1.00 25.97  ? 56  LEU A CD1 1 
ATOM   500   C CD2 . LEU A  1 56  ? -26.242 -30.022 31.313   1.00 25.48  ? 56  LEU A CD2 1 
ATOM   501   N N   . THR A  1 57  ? -26.659 -25.523 28.998   1.00 20.20  ? 57  THR A N   1 
ATOM   502   C CA  . THR A  1 57  ? -27.258 -24.491 28.178   1.00 23.63  ? 57  THR A CA  1 
ATOM   503   C C   . THR A  1 57  ? -28.585 -24.990 27.605   1.00 22.40  ? 57  THR A C   1 
ATOM   504   O O   . THR A  1 57  ? -28.765 -26.191 27.366   1.00 20.45  ? 57  THR A O   1 
ATOM   505   C CB  . THR A  1 57  ? -26.319 -24.047 27.050   1.00 21.20  ? 57  THR A CB  1 
ATOM   506   O OG1 . THR A  1 57  ? -26.065 -25.158 26.192   1.00 19.16  ? 57  THR A OG1 1 
ATOM   507   C CG2 . THR A  1 57  ? -24.999 -23.542 27.654   1.00 20.07  ? 57  THR A CG2 1 
ATOM   508   N N   . PRO A  1 58  ? -29.558 -24.096 27.444   1.00 17.96  ? 58  PRO A N   1 
ATOM   509   C CA  . PRO A  1 58  ? -30.846 -24.530 26.879   1.00 24.07  ? 58  PRO A CA  1 
ATOM   510   C C   . PRO A  1 58  ? -30.719 -25.065 25.467   1.00 20.28  ? 58  PRO A C   1 
ATOM   511   O O   . PRO A  1 58  ? -31.470 -25.973 25.096   1.00 21.09  ? 58  PRO A O   1 
ATOM   512   C CB  . PRO A  1 58  ? -31.698 -23.253 26.918   1.00 21.74  ? 58  PRO A CB  1 
ATOM   513   C CG  . PRO A  1 58  ? -31.088 -22.418 28.007   1.00 20.56  ? 58  PRO A CG  1 
ATOM   514   C CD  . PRO A  1 58  ? -29.594 -22.701 27.914   1.00 16.95  ? 58  PRO A CD  1 
ATOM   515   N N   . VAL A  1 59  ? -29.770 -24.551 24.680   1.00 16.24  ? 59  VAL A N   1 
ATOM   516   C CA  . VAL A  1 59  ? -29.583 -25.085 23.328   1.00 18.28  ? 59  VAL A CA  1 
ATOM   517   C C   . VAL A  1 59  ? -29.065 -26.523 23.403   1.00 21.78  ? 59  VAL A C   1 
ATOM   518   O O   . VAL A  1 59  ? -29.462 -27.373 22.598   1.00 19.85  ? 59  VAL A O   1 
ATOM   519   C CB  . VAL A  1 59  ? -28.662 -24.159 22.494   1.00 21.06  ? 59  VAL A CB  1 
ATOM   520   C CG1 . VAL A  1 59  ? -27.297 -23.989 23.142   1.00 24.85  ? 59  VAL A CG1 1 
ATOM   521   C CG2 . VAL A  1 59  ? -28.535 -24.635 21.004   1.00 21.35  ? 59  VAL A CG2 1 
ATOM   522   N N   . LEU A  1 60  ? -28.232 -26.842 24.402   1.00 16.93  ? 60  LEU A N   1 
ATOM   523   C CA  . LEU A  1 60  ? -27.762 -28.222 24.549   1.00 17.19  ? 60  LEU A CA  1 
ATOM   524   C C   . LEU A  1 60  ? -28.888 -29.134 25.028   1.00 20.26  ? 60  LEU A C   1 
ATOM   525   O O   . LEU A  1 60  ? -29.014 -30.274 24.577   1.00 23.69  ? 60  LEU A O   1 
ATOM   526   C CB  . LEU A  1 60  ? -26.584 -28.280 25.532   1.00 19.12  ? 60  LEU A CB  1 
ATOM   527   C CG  . LEU A  1 60  ? -26.233 -29.700 26.004   1.00 23.25  ? 60  LEU A CG  1 
ATOM   528   C CD1 . LEU A  1 60  ? -25.707 -30.581 24.826   1.00 21.84  ? 60  LEU A CD1 1 
ATOM   529   C CD2 . LEU A  1 60  ? -25.252 -29.678 27.163   1.00 16.31  ? 60  LEU A CD2 1 
ATOM   530   N N   . ILE A  1 61  ? -29.723 -28.649 25.938   1.00 23.73  ? 61  ILE A N   1 
ATOM   531   C CA  . ILE A  1 61  ? -30.852 -29.462 26.386   1.00 24.82  ? 61  ILE A CA  1 
ATOM   532   C C   . ILE A  1 61  ? -31.745 -29.837 25.203   1.00 27.07  ? 61  ILE A C   1 
ATOM   533   O O   . ILE A  1 61  ? -32.178 -30.994 25.067   1.00 26.11  ? 61  ILE A O   1 
ATOM   534   C CB  . ILE A  1 61  ? -31.644 -28.708 27.459   1.00 16.76  ? 61  ILE A CB  1 
ATOM   535   C CG1 . ILE A  1 61  ? -30.756 -28.463 28.690   1.00 21.51  ? 61  ILE A CG1 1 
ATOM   536   C CG2 . ILE A  1 61  ? -32.964 -29.444 27.751   1.00 19.42  ? 61  ILE A CG2 1 
ATOM   537   C CD1 . ILE A  1 61  ? -31.462 -27.762 29.824   1.00 21.01  ? 61  ILE A CD1 1 
ATOM   538   N N   . ASP A  1 62  ? -32.052 -28.856 24.348   1.00 22.67  ? 62  ASP A N   1 
ATOM   539   C CA  . ASP A  1 62  ? -32.898 -29.112 23.176   1.00 25.02  ? 62  ASP A CA  1 
ATOM   540   C C   . ASP A  1 62  ? -32.370 -30.290 22.376   1.00 23.56  ? 62  ASP A C   1 
ATOM   541   O O   . ASP A  1 62  ? -33.122 -31.177 21.972   1.00 24.69  ? 62  ASP A O   1 
ATOM   542   C CB  . ASP A  1 62  ? -32.955 -27.877 22.272   1.00 30.10  ? 62  ASP A CB  1 
ATOM   543   C CG  . ASP A  1 62  ? -33.917 -26.823 22.759   1.00 36.11  ? 62  ASP A CG  1 
ATOM   544   O OD1 . ASP A  1 62  ? -34.825 -27.165 23.551   1.00 36.30  ? 62  ASP A OD1 1 
ATOM   545   O OD2 . ASP A  1 62  ? -33.765 -25.648 22.328   1.00 32.72  ? 62  ASP A OD2 1 
ATOM   546   N N   . GLN A  1 63  ? -31.061 -30.301 22.133   1.00 26.78  ? 63  GLN A N   1 
ATOM   547   C CA  . GLN A  1 63  ? -30.469 -31.345 21.314   1.00 27.02  ? 63  GLN A CA  1 
ATOM   548   C C   . GLN A  1 63  ? -30.473 -32.684 22.030   1.00 26.11  ? 63  GLN A C   1 
ATOM   549   O O   . GLN A  1 63  ? -30.811 -33.709 21.427   1.00 22.41  ? 63  GLN A O   1 
ATOM   550   C CB  . GLN A  1 63  ? -29.050 -30.951 20.924   1.00 28.35  ? 63  GLN A CB  1 
ATOM   551   C CG  . GLN A  1 63  ? -28.952 -29.621 20.181   1.00 27.37  ? 63  GLN A CG  1 
ATOM   552   C CD  . GLN A  1 63  ? -27.508 -29.269 19.869   1.00 25.84  ? 63  GLN A CD  1 
ATOM   553   O OE1 . GLN A  1 63  ? -26.862 -29.945 19.065   1.00 27.83  ? 63  GLN A OE1 1 
ATOM   554   N NE2 . GLN A  1 63  ? -26.985 -28.226 20.519   1.00 19.83  ? 63  GLN A NE2 1 
ATOM   555   N N   . ILE A  1 64  ? -30.089 -32.701 23.314   1.00 28.13  ? 64  ILE A N   1 
ATOM   556   C CA  . ILE A  1 64  ? -30.207 -33.935 24.086   1.00 26.31  ? 64  ILE A CA  1 
ATOM   557   C C   . ILE A  1 64  ? -31.626 -34.480 23.983   1.00 23.36  ? 64  ILE A C   1 
ATOM   558   O O   . ILE A  1 64  ? -31.833 -35.685 23.780   1.00 20.59  ? 64  ILE A O   1 
ATOM   559   C CB  . ILE A  1 64  ? -29.785 -33.695 25.555   1.00 20.96  ? 64  ILE A CB  1 
ATOM   560   C CG1 . ILE A  1 64  ? -28.279 -33.387 25.618   1.00 19.65  ? 64  ILE A CG1 1 
ATOM   561   C CG2 . ILE A  1 64  ? -30.151 -34.894 26.415   1.00 20.21  ? 64  ILE A CG2 1 
ATOM   562   C CD1 . ILE A  1 64  ? -27.735 -33.000 27.010   1.00 21.03  ? 64  ILE A CD1 1 
ATOM   563   N N   . GLN A  1 65  ? -32.630 -33.603 24.118   1.00 21.23  ? 65  GLN A N   1 
ATOM   564   C CA  . GLN A  1 65  ? -34.016 -34.063 24.007   1.00 27.95  ? 65  GLN A CA  1 
ATOM   565   C C   . GLN A  1 65  ? -34.279 -34.699 22.648   1.00 28.44  ? 65  GLN A C   1 
ATOM   566   O O   . GLN A  1 65  ? -35.063 -35.652 22.537   1.00 26.80  ? 65  GLN A O   1 
ATOM   567   C CB  . GLN A  1 65  ? -34.994 -32.906 24.223   1.00 32.40  ? 65  GLN A CB  1 
ATOM   568   C CG  . GLN A  1 65  ? -35.277 -32.577 25.671   1.00 32.33  ? 65  GLN A CG  1 
ATOM   569   C CD  . GLN A  1 65  ? -36.198 -31.389 25.813   1.00 37.54  ? 65  GLN A CD  1 
ATOM   570   O OE1 . GLN A  1 65  ? -35.966 -30.336 25.224   1.00 35.49  ? 65  GLN A OE1 1 
ATOM   571   N NE2 . GLN A  1 65  ? -37.266 -31.558 26.582   1.00 37.25  ? 65  GLN A NE2 1 
ATOM   572   N N   . GLU A  1 66  ? -33.644 -34.179 21.594   1.00 29.23  ? 66  GLU A N   1 
ATOM   573   C CA  . GLU A  1 66  ? -33.973 -34.681 20.266   1.00 33.45  ? 66  GLU A CA  1 
ATOM   574   C C   . GLU A  1 66  ? -33.321 -36.034 20.015   1.00 29.26  ? 66  GLU A C   1 
ATOM   575   O O   . GLU A  1 66  ? -33.938 -36.912 19.405   1.00 27.05  ? 66  GLU A O   1 
ATOM   576   C CB  . GLU A  1 66  ? -33.571 -33.668 19.193   1.00 35.87  ? 66  GLU A CB  1 
ATOM   577   C CG  . GLU A  1 66  ? -34.696 -33.284 18.239   1.00 43.71  ? 66  GLU A CG  1 
ATOM   578   C CD  . GLU A  1 66  ? -34.176 -32.743 16.907   1.00 46.45  ? 66  GLU A CD  1 
ATOM   579   O OE1 . GLU A  1 66  ? -33.238 -31.921 16.930   1.00 46.50  ? 66  GLU A OE1 1 
ATOM   580   O OE2 . GLU A  1 66  ? -34.696 -33.146 15.840   1.00 48.58  ? 66  GLU A OE2 1 
ATOM   581   N N   . TYR A  1 67  ? -32.086 -36.229 20.486   1.00 26.82  ? 67  TYR A N   1 
ATOM   582   C CA  . TYR A  1 67  ? -31.491 -37.558 20.385   1.00 25.12  ? 67  TYR A CA  1 
ATOM   583   C C   . TYR A  1 67  ? -32.250 -38.566 21.233   1.00 25.29  ? 67  TYR A C   1 
ATOM   584   O O   . TYR A  1 67  ? -32.527 -39.680 20.775   1.00 25.88  ? 67  TYR A O   1 
ATOM   585   C CB  . TYR A  1 67  ? -30.029 -37.531 20.802   1.00 20.74  ? 67  TYR A CB  1 
ATOM   586   C CG  . TYR A  1 67  ? -29.100 -36.996 19.750   1.00 17.91  ? 67  TYR A CG  1 
ATOM   587   C CD1 . TYR A  1 67  ? -28.612 -37.810 18.732   1.00 23.05  ? 67  TYR A CD1 1 
ATOM   588   C CD2 . TYR A  1 67  ? -28.702 -35.675 19.778   1.00 23.36  ? 67  TYR A CD2 1 
ATOM   589   C CE1 . TYR A  1 67  ? -27.749 -37.307 17.762   1.00 21.90  ? 67  TYR A CE1 1 
ATOM   590   C CE2 . TYR A  1 67  ? -27.839 -35.160 18.812   1.00 27.43  ? 67  TYR A CE2 1 
ATOM   591   C CZ  . TYR A  1 67  ? -27.378 -35.980 17.805   1.00 24.11  ? 67  TYR A CZ  1 
ATOM   592   O OH  . TYR A  1 67  ? -26.512 -35.475 16.875   1.00 26.05  ? 67  TYR A OH  1 
ATOM   593   N N   . ALA A  1 68  ? -32.595 -38.193 22.476   1.00 29.15  ? 68  ALA A N   1 
ATOM   594   C CA  . ALA A  1 68  ? -33.313 -39.119 23.357   1.00 24.51  ? 68  ALA A CA  1 
ATOM   595   C C   . ALA A  1 68  ? -34.650 -39.550 22.768   1.00 27.79  ? 68  ALA A C   1 
ATOM   596   O O   . ALA A  1 68  ? -35.054 -40.702 22.945   1.00 31.57  ? 68  ALA A O   1 
ATOM   597   C CB  . ALA A  1 68  ? -33.520 -38.494 24.739   1.00 23.19  ? 68  ALA A CB  1 
ATOM   598   N N   . GLN A  1 69  ? -35.342 -38.668 22.044   1.00 32.72  ? 69  GLN A N   1 
ATOM   599   C CA  . GLN A  1 69  ? -36.626 -39.048 21.457   1.00 35.31  ? 69  GLN A CA  1 
ATOM   600   C C   . GLN A  1 69  ? -36.476 -39.785 20.131   1.00 40.68  ? 69  GLN A C   1 
ATOM   601   O O   . GLN A  1 69  ? -37.491 -40.120 19.510   1.00 45.61  ? 69  GLN A O   1 
ATOM   602   C CB  . GLN A  1 69  ? -37.506 -37.809 21.254   1.00 39.40  ? 69  GLN A CB  1 
ATOM   603   C CG  . GLN A  1 69  ? -38.076 -37.222 22.548   1.00 45.17  ? 69  GLN A CG  1 
ATOM   604   C CD  . GLN A  1 69  ? -38.490 -35.754 22.418   1.00 50.03  ? 69  GLN A CD  1 
ATOM   605   O OE1 . GLN A  1 69  ? -38.819 -35.283 21.334   1.00 54.11  ? 69  GLN A OE1 1 
ATOM   606   N NE2 . GLN A  1 69  ? -38.472 -35.031 23.530   1.00 51.52  ? 69  GLN A NE2 1 
ATOM   607   N N   . GLY A  1 70  ? -35.250 -40.034 19.677   1.00 39.67  ? 70  GLY A N   1 
ATOM   608   C CA  . GLY A  1 70  ? -35.048 -40.689 18.402   1.00 39.46  ? 70  GLY A CA  1 
ATOM   609   C C   . GLY A  1 70  ? -35.325 -39.833 17.187   1.00 40.25  ? 70  GLY A C   1 
ATOM   610   O O   . GLY A  1 70  ? -35.500 -40.375 16.096   1.00 44.28  ? 70  GLY A O   1 
ATOM   611   N N   . LYS A  1 71  ? -35.351 -38.506 17.328   1.00 40.33  ? 71  LYS A N   1 
ATOM   612   C CA  . LYS A  1 71  ? -35.718 -37.631 16.219   1.00 40.05  ? 71  LYS A CA  1 
ATOM   613   C C   . LYS A  1 71  ? -34.525 -36.942 15.563   1.00 40.32  ? 71  LYS A C   1 
ATOM   614   O O   . LYS A  1 71  ? -34.700 -36.291 14.526   1.00 38.88  ? 71  LYS A O   1 
ATOM   615   C CB  . LYS A  1 71  ? -36.730 -36.571 16.689   1.00 33.54  ? 71  LYS A CB  1 
ATOM   616   N N   . ALA A  1 72  ? -33.327 -37.064 16.126   1.00 34.50  ? 72  ALA A N   1 
ATOM   617   C CA  . ALA A  1 72  ? -32.159 -36.394 15.572   1.00 30.22  ? 72  ALA A CA  1 
ATOM   618   C C   . ALA A  1 72  ? -31.620 -37.153 14.365   1.00 31.16  ? 72  ALA A C   1 
ATOM   619   O O   . ALA A  1 72  ? -31.360 -38.358 14.439   1.00 31.51  ? 72  ALA A O   1 
ATOM   620   C CB  . ALA A  1 72  ? -31.074 -36.263 16.637   1.00 28.63  ? 72  ALA A CB  1 
ATOM   621   N N   . LYS A  1 73  ? -31.448 -36.442 13.255   1.00 32.08  ? 73  LYS A N   1 
ATOM   622   C CA  . LYS A  1 73  ? -30.871 -36.996 12.026   1.00 30.20  ? 73  LYS A CA  1 
ATOM   623   C C   . LYS A  1 73  ? -29.412 -36.564 11.966   1.00 27.61  ? 73  LYS A C   1 
ATOM   624   O O   . LYS A  1 73  ? -29.107 -35.437 11.572   1.00 34.30  ? 73  LYS A O   1 
ATOM   625   C CB  . LYS A  1 73  ? -31.639 -36.507 10.799   1.00 33.06  ? 73  LYS A CB  1 
ATOM   626   C CG  . LYS A  1 73  ? -33.141 -36.702 10.885   1.00 39.42  ? 73  LYS A CG  1 
ATOM   627   C CD  . LYS A  1 73  ? -33.543 -38.104 10.445   1.00 52.03  ? 73  LYS A CD  1 
ATOM   628   C CE  . LYS A  1 73  ? -33.814 -39.019 11.634   1.00 60.00  ? 73  LYS A CE  1 
ATOM   629   N NZ  . LYS A  1 73  ? -33.837 -40.468 11.259   1.00 61.82  ? 73  LYS A NZ  1 
ATOM   630   N N   . ASP A  1 74  ? -28.509 -37.467 12.338   1.00 28.71  ? 74  ASP A N   1 
ATOM   631   C CA  . ASP A  1 74  ? -27.088 -37.169 12.528   1.00 25.22  ? 74  ASP A CA  1 
ATOM   632   C C   . ASP A  1 74  ? -26.314 -37.835 11.392   1.00 28.48  ? 74  ASP A C   1 
ATOM   633   O O   . ASP A  1 74  ? -26.269 -39.072 11.301   1.00 28.65  ? 74  ASP A O   1 
ATOM   634   C CB  . ASP A  1 74  ? -26.633 -37.664 13.916   1.00 23.65  ? 74  ASP A CB  1 
ATOM   635   C CG  . ASP A  1 74  ? -25.260 -37.142 14.316   1.00 28.92  ? 74  ASP A CG  1 
ATOM   636   O OD1 . ASP A  1 74  ? -24.380 -37.066 13.428   1.00 28.99  ? 74  ASP A OD1 1 
ATOM   637   O OD2 . ASP A  1 74  ? -25.048 -36.831 15.523   1.00 28.08  ? 74  ASP A OD2 1 
ATOM   638   N N   . VAL A  1 75  ? -25.704 -37.015 10.525   1.00 31.16  ? 75  VAL A N   1 
ATOM   639   C CA  . VAL A  1 75  ? -25.135 -37.544 9.286    1.00 32.02  ? 75  VAL A CA  1 
ATOM   640   C C   . VAL A  1 75  ? -23.911 -38.396 9.579    1.00 31.50  ? 75  VAL A C   1 
ATOM   641   O O   . VAL A  1 75  ? -23.724 -39.457 8.970    1.00 28.12  ? 75  VAL A O   1 
ATOM   642   C CB  . VAL A  1 75  ? -24.813 -36.414 8.290    1.00 30.76  ? 75  VAL A CB  1 
ATOM   643   C CG1 . VAL A  1 75  ? -26.090 -35.798 7.783    1.00 34.15  ? 75  VAL A CG1 1 
ATOM   644   C CG2 . VAL A  1 75  ? -23.928 -35.349 8.922    1.00 30.77  ? 75  VAL A CG2 1 
ATOM   645   N N   . PHE A  1 76  ? -23.056 -37.950 10.509   1.00 27.03  ? 76  PHE A N   1 
ATOM   646   C CA  . PHE A  1 76  ? -21.885 -38.741 10.863   1.00 30.16  ? 76  PHE A CA  1 
ATOM   647   C C   . PHE A  1 76  ? -22.301 -40.044 11.521   1.00 33.12  ? 76  PHE A C   1 
ATOM   648   O O   . PHE A  1 76  ? -21.720 -41.104 11.256   1.00 26.49  ? 76  PHE A O   1 
ATOM   649   C CB  . PHE A  1 76  ? -20.967 -37.946 11.789   1.00 32.69  ? 76  PHE A CB  1 
ATOM   650   C CG  . PHE A  1 76  ? -20.013 -37.044 11.072   1.00 43.11  ? 76  PHE A CG  1 
ATOM   651   C CD1 . PHE A  1 76  ? -20.420 -35.781 10.632   1.00 49.12  ? 76  PHE A CD1 1 
ATOM   652   C CD2 . PHE A  1 76  ? -18.705 -37.443 10.845   1.00 44.72  ? 76  PHE A CD2 1 
ATOM   653   C CE1 . PHE A  1 76  ? -19.538 -34.937 9.966    1.00 50.34  ? 76  PHE A CE1 1 
ATOM   654   C CE2 . PHE A  1 76  ? -17.816 -36.603 10.184   1.00 48.29  ? 76  PHE A CE2 1 
ATOM   655   C CZ  . PHE A  1 76  ? -18.234 -35.346 9.744    1.00 50.21  ? 76  PHE A CZ  1 
ATOM   656   N N   . LEU A  1 77  ? -23.314 -39.985 12.385   1.00 32.06  ? 77  LEU A N   1 
ATOM   657   C CA  . LEU A  1 77  ? -23.742 -41.189 13.079   1.00 28.83  ? 77  LEU A CA  1 
ATOM   658   C C   . LEU A  1 77  ? -24.372 -42.193 12.132   1.00 29.51  ? 77  LEU A C   1 
ATOM   659   O O   . LEU A  1 77  ? -24.210 -43.402 12.327   1.00 32.92  ? 77  LEU A O   1 
ATOM   660   C CB  . LEU A  1 77  ? -24.710 -40.819 14.196   1.00 30.94  ? 77  LEU A CB  1 
ATOM   661   C CG  . LEU A  1 77  ? -24.990 -41.912 15.218   1.00 31.73  ? 77  LEU A CG  1 
ATOM   662   C CD1 . LEU A  1 77  ? -23.686 -42.436 15.816   1.00 27.23  ? 77  LEU A CD1 1 
ATOM   663   C CD2 . LEU A  1 77  ? -25.903 -41.329 16.276   1.00 33.42  ? 77  LEU A CD2 1 
ATOM   664   N N   . GLU A  1 78  ? -25.080 -41.729 11.090   1.00 34.38  ? 78  GLU A N   1 
ATOM   665   C CA  . GLU A  1 78  ? -25.682 -42.676 10.163   1.00 39.64  ? 78  GLU A CA  1 
ATOM   666   C C   . GLU A  1 78  ? -24.612 -43.412 9.371    1.00 34.30  ? 78  GLU A C   1 
ATOM   667   O O   . GLU A  1 78  ? -24.808 -44.573 8.994    1.00 32.23  ? 78  GLU A O   1 
ATOM   668   C CB  . GLU A  1 78  ? -26.666 -41.966 9.227    1.00 51.54  ? 78  GLU A CB  1 
ATOM   669   C CG  . GLU A  1 78  ? -26.056 -41.490 7.920    1.00 66.99  ? 78  GLU A CG  1 
ATOM   670   C CD  . GLU A  1 78  ? -27.005 -40.633 7.081    1.00 77.98  ? 78  GLU A CD  1 
ATOM   671   O OE1 . GLU A  1 78  ? -26.984 -40.776 5.835    1.00 80.48  ? 78  GLU A OE1 1 
ATOM   672   O OE2 . GLU A  1 78  ? -27.766 -39.823 7.662    1.00 79.15  ? 78  GLU A OE2 1 
ATOM   673   N N   . ALA A  1 79  ? -23.470 -42.764 9.139    1.00 33.63  ? 79  ALA A N   1 
ATOM   674   C CA  . ALA A  1 79  ? -22.348 -43.440 8.511    1.00 34.15  ? 79  ALA A CA  1 
ATOM   675   C C   . ALA A  1 79  ? -21.766 -44.497 9.440    1.00 34.43  ? 79  ALA A C   1 
ATOM   676   O O   . ALA A  1 79  ? -21.328 -45.556 8.979    1.00 40.78  ? 79  ALA A O   1 
ATOM   677   C CB  . ALA A  1 79  ? -21.287 -42.416 8.113    1.00 30.42  ? 79  ALA A CB  1 
ATOM   678   N N   . ILE A  1 80  ? -21.777 -44.233 10.750   1.00 34.56  ? 80  ILE A N   1 
ATOM   679   C CA  . ILE A  1 80  ? -21.407 -45.257 11.731   1.00 31.69  ? 80  ILE A CA  1 
ATOM   680   C C   . ILE A  1 80  ? -22.384 -46.423 11.683   1.00 24.98  ? 80  ILE A C   1 
ATOM   681   O O   . ILE A  1 80  ? -21.987 -47.595 11.602   1.00 28.29  ? 80  ILE A O   1 
ATOM   682   C CB  . ILE A  1 80  ? -21.344 -44.646 13.144   1.00 31.78  ? 80  ILE A CB  1 
ATOM   683   C CG1 . ILE A  1 80  ? -20.244 -43.590 13.229   1.00 33.01  ? 80  ILE A CG1 1 
ATOM   684   C CG2 . ILE A  1 80  ? -21.138 -45.729 14.177   1.00 28.46  ? 80  ILE A CG2 1 
ATOM   685   C CD1 . ILE A  1 80  ? -18.892 -44.161 13.071   1.00 37.02  ? 80  ILE A CD1 1 
ATOM   686   N N   . ARG A  1 81  ? -23.683 -46.121 11.699   1.00 26.61  ? 81  ARG A N   1 
ATOM   687   C CA  . ARG A  1 81  ? -24.686 -47.177 11.823   1.00 29.70  ? 81  ARG A CA  1 
ATOM   688   C C   . ARG A  1 81  ? -24.663 -48.129 10.638   1.00 32.89  ? 81  ARG A C   1 
ATOM   689   O O   . ARG A  1 81  ? -24.876 -49.338 10.800   1.00 36.83  ? 81  ARG A O   1 
ATOM   690   C CB  . ARG A  1 81  ? -26.084 -46.576 11.972   1.00 33.81  ? 81  ARG A CB  1 
ATOM   691   C CG  . ARG A  1 81  ? -27.102 -47.549 12.536   1.00 42.90  ? 81  ARG A CG  1 
ATOM   692   C CD  . ARG A  1 81  ? -28.517 -46.993 12.454   1.00 54.34  ? 81  ARG A CD  1 
ATOM   693   N NE  . ARG A  1 81  ? -28.677 -45.747 13.210   1.00 62.64  ? 81  ARG A NE  1 
ATOM   694   C CZ  . ARG A  1 81  ? -28.971 -45.668 14.509   1.00 67.54  ? 81  ARG A CZ  1 
ATOM   695   N NH1 . ARG A  1 81  ? -29.145 -46.771 15.230   1.00 67.57  ? 81  ARG A NH1 1 
ATOM   696   N NH2 . ARG A  1 81  ? -29.096 -44.475 15.088   1.00 67.89  ? 81  ARG A NH2 1 
ATOM   697   N N   . LYS A  1 82  ? -24.430 -47.607 9.434    1.00 33.31  ? 82  LYS A N   1 
ATOM   698   C CA  . LYS A  1 82  ? -24.644 -48.397 8.226    1.00 30.53  ? 82  LYS A CA  1 
ATOM   699   C C   . LYS A  1 82  ? -23.701 -49.597 8.149    1.00 25.37  ? 82  LYS A C   1 
ATOM   700   O O   . LYS A  1 82  ? -22.551 -49.548 8.602    1.00 24.95  ? 82  LYS A O   1 
ATOM   701   C CB  . LYS A  1 82  ? -24.460 -47.515 6.984    1.00 31.11  ? 82  LYS A CB  1 
ATOM   702   C CG  . LYS A  1 82  ? -25.746 -46.918 6.479    1.00 40.83  ? 82  LYS A CG  1 
ATOM   703   C CD  . LYS A  1 82  ? -25.582 -46.393 5.057    1.00 50.96  ? 82  LYS A CD  1 
ATOM   704   C CE  . LYS A  1 82  ? -25.511 -44.876 5.028    1.00 52.83  ? 82  LYS A CE  1 
ATOM   705   N NZ  . LYS A  1 82  ? -25.118 -44.371 3.674    1.00 53.42  ? 82  LYS A NZ  1 
ATOM   706   N N   . ASP A  1 83  ? -24.212 -50.685 7.585    1.00 30.52  ? 83  ASP A N   1 
ATOM   707   C CA  . ASP A  1 83  ? -23.354 -51.726 7.037    1.00 37.21  ? 83  ASP A CA  1 
ATOM   708   C C   . ASP A  1 83  ? -22.332 -51.088 6.094    1.00 34.83  ? 83  ASP A C   1 
ATOM   709   O O   . ASP A  1 83  ? -22.689 -50.195 5.315    1.00 34.85  ? 83  ASP A O   1 
ATOM   710   C CB  . ASP A  1 83  ? -24.196 -52.765 6.284    1.00 42.45  ? 83  ASP A CB  1 
ATOM   711   C CG  . ASP A  1 83  ? -23.391 -54.004 5.861    1.00 47.82  ? 83  ASP A CG  1 
ATOM   712   O OD1 . ASP A  1 83  ? -22.526 -53.890 4.965    1.00 44.19  ? 83  ASP A OD1 1 
ATOM   713   O OD2 . ASP A  1 83  ? -23.629 -55.105 6.427    1.00 49.21  ? 83  ASP A OD2 1 
ATOM   714   N N   . PRO A  1 84  ? -21.056 -51.492 6.156    1.00 33.37  ? 84  PRO A N   1 
ATOM   715   C CA  . PRO A  1 84  ? -20.042 -50.856 5.298    1.00 34.48  ? 84  PRO A CA  1 
ATOM   716   C C   . PRO A  1 84  ? -20.311 -51.006 3.812    1.00 29.29  ? 84  PRO A C   1 
ATOM   717   O O   . PRO A  1 84  ? -19.837 -50.177 3.032    1.00 33.09  ? 84  PRO A O   1 
ATOM   718   C CB  . PRO A  1 84  ? -18.740 -51.564 5.701    1.00 31.14  ? 84  PRO A CB  1 
ATOM   719   C CG  . PRO A  1 84  ? -19.012 -52.100 7.070    1.00 30.74  ? 84  PRO A CG  1 
ATOM   720   C CD  . PRO A  1 84  ? -20.461 -52.498 7.049    1.00 30.97  ? 84  PRO A CD  1 
ATOM   721   N N   . ASP A  1 85  ? -21.037 -52.036 3.379    1.00 34.02  ? 85  ASP A N   1 
ATOM   722   C CA  . ASP A  1 85  ? -21.293 -52.139 1.942    1.00 37.23  ? 85  ASP A CA  1 
ATOM   723   C C   . ASP A  1 85  ? -22.244 -51.067 1.436    1.00 35.43  ? 85  ASP A C   1 
ATOM   724   O O   . ASP A  1 85  ? -22.369 -50.890 0.215    1.00 37.17  ? 85  ASP A O   1 
ATOM   725   C CB  . ASP A  1 85  ? -21.854 -53.506 1.606    1.00 41.37  ? 85  ASP A CB  1 
ATOM   726   C CG  . ASP A  1 85  ? -20.882 -54.603 1.888    1.00 47.46  ? 85  ASP A CG  1 
ATOM   727   O OD1 . ASP A  1 85  ? -19.662 -54.328 1.957    1.00 50.63  ? 85  ASP A OD1 1 
ATOM   728   O OD2 . ASP A  1 85  ? -21.344 -55.743 2.050    1.00 51.28  ? 85  ASP A OD2 1 
ATOM   729   N N   . ASP A  1 86  ? -22.910 -50.355 2.335    1.00 33.70  ? 86  ASP A N   1 
ATOM   730   C CA  . ASP A  1 86  ? -23.798 -49.260 1.983    1.00 39.82  ? 86  ASP A CA  1 
ATOM   731   C C   . ASP A  1 86  ? -23.138 -47.892 2.072    1.00 36.97  ? 86  ASP A C   1 
ATOM   732   O O   . ASP A  1 86  ? -23.771 -46.899 1.706    1.00 40.89  ? 86  ASP A O   1 
ATOM   733   C CB  . ASP A  1 86  ? -25.030 -49.278 2.892    1.00 45.65  ? 86  ASP A CB  1 
ATOM   734   C CG  . ASP A  1 86  ? -25.833 -50.544 2.751    1.00 52.62  ? 86  ASP A CG  1 
ATOM   735   O OD1 . ASP A  1 86  ? -25.594 -51.312 1.792    1.00 54.22  ? 86  ASP A OD1 1 
ATOM   736   O OD2 . ASP A  1 86  ? -26.718 -50.763 3.598    1.00 53.41  ? 86  ASP A OD2 1 
ATOM   737   N N   . LEU A  1 87  ? -21.905 -47.810 2.563    1.00 29.97  ? 87  LEU A N   1 
ATOM   738   C CA  . LEU A  1 87  ? -21.264 -46.518 2.744    1.00 32.43  ? 87  LEU A CA  1 
ATOM   739   C C   . LEU A  1 87  ? -21.018 -45.845 1.401    1.00 32.55  ? 87  LEU A C   1 
ATOM   740   O O   . LEU A  1 87  ? -20.624 -46.488 0.423    1.00 33.82  ? 87  LEU A O   1 
ATOM   741   C CB  . LEU A  1 87  ? -19.941 -46.681 3.498    1.00 30.37  ? 87  LEU A CB  1 
ATOM   742   C CG  . LEU A  1 87  ? -20.066 -47.076 4.971    1.00 32.14  ? 87  LEU A CG  1 
ATOM   743   C CD1 . LEU A  1 87  ? -18.689 -47.146 5.625    1.00 30.98  ? 87  LEU A CD1 1 
ATOM   744   C CD2 . LEU A  1 87  ? -20.981 -46.101 5.714    1.00 29.31  ? 87  LEU A CD2 1 
ATOM   745   N N   . GLU A  1 88  ? -21.261 -44.540 1.357    1.00 32.32  ? 88  GLU A N   1 
ATOM   746   C CA  . GLU A  1 88  ? -20.832 -43.781 0.201    1.00 37.04  ? 88  GLU A CA  1 
ATOM   747   C C   . GLU A  1 88  ? -19.360 -43.427 0.354    1.00 41.26  ? 88  GLU A C   1 
ATOM   748   O O   . GLU A  1 88  ? -18.812 -43.379 1.469    1.00 30.08  ? 88  GLU A O   1 
ATOM   749   C CB  . GLU A  1 88  ? -21.672 -42.518 0.041    1.00 38.84  ? 88  GLU A CB  1 
ATOM   750   C CG  . GLU A  1 88  ? -23.155 -42.802 -0.062   1.00 43.39  ? 88  GLU A CG  1 
ATOM   751   C CD  . GLU A  1 88  ? -24.003 -41.612 0.310    1.00 52.82  ? 88  GLU A CD  1 
ATOM   752   O OE1 . GLU A  1 88  ? -25.236 -41.697 0.118    1.00 56.73  ? 88  GLU A OE1 1 
ATOM   753   O OE2 . GLU A  1 88  ? -23.439 -40.598 0.794    1.00 54.05  ? 88  GLU A OE2 1 
ATOM   754   N N   . LYS A  1 89  ? -18.707 -43.212 -0.789   1.00 32.73  ? 89  LYS A N   1 
ATOM   755   C CA  . LYS A  1 89  ? -17.344 -42.696 -0.762   1.00 36.17  ? 89  LYS A CA  1 
ATOM   756   C C   . LYS A  1 89  ? -17.225 -41.502 0.153    1.00 36.02  ? 89  LYS A C   1 
ATOM   757   O O   . LYS A  1 89  ? -16.258 -41.398 0.920    1.00 39.76  ? 89  LYS A O   1 
ATOM   758   C CB  . LYS A  1 89  ? -16.899 -42.301 -2.170   1.00 35.05  ? 89  LYS A CB  1 
ATOM   759   C CG  . LYS A  1 89  ? -17.252 -43.292 -3.212   1.00 52.76  ? 89  LYS A CG  1 
ATOM   760   C CD  . LYS A  1 89  ? -16.123 -43.543 -4.179   1.00 53.69  ? 89  LYS A CD  1 
ATOM   761   C CE  . LYS A  1 89  ? -16.615 -44.504 -5.233   1.00 58.36  ? 89  LYS A CE  1 
ATOM   762   N NZ  . LYS A  1 89  ? -16.056 -45.868 -5.037   1.00 65.05  ? 89  LYS A NZ  1 
ATOM   763   N N   . GLU A  1 90  ? -18.202 -40.586 0.082    1.00 35.20  ? 90  GLU A N   1 
ATOM   764   C CA  . GLU A  1 90  ? -18.156 -39.386 0.901    1.00 35.18  ? 90  GLU A CA  1 
ATOM   765   C C   . GLU A  1 90  ? -18.216 -39.738 2.382    1.00 30.11  ? 90  GLU A C   1 
ATOM   766   O O   . GLU A  1 90  ? -17.601 -39.062 3.212    1.00 30.41  ? 90  GLU A O   1 
ATOM   767   C CB  . GLU A  1 90  ? -19.308 -38.444 0.560    1.00 35.49  ? 90  GLU A CB  1 
ATOM   768   C CG  . GLU A  1 90  ? -19.270 -37.861 -0.818   1.00 47.71  ? 90  GLU A CG  1 
ATOM   769   C CD  . GLU A  1 90  ? -20.300 -36.770 -0.994   1.00 49.66  ? 90  GLU A CD  1 
ATOM   770   O OE1 . GLU A  1 90  ? -20.450 -36.248 -2.124   1.00 55.02  ? 90  GLU A OE1 1 
ATOM   771   O OE2 . GLU A  1 90  ? -20.970 -36.447 0.007    1.00 42.66  ? 90  GLU A OE2 1 
ATOM   772   N N   . GLU A  1 91  ? -18.962 -40.793 2.721    1.00 30.56  ? 91  GLU A N   1 
ATOM   773   C CA  . GLU A  1 91  ? -19.103 -41.215 4.106    1.00 29.19  ? 91  GLU A CA  1 
ATOM   774   C C   . GLU A  1 91  ? -17.841 -41.913 4.601    1.00 29.69  ? 91  GLU A C   1 
ATOM   775   O O   . GLU A  1 91  ? -17.413 -41.685 5.738    1.00 29.38  ? 91  GLU A O   1 
ATOM   776   C CB  . GLU A  1 91  ? -20.318 -42.132 4.260    1.00 31.15  ? 91  GLU A CB  1 
ATOM   777   C CG  . GLU A  1 91  ? -21.650 -41.418 4.044    1.00 34.28  ? 91  GLU A CG  1 
ATOM   778   C CD  . GLU A  1 91  ? -22.845 -42.358 4.158    1.00 37.62  ? 91  GLU A CD  1 
ATOM   779   O OE1 . GLU A  1 91  ? -22.880 -43.398 3.457    1.00 34.21  ? 91  GLU A OE1 1 
ATOM   780   O OE2 . GLU A  1 91  ? -23.746 -42.064 4.977    1.00 40.76  ? 91  GLU A OE2 1 
ATOM   781   N N   . VAL A  1 92  ? -17.234 -42.761 3.770    1.00 30.30  ? 92  VAL A N   1 
ATOM   782   C CA  . VAL A  1 92  ? -15.942 -43.342 4.133    1.00 35.43  ? 92  VAL A CA  1 
ATOM   783   C C   . VAL A  1 92  ? -14.904 -42.239 4.341    1.00 34.56  ? 92  VAL A C   1 
ATOM   784   O O   . VAL A  1 92  ? -14.101 -42.297 5.279    1.00 31.73  ? 92  VAL A O   1 
ATOM   785   C CB  . VAL A  1 92  ? -15.485 -44.370 3.076    1.00 33.61  ? 92  VAL A CB  1 
ATOM   786   C CG1 . VAL A  1 92  ? -14.129 -44.983 3.461    1.00 30.28  ? 92  VAL A CG1 1 
ATOM   787   C CG2 . VAL A  1 92  ? -16.517 -45.486 2.914    1.00 28.84  ? 92  VAL A CG2 1 
ATOM   788   N N   . GLU A  1 93  ? -14.909 -41.214 3.480    1.00 33.15  ? 93  GLU A N   1 
ATOM   789   C CA  . GLU A  1 93  ? -13.942 -40.124 3.621    1.00 35.90  ? 93  GLU A CA  1 
ATOM   790   C C   . GLU A  1 93  ? -14.175 -39.355 4.912    1.00 32.66  ? 93  GLU A C   1 
ATOM   791   O O   . GLU A  1 93  ? -13.216 -38.996 5.609    1.00 29.45  ? 93  GLU A O   1 
ATOM   792   C CB  . GLU A  1 93  ? -14.003 -39.175 2.415    1.00 37.86  ? 93  GLU A CB  1 
ATOM   793   C CG  . GLU A  1 93  ? -13.283 -39.697 1.159    1.00 45.40  ? 93  GLU A CG  1 
ATOM   794   C CD  . GLU A  1 93  ? -13.619 -38.919 -0.122   1.00 53.30  ? 93  GLU A CD  1 
ATOM   795   O OE1 . GLU A  1 93  ? -14.292 -37.869 -0.044   1.00 53.23  ? 93  GLU A OE1 1 
ATOM   796   O OE2 . GLU A  1 93  ? -13.223 -39.377 -1.221   1.00 54.15  ? 93  GLU A OE2 1 
ATOM   797   N N   . LYS A  1 94  ? -15.441 -39.077 5.240    1.00 32.48  ? 94  LYS A N   1 
ATOM   798   C CA  . LYS A  1 94  ? -15.731 -38.350 6.472    1.00 35.50  ? 94  LYS A CA  1 
ATOM   799   C C   . LYS A  1 94  ? -15.350 -39.180 7.691    1.00 34.53  ? 94  LYS A C   1 
ATOM   800   O O   . LYS A  1 94  ? -14.846 -38.646 8.684    1.00 28.87  ? 94  LYS A O   1 
ATOM   801   C CB  . LYS A  1 94  ? -17.210 -37.955 6.523    1.00 40.58  ? 94  LYS A CB  1 
ATOM   802   C CG  . LYS A  1 94  ? -17.498 -36.558 5.972    1.00 47.34  ? 94  LYS A CG  1 
ATOM   803   C CD  . LYS A  1 94  ? -18.915 -36.455 5.419    1.00 54.73  ? 94  LYS A CD  1 
ATOM   804   C CE  . LYS A  1 94  ? -19.069 -35.237 4.516    1.00 62.05  ? 94  LYS A CE  1 
ATOM   805   N NZ  . LYS A  1 94  ? -18.971 -33.974 5.299    1.00 66.46  ? 94  LYS A NZ  1 
ATOM   806   N N   . LEU A  1 95  ? -15.559 -40.494 7.613    1.00 31.74  ? 95  LEU A N   1 
ATOM   807   C CA  . LEU A  1 95  ? -15.192 -41.385 8.705    1.00 35.17  ? 95  LEU A CA  1 
ATOM   808   C C   . LEU A  1 95  ? -13.681 -41.431 8.900    1.00 31.89  ? 95  LEU A C   1 
ATOM   809   O O   . LEU A  1 95  ? -13.188 -41.379 10.038   1.00 29.20  ? 95  LEU A O   1 
ATOM   810   C CB  . LEU A  1 95  ? -15.746 -42.773 8.420    1.00 35.19  ? 95  LEU A CB  1 
ATOM   811   C CG  . LEU A  1 95  ? -15.656 -43.783 9.542    1.00 45.31  ? 95  LEU A CG  1 
ATOM   812   C CD1 . LEU A  1 95  ? -16.581 -43.354 10.665   1.00 41.91  ? 95  LEU A CD1 1 
ATOM   813   C CD2 . LEU A  1 95  ? -16.007 -45.171 9.015    1.00 49.16  ? 95  LEU A CD2 1 
ATOM   814   N N   . ILE A  1 96  ? -12.932 -41.517 7.799    1.00 29.57  ? 96  ILE A N   1 
ATOM   815   C CA  . ILE A  1 96  ? -11.474 -41.453 7.874    1.00 30.37  ? 96  ILE A CA  1 
ATOM   816   C C   . ILE A  1 96  ? -11.037 -40.097 8.409    1.00 29.94  ? 96  ILE A C   1 
ATOM   817   O O   . ILE A  1 96  ? -10.205 -40.009 9.325    1.00 30.98  ? 96  ILE A O   1 
ATOM   818   C CB  . ILE A  1 96  ? -10.850 -41.752 6.495    1.00 32.37  ? 96  ILE A CB  1 
ATOM   819   C CG1 . ILE A  1 96  ? -11.037 -43.220 6.133    1.00 31.13  ? 96  ILE A CG1 1 
ATOM   820   C CG2 . ILE A  1 96  ? -9.366  -41.433 6.490    1.00 34.07  ? 96  ILE A CG2 1 
ATOM   821   C CD1 . ILE A  1 96  ? -10.743 -43.514 4.678    1.00 38.95  ? 96  ILE A CD1 1 
ATOM   822   N N   . GLU A  1 97  ? -11.620 -39.020 7.871    1.00 27.47  ? 97  GLU A N   1 
ATOM   823   C CA  . GLU A  1 97  ? -11.275 -37.680 8.334    1.00 31.47  ? 97  GLU A CA  1 
ATOM   824   C C   . GLU A  1 97  ? -11.557 -37.530 9.821    1.00 31.86  ? 97  GLU A C   1 
ATOM   825   O O   . GLU A  1 97  ? -10.766 -36.931 10.554   1.00 26.50  ? 97  GLU A O   1 
ATOM   826   C CB  . GLU A  1 97  ? -12.052 -36.617 7.555    1.00 36.42  ? 97  GLU A CB  1 
ATOM   827   C CG  . GLU A  1 97  ? -11.538 -36.339 6.155    1.00 49.46  ? 97  GLU A CG  1 
ATOM   828   C CD  . GLU A  1 97  ? -12.574 -35.641 5.279    1.00 61.68  ? 97  GLU A CD  1 
ATOM   829   O OE1 . GLU A  1 97  ? -13.785 -35.904 5.462    1.00 63.63  ? 97  GLU A OE1 1 
ATOM   830   O OE2 . GLU A  1 97  ? -12.176 -34.855 4.388    1.00 69.46  ? 97  GLU A OE2 1 
ATOM   831   N N   . PHE A  1 98  ? -12.689 -38.051 10.280   1.00 30.56  ? 98  PHE A N   1 
ATOM   832   C CA  . PHE A  1 98  ? -13.014 -37.909 11.692   1.00 28.19  ? 98  PHE A CA  1 
ATOM   833   C C   . PHE A  1 98  ? -12.006 -38.656 12.561   1.00 30.64  ? 98  PHE A C   1 
ATOM   834   O O   . PHE A  1 98  ? -11.610 -38.166 13.628   1.00 28.22  ? 98  PHE A O   1 
ATOM   835   C CB  . PHE A  1 98  ? -14.433 -38.398 11.942   1.00 28.04  ? 98  PHE A CB  1 
ATOM   836   C CG  . PHE A  1 98  ? -14.964 -38.046 13.298   1.00 32.00  ? 98  PHE A CG  1 
ATOM   837   C CD1 . PHE A  1 98  ? -15.428 -36.764 13.559   1.00 34.49  ? 98  PHE A CD1 1 
ATOM   838   C CD2 . PHE A  1 98  ? -15.008 -38.994 14.309   1.00 33.81  ? 98  PHE A CD2 1 
ATOM   839   C CE1 . PHE A  1 98  ? -15.937 -36.444 14.799   1.00 32.26  ? 98  PHE A CE1 1 
ATOM   840   C CE2 . PHE A  1 98  ? -15.509 -38.665 15.566   1.00 29.66  ? 98  PHE A CE2 1 
ATOM   841   C CZ  . PHE A  1 98  ? -15.972 -37.387 15.801   1.00 28.91  ? 98  PHE A CZ  1 
ATOM   842   N N   . THR A  1 99  ? -11.554 -39.827 12.097   1.00 28.43  ? 99  THR A N   1 
ATOM   843   C CA  . THR A  1 99  ? -10.566 -40.614 12.829   1.00 34.90  ? 99  THR A CA  1 
ATOM   844   C C   . THR A  1 99  ? -9.235  -39.878 12.979   1.00 31.90  ? 99  THR A C   1 
ATOM   845   O O   . THR A  1 99  ? -8.683  -39.805 14.087   1.00 26.40  ? 99  THR A O   1 
ATOM   846   C CB  . THR A  1 99  ? -10.357 -41.971 12.145   1.00 31.87  ? 99  THR A CB  1 
ATOM   847   O OG1 . THR A  1 99  ? -11.610 -42.654 12.015   1.00 29.30  ? 99  THR A OG1 1 
ATOM   848   C CG2 . THR A  1 99  ? -9.421  -42.828 12.962   1.00 33.78  ? 99  THR A CG2 1 
ATOM   849   N N   . LYS A  1 100 ? -8.692  -39.327 11.879   1.00 26.33  ? 100 LYS A N   1 
ATOM   850   C CA  . LYS A  1 100 ? -7.380  -38.684 11.967   1.00 35.48  ? 100 LYS A CA  1 
ATOM   851   C C   . LYS A  1 100 ? -7.444  -37.375 12.769   1.00 35.33  ? 100 LYS A C   1 
ATOM   852   O O   . LYS A  1 100 ? -6.425  -36.911 13.287   1.00 36.14  ? 100 LYS A O   1 
ATOM   853   C CB  . LYS A  1 100 ? -6.790  -38.440 10.564   1.00 44.88  ? 100 LYS A CB  1 
ATOM   854   C CG  . LYS A  1 100 ? -7.617  -37.647 9.527    1.00 58.81  ? 100 LYS A CG  1 
ATOM   855   C CD  . LYS A  1 100 ? -7.999  -36.240 9.976    1.00 63.41  ? 100 LYS A CD  1 
ATOM   856   C CE  . LYS A  1 100 ? -8.705  -35.392 8.934    1.00 66.80  ? 100 LYS A CE  1 
ATOM   857   N NZ  . LYS A  1 100 ? -9.302  -34.241 9.676    1.00 62.86  ? 100 LYS A NZ  1 
ATOM   858   N N   . LEU A  1 101 ? -8.629  -36.762 12.878   1.00 30.90  ? 101 LEU A N   1 
ATOM   859   C CA  . LEU A  1 101 ? -8.780  -35.562 13.703   1.00 31.14  ? 101 LEU A CA  1 
ATOM   860   C C   . LEU A  1 101 ? -8.629  -35.902 15.179   1.00 27.72  ? 101 LEU A C   1 
ATOM   861   O O   . LEU A  1 101 ? -8.052  -35.125 15.945   1.00 31.38  ? 101 LEU A O   1 
ATOM   862   C CB  . LEU A  1 101 ? -10.137 -34.924 13.423   1.00 30.89  ? 101 LEU A CB  1 
ATOM   863   C CG  . LEU A  1 101 ? -10.654 -33.874 14.390   1.00 37.97  ? 101 LEU A CG  1 
ATOM   864   C CD1 . LEU A  1 101 ? -9.783  -32.616 14.328   1.00 41.26  ? 101 LEU A CD1 1 
ATOM   865   C CD2 . LEU A  1 101 ? -12.111 -33.536 14.080   1.00 40.04  ? 101 LEU A CD2 1 
ATOM   866   N N   . ASN A  1 102 ? -9.135  -37.062 15.584   1.00 26.83  ? 102 ASN A N   1 
ATOM   867   C CA  . ASN A  1 102 ? -9.080  -37.547 16.958   1.00 27.09  ? 102 ASN A CA  1 
ATOM   868   C C   . ASN A  1 102 ? -7.943  -38.540 17.204   1.00 32.95  ? 102 ASN A C   1 
ATOM   869   O O   . ASN A  1 102 ? -7.811  -39.043 18.320   1.00 27.26  ? 102 ASN A O   1 
ATOM   870   C CB  . ASN A  1 102 ? -10.410 -38.199 17.322   1.00 24.17  ? 102 ASN A CB  1 
ATOM   871   C CG  . ASN A  1 102 ? -11.560 -37.224 17.275   1.00 29.91  ? 102 ASN A CG  1 
ATOM   872   O OD1 . ASN A  1 102 ? -11.657 -36.335 18.125   1.00 34.81  ? 102 ASN A OD1 1 
ATOM   873   N ND2 . ASN A  1 102 ? -12.451 -37.385 16.294   1.00 23.52  ? 102 ASN A ND2 1 
ATOM   874   N N   . TYR A  1 103 ? -7.096  -38.782 16.200   1.00 33.89  ? 103 TYR A N   1 
ATOM   875   C CA  . TYR A  1 103 ? -6.164  -39.909 16.200   1.00 33.31  ? 103 TYR A CA  1 
ATOM   876   C C   . TYR A  1 103 ? -5.212  -39.908 17.402   1.00 32.42  ? 103 TYR A C   1 
ATOM   877   O O   . TYR A  1 103 ? -4.830  -40.976 17.899   1.00 33.30  ? 103 TYR A O   1 
ATOM   878   C CB  . TYR A  1 103 ? -5.364  -39.873 14.891   1.00 38.35  ? 103 TYR A CB  1 
ATOM   879   C CG  . TYR A  1 103 ? -4.386  -40.996 14.728   1.00 39.90  ? 103 TYR A CG  1 
ATOM   880   C CD1 . TYR A  1 103 ? -4.799  -42.230 14.270   1.00 42.18  ? 103 TYR A CD1 1 
ATOM   881   C CD2 . TYR A  1 103 ? -3.046  -40.821 15.037   1.00 46.47  ? 103 TYR A CD2 1 
ATOM   882   C CE1 . TYR A  1 103 ? -3.909  -43.263 14.117   1.00 48.86  ? 103 TYR A CE1 1 
ATOM   883   C CE2 . TYR A  1 103 ? -2.142  -41.847 14.891   1.00 49.63  ? 103 TYR A CE2 1 
ATOM   884   C CZ  . TYR A  1 103 ? -2.576  -43.068 14.431   1.00 53.12  ? 103 TYR A CZ  1 
ATOM   885   O OH  . TYR A  1 103 ? -1.677  -44.101 14.280   1.00 58.61  ? 103 TYR A OH  1 
ATOM   886   N N   . GLU A  1 104 ? -4.785  -38.732 17.857   1.00 31.96  ? 104 GLU A N   1 
ATOM   887   C CA  . GLU A  1 104 ? -3.735  -38.654 18.866   1.00 34.81  ? 104 GLU A CA  1 
ATOM   888   C C   . GLU A  1 104 ? -4.280  -38.531 20.283   1.00 30.92  ? 104 GLU A C   1 
ATOM   889   O O   . GLU A  1 104 ? -3.494  -38.438 21.230   1.00 31.54  ? 104 GLU A O   1 
ATOM   890   C CB  . GLU A  1 104 ? -2.800  -37.475 18.576   1.00 41.55  ? 104 GLU A CB  1 
ATOM   891   C CG  . GLU A  1 104 ? -1.969  -37.621 17.312   1.00 52.76  ? 104 GLU A CG  1 
ATOM   892   C CD  . GLU A  1 104 ? -0.765  -38.524 17.499   1.00 65.83  ? 104 GLU A CD  1 
ATOM   893   O OE1 . GLU A  1 104 ? -0.477  -38.918 18.653   1.00 70.04  ? 104 GLU A OE1 1 
ATOM   894   O OE2 . GLU A  1 104 ? -0.099  -38.833 16.488   1.00 71.83  ? 104 GLU A OE2 1 
ATOM   895   N N   . LYS A  1 105 ? -5.575  -38.521 20.444   1.00 27.78  ? 105 LYS A N   1 
ATOM   896   C CA  . LYS A  1 105 ? -6.182  -38.457 21.769   1.00 26.64  ? 105 LYS A CA  1 
ATOM   897   C C   . LYS A  1 105 ? -6.098  -39.812 22.468   1.00 28.14  ? 105 LYS A C   1 
ATOM   898   O O   . LYS A  1 105 ? -6.326  -40.848 21.841   1.00 26.71  ? 105 LYS A O   1 
ATOM   899   C CB  . LYS A  1 105 ? -7.635  -38.025 21.656   1.00 27.02  ? 105 LYS A CB  1 
ATOM   900   C CG  . LYS A  1 105 ? -7.786  -36.605 21.171   1.00 27.33  ? 105 LYS A CG  1 
ATOM   901   C CD  . LYS A  1 105 ? -9.188  -36.353 20.705   1.00 23.36  ? 105 LYS A CD  1 
ATOM   902   C CE  . LYS A  1 105 ? -9.295  -34.958 20.148   1.00 24.96  ? 105 LYS A CE  1 
ATOM   903   N NZ  . LYS A  1 105 ? -10.702 -34.663 19.746   1.00 23.53  ? 105 LYS A NZ  1 
ATOM   904   N N   . PRO A  1 106 ? -5.787  -39.827 23.770   1.00 30.75  ? 106 PRO A N   1 
ATOM   905   C CA  . PRO A  1 106 ? -5.729  -41.101 24.503   1.00 29.92  ? 106 PRO A CA  1 
ATOM   906   C C   . PRO A  1 106 ? -6.970  -41.967 24.358   1.00 24.03  ? 106 PRO A C   1 
ATOM   907   O O   . PRO A  1 106 ? -6.855  -43.201 24.416   1.00 24.48  ? 106 PRO A O   1 
ATOM   908   C CB  . PRO A  1 106 ? -5.530  -40.645 25.959   1.00 29.74  ? 106 PRO A CB  1 
ATOM   909   C CG  . PRO A  1 106 ? -4.779  -39.338 25.824   1.00 31.72  ? 106 PRO A CG  1 
ATOM   910   C CD  . PRO A  1 106 ? -5.346  -38.686 24.593   1.00 24.32  ? 106 PRO A CD  1 
ATOM   911   N N   . ILE A  1 107 ? -8.154  -41.383 24.168   1.00 21.77  ? 107 ILE A N   1 
ATOM   912   C CA  . ILE A  1 107 ? -9.339  -42.224 24.034   1.00 23.52  ? 107 ILE A CA  1 
ATOM   913   C C   . ILE A  1 107 ? -9.394  -42.943 22.693   1.00 27.31  ? 107 ILE A C   1 
ATOM   914   O O   . ILE A  1 107 ? -10.196 -43.876 22.523   1.00 22.38  ? 107 ILE A O   1 
ATOM   915   C CB  . ILE A  1 107 ? -10.627 -41.409 24.259   1.00 21.91  ? 107 ILE A CB  1 
ATOM   916   C CG1 . ILE A  1 107 ? -10.724 -40.268 23.257   1.00 21.72  ? 107 ILE A CG1 1 
ATOM   917   C CG2 . ILE A  1 107 ? -10.711 -40.888 25.726   1.00 19.78  ? 107 ILE A CG2 1 
ATOM   918   C CD1 . ILE A  1 107 ? -12.089 -39.592 23.276   1.00 25.57  ? 107 ILE A CD1 1 
ATOM   919   N N   . TYR A  1 108 ? -8.540  -42.553 21.744   1.00 28.26  ? 108 TYR A N   1 
ATOM   920   C CA  . TYR A  1 108 ? -8.418  -43.248 20.472   1.00 31.43  ? 108 TYR A CA  1 
ATOM   921   C C   . TYR A  1 108 ? -7.240  -44.225 20.427   1.00 30.62  ? 108 TYR A C   1 
ATOM   922   O O   . TYR A  1 108 ? -6.908  -44.728 19.350   1.00 26.54  ? 108 TYR A O   1 
ATOM   923   C CB  . TYR A  1 108 ? -8.307  -42.224 19.339   1.00 29.15  ? 108 TYR A CB  1 
ATOM   924   C CG  . TYR A  1 108 ? -9.659  -41.857 18.782   1.00 28.77  ? 108 TYR A CG  1 
ATOM   925   C CD1 . TYR A  1 108 ? -10.563 -41.116 19.532   1.00 25.17  ? 108 TYR A CD1 1 
ATOM   926   C CD2 . TYR A  1 108 ? -10.036 -42.261 17.508   1.00 27.43  ? 108 TYR A CD2 1 
ATOM   927   C CE1 . TYR A  1 108 ? -11.810 -40.782 19.025   1.00 27.16  ? 108 TYR A CE1 1 
ATOM   928   C CE2 . TYR A  1 108 ? -11.272 -41.944 17.002   1.00 28.65  ? 108 TYR A CE2 1 
ATOM   929   C CZ  . TYR A  1 108 ? -12.155 -41.216 17.757   1.00 26.87  ? 108 TYR A CZ  1 
ATOM   930   O OH  . TYR A  1 108 ? -13.383 -40.902 17.238   1.00 25.18  ? 108 TYR A OH  1 
ATOM   931   N N   . ARG A  1 109 ? -6.601  -44.518 21.563   1.00 25.83  ? 109 ARG A N   1 
ATOM   932   C CA  . ARG A  1 109 ? -5.436  -45.395 21.535   1.00 27.17  ? 109 ARG A CA  1 
ATOM   933   C C   . ARG A  1 109 ? -5.902  -46.847 21.462   1.00 30.69  ? 109 ARG A C   1 
ATOM   934   O O   . ARG A  1 109 ? -5.970  -47.577 22.454   1.00 33.73  ? 109 ARG A O   1 
ATOM   935   C CB  . ARG A  1 109 ? -4.526  -45.143 22.729   1.00 32.58  ? 109 ARG A CB  1 
ATOM   936   C CG  . ARG A  1 109 ? -3.068  -45.091 22.329   1.00 42.43  ? 109 ARG A CG  1 
ATOM   937   C CD  . ARG A  1 109 ? -2.251  -44.366 23.366   1.00 51.40  ? 109 ARG A CD  1 
ATOM   938   N NE  . ARG A  1 109 ? -2.470  -44.934 24.689   1.00 54.85  ? 109 ARG A NE  1 
ATOM   939   C CZ  . ARG A  1 109 ? -2.457  -44.231 25.816   1.00 55.16  ? 109 ARG A CZ  1 
ATOM   940   N NH1 . ARG A  1 109 ? -2.234  -42.917 25.778   1.00 53.45  ? 109 ARG A NH1 1 
ATOM   941   N NH2 . ARG A  1 109 ? -2.668  -44.840 26.980   1.00 54.71  ? 109 ARG A NH2 1 
ATOM   942   N N   . PHE A  1 110 ? -6.253  -47.253 20.249   1.00 30.77  ? 110 PHE A N   1 
ATOM   943   C CA  . PHE A  1 110 ? -6.470  -48.644 19.885   1.00 31.43  ? 110 PHE A CA  1 
ATOM   944   C C   . PHE A  1 110 ? -5.438  -48.991 18.824   1.00 31.38  ? 110 PHE A C   1 
ATOM   945   O O   . PHE A  1 110 ? -5.269  -48.240 17.859   1.00 33.52  ? 110 PHE A O   1 
ATOM   946   C CB  . PHE A  1 110 ? -7.880  -48.874 19.328   1.00 26.38  ? 110 PHE A CB  1 
ATOM   947   C CG  . PHE A  1 110 ? -8.989  -48.562 20.292   1.00 31.59  ? 110 PHE A CG  1 
ATOM   948   C CD1 . PHE A  1 110 ? -9.531  -47.286 20.365   1.00 31.50  ? 110 PHE A CD1 1 
ATOM   949   C CD2 . PHE A  1 110 ? -9.516  -49.556 21.104   1.00 33.88  ? 110 PHE A CD2 1 
ATOM   950   C CE1 . PHE A  1 110 ? -10.568 -47.006 21.238   1.00 27.98  ? 110 PHE A CE1 1 
ATOM   951   C CE2 . PHE A  1 110 ? -10.555 -49.277 21.988   1.00 31.64  ? 110 PHE A CE2 1 
ATOM   952   C CZ  . PHE A  1 110 ? -11.078 -48.000 22.052   1.00 29.63  ? 110 PHE A CZ  1 
ATOM   953   N N   . GLU A  1 111 ? -4.742  -50.117 18.992   1.00 34.70  ? 111 GLU A N   1 
ATOM   954   C CA  . GLU A  1 111 ? -3.769  -50.490 17.971   1.00 39.82  ? 111 GLU A CA  1 
ATOM   955   C C   . GLU A  1 111 ? -4.444  -50.659 16.615   1.00 34.62  ? 111 GLU A C   1 
ATOM   956   O O   . GLU A  1 111 ? -3.859  -50.319 15.579   1.00 31.22  ? 111 GLU A O   1 
ATOM   957   C CB  . GLU A  1 111 ? -3.028  -51.765 18.374   1.00 54.31  ? 111 GLU A CB  1 
ATOM   958   C CG  . GLU A  1 111 ? -1.908  -52.165 17.422   1.00 66.17  ? 111 GLU A CG  1 
ATOM   959   C CD  . GLU A  1 111 ? -0.740  -51.192 17.450   1.00 77.55  ? 111 GLU A CD  1 
ATOM   960   O OE1 . GLU A  1 111 ? -0.533  -50.476 16.443   1.00 81.60  ? 111 GLU A OE1 1 
ATOM   961   O OE2 . GLU A  1 111 ? -0.035  -51.134 18.483   1.00 81.10  ? 111 GLU A OE2 1 
ATOM   962   N N   . ARG A  1 112 ? -5.693  -51.131 16.609   1.00 32.03  ? 112 ARG A N   1 
ATOM   963   C CA  . ARG A  1 112 ? -6.392  -51.350 15.347   1.00 36.42  ? 112 ARG A CA  1 
ATOM   964   C C   . ARG A  1 112 ? -6.577  -50.044 14.583   1.00 36.16  ? 112 ARG A C   1 
ATOM   965   O O   . ARG A  1 112 ? -6.519  -50.030 13.347   1.00 34.96  ? 112 ARG A O   1 
ATOM   966   C CB  . ARG A  1 112 ? -7.743  -52.028 15.603   1.00 35.48  ? 112 ARG A CB  1 
ATOM   967   C CG  . ARG A  1 112 ? -8.532  -52.339 14.336   1.00 35.34  ? 112 ARG A CG  1 
ATOM   968   C CD  . ARG A  1 112 ? -7.772  -53.265 13.397   1.00 36.71  ? 112 ARG A CD  1 
ATOM   969   N NE  . ARG A  1 112 ? -8.707  -54.074 12.623   1.00 36.77  ? 112 ARG A NE  1 
ATOM   970   C CZ  . ARG A  1 112 ? -8.444  -54.613 11.438   1.00 37.93  ? 112 ARG A CZ  1 
ATOM   971   N NH1 . ARG A  1 112 ? -7.259  -54.437 10.865   1.00 39.70  ? 112 ARG A NH1 1 
ATOM   972   N NH2 . ARG A  1 112 ? -9.374  -55.325 10.828   1.00 34.45  ? 112 ARG A NH2 1 
ATOM   973   N N   . ILE A  1 113 ? -6.801  -48.934 15.300   1.00 35.85  ? 113 ILE A N   1 
ATOM   974   C CA  . ILE A  1 113 ? -6.910  -47.636 14.629   1.00 33.55  ? 113 ILE A CA  1 
ATOM   975   C C   . ILE A  1 113 ? -5.613  -47.319 13.894   1.00 34.38  ? 113 ILE A C   1 
ATOM   976   O O   . ILE A  1 113 ? -5.627  -46.862 12.748   1.00 36.09  ? 113 ILE A O   1 
ATOM   977   C CB  . ILE A  1 113 ? -7.265  -46.526 15.639   1.00 29.88  ? 113 ILE A CB  1 
ATOM   978   C CG1 . ILE A  1 113 ? -8.697  -46.679 16.167   1.00 33.13  ? 113 ILE A CG1 1 
ATOM   979   C CG2 . ILE A  1 113 ? -7.069  -45.161 15.013   1.00 30.21  ? 113 ILE A CG2 1 
ATOM   980   C CD1 . ILE A  1 113 ? -9.768  -46.290 15.182   1.00 34.25  ? 113 ILE A CD1 1 
ATOM   981   N N   . ARG A  1 114 ? -4.471  -47.578 14.536   1.00 36.39  ? 114 ARG A N   1 
ATOM   982   C CA  . ARG A  1 114 ? -3.191  -47.330 13.885   1.00 43.75  ? 114 ARG A CA  1 
ATOM   983   C C   . ARG A  1 114 ? -3.068  -48.147 12.608   1.00 48.63  ? 114 ARG A C   1 
ATOM   984   O O   . ARG A  1 114 ? -2.630  -47.630 11.571   1.00 48.02  ? 114 ARG A O   1 
ATOM   985   C CB  . ARG A  1 114 ? -2.042  -47.640 14.849   1.00 47.86  ? 114 ARG A CB  1 
ATOM   986   C CG  . ARG A  1 114 ? -2.259  -47.086 16.259   1.00 55.61  ? 114 ARG A CG  1 
ATOM   987   C CD  . ARG A  1 114 ? -1.082  -47.394 17.192   1.00 62.61  ? 114 ARG A CD  1 
ATOM   988   N NE  . ARG A  1 114 ? -1.465  -47.320 18.603   1.00 63.71  ? 114 ARG A NE  1 
ATOM   989   C CZ  . ARG A  1 114 ? -0.904  -48.036 19.575   1.00 64.52  ? 114 ARG A CZ  1 
ATOM   990   N NH1 . ARG A  1 114 ? 0.076   -48.892 19.301   1.00 65.34  ? 114 ARG A NH1 1 
ATOM   991   N NH2 . ARG A  1 114 ? -1.323  -47.895 20.827   1.00 62.97  ? 114 ARG A NH2 1 
ATOM   992   N N   . GLU A  1 115 ? -3.487  -49.415 12.655   1.00 51.47  ? 115 GLU A N   1 
ATOM   993   C CA  . GLU A  1 115 ? -3.439  -50.266 11.469   1.00 49.69  ? 115 GLU A CA  1 
ATOM   994   C C   . GLU A  1 115 ? -4.324  -49.714 10.358   1.00 48.32  ? 115 GLU A C   1 
ATOM   995   O O   . GLU A  1 115 ? -3.867  -49.521 9.227    1.00 53.96  ? 115 GLU A O   1 
ATOM   996   C CB  . GLU A  1 115 ? -3.859  -51.689 11.834   1.00 51.03  ? 115 GLU A CB  1 
ATOM   997   C CG  . GLU A  1 115 ? -2.942  -52.350 12.852   1.00 57.03  ? 115 GLU A CG  1 
ATOM   998   C CD  . GLU A  1 115 ? -3.540  -53.603 13.485   1.00 61.73  ? 115 GLU A CD  1 
ATOM   999   O OE1 . GLU A  1 115 ? -4.587  -54.090 13.002   1.00 63.34  ? 115 GLU A OE1 1 
ATOM   1000  O OE2 . GLU A  1 115 ? -2.955  -54.103 14.470   1.00 62.17  ? 115 GLU A OE2 1 
ATOM   1001  N N   . LEU A  1 116 ? -5.595  -49.445 10.668   1.00 44.27  ? 116 LEU A N   1 
ATOM   1002  C CA  . LEU A  1 116 ? -6.539  -48.987 9.653    1.00 42.03  ? 116 LEU A CA  1 
ATOM   1003  C C   . LEU A  1 116 ? -6.092  -47.682 9.004    1.00 43.83  ? 116 LEU A C   1 
ATOM   1004  O O   . LEU A  1 116 ? -6.301  -47.477 7.803    1.00 43.81  ? 116 LEU A O   1 
ATOM   1005  C CB  . LEU A  1 116 ? -7.925  -48.809 10.270   1.00 38.69  ? 116 LEU A CB  1 
ATOM   1006  C CG  . LEU A  1 116 ? -8.536  -50.051 10.910   1.00 39.30  ? 116 LEU A CG  1 
ATOM   1007  C CD1 . LEU A  1 116 ? -9.816  -49.712 11.676   1.00 35.74  ? 116 LEU A CD1 1 
ATOM   1008  C CD2 . LEU A  1 116 ? -8.790  -51.101 9.833    1.00 40.08  ? 116 LEU A CD2 1 
ATOM   1009  N N   . MET A  1 117 ? -5.435  -46.825 9.716    1.00 47.09  ? 117 MET A N   1 
ATOM   1010  C CA  . MET A  1 117 ? -5.083  -45.496 9.217    1.00 50.28  ? 117 MET A CA  1 
ATOM   1011  C C   . MET A  1 117 ? -3.962  -45.581 8.240    1.00 55.91  ? 117 MET A C   1 
ATOM   1012  O O   . MET A  1 117 ? -3.846  -44.795 7.334    1.00 54.88  ? 117 MET A O   1 
ATOM   1013  C CB  . MET A  1 117 ? -4.679  -44.655 10.392   1.00 48.73  ? 117 MET A CB  1 
ATOM   1014  C CG  . MET A  1 117 ? -5.871  -44.009 11.069   1.00 50.98  ? 117 MET A CG  1 
ATOM   1015  S SD  . MET A  1 117 ? -7.211  -43.678 9.923    1.00 52.91  ? 117 MET A SD  1 
ATOM   1016  C CE  . MET A  1 117 ? -7.277  -41.909 10.027   1.00 53.87  ? 117 MET A CE  1 
ATOM   1017  N N   . ASN A  1 118 ? -3.182  -46.630 8.408    1.00 60.29  ? 118 ASN A N   1 
ATOM   1018  C CA  . ASN A  1 118 ? -2.078  -46.851 7.554    1.00 65.24  ? 118 ASN A CA  1 
ATOM   1019  C C   . ASN A  1 118 ? -2.494  -47.602 6.353    1.00 67.74  ? 118 ASN A C   1 
ATOM   1020  O O   . ASN A  1 118 ? -1.656  -48.152 5.666    1.00 70.13  ? 118 ASN A O   1 
ATOM   1021  C CB  . ASN A  1 118 ? -1.142  -47.741 8.338    1.00 68.13  ? 118 ASN A CB  1 
ATOM   1022  C CG  . ASN A  1 118 ? -0.156  -46.967 9.173    1.00 72.40  ? 118 ASN A CG  1 
ATOM   1023  O OD1 . ASN A  1 118 ? -0.138  -45.746 9.164    1.00 74.34  ? 118 ASN A OD1 1 
ATOM   1024  N ND2 . ASN A  1 118 ? 0.678   -47.684 9.904    1.00 73.50  ? 118 ASN A ND2 1 
ATOM   1025  N N   . LYS A  1 119 ? -3.760  -47.610 6.026    1.00 65.60  ? 119 LYS A N   1 
ATOM   1026  C CA  . LYS A  1 119 ? -4.173  -48.472 4.978    1.00 64.38  ? 119 LYS A CA  1 
ATOM   1027  C C   . LYS A  1 119 ? -4.796  -47.915 3.723    1.00 69.98  ? 119 LYS A C   1 
ATOM   1028  O O   . LYS A  1 119 ? -5.430  -46.883 3.734    1.00 70.23  ? 119 LYS A O   1 
ATOM   1029  C CB  . LYS A  1 119 ? -5.151  -49.430 5.557    1.00 58.51  ? 119 LYS A CB  1 
ATOM   1030  C CG  . LYS A  1 119 ? -4.704  -50.882 5.558    1.00 57.43  ? 119 LYS A CG  1 
ATOM   1031  C CD  . LYS A  1 119 ? -5.040  -51.535 6.886    1.00 56.28  ? 119 LYS A CD  1 
ATOM   1032  C CE  . LYS A  1 119 ? -5.332  -53.016 6.748    1.00 56.79  ? 119 LYS A CE  1 
ATOM   1033  N NZ  . LYS A  1 119 ? -4.377  -53.886 7.483    1.00 56.71  ? 119 LYS A NZ  1 
ATOM   1034  N N   . GLU A  1 120 ? -4.743  -48.698 2.671    1.00 74.25  ? 120 GLU A N   1 
ATOM   1035  C CA  . GLU A  1 120 ? -5.159  -48.255 1.357    1.00 76.48  ? 120 GLU A CA  1 
ATOM   1036  C C   . GLU A  1 120 ? -6.593  -48.194 1.063    1.00 73.55  ? 120 GLU A C   1 
ATOM   1037  O O   . GLU A  1 120 ? -7.146  -47.120 0.951    1.00 74.18  ? 120 GLU A O   1 
ATOM   1038  C CB  . GLU A  1 120 ? -4.574  -49.240 0.374    1.00 78.72  ? 120 GLU A CB  1 
ATOM   1039  N N   . LYS A  1 121 ? -7.164  -49.347 0.844    1.00 68.26  ? 121 LYS A N   1 
ATOM   1040  C CA  . LYS A  1 121 ? -8.544  -49.365 0.669    1.00 62.94  ? 121 LYS A CA  1 
ATOM   1041  C C   . LYS A  1 121 ? -8.895  -50.148 1.900    1.00 61.38  ? 121 LYS A C   1 
ATOM   1042  O O   . LYS A  1 121 ? -8.049  -50.808 2.458    1.00 65.77  ? 121 LYS A O   1 
ATOM   1043  C CB  . LYS A  1 121 ? -8.951  -50.125 -0.556   1.00 61.92  ? 121 LYS A CB  1 
ATOM   1044  N N   . LEU A  1 122 ? -10.135 -50.097 2.314    1.00 51.41  ? 122 LEU A N   1 
ATOM   1045  C CA  . LEU A  1 122 ? -10.471 -50.748 3.490    1.00 44.25  ? 122 LEU A CA  1 
ATOM   1046  C C   . LEU A  1 122 ? -11.566 -51.617 3.106    1.00 46.71  ? 122 LEU A C   1 
ATOM   1047  O O   . LEU A  1 122 ? -12.467 -51.192 2.453    1.00 50.79  ? 122 LEU A O   1 
ATOM   1048  C CB  . LEU A  1 122 ? -10.875 -49.734 4.509    1.00 42.59  ? 122 LEU A CB  1 
ATOM   1049  C CG  . LEU A  1 122 ? -9.994  -49.333 5.661    1.00 44.91  ? 122 LEU A CG  1 
ATOM   1050  C CD1 . LEU A  1 122 ? -8.530  -49.478 5.335    1.00 48.46  ? 122 LEU A CD1 1 
ATOM   1051  C CD2 . LEU A  1 122 ? -10.337 -47.894 6.003    1.00 42.02  ? 122 LEU A CD2 1 
ATOM   1052  N N   . ASN A  1 123 ? -11.505 -52.840 3.534    1.00 43.81  ? 123 ASN A N   1 
ATOM   1053  C CA  . ASN A  1 123 ? -12.539 -53.802 3.235    1.00 40.09  ? 123 ASN A CA  1 
ATOM   1054  C C   . ASN A  1 123 ? -13.694 -53.763 4.222    1.00 40.06  ? 123 ASN A C   1 
ATOM   1055  O O   . ASN A  1 123 ? -13.690 -52.990 5.137    1.00 41.01  ? 123 ASN A O   1 
ATOM   1056  C CB  . ASN A  1 123 ? -11.968 -55.195 3.136    1.00 38.50  ? 123 ASN A CB  1 
ATOM   1057  C CG  . ASN A  1 123 ? -11.422 -55.710 4.427    1.00 40.69  ? 123 ASN A CG  1 
ATOM   1058  O OD1 . ASN A  1 123 ? -11.873 -55.362 5.496    1.00 38.65  ? 123 ASN A OD1 1 
ATOM   1059  N ND2 . ASN A  1 123 ? -10.445 -56.577 4.320    1.00 40.44  ? 123 ASN A ND2 1 
ATOM   1060  N N   . ARG A  1 124 ? -14.658 -54.578 4.009    1.00 31.76  ? 124 ARG A N   1 
ATOM   1061  C CA  . ARG A  1 124 ? -15.854 -54.447 4.828    1.00 31.11  ? 124 ARG A CA  1 
ATOM   1062  C C   . ARG A  1 124 ? -15.537 -54.637 6.308    1.00 33.83  ? 124 ARG A C   1 
ATOM   1063  O O   . ARG A  1 124 ? -15.974 -53.850 7.154    1.00 33.34  ? 124 ARG A O   1 
ATOM   1064  C CB  . ARG A  1 124 ? -16.907 -55.445 4.377    1.00 32.70  ? 124 ARG A CB  1 
ATOM   1065  C CG  . ARG A  1 124 ? -18.041 -55.559 5.376    1.00 34.05  ? 124 ARG A CG  1 
ATOM   1066  C CD  . ARG A  1 124 ? -19.271 -56.187 4.758    1.00 40.69  ? 124 ARG A CD  1 
ATOM   1067  N NE  . ARG A  1 124 ? -20.435 -56.006 5.612    1.00 41.48  ? 124 ARG A NE  1 
ATOM   1068  C CZ  . ARG A  1 124 ? -20.652 -56.711 6.719    1.00 49.16  ? 124 ARG A CZ  1 
ATOM   1069  N NH1 . ARG A  1 124 ? -19.781 -57.641 7.088    1.00 53.10  ? 124 ARG A NH1 1 
ATOM   1070  N NH2 . ARG A  1 124 ? -21.731 -56.487 7.462    1.00 48.24  ? 124 ARG A NH2 1 
ATOM   1071  N N   . GLU A  1 125 ? -14.785 -55.686 6.636    1.00 37.94  ? 125 GLU A N   1 
ATOM   1072  C CA  . GLU A  1 125 ? -14.472 -55.975 8.030    1.00 39.17  ? 125 GLU A CA  1 
ATOM   1073  C C   . GLU A  1 125 ? -13.655 -54.849 8.650    1.00 33.21  ? 125 GLU A C   1 
ATOM   1074  O O   . GLU A  1 125 ? -13.819 -54.524 9.835    1.00 28.32  ? 125 GLU A O   1 
ATOM   1075  C CB  . GLU A  1 125 ? -13.724 -57.307 8.126    1.00 45.13  ? 125 GLU A CB  1 
ATOM   1076  C CG  . GLU A  1 125 ? -14.451 -58.534 7.544    1.00 54.79  ? 125 GLU A CG  1 
ATOM   1077  C CD  . GLU A  1 125 ? -14.646 -58.506 6.005    1.00 62.36  ? 125 GLU A CD  1 
ATOM   1078  O OE1 . GLU A  1 125 ? -15.776 -58.779 5.543    1.00 65.10  ? 125 GLU A OE1 1 
ATOM   1079  O OE2 . GLU A  1 125 ? -13.679 -58.209 5.257    1.00 62.84  ? 125 GLU A OE2 1 
ATOM   1080  N N   . GLU A  1 126 ? -12.760 -54.255 7.865    1.00 32.87  ? 126 GLU A N   1 
ATOM   1081  C CA  . GLU A  1 126 ? -11.946 -53.150 8.357    1.00 31.07  ? 126 GLU A CA  1 
ATOM   1082  C C   . GLU A  1 126 ? -12.780 -51.880 8.522    1.00 31.66  ? 126 GLU A C   1 
ATOM   1083  O O   . GLU A  1 126 ? -12.542 -51.092 9.444    1.00 30.43  ? 126 GLU A O   1 
ATOM   1084  C CB  . GLU A  1 126 ? -10.764 -52.916 7.399    1.00 31.17  ? 126 GLU A CB  1 
ATOM   1085  C CG  . GLU A  1 126 ? -9.701  -54.021 7.433    1.00 35.27  ? 126 GLU A CG  1 
ATOM   1086  C CD  . GLU A  1 126 ? -8.812  -54.071 6.187    1.00 45.38  ? 126 GLU A CD  1 
ATOM   1087  O OE1 . GLU A  1 126 ? -9.099  -53.368 5.190    1.00 47.01  ? 126 GLU A OE1 1 
ATOM   1088  O OE2 . GLU A  1 126 ? -7.825  -54.835 6.208    1.00 48.04  ? 126 GLU A OE2 1 
ATOM   1089  N N   . LEU A  1 127 ? -13.759 -51.657 7.636    1.00 28.63  ? 127 LEU A N   1 
ATOM   1090  C CA  . LEU A  1 127 ? -14.624 -50.493 7.804    1.00 28.90  ? 127 LEU A CA  1 
ATOM   1091  C C   . LEU A  1 127 ? -15.522 -50.651 9.021    1.00 26.97  ? 127 LEU A C   1 
ATOM   1092  O O   . LEU A  1 127 ? -15.845 -49.661 9.685    1.00 32.65  ? 127 LEU A O   1 
ATOM   1093  C CB  . LEU A  1 127 ? -15.476 -50.272 6.558    1.00 28.00  ? 127 LEU A CB  1 
ATOM   1094  C CG  . LEU A  1 127 ? -14.800 -49.641 5.336    1.00 29.01  ? 127 LEU A CG  1 
ATOM   1095  C CD1 . LEU A  1 127 ? -15.726 -49.744 4.151    1.00 31.83  ? 127 LEU A CD1 1 
ATOM   1096  C CD2 . LEU A  1 127 ? -14.453 -48.190 5.615    1.00 29.38  ? 127 LEU A CD2 1 
ATOM   1097  N N   . LEU A  1 128 ? -15.941 -51.883 9.311    1.00 26.37  ? 128 LEU A N   1 
ATOM   1098  C CA  . LEU A  1 128 ? -16.735 -52.142 10.510   1.00 26.78  ? 128 LEU A CA  1 
ATOM   1099  C C   . LEU A  1 128 ? -15.944 -51.819 11.764   1.00 27.76  ? 128 LEU A C   1 
ATOM   1100  O O   . LEU A  1 128 ? -16.504 -51.323 12.752   1.00 27.14  ? 128 LEU A O   1 
ATOM   1101  C CB  . LEU A  1 128 ? -17.179 -53.602 10.538   1.00 23.50  ? 128 LEU A CB  1 
ATOM   1102  C CG  . LEU A  1 128 ? -18.648 -53.884 10.242   1.00 28.37  ? 128 LEU A CG  1 
ATOM   1103  C CD1 . LEU A  1 128 ? -18.911 -55.406 10.166   1.00 27.13  ? 128 LEU A CD1 1 
ATOM   1104  C CD2 . LEU A  1 128 ? -19.484 -53.234 11.315   1.00 30.07  ? 128 LEU A CD2 1 
ATOM   1105  N N   . ASP A  1 129 ? -14.639 -52.110 11.752   1.00 29.86  ? 129 ASP A N   1 
ATOM   1106  C CA  . ASP A  1 129 ? -13.811 -51.771 12.907   1.00 30.16  ? 129 ASP A CA  1 
ATOM   1107  C C   . ASP A  1 129 ? -13.583 -50.277 12.993   1.00 30.41  ? 129 ASP A C   1 
ATOM   1108  O O   . ASP A  1 129 ? -13.534 -49.722 14.090   1.00 27.80  ? 129 ASP A O   1 
ATOM   1109  C CB  . ASP A  1 129 ? -12.472 -52.503 12.856   1.00 33.53  ? 129 ASP A CB  1 
ATOM   1110  C CG  . ASP A  1 129 ? -12.608 -53.956 13.200   1.00 31.64  ? 129 ASP A CG  1 
ATOM   1111  O OD1 . ASP A  1 129 ? -13.760 -54.379 13.410   1.00 31.40  ? 129 ASP A OD1 1 
ATOM   1112  O OD2 . ASP A  1 129 ? -11.585 -54.671 13.243   1.00 34.16  ? 129 ASP A OD2 1 
ATOM   1113  N N   . LEU A  1 130 ? -13.449 -49.595 11.852   1.00 33.70  ? 130 LEU A N   1 
ATOM   1114  C CA  . LEU A  1 130 ? -13.335 -48.141 11.922   1.00 31.04  ? 130 LEU A CA  1 
ATOM   1115  C C   . LEU A  1 130 ? -14.624 -47.531 12.453   1.00 30.01  ? 130 LEU A C   1 
ATOM   1116  O O   . LEU A  1 130 ? -14.590 -46.588 13.254   1.00 27.71  ? 130 LEU A O   1 
ATOM   1117  C CB  . LEU A  1 130 ? -12.975 -47.556 10.554   1.00 25.02  ? 130 LEU A CB  1 
ATOM   1118  C CG  . LEU A  1 130 ? -12.551 -46.087 10.527   1.00 26.30  ? 130 LEU A CG  1 
ATOM   1119  C CD1 . LEU A  1 130 ? -11.338 -45.895 11.415   1.00 31.55  ? 130 LEU A CD1 1 
ATOM   1120  C CD2 . LEU A  1 130 ? -12.233 -45.625 9.101    1.00 32.46  ? 130 LEU A CD2 1 
ATOM   1121  N N   . GLN A  1 131 ? -15.774 -48.065 12.029   1.00 24.10  ? 131 GLN A N   1 
ATOM   1122  C CA  . GLN A  1 131 ? -17.046 -47.553 12.528   1.00 24.81  ? 131 GLN A CA  1 
ATOM   1123  C C   . GLN A  1 131 ? -17.167 -47.760 14.035   1.00 20.89  ? 131 GLN A C   1 
ATOM   1124  O O   . GLN A  1 131 ? -17.490 -46.830 14.776   1.00 28.35  ? 131 GLN A O   1 
ATOM   1125  C CB  . GLN A  1 131 ? -18.215 -48.233 11.829   1.00 22.40  ? 131 GLN A CB  1 
ATOM   1126  C CG  . GLN A  1 131 ? -18.433 -47.783 10.376   1.00 25.07  ? 131 GLN A CG  1 
ATOM   1127  C CD  . GLN A  1 131 ? -19.491 -48.607 9.697    1.00 27.94  ? 131 GLN A CD  1 
ATOM   1128  O OE1 . GLN A  1 131 ? -19.604 -49.810 9.943    1.00 28.95  ? 131 GLN A OE1 1 
ATOM   1129  N NE2 . GLN A  1 131 ? -20.292 -47.966 8.845    1.00 32.48  ? 131 GLN A NE2 1 
ATOM   1130  N N   . THR A  1 132 ? -16.930 -48.984 14.492   1.00 19.91  ? 132 THR A N   1 
ATOM   1131  C CA  . THR A  1 132 ? -17.238 -49.351 15.872   1.00 18.77  ? 132 THR A CA  1 
ATOM   1132  C C   . THR A  1 132 ? -16.193 -48.823 16.837   1.00 23.96  ? 132 THR A C   1 
ATOM   1133  O O   . THR A  1 132 ? -16.520 -48.496 17.988   1.00 23.45  ? 132 THR A O   1 
ATOM   1134  C CB  . THR A  1 132 ? -17.325 -50.870 15.996   1.00 19.41  ? 132 THR A CB  1 
ATOM   1135  O OG1 . THR A  1 132 ? -18.137 -51.400 14.939   1.00 26.43  ? 132 THR A OG1 1 
ATOM   1136  C CG2 . THR A  1 132 ? -17.918 -51.270 17.342   1.00 20.11  ? 132 THR A CG2 1 
ATOM   1137  N N   . LEU A  1 133 ? -14.930 -48.764 16.398   1.00 20.35  ? 133 LEU A N   1 
ATOM   1138  C CA  . LEU A  1 133 ? -13.902 -48.165 17.244   1.00 24.08  ? 133 LEU A CA  1 
ATOM   1139  C C   . LEU A  1 133 ? -14.120 -46.659 17.395   1.00 25.47  ? 133 LEU A C   1 
ATOM   1140  O O   . LEU A  1 133 ? -13.876 -46.096 18.479   1.00 21.25  ? 133 LEU A O   1 
ATOM   1141  C CB  . LEU A  1 133 ? -12.515 -48.490 16.687   1.00 23.18  ? 133 LEU A CB  1 
ATOM   1142  C CG  . LEU A  1 133 ? -12.119 -49.953 16.958   1.00 28.05  ? 133 LEU A CG  1 
ATOM   1143  C CD1 . LEU A  1 133 ? -10.871 -50.385 16.184   1.00 26.32  ? 133 LEU A CD1 1 
ATOM   1144  C CD2 . LEU A  1 133 ? -11.932 -50.215 18.456   1.00 24.93  ? 133 LEU A CD2 1 
ATOM   1145  N N   . ASN A  1 134 ? -14.626 -45.989 16.355   1.00 21.64  ? 134 ASN A N   1 
ATOM   1146  C CA  . ASN A  1 134 ? -14.985 -44.588 16.541   1.00 21.59  ? 134 ASN A CA  1 
ATOM   1147  C C   . ASN A  1 134 ? -16.075 -44.439 17.598   1.00 24.12  ? 134 ASN A C   1 
ATOM   1148  O O   . ASN A  1 134 ? -15.968 -43.595 18.490   1.00 32.06  ? 134 ASN A O   1 
ATOM   1149  C CB  . ASN A  1 134 ? -15.401 -43.953 15.217   1.00 18.19  ? 134 ASN A CB  1 
ATOM   1150  C CG  . ASN A  1 134 ? -14.217 -43.370 14.489   1.00 21.75  ? 134 ASN A CG  1 
ATOM   1151  O OD1 . ASN A  1 134 ? -13.760 -42.276 14.811   1.00 20.54  ? 134 ASN A OD1 1 
ATOM   1152  N ND2 . ASN A  1 134 ? -13.690 -44.113 13.520   1.00 27.75  ? 134 ASN A ND2 1 
ATOM   1153  N N   . LEU A  1 135 ? -17.121 -45.262 17.520   1.00 23.74  ? 135 LEU A N   1 
ATOM   1154  C CA  . LEU A  1 135 ? -18.134 -45.327 18.574   1.00 25.34  ? 135 LEU A CA  1 
ATOM   1155  C C   . LEU A  1 135 ? -17.517 -45.559 19.955   1.00 23.08  ? 135 LEU A C   1 
ATOM   1156  O O   . LEU A  1 135 ? -17.743 -44.786 20.898   1.00 22.50  ? 135 LEU A O   1 
ATOM   1157  C CB  . LEU A  1 135 ? -19.107 -46.455 18.261   1.00 31.51  ? 135 LEU A CB  1 
ATOM   1158  C CG  . LEU A  1 135 ? -20.491 -46.155 17.715   1.00 34.48  ? 135 LEU A CG  1 
ATOM   1159  C CD1 . LEU A  1 135 ? -21.305 -47.450 17.707   1.00 33.57  ? 135 LEU A CD1 1 
ATOM   1160  C CD2 . LEU A  1 135 ? -21.190 -45.047 18.491   1.00 30.37  ? 135 LEU A CD2 1 
ATOM   1161  N N   . LEU A  1 136 ? -16.760 -46.655 20.096   1.00 21.47  ? 136 LEU A N   1 
ATOM   1162  C CA  . LEU A  1 136 ? -16.287 -47.088 21.412   1.00 24.09  ? 136 LEU A CA  1 
ATOM   1163  C C   . LEU A  1 136 ? -15.261 -46.131 21.988   1.00 26.99  ? 136 LEU A C   1 
ATOM   1164  O O   . LEU A  1 136 ? -15.090 -46.077 23.210   1.00 26.55  ? 136 LEU A O   1 
ATOM   1165  C CB  . LEU A  1 136 ? -15.682 -48.497 21.337   1.00 21.14  ? 136 LEU A CB  1 
ATOM   1166  C CG  . LEU A  1 136 ? -16.665 -49.644 21.211   1.00 26.79  ? 136 LEU A CG  1 
ATOM   1167  C CD1 . LEU A  1 136 ? -15.966 -50.921 20.761   1.00 29.58  ? 136 LEU A CD1 1 
ATOM   1168  C CD2 . LEU A  1 136 ? -17.396 -49.843 22.563   1.00 25.71  ? 136 LEU A CD2 1 
ATOM   1169  N N   . ALA A  1 137 ? -14.540 -45.402 21.133   1.00 27.46  ? 137 ALA A N   1 
ATOM   1170  C CA  . ALA A  1 137 ? -13.630 -44.371 21.624   1.00 28.97  ? 137 ALA A CA  1 
ATOM   1171  C C   . ALA A  1 137 ? -14.331 -43.363 22.530   1.00 26.96  ? 137 ALA A C   1 
ATOM   1172  O O   . ALA A  1 137 ? -13.709 -42.807 23.445   1.00 23.66  ? 137 ALA A O   1 
ATOM   1173  C CB  . ALA A  1 137 ? -12.980 -43.629 20.457   1.00 24.15  ? 137 ALA A CB  1 
ATOM   1174  N N   . TRP A  1 138 ? -15.614 -43.112 22.292   1.00 24.89  ? 138 TRP A N   1 
ATOM   1175  C CA  . TRP A  1 138 ? -16.359 -42.077 22.993   1.00 23.48  ? 138 TRP A CA  1 
ATOM   1176  C C   . TRP A  1 138 ? -17.166 -42.640 24.149   1.00 25.94  ? 138 TRP A C   1 
ATOM   1177  O O   . TRP A  1 138 ? -18.036 -41.947 24.683   1.00 23.41  ? 138 TRP A O   1 
ATOM   1178  C CB  . TRP A  1 138 ? -17.251 -41.338 22.000   1.00 17.70  ? 138 TRP A CB  1 
ATOM   1179  C CG  . TRP A  1 138 ? -16.387 -40.559 21.080   1.00 24.04  ? 138 TRP A CG  1 
ATOM   1180  C CD1 . TRP A  1 138 ? -15.838 -40.992 19.904   1.00 21.57  ? 138 TRP A CD1 1 
ATOM   1181  C CD2 . TRP A  1 138 ? -15.925 -39.216 21.272   1.00 25.10  ? 138 TRP A CD2 1 
ATOM   1182  N NE1 . TRP A  1 138 ? -15.056 -40.000 19.356   1.00 19.86  ? 138 TRP A NE1 1 
ATOM   1183  C CE2 . TRP A  1 138 ? -15.095 -38.898 20.167   1.00 23.62  ? 138 TRP A CE2 1 
ATOM   1184  C CE3 . TRP A  1 138 ? -16.120 -38.256 22.271   1.00 24.45  ? 138 TRP A CE3 1 
ATOM   1185  C CZ2 . TRP A  1 138 ? -14.472 -37.651 20.030   1.00 19.74  ? 138 TRP A CZ2 1 
ATOM   1186  C CZ3 . TRP A  1 138 ? -15.508 -37.008 22.133   1.00 22.29  ? 138 TRP A CZ3 1 
ATOM   1187  C CH2 . TRP A  1 138 ? -14.688 -36.724 21.016   1.00 27.98  ? 138 TRP A CH2 1 
ATOM   1188  N N   . CYS A  1 139 ? -16.878 -43.879 24.544   1.00 19.59  ? 139 CYS A N   1 
ATOM   1189  C CA  . CYS A  1 139 ? -17.644 -44.564 25.573   1.00 23.00  ? 139 CYS A CA  1 
ATOM   1190  C C   . CYS A  1 139 ? -17.434 -43.929 26.944   1.00 21.59  ? 139 CYS A C   1 
ATOM   1191  O O   . CYS A  1 139 ? -16.298 -43.650 27.341   1.00 21.16  ? 139 CYS A O   1 
ATOM   1192  C CB  . CYS A  1 139 ? -17.228 -46.034 25.611   1.00 26.73  ? 139 CYS A CB  1 
ATOM   1193  S SG  . CYS A  1 139 ? -18.271 -47.024 26.661   1.00 26.59  ? 139 CYS A SG  1 
ATOM   1194  N N   . GLY A  1 140 ? -18.545 -43.723 27.686   1.00 21.30  ? 140 GLY A N   1 
ATOM   1195  C CA  . GLY A  1 140 ? -18.467 -43.068 28.978   1.00 23.28  ? 140 GLY A CA  1 
ATOM   1196  C C   . GLY A  1 140 ? -18.086 -44.019 30.102   1.00 23.45  ? 140 GLY A C   1 
ATOM   1197  O O   . GLY A  1 140 ? -17.971 -45.231 29.921   1.00 27.72  ? 140 GLY A O   1 
ATOM   1198  N N   . ARG A  1 141 ? -17.876 -43.429 31.279   1.00 18.16  ? 141 ARG A N   1 
ATOM   1199  C CA  . ARG A  1 141 ? -17.522 -44.199 32.471   1.00 21.12  ? 141 ARG A CA  1 
ATOM   1200  C C   . ARG A  1 141 ? -18.482 -45.365 32.693   1.00 23.97  ? 141 ARG A C   1 
ATOM   1201  O O   . ARG A  1 141 ? -18.051 -46.516 32.847   1.00 26.22  ? 141 ARG A O   1 
ATOM   1202  C CB  . ARG A  1 141 ? -17.492 -43.266 33.688   1.00 18.32  ? 141 ARG A CB  1 
ATOM   1203  C CG  . ARG A  1 141 ? -17.137 -43.986 34.975   1.00 19.31  ? 141 ARG A CG  1 
ATOM   1204  C CD  . ARG A  1 141 ? -16.828 -43.048 36.099   1.00 21.61  ? 141 ARG A CD  1 
ATOM   1205  N NE  . ARG A  1 141 ? -16.932 -43.687 37.402   1.00 29.60  ? 141 ARG A NE  1 
ATOM   1206  C CZ  . ARG A  1 141 ? -18.030 -43.727 38.155   1.00 33.62  ? 141 ARG A CZ  1 
ATOM   1207  N NH1 . ARG A  1 141 ? -19.160 -43.160 37.755   1.00 26.57  ? 141 ARG A NH1 1 
ATOM   1208  N NH2 . ARG A  1 141 ? -17.983 -44.345 39.329   1.00 38.24  ? 141 ARG A NH2 1 
ATOM   1209  N N   . THR A  1 142 ? -19.792 -45.087 32.701   1.00 25.52  ? 142 THR A N   1 
ATOM   1210  C CA  . THR A  1 142 ? -20.798 -46.109 33.026   1.00 26.38  ? 142 THR A CA  1 
ATOM   1211  C C   . THR A  1 142 ? -20.702 -47.317 32.089   1.00 25.79  ? 142 THR A C   1 
ATOM   1212  O O   . THR A  1 142 ? -20.657 -48.469 32.539   1.00 28.74  ? 142 THR A O   1 
ATOM   1213  C CB  . THR A  1 142 ? -22.206 -45.482 32.965   1.00 26.01  ? 142 THR A CB  1 
ATOM   1214  O OG1 . THR A  1 142 ? -22.326 -44.407 33.914   1.00 24.83  ? 142 THR A OG1 1 
ATOM   1215  C CG2 . THR A  1 142 ? -23.289 -46.496 33.242   1.00 21.70  ? 142 THR A CG2 1 
ATOM   1216  N N   . LEU A  1 143 ? -20.631 -47.082 30.774   1.00 25.20  ? 143 LEU A N   1 
ATOM   1217  C CA  . LEU A  1 143 ? -20.654 -48.211 29.851   1.00 24.26  ? 143 LEU A CA  1 
ATOM   1218  C C   . LEU A  1 143 ? -19.285 -48.831 29.645   1.00 30.22  ? 143 LEU A C   1 
ATOM   1219  O O   . LEU A  1 143 ? -19.203 -49.962 29.155   1.00 28.61  ? 143 LEU A O   1 
ATOM   1220  C CB  . LEU A  1 143 ? -21.217 -47.799 28.497   1.00 21.01  ? 143 LEU A CB  1 
ATOM   1221  C CG  . LEU A  1 143 ? -22.715 -47.489 28.490   1.00 26.80  ? 143 LEU A CG  1 
ATOM   1222  C CD1 . LEU A  1 143 ? -23.209 -47.179 27.084   1.00 25.55  ? 143 LEU A CD1 1 
ATOM   1223  C CD2 . LEU A  1 143 ? -23.509 -48.630 29.084   1.00 25.01  ? 143 LEU A CD2 1 
ATOM   1224  N N   . ARG A  1 144 ? -18.208 -48.125 29.992   1.00 29.95  ? 144 ARG A N   1 
ATOM   1225  C CA  . ARG A  1 144 ? -16.903 -48.770 29.947   1.00 32.66  ? 144 ARG A CA  1 
ATOM   1226  C C   . ARG A  1 144 ? -16.826 -50.003 30.843   1.00 35.76  ? 144 ARG A C   1 
ATOM   1227  O O   . ARG A  1 144 ? -15.935 -50.837 30.644   1.00 41.12  ? 144 ARG A O   1 
ATOM   1228  C CB  . ARG A  1 144 ? -15.810 -47.778 30.319   1.00 30.97  ? 144 ARG A CB  1 
ATOM   1229  C CG  . ARG A  1 144 ? -15.231 -47.070 29.109   1.00 32.74  ? 144 ARG A CG  1 
ATOM   1230  C CD  . ARG A  1 144 ? -14.386 -45.891 29.528   1.00 32.87  ? 144 ARG A CD  1 
ATOM   1231  N NE  . ARG A  1 144 ? -13.871 -45.101 28.408   1.00 33.31  ? 144 ARG A NE  1 
ATOM   1232  C CZ  . ARG A  1 144 ? -12.658 -45.234 27.877   1.00 36.25  ? 144 ARG A CZ  1 
ATOM   1233  N NH1 . ARG A  1 144 ? -11.824 -46.163 28.333   1.00 43.10  ? 144 ARG A NH1 1 
ATOM   1234  N NH2 . ARG A  1 144 ? -12.280 -44.447 26.872   1.00 29.73  ? 144 ARG A NH2 1 
ATOM   1235  N N   . LYS A  1 145 ? -17.740 -50.152 31.806   1.00 37.31  ? 145 LYS A N   1 
ATOM   1236  C CA  . LYS A  1 145 ? -17.837 -51.382 32.588   1.00 39.30  ? 145 LYS A CA  1 
ATOM   1237  C C   . LYS A  1 145 ? -18.753 -52.415 31.943   1.00 37.21  ? 145 LYS A C   1 
ATOM   1238  O O   . LYS A  1 145 ? -18.356 -53.570 31.781   1.00 41.94  ? 145 LYS A O   1 
ATOM   1239  C CB  . LYS A  1 145 ? -18.328 -51.075 33.998   1.00 46.90  ? 145 LYS A CB  1 
ATOM   1240  C CG  . LYS A  1 145 ? -17.604 -49.947 34.657   1.00 52.64  ? 145 LYS A CG  1 
ATOM   1241  C CD  . LYS A  1 145 ? -18.587 -49.117 35.457   1.00 58.77  ? 145 LYS A CD  1 
ATOM   1242  C CE  . LYS A  1 145 ? -17.876 -48.110 36.351   1.00 60.68  ? 145 LYS A CE  1 
ATOM   1243  N NZ  . LYS A  1 145 ? -18.718 -46.920 36.633   1.00 59.92  ? 145 LYS A NZ  1 
ATOM   1244  N N   . ASP A  1 146 ? -19.977 -52.017 31.574   1.00 35.93  ? 146 ASP A N   1 
ATOM   1245  C CA  . ASP A  1 146 ? -20.895 -52.938 30.905   1.00 40.14  ? 146 ASP A CA  1 
ATOM   1246  C C   . ASP A  1 146 ? -20.291 -53.505 29.616   1.00 43.36  ? 146 ASP A C   1 
ATOM   1247  O O   . ASP A  1 146 ? -20.427 -54.700 29.331   1.00 45.22  ? 146 ASP A O   1 
ATOM   1248  C CB  . ASP A  1 146 ? -22.218 -52.226 30.596   1.00 48.41  ? 146 ASP A CB  1 
ATOM   1249  C CG  . ASP A  1 146 ? -22.939 -51.716 31.847   1.00 53.95  ? 146 ASP A CG  1 
ATOM   1250  O OD1 . ASP A  1 146 ? -22.292 -51.537 32.907   1.00 53.91  ? 146 ASP A OD1 1 
ATOM   1251  O OD2 . ASP A  1 146 ? -24.165 -51.473 31.755   1.00 54.90  ? 146 ASP A OD2 1 
ATOM   1252  N N   . LEU A  1 147 ? -19.641 -52.661 28.807   1.00 35.47  ? 147 LEU A N   1 
ATOM   1253  C CA  . LEU A  1 147 ? -19.098 -53.091 27.525   1.00 33.24  ? 147 LEU A CA  1 
ATOM   1254  C C   . LEU A  1 147 ? -17.622 -53.472 27.611   1.00 31.97  ? 147 LEU A C   1 
ATOM   1255  O O   . LEU A  1 147 ? -16.932 -53.471 26.586   1.00 28.65  ? 147 LEU A O   1 
ATOM   1256  C CB  . LEU A  1 147 ? -19.293 -51.993 26.466   1.00 27.92  ? 147 LEU A CB  1 
ATOM   1257  C CG  . LEU A  1 147 ? -20.650 -51.283 26.430   1.00 32.14  ? 147 LEU A CG  1 
ATOM   1258  C CD1 . LEU A  1 147 ? -20.670 -50.146 25.418   1.00 30.83  ? 147 LEU A CD1 1 
ATOM   1259  C CD2 . LEU A  1 147 ? -21.770 -52.270 26.144   1.00 37.72  ? 147 LEU A CD2 1 
ATOM   1260  N N   . LYS A  1 148 ? -17.133 -53.814 28.808   1.00 34.21  ? 148 LYS A N   1 
ATOM   1261  C CA  . LYS A  1 148 ? -15.700 -54.019 29.010   1.00 35.25  ? 148 LYS A CA  1 
ATOM   1262  C C   . LYS A  1 148 ? -15.130 -55.078 28.063   1.00 36.35  ? 148 LYS A C   1 
ATOM   1263  O O   . LYS A  1 148 ? -14.009 -54.928 27.556   1.00 36.40  ? 148 LYS A O   1 
ATOM   1264  C CB  . LYS A  1 148 ? -15.438 -54.399 30.471   1.00 38.28  ? 148 LYS A CB  1 
ATOM   1265  C CG  . LYS A  1 148 ? -14.191 -55.250 30.689   1.00 43.98  ? 148 LYS A CG  1 
ATOM   1266  C CD  . LYS A  1 148 ? -13.678 -55.177 32.139   1.00 50.54  ? 148 LYS A CD  1 
ATOM   1267  C CE  . LYS A  1 148 ? -12.751 -56.360 32.483   1.00 54.63  ? 148 LYS A CE  1 
ATOM   1268  N NZ  . LYS A  1 148 ? -11.565 -56.491 31.570   1.00 55.03  ? 148 LYS A NZ  1 
ATOM   1269  N N   . ASP A  1 149 ? -15.889 -56.146 27.796   1.00 32.92  ? 149 ASP A N   1 
ATOM   1270  C CA  . ASP A  1 149 ? -15.385 -57.199 26.919   1.00 39.54  ? 149 ASP A CA  1 
ATOM   1271  C C   . ASP A  1 149 ? -15.280 -56.722 25.467   1.00 35.76  ? 149 ASP A C   1 
ATOM   1272  O O   . ASP A  1 149 ? -14.350 -57.111 24.751   1.00 34.04  ? 149 ASP A O   1 
ATOM   1273  C CB  . ASP A  1 149 ? -16.275 -58.444 27.004   1.00 42.85  ? 149 ASP A CB  1 
ATOM   1274  C CG  . ASP A  1 149 ? -16.392 -59.007 28.425   1.00 54.49  ? 149 ASP A CG  1 
ATOM   1275  O OD1 . ASP A  1 149 ? -15.407 -58.922 29.201   1.00 65.70  ? 149 ASP A OD1 1 
ATOM   1276  O OD2 . ASP A  1 149 ? -17.475 -59.556 28.746   1.00 54.21  ? 149 ASP A OD2 1 
ATOM   1277  N N   . LEU A  1 150 ? -16.219 -55.885 25.012   1.00 28.61  ? 150 LEU A N   1 
ATOM   1278  C CA  . LEU A  1 150 ? -16.150 -55.391 23.635   1.00 30.78  ? 150 LEU A CA  1 
ATOM   1279  C C   . LEU A  1 150 ? -15.007 -54.398 23.460   1.00 34.00  ? 150 LEU A C   1 
ATOM   1280  O O   . LEU A  1 150 ? -14.351 -54.382 22.414   1.00 31.95  ? 150 LEU A O   1 
ATOM   1281  C CB  . LEU A  1 150 ? -17.473 -54.743 23.227   1.00 30.72  ? 150 LEU A CB  1 
ATOM   1282  C CG  . LEU A  1 150 ? -18.683 -55.656 23.092   1.00 33.24  ? 150 LEU A CG  1 
ATOM   1283  C CD1 . LEU A  1 150 ? -19.877 -54.892 22.515   1.00 33.86  ? 150 LEU A CD1 1 
ATOM   1284  C CD2 . LEU A  1 150 ? -18.340 -56.878 22.228   1.00 32.98  ? 150 LEU A CD2 1 
ATOM   1285  N N   . LEU A  1 151 ? -14.764 -53.555 24.469   1.00 35.92  ? 151 LEU A N   1 
ATOM   1286  C CA  . LEU A  1 151 ? -13.652 -52.610 24.418   1.00 36.77  ? 151 LEU A CA  1 
ATOM   1287  C C   . LEU A  1 151 ? -12.307 -53.328 24.326   1.00 41.56  ? 151 LEU A C   1 
ATOM   1288  O O   . LEU A  1 151 ? -11.448 -52.955 23.515   1.00 41.49  ? 151 LEU A O   1 
ATOM   1289  C CB  . LEU A  1 151 ? -13.682 -51.707 25.652   1.00 34.37  ? 151 LEU A CB  1 
ATOM   1290  C CG  . LEU A  1 151 ? -14.629 -50.517 25.639   1.00 37.19  ? 151 LEU A CG  1 
ATOM   1291  C CD1 . LEU A  1 151 ? -14.761 -49.986 27.056   1.00 42.69  ? 151 LEU A CD1 1 
ATOM   1292  C CD2 . LEU A  1 151 ? -14.140 -49.424 24.703   1.00 29.89  ? 151 LEU A CD2 1 
ATOM   1293  N N   . ASN A  1 152 ? -12.092 -54.342 25.177   1.00 45.40  ? 152 ASN A N   1 
ATOM   1294  C CA  . ASN A  1 152 ? -10.826 -55.087 25.164   1.00 45.99  ? 152 ASN A CA  1 
ATOM   1295  C C   . ASN A  1 152 ? -10.630 -55.863 23.872   1.00 39.17  ? 152 ASN A C   1 
ATOM   1296  O O   . ASN A  1 152 ? -9.491  -56.163 23.493   1.00 38.75  ? 152 ASN A O   1 
ATOM   1297  C CB  . ASN A  1 152 ? -10.753 -56.064 26.337   1.00 48.69  ? 152 ASN A CB  1 
ATOM   1298  C CG  . ASN A  1 152 ? -10.628 -55.370 27.667   1.00 57.56  ? 152 ASN A CG  1 
ATOM   1299  O OD1 . ASN A  1 152 ? -10.941 -55.950 28.711   1.00 59.86  ? 152 ASN A OD1 1 
ATOM   1300  N ND2 . ASN A  1 152 ? -10.183 -54.114 27.644   1.00 58.82  ? 152 ASN A ND2 1 
ATOM   1301  N N   . LYS A  1 153 ? -11.724 -56.242 23.218   1.00 34.06  ? 153 LYS A N   1 
ATOM   1302  C CA  . LYS A  1 153 ? -11.640 -56.866 21.909   1.00 34.00  ? 153 LYS A CA  1 
ATOM   1303  C C   . LYS A  1 153 ? -10.756 -56.055 20.968   1.00 37.43  ? 153 LYS A C   1 
ATOM   1304  O O   . LYS A  1 153 ? -9.820  -56.588 20.361   1.00 40.83  ? 153 LYS A O   1 
ATOM   1305  C CB  . LYS A  1 153 ? -13.057 -57.017 21.356   1.00 37.35  ? 153 LYS A CB  1 
ATOM   1306  C CG  . LYS A  1 153 ? -13.141 -57.671 20.040   1.00 42.08  ? 153 LYS A CG  1 
ATOM   1307  C CD  . LYS A  1 153 ? -14.578 -57.813 19.600   1.00 41.01  ? 153 LYS A CD  1 
ATOM   1308  C CE  . LYS A  1 153 ? -14.647 -58.795 18.472   1.00 38.45  ? 153 LYS A CE  1 
ATOM   1309  N NZ  . LYS A  1 153 ? -16.042 -59.227 18.195   1.00 46.58  ? 153 LYS A NZ  1 
ATOM   1310  N N   . GLY A  1 154 ? -11.054 -54.758 20.825   1.00 37.57  ? 154 GLY A N   1 
ATOM   1311  C CA  . GLY A  1 154 ? -10.245 -53.819 20.074   1.00 35.80  ? 154 GLY A CA  1 
ATOM   1312  C C   . GLY A  1 154 ? -10.243 -53.980 18.566   1.00 37.09  ? 154 GLY A C   1 
ATOM   1313  O O   . GLY A  1 154 ? -9.669  -53.125 17.880   1.00 31.32  ? 154 GLY A O   1 
ATOM   1314  N N   . ARG A  1 155 ? -10.855 -55.034 18.022   1.00 36.58  ? 155 ARG A N   1 
ATOM   1315  C CA  . ARG A  1 155 ? -10.798 -55.314 16.585   1.00 34.57  ? 155 ARG A CA  1 
ATOM   1316  C C   . ARG A  1 155 ? -11.855 -56.354 16.249   1.00 31.60  ? 155 ARG A C   1 
ATOM   1317  O O   . ARG A  1 155 ? -12.440 -56.974 17.140   1.00 33.53  ? 155 ARG A O   1 
ATOM   1318  C CB  . ARG A  1 155 ? -9.413  -55.813 16.181   1.00 37.05  ? 155 ARG A CB  1 
ATOM   1319  C CG  . ARG A  1 155 ? -8.933  -56.945 17.100   1.00 40.48  ? 155 ARG A CG  1 
ATOM   1320  C CD  . ARG A  1 155 ? -7.593  -57.499 16.682   1.00 46.40  ? 155 ARG A CD  1 
ATOM   1321  N NE  . ARG A  1 155 ? -6.527  -56.510 16.800   1.00 49.16  ? 155 ARG A NE  1 
ATOM   1322  C CZ  . ARG A  1 155 ? -5.892  -55.980 15.758   1.00 53.06  ? 155 ARG A CZ  1 
ATOM   1323  N NH1 . ARG A  1 155 ? -4.927  -55.088 15.948   1.00 55.37  ? 155 ARG A NH1 1 
ATOM   1324  N NH2 . ARG A  1 155 ? -6.230  -56.337 14.524   1.00 51.28  ? 155 ARG A NH2 1 
ATOM   1325  N N   . ASN A  1 156 ? -12.092 -56.535 14.944   1.00 31.19  ? 156 ASN A N   1 
ATOM   1326  C CA  . ASN A  1 156 ? -12.925 -57.621 14.421   1.00 36.87  ? 156 ASN A CA  1 
ATOM   1327  C C   . ASN A  1 156 ? -14.345 -57.537 14.974   1.00 37.32  ? 156 ASN A C   1 
ATOM   1328  O O   . ASN A  1 156 ? -14.935 -58.531 15.411   1.00 35.95  ? 156 ASN A O   1 
ATOM   1329  C CB  . ASN A  1 156 ? -12.308 -58.990 14.719   1.00 41.51  ? 156 ASN A CB  1 
ATOM   1330  C CG  . ASN A  1 156 ? -10.891 -59.112 14.202   1.00 46.76  ? 156 ASN A CG  1 
ATOM   1331  O OD1 . ASN A  1 156 ? -9.955  -59.330 14.975   1.00 50.13  ? 156 ASN A OD1 1 
ATOM   1332  N ND2 . ASN A  1 156 ? -10.724 -58.984 12.893   1.00 46.92  ? 156 ASN A ND2 1 
ATOM   1333  N N   . TYR A  1 157 ? -14.897 -56.332 14.942   1.00 26.29  ? 157 TYR A N   1 
ATOM   1334  C CA  . TYR A  1 157 ? -16.263 -56.124 15.391   1.00 26.71  ? 157 TYR A CA  1 
ATOM   1335  C C   . TYR A  1 157 ? -17.255 -56.572 14.330   1.00 27.30  ? 157 TYR A C   1 
ATOM   1336  O O   . TYR A  1 157 ? -16.968 -56.564 13.128   1.00 24.22  ? 157 TYR A O   1 
ATOM   1337  C CB  . TYR A  1 157 ? -16.487 -54.648 15.730   1.00 26.99  ? 157 TYR A CB  1 
ATOM   1338  C CG  . TYR A  1 157 ? -15.703 -54.257 16.939   1.00 25.65  ? 157 TYR A CG  1 
ATOM   1339  C CD1 . TYR A  1 157 ? -16.147 -54.604 18.216   1.00 23.74  ? 157 TYR A CD1 1 
ATOM   1340  C CD2 . TYR A  1 157 ? -14.507 -53.577 16.823   1.00 22.24  ? 157 TYR A CD2 1 
ATOM   1341  C CE1 . TYR A  1 157 ? -15.423 -54.281 19.339   1.00 25.87  ? 157 TYR A CE1 1 
ATOM   1342  C CE2 . TYR A  1 157 ? -13.778 -53.237 17.952   1.00 21.07  ? 157 TYR A CE2 1 
ATOM   1343  C CZ  . TYR A  1 157 ? -14.249 -53.587 19.205   1.00 24.42  ? 157 TYR A CZ  1 
ATOM   1344  O OH  . TYR A  1 157 ? -13.530 -53.261 20.330   1.00 28.30  ? 157 TYR A OH  1 
ATOM   1345  N N   . THR A  1 158 ? -18.435 -56.969 14.784   1.00 26.33  ? 158 THR A N   1 
ATOM   1346  C CA  . THR A  1 158 ? -19.511 -57.308 13.872   1.00 25.49  ? 158 THR A CA  1 
ATOM   1347  C C   . THR A  1 158 ? -20.575 -56.223 13.902   1.00 25.25  ? 158 THR A C   1 
ATOM   1348  O O   . THR A  1 158 ? -20.638 -55.412 14.820   1.00 27.07  ? 158 THR A O   1 
ATOM   1349  C CB  . THR A  1 158 ? -20.112 -58.670 14.200   1.00 24.18  ? 158 THR A CB  1 
ATOM   1350  O OG1 . THR A  1 158 ? -20.726 -58.650 15.500   1.00 27.29  ? 158 THR A OG1 1 
ATOM   1351  C CG2 . THR A  1 158 ? -19.016 -59.690 14.190   1.00 26.97  ? 158 THR A CG2 1 
ATOM   1352  N N   . GLN A  1 159 ? -21.401 -56.206 12.849   1.00 24.96  ? 159 GLN A N   1 
ATOM   1353  C CA  . GLN A  1 159 ? -22.503 -55.254 12.783   1.00 24.74  ? 159 GLN A CA  1 
ATOM   1354  C C   . GLN A  1 159 ? -23.425 -55.389 13.996   1.00 25.79  ? 159 GLN A C   1 
ATOM   1355  O O   . GLN A  1 159 ? -23.920 -54.387 14.521   1.00 29.02  ? 159 GLN A O   1 
ATOM   1356  C CB  . GLN A  1 159 ? -23.268 -55.460 11.472   1.00 25.33  ? 159 GLN A CB  1 
ATOM   1357  C CG  . GLN A  1 159 ? -24.498 -54.594 11.292   1.00 31.26  ? 159 GLN A CG  1 
ATOM   1358  C CD  . GLN A  1 159 ? -24.166 -53.156 10.965   1.00 31.24  ? 159 GLN A CD  1 
ATOM   1359  O OE1 . GLN A  1 159 ? -23.073 -52.849 10.502   1.00 34.88  ? 159 GLN A OE1 1 
ATOM   1360  N NE2 . GLN A  1 159 ? -25.117 -52.262 11.199   1.00 34.62  ? 159 GLN A NE2 1 
ATOM   1361  N N   . GLU A  1 160 ? -23.674 -56.619 14.449   1.00 22.87  ? 160 GLU A N   1 
ATOM   1362  C CA  . GLU A  1 160 ? -24.569 -56.805 15.585   1.00 34.26  ? 160 GLU A CA  1 
ATOM   1363  C C   . GLU A  1 160 ? -23.954 -56.278 16.874   1.00 32.96  ? 160 GLU A C   1 
ATOM   1364  O O   . GLU A  1 160 ? -24.686 -55.857 17.777   1.00 34.79  ? 160 GLU A O   1 
ATOM   1365  C CB  . GLU A  1 160 ? -24.944 -58.281 15.741   1.00 39.53  ? 160 GLU A CB  1 
ATOM   1366  C CG  . GLU A  1 160 ? -26.089 -58.532 16.732   1.00 48.51  ? 160 GLU A CG  1 
ATOM   1367  C CD  . GLU A  1 160 ? -25.574 -58.753 18.127   1.00 61.00  ? 160 GLU A CD  1 
ATOM   1368  O OE1 . GLU A  1 160 ? -26.274 -58.413 19.110   1.00 65.83  ? 160 GLU A OE1 1 
ATOM   1369  O OE2 . GLU A  1 160 ? -24.436 -59.259 18.230   1.00 65.84  ? 160 GLU A OE2 1 
ATOM   1370  N N   . GLU A  1 161 ? -22.621 -56.300 16.982   1.00 27.01  ? 161 GLU A N   1 
ATOM   1371  C CA  . GLU A  1 161 ? -21.980 -55.709 18.153   1.00 25.17  ? 161 GLU A CA  1 
ATOM   1372  C C   . GLU A  1 161 ? -22.017 -54.192 18.078   1.00 26.28  ? 161 GLU A C   1 
ATOM   1373  O O   . GLU A  1 161 ? -22.250 -53.509 19.087   1.00 22.50  ? 161 GLU A O   1 
ATOM   1374  C CB  . GLU A  1 161 ? -20.537 -56.198 18.272   1.00 25.31  ? 161 GLU A CB  1 
ATOM   1375  C CG  . GLU A  1 161 ? -20.438 -57.642 18.651   1.00 24.79  ? 161 GLU A CG  1 
ATOM   1376  C CD  . GLU A  1 161 ? -19.059 -58.218 18.431   1.00 36.77  ? 161 GLU A CD  1 
ATOM   1377  O OE1 . GLU A  1 161 ? -18.193 -57.513 17.860   1.00 35.13  ? 161 GLU A OE1 1 
ATOM   1378  O OE2 . GLU A  1 161 ? -18.852 -59.387 18.832   1.00 38.53  ? 161 GLU A OE2 1 
ATOM   1379  N N   . LYS A  1 162 ? -21.761 -53.645 16.885   1.00 24.66  ? 162 LYS A N   1 
ATOM   1380  C CA  . LYS A  1 162 ? -21.862 -52.206 16.710   1.00 24.31  ? 162 LYS A CA  1 
ATOM   1381  C C   . LYS A  1 162 ? -23.258 -51.725 17.068   1.00 24.99  ? 162 LYS A C   1 
ATOM   1382  O O   . LYS A  1 162 ? -23.421 -50.681 17.713   1.00 25.44  ? 162 LYS A O   1 
ATOM   1383  C CB  . LYS A  1 162 ? -21.512 -51.839 15.265   1.00 19.94  ? 162 LYS A CB  1 
ATOM   1384  C CG  . LYS A  1 162 ? -21.701 -50.379 14.929   1.00 25.10  ? 162 LYS A CG  1 
ATOM   1385  C CD  . LYS A  1 162 ? -21.242 -50.084 13.482   1.00 22.91  ? 162 LYS A CD  1 
ATOM   1386  C CE  . LYS A  1 162 ? -22.141 -50.736 12.468   1.00 25.17  ? 162 LYS A CE  1 
ATOM   1387  N NZ  . LYS A  1 162 ? -21.804 -50.323 11.037   1.00 25.91  ? 162 LYS A NZ  1 
ATOM   1388  N N   . GLU A  1 163 ? -24.280 -52.482 16.665   1.00 24.83  ? 163 GLU A N   1 
ATOM   1389  C CA  . GLU A  1 163 ? -25.649 -52.064 16.957   1.00 28.84  ? 163 GLU A CA  1 
ATOM   1390  C C   . GLU A  1 163 ? -25.972 -52.215 18.435   1.00 27.17  ? 163 GLU A C   1 
ATOM   1391  O O   . GLU A  1 163 ? -26.709 -51.396 18.998   1.00 26.12  ? 163 GLU A O   1 
ATOM   1392  C CB  . GLU A  1 163 ? -26.625 -52.860 16.090   1.00 29.50  ? 163 GLU A CB  1 
ATOM   1393  C CG  . GLU A  1 163 ? -26.495 -52.495 14.603   1.00 27.63  ? 163 GLU A CG  1 
ATOM   1394  C CD  . GLU A  1 163 ? -27.331 -53.384 13.702   1.00 41.15  ? 163 GLU A CD  1 
ATOM   1395  O OE1 . GLU A  1 163 ? -27.586 -52.968 12.553   1.00 42.41  ? 163 GLU A OE1 1 
ATOM   1396  O OE2 . GLU A  1 163 ? -27.715 -54.502 14.128   1.00 40.29  ? 163 GLU A OE2 1 
ATOM   1397  N N   . TYR A  1 164 ? -25.427 -53.249 19.074   1.00 27.52  ? 164 TYR A N   1 
ATOM   1398  C CA  . TYR A  1 164 ? -25.575 -53.386 20.520   1.00 30.90  ? 164 TYR A CA  1 
ATOM   1399  C C   . TYR A  1 164 ? -25.027 -52.153 21.234   1.00 29.70  ? 164 TYR A C   1 
ATOM   1400  O O   . TYR A  1 164 ? -25.701 -51.549 22.078   1.00 29.50  ? 164 TYR A O   1 
ATOM   1401  C CB  . TYR A  1 164 ? -24.870 -54.658 20.994   1.00 26.46  ? 164 TYR A CB  1 
ATOM   1402  C CG  . TYR A  1 164 ? -25.023 -54.827 22.485   1.00 25.52  ? 164 TYR A CG  1 
ATOM   1403  C CD1 . TYR A  1 164 ? -26.235 -55.214 23.022   1.00 30.63  ? 164 TYR A CD1 1 
ATOM   1404  C CD2 . TYR A  1 164 ? -23.979 -54.547 23.352   1.00 26.81  ? 164 TYR A CD2 1 
ATOM   1405  C CE1 . TYR A  1 164 ? -26.403 -55.341 24.392   1.00 35.75  ? 164 TYR A CE1 1 
ATOM   1406  C CE2 . TYR A  1 164 ? -24.140 -54.665 24.727   1.00 24.27  ? 164 TYR A CE2 1 
ATOM   1407  C CZ  . TYR A  1 164 ? -25.352 -55.061 25.239   1.00 31.94  ? 164 TYR A CZ  1 
ATOM   1408  O OH  . TYR A  1 164 ? -25.520 -55.185 26.605   1.00 35.91  ? 164 TYR A OH  1 
ATOM   1409  N N   . VAL A  1 165 ? -23.817 -51.737 20.859   1.00 30.32  ? 165 VAL A N   1 
ATOM   1410  C CA  . VAL A  1 165 ? -23.207 -50.536 21.418   1.00 26.61  ? 165 VAL A CA  1 
ATOM   1411  C C   . VAL A  1 165 ? -24.094 -49.313 21.188   1.00 30.58  ? 165 VAL A C   1 
ATOM   1412  O O   . VAL A  1 165 ? -24.318 -48.509 22.104   1.00 23.62  ? 165 VAL A O   1 
ATOM   1413  C CB  . VAL A  1 165 ? -21.804 -50.335 20.824   1.00 19.21  ? 165 VAL A CB  1 
ATOM   1414  C CG1 . VAL A  1 165 ? -21.217 -49.000 21.275   1.00 18.07  ? 165 VAL A CG1 1 
ATOM   1415  C CG2 . VAL A  1 165 ? -20.895 -51.499 21.224   1.00 21.23  ? 165 VAL A CG2 1 
ATOM   1416  N N   . LEU A  1 166 ? -24.617 -49.154 19.960   1.00 26.96  ? 166 LEU A N   1 
ATOM   1417  C CA  . LEU A  1 166 ? -25.441 -47.980 19.649   1.00 20.62  ? 166 LEU A CA  1 
ATOM   1418  C C   . LEU A  1 166 ? -26.689 -47.927 20.525   1.00 21.71  ? 166 LEU A C   1 
ATOM   1419  O O   . LEU A  1 166 ? -27.092 -46.852 20.996   1.00 22.76  ? 166 LEU A O   1 
ATOM   1420  C CB  . LEU A  1 166 ? -25.843 -47.985 18.169   1.00 21.11  ? 166 LEU A CB  1 
ATOM   1421  C CG  . LEU A  1 166 ? -24.846 -47.328 17.221   1.00 26.95  ? 166 LEU A CG  1 
ATOM   1422  C CD1 . LEU A  1 166 ? -25.214 -47.664 15.783   1.00 33.33  ? 166 LEU A CD1 1 
ATOM   1423  C CD2 . LEU A  1 166 ? -24.808 -45.802 17.460   1.00 26.43  ? 166 LEU A CD2 1 
ATOM   1424  N N   . ASN A  1 167 ? -27.321 -49.081 20.736   1.00 20.48  ? 167 ASN A N   1 
ATOM   1425  C CA  . ASN A  1 167 ? -28.523 -49.149 21.562   1.00 29.83  ? 167 ASN A CA  1 
ATOM   1426  C C   . ASN A  1 167 ? -28.234 -48.700 22.990   1.00 29.03  ? 167 ASN A C   1 
ATOM   1427  O O   . ASN A  1 167 ? -28.994 -47.911 23.571   1.00 27.52  ? 167 ASN A O   1 
ATOM   1428  C CB  . ASN A  1 167 ? -29.081 -50.574 21.547   1.00 34.54  ? 167 ASN A CB  1 
ATOM   1429  C CG  . ASN A  1 167 ? -30.244 -50.755 22.510   1.00 53.85  ? 167 ASN A CG  1 
ATOM   1430  O OD1 . ASN A  1 167 ? -31.250 -50.049 22.419   1.00 61.76  ? 167 ASN A OD1 1 
ATOM   1431  N ND2 . ASN A  1 167 ? -30.111 -51.701 23.443   1.00 58.18  ? 167 ASN A ND2 1 
ATOM   1432  N N   . LYS A  1 168 ? -27.132 -49.201 23.568   1.00 25.76  ? 168 LYS A N   1 
ATOM   1433  C CA  . LYS A  1 168 ? -26.751 -48.825 24.925   1.00 25.66  ? 168 LYS A CA  1 
ATOM   1434  C C   . LYS A  1 168 ? -26.459 -47.339 25.008   1.00 26.21  ? 168 LYS A C   1 
ATOM   1435  O O   . LYS A  1 168 ? -26.852 -46.676 25.976   1.00 23.21  ? 168 LYS A O   1 
ATOM   1436  C CB  . LYS A  1 168 ? -25.533 -49.635 25.385   1.00 23.30  ? 168 LYS A CB  1 
ATOM   1437  C CG  . LYS A  1 168 ? -25.774 -51.134 25.363   1.00 25.01  ? 168 LYS A CG  1 
ATOM   1438  C CD  . LYS A  1 168 ? -26.849 -51.514 26.367   1.00 33.06  ? 168 LYS A CD  1 
ATOM   1439  C CE  . LYS A  1 168 ? -26.308 -51.498 27.782   1.00 41.49  ? 168 LYS A CE  1 
ATOM   1440  N NZ  . LYS A  1 168 ? -27.351 -51.884 28.786   1.00 48.57  ? 168 LYS A NZ  1 
ATOM   1441  N N   . TYR A  1 169 ? -25.775 -46.801 23.993   1.00 23.07  ? 169 TYR A N   1 
ATOM   1442  C CA  . TYR A  1 169 ? -25.505 -45.368 23.935   1.00 18.61  ? 169 TYR A CA  1 
ATOM   1443  C C   . TYR A  1 169 ? -26.790 -44.546 23.992   1.00 25.72  ? 169 TYR A C   1 
ATOM   1444  O O   . TYR A  1 169 ? -26.844 -43.524 24.687   1.00 22.86  ? 169 TYR A O   1 
ATOM   1445  C CB  . TYR A  1 169 ? -24.721 -45.024 22.662   1.00 17.89  ? 169 TYR A CB  1 
ATOM   1446  C CG  . TYR A  1 169 ? -23.221 -45.230 22.790   1.00 22.67  ? 169 TYR A CG  1 
ATOM   1447  C CD1 . TYR A  1 169 ? -22.686 -46.092 23.756   1.00 23.55  ? 169 TYR A CD1 1 
ATOM   1448  C CD2 . TYR A  1 169 ? -22.340 -44.598 21.919   1.00 24.19  ? 169 TYR A CD2 1 
ATOM   1449  C CE1 . TYR A  1 169 ? -21.308 -46.287 23.870   1.00 19.16  ? 169 TYR A CE1 1 
ATOM   1450  C CE2 . TYR A  1 169 ? -20.974 -44.785 22.024   1.00 24.47  ? 169 TYR A CE2 1 
ATOM   1451  C CZ  . TYR A  1 169 ? -20.466 -45.618 23.003   1.00 23.34  ? 169 TYR A CZ  1 
ATOM   1452  O OH  . TYR A  1 169 ? -19.112 -45.791 23.065   1.00 24.29  ? 169 TYR A OH  1 
ATOM   1453  N N   . PHE A  1 170 ? -27.824 -44.943 23.236   1.00 28.50  ? 170 PHE A N   1 
ATOM   1454  C CA  . PHE A  1 170 ? -29.056 -44.154 23.250   1.00 25.73  ? 170 PHE A CA  1 
ATOM   1455  C C   . PHE A  1 170 ? -29.809 -44.300 24.573   1.00 23.75  ? 170 PHE A C   1 
ATOM   1456  O O   . PHE A  1 170 ? -30.534 -43.383 24.973   1.00 29.35  ? 170 PHE A O   1 
ATOM   1457  C CB  . PHE A  1 170 ? -29.948 -44.524 22.053   1.00 26.31  ? 170 PHE A CB  1 
ATOM   1458  C CG  . PHE A  1 170 ? -29.579 -43.775 20.788   1.00 28.17  ? 170 PHE A CG  1 
ATOM   1459  C CD1 . PHE A  1 170 ? -29.782 -42.400 20.698   1.00 29.68  ? 170 PHE A CD1 1 
ATOM   1460  C CD2 . PHE A  1 170 ? -28.982 -44.431 19.715   1.00 33.14  ? 170 PHE A CD2 1 
ATOM   1461  C CE1 . PHE A  1 170 ? -29.413 -41.694 19.551   1.00 33.40  ? 170 PHE A CE1 1 
ATOM   1462  C CE2 . PHE A  1 170 ? -28.612 -43.733 18.562   1.00 35.07  ? 170 PHE A CE2 1 
ATOM   1463  C CZ  . PHE A  1 170 ? -28.831 -42.365 18.481   1.00 36.81  ? 170 PHE A CZ  1 
ATOM   1464  N N   . GLU A  1 171 ? -29.652 -45.430 25.256   1.00 27.23  ? 171 GLU A N   1 
ATOM   1465  C CA  . GLU A  1 171 ? -30.219 -45.568 26.597   1.00 31.36  ? 171 GLU A CA  1 
ATOM   1466  C C   . GLU A  1 171 ? -29.580 -44.575 27.563   1.00 28.78  ? 171 GLU A C   1 
ATOM   1467  O O   . GLU A  1 171 ? -30.255 -44.034 28.440   1.00 31.02  ? 171 GLU A O   1 
ATOM   1468  C CB  . GLU A  1 171 ? -30.043 -47.000 27.103   1.00 29.37  ? 171 GLU A CB  1 
ATOM   1469  C CG  . GLU A  1 171 ? -31.000 -48.013 26.509   1.00 39.66  ? 171 GLU A CG  1 
ATOM   1470  C CD  . GLU A  1 171 ? -30.699 -49.441 26.969   1.00 52.40  ? 171 GLU A CD  1 
ATOM   1471  O OE1 . GLU A  1 171 ? -29.897 -49.603 27.913   1.00 55.09  ? 171 GLU A OE1 1 
ATOM   1472  O OE2 . GLU A  1 171 ? -31.253 -50.400 26.382   1.00 56.60  ? 171 GLU A OE2 1 
ATOM   1473  N N   . ILE A  1 172 ? -28.281 -44.311 27.393   1.00 26.95  ? 172 ILE A N   1 
ATOM   1474  C CA  . ILE A  1 172 ? -27.586 -43.324 28.211   1.00 25.59  ? 172 ILE A CA  1 
ATOM   1475  C C   . ILE A  1 172 ? -28.155 -41.927 27.977   1.00 27.46  ? 172 ILE A C   1 
ATOM   1476  O O   . ILE A  1 172 ? -28.337 -41.146 28.921   1.00 20.71  ? 172 ILE A O   1 
ATOM   1477  C CB  . ILE A  1 172 ? -26.078 -43.368 27.907   1.00 26.52  ? 172 ILE A CB  1 
ATOM   1478  C CG1 . ILE A  1 172 ? -25.463 -44.686 28.376   1.00 26.78  ? 172 ILE A CG1 1 
ATOM   1479  C CG2 . ILE A  1 172 ? -25.367 -42.192 28.537   1.00 24.74  ? 172 ILE A CG2 1 
ATOM   1480  C CD1 . ILE A  1 172 ? -25.331 -44.813 29.888   1.00 23.54  ? 172 ILE A CD1 1 
ATOM   1481  N N   . ILE A  1 173 ? -28.380 -41.565 26.705   1.00 22.21  ? 173 ILE A N   1 
ATOM   1482  C CA  . ILE A  1 173 ? -28.941 -40.256 26.393   1.00 23.75  ? 173 ILE A CA  1 
ATOM   1483  C C   . ILE A  1 173 ? -30.352 -40.133 26.953   1.00 22.46  ? 173 ILE A C   1 
ATOM   1484  O O   . ILE A  1 173 ? -30.724 -39.097 27.526   1.00 27.75  ? 173 ILE A O   1 
ATOM   1485  C CB  . ILE A  1 173 ? -28.915 -40.024 24.866   1.00 27.12  ? 173 ILE A CB  1 
ATOM   1486  C CG1 . ILE A  1 173 ? -27.466 -40.138 24.344   1.00 24.50  ? 173 ILE A CG1 1 
ATOM   1487  C CG2 . ILE A  1 173 ? -29.569 -38.676 24.537   1.00 25.73  ? 173 ILE A CG2 1 
ATOM   1488  C CD1 . ILE A  1 173 ? -27.345 -40.191 22.804   1.00 29.23  ? 173 ILE A CD1 1 
ATOM   1489  N N   . LYS A  1 174 ? -31.159 -41.183 26.800   1.00 21.75  ? 174 LYS A N   1 
ATOM   1490  C CA  . LYS A  1 174 ? -32.504 -41.172 27.364   1.00 27.46  ? 174 LYS A CA  1 
ATOM   1491  C C   . LYS A  1 174 ? -32.507 -40.976 28.884   1.00 29.95  ? 174 LYS A C   1 
ATOM   1492  O O   . LYS A  1 174 ? -33.522 -40.539 29.428   1.00 31.35  ? 174 LYS A O   1 
ATOM   1493  C CB  . LYS A  1 174 ? -33.241 -42.466 27.023   1.00 31.34  ? 174 LYS A CB  1 
ATOM   1494  C CG  . LYS A  1 174 ? -33.668 -42.588 25.570   1.00 35.06  ? 174 LYS A CG  1 
ATOM   1495  C CD  . LYS A  1 174 ? -34.528 -43.830 25.373   1.00 40.88  ? 174 LYS A CD  1 
ATOM   1496  C CE  . LYS A  1 174 ? -34.903 -44.023 23.901   1.00 48.01  ? 174 LYS A CE  1 
ATOM   1497  N NZ  . LYS A  1 174 ? -35.576 -45.337 23.641   1.00 51.09  ? 174 LYS A NZ  1 
ATOM   1498  N N   . LYS A  1 175 ? -31.403 -41.281 29.572   1.00 29.17  ? 175 LYS A N   1 
ATOM   1499  C CA  . LYS A  1 175 ? -31.284 -41.172 31.034   1.00 31.10  ? 175 LYS A CA  1 
ATOM   1500  C C   . LYS A  1 175 ? -30.747 -39.819 31.480   1.00 28.61  ? 175 LYS A C   1 
ATOM   1501  O O   . LYS A  1 175 ? -30.663 -39.559 32.688   1.00 28.31  ? 175 LYS A O   1 
ATOM   1502  C CB  . LYS A  1 175 ? -30.327 -42.249 31.574   1.00 31.21  ? 175 LYS A CB  1 
ATOM   1503  C CG  . LYS A  1 175 ? -30.812 -43.692 31.590   1.00 37.83  ? 175 LYS A CG  1 
ATOM   1504  C CD  . LYS A  1 175 ? -29.933 -44.545 32.530   1.00 49.08  ? 175 LYS A CD  1 
ATOM   1505  C CE  . LYS A  1 175 ? -28.814 -45.314 31.783   1.00 54.56  ? 175 LYS A CE  1 
ATOM   1506  N NZ  . LYS A  1 175 ? -27.534 -45.446 32.566   1.00 57.33  ? 175 LYS A NZ  1 
ATOM   1507  N N   . THR A  1 176 ? -30.324 -38.978 30.540   1.00 20.93  ? 176 THR A N   1 
ATOM   1508  C CA  . THR A  1 176 ? -29.390 -37.905 30.876   1.00 19.23  ? 176 THR A CA  1 
ATOM   1509  C C   . THR A  1 176 ? -30.068 -36.729 31.575   1.00 27.70  ? 176 THR A C   1 
ATOM   1510  O O   . THR A  1 176 ? -29.563 -36.229 32.591   1.00 31.62  ? 176 THR A O   1 
ATOM   1511  C CB  . THR A  1 176 ? -28.667 -37.469 29.613   1.00 19.90  ? 176 THR A CB  1 
ATOM   1512  O OG1 . THR A  1 176 ? -27.859 -38.563 29.182   1.00 24.34  ? 176 THR A OG1 1 
ATOM   1513  C CG2 . THR A  1 176 ? -27.807 -36.259 29.857   1.00 21.17  ? 176 THR A CG2 1 
ATOM   1514  N N   . LEU A  1 177 ? -31.207 -36.261 31.059   1.00 23.29  ? 177 LEU A N   1 
ATOM   1515  C CA  . LEU A  1 177 ? -31.864 -35.161 31.752   1.00 22.92  ? 177 LEU A CA  1 
ATOM   1516  C C   . LEU A  1 177 ? -32.430 -35.626 33.090   1.00 23.64  ? 177 LEU A C   1 
ATOM   1517  O O   . LEU A  1 177 ? -32.514 -34.831 34.035   1.00 24.56  ? 177 LEU A O   1 
ATOM   1518  C CB  . LEU A  1 177 ? -32.967 -34.560 30.889   1.00 27.61  ? 177 LEU A CB  1 
ATOM   1519  C CG  . LEU A  1 177 ? -32.511 -33.886 29.593   1.00 26.41  ? 177 LEU A CG  1 
ATOM   1520  C CD1 . LEU A  1 177 ? -33.717 -33.460 28.767   1.00 30.59  ? 177 LEU A CD1 1 
ATOM   1521  C CD2 . LEU A  1 177 ? -31.639 -32.683 29.901   1.00 24.08  ? 177 LEU A CD2 1 
ATOM   1522  N N   . SER A  1 178 ? -32.788 -36.916 33.196   1.00 23.60  ? 178 SER A N   1 
ATOM   1523  C CA  . SER A  1 178 ? -33.365 -37.431 34.436   1.00 23.09  ? 178 SER A CA  1 
ATOM   1524  C C   . SER A  1 178 ? -32.337 -37.482 35.553   1.00 20.86  ? 178 SER A C   1 
ATOM   1525  O O   . SER A  1 178 ? -32.701 -37.404 36.728   1.00 22.64  ? 178 SER A O   1 
ATOM   1526  C CB  . SER A  1 178 ? -33.955 -38.826 34.227   1.00 33.43  ? 178 SER A CB  1 
ATOM   1527  O OG  . SER A  1 178 ? -35.245 -38.755 33.645   1.00 39.98  ? 178 SER A OG  1 
ATOM   1528  N N   . ILE A  1 179 ? -31.058 -37.621 35.222   1.00 25.43  ? 179 ILE A N   1 
ATOM   1529  C CA  . ILE A  1 179 ? -30.093 -37.704 36.308   1.00 30.37  ? 179 ILE A CA  1 
ATOM   1530  C C   . ILE A  1 179 ? -29.735 -36.311 36.817   1.00 25.88  ? 179 ILE A C   1 
ATOM   1531  O O   . ILE A  1 179 ? -29.449 -36.147 38.007   1.00 27.76  ? 179 ILE A O   1 
ATOM   1532  C CB  . ILE A  1 179 ? -28.845 -38.501 35.894   1.00 27.24  ? 179 ILE A CB  1 
ATOM   1533  C CG1 . ILE A  1 179 ? -28.001 -38.793 37.140   1.00 32.56  ? 179 ILE A CG1 1 
ATOM   1534  C CG2 . ILE A  1 179 ? -28.027 -37.728 34.885   1.00 23.83  ? 179 ILE A CG2 1 
ATOM   1535  C CD1 . ILE A  1 179 ? -26.871 -39.770 36.911   1.00 35.53  ? 179 ILE A CD1 1 
ATOM   1536  N N   . TYR A  1 180 ? -29.747 -35.291 35.949   1.00 21.17  ? 180 TYR A N   1 
ATOM   1537  C CA  . TYR A  1 180 ? -29.594 -33.921 36.438   1.00 20.80  ? 180 TYR A CA  1 
ATOM   1538  C C   . TYR A  1 180 ? -30.724 -33.558 37.391   1.00 24.69  ? 180 TYR A C   1 
ATOM   1539  O O   . TYR A  1 180 ? -30.494 -32.942 38.438   1.00 23.05  ? 180 TYR A O   1 
ATOM   1540  C CB  . TYR A  1 180 ? -29.542 -32.947 35.280   1.00 25.90  ? 180 TYR A CB  1 
ATOM   1541  C CG  . TYR A  1 180 ? -28.205 -32.959 34.588   1.00 23.72  ? 180 TYR A CG  1 
ATOM   1542  C CD1 . TYR A  1 180 ? -27.086 -32.418 35.205   1.00 24.22  ? 180 TYR A CD1 1 
ATOM   1543  C CD2 . TYR A  1 180 ? -28.054 -33.537 33.333   1.00 26.42  ? 180 TYR A CD2 1 
ATOM   1544  C CE1 . TYR A  1 180 ? -25.855 -32.419 34.582   1.00 23.67  ? 180 TYR A CE1 1 
ATOM   1545  C CE2 . TYR A  1 180 ? -26.824 -33.546 32.698   1.00 24.43  ? 180 TYR A CE2 1 
ATOM   1546  C CZ  . TYR A  1 180 ? -25.727 -32.976 33.335   1.00 23.90  ? 180 TYR A CZ  1 
ATOM   1547  O OH  . TYR A  1 180 ? -24.489 -32.977 32.730   1.00 21.93  ? 180 TYR A OH  1 
ATOM   1548  N N   . ARG A  1 181 ? -31.947 -33.944 37.049   1.00 24.04  ? 181 ARG A N   1 
ATOM   1549  C CA  . ARG A  1 181 ? -33.073 -33.700 37.941   1.00 24.06  ? 181 ARG A CA  1 
ATOM   1550  C C   . ARG A  1 181 ? -32.968 -34.516 39.228   1.00 26.28  ? 181 ARG A C   1 
ATOM   1551  O O   . ARG A  1 181 ? -33.401 -34.051 40.291   1.00 28.13  ? 181 ARG A O   1 
ATOM   1552  C CB  . ARG A  1 181 ? -34.362 -34.004 37.193   1.00 22.27  ? 181 ARG A CB  1 
ATOM   1553  C CG  . ARG A  1 181 ? -35.629 -33.838 37.982   1.00 26.05  ? 181 ARG A CG  1 
ATOM   1554  C CD  . ARG A  1 181 ? -36.826 -34.205 37.091   1.00 28.99  ? 181 ARG A CD  1 
ATOM   1555  N NE  . ARG A  1 181 ? -36.705 -33.579 35.778   1.00 28.78  ? 181 ARG A NE  1 
ATOM   1556  C CZ  . ARG A  1 181 ? -36.682 -34.228 34.614   1.00 32.22  ? 181 ARG A CZ  1 
ATOM   1557  N NH1 . ARG A  1 181 ? -36.772 -35.559 34.564   1.00 33.16  ? 181 ARG A NH1 1 
ATOM   1558  N NH2 . ARG A  1 181 ? -36.576 -33.533 33.491   1.00 28.67  ? 181 ARG A NH2 1 
ATOM   1559  N N   . GLU A  1 182 ? -32.403 -35.728 39.167   1.00 21.36  ? 182 GLU A N   1 
ATOM   1560  C CA  . GLU A  1 182 ? -32.266 -36.531 40.384   1.00 29.02  ? 182 GLU A CA  1 
ATOM   1561  C C   . GLU A  1 182 ? -31.200 -35.955 41.318   1.00 25.57  ? 182 GLU A C   1 
ATOM   1562  O O   . GLU A  1 182 ? -31.421 -35.846 42.531   1.00 27.31  ? 182 GLU A O   1 
ATOM   1563  C CB  . GLU A  1 182 ? -31.959 -37.998 40.031   1.00 25.92  ? 182 GLU A CB  1 
ATOM   1564  C CG  . GLU A  1 182 ? -31.555 -38.844 41.242   1.00 30.36  ? 182 GLU A CG  1 
ATOM   1565  C CD  . GLU A  1 182 ? -31.277 -40.323 40.949   1.00 37.16  ? 182 GLU A CD  1 
ATOM   1566  O OE1 . GLU A  1 182 ? -31.055 -41.060 41.940   1.00 41.20  ? 182 GLU A OE1 1 
ATOM   1567  O OE2 . GLU A  1 182 ? -31.264 -40.761 39.767   1.00 33.79  ? 182 GLU A OE2 1 
ATOM   1568  N N   . ILE A  1 183 ? -30.012 -35.625 40.792   1.00 21.47  ? 183 ILE A N   1 
ATOM   1569  C CA  . ILE A  1 183 ? -28.990 -35.061 41.678   1.00 25.31  ? 183 ILE A CA  1 
ATOM   1570  C C   . ILE A  1 183 ? -29.462 -33.724 42.243   1.00 28.84  ? 183 ILE A C   1 
ATOM   1571  O O   . ILE A  1 183 ? -29.175 -33.385 43.404   1.00 28.86  ? 183 ILE A O   1 
ATOM   1572  C CB  . ILE A  1 183 ? -27.625 -34.918 40.956   1.00 25.80  ? 183 ILE A CB  1 
ATOM   1573  C CG1 . ILE A  1 183 ? -27.686 -33.854 39.856   1.00 27.59  ? 183 ILE A CG1 1 
ATOM   1574  C CG2 . ILE A  1 183 ? -27.172 -36.254 40.410   1.00 23.00  ? 183 ILE A CG2 1 
ATOM   1575  C CD1 . ILE A  1 183 ? -27.162 -32.470 40.285   1.00 21.92  ? 183 ILE A CD1 1 
ATOM   1576  N N   . LYS A  1 184 ? -30.203 -32.950 41.448   1.00 20.67  ? 184 LYS A N   1 
ATOM   1577  C CA  . LYS A  1 184 ? -30.785 -31.718 41.978   1.00 23.47  ? 184 LYS A CA  1 
ATOM   1578  C C   . LYS A  1 184 ? -31.775 -32.018 43.101   1.00 22.24  ? 184 LYS A C   1 
ATOM   1579  O O   . LYS A  1 184 ? -31.774 -31.351 44.138   1.00 24.86  ? 184 LYS A O   1 
ATOM   1580  C CB  . LYS A  1 184 ? -31.469 -30.937 40.853   1.00 22.96  ? 184 LYS A CB  1 
ATOM   1581  C CG  . LYS A  1 184 ? -32.023 -29.577 41.286   1.00 23.93  ? 184 LYS A CG  1 
ATOM   1582  C CD  . LYS A  1 184 ? -32.683 -28.871 40.101   1.00 25.79  ? 184 LYS A CD  1 
ATOM   1583  C CE  . LYS A  1 184 ? -33.235 -27.524 40.526   1.00 31.46  ? 184 LYS A CE  1 
ATOM   1584  N NZ  . LYS A  1 184 ? -34.217 -27.683 41.636   1.00 37.11  ? 184 LYS A NZ  1 
ATOM   1585  N N   . GLU A  1 185 ? -32.614 -33.031 42.926   1.00 28.61  ? 185 GLU A N   1 
ATOM   1586  C CA  . GLU A  1 185 ? -33.635 -33.290 43.933   1.00 28.45  ? 185 GLU A CA  1 
ATOM   1587  C C   . GLU A  1 185 ? -33.026 -33.894 45.192   1.00 32.36  ? 185 GLU A C   1 
ATOM   1588  O O   . GLU A  1 185 ? -33.483 -33.618 46.302   1.00 34.74  ? 185 GLU A O   1 
ATOM   1589  C CB  . GLU A  1 185 ? -34.716 -34.207 43.374   1.00 33.81  ? 185 GLU A CB  1 
ATOM   1590  C CG  . GLU A  1 185 ? -36.055 -34.097 44.120   1.00 47.80  ? 185 GLU A CG  1 
ATOM   1591  C CD  . GLU A  1 185 ? -36.100 -34.886 45.434   1.00 60.41  ? 185 GLU A CD  1 
ATOM   1592  O OE1 . GLU A  1 185 ? -36.921 -34.542 46.311   1.00 63.12  ? 185 GLU A OE1 1 
ATOM   1593  O OE2 . GLU A  1 185 ? -35.328 -35.856 45.589   1.00 62.79  ? 185 GLU A OE2 1 
ATOM   1594  N N   . GLU A  1 186 ? -31.993 -34.712 45.041   1.00 33.60  ? 186 GLU A N   1 
ATOM   1595  C CA  . GLU A  1 186 ? -31.376 -35.362 46.182   1.00 30.43  ? 186 GLU A CA  1 
ATOM   1596  C C   . GLU A  1 186 ? -30.422 -34.450 46.948   1.00 32.07  ? 186 GLU A C   1 
ATOM   1597  O O   . GLU A  1 186 ? -29.813 -34.903 47.929   1.00 34.37  ? 186 GLU A O   1 
ATOM   1598  C CB  . GLU A  1 186 ? -30.669 -36.634 45.707   1.00 32.47  ? 186 GLU A CB  1 
ATOM   1599  C CG  . GLU A  1 186 ? -31.639 -37.659 45.133   1.00 31.30  ? 186 GLU A CG  1 
ATOM   1600  C CD  . GLU A  1 186 ? -30.946 -38.886 44.577   1.00 36.91  ? 186 GLU A CD  1 
ATOM   1601  O OE1 . GLU A  1 186 ? -29.733 -38.805 44.274   1.00 37.82  ? 186 GLU A OE1 1 
ATOM   1602  O OE2 . GLU A  1 186 ? -31.622 -39.928 44.427   1.00 39.32  ? 186 GLU A OE2 1 
ATOM   1603  N N   . GLY A  1 187 ? -30.299 -33.182 46.546   1.00 26.94  ? 187 GLY A N   1 
ATOM   1604  C CA  . GLY A  1 187 ? -29.375 -32.269 47.183   1.00 27.12  ? 187 GLY A CA  1 
ATOM   1605  C C   . GLY A  1 187 ? -27.919 -32.555 46.910   1.00 29.10  ? 187 GLY A C   1 
ATOM   1606  O O   . GLY A  1 187 ? -27.052 -32.041 47.619   1.00 29.22  ? 187 GLY A O   1 
ATOM   1607  N N   . LYS A  1 188 ? -27.616 -33.362 45.894   1.00 32.94  ? 188 LYS A N   1 
ATOM   1608  C CA  . LYS A  1 188 ? -26.227 -33.677 45.581   1.00 30.38  ? 188 LYS A CA  1 
ATOM   1609  C C   . LYS A  1 188 ? -25.564 -32.634 44.688   1.00 30.58  ? 188 LYS A C   1 
ATOM   1610  O O   . LYS A  1 188 ? -24.332 -32.635 44.566   1.00 27.22  ? 188 LYS A O   1 
ATOM   1611  C CB  . LYS A  1 188 ? -26.150 -35.058 44.932   1.00 27.46  ? 188 LYS A CB  1 
ATOM   1612  C CG  . LYS A  1 188 ? -26.790 -36.154 45.758   1.00 33.65  ? 188 LYS A CG  1 
ATOM   1613  C CD  . LYS A  1 188 ? -26.594 -37.545 45.137   1.00 32.75  ? 188 LYS A CD  1 
ATOM   1614  C CE  . LYS A  1 188 ? -27.032 -38.595 46.136   1.00 40.18  ? 188 LYS A CE  1 
ATOM   1615  N NZ  . LYS A  1 188 ? -27.013 -39.962 45.595   1.00 47.84  ? 188 LYS A NZ  1 
ATOM   1616  N N   . GLY A  1 189 ? -26.339 -31.749 44.077   1.00 24.30  ? 189 GLY A N   1 
ATOM   1617  C CA  . GLY A  1 189 ? -25.777 -30.693 43.258   1.00 27.99  ? 189 GLY A CA  1 
ATOM   1618  C C   . GLY A  1 189 ? -26.854 -29.710 42.875   1.00 30.24  ? 189 GLY A C   1 
ATOM   1619  O O   . GLY A  1 189 ? -28.048 -30.016 42.941   1.00 28.58  ? 189 GLY A O   1 
ATOM   1620  N N   . SER A  1 190 ? -26.423 -28.508 42.505   1.00 26.55  ? 190 SER A N   1 
ATOM   1621  C CA  . SER A  1 190 ? -27.336 -27.553 41.910   1.00 20.45  ? 190 SER A CA  1 
ATOM   1622  C C   . SER A  1 190 ? -27.107 -27.565 40.401   1.00 24.03  ? 190 SER A C   1 
ATOM   1623  O O   . SER A  1 190 ? -26.016 -27.888 39.929   1.00 22.32  ? 190 SER A O   1 
ATOM   1624  C CB  . SER A  1 190 ? -27.142 -26.145 42.497   1.00 21.52  ? 190 SER A CB  1 
ATOM   1625  O OG  . SER A  1 190 ? -27.447 -26.104 43.896   1.00 24.70  ? 190 SER A OG  1 
ATOM   1626  N N   . VAL A  1 191 ? -28.161 -27.288 39.644   1.00 21.99  ? 191 VAL A N   1 
ATOM   1627  C CA  . VAL A  1 191 ? -28.057 -27.192 38.194   1.00 22.14  ? 191 VAL A CA  1 
ATOM   1628  C C   . VAL A  1 191 ? -28.414 -25.762 37.799   1.00 26.50  ? 191 VAL A C   1 
ATOM   1629  O O   . VAL A  1 191 ? -29.450 -25.237 38.219   1.00 24.51  ? 191 VAL A O   1 
ATOM   1630  C CB  . VAL A  1 191 ? -28.960 -28.211 37.473   1.00 20.19  ? 191 VAL A CB  1 
ATOM   1631  C CG1 . VAL A  1 191 ? -28.794 -28.027 35.917   1.00 17.96  ? 191 VAL A CG1 1 
ATOM   1632  C CG2 . VAL A  1 191 ? -28.631 -29.661 37.910   1.00 17.38  ? 191 VAL A CG2 1 
ATOM   1633  N N   . SER A  1 192 ? -27.557 -25.131 37.004   1.00 25.63  ? 192 SER A N   1 
ATOM   1634  C CA  . SER A  1 192 ? -27.828 -23.799 36.497   1.00 20.05  ? 192 SER A CA  1 
ATOM   1635  C C   . SER A  1 192 ? -28.059 -23.877 34.988   1.00 27.83  ? 192 SER A C   1 
ATOM   1636  O O   . SER A  1 192 ? -27.925 -24.935 34.358   1.00 15.39  ? 192 SER A O   1 
ATOM   1637  C CB  . SER A  1 192 ? -26.674 -22.858 36.818   1.00 19.07  ? 192 SER A CB  1 
ATOM   1638  O OG  . SER A  1 192 ? -25.536 -23.223 36.058   1.00 19.87  ? 192 SER A OG  1 
ATOM   1639  N N   . THR A  1 193 ? -28.415 -22.741 34.398   1.00 22.33  ? 193 THR A N   1 
ATOM   1640  C CA  . THR A  1 193 ? -28.455 -22.668 32.947   1.00 21.69  ? 193 THR A CA  1 
ATOM   1641  C C   . THR A  1 193 ? -27.809 -21.360 32.508   1.00 23.98  ? 193 THR A C   1 
ATOM   1642  O O   . THR A  1 193 ? -27.399 -20.551 33.337   1.00 23.32  ? 193 THR A O   1 
ATOM   1643  C CB  . THR A  1 193 ? -29.879 -22.826 32.413   1.00 16.77  ? 193 THR A CB  1 
ATOM   1644  O OG1 . THR A  1 193 ? -29.796 -22.998 30.992   1.00 21.39  ? 193 THR A OG1 1 
ATOM   1645  C CG2 . THR A  1 193 ? -30.741 -21.606 32.742   1.00 21.47  ? 193 THR A CG2 1 
ATOM   1646  N N   . SER A  1 194 ? -27.697 -21.155 31.165   1.00 18.85  ? 194 SER A N   1 
ATOM   1647  C CA  . SER A  1 194 ? -27.164 -19.911 30.614   1.00 23.39  ? 194 SER A CA  1 
ATOM   1648  C C   . SER A  1 194 ? -28.221 -19.219 29.747   1.00 23.13  ? 194 SER A C   1 
ATOM   1649  O O   . SER A  1 194 ? -29.246 -19.837 29.443   1.00 18.30  ? 194 SER A O   1 
ATOM   1650  C CB  . SER A  1 194 ? -25.910 -20.189 29.774   1.00 22.12  ? 194 SER A CB  1 
ATOM   1651  O OG  . SER A  1 194 ? -24.811 -20.624 30.552   1.00 22.43  ? 194 SER A OG  1 
ATOM   1652  N N   . PRO A  1 195 ? -28.038 -17.958 29.340   1.00 25.55  ? 195 PRO A N   1 
ATOM   1653  C CA  . PRO A  1 195 ? -28.893 -17.411 28.276   1.00 24.98  ? 195 PRO A CA  1 
ATOM   1654  C C   . PRO A  1 195 ? -28.886 -18.358 27.078   1.00 24.19  ? 195 PRO A C   1 
ATOM   1655  O O   . PRO A  1 195 ? -27.867 -18.988 26.775   1.00 15.62  ? 195 PRO A O   1 
ATOM   1656  C CB  . PRO A  1 195 ? -28.244 -16.062 27.954   1.00 26.03  ? 195 PRO A CB  1 
ATOM   1657  C CG  . PRO A  1 195 ? -27.620 -15.648 29.259   1.00 33.50  ? 195 PRO A CG  1 
ATOM   1658  C CD  . PRO A  1 195 ? -27.137 -16.931 29.902   1.00 28.15  ? 195 PRO A CD  1 
ATOM   1659  N N   . TYR A  1 196 ? -30.042 -18.425 26.397   1.00 25.00  ? 196 TYR A N   1 
ATOM   1660  C CA  . TYR A  1 196 ? -30.473 -19.624 25.683   1.00 23.55  ? 196 TYR A CA  1 
ATOM   1661  C C   . TYR A  1 196 ? -29.394 -20.198 24.765   1.00 26.62  ? 196 TYR A C   1 
ATOM   1662  O O   . TYR A  1 196 ? -29.071 -21.393 24.842   1.00 22.07  ? 196 TYR A O   1 
ATOM   1663  C CB  . TYR A  1 196 ? -31.760 -19.330 24.895   1.00 17.34  ? 196 TYR A CB  1 
ATOM   1664  C CG  . TYR A  1 196 ? -32.556 -20.580 24.612   1.00 24.54  ? 196 TYR A CG  1 
ATOM   1665  C CD1 . TYR A  1 196 ? -32.148 -21.473 23.625   1.00 27.50  ? 196 TYR A CD1 1 
ATOM   1666  C CD2 . TYR A  1 196 ? -33.702 -20.884 25.345   1.00 21.56  ? 196 TYR A CD2 1 
ATOM   1667  C CE1 . TYR A  1 196 ? -32.846 -22.623 23.375   1.00 26.92  ? 196 TYR A CE1 1 
ATOM   1668  C CE2 . TYR A  1 196 ? -34.417 -22.028 25.100   1.00 18.55  ? 196 TYR A CE2 1 
ATOM   1669  C CZ  . TYR A  1 196 ? -33.984 -22.898 24.114   1.00 27.90  ? 196 TYR A CZ  1 
ATOM   1670  O OH  . TYR A  1 196 ? -34.687 -24.051 23.856   1.00 29.62  ? 196 TYR A OH  1 
ATOM   1671  N N   . TYR A  1 197 ? -28.838 -19.376 23.873   1.00 23.17  ? 197 TYR A N   1 
ATOM   1672  C CA  . TYR A  1 197 ? -27.916 -19.877 22.859   1.00 20.68  ? 197 TYR A CA  1 
ATOM   1673  C C   . TYR A  1 197 ? -26.455 -19.541 23.158   1.00 19.95  ? 197 TYR A C   1 
ATOM   1674  O O   . TYR A  1 197 ? -25.651 -19.452 22.230   1.00 18.81  ? 197 TYR A O   1 
ATOM   1675  C CB  . TYR A  1 197 ? -28.323 -19.354 21.475   1.00 19.72  ? 197 TYR A CB  1 
ATOM   1676  C CG  . TYR A  1 197 ? -29.636 -19.954 21.022   1.00 20.51  ? 197 TYR A CG  1 
ATOM   1677  C CD1 . TYR A  1 197 ? -29.717 -21.298 20.667   1.00 16.92  ? 197 TYR A CD1 1 
ATOM   1678  C CD2 . TYR A  1 197 ? -30.798 -19.203 21.019   1.00 20.37  ? 197 TYR A CD2 1 
ATOM   1679  C CE1 . TYR A  1 197 ? -30.916 -21.863 20.281   1.00 22.62  ? 197 TYR A CE1 1 
ATOM   1680  C CE2 . TYR A  1 197 ? -32.009 -19.763 20.642   1.00 19.48  ? 197 TYR A CE2 1 
ATOM   1681  C CZ  . TYR A  1 197 ? -32.055 -21.096 20.279   1.00 23.71  ? 197 TYR A CZ  1 
ATOM   1682  O OH  . TYR A  1 197 ? -33.252 -21.660 19.905   1.00 28.71  ? 197 TYR A OH  1 
ATOM   1683  N N   . HIS A  1 198 ? -26.079 -19.368 24.427   1.00 23.28  ? 198 HIS A N   1 
ATOM   1684  C CA  . HIS A  1 198 ? -24.698 -19.072 24.806   1.00 23.55  ? 198 HIS A CA  1 
ATOM   1685  C C   . HIS A  1 198 ? -24.139 -17.824 24.101   1.00 18.82  ? 198 HIS A C   1 
ATOM   1686  O O   . HIS A  1 198 ? -23.035 -17.848 23.552   1.00 25.29  ? 198 HIS A O   1 
ATOM   1687  C CB  . HIS A  1 198 ? -23.826 -20.299 24.530   1.00 22.88  ? 198 HIS A CB  1 
ATOM   1688  C CG  . HIS A  1 198 ? -22.576 -20.394 25.354   1.00 20.66  ? 198 HIS A CG  1 
ATOM   1689  N ND1 . HIS A  1 198 ? -21.338 -20.021 24.872   1.00 22.28  ? 198 HIS A ND1 1 
ATOM   1690  C CD2 . HIS A  1 198 ? -22.363 -20.873 26.604   1.00 22.27  ? 198 HIS A CD2 1 
ATOM   1691  C CE1 . HIS A  1 198 ? -20.422 -20.232 25.801   1.00 24.15  ? 198 HIS A CE1 1 
ATOM   1692  N NE2 . HIS A  1 198 ? -21.019 -20.749 26.864   1.00 21.05  ? 198 HIS A NE2 1 
ATOM   1693  N N   . PRO A  1 199 ? -24.876 -16.711 24.082   1.00 17.78  ? 199 PRO A N   1 
ATOM   1694  C CA  . PRO A  1 199 ? -24.343 -15.474 23.493   1.00 21.07  ? 199 PRO A CA  1 
ATOM   1695  C C   . PRO A  1 199 ? -23.457 -14.716 24.468   1.00 30.39  ? 199 PRO A C   1 
ATOM   1696  O O   . PRO A  1 199 ? -23.471 -14.944 25.685   1.00 25.73  ? 199 PRO A O   1 
ATOM   1697  C CB  . PRO A  1 199 ? -25.595 -14.658 23.243   1.00 20.45  ? 199 PRO A CB  1 
ATOM   1698  C CG  . PRO A  1 199 ? -26.426 -15.006 24.436   1.00 18.16  ? 199 PRO A CG  1 
ATOM   1699  C CD  . PRO A  1 199 ? -26.218 -16.483 24.651   1.00 20.51  ? 199 PRO A CD  1 
ATOM   1700  N N   . LEU A  1 200 ? -22.747 -13.736 23.917   1.00 26.22  ? 200 LEU A N   1 
ATOM   1701  C CA  . LEU A  1 200 ? -22.029 -12.762 24.733   1.00 28.48  ? 200 LEU A CA  1 
ATOM   1702  C C   . LEU A  1 200 ? -22.999 -11.651 25.131   1.00 28.06  ? 200 LEU A C   1 
ATOM   1703  O O   . LEU A  1 200 ? -23.187 -10.681 24.400   1.00 25.37  ? 200 LEU A O   1 
ATOM   1704  C CB  . LEU A  1 200 ? -20.816 -12.219 23.983   1.00 28.07  ? 200 LEU A CB  1 
ATOM   1705  C CG  . LEU A  1 200 ? -19.757 -13.294 23.723   1.00 30.70  ? 200 LEU A CG  1 
ATOM   1706  C CD1 . LEU A  1 200 ? -18.886 -12.913 22.522   1.00 33.12  ? 200 LEU A CD1 1 
ATOM   1707  C CD2 . LEU A  1 200 ? -18.894 -13.560 24.974   1.00 31.08  ? 200 LEU A CD2 1 
ATOM   1708  N N   . ILE A  1 201 ? -23.619 -11.799 26.324   1.00 24.86  ? 201 ILE A N   1 
ATOM   1709  C CA  . ILE A  1 201 ? -24.600 -10.809 26.782   1.00 18.24  ? 201 ILE A CA  1 
ATOM   1710  C C   . ILE A  1 201 ? -24.030 -9.401  26.864   1.00 20.81  ? 201 ILE A C   1 
ATOM   1711  O O   . ILE A  1 201 ? -24.730 -8.455  26.478   1.00 21.61  ? 201 ILE A O   1 
ATOM   1712  C CB  . ILE A  1 201 ? -25.237 -11.264 28.104   1.00 22.10  ? 201 ILE A CB  1 
ATOM   1713  C CG1 . ILE A  1 201 ? -26.035 -12.547 27.893   1.00 24.93  ? 201 ILE A CG1 1 
ATOM   1714  C CG2 . ILE A  1 201 ? -26.128 -10.137 28.710   1.00 20.63  ? 201 ILE A CG2 1 
ATOM   1715  C CD1 . ILE A  1 201 ? -27.398 -12.305 27.247   1.00 24.94  ? 201 ILE A CD1 1 
ATOM   1716  N N   . PRO A  1 202 ? -22.823 -9.164  27.396   1.00 22.24  ? 202 PRO A N   1 
ATOM   1717  C CA  . PRO A  1 202 ? -22.340 -7.775  27.431   1.00 19.90  ? 202 PRO A CA  1 
ATOM   1718  C C   . PRO A  1 202 ? -22.299 -7.138  26.054   1.00 19.57  ? 202 PRO A C   1 
ATOM   1719  O O   . PRO A  1 202 ? -22.642 -5.953  25.910   1.00 23.58  ? 202 PRO A O   1 
ATOM   1720  C CB  . PRO A  1 202 ? -20.942 -7.902  28.045   1.00 20.07  ? 202 PRO A CB  1 
ATOM   1721  C CG  . PRO A  1 202 ? -21.048 -9.143  28.919   1.00 22.78  ? 202 PRO A CG  1 
ATOM   1722  C CD  . PRO A  1 202 ? -21.886 -10.074 28.079   1.00 22.17  ? 202 PRO A CD  1 
ATOM   1723  N N   . ILE A  1 203 ? -21.896 -7.888  25.032   1.00 20.13  ? 203 ILE A N   1 
ATOM   1724  C CA  . ILE A  1 203 ? -21.847 -7.279  23.703   1.00 23.95  ? 203 ILE A CA  1 
ATOM   1725  C C   . ILE A  1 203 ? -23.256 -6.987  23.203   1.00 24.60  ? 203 ILE A C   1 
ATOM   1726  O O   . ILE A  1 203 ? -23.518 -5.914  22.656   1.00 28.80  ? 203 ILE A O   1 
ATOM   1727  C CB  . ILE A  1 203 ? -21.058 -8.160  22.717   1.00 24.90  ? 203 ILE A CB  1 
ATOM   1728  C CG1 . ILE A  1 203 ? -19.576 -8.173  23.096   1.00 21.06  ? 203 ILE A CG1 1 
ATOM   1729  C CG2 . ILE A  1 203 ? -21.262 -7.656  21.243   1.00 25.11  ? 203 ILE A CG2 1 
ATOM   1730  C CD1 . ILE A  1 203 ? -18.715 -8.894  22.103   1.00 24.11  ? 203 ILE A CD1 1 
ATOM   1731  N N   . LEU A  1 204 ? -24.192 -7.920  23.389   1.00 24.60  ? 204 LEU A N   1 
ATOM   1732  C CA  . LEU A  1 204 ? -25.545 -7.661  22.901   1.00 23.85  ? 204 LEU A CA  1 
ATOM   1733  C C   . LEU A  1 204 ? -26.150 -6.446  23.587   1.00 26.70  ? 204 LEU A C   1 
ATOM   1734  O O   . LEU A  1 204 ? -26.903 -5.684  22.973   1.00 26.79  ? 204 LEU A O   1 
ATOM   1735  C CB  . LEU A  1 204 ? -26.433 -8.879  23.110   1.00 25.95  ? 204 LEU A CB  1 
ATOM   1736  C CG  . LEU A  1 204 ? -26.094 -10.188 22.403   1.00 23.66  ? 204 LEU A CG  1 
ATOM   1737  C CD1 . LEU A  1 204 ? -27.231 -11.163 22.667   1.00 18.69  ? 204 LEU A CD1 1 
ATOM   1738  C CD2 . LEU A  1 204 ? -25.843 -9.995  20.888   1.00 18.75  ? 204 LEU A CD2 1 
ATOM   1739  N N   . LEU A  1 205 ? -25.830 -6.240  24.867   1.00 26.69  ? 205 LEU A N   1 
ATOM   1740  C CA  . LEU A  1 205 ? -26.369 -5.086  25.568   1.00 23.07  ? 205 LEU A CA  1 
ATOM   1741  C C   . LEU A  1 205 ? -25.677 -3.798  25.138   1.00 26.23  ? 205 LEU A C   1 
ATOM   1742  O O   . LEU A  1 205 ? -26.320 -2.745  25.058   1.00 25.86  ? 205 LEU A O   1 
ATOM   1743  C CB  . LEU A  1 205 ? -26.248 -5.280  27.082   1.00 21.88  ? 205 LEU A CB  1 
ATOM   1744  C CG  . LEU A  1 205 ? -27.276 -6.237  27.711   1.00 24.30  ? 205 LEU A CG  1 
ATOM   1745  C CD1 . LEU A  1 205 ? -26.980 -6.457  29.194   1.00 20.31  ? 205 LEU A CD1 1 
ATOM   1746  C CD2 . LEU A  1 205 ? -28.686 -5.718  27.560   1.00 22.93  ? 205 LEU A CD2 1 
ATOM   1747  N N   . ASN A  1 206 ? -24.369 -3.854  24.870   1.00 25.58  ? 206 ASN A N   1 
ATOM   1748  C CA  . ASN A  1 206 ? -23.608 -2.632  24.635   1.00 26.39  ? 206 ASN A CA  1 
ATOM   1749  C C   . ASN A  1 206 ? -22.266 -2.969  23.999   1.00 22.73  ? 206 ASN A C   1 
ATOM   1750  O O   . ASN A  1 206 ? -21.291 -3.257  24.707   1.00 20.60  ? 206 ASN A O   1 
ATOM   1751  C CB  . ASN A  1 206 ? -23.393 -1.868  25.949   1.00 31.14  ? 206 ASN A CB  1 
ATOM   1752  C CG  . ASN A  1 206 ? -22.566 -0.603  25.757   1.00 34.32  ? 206 ASN A CG  1 
ATOM   1753  O OD1 . ASN A  1 206 ? -22.223 -0.219  24.633   1.00 32.98  ? 206 ASN A OD1 1 
ATOM   1754  N ND2 . ASN A  1 206 ? -22.221 0.035   26.859   1.00 31.82  ? 206 ASN A ND2 1 
ATOM   1755  N N   . PRO A  1 207 ? -22.187 -2.942  22.669   1.00 19.76  ? 207 PRO A N   1 
ATOM   1756  C CA  . PRO A  1 207 ? -20.935 -3.304  21.983   1.00 25.94  ? 207 PRO A CA  1 
ATOM   1757  C C   . PRO A  1 207 ? -19.735 -2.463  22.378   1.00 27.11  ? 207 PRO A C   1 
ATOM   1758  O O   . PRO A  1 207 ? -18.596 -2.933  22.255   1.00 33.33  ? 207 PRO A O   1 
ATOM   1759  C CB  . PRO A  1 207 ? -21.294 -3.115  20.498   1.00 20.50  ? 207 PRO A CB  1 
ATOM   1760  C CG  . PRO A  1 207 ? -22.779 -3.351  20.459   1.00 21.88  ? 207 PRO A CG  1 
ATOM   1761  C CD  . PRO A  1 207 ? -23.315 -2.777  21.737   1.00 20.58  ? 207 PRO A CD  1 
ATOM   1762  N N   . ASN A  1 208 ? -19.946 -1.229  22.827   1.00 22.79  ? 208 ASN A N   1 
ATOM   1763  C CA  . ASN A  1 208 ? -18.833 -0.404  23.262   1.00 28.39  ? 208 ASN A CA  1 
ATOM   1764  C C   . ASN A  1 208 ? -18.172 -0.942  24.526   1.00 28.64  ? 208 ASN A C   1 
ATOM   1765  O O   . ASN A  1 208 ? -17.071 -0.499  24.860   1.00 29.55  ? 208 ASN A O   1 
ATOM   1766  C CB  . ASN A  1 208 ? -19.307 1.044   23.481   1.00 23.53  ? 208 ASN A CB  1 
ATOM   1767  C CG  . ASN A  1 208 ? -20.007 1.627   22.250   1.00 28.06  ? 208 ASN A CG  1 
ATOM   1768  O OD1 . ASN A  1 208 ? -19.589 1.408   21.119   1.00 24.91  ? 208 ASN A OD1 1 
ATOM   1769  N ND2 . ASN A  1 208 ? -21.074 2.374   22.478   1.00 35.69  ? 208 ASN A ND2 1 
ATOM   1770  N N   . CYS A  1 209 ? -18.791 -1.896  25.229   1.00 25.38  ? 209 CYS A N   1 
ATOM   1771  C CA  . CYS A  1 209 ? -18.102 -2.426  26.397   1.00 30.22  ? 209 CYS A CA  1 
ATOM   1772  C C   . CYS A  1 209 ? -16.772 -3.100  26.046   1.00 30.65  ? 209 CYS A C   1 
ATOM   1773  O O   . CYS A  1 209 ? -15.933 -3.255  26.939   1.00 26.58  ? 209 CYS A O   1 
ATOM   1774  C CB  . CYS A  1 209 ? -19.018 -3.387  27.163   1.00 28.91  ? 209 CYS A CB  1 
ATOM   1775  S SG  . CYS A  1 209 ? -19.136 -5.032  26.469   1.00 29.86  ? 209 CYS A SG  1 
ATOM   1776  N N   . VAL A  1 210 ? -16.514 -3.444  24.774   1.00 28.78  ? 210 VAL A N   1 
ATOM   1777  C CA  . VAL A  1 210 ? -15.207 -4.022  24.455   1.00 25.88  ? 210 VAL A CA  1 
ATOM   1778  C C   . VAL A  1 210 ? -14.079 -3.024  24.702   1.00 23.93  ? 210 VAL A C   1 
ATOM   1779  O O   . VAL A  1 210 ? -12.947 -3.433  24.990   1.00 28.46  ? 210 VAL A O   1 
ATOM   1780  C CB  . VAL A  1 210 ? -15.151 -4.562  23.002   1.00 30.24  ? 210 VAL A CB  1 
ATOM   1781  C CG1 . VAL A  1 210 ? -16.289 -5.559  22.744   1.00 31.50  ? 210 VAL A CG1 1 
ATOM   1782  C CG2 . VAL A  1 210 ? -15.182 -3.437  21.992   1.00 25.29  ? 210 VAL A CG2 1 
ATOM   1783  N N   . TYR A  1 211 ? -14.360 -1.722  24.636   1.00 21.69  ? 211 TYR A N   1 
ATOM   1784  C CA  . TYR A  1 211 ? -13.352 -0.689  24.848   1.00 22.34  ? 211 TYR A CA  1 
ATOM   1785  C C   . TYR A  1 211 ? -12.939 -0.526  26.313   1.00 25.98  ? 211 TYR A C   1 
ATOM   1786  O O   . TYR A  1 211 ? -12.051 0.283   26.604   1.00 25.75  ? 211 TYR A O   1 
ATOM   1787  C CB  . TYR A  1 211 ? -13.868 0.642   24.292   1.00 28.43  ? 211 TYR A CB  1 
ATOM   1788  C CG  . TYR A  1 211 ? -14.172 0.497   22.825   1.00 30.55  ? 211 TYR A CG  1 
ATOM   1789  C CD1 . TYR A  1 211 ? -13.159 0.166   21.934   1.00 33.03  ? 211 TYR A CD1 1 
ATOM   1790  C CD2 . TYR A  1 211 ? -15.466 0.609   22.339   1.00 32.55  ? 211 TYR A CD2 1 
ATOM   1791  C CE1 . TYR A  1 211 ? -13.409 -0.009  20.596   1.00 33.22  ? 211 TYR A CE1 1 
ATOM   1792  C CE2 . TYR A  1 211 ? -15.736 0.427   20.970   1.00 33.85  ? 211 TYR A CE2 1 
ATOM   1793  C CZ  . TYR A  1 211 ? -14.693 0.104   20.119   1.00 39.22  ? 211 TYR A CZ  1 
ATOM   1794  O OH  . TYR A  1 211 ? -14.893 -0.075  18.767   1.00 47.38  ? 211 TYR A OH  1 
ATOM   1795  N N   . GLU A  1 212 ? -13.551 -1.241  27.250   1.00 26.75  ? 212 GLU A N   1 
ATOM   1796  C CA  . GLU A  1 212 ? -13.045 -1.131  28.618   1.00 27.70  ? 212 GLU A CA  1 
ATOM   1797  C C   . GLU A  1 212 ? -11.706 -1.842  28.785   1.00 33.05  ? 212 GLU A C   1 
ATOM   1798  O O   . GLU A  1 212 ? -10.930 -1.486  29.682   1.00 34.85  ? 212 GLU A O   1 
ATOM   1799  C CB  . GLU A  1 212 ? -14.072 -1.682  29.610   1.00 28.23  ? 212 GLU A CB  1 
ATOM   1800  C CG  . GLU A  1 212 ? -15.418 -0.945  29.594   1.00 32.32  ? 212 GLU A CG  1 
ATOM   1801  C CD  . GLU A  1 212 ? -16.479 -1.608  30.476   1.00 42.55  ? 212 GLU A CD  1 
ATOM   1802  O OE1 . GLU A  1 212 ? -17.668 -1.603  30.095   1.00 46.05  ? 212 GLU A OE1 1 
ATOM   1803  O OE2 . GLU A  1 212 ? -16.126 -2.147  31.546   1.00 43.75  ? 212 GLU A OE2 1 
ATOM   1804  N N   . THR A  1 213 ? -11.414 -2.834  27.939   1.00 31.65  ? 213 THR A N   1 
ATOM   1805  C CA  . THR A  1 213 ? -10.189 -3.620  28.035   1.00 32.08  ? 213 THR A CA  1 
ATOM   1806  C C   . THR A  1 213 ? -9.276  -3.463  26.831   1.00 30.60  ? 213 THR A C   1 
ATOM   1807  O O   . THR A  1 213 ? -8.054  -3.478  26.986   1.00 33.18  ? 213 THR A O   1 
ATOM   1808  C CB  . THR A  1 213 ? -10.521 -5.111  28.205   1.00 34.41  ? 213 THR A CB  1 
ATOM   1809  O OG1 . THR A  1 213 ? -11.355 -5.535  27.116   1.00 31.61  ? 213 THR A OG1 1 
ATOM   1810  C CG2 . THR A  1 213 ? -11.231 -5.352  29.535   1.00 36.77  ? 213 THR A CG2 1 
ATOM   1811  N N   . THR A  1 214 ? -9.832  -3.324  25.634   1.00 28.42  ? 214 THR A N   1 
ATOM   1812  C CA  . THR A  1 214 ? -9.053  -3.278  24.391   1.00 29.19  ? 214 THR A CA  1 
ATOM   1813  C C   . THR A  1 214 ? -9.466  -2.030  23.626   1.00 31.72  ? 214 THR A C   1 
ATOM   1814  O O   . THR A  1 214 ? -10.269 -2.096  22.688   1.00 36.79  ? 214 THR A O   1 
ATOM   1815  C CB  . THR A  1 214 ? -9.263  -4.545  23.558   1.00 30.18  ? 214 THR A CB  1 
ATOM   1816  O OG1 . THR A  1 214 ? -10.662 -4.722  23.324   1.00 36.14  ? 214 THR A OG1 1 
ATOM   1817  C CG2 . THR A  1 214 ? -8.739  -5.783  24.297   1.00 27.31  ? 214 THR A CG2 1 
ATOM   1818  N N   . PRO A  1 215 ? -8.940  -0.868  24.008   1.00 35.65  ? 215 PRO A N   1 
ATOM   1819  C CA  . PRO A  1 215 ? -9.393  0.382   23.375   1.00 39.41  ? 215 PRO A CA  1 
ATOM   1820  C C   . PRO A  1 215 ? -9.086  0.484   21.885   1.00 38.97  ? 215 PRO A C   1 
ATOM   1821  O O   . PRO A  1 215 ? -9.777  1.232   21.181   1.00 40.96  ? 215 PRO A O   1 
ATOM   1822  C CB  . PRO A  1 215 ? -8.654  1.468   24.177   1.00 43.38  ? 215 PRO A CB  1 
ATOM   1823  C CG  . PRO A  1 215 ? -7.509  0.755   24.850   1.00 40.81  ? 215 PRO A CG  1 
ATOM   1824  C CD  . PRO A  1 215 ? -8.024  -0.624  25.137   1.00 36.94  ? 215 PRO A CD  1 
ATOM   1825  N N   . ASN A  1 216 ? -8.089  -0.232  21.378   1.00 35.14  ? 216 ASN A N   1 
ATOM   1826  C CA  . ASN A  1 216 ? -7.680  -0.072  19.986   1.00 38.02  ? 216 ASN A CA  1 
ATOM   1827  C C   . ASN A  1 216 ? -8.429  -0.992  19.039   1.00 41.02  ? 216 ASN A C   1 
ATOM   1828  O O   . ASN A  1 216 ? -8.181  -0.954  17.827   1.00 45.21  ? 216 ASN A O   1 
ATOM   1829  C CB  . ASN A  1 216 ? -6.176  -0.309  19.841   1.00 41.74  ? 216 ASN A CB  1 
ATOM   1830  C CG  . ASN A  1 216 ? -5.352  0.644   20.687   1.00 50.71  ? 216 ASN A CG  1 
ATOM   1831  O OD1 . ASN A  1 216 ? -4.429  0.223   21.385   1.00 53.60  ? 216 ASN A OD1 1 
ATOM   1832  N ND2 . ASN A  1 216 ? -5.674  1.939   20.621   1.00 53.76  ? 216 ASN A ND2 1 
ATOM   1833  N N   . VAL A  1 217 ? -9.332  -1.818  19.556   1.00 41.13  ? 217 VAL A N   1 
ATOM   1834  C CA  . VAL A  1 217 ? -10.006 -2.788  18.712   1.00 37.82  ? 217 VAL A CA  1 
ATOM   1835  C C   . VAL A  1 217 ? -10.941 -2.067  17.745   1.00 32.68  ? 217 VAL A C   1 
ATOM   1836  O O   . VAL A  1 217 ? -11.498 -0.999  18.044   1.00 31.24  ? 217 VAL A O   1 
ATOM   1837  C CB  . VAL A  1 217 ? -10.760 -3.815  19.579   1.00 35.67  ? 217 VAL A CB  1 
ATOM   1838  C CG1 . VAL A  1 217 ? -11.956 -3.177  20.250   1.00 36.78  ? 217 VAL A CG1 1 
ATOM   1839  C CG2 . VAL A  1 217 ? -11.196 -5.000  18.758   1.00 38.60  ? 217 VAL A CG2 1 
ATOM   1840  N N   . LYS A  1 218 ? -11.107 -2.656  16.568   1.00 32.92  ? 218 LYS A N   1 
ATOM   1841  C CA  . LYS A  1 218 ? -12.020 -2.159  15.553   1.00 29.42  ? 218 LYS A CA  1 
ATOM   1842  C C   . LYS A  1 218 ? -13.255 -3.053  15.549   1.00 26.16  ? 218 LYS A C   1 
ATOM   1843  O O   . LYS A  1 218 ? -13.143 -4.280  15.520   1.00 35.97  ? 218 LYS A O   1 
ATOM   1844  C CB  . LYS A  1 218 ? -11.348 -2.130  14.173   1.00 38.64  ? 218 LYS A CB  1 
ATOM   1845  C CG  . LYS A  1 218 ? -9.967  -1.395  14.117   1.00 51.16  ? 218 LYS A CG  1 
ATOM   1846  C CD  . LYS A  1 218 ? -8.812  -2.233  14.747   1.00 59.66  ? 218 LYS A CD  1 
ATOM   1847  C CE  . LYS A  1 218 ? -7.383  -1.759  14.442   1.00 64.03  ? 218 LYS A CE  1 
ATOM   1848  N NZ  . LYS A  1 218 ? -6.412  -2.414  15.385   1.00 62.84  ? 218 LYS A NZ  1 
ATOM   1849  N N   . ILE A  1 219 ? -14.431 -2.445  15.618   1.00 22.69  ? 219 ILE A N   1 
ATOM   1850  C CA  . ILE A  1 219 ? -15.666 -3.224  15.582   1.00 28.45  ? 219 ILE A CA  1 
ATOM   1851  C C   . ILE A  1 219 ? -16.583 -2.627  14.523   1.00 26.86  ? 219 ILE A C   1 
ATOM   1852  O O   . ILE A  1 219 ? -16.433 -1.456  14.140   1.00 28.82  ? 219 ILE A O   1 
ATOM   1853  C CB  . ILE A  1 219 ? -16.353 -3.269  16.968   1.00 29.13  ? 219 ILE A CB  1 
ATOM   1854  C CG1 . ILE A  1 219 ? -16.959 -1.911  17.314   1.00 28.74  ? 219 ILE A CG1 1 
ATOM   1855  C CG2 . ILE A  1 219 ? -15.365 -3.689  18.055   1.00 28.50  ? 219 ILE A CG2 1 
ATOM   1856  C CD1 . ILE A  1 219 ? -17.963 -2.006  18.452   1.00 27.76  ? 219 ILE A CD1 1 
ATOM   1857  N N   . PRO A  1 220 ? -17.540 -3.408  14.019   1.00 28.48  ? 220 PRO A N   1 
ATOM   1858  C CA  . PRO A  1 220 ? -18.434 -2.895  12.970   1.00 32.14  ? 220 PRO A CA  1 
ATOM   1859  C C   . PRO A  1 220 ? -19.466 -1.924  13.524   1.00 31.74  ? 220 PRO A C   1 
ATOM   1860  O O   . PRO A  1 220 ? -19.592 -1.701  14.732   1.00 31.59  ? 220 PRO A O   1 
ATOM   1861  C CB  . PRO A  1 220 ? -19.095 -4.156  12.400   1.00 31.01  ? 220 PRO A CB  1 
ATOM   1862  C CG  . PRO A  1 220 ? -18.964 -5.188  13.490   1.00 29.97  ? 220 PRO A CG  1 
ATOM   1863  C CD  . PRO A  1 220 ? -17.673 -4.868  14.196   1.00 27.23  ? 220 PRO A CD  1 
ATOM   1864  N N   . ASP A  1 221 ? -20.204 -1.325  12.593   1.00 28.20  ? 221 ASP A N   1 
ATOM   1865  C CA  . ASP A  1 221 ? -21.246 -0.343  12.895   1.00 29.19  ? 221 ASP A CA  1 
ATOM   1866  C C   . ASP A  1 221 ? -22.466 -1.099  13.429   1.00 29.73  ? 221 ASP A C   1 
ATOM   1867  O O   . ASP A  1 221 ? -23.222 -1.703  12.667   1.00 28.13  ? 221 ASP A O   1 
ATOM   1868  C CB  . ASP A  1 221 ? -21.577 0.475   11.645   1.00 29.63  ? 221 ASP A CB  1 
ATOM   1869  C CG  . ASP A  1 221 ? -22.379 1.741   11.955   1.00 33.28  ? 221 ASP A CG  1 
ATOM   1870  O OD1 . ASP A  1 221 ? -22.549 2.081   13.138   1.00 35.62  ? 221 ASP A OD1 1 
ATOM   1871  O OD2 . ASP A  1 221 ? -22.852 2.402   11.017   1.00 41.06  ? 221 ASP A OD2 1 
ATOM   1872  N N   . PHE A  1 222 ? -22.667 -1.080  14.753   1.00 26.86  ? 222 PHE A N   1 
ATOM   1873  C CA  . PHE A  1 222 ? -23.829 -1.738  15.354   1.00 23.08  ? 222 PHE A CA  1 
ATOM   1874  C C   . PHE A  1 222 ? -25.054 -0.842  15.166   1.00 32.49  ? 222 PHE A C   1 
ATOM   1875  O O   . PHE A  1 222 ? -25.503 -0.130  16.068   1.00 32.41  ? 222 PHE A O   1 
ATOM   1876  C CB  . PHE A  1 222 ? -23.560 -2.063  16.821   1.00 22.10  ? 222 PHE A CB  1 
ATOM   1877  C CG  . PHE A  1 222 ? -22.849 -3.369  17.003   1.00 25.19  ? 222 PHE A CG  1 
ATOM   1878  C CD1 . PHE A  1 222 ? -21.477 -3.457  16.811   1.00 21.85  ? 222 PHE A CD1 1 
ATOM   1879  C CD2 . PHE A  1 222 ? -23.555 -4.513  17.303   1.00 20.92  ? 222 PHE A CD2 1 
ATOM   1880  C CE1 . PHE A  1 222 ? -20.830 -4.648  16.939   1.00 20.81  ? 222 PHE A CE1 1 
ATOM   1881  C CE2 . PHE A  1 222 ? -22.905 -5.715  17.435   1.00 26.82  ? 222 PHE A CE2 1 
ATOM   1882  C CZ  . PHE A  1 222 ? -21.541 -5.783  17.249   1.00 28.23  ? 222 PHE A CZ  1 
ATOM   1883  N N   . ALA A  1 223 ? -25.611 -0.887  13.951   1.00 36.59  ? 223 ALA A N   1 
ATOM   1884  C CA  . ALA A  1 223 ? -26.708 -0.003  13.574   1.00 32.68  ? 223 ALA A CA  1 
ATOM   1885  C C   . ALA A  1 223 ? -28.075 -0.505  14.028   1.00 32.63  ? 223 ALA A C   1 
ATOM   1886  O O   . ALA A  1 223 ? -29.079 0.159   13.736   1.00 37.67  ? 223 ALA A O   1 
ATOM   1887  C CB  . ALA A  1 223 ? -26.727 0.215   12.052   1.00 30.62  ? 223 ALA A CB  1 
ATOM   1888  N N   . VAL A  1 224 ? -28.157 -1.648  14.708   1.00 27.00  ? 224 VAL A N   1 
ATOM   1889  C CA  . VAL A  1 224 ? -29.405 -2.083  15.326   1.00 28.36  ? 224 VAL A CA  1 
ATOM   1890  C C   . VAL A  1 224 ? -29.153 -2.362  16.805   1.00 24.13  ? 224 VAL A C   1 
ATOM   1891  O O   . VAL A  1 224 ? -28.013 -2.497  17.250   1.00 25.18  ? 224 VAL A O   1 
ATOM   1892  C CB  . VAL A  1 224 ? -30.002 -3.326  14.643   1.00 33.67  ? 224 VAL A CB  1 
ATOM   1893  C CG1 . VAL A  1 224 ? -30.551 -2.954  13.305   1.00 40.57  ? 224 VAL A CG1 1 
ATOM   1894  C CG2 . VAL A  1 224 ? -28.936 -4.425  14.513   1.00 38.61  ? 224 VAL A CG2 1 
ATOM   1895  N N   . SER A  1 225 ? -30.242 -2.467  17.565   1.00 26.17  ? 225 SER A N   1 
ATOM   1896  C CA  . SER A  1 225 ? -30.168 -2.798  18.989   1.00 24.09  ? 225 SER A CA  1 
ATOM   1897  C C   . SER A  1 225 ? -30.311 -4.305  19.197   1.00 24.70  ? 225 SER A C   1 
ATOM   1898  O O   . SER A  1 225 ? -31.212 -4.938  18.637   1.00 25.60  ? 225 SER A O   1 
ATOM   1899  C CB  . SER A  1 225 ? -31.253 -2.059  19.770   1.00 28.48  ? 225 SER A CB  1 
ATOM   1900  O OG  . SER A  1 225 ? -31.163 -2.327  21.160   1.00 24.64  ? 225 SER A OG  1 
ATOM   1901  N N   . PHE A  1 226 ? -29.424 -4.878  19.995   1.00 25.19  ? 226 PHE A N   1 
ATOM   1902  C CA  . PHE A  1 226 ? -29.566 -6.269  20.402   1.00 27.55  ? 226 PHE A CA  1 
ATOM   1903  C C   . PHE A  1 226 ? -30.007 -6.400  21.856   1.00 29.26  ? 226 PHE A C   1 
ATOM   1904  O O   . PHE A  1 226 ? -30.019 -7.523  22.386   1.00 22.94  ? 226 PHE A O   1 
ATOM   1905  C CB  . PHE A  1 226 ? -28.255 -7.019  20.201   1.00 30.84  ? 226 PHE A CB  1 
ATOM   1906  C CG  . PHE A  1 226 ? -27.886 -7.239  18.759   1.00 28.24  ? 226 PHE A CG  1 
ATOM   1907  C CD1 . PHE A  1 226 ? -28.428 -8.295  18.056   1.00 25.46  ? 226 PHE A CD1 1 
ATOM   1908  C CD2 . PHE A  1 226 ? -26.955 -6.431  18.137   1.00 28.42  ? 226 PHE A CD2 1 
ATOM   1909  C CE1 . PHE A  1 226 ? -28.076 -8.527  16.722   1.00 30.46  ? 226 PHE A CE1 1 
ATOM   1910  C CE2 . PHE A  1 226 ? -26.586 -6.660  16.794   1.00 28.57  ? 226 PHE A CE2 1 
ATOM   1911  C CZ  . PHE A  1 226 ? -27.147 -7.705  16.101   1.00 27.38  ? 226 PHE A CZ  1 
ATOM   1912  N N   . ARG A  1 227 ? -30.367 -5.280  22.506   1.00 23.51  ? 227 ARG A N   1 
ATOM   1913  C CA  . ARG A  1 227 ? -30.660 -5.285  23.938   1.00 31.29  ? 227 ARG A CA  1 
ATOM   1914  C C   . ARG A  1 227 ? -31.893 -6.120  24.261   1.00 30.91  ? 227 ARG A C   1 
ATOM   1915  O O   . ARG A  1 227 ? -31.936 -6.790  25.294   1.00 32.20  ? 227 ARG A O   1 
ATOM   1916  C CB  . ARG A  1 227 ? -30.857 -3.854  24.444   1.00 34.42  ? 227 ARG A CB  1 
ATOM   1917  C CG  . ARG A  1 227 ? -29.629 -2.965  24.334   1.00 33.69  ? 227 ARG A CG  1 
ATOM   1918  C CD  . ARG A  1 227 ? -29.919 -1.567  24.861   1.00 23.09  ? 227 ARG A CD  1 
ATOM   1919  N NE  . ARG A  1 227 ? -30.441 -1.608  26.224   1.00 26.74  ? 227 ARG A NE  1 
ATOM   1920  C CZ  . ARG A  1 227 ? -29.679 -1.604  27.313   1.00 33.18  ? 227 ARG A CZ  1 
ATOM   1921  N NH1 . ARG A  1 227 ? -28.356 -1.577  27.200   1.00 36.68  ? 227 ARG A NH1 1 
ATOM   1922  N NH2 . ARG A  1 227 ? -30.235 -1.627  28.517   1.00 33.91  ? 227 ARG A NH2 1 
ATOM   1923  N N   . GLU A  1 228 ? -32.931 -6.061  23.428   1.00 27.90  ? 228 GLU A N   1 
ATOM   1924  C CA  . GLU A  1 228 ? -34.079 -6.902  23.746   1.00 33.61  ? 228 GLU A CA  1 
ATOM   1925  C C   . GLU A  1 228 ? -33.816 -8.370  23.413   1.00 31.66  ? 228 GLU A C   1 
ATOM   1926  O O   . GLU A  1 228 ? -34.358 -9.255  24.082   1.00 29.83  ? 228 GLU A O   1 
ATOM   1927  C CB  . GLU A  1 228 ? -35.337 -6.388  23.046   1.00 46.10  ? 228 GLU A CB  1 
ATOM   1928  C CG  . GLU A  1 228 ? -35.974 -5.193  23.772   1.00 59.26  ? 228 GLU A CG  1 
ATOM   1929  C CD  . GLU A  1 228 ? -35.992 -5.358  25.302   1.00 69.78  ? 228 GLU A CD  1 
ATOM   1930  O OE1 . GLU A  1 228 ? -35.041 -4.899  25.978   1.00 72.25  ? 228 GLU A OE1 1 
ATOM   1931  O OE2 . GLU A  1 228 ? -36.964 -5.946  25.820   1.00 72.26  ? 228 GLU A OE2 1 
ATOM   1932  N N   . ASP A  1 229 ? -32.971 -8.656  22.416   1.00 26.29  ? 229 ASP A N   1 
ATOM   1933  C CA  . ASP A  1 229 ? -32.558 -10.040 22.198   1.00 27.18  ? 229 ASP A CA  1 
ATOM   1934  C C   . ASP A  1 229 ? -31.806 -10.581 23.412   1.00 27.99  ? 229 ASP A C   1 
ATOM   1935  O O   . ASP A  1 229 ? -31.951 -11.759 23.768   1.00 28.23  ? 229 ASP A O   1 
ATOM   1936  C CB  . ASP A  1 229 ? -31.692 -10.156 20.936   1.00 20.17  ? 229 ASP A CB  1 
ATOM   1937  C CG  . ASP A  1 229 ? -32.519 -10.269 19.673   1.00 21.12  ? 229 ASP A CG  1 
ATOM   1938  O OD1 . ASP A  1 229 ? -33.771 -10.236 19.771   1.00 24.77  ? 229 ASP A OD1 1 
ATOM   1939  O OD2 . ASP A  1 229 ? -31.916 -10.374 18.577   1.00 29.18  ? 229 ASP A OD2 1 
ATOM   1940  N N   . ALA A  1 230 ? -30.980 -9.747  24.047   1.00 22.64  ? 230 ALA A N   1 
ATOM   1941  C CA  . ALA A  1 230 ? -30.260 -10.206 25.237   1.00 25.51  ? 230 ALA A CA  1 
ATOM   1942  C C   . ALA A  1 230 ? -31.236 -10.641 26.326   1.00 23.77  ? 230 ALA A C   1 
ATOM   1943  O O   . ALA A  1 230 ? -31.081 -11.712 26.924   1.00 24.98  ? 230 ALA A O   1 
ATOM   1944  C CB  . ALA A  1 230 ? -29.331 -9.108  25.753   1.00 27.74  ? 230 ALA A CB  1 
ATOM   1945  N N   . SER A  1 231 ? -32.282 -9.852  26.542   1.00 25.54  ? 231 SER A N   1 
ATOM   1946  C CA  . SER A  1 231 ? -33.323 -10.244 27.480   1.00 29.71  ? 231 SER A CA  1 
ATOM   1947  C C   . SER A  1 231 ? -33.991 -11.544 27.074   1.00 27.16  ? 231 SER A C   1 
ATOM   1948  O O   . SER A  1 231 ? -34.347 -12.353 27.936   1.00 25.23  ? 231 SER A O   1 
ATOM   1949  C CB  . SER A  1 231 ? -34.367 -9.146  27.598   1.00 27.36  ? 231 SER A CB  1 
ATOM   1950  O OG  . SER A  1 231 ? -33.929 -8.186  28.520   1.00 32.90  ? 231 SER A OG  1 
ATOM   1951  N N   . LYS A  1 232 ? -34.216 -11.746 25.773   1.00 26.63  ? 232 LYS A N   1 
ATOM   1952  C CA  . LYS A  1 232 ? -34.942 -12.934 25.355   1.00 28.24  ? 232 LYS A CA  1 
ATOM   1953  C C   . LYS A  1 232 ? -34.102 -14.184 25.567   1.00 23.56  ? 232 LYS A C   1 
ATOM   1954  O O   . LYS A  1 232 ? -34.630 -15.231 25.956   1.00 26.21  ? 232 LYS A O   1 
ATOM   1955  C CB  . LYS A  1 232 ? -35.402 -12.802 23.896   1.00 38.37  ? 232 LYS A CB  1 
ATOM   1956  C CG  . LYS A  1 232 ? -36.609 -13.685 23.588   1.00 45.49  ? 232 LYS A CG  1 
ATOM   1957  C CD  . LYS A  1 232 ? -37.351 -13.297 22.309   1.00 50.56  ? 232 LYS A CD  1 
ATOM   1958  C CE  . LYS A  1 232 ? -38.550 -14.236 22.088   1.00 53.40  ? 232 LYS A CE  1 
ATOM   1959  N NZ  . LYS A  1 232 ? -39.264 -13.960 20.808   1.00 52.70  ? 232 LYS A NZ  1 
ATOM   1960  N N   . HIS A  1 233 ? -32.787 -14.095 25.350   1.00 21.27  ? 233 HIS A N   1 
ATOM   1961  C CA  . HIS A  1 233 ? -31.935 -15.241 25.664   1.00 23.40  ? 233 HIS A CA  1 
ATOM   1962  C C   . HIS A  1 233 ? -32.119 -15.647 27.130   1.00 26.36  ? 233 HIS A C   1 
ATOM   1963  O O   . HIS A  1 233 ? -32.240 -16.834 27.442   1.00 23.21  ? 233 HIS A O   1 
ATOM   1964  C CB  . HIS A  1 233 ? -30.459 -14.916 25.380   1.00 25.09  ? 233 HIS A CB  1 
ATOM   1965  C CG  . HIS A  1 233 ? -30.061 -14.974 23.920   1.00 23.40  ? 233 HIS A CG  1 
ATOM   1966  N ND1 . HIS A  1 233 ? -29.711 -16.147 23.277   1.00 24.30  ? 233 HIS A ND1 1 
ATOM   1967  C CD2 . HIS A  1 233 ? -29.873 -13.984 23.015   1.00 22.00  ? 233 HIS A CD2 1 
ATOM   1968  C CE1 . HIS A  1 233 ? -29.369 -15.879 22.023   1.00 25.05  ? 233 HIS A CE1 1 
ATOM   1969  N NE2 . HIS A  1 233 ? -29.458 -14.571 21.838   1.00 23.67  ? 233 HIS A NE2 1 
ATOM   1970  N N   . VAL A  1 234 ? -32.198 -14.666 28.032   1.00 22.80  ? 234 VAL A N   1 
ATOM   1971  C CA  . VAL A  1 234 ? -32.344 -14.989 29.454   1.00 23.72  ? 234 VAL A CA  1 
ATOM   1972  C C   . VAL A  1 234 ? -33.756 -15.485 29.731   1.00 24.75  ? 234 VAL A C   1 
ATOM   1973  O O   . VAL A  1 234 ? -33.954 -16.540 30.336   1.00 27.19  ? 234 VAL A O   1 
ATOM   1974  C CB  . VAL A  1 234 ? -31.973 -13.775 30.325   1.00 18.48  ? 234 VAL A CB  1 
ATOM   1975  C CG1 . VAL A  1 234 ? -32.006 -14.137 31.834   1.00 17.82  ? 234 VAL A CG1 1 
ATOM   1976  C CG2 . VAL A  1 234 ? -30.593 -13.283 29.973   1.00 20.66  ? 234 VAL A CG2 1 
ATOM   1977  N N   . GLU A  1 235 ? -34.759 -14.762 29.234   1.00 28.67  ? 235 GLU A N   1 
ATOM   1978  C CA  . GLU A  1 235 ? -36.140 -15.150 29.490   1.00 31.46  ? 235 GLU A CA  1 
ATOM   1979  C C   . GLU A  1 235 ? -36.435 -16.556 28.972   1.00 28.46  ? 235 GLU A C   1 
ATOM   1980  O O   . GLU A  1 235 ? -37.007 -17.380 29.689   1.00 28.09  ? 235 GLU A O   1 
ATOM   1981  C CB  . GLU A  1 235 ? -37.088 -14.134 28.868   1.00 38.37  ? 235 GLU A CB  1 
ATOM   1982  C CG  . GLU A  1 235 ? -38.454 -14.144 29.517   1.00 51.10  ? 235 GLU A CG  1 
ATOM   1983  C CD  . GLU A  1 235 ? -38.385 -13.798 30.992   1.00 59.25  ? 235 GLU A CD  1 
ATOM   1984  O OE1 . GLU A  1 235 ? -38.028 -12.644 31.328   1.00 61.91  ? 235 GLU A OE1 1 
ATOM   1985  O OE2 . GLU A  1 235 ? -38.688 -14.689 31.812   1.00 61.63  ? 235 GLU A OE2 1 
ATOM   1986  N N   . LEU A  1 236 ? -36.063 -16.849 27.723   1.00 25.89  ? 236 LEU A N   1 
ATOM   1987  C CA  . LEU A  1 236 ? -36.356 -18.167 27.169   1.00 26.92  ? 236 LEU A CA  1 
ATOM   1988  C C   . LEU A  1 236 ? -35.590 -19.266 27.895   1.00 23.63  ? 236 LEU A C   1 
ATOM   1989  O O   . LEU A  1 236 ? -36.088 -20.396 28.014   1.00 25.71  ? 236 LEU A O   1 
ATOM   1990  C CB  . LEU A  1 236 ? -36.032 -18.192 25.674   1.00 32.11  ? 236 LEU A CB  1 
ATOM   1991  C CG  . LEU A  1 236 ? -36.900 -17.332 24.748   1.00 31.61  ? 236 LEU A CG  1 
ATOM   1992  C CD1 . LEU A  1 236 ? -36.261 -17.222 23.374   1.00 27.95  ? 236 LEU A CD1 1 
ATOM   1993  C CD2 . LEU A  1 236 ? -38.280 -17.919 24.625   1.00 32.54  ? 236 LEU A CD2 1 
ATOM   1994  N N   . ALA A  1 237 ? -34.392 -18.955 28.397   1.00 21.28  ? 237 ALA A N   1 
ATOM   1995  C CA  . ALA A  1 237 ? -33.636 -19.925 29.183   1.00 22.40  ? 237 ALA A CA  1 
ATOM   1996  C C   . ALA A  1 237 ? -34.374 -20.280 30.468   1.00 29.30  ? 237 ALA A C   1 
ATOM   1997  O O   . ALA A  1 237 ? -34.427 -21.455 30.866   1.00 28.15  ? 237 ALA A O   1 
ATOM   1998  C CB  . ALA A  1 237 ? -32.258 -19.369 29.506   1.00 16.54  ? 237 ALA A CB  1 
ATOM   1999  N N   . LYS A  1 238 ? -34.943 -19.265 31.124   1.00 21.59  ? 238 LYS A N   1 
ATOM   2000  C CA  . LYS A  1 238 ? -35.763 -19.476 32.311   1.00 21.33  ? 238 LYS A CA  1 
ATOM   2001  C C   . LYS A  1 238 ? -36.935 -20.405 32.020   1.00 20.00  ? 238 LYS A C   1 
ATOM   2002  O O   . LYS A  1 238 ? -37.309 -21.221 32.872   1.00 26.67  ? 238 LYS A O   1 
ATOM   2003  C CB  . LYS A  1 238 ? -36.260 -18.123 32.828   1.00 30.76  ? 238 LYS A CB  1 
ATOM   2004  C CG  . LYS A  1 238 ? -35.182 -17.258 33.489   1.00 29.15  ? 238 LYS A CG  1 
ATOM   2005  C CD  . LYS A  1 238 ? -35.702 -15.870 33.819   1.00 30.23  ? 238 LYS A CD  1 
ATOM   2006  C CE  . LYS A  1 238 ? -36.933 -15.915 34.729   1.00 33.00  ? 238 LYS A CE  1 
ATOM   2007  N NZ  . LYS A  1 238 ? -37.352 -14.534 35.142   1.00 34.28  ? 238 LYS A NZ  1 
ATOM   2008  N N   . GLU A  1 239 ? -37.555 -20.274 30.838   1.00 20.34  ? 239 GLU A N   1 
ATOM   2009  C CA  . GLU A  1 239 ? -38.678 -21.142 30.477   1.00 19.27  ? 239 GLU A CA  1 
ATOM   2010  C C   . GLU A  1 239 ? -38.218 -22.578 30.252   1.00 24.41  ? 239 GLU A C   1 
ATOM   2011  O O   . GLU A  1 239 ? -38.885 -23.521 30.688   1.00 27.06  ? 239 GLU A O   1 
ATOM   2012  C CB  . GLU A  1 239 ? -39.382 -20.645 29.205   1.00 29.75  ? 239 GLU A CB  1 
ATOM   2013  C CG  . GLU A  1 239 ? -39.925 -19.224 29.258   1.00 42.80  ? 239 GLU A CG  1 
ATOM   2014  C CD  . GLU A  1 239 ? -40.497 -18.770 27.919   1.00 52.02  ? 239 GLU A CD  1 
ATOM   2015  O OE1 . GLU A  1 239 ? -40.566 -17.541 27.682   1.00 50.56  ? 239 GLU A OE1 1 
ATOM   2016  O OE2 . GLU A  1 239 ? -40.877 -19.650 27.108   1.00 54.61  ? 239 GLU A OE2 1 
ATOM   2017  N N   . LYS A  1 240 ? -37.119 -22.769 29.516   1.00 19.75  ? 240 LYS A N   1 
ATOM   2018  C CA  . LYS A  1 240 ? -36.652 -24.125 29.276   1.00 25.33  ? 240 LYS A CA  1 
ATOM   2019  C C   . LYS A  1 240 ? -36.208 -24.779 30.570   1.00 25.74  ? 240 LYS A C   1 
ATOM   2020  O O   . LYS A  1 240 ? -36.475 -25.961 30.795   1.00 26.14  ? 240 LYS A O   1 
ATOM   2021  C CB  . LYS A  1 240 ? -35.503 -24.143 28.273   1.00 23.98  ? 240 LYS A CB  1 
ATOM   2022  C CG  . LYS A  1 240 ? -35.183 -25.554 27.792   1.00 28.42  ? 240 LYS A CG  1 
ATOM   2023  C CD  . LYS A  1 240 ? -36.250 -26.081 26.815   1.00 30.89  ? 240 LYS A CD  1 
ATOM   2024  C CE  . LYS A  1 240 ? -36.062 -27.575 26.597   1.00 31.44  ? 240 LYS A CE  1 
ATOM   2025  N NZ  . LYS A  1 240 ? -37.118 -28.191 25.746   1.00 29.18  ? 240 LYS A NZ  1 
ATOM   2026  N N   . TYR A  1 241 ? -35.518 -24.029 31.427   1.00 24.85  ? 241 TYR A N   1 
ATOM   2027  C CA  . TYR A  1 241 ? -35.127 -24.572 32.727   1.00 23.31  ? 241 TYR A CA  1 
ATOM   2028  C C   . TYR A  1 241 ? -36.357 -24.908 33.563   1.00 26.07  ? 241 TYR A C   1 
ATOM   2029  O O   . TYR A  1 241 ? -36.393 -25.934 34.254   1.00 25.19  ? 241 TYR A O   1 
ATOM   2030  C CB  . TYR A  1 241 ? -34.236 -23.565 33.447   1.00 22.15  ? 241 TYR A CB  1 
ATOM   2031  C CG  . TYR A  1 241 ? -33.656 -24.052 34.749   1.00 25.37  ? 241 TYR A CG  1 
ATOM   2032  C CD1 . TYR A  1 241 ? -34.400 -23.989 35.926   1.00 20.13  ? 241 TYR A CD1 1 
ATOM   2033  C CD2 . TYR A  1 241 ? -32.369 -24.570 34.814   1.00 20.02  ? 241 TYR A CD2 1 
ATOM   2034  C CE1 . TYR A  1 241 ? -33.879 -24.428 37.133   1.00 21.02  ? 241 TYR A CE1 1 
ATOM   2035  C CE2 . TYR A  1 241 ? -31.838 -25.006 36.041   1.00 21.44  ? 241 TYR A CE2 1 
ATOM   2036  C CZ  . TYR A  1 241 ? -32.600 -24.937 37.185   1.00 21.64  ? 241 TYR A CZ  1 
ATOM   2037  O OH  . TYR A  1 241 ? -32.101 -25.369 38.406   1.00 25.64  ? 241 TYR A OH  1 
ATOM   2038  N N   . PHE A  1 242 ? -37.381 -24.056 33.510   1.00 24.83  ? 242 PHE A N   1 
ATOM   2039  C CA  . PHE A  1 242 ? -38.595 -24.344 34.263   1.00 26.63  ? 242 PHE A CA  1 
ATOM   2040  C C   . PHE A  1 242 ? -39.246 -25.634 33.785   1.00 23.15  ? 242 PHE A C   1 
ATOM   2041  O O   . PHE A  1 242 ? -39.754 -26.423 34.593   1.00 27.75  ? 242 PHE A O   1 
ATOM   2042  C CB  . PHE A  1 242 ? -39.585 -23.184 34.162   1.00 18.68  ? 242 PHE A CB  1 
ATOM   2043  C CG  . PHE A  1 242 ? -40.857 -23.435 34.915   1.00 20.90  ? 242 PHE A CG  1 
ATOM   2044  C CD1 . PHE A  1 242 ? -41.922 -24.084 34.311   1.00 20.10  ? 242 PHE A CD1 1 
ATOM   2045  C CD2 . PHE A  1 242 ? -40.964 -23.061 36.248   1.00 24.42  ? 242 PHE A CD2 1 
ATOM   2046  C CE1 . PHE A  1 242 ? -43.092 -24.343 35.021   1.00 20.71  ? 242 PHE A CE1 1 
ATOM   2047  C CE2 . PHE A  1 242 ? -42.121 -23.315 36.965   1.00 24.21  ? 242 PHE A CE2 1 
ATOM   2048  C CZ  . PHE A  1 242 ? -43.183 -23.958 36.355   1.00 25.19  ? 242 PHE A CZ  1 
ATOM   2049  N N   . GLU A  1 243 ? -39.258 -25.859 32.471   1.00 24.16  ? 243 GLU A N   1 
ATOM   2050  C CA  . GLU A  1 243 ? -39.802 -27.104 31.943   1.00 28.87  ? 243 GLU A CA  1 
ATOM   2051  C C   . GLU A  1 243 ? -39.035 -28.309 32.469   1.00 27.46  ? 243 GLU A C   1 
ATOM   2052  O O   . GLU A  1 243 ? -39.633 -29.330 32.829   1.00 24.19  ? 243 GLU A O   1 
ATOM   2053  C CB  . GLU A  1 243 ? -39.770 -27.088 30.407   1.00 30.90  ? 243 GLU A CB  1 
ATOM   2054  C CG  . GLU A  1 243 ? -40.412 -28.315 29.773   1.00 32.08  ? 243 GLU A CG  1 
ATOM   2055  C CD  . GLU A  1 243 ? -39.836 -28.676 28.415   1.00 36.92  ? 243 GLU A CD  1 
ATOM   2056  O OE1 . GLU A  1 243 ? -40.085 -29.814 27.981   1.00 41.45  ? 243 GLU A OE1 1 
ATOM   2057  O OE2 . GLU A  1 243 ? -39.122 -27.854 27.796   1.00 36.42  ? 243 GLU A OE2 1 
ATOM   2058  N N   . ILE A  1 244 ? -37.711 -28.217 32.522   1.00 24.97  ? 244 ILE A N   1 
ATOM   2059  C CA  . ILE A  1 244 ? -36.932 -29.407 32.833   1.00 28.83  ? 244 ILE A CA  1 
ATOM   2060  C C   . ILE A  1 244 ? -36.848 -29.636 34.334   1.00 27.69  ? 244 ILE A C   1 
ATOM   2061  O O   . ILE A  1 244 ? -36.873 -30.784 34.790   1.00 29.04  ? 244 ILE A O   1 
ATOM   2062  C CB  . ILE A  1 244 ? -35.537 -29.307 32.196   1.00 27.89  ? 244 ILE A CB  1 
ATOM   2063  C CG1 . ILE A  1 244 ? -35.680 -29.120 30.682   1.00 24.38  ? 244 ILE A CG1 1 
ATOM   2064  C CG2 . ILE A  1 244 ? -34.759 -30.583 32.458   1.00 27.36  ? 244 ILE A CG2 1 
ATOM   2065  C CD1 . ILE A  1 244 ? -36.388 -30.281 30.006   1.00 26.82  ? 244 ILE A CD1 1 
ATOM   2066  N N   . PHE A  1 245 ? -36.716 -28.566 35.121   1.00 25.40  ? 245 PHE A N   1 
ATOM   2067  C CA  . PHE A  1 245 ? -36.440 -28.700 36.553   1.00 26.82  ? 245 PHE A CA  1 
ATOM   2068  C C   . PHE A  1 245 ? -37.527 -28.131 37.447   1.00 29.63  ? 245 PHE A C   1 
ATOM   2069  O O   . PHE A  1 245 ? -37.430 -28.252 38.678   1.00 29.53  ? 245 PHE A O   1 
ATOM   2070  C CB  . PHE A  1 245 ? -35.091 -28.056 36.895   1.00 20.02  ? 245 PHE A CB  1 
ATOM   2071  C CG  . PHE A  1 245 ? -33.956 -28.646 36.135   1.00 25.28  ? 245 PHE A CG  1 
ATOM   2072  C CD1 . PHE A  1 245 ? -33.503 -29.928 36.438   1.00 27.31  ? 245 PHE A CD1 1 
ATOM   2073  C CD2 . PHE A  1 245 ? -33.373 -27.967 35.074   1.00 28.36  ? 245 PHE A CD2 1 
ATOM   2074  C CE1 . PHE A  1 245 ? -32.484 -30.508 35.717   1.00 28.51  ? 245 PHE A CE1 1 
ATOM   2075  C CE2 . PHE A  1 245 ? -32.330 -28.543 34.354   1.00 26.03  ? 245 PHE A CE2 1 
ATOM   2076  C CZ  . PHE A  1 245 ? -31.889 -29.808 34.672   1.00 30.30  ? 245 PHE A CZ  1 
ATOM   2077  N N   . GLY A  1 246 ? -38.560 -27.524 36.873   1.00 29.99  ? 246 GLY A N   1 
ATOM   2078  C CA  . GLY A  1 246 ? -39.738 -27.162 37.633   1.00 30.54  ? 246 GLY A CA  1 
ATOM   2079  C C   . GLY A  1 246 ? -39.618 -25.939 38.507   1.00 28.64  ? 246 GLY A C   1 
ATOM   2080  O O   . GLY A  1 246 ? -40.416 -25.782 39.443   1.00 24.10  ? 246 GLY A O   1 
ATOM   2081  N N   . GLU A  1 247 ? -38.620 -25.097 38.262   1.00 30.97  ? 247 GLU A N   1 
ATOM   2082  C CA  . GLU A  1 247 ? -38.466 -23.819 38.938   1.00 33.03  ? 247 GLU A CA  1 
ATOM   2083  C C   . GLU A  1 247 ? -37.814 -22.864 37.961   1.00 28.72  ? 247 GLU A C   1 
ATOM   2084  O O   . GLU A  1 247 ? -37.128 -23.284 37.028   1.00 29.60  ? 247 GLU A O   1 
ATOM   2085  C CB  . GLU A  1 247 ? -37.577 -23.893 40.195   1.00 34.84  ? 247 GLU A CB  1 
ATOM   2086  C CG  . GLU A  1 247 ? -37.507 -25.232 40.899   1.00 41.49  ? 247 GLU A CG  1 
ATOM   2087  C CD  . GLU A  1 247 ? -36.383 -25.289 41.917   1.00 43.91  ? 247 GLU A CD  1 
ATOM   2088  O OE1 . GLU A  1 247 ? -35.213 -25.102 41.525   1.00 40.15  ? 247 GLU A OE1 1 
ATOM   2089  O OE2 . GLU A  1 247 ? -36.676 -25.500 43.118   1.00 49.72  ? 247 GLU A OE2 1 
ATOM   2090  N N   . HIS A  1 248 ? -37.998 -21.586 38.202   1.00 27.32  ? 248 HIS A N   1 
ATOM   2091  C CA  . HIS A  1 248 ? -37.149 -20.667 37.462   1.00 28.54  ? 248 HIS A CA  1 
ATOM   2092  C C   . HIS A  1 248 ? -35.730 -20.715 38.038   1.00 24.65  ? 248 HIS A C   1 
ATOM   2093  O O   . HIS A  1 248 ? -35.556 -20.905 39.245   1.00 27.53  ? 248 HIS A O   1 
ATOM   2094  C CB  . HIS A  1 248 ? -37.727 -19.249 37.519   1.00 30.84  ? 248 HIS A CB  1 
ATOM   2095  C CG  . HIS A  1 248 ? -38.988 -19.097 36.722   1.00 40.28  ? 248 HIS A CG  1 
ATOM   2096  N ND1 . HIS A  1 248 ? -40.198 -18.754 37.290   1.00 45.57  ? 248 HIS A ND1 1 
ATOM   2097  C CD2 . HIS A  1 248 ? -39.233 -19.286 35.403   1.00 42.68  ? 248 HIS A CD2 1 
ATOM   2098  C CE1 . HIS A  1 248 ? -41.130 -18.724 36.354   1.00 43.69  ? 248 HIS A CE1 1 
ATOM   2099  N NE2 . HIS A  1 248 ? -40.570 -19.042 35.199   1.00 45.16  ? 248 HIS A NE2 1 
ATOM   2100  N N   . PRO A  1 249 ? -34.701 -20.602 37.198   1.00 23.54  ? 249 PRO A N   1 
ATOM   2101  C CA  . PRO A  1 249 ? -33.322 -20.752 37.695   1.00 25.16  ? 249 PRO A CA  1 
ATOM   2102  C C   . PRO A  1 249 ? -32.874 -19.525 38.480   1.00 25.84  ? 249 PRO A C   1 
ATOM   2103  O O   . PRO A  1 249 ? -33.053 -18.385 38.049   1.00 30.40  ? 249 PRO A O   1 
ATOM   2104  C CB  . PRO A  1 249 ? -32.496 -20.936 36.414   1.00 22.58  ? 249 PRO A CB  1 
ATOM   2105  C CG  . PRO A  1 249 ? -33.328 -20.229 35.336   1.00 19.81  ? 249 PRO A CG  1 
ATOM   2106  C CD  . PRO A  1 249 ? -34.768 -20.450 35.730   1.00 21.47  ? 249 PRO A CD  1 
ATOM   2107  N N   . VAL A  1 250 ? -32.293 -19.754 39.653   1.00 27.62  ? 250 VAL A N   1 
ATOM   2108  C CA  . VAL A  1 250 ? -31.753 -18.626 40.400   1.00 29.35  ? 250 VAL A CA  1 
ATOM   2109  C C   . VAL A  1 250 ? -30.245 -18.518 40.240   1.00 25.54  ? 250 VAL A C   1 
ATOM   2110  O O   . VAL A  1 250 ? -29.672 -17.492 40.636   1.00 23.29  ? 250 VAL A O   1 
ATOM   2111  C CB  . VAL A  1 250 ? -32.157 -18.679 41.884   1.00 31.68  ? 250 VAL A CB  1 
ATOM   2112  C CG1 . VAL A  1 250 ? -33.680 -18.513 42.003   1.00 30.88  ? 250 VAL A CG1 1 
ATOM   2113  C CG2 . VAL A  1 250 ? -31.689 -19.958 42.511   1.00 31.25  ? 250 VAL A CG2 1 
ATOM   2114  N N   . TYR A  1 251 ? -29.598 -19.516 39.623   1.00 19.46  ? 251 TYR A N   1 
ATOM   2115  C CA  . TYR A  1 251 ? -28.181 -19.475 39.280   1.00 18.24  ? 251 TYR A CA  1 
ATOM   2116  C C   . TYR A  1 251 ? -28.029 -19.513 37.768   1.00 21.71  ? 251 TYR A C   1 
ATOM   2117  O O   . TYR A  1 251 ? -28.712 -20.283 37.093   1.00 23.38  ? 251 TYR A O   1 
ATOM   2118  C CB  . TYR A  1 251 ? -27.401 -20.666 39.891   1.00 24.44  ? 251 TYR A CB  1 
ATOM   2119  C CG  . TYR A  1 251 ? -27.768 -20.877 41.336   1.00 31.20  ? 251 TYR A CG  1 
ATOM   2120  C CD1 . TYR A  1 251 ? -27.167 -20.127 42.323   1.00 36.94  ? 251 TYR A CD1 1 
ATOM   2121  C CD2 . TYR A  1 251 ? -28.742 -21.793 41.702   1.00 38.96  ? 251 TYR A CD2 1 
ATOM   2122  C CE1 . TYR A  1 251 ? -27.508 -20.296 43.641   1.00 42.77  ? 251 TYR A CE1 1 
ATOM   2123  C CE2 . TYR A  1 251 ? -29.093 -21.963 43.030   1.00 41.88  ? 251 TYR A CE2 1 
ATOM   2124  C CZ  . TYR A  1 251 ? -28.478 -21.201 43.991   1.00 43.75  ? 251 TYR A CZ  1 
ATOM   2125  O OH  . TYR A  1 251 ? -28.830 -21.338 45.315   1.00 43.01  ? 251 TYR A OH  1 
ATOM   2126  N N   . MET A  1 252 ? -27.104 -18.715 37.243   1.00 17.25  ? 252 MET A N   1 
ATOM   2127  C CA  . MET A  1 252 ? -26.750 -18.838 35.842   1.00 16.15  ? 252 MET A CA  1 
ATOM   2128  C C   . MET A  1 252 ? -25.240 -18.800 35.711   1.00 21.32  ? 252 MET A C   1 
ATOM   2129  O O   . MET A  1 252 ? -24.538 -18.195 36.527   1.00 23.88  ? 252 MET A O   1 
ATOM   2130  C CB  . MET A  1 252 ? -27.396 -17.730 34.987   1.00 22.03  ? 252 MET A CB  1 
ATOM   2131  C CG  . MET A  1 252 ? -28.829 -18.035 34.561   1.00 27.02  ? 252 MET A CG  1 
ATOM   2132  S SD  . MET A  1 252 ? -29.496 -16.984 33.232   1.00 28.79  ? 252 MET A SD  1 
ATOM   2133  C CE  . MET A  1 252 ? -31.167 -17.636 33.109   1.00 28.78  ? 252 MET A CE  1 
ATOM   2134  N N   . TRP A  1 253 ? -24.744 -19.475 34.681   1.00 23.26  ? 253 TRP A N   1 
ATOM   2135  C CA  . TRP A  1 253 ? -23.359 -19.324 34.280   1.00 18.48  ? 253 TRP A CA  1 
ATOM   2136  C C   . TRP A  1 253 ? -23.344 -18.417 33.071   1.00 22.06  ? 253 TRP A C   1 
ATOM   2137  O O   . TRP A  1 253 ? -23.950 -18.783 32.047   1.00 20.15  ? 253 TRP A O   1 
ATOM   2138  C CB  . TRP A  1 253 ? -22.719 -20.667 33.933   1.00 16.58  ? 253 TRP A CB  1 
ATOM   2139  C CG  . TRP A  1 253 ? -21.404 -20.484 33.195   1.00 16.59  ? 253 TRP A CG  1 
ATOM   2140  C CD1 . TRP A  1 253 ? -21.152 -20.734 31.870   1.00 18.82  ? 253 TRP A CD1 1 
ATOM   2141  C CD2 . TRP A  1 253 ? -20.198 -19.967 33.747   1.00 17.20  ? 253 TRP A CD2 1 
ATOM   2142  N NE1 . TRP A  1 253 ? -19.840 -20.415 31.579   1.00 20.24  ? 253 TRP A NE1 1 
ATOM   2143  C CE2 . TRP A  1 253 ? -19.242 -19.936 32.719   1.00 16.54  ? 253 TRP A CE2 1 
ATOM   2144  C CE3 . TRP A  1 253 ? -19.830 -19.537 35.033   1.00 21.31  ? 253 TRP A CE3 1 
ATOM   2145  C CZ2 . TRP A  1 253 ? -17.936 -19.499 32.932   1.00 20.35  ? 253 TRP A CZ2 1 
ATOM   2146  C CZ3 . TRP A  1 253 ? -18.548 -19.100 35.243   1.00 23.06  ? 253 TRP A CZ3 1 
ATOM   2147  C CH2 . TRP A  1 253 ? -17.609 -19.078 34.199   1.00 20.33  ? 253 TRP A CH2 1 
ATOM   2148  N N   . PRO A  1 254 ? -22.737 -17.232 33.148   1.00 20.54  ? 254 PRO A N   1 
ATOM   2149  C CA  . PRO A  1 254 ? -22.642 -16.373 31.972   1.00 19.21  ? 254 PRO A CA  1 
ATOM   2150  C C   . PRO A  1 254 ? -21.696 -16.973 30.953   1.00 23.20  ? 254 PRO A C   1 
ATOM   2151  O O   . PRO A  1 254 ? -20.538 -17.296 31.282   1.00 23.32  ? 254 PRO A O   1 
ATOM   2152  C CB  . PRO A  1 254 ? -22.099 -15.045 32.534   1.00 16.79  ? 254 PRO A CB  1 
ATOM   2153  C CG  . PRO A  1 254 ? -21.350 -15.441 33.782   1.00 19.35  ? 254 PRO A CG  1 
ATOM   2154  C CD  . PRO A  1 254 ? -22.099 -16.635 34.336   1.00 19.67  ? 254 PRO A CD  1 
ATOM   2155  N N   . PRO A  1 255 ? -22.150 -17.128 29.707   1.00 21.40  ? 255 PRO A N   1 
ATOM   2156  C CA  . PRO A  1 255 ? -21.275 -17.658 28.662   1.00 17.54  ? 255 PRO A CA  1 
ATOM   2157  C C   . PRO A  1 255 ? -19.942 -16.940 28.657   1.00 16.95  ? 255 PRO A C   1 
ATOM   2158  O O   . PRO A  1 255 ? -19.876 -15.704 28.716   1.00 18.13  ? 255 PRO A O   1 
ATOM   2159  C CB  . PRO A  1 255 ? -22.072 -17.402 27.373   1.00 19.44  ? 255 PRO A CB  1 
ATOM   2160  C CG  . PRO A  1 255 ? -23.495 -17.483 27.815   1.00 20.22  ? 255 PRO A CG  1 
ATOM   2161  C CD  . PRO A  1 255 ? -23.519 -16.888 29.206   1.00 21.34  ? 255 PRO A CD  1 
ATOM   2162  N N   . GLU A  1 256 ? -18.905 -17.697 28.603   1.00 15.15  ? 256 GLU A N   1 
ATOM   2163  C CA  . GLU A  1 256 ? -17.547 -17.162 28.588   1.00 17.85  ? 256 GLU A CA  1 
ATOM   2164  C C   . GLU A  1 256 ? -17.198 -16.395 29.860   1.00 17.84  ? 256 GLU A C   1 
ATOM   2165  O O   . GLU A  1 256 ? -16.297 -15.630 29.840   1.00 19.17  ? 256 GLU A O   1 
ATOM   2166  C CB  . GLU A  1 256 ? -17.258 -16.409 27.263   1.00 23.88  ? 256 GLU A CB  1 
ATOM   2167  C CG  . GLU A  1 256 ? -17.648 -17.125 25.997   1.00 23.45  ? 256 GLU A CG  1 
ATOM   2168  C CD  . GLU A  1 256 ? -16.963 -18.455 25.835   1.00 25.14  ? 256 GLU A CD  1 
ATOM   2169  O OE1 . GLU A  1 256 ? -15.950 -18.709 26.451   1.00 31.81  ? 256 GLU A OE1 1 
ATOM   2170  O OE2 . GLU A  1 256 ? -17.448 -19.264 25.082   1.00 30.21  ? 256 GLU A OE2 1 
ATOM   2171  N N   . ALA A  1 257 ? -17.840 -16.718 30.976   1.00 17.12  ? 257 ALA A N   1 
ATOM   2172  C CA  . ALA A  1 257 ? -17.697 -15.956 32.220   1.00 14.82  ? 257 ALA A CA  1 
ATOM   2173  C C   . ALA A  1 257 ? -17.954 -14.477 32.006   1.00 19.72  ? 257 ALA A C   1 
ATOM   2174  O O   . ALA A  1 257 ? -17.526 -13.654 32.807   1.00 16.81  ? 257 ALA A O   1 
ATOM   2175  C CB  . ALA A  1 257 ? -16.312 -16.130 32.854   1.00 15.11  ? 257 ALA A CB  1 
ATOM   2176  N N   A SER A  1 258 ? -18.635 -14.117 30.920   0.24 21.35  ? 258 SER A N   1 
ATOM   2177  N N   B SER A  1 258 ? -18.658 -14.120 30.937   0.76 20.73  ? 258 SER A N   1 
ATOM   2178  C CA  A SER A  1 258 ? -18.652 -12.737 30.450   0.24 22.83  ? 258 SER A CA  1 
ATOM   2179  C CA  B SER A  1 258 ? -18.649 -12.742 30.487   0.76 23.86  ? 258 SER A CA  1 
ATOM   2180  C C   A SER A  1 258 ? -19.640 -11.911 31.259   0.24 22.98  ? 258 SER A C   1 
ATOM   2181  C C   B SER A  1 258 ? -19.647 -11.904 31.261   0.76 22.98  ? 258 SER A C   1 
ATOM   2182  O O   A SER A  1 258 ? -20.827 -12.248 31.335   0.24 24.40  ? 258 SER A O   1 
ATOM   2183  O O   B SER A  1 258 ? -20.846 -12.206 31.292   0.76 25.28  ? 258 SER A O   1 
ATOM   2184  C CB  A SER A  1 258 ? -19.006 -12.684 28.964   0.24 21.85  ? 258 SER A CB  1 
ATOM   2185  C CB  B SER A  1 258 ? -18.946 -12.655 28.987   0.76 21.77  ? 258 SER A CB  1 
ATOM   2186  O OG  A SER A  1 258 ? -20.370 -13.006 28.766   0.24 20.86  ? 258 SER A OG  1 
ATOM   2187  O OG  B SER A  1 258 ? -18.910 -11.297 28.606   0.76 20.39  ? 258 SER A OG  1 
ATOM   2188  N N   . VAL A  1 259 ? -19.157 -10.814 31.844   1.00 19.33  ? 259 VAL A N   1 
ATOM   2189  C CA  . VAL A  1 259 ? -19.994 -9.909  32.610   1.00 21.64  ? 259 VAL A CA  1 
ATOM   2190  C C   . VAL A  1 259 ? -19.613 -8.478  32.259   1.00 25.59  ? 259 VAL A C   1 
ATOM   2191  O O   . VAL A  1 259 ? -18.554 -8.203  31.685   1.00 25.06  ? 259 VAL A O   1 
ATOM   2192  C CB  . VAL A  1 259 ? -19.878 -10.161 34.146   1.00 20.02  ? 259 VAL A CB  1 
ATOM   2193  C CG1 . VAL A  1 259 ? -20.329 -11.563 34.480   1.00 19.62  ? 259 VAL A CG1 1 
ATOM   2194  C CG2 . VAL A  1 259 ? -18.454 -10.008 34.604   1.00 18.13  ? 259 VAL A CG2 1 
ATOM   2195  N N   . SER A  1 260 ? -20.522 -7.577  32.591   1.00 16.34  ? 260 SER A N   1 
ATOM   2196  C CA  . SER A  1 260 ? -20.339 -6.135  32.529   1.00 19.90  ? 260 SER A CA  1 
ATOM   2197  C C   . SER A  1 260 ? -21.319 -5.547  33.534   1.00 20.60  ? 260 SER A C   1 
ATOM   2198  O O   . SER A  1 260 ? -22.189 -6.254  34.046   1.00 25.21  ? 260 SER A O   1 
ATOM   2199  C CB  . SER A  1 260 ? -20.592 -5.596  31.114   1.00 23.51  ? 260 SER A CB  1 
ATOM   2200  O OG  . SER A  1 260 ? -21.968 -5.663  30.786   1.00 21.16  ? 260 SER A OG  1 
ATOM   2201  N N   . ASN A  1 261 ? -21.178 -4.250  33.828   1.00 20.48  ? 261 ASN A N   1 
ATOM   2202  C CA  . ASN A  1 261 ? -22.167 -3.619  34.703   1.00 23.10  ? 261 ASN A CA  1 
ATOM   2203  C C   . ASN A  1 261 ? -23.584 -3.816  34.172   1.00 23.09  ? 261 ASN A C   1 
ATOM   2204  O O   . ASN A  1 261 ? -24.500 -4.147  34.932   1.00 21.76  ? 261 ASN A O   1 
ATOM   2205  C CB  . ASN A  1 261 ? -21.851 -2.130  34.873   1.00 19.77  ? 261 ASN A CB  1 
ATOM   2206  C CG  . ASN A  1 261 ? -20.568 -1.899  35.637   1.00 23.08  ? 261 ASN A CG  1 
ATOM   2207  O OD1 . ASN A  1 261 ? -20.099 -2.776  36.362   1.00 23.32  ? 261 ASN A OD1 1 
ATOM   2208  N ND2 . ASN A  1 261 ? -19.966 -0.745  35.440   1.00 26.25  ? 261 ASN A ND2 1 
ATOM   2209  N N   . GLU A  1 262 ? -23.784 -3.646  32.862   1.00 21.42  ? 262 GLU A N   1 
ATOM   2210  C CA  . GLU A  1 262 ? -25.125 -3.750  32.295   1.00 20.10  ? 262 GLU A CA  1 
ATOM   2211  C C   . GLU A  1 262 ? -25.622 -5.187  32.271   1.00 21.29  ? 262 GLU A C   1 
ATOM   2212  O O   . GLU A  1 262 ? -26.819 -5.435  32.459   1.00 23.75  ? 262 GLU A O   1 
ATOM   2213  C CB  . GLU A  1 262 ? -25.143 -3.156  30.882   1.00 24.28  ? 262 GLU A CB  1 
ATOM   2214  C CG  . GLU A  1 262 ? -24.900 -1.631  30.851   1.00 25.27  ? 262 GLU A CG  1 
ATOM   2215  C CD  . GLU A  1 262 ? -25.127 -1.035  29.474   1.00 33.16  ? 262 GLU A CD  1 
ATOM   2216  O OE1 . GLU A  1 262 ? -26.209 -1.285  28.896   1.00 29.57  ? 262 GLU A OE1 1 
ATOM   2217  O OE2 . GLU A  1 262 ? -24.218 -0.326  28.976   1.00 36.93  ? 262 GLU A OE2 1 
ATOM   2218  N N   . ALA A  1 263 ? -24.732 -6.155  32.047   1.00 23.84  ? 263 ALA A N   1 
ATOM   2219  C CA  . ALA A  1 263 ? -25.196 -7.537  32.026   1.00 23.05  ? 263 ALA A CA  1 
ATOM   2220  C C   . ALA A  1 263 ? -25.548 -8.007  33.434   1.00 22.84  ? 263 ALA A C   1 
ATOM   2221  O O   . ALA A  1 263 ? -26.522 -8.750  33.623   1.00 26.88  ? 263 ALA A O   1 
ATOM   2222  C CB  . ALA A  1 263 ? -24.151 -8.445  31.378   1.00 23.23  ? 263 ALA A CB  1 
ATOM   2223  N N   . LEU A  1 264 ? -24.786 -7.557  34.436   1.00 18.55  ? 264 LEU A N   1 
ATOM   2224  C CA  . LEU A  1 264 ? -25.106 -7.907  35.821   1.00 21.88  ? 264 LEU A CA  1 
ATOM   2225  C C   . LEU A  1 264 ? -26.473 -7.382  36.227   1.00 25.75  ? 264 LEU A C   1 
ATOM   2226  O O   . LEU A  1 264 ? -27.223 -8.064  36.944   1.00 25.81  ? 264 LEU A O   1 
ATOM   2227  C CB  . LEU A  1 264 ? -24.029 -7.359  36.750   1.00 20.39  ? 264 LEU A CB  1 
ATOM   2228  C CG  . LEU A  1 264 ? -22.747 -8.172  36.624   1.00 26.69  ? 264 LEU A CG  1 
ATOM   2229  C CD1 . LEU A  1 264 ? -21.665 -7.594  37.504   1.00 32.64  ? 264 LEU A CD1 1 
ATOM   2230  C CD2 . LEU A  1 264 ? -23.053 -9.599  36.991   1.00 27.55  ? 264 LEU A CD2 1 
ATOM   2231  N N   . GLU A  1 265 ? -26.804 -6.159  35.786   1.00 22.73  ? 265 GLU A N   1 
ATOM   2232  C CA  . GLU A  1 265 ? -28.120 -5.584  36.033   1.00 27.55  ? 265 GLU A CA  1 
ATOM   2233  C C   . GLU A  1 265 ? -29.223 -6.396  35.365   1.00 28.15  ? 265 GLU A C   1 
ATOM   2234  O O   . GLU A  1 265 ? -30.260 -6.660  35.988   1.00 29.50  ? 265 GLU A O   1 
ATOM   2235  C CB  . GLU A  1 265 ? -28.154 -4.115  35.568   1.00 32.86  ? 265 GLU A CB  1 
ATOM   2236  C CG  . GLU A  1 265 ? -27.036 -3.263  36.197   1.00 49.11  ? 265 GLU A CG  1 
ATOM   2237  C CD  . GLU A  1 265 ? -27.515 -1.961  36.846   1.00 60.77  ? 265 GLU A CD  1 
ATOM   2238  O OE1 . GLU A  1 265 ? -27.107 -1.672  38.001   1.00 57.60  ? 265 GLU A OE1 1 
ATOM   2239  O OE2 . GLU A  1 265 ? -28.290 -1.225  36.200   1.00 67.74  ? 265 GLU A OE2 1 
ATOM   2240  N N   . LEU A  1 266 ? -29.015 -6.809  34.105   1.00 25.97  ? 266 LEU A N   1 
ATOM   2241  C CA  . LEU A  1 266 ? -30.012 -7.609  33.396   1.00 29.38  ? 266 LEU A CA  1 
ATOM   2242  C C   . LEU A  1 266 ? -30.274 -8.927  34.116   1.00 26.08  ? 266 LEU A C   1 
ATOM   2243  O O   . LEU A  1 266 ? -31.431 -9.324  34.299   1.00 27.82  ? 266 LEU A O   1 
ATOM   2244  C CB  . LEU A  1 266 ? -29.575 -7.867  31.946   1.00 27.21  ? 266 LEU A CB  1 
ATOM   2245  C CG  . LEU A  1 266 ? -30.418 -8.858  31.125   1.00 27.19  ? 266 LEU A CG  1 
ATOM   2246  C CD1 . LEU A  1 266 ? -31.841 -8.355  30.959   1.00 32.82  ? 266 LEU A CD1 1 
ATOM   2247  C CD2 . LEU A  1 266 ? -29.818 -9.122  29.752   1.00 26.77  ? 266 LEU A CD2 1 
ATOM   2248  N N   . TYR A  1 267 ? -29.208 -9.625  34.524   1.00 22.24  ? 267 TYR A N   1 
ATOM   2249  C CA  . TYR A  1 267 ? -29.392 -10.882 35.245   1.00 25.11  ? 267 TYR A CA  1 
ATOM   2250  C C   . TYR A  1 267 ? -30.170 -10.657 36.536   1.00 28.01  ? 267 TYR A C   1 
ATOM   2251  O O   . TYR A  1 267 ? -31.078 -11.435 36.863   1.00 29.34  ? 267 TYR A O   1 
ATOM   2252  C CB  . TYR A  1 267 ? -28.041 -11.536 35.545   1.00 24.60  ? 267 TYR A CB  1 
ATOM   2253  C CG  . TYR A  1 267 ? -27.371 -12.220 34.371   1.00 23.42  ? 267 TYR A CG  1 
ATOM   2254  C CD1 . TYR A  1 267 ? -27.982 -13.287 33.710   1.00 26.46  ? 267 TYR A CD1 1 
ATOM   2255  C CD2 . TYR A  1 267 ? -26.107 -11.821 33.951   1.00 21.37  ? 267 TYR A CD2 1 
ATOM   2256  C CE1 . TYR A  1 267 ? -27.355 -13.915 32.635   1.00 24.83  ? 267 TYR A CE1 1 
ATOM   2257  C CE2 . TYR A  1 267 ? -25.482 -12.426 32.904   1.00 25.92  ? 267 TYR A CE2 1 
ATOM   2258  C CZ  . TYR A  1 267 ? -26.107 -13.471 32.241   1.00 29.05  ? 267 TYR A CZ  1 
ATOM   2259  O OH  . TYR A  1 267 ? -25.454 -14.071 31.196   1.00 29.82  ? 267 TYR A OH  1 
ATOM   2260  N N   . TYR A  1 268 ? -29.847 -9.583  37.273   1.00 22.67  ? 268 TYR A N   1 
ATOM   2261  C CA  . TYR A  1 268 ? -30.615 -9.254  38.471   1.00 25.43  ? 268 TYR A CA  1 
ATOM   2262  C C   . TYR A  1 268 ? -32.075 -9.015  38.122   1.00 27.28  ? 268 TYR A C   1 
ATOM   2263  O O   . TYR A  1 268 ? -32.977 -9.544  38.786   1.00 25.81  ? 268 TYR A O   1 
ATOM   2264  C CB  . TYR A  1 268 ? -30.023 -8.025  39.179   1.00 25.06  ? 268 TYR A CB  1 
ATOM   2265  C CG  . TYR A  1 268 ? -31.052 -7.179  39.892   1.00 27.61  ? 268 TYR A CG  1 
ATOM   2266  C CD1 . TYR A  1 268 ? -31.561 -7.563  41.135   1.00 28.31  ? 268 TYR A CD1 1 
ATOM   2267  C CD2 . TYR A  1 268 ? -31.520 -6.004  39.324   1.00 31.52  ? 268 TYR A CD2 1 
ATOM   2268  C CE1 . TYR A  1 268 ? -32.510 -6.792  41.792   1.00 31.86  ? 268 TYR A CE1 1 
ATOM   2269  C CE2 . TYR A  1 268 ? -32.465 -5.228  39.962   1.00 36.76  ? 268 TYR A CE2 1 
ATOM   2270  C CZ  . TYR A  1 268 ? -32.955 -5.627  41.195   1.00 39.14  ? 268 TYR A CZ  1 
ATOM   2271  O OH  . TYR A  1 268 ? -33.894 -4.850  41.810   1.00 40.15  ? 268 TYR A OH  1 
ATOM   2272  N N   . GLU A  1 269 ? -32.329 -8.224  37.066   1.00 25.13  ? 269 GLU A N   1 
ATOM   2273  C CA  . GLU A  1 269 ? -33.711 -7.918  36.707   1.00 24.04  ? 269 GLU A CA  1 
ATOM   2274  C C   . GLU A  1 269 ? -34.482 -9.171  36.356   1.00 24.83  ? 269 GLU A C   1 
ATOM   2275  O O   . GLU A  1 269 ? -35.703 -9.210  36.534   1.00 26.30  ? 269 GLU A O   1 
ATOM   2276  C CB  . GLU A  1 269 ? -33.767 -6.932  35.538   1.00 31.16  ? 269 GLU A CB  1 
ATOM   2277  C CG  . GLU A  1 269 ? -33.420 -5.509  35.926   1.00 39.96  ? 269 GLU A CG  1 
ATOM   2278  C CD  . GLU A  1 269 ? -33.089 -4.651  34.725   1.00 51.72  ? 269 GLU A CD  1 
ATOM   2279  O OE1 . GLU A  1 269 ? -32.722 -3.473  34.921   1.00 52.92  ? 269 GLU A OE1 1 
ATOM   2280  O OE2 . GLU A  1 269 ? -33.197 -5.157  33.583   1.00 55.82  ? 269 GLU A OE2 1 
ATOM   2281  N N   . LYS A  1 270 ? -33.794 -10.201 35.862   1.00 25.47  ? 270 LYS A N   1 
ATOM   2282  C CA  . LYS A  1 270 ? -34.430 -11.440 35.426   1.00 30.62  ? 270 LYS A CA  1 
ATOM   2283  C C   . LYS A  1 270 ? -34.500 -12.504 36.514   1.00 31.37  ? 270 LYS A C   1 
ATOM   2284  O O   . LYS A  1 270 ? -34.803 -13.663 36.208   1.00 30.57  ? 270 LYS A O   1 
ATOM   2285  C CB  . LYS A  1 270 ? -33.705 -12.005 34.206   1.00 28.25  ? 270 LYS A CB  1 
ATOM   2286  C CG  . LYS A  1 270 ? -33.934 -11.179 32.949   1.00 33.16  ? 270 LYS A CG  1 
ATOM   2287  C CD  . LYS A  1 270 ? -35.415 -10.911 32.707   1.00 35.40  ? 270 LYS A CD  1 
ATOM   2288  C CE  . LYS A  1 270 ? -35.660 -10.421 31.277   1.00 42.31  ? 270 LYS A CE  1 
ATOM   2289  N NZ  . LYS A  1 270 ? -36.643 -9.292  31.186   1.00 44.81  ? 270 LYS A NZ  1 
ATOM   2290  N N   . GLY A  1 271 ? -34.227 -12.141 37.762   1.00 31.20  ? 271 GLY A N   1 
ATOM   2291  C CA  . GLY A  1 271 ? -34.399 -13.036 38.891   1.00 30.17  ? 271 GLY A CA  1 
ATOM   2292  C C   . GLY A  1 271 ? -33.225 -13.933 39.192   1.00 31.07  ? 271 GLY A C   1 
ATOM   2293  O O   . GLY A  1 271 ? -33.386 -14.901 39.943   1.00 29.27  ? 271 GLY A O   1 
ATOM   2294  N N   . ILE A  1 272 ? -32.061 -13.673 38.612   1.00 24.62  ? 272 ILE A N   1 
ATOM   2295  C CA  . ILE A  1 272 ? -30.882 -14.465 38.930   1.00 26.01  ? 272 ILE A CA  1 
ATOM   2296  C C   . ILE A  1 272 ? -30.282 -13.934 40.222   1.00 27.47  ? 272 ILE A C   1 
ATOM   2297  O O   . ILE A  1 272 ? -30.017 -12.730 40.353   1.00 24.46  ? 272 ILE A O   1 
ATOM   2298  C CB  . ILE A  1 272 ? -29.854 -14.416 37.789   1.00 27.45  ? 272 ILE A CB  1 
ATOM   2299  C CG1 . ILE A  1 272 ? -30.502 -14.779 36.450   1.00 30.03  ? 272 ILE A CG1 1 
ATOM   2300  C CG2 . ILE A  1 272 ? -28.672 -15.336 38.124   1.00 26.09  ? 272 ILE A CG2 1 
ATOM   2301  C CD1 . ILE A  1 272 ? -31.229 -16.096 36.477   1.00 33.67  ? 272 ILE A CD1 1 
ATOM   2302  N N   . ASN A  1 273 ? -30.065 -14.821 41.184   1.00 23.37  ? 273 ASN A N   1 
ATOM   2303  C CA  . ASN A  1 273 ? -29.551 -14.348 42.457   1.00 28.99  ? 273 ASN A CA  1 
ATOM   2304  C C   . ASN A  1 273 ? -28.067 -14.578 42.622   1.00 27.98  ? 273 ASN A C   1 
ATOM   2305  O O   . ASN A  1 273 ? -27.456 -13.934 43.479   1.00 28.62  ? 273 ASN A O   1 
ATOM   2306  C CB  . ASN A  1 273 ? -30.290 -15.002 43.621   1.00 33.76  ? 273 ASN A CB  1 
ATOM   2307  C CG  . ASN A  1 273 ? -31.746 -14.660 43.638   1.00 45.09  ? 273 ASN A CG  1 
ATOM   2308  O OD1 . ASN A  1 273 ? -32.143 -13.508 43.411   1.00 48.51  ? 273 ASN A OD1 1 
ATOM   2309  N ND2 . ASN A  1 273 ? -32.567 -15.663 43.892   1.00 47.79  ? 273 ASN A ND2 1 
ATOM   2310  N N   A MET A  1 274 ? -27.509 -15.482 41.842   0.50 29.05  ? 274 MET A N   1 
ATOM   2311  N N   B MET A  1 274 ? -27.506 -15.481 41.842   0.50 29.05  ? 274 MET A N   1 
ATOM   2312  C CA  A MET A  1 274 ? -26.069 -15.675 41.844   0.50 31.47  ? 274 MET A CA  1 
ATOM   2313  C CA  B MET A  1 274 ? -26.066 -15.686 41.850   0.50 31.47  ? 274 MET A CA  1 
ATOM   2314  C C   A MET A  1 274 ? -25.454 -16.139 40.548   0.50 26.12  ? 274 MET A C   1 
ATOM   2315  C C   B MET A  1 274 ? -25.450 -16.148 40.554   0.50 26.12  ? 274 MET A C   1 
ATOM   2316  O O   A MET A  1 274 ? -26.071 -16.848 39.789   0.50 26.19  ? 274 MET A O   1 
ATOM   2317  O O   B MET A  1 274 ? -26.072 -16.845 39.788   0.50 26.19  ? 274 MET A O   1 
ATOM   2318  C CB  A MET A  1 274 ? -25.683 -16.718 42.860   0.50 40.07  ? 274 MET A CB  1 
ATOM   2319  C CB  B MET A  1 274 ? -25.710 -16.748 42.858   0.50 40.07  ? 274 MET A CB  1 
ATOM   2320  C CG  A MET A  1 274 ? -24.197 -16.807 43.120   0.50 56.94  ? 274 MET A CG  1 
ATOM   2321  C CG  B MET A  1 274 ? -24.232 -16.975 43.087   0.50 56.94  ? 274 MET A CG  1 
ATOM   2322  S SD  A MET A  1 274 ? -23.488 -18.185 42.219   0.50 69.07  ? 274 MET A SD  1 
ATOM   2323  S SD  B MET A  1 274 ? -23.975 -18.508 43.988   0.50 69.07  ? 274 MET A SD  1 
ATOM   2324  C CE  A MET A  1 274 ? -23.924 -19.486 43.367   0.50 70.01  ? 274 MET A CE  1 
ATOM   2325  C CE  B MET A  1 274 ? -23.862 -19.647 42.618   0.50 70.01  ? 274 MET A CE  1 
ATOM   2326  N N   . LEU A  1 275 ? -24.257 -15.680 40.281   1.00 23.28  ? 275 LEU A N   1 
ATOM   2327  C CA  . LEU A  1 275 ? -23.514 -16.206 39.159   1.00 24.23  ? 275 LEU A CA  1 
ATOM   2328  C C   . LEU A  1 275 ? -22.055 -16.305 39.578   1.00 22.59  ? 275 LEU A C   1 
ATOM   2329  O O   . LEU A  1 275 ? -21.690 -15.955 40.699   1.00 26.42  ? 275 LEU A O   1 
ATOM   2330  C CB  . LEU A  1 275 ? -23.728 -15.336 37.912   1.00 30.08  ? 275 LEU A CB  1 
ATOM   2331  C CG  . LEU A  1 275 ? -23.566 -13.819 37.999   1.00 30.43  ? 275 LEU A CG  1 
ATOM   2332  C CD1 . LEU A  1 275 ? -22.107 -13.459 37.910   1.00 24.42  ? 275 LEU A CD1 1 
ATOM   2333  C CD2 . LEU A  1 275 ? -24.342 -13.135 36.875   1.00 35.47  ? 275 LEU A CD2 1 
ATOM   2334  N N   . ALA A  1 276 ? -21.223 -16.818 38.683   1.00 22.29  ? 276 ALA A N   1 
ATOM   2335  C CA  . ALA A  1 276 ? -19.778 -16.797 38.840   1.00 18.91  ? 276 ALA A CA  1 
ATOM   2336  C C   . ALA A  1 276 ? -19.184 -16.214 37.575   1.00 20.33  ? 276 ALA A C   1 
ATOM   2337  O O   . ALA A  1 276 ? -19.810 -16.225 36.516   1.00 19.94  ? 276 ALA A O   1 
ATOM   2338  C CB  . ALA A  1 276 ? -19.167 -18.203 39.087   1.00 17.33  ? 276 ALA A CB  1 
ATOM   2339  N N   . THR A  1 277 ? -17.988 -15.663 37.708   1.00 22.05  ? 277 THR A N   1 
ATOM   2340  C CA  . THR A  1 277 ? -17.212 -15.193 36.568   1.00 20.09  ? 277 THR A CA  1 
ATOM   2341  C C   . THR A  1 277 ? -15.756 -15.481 36.906   1.00 24.46  ? 277 THR A C   1 
ATOM   2342  O O   . THR A  1 277 ? -15.455 -16.258 37.817   1.00 23.95  ? 277 THR A O   1 
ATOM   2343  C CB  . THR A  1 277 ? -17.468 -13.702 36.256   1.00 22.14  ? 277 THR A CB  1 
ATOM   2344  O OG1 . THR A  1 277 ? -16.677 -13.319 35.118   1.00 21.71  ? 277 THR A OG1 1 
ATOM   2345  C CG2 . THR A  1 277 ? -17.105 -12.796 37.456   1.00 20.94  ? 277 THR A CG2 1 
ATOM   2346  N N   . ASP A  1 278 ? -14.832 -14.825 36.211   1.00 22.49  ? 278 ASP A N   1 
ATOM   2347  C CA  . ASP A  1 278 ? -13.442 -15.243 36.254   1.00 22.83  ? 278 ASP A CA  1 
ATOM   2348  C C   . ASP A  1 278 ? -12.585 -14.357 37.152   1.00 17.89  ? 278 ASP A C   1 
ATOM   2349  O O   . ASP A  1 278 ? -12.823 -13.157 37.302   1.00 19.84  ? 278 ASP A O   1 
ATOM   2350  C CB  . ASP A  1 278 ? -12.849 -15.247 34.841   1.00 23.25  ? 278 ASP A CB  1 
ATOM   2351  C CG  . ASP A  1 278 ? -11.461 -15.823 34.802   1.00 30.09  ? 278 ASP A CG  1 
ATOM   2352  O OD1 . ASP A  1 278 ? -11.262 -16.956 35.300   1.00 31.82  ? 278 ASP A OD1 1 
ATOM   2353  O OD2 . ASP A  1 278 ? -10.570 -15.129 34.272   1.00 36.06  ? 278 ASP A OD2 1 
ATOM   2354  N N   . GLU A  1 279 ? -11.530 -14.957 37.684   1.00 23.65  ? 279 GLU A N   1 
ATOM   2355  C CA  . GLU A  1 279 ? -10.597 -14.207 38.517   1.00 30.27  ? 279 GLU A CA  1 
ATOM   2356  C C   . GLU A  1 279 ? -9.946  -13.038 37.770   1.00 28.17  ? 279 GLU A C   1 
ATOM   2357  O O   . GLU A  1 279 ? -9.606  -12.025 38.395   1.00 27.15  ? 279 GLU A O   1 
ATOM   2358  C CB  . GLU A  1 279 ? -9.532  -15.157 39.055   1.00 32.21  ? 279 GLU A CB  1 
ATOM   2359  C CG  . GLU A  1 279 ? -8.559  -14.508 40.018   1.00 37.31  ? 279 GLU A CG  1 
ATOM   2360  C CD  . GLU A  1 279 ? -7.711  -15.525 40.768   1.00 39.96  ? 279 GLU A CD  1 
ATOM   2361  O OE1 . GLU A  1 279 ? -7.843  -16.749 40.508   1.00 32.38  ? 279 GLU A OE1 1 
ATOM   2362  O OE2 . GLU A  1 279 ? -6.898  -15.080 41.605   1.00 44.56  ? 279 GLU A OE2 1 
ATOM   2363  N N   . VAL A  1 280 ? -9.732  -13.153 36.449   1.00 27.27  ? 280 VAL A N   1 
ATOM   2364  C CA  . VAL A  1 280 ? -9.103  -12.044 35.731   1.00 26.11  ? 280 VAL A CA  1 
ATOM   2365  C C   . VAL A  1 280 ? -10.008 -10.821 35.761   1.00 27.25  ? 280 VAL A C   1 
ATOM   2366  O O   . VAL A  1 280 ? -9.529  -9.680  35.832   1.00 27.23  ? 280 VAL A O   1 
ATOM   2367  C CB  . VAL A  1 280 ? -8.748  -12.438 34.278   1.00 24.50  ? 280 VAL A CB  1 
ATOM   2368  C CG1 . VAL A  1 280 ? -8.254  -11.210 33.507   1.00 28.85  ? 280 VAL A CG1 1 
ATOM   2369  C CG2 . VAL A  1 280 ? -7.698  -13.532 34.258   1.00 27.35  ? 280 VAL A CG2 1 
ATOM   2370  N N   . ILE A  1 281 ? -11.331 -11.041 35.700   1.00 26.06  ? 281 ILE A N   1 
ATOM   2371  C CA  . ILE A  1 281 ? -12.295 -9.942  35.806   1.00 29.15  ? 281 ILE A CA  1 
ATOM   2372  C C   . ILE A  1 281 ? -12.140 -9.232  37.141   1.00 29.22  ? 281 ILE A C   1 
ATOM   2373  O O   . ILE A  1 281 ? -12.087 -7.998  37.205   1.00 27.92  ? 281 ILE A O   1 
ATOM   2374  C CB  . ILE A  1 281 ? -13.742 -10.447 35.638   1.00 31.46  ? 281 ILE A CB  1 
ATOM   2375  C CG1 . ILE A  1 281 ? -13.924 -11.235 34.335   1.00 33.42  ? 281 ILE A CG1 1 
ATOM   2376  C CG2 . ILE A  1 281 ? -14.719 -9.275  35.729   1.00 31.25  ? 281 ILE A CG2 1 
ATOM   2377  C CD1 . ILE A  1 281 ? -13.725 -10.412 33.104   1.00 30.90  ? 281 ILE A CD1 1 
ATOM   2378  N N   . LEU A  1 282 ? -12.118 -10.008 38.228   1.00 32.55  ? 282 LEU A N   1 
ATOM   2379  C CA  . LEU A  1 282 ? -11.947 -9.442  39.563   1.00 34.57  ? 282 LEU A CA  1 
ATOM   2380  C C   . LEU A  1 282 ? -10.673 -8.616  39.653   1.00 31.27  ? 282 LEU A C   1 
ATOM   2381  O O   . LEU A  1 282 ? -10.682 -7.498  40.185   1.00 25.26  ? 282 LEU A O   1 
ATOM   2382  C CB  . LEU A  1 282 ? -11.920 -10.568 40.604   1.00 33.81  ? 282 LEU A CB  1 
ATOM   2383  C CG  . LEU A  1 282 ? -11.733 -10.135 42.065   1.00 33.46  ? 282 LEU A CG  1 
ATOM   2384  C CD1 . LEU A  1 282 ? -12.908 -9.266  42.592   1.00 25.06  ? 282 LEU A CD1 1 
ATOM   2385  C CD2 . LEU A  1 282 ? -11.508 -11.366 42.948   1.00 26.32  ? 282 LEU A CD2 1 
ATOM   2386  N N   . LYS A  1 283 ? -9.555  -9.175  39.170   1.00 32.85  ? 283 LYS A N   1 
ATOM   2387  C CA  . LYS A  1 283 ? -8.269  -8.481  39.233   1.00 33.34  ? 283 LYS A CA  1 
ATOM   2388  C C   . LYS A  1 283 ? -8.304  -7.180  38.450   1.00 32.44  ? 283 LYS A C   1 
ATOM   2389  O O   . LYS A  1 283 ? -7.750  -6.169  38.895   1.00 38.36  ? 283 LYS A O   1 
ATOM   2390  C CB  . LYS A  1 283 ? -7.147  -9.378  38.702   1.00 38.08  ? 283 LYS A CB  1 
ATOM   2391  C CG  . LYS A  1 283 ? -6.758  -10.537 39.615   1.00 47.27  ? 283 LYS A CG  1 
ATOM   2392  C CD  . LYS A  1 283 ? -6.959  -10.187 41.085   1.00 52.45  ? 283 LYS A CD  1 
ATOM   2393  C CE  . LYS A  1 283 ? -6.192  -11.123 41.994   1.00 58.17  ? 283 LYS A CE  1 
ATOM   2394  N NZ  . LYS A  1 283 ? -6.115  -10.590 43.382   1.00 60.73  ? 283 LYS A NZ  1 
ATOM   2395  N N   . ASN A  1 284 ? -8.955  -7.186  37.278   1.00 27.82  ? 284 ASN A N   1 
ATOM   2396  C CA  . ASN A  1 284 ? -9.120  -5.974  36.477   1.00 29.88  ? 284 ASN A CA  1 
ATOM   2397  C C   . ASN A  1 284 ? -9.998  -4.924  37.151   1.00 30.13  ? 284 ASN A C   1 
ATOM   2398  O O   . ASN A  1 284 ? -9.890  -3.740  36.813   1.00 30.97  ? 284 ASN A O   1 
ATOM   2399  C CB  . ASN A  1 284 ? -9.748  -6.314  35.122   1.00 28.55  ? 284 ASN A CB  1 
ATOM   2400  C CG  . ASN A  1 284 ? -8.764  -6.899  34.164   1.00 31.58  ? 284 ASN A CG  1 
ATOM   2401  O OD1 . ASN A  1 284 ? -7.581  -7.019  34.472   1.00 38.33  ? 284 ASN A OD1 1 
ATOM   2402  N ND2 . ASN A  1 284 ? -9.239  -7.278  32.986   1.00 31.77  ? 284 ASN A ND2 1 
ATOM   2403  N N   . SER A  1 285 ? -10.892 -5.340  38.050   1.00 28.55  ? 285 SER A N   1 
ATOM   2404  C CA  . SER A  1 285 ? -11.985 -4.527  38.573   1.00 32.50  ? 285 SER A CA  1 
ATOM   2405  C C   . SER A  1 285 ? -11.717 -3.953  39.954   1.00 36.01  ? 285 SER A C   1 
ATOM   2406  O O   . SER A  1 285 ? -12.179 -2.845  40.248   1.00 38.37  ? 285 SER A O   1 
ATOM   2407  C CB  . SER A  1 285 ? -13.272 -5.361  38.645   1.00 26.92  ? 285 SER A CB  1 
ATOM   2408  O OG  . SER A  1 285 ? -13.639 -5.850  37.362   1.00 28.74  ? 285 SER A OG  1 
ATOM   2409  N N   . VAL A  1 286 ? -11.006 -4.688  40.809   1.00 31.40  ? 286 VAL A N   1 
ATOM   2410  C CA  . VAL A  1 286 ? -10.761 -4.288  42.189   1.00 33.26  ? 286 VAL A CA  1 
ATOM   2411  C C   . VAL A  1 286 ? -9.285  -4.473  42.511   1.00 35.89  ? 286 VAL A C   1 
ATOM   2412  O O   . VAL A  1 286 ? -8.713  -5.535  42.238   1.00 29.58  ? 286 VAL A O   1 
ATOM   2413  C CB  . VAL A  1 286 ? -11.601 -5.106  43.184   1.00 30.74  ? 286 VAL A CB  1 
ATOM   2414  C CG1 . VAL A  1 286 ? -11.479 -4.496  44.563   1.00 34.23  ? 286 VAL A CG1 1 
ATOM   2415  C CG2 . VAL A  1 286 ? -13.048 -5.190  42.741   1.00 29.09  ? 286 VAL A CG2 1 
ATOM   2416  N N   . GLU A  1 287 ? -8.681  -3.450  43.115   1.00 42.41  ? 287 GLU A N   1 
ATOM   2417  C CA  . GLU A  1 287 ? -7.344  -3.580  43.693   1.00 54.21  ? 287 GLU A CA  1 
ATOM   2418  C C   . GLU A  1 287 ? -7.267  -4.740  44.678   1.00 60.25  ? 287 GLU A C   1 
ATOM   2419  O O   . GLU A  1 287 ? -6.511  -5.698  44.476   1.00 62.93  ? 287 GLU A O   1 
ATOM   2420  C CB  . GLU A  1 287 ? -6.966  -2.276  44.396   1.00 59.69  ? 287 GLU A CB  1 
ATOM   2421  C CG  . GLU A  1 287 ? -6.399  -1.214  43.501   1.00 62.33  ? 287 GLU A CG  1 
ATOM   2422  C CD  . GLU A  1 287 ? -4.899  -1.332  43.341   1.00 64.92  ? 287 GLU A CD  1 
ATOM   2423  O OE1 . GLU A  1 287 ? -4.287  -0.349  42.875   1.00 69.19  ? 287 GLU A OE1 1 
ATOM   2424  O OE2 . GLU A  1 287 ? -4.335  -2.401  43.669   1.00 62.85  ? 287 GLU A OE2 1 
ATOM   2425  N N   . ARG A  1 288 ? -8.038  -4.650  45.765   1.00 61.65  ? 288 ARG A N   1 
ATOM   2426  C CA  . ARG A  1 288 ? -8.043  -5.648  46.831   1.00 63.36  ? 288 ARG A CA  1 
ATOM   2427  C C   . ARG A  1 288 ? -8.950  -6.808  46.448   1.00 65.57  ? 288 ARG A C   1 
ATOM   2428  O O   . ARG A  1 288 ? -10.162 -6.765  46.672   1.00 73.14  ? 288 ARG A O   1 
ATOM   2429  C CB  . ARG A  1 288 ? -8.503  -5.039  48.143   1.00 65.69  ? 288 ARG A CB  1 
ATOM   2430  C CG  . ARG A  1 288 ? -8.563  -6.063  49.236   1.00 65.78  ? 288 ARG A CG  1 
ATOM   2431  C CD  . ARG A  1 288 ? -7.443  -5.846  50.210   1.00 63.88  ? 288 ARG A CD  1 
ATOM   2432  N NE  . ARG A  1 288 ? -7.322  -4.450  50.622   1.00 61.47  ? 288 ARG A NE  1 
ATOM   2433  C CZ  . ARG A  1 288 ? -8.228  -3.788  51.339   1.00 56.86  ? 288 ARG A CZ  1 
ATOM   2434  N NH1 . ARG A  1 288 ? -8.005  -2.523  51.667   1.00 52.61  ? 288 ARG A NH1 1 
ATOM   2435  N NH2 . ARG A  1 288 ? -9.356  -4.375  51.719   1.00 57.44  ? 288 ARG A NH2 1 
ATOM   2436  N N   . ALA A  1 289 ? -8.369  -7.872  45.902   1.00 57.88  ? 289 ALA A N   1 
ATOM   2437  C CA  . ALA A  1 289 ? -9.154  -8.906  45.234   1.00 53.61  ? 289 ALA A CA  1 
ATOM   2438  C C   . ALA A  1 289 ? -8.792  -10.287 45.775   1.00 40.68  ? 289 ALA A C   1 
ATOM   2439  O O   . ALA A  1 289 ? -7.950  -10.973 45.194   1.00 37.81  ? 289 ALA A O   1 
ATOM   2440  C CB  . ALA A  1 289 ? -8.932  -8.814  43.720   1.00 59.29  ? 289 ALA A CB  1 
ATOM   2441  N N   . SER A  1 290 ? -9.439  -10.705 46.904   1.00 36.66  ? 290 SER A N   1 
ATOM   2442  C CA  . SER A  1 290 ? -9.382  -12.131 47.227   1.00 33.29  ? 290 SER A CA  1 
ATOM   2443  C C   . SER A  1 290 ? -10.523 -12.866 46.534   1.00 33.17  ? 290 SER A C   1 
ATOM   2444  O O   . SER A  1 290 ? -11.687 -12.468 46.686   1.00 33.22  ? 290 SER A O   1 
ATOM   2445  C CB  . SER A  1 290 ? -9.476  -12.372 48.726   1.00 33.60  ? 290 SER A CB  1 
ATOM   2446  O OG  . SER A  1 290 ? -9.811  -13.734 48.946   1.00 31.60  ? 290 SER A OG  1 
ATOM   2447  N N   . PRO A  1 291 ? -10.254 -13.942 45.789   1.00 32.23  ? 291 PRO A N   1 
ATOM   2448  C CA  . PRO A  1 291 ? -11.338 -14.711 45.166   1.00 27.31  ? 291 PRO A CA  1 
ATOM   2449  C C   . PRO A  1 291 ? -12.019 -15.694 46.103   1.00 24.85  ? 291 PRO A C   1 
ATOM   2450  O O   . PRO A  1 291 ? -12.813 -16.514 45.640   1.00 21.33  ? 291 PRO A O   1 
ATOM   2451  C CB  . PRO A  1 291 ? -10.608 -15.465 44.047   1.00 30.75  ? 291 PRO A CB  1 
ATOM   2452  C CG  . PRO A  1 291 ? -9.272  -15.770 44.677   1.00 31.96  ? 291 PRO A CG  1 
ATOM   2453  C CD  . PRO A  1 291 ? -8.940  -14.568 45.554   1.00 30.53  ? 291 PRO A CD  1 
ATOM   2454  N N   . TYR A  1 292 ? -11.718 -15.646 47.396   1.00 20.99  ? 292 TYR A N   1 
ATOM   2455  C CA  . TYR A  1 292 ? -12.254 -16.606 48.342   1.00 24.85  ? 292 TYR A CA  1 
ATOM   2456  C C   . TYR A  1 292 ? -13.500 -16.104 49.042   1.00 25.95  ? 292 TYR A C   1 
ATOM   2457  O O   . TYR A  1 292 ? -14.035 -16.809 49.912   1.00 24.39  ? 292 TYR A O   1 
ATOM   2458  C CB  . TYR A  1 292 ? -11.180 -16.963 49.375   1.00 24.18  ? 292 TYR A CB  1 
ATOM   2459  C CG  . TYR A  1 292 ? -9.936  -17.550 48.734   1.00 29.30  ? 292 TYR A CG  1 
ATOM   2460  C CD1 . TYR A  1 292 ? -10.039 -18.463 47.688   1.00 32.51  ? 292 TYR A CD1 1 
ATOM   2461  C CD2 . TYR A  1 292 ? -8.663  -17.192 49.165   1.00 37.72  ? 292 TYR A CD2 1 
ATOM   2462  C CE1 . TYR A  1 292 ? -8.917  -19.005 47.090   1.00 33.11  ? 292 TYR A CE1 1 
ATOM   2463  C CE2 . TYR A  1 292 ? -7.528  -17.731 48.565   1.00 39.00  ? 292 TYR A CE2 1 
ATOM   2464  C CZ  . TYR A  1 292 ? -7.669  -18.634 47.523   1.00 37.41  ? 292 TYR A CZ  1 
ATOM   2465  O OH  . TYR A  1 292 ? -6.564  -19.196 46.924   1.00 42.22  ? 292 TYR A OH  1 
ATOM   2466  N N   . LEU A  1 293 ? -13.966 -14.918 48.664   1.00 22.98  ? 293 LEU A N   1 
ATOM   2467  C CA  . LEU A  1 293 ? -15.089 -14.234 49.271   1.00 25.71  ? 293 LEU A CA  1 
ATOM   2468  C C   . LEU A  1 293 ? -16.322 -14.412 48.404   1.00 25.55  ? 293 LEU A C   1 
ATOM   2469  O O   . LEU A  1 293 ? -16.222 -14.641 47.199   1.00 22.02  ? 293 LEU A O   1 
ATOM   2470  C CB  . LEU A  1 293 ? -14.787 -12.739 49.434   1.00 28.57  ? 293 LEU A CB  1 
ATOM   2471  C CG  . LEU A  1 293 ? -13.962 -12.206 50.617   1.00 33.32  ? 293 LEU A CG  1 
ATOM   2472  C CD1 . LEU A  1 293 ? -12.862 -13.145 51.047   1.00 33.21  ? 293 LEU A CD1 1 
ATOM   2473  C CD2 . LEU A  1 293 ? -13.367 -10.834 50.290   1.00 30.06  ? 293 LEU A CD2 1 
ATOM   2474  N N   . ARG A  1 294 ? -17.493 -14.311 49.029   1.00 24.25  ? 294 ARG A N   1 
ATOM   2475  C CA  . ARG A  1 294 ? -18.738 -14.163 48.285   1.00 23.97  ? 294 ARG A CA  1 
ATOM   2476  C C   . ARG A  1 294 ? -18.952 -12.673 48.037   1.00 23.64  ? 294 ARG A C   1 
ATOM   2477  O O   . ARG A  1 294 ? -18.983 -11.889 48.986   1.00 24.19  ? 294 ARG A O   1 
ATOM   2478  C CB  . ARG A  1 294 ? -19.918 -14.770 49.061   1.00 23.75  ? 294 ARG A CB  1 
ATOM   2479  C CG  . ARG A  1 294 ? -21.261 -14.590 48.324   1.00 28.06  ? 294 ARG A CG  1 
ATOM   2480  C CD  . ARG A  1 294 ? -22.368 -15.462 48.916   1.00 26.73  ? 294 ARG A CD  1 
ATOM   2481  N NE  . ARG A  1 294 ? -22.722 -15.067 50.274   1.00 30.66  ? 294 ARG A NE  1 
ATOM   2482  C CZ  . ARG A  1 294 ? -22.700 -15.872 51.339   1.00 30.14  ? 294 ARG A CZ  1 
ATOM   2483  N NH1 . ARG A  1 294 ? -22.336 -17.153 51.243   1.00 28.99  ? 294 ARG A NH1 1 
ATOM   2484  N NH2 . ARG A  1 294 ? -23.047 -15.387 52.517   1.00 33.82  ? 294 ARG A NH2 1 
ATOM   2485  N N   . TYR A  1 295 ? -19.049 -12.267 46.768   1.00 18.34  ? 295 TYR A N   1 
ATOM   2486  C CA  . TYR A  1 295 ? -19.219 -10.859 46.446   1.00 20.56  ? 295 TYR A CA  1 
ATOM   2487  C C   . TYR A  1 295 ? -20.682 -10.528 46.193   1.00 23.15  ? 295 TYR A C   1 
ATOM   2488  O O   . TYR A  1 295 ? -21.481 -11.386 45.814   1.00 25.07  ? 295 TYR A O   1 
ATOM   2489  C CB  . TYR A  1 295 ? -18.381 -10.460 45.224   1.00 23.90  ? 295 TYR A CB  1 
ATOM   2490  C CG  . TYR A  1 295 ? -16.904 -10.358 45.549   1.00 26.55  ? 295 TYR A CG  1 
ATOM   2491  C CD1 . TYR A  1 295 ? -16.111 -11.500 45.614   1.00 21.42  ? 295 TYR A CD1 1 
ATOM   2492  C CD2 . TYR A  1 295 ? -16.309 -9.122  45.816   1.00 23.73  ? 295 TYR A CD2 1 
ATOM   2493  C CE1 . TYR A  1 295 ? -14.758 -11.420 45.919   1.00 26.92  ? 295 TYR A CE1 1 
ATOM   2494  C CE2 . TYR A  1 295 ? -14.952 -9.035  46.115   1.00 29.25  ? 295 TYR A CE2 1 
ATOM   2495  C CZ  . TYR A  1 295 ? -14.182 -10.189 46.170   1.00 30.08  ? 295 TYR A CZ  1 
ATOM   2496  O OH  . TYR A  1 295 ? -12.832 -10.103 46.487   1.00 30.76  ? 295 TYR A OH  1 
ATOM   2497  N N   . TYR A  1 296 ? -21.029 -9.263  46.417   1.00 24.40  ? 296 TYR A N   1 
ATOM   2498  C CA  . TYR A  1 296 ? -22.367 -8.780  46.104   1.00 32.10  ? 296 TYR A CA  1 
ATOM   2499  C C   . TYR A  1 296 ? -22.224 -7.571  45.199   1.00 32.38  ? 296 TYR A C   1 
ATOM   2500  O O   . TYR A  1 296 ? -21.713 -6.532  45.626   1.00 30.86  ? 296 TYR A O   1 
ATOM   2501  C CB  . TYR A  1 296 ? -23.158 -8.439  47.366   1.00 35.95  ? 296 TYR A CB  1 
ATOM   2502  C CG  . TYR A  1 296 ? -23.415 -9.625  48.265   1.00 44.14  ? 296 TYR A CG  1 
ATOM   2503  C CD1 . TYR A  1 296 ? -24.499 -10.472 48.052   1.00 44.37  ? 296 TYR A CD1 1 
ATOM   2504  C CD2 . TYR A  1 296 ? -22.570 -9.905  49.330   1.00 50.29  ? 296 TYR A CD2 1 
ATOM   2505  C CE1 . TYR A  1 296 ? -24.731 -11.561 48.889   1.00 46.72  ? 296 TYR A CE1 1 
ATOM   2506  C CE2 . TYR A  1 296 ? -22.794 -10.986 50.160   1.00 50.24  ? 296 TYR A CE2 1 
ATOM   2507  C CZ  . TYR A  1 296 ? -23.867 -11.809 49.939   1.00 49.11  ? 296 TYR A CZ  1 
ATOM   2508  O OH  . TYR A  1 296 ? -24.055 -12.874 50.794   1.00 53.03  ? 296 TYR A OH  1 
ATOM   2509  N N   . PHE A  1 297 ? -22.660 -7.709  43.945   1.00 28.97  ? 297 PHE A N   1 
ATOM   2510  C CA  . PHE A  1 297 ? -22.589 -6.600  43.003   1.00 23.19  ? 297 PHE A CA  1 
ATOM   2511  C C   . PHE A  1 297 ? -23.709 -5.611  43.312   1.00 23.11  ? 297 PHE A C   1 
ATOM   2512  O O   . PHE A  1 297 ? -24.889 -5.920  43.106   1.00 27.10  ? 297 PHE A O   1 
ATOM   2513  C CB  . PHE A  1 297 ? -22.679 -7.105  41.561   1.00 21.98  ? 297 PHE A CB  1 
ATOM   2514  C CG  . PHE A  1 297 ? -22.672 -5.999  40.539   1.00 24.61  ? 297 PHE A CG  1 
ATOM   2515  C CD1 . PHE A  1 297 ? -21.489 -5.345  40.211   1.00 23.38  ? 297 PHE A CD1 1 
ATOM   2516  C CD2 . PHE A  1 297 ? -23.849 -5.592  39.923   1.00 25.08  ? 297 PHE A CD2 1 
ATOM   2517  C CE1 . PHE A  1 297 ? -21.472 -4.331  39.249   1.00 25.03  ? 297 PHE A CE1 1 
ATOM   2518  C CE2 . PHE A  1 297 ? -23.841 -4.576  38.972   1.00 23.21  ? 297 PHE A CE2 1 
ATOM   2519  C CZ  . PHE A  1 297 ? -22.642 -3.945  38.637   1.00 21.71  ? 297 PHE A CZ  1 
ATOM   2520  N N   . ARG A  1 298 ? -23.336 -4.425  43.812   1.00 24.51  ? 298 ARG A N   1 
ATOM   2521  C CA  . ARG A  1 298 ? -24.280 -3.336  44.141   1.00 23.08  ? 298 ARG A CA  1 
ATOM   2522  C C   . ARG A  1 298 ? -25.408 -3.824  45.045   1.00 29.99  ? 298 ARG A C   1 
ATOM   2523  O O   . ARG A  1 298 ? -26.527 -3.305  44.995   1.00 34.97  ? 298 ARG A O   1 
ATOM   2524  C CB  . ARG A  1 298 ? -24.861 -2.694  42.866   1.00 28.05  ? 298 ARG A CB  1 
ATOM   2525  C CG  . ARG A  1 298 ? -23.795 -2.152  41.914   1.00 29.94  ? 298 ARG A CG  1 
ATOM   2526  C CD  . ARG A  1 298 ? -24.358 -1.488  40.662   1.00 26.30  ? 298 ARG A CD  1 
ATOM   2527  N NE  . ARG A  1 298 ? -23.275 -0.922  39.870   1.00 30.06  ? 298 ARG A NE  1 
ATOM   2528  C CZ  . ARG A  1 298 ? -23.401 -0.500  38.611   1.00 30.59  ? 298 ARG A CZ  1 
ATOM   2529  N NH1 . ARG A  1 298 ? -24.573 -0.581  37.987   1.00 29.15  ? 298 ARG A NH1 1 
ATOM   2530  N NH2 . ARG A  1 298 ? -22.351 -0.007  37.970   1.00 30.07  ? 298 ARG A NH2 1 
ATOM   2531  N N   . GLU A  1 299 ? -25.132 -4.841  45.861   1.00 32.55  ? 299 GLU A N   1 
ATOM   2532  C CA  . GLU A  1 299 ? -26.145 -5.447  46.735   1.00 36.98  ? 299 GLU A CA  1 
ATOM   2533  C C   . GLU A  1 299 ? -27.356 -5.937  45.931   1.00 37.83  ? 299 GLU A C   1 
ATOM   2534  O O   . GLU A  1 299 ? -28.464 -6.058  46.453   1.00 40.04  ? 299 GLU A O   1 
ATOM   2535  C CB  . GLU A  1 299 ? -26.562 -4.469  47.848   1.00 40.91  ? 299 GLU A CB  1 
ATOM   2536  C CG  . GLU A  1 299 ? -25.885 -4.763  49.198   1.00 51.27  ? 299 GLU A CG  1 
ATOM   2537  C CD  . GLU A  1 299 ? -25.704 -3.536  50.095   1.00 58.93  ? 299 GLU A CD  1 
ATOM   2538  O OE1 . GLU A  1 299 ? -26.323 -2.479  49.838   1.00 62.93  ? 299 GLU A OE1 1 
ATOM   2539  O OE2 . GLU A  1 299 ? -24.929 -3.635  51.070   1.00 59.32  ? 299 GLU A OE2 1 
ATOM   2540  N N   . LEU A  1 300 ? -27.154 -6.228  44.642   1.00 35.32  ? 300 LEU A N   1 
ATOM   2541  C CA  . LEU A  1 300 ? -28.232 -6.679  43.768   1.00 34.46  ? 300 LEU A CA  1 
ATOM   2542  C C   . LEU A  1 300 ? -28.183 -8.170  43.461   1.00 31.50  ? 300 LEU A C   1 
ATOM   2543  O O   . LEU A  1 300 ? -29.235 -8.790  43.290   1.00 30.99  ? 300 LEU A O   1 
ATOM   2544  C CB  . LEU A  1 300 ? -28.219 -5.886  42.449   1.00 37.90  ? 300 LEU A CB  1 
ATOM   2545  C CG  . LEU A  1 300 ? -28.616 -4.394  42.547   1.00 43.16  ? 300 LEU A CG  1 
ATOM   2546  C CD1 . LEU A  1 300 ? -28.500 -3.684  41.212   1.00 44.58  ? 300 LEU A CD1 1 
ATOM   2547  C CD2 . LEU A  1 300 ? -30.016 -4.199  43.105   1.00 44.72  ? 300 LEU A CD2 1 
ATOM   2548  N N   . ILE A  1 301 ? -26.993 -8.768  43.436   1.00 25.25  ? 301 ILE A N   1 
ATOM   2549  C CA  . ILE A  1 301 ? -26.827 -10.135 42.973   1.00 29.57  ? 301 ILE A CA  1 
ATOM   2550  C C   . ILE A  1 301 ? -25.515 -10.641 43.544   1.00 28.04  ? 301 ILE A C   1 
ATOM   2551  O O   . ILE A  1 301 ? -24.559 -9.880  43.693   1.00 31.95  ? 301 ILE A O   1 
ATOM   2552  C CB  . ILE A  1 301 ? -26.869 -10.197 41.419   1.00 27.78  ? 301 ILE A CB  1 
ATOM   2553  C CG1 . ILE A  1 301 ? -26.844 -11.642 40.913   1.00 28.11  ? 301 ILE A CG1 1 
ATOM   2554  C CG2 . ILE A  1 301 ? -25.745 -9.353  40.764   1.00 24.90  ? 301 ILE A CG2 1 
ATOM   2555  C CD1 . ILE A  1 301 ? -26.980 -11.760 39.364   1.00 26.11  ? 301 ILE A CD1 1 
ATOM   2556  N N   . SER A  1 302 ? -25.471 -11.925 43.884   1.00 28.45  ? 302 SER A N   1 
ATOM   2557  C CA  . SER A  1 302 ? -24.227 -12.504 44.374   1.00 27.76  ? 302 SER A CA  1 
ATOM   2558  C C   . SER A  1 302 ? -23.340 -12.932 43.215   1.00 26.48  ? 302 SER A C   1 
ATOM   2559  O O   . SER A  1 302 ? -23.824 -13.370 42.166   1.00 28.37  ? 302 SER A O   1 
ATOM   2560  C CB  . SER A  1 302 ? -24.505 -13.700 45.273   1.00 27.89  ? 302 SER A CB  1 
ATOM   2561  O OG  . SER A  1 302 ? -25.276 -13.277 46.377   1.00 29.06  ? 302 SER A OG  1 
ATOM   2562  N N   . VAL A  1 303 ? -22.028 -12.809 43.415   1.00 26.84  ? 303 VAL A N   1 
ATOM   2563  C CA  . VAL A  1 303 ? -21.030 -13.101 42.393   1.00 23.48  ? 303 VAL A CA  1 
ATOM   2564  C C   . VAL A  1 303 ? -19.858 -13.813 43.061   1.00 23.65  ? 303 VAL A C   1 
ATOM   2565  O O   . VAL A  1 303 ? -19.232 -13.258 43.969   1.00 25.98  ? 303 VAL A O   1 
ATOM   2566  C CB  . VAL A  1 303 ? -20.540 -11.824 41.690   1.00 25.47  ? 303 VAL A CB  1 
ATOM   2567  C CG1 . VAL A  1 303 ? -19.393 -12.159 40.728   1.00 23.74  ? 303 VAL A CG1 1 
ATOM   2568  C CG2 . VAL A  1 303 ? -21.692 -11.132 40.956   1.00 24.23  ? 303 VAL A CG2 1 
ATOM   2569  N N   . PHE A  1 304 ? -19.555 -15.030 42.619   1.00 22.04  ? 304 PHE A N   1 
ATOM   2570  C CA  . PHE A  1 304 ? -18.291 -15.660 42.966   1.00 22.94  ? 304 PHE A CA  1 
ATOM   2571  C C   . PHE A  1 304 ? -17.301 -15.502 41.812   1.00 25.04  ? 304 PHE A C   1 
ATOM   2572  O O   . PHE A  1 304 ? -17.679 -15.491 40.640   1.00 22.08  ? 304 PHE A O   1 
ATOM   2573  C CB  . PHE A  1 304 ? -18.479 -17.146 43.315   1.00 15.40  ? 304 PHE A CB  1 
ATOM   2574  C CG  . PHE A  1 304 ? -19.063 -17.373 44.707   1.00 21.38  ? 304 PHE A CG  1 
ATOM   2575  C CD1 . PHE A  1 304 ? -18.263 -17.298 45.843   1.00 21.36  ? 304 PHE A CD1 1 
ATOM   2576  C CD2 . PHE A  1 304 ? -20.406 -17.633 44.870   1.00 23.39  ? 304 PHE A CD2 1 
ATOM   2577  C CE1 . PHE A  1 304 ? -18.814 -17.491 47.123   1.00 23.61  ? 304 PHE A CE1 1 
ATOM   2578  C CE2 . PHE A  1 304 ? -20.959 -17.826 46.150   1.00 25.14  ? 304 PHE A CE2 1 
ATOM   2579  C CZ  . PHE A  1 304 ? -20.162 -17.750 47.268   1.00 24.38  ? 304 PHE A CZ  1 
ATOM   2580  N N   . PHE A  1 305 ? -16.027 -15.366 42.148   1.00 23.82  ? 305 PHE A N   1 
ATOM   2581  C CA  . PHE A  1 305 ? -14.970 -15.319 41.141   1.00 15.54  ? 305 PHE A CA  1 
ATOM   2582  C C   . PHE A  1 305 ? -14.204 -16.628 41.216   1.00 24.24  ? 305 PHE A C   1 
ATOM   2583  O O   . PHE A  1 305 ? -13.636 -16.955 42.265   1.00 23.91  ? 305 PHE A O   1 
ATOM   2584  C CB  . PHE A  1 305 ? -14.064 -14.118 41.371   1.00 17.82  ? 305 PHE A CB  1 
ATOM   2585  C CG  . PHE A  1 305 ? -14.768 -12.811 41.199   1.00 26.00  ? 305 PHE A CG  1 
ATOM   2586  C CD1 . PHE A  1 305 ? -15.442 -12.223 42.270   1.00 28.15  ? 305 PHE A CD1 1 
ATOM   2587  C CD2 . PHE A  1 305 ? -14.792 -12.182 39.966   1.00 23.13  ? 305 PHE A CD2 1 
ATOM   2588  C CE1 . PHE A  1 305 ? -16.115 -11.025 42.116   1.00 25.05  ? 305 PHE A CE1 1 
ATOM   2589  C CE2 . PHE A  1 305 ? -15.464 -10.970 39.804   1.00 19.91  ? 305 PHE A CE2 1 
ATOM   2590  C CZ  . PHE A  1 305 ? -16.127 -10.397 40.883   1.00 27.09  ? 305 PHE A CZ  1 
ATOM   2591  N N   . ARG A  1 306 ? -14.226 -17.396 40.125   1.00 19.67  ? 306 ARG A N   1 
ATOM   2592  C CA  . ARG A  1 306 ? -13.640 -18.724 40.163   1.00 24.33  ? 306 ARG A CA  1 
ATOM   2593  C C   . ARG A  1 306 ? -12.134 -18.641 40.405   1.00 25.53  ? 306 ARG A C   1 
ATOM   2594  O O   . ARG A  1 306 ? -11.483 -17.626 40.136   1.00 31.00  ? 306 ARG A O   1 
ATOM   2595  C CB  . ARG A  1 306 ? -13.917 -19.475 38.865   1.00 29.66  ? 306 ARG A CB  1 
ATOM   2596  C CG  . ARG A  1 306 ? -13.097 -18.960 37.700   1.00 30.65  ? 306 ARG A CG  1 
ATOM   2597  C CD  . ARG A  1 306 ? -13.028 -19.954 36.575   1.00 32.34  ? 306 ARG A CD  1 
ATOM   2598  N NE  . ARG A  1 306 ? -12.053 -19.476 35.614   1.00 34.81  ? 306 ARG A NE  1 
ATOM   2599  C CZ  . ARG A  1 306 ? -11.551 -20.196 34.621   1.00 28.57  ? 306 ARG A CZ  1 
ATOM   2600  N NH1 . ARG A  1 306 ? -11.940 -21.456 34.425   1.00 25.04  ? 306 ARG A NH1 1 
ATOM   2601  N NH2 . ARG A  1 306 ? -10.667 -19.635 33.821   1.00 27.54  ? 306 ARG A NH2 1 
ATOM   2602  N N   . ASP A  1 307 ? -11.587 -19.730 40.932   1.00 25.28  ? 307 ASP A N   1 
ATOM   2603  C CA  . ASP A  1 307 ? -10.148 -19.875 41.138   1.00 24.79  ? 307 ASP A CA  1 
ATOM   2604  C C   . ASP A  1 307 ? -9.543  -20.328 39.821   1.00 24.21  ? 307 ASP A C   1 
ATOM   2605  O O   . ASP A  1 307 ? -9.598  -21.509 39.465   1.00 26.29  ? 307 ASP A O   1 
ATOM   2606  C CB  . ASP A  1 307 ? -9.845  -20.878 42.251   1.00 20.63  ? 307 ASP A CB  1 
ATOM   2607  C CG  . ASP A  1 307 ? -8.376  -20.887 42.649   1.00 27.20  ? 307 ASP A CG  1 
ATOM   2608  O OD1 . ASP A  1 307 ? -7.491  -20.963 41.771   1.00 31.50  ? 307 ASP A OD1 1 
ATOM   2609  O OD2 . ASP A  1 307 ? -8.100  -20.804 43.856   1.00 29.32  ? 307 ASP A OD2 1 
ATOM   2610  N N   . LYS A  1 308 ? -8.910  -19.391 39.129   1.00 22.88  ? 308 LYS A N   1 
ATOM   2611  C CA  . LYS A  1 308 ? -8.387  -19.662 37.797   1.00 17.95  ? 308 LYS A CA  1 
ATOM   2612  C C   . LYS A  1 308 ? -7.349  -20.782 37.810   1.00 21.67  ? 308 LYS A C   1 
ATOM   2613  O O   . LYS A  1 308 ? -7.397  -21.684 36.969   1.00 19.04  ? 308 LYS A O   1 
ATOM   2614  C CB  . LYS A  1 308 ? -7.798  -18.385 37.216   1.00 17.54  ? 308 LYS A CB  1 
ATOM   2615  C CG  . LYS A  1 308 ? -7.401  -18.519 35.728   1.00 25.79  ? 308 LYS A CG  1 
ATOM   2616  C CD  . LYS A  1 308 ? -6.759  -17.237 35.179   1.00 27.75  ? 308 LYS A CD  1 
ATOM   2617  C CE  . LYS A  1 308 ? -6.681  -17.236 33.658   1.00 34.41  ? 308 LYS A CE  1 
ATOM   2618  N NZ  . LYS A  1 308 ? -6.490  -18.589 33.058   1.00 36.03  ? 308 LYS A NZ  1 
ATOM   2619  N N   . THR A  1 309 ? -6.391  -20.739 38.749   1.00 22.66  ? 309 THR A N   1 
ATOM   2620  C CA  . THR A  1 309 ? -5.303  -21.709 38.711   1.00 27.37  ? 309 THR A CA  1 
ATOM   2621  C C   . THR A  1 309 ? -5.820  -23.132 38.904   1.00 24.64  ? 309 THR A C   1 
ATOM   2622  O O   . THR A  1 309 ? -5.403  -24.055 38.198   1.00 25.71  ? 309 THR A O   1 
ATOM   2623  C CB  . THR A  1 309 ? -4.249  -21.383 39.774   1.00 31.66  ? 309 THR A CB  1 
ATOM   2624  O OG1 . THR A  1 309 ? -4.827  -21.547 41.071   1.00 45.29  ? 309 THR A OG1 1 
ATOM   2625  C CG2 . THR A  1 309 ? -3.764  -19.986 39.641   1.00 25.37  ? 309 THR A CG2 1 
ATOM   2626  N N   . LEU A  1 310 ? -6.700  -23.338 39.890   1.00 25.39  ? 310 LEU A N   1 
ATOM   2627  C CA  . LEU A  1 310 ? -7.240  -24.670 40.126   1.00 19.28  ? 310 LEU A CA  1 
ATOM   2628  C C   . LEU A  1 310 ? -8.084  -25.135 38.954   1.00 21.32  ? 310 LEU A C   1 
ATOM   2629  O O   . LEU A  1 310 ? -8.044  -26.316 38.571   1.00 19.97  ? 310 LEU A O   1 
ATOM   2630  C CB  . LEU A  1 310 ? -8.073  -24.687 41.414   1.00 18.16  ? 310 LEU A CB  1 
ATOM   2631  C CG  . LEU A  1 310 ? -7.280  -24.598 42.726   1.00 27.12  ? 310 LEU A CG  1 
ATOM   2632  C CD1 . LEU A  1 310 ? -8.212  -24.637 43.920   1.00 26.42  ? 310 LEU A CD1 1 
ATOM   2633  C CD2 . LEU A  1 310 ? -6.236  -25.691 42.842   1.00 27.23  ? 310 LEU A CD2 1 
ATOM   2634  N N   . SER A  1 311 ? -8.872  -24.221 38.386   1.00 21.75  ? 311 SER A N   1 
ATOM   2635  C CA  . SER A  1 311 ? -9.664  -24.558 37.215   1.00 22.32  ? 311 SER A CA  1 
ATOM   2636  C C   . SER A  1 311 ? -8.762  -24.916 36.033   1.00 23.67  ? 311 SER A C   1 
ATOM   2637  O O   . SER A  1 311 ? -9.045  -25.867 35.303   1.00 26.38  ? 311 SER A O   1 
ATOM   2638  C CB  . SER A  1 311 ? -10.604 -23.396 36.890   1.00 18.41  ? 311 SER A CB  1 
ATOM   2639  O OG  . SER A  1 311 ? -11.412 -23.107 38.027   1.00 20.52  ? 311 SER A OG  1 
ATOM   2640  N N   . ASP A  1 312 ? -7.638  -24.210 35.869   1.00 25.28  ? 312 ASP A N   1 
ATOM   2641  C CA  . ASP A  1 312 ? -6.759  -24.466 34.726   1.00 28.44  ? 312 ASP A CA  1 
ATOM   2642  C C   . ASP A  1 312 ? -5.894  -25.704 34.937   1.00 28.78  ? 312 ASP A C   1 
ATOM   2643  O O   . ASP A  1 312 ? -5.452  -26.328 33.963   1.00 22.00  ? 312 ASP A O   1 
ATOM   2644  C CB  . ASP A  1 312 ? -5.866  -23.249 34.441   1.00 20.92  ? 312 ASP A CB  1 
ATOM   2645  C CG  . ASP A  1 312 ? -6.621  -22.077 33.757   1.00 22.11  ? 312 ASP A CG  1 
ATOM   2646  O OD1 . ASP A  1 312 ? -7.774  -22.234 33.310   1.00 22.51  ? 312 ASP A OD1 1 
ATOM   2647  O OD2 . ASP A  1 312 ? -6.045  -20.975 33.647   1.00 22.60  ? 312 ASP A OD2 1 
ATOM   2648  N N   . LEU A  1 313 ? -5.647  -26.087 36.187   1.00 25.01  ? 313 LEU A N   1 
ATOM   2649  C CA  . LEU A  1 313 ? -4.934  -27.333 36.429   1.00 21.19  ? 313 LEU A CA  1 
ATOM   2650  C C   . LEU A  1 313 ? -5.682  -28.509 35.809   1.00 19.44  ? 313 LEU A C   1 
ATOM   2651  O O   . LEU A  1 313 ? -5.088  -29.344 35.119   1.00 22.07  ? 313 LEU A O   1 
ATOM   2652  C CB  . LEU A  1 313 ? -4.753  -27.536 37.932   1.00 19.51  ? 313 LEU A CB  1 
ATOM   2653  C CG  . LEU A  1 313 ? -3.681  -26.771 38.688   1.00 21.03  ? 313 LEU A CG  1 
ATOM   2654  C CD1 . LEU A  1 313 ? -3.872  -26.980 40.203   1.00 17.37  ? 313 LEU A CD1 1 
ATOM   2655  C CD2 . LEU A  1 313 ? -2.298  -27.225 38.250   1.00 24.62  ? 313 LEU A CD2 1 
ATOM   2656  N N   . ILE A  1 314 ? -7.000  -28.572 36.030   1.00 16.03  ? 314 ILE A N   1 
ATOM   2657  C CA  . ILE A  1 314 ? -7.804  -29.674 35.508   1.00 15.84  ? 314 ILE A CA  1 
ATOM   2658  C C   . ILE A  1 314 ? -7.968  -29.544 33.997   1.00 21.97  ? 314 ILE A C   1 
ATOM   2659  O O   . ILE A  1 314 ? -7.820  -30.518 33.249   1.00 22.43  ? 314 ILE A O   1 
ATOM   2660  C CB  . ILE A  1 314 ? -9.174  -29.684 36.204   1.00 17.79  ? 314 ILE A CB  1 
ATOM   2661  C CG1 . ILE A  1 314 ? -9.026  -30.100 37.663   1.00 17.62  ? 314 ILE A CG1 1 
ATOM   2662  C CG2 . ILE A  1 314 ? -10.169 -30.534 35.454   1.00 16.51  ? 314 ILE A CG2 1 
ATOM   2663  C CD1 . ILE A  1 314 ? -10.379 -30.068 38.409   1.00 17.44  ? 314 ILE A CD1 1 
ATOM   2664  N N   . GLY A  1 315 ? -8.286  -28.335 33.534   1.00 20.39  ? 315 GLY A N   1 
ATOM   2665  C CA  . GLY A  1 315 ? -8.585  -28.118 32.124   1.00 23.16  ? 315 GLY A CA  1 
ATOM   2666  C C   . GLY A  1 315 ? -7.373  -28.026 31.218   1.00 25.27  ? 315 GLY A C   1 
ATOM   2667  O O   . GLY A  1 315 ? -7.489  -28.296 30.011   1.00 27.48  ? 315 GLY A O   1 
ATOM   2668  N N   . PHE A  1 316 ? -6.220  -27.658 31.757   1.00 21.62  ? 316 PHE A N   1 
ATOM   2669  C CA  . PHE A  1 316 ? -5.040  -27.445 30.913   1.00 23.45  ? 316 PHE A CA  1 
ATOM   2670  C C   . PHE A  1 316 ? -3.884  -28.366 31.245   1.00 24.91  ? 316 PHE A C   1 
ATOM   2671  O O   . PHE A  1 316 ? -3.132  -28.742 30.354   1.00 26.13  ? 316 PHE A O   1 
ATOM   2672  C CB  . PHE A  1 316 ? -4.513  -26.010 31.030   1.00 32.23  ? 316 PHE A CB  1 
ATOM   2673  C CG  . PHE A  1 316 ? -5.425  -24.969 30.477   1.00 46.47  ? 316 PHE A CG  1 
ATOM   2674  C CD1 . PHE A  1 316 ? -6.284  -25.253 29.427   1.00 52.97  ? 316 PHE A CD1 1 
ATOM   2675  C CD2 . PHE A  1 316 ? -5.416  -23.686 31.002   1.00 52.57  ? 316 PHE A CD2 1 
ATOM   2676  C CE1 . PHE A  1 316 ? -7.129  -24.278 28.923   1.00 54.24  ? 316 PHE A CE1 1 
ATOM   2677  C CE2 . PHE A  1 316 ? -6.259  -22.706 30.500   1.00 55.26  ? 316 PHE A CE2 1 
ATOM   2678  C CZ  . PHE A  1 316 ? -7.115  -23.004 29.461   1.00 54.43  ? 316 PHE A CZ  1 
ATOM   2679  N N   . SER A  1 317 ? -3.677  -28.691 32.518   1.00 24.72  ? 317 SER A N   1 
ATOM   2680  C CA  . SER A  1 317 ? -2.403  -29.281 32.890   1.00 27.30  ? 317 SER A CA  1 
ATOM   2681  C C   . SER A  1 317 ? -2.448  -30.802 33.021   1.00 24.54  ? 317 SER A C   1 
ATOM   2682  O O   . SER A  1 317 ? -1.559  -31.488 32.515   1.00 22.43  ? 317 SER A O   1 
ATOM   2683  C CB  . SER A  1 317 ? -1.925  -28.637 34.200   1.00 30.84  ? 317 SER A CB  1 
ATOM   2684  O OG  . SER A  1 317 ? -0.622  -29.077 34.515   1.00 42.31  ? 317 SER A OG  1 
ATOM   2685  N N   . TYR A  1 318 ? -3.485  -31.340 33.673   1.00 23.35  ? 318 TYR A N   1 
ATOM   2686  C CA  . TYR A  1 318 ? -3.441  -32.663 34.282   1.00 22.32  ? 318 TYR A CA  1 
ATOM   2687  C C   . TYR A  1 318 ? -3.626  -33.790 33.280   1.00 26.58  ? 318 TYR A C   1 
ATOM   2688  O O   . TYR A  1 318 ? -3.283  -34.942 33.585   1.00 24.22  ? 318 TYR A O   1 
ATOM   2689  C CB  . TYR A  1 318 ? -4.529  -32.768 35.367   1.00 20.28  ? 318 TYR A CB  1 
ATOM   2690  C CG  . TYR A  1 318 ? -4.219  -32.112 36.701   1.00 22.57  ? 318 TYR A CG  1 
ATOM   2691  C CD1 . TYR A  1 318 ? -2.917  -31.791 37.067   1.00 22.47  ? 318 TYR A CD1 1 
ATOM   2692  C CD2 . TYR A  1 318 ? -5.245  -31.857 37.626   1.00 22.67  ? 318 TYR A CD2 1 
ATOM   2693  C CE1 . TYR A  1 318 ? -2.644  -31.204 38.323   1.00 23.51  ? 318 TYR A CE1 1 
ATOM   2694  C CE2 . TYR A  1 318 ? -4.976  -31.287 38.871   1.00 21.39  ? 318 TYR A CE2 1 
ATOM   2695  C CZ  . TYR A  1 318 ? -3.682  -30.968 39.206   1.00 22.65  ? 318 TYR A CZ  1 
ATOM   2696  O OH  . TYR A  1 318 ? -3.429  -30.406 40.427   1.00 30.94  ? 318 TYR A OH  1 
ATOM   2697  N N   . HIS A  1 319 ? -4.160  -33.494 32.092   1.00 27.37  ? 319 HIS A N   1 
ATOM   2698  C CA  . HIS A  1 319 ? -4.224  -34.501 31.042   1.00 28.73  ? 319 HIS A CA  1 
ATOM   2699  C C   . HIS A  1 319 ? -2.857  -35.113 30.766   1.00 29.95  ? 319 HIS A C   1 
ATOM   2700  O O   . HIS A  1 319 ? -2.762  -36.271 30.341   1.00 32.91  ? 319 HIS A O   1 
ATOM   2701  C CB  . HIS A  1 319 ? -4.765  -33.877 29.762   1.00 28.18  ? 319 HIS A CB  1 
ATOM   2702  C CG  . HIS A  1 319 ? -3.762  -33.017 29.061   1.00 29.18  ? 319 HIS A CG  1 
ATOM   2703  N ND1 . HIS A  1 319 ? -3.503  -31.716 29.441   1.00 31.25  ? 319 HIS A ND1 1 
ATOM   2704  C CD2 . HIS A  1 319 ? -2.936  -33.280 28.022   1.00 32.33  ? 319 HIS A CD2 1 
ATOM   2705  C CE1 . HIS A  1 319 ? -2.572  -31.209 28.650   1.00 34.50  ? 319 HIS A CE1 1 
ATOM   2706  N NE2 . HIS A  1 319 ? -2.209  -32.139 27.784   1.00 34.35  ? 319 HIS A NE2 1 
ATOM   2707  N N   . ALA A  1 320 ? -1.797  -34.347 30.984   1.00 26.89  ? 320 ALA A N   1 
ATOM   2708  C CA  . ALA A  1 320 ? -0.429  -34.759 30.715   1.00 29.71  ? 320 ALA A CA  1 
ATOM   2709  C C   . ALA A  1 320 ? 0.230   -35.443 31.911   1.00 30.83  ? 320 ALA A C   1 
ATOM   2710  O O   . ALA A  1 320 ? 1.406   -35.812 31.828   1.00 32.84  ? 320 ALA A O   1 
ATOM   2711  C CB  . ALA A  1 320 ? 0.387   -33.533 30.281   1.00 31.32  ? 320 ALA A CB  1 
ATOM   2712  N N   . TRP A  1 321 ? -0.492  -35.619 33.013   1.00 30.60  ? 321 TRP A N   1 
ATOM   2713  C CA  . TRP A  1 321 ? 0.028   -36.227 34.228   1.00 32.23  ? 321 TRP A CA  1 
ATOM   2714  C C   . TRP A  1 321 ? -0.597  -37.597 34.452   1.00 32.14  ? 321 TRP A C   1 
ATOM   2715  O O   . TRP A  1 321 ? -1.717  -37.878 34.021   1.00 33.31  ? 321 TRP A O   1 
ATOM   2716  C CB  . TRP A  1 321 ? -0.277  -35.384 35.479   1.00 29.45  ? 321 TRP A CB  1 
ATOM   2717  C CG  . TRP A  1 321 ? 0.231   -33.970 35.510   1.00 33.23  ? 321 TRP A CG  1 
ATOM   2718  C CD1 . TRP A  1 321 ? 0.395   -33.118 34.456   1.00 33.42  ? 321 TRP A CD1 1 
ATOM   2719  C CD2 . TRP A  1 321 ? 0.605   -33.237 36.677   1.00 32.92  ? 321 TRP A CD2 1 
ATOM   2720  N NE1 . TRP A  1 321 ? 0.865   -31.906 34.896   1.00 35.71  ? 321 TRP A NE1 1 
ATOM   2721  C CE2 . TRP A  1 321 ? 0.998   -31.952 36.258   1.00 37.06  ? 321 TRP A CE2 1 
ATOM   2722  C CE3 . TRP A  1 321 ? 0.634   -33.540 38.038   1.00 31.81  ? 321 TRP A CE3 1 
ATOM   2723  C CZ2 . TRP A  1 321 ? 1.420   -30.970 37.154   1.00 35.61  ? 321 TRP A CZ2 1 
ATOM   2724  C CZ3 . TRP A  1 321 ? 1.072   -32.570 38.923   1.00 33.96  ? 321 TRP A CZ3 1 
ATOM   2725  C CH2 . TRP A  1 321 ? 1.447   -31.300 38.478   1.00 37.41  ? 321 TRP A CH2 1 
ATOM   2726  N N   . ASN A  1 322 ? 0.128   -38.427 35.191   1.00 29.30  ? 322 ASN A N   1 
ATOM   2727  C CA  . ASN A  1 322 ? -0.466  -39.599 35.816   1.00 34.50  ? 322 ASN A CA  1 
ATOM   2728  C C   . ASN A  1 322 ? -1.517  -39.160 36.836   1.00 32.79  ? 322 ASN A C   1 
ATOM   2729  O O   . ASN A  1 322 ? -1.349  -38.152 37.522   1.00 35.69  ? 322 ASN A O   1 
ATOM   2730  C CB  . ASN A  1 322 ? 0.648   -40.436 36.471   1.00 43.00  ? 322 ASN A CB  1 
ATOM   2731  C CG  . ASN A  1 322 ? 0.131   -41.408 37.510   1.00 53.41  ? 322 ASN A CG  1 
ATOM   2732  O OD1 . ASN A  1 322 ? 0.021   -41.077 38.689   1.00 56.49  ? 322 ASN A OD1 1 
ATOM   2733  N ND2 . ASN A  1 322 ? -0.178  -42.622 37.079   1.00 58.18  ? 322 ASN A ND2 1 
ATOM   2734  N N   . ALA A  1 323 ? -2.614  -39.921 36.927   1.00 33.16  ? 323 ALA A N   1 
ATOM   2735  C CA  . ALA A  1 323 ? -3.740  -39.531 37.780   1.00 33.98  ? 323 ALA A CA  1 
ATOM   2736  C C   . ALA A  1 323 ? -3.319  -39.343 39.238   1.00 35.64  ? 323 ALA A C   1 
ATOM   2737  O O   . ALA A  1 323 ? -3.689  -38.355 39.876   1.00 34.90  ? 323 ALA A O   1 
ATOM   2738  C CB  . ALA A  1 323 ? -4.856  -40.572 37.679   1.00 28.55  ? 323 ALA A CB  1 
ATOM   2739  N N   . GLU A  1 324 ? -2.558  -40.290 39.791   1.00 37.71  ? 324 GLU A N   1 
ATOM   2740  C CA  . GLU A  1 324 ? -2.128  -40.178 41.187   1.00 42.72  ? 324 GLU A CA  1 
ATOM   2741  C C   . GLU A  1 324 ? -1.379  -38.870 41.446   1.00 38.26  ? 324 GLU A C   1 
ATOM   2742  O O   . GLU A  1 324 ? -1.669  -38.154 42.412   1.00 41.65  ? 324 GLU A O   1 
ATOM   2743  C CB  . GLU A  1 324 ? -1.260  -41.379 41.565   1.00 53.84  ? 324 GLU A CB  1 
ATOM   2744  C CG  . GLU A  1 324 ? -1.535  -41.945 42.948   1.00 65.26  ? 324 GLU A CG  1 
ATOM   2745  C CD  . GLU A  1 324 ? -0.604  -41.379 44.008   1.00 77.43  ? 324 GLU A CD  1 
ATOM   2746  O OE1 . GLU A  1 324 ? -1.038  -41.250 45.174   1.00 80.77  ? 324 GLU A OE1 1 
ATOM   2747  O OE2 . GLU A  1 324 ? 0.562   -41.070 43.679   1.00 82.15  ? 324 GLU A OE2 1 
ATOM   2748  N N   . ASP A  1 325 ? -0.417  -38.538 40.585   1.00 28.82  ? 325 ASP A N   1 
ATOM   2749  C CA  . ASP A  1 325 ? 0.377   -37.332 40.793   1.00 31.28  ? 325 ASP A CA  1 
ATOM   2750  C C   . ASP A  1 325 ? -0.472  -36.071 40.657   1.00 30.77  ? 325 ASP A C   1 
ATOM   2751  O O   . ASP A  1 325 ? -0.286  -35.113 41.416   1.00 35.04  ? 325 ASP A O   1 
ATOM   2752  C CB  . ASP A  1 325 ? 1.552   -37.304 39.815   1.00 38.70  ? 325 ASP A CB  1 
ATOM   2753  C CG  . ASP A  1 325 ? 2.497   -38.476 40.004   1.00 48.90  ? 325 ASP A CG  1 
ATOM   2754  O OD1 . ASP A  1 325 ? 2.197   -39.376 40.812   1.00 50.65  ? 325 ASP A OD1 1 
ATOM   2755  O OD2 . ASP A  1 325 ? 3.552   -38.498 39.331   1.00 54.57  ? 325 ASP A OD2 1 
ATOM   2756  N N   . ALA A  1 326 ? -1.405  -36.063 39.698   1.00 26.92  ? 326 ALA A N   1 
ATOM   2757  C CA  . ALA A  1 326 ? -2.340  -34.954 39.531   1.00 23.70  ? 326 ALA A CA  1 
ATOM   2758  C C   . ALA A  1 326 ? -3.157  -34.710 40.795   1.00 26.11  ? 326 ALA A C   1 
ATOM   2759  O O   . ALA A  1 326 ? -3.270  -33.571 41.266   1.00 25.81  ? 326 ALA A O   1 
ATOM   2760  C CB  . ALA A  1 326 ? -3.281  -35.237 38.348   1.00 19.44  ? 326 ALA A CB  1 
ATOM   2761  N N   . VAL A  1 327 ? -3.748  -35.773 41.343   1.00 22.84  ? 327 VAL A N   1 
ATOM   2762  C CA  . VAL A  1 327 ? -4.635  -35.672 42.510   1.00 26.01  ? 327 VAL A CA  1 
ATOM   2763  C C   . VAL A  1 327 ? -3.867  -35.227 43.757   1.00 25.97  ? 327 VAL A C   1 
ATOM   2764  O O   . VAL A  1 327 ? -4.307  -34.337 44.496   1.00 29.85  ? 327 VAL A O   1 
ATOM   2765  C CB  . VAL A  1 327 ? -5.343  -37.023 42.740   1.00 26.42  ? 327 VAL A CB  1 
ATOM   2766  C CG1 . VAL A  1 327 ? -5.980  -37.095 44.129   1.00 27.01  ? 327 VAL A CG1 1 
ATOM   2767  C CG2 . VAL A  1 327 ? -6.398  -37.238 41.670   1.00 28.24  ? 327 VAL A CG2 1 
ATOM   2768  N N   . ARG A  1 328 ? -2.708  -35.820 44.010   1.00 24.88  ? 328 ARG A N   1 
ATOM   2769  C CA  . ARG A  1 328 ? -1.887  -35.357 45.126   1.00 32.03  ? 328 ARG A CA  1 
ATOM   2770  C C   . ARG A  1 328 ? -1.488  -33.896 44.961   1.00 31.80  ? 328 ARG A C   1 
ATOM   2771  O O   . ARG A  1 328 ? -1.377  -33.169 45.954   1.00 29.87  ? 328 ARG A O   1 
ATOM   2772  C CB  . ARG A  1 328 ? -0.645  -36.232 45.264   1.00 39.66  ? 328 ARG A CB  1 
ATOM   2773  C CG  . ARG A  1 328 ? -0.904  -37.678 45.725   1.00 54.02  ? 328 ARG A CG  1 
ATOM   2774  C CD  . ARG A  1 328 ? -2.001  -37.848 46.829   1.00 62.77  ? 328 ARG A CD  1 
ATOM   2775  N NE  . ARG A  1 328 ? -2.240  -39.265 47.146   1.00 70.34  ? 328 ARG A NE  1 
ATOM   2776  C CZ  . ARG A  1 328 ? -3.447  -39.812 47.334   1.00 75.19  ? 328 ARG A CZ  1 
ATOM   2777  N NH1 . ARG A  1 328 ? -3.567  -41.114 47.608   1.00 76.52  ? 328 ARG A NH1 1 
ATOM   2778  N NH2 . ARG A  1 328 ? -4.542  -39.073 47.201   1.00 73.98  ? 328 ARG A NH2 1 
ATOM   2779  N N   . ASP A  1 329 ? -1.289  -33.443 43.719   1.00 30.54  ? 329 ASP A N   1 
ATOM   2780  C CA  . ASP A  1 329 ? -0.932  -32.047 43.488   1.00 27.72  ? 329 ASP A CA  1 
ATOM   2781  C C   . ASP A  1 329 ? -2.101  -31.137 43.813   1.00 26.71  ? 329 ASP A C   1 
ATOM   2782  O O   . ASP A  1 329 ? -1.944  -30.119 44.501   1.00 26.32  ? 329 ASP A O   1 
ATOM   2783  C CB  . ASP A  1 329 ? -0.503  -31.846 42.033   1.00 30.37  ? 329 ASP A CB  1 
ATOM   2784  C CG  . ASP A  1 329 ? -0.217  -30.386 41.698   1.00 31.00  ? 329 ASP A CG  1 
ATOM   2785  O OD1 . ASP A  1 329 ? -1.162  -29.641 41.323   1.00 24.45  ? 329 ASP A OD1 1 
ATOM   2786  O OD2 . ASP A  1 329 ? 0.966   -29.994 41.794   1.00 33.25  ? 329 ASP A OD2 1 
ATOM   2787  N N   . PHE A  1 330 ? -3.281  -31.501 43.312   1.00 19.41  ? 330 PHE A N   1 
ATOM   2788  C CA  . PHE A  1 330 ? -4.499  -30.746 43.550   1.00 20.92  ? 330 PHE A CA  1 
ATOM   2789  C C   . PHE A  1 330 ? -4.834  -30.661 45.042   1.00 18.78  ? 330 PHE A C   1 
ATOM   2790  O O   . PHE A  1 330 ? -5.200  -29.589 45.545   1.00 19.31  ? 330 PHE A O   1 
ATOM   2791  C CB  . PHE A  1 330 ? -5.644  -31.401 42.788   1.00 18.71  ? 330 PHE A CB  1 
ATOM   2792  C CG  . PHE A  1 330 ? -6.848  -30.504 42.595   1.00 21.20  ? 330 PHE A CG  1 
ATOM   2793  C CD1 . PHE A  1 330 ? -6.859  -29.543 41.602   1.00 19.70  ? 330 PHE A CD1 1 
ATOM   2794  C CD2 . PHE A  1 330 ? -7.979  -30.661 43.389   1.00 23.26  ? 330 PHE A CD2 1 
ATOM   2795  C CE1 . PHE A  1 330 ? -7.975  -28.727 41.411   1.00 20.29  ? 330 PHE A CE1 1 
ATOM   2796  C CE2 . PHE A  1 330 ? -9.087  -29.862 43.205   1.00 23.95  ? 330 PHE A CE2 1 
ATOM   2797  C CZ  . PHE A  1 330 ? -9.089  -28.896 42.210   1.00 22.13  ? 330 PHE A CZ  1 
ATOM   2798  N N   . ILE A  1 331 ? -4.809  -31.796 45.732   1.00 21.50  ? 331 ILE A N   1 
ATOM   2799  C CA  . ILE A  1 331 ? -5.086  -31.808 47.175   1.00 26.71  ? 331 ILE A CA  1 
ATOM   2800  C C   . ILE A  1 331 ? -4.054  -30.973 47.927   1.00 30.20  ? 331 ILE A C   1 
ATOM   2801  O O   . ILE A  1 331 ? -4.385  -30.265 48.889   1.00 33.04  ? 331 ILE A O   1 
ATOM   2802  C CB  . ILE A  1 331 ? -5.117  -33.256 47.702   1.00 30.20  ? 331 ILE A CB  1 
ATOM   2803  C CG1 . ILE A  1 331 ? -6.186  -34.075 46.986   1.00 33.05  ? 331 ILE A CG1 1 
ATOM   2804  C CG2 . ILE A  1 331 ? -5.310  -33.292 49.246   1.00 30.47  ? 331 ILE A CG2 1 
ATOM   2805  C CD1 . ILE A  1 331 ? -7.519  -33.411 46.937   1.00 31.85  ? 331 ILE A CD1 1 
ATOM   2806  N N   . GLY A  1 332 ? -2.783  -31.072 47.526   1.00 28.42  ? 332 GLY A N   1 
ATOM   2807  C CA  . GLY A  1 332 ? -1.763  -30.209 48.096   1.00 29.10  ? 332 GLY A CA  1 
ATOM   2808  C C   . GLY A  1 332 ? -2.084  -28.730 47.952   1.00 33.17  ? 332 GLY A C   1 
ATOM   2809  O O   . GLY A  1 332 ? -1.848  -27.945 48.875   1.00 29.14  ? 332 GLY A O   1 
ATOM   2810  N N   . ARG A  1 333 ? -2.615  -28.322 46.789   1.00 32.91  ? 333 ARG A N   1 
ATOM   2811  C CA  . ARG A  1 333 ? -2.887  -26.901 46.576   1.00 26.36  ? 333 ARG A CA  1 
ATOM   2812  C C   . ARG A  1 333 ? -4.034  -26.423 47.448   1.00 23.67  ? 333 ARG A C   1 
ATOM   2813  O O   . ARG A  1 333 ? -3.974  -25.325 48.017   1.00 29.47  ? 333 ARG A O   1 
ATOM   2814  C CB  . ARG A  1 333 ? -3.199  -26.614 45.105   1.00 24.38  ? 333 ARG A CB  1 
ATOM   2815  C CG  . ARG A  1 333 ? -2.108  -27.056 44.199   1.00 34.27  ? 333 ARG A CG  1 
ATOM   2816  C CD  . ARG A  1 333 ? -1.941  -26.173 42.987   1.00 40.54  ? 333 ARG A CD  1 
ATOM   2817  N NE  . ARG A  1 333 ? -1.005  -26.806 42.061   1.00 41.38  ? 333 ARG A NE  1 
ATOM   2818  C CZ  . ARG A  1 333 ? 0.310   -26.845 42.244   1.00 49.05  ? 333 ARG A CZ  1 
ATOM   2819  N NH1 . ARG A  1 333 ? 0.857   -26.267 43.309   1.00 51.02  ? 333 ARG A NH1 1 
ATOM   2820  N NH2 . ARG A  1 333 ? 1.084   -27.457 41.360   1.00 52.77  ? 333 ARG A NH2 1 
ATOM   2821  N N   . LEU A  1 334 ? -5.107  -27.210 47.515   1.00 25.19  ? 334 LEU A N   1 
ATOM   2822  C CA  . LEU A  1 334 ? -6.199  -26.915 48.436   1.00 26.22  ? 334 LEU A CA  1 
ATOM   2823  C C   . LEU A  1 334 ? -5.700  -26.807 49.870   1.00 23.79  ? 334 LEU A C   1 
ATOM   2824  O O   . LEU A  1 334 ? -6.162  -25.953 50.636   1.00 26.77  ? 334 LEU A O   1 
ATOM   2825  C CB  . LEU A  1 334 ? -7.265  -28.005 48.325   1.00 27.69  ? 334 LEU A CB  1 
ATOM   2826  C CG  . LEU A  1 334 ? -7.919  -28.098 46.951   1.00 25.16  ? 334 LEU A CG  1 
ATOM   2827  C CD1 . LEU A  1 334 ? -8.787  -29.332 46.894   1.00 23.90  ? 334 LEU A CD1 1 
ATOM   2828  C CD2 . LEU A  1 334 ? -8.727  -26.824 46.683   1.00 26.19  ? 334 LEU A CD2 1 
ATOM   2829  N N   . LYS A  1 335 ? -4.746  -27.660 50.247   1.00 27.55  ? 335 LYS A N   1 
ATOM   2830  C CA  . LYS A  1 335 ? -4.213  -27.615 51.609   1.00 26.20  ? 335 LYS A CA  1 
ATOM   2831  C C   . LYS A  1 335 ? -3.518  -26.287 51.904   1.00 30.19  ? 335 LYS A C   1 
ATOM   2832  O O   . LYS A  1 335 ? -3.659  -25.736 53.004   1.00 31.07  ? 335 LYS A O   1 
ATOM   2833  C CB  . LYS A  1 335 ? -3.253  -28.781 51.843   1.00 29.09  ? 335 LYS A CB  1 
ATOM   2834  C CG  . LYS A  1 335 ? -2.551  -28.678 53.192   1.00 40.13  ? 335 LYS A CG  1 
ATOM   2835  C CD  . LYS A  1 335 ? -2.212  -30.028 53.786   1.00 51.56  ? 335 LYS A CD  1 
ATOM   2836  C CE  . LYS A  1 335 ? -1.088  -30.701 53.027   1.00 58.87  ? 335 LYS A CE  1 
ATOM   2837  N NZ  . LYS A  1 335 ? -0.551  -31.860 53.795   1.00 65.82  ? 335 LYS A NZ  1 
ATOM   2838  N N   . LYS A  1 336 ? -2.748  -25.761 50.941   1.00 28.21  ? 336 LYS A N   1 
ATOM   2839  C CA  . LYS A  1 336 ? -2.105  -24.463 51.139   1.00 31.93  ? 336 LYS A CA  1 
ATOM   2840  C C   . LYS A  1 336 ? -3.125  -23.335 51.203   1.00 27.41  ? 336 LYS A C   1 
ATOM   2841  O O   . LYS A  1 336 ? -2.972  -22.396 51.991   1.00 30.74  ? 336 LYS A O   1 
ATOM   2842  C CB  . LYS A  1 336 ? -1.086  -24.189 50.032   1.00 41.98  ? 336 LYS A CB  1 
ATOM   2843  C CG  . LYS A  1 336 ? -0.374  -25.421 49.520   1.00 51.44  ? 336 LYS A CG  1 
ATOM   2844  C CD  . LYS A  1 336 ? 0.450   -26.125 50.601   1.00 59.56  ? 336 LYS A CD  1 
ATOM   2845  C CE  . LYS A  1 336 ? 0.984   -27.480 50.106   1.00 62.33  ? 336 LYS A CE  1 
ATOM   2846  N NZ  . LYS A  1 336 ? 0.169   -28.641 50.589   1.00 59.48  ? 336 LYS A NZ  1 
ATOM   2847  N N   . ILE A  1 337 ? -4.163  -23.389 50.369   1.00 24.90  ? 337 ILE A N   1 
ATOM   2848  C CA  . ILE A  1 337 ? -5.261  -22.435 50.514   1.00 24.58  ? 337 ILE A CA  1 
ATOM   2849  C C   . ILE A  1 337 ? -5.869  -22.539 51.910   1.00 24.08  ? 337 ILE A C   1 
ATOM   2850  O O   . ILE A  1 337 ? -6.089  -21.531 52.593   1.00 28.81  ? 337 ILE A O   1 
ATOM   2851  C CB  . ILE A  1 337 ? -6.322  -22.667 49.426   1.00 21.02  ? 337 ILE A CB  1 
ATOM   2852  C CG1 . ILE A  1 337 ? -5.755  -22.349 48.036   1.00 21.72  ? 337 ILE A CG1 1 
ATOM   2853  C CG2 . ILE A  1 337 ? -7.540  -21.824 49.698   1.00 18.19  ? 337 ILE A CG2 1 
ATOM   2854  C CD1 . ILE A  1 337 ? -6.651  -22.842 46.875   1.00 24.01  ? 337 ILE A CD1 1 
ATOM   2855  N N   . HIS A  1 338 ? -6.155  -23.766 52.349   1.00 25.48  ? 338 HIS A N   1 
ATOM   2856  C CA  . HIS A  1 338 ? -6.773  -23.959 53.662   1.00 26.41  ? 338 HIS A CA  1 
ATOM   2857  C C   . HIS A  1 338 ? -5.898  -23.365 54.757   1.00 34.14  ? 338 HIS A C   1 
ATOM   2858  O O   . HIS A  1 338 ? -6.397  -22.726 55.690   1.00 36.78  ? 338 HIS A O   1 
ATOM   2859  C CB  . HIS A  1 338 ? -7.024  -25.455 53.899   1.00 25.05  ? 338 HIS A CB  1 
ATOM   2860  C CG  . HIS A  1 338 ? -7.519  -25.787 55.278   1.00 27.19  ? 338 HIS A CG  1 
ATOM   2861  N ND1 . HIS A  1 338 ? -6.761  -26.491 56.191   1.00 33.33  ? 338 HIS A ND1 1 
ATOM   2862  C CD2 . HIS A  1 338 ? -8.701  -25.530 55.890   1.00 27.95  ? 338 HIS A CD2 1 
ATOM   2863  C CE1 . HIS A  1 338 ? -7.443  -26.628 57.318   1.00 32.41  ? 338 HIS A CE1 1 
ATOM   2864  N NE2 . HIS A  1 338 ? -8.624  -26.054 57.160   1.00 33.52  ? 338 HIS A NE2 1 
ATOM   2865  N N   . GLU A  1 339 ? -4.585  -23.528 54.633   1.00 35.10  ? 339 GLU A N   1 
ATOM   2866  C CA  . GLU A  1 339 ? -3.650  -23.022 55.618   1.00 37.42  ? 339 GLU A CA  1 
ATOM   2867  C C   . GLU A  1 339 ? -3.244  -21.582 55.367   1.00 34.55  ? 339 GLU A C   1 
ATOM   2868  O O   . GLU A  1 339 ? -2.545  -21.008 56.204   1.00 39.77  ? 339 GLU A O   1 
ATOM   2869  C CB  . GLU A  1 339 ? -2.397  -23.895 55.665   1.00 38.88  ? 339 GLU A CB  1 
ATOM   2870  C CG  . GLU A  1 339 ? -2.644  -25.315 56.128   1.00 47.02  ? 339 GLU A CG  1 
ATOM   2871  C CD  . GLU A  1 339 ? -1.527  -26.253 55.712   1.00 54.79  ? 339 GLU A CD  1 
ATOM   2872  O OE1 . GLU A  1 339 ? -0.740  -25.876 54.813   1.00 59.73  ? 339 GLU A OE1 1 
ATOM   2873  O OE2 . GLU A  1 339 ? -1.444  -27.371 56.265   1.00 55.81  ? 339 GLU A OE2 1 
ATOM   2874  N N   . SER A  1 340 ? -3.661  -20.981 54.255   1.00 31.51  ? 340 SER A N   1 
ATOM   2875  C CA  . SER A  1 340 ? -3.237  -19.617 53.956   1.00 30.25  ? 340 SER A CA  1 
ATOM   2876  C C   . SER A  1 340 ? -4.132  -18.552 54.575   1.00 28.54  ? 340 SER A C   1 
ATOM   2877  O O   . SER A  1 340 ? -3.717  -17.388 54.647   1.00 32.86  ? 340 SER A O   1 
ATOM   2878  C CB  . SER A  1 340 ? -3.167  -19.383 52.442   1.00 31.88  ? 340 SER A CB  1 
ATOM   2879  O OG  . SER A  1 340 ? -4.453  -19.178 51.880   1.00 33.71  ? 340 SER A OG  1 
ATOM   2880  N N   . VAL A  1 341 ? -5.338  -18.898 55.019   1.00 27.16  ? 341 VAL A N   1 
ATOM   2881  C CA  . VAL A  1 341 ? -6.251  -17.888 55.548   1.00 33.08  ? 341 VAL A CA  1 
ATOM   2882  C C   . VAL A  1 341 ? -6.839  -18.374 56.866   1.00 32.14  ? 341 VAL A C   1 
ATOM   2883  O O   . VAL A  1 341 ? -6.949  -19.578 57.107   1.00 28.55  ? 341 VAL A O   1 
ATOM   2884  C CB  . VAL A  1 341 ? -7.376  -17.539 54.546   1.00 30.18  ? 341 VAL A CB  1 
ATOM   2885  C CG1 . VAL A  1 341 ? -6.794  -16.876 53.320   1.00 32.57  ? 341 VAL A CG1 1 
ATOM   2886  C CG2 . VAL A  1 341 ? -8.168  -18.786 54.169   1.00 32.09  ? 341 VAL A CG2 1 
ATOM   2887  N N   . ASP A  1 342 ? -7.224  -17.425 57.718   1.00 35.72  ? 342 ASP A N   1 
ATOM   2888  C CA  . ASP A  1 342 ? -7.848  -17.747 58.995   1.00 36.31  ? 342 ASP A CA  1 
ATOM   2889  C C   . ASP A  1 342 ? -9.356  -17.925 58.897   1.00 35.53  ? 342 ASP A C   1 
ATOM   2890  O O   . ASP A  1 342 ? -9.963  -18.427 59.842   1.00 41.48  ? 342 ASP A O   1 
ATOM   2891  C CB  . ASP A  1 342 ? -7.535  -16.657 60.023   1.00 48.18  ? 342 ASP A CB  1 
ATOM   2892  C CG  . ASP A  1 342 ? -6.295  -16.962 60.830   1.00 55.22  ? 342 ASP A CG  1 
ATOM   2893  O OD1 . ASP A  1 342 ? -5.322  -17.486 60.248   1.00 58.02  ? 342 ASP A OD1 1 
ATOM   2894  O OD2 . ASP A  1 342 ? -6.290  -16.681 62.047   1.00 59.45  ? 342 ASP A OD2 1 
ATOM   2895  N N   . PHE A  1 343 ? -9.981  -17.542 57.789   1.00 33.47  ? 343 PHE A N   1 
ATOM   2896  C CA  . PHE A  1 343 ? -11.414 -17.722 57.634   1.00 32.05  ? 343 PHE A CA  1 
ATOM   2897  C C   . PHE A  1 343 ? -11.670 -18.956 56.766   1.00 29.95  ? 343 PHE A C   1 
ATOM   2898  O O   . PHE A  1 343 ? -10.746 -19.652 56.341   1.00 30.69  ? 343 PHE A O   1 
ATOM   2899  C CB  . PHE A  1 343 ? -12.062 -16.446 57.069   1.00 28.07  ? 343 PHE A CB  1 
ATOM   2900  C CG  . PHE A  1 343 ? -11.551 -16.041 55.718   1.00 25.81  ? 343 PHE A CG  1 
ATOM   2901  C CD1 . PHE A  1 343 ? -10.369 -15.309 55.588   1.00 25.63  ? 343 PHE A CD1 1 
ATOM   2902  C CD2 . PHE A  1 343 ? -12.262 -16.371 54.573   1.00 25.65  ? 343 PHE A CD2 1 
ATOM   2903  C CE1 . PHE A  1 343 ? -9.908  -14.930 54.329   1.00 27.98  ? 343 PHE A CE1 1 
ATOM   2904  C CE2 . PHE A  1 343 ? -11.811 -16.003 53.317   1.00 28.00  ? 343 PHE A CE2 1 
ATOM   2905  C CZ  . PHE A  1 343 ? -10.630 -15.274 53.187   1.00 29.67  ? 343 PHE A CZ  1 
ATOM   2906  N N   . GLN A  1 344 ? -12.938 -19.265 56.538   1.00 28.99  ? 344 GLN A N   1 
ATOM   2907  C CA  . GLN A  1 344 ? -13.246 -20.401 55.681   1.00 21.13  ? 344 GLN A CA  1 
ATOM   2908  C C   . GLN A  1 344 ? -13.413 -19.905 54.244   1.00 22.87  ? 344 GLN A C   1 
ATOM   2909  O O   . GLN A  1 344 ? -14.443 -19.309 53.908   1.00 26.90  ? 344 GLN A O   1 
ATOM   2910  C CB  . GLN A  1 344 ? -14.508 -21.117 56.160   1.00 24.40  ? 344 GLN A CB  1 
ATOM   2911  C CG  . GLN A  1 344 ? -14.409 -21.565 57.615   1.00 25.01  ? 344 GLN A CG  1 
ATOM   2912  C CD  . GLN A  1 344 ? -15.625 -22.339 58.085   1.00 29.28  ? 344 GLN A CD  1 
ATOM   2913  O OE1 . GLN A  1 344 ? -15.542 -23.529 58.403   1.00 28.47  ? 344 GLN A OE1 1 
ATOM   2914  N NE2 . GLN A  1 344 ? -16.756 -21.659 58.159   1.00 28.71  ? 344 GLN A NE2 1 
ATOM   2915  N N   . PRO A  1 345 ? -12.428 -20.121 53.378   1.00 23.13  ? 345 PRO A N   1 
ATOM   2916  C CA  . PRO A  1 345 ? -12.527 -19.618 51.998   1.00 19.96  ? 345 PRO A CA  1 
ATOM   2917  C C   . PRO A  1 345 ? -13.509 -20.414 51.151   1.00 21.32  ? 345 PRO A C   1 
ATOM   2918  O O   . PRO A  1 345 ? -13.755 -21.597 51.389   1.00 27.61  ? 345 PRO A O   1 
ATOM   2919  C CB  . PRO A  1 345 ? -11.105 -19.797 51.466   1.00 18.53  ? 345 PRO A CB  1 
ATOM   2920  C CG  . PRO A  1 345 ? -10.641 -21.014 52.125   1.00 20.63  ? 345 PRO A CG  1 
ATOM   2921  C CD  . PRO A  1 345 ? -11.232 -20.973 53.552   1.00 24.85  ? 345 PRO A CD  1 
ATOM   2922  N N   . VAL A  1 346 ? -14.058 -19.758 50.129   1.00 19.48  ? 346 VAL A N   1 
ATOM   2923  C CA  . VAL A  1 346 ? -14.941 -20.412 49.165   1.00 23.52  ? 346 VAL A CA  1 
ATOM   2924  C C   . VAL A  1 346 ? -14.182 -20.501 47.847   1.00 23.98  ? 346 VAL A C   1 
ATOM   2925  O O   . VAL A  1 346 ? -13.739 -19.483 47.303   1.00 22.02  ? 346 VAL A O   1 
ATOM   2926  C CB  . VAL A  1 346 ? -16.280 -19.676 49.000   1.00 25.08  ? 346 VAL A CB  1 
ATOM   2927  C CG1 . VAL A  1 346 ? -17.144 -20.412 47.981   1.00 27.71  ? 346 VAL A CG1 1 
ATOM   2928  C CG2 . VAL A  1 346 ? -17.014 -19.616 50.316   1.00 27.66  ? 346 VAL A CG2 1 
ATOM   2929  N N   . VAL A  1 347 ? -13.989 -21.722 47.358   1.00 24.83  ? 347 VAL A N   1 
ATOM   2930  C CA  . VAL A  1 347 ? -13.095 -21.976 46.236   1.00 22.78  ? 347 VAL A CA  1 
ATOM   2931  C C   . VAL A  1 347 ? -13.918 -22.560 45.102   1.00 19.30  ? 347 VAL A C   1 
ATOM   2932  O O   . VAL A  1 347 ? -14.319 -23.732 45.153   1.00 22.88  ? 347 VAL A O   1 
ATOM   2933  C CB  . VAL A  1 347 ? -11.939 -22.912 46.615   1.00 25.21  ? 347 VAL A CB  1 
ATOM   2934  C CG1 . VAL A  1 347 ? -10.934 -22.971 45.472   1.00 21.63  ? 347 VAL A CG1 1 
ATOM   2935  C CG2 . VAL A  1 347 ? -11.265 -22.427 47.916   1.00 29.01  ? 347 VAL A CG2 1 
ATOM   2936  N N   . PHE A  1 348 ? -14.144 -21.758 44.068   1.00 21.89  ? 348 PHE A N   1 
ATOM   2937  C CA  . PHE A  1 348 ? -14.955 -22.153 42.925   1.00 19.86  ? 348 PHE A CA  1 
ATOM   2938  C C   . PHE A  1 348 ? -14.050 -22.698 41.832   1.00 20.98  ? 348 PHE A C   1 
ATOM   2939  O O   . PHE A  1 348 ? -13.157 -21.995 41.365   1.00 23.20  ? 348 PHE A O   1 
ATOM   2940  C CB  . PHE A  1 348 ? -15.763 -20.968 42.414   1.00 17.92  ? 348 PHE A CB  1 
ATOM   2941  C CG  . PHE A  1 348 ? -17.181 -20.960 42.879   1.00 22.77  ? 348 PHE A CG  1 
ATOM   2942  C CD1 . PHE A  1 348 ? -17.485 -20.738 44.218   1.00 25.05  ? 348 PHE A CD1 1 
ATOM   2943  C CD2 . PHE A  1 348 ? -18.211 -21.139 41.977   1.00 23.57  ? 348 PHE A CD2 1 
ATOM   2944  C CE1 . PHE A  1 348 ? -18.794 -20.709 44.652   1.00 22.28  ? 348 PHE A CE1 1 
ATOM   2945  C CE2 . PHE A  1 348 ? -19.521 -21.126 42.408   1.00 21.03  ? 348 PHE A CE2 1 
ATOM   2946  C CZ  . PHE A  1 348 ? -19.809 -20.913 43.751   1.00 25.49  ? 348 PHE A CZ  1 
ATOM   2947  N N   . VAL A  1 349 ? -14.240 -23.969 41.479   1.00 19.32  ? 349 VAL A N   1 
ATOM   2948  C CA  . VAL A  1 349 ? -13.545 -24.613 40.366   1.00 14.78  ? 349 VAL A CA  1 
ATOM   2949  C C   . VAL A  1 349 ? -14.566 -24.688 39.234   1.00 19.21  ? 349 VAL A C   1 
ATOM   2950  O O   . VAL A  1 349 ? -15.563 -25.423 39.323   1.00 21.89  ? 349 VAL A O   1 
ATOM   2951  C CB  . VAL A  1 349 ? -13.017 -26.004 40.756   1.00 16.99  ? 349 VAL A CB  1 
ATOM   2952  C CG1 . VAL A  1 349 ? -12.499 -26.766 39.555   1.00 20.70  ? 349 VAL A CG1 1 
ATOM   2953  C CG2 . VAL A  1 349 ? -11.928 -25.889 41.884   1.00 17.61  ? 349 VAL A CG2 1 
ATOM   2954  N N   . VAL A  1 350 ? -14.363 -23.882 38.199   1.00 20.97  ? 350 VAL A N   1 
ATOM   2955  C CA  . VAL A  1 350 ? -15.359 -23.722 37.144   1.00 21.09  ? 350 VAL A CA  1 
ATOM   2956  C C   . VAL A  1 350 ? -14.689 -23.922 35.791   1.00 20.49  ? 350 VAL A C   1 
ATOM   2957  O O   . VAL A  1 350 ? -13.775 -23.173 35.434   1.00 17.28  ? 350 VAL A O   1 
ATOM   2958  C CB  . VAL A  1 350 ? -16.042 -22.344 37.192   1.00 20.10  ? 350 VAL A CB  1 
ATOM   2959  C CG1 . VAL A  1 350 ? -17.144 -22.288 36.125   1.00 22.59  ? 350 VAL A CG1 1 
ATOM   2960  C CG2 . VAL A  1 350 ? -16.627 -22.079 38.584   1.00 24.12  ? 350 VAL A CG2 1 
ATOM   2961  N N   . LEU A  1 351 ? -15.157 -24.912 35.037   1.00 19.91  ? 351 LEU A N   1 
ATOM   2962  C CA  . LEU A  1 351 ? -14.677 -25.106 33.674   1.00 22.91  ? 351 LEU A CA  1 
ATOM   2963  C C   . LEU A  1 351 ? -15.698 -25.931 32.906   1.00 20.02  ? 351 LEU A C   1 
ATOM   2964  O O   . LEU A  1 351 ? -16.708 -26.390 33.453   1.00 17.19  ? 351 LEU A O   1 
ATOM   2965  C CB  . LEU A  1 351 ? -13.294 -25.759 33.664   1.00 23.44  ? 351 LEU A CB  1 
ATOM   2966  C CG  . LEU A  1 351 ? -13.129 -27.127 34.308   1.00 23.19  ? 351 LEU A CG  1 
ATOM   2967  C CD1 . LEU A  1 351 ? -11.996 -27.873 33.614   1.00 24.41  ? 351 LEU A CD1 1 
ATOM   2968  C CD2 . LEU A  1 351 ? -12.826 -26.956 35.784   1.00 27.79  ? 351 LEU A CD2 1 
ATOM   2969  N N   . ASN A  1 352 ? -15.437 -26.092 31.617   1.00 19.54  ? 352 ASN A N   1 
ATOM   2970  C CA  . ASN A  1 352 ? -16.258 -26.950 30.804   1.00 21.16  ? 352 ASN A CA  1 
ATOM   2971  C C   . ASN A  1 352 ? -16.166 -28.407 31.345   1.00 19.09  ? 352 ASN A C   1 
ATOM   2972  O O   . ASN A  1 352 ? -15.154 -28.816 31.761   1.00 19.05  ? 352 ASN A O   1 
ATOM   2973  C CB  . ASN A  1 352 ? -15.889 -26.875 29.331   1.00 23.67  ? 352 ASN A CB  1 
ATOM   2974  C CG  . ASN A  1 352 ? -16.684 -25.874 28.557   1.00 27.44  ? 352 ASN A CG  1 
ATOM   2975  O OD1 . ASN A  1 352 ? -16.296 -24.741 28.453   1.00 26.78  ? 352 ASN A OD1 1 
ATOM   2976  N ND2 . ASN A  1 352 ? -17.769 -26.321 27.949   1.00 23.94  ? 352 ASN A ND2 1 
ATOM   2977  N N   . GLY A  1 353 ? -17.318 -29.046 31.445   1.00 14.98  ? 353 GLY A N   1 
ATOM   2978  C CA  . GLY A  1 353 ? -17.374 -30.407 31.945   1.00 17.06  ? 353 GLY A CA  1 
ATOM   2979  C C   . GLY A  1 353 ? -17.143 -31.539 30.960   1.00 21.88  ? 353 GLY A C   1 
ATOM   2980  O O   . GLY A  1 353 ? -17.155 -32.712 31.367   1.00 18.55  ? 353 GLY A O   1 
ATOM   2981  N N   . GLU A  1 354 ? -16.874 -31.253 29.675   1.00 20.47  ? 354 GLU A N   1 
ATOM   2982  C CA  . GLU A  1 354 ? -16.875 -32.341 28.706   1.00 19.35  ? 354 GLU A CA  1 
ATOM   2983  C C   . GLU A  1 354 ? -15.725 -32.308 27.701   1.00 19.86  ? 354 GLU A C   1 
ATOM   2984  O O   . GLU A  1 354 ? -15.592 -33.260 26.931   1.00 24.34  ? 354 GLU A O   1 
ATOM   2985  C CB  . GLU A  1 354 ? -18.226 -32.371 27.956   1.00 21.93  ? 354 GLU A CB  1 
ATOM   2986  C CG  . GLU A  1 354 ? -18.363 -31.386 26.777   1.00 21.55  ? 354 GLU A CG  1 
ATOM   2987  C CD  . GLU A  1 354 ? -18.754 -29.952 27.190   1.00 22.18  ? 354 GLU A CD  1 
ATOM   2988  O OE1 . GLU A  1 354 ? -19.808 -29.457 26.743   1.00 20.79  ? 354 GLU A OE1 1 
ATOM   2989  O OE2 . GLU A  1 354 ? -17.998 -29.310 27.942   1.00 22.61  ? 354 GLU A OE2 1 
ATOM   2990  N N   . ASN A  1 355 ? -14.870 -31.287 27.706   1.00 19.99  ? 355 ASN A N   1 
ATOM   2991  C CA  . ASN A  1 355 ? -13.885 -31.151 26.635   1.00 19.21  ? 355 ASN A CA  1 
ATOM   2992  C C   . ASN A  1 355 ? -12.470 -31.558 27.027   1.00 20.56  ? 355 ASN A C   1 
ATOM   2993  O O   . ASN A  1 355 ? -11.658 -31.840 26.134   1.00 17.65  ? 355 ASN A O   1 
ATOM   2994  C CB  . ASN A  1 355 ? -13.873 -29.703 26.123   1.00 20.63  ? 355 ASN A CB  1 
ATOM   2995  C CG  . ASN A  1 355 ? -15.193 -29.312 25.481   1.00 22.22  ? 355 ASN A CG  1 
ATOM   2996  O OD1 . ASN A  1 355 ? -15.857 -30.150 24.900   1.00 26.26  ? 355 ASN A OD1 1 
ATOM   2997  N ND2 . ASN A  1 355 ? -15.584 -28.051 25.603   1.00 20.45  ? 355 ASN A ND2 1 
ATOM   2998  N N   . CYS A  1 356 ? -12.142 -31.602 28.321   1.00 20.62  ? 356 CYS A N   1 
ATOM   2999  C CA  . CYS A  1 356 ? -10.765 -31.887 28.699   1.00 17.12  ? 356 CYS A CA  1 
ATOM   3000  C C   . CYS A  1 356 ? -10.488 -33.381 28.831   1.00 18.85  ? 356 CYS A C   1 
ATOM   3001  O O   . CYS A  1 356 ? -9.335  -33.795 28.672   1.00 27.12  ? 356 CYS A O   1 
ATOM   3002  C CB  . CYS A  1 356 ? -10.410 -31.163 30.008   1.00 21.63  ? 356 CYS A CB  1 
ATOM   3003  S SG  . CYS A  1 356 ? -11.433 -31.686 31.393   1.00 20.99  ? 356 CYS A SG  1 
ATOM   3004  N N   . TRP A  1 357 ? -11.516 -34.204 29.068   1.00 23.28  ? 357 TRP A N   1 
ATOM   3005  C CA  . TRP A  1 357 ? -11.290 -35.612 29.410   1.00 22.23  ? 357 TRP A CA  1 
ATOM   3006  C C   . TRP A  1 357 ? -10.802 -36.442 28.224   1.00 22.14  ? 357 TRP A C   1 
ATOM   3007  O O   . TRP A  1 357 ? -10.080 -37.426 28.422   1.00 22.64  ? 357 TRP A O   1 
ATOM   3008  C CB  . TRP A  1 357 ? -12.565 -36.225 29.986   1.00 20.97  ? 357 TRP A CB  1 
ATOM   3009  C CG  . TRP A  1 357 ? -13.210 -35.325 30.980   1.00 25.45  ? 357 TRP A CG  1 
ATOM   3010  C CD1 . TRP A  1 357 ? -14.430 -34.729 30.870   1.00 24.02  ? 357 TRP A CD1 1 
ATOM   3011  C CD2 . TRP A  1 357 ? -12.644 -34.857 32.214   1.00 25.12  ? 357 TRP A CD2 1 
ATOM   3012  N NE1 . TRP A  1 357 ? -14.665 -33.939 31.955   1.00 25.75  ? 357 TRP A NE1 1 
ATOM   3013  C CE2 . TRP A  1 357 ? -13.585 -33.989 32.794   1.00 23.37  ? 357 TRP A CE2 1 
ATOM   3014  C CE3 . TRP A  1 357 ? -11.430 -35.086 32.882   1.00 25.86  ? 357 TRP A CE3 1 
ATOM   3015  C CZ2 . TRP A  1 357 ? -13.382 -33.373 34.040   1.00 20.69  ? 357 TRP A CZ2 1 
ATOM   3016  C CZ3 . TRP A  1 357 ? -11.219 -34.456 34.109   1.00 27.25  ? 357 TRP A CZ3 1 
ATOM   3017  C CH2 . TRP A  1 357 ? -12.194 -33.600 34.665   1.00 22.12  ? 357 TRP A CH2 1 
ATOM   3018  N N   . GLU A  1 358 ? -11.186 -36.095 26.992   1.00 19.84  ? 358 GLU A N   1 
ATOM   3019  C CA  . GLU A  1 358 ? -10.711 -36.889 25.857   1.00 16.75  ? 358 GLU A CA  1 
ATOM   3020  C C   . GLU A  1 358 ? -9.194  -36.857 25.721   1.00 20.41  ? 358 GLU A C   1 
ATOM   3021  O O   . GLU A  1 358 ? -8.626  -37.719 25.026   1.00 19.01  ? 358 GLU A O   1 
ATOM   3022  C CB  . GLU A  1 358 ? -11.354 -36.400 24.545   1.00 16.91  ? 358 GLU A CB  1 
ATOM   3023  C CG  . GLU A  1 358 ? -11.106 -34.933 24.283   1.00 26.85  ? 358 GLU A CG  1 
ATOM   3024  C CD  . GLU A  1 358 ? -12.141 -34.342 23.355   1.00 29.78  ? 358 GLU A CD  1 
ATOM   3025  O OE1 . GLU A  1 358 ? -11.769 -33.958 22.223   1.00 36.34  ? 358 GLU A OE1 1 
ATOM   3026  O OE2 . GLU A  1 358 ? -13.322 -34.283 23.757   1.00 25.33  ? 358 GLU A OE2 1 
ATOM   3027  N N   . TYR A  1 359 ? -8.528  -35.895 26.362   1.00 17.28  ? 359 TYR A N   1 
ATOM   3028  C CA  . TYR A  1 359 ? -7.071  -35.817 26.331   1.00 25.14  ? 359 TYR A CA  1 
ATOM   3029  C C   . TYR A  1 359 ? -6.410  -36.495 27.526   1.00 25.85  ? 359 TYR A C   1 
ATOM   3030  O O   . TYR A  1 359 ? -5.179  -36.602 27.552   1.00 22.83  ? 359 TYR A O   1 
ATOM   3031  C CB  . TYR A  1 359 ? -6.616  -34.351 26.254   1.00 28.70  ? 359 TYR A CB  1 
ATOM   3032  C CG  . TYR A  1 359 ? -7.155  -33.642 25.037   1.00 32.18  ? 359 TYR A CG  1 
ATOM   3033  C CD1 . TYR A  1 359 ? -6.579  -33.837 23.773   1.00 31.79  ? 359 TYR A CD1 1 
ATOM   3034  C CD2 . TYR A  1 359 ? -8.264  -32.812 25.136   1.00 33.35  ? 359 TYR A CD2 1 
ATOM   3035  C CE1 . TYR A  1 359 ? -7.083  -33.203 22.660   1.00 32.85  ? 359 TYR A CE1 1 
ATOM   3036  C CE2 . TYR A  1 359 ? -8.781  -32.177 24.019   1.00 35.53  ? 359 TYR A CE2 1 
ATOM   3037  C CZ  . TYR A  1 359 ? -8.186  -32.373 22.788   1.00 38.48  ? 359 TYR A CZ  1 
ATOM   3038  O OH  . TYR A  1 359 ? -8.708  -31.736 21.682   1.00 39.47  ? 359 TYR A OH  1 
ATOM   3039  N N   . TYR A  1 360 ? -7.186  -36.949 28.508   1.00 25.93  ? 360 TYR A N   1 
ATOM   3040  C CA  . TYR A  1 360 ? -6.647  -37.698 29.632   1.00 26.58  ? 360 TYR A CA  1 
ATOM   3041  C C   . TYR A  1 360 ? -6.605  -39.182 29.282   1.00 25.95  ? 360 TYR A C   1 
ATOM   3042  O O   . TYR A  1 360 ? -7.450  -39.678 28.540   1.00 25.76  ? 360 TYR A O   1 
ATOM   3043  C CB  . TYR A  1 360 ? -7.524  -37.536 30.872   1.00 22.06  ? 360 TYR A CB  1 
ATOM   3044  C CG  . TYR A  1 360 ? -7.476  -36.248 31.658   1.00 20.14  ? 360 TYR A CG  1 
ATOM   3045  C CD1 . TYR A  1 360 ? -7.904  -35.035 31.119   1.00 16.64  ? 360 TYR A CD1 1 
ATOM   3046  C CD2 . TYR A  1 360 ? -7.071  -36.262 32.995   1.00 20.03  ? 360 TYR A CD2 1 
ATOM   3047  C CE1 . TYR A  1 360 ? -7.898  -33.858 31.895   1.00 19.73  ? 360 TYR A CE1 1 
ATOM   3048  C CE2 . TYR A  1 360 ? -7.064  -35.109 33.758   1.00 21.47  ? 360 TYR A CE2 1 
ATOM   3049  C CZ  . TYR A  1 360 ? -7.476  -33.920 33.213   1.00 20.08  ? 360 TYR A CZ  1 
ATOM   3050  O OH  . TYR A  1 360 ? -7.433  -32.799 34.001   1.00 20.04  ? 360 TYR A OH  1 
ATOM   3051  N N   . GLU A  1 361 ? -5.661  -39.905 29.879   1.00 23.58  ? 361 GLU A N   1 
ATOM   3052  C CA  . GLU A  1 361 ? -5.698  -41.359 29.788   1.00 29.59  ? 361 GLU A CA  1 
ATOM   3053  C C   . GLU A  1 361 ? -7.040  -41.887 30.285   1.00 27.85  ? 361 GLU A C   1 
ATOM   3054  O O   . GLU A  1 361 ? -7.572  -41.430 31.298   1.00 29.26  ? 361 GLU A O   1 
ATOM   3055  C CB  . GLU A  1 361 ? -4.555  -41.986 30.592   1.00 40.83  ? 361 GLU A CB  1 
ATOM   3056  C CG  . GLU A  1 361 ? -3.156  -41.525 30.152   1.00 52.58  ? 361 GLU A CG  1 
ATOM   3057  C CD  . GLU A  1 361 ? -2.846  -41.734 28.652   1.00 62.66  ? 361 GLU A CD  1 
ATOM   3058  O OE1 . GLU A  1 361 ? -3.582  -42.462 27.944   1.00 66.40  ? 361 GLU A OE1 1 
ATOM   3059  O OE2 . GLU A  1 361 ? -1.851  -41.143 28.175   1.00 66.20  ? 361 GLU A OE2 1 
ATOM   3060  N N   . GLU A  1 362 ? -7.591  -42.841 29.536   1.00 29.53  ? 362 GLU A N   1 
ATOM   3061  C CA  . GLU A  1 362 ? -8.881  -43.470 29.827   1.00 29.20  ? 362 GLU A CA  1 
ATOM   3062  C C   . GLU A  1 362 ? -9.975  -42.455 30.140   1.00 31.22  ? 362 GLU A C   1 
ATOM   3063  O O   . GLU A  1 362 ? -10.774 -42.641 31.062   1.00 31.87  ? 362 GLU A O   1 
ATOM   3064  C CB  . GLU A  1 362 ? -8.747  -44.476 30.964   1.00 37.35  ? 362 GLU A CB  1 
ATOM   3065  C CG  . GLU A  1 362 ? -8.394  -45.864 30.490   1.00 47.05  ? 362 GLU A CG  1 
ATOM   3066  C CD  . GLU A  1 362 ? -7.937  -46.749 31.617   1.00 56.95  ? 362 GLU A CD  1 
ATOM   3067  O OE1 . GLU A  1 362 ? -6.741  -47.102 31.642   1.00 64.18  ? 362 GLU A OE1 1 
ATOM   3068  O OE2 . GLU A  1 362 ? -8.775  -47.079 32.484   1.00 54.99  ? 362 GLU A OE2 1 
ATOM   3069  N N   . ASN A  1 363 ? -10.036 -41.385 29.349   1.00 29.95  ? 363 ASN A N   1 
ATOM   3070  C CA  . ASN A  1 363 ? -11.142 -40.433 29.434   1.00 25.45  ? 363 ASN A CA  1 
ATOM   3071  C C   . ASN A  1 363 ? -11.218 -39.775 30.810   1.00 23.77  ? 363 ASN A C   1 
ATOM   3072  O O   . ASN A  1 363 ? -12.302 -39.414 31.284   1.00 18.73  ? 363 ASN A O   1 
ATOM   3073  C CB  . ASN A  1 363 ? -12.475 -41.111 29.086   1.00 27.61  ? 363 ASN A CB  1 
ATOM   3074  C CG  . ASN A  1 363 ? -13.553 -40.115 28.766   1.00 26.94  ? 363 ASN A CG  1 
ATOM   3075  O OD1 . ASN A  1 363 ? -13.271 -39.062 28.203   1.00 24.20  ? 363 ASN A OD1 1 
ATOM   3076  N ND2 . ASN A  1 363 ? -14.788 -40.423 29.142   1.00 28.50  ? 363 ASN A ND2 1 
ATOM   3077  N N   . GLY A  1 364 ? -10.068 -39.613 31.458   1.00 21.64  ? 364 GLY A N   1 
ATOM   3078  C CA  . GLY A  1 364 ? -10.037 -38.973 32.757   1.00 23.06  ? 364 GLY A CA  1 
ATOM   3079  C C   . GLY A  1 364 ? -10.697 -39.731 33.882   1.00 26.06  ? 364 GLY A C   1 
ATOM   3080  O O   . GLY A  1 364 ? -10.885 -39.161 34.964   1.00 25.02  ? 364 GLY A O   1 
ATOM   3081  N N   . ILE A  1 365 ? -11.040 -40.999 33.685   1.00 28.10  ? 365 ILE A N   1 
ATOM   3082  C CA  . ILE A  1 365 ? -11.796 -41.716 34.708   1.00 24.74  ? 365 ILE A CA  1 
ATOM   3083  C C   . ILE A  1 365 ? -10.873 -42.048 35.880   1.00 25.92  ? 365 ILE A C   1 
ATOM   3084  O O   . ILE A  1 365 ? -11.262 -41.798 37.027   1.00 25.02  ? 365 ILE A O   1 
ATOM   3085  C CB  . ILE A  1 365 ? -12.507 -42.942 34.117   1.00 26.09  ? 365 ILE A CB  1 
ATOM   3086  C CG1 . ILE A  1 365 ? -13.508 -42.472 33.049   1.00 27.83  ? 365 ILE A CG1 1 
ATOM   3087  C CG2 . ILE A  1 365 ? -13.234 -43.713 35.206   1.00 28.31  ? 365 ILE A CG2 1 
ATOM   3088  C CD1 . ILE A  1 365 ? -14.010 -43.549 32.115   1.00 27.49  ? 365 ILE A CD1 1 
ATOM   3089  N N   . PRO A  1 366 ? -9.651  -42.564 35.669   1.00 22.98  ? 366 PRO A N   1 
ATOM   3090  C CA  . PRO A  1 366 ? -8.744  -42.726 36.823   1.00 27.81  ? 366 PRO A CA  1 
ATOM   3091  C C   . PRO A  1 366 ? -8.510  -41.426 37.576   1.00 30.56  ? 366 PRO A C   1 
ATOM   3092  O O   . PRO A  1 366 ? -8.443  -41.426 38.814   1.00 34.23  ? 366 PRO A O   1 
ATOM   3093  C CB  . PRO A  1 366 ? -7.457  -43.270 36.185   1.00 25.02  ? 366 PRO A CB  1 
ATOM   3094  C CG  . PRO A  1 366 ? -7.930  -44.002 34.964   1.00 24.15  ? 366 PRO A CG  1 
ATOM   3095  C CD  . PRO A  1 366 ? -9.080  -43.157 34.443   1.00 25.23  ? 366 PRO A CD  1 
ATOM   3096  N N   . PHE A  1 367 ? -8.410  -40.306 36.865   1.00 26.67  ? 367 PHE A N   1 
ATOM   3097  C CA  . PHE A  1 367 ? -8.211  -39.030 37.541   1.00 25.41  ? 367 PHE A CA  1 
ATOM   3098  C C   . PHE A  1 367 ? -9.418  -38.644 38.387   1.00 27.70  ? 367 PHE A C   1 
ATOM   3099  O O   . PHE A  1 367 ? -9.278  -38.310 39.573   1.00 25.38  ? 367 PHE A O   1 
ATOM   3100  C CB  . PHE A  1 367 ? -7.930  -37.922 36.550   1.00 23.81  ? 367 PHE A CB  1 
ATOM   3101  C CG  . PHE A  1 367 ? -7.932  -36.586 37.186   1.00 24.24  ? 367 PHE A CG  1 
ATOM   3102  C CD1 . PHE A  1 367 ? -6.908  -36.233 38.051   1.00 22.72  ? 367 PHE A CD1 1 
ATOM   3103  C CD2 . PHE A  1 367 ? -8.983  -35.699 36.984   1.00 24.15  ? 367 PHE A CD2 1 
ATOM   3104  C CE1 . PHE A  1 367 ? -6.902  -35.006 38.671   1.00 24.84  ? 367 PHE A CE1 1 
ATOM   3105  C CE2 . PHE A  1 367 ? -8.978  -34.469 37.605   1.00 19.72  ? 367 PHE A CE2 1 
ATOM   3106  C CZ  . PHE A  1 367 ? -7.930  -34.132 38.463   1.00 18.98  ? 367 PHE A CZ  1 
ATOM   3107  N N   . LEU A  1 368 ? -10.613 -38.667 37.799   1.00 21.17  ? 368 LEU A N   1 
ATOM   3108  C CA  . LEU A  1 368 ? -11.776 -38.191 38.539   1.00 23.77  ? 368 LEU A CA  1 
ATOM   3109  C C   . LEU A  1 368 ? -12.160 -39.148 39.659   1.00 27.20  ? 368 LEU A C   1 
ATOM   3110  O O   . LEU A  1 368 ? -12.598 -38.706 40.729   1.00 28.81  ? 368 LEU A O   1 
ATOM   3111  C CB  . LEU A  1 368 ? -12.954 -37.961 37.591   1.00 20.00  ? 368 LEU A CB  1 
ATOM   3112  C CG  . LEU A  1 368 ? -12.879 -36.686 36.743   1.00 23.26  ? 368 LEU A CG  1 
ATOM   3113  C CD1 . LEU A  1 368 ? -14.103 -36.629 35.840   1.00 21.46  ? 368 LEU A CD1 1 
ATOM   3114  C CD2 . LEU A  1 368 ? -12.788 -35.449 37.610   1.00 20.85  ? 368 LEU A CD2 1 
ATOM   3115  N N   . GLU A  1 369 ? -12.024 -40.463 39.438   1.00 26.29  ? 369 GLU A N   1 
ATOM   3116  C CA  . GLU A  1 369 ? -12.345 -41.404 40.509   1.00 30.41  ? 369 GLU A CA  1 
ATOM   3117  C C   . GLU A  1 369 ? -11.393 -41.244 41.689   1.00 30.08  ? 369 GLU A C   1 
ATOM   3118  O O   . GLU A  1 369 ? -11.801 -41.385 42.847   1.00 27.21  ? 369 GLU A O   1 
ATOM   3119  C CB  . GLU A  1 369 ? -12.323 -42.843 39.990   1.00 26.19  ? 369 GLU A CB  1 
ATOM   3120  C CG  . GLU A  1 369 ? -13.540 -43.220 39.130   1.00 22.98  ? 369 GLU A CG  1 
ATOM   3121  C CD  . GLU A  1 369 ? -13.514 -44.671 38.707   1.00 28.67  ? 369 GLU A CD  1 
ATOM   3122  O OE1 . GLU A  1 369 ? -12.448 -45.310 38.848   1.00 31.76  ? 369 GLU A OE1 1 
ATOM   3123  O OE2 . GLU A  1 369 ? -14.562 -45.178 38.246   1.00 31.90  ? 369 GLU A OE2 1 
ATOM   3124  N N   . LYS A  1 370 ? -10.121 -40.953 41.429   1.00 25.36  ? 370 LYS A N   1 
ATOM   3125  C CA  . LYS A  1 370 ? -9.212  -40.745 42.550   1.00 26.22  ? 370 LYS A CA  1 
ATOM   3126  C C   . LYS A  1 370 ? -9.393  -39.349 43.152   1.00 27.69  ? 370 LYS A C   1 
ATOM   3127  O O   . LYS A  1 370 ? -9.298  -39.178 44.370   1.00 26.34  ? 370 LYS A O   1 
ATOM   3128  C CB  . LYS A  1 370 ? -7.769  -40.975 42.107   1.00 30.85  ? 370 LYS A CB  1 
ATOM   3129  C CG  . LYS A  1 370 ? -6.752  -40.658 43.182   1.00 44.40  ? 370 LYS A CG  1 
ATOM   3130  C CD  . LYS A  1 370 ? -5.604  -41.659 43.189   1.00 54.90  ? 370 LYS A CD  1 
ATOM   3131  C CE  . LYS A  1 370 ? -4.782  -41.512 44.464   1.00 61.25  ? 370 LYS A CE  1 
ATOM   3132  N NZ  . LYS A  1 370 ? -5.674  -41.589 45.662   1.00 64.11  ? 370 LYS A NZ  1 
ATOM   3133  N N   . LEU A  1 371 ? -9.702  -38.344 42.327   1.00 23.44  ? 371 LEU A N   1 
ATOM   3134  C CA  . LEU A  1 371 ? -9.977  -37.013 42.867   1.00 20.74  ? 371 LEU A CA  1 
ATOM   3135  C C   . LEU A  1 371 ? -11.166 -37.051 43.826   1.00 23.71  ? 371 LEU A C   1 
ATOM   3136  O O   . LEU A  1 371 ? -11.057 -36.675 44.999   1.00 24.36  ? 371 LEU A O   1 
ATOM   3137  C CB  . LEU A  1 371 ? -10.225 -36.025 41.728   1.00 17.96  ? 371 LEU A CB  1 
ATOM   3138  C CG  . LEU A  1 371 ? -10.666 -34.633 42.212   1.00 21.27  ? 371 LEU A CG  1 
ATOM   3139  C CD1 . LEU A  1 371 ? -9.592  -34.085 43.123   1.00 25.59  ? 371 LEU A CD1 1 
ATOM   3140  C CD2 . LEU A  1 371 ? -10.967 -33.655 41.083   1.00 25.40  ? 371 LEU A CD2 1 
ATOM   3141  N N   . TYR A  1 372 ? -12.291 -37.570 43.353   1.00 27.04  ? 372 TYR A N   1 
ATOM   3142  C CA  . TYR A  1 372 ? -13.522 -37.565 44.129   1.00 22.03  ? 372 TYR A CA  1 
ATOM   3143  C C   . TYR A  1 372 ? -13.410 -38.438 45.372   1.00 30.78  ? 372 TYR A C   1 
ATOM   3144  O O   . TYR A  1 372 ? -13.961 -38.101 46.428   1.00 31.35  ? 372 TYR A O   1 
ATOM   3145  C CB  . TYR A  1 372 ? -14.653 -38.040 43.239   1.00 19.49  ? 372 TYR A CB  1 
ATOM   3146  C CG  . TYR A  1 372 ? -15.021 -37.059 42.144   1.00 22.32  ? 372 TYR A CG  1 
ATOM   3147  C CD1 . TYR A  1 372 ? -14.592 -35.722 42.199   1.00 20.04  ? 372 TYR A CD1 1 
ATOM   3148  C CD2 . TYR A  1 372 ? -15.827 -37.447 41.085   1.00 24.77  ? 372 TYR A CD2 1 
ATOM   3149  C CE1 . TYR A  1 372 ? -14.956 -34.819 41.230   1.00 23.35  ? 372 TYR A CE1 1 
ATOM   3150  C CE2 . TYR A  1 372 ? -16.184 -36.543 40.094   1.00 24.50  ? 372 TYR A CE2 1 
ATOM   3151  C CZ  . TYR A  1 372 ? -15.747 -35.237 40.182   1.00 23.50  ? 372 TYR A CZ  1 
ATOM   3152  O OH  . TYR A  1 372 ? -16.112 -34.323 39.233   1.00 19.15  ? 372 TYR A OH  1 
ATOM   3153  N N   . SER A  1 373 ? -12.730 -39.581 45.249   1.00 29.87  ? 373 SER A N   1 
ATOM   3154  C CA  . SER A  1 373 ? -12.515 -40.460 46.387   1.00 27.54  ? 373 SER A CA  1 
ATOM   3155  C C   . SER A  1 373 ? -11.648 -39.795 47.448   1.00 27.50  ? 373 SER A C   1 
ATOM   3156  O O   . SER A  1 373 ? -11.871 -39.987 48.649   1.00 27.92  ? 373 SER A O   1 
ATOM   3157  C CB  . SER A  1 373 ? -11.865 -41.769 45.921   1.00 28.66  ? 373 SER A CB  1 
ATOM   3158  O OG  . SER A  1 373 ? -11.319 -42.461 47.025   1.00 35.53  ? 373 SER A OG  1 
ATOM   3159  N N   . THR A  1 374 ? -10.616 -39.070 47.028   1.00 23.09  ? 374 THR A N   1 
ATOM   3160  C CA  . THR A  1 374 ? -9.760  -38.373 47.981   1.00 31.96  ? 374 THR A CA  1 
ATOM   3161  C C   . THR A  1 374 ? -10.474 -37.170 48.590   1.00 33.36  ? 374 THR A C   1 
ATOM   3162  O O   . THR A  1 374 ? -10.330 -36.894 49.785   1.00 34.31  ? 374 THR A O   1 
ATOM   3163  C CB  . THR A  1 374 ? -8.477  -37.937 47.280   1.00 32.93  ? 374 THR A CB  1 
ATOM   3164  O OG1 . THR A  1 374 ? -7.881  -39.084 46.663   1.00 30.25  ? 374 THR A OG1 1 
ATOM   3165  C CG2 . THR A  1 374 ? -7.507  -37.279 48.267   1.00 32.24  ? 374 THR A CG2 1 
ATOM   3166  N N   . LEU A  1 375 ? -11.246 -36.442 47.781   1.00 26.20  ? 375 LEU A N   1 
ATOM   3167  C CA  . LEU A  1 375 ? -11.999 -35.303 48.306   1.00 27.49  ? 375 LEU A CA  1 
ATOM   3168  C C   . LEU A  1 375 ? -12.961 -35.735 49.397   1.00 31.83  ? 375 LEU A C   1 
ATOM   3169  O O   . LEU A  1 375 ? -13.020 -35.112 50.467   1.00 32.91  ? 375 LEU A O   1 
ATOM   3170  C CB  . LEU A  1 375 ? -12.759 -34.607 47.176   1.00 27.58  ? 375 LEU A CB  1 
ATOM   3171  C CG  . LEU A  1 375 ? -11.908 -33.890 46.136   1.00 28.86  ? 375 LEU A CG  1 
ATOM   3172  C CD1 . LEU A  1 375 ? -12.806 -33.189 45.099   1.00 28.58  ? 375 LEU A CD1 1 
ATOM   3173  C CD2 . LEU A  1 375 ? -11.012 -32.899 46.836   1.00 24.05  ? 375 LEU A CD2 1 
ATOM   3174  N N   . GLU A  1 376 ? -13.713 -36.807 49.149   1.00 37.86  ? 376 GLU A N   1 
ATOM   3175  C CA  . GLU A  1 376 ? -14.693 -37.264 50.116   1.00 38.82  ? 376 GLU A CA  1 
ATOM   3176  C C   . GLU A  1 376 ? -14.051 -37.752 51.410   1.00 42.67  ? 376 GLU A C   1 
ATOM   3177  O O   . GLU A  1 376 ? -14.771 -37.956 52.393   1.00 47.93  ? 376 GLU A O   1 
ATOM   3178  C CB  . GLU A  1 376 ? -15.563 -38.363 49.495   1.00 32.79  ? 376 GLU A CB  1 
ATOM   3179  C CG  . GLU A  1 376 ? -14.891 -39.734 49.412   1.00 38.46  ? 376 GLU A CG  1 
ATOM   3180  C CD  . GLU A  1 376 ? -15.738 -40.778 48.690   1.00 46.03  ? 376 GLU A CD  1 
ATOM   3181  O OE1 . GLU A  1 376 ? -15.266 -41.921 48.525   1.00 50.54  ? 376 GLU A OE1 1 
ATOM   3182  O OE2 . GLU A  1 376 ? -16.877 -40.467 48.284   1.00 48.75  ? 376 GLU A OE2 1 
ATOM   3183  N N   . LYS A  1 377 ? -12.727 -37.937 51.432   1.00 44.65  ? 377 LYS A N   1 
ATOM   3184  C CA  . LYS A  1 377 ? -12.008 -38.386 52.620   1.00 45.39  ? 377 LYS A CA  1 
ATOM   3185  C C   . LYS A  1 377 ? -11.529 -37.251 53.511   1.00 46.63  ? 377 LYS A C   1 
ATOM   3186  O O   . LYS A  1 377 ? -11.189 -37.502 54.679   1.00 53.29  ? 377 LYS A O   1 
ATOM   3187  C CB  . LYS A  1 377 ? -10.771 -39.215 52.238   1.00 45.11  ? 377 LYS A CB  1 
ATOM   3188  C CG  . LYS A  1 377 ? -11.043 -40.522 51.543   1.00 48.18  ? 377 LYS A CG  1 
ATOM   3189  C CD  . LYS A  1 377 ? -9.754  -41.359 51.433   1.00 51.03  ? 377 LYS A CD  1 
ATOM   3190  C CE  . LYS A  1 377 ? -9.887  -42.479 50.423   1.00 50.02  ? 377 LYS A CE  1 
ATOM   3191  N NZ  . LYS A  1 377 ? -9.186  -42.121 49.151   1.00 54.19  ? 377 LYS A NZ  1 
ATOM   3192  N N   . GLU A  1 378 ? -11.465 -36.024 53.003   1.00 43.47  ? 378 GLU A N   1 
ATOM   3193  C CA  . GLU A  1 378 ? -10.821 -34.932 53.727   1.00 40.15  ? 378 GLU A CA  1 
ATOM   3194  C C   . GLU A  1 378 ? -11.818 -34.245 54.654   1.00 35.39  ? 378 GLU A C   1 
ATOM   3195  O O   . GLU A  1 378 ? -12.796 -33.645 54.192   1.00 30.98  ? 378 GLU A O   1 
ATOM   3196  C CB  . GLU A  1 378 ? -10.204 -33.930 52.754   1.00 35.50  ? 378 GLU A CB  1 
ATOM   3197  C CG  . GLU A  1 378 ? -9.228  -34.554 51.757   1.00 36.69  ? 378 GLU A CG  1 
ATOM   3198  C CD  . GLU A  1 378 ? -7.854  -34.870 52.347   1.00 43.66  ? 378 GLU A CD  1 
ATOM   3199  O OE1 . GLU A  1 378 ? -7.709  -34.967 53.594   1.00 46.55  ? 378 GLU A OE1 1 
ATOM   3200  O OE2 . GLU A  1 378 ? -6.911  -35.049 51.548   1.00 44.45  ? 378 GLU A OE2 1 
ATOM   3201  N N   . GLU A  1 379 ? -11.554 -34.323 55.966   1.00 33.65  ? 379 GLU A N   1 
ATOM   3202  C CA  . GLU A  1 379 ? -12.448 -33.717 56.947   1.00 27.56  ? 379 GLU A CA  1 
ATOM   3203  C C   . GLU A  1 379 ? -12.491 -32.195 56.825   1.00 30.38  ? 379 GLU A C   1 
ATOM   3204  O O   . GLU A  1 379 ? -13.522 -31.583 57.119   1.00 31.27  ? 379 GLU A O   1 
ATOM   3205  C CB  . GLU A  1 379 ? -12.019 -34.123 58.368   1.00 33.69  ? 379 GLU A CB  1 
ATOM   3206  N N   . TRP A  1 380 ? -11.395 -31.571 56.380   1.00 29.08  ? 380 TRP A N   1 
ATOM   3207  C CA  . TRP A  1 380 ? -11.286 -30.121 56.260   1.00 31.57  ? 380 TRP A CA  1 
ATOM   3208  C C   . TRP A  1 380 ? -11.799 -29.568 54.925   1.00 30.67  ? 380 TRP A C   1 
ATOM   3209  O O   . TRP A  1 380 ? -11.754 -28.348 54.721   1.00 29.14  ? 380 TRP A O   1 
ATOM   3210  C CB  . TRP A  1 380 ? -9.826  -29.688 56.466   1.00 33.03  ? 380 TRP A CB  1 
ATOM   3211  C CG  . TRP A  1 380 ? -8.851  -30.445 55.604   1.00 33.17  ? 380 TRP A CG  1 
ATOM   3212  C CD1 . TRP A  1 380 ? -8.299  -31.671 55.867   1.00 36.39  ? 380 TRP A CD1 1 
ATOM   3213  C CD2 . TRP A  1 380 ? -8.324  -30.035 54.331   1.00 30.69  ? 380 TRP A CD2 1 
ATOM   3214  N NE1 . TRP A  1 380 ? -7.459  -32.045 54.842   1.00 34.75  ? 380 TRP A NE1 1 
ATOM   3215  C CE2 . TRP A  1 380 ? -7.460  -31.063 53.885   1.00 35.09  ? 380 TRP A CE2 1 
ATOM   3216  C CE3 . TRP A  1 380 ? -8.496  -28.907 53.529   1.00 26.41  ? 380 TRP A CE3 1 
ATOM   3217  C CZ2 . TRP A  1 380 ? -6.771  -30.992 52.666   1.00 33.48  ? 380 TRP A CZ2 1 
ATOM   3218  C CZ3 . TRP A  1 380 ? -7.810  -28.838 52.308   1.00 29.12  ? 380 TRP A CZ3 1 
ATOM   3219  C CH2 . TRP A  1 380 ? -6.958  -29.874 51.896   1.00 28.65  ? 380 TRP A CH2 1 
ATOM   3220  N N   . ILE A  1 381 ? -12.291 -30.411 54.021   1.00 30.19  ? 381 ILE A N   1 
ATOM   3221  C CA  . ILE A  1 381 ? -12.960 -29.965 52.805   1.00 25.68  ? 381 ILE A CA  1 
ATOM   3222  C C   . ILE A  1 381 ? -14.442 -30.298 52.918   1.00 28.05  ? 381 ILE A C   1 
ATOM   3223  O O   . ILE A  1 381 ? -14.804 -31.450 53.182   1.00 28.42  ? 381 ILE A O   1 
ATOM   3224  C CB  . ILE A  1 381 ? -12.374 -30.624 51.544   1.00 23.71  ? 381 ILE A CB  1 
ATOM   3225  C CG1 . ILE A  1 381 ? -10.874 -30.374 51.440   1.00 24.36  ? 381 ILE A CG1 1 
ATOM   3226  C CG2 . ILE A  1 381 ? -13.095 -30.084 50.285   1.00 22.77  ? 381 ILE A CG2 1 
ATOM   3227  C CD1 . ILE A  1 381 ? -10.274 -30.924 50.171   1.00 22.47  ? 381 ILE A CD1 1 
ATOM   3228  N N   . GLU A  1 382 ? -15.298 -29.295 52.709   1.00 25.72  ? 382 GLU A N   1 
ATOM   3229  C CA  . GLU A  1 382 ? -16.726 -29.512 52.502   1.00 26.03  ? 382 GLU A CA  1 
ATOM   3230  C C   . GLU A  1 382 ? -17.072 -29.022 51.098   1.00 22.52  ? 382 GLU A C   1 
ATOM   3231  O O   . GLU A  1 382 ? -17.044 -27.816 50.832   1.00 23.90  ? 382 GLU A O   1 
ATOM   3232  C CB  . GLU A  1 382 ? -17.572 -28.787 53.541   1.00 29.51  ? 382 GLU A CB  1 
ATOM   3233  C CG  . GLU A  1 382 ? -19.059 -29.022 53.374   1.00 31.97  ? 382 GLU A CG  1 
ATOM   3234  C CD  . GLU A  1 382 ? -19.891 -28.244 54.386   1.00 44.15  ? 382 GLU A CD  1 
ATOM   3235  O OE1 . GLU A  1 382 ? -21.134 -28.245 54.220   1.00 49.91  ? 382 GLU A OE1 1 
ATOM   3236  O OE2 . GLU A  1 382 ? -19.309 -27.630 55.327   1.00 37.70  ? 382 GLU A OE2 1 
ATOM   3237  N N   . THR A  1 383 ? -17.418 -29.942 50.216   1.00 19.08  ? 383 THR A N   1 
ATOM   3238  C CA  . THR A  1 383 ? -17.907 -29.518 48.902   1.00 19.55  ? 383 THR A CA  1 
ATOM   3239  C C   . THR A  1 383 ? -19.335 -29.004 49.046   1.00 23.07  ? 383 THR A C   1 
ATOM   3240  O O   . THR A  1 383 ? -20.114 -29.506 49.866   1.00 25.70  ? 383 THR A O   1 
ATOM   3241  C CB  . THR A  1 383 ? -17.828 -30.659 47.892   1.00 24.45  ? 383 THR A CB  1 
ATOM   3242  O OG1 . THR A  1 383 ? -18.554 -31.796 48.372   1.00 24.74  ? 383 THR A OG1 1 
ATOM   3243  C CG2 . THR A  1 383 ? -16.373 -31.054 47.651   1.00 25.49  ? 383 THR A CG2 1 
ATOM   3244  N N   . LEU A  1 384 ? -19.653 -27.948 48.306   1.00 20.91  ? 384 LEU A N   1 
ATOM   3245  C CA  . LEU A  1 384 ? -20.945 -27.283 48.410   1.00 20.55  ? 384 LEU A CA  1 
ATOM   3246  C C   . LEU A  1 384 ? -21.714 -27.369 47.095   1.00 21.37  ? 384 LEU A C   1 
ATOM   3247  O O   . LEU A  1 384 ? -21.137 -27.288 46.017   1.00 19.17  ? 384 LEU A O   1 
ATOM   3248  C CB  . LEU A  1 384 ? -20.772 -25.813 48.762   1.00 24.48  ? 384 LEU A CB  1 
ATOM   3249  C CG  . LEU A  1 384 ? -20.061 -25.511 50.068   1.00 23.48  ? 384 LEU A CG  1 
ATOM   3250  C CD1 . LEU A  1 384 ? -20.047 -24.005 50.289   1.00 24.45  ? 384 LEU A CD1 1 
ATOM   3251  C CD2 . LEU A  1 384 ? -20.784 -26.254 51.215   1.00 28.09  ? 384 LEU A CD2 1 
ATOM   3252  N N   . THR A  1 385 ? -23.030 -27.477 47.198   1.00 28.16  ? 385 THR A N   1 
ATOM   3253  C CA  . THR A  1 385 ? -23.850 -27.142 46.052   1.00 27.12  ? 385 THR A CA  1 
ATOM   3254  C C   . THR A  1 385 ? -23.813 -25.630 45.835   1.00 30.29  ? 385 THR A C   1 
ATOM   3255  O O   . THR A  1 385 ? -23.358 -24.870 46.694   1.00 24.58  ? 385 THR A O   1 
ATOM   3256  C CB  . THR A  1 385 ? -25.290 -27.595 46.271   1.00 24.65  ? 385 THR A CB  1 
ATOM   3257  O OG1 . THR A  1 385 ? -25.861 -26.798 47.306   1.00 23.62  ? 385 THR A OG1 1 
ATOM   3258  C CG2 . THR A  1 385 ? -25.360 -29.078 46.660   1.00 24.64  ? 385 THR A CG2 1 
ATOM   3259  N N   . LEU A  1 386 ? -24.297 -25.183 44.668   1.00 27.36  ? 386 LEU A N   1 
ATOM   3260  C CA  . LEU A  1 386 ? -24.421 -23.743 44.455   1.00 25.65  ? 386 LEU A CA  1 
ATOM   3261  C C   . LEU A  1 386 ? -25.346 -23.113 45.483   1.00 26.34  ? 386 LEU A C   1 
ATOM   3262  O O   . LEU A  1 386 ? -25.113 -21.984 45.930   1.00 25.76  ? 386 LEU A O   1 
ATOM   3263  C CB  . LEU A  1 386 ? -24.941 -23.453 43.048   1.00 28.43  ? 386 LEU A CB  1 
ATOM   3264  C CG  . LEU A  1 386 ? -24.050 -23.927 41.901   1.00 25.88  ? 386 LEU A CG  1 
ATOM   3265  C CD1 . LEU A  1 386 ? -24.660 -23.510 40.536   1.00 21.13  ? 386 LEU A CD1 1 
ATOM   3266  C CD2 . LEU A  1 386 ? -22.635 -23.411 42.074   1.00 19.27  ? 386 LEU A CD2 1 
ATOM   3267  N N   . GLU A  1 387 ? -26.439 -23.801 45.816   1.00 25.11  ? 387 GLU A N   1 
ATOM   3268  C CA  . GLU A  1 387 ? -27.376 -23.281 46.803   1.00 27.63  ? 387 GLU A CA  1 
ATOM   3269  C C   . GLU A  1 387 ? -26.677 -23.037 48.128   1.00 26.80  ? 387 GLU A C   1 
ATOM   3270  O O   . GLU A  1 387 ? -26.839 -21.976 48.743   1.00 26.74  ? 387 GLU A O   1 
ATOM   3271  C CB  . GLU A  1 387 ? -28.549 -24.244 46.977   1.00 36.48  ? 387 GLU A CB  1 
ATOM   3272  C CG  . GLU A  1 387 ? -29.561 -23.830 48.054   1.00 49.29  ? 387 GLU A CG  1 
ATOM   3273  C CD  . GLU A  1 387 ? -30.469 -22.696 47.606   1.00 65.97  ? 387 GLU A CD  1 
ATOM   3274  O OE1 . GLU A  1 387 ? -30.513 -22.419 46.386   1.00 70.94  ? 387 GLU A OE1 1 
ATOM   3275  O OE2 . GLU A  1 387 ? -31.143 -22.083 48.465   1.00 72.10  ? 387 GLU A OE2 1 
ATOM   3276  N N   . GLU A  1 388 ? -25.859 -23.998 48.557   1.00 24.69  ? 388 GLU A N   1 
ATOM   3277  C CA  . GLU A  1 388 ? -25.141 -23.853 49.819   1.00 26.20  ? 388 GLU A CA  1 
ATOM   3278  C C   . GLU A  1 388 ? -24.136 -22.712 49.756   1.00 26.50  ? 388 GLU A C   1 
ATOM   3279  O O   . GLU A  1 388 ? -24.058 -21.902 50.684   1.00 33.19  ? 388 GLU A O   1 
ATOM   3280  C CB  . GLU A  1 388 ? -24.466 -25.175 50.179   1.00 33.68  ? 388 GLU A CB  1 
ATOM   3281  C CG  . GLU A  1 388 ? -25.479 -26.280 50.490   1.00 41.47  ? 388 GLU A CG  1 
ATOM   3282  C CD  . GLU A  1 388 ? -24.852 -27.657 50.699   1.00 47.41  ? 388 GLU A CD  1 
ATOM   3283  O OE1 . GLU A  1 388 ? -23.871 -28.002 50.006   1.00 41.02  ? 388 GLU A OE1 1 
ATOM   3284  O OE2 . GLU A  1 388 ? -25.360 -28.403 51.567   1.00 51.28  ? 388 GLU A OE2 1 
ATOM   3285  N N   . ALA A  1 389 ? -23.377 -22.612 48.657   1.00 23.17  ? 389 ALA A N   1 
ATOM   3286  C CA  . ALA A  1 389 ? -22.408 -21.532 48.534   1.00 22.21  ? 389 ALA A CA  1 
ATOM   3287  C C   . ALA A  1 389 ? -23.086 -20.172 48.604   1.00 27.11  ? 389 ALA A C   1 
ATOM   3288  O O   . ALA A  1 389 ? -22.498 -19.203 49.099   1.00 29.01  ? 389 ALA A O   1 
ATOM   3289  C CB  . ALA A  1 389 ? -21.631 -21.666 47.215   1.00 23.87  ? 389 ALA A CB  1 
ATOM   3290  N N   . MET A  1 390 ? -24.324 -20.082 48.120   1.00 26.08  ? 390 MET A N   1 
ATOM   3291  C CA  . MET A  1 390 ? -25.011 -18.802 48.093   1.00 33.17  ? 390 MET A CA  1 
ATOM   3292  C C   . MET A  1 390 ? -25.525 -18.428 49.483   1.00 35.48  ? 390 MET A C   1 
ATOM   3293  O O   . MET A  1 390 ? -25.454 -17.258 49.874   1.00 31.38  ? 390 MET A O   1 
ATOM   3294  C CB  . MET A  1 390 ? -26.154 -18.843 47.073   1.00 33.82  ? 390 MET A CB  1 
ATOM   3295  C CG  . MET A  1 390 ? -26.959 -17.552 47.020   1.00 45.66  ? 390 MET A CG  1 
ATOM   3296  S SD  . MET A  1 390 ? -28.622 -17.834 46.408   1.00 56.49  ? 390 MET A SD  1 
ATOM   3297  C CE  . MET A  1 390 ? -28.401 -17.503 44.700   1.00 61.68  ? 390 MET A CE  1 
ATOM   3298  N N   . ARG A  1 391 ? -26.005 -19.409 50.256   1.00 32.21  ? 391 ARG A N   1 
ATOM   3299  C CA  . ARG A  1 391 ? -26.630 -19.142 51.548   1.00 32.26  ? 391 ARG A CA  1 
ATOM   3300  C C   . ARG A  1 391 ? -25.700 -19.334 52.745   1.00 33.08  ? 391 ARG A C   1 
ATOM   3301  O O   . ARG A  1 391 ? -26.064 -18.919 53.852   1.00 36.85  ? 391 ARG A O   1 
ATOM   3302  C CB  . ARG A  1 391 ? -27.864 -20.038 51.732   1.00 31.82  ? 391 ARG A CB  1 
ATOM   3303  C CG  . ARG A  1 391 ? -28.869 -19.968 50.584   1.00 38.22  ? 391 ARG A CG  1 
ATOM   3304  C CD  . ARG A  1 391 ? -30.301 -19.837 51.070   1.00 52.49  ? 391 ARG A CD  1 
ATOM   3305  N NE  . ARG A  1 391 ? -31.272 -19.919 49.980   1.00 59.93  ? 391 ARG A NE  1 
ATOM   3306  C CZ  . ARG A  1 391 ? -31.648 -18.883 49.234   1.00 68.43  ? 391 ARG A CZ  1 
ATOM   3307  N NH1 . ARG A  1 391 ? -31.128 -17.679 49.452   1.00 70.85  ? 391 ARG A NH1 1 
ATOM   3308  N NH2 . ARG A  1 391 ? -32.542 -19.050 48.267   1.00 72.71  ? 391 ARG A NH2 1 
ATOM   3309  N N   . LYS A  1 392 ? -24.536 -19.966 52.562   1.00 26.81  ? 392 LYS A N   1 
ATOM   3310  C CA  . LYS A  1 392 ? -23.609 -20.256 53.657   1.00 34.76  ? 392 LYS A CA  1 
ATOM   3311  C C   . LYS A  1 392 ? -23.279 -19.005 54.469   1.00 38.75  ? 392 LYS A C   1 
ATOM   3312  O O   . LYS A  1 392 ? -22.893 -17.969 53.921   1.00 35.92  ? 392 LYS A O   1 
ATOM   3313  C CB  . LYS A  1 392 ? -22.324 -20.860 53.087   1.00 42.19  ? 392 LYS A CB  1 
ATOM   3314  C CG  . LYS A  1 392 ? -21.433 -21.527 54.105   1.00 46.92  ? 392 LYS A CG  1 
ATOM   3315  C CD  . LYS A  1 392 ? -22.133 -22.703 54.753   1.00 50.29  ? 392 LYS A CD  1 
ATOM   3316  C CE  . LYS A  1 392 ? -21.550 -24.019 54.287   1.00 50.17  ? 392 LYS A CE  1 
ATOM   3317  N NZ  . LYS A  1 392 ? -22.185 -25.140 55.028   1.00 51.63  ? 392 LYS A NZ  1 
ATOM   3318  N N   . GLU A  1 393 ? -23.411 -19.114 55.790   1.00 37.01  ? 393 GLU A N   1 
ATOM   3319  C CA  . GLU A  1 393 ? -23.302 -17.948 56.656   1.00 41.04  ? 393 GLU A CA  1 
ATOM   3320  C C   . GLU A  1 393 ? -21.907 -17.738 57.233   1.00 41.21  ? 393 GLU A C   1 
ATOM   3321  O O   . GLU A  1 393 ? -21.551 -16.596 57.545   1.00 40.39  ? 393 GLU A O   1 
ATOM   3322  C CB  . GLU A  1 393 ? -24.309 -18.056 57.808   1.00 49.46  ? 393 GLU A CB  1 
ATOM   3323  C CG  . GLU A  1 393 ? -25.552 -17.206 57.610   1.00 58.25  ? 393 GLU A CG  1 
ATOM   3324  C CD  . GLU A  1 393 ? -26.556 -17.351 58.749   1.00 66.99  ? 393 GLU A CD  1 
ATOM   3325  O OE1 . GLU A  1 393 ? -27.763 -17.131 58.507   1.00 70.36  ? 393 GLU A OE1 1 
ATOM   3326  O OE2 . GLU A  1 393 ? -26.144 -17.690 59.882   1.00 68.04  ? 393 GLU A OE2 1 
ATOM   3327  N N   . ASP A  1 394 ? -21.119 -18.797 57.399   1.00 33.50  ? 394 ASP A N   1 
ATOM   3328  C CA  . ASP A  1 394 ? -19.790 -18.678 57.997   1.00 38.09  ? 394 ASP A CA  1 
ATOM   3329  C C   . ASP A  1 394 ? -18.729 -18.438 56.919   1.00 36.00  ? 394 ASP A C   1 
ATOM   3330  O O   . ASP A  1 394 ? -17.680 -19.074 56.878   1.00 34.44  ? 394 ASP A O   1 
ATOM   3331  C CB  . ASP A  1 394 ? -19.474 -19.918 58.835   1.00 43.85  ? 394 ASP A CB  1 
ATOM   3332  C CG  . ASP A  1 394 ? -19.854 -21.226 58.131   1.00 53.93  ? 394 ASP A CG  1 
ATOM   3333  O OD1 . ASP A  1 394 ? -20.366 -21.161 56.997   1.00 57.31  ? 394 ASP A OD1 1 
ATOM   3334  O OD2 . ASP A  1 394 ? -19.628 -22.321 58.696   1.00 56.56  ? 394 ASP A OD2 1 
ATOM   3335  N N   . VAL A  1 395 ? -19.029 -17.507 56.021   1.00 36.58  ? 395 VAL A N   1 
ATOM   3336  C CA  . VAL A  1 395 ? -18.214 -17.193 54.856   1.00 36.82  ? 395 VAL A CA  1 
ATOM   3337  C C   . VAL A  1 395 ? -18.009 -15.685 54.858   1.00 38.09  ? 395 VAL A C   1 
ATOM   3338  O O   . VAL A  1 395 ? -18.823 -14.942 55.413   1.00 40.40  ? 395 VAL A O   1 
ATOM   3339  C CB  . VAL A  1 395 ? -18.905 -17.689 53.556   1.00 40.16  ? 395 VAL A CB  1 
ATOM   3340  C CG1 . VAL A  1 395 ? -18.498 -16.882 52.329   1.00 47.84  ? 395 VAL A CG1 1 
ATOM   3341  C CG2 . VAL A  1 395 ? -18.630 -19.191 53.337   1.00 34.41  ? 395 VAL A CG2 1 
ATOM   3342  N N   . LYS A  1 396 ? -16.896 -15.226 54.284   1.00 28.52  ? 396 LYS A N   1 
ATOM   3343  C CA  . LYS A  1 396 ? -16.650 -13.797 54.258   1.00 29.13  ? 396 LYS A CA  1 
ATOM   3344  C C   . LYS A  1 396 ? -17.138 -13.184 52.950   1.00 31.07  ? 396 LYS A C   1 
ATOM   3345  O O   . LYS A  1 396 ? -17.236 -13.848 51.906   1.00 27.69  ? 396 LYS A O   1 
ATOM   3346  C CB  . LYS A  1 396 ? -15.173 -13.502 54.509   1.00 37.40  ? 396 LYS A CB  1 
ATOM   3347  C CG  . LYS A  1 396 ? -14.729 -13.939 55.939   1.00 40.26  ? 396 LYS A CG  1 
ATOM   3348  C CD  . LYS A  1 396 ? -15.484 -13.191 57.046   1.00 40.94  ? 396 LYS A CD  1 
ATOM   3349  C CE  . LYS A  1 396 ? -15.086 -13.672 58.446   1.00 43.92  ? 396 LYS A CE  1 
ATOM   3350  N NZ  . LYS A  1 396 ? -16.244 -13.726 59.399   1.00 47.11  ? 396 LYS A NZ  1 
ATOM   3351  N N   . THR A  1 397 ? -17.457 -11.901 53.028   1.00 33.82  ? 397 THR A N   1 
ATOM   3352  C CA  . THR A  1 397 ? -18.376 -11.269 52.103   1.00 34.85  ? 397 THR A CA  1 
ATOM   3353  C C   . THR A  1 397 ? -17.821 -9.904  51.724   1.00 32.58  ? 397 THR A C   1 
ATOM   3354  O O   . THR A  1 397 ? -17.072 -9.297  52.492   1.00 34.65  ? 397 THR A O   1 
ATOM   3355  C CB  . THR A  1 397 ? -19.756 -11.192 52.786   1.00 36.32  ? 397 THR A CB  1 
ATOM   3356  O OG1 . THR A  1 397 ? -20.683 -12.041 52.105   1.00 40.41  ? 397 THR A OG1 1 
ATOM   3357  C CG2 . THR A  1 397 ? -20.292 -9.746  52.910   1.00 35.77  ? 397 THR A CG2 1 
ATOM   3358  N N   . GLU A  1 398 ? -18.173 -9.426  50.535   1.00 30.97  ? 398 GLU A N   1 
ATOM   3359  C CA  . GLU A  1 398 ? -17.710 -8.109  50.117   1.00 32.11  ? 398 GLU A CA  1 
ATOM   3360  C C   . GLU A  1 398 ? -18.663 -7.556  49.066   1.00 31.52  ? 398 GLU A C   1 
ATOM   3361  O O   . GLU A  1 398 ? -19.191 -8.307  48.243   1.00 34.49  ? 398 GLU A O   1 
ATOM   3362  C CB  . GLU A  1 398 ? -16.280 -8.158  49.567   1.00 37.64  ? 398 GLU A CB  1 
ATOM   3363  C CG  . GLU A  1 398 ? -15.722 -6.804  49.118   1.00 49.76  ? 398 GLU A CG  1 
ATOM   3364  C CD  . GLU A  1 398 ? -15.538 -5.818  50.266   1.00 62.75  ? 398 GLU A CD  1 
ATOM   3365  O OE1 . GLU A  1 398 ? -16.532 -5.180  50.685   1.00 66.43  ? 398 GLU A OE1 1 
ATOM   3366  O OE2 . GLU A  1 398 ? -14.393 -5.681  50.749   1.00 68.15  ? 398 GLU A OE2 1 
ATOM   3367  N N   . VAL A  1 399 ? -18.868 -6.244  49.098   1.00 30.18  ? 399 VAL A N   1 
ATOM   3368  C CA  . VAL A  1 399 ? -19.658 -5.561  48.084   1.00 31.31  ? 399 VAL A CA  1 
ATOM   3369  C C   . VAL A  1 399 ? -18.722 -5.026  47.014   1.00 33.60  ? 399 VAL A C   1 
ATOM   3370  O O   . VAL A  1 399 ? -17.641 -4.517  47.325   1.00 33.19  ? 399 VAL A O   1 
ATOM   3371  C CB  . VAL A  1 399 ? -20.487 -4.434  48.723   1.00 33.58  ? 399 VAL A CB  1 
ATOM   3372  C CG1 . VAL A  1 399 ? -21.236 -3.656  47.655   1.00 32.74  ? 399 VAL A CG1 1 
ATOM   3373  C CG2 . VAL A  1 399 ? -21.456 -5.037  49.713   1.00 30.85  ? 399 VAL A CG2 1 
ATOM   3374  N N   . ILE A  1 400 ? -19.134 -5.144  45.748   1.00 29.49  ? 400 ILE A N   1 
ATOM   3375  C CA  . ILE A  1 400 ? -18.412 -4.565  44.623   1.00 31.99  ? 400 ILE A CA  1 
ATOM   3376  C C   . ILE A  1 400 ? -19.396 -3.703  43.830   1.00 28.94  ? 400 ILE A C   1 
ATOM   3377  O O   . ILE A  1 400 ? -20.573 -4.058  43.683   1.00 27.27  ? 400 ILE A O   1 
ATOM   3378  C CB  . ILE A  1 400 ? -17.754 -5.676  43.767   1.00 32.51  ? 400 ILE A CB  1 
ATOM   3379  C CG1 . ILE A  1 400 ? -16.893 -5.100  42.650   1.00 39.02  ? 400 ILE A CG1 1 
ATOM   3380  C CG2 . ILE A  1 400 ? -18.772 -6.632  43.167   1.00 28.48  ? 400 ILE A CG2 1 
ATOM   3381  C CD1 . ILE A  1 400 ? -16.320 -6.187  41.755   1.00 37.59  ? 400 ILE A CD1 1 
ATOM   3382  N N   . GLU A  1 401 ? -18.943 -2.530  43.375   1.00 29.11  ? 401 GLU A N   1 
ATOM   3383  C CA  . GLU A  1 401 ? -19.863 -1.597  42.720   1.00 28.89  ? 401 GLU A CA  1 
ATOM   3384  C C   . GLU A  1 401 ? -19.694 -1.537  41.208   1.00 24.68  ? 401 GLU A C   1 
ATOM   3385  O O   . GLU A  1 401 ? -20.618 -1.089  40.520   1.00 26.43  ? 401 GLU A O   1 
ATOM   3386  C CB  . GLU A  1 401 ? -19.705 -0.181  43.300   1.00 32.61  ? 401 GLU A CB  1 
ATOM   3387  C CG  . GLU A  1 401 ? -19.848 -0.112  44.824   1.00 37.14  ? 401 GLU A CG  1 
ATOM   3388  C CD  . GLU A  1 401 ? -21.287 -0.271  45.277   1.00 42.94  ? 401 GLU A CD  1 
ATOM   3389  O OE1 . GLU A  1 401 ? -21.518 -0.502  46.482   1.00 48.24  ? 401 GLU A OE1 1 
ATOM   3390  O OE2 . GLU A  1 401 ? -22.193 -0.151  44.427   1.00 44.33  ? 401 GLU A OE2 1 
ATOM   3391  N N   . SER A  1 402 ? -18.561 -1.997  40.684   1.00 24.70  ? 402 SER A N   1 
ATOM   3392  C CA  . SER A  1 402 ? -18.256 -1.883  39.269   1.00 29.34  ? 402 SER A CA  1 
ATOM   3393  C C   . SER A  1 402 ? -17.365 -3.043  38.837   1.00 29.11  ? 402 SER A C   1 
ATOM   3394  O O   . SER A  1 402 ? -16.522 -3.526  39.599   1.00 23.69  ? 402 SER A O   1 
ATOM   3395  C CB  . SER A  1 402 ? -17.576 -0.546  38.962   1.00 28.49  ? 402 SER A CB  1 
ATOM   3396  O OG  . SER A  1 402 ? -17.311 -0.419  37.571   1.00 31.05  ? 402 SER A OG  1 
ATOM   3397  N N   . VAL A  1 403 ? -17.566 -3.493  37.602   1.00 26.29  ? 403 VAL A N   1 
ATOM   3398  C CA  . VAL A  1 403 ? -16.700 -4.489  36.989   1.00 28.54  ? 403 VAL A CA  1 
ATOM   3399  C C   . VAL A  1 403 ? -16.254 -3.963  35.634   1.00 29.07  ? 403 VAL A C   1 
ATOM   3400  O O   . VAL A  1 403 ? -16.959 -3.179  34.987   1.00 29.22  ? 403 VAL A O   1 
ATOM   3401  C CB  . VAL A  1 403 ? -17.380 -5.877  36.830   1.00 25.45  ? 403 VAL A CB  1 
ATOM   3402  C CG1 . VAL A  1 403 ? -18.041 -6.317  38.139   1.00 25.59  ? 403 VAL A CG1 1 
ATOM   3403  C CG2 . VAL A  1 403 ? -18.386 -5.853  35.672   1.00 29.34  ? 403 VAL A CG2 1 
ATOM   3404  N N   . LYS A  1 404 ? -15.058 -4.383  35.226   1.00 27.12  ? 404 LYS A N   1 
ATOM   3405  C CA  . LYS A  1 404 ? -14.527 -4.116  33.893   1.00 28.80  ? 404 LYS A CA  1 
ATOM   3406  C C   . LYS A  1 404 ? -14.974 -5.253  32.974   1.00 24.59  ? 404 LYS A C   1 
ATOM   3407  O O   . LYS A  1 404 ? -14.560 -6.406  33.153   1.00 23.08  ? 404 LYS A O   1 
ATOM   3408  C CB  . LYS A  1 404 ? -13.005 -3.989  33.955   1.00 32.79  ? 404 LYS A CB  1 
ATOM   3409  C CG  . LYS A  1 404 ? -12.355 -3.599  32.650   1.00 36.91  ? 404 LYS A CG  1 
ATOM   3410  C CD  . LYS A  1 404 ? -11.077 -2.825  32.904   1.00 41.49  ? 404 LYS A CD  1 
ATOM   3411  C CE  . LYS A  1 404 ? -11.385 -1.527  33.638   1.00 48.19  ? 404 LYS A CE  1 
ATOM   3412  N NZ  . LYS A  1 404 ? -12.606 -0.849  33.083   1.00 51.93  ? 404 LYS A NZ  1 
ATOM   3413  N N   . ALA A  1 405 ? -15.834 -4.928  32.003   1.00 22.28  ? 405 ALA A N   1 
ATOM   3414  C CA  . ALA A  1 405 ? -16.400 -5.927  31.096   1.00 25.34  ? 405 ALA A CA  1 
ATOM   3415  C C   . ALA A  1 405 ? -15.315 -6.823  30.506   1.00 20.89  ? 405 ALA A C   1 
ATOM   3416  O O   . ALA A  1 405 ? -14.204 -6.368  30.221   1.00 22.19  ? 405 ALA A O   1 
ATOM   3417  C CB  . ALA A  1 405 ? -17.179 -5.228  29.972   1.00 18.54  ? 405 ALA A CB  1 
ATOM   3418  N N   . GLY A  1 406 ? -15.633 -8.103  30.330   1.00 21.72  ? 406 GLY A N   1 
ATOM   3419  C CA  . GLY A  1 406 ? -14.632 -9.034  29.837   1.00 22.32  ? 406 GLY A CA  1 
ATOM   3420  C C   . GLY A  1 406 ? -15.138 -10.462 29.802   1.00 19.20  ? 406 GLY A C   1 
ATOM   3421  O O   . GLY A  1 406 ? -16.315 -10.737 30.034   1.00 22.88  ? 406 GLY A O   1 
ATOM   3422  N N   . THR A  1 407 ? -14.219 -11.376 29.499   1.00 22.91  ? 407 THR A N   1 
ATOM   3423  C CA  . THR A  1 407 ? -14.481 -12.812 29.470   1.00 17.80  ? 407 THR A CA  1 
ATOM   3424  C C   . THR A  1 407 ? -13.340 -13.509 30.184   1.00 19.25  ? 407 THR A C   1 
ATOM   3425  O O   . THR A  1 407 ? -12.338 -12.884 30.527   1.00 25.20  ? 407 THR A O   1 
ATOM   3426  C CB  . THR A  1 407 ? -14.562 -13.361 28.048   1.00 22.57  ? 407 THR A CB  1 
ATOM   3427  O OG1 . THR A  1 407 ? -13.240 -13.342 27.488   1.00 21.06  ? 407 THR A OG1 1 
ATOM   3428  C CG2 . THR A  1 407 ? -15.526 -12.512 27.174   1.00 20.60  ? 407 THR A CG2 1 
ATOM   3429  N N   . TRP A  1 408 ? -13.457 -14.830 30.349   1.00 18.24  ? 408 TRP A N   1 
ATOM   3430  C CA  . TRP A  1 408 ? -12.336 -15.574 30.920   1.00 18.93  ? 408 TRP A CA  1 
ATOM   3431  C C   . TRP A  1 408 ? -11.221 -15.843 29.918   1.00 25.30  ? 408 TRP A C   1 
ATOM   3432  O O   . TRP A  1 408 ? -10.232 -16.491 30.281   1.00 22.57  ? 408 TRP A O   1 
ATOM   3433  C CB  . TRP A  1 408 ? -12.804 -16.906 31.553   1.00 20.16  ? 408 TRP A CB  1 
ATOM   3434  C CG  . TRP A  1 408 ? -13.531 -17.916 30.648   1.00 23.05  ? 408 TRP A CG  1 
ATOM   3435  C CD1 . TRP A  1 408 ? -13.774 -17.819 29.277   1.00 24.06  ? 408 TRP A CD1 1 
ATOM   3436  C CD2 . TRP A  1 408 ? -14.137 -19.155 31.068   1.00 20.82  ? 408 TRP A CD2 1 
ATOM   3437  N NE1 . TRP A  1 408 ? -14.469 -18.948 28.842   1.00 20.17  ? 408 TRP A NE1 1 
ATOM   3438  C CE2 . TRP A  1 408 ? -14.705 -19.767 29.920   1.00 21.95  ? 408 TRP A CE2 1 
ATOM   3439  C CE3 . TRP A  1 408 ? -14.232 -19.823 32.306   1.00 24.44  ? 408 TRP A CE3 1 
ATOM   3440  C CZ2 . TRP A  1 408 ? -15.359 -21.008 29.981   1.00 23.25  ? 408 TRP A CZ2 1 
ATOM   3441  C CZ3 . TRP A  1 408 ? -14.884 -21.039 32.359   1.00 21.92  ? 408 TRP A CZ3 1 
ATOM   3442  C CH2 . TRP A  1 408 ? -15.440 -21.619 31.205   1.00 25.06  ? 408 TRP A CH2 1 
ATOM   3443  N N   . PHE A  1 409 ? -11.351 -15.396 28.661   1.00 23.79  ? 409 PHE A N   1 
ATOM   3444  C CA  . PHE A  1 409 ? -10.213 -15.374 27.731   1.00 27.35  ? 409 PHE A CA  1 
ATOM   3445  C C   . PHE A  1 409 ? -9.552  -14.000 27.808   1.00 27.61  ? 409 PHE A C   1 
ATOM   3446  O O   . PHE A  1 409 ? -9.985  -13.052 27.142   1.00 28.28  ? 409 PHE A O   1 
ATOM   3447  C CB  . PHE A  1 409 ? -10.637 -15.694 26.299   1.00 26.70  ? 409 PHE A CB  1 
ATOM   3448  C CG  . PHE A  1 409 ? -9.485  -16.101 25.420   1.00 38.06  ? 409 PHE A CG  1 
ATOM   3449  C CD1 . PHE A  1 409 ? -8.485  -15.193 25.096   1.00 40.77  ? 409 PHE A CD1 1 
ATOM   3450  C CD2 . PHE A  1 409 ? -9.383  -17.404 24.948   1.00 42.08  ? 409 PHE A CD2 1 
ATOM   3451  C CE1 . PHE A  1 409 ? -7.408  -15.575 24.297   1.00 45.48  ? 409 PHE A CE1 1 
ATOM   3452  C CE2 . PHE A  1 409 ? -8.309  -17.794 24.151   1.00 41.20  ? 409 PHE A CE2 1 
ATOM   3453  C CZ  . PHE A  1 409 ? -7.323  -16.878 23.829   1.00 42.36  ? 409 PHE A CZ  1 
ATOM   3454  N N   . ASP A  1 410 ? -8.502  -13.900 28.628   1.00 24.95  ? 410 ASP A N   1 
ATOM   3455  C CA  . ASP A  1 410 ? -7.655  -12.718 28.787   1.00 31.30  ? 410 ASP A CA  1 
ATOM   3456  C C   . ASP A  1 410 ? -8.395  -11.517 29.364   1.00 30.02  ? 410 ASP A C   1 
ATOM   3457  O O   . ASP A  1 410 ? -7.878  -10.394 29.311   1.00 32.53  ? 410 ASP A O   1 
ATOM   3458  C CB  . ASP A  1 410 ? -6.992  -12.308 27.462   1.00 38.03  ? 410 ASP A CB  1 
ATOM   3459  C CG  . ASP A  1 410 ? -6.002  -13.335 26.963   1.00 48.33  ? 410 ASP A CG  1 
ATOM   3460  O OD1 . ASP A  1 410 ? -5.569  -14.178 27.774   1.00 46.71  ? 410 ASP A OD1 1 
ATOM   3461  O OD2 . ASP A  1 410 ? -5.644  -13.290 25.763   1.00 56.70  ? 410 ASP A OD2 1 
ATOM   3462  N N   . GLY A  1 411 ? -9.589  -11.717 29.907   1.00 25.26  ? 411 GLY A N   1 
ATOM   3463  C CA  . GLY A  1 411 ? -10.371 -10.596 30.367   1.00 26.82  ? 411 GLY A CA  1 
ATOM   3464  C C   . GLY A  1 411 ? -10.906 -9.704  29.272   1.00 25.49  ? 411 GLY A C   1 
ATOM   3465  O O   . GLY A  1 411 ? -11.244 -8.553  29.549   1.00 26.90  ? 411 GLY A O   1 
ATOM   3466  N N   . ASN A  1 412 ? -10.991 -10.183 28.031   1.00 21.66  ? 412 ASN A N   1 
ATOM   3467  C CA  . ASN A  1 412 ? -11.461 -9.310  26.954   1.00 24.08  ? 412 ASN A CA  1 
ATOM   3468  C C   . ASN A  1 412 ? -12.230 -10.146 25.939   1.00 24.89  ? 412 ASN A C   1 
ATOM   3469  O O   . ASN A  1 412 ? -12.407 -11.354 26.109   1.00 25.81  ? 412 ASN A O   1 
ATOM   3470  C CB  . ASN A  1 412 ? -10.296 -8.538  26.323   1.00 27.21  ? 412 ASN A CB  1 
ATOM   3471  C CG  . ASN A  1 412 ? -9.315  -9.437  25.606   1.00 30.71  ? 412 ASN A CG  1 
ATOM   3472  O OD1 . ASN A  1 412 ? -9.709  -10.316 24.850   1.00 35.05  ? 412 ASN A OD1 1 
ATOM   3473  N ND2 . ASN A  1 412 ? -8.025  -9.213  25.830   1.00 31.29  ? 412 ASN A ND2 1 
ATOM   3474  N N   . PHE A  1 413 ? -12.665 -9.487  24.859   1.00 27.79  ? 413 PHE A N   1 
ATOM   3475  C CA  . PHE A  1 413 ? -13.591 -10.056 23.886   1.00 25.14  ? 413 PHE A CA  1 
ATOM   3476  C C   . PHE A  1 413 ? -12.936 -10.358 22.547   1.00 26.37  ? 413 PHE A C   1 
ATOM   3477  O O   . PHE A  1 413 ? -13.647 -10.577 21.559   1.00 22.01  ? 413 PHE A O   1 
ATOM   3478  C CB  . PHE A  1 413 ? -14.765 -9.103  23.661   1.00 23.83  ? 413 PHE A CB  1 
ATOM   3479  C CG  . PHE A  1 413 ? -15.629 -8.913  24.868   1.00 26.15  ? 413 PHE A CG  1 
ATOM   3480  C CD1 . PHE A  1 413 ? -15.353 -7.905  25.784   1.00 30.76  ? 413 PHE A CD1 1 
ATOM   3481  C CD2 . PHE A  1 413 ? -16.726 -9.720  25.074   1.00 23.79  ? 413 PHE A CD2 1 
ATOM   3482  C CE1 . PHE A  1 413 ? -16.149 -7.723  26.899   1.00 27.31  ? 413 PHE A CE1 1 
ATOM   3483  C CE2 . PHE A  1 413 ? -17.538 -9.542  26.208   1.00 23.60  ? 413 PHE A CE2 1 
ATOM   3484  C CZ  . PHE A  1 413 ? -17.241 -8.547  27.106   1.00 24.83  ? 413 PHE A CZ  1 
ATOM   3485  N N   . LEU A  1 414 ? -11.600 -10.379 22.495   1.00 27.75  ? 414 LEU A N   1 
ATOM   3486  C CA  . LEU A  1 414 ? -10.908 -10.428 21.207   1.00 32.81  ? 414 LEU A CA  1 
ATOM   3487  C C   . LEU A  1 414 ? -11.189 -11.717 20.442   1.00 34.19  ? 414 LEU A C   1 
ATOM   3488  O O   . LEU A  1 414 ? -11.131 -11.723 19.207   1.00 40.85  ? 414 LEU A O   1 
ATOM   3489  C CB  . LEU A  1 414 ? -9.406  -10.266 21.417   1.00 31.67  ? 414 LEU A CB  1 
ATOM   3490  C CG  . LEU A  1 414 ? -8.885  -8.935  21.933   1.00 28.54  ? 414 LEU A CG  1 
ATOM   3491  C CD1 . LEU A  1 414 ? -7.380  -8.860  21.684   1.00 27.53  ? 414 LEU A CD1 1 
ATOM   3492  C CD2 . LEU A  1 414 ? -9.626  -7.771  21.279   1.00 29.78  ? 414 LEU A CD2 1 
ATOM   3493  N N   . LYS A  1 415 ? -11.513 -12.805 21.140   1.00 29.64  ? 415 LYS A N   1 
ATOM   3494  C CA  . LYS A  1 415 ? -11.716 -14.084 20.471   1.00 32.45  ? 415 LYS A CA  1 
ATOM   3495  C C   . LYS A  1 415 ? -13.059 -14.188 19.756   1.00 23.40  ? 415 LYS A C   1 
ATOM   3496  O O   . LYS A  1 415 ? -13.304 -15.215 19.110   1.00 22.51  ? 415 LYS A O   1 
ATOM   3497  C CB  . LYS A  1 415 ? -11.551 -15.236 21.469   1.00 37.75  ? 415 LYS A CB  1 
ATOM   3498  C CG  . LYS A  1 415 ? -10.125 -15.329 22.025   1.00 44.78  ? 415 LYS A CG  1 
ATOM   3499  C CD  . LYS A  1 415 ? -9.114  -15.724 20.948   1.00 49.90  ? 415 LYS A CD  1 
ATOM   3500  C CE  . LYS A  1 415 ? -9.202  -17.205 20.608   1.00 54.36  ? 415 LYS A CE  1 
ATOM   3501  N NZ  . LYS A  1 415 ? -8.177  -17.623 19.613   1.00 57.72  ? 415 LYS A NZ  1 
ATOM   3502  N N   . TRP A  1 416 ? -13.898 -13.144 19.815   1.00 23.24  ? 416 TRP A N   1 
ATOM   3503  C CA  . TRP A  1 416 ? -15.215 -13.128 19.173   1.00 23.05  ? 416 TRP A CA  1 
ATOM   3504  C C   . TRP A  1 416 ? -15.527 -11.832 18.423   1.00 28.77  ? 416 TRP A C   1 
ATOM   3505  O O   . TRP A  1 416 ? -16.553 -11.767 17.731   1.00 25.78  ? 416 TRP A O   1 
ATOM   3506  C CB  . TRP A  1 416 ? -16.330 -13.365 20.213   1.00 23.60  ? 416 TRP A CB  1 
ATOM   3507  C CG  . TRP A  1 416 ? -16.151 -14.605 21.037   1.00 25.23  ? 416 TRP A CG  1 
ATOM   3508  C CD1 . TRP A  1 416 ? -16.605 -15.874 20.748   1.00 21.32  ? 416 TRP A CD1 1 
ATOM   3509  C CD2 . TRP A  1 416 ? -15.459 -14.709 22.289   1.00 22.89  ? 416 TRP A CD2 1 
ATOM   3510  N NE1 . TRP A  1 416 ? -16.234 -16.748 21.749   1.00 18.22  ? 416 TRP A NE1 1 
ATOM   3511  C CE2 . TRP A  1 416 ? -15.518 -16.063 22.693   1.00 21.55  ? 416 TRP A CE2 1 
ATOM   3512  C CE3 . TRP A  1 416 ? -14.767 -13.796 23.092   1.00 19.38  ? 416 TRP A CE3 1 
ATOM   3513  C CZ2 . TRP A  1 416 ? -14.936 -16.512 23.874   1.00 20.30  ? 416 TRP A CZ2 1 
ATOM   3514  C CZ3 . TRP A  1 416 ? -14.172 -14.254 24.255   1.00 22.62  ? 416 TRP A CZ3 1 
ATOM   3515  C CH2 . TRP A  1 416 ? -14.272 -15.596 24.638   1.00 22.75  ? 416 TRP A CH2 1 
ATOM   3516  N N   . ILE A  1 417 ? -14.696 -10.802 18.546   1.00 19.83  ? 417 ILE A N   1 
ATOM   3517  C CA  . ILE A  1 417 ? -14.868 -9.576  17.784   1.00 26.88  ? 417 ILE A CA  1 
ATOM   3518  C C   . ILE A  1 417 ? -13.493 -8.944  17.620   1.00 29.40  ? 417 ILE A C   1 
ATOM   3519  O O   . ILE A  1 417 ? -12.596 -9.148  18.443   1.00 26.14  ? 417 ILE A O   1 
ATOM   3520  C CB  . ILE A  1 417 ? -15.884 -8.633  18.478   1.00 27.33  ? 417 ILE A CB  1 
ATOM   3521  C CG1 . ILE A  1 417 ? -16.286 -7.465  17.573   1.00 27.26  ? 417 ILE A CG1 1 
ATOM   3522  C CG2 . ILE A  1 417 ? -15.342 -8.148  19.809   1.00 28.33  ? 417 ILE A CG2 1 
ATOM   3523  C CD1 . ILE A  1 417 ? -17.684 -6.977  17.839   1.00 26.28  ? 417 ILE A CD1 1 
ATOM   3524  N N   . GLY A  1 418 ? -13.302 -8.224  16.525   1.00 27.08  ? 418 GLY A N   1 
ATOM   3525  C CA  . GLY A  1 418 ? -12.103 -7.417  16.440   1.00 32.83  ? 418 GLY A CA  1 
ATOM   3526  C C   . GLY A  1 418 ? -11.235 -7.577  15.214   1.00 39.67  ? 418 GLY A C   1 
ATOM   3527  O O   . GLY A  1 418 ? -10.557 -6.626  14.821   1.00 56.95  ? 418 GLY A O   1 
ATOM   3528  N N   . ASN A  1 419 ? -11.209 -8.752  14.606   1.00 32.98  ? 419 ASN A N   1 
ATOM   3529  C CA  . ASN A  1 419 ? -10.461 -8.905  13.373   1.00 35.13  ? 419 ASN A CA  1 
ATOM   3530  C C   . ASN A  1 419 ? -11.434 -8.891  12.197   1.00 35.25  ? 419 ASN A C   1 
ATOM   3531  O O   . ASN A  1 419 ? -12.658 -8.914  12.370   1.00 35.85  ? 419 ASN A O   1 
ATOM   3532  C CB  . ASN A  1 419 ? -9.585  -10.172 13.402   1.00 34.88  ? 419 ASN A CB  1 
ATOM   3533  C CG  . ASN A  1 419 ? -10.380 -11.467 13.328   1.00 35.72  ? 419 ASN A CG  1 
ATOM   3534  O OD1 . ASN A  1 419 ? -11.518 -11.503 12.864   1.00 36.13  ? 419 ASN A OD1 1 
ATOM   3535  N ND2 . ASN A  1 419 ? -9.759  -12.556 13.771   1.00 37.07  ? 419 ASN A ND2 1 
ATOM   3536  N N   . LYS A  1 420 ? -10.872 -8.859  10.988   1.00 31.88  ? 420 LYS A N   1 
ATOM   3537  C CA  . LYS A  1 420 ? -11.698 -8.704  9.795    1.00 34.35  ? 420 LYS A CA  1 
ATOM   3538  C C   . LYS A  1 420 ? -12.733 -9.813  9.700    1.00 32.27  ? 420 LYS A C   1 
ATOM   3539  O O   . LYS A  1 420 ? -13.915 -9.548  9.448    1.00 30.80  ? 420 LYS A O   1 
ATOM   3540  C CB  . LYS A  1 420 ? -10.814 -8.667  8.549    1.00 41.36  ? 420 LYS A CB  1 
ATOM   3541  C CG  . LYS A  1 420 ? -9.918  -7.433  8.493    1.00 55.16  ? 420 LYS A CG  1 
ATOM   3542  C CD  . LYS A  1 420 ? -8.642  -7.682  7.682    1.00 64.32  ? 420 LYS A CD  1 
ATOM   3543  C CE  . LYS A  1 420 ? -7.695  -6.483  7.741    1.00 69.88  ? 420 LYS A CE  1 
ATOM   3544  N NZ  . LYS A  1 420 ? -6.387  -6.835  8.376    1.00 73.13  ? 420 LYS A NZ  1 
ATOM   3545  N N   . GLU A  1 421 ? -12.316 -11.060 9.959    1.00 28.07  ? 421 GLU A N   1 
ATOM   3546  C CA  . GLU A  1 421 ? -13.204 -12.194 9.733    1.00 29.49  ? 421 GLU A CA  1 
ATOM   3547  C C   . GLU A  1 421 ? -14.289 -12.275 10.801   1.00 27.66  ? 421 GLU A C   1 
ATOM   3548  O O   . GLU A  1 421 ? -15.464 -12.488 10.480   1.00 27.99  ? 421 GLU A O   1 
ATOM   3549  C CB  . GLU A  1 421 ? -12.392 -13.495 9.666    1.00 38.71  ? 421 GLU A CB  1 
ATOM   3550  C CG  . GLU A  1 421 ? -11.300 -13.497 8.593    1.00 46.92  ? 421 GLU A CG  1 
ATOM   3551  C CD  . GLU A  1 421 ? -9.935  -13.083 9.134    1.00 57.89  ? 421 GLU A CD  1 
ATOM   3552  O OE1 . GLU A  1 421 ? -8.920  -13.661 8.693    1.00 64.48  ? 421 GLU A OE1 1 
ATOM   3553  O OE2 . GLU A  1 421 ? -9.871  -12.182 10.000   1.00 61.73  ? 421 GLU A OE2 1 
ATOM   3554  N N   . LYS A  1 422 ? -13.980 -12.059 12.049   1.00 28.32  ? 422 LYS A N   1 
ATOM   3555  C CA  . LYS A  1 422 ? -14.986 -12.048 13.094   1.00 23.55  ? 422 LYS A CA  1 
ATOM   3556  C C   . LYS A  1 422 ? -15.949 -10.843 12.920   1.00 29.02  ? 422 LYS A C   1 
ATOM   3557  O O   . LYS A  1 422 ? -17.109 -10.941 13.141   1.00 21.75  ? 422 LYS A O   1 
ATOM   3558  C CB  . LYS A  1 422 ? -14.285 -12.088 14.431   1.00 21.72  ? 422 LYS A CB  1 
ATOM   3559  C CG  . LYS A  1 422 ? -13.576 -13.388 14.741   1.00 27.41  ? 422 LYS A CG  1 
ATOM   3560  C CD  . LYS A  1 422 ? -12.942 -13.376 16.110   1.00 23.40  ? 422 LYS A CD  1 
ATOM   3561  C CE  . LYS A  1 422 ? -11.953 -14.505 16.254   1.00 25.81  ? 422 LYS A CE  1 
ATOM   3562  N NZ  . LYS A  1 422 ? -12.584 -15.832 16.190   1.00 26.75  ? 422 LYS A NZ  1 
ATOM   3563  N N   . ASN A  1 423 ? -15.374 -9.704  12.525   1.00 22.92  ? 423 ASN A N   1 
ATOM   3564  C CA  . ASN A  1 423 ? -16.212 -8.525  12.334   1.00 25.38  ? 423 ASN A CA  1 
ATOM   3565  C C   . ASN A  1 423 ? -17.235 -8.716  11.203   1.00 28.60  ? 423 ASN A C   1 
ATOM   3566  O O   . ASN A  1 423 ? -18.300 -8.200  11.245   1.00 26.75  ? 423 ASN A O   1 
ATOM   3567  C CB  . ASN A  1 423 ? -15.392 -7.271  12.198   1.00 24.58  ? 423 ASN A CB  1 
ATOM   3568  C CG  . ASN A  1 423 ? -14.774 -6.805  13.492   1.00 28.96  ? 423 ASN A CG  1 
ATOM   3569  O OD1 . ASN A  1 423 ? -15.134 -7.229  14.563   1.00 26.54  ? 423 ASN A OD1 1 
ATOM   3570  N ND2 . ASN A  1 423 ? -13.820 -5.907  13.372   1.00 31.02  ? 423 ASN A ND2 1 
ATOM   3571  N N   . GLU A  1 424 ? -16.878 -9.552  10.252   1.00 33.44  ? 424 GLU A N   1 
ATOM   3572  C CA  . GLU A  1 424 ? -17.774 -9.803  9.135    1.00 38.90  ? 424 GLU A CA  1 
ATOM   3573  C C   . GLU A  1 424 ? -18.993 -10.548 9.597    1.00 35.89  ? 424 GLU A C   1 
ATOM   3574  O O   . GLU A  1 424 ? -20.057 -10.256 9.150    1.00 31.53  ? 424 GLU A O   1 
ATOM   3575  C CB  . GLU A  1 424 ? -17.081 -10.494 7.976    1.00 41.42  ? 424 GLU A CB  1 
ATOM   3576  C CG  . GLU A  1 424 ? -18.039 -11.117 6.977    1.00 45.48  ? 424 GLU A CG  1 
ATOM   3577  C CD  . GLU A  1 424 ? -18.619 -10.109 6.005    1.00 54.30  ? 424 GLU A CD  1 
ATOM   3578  O OE1 . GLU A  1 424 ? -19.301 -10.524 5.048    1.00 55.16  ? 424 GLU A OE1 1 
ATOM   3579  O OE2 . GLU A  1 424 ? -18.394 -8.905  6.193    1.00 56.47  ? 424 GLU A OE2 1 
ATOM   3580  N N   . TYR A  1 425 ? -18.818 -11.493 10.523   1.00 33.29  ? 425 TYR A N   1 
ATOM   3581  C CA  . TYR A  1 425 ? -19.941 -12.212 11.088   1.00 28.45  ? 425 TYR A CA  1 
ATOM   3582  C C   . TYR A  1 425 ? -20.867 -11.235 11.810   1.00 29.90  ? 425 TYR A C   1 
ATOM   3583  O O   . TYR A  1 425 ? -22.047 -11.290 11.671   1.00 25.32  ? 425 TYR A O   1 
ATOM   3584  C CB  . TYR A  1 425 ? -19.450 -13.254 12.009   1.00 27.15  ? 425 TYR A CB  1 
ATOM   3585  C CG  . TYR A  1 425 ? -19.297 -14.639 11.441   1.00 30.56  ? 425 TYR A CG  1 
ATOM   3586  C CD1 . TYR A  1 425 ? -18.946 -14.838 10.120   1.00 27.02  ? 425 TYR A CD1 1 
ATOM   3587  C CD2 . TYR A  1 425 ? -19.452 -15.753 12.244   1.00 24.50  ? 425 TYR A CD2 1 
ATOM   3588  C CE1 . TYR A  1 425 ? -18.788 -16.103 9.612    1.00 26.92  ? 425 TYR A CE1 1 
ATOM   3589  C CE2 . TYR A  1 425 ? -19.301 -17.020 11.747   1.00 26.60  ? 425 TYR A CE2 1 
ATOM   3590  C CZ  . TYR A  1 425 ? -18.967 -17.192 10.423   1.00 31.50  ? 425 TYR A CZ  1 
ATOM   3591  O OH  . TYR A  1 425 ? -18.811 -18.443 9.919    1.00 23.81  ? 425 TYR A OH  1 
ATOM   3592  N N   . TRP A  1 426 ? -20.275 -10.326 12.546   1.00 21.80  ? 426 TRP A N   1 
ATOM   3593  C CA  . TRP A  1 426 ? -21.082 -9.368  13.209   1.00 28.44  ? 426 TRP A CA  1 
ATOM   3594  C C   . TRP A  1 426 ? -21.918 -8.471  12.225   1.00 24.79  ? 426 TRP A C   1 
ATOM   3595  O O   . TRP A  1 426 ? -23.040 -8.268  12.443   1.00 27.55  ? 426 TRP A O   1 
ATOM   3596  C CB  . TRP A  1 426 ? -20.285 -8.535  14.210   1.00 28.83  ? 426 TRP A CB  1 
ATOM   3597  C CG  . TRP A  1 426 ? -19.885 -9.254  15.443   1.00 22.10  ? 426 TRP A CG  1 
ATOM   3598  C CD1 . TRP A  1 426 ? -18.665 -9.727  15.740   1.00 20.53  ? 426 TRP A CD1 1 
ATOM   3599  C CD2 . TRP A  1 426 ? -20.719 -9.573  16.544   1.00 21.05  ? 426 TRP A CD2 1 
ATOM   3600  N NE1 . TRP A  1 426 ? -18.674 -10.329 16.954   1.00 21.98  ? 426 TRP A NE1 1 
ATOM   3601  C CE2 . TRP A  1 426 ? -19.931 -10.252 17.473   1.00 25.61  ? 426 TRP A CE2 1 
ATOM   3602  C CE3 . TRP A  1 426 ? -22.062 -9.362  16.830   1.00 27.16  ? 426 TRP A CE3 1 
ATOM   3603  C CZ2 . TRP A  1 426 ? -20.434 -10.711 18.675   1.00 27.53  ? 426 TRP A CZ2 1 
ATOM   3604  C CZ3 . TRP A  1 426 ? -22.560 -9.819  18.024   1.00 27.93  ? 426 TRP A CZ3 1 
ATOM   3605  C CH2 . TRP A  1 426 ? -21.747 -10.490 18.929   1.00 27.17  ? 426 TRP A CH2 1 
ATOM   3606  N N   . LYS A  1 427 ? -21.300 -8.013  11.177   1.00 24.15  ? 427 LYS A N   1 
ATOM   3607  C CA  . LYS A  1 427 ? -22.033 -7.200  10.179   1.00 28.64  ? 427 LYS A CA  1 
ATOM   3608  C C   . LYS A  1 427 ? -23.142 -7.995  9.518    1.00 25.86  ? 427 LYS A C   1 
ATOM   3609  O O   . LYS A  1 427 ? -24.168 -7.511  9.305    1.00 28.35  ? 427 LYS A O   1 
ATOM   3610  C CB  . LYS A  1 427 ? -21.044 -6.524  9.223    1.00 36.35  ? 427 LYS A CB  1 
ATOM   3611  C CG  . LYS A  1 427 ? -21.540 -5.216  8.621    1.00 50.80  ? 427 LYS A CG  1 
ATOM   3612  C CD  . LYS A  1 427 ? -22.666 -4.564  9.419    1.00 46.35  ? 427 LYS A CD  1 
ATOM   3613  C CE  . LYS A  1 427 ? -22.109 -3.510  10.372   1.00 45.42  ? 427 LYS A CE  1 
ATOM   3614  N NZ  . LYS A  1 427 ? -22.784 -2.203  10.215   1.00 42.67  ? 427 LYS A NZ  1 
ATOM   3615  N N   . ILE A  1 428 ? -22.900 -9.246  9.270    1.00 25.34  ? 428 ILE A N   1 
ATOM   3616  C CA  . ILE A  1 428 ? -23.897 -10.123 8.739    1.00 29.35  ? 428 ILE A CA  1 
ATOM   3617  C C   . ILE A  1 428 ? -25.050 -10.226 9.715    1.00 29.88  ? 428 ILE A C   1 
ATOM   3618  O O   . ILE A  1 428 ? -26.156 -10.114 9.323    1.00 30.05  ? 428 ILE A O   1 
ATOM   3619  C CB  . ILE A  1 428 ? -23.317 -11.525 8.460    1.00 30.76  ? 428 ILE A CB  1 
ATOM   3620  C CG1 . ILE A  1 428 ? -22.323 -11.459 7.299    1.00 30.60  ? 428 ILE A CG1 1 
ATOM   3621  C CG2 . ILE A  1 428 ? -24.400 -12.546 8.162    1.00 27.52  ? 428 ILE A CG2 1 
ATOM   3622  C CD1 . ILE A  1 428 ? -21.596 -12.747 7.028    1.00 31.83  ? 428 ILE A CD1 1 
ATOM   3623  N N   . LEU A  1 429 ? -24.743 -10.359 10.984   1.00 23.19  ? 429 LEU A N   1 
ATOM   3624  C CA  . LEU A  1 429 ? -25.766 -10.419 12.026   1.00 27.73  ? 429 LEU A CA  1 
ATOM   3625  C C   . LEU A  1 429 ? -26.550 -9.141  12.135   1.00 23.16  ? 429 LEU A C   1 
ATOM   3626  O O   . LEU A  1 429 ? -27.720 -9.165  12.183   1.00 30.73  ? 429 LEU A O   1 
ATOM   3627  C CB  . LEU A  1 429 ? -25.136 -10.751 13.361   1.00 27.05  ? 429 LEU A CB  1 
ATOM   3628  C CG  . LEU A  1 429 ? -26.070 -11.100 14.499   1.00 28.72  ? 429 LEU A CG  1 
ATOM   3629  C CD1 . LEU A  1 429 ? -26.797 -12.393 14.219   1.00 25.32  ? 429 LEU A CD1 1 
ATOM   3630  C CD2 . LEU A  1 429 ? -25.273 -11.169 15.786   1.00 29.14  ? 429 LEU A CD2 1 
ATOM   3631  N N   . ILE A  1 430 ? -25.868 -8.044  12.122   1.00 23.31  ? 430 ILE A N   1 
ATOM   3632  C CA  . ILE A  1 430 ? -26.533 -6.740  12.156   1.00 29.22  ? 430 ILE A CA  1 
ATOM   3633  C C   . ILE A  1 430 ? -27.527 -6.514  10.992   1.00 32.17  ? 430 ILE A C   1 
ATOM   3634  O O   . ILE A  1 430 ? -28.627 -6.195  11.179   1.00 27.95  ? 430 ILE A O   1 
ATOM   3635  C CB  . ILE A  1 430 ? -25.491 -5.656  12.212   1.00 30.73  ? 430 ILE A CB  1 
ATOM   3636  C CG1 . ILE A  1 430 ? -24.762 -5.713  13.555   1.00 31.30  ? 430 ILE A CG1 1 
ATOM   3637  C CG2 . ILE A  1 430 ? -26.105 -4.281  12.010   1.00 31.25  ? 430 ILE A CG2 1 
ATOM   3638  C CD1 . ILE A  1 430 ? -23.359 -5.175  13.514   1.00 33.41  ? 430 ILE A CD1 1 
ATOM   3639  N N   . GLU A  1 431 ? -27.041 -6.722  9.802    1.00 31.15  ? 431 GLU A N   1 
ATOM   3640  C CA  . GLU A  1 431 ? -27.888 -6.566  8.644    1.00 35.92  ? 431 GLU A CA  1 
ATOM   3641  C C   . GLU A  1 431 ? -29.063 -7.488  8.732    1.00 35.02  ? 431 GLU A C   1 
ATOM   3642  O O   . GLU A  1 431 ? -30.151 -7.079  8.560    1.00 36.93  ? 431 GLU A O   1 
ATOM   3643  C CB  . GLU A  1 431 ? -27.088 -6.808  7.397    1.00 40.88  ? 431 GLU A CB  1 
ATOM   3644  C CG  . GLU A  1 431 ? -26.017 -5.794  7.095    1.00 50.06  ? 431 GLU A CG  1 
ATOM   3645  C CD  . GLU A  1 431 ? -26.540 -4.373  7.100    1.00 59.82  ? 431 GLU A CD  1 
ATOM   3646  O OE1 . GLU A  1 431 ? -25.883 -3.523  7.720    1.00 62.31  ? 431 GLU A OE1 1 
ATOM   3647  O OE2 . GLU A  1 431 ? -27.601 -4.109  6.497    1.00 60.08  ? 431 GLU A OE2 1 
ATOM   3648  N N   . ALA A  1 432 ? -28.814 -8.717  9.096    1.00 27.84  ? 432 ALA A N   1 
ATOM   3649  C CA  . ALA A  1 432 ? -29.862 -9.681  9.254    1.00 32.96  ? 432 ALA A CA  1 
ATOM   3650  C C   . ALA A  1 432 ? -30.894 -9.387  10.378   1.00 33.68  ? 432 ALA A C   1 
ATOM   3651  O O   . ALA A  1 432 ? -32.040 -9.658  10.229   1.00 30.58  ? 432 ALA A O   1 
ATOM   3652  C CB  . ALA A  1 432 ? -29.228 -11.039 9.446    1.00 31.34  ? 432 ALA A CB  1 
ATOM   3653  N N   . LYS A  1 433 ? -30.431 -8.863  11.503   1.00 29.89  ? 433 LYS A N   1 
ATOM   3654  C CA  . LYS A  1 433 ? -31.292 -8.454  12.603   1.00 34.67  ? 433 LYS A CA  1 
ATOM   3655  C C   . LYS A  1 433 ? -32.332 -7.421  12.128   1.00 36.09  ? 433 LYS A C   1 
ATOM   3656  O O   . LYS A  1 433 ? -33.439 -7.427  12.549   1.00 29.89  ? 433 LYS A O   1 
ATOM   3657  C CB  . LYS A  1 433 ? -30.456 -7.912  13.776   1.00 33.93  ? 433 LYS A CB  1 
ATOM   3658  C CG  . LYS A  1 433 ? -31.223 -7.418  14.962   1.00 38.52  ? 433 LYS A CG  1 
ATOM   3659  C CD  . LYS A  1 433 ? -32.218 -8.416  15.478   1.00 37.34  ? 433 LYS A CD  1 
ATOM   3660  C CE  . LYS A  1 433 ? -32.900 -7.826  16.693   1.00 35.24  ? 433 LYS A CE  1 
ATOM   3661  N NZ  . LYS A  1 433 ? -34.008 -8.643  17.205   1.00 34.16  ? 433 LYS A NZ  1 
ATOM   3662  N N   . LYS A  1 434 ? -31.900 -6.601  11.204   1.00 36.73  ? 434 LYS A N   1 
ATOM   3663  C CA  . LYS A  1 434 ? -32.791 -5.630  10.672   1.00 39.77  ? 434 LYS A CA  1 
ATOM   3664  C C   . LYS A  1 434 ? -33.917 -6.265  9.939    1.00 40.09  ? 434 LYS A C   1 
ATOM   3665  O O   . LYS A  1 434 ? -34.940 -5.693  9.818    1.00 39.01  ? 434 LYS A O   1 
ATOM   3666  C CB  . LYS A  1 434 ? -32.072 -4.809  9.707    1.00 48.08  ? 434 LYS A CB  1 
ATOM   3667  C CG  . LYS A  1 434 ? -30.855 -4.048  10.208   1.00 49.82  ? 434 LYS A CG  1 
ATOM   3668  C CD  . LYS A  1 434 ? -30.358 -3.087  9.144    1.00 52.45  ? 434 LYS A CD  1 
ATOM   3669  C CE  . LYS A  1 434 ? -29.234 -2.205  9.648    1.00 51.54  ? 434 LYS A CE  1 
ATOM   3670  N NZ  . LYS A  1 434 ? -28.471 -1.580  8.543    1.00 51.05  ? 434 LYS A NZ  1 
ATOM   3671  N N   . LYS A  1 435 ? -33.676 -7.441  9.407    1.00 40.88  ? 435 LYS A N   1 
ATOM   3672  C CA  . LYS A  1 435 ? -34.679 -8.131  8.600    1.00 40.90  ? 435 LYS A CA  1 
ATOM   3673  C C   . LYS A  1 435 ? -35.246 -9.356  9.221    1.00 39.23  ? 435 LYS A C   1 
ATOM   3674  O O   . LYS A  1 435 ? -35.871 -10.131 8.581    1.00 40.53  ? 435 LYS A O   1 
ATOM   3675  C CB  . LYS A  1 435 ? -34.082 -8.443  7.199    1.00 43.06  ? 435 LYS A CB  1 
ATOM   3676  C CG  . LYS A  1 435 ? -33.785 -7.198  6.391    1.00 45.56  ? 435 LYS A CG  1 
ATOM   3677  C CD  . LYS A  1 435 ? -32.850 -7.469  5.246    1.00 50.84  ? 435 LYS A CD  1 
ATOM   3678  C CE  . LYS A  1 435 ? -33.517 -8.307  4.166    1.00 57.43  ? 435 LYS A CE  1 
ATOM   3679  N NZ  . LYS A  1 435 ? -32.791 -9.578  3.895    1.00 62.51  ? 435 LYS A NZ  1 
ATOM   3680  N N   . ALA A  1 436 ? -35.071 -9.503  10.502   1.00 38.31  ? 436 ALA A N   1 
ATOM   3681  C CA  . ALA A  1 436 ? -35.447 -10.699 11.164   1.00 38.81  ? 436 ALA A CA  1 
ATOM   3682  C C   . ALA A  1 436 ? -36.880 -10.835 11.471   1.00 37.20  ? 436 ALA A C   1 
ATOM   3683  O O   . ALA A  1 436 ? -37.512 -9.910  11.808   1.00 35.52  ? 436 ALA A O   1 
ATOM   3684  C CB  . ALA A  1 436 ? -34.639 -10.843 12.437   1.00 37.62  ? 436 ALA A CB  1 
ATOM   3685  N N   . LYS A  1 437 ? -37.347 -12.044 11.343   1.00 37.88  ? 437 LYS A N   1 
ATOM   3686  C CA  . LYS A  1 437 ? -38.720 -12.339 11.569   1.00 38.59  ? 437 LYS A CA  1 
ATOM   3687  C C   . LYS A  1 437 ? -38.955 -13.445 12.514   1.00 38.02  ? 437 LYS A C   1 
ATOM   3688  O O   . LYS A  1 437 ? -40.068 -13.714 12.835   1.00 44.88  ? 437 LYS A O   1 
ATOM   3689  C CB  . LYS A  1 437 ? -39.359 -12.718 10.211   1.00 41.12  ? 437 LYS A CB  1 
ATOM   3690  C CG  . LYS A  1 437 ? -39.509 -11.546 9.270    1.00 50.04  ? 437 LYS A CG  1 
ATOM   3691  C CD  . LYS A  1 437 ? -38.937 -11.825 7.894    1.00 55.50  ? 437 LYS A CD  1 
ATOM   3692  C CE  . LYS A  1 437 ? -38.562 -10.540 7.177    1.00 56.61  ? 437 LYS A CE  1 
ATOM   3693  N NZ  . LYS A  1 437 ? -37.246 -10.604 6.484    1.00 52.16  ? 437 LYS A NZ  1 
ATOM   3694  N N   . ASN A  1 438 ? -37.916 -14.134 12.919   1.00 32.26  ? 438 ASN A N   1 
ATOM   3695  C CA  . ASN A  1 438 ? -38.063 -15.184 13.865   1.00 35.30  ? 438 ASN A CA  1 
ATOM   3696  C C   . ASN A  1 438 ? -36.837 -15.427 14.791   1.00 34.82  ? 438 ASN A C   1 
ATOM   3697  O O   . ASN A  1 438 ? -35.833 -14.809 14.646   1.00 30.19  ? 438 ASN A O   1 
ATOM   3698  C CB  . ASN A  1 438 ? -38.396 -16.502 13.179   1.00 33.44  ? 438 ASN A CB  1 
ATOM   3699  C CG  . ASN A  1 438 ? -37.359 -16.924 12.215   1.00 32.19  ? 438 ASN A CG  1 
ATOM   3700  O OD1 . ASN A  1 438 ? -36.272 -17.307 12.597   1.00 34.02  ? 438 ASN A OD1 1 
ATOM   3701  N ND2 . ASN A  1 438 ? -37.691 -16.860 10.949   1.00 32.91  ? 438 ASN A ND2 1 
ATOM   3702  N N   . ASP A  1 439 ? -36.966 -16.409 15.668   1.00 33.26  ? 439 ASP A N   1 
ATOM   3703  C CA  . ASP A  1 439 ? -35.933 -16.653 16.692   1.00 33.85  ? 439 ASP A CA  1 
ATOM   3704  C C   . ASP A  1 439 ? -34.662 -17.338 16.294   1.00 28.85  ? 439 ASP A C   1 
ATOM   3705  O O   . ASP A  1 439 ? -33.811 -17.591 17.107   1.00 27.68  ? 439 ASP A O   1 
ATOM   3706  C CB  . ASP A  1 439 ? -36.586 -17.302 17.928   1.00 42.47  ? 439 ASP A CB  1 
ATOM   3707  C CG  . ASP A  1 439 ? -37.260 -16.306 18.803   1.00 47.51  ? 439 ASP A CG  1 
ATOM   3708  O OD1 . ASP A  1 439 ? -37.140 -15.101 18.586   1.00 49.21  ? 439 ASP A OD1 1 
ATOM   3709  O OD2 . ASP A  1 439 ? -37.925 -16.731 19.721   1.00 53.11  ? 439 ASP A OD2 1 
ATOM   3710  N N   . TYR A  1 440 ? -34.538 -17.633 15.042   1.00 28.56  ? 440 TYR A N   1 
ATOM   3711  C CA  . TYR A  1 440 ? -33.310 -18.164 14.549   1.00 25.40  ? 440 TYR A CA  1 
ATOM   3712  C C   . TYR A  1 440 ? -32.180 -17.127 14.604   1.00 23.26  ? 440 TYR A C   1 
ATOM   3713  O O   . TYR A  1 440 ? -31.060 -17.498 14.559   1.00 26.64  ? 440 TYR A O   1 
ATOM   3714  C CB  . TYR A  1 440 ? -33.517 -18.783 13.189   1.00 31.93  ? 440 TYR A CB  1 
ATOM   3715  C CG  . TYR A  1 440 ? -33.934 -20.201 13.196   1.00 28.51  ? 440 TYR A CG  1 
ATOM   3716  C CD1 . TYR A  1 440 ? -33.054 -21.183 13.522   1.00 30.62  ? 440 TYR A CD1 1 
ATOM   3717  C CD2 . TYR A  1 440 ? -35.218 -20.554 12.879   1.00 36.43  ? 440 TYR A CD2 1 
ATOM   3718  C CE1 . TYR A  1 440 ? -33.427 -22.496 13.520   1.00 37.96  ? 440 TYR A CE1 1 
ATOM   3719  C CE2 . TYR A  1 440 ? -35.613 -21.866 12.880   1.00 40.74  ? 440 TYR A CE2 1 
ATOM   3720  C CZ  . TYR A  1 440 ? -34.707 -22.832 13.202   1.00 42.06  ? 440 TYR A CZ  1 
ATOM   3721  O OH  . TYR A  1 440 ? -35.074 -24.133 13.214   1.00 47.13  ? 440 TYR A OH  1 
ATOM   3722  N N   . ILE A  1 441 ? -32.501 -15.864 14.682   1.00 25.05  ? 441 ILE A N   1 
ATOM   3723  C CA  . ILE A  1 441 ? -31.558 -14.781 14.868   1.00 24.86  ? 441 ILE A CA  1 
ATOM   3724  C C   . ILE A  1 441 ? -30.865 -14.923 16.229   1.00 21.46  ? 441 ILE A C   1 
ATOM   3725  O O   . ILE A  1 441 ? -29.752 -14.602 16.358   1.00 24.54  ? 441 ILE A O   1 
ATOM   3726  C CB  . ILE A  1 441 ? -32.275 -13.377 14.750   1.00 26.46  ? 441 ILE A CB  1 
ATOM   3727  C CG1 . ILE A  1 441 ? -31.256 -12.250 14.693   1.00 23.98  ? 441 ILE A CG1 1 
ATOM   3728  C CG2 . ILE A  1 441 ? -33.240 -13.146 15.881   1.00 27.51  ? 441 ILE A CG2 1 
ATOM   3729  C CD1 . ILE A  1 441 ? -30.658 -12.020 13.338   1.00 24.76  ? 441 ILE A CD1 1 
ATOM   3730  N N   . LEU A  1 442 ? -31.570 -15.388 17.217   1.00 21.81  ? 442 LEU A N   1 
ATOM   3731  C CA  . LEU A  1 442 ? -31.020 -15.720 18.501   1.00 19.95  ? 442 LEU A CA  1 
ATOM   3732  C C   . LEU A  1 442 ? -29.997 -16.879 18.402   1.00 20.83  ? 442 LEU A C   1 
ATOM   3733  O O   . LEU A  1 442 ? -29.016 -16.880 19.077   1.00 23.43  ? 442 LEU A O   1 
ATOM   3734  C CB  . LEU A  1 442 ? -32.167 -16.103 19.407   1.00 20.29  ? 442 LEU A CB  1 
ATOM   3735  C CG  . LEU A  1 442 ? -33.209 -15.041 19.714   1.00 29.56  ? 442 LEU A CG  1 
ATOM   3736  C CD1 . LEU A  1 442 ? -34.280 -15.570 20.640   1.00 36.24  ? 442 LEU A CD1 1 
ATOM   3737  C CD2 . LEU A  1 442 ? -32.599 -13.767 20.262   1.00 26.44  ? 442 LEU A CD2 1 
ATOM   3738  N N   . VAL A  1 443 ? -30.303 -17.862 17.597   1.00 19.92  ? 443 VAL A N   1 
ATOM   3739  C CA  . VAL A  1 443 ? -29.387 -18.960 17.364   1.00 23.00  ? 443 VAL A CA  1 
ATOM   3740  C C   . VAL A  1 443 ? -28.077 -18.401 16.786   1.00 26.98  ? 443 VAL A C   1 
ATOM   3741  O O   . VAL A  1 443 ? -27.016 -18.749 17.226   1.00 27.17  ? 443 VAL A O   1 
ATOM   3742  C CB  . VAL A  1 443 ? -29.993 -20.041 16.485   1.00 31.89  ? 443 VAL A CB  1 
ATOM   3743  C CG1 . VAL A  1 443 ? -29.056 -21.218 16.288   1.00 33.54  ? 443 VAL A CG1 1 
ATOM   3744  C CG2 . VAL A  1 443 ? -31.361 -20.467 16.968   1.00 31.90  ? 443 VAL A CG2 1 
ATOM   3745  N N   . ALA A  1 444 ? -28.174 -17.519 15.840   1.00 26.68  ? 444 ALA A N   1 
ATOM   3746  C CA  . ALA A  1 444 ? -27.010 -16.925 15.238   1.00 24.73  ? 444 ALA A CA  1 
ATOM   3747  C C   . ALA A  1 444 ? -26.203 -15.999 16.148   1.00 25.31  ? 444 ALA A C   1 
ATOM   3748  O O   . ALA A  1 444 ? -25.139 -15.639 15.822   1.00 26.53  ? 444 ALA A O   1 
ATOM   3749  C CB  . ALA A  1 444 ? -27.440 -16.164 14.021   1.00 22.90  ? 444 ALA A CB  1 
ATOM   3750  N N   . GLU A  1 445 ? -26.778 -15.634 17.270   1.00 24.92  ? 445 GLU A N   1 
ATOM   3751  C CA  . GLU A  1 445 ? -26.060 -14.816 18.223   1.00 25.74  ? 445 GLU A CA  1 
ATOM   3752  C C   . GLU A  1 445 ? -25.165 -15.667 19.205   1.00 25.97  ? 445 GLU A C   1 
ATOM   3753  O O   . GLU A  1 445 ? -24.580 -15.168 20.069   1.00 25.21  ? 445 GLU A O   1 
ATOM   3754  C CB  . GLU A  1 445 ? -27.009 -13.871 18.927   1.00 27.07  ? 445 GLU A CB  1 
ATOM   3755  C CG  . GLU A  1 445 ? -27.576 -12.741 18.117   1.00 30.43  ? 445 GLU A CG  1 
ATOM   3756  C CD  . GLU A  1 445 ? -28.917 -12.266 18.614   1.00 35.01  ? 445 GLU A CD  1 
ATOM   3757  O OE1 . GLU A  1 445 ? -29.346 -12.632 19.720   1.00 36.30  ? 445 GLU A OE1 1 
ATOM   3758  O OE2 . GLU A  1 445 ? -29.541 -11.501 17.896   1.00 31.87  ? 445 GLU A OE2 1 
ATOM   3759  N N   . GLY A  1 446 ? -25.138 -16.940 19.003   1.00 24.43  ? 446 GLY A N   1 
ATOM   3760  C CA  . GLY A  1 446 ? -24.341 -17.806 19.787   1.00 23.42  ? 446 GLY A CA  1 
ATOM   3761  C C   . GLY A  1 446 ? -22.899 -17.502 19.625   1.00 22.99  ? 446 GLY A C   1 
ATOM   3762  O O   . GLY A  1 446 ? -22.429 -17.263 18.577   1.00 16.47  ? 446 GLY A O   1 
ATOM   3763  N N   . SER A  1 447 ? -22.220 -17.560 20.766   1.00 20.52  ? 447 SER A N   1 
ATOM   3764  C CA  . SER A  1 447 ? -20.798 -17.299 20.783   1.00 26.49  ? 447 SER A CA  1 
ATOM   3765  C C   . SER A  1 447 ? -19.936 -18.161 19.841   1.00 21.77  ? 447 SER A C   1 
ATOM   3766  O O   . SER A  1 447 ? -19.015 -17.691 19.248   1.00 22.12  ? 447 SER A O   1 
ATOM   3767  C CB  . SER A  1 447 ? -20.235 -17.468 22.271   1.00 23.81  ? 447 SER A CB  1 
ATOM   3768  O OG  . SER A  1 447 ? -20.272 -18.753 22.741   1.00 23.83  ? 447 SER A OG  1 
ATOM   3769  N N   . ASP A  1 448 ? -20.262 -19.432 19.784   1.00 19.46  ? 448 ASP A N   1 
ATOM   3770  C CA  . ASP A  1 448 ? -19.429 -20.425 19.097   1.00 18.91  ? 448 ASP A CA  1 
ATOM   3771  C C   . ASP A  1 448 ? -19.061 -20.082 17.622   1.00 22.36  ? 448 ASP A C   1 
ATOM   3772  O O   . ASP A  1 448 ? -17.985 -20.317 17.183   1.00 22.97  ? 448 ASP A O   1 
ATOM   3773  C CB  . ASP A  1 448 ? -20.107 -21.714 19.135   1.00 20.43  ? 448 ASP A CB  1 
ATOM   3774  C CG  . ASP A  1 448 ? -20.566 -22.143 20.523   1.00 22.47  ? 448 ASP A CG  1 
ATOM   3775  O OD1 . ASP A  1 448 ? -21.683 -21.816 20.905   1.00 24.73  ? 448 ASP A OD1 1 
ATOM   3776  O OD2 . ASP A  1 448 ? -19.835 -22.864 21.186   1.00 24.83  ? 448 ASP A OD2 1 
ATOM   3777  N N   . TRP A  1 449 ? -20.005 -19.477 16.929   1.00 24.88  ? 449 TRP A N   1 
ATOM   3778  C CA  . TRP A  1 449 ? -19.805 -19.047 15.517   1.00 27.05  ? 449 TRP A CA  1 
ATOM   3779  C C   . TRP A  1 449 ? -18.692 -18.040 15.384   1.00 22.33  ? 449 TRP A C   1 
ATOM   3780  O O   . TRP A  1 449 ? -17.882 -18.100 14.540   1.00 22.04  ? 449 TRP A O   1 
ATOM   3781  C CB  . TRP A  1 449 ? -21.131 -18.493 14.982   1.00 25.93  ? 449 TRP A CB  1 
ATOM   3782  C CG  . TRP A  1 449 ? -22.404 -19.247 15.380   1.00 23.37  ? 449 TRP A CG  1 
ATOM   3783  C CD1 . TRP A  1 449 ? -23.490 -18.729 16.001   1.00 24.75  ? 449 TRP A CD1 1 
ATOM   3784  C CD2 . TRP A  1 449 ? -22.702 -20.626 15.154   1.00 18.17  ? 449 TRP A CD2 1 
ATOM   3785  N NE1 . TRP A  1 449 ? -24.444 -19.691 16.184   1.00 22.53  ? 449 TRP A NE1 1 
ATOM   3786  C CE2 . TRP A  1 449 ? -23.984 -20.867 15.671   1.00 18.34  ? 449 TRP A CE2 1 
ATOM   3787  C CE3 . TRP A  1 449 ? -22.018 -21.673 14.558   1.00 23.24  ? 449 TRP A CE3 1 
ATOM   3788  C CZ2 . TRP A  1 449 ? -24.584 -22.110 15.618   1.00 19.56  ? 449 TRP A CZ2 1 
ATOM   3789  C CZ3 . TRP A  1 449 ? -22.612 -22.899 14.504   1.00 23.62  ? 449 TRP A CZ3 1 
ATOM   3790  C CH2 . TRP A  1 449 ? -23.887 -23.112 15.031   1.00 18.97  ? 449 TRP A CH2 1 
ATOM   3791  N N   . PHE A  1 450 ? -18.698 -17.145 16.301   1.00 23.39  ? 450 PHE A N   1 
ATOM   3792  C CA  . PHE A  1 450 ? -17.685 -16.131 16.299   1.00 27.78  ? 450 PHE A CA  1 
ATOM   3793  C C   . PHE A  1 450 ? -16.316 -16.671 16.742   1.00 24.80  ? 450 PHE A C   1 
ATOM   3794  O O   . PHE A  1 450 ? -15.337 -16.282 16.218   1.00 23.49  ? 450 PHE A O   1 
ATOM   3795  C CB  . PHE A  1 450 ? -18.138 -14.901 17.064   1.00 28.58  ? 450 PHE A CB  1 
ATOM   3796  C CG  . PHE A  1 450 ? -19.433 -14.354 16.632   1.00 23.64  ? 450 PHE A CG  1 
ATOM   3797  C CD1 . PHE A  1 450 ? -20.605 -14.800 17.200   1.00 23.76  ? 450 PHE A CD1 1 
ATOM   3798  C CD2 . PHE A  1 450 ? -19.479 -13.371 15.677   1.00 21.85  ? 450 PHE A CD2 1 
ATOM   3799  C CE1 . PHE A  1 450 ? -21.806 -14.284 16.807   1.00 24.89  ? 450 PHE A CE1 1 
ATOM   3800  C CE2 . PHE A  1 450 ? -20.677 -12.855 15.277   1.00 25.05  ? 450 PHE A CE2 1 
ATOM   3801  C CZ  . PHE A  1 450 ? -21.846 -13.317 15.838   1.00 26.17  ? 450 PHE A CZ  1 
ATOM   3802  N N   . TRP A  1 451 ? -16.318 -17.581 17.682   1.00 25.76  ? 451 TRP A N   1 
ATOM   3803  C CA  . TRP A  1 451 ? -15.063 -18.233 18.095   1.00 27.67  ? 451 TRP A CA  1 
ATOM   3804  C C   . TRP A  1 451 ? -14.321 -18.892 16.944   1.00 28.12  ? 451 TRP A C   1 
ATOM   3805  O O   . TRP A  1 451 ? -13.172 -18.729 16.818   1.00 30.25  ? 451 TRP A O   1 
ATOM   3806  C CB  . TRP A  1 451 ? -15.347 -19.284 19.180   1.00 24.03  ? 451 TRP A CB  1 
ATOM   3807  C CG  . TRP A  1 451 ? -14.284 -20.210 19.524   1.00 30.20  ? 451 TRP A CG  1 
ATOM   3808  C CD1 . TRP A  1 451 ? -14.139 -21.472 19.098   1.00 32.47  ? 451 TRP A CD1 1 
ATOM   3809  C CD2 . TRP A  1 451 ? -13.215 -19.963 20.411   1.00 35.40  ? 451 TRP A CD2 1 
ATOM   3810  N NE1 . TRP A  1 451 ? -13.029 -22.036 19.643   1.00 31.23  ? 451 TRP A NE1 1 
ATOM   3811  C CE2 . TRP A  1 451 ? -12.446 -21.122 20.467   1.00 36.58  ? 451 TRP A CE2 1 
ATOM   3812  C CE3 . TRP A  1 451 ? -12.833 -18.870 21.172   1.00 41.35  ? 451 TRP A CE3 1 
ATOM   3813  C CZ2 . TRP A  1 451 ? -11.314 -21.212 21.233   1.00 38.47  ? 451 TRP A CZ2 1 
ATOM   3814  C CZ3 . TRP A  1 451 ? -11.717 -18.962 21.927   1.00 41.68  ? 451 TRP A CZ3 1 
ATOM   3815  C CH2 . TRP A  1 451 ? -10.966 -20.123 21.955   1.00 41.93  ? 451 TRP A CH2 1 
ATOM   3816  N N   . TRP A  1 452 ? -15.019 -19.716 16.183   1.00 21.00  ? 452 TRP A N   1 
ATOM   3817  C CA  . TRP A  1 452 ? -14.394 -20.459 15.129   1.00 24.29  ? 452 TRP A CA  1 
ATOM   3818  C C   . TRP A  1 452 ? -13.975 -19.609 13.900   1.00 25.76  ? 452 TRP A C   1 
ATOM   3819  O O   . TRP A  1 452 ? -13.101 -19.960 13.181   1.00 23.78  ? 452 TRP A O   1 
ATOM   3820  C CB  . TRP A  1 452 ? -15.284 -21.589 14.737   1.00 22.50  ? 452 TRP A CB  1 
ATOM   3821  C CG  . TRP A  1 452 ? -15.487 -22.605 15.801   1.00 26.12  ? 452 TRP A CG  1 
ATOM   3822  C CD1 . TRP A  1 452 ? -16.635 -22.884 16.451   1.00 28.55  ? 452 TRP A CD1 1 
ATOM   3823  C CD2 . TRP A  1 452 ? -14.508 -23.491 16.332   1.00 25.89  ? 452 TRP A CD2 1 
ATOM   3824  N NE1 . TRP A  1 452 ? -16.442 -23.881 17.349   1.00 25.37  ? 452 TRP A NE1 1 
ATOM   3825  C CE2 . TRP A  1 452 ? -15.137 -24.269 17.303   1.00 25.15  ? 452 TRP A CE2 1 
ATOM   3826  C CE3 . TRP A  1 452 ? -13.156 -23.689 16.090   1.00 24.55  ? 452 TRP A CE3 1 
ATOM   3827  C CZ2 . TRP A  1 452 ? -14.467 -25.229 18.027   1.00 27.08  ? 452 TRP A CZ2 1 
ATOM   3828  C CZ3 . TRP A  1 452 ? -12.498 -24.641 16.796   1.00 29.25  ? 452 TRP A CZ3 1 
ATOM   3829  C CH2 . TRP A  1 452 ? -13.148 -25.403 17.758   1.00 30.32  ? 452 TRP A CH2 1 
ATOM   3830  N N   . GLN A  1 453 ? -14.624 -18.484 13.747   1.00 22.84  ? 453 GLN A N   1 
ATOM   3831  C CA  . GLN A  1 453 ? -14.328 -17.657 12.629   1.00 30.25  ? 453 GLN A CA  1 
ATOM   3832  C C   . GLN A  1 453 ? -13.069 -16.947 12.778   1.00 36.70  ? 453 GLN A C   1 
ATOM   3833  O O   . GLN A  1 453 ? -12.658 -16.580 13.800   1.00 34.76  ? 453 GLN A O   1 
ATOM   3834  C CB  . GLN A  1 453 ? -15.395 -16.620 12.453   1.00 25.86  ? 453 GLN A CB  1 
ATOM   3835  C CG  . GLN A  1 453 ? -15.177 -15.573 11.386   1.00 24.21  ? 453 GLN A CG  1 
ATOM   3836  C CD  . GLN A  1 453 ? -15.368 -16.109 9.990    1.00 29.55  ? 453 GLN A CD  1 
ATOM   3837  O OE1 . GLN A  1 453 ? -15.357 -17.296 9.771    1.00 34.71  ? 453 GLN A OE1 1 
ATOM   3838  N NE2 . GLN A  1 453 ? -15.538 -15.228 9.047    1.00 33.43  ? 453 GLN A NE2 1 
ATOM   3839  N N   . GLY A  1 454 ? -12.492 -16.708 11.665   1.00 41.92  ? 454 GLY A N   1 
ATOM   3840  C CA  . GLY A  1 454 ? -11.344 -15.845 11.715   1.00 49.55  ? 454 GLY A CA  1 
ATOM   3841  C C   . GLY A  1 454 ? -10.222 -16.493 12.305   1.00 55.59  ? 454 GLY A C   1 
ATOM   3842  O O   . GLY A  1 454 ? -9.470  -15.893 13.008   1.00 55.40  ? 454 GLY A O   1 
ATOM   3843  N N   . GLU A  1 455 ? -10.176 -17.763 12.064   1.00 63.51  ? 455 GLU A N   1 
ATOM   3844  C CA  . GLU A  1 455 ? -9.089  -18.552 12.505   1.00 67.04  ? 455 GLU A CA  1 
ATOM   3845  C C   . GLU A  1 455 ? -9.576  -19.814 12.051   1.00 70.84  ? 455 GLU A C   1 
ATOM   3846  O O   . GLU A  1 455 ? -10.062 -20.570 12.861   1.00 68.81  ? 455 GLU A O   1 
ATOM   3847  C CB  . GLU A  1 455 ? -9.010  -18.778 13.981   1.00 66.69  ? 455 GLU A CB  1 
ATOM   3848  C CG  . GLU A  1 455 ? -10.156 -18.375 14.894   1.00 66.24  ? 455 GLU A CG  1 
ATOM   3849  C CD  . GLU A  1 455 ? -9.611  -17.601 16.064   1.00 69.41  ? 455 GLU A CD  1 
ATOM   3850  O OE1 . GLU A  1 455 ? -8.393  -17.346 16.061   1.00 72.16  ? 455 GLU A OE1 1 
ATOM   3851  O OE2 . GLU A  1 455 ? -10.368 -17.230 16.969   1.00 71.16  ? 455 GLU A OE2 1 
ATOM   3852  N N   . GLU A  1 456 ? -9.572  -20.085 10.777   1.00 75.08  ? 456 GLU A N   1 
ATOM   3853  C CA  . GLU A  1 456 ? -10.064 -21.449 10.437   1.00 76.72  ? 456 GLU A CA  1 
ATOM   3854  C C   . GLU A  1 456 ? -8.906  -22.417 10.580   1.00 73.80  ? 456 GLU A C   1 
ATOM   3855  O O   . GLU A  1 456 ? -8.508  -22.676 11.700   1.00 69.91  ? 456 GLU A O   1 
ATOM   3856  C CB  . GLU A  1 456 ? -10.770 -21.555 9.086    1.00 78.25  ? 456 GLU A CB  1 
ATOM   3857  N N   . LYS A  1 457 ? -8.421  -22.960 9.468    1.00 74.36  ? 457 LYS A N   1 
ATOM   3858  C CA  . LYS A  1 457 ? -7.287  -23.792 9.544    1.00 74.77  ? 457 LYS A CA  1 
ATOM   3859  C C   . LYS A  1 457 ? -7.549  -25.193 10.093   1.00 76.56  ? 457 LYS A C   1 
ATOM   3860  O O   . LYS A  1 457 ? -6.623  -25.923 10.305   1.00 80.47  ? 457 LYS A O   1 
ATOM   3861  C CB  . LYS A  1 457 ? -6.271  -23.081 10.428   1.00 76.26  ? 457 LYS A CB  1 
ATOM   3862  N N   . ALA A  1 458 ? -8.813  -25.551 10.295   1.00 72.51  ? 458 ALA A N   1 
ATOM   3863  C CA  . ALA A  1 458 ? -9.162  -26.854 10.906   1.00 65.12  ? 458 ALA A CA  1 
ATOM   3864  C C   . ALA A  1 458 ? -10.122 -27.676 10.197   1.00 52.25  ? 458 ALA A C   1 
ATOM   3865  O O   . ALA A  1 458 ? -11.002 -27.202 9.547    1.00 47.24  ? 458 ALA A O   1 
ATOM   3866  C CB  . ALA A  1 458 ? -9.719  -26.661 12.310   1.00 65.92  ? 458 ALA A CB  1 
ATOM   3867  N N   . PRO A  1 459 ? -9.996  -28.931 10.416   1.00 45.96  ? 459 PRO A N   1 
ATOM   3868  C CA  . PRO A  1 459 ? -10.938 -29.826 9.834    1.00 45.48  ? 459 PRO A CA  1 
ATOM   3869  C C   . PRO A  1 459 ? -12.380 -29.633 10.412   1.00 49.92  ? 459 PRO A C   1 
ATOM   3870  O O   . PRO A  1 459 ? -12.548 -29.559 11.606   1.00 50.47  ? 459 PRO A O   1 
ATOM   3871  C CB  . PRO A  1 459 ? -10.297 -31.158 10.120   1.00 44.86  ? 459 PRO A CB  1 
ATOM   3872  C CG  . PRO A  1 459 ? -8.875  -30.904 10.398   1.00 44.88  ? 459 PRO A CG  1 
ATOM   3873  C CD  . PRO A  1 459 ? -8.937  -29.637 11.136   1.00 47.87  ? 459 PRO A CD  1 
ATOM   3874  N N   . PHE A  1 460 ? -13.371 -29.484 9.565    1.00 45.77  ? 460 PHE A N   1 
ATOM   3875  C CA  . PHE A  1 460 ? -14.783 -29.221 9.964    1.00 38.42  ? 460 PHE A CA  1 
ATOM   3876  C C   . PHE A  1 460 ? -15.209 -27.776 10.312   1.00 28.34  ? 460 PHE A C   1 
ATOM   3877  O O   . PHE A  1 460 ? -16.346 -27.555 10.517   1.00 28.20  ? 460 PHE A O   1 
ATOM   3878  C CB  . PHE A  1 460 ? -15.254 -30.221 10.980   1.00 40.15  ? 460 PHE A CB  1 
ATOM   3879  C CG  . PHE A  1 460 ? -15.103 -31.640 10.524   1.00 45.57  ? 460 PHE A CG  1 
ATOM   3880  C CD1 . PHE A  1 460 ? -15.725 -32.080 9.385    1.00 44.24  ? 460 PHE A CD1 1 
ATOM   3881  C CD2 . PHE A  1 460 ? -14.319 -32.525 11.223   1.00 47.61  ? 460 PHE A CD2 1 
ATOM   3882  C CE1 . PHE A  1 460 ? -15.577 -33.379 8.961    1.00 43.91  ? 460 PHE A CE1 1 
ATOM   3883  C CE2 . PHE A  1 460 ? -14.162 -33.816 10.802   1.00 46.61  ? 460 PHE A CE2 1 
ATOM   3884  C CZ  . PHE A  1 460 ? -14.792 -34.246 9.671    1.00 45.70  ? 460 PHE A CZ  1 
ATOM   3885  N N   . VAL A  1 461 ? -14.325 -26.827 10.321   1.00 27.64  ? 461 VAL A N   1 
ATOM   3886  C CA  . VAL A  1 461 ? -14.754 -25.482 10.703   1.00 35.94  ? 461 VAL A CA  1 
ATOM   3887  C C   . VAL A  1 461 ? -15.711 -24.860 9.697    1.00 37.36  ? 461 VAL A C   1 
ATOM   3888  O O   . VAL A  1 461 ? -16.480 -23.959 10.061   1.00 42.71  ? 461 VAL A O   1 
ATOM   3889  C CB  . VAL A  1 461 ? -13.556 -24.540 10.903   1.00 47.74  ? 461 VAL A CB  1 
ATOM   3890  C CG1 . VAL A  1 461 ? -12.529 -25.194 11.802   1.00 51.28  ? 461 VAL A CG1 1 
ATOM   3891  C CG2 . VAL A  1 461 ? -12.973 -24.115 9.541    1.00 51.58  ? 461 VAL A CG2 1 
ATOM   3892  N N   . GLU A  1 462 ? -15.691 -25.306 8.438    1.00 27.16  ? 462 GLU A N   1 
ATOM   3893  C CA  . GLU A  1 462 ? -16.648 -24.789 7.469    1.00 30.68  ? 462 GLU A CA  1 
ATOM   3894  C C   . GLU A  1 462 ? -18.068 -25.190 7.834    1.00 27.18  ? 462 GLU A C   1 
ATOM   3895  O O   . GLU A  1 462 ? -19.015 -24.495 7.466    1.00 30.85  ? 462 GLU A O   1 
ATOM   3896  C CB  . GLU A  1 462 ? -16.310 -25.279 6.057    1.00 39.78  ? 462 GLU A CB  1 
ATOM   3897  C CG  . GLU A  1 462 ? -14.825 -25.383 5.742    1.00 54.42  ? 462 GLU A CG  1 
ATOM   3898  C CD  . GLU A  1 462 ? -14.251 -26.758 6.095    1.00 67.35  ? 462 GLU A CD  1 
ATOM   3899  O OE1 . GLU A  1 462 ? -15.038 -27.716 6.279    1.00 68.84  ? 462 GLU A OE1 1 
ATOM   3900  O OE2 . GLU A  1 462 ? -13.011 -26.877 6.200    1.00 73.06  ? 462 GLU A OE2 1 
ATOM   3901  N N   . VAL A  1 463 ? -18.237 -26.302 8.552    1.00 28.25  ? 463 VAL A N   1 
ATOM   3902  C CA  . VAL A  1 463 ? -19.566 -26.688 9.023    1.00 26.74  ? 463 VAL A CA  1 
ATOM   3903  C C   . VAL A  1 463 ? -20.149 -25.625 9.953    1.00 26.95  ? 463 VAL A C   1 
ATOM   3904  O O   . VAL A  1 463 ? -21.340 -25.308 9.871    1.00 21.96  ? 463 VAL A O   1 
ATOM   3905  C CB  . VAL A  1 463 ? -19.513 -28.068 9.698    1.00 30.06  ? 463 VAL A CB  1 
ATOM   3906  C CG1 . VAL A  1 463 ? -20.890 -28.443 10.249   1.00 29.87  ? 463 VAL A CG1 1 
ATOM   3907  C CG2 . VAL A  1 463 ? -19.007 -29.103 8.709    1.00 29.09  ? 463 VAL A CG2 1 
ATOM   3908  N N   . PHE A  1 464 ? -19.333 -25.071 10.867   1.00 28.94  ? 464 PHE A N   1 
ATOM   3909  C CA  . PHE A  1 464 ? -19.816 -23.989 11.728   1.00 23.56  ? 464 PHE A CA  1 
ATOM   3910  C C   . PHE A  1 464 ? -20.228 -22.779 10.905   1.00 29.26  ? 464 PHE A C   1 
ATOM   3911  O O   . PHE A  1 464 ? -21.207 -22.096 11.229   1.00 23.19  ? 464 PHE A O   1 
ATOM   3912  C CB  . PHE A  1 464 ? -18.747 -23.584 12.741   1.00 18.13  ? 464 PHE A CB  1 
ATOM   3913  C CG  . PHE A  1 464 ? -18.508 -24.639 13.806   1.00 21.69  ? 464 PHE A CG  1 
ATOM   3914  C CD1 . PHE A  1 464 ? -19.356 -24.750 14.894   1.00 25.71  ? 464 PHE A CD1 1 
ATOM   3915  C CD2 . PHE A  1 464 ? -17.472 -25.548 13.674   1.00 22.78  ? 464 PHE A CD2 1 
ATOM   3916  C CE1 . PHE A  1 464 ? -19.147 -25.737 15.868   1.00 29.82  ? 464 PHE A CE1 1 
ATOM   3917  C CE2 . PHE A  1 464 ? -17.259 -26.551 14.643   1.00 28.06  ? 464 PHE A CE2 1 
ATOM   3918  C CZ  . PHE A  1 464 ? -18.101 -26.639 15.731   1.00 25.17  ? 464 PHE A CZ  1 
ATOM   3919  N N   . ASP A  1 465 ? -19.473 -22.484 9.849    1.00 29.61  ? 465 ASP A N   1 
ATOM   3920  C CA  . ASP A  1 465 ? -19.821 -21.366 8.986    1.00 24.18  ? 465 ASP A CA  1 
ATOM   3921  C C   . ASP A  1 465 ? -21.121 -21.638 8.233    1.00 26.94  ? 465 ASP A C   1 
ATOM   3922  O O   . ASP A  1 465 ? -21.969 -20.748 8.112    1.00 25.94  ? 465 ASP A O   1 
ATOM   3923  C CB  . ASP A  1 465 ? -18.673 -21.084 8.021    1.00 25.66  ? 465 ASP A CB  1 
ATOM   3924  C CG  . ASP A  1 465 ? -19.038 -20.031 6.989    1.00 27.81  ? 465 ASP A CG  1 
ATOM   3925  O OD1 . ASP A  1 465 ? -18.999 -18.837 7.339    1.00 27.95  ? 465 ASP A OD1 1 
ATOM   3926  O OD2 . ASP A  1 465 ? -19.377 -20.406 5.838    1.00 31.31  ? 465 ASP A OD2 1 
ATOM   3927  N N   . LYS A  1 466 ? -21.308 -22.871 7.757    1.00 27.15  ? 466 LYS A N   1 
ATOM   3928  C CA  . LYS A  1 466 ? -22.553 -23.231 7.083    1.00 27.13  ? 466 LYS A CA  1 
ATOM   3929  C C   . LYS A  1 466 ? -23.737 -23.112 8.032    1.00 26.86  ? 466 LYS A C   1 
ATOM   3930  O O   . LYS A  1 466 ? -24.807 -22.626 7.648    1.00 25.49  ? 466 LYS A O   1 
ATOM   3931  C CB  . LYS A  1 466 ? -22.451 -24.651 6.517    1.00 26.43  ? 466 LYS A CB  1 
ATOM   3932  C CG  . LYS A  1 466 ? -23.772 -25.269 6.072    1.00 34.35  ? 466 LYS A CG  1 
ATOM   3933  C CD  . LYS A  1 466 ? -23.548 -26.426 5.089    1.00 34.01  ? 466 LYS A CD  1 
ATOM   3934  C CE  . LYS A  1 466 ? -24.639 -27.486 5.193    1.00 40.16  ? 466 LYS A CE  1 
ATOM   3935  N NZ  . LYS A  1 466 ? -25.759 -27.336 4.212    1.00 45.75  ? 466 LYS A NZ  1 
ATOM   3936  N N   . LEU A  1 467 ? -23.562 -23.559 9.276    1.00 21.93  ? 467 LEU A N   1 
ATOM   3937  C CA  . LEU A  1 467 ? -24.627 -23.435 10.265   1.00 25.10  ? 467 LEU A CA  1 
ATOM   3938  C C   . LEU A  1 467 ? -24.973 -21.976 10.537   1.00 26.62  ? 467 LEU A C   1 
ATOM   3939  O O   . LEU A  1 467 ? -26.143 -21.585 10.473   1.00 25.81  ? 467 LEU A O   1 
ATOM   3940  C CB  . LEU A  1 467 ? -24.218 -24.146 11.559   1.00 22.38  ? 467 LEU A CB  1 
ATOM   3941  C CG  . LEU A  1 467 ? -24.313 -25.668 11.382   1.00 21.39  ? 467 LEU A CG  1 
ATOM   3942  C CD1 . LEU A  1 467 ? -23.615 -26.435 12.512   1.00 24.46  ? 467 LEU A CD1 1 
ATOM   3943  C CD2 . LEU A  1 467 ? -25.789 -26.083 11.228   1.00 19.16  ? 467 LEU A CD2 1 
ATOM   3944  N N   . PHE A  1 468 ? -23.970 -21.157 10.864   1.00 25.16  ? 468 PHE A N   1 
ATOM   3945  C CA  . PHE A  1 468 ? -24.236 -19.751 11.163   1.00 26.71  ? 468 PHE A CA  1 
ATOM   3946  C C   . PHE A  1 468 ? -24.986 -19.078 10.015   1.00 28.65  ? 468 PHE A C   1 
ATOM   3947  O O   . PHE A  1 468 ? -26.040 -18.456 10.217   1.00 26.93  ? 468 PHE A O   1 
ATOM   3948  C CB  . PHE A  1 468 ? -22.915 -19.036 11.459   1.00 29.19  ? 468 PHE A CB  1 
ATOM   3949  C CG  . PHE A  1 468 ? -23.031 -17.537 11.577   1.00 29.69  ? 468 PHE A CG  1 
ATOM   3950  C CD1 . PHE A  1 468 ? -23.552 -16.948 12.730   1.00 28.27  ? 468 PHE A CD1 1 
ATOM   3951  C CD2 . PHE A  1 468 ? -22.586 -16.713 10.550   1.00 28.23  ? 468 PHE A CD2 1 
ATOM   3952  C CE1 . PHE A  1 468 ? -23.649 -15.558 12.850   1.00 25.87  ? 468 PHE A CE1 1 
ATOM   3953  C CE2 . PHE A  1 468 ? -22.678 -15.319 10.659   1.00 23.16  ? 468 PHE A CE2 1 
ATOM   3954  C CZ  . PHE A  1 468 ? -23.210 -14.743 11.813   1.00 30.06  ? 468 PHE A CZ  1 
ATOM   3955  N N   . ARG A  1 469 ? -24.474 -19.213 8.793    1.00 26.41  ? 469 ARG A N   1 
ATOM   3956  C CA  . ARG A  1 469 ? -25.120 -18.536 7.674    1.00 28.35  ? 469 ARG A CA  1 
ATOM   3957  C C   . ARG A  1 469 ? -26.502 -19.106 7.401    1.00 30.21  ? 469 ARG A C   1 
ATOM   3958  O O   . ARG A  1 469 ? -27.411 -18.358 7.031    1.00 32.26  ? 469 ARG A O   1 
ATOM   3959  C CB  . ARG A  1 469 ? -24.231 -18.605 6.428    1.00 27.98  ? 469 ARG A CB  1 
ATOM   3960  C CG  . ARG A  1 469 ? -22.923 -17.838 6.625    1.00 31.39  ? 469 ARG A CG  1 
ATOM   3961  C CD  . ARG A  1 469 ? -21.913 -18.118 5.508    1.00 27.39  ? 469 ARG A CD  1 
ATOM   3962  N NE  . ARG A  1 469 ? -20.703 -17.306 5.612    1.00 22.10  ? 469 ARG A NE  1 
ATOM   3963  C CZ  . ARG A  1 469 ? -20.589 -16.073 5.139    1.00 29.48  ? 469 ARG A CZ  1 
ATOM   3964  N NH1 . ARG A  1 469 ? -21.611 -15.500 4.508    1.00 29.62  ? 469 ARG A NH1 1 
ATOM   3965  N NH2 . ARG A  1 469 ? -19.439 -15.422 5.264    1.00 29.91  ? 469 ARG A NH2 1 
ATOM   3966  N N   . SER A  1 470 ? -26.691 -20.409 7.619    1.00 30.71  ? 470 SER A N   1 
ATOM   3967  C CA  . SER A  1 470 ? -28.013 -21.003 7.443    1.00 34.41  ? 470 SER A CA  1 
ATOM   3968  C C   . SER A  1 470 ? -29.006 -20.456 8.459    1.00 30.20  ? 470 SER A C   1 
ATOM   3969  O O   . SER A  1 470 ? -30.164 -20.184 8.120    1.00 27.27  ? 470 SER A O   1 
ATOM   3970  C CB  . SER A  1 470 ? -27.920 -22.524 7.563    1.00 37.22  ? 470 SER A CB  1 
ATOM   3971  O OG  . SER A  1 470 ? -27.160 -23.065 6.495    1.00 43.82  ? 470 SER A OG  1 
ATOM   3972  N N   . PHE A  1 471 ? -28.578 -20.315 9.717    1.00 29.15  ? 471 PHE A N   1 
ATOM   3973  C CA  . PHE A  1 471 ? -29.444 -19.725 10.732   1.00 22.99  ? 471 PHE A CA  1 
ATOM   3974  C C   . PHE A  1 471 ? -29.733 -18.262 10.412   1.00 24.02  ? 471 PHE A C   1 
ATOM   3975  O O   . PHE A  1 471 ? -30.870 -17.798 10.554   1.00 28.44  ? 471 PHE A O   1 
ATOM   3976  C CB  . PHE A  1 471 ? -28.785 -19.860 12.113   1.00 24.08  ? 471 PHE A CB  1 
ATOM   3977  C CG  . PHE A  1 471 ? -28.644 -21.298 12.604   1.00 26.24  ? 471 PHE A CG  1 
ATOM   3978  C CD1 . PHE A  1 471 ? -29.708 -22.173 12.547   1.00 28.73  ? 471 PHE A CD1 1 
ATOM   3979  C CD2 . PHE A  1 471 ? -27.445 -21.753 13.144   1.00 29.80  ? 471 PHE A CD2 1 
ATOM   3980  C CE1 . PHE A  1 471 ? -29.590 -23.476 13.001   1.00 27.33  ? 471 PHE A CE1 1 
ATOM   3981  C CE2 . PHE A  1 471 ? -27.313 -23.067 13.600   1.00 24.61  ? 471 PHE A CE2 1 
ATOM   3982  C CZ  . PHE A  1 471 ? -28.391 -23.923 13.529   1.00 24.33  ? 471 PHE A CZ  1 
ATOM   3983  N N   . VAL A  1 472 ? -28.708 -17.522 9.974    1.00 24.78  ? 472 VAL A N   1 
ATOM   3984  C CA  . VAL A  1 472 ? -28.887 -16.135 9.545    1.00 31.18  ? 472 VAL A CA  1 
ATOM   3985  C C   . VAL A  1 472 ? -29.907 -16.045 8.420    1.00 31.41  ? 472 VAL A C   1 
ATOM   3986  O O   . VAL A  1 472 ? -30.724 -15.114 8.373    1.00 28.75  ? 472 VAL A O   1 
ATOM   3987  C CB  . VAL A  1 472 ? -27.538 -15.534 9.109    1.00 33.36  ? 472 VAL A CB  1 
ATOM   3988  C CG1 . VAL A  1 472 ? -27.766 -14.297 8.288    1.00 36.00  ? 472 VAL A CG1 1 
ATOM   3989  C CG2 . VAL A  1 472 ? -26.655 -15.228 10.336   1.00 35.11  ? 472 VAL A CG2 1 
ATOM   3990  N N   . ARG A  1 473 ? -29.864 -16.994 7.479    1.00 29.81  ? 473 ARG A N   1 
ATOM   3991  C CA  . ARG A  1 473 ? -30.792 -16.938 6.353    1.00 31.24  ? 473 ARG A CA  1 
ATOM   3992  C C   . ARG A  1 473 ? -32.188 -17.323 6.799    1.00 31.82  ? 473 ARG A C   1 
ATOM   3993  O O   . ARG A  1 473 ? -33.170 -16.668 6.431    1.00 28.23  ? 473 ARG A O   1 
ATOM   3994  C CB  . ARG A  1 473 ? -30.327 -17.854 5.222    1.00 35.66  ? 473 ARG A CB  1 
ATOM   3995  C CG  . ARG A  1 473 ? -31.388 -18.057 4.122    1.00 41.19  ? 473 ARG A CG  1 
ATOM   3996  C CD  . ARG A  1 473 ? -30.779 -18.535 2.818    1.00 50.14  ? 473 ARG A CD  1 
ATOM   3997  N NE  . ARG A  1 473 ? -30.401 -19.946 2.856    1.00 57.82  ? 473 ARG A NE  1 
ATOM   3998  C CZ  . ARG A  1 473 ? -31.125 -20.938 2.339    1.00 63.89  ? 473 ARG A CZ  1 
ATOM   3999  N NH1 . ARG A  1 473 ? -32.286 -20.685 1.739    1.00 65.44  ? 473 ARG A NH1 1 
ATOM   4000  N NH2 . ARG A  1 473 ? -30.686 -22.189 2.423    1.00 63.35  ? 473 ARG A NH2 1 
ATOM   4001  N N   . ARG A  1 474 ? -32.288 -18.373 7.615    1.00 32.99  ? 474 ARG A N   1 
ATOM   4002  C CA  . ARG A  1 474 ? -33.578 -18.804 8.141    1.00 34.69  ? 474 ARG A CA  1 
ATOM   4003  C C   . ARG A  1 474 ? -34.254 -17.711 8.970    1.00 34.70  ? 474 ARG A C   1 
ATOM   4004  O O   . ARG A  1 474 ? -35.484 -17.570 8.933    1.00 36.66  ? 474 ARG A O   1 
ATOM   4005  C CB  . ARG A  1 474 ? -33.380 -20.070 8.964    1.00 34.76  ? 474 ARG A CB  1 
ATOM   4006  C CG  . ARG A  1 474 ? -34.638 -20.806 9.294    1.00 39.71  ? 474 ARG A CG  1 
ATOM   4007  C CD  . ARG A  1 474 ? -35.456 -21.068 8.059    1.00 49.99  ? 474 ARG A CD  1 
ATOM   4008  N NE  . ARG A  1 474 ? -36.048 -22.401 8.083    1.00 60.20  ? 474 ARG A NE  1 
ATOM   4009  C CZ  . ARG A  1 474 ? -37.049 -22.767 8.879    1.00 70.61  ? 474 ARG A CZ  1 
ATOM   4010  N NH1 . ARG A  1 474 ? -37.593 -21.895 9.723    1.00 73.63  ? 474 ARG A NH1 1 
ATOM   4011  N NH2 . ARG A  1 474 ? -37.515 -24.009 8.825    1.00 73.89  ? 474 ARG A NH2 1 
ATOM   4012  N N   . ALA A  1 475 ? -33.470 -16.913 9.697    1.00 33.44  ? 475 ALA A N   1 
ATOM   4013  C CA  . ALA A  1 475 ? -34.029 -15.869 10.548   1.00 31.42  ? 475 ALA A CA  1 
ATOM   4014  C C   . ALA A  1 475 ? -34.802 -14.805 9.769    1.00 34.79  ? 475 ALA A C   1 
ATOM   4015  O O   . ALA A  1 475 ? -35.633 -14.107 10.361   1.00 37.25  ? 475 ALA A O   1 
ATOM   4016  C CB  . ALA A  1 475 ? -32.906 -15.215 11.355   1.00 31.75  ? 475 ALA A CB  1 
ATOM   4017  N N   . GLN A  1 476 ? -34.563 -14.662 8.464    1.00 35.09  ? 476 GLN A N   1 
ATOM   4018  C CA  . GLN A  1 476 ? -35.204 -13.615 7.674    1.00 38.48  ? 476 GLN A CA  1 
ATOM   4019  C C   . GLN A  1 476 ? -36.370 -14.134 6.841    1.00 41.45  ? 476 GLN A C   1 
ATOM   4020  O O   . GLN A  1 476 ? -36.909 -13.393 6.011    1.00 41.94  ? 476 GLN A O   1 
ATOM   4021  C CB  . GLN A  1 476 ? -34.164 -12.930 6.778    1.00 36.76  ? 476 GLN A CB  1 
ATOM   4022  C CG  . GLN A  1 476 ? -32.872 -12.558 7.536    1.00 35.69  ? 476 GLN A CG  1 
ATOM   4023  C CD  . GLN A  1 476 ? -31.768 -12.008 6.637    1.00 36.07  ? 476 GLN A CD  1 
ATOM   4024  O OE1 . GLN A  1 476 ? -31.888 -10.921 6.084    1.00 41.93  ? 476 GLN A OE1 1 
ATOM   4025  N NE2 . GLN A  1 476 ? -30.676 -12.753 6.512    1.00 34.70  ? 476 GLN A NE2 1 
ATOM   4026  N N   . GLU A  1 477 ? -36.788 -15.377 7.047    1.00 44.02  ? 477 GLU A N   1 
ATOM   4027  C CA  . GLU A  1 477 ? -37.821 -15.956 6.200    1.00 51.66  ? 477 GLU A CA  1 
ATOM   4028  C C   . GLU A  1 477 ? -39.111 -16.297 6.950    1.00 54.22  ? 477 GLU A C   1 
ATOM   4029  O O   . GLU A  1 477 ? -39.143 -16.359 8.181    1.00 52.28  ? 477 GLU A O   1 
ATOM   4030  C CB  . GLU A  1 477 ? -37.270 -17.200 5.500    1.00 56.56  ? 477 GLU A CB  1 
ATOM   4031  C CG  . GLU A  1 477 ? -36.035 -16.915 4.650    1.00 60.63  ? 477 GLU A CG  1 
ATOM   4032  C CD  . GLU A  1 477 ? -35.580 -18.124 3.854    1.00 65.50  ? 477 GLU A CD  1 
ATOM   4033  O OE1 . GLU A  1 477 ? -34.895 -17.933 2.822    1.00 63.65  ? 477 GLU A OE1 1 
ATOM   4034  O OE2 . GLU A  1 477 ? -35.903 -19.262 4.265    1.00 67.80  ? 477 GLU A OE2 1 
ATOM   4035  N N   . LYS B  1 2   ? -23.683 -38.554 -58.698  1.00 48.07  ? 2   LYS B N   1 
ATOM   4036  C CA  . LYS B  1 2   ? -23.294 -39.451 -57.604  1.00 49.28  ? 2   LYS B CA  1 
ATOM   4037  C C   . LYS B  1 2   ? -22.971 -38.659 -56.334  1.00 49.34  ? 2   LYS B C   1 
ATOM   4038  O O   . LYS B  1 2   ? -22.018 -37.881 -56.290  1.00 53.50  ? 2   LYS B O   1 
ATOM   4039  C CB  . LYS B  1 2   ? -22.093 -40.309 -58.017  1.00 52.90  ? 2   LYS B CB  1 
ATOM   4040  C CG  . LYS B  1 2   ? -21.785 -41.471 -57.079  1.00 51.18  ? 2   LYS B CG  1 
ATOM   4041  C CD  . LYS B  1 2   ? -20.307 -41.521 -56.712  1.00 50.93  ? 2   LYS B CD  1 
ATOM   4042  C CE  . LYS B  1 2   ? -19.505 -42.361 -57.686  1.00 57.18  ? 2   LYS B CE  1 
ATOM   4043  N NZ  . LYS B  1 2   ? -18.068 -42.474 -57.282  1.00 55.24  ? 2   LYS B NZ  1 
ATOM   4044  N N   . LYS B  1 3   ? -23.765 -38.854 -55.293  1.00 44.46  ? 3   LYS B N   1 
ATOM   4045  C CA  . LYS B  1 3   ? -23.602 -38.082 -54.078  1.00 46.66  ? 3   LYS B CA  1 
ATOM   4046  C C   . LYS B  1 3   ? -23.061 -38.958 -52.956  1.00 47.25  ? 3   LYS B C   1 
ATOM   4047  O O   . LYS B  1 3   ? -23.181 -40.184 -52.974  1.00 49.04  ? 3   LYS B O   1 
ATOM   4048  C CB  . LYS B  1 3   ? -24.928 -37.451 -53.655  1.00 48.52  ? 3   LYS B CB  1 
ATOM   4049  C CG  . LYS B  1 3   ? -25.150 -36.038 -54.164  1.00 55.28  ? 3   LYS B CG  1 
ATOM   4050  C CD  . LYS B  1 3   ? -26.243 -36.001 -55.210  1.00 60.72  ? 3   LYS B CD  1 
ATOM   4051  C CE  . LYS B  1 3   ? -26.851 -34.613 -55.311  1.00 63.59  ? 3   LYS B CE  1 
ATOM   4052  N NZ  . LYS B  1 3   ? -25.846 -33.595 -55.713  1.00 64.09  ? 3   LYS B NZ  1 
ATOM   4053  N N   . LEU B  1 4   ? -22.414 -38.308 -52.002  1.00 41.27  ? 4   LEU B N   1 
ATOM   4054  C CA  . LEU B  1 4   ? -22.123 -38.904 -50.711  1.00 39.26  ? 4   LEU B CA  1 
ATOM   4055  C C   . LEU B  1 4   ? -23.227 -38.461 -49.768  1.00 38.22  ? 4   LEU B C   1 
ATOM   4056  O O   . LEU B  1 4   ? -23.583 -37.278 -49.741  1.00 41.39  ? 4   LEU B O   1 
ATOM   4057  C CB  . LEU B  1 4   ? -20.754 -38.471 -50.187  1.00 36.63  ? 4   LEU B CB  1 
ATOM   4058  C CG  . LEU B  1 4   ? -20.328 -38.948 -48.789  1.00 35.08  ? 4   LEU B CG  1 
ATOM   4059  C CD1 . LEU B  1 4   ? -18.823 -39.189 -48.805  1.00 38.20  ? 4   LEU B CD1 1 
ATOM   4060  C CD2 . LEU B  1 4   ? -20.690 -37.957 -47.703  1.00 34.43  ? 4   LEU B CD2 1 
ATOM   4061  N N   . PHE B  1 5   ? -23.792 -39.406 -49.030  1.00 37.58  ? 5   PHE B N   1 
ATOM   4062  C CA  . PHE B  1 5   ? -24.848 -39.108 -48.072  1.00 36.35  ? 5   PHE B CA  1 
ATOM   4063  C C   . PHE B  1 5   ? -24.228 -39.034 -46.682  1.00 34.28  ? 5   PHE B C   1 
ATOM   4064  O O   . PHE B  1 5   ? -23.701 -40.032 -46.185  1.00 36.53  ? 5   PHE B O   1 
ATOM   4065  C CB  . PHE B  1 5   ? -25.949 -40.166 -48.131  1.00 38.29  ? 5   PHE B CB  1 
ATOM   4066  C CG  . PHE B  1 5   ? -26.703 -40.193 -49.454  1.00 40.66  ? 5   PHE B CG  1 
ATOM   4067  C CD1 . PHE B  1 5   ? -27.305 -39.050 -49.949  1.00 39.67  ? 5   PHE B CD1 1 
ATOM   4068  C CD2 . PHE B  1 5   ? -26.805 -41.370 -50.187  1.00 42.34  ? 5   PHE B CD2 1 
ATOM   4069  C CE1 . PHE B  1 5   ? -28.000 -39.072 -51.148  1.00 41.94  ? 5   PHE B CE1 1 
ATOM   4070  C CE2 . PHE B  1 5   ? -27.494 -41.410 -51.386  1.00 40.80  ? 5   PHE B CE2 1 
ATOM   4071  C CZ  . PHE B  1 5   ? -28.090 -40.255 -51.874  1.00 45.20  ? 5   PHE B CZ  1 
ATOM   4072  N N   . LEU B  1 6   ? -24.278 -37.853 -46.074  1.00 30.43  ? 6   LEU B N   1 
ATOM   4073  C CA  . LEU B  1 6   ? -23.660 -37.587 -44.782  1.00 33.31  ? 6   LEU B CA  1 
ATOM   4074  C C   . LEU B  1 6   ? -24.746 -37.418 -43.732  1.00 34.47  ? 6   LEU B C   1 
ATOM   4075  O O   . LEU B  1 6   ? -25.711 -36.677 -43.948  1.00 34.91  ? 6   LEU B O   1 
ATOM   4076  C CB  . LEU B  1 6   ? -22.788 -36.331 -44.850  1.00 36.48  ? 6   LEU B CB  1 
ATOM   4077  C CG  . LEU B  1 6   ? -22.001 -35.900 -43.606  1.00 35.50  ? 6   LEU B CG  1 
ATOM   4078  C CD1 . LEU B  1 6   ? -20.983 -36.953 -43.225  1.00 35.48  ? 6   LEU B CD1 1 
ATOM   4079  C CD2 . LEU B  1 6   ? -21.314 -34.569 -43.871  1.00 34.26  ? 6   LEU B CD2 1 
ATOM   4080  N N   . VAL B  1 7   ? -24.590 -38.095 -42.597  1.00 34.50  ? 7   VAL B N   1 
ATOM   4081  C CA  . VAL B  1 7   ? -25.610 -38.114 -41.553  1.00 33.80  ? 7   VAL B CA  1 
ATOM   4082  C C   . VAL B  1 7   ? -24.928 -37.811 -40.230  1.00 32.83  ? 7   VAL B C   1 
ATOM   4083  O O   . VAL B  1 7   ? -24.182 -38.651 -39.707  1.00 33.86  ? 7   VAL B O   1 
ATOM   4084  C CB  . VAL B  1 7   ? -26.356 -39.454 -41.486  1.00 31.83  ? 7   VAL B CB  1 
ATOM   4085  C CG1 . VAL B  1 7   ? -27.472 -39.389 -40.461  1.00 32.60  ? 7   VAL B CG1 1 
ATOM   4086  C CG2 . VAL B  1 7   ? -26.915 -39.834 -42.874  1.00 34.41  ? 7   VAL B CG2 1 
ATOM   4087  N N   . PHE B  1 8   ? -25.158 -36.609 -39.706  1.00 27.03  ? 8   PHE B N   1 
ATOM   4088  C CA  . PHE B  1 8   ? -24.769 -36.266 -38.340  1.00 23.56  ? 8   PHE B CA  1 
ATOM   4089  C C   . PHE B  1 8   ? -25.872 -36.655 -37.374  1.00 23.65  ? 8   PHE B C   1 
ATOM   4090  O O   . PHE B  1 8   ? -27.032 -36.277 -37.559  1.00 26.10  ? 8   PHE B O   1 
ATOM   4091  C CB  . PHE B  1 8   ? -24.500 -34.772 -38.202  1.00 32.24  ? 8   PHE B CB  1 
ATOM   4092  C CG  . PHE B  1 8   ? -23.270 -34.317 -38.908  1.00 33.30  ? 8   PHE B CG  1 
ATOM   4093  C CD1 . PHE B  1 8   ? -22.030 -34.394 -38.288  1.00 27.51  ? 8   PHE B CD1 1 
ATOM   4094  C CD2 . PHE B  1 8   ? -23.349 -33.816 -40.196  1.00 35.27  ? 8   PHE B CD2 1 
ATOM   4095  C CE1 . PHE B  1 8   ? -20.884 -33.965 -38.947  1.00 31.94  ? 8   PHE B CE1 1 
ATOM   4096  C CE2 . PHE B  1 8   ? -22.209 -33.391 -40.864  1.00 36.15  ? 8   PHE B CE2 1 
ATOM   4097  C CZ  . PHE B  1 8   ? -20.974 -33.470 -40.241  1.00 34.34  ? 8   PHE B CZ  1 
ATOM   4098  N N   . TRP B  1 9   ? -25.496 -37.366 -36.313  1.00 24.73  ? 9   TRP B N   1 
ATOM   4099  C CA  . TRP B  1 9   ? -26.412 -37.735 -35.237  1.00 26.81  ? 9   TRP B CA  1 
ATOM   4100  C C   . TRP B  1 9   ? -25.698 -37.385 -33.927  1.00 21.93  ? 9   TRP B C   1 
ATOM   4101  O O   . TRP B  1 9   ? -24.801 -38.109 -33.489  1.00 23.30  ? 9   TRP B O   1 
ATOM   4102  C CB  . TRP B  1 9   ? -26.768 -39.215 -35.323  1.00 23.62  ? 9   TRP B CB  1 
ATOM   4103  C CG  . TRP B  1 9   ? -27.992 -39.667 -34.554  1.00 23.30  ? 9   TRP B CG  1 
ATOM   4104  C CD1 . TRP B  1 9   ? -28.729 -38.949 -33.636  1.00 25.54  ? 9   TRP B CD1 1 
ATOM   4105  C CD2 . TRP B  1 9   ? -28.600 -40.957 -34.634  1.00 26.60  ? 9   TRP B CD2 1 
ATOM   4106  N NE1 . TRP B  1 9   ? -29.765 -39.721 -33.160  1.00 25.16  ? 9   TRP B NE1 1 
ATOM   4107  C CE2 . TRP B  1 9   ? -29.702 -40.959 -33.753  1.00 25.86  ? 9   TRP B CE2 1 
ATOM   4108  C CE3 . TRP B  1 9   ? -28.322 -42.116 -35.385  1.00 29.37  ? 9   TRP B CE3 1 
ATOM   4109  C CZ2 . TRP B  1 9   ? -30.524 -42.079 -33.590  1.00 29.15  ? 9   TRP B CZ2 1 
ATOM   4110  C CZ3 . TRP B  1 9   ? -29.141 -43.227 -35.229  1.00 32.17  ? 9   TRP B CZ3 1 
ATOM   4111  C CH2 . TRP B  1 9   ? -30.226 -43.204 -34.329  1.00 34.08  ? 9   TRP B CH2 1 
ATOM   4112  N N   . TRP B  1 10  ? -26.075 -36.299 -33.349  1.00 26.15  ? 10  TRP B N   1 
ATOM   4113  C CA  . TRP B  1 10  ? -25.492 -35.780 -32.135  1.00 22.14  ? 10  TRP B CA  1 
ATOM   4114  C C   . TRP B  1 10  ? -26.245 -36.285 -30.906  1.00 22.21  ? 10  TRP B C   1 
ATOM   4115  O O   . TRP B  1 10  ? -27.391 -36.067 -30.794  1.00 25.28  ? 10  TRP B O   1 
ATOM   4116  C CB  . TRP B  1 10  ? -25.511 -34.246 -32.195  1.00 22.59  ? 10  TRP B CB  1 
ATOM   4117  C CG  . TRP B  1 10  ? -24.812 -33.563 -33.295  1.00 27.93  ? 10  TRP B CG  1 
ATOM   4118  C CD1 . TRP B  1 10  ? -25.382 -32.903 -34.329  1.00 24.48  ? 10  TRP B CD1 1 
ATOM   4119  C CD2 . TRP B  1 10  ? -23.406 -33.410 -33.450  1.00 27.54  ? 10  TRP B CD2 1 
ATOM   4120  N NE1 . TRP B  1 10  ? -24.426 -32.353 -35.123  1.00 28.25  ? 10  TRP B NE1 1 
ATOM   4121  C CE2 . TRP B  1 10  ? -23.199 -32.655 -34.611  1.00 29.46  ? 10  TRP B CE2 1 
ATOM   4122  C CE3 . TRP B  1 10  ? -22.301 -33.848 -32.729  1.00 23.46  ? 10  TRP B CE3 1 
ATOM   4123  C CZ2 . TRP B  1 10  ? -21.940 -32.334 -35.062  1.00 30.53  ? 10  TRP B CZ2 1 
ATOM   4124  C CZ3 . TRP B  1 10  ? -21.065 -33.532 -33.176  1.00 21.63  ? 10  TRP B CZ3 1 
ATOM   4125  C CH2 . TRP B  1 10  ? -20.885 -32.785 -34.336  1.00 26.16  ? 10  TRP B CH2 1 
ATOM   4126  N N   . HIS B  1 11  ? -25.561 -36.933 -30.015  1.00 22.09  ? 11  HIS B N   1 
ATOM   4127  C CA  . HIS B  1 11  ? -26.157 -37.542 -28.859  1.00 26.18  ? 11  HIS B CA  1 
ATOM   4128  C C   . HIS B  1 11  ? -26.054 -36.684 -27.634  1.00 28.87  ? 11  HIS B C   1 
ATOM   4129  O O   . HIS B  1 11  ? -25.009 -36.255 -27.286  1.00 29.89  ? 11  HIS B O   1 
ATOM   4130  C CB  . HIS B  1 11  ? -25.559 -38.927 -28.614  1.00 23.59  ? 11  HIS B CB  1 
ATOM   4131  C CG  . HIS B  1 11  ? -25.857 -39.537 -27.294  1.00 23.41  ? 11  HIS B CG  1 
ATOM   4132  N ND1 . HIS B  1 11  ? -27.125 -39.871 -26.899  1.00 21.16  ? 11  HIS B ND1 1 
ATOM   4133  C CD2 . HIS B  1 11  ? -25.033 -39.961 -26.311  1.00 23.59  ? 11  HIS B CD2 1 
ATOM   4134  C CE1 . HIS B  1 11  ? -27.078 -40.431 -25.708  1.00 20.39  ? 11  HIS B CE1 1 
ATOM   4135  N NE2 . HIS B  1 11  ? -25.819 -40.503 -25.332  1.00 23.36  ? 11  HIS B NE2 1 
ATOM   4136  N N   . MET B  1 12  ? -27.186 -36.501 -26.997  1.00 24.07  ? 12  MET B N   1 
ATOM   4137  C CA  . MET B  1 12  ? -27.263 -35.628 -25.874  1.00 22.06  ? 12  MET B CA  1 
ATOM   4138  C C   . MET B  1 12  ? -27.794 -36.330 -24.654  1.00 25.44  ? 12  MET B C   1 
ATOM   4139  O O   . MET B  1 12  ? -28.893 -36.832 -24.646  1.00 28.27  ? 12  MET B O   1 
ATOM   4140  C CB  . MET B  1 12  ? -28.087 -34.390 -26.172  1.00 25.62  ? 12  MET B CB  1 
ATOM   4141  C CG  . MET B  1 12  ? -27.844 -33.712 -27.493  1.00 26.42  ? 12  MET B CG  1 
ATOM   4142  S SD  . MET B  1 12  ? -26.249 -32.943 -27.582  1.00 32.39  ? 12  MET B SD  1 
ATOM   4143  C CE  . MET B  1 12  ? -26.566 -31.691 -28.804  1.00 40.99  ? 12  MET B CE  1 
ATOM   4144  N N   . HIS B  1 13  ? -26.997 -36.284 -23.615  1.00 21.13  ? 13  HIS B N   1 
ATOM   4145  C CA  . HIS B  1 13  ? -27.354 -36.953 -22.421  1.00 20.17  ? 13  HIS B CA  1 
ATOM   4146  C C   . HIS B  1 13  ? -26.724 -36.492 -21.140  1.00 21.82  ? 13  HIS B C   1 
ATOM   4147  O O   . HIS B  1 13  ? -25.624 -36.069 -21.166  1.00 21.72  ? 13  HIS B O   1 
ATOM   4148  C CB  . HIS B  1 13  ? -27.053 -38.495 -22.580  1.00 22.70  ? 13  HIS B CB  1 
ATOM   4149  C CG  . HIS B  1 13  ? -27.101 -39.291 -21.316  1.00 24.06  ? 13  HIS B CG  1 
ATOM   4150  N ND1 . HIS B  1 13  ? -28.254 -39.481 -20.598  1.00 22.53  ? 13  HIS B ND1 1 
ATOM   4151  C CD2 . HIS B  1 13  ? -26.143 -39.999 -20.681  1.00 21.81  ? 13  HIS B CD2 1 
ATOM   4152  C CE1 . HIS B  1 13  ? -27.993 -40.231 -19.547  1.00 21.90  ? 13  HIS B CE1 1 
ATOM   4153  N NE2 . HIS B  1 13  ? -26.721 -40.565 -19.580  1.00 21.73  ? 13  HIS B NE2 1 
ATOM   4154  N N   . GLN B  1 14  ? -27.532 -36.458 -20.075  1.00 19.57  ? 14  GLN B N   1 
ATOM   4155  C CA  . GLN B  1 14  ? -26.997 -36.307 -18.719  1.00 22.41  ? 14  GLN B CA  1 
ATOM   4156  C C   . GLN B  1 14  ? -27.695 -37.305 -17.803  1.00 23.33  ? 14  GLN B C   1 
ATOM   4157  O O   . GLN B  1 14  ? -28.918 -37.486 -17.910  1.00 25.12  ? 14  GLN B O   1 
ATOM   4158  C CB  . GLN B  1 14  ? -27.212 -34.889 -18.146  1.00 18.97  ? 14  GLN B CB  1 
ATOM   4159  C CG  . GLN B  1 14  ? -26.486 -33.734 -18.835  1.00 22.02  ? 14  GLN B CG  1 
ATOM   4160  C CD  . GLN B  1 14  ? -24.975 -33.820 -18.753  1.00 24.79  ? 14  GLN B CD  1 
ATOM   4161  O OE1 . GLN B  1 14  ? -24.421 -34.459 -17.868  1.00 25.41  ? 14  GLN B OE1 1 
ATOM   4162  N NE2 . GLN B  1 14  ? -24.295 -33.194 -19.715  1.00 31.29  ? 14  GLN B NE2 1 
ATOM   4163  N N   . PRO B  1 15  ? -26.973 -37.962 -16.890  1.00 24.53  ? 15  PRO B N   1 
ATOM   4164  C CA  . PRO B  1 15  ? -27.654 -38.730 -15.846  1.00 29.85  ? 15  PRO B CA  1 
ATOM   4165  C C   . PRO B  1 15  ? -28.372 -37.785 -14.889  1.00 26.93  ? 15  PRO B C   1 
ATOM   4166  O O   . PRO B  1 15  ? -28.195 -36.568 -14.919  1.00 26.76  ? 15  PRO B O   1 
ATOM   4167  C CB  . PRO B  1 15  ? -26.521 -39.502 -15.151  1.00 27.37  ? 15  PRO B CB  1 
ATOM   4168  C CG  . PRO B  1 15  ? -25.293 -38.688 -15.397  1.00 20.66  ? 15  PRO B CG  1 
ATOM   4169  C CD  . PRO B  1 15  ? -25.508 -38.056 -16.777  1.00 18.72  ? 15  PRO B CD  1 
ATOM   4170  N N   . LEU B  1 16  ? -29.213 -38.362 -14.037  1.00 26.32  ? 16  LEU B N   1 
ATOM   4171  C CA  . LEU B  1 16  ? -30.021 -37.573 -13.110  1.00 24.48  ? 16  LEU B CA  1 
ATOM   4172  C C   . LEU B  1 16  ? -29.170 -37.089 -11.938  1.00 28.93  ? 16  LEU B C   1 
ATOM   4173  O O   . LEU B  1 16  ? -28.812 -37.871 -11.046  1.00 29.40  ? 16  LEU B O   1 
ATOM   4174  C CB  . LEU B  1 16  ? -31.210 -38.389 -12.620  1.00 24.16  ? 16  LEU B CB  1 
ATOM   4175  C CG  . LEU B  1 16  ? -32.223 -37.609 -11.791  1.00 27.68  ? 16  LEU B CG  1 
ATOM   4176  C CD1 . LEU B  1 16  ? -32.791 -36.424 -12.606  1.00 26.47  ? 16  LEU B CD1 1 
ATOM   4177  C CD2 . LEU B  1 16  ? -33.321 -38.558 -11.294  1.00 32.56  ? 16  LEU B CD2 1 
ATOM   4178  N N   . TYR B  1 17  ? -28.871 -35.784 -11.919  1.00 29.99  ? 17  TYR B N   1 
ATOM   4179  C CA  . TYR B  1 17  ? -28.100 -35.202 -10.830  1.00 25.38  ? 17  TYR B CA  1 
ATOM   4180  C C   . TYR B  1 17  ? -28.969 -34.793 -9.647   1.00 27.14  ? 17  TYR B C   1 
ATOM   4181  O O   . TYR B  1 17  ? -28.427 -34.364 -8.628   1.00 26.11  ? 17  TYR B O   1 
ATOM   4182  C CB  . TYR B  1 17  ? -27.309 -33.989 -11.313  1.00 23.22  ? 17  TYR B CB  1 
ATOM   4183  C CG  . TYR B  1 17  ? -26.317 -34.286 -12.408  1.00 24.79  ? 17  TYR B CG  1 
ATOM   4184  C CD1 . TYR B  1 17  ? -25.239 -35.133 -12.188  1.00 25.63  ? 17  TYR B CD1 1 
ATOM   4185  C CD2 . TYR B  1 17  ? -26.461 -33.717 -13.670  1.00 27.86  ? 17  TYR B CD2 1 
ATOM   4186  C CE1 . TYR B  1 17  ? -24.327 -35.408 -13.205  1.00 26.38  ? 17  TYR B CE1 1 
ATOM   4187  C CE2 . TYR B  1 17  ? -25.564 -33.973 -14.676  1.00 27.64  ? 17  TYR B CE2 1 
ATOM   4188  C CZ  . TYR B  1 17  ? -24.501 -34.827 -14.447  1.00 25.68  ? 17  TYR B CZ  1 
ATOM   4189  O OH  . TYR B  1 17  ? -23.610 -35.089 -15.464  1.00 22.46  ? 17  TYR B OH  1 
ATOM   4190  N N   . ARG B  1 18  ? -30.289 -34.931 -9.762   1.00 27.38  ? 18  ARG B N   1 
ATOM   4191  C CA  . ARG B  1 18  ? -31.229 -34.484 -8.744   1.00 32.32  ? 18  ARG B CA  1 
ATOM   4192  C C   . ARG B  1 18  ? -31.307 -35.539 -7.651   1.00 31.59  ? 18  ARG B C   1 
ATOM   4193  O O   . ARG B  1 18  ? -31.851 -36.631 -7.869   1.00 29.27  ? 18  ARG B O   1 
ATOM   4194  C CB  . ARG B  1 18  ? -32.598 -34.240 -9.365   1.00 31.88  ? 18  ARG B CB  1 
ATOM   4195  C CG  . ARG B  1 18  ? -33.592 -33.595 -8.441   1.00 33.83  ? 18  ARG B CG  1 
ATOM   4196  C CD  . ARG B  1 18  ? -34.972 -33.652 -9.056   1.00 39.53  ? 18  ARG B CD  1 
ATOM   4197  N NE  . ARG B  1 18  ? -35.971 -32.967 -8.245   1.00 41.01  ? 18  ARG B NE  1 
ATOM   4198  C CZ  . ARG B  1 18  ? -36.641 -33.522 -7.239   1.00 46.61  ? 18  ARG B CZ  1 
ATOM   4199  N NH1 . ARG B  1 18  ? -36.430 -34.790 -6.904   1.00 46.71  ? 18  ARG B NH1 1 
ATOM   4200  N NH2 . ARG B  1 18  ? -37.535 -32.807 -6.572   1.00 43.28  ? 18  ARG B NH2 1 
ATOM   4201  N N   . GLU B  1 19  ? -30.746 -35.215 -6.490   1.00 33.38  ? 19  GLU B N   1 
ATOM   4202  C CA  . GLU B  1 19  ? -30.778 -36.122 -5.349   1.00 32.85  ? 19  GLU B CA  1 
ATOM   4203  C C   . GLU B  1 19  ? -32.214 -36.299 -4.875   1.00 36.14  ? 19  GLU B C   1 
ATOM   4204  O O   . GLU B  1 19  ? -32.894 -35.306 -4.597   1.00 39.73  ? 19  GLU B O   1 
ATOM   4205  C CB  . GLU B  1 19  ? -29.923 -35.577 -4.210   1.00 35.91  ? 19  GLU B CB  1 
ATOM   4206  C CG  . GLU B  1 19  ? -29.349 -36.661 -3.319   1.00 42.21  ? 19  GLU B CG  1 
ATOM   4207  C CD  . GLU B  1 19  ? -30.261 -37.006 -2.148   1.00 45.96  ? 19  GLU B CD  1 
ATOM   4208  O OE1 . GLU B  1 19  ? -31.222 -36.253 -1.875   1.00 44.77  ? 19  GLU B OE1 1 
ATOM   4209  O OE2 . GLU B  1 19  ? -30.013 -38.045 -1.506   1.00 49.93  ? 19  GLU B OE2 1 
ATOM   4210  N N   . PRO B  1 20  ? -32.708 -37.530 -4.755   1.00 34.52  ? 20  PRO B N   1 
ATOM   4211  C CA  . PRO B  1 20  ? -34.153 -37.705 -4.559   1.00 38.56  ? 20  PRO B CA  1 
ATOM   4212  C C   . PRO B  1 20  ? -34.647 -37.335 -3.165   1.00 41.45  ? 20  PRO B C   1 
ATOM   4213  O O   . PRO B  1 20  ? -35.852 -37.106 -3.009   1.00 46.08  ? 20  PRO B O   1 
ATOM   4214  C CB  . PRO B  1 20  ? -34.375 -39.193 -4.878   1.00 39.25  ? 20  PRO B CB  1 
ATOM   4215  C CG  . PRO B  1 20  ? -33.064 -39.845 -4.612   1.00 37.85  ? 20  PRO B CG  1 
ATOM   4216  C CD  . PRO B  1 20  ? -32.000 -38.817 -4.900   1.00 34.82  ? 20  PRO B CD  1 
ATOM   4217  N N   . TYR B  1 21  ? -33.779 -37.239 -2.153   1.00 37.10  ? 21  TYR B N   1 
ATOM   4218  C CA  . TYR B  1 21  ? -34.267 -36.903 -0.818   1.00 42.03  ? 21  TYR B CA  1 
ATOM   4219  C C   . TYR B  1 21  ? -34.237 -35.409 -0.532   1.00 45.28  ? 21  TYR B C   1 
ATOM   4220  O O   . TYR B  1 21  ? -35.052 -34.924 0.260    1.00 47.86  ? 21  TYR B O   1 
ATOM   4221  C CB  . TYR B  1 21  ? -33.458 -37.635 0.253    1.00 42.16  ? 21  TYR B CB  1 
ATOM   4222  C CG  . TYR B  1 21  ? -33.663 -39.126 0.253    1.00 43.10  ? 21  TYR B CG  1 
ATOM   4223  C CD1 . TYR B  1 21  ? -32.861 -39.951 -0.529   1.00 41.89  ? 21  TYR B CD1 1 
ATOM   4224  C CD2 . TYR B  1 21  ? -34.659 -39.715 1.026    1.00 47.00  ? 21  TYR B CD2 1 
ATOM   4225  C CE1 . TYR B  1 21  ? -33.033 -41.314 -0.538   1.00 42.70  ? 21  TYR B CE1 1 
ATOM   4226  C CE2 . TYR B  1 21  ? -34.839 -41.091 1.027    1.00 49.48  ? 21  TYR B CE2 1 
ATOM   4227  C CZ  . TYR B  1 21  ? -34.020 -41.884 0.233    1.00 47.31  ? 21  TYR B CZ  1 
ATOM   4228  O OH  . TYR B  1 21  ? -34.169 -43.251 0.205    1.00 48.10  ? 21  TYR B OH  1 
ATOM   4229  N N   . THR B  1 22  ? -33.323 -34.667 -1.151   1.00 42.95  ? 22  THR B N   1 
ATOM   4230  C CA  . THR B  1 22  ? -33.286 -33.222 -0.997   1.00 41.24  ? 22  THR B CA  1 
ATOM   4231  C C   . THR B  1 22  ? -33.834 -32.469 -2.204   1.00 40.84  ? 22  THR B C   1 
ATOM   4232  O O   . THR B  1 22  ? -34.189 -31.294 -2.067   1.00 41.28  ? 22  THR B O   1 
ATOM   4233  C CB  . THR B  1 22  ? -31.852 -32.744 -0.754   1.00 40.50  ? 22  THR B CB  1 
ATOM   4234  O OG1 . THR B  1 22  ? -31.051 -33.090 -1.889   1.00 38.68  ? 22  THR B OG1 1 
ATOM   4235  C CG2 . THR B  1 22  ? -31.255 -33.364 0.518    1.00 35.22  ? 22  THR B CG2 1 
ATOM   4236  N N   . GLY B  1 23  ? -33.893 -33.102 -3.373   1.00 41.50  ? 23  GLY B N   1 
ATOM   4237  C CA  . GLY B  1 23  ? -34.280 -32.412 -4.592   1.00 40.72  ? 23  GLY B CA  1 
ATOM   4238  C C   . GLY B  1 23  ? -33.224 -31.504 -5.170   1.00 41.26  ? 23  GLY B C   1 
ATOM   4239  O O   . GLY B  1 23  ? -33.488 -30.808 -6.157   1.00 44.39  ? 23  GLY B O   1 
ATOM   4240  N N   . GLU B  1 24  ? -32.030 -31.487 -4.597   1.00 36.29  ? 24  GLU B N   1 
ATOM   4241  C CA  . GLU B  1 24  ? -30.969 -30.613 -5.069   1.00 33.23  ? 24  GLU B CA  1 
ATOM   4242  C C   . GLU B  1 24  ? -30.186 -31.260 -6.206   1.00 29.77  ? 24  GLU B C   1 
ATOM   4243  O O   . GLU B  1 24  ? -29.894 -32.462 -6.179   1.00 26.79  ? 24  GLU B O   1 
ATOM   4244  C CB  . GLU B  1 24  ? -30.040 -30.245 -3.910   1.00 33.46  ? 24  GLU B CB  1 
ATOM   4245  C CG  . GLU B  1 24  ? -30.777 -29.724 -2.682   1.00 45.01  ? 24  GLU B CG  1 
ATOM   4246  C CD  . GLU B  1 24  ? -29.884 -29.682 -1.464   1.00 58.22  ? 24  GLU B CD  1 
ATOM   4247  O OE1 . GLU B  1 24  ? -28.664 -29.863 -1.648   1.00 62.53  ? 24  GLU B OE1 1 
ATOM   4248  O OE2 . GLU B  1 24  ? -30.386 -29.490 -0.330   1.00 68.37  ? 24  GLU B OE2 1 
ATOM   4249  N N   . TYR B  1 25  ? -29.868 -30.462 -7.222   1.00 28.97  ? 25  TYR B N   1 
ATOM   4250  C CA  . TYR B  1 25  ? -28.987 -30.932 -8.281   1.00 27.46  ? 25  TYR B CA  1 
ATOM   4251  C C   . TYR B  1 25  ? -27.563 -30.834 -7.763   1.00 25.14  ? 25  TYR B C   1 
ATOM   4252  O O   . TYR B  1 25  ? -27.049 -29.730 -7.559   1.00 25.60  ? 25  TYR B O   1 
ATOM   4253  C CB  . TYR B  1 25  ? -29.173 -30.117 -9.554   1.00 25.98  ? 25  TYR B CB  1 
ATOM   4254  C CG  . TYR B  1 25  ? -30.368 -30.548 -10.355  1.00 27.18  ? 25  TYR B CG  1 
ATOM   4255  C CD1 . TYR B  1 25  ? -31.660 -30.389 -9.858   1.00 24.45  ? 25  TYR B CD1 1 
ATOM   4256  C CD2 . TYR B  1 25  ? -30.206 -31.126 -11.612  1.00 28.14  ? 25  TYR B CD2 1 
ATOM   4257  C CE1 . TYR B  1 25  ? -32.761 -30.790 -10.602  1.00 30.05  ? 25  TYR B CE1 1 
ATOM   4258  C CE2 . TYR B  1 25  ? -31.290 -31.519 -12.362  1.00 30.49  ? 25  TYR B CE2 1 
ATOM   4259  C CZ  . TYR B  1 25  ? -32.562 -31.353 -11.860  1.00 31.68  ? 25  TYR B CZ  1 
ATOM   4260  O OH  . TYR B  1 25  ? -33.626 -31.767 -12.633  1.00 30.11  ? 25  TYR B OH  1 
ATOM   4261  N N   . LEU B  1 26  ? -26.932 -31.990 -7.539   1.00 22.58  ? 26  LEU B N   1 
ATOM   4262  C CA  . LEU B  1 26  ? -25.646 -32.038 -6.854   1.00 25.14  ? 26  LEU B CA  1 
ATOM   4263  C C   . LEU B  1 26  ? -24.487 -31.593 -7.741   1.00 27.79  ? 26  LEU B C   1 
ATOM   4264  O O   . LEU B  1 26  ? -23.460 -31.150 -7.209   1.00 30.14  ? 26  LEU B O   1 
ATOM   4265  C CB  . LEU B  1 26  ? -25.396 -33.456 -6.320   1.00 27.38  ? 26  LEU B CB  1 
ATOM   4266  C CG  . LEU B  1 26  ? -26.422 -33.957 -5.291   1.00 31.84  ? 26  LEU B CG  1 
ATOM   4267  C CD1 . LEU B  1 26  ? -25.914 -35.176 -4.567   1.00 31.01  ? 26  LEU B CD1 1 
ATOM   4268  C CD2 . LEU B  1 26  ? -26.761 -32.848 -4.306   1.00 33.52  ? 26  LEU B CD2 1 
ATOM   4269  N N   . LEU B  1 27  ? -24.629 -31.702 -9.062   1.00 30.40  ? 27  LEU B N   1 
ATOM   4270  C CA  . LEU B  1 27  ? -23.681 -31.189 -10.042  1.00 29.76  ? 27  LEU B CA  1 
ATOM   4271  C C   . LEU B  1 27  ? -24.400 -30.277 -11.031  1.00 30.18  ? 27  LEU B C   1 
ATOM   4272  O O   . LEU B  1 27  ? -25.608 -30.422 -11.255  1.00 27.91  ? 27  LEU B O   1 
ATOM   4273  C CB  . LEU B  1 27  ? -22.975 -32.336 -10.780  1.00 32.57  ? 27  LEU B CB  1 
ATOM   4274  C CG  . LEU B  1 27  ? -21.996 -33.133 -9.896   1.00 34.21  ? 27  LEU B CG  1 
ATOM   4275  C CD1 . LEU B  1 27  ? -21.476 -34.412 -10.572  1.00 30.99  ? 27  LEU B CD1 1 
ATOM   4276  C CD2 . LEU B  1 27  ? -20.839 -32.271 -9.426   1.00 32.52  ? 27  LEU B CD2 1 
ATOM   4277  N N   . PRO B  1 28  ? -23.695 -29.287 -11.602  1.00 28.51  ? 28  PRO B N   1 
ATOM   4278  C CA  . PRO B  1 28  ? -24.370 -28.311 -12.479  1.00 28.63  ? 28  PRO B CA  1 
ATOM   4279  C C   . PRO B  1 28  ? -24.252 -28.629 -13.966  1.00 27.62  ? 28  PRO B C   1 
ATOM   4280  O O   . PRO B  1 28  ? -24.495 -27.762 -14.808  1.00 28.75  ? 28  PRO B O   1 
ATOM   4281  C CB  . PRO B  1 28  ? -23.642 -27.004 -12.156  1.00 26.73  ? 28  PRO B CB  1 
ATOM   4282  C CG  . PRO B  1 28  ? -22.221 -27.459 -11.895  1.00 29.52  ? 28  PRO B CG  1 
ATOM   4283  C CD  . PRO B  1 28  ? -22.328 -28.856 -11.255  1.00 30.82  ? 28  PRO B CD  1 
ATOM   4284  N N   . TRP B  1 29  ? -23.867 -29.854 -14.303  1.00 21.11  ? 29  TRP B N   1 
ATOM   4285  C CA  . TRP B  1 29  ? -23.496 -30.141 -15.689  1.00 24.68  ? 29  TRP B CA  1 
ATOM   4286  C C   . TRP B  1 29  ? -24.685 -30.101 -16.637  1.00 25.39  ? 29  TRP B C   1 
ATOM   4287  O O   . TRP B  1 29  ? -24.512 -29.795 -17.814  1.00 23.45  ? 29  TRP B O   1 
ATOM   4288  C CB  . TRP B  1 29  ? -22.837 -31.513 -15.782  1.00 21.10  ? 29  TRP B CB  1 
ATOM   4289  C CG  . TRP B  1 29  ? -21.556 -31.658 -15.025  1.00 19.08  ? 29  TRP B CG  1 
ATOM   4290  C CD1 . TRP B  1 29  ? -21.244 -32.645 -14.160  1.00 21.59  ? 29  TRP B CD1 1 
ATOM   4291  C CD2 . TRP B  1 29  ? -20.384 -30.834 -15.137  1.00 24.92  ? 29  TRP B CD2 1 
ATOM   4292  N NE1 . TRP B  1 29  ? -19.962 -32.492 -13.702  1.00 25.11  ? 29  TRP B NE1 1 
ATOM   4293  C CE2 . TRP B  1 29  ? -19.410 -31.385 -14.286  1.00 26.36  ? 29  TRP B CE2 1 
ATOM   4294  C CE3 . TRP B  1 29  ? -20.065 -29.695 -15.879  1.00 28.45  ? 29  TRP B CE3 1 
ATOM   4295  C CZ2 . TRP B  1 29  ? -18.142 -30.835 -14.146  1.00 30.69  ? 29  TRP B CZ2 1 
ATOM   4296  C CZ3 . TRP B  1 29  ? -18.810 -29.142 -15.732  1.00 30.29  ? 29  TRP B CZ3 1 
ATOM   4297  C CH2 . TRP B  1 29  ? -17.860 -29.716 -14.875  1.00 30.55  ? 29  TRP B CH2 1 
ATOM   4298  N N   . THR B  1 30  ? -25.883 -30.469 -16.179  1.00 24.58  ? 30  THR B N   1 
ATOM   4299  C CA  . THR B  1 30  ? -27.047 -30.289 -17.039  1.00 24.82  ? 30  THR B CA  1 
ATOM   4300  C C   . THR B  1 30  ? -27.266 -28.815 -17.360  1.00 26.70  ? 30  THR B C   1 
ATOM   4301  O O   . THR B  1 30  ? -27.538 -28.451 -18.515  1.00 31.37  ? 30  THR B O   1 
ATOM   4302  C CB  . THR B  1 30  ? -28.276 -30.883 -16.370  1.00 23.51  ? 30  THR B CB  1 
ATOM   4303  O OG1 . THR B  1 30  ? -28.060 -32.284 -16.229  1.00 23.70  ? 30  THR B OG1 1 
ATOM   4304  C CG2 . THR B  1 30  ? -29.533 -30.644 -17.233  1.00 26.42  ? 30  THR B CG2 1 
ATOM   4305  N N   . PHE B  1 31  ? -27.113 -27.950 -16.358  1.00 21.12  ? 31  PHE B N   1 
ATOM   4306  C CA  . PHE B  1 31  ? -27.296 -26.519 -16.578  1.00 25.31  ? 31  PHE B CA  1 
ATOM   4307  C C   . PHE B  1 31  ? -26.243 -25.968 -17.528  1.00 27.53  ? 31  PHE B C   1 
ATOM   4308  O O   . PHE B  1 31  ? -26.564 -25.193 -18.434  1.00 28.70  ? 31  PHE B O   1 
ATOM   4309  C CB  . PHE B  1 31  ? -27.236 -25.751 -15.262  1.00 26.08  ? 31  PHE B CB  1 
ATOM   4310  C CG  . PHE B  1 31  ? -27.309 -24.260 -15.429  1.00 21.82  ? 31  PHE B CG  1 
ATOM   4311  C CD1 . PHE B  1 31  ? -28.530 -23.629 -15.558  1.00 19.46  ? 31  PHE B CD1 1 
ATOM   4312  C CD2 . PHE B  1 31  ? -26.161 -23.491 -15.450  1.00 22.17  ? 31  PHE B CD2 1 
ATOM   4313  C CE1 . PHE B  1 31  ? -28.610 -22.258 -15.712  1.00 20.99  ? 31  PHE B CE1 1 
ATOM   4314  C CE2 . PHE B  1 31  ? -26.240 -22.112 -15.606  1.00 19.95  ? 31  PHE B CE2 1 
ATOM   4315  C CZ  . PHE B  1 31  ? -27.460 -21.503 -15.729  1.00 22.09  ? 31  PHE B CZ  1 
ATOM   4316  N N   . PHE B  1 32  ? -24.970 -26.302 -17.299  1.00 21.92  ? 32  PHE B N   1 
ATOM   4317  C CA  . PHE B  1 32  ? -23.935 -25.674 -18.113  1.00 24.65  ? 32  PHE B CA  1 
ATOM   4318  C C   . PHE B  1 32  ? -23.989 -26.187 -19.550  1.00 26.54  ? 32  PHE B C   1 
ATOM   4319  O O   . PHE B  1 32  ? -23.773 -25.417 -20.492  1.00 23.88  ? 32  PHE B O   1 
ATOM   4320  C CB  . PHE B  1 32  ? -22.553 -25.889 -17.498  1.00 18.10  ? 32  PHE B CB  1 
ATOM   4321  C CG  . PHE B  1 32  ? -22.249 -24.959 -16.343  1.00 27.25  ? 32  PHE B CG  1 
ATOM   4322  C CD1 . PHE B  1 32  ? -22.400 -23.587 -16.460  1.00 23.43  ? 32  PHE B CD1 1 
ATOM   4323  C CD2 . PHE B  1 32  ? -21.863 -25.473 -15.115  1.00 32.48  ? 32  PHE B CD2 1 
ATOM   4324  C CE1 . PHE B  1 32  ? -22.142 -22.756 -15.387  1.00 28.37  ? 32  PHE B CE1 1 
ATOM   4325  C CE2 . PHE B  1 32  ? -21.598 -24.642 -14.042  1.00 30.70  ? 32  PHE B CE2 1 
ATOM   4326  C CZ  . PHE B  1 32  ? -21.735 -23.289 -14.178  1.00 26.32  ? 32  PHE B CZ  1 
ATOM   4327  N N   . HIS B  1 33  ? -24.290 -27.477 -19.750  1.00 26.97  ? 33  HIS B N   1 
ATOM   4328  C CA  . HIS B  1 33  ? -24.398 -27.963 -21.126  1.00 27.43  ? 33  HIS B CA  1 
ATOM   4329  C C   . HIS B  1 33  ? -25.703 -27.541 -21.794  1.00 28.18  ? 33  HIS B C   1 
ATOM   4330  O O   . HIS B  1 33  ? -25.750 -27.442 -23.034  1.00 27.72  ? 33  HIS B O   1 
ATOM   4331  C CB  . HIS B  1 33  ? -24.230 -29.486 -21.161  1.00 24.85  ? 33  HIS B CB  1 
ATOM   4332  C CG  . HIS B  1 33  ? -22.807 -29.923 -21.055  1.00 30.80  ? 33  HIS B CG  1 
ATOM   4333  N ND1 . HIS B  1 33  ? -21.823 -29.453 -21.903  1.00 31.23  ? 33  HIS B ND1 1 
ATOM   4334  C CD2 . HIS B  1 33  ? -22.191 -30.767 -20.193  1.00 29.96  ? 33  HIS B CD2 1 
ATOM   4335  C CE1 . HIS B  1 33  ? -20.665 -29.995 -21.568  1.00 32.60  ? 33  HIS B CE1 1 
ATOM   4336  N NE2 . HIS B  1 33  ? -20.861 -30.796 -20.533  1.00 31.20  ? 33  HIS B NE2 1 
ATOM   4337  N N   . ALA B  1 34  ? -26.747 -27.249 -21.010  1.00 23.79  ? 34  ALA B N   1 
ATOM   4338  C CA  . ALA B  1 34  ? -27.973 -26.700 -21.586  1.00 23.95  ? 34  ALA B CA  1 
ATOM   4339  C C   . ALA B  1 34  ? -27.762 -25.271 -22.088  1.00 29.99  ? 34  ALA B C   1 
ATOM   4340  O O   . ALA B  1 34  ? -28.205 -24.921 -23.186  1.00 29.86  ? 34  ALA B O   1 
ATOM   4341  C CB  . ALA B  1 34  ? -29.115 -26.765 -20.563  1.00 22.54  ? 34  ALA B CB  1 
ATOM   4342  N N   . VAL B  1 35  ? -27.056 -24.438 -21.320  1.00 30.74  ? 35  VAL B N   1 
ATOM   4343  C CA  . VAL B  1 35  ? -26.789 -23.084 -21.793  1.00 26.69  ? 35  VAL B CA  1 
ATOM   4344  C C   . VAL B  1 35  ? -25.658 -23.037 -22.815  1.00 27.79  ? 35  VAL B C   1 
ATOM   4345  O O   . VAL B  1 35  ? -25.553 -22.054 -23.560  1.00 31.69  ? 35  VAL B O   1 
ATOM   4346  C CB  . VAL B  1 35  ? -26.462 -22.141 -20.624  1.00 28.76  ? 35  VAL B CB  1 
ATOM   4347  C CG1 . VAL B  1 35  ? -27.563 -22.194 -19.581  1.00 29.11  ? 35  VAL B CG1 1 
ATOM   4348  C CG2 . VAL B  1 35  ? -25.128 -22.513 -20.012  1.00 30.12  ? 35  VAL B CG2 1 
ATOM   4349  N N   . LYS B  1 36  ? -24.809 -24.061 -22.891  1.00 27.81  ? 36  LYS B N   1 
ATOM   4350  C CA  . LYS B  1 36  ? -23.725 -24.030 -23.871  1.00 31.28  ? 36  LYS B CA  1 
ATOM   4351  C C   . LYS B  1 36  ? -24.041 -24.804 -25.144  1.00 31.38  ? 36  LYS B C   1 
ATOM   4352  O O   . LYS B  1 36  ? -23.671 -24.361 -26.242  1.00 32.81  ? 36  LYS B O   1 
ATOM   4353  C CB  . LYS B  1 36  ? -22.426 -24.580 -23.269  1.00 24.05  ? 36  LYS B CB  1 
ATOM   4354  C CG  . LYS B  1 36  ? -21.174 -24.186 -24.046  1.00 25.55  ? 36  LYS B CG  1 
ATOM   4355  C CD  . LYS B  1 36  ? -19.893 -24.621 -23.324  1.00 29.50  ? 36  LYS B CD  1 
ATOM   4356  C CE  . LYS B  1 36  ? -19.718 -26.132 -23.351  1.00 29.09  ? 36  LYS B CE  1 
ATOM   4357  N NZ  . LYS B  1 36  ? -19.456 -26.629 -24.728  1.00 27.82  ? 36  LYS B NZ  1 
ATOM   4358  N N   . ASP B  1 37  ? -24.701 -25.959 -25.031  1.00 29.95  ? 37  ASP B N   1 
ATOM   4359  C CA  . ASP B  1 37  ? -24.752 -26.865 -26.175  1.00 25.71  ? 37  ASP B CA  1 
ATOM   4360  C C   . ASP B  1 37  ? -26.163 -27.283 -26.576  1.00 26.41  ? 37  ASP B C   1 
ATOM   4361  O O   . ASP B  1 37  ? -26.454 -27.346 -27.775  1.00 26.11  ? 37  ASP B O   1 
ATOM   4362  C CB  . ASP B  1 37  ? -23.876 -28.131 -25.896  1.00 24.85  ? 37  ASP B CB  1 
ATOM   4363  C CG  . ASP B  1 37  ? -22.481 -27.771 -25.406  1.00 29.73  ? 37  ASP B CG  1 
ATOM   4364  O OD1 . ASP B  1 37  ? -21.689 -27.180 -26.178  1.00 26.89  ? 37  ASP B OD1 1 
ATOM   4365  O OD2 . ASP B  1 37  ? -22.187 -28.029 -24.216  1.00 28.90  ? 37  ASP B OD2 1 
ATOM   4366  N N   . TYR B  1 38  ? -27.055 -27.547 -25.618  1.00 22.15  ? 38  TYR B N   1 
ATOM   4367  C CA  . TYR B  1 38  ? -28.303 -28.241 -25.959  1.00 22.28  ? 38  TYR B CA  1 
ATOM   4368  C C   . TYR B  1 38  ? -29.245 -27.395 -26.800  1.00 26.63  ? 38  TYR B C   1 
ATOM   4369  O O   . TYR B  1 38  ? -30.013 -27.942 -27.599  1.00 27.34  ? 38  TYR B O   1 
ATOM   4370  C CB  . TYR B  1 38  ? -29.002 -28.704 -24.685  1.00 27.63  ? 38  TYR B CB  1 
ATOM   4371  C CG  . TYR B  1 38  ? -28.224 -29.812 -24.001  1.00 31.71  ? 38  TYR B CG  1 
ATOM   4372  C CD1 . TYR B  1 38  ? -27.543 -30.766 -24.761  1.00 29.71  ? 38  TYR B CD1 1 
ATOM   4373  C CD2 . TYR B  1 38  ? -28.149 -29.893 -22.608  1.00 28.38  ? 38  TYR B CD2 1 
ATOM   4374  C CE1 . TYR B  1 38  ? -26.805 -31.786 -24.152  1.00 30.13  ? 38  TYR B CE1 1 
ATOM   4375  C CE2 . TYR B  1 38  ? -27.418 -30.895 -21.986  1.00 29.06  ? 38  TYR B CE2 1 
ATOM   4376  C CZ  . TYR B  1 38  ? -26.759 -31.840 -22.748  1.00 29.35  ? 38  TYR B CZ  1 
ATOM   4377  O OH  . TYR B  1 38  ? -26.034 -32.834 -22.141  1.00 31.44  ? 38  TYR B OH  1 
ATOM   4378  N N   . TYR B  1 39  ? -29.245 -26.074 -26.609  1.00 27.03  ? 39  TYR B N   1 
ATOM   4379  C CA  . TYR B  1 39  ? -29.956 -25.208 -27.532  1.00 25.64  ? 39  TYR B CA  1 
ATOM   4380  C C   . TYR B  1 39  ? -29.077 -24.844 -28.717  1.00 24.23  ? 39  TYR B C   1 
ATOM   4381  O O   . TYR B  1 39  ? -29.546 -24.800 -29.859  1.00 24.59  ? 39  TYR B O   1 
ATOM   4382  C CB  . TYR B  1 39  ? -30.426 -23.935 -26.811  1.00 27.03  ? 39  TYR B CB  1 
ATOM   4383  C CG  . TYR B  1 39  ? -30.983 -22.872 -27.752  1.00 28.28  ? 39  TYR B CG  1 
ATOM   4384  C CD1 . TYR B  1 39  ? -32.323 -22.886 -28.122  1.00 27.59  ? 39  TYR B CD1 1 
ATOM   4385  C CD2 . TYR B  1 39  ? -30.168 -21.866 -28.270  1.00 26.73  ? 39  TYR B CD2 1 
ATOM   4386  C CE1 . TYR B  1 39  ? -32.843 -21.939 -28.972  1.00 30.98  ? 39  TYR B CE1 1 
ATOM   4387  C CE2 . TYR B  1 39  ? -30.681 -20.909 -29.138  1.00 29.23  ? 39  TYR B CE2 1 
ATOM   4388  C CZ  . TYR B  1 39  ? -32.019 -20.953 -29.482  1.00 31.22  ? 39  TYR B CZ  1 
ATOM   4389  O OH  . TYR B  1 39  ? -32.542 -20.008 -30.328  1.00 32.63  ? 39  TYR B OH  1 
ATOM   4390  N N   . ASP B  1 40  ? -27.796 -24.591 -28.463  1.00 22.36  ? 40  ASP B N   1 
ATOM   4391  C CA  . ASP B  1 40  ? -26.960 -24.020 -29.507  1.00 25.69  ? 40  ASP B CA  1 
ATOM   4392  C C   . ASP B  1 40  ? -26.618 -25.019 -30.606  1.00 29.19  ? 40  ASP B C   1 
ATOM   4393  O O   . ASP B  1 40  ? -26.387 -24.600 -31.744  1.00 29.96  ? 40  ASP B O   1 
ATOM   4394  C CB  . ASP B  1 40  ? -25.697 -23.418 -28.892  1.00 27.08  ? 40  ASP B CB  1 
ATOM   4395  C CG  . ASP B  1 40  ? -25.902 -21.959 -28.490  1.00 33.60  ? 40  ASP B CG  1 
ATOM   4396  O OD1 . ASP B  1 40  ? -25.971 -21.108 -29.401  1.00 30.72  ? 40  ASP B OD1 1 
ATOM   4397  O OD2 . ASP B  1 40  ? -26.034 -21.666 -27.268  1.00 30.86  ? 40  ASP B OD2 1 
ATOM   4398  N N   . MET B  1 41  ? -26.562 -26.336 -30.308  1.00 27.91  ? 41  MET B N   1 
ATOM   4399  C CA  . MET B  1 41  ? -26.235 -27.284 -31.373  1.00 26.30  ? 41  MET B CA  1 
ATOM   4400  C C   . MET B  1 41  ? -27.325 -27.325 -32.442  1.00 29.08  ? 41  MET B C   1 
ATOM   4401  O O   . MET B  1 41  ? -27.008 -27.094 -33.628  1.00 29.41  ? 41  MET B O   1 
ATOM   4402  C CB  . MET B  1 41  ? -25.913 -28.662 -30.770  1.00 21.89  ? 41  MET B CB  1 
ATOM   4403  C CG  . MET B  1 41  ? -24.501 -28.735 -30.145  1.00 21.85  ? 41  MET B CG  1 
ATOM   4404  S SD  . MET B  1 41  ? -23.182 -28.600 -31.395  1.00 26.77  ? 41  MET B SD  1 
ATOM   4405  C CE  . MET B  1 41  ? -23.097 -30.296 -31.998  1.00 22.71  ? 41  MET B CE  1 
ATOM   4406  N N   . PRO B  1 42  ? -28.606 -27.556 -32.121  1.00 26.31  ? 42  PRO B N   1 
ATOM   4407  C CA  . PRO B  1 42  ? -29.642 -27.418 -33.162  1.00 28.06  ? 42  PRO B CA  1 
ATOM   4408  C C   . PRO B  1 42  ? -29.849 -25.987 -33.651  1.00 27.85  ? 42  PRO B C   1 
ATOM   4409  O O   . PRO B  1 42  ? -30.360 -25.811 -34.763  1.00 30.46  ? 42  PRO B O   1 
ATOM   4410  C CB  . PRO B  1 42  ? -30.910 -27.954 -32.478  1.00 25.28  ? 42  PRO B CB  1 
ATOM   4411  C CG  . PRO B  1 42  ? -30.650 -27.772 -31.018  1.00 22.64  ? 42  PRO B CG  1 
ATOM   4412  C CD  . PRO B  1 42  ? -29.187 -28.009 -30.838  1.00 23.10  ? 42  PRO B CD  1 
ATOM   4413  N N   . ALA B  1 43  ? -29.495 -24.964 -32.863  1.00 26.77  ? 43  ALA B N   1 
ATOM   4414  C CA  . ALA B  1 43  ? -29.627 -23.598 -33.353  1.00 25.07  ? 43  ALA B CA  1 
ATOM   4415  C C   . ALA B  1 43  ? -28.740 -23.327 -34.563  1.00 30.24  ? 43  ALA B C   1 
ATOM   4416  O O   . ALA B  1 43  ? -29.023 -22.394 -35.318  1.00 28.60  ? 43  ALA B O   1 
ATOM   4417  C CB  . ALA B  1 43  ? -29.327 -22.576 -32.253  1.00 25.22  ? 43  ALA B CB  1 
ATOM   4418  N N   . TYR B  1 44  ? -27.694 -24.127 -34.786  1.00 30.77  ? 44  TYR B N   1 
ATOM   4419  C CA  . TYR B  1 44  ? -26.908 -23.933 -36.007  1.00 32.34  ? 44  TYR B CA  1 
ATOM   4420  C C   . TYR B  1 44  ? -27.782 -24.044 -37.245  1.00 32.17  ? 44  TYR B C   1 
ATOM   4421  O O   . TYR B  1 44  ? -27.522 -23.373 -38.247  1.00 31.59  ? 44  TYR B O   1 
ATOM   4422  C CB  . TYR B  1 44  ? -25.782 -24.959 -36.106  1.00 28.80  ? 44  TYR B CB  1 
ATOM   4423  C CG  . TYR B  1 44  ? -24.520 -24.622 -35.347  1.00 29.92  ? 44  TYR B CG  1 
ATOM   4424  C CD1 . TYR B  1 44  ? -23.491 -23.919 -35.953  1.00 28.86  ? 44  TYR B CD1 1 
ATOM   4425  C CD2 . TYR B  1 44  ? -24.349 -25.039 -34.031  1.00 25.71  ? 44  TYR B CD2 1 
ATOM   4426  C CE1 . TYR B  1 44  ? -22.325 -23.637 -35.271  1.00 30.94  ? 44  TYR B CE1 1 
ATOM   4427  C CE2 . TYR B  1 44  ? -23.191 -24.764 -33.336  1.00 24.78  ? 44  TYR B CE2 1 
ATOM   4428  C CZ  . TYR B  1 44  ? -22.181 -24.066 -33.961  1.00 30.97  ? 44  TYR B CZ  1 
ATOM   4429  O OH  . TYR B  1 44  ? -21.025 -23.778 -33.269  1.00 31.39  ? 44  TYR B OH  1 
ATOM   4430  N N   . LEU B  1 45  ? -28.808 -24.902 -37.195  1.00 32.24  ? 45  LEU B N   1 
ATOM   4431  C CA  . LEU B  1 45  ? -29.727 -25.060 -38.313  1.00 35.89  ? 45  LEU B CA  1 
ATOM   4432  C C   . LEU B  1 45  ? -30.417 -23.756 -38.687  1.00 35.94  ? 45  LEU B C   1 
ATOM   4433  O O   . LEU B  1 45  ? -30.926 -23.635 -39.809  1.00 34.94  ? 45  LEU B O   1 
ATOM   4434  C CB  . LEU B  1 45  ? -30.763 -26.134 -37.985  1.00 31.83  ? 45  LEU B CB  1 
ATOM   4435  C CG  . LEU B  1 45  ? -30.151 -27.535 -37.857  1.00 30.30  ? 45  LEU B CG  1 
ATOM   4436  C CD1 . LEU B  1 45  ? -31.191 -28.560 -37.431  1.00 27.39  ? 45  LEU B CD1 1 
ATOM   4437  C CD2 . LEU B  1 45  ? -29.432 -27.969 -39.148  1.00 28.41  ? 45  LEU B CD2 1 
ATOM   4438  N N   . LYS B  1 46  ? -30.443 -22.778 -37.786  1.00 33.02  ? 46  LYS B N   1 
ATOM   4439  C CA  . LYS B  1 46  ? -31.046 -21.497 -38.132  1.00 34.93  ? 46  LYS B CA  1 
ATOM   4440  C C   . LYS B  1 46  ? -30.227 -20.773 -39.192  1.00 39.17  ? 46  LYS B C   1 
ATOM   4441  O O   . LYS B  1 46  ? -30.785 -20.021 -39.997  1.00 39.17  ? 46  LYS B O   1 
ATOM   4442  C CB  . LYS B  1 46  ? -31.182 -20.627 -36.890  1.00 34.51  ? 46  LYS B CB  1 
ATOM   4443  C CG  . LYS B  1 46  ? -32.263 -21.079 -35.906  1.00 41.05  ? 46  LYS B CG  1 
ATOM   4444  C CD  . LYS B  1 46  ? -32.258 -20.187 -34.660  1.00 46.43  ? 46  LYS B CD  1 
ATOM   4445  C CE  . LYS B  1 46  ? -33.633 -20.107 -34.005  1.00 53.64  ? 46  LYS B CE  1 
ATOM   4446  N NZ  . LYS B  1 46  ? -34.576 -19.182 -34.713  1.00 60.26  ? 46  LYS B NZ  1 
ATOM   4447  N N   . ASP B  1 47  ? -28.912 -21.004 -39.219  1.00 36.75  ? 47  ASP B N   1 
ATOM   4448  C CA  . ASP B  1 47  ? -28.010 -20.253 -40.078  1.00 40.38  ? 47  ASP B CA  1 
ATOM   4449  C C   . ASP B  1 47  ? -27.421 -21.067 -41.224  1.00 39.13  ? 47  ASP B C   1 
ATOM   4450  O O   . ASP B  1 47  ? -26.803 -20.480 -42.114  1.00 37.90  ? 47  ASP B O   1 
ATOM   4451  C CB  . ASP B  1 47  ? -26.856 -19.666 -39.247  1.00 41.62  ? 47  ASP B CB  1 
ATOM   4452  C CG  . ASP B  1 47  ? -27.338 -18.897 -38.023  1.00 47.03  ? 47  ASP B CG  1 
ATOM   4453  O OD1 . ASP B  1 47  ? -28.340 -18.156 -38.122  1.00 47.39  ? 47  ASP B OD1 1 
ATOM   4454  O OD2 . ASP B  1 47  ? -26.707 -19.048 -36.952  1.00 47.97  ? 47  ASP B OD2 1 
ATOM   4455  N N   . PHE B  1 48  ? -27.575 -22.387 -41.229  1.00 37.92  ? 48  PHE B N   1 
ATOM   4456  C CA  . PHE B  1 48  ? -26.922 -23.226 -42.225  1.00 41.34  ? 48  PHE B CA  1 
ATOM   4457  C C   . PHE B  1 48  ? -27.937 -24.186 -42.818  1.00 42.95  ? 48  PHE B C   1 
ATOM   4458  O O   . PHE B  1 48  ? -28.681 -24.844 -42.084  1.00 40.88  ? 48  PHE B O   1 
ATOM   4459  C CB  . PHE B  1 48  ? -25.742 -23.992 -41.619  1.00 36.68  ? 48  PHE B CB  1 
ATOM   4460  C CG  . PHE B  1 48  ? -24.655 -23.100 -41.088  1.00 35.44  ? 48  PHE B CG  1 
ATOM   4461  C CD1 . PHE B  1 48  ? -23.736 -22.518 -41.955  1.00 37.99  ? 48  PHE B CD1 1 
ATOM   4462  C CD2 . PHE B  1 48  ? -24.545 -22.843 -39.724  1.00 35.32  ? 48  PHE B CD2 1 
ATOM   4463  C CE1 . PHE B  1 48  ? -22.728 -21.689 -41.469  1.00 37.42  ? 48  PHE B CE1 1 
ATOM   4464  C CE2 . PHE B  1 48  ? -23.541 -22.013 -39.236  1.00 32.18  ? 48  PHE B CE2 1 
ATOM   4465  C CZ  . PHE B  1 48  ? -22.630 -21.438 -40.112  1.00 30.02  ? 48  PHE B CZ  1 
ATOM   4466  N N   . GLU B  1 49  ? -27.986 -24.237 -44.146  1.00 41.85  ? 49  GLU B N   1 
ATOM   4467  C CA  . GLU B  1 49  ? -28.955 -25.078 -44.850  1.00 46.05  ? 49  GLU B CA  1 
ATOM   4468  C C   . GLU B  1 49  ? -28.361 -26.470 -45.055  1.00 40.99  ? 49  GLU B C   1 
ATOM   4469  O O   . GLU B  1 49  ? -27.991 -26.879 -46.153  1.00 37.35  ? 49  GLU B O   1 
ATOM   4470  C CB  . GLU B  1 49  ? -29.362 -24.437 -46.170  1.00 53.65  ? 49  GLU B CB  1 
ATOM   4471  C CG  . GLU B  1 49  ? -30.120 -23.131 -45.995  1.00 63.93  ? 49  GLU B CG  1 
ATOM   4472  C CD  . GLU B  1 49  ? -31.611 -23.327 -45.747  1.00 73.28  ? 49  GLU B CD  1 
ATOM   4473  O OE1 . GLU B  1 49  ? -32.400 -23.109 -46.696  1.00 78.37  ? 49  GLU B OE1 1 
ATOM   4474  O OE2 . GLU B  1 49  ? -31.998 -23.675 -44.608  1.00 72.07  ? 49  GLU B OE2 1 
ATOM   4475  N N   . ILE B  1 50  ? -28.226 -27.177 -43.938  1.00 35.80  ? 50  ILE B N   1 
ATOM   4476  C CA  . ILE B  1 50  ? -27.847 -28.580 -43.914  1.00 40.98  ? 50  ILE B CA  1 
ATOM   4477  C C   . ILE B  1 50  ? -28.820 -29.309 -43.000  1.00 36.53  ? 50  ILE B C   1 
ATOM   4478  O O   . ILE B  1 50  ? -29.654 -28.701 -42.327  1.00 34.41  ? 50  ILE B O   1 
ATOM   4479  C CB  . ILE B  1 50  ? -26.401 -28.790 -43.427  1.00 38.08  ? 50  ILE B CB  1 
ATOM   4480  C CG1 . ILE B  1 50  ? -26.235 -28.217 -42.022  1.00 37.40  ? 50  ILE B CG1 1 
ATOM   4481  C CG2 . ILE B  1 50  ? -25.429 -28.113 -44.367  1.00 40.45  ? 50  ILE B CG2 1 
ATOM   4482  C CD1 . ILE B  1 50  ? -25.004 -28.705 -41.345  1.00 35.38  ? 50  ILE B CD1 1 
ATOM   4483  N N   . LYS B  1 51  ? -28.706 -30.630 -42.983  1.00 33.64  ? 51  LYS B N   1 
ATOM   4484  C CA  . LYS B  1 51  ? -29.505 -31.463 -42.099  1.00 29.21  ? 51  LYS B CA  1 
ATOM   4485  C C   . LYS B  1 51  ? -28.632 -31.894 -40.931  1.00 26.78  ? 51  LYS B C   1 
ATOM   4486  O O   . LYS B  1 51  ? -27.490 -32.324 -41.135  1.00 28.02  ? 51  LYS B O   1 
ATOM   4487  C CB  . LYS B  1 51  ? -30.063 -32.693 -42.825  1.00 31.03  ? 51  LYS B CB  1 
ATOM   4488  C CG  . LYS B  1 51  ? -30.839 -32.409 -44.120  1.00 37.06  ? 51  LYS B CG  1 
ATOM   4489  C CD  . LYS B  1 51  ? -31.981 -31.433 -43.889  1.00 38.00  ? 51  LYS B CD  1 
ATOM   4490  C CE  . LYS B  1 51  ? -32.798 -31.213 -45.154  1.00 44.67  ? 51  LYS B CE  1 
ATOM   4491  N NZ  . LYS B  1 51  ? -32.742 -29.779 -45.567  1.00 48.28  ? 51  LYS B NZ  1 
ATOM   4492  N N   . LEU B  1 52  ? -29.167 -31.787 -39.709  1.00 24.76  ? 52  LEU B N   1 
ATOM   4493  C CA  . LEU B  1 52  ? -28.476 -32.270 -38.524  1.00 29.30  ? 52  LEU B CA  1 
ATOM   4494  C C   . LEU B  1 52  ? -29.478 -33.000 -37.638  1.00 31.41  ? 52  LEU B C   1 
ATOM   4495  O O   . LEU B  1 52  ? -30.602 -32.535 -37.466  1.00 29.55  ? 52  LEU B O   1 
ATOM   4496  C CB  . LEU B  1 52  ? -27.816 -31.131 -37.720  1.00 28.80  ? 52  LEU B CB  1 
ATOM   4497  C CG  . LEU B  1 52  ? -26.667 -30.322 -38.352  1.00 31.10  ? 52  LEU B CG  1 
ATOM   4498  C CD1 . LEU B  1 52  ? -26.198 -29.249 -37.385  1.00 31.52  ? 52  LEU B CD1 1 
ATOM   4499  C CD2 . LEU B  1 52  ? -25.491 -31.188 -38.816  1.00 29.58  ? 52  LEU B CD2 1 
ATOM   4500  N N   . ASN B  1 53  ? -29.066 -34.137 -37.069  1.00 31.25  ? 53  ASN B N   1 
ATOM   4501  C CA  . ASN B  1 53  ? -29.964 -34.969 -36.288  1.00 24.38  ? 53  ASN B CA  1 
ATOM   4502  C C   . ASN B  1 53  ? -29.463 -35.076 -34.855  1.00 23.25  ? 53  ASN B C   1 
ATOM   4503  O O   . ASN B  1 53  ? -28.275 -34.890 -34.568  1.00 24.76  ? 53  ASN B O   1 
ATOM   4504  C CB  . ASN B  1 53  ? -30.109 -36.363 -36.896  1.00 22.59  ? 53  ASN B CB  1 
ATOM   4505  C CG  . ASN B  1 53  ? -30.417 -36.313 -38.378  1.00 27.40  ? 53  ASN B CG  1 
ATOM   4506  O OD1 . ASN B  1 53  ? -31.548 -36.045 -38.783  1.00 31.69  ? 53  ASN B OD1 1 
ATOM   4507  N ND2 . ASN B  1 53  ? -29.402 -36.542 -39.188  1.00 25.44  ? 53  ASN B ND2 1 
ATOM   4508  N N   . PHE B  1 54  ? -30.397 -35.379 -33.956  1.00 26.58  ? 54  PHE B N   1 
ATOM   4509  C CA  . PHE B  1 54  ? -30.153 -35.264 -32.523  1.00 26.94  ? 54  PHE B CA  1 
ATOM   4510  C C   . PHE B  1 54  ? -30.798 -36.421 -31.783  1.00 24.74  ? 54  PHE B C   1 
ATOM   4511  O O   . PHE B  1 54  ? -31.900 -36.860 -32.124  1.00 24.51  ? 54  PHE B O   1 
ATOM   4512  C CB  . PHE B  1 54  ? -30.672 -33.909 -31.978  1.00 27.11  ? 54  PHE B CB  1 
ATOM   4513  C CG  . PHE B  1 54  ? -29.941 -32.755 -32.557  1.00 29.83  ? 54  PHE B CG  1 
ATOM   4514  C CD1 . PHE B  1 54  ? -28.791 -32.275 -31.946  1.00 28.10  ? 54  PHE B CD1 1 
ATOM   4515  C CD2 . PHE B  1 54  ? -30.341 -32.208 -33.770  1.00 31.17  ? 54  PHE B CD2 1 
ATOM   4516  C CE1 . PHE B  1 54  ? -28.075 -31.236 -32.527  1.00 29.72  ? 54  PHE B CE1 1 
ATOM   4517  C CE2 . PHE B  1 54  ? -29.634 -31.180 -34.353  1.00 30.21  ? 54  PHE B CE2 1 
ATOM   4518  C CZ  . PHE B  1 54  ? -28.497 -30.692 -33.726  1.00 31.10  ? 54  PHE B CZ  1 
ATOM   4519  N N   . ASN B  1 55  ? -30.092 -36.916 -30.773  1.00 25.33  ? 55  ASN B N   1 
ATOM   4520  C CA  . ASN B  1 55  ? -30.671 -37.804 -29.781  1.00 30.13  ? 55  ASN B CA  1 
ATOM   4521  C C   . ASN B  1 55  ? -30.764 -37.056 -28.458  1.00 29.52  ? 55  ASN B C   1 
ATOM   4522  O O   . ASN B  1 55  ? -29.782 -36.442 -28.025  1.00 27.75  ? 55  ASN B O   1 
ATOM   4523  C CB  . ASN B  1 55  ? -29.826 -39.077 -29.624  1.00 18.61  ? 55  ASN B CB  1 
ATOM   4524  C CG  . ASN B  1 55  ? -30.434 -40.051 -28.656  1.00 25.26  ? 55  ASN B CG  1 
ATOM   4525  O OD1 . ASN B  1 55  ? -31.380 -40.751 -28.991  1.00 28.38  ? 55  ASN B OD1 1 
ATOM   4526  N ND2 . ASN B  1 55  ? -29.881 -40.121 -27.445  1.00 24.40  ? 55  ASN B ND2 1 
ATOM   4527  N N   . LEU B  1 56  ? -31.937 -37.111 -27.818  1.00 27.95  ? 56  LEU B N   1 
ATOM   4528  C CA  . LEU B  1 56  ? -32.123 -36.611 -26.460  1.00 32.01  ? 56  LEU B CA  1 
ATOM   4529  C C   . LEU B  1 56  ? -32.594 -37.761 -25.578  1.00 31.85  ? 56  LEU B C   1 
ATOM   4530  O O   . LEU B  1 56  ? -33.646 -38.355 -25.842  1.00 31.24  ? 56  LEU B O   1 
ATOM   4531  C CB  . LEU B  1 56  ? -33.140 -35.462 -26.422  1.00 27.79  ? 56  LEU B CB  1 
ATOM   4532  C CG  . LEU B  1 56  ? -32.920 -34.287 -27.372  1.00 27.06  ? 56  LEU B CG  1 
ATOM   4533  C CD1 . LEU B  1 56  ? -34.048 -33.262 -27.296  1.00 30.68  ? 56  LEU B CD1 1 
ATOM   4534  C CD2 . LEU B  1 56  ? -31.589 -33.636 -27.061  1.00 32.35  ? 56  LEU B CD2 1 
ATOM   4535  N N   . THR B  1 57  ? -31.815 -38.095 -24.549  1.00 28.33  ? 57  THR B N   1 
ATOM   4536  C CA  . THR B  1 57  ? -32.280 -39.111 -23.620  1.00 27.86  ? 57  THR B CA  1 
ATOM   4537  C C   . THR B  1 57  ? -33.416 -38.538 -22.769  1.00 26.66  ? 57  THR B C   1 
ATOM   4538  O O   . THR B  1 57  ? -33.420 -37.344 -22.448  1.00 23.99  ? 57  THR B O   1 
ATOM   4539  C CB  . THR B  1 57  ? -31.157 -39.604 -22.694  1.00 26.60  ? 57  THR B CB  1 
ATOM   4540  O OG1 . THR B  1 57  ? -30.659 -38.504 -21.930  1.00 22.79  ? 57  THR B OG1 1 
ATOM   4541  C CG2 . THR B  1 57  ? -30.023 -40.248 -23.495  1.00 24.59  ? 57  THR B CG2 1 
ATOM   4542  N N   . PRO B  1 58  ? -34.391 -39.376 -22.389  1.00 28.24  ? 58  PRO B N   1 
ATOM   4543  C CA  . PRO B  1 58  ? -35.509 -38.880 -21.566  1.00 28.67  ? 58  PRO B CA  1 
ATOM   4544  C C   . PRO B  1 58  ? -35.080 -38.284 -20.234  1.00 26.63  ? 58  PRO B C   1 
ATOM   4545  O O   . PRO B  1 58  ? -35.670 -37.286 -19.794  1.00 24.98  ? 58  PRO B O   1 
ATOM   4546  C CB  . PRO B  1 58  ? -36.378 -40.134 -21.378  1.00 28.51  ? 58  PRO B CB  1 
ATOM   4547  C CG  . PRO B  1 58  ? -36.038 -41.013 -22.573  1.00 25.31  ? 58  PRO B CG  1 
ATOM   4548  C CD  . PRO B  1 58  ? -34.568 -40.792 -22.771  1.00 24.29  ? 58  PRO B CD  1 
ATOM   4549  N N   . VAL B  1 59  ? -34.057 -38.852 -19.590  1.00 23.52  ? 59  VAL B N   1 
ATOM   4550  C CA  . VAL B  1 59  ? -33.613 -38.311 -18.305  1.00 23.52  ? 59  VAL B CA  1 
ATOM   4551  C C   . VAL B  1 59  ? -33.022 -36.915 -18.484  1.00 27.26  ? 59  VAL B C   1 
ATOM   4552  O O   . VAL B  1 59  ? -33.135 -36.072 -17.591  1.00 23.40  ? 59  VAL B O   1 
ATOM   4553  C CB  . VAL B  1 59  ? -32.628 -39.280 -17.626  1.00 22.99  ? 59  VAL B CB  1 
ATOM   4554  C CG1 . VAL B  1 59  ? -31.420 -39.559 -18.508  1.00 24.89  ? 59  VAL B CG1 1 
ATOM   4555  C CG2 . VAL B  1 59  ? -32.183 -38.742 -16.241  1.00 19.12  ? 59  VAL B CG2 1 
ATOM   4556  N N   . LEU B  1 60  ? -32.410 -36.631 -19.643  1.00 23.68  ? 60  LEU B N   1 
ATOM   4557  C CA  . LEU B  1 60  ? -31.965 -35.272 -19.913  1.00 25.18  ? 60  LEU B CA  1 
ATOM   4558  C C   . LEU B  1 60  ? -33.154 -34.336 -20.086  1.00 29.13  ? 60  LEU B C   1 
ATOM   4559  O O   . LEU B  1 60  ? -33.185 -33.234 -19.516  1.00 30.14  ? 60  LEU B O   1 
ATOM   4560  C CB  . LEU B  1 60  ? -31.089 -35.235 -21.165  1.00 20.12  ? 60  LEU B CB  1 
ATOM   4561  C CG  . LEU B  1 60  ? -30.695 -33.824 -21.583  1.00 22.18  ? 60  LEU B CG  1 
ATOM   4562  C CD1 . LEU B  1 60  ? -29.852 -33.160 -20.515  1.00 28.18  ? 60  LEU B CD1 1 
ATOM   4563  C CD2 . LEU B  1 60  ? -29.927 -33.887 -22.880  1.00 21.57  ? 60  LEU B CD2 1 
ATOM   4564  N N   . ILE B  1 61  ? -34.141 -34.754 -20.883  1.00 25.29  ? 61  ILE B N   1 
ATOM   4565  C CA  . ILE B  1 61  ? -35.315 -33.919 -21.088  1.00 24.39  ? 61  ILE B CA  1 
ATOM   4566  C C   . ILE B  1 61  ? -35.945 -33.548 -19.750  1.00 23.59  ? 61  ILE B C   1 
ATOM   4567  O O   . ILE B  1 61  ? -36.272 -32.377 -19.503  1.00 28.02  ? 61  ILE B O   1 
ATOM   4568  C CB  . ILE B  1 61  ? -36.310 -34.623 -22.029  1.00 26.09  ? 61  ILE B CB  1 
ATOM   4569  C CG1 . ILE B  1 61  ? -35.657 -34.839 -23.401  1.00 25.90  ? 61  ILE B CG1 1 
ATOM   4570  C CG2 . ILE B  1 61  ? -37.580 -33.800 -22.160  1.00 23.74  ? 61  ILE B CG2 1 
ATOM   4571  C CD1 . ILE B  1 61  ? -36.489 -35.668 -24.364  1.00 30.44  ? 61  ILE B CD1 1 
ATOM   4572  N N   . ASP B  1 62  ? -36.087 -34.522 -18.852  1.00 23.98  ? 62  ASP B N   1 
ATOM   4573  C CA  . ASP B  1 62  ? -36.672 -34.248 -17.538  1.00 29.56  ? 62  ASP B CA  1 
ATOM   4574  C C   . ASP B  1 62  ? -35.946 -33.107 -16.837  1.00 30.36  ? 62  ASP B C   1 
ATOM   4575  O O   . ASP B  1 62  ? -36.577 -32.188 -16.296  1.00 27.47  ? 62  ASP B O   1 
ATOM   4576  C CB  . ASP B  1 62  ? -36.634 -35.506 -16.680  1.00 32.05  ? 62  ASP B CB  1 
ATOM   4577  C CG  . ASP B  1 62  ? -37.750 -36.460 -17.011  1.00 37.83  ? 62  ASP B CG  1 
ATOM   4578  O OD1 . ASP B  1 62  ? -38.816 -35.975 -17.455  1.00 36.78  ? 62  ASP B OD1 1 
ATOM   4579  O OD2 . ASP B  1 62  ? -37.556 -37.689 -16.837  1.00 40.51  ? 62  ASP B OD2 1 
ATOM   4580  N N   . GLN B  1 63  ? -34.612 -33.137 -16.862  1.00 32.43  ? 63  GLN B N   1 
ATOM   4581  C CA  . GLN B  1 63  ? -33.835 -32.080 -16.225  1.00 30.23  ? 63  GLN B CA  1 
ATOM   4582  C C   . GLN B  1 63  ? -33.971 -30.761 -16.972  1.00 29.80  ? 63  GLN B C   1 
ATOM   4583  O O   . GLN B  1 63  ? -34.109 -29.707 -16.354  1.00 29.81  ? 63  GLN B O   1 
ATOM   4584  C CB  . GLN B  1 63  ? -32.367 -32.487 -16.137  1.00 23.70  ? 63  GLN B CB  1 
ATOM   4585  C CG  . GLN B  1 63  ? -32.128 -33.668 -15.225  1.00 25.87  ? 63  GLN B CG  1 
ATOM   4586  C CD  . GLN B  1 63  ? -30.690 -34.141 -15.268  1.00 28.88  ? 63  GLN B CD  1 
ATOM   4587  O OE1 . GLN B  1 63  ? -29.800 -33.552 -14.628  1.00 30.02  ? 63  GLN B OE1 1 
ATOM   4588  N NE2 . GLN B  1 63  ? -30.448 -35.210 -16.029  1.00 24.85  ? 63  GLN B NE2 1 
ATOM   4589  N N   . ILE B  1 64  ? -33.901 -30.786 -18.305  1.00 30.04  ? 64  ILE B N   1 
ATOM   4590  C CA  . ILE B  1 64  ? -34.090 -29.537 -19.029  1.00 27.16  ? 64  ILE B CA  1 
ATOM   4591  C C   . ILE B  1 64  ? -35.416 -28.908 -18.636  1.00 28.28  ? 64  ILE B C   1 
ATOM   4592  O O   . ILE B  1 64  ? -35.494 -27.707 -18.342  1.00 29.40  ? 64  ILE B O   1 
ATOM   4593  C CB  . ILE B  1 64  ? -33.996 -29.770 -20.545  1.00 31.11  ? 64  ILE B CB  1 
ATOM   4594  C CG1 . ILE B  1 64  ? -32.564 -30.131 -20.915  1.00 29.39  ? 64  ILE B CG1 1 
ATOM   4595  C CG2 . ILE B  1 64  ? -34.477 -28.511 -21.301  1.00 35.02  ? 64  ILE B CG2 1 
ATOM   4596  C CD1 . ILE B  1 64  ? -32.363 -30.383 -22.359  1.00 27.58  ? 64  ILE B CD1 1 
ATOM   4597  N N   . GLN B  1 65  ? -36.469 -29.721 -18.573  1.00 26.39  ? 65  GLN B N   1 
ATOM   4598  C CA  . GLN B  1 65  ? -37.778 -29.210 -18.192  1.00 26.17  ? 65  GLN B CA  1 
ATOM   4599  C C   . GLN B  1 65  ? -37.757 -28.595 -16.803  1.00 29.87  ? 65  GLN B C   1 
ATOM   4600  O O   . GLN B  1 65  ? -38.338 -27.522 -16.581  1.00 30.81  ? 65  GLN B O   1 
ATOM   4601  C CB  . GLN B  1 65  ? -38.815 -30.327 -18.262  1.00 27.90  ? 65  GLN B CB  1 
ATOM   4602  C CG  . GLN B  1 65  ? -39.303 -30.587 -19.684  1.00 30.45  ? 65  GLN B CG  1 
ATOM   4603  C CD  . GLN B  1 65  ? -40.269 -31.753 -19.773  1.00 38.28  ? 65  GLN B CD  1 
ATOM   4604  O OE1 . GLN B  1 65  ? -39.995 -32.851 -19.288  1.00 39.15  ? 65  GLN B OE1 1 
ATOM   4605  N NE2 . GLN B  1 65  ? -41.407 -31.518 -20.406  1.00 45.63  ? 65  GLN B NE2 1 
ATOM   4606  N N   . GLU B  1 66  ? -37.093 -29.259 -15.850  1.00 30.23  ? 66  GLU B N   1 
ATOM   4607  C CA  . GLU B  1 66  ? -37.057 -28.744 -14.487  1.00 32.25  ? 66  GLU B CA  1 
ATOM   4608  C C   . GLU B  1 66  ? -36.335 -27.402 -14.418  1.00 31.09  ? 66  GLU B C   1 
ATOM   4609  O O   . GLU B  1 66  ? -36.816 -26.471 -13.764  1.00 32.04  ? 66  GLU B O   1 
ATOM   4610  C CB  . GLU B  1 66  ? -36.410 -29.767 -13.545  1.00 32.19  ? 66  GLU B CB  1 
ATOM   4611  C CG  . GLU B  1 66  ? -36.909 -29.628 -12.110  1.00 39.23  ? 66  GLU B CG  1 
ATOM   4612  C CD  . GLU B  1 66  ? -36.266 -30.601 -11.128  1.00 44.38  ? 66  GLU B CD  1 
ATOM   4613  O OE1 . GLU B  1 66  ? -36.190 -30.273 -9.915   1.00 46.50  ? 66  GLU B OE1 1 
ATOM   4614  O OE2 . GLU B  1 66  ? -35.853 -31.696 -11.562  1.00 44.79  ? 66  GLU B OE2 1 
ATOM   4615  N N   . TYR B  1 67  ? -35.184 -27.276 -15.091  1.00 29.02  ? 67  TYR B N   1 
ATOM   4616  C CA  . TYR B  1 67  ? -34.502 -25.985 -15.121  1.00 31.97  ? 67  TYR B CA  1 
ATOM   4617  C C   . TYR B  1 67  ? -35.346 -24.919 -15.821  1.00 32.14  ? 67  TYR B C   1 
ATOM   4618  O O   . TYR B  1 67  ? -35.370 -23.757 -15.397  1.00 32.41  ? 67  TYR B O   1 
ATOM   4619  C CB  . TYR B  1 67  ? -33.149 -26.120 -15.812  1.00 27.44  ? 67  TYR B CB  1 
ATOM   4620  C CG  . TYR B  1 67  ? -32.048 -26.666 -14.924  1.00 26.94  ? 67  TYR B CG  1 
ATOM   4621  C CD1 . TYR B  1 67  ? -31.325 -25.826 -14.071  1.00 28.57  ? 67  TYR B CD1 1 
ATOM   4622  C CD2 . TYR B  1 67  ? -31.719 -28.021 -14.951  1.00 27.38  ? 67  TYR B CD2 1 
ATOM   4623  C CE1 . TYR B  1 67  ? -30.295 -26.334 -13.262  1.00 27.12  ? 67  TYR B CE1 1 
ATOM   4624  C CE2 . TYR B  1 67  ? -30.698 -28.529 -14.159  1.00 26.69  ? 67  TYR B CE2 1 
ATOM   4625  C CZ  . TYR B  1 67  ? -30.002 -27.684 -13.307  1.00 29.65  ? 67  TYR B CZ  1 
ATOM   4626  O OH  . TYR B  1 67  ? -28.991 -28.204 -12.534  1.00 28.47  ? 67  TYR B OH  1 
ATOM   4627  N N   . ALA B  1 68  ? -36.038 -25.295 -16.901  1.00 33.28  ? 68  ALA B N   1 
ATOM   4628  C CA  . ALA B  1 68  ? -36.861 -24.333 -17.631  1.00 33.93  ? 68  ALA B CA  1 
ATOM   4629  C C   . ALA B  1 68  ? -37.997 -23.797 -16.764  1.00 37.86  ? 68  ALA B C   1 
ATOM   4630  O O   . ALA B  1 68  ? -38.299 -22.599 -16.799  1.00 43.29  ? 68  ALA B O   1 
ATOM   4631  C CB  . ALA B  1 68  ? -37.414 -24.975 -18.905  1.00 33.58  ? 68  ALA B CB  1 
ATOM   4632  N N   . GLN B  1 69  ? -38.637 -24.663 -15.983  1.00 36.90  ? 69  GLN B N   1 
ATOM   4633  C CA  . GLN B  1 69  ? -39.718 -24.239 -15.098  1.00 40.30  ? 69  GLN B CA  1 
ATOM   4634  C C   . GLN B  1 69  ? -39.231 -23.522 -13.843  1.00 40.71  ? 69  GLN B C   1 
ATOM   4635  O O   . GLN B  1 69  ? -40.060 -23.157 -13.004  1.00 48.37  ? 69  GLN B O   1 
ATOM   4636  C CB  . GLN B  1 69  ? -40.574 -25.445 -14.700  1.00 42.93  ? 69  GLN B CB  1 
ATOM   4637  C CG  . GLN B  1 69  ? -41.373 -26.048 -15.855  1.00 49.24  ? 69  GLN B CG  1 
ATOM   4638  C CD  . GLN B  1 69  ? -41.671 -27.539 -15.672  1.00 57.50  ? 69  GLN B CD  1 
ATOM   4639  O OE1 . GLN B  1 69  ? -41.516 -28.091 -14.582  1.00 59.05  ? 69  GLN B OE1 1 
ATOM   4640  N NE2 . GLN B  1 69  ? -42.098 -28.194 -16.747  1.00 60.17  ? 69  GLN B NE2 1 
ATOM   4641  N N   . GLY B  1 70  ? -37.926 -23.311 -13.680  1.00 38.37  ? 70  GLY B N   1 
ATOM   4642  C CA  . GLY B  1 70  ? -37.451 -22.659 -12.470  1.00 41.12  ? 70  GLY B CA  1 
ATOM   4643  C C   . GLY B  1 70  ? -37.544 -23.495 -11.213  1.00 41.16  ? 70  GLY B C   1 
ATOM   4644  O O   . GLY B  1 70  ? -37.521 -22.949 -10.108  1.00 43.79  ? 70  GLY B O   1 
ATOM   4645  N N   . LYS B  1 71  ? -37.641 -24.816 -11.344  1.00 42.77  ? 71  LYS B N   1 
ATOM   4646  C CA  . LYS B  1 71  ? -37.836 -25.691 -10.201  1.00 37.84  ? 71  LYS B CA  1 
ATOM   4647  C C   . LYS B  1 71  ? -36.568 -26.432 -9.793   1.00 38.02  ? 71  LYS B C   1 
ATOM   4648  O O   . LYS B  1 71  ? -36.568 -27.130 -8.770   1.00 36.93  ? 71  LYS B O   1 
ATOM   4649  C CB  . LYS B  1 71  ? -38.957 -26.696 -10.504  1.00 39.04  ? 71  LYS B CB  1 
ATOM   4650  N N   . ALA B  1 72  ? -35.485 -26.273 -10.539  1.00 35.16  ? 72  ALA B N   1 
ATOM   4651  C CA  . ALA B  1 72  ? -34.248 -26.991 -10.268  1.00 31.08  ? 72  ALA B CA  1 
ATOM   4652  C C   . ALA B  1 72  ? -33.482 -26.298 -9.144   1.00 33.47  ? 72  ALA B C   1 
ATOM   4653  O O   . ALA B  1 72  ? -33.166 -25.104 -9.232   1.00 34.06  ? 72  ALA B O   1 
ATOM   4654  C CB  . ALA B  1 72  ? -33.403 -27.080 -11.538  1.00 28.30  ? 72  ALA B CB  1 
ATOM   4655  N N   . LYS B  1 73  ? -33.205 -27.036 -8.076   1.00 33.58  ? 73  LYS B N   1 
ATOM   4656  C CA  . LYS B  1 73  ? -32.374 -26.534 -6.984   1.00 33.14  ? 73  LYS B CA  1 
ATOM   4657  C C   . LYS B  1 73  ? -30.953 -26.998 -7.263   1.00 33.12  ? 73  LYS B C   1 
ATOM   4658  O O   . LYS B  1 73  ? -30.604 -28.152 -7.015   1.00 41.29  ? 73  LYS B O   1 
ATOM   4659  C CB  . LYS B  1 73  ? -32.889 -27.029 -5.635   1.00 33.22  ? 73  LYS B CB  1 
ATOM   4660  C CG  . LYS B  1 73  ? -34.255 -26.461 -5.266   1.00 42.91  ? 73  LYS B CG  1 
ATOM   4661  C CD  . LYS B  1 73  ? -34.991 -27.301 -4.216   1.00 51.54  ? 73  LYS B CD  1 
ATOM   4662  C CE  . LYS B  1 73  ? -35.544 -28.596 -4.825   1.00 57.11  ? 73  LYS B CE  1 
ATOM   4663  N NZ  . LYS B  1 73  ? -36.692 -28.371 -5.763   1.00 56.91  ? 73  LYS B NZ  1 
ATOM   4664  N N   . ASP B  1 74  ? -30.139 -26.113 -7.815   1.00 27.43  ? 74  ASP B N   1 
ATOM   4665  C CA  . ASP B  1 74  ? -28.795 -26.445 -8.282   1.00 25.75  ? 74  ASP B CA  1 
ATOM   4666  C C   . ASP B  1 74  ? -27.819 -25.843 -7.278   1.00 27.35  ? 74  ASP B C   1 
ATOM   4667  O O   . ASP B  1 74  ? -27.699 -24.619 -7.195   1.00 27.51  ? 74  ASP B O   1 
ATOM   4668  C CB  . ASP B  1 74  ? -28.580 -25.891 -9.692   1.00 29.00  ? 74  ASP B CB  1 
ATOM   4669  C CG  . ASP B  1 74  ? -27.216 -26.241 -10.266  1.00 34.07  ? 74  ASP B CG  1 
ATOM   4670  O OD1 . ASP B  1 74  ? -26.193 -26.133 -9.544   1.00 33.92  ? 74  ASP B OD1 1 
ATOM   4671  O OD2 . ASP B  1 74  ? -27.167 -26.587 -11.467  1.00 32.87  ? 74  ASP B OD2 1 
ATOM   4672  N N   . VAL B  1 75  ? -27.127 -26.689 -6.505   1.00 29.70  ? 75  VAL B N   1 
ATOM   4673  C CA  . VAL B  1 75  ? -26.372 -26.134 -5.383   1.00 34.44  ? 75  VAL B CA  1 
ATOM   4674  C C   . VAL B  1 75  ? -25.183 -25.343 -5.887   1.00 32.43  ? 75  VAL B C   1 
ATOM   4675  O O   . VAL B  1 75  ? -24.876 -24.259 -5.371   1.00 33.07  ? 75  VAL B O   1 
ATOM   4676  C CB  . VAL B  1 75  ? -25.948 -27.222 -4.375   1.00 41.21  ? 75  VAL B CB  1 
ATOM   4677  C CG1 . VAL B  1 75  ? -27.171 -27.826 -3.718   1.00 46.62  ? 75  VAL B CG1 1 
ATOM   4678  C CG2 . VAL B  1 75  ? -25.094 -28.298 -5.031   1.00 42.18  ? 75  VAL B CG2 1 
ATOM   4679  N N   . PHE B  1 76  ? -24.504 -25.827 -6.893   1.00 33.97  ? 76  PHE B N   1 
ATOM   4680  C CA  . PHE B  1 76  ? -23.376 -25.092 -7.512   1.00 34.97  ? 76  PHE B CA  1 
ATOM   4681  C C   . PHE B  1 76  ? -23.841 -23.817 -8.136   1.00 35.66  ? 76  PHE B C   1 
ATOM   4682  O O   . PHE B  1 76  ? -23.182 -22.899 -8.008   1.00 33.24  ? 76  PHE B O   1 
ATOM   4683  C CB  . PHE B  1 76  ? -22.680 -25.776 -8.574   1.00 40.97  ? 76  PHE B CB  1 
ATOM   4684  C CG  . PHE B  1 76  ? -21.530 -26.537 -8.154   1.00 52.66  ? 76  PHE B CG  1 
ATOM   4685  C CD1 . PHE B  1 76  ? -21.685 -27.860 -7.673   1.00 55.32  ? 76  PHE B CD1 1 
ATOM   4686  C CD2 . PHE B  1 76  ? -20.280 -26.013 -8.237   1.00 57.26  ? 76  PHE B CD2 1 
ATOM   4687  C CE1 . PHE B  1 76  ? -20.616 -28.639 -7.266   1.00 60.71  ? 76  PHE B CE1 1 
ATOM   4688  C CE2 . PHE B  1 76  ? -19.208 -26.806 -7.842   1.00 59.40  ? 76  PHE B CE2 1 
ATOM   4689  C CZ  . PHE B  1 76  ? -19.368 -28.104 -7.361   1.00 60.91  ? 76  PHE B CZ  1 
ATOM   4690  N N   . LEU B  1 77  ? -24.991 -23.799 -8.806   1.00 35.60  ? 77  LEU B N   1 
ATOM   4691  C CA  . LEU B  1 77  ? -25.492 -22.546 -9.376   1.00 37.59  ? 77  LEU B CA  1 
ATOM   4692  C C   . LEU B  1 77  ? -25.916 -21.555 -8.300   1.00 37.60  ? 77  LEU B C   1 
ATOM   4693  O O   . LEU B  1 77  ? -25.834 -20.342 -8.521   1.00 35.68  ? 77  LEU B O   1 
ATOM   4694  C CB  . LEU B  1 77  ? -26.661 -22.813 -10.328  1.00 35.14  ? 77  LEU B CB  1 
ATOM   4695  C CG  . LEU B  1 77  ? -27.094 -21.660 -11.233  1.00 36.85  ? 77  LEU B CG  1 
ATOM   4696  C CD1 . LEU B  1 77  ? -25.936 -21.097 -12.083  1.00 29.63  ? 77  LEU B CD1 1 
ATOM   4697  C CD2 . LEU B  1 77  ? -28.233 -22.134 -12.109  1.00 40.36  ? 77  LEU B CD2 1 
ATOM   4698  N N   . GLU B  1 78  ? -26.378 -22.044 -7.139   1.00 38.46  ? 78  GLU B N   1 
ATOM   4699  C CA  . GLU B  1 78  ? -26.688 -21.151 -6.026   1.00 38.09  ? 78  GLU B CA  1 
ATOM   4700  C C   . GLU B  1 78  ? -25.441 -20.417 -5.545   1.00 33.93  ? 78  GLU B C   1 
ATOM   4701  O O   . GLU B  1 78  ? -25.494 -19.222 -5.222   1.00 33.68  ? 78  GLU B O   1 
ATOM   4702  C CB  . GLU B  1 78  ? -27.330 -21.937 -4.876   1.00 45.16  ? 78  GLU B CB  1 
ATOM   4703  C CG  . GLU B  1 78  ? -28.762 -22.429 -5.153   1.00 56.83  ? 78  GLU B CG  1 
ATOM   4704  C CD  . GLU B  1 78  ? -29.295 -23.371 -4.070   1.00 69.20  ? 78  GLU B CD  1 
ATOM   4705  O OE1 . GLU B  1 78  ? -29.420 -22.933 -2.905   1.00 73.50  ? 78  GLU B OE1 1 
ATOM   4706  O OE2 . GLU B  1 78  ? -29.592 -24.549 -4.377   1.00 71.80  ? 78  GLU B OE2 1 
ATOM   4707  N N   . ALA B  1 79  ? -24.313 -21.117 -5.480   1.00 34.64  ? 79  ALA B N   1 
ATOM   4708  C CA  . ALA B  1 79  ? -23.050 -20.473 -5.132   1.00 33.23  ? 79  ALA B CA  1 
ATOM   4709  C C   . ALA B  1 79  ? -22.639 -19.413 -6.154   1.00 29.86  ? 79  ALA B C   1 
ATOM   4710  O O   . ALA B  1 79  ? -22.012 -18.409 -5.793   1.00 29.48  ? 79  ALA B O   1 
ATOM   4711  C CB  . ALA B  1 79  ? -21.953 -21.530 -5.005   1.00 29.09  ? 79  ALA B CB  1 
ATOM   4712  N N   . ILE B  1 80  ? -22.946 -19.624 -7.430   1.00 29.38  ? 80  ILE B N   1 
ATOM   4713  C CA  . ILE B  1 80  ? -22.644 -18.602 -8.428   1.00 26.45  ? 80  ILE B CA  1 
ATOM   4714  C C   . ILE B  1 80  ? -23.522 -17.382 -8.204   1.00 24.90  ? 80  ILE B C   1 
ATOM   4715  O O   . ILE B  1 80  ? -23.056 -16.236 -8.223   1.00 25.06  ? 80  ILE B O   1 
ATOM   4716  C CB  . ILE B  1 80  ? -22.837 -19.165 -9.852   1.00 27.10  ? 80  ILE B CB  1 
ATOM   4717  C CG1 . ILE B  1 80  ? -21.838 -20.283 -10.161  1.00 34.84  ? 80  ILE B CG1 1 
ATOM   4718  C CG2 . ILE B  1 80  ? -22.753 -18.050 -10.889  1.00 28.73  ? 80  ILE B CG2 1 
ATOM   4719  C CD1 . ILE B  1 80  ? -20.480 -19.785 -10.567  1.00 37.82  ? 80  ILE B CD1 1 
ATOM   4720  N N   . ARG B  1 81  ? -24.815 -17.615 -7.992   1.00 32.16  ? 81  ARG B N   1 
ATOM   4721  C CA  . ARG B  1 81  ? -25.783 -16.530 -8.041   1.00 35.16  ? 81  ARG B CA  1 
ATOM   4722  C C   . ARG B  1 81  ? -25.648 -15.600 -6.845   1.00 35.44  ? 81  ARG B C   1 
ATOM   4723  O O   . ARG B  1 81  ? -25.852 -14.387 -6.981   1.00 29.26  ? 81  ARG B O   1 
ATOM   4724  C CB  . ARG B  1 81  ? -27.187 -17.128 -8.127   1.00 38.59  ? 81  ARG B CB  1 
ATOM   4725  C CG  . ARG B  1 81  ? -28.298 -16.242 -7.600   1.00 44.82  ? 81  ARG B CG  1 
ATOM   4726  C CD  . ARG B  1 81  ? -29.611 -16.537 -8.311   1.00 51.47  ? 81  ARG B CD  1 
ATOM   4727  N NE  . ARG B  1 81  ? -29.866 -17.971 -8.453   1.00 58.76  ? 81  ARG B NE  1 
ATOM   4728  C CZ  . ARG B  1 81  ? -30.564 -18.517 -9.446   1.00 60.71  ? 81  ARG B CZ  1 
ATOM   4729  N NH1 . ARG B  1 81  ? -31.076 -17.741 -10.400  1.00 62.65  ? 81  ARG B NH1 1 
ATOM   4730  N NH2 . ARG B  1 81  ? -30.747 -19.836 -9.488   1.00 59.31  ? 81  ARG B NH2 1 
ATOM   4731  N N   . LYS B  1 82  ? -25.278 -16.149 -5.684   1.00 39.17  ? 82  LYS B N   1 
ATOM   4732  C CA  . LYS B  1 82  ? -25.204 -15.397 -4.436   1.00 37.95  ? 82  LYS B CA  1 
ATOM   4733  C C   . LYS B  1 82  ? -24.295 -14.180 -4.561   1.00 33.09  ? 82  LYS B C   1 
ATOM   4734  O O   . LYS B  1 82  ? -23.235 -14.238 -5.196   1.00 33.04  ? 82  LYS B O   1 
ATOM   4735  C CB  . LYS B  1 82  ? -24.647 -16.297 -3.323   1.00 40.26  ? 82  LYS B CB  1 
ATOM   4736  C CG  . LYS B  1 82  ? -25.636 -17.142 -2.541   1.00 46.19  ? 82  LYS B CG  1 
ATOM   4737  C CD  . LYS B  1 82  ? -24.949 -17.706 -1.298   1.00 47.42  ? 82  LYS B CD  1 
ATOM   4738  C CE  . LYS B  1 82  ? -25.813 -18.715 -0.577   1.00 51.30  ? 82  LYS B CE  1 
ATOM   4739  N NZ  . LYS B  1 82  ? -25.120 -19.244 0.631    1.00 54.11  ? 82  LYS B NZ  1 
ATOM   4740  N N   . ASP B  1 83  ? -24.689 -13.089 -3.924   1.00 29.74  ? 83  ASP B N   1 
ATOM   4741  C CA  . ASP B  1 83  ? -23.718 -12.054 -3.598   1.00 35.36  ? 83  ASP B CA  1 
ATOM   4742  C C   . ASP B  1 83  ? -22.577 -12.674 -2.787   1.00 37.51  ? 83  ASP B C   1 
ATOM   4743  O O   . ASP B  1 83  ? -22.839 -13.409 -1.820   1.00 39.45  ? 83  ASP B O   1 
ATOM   4744  C CB  . ASP B  1 83  ? -24.382 -10.926 -2.816   1.00 39.73  ? 83  ASP B CB  1 
ATOM   4745  C CG  . ASP B  1 83  ? -23.448 -9.760  -2.561   1.00 43.55  ? 83  ASP B CG  1 
ATOM   4746  O OD1 . ASP B  1 83  ? -22.500 -9.910  -1.763   1.00 42.14  ? 83  ASP B OD1 1 
ATOM   4747  O OD2 . ASP B  1 83  ? -23.667 -8.685  -3.162   1.00 49.37  ? 83  ASP B OD2 1 
ATOM   4748  N N   . PRO B  1 84  ? -21.314 -12.414 -3.147   1.00 38.45  ? 84  PRO B N   1 
ATOM   4749  C CA  . PRO B  1 84  ? -20.196 -13.125 -2.497   1.00 39.14  ? 84  PRO B CA  1 
ATOM   4750  C C   . PRO B  1 84  ? -20.154 -12.980 -0.983   1.00 34.28  ? 84  PRO B C   1 
ATOM   4751  O O   . PRO B  1 84  ? -19.587 -13.845 -0.312   1.00 35.64  ? 84  PRO B O   1 
ATOM   4752  C CB  . PRO B  1 84  ? -18.953 -12.492 -3.143   1.00 41.54  ? 84  PRO B CB  1 
ATOM   4753  C CG  . PRO B  1 84  ? -19.449 -11.938 -4.468   1.00 39.54  ? 84  PRO B CG  1 
ATOM   4754  C CD  . PRO B  1 84  ? -20.856 -11.488 -4.203   1.00 40.46  ? 84  PRO B CD  1 
ATOM   4755  N N   . ASP B  1 85  ? -20.720 -11.915 -0.423   1.00 34.36  ? 85  ASP B N   1 
ATOM   4756  C CA  . ASP B  1 85  ? -20.713 -11.773 1.030    1.00 37.51  ? 85  ASP B CA  1 
ATOM   4757  C C   . ASP B  1 85  ? -21.628 -12.781 1.717    1.00 36.21  ? 85  ASP B C   1 
ATOM   4758  O O   . ASP B  1 85  ? -21.483 -13.014 2.922    1.00 34.41  ? 85  ASP B O   1 
ATOM   4759  C CB  . ASP B  1 85  ? -21.103 -10.350 1.422    1.00 45.08  ? 85  ASP B CB  1 
ATOM   4760  C CG  . ASP B  1 85  ? -20.032 -9.334  1.067    1.00 45.84  ? 85  ASP B CG  1 
ATOM   4761  O OD1 . ASP B  1 85  ? -18.853 -9.714  0.895    1.00 48.44  ? 85  ASP B OD1 1 
ATOM   4762  O OD2 . ASP B  1 85  ? -20.379 -8.152  0.955    1.00 41.94  ? 85  ASP B OD2 1 
ATOM   4763  N N   . ASP B  1 86  ? -22.559 -13.380 0.985    1.00 37.88  ? 86  ASP B N   1 
ATOM   4764  C CA  . ASP B  1 86  ? -23.401 -14.433 1.530    1.00 39.48  ? 86  ASP B CA  1 
ATOM   4765  C C   . ASP B  1 86  ? -22.815 -15.823 1.313    1.00 35.78  ? 86  ASP B C   1 
ATOM   4766  O O   . ASP B  1 86  ? -23.417 -16.809 1.750    1.00 33.98  ? 86  ASP B O   1 
ATOM   4767  C CB  . ASP B  1 86  ? -24.794 -14.368 0.901    1.00 40.74  ? 86  ASP B CB  1 
ATOM   4768  C CG  . ASP B  1 86  ? -25.458 -13.019 1.080    1.00 42.40  ? 86  ASP B CG  1 
ATOM   4769  O OD1 . ASP B  1 86  ? -25.104 -12.278 2.023    1.00 42.65  ? 86  ASP B OD1 1 
ATOM   4770  O OD2 . ASP B  1 86  ? -26.346 -12.707 0.258    1.00 45.35  ? 86  ASP B OD2 1 
ATOM   4771  N N   . LEU B  1 87  ? -21.666 -15.920 0.647    1.00 30.38  ? 87  LEU B N   1 
ATOM   4772  C CA  . LEU B  1 87  ? -21.060 -17.213 0.357    1.00 30.01  ? 87  LEU B CA  1 
ATOM   4773  C C   . LEU B  1 87  ? -20.609 -17.913 1.629    1.00 32.73  ? 87  LEU B C   1 
ATOM   4774  O O   . LEU B  1 87  ? -19.987 -17.307 2.507    1.00 33.65  ? 87  LEU B O   1 
ATOM   4775  C CB  . LEU B  1 87  ? -19.857 -17.034 -0.562   1.00 27.87  ? 87  LEU B CB  1 
ATOM   4776  C CG  . LEU B  1 87  ? -20.220 -16.861 -2.032   1.00 28.51  ? 87  LEU B CG  1 
ATOM   4777  C CD1 . LEU B  1 87  ? -18.977 -16.429 -2.817   1.00 27.47  ? 87  LEU B CD1 1 
ATOM   4778  C CD2 . LEU B  1 87  ? -20.819 -18.165 -2.595   1.00 27.63  ? 87  LEU B CD2 1 
ATOM   4779  N N   . GLU B  1 88  ? -20.909 -19.205 1.714    1.00 32.61  ? 88  GLU B N   1 
ATOM   4780  C CA  . GLU B  1 88  ? -20.315 -20.015 2.763    1.00 32.73  ? 88  GLU B CA  1 
ATOM   4781  C C   . GLU B  1 88  ? -18.911 -20.406 2.349    1.00 29.83  ? 88  GLU B C   1 
ATOM   4782  O O   . GLU B  1 88  ? -18.569 -20.415 1.166    1.00 30.29  ? 88  GLU B O   1 
ATOM   4783  C CB  . GLU B  1 88  ? -21.158 -21.257 3.038    1.00 32.73  ? 88  GLU B CB  1 
ATOM   4784  C CG  . GLU B  1 88  ? -22.605 -20.929 3.259    1.00 38.08  ? 88  GLU B CG  1 
ATOM   4785  C CD  . GLU B  1 88  ? -23.502 -22.140 3.162    1.00 47.00  ? 88  GLU B CD  1 
ATOM   4786  O OE1 . GLU B  1 88  ? -24.722 -21.979 3.373    1.00 51.56  ? 88  GLU B OE1 1 
ATOM   4787  O OE2 . GLU B  1 88  ? -22.998 -23.250 2.881    1.00 48.44  ? 88  GLU B OE2 1 
ATOM   4788  N N   . LYS B  1 89  ? -18.073 -20.678 3.343    1.00 25.84  ? 89  LYS B N   1 
ATOM   4789  C CA  . LYS B  1 89  ? -16.733 -21.179 3.046    1.00 35.33  ? 89  LYS B CA  1 
ATOM   4790  C C   . LYS B  1 89  ? -16.779 -22.414 2.153    1.00 33.44  ? 89  LYS B C   1 
ATOM   4791  O O   . LYS B  1 89  ? -15.959 -22.554 1.241    1.00 33.66  ? 89  LYS B O   1 
ATOM   4792  C CB  . LYS B  1 89  ? -15.979 -21.492 4.343    1.00 30.24  ? 89  LYS B CB  1 
ATOM   4793  C CG  . LYS B  1 89  ? -15.726 -20.281 5.212    1.00 35.51  ? 89  LYS B CG  1 
ATOM   4794  C CD  . LYS B  1 89  ? -14.885 -20.678 6.436    1.00 38.54  ? 89  LYS B CD  1 
ATOM   4795  C CE  . LYS B  1 89  ? -14.626 -19.508 7.366    1.00 47.24  ? 89  LYS B CE  1 
ATOM   4796  N NZ  . LYS B  1 89  ? -15.777 -18.566 7.451    1.00 49.32  ? 89  LYS B NZ  1 
ATOM   4797  N N   . GLU B  1 90  ? -17.722 -23.327 2.411    1.00 32.34  ? 90  GLU B N   1 
ATOM   4798  C CA  . GLU B  1 90  ? -17.852 -24.520 1.576    1.00 37.65  ? 90  GLU B CA  1 
ATOM   4799  C C   . GLU B  1 90  ? -18.174 -24.152 0.130    1.00 37.74  ? 90  GLU B C   1 
ATOM   4800  O O   . GLU B  1 90  ? -17.730 -24.832 -0.806   1.00 34.85  ? 90  GLU B O   1 
ATOM   4801  C CB  . GLU B  1 90  ? -18.932 -25.447 2.144    1.00 45.36  ? 90  GLU B CB  1 
ATOM   4802  C CG  . GLU B  1 90  ? -20.336 -24.838 2.141    1.00 60.11  ? 90  GLU B CG  1 
ATOM   4803  C CD  . GLU B  1 90  ? -21.434 -25.858 1.845    1.00 75.14  ? 90  GLU B CD  1 
ATOM   4804  O OE1 . GLU B  1 90  ? -22.220 -25.640 0.885    1.00 75.32  ? 90  GLU B OE1 1 
ATOM   4805  O OE2 . GLU B  1 90  ? -21.524 -26.866 2.582    1.00 81.78  ? 90  GLU B OE2 1 
ATOM   4806  N N   . GLU B  1 91  ? -18.914 -23.063 -0.076   1.00 35.21  ? 91  GLU B N   1 
ATOM   4807  C CA  . GLU B  1 91  ? -19.270 -22.663 -1.431   1.00 29.50  ? 91  GLU B CA  1 
ATOM   4808  C C   . GLU B  1 91  ? -18.089 -22.012 -2.144   1.00 31.26  ? 91  GLU B C   1 
ATOM   4809  O O   . GLU B  1 91  ? -17.907 -22.215 -3.345   1.00 35.94  ? 91  GLU B O   1 
ATOM   4810  C CB  . GLU B  1 91  ? -20.481 -21.723 -1.395   1.00 34.54  ? 91  GLU B CB  1 
ATOM   4811  C CG  . GLU B  1 91  ? -21.757 -22.357 -0.808   1.00 35.71  ? 91  GLU B CG  1 
ATOM   4812  C CD  . GLU B  1 91  ? -22.960 -21.414 -0.817   1.00 36.90  ? 91  GLU B CD  1 
ATOM   4813  O OE1 . GLU B  1 91  ? -22.882 -20.315 -0.223   1.00 36.60  ? 91  GLU B OE1 1 
ATOM   4814  O OE2 . GLU B  1 91  ? -23.983 -21.762 -1.446   1.00 38.67  ? 91  GLU B OE2 1 
ATOM   4815  N N   . VAL B  1 92  ? -17.273 -21.230 -1.429   1.00 29.18  ? 92  VAL B N   1 
ATOM   4816  C CA  . VAL B  1 92  ? -16.045 -20.714 -2.029   1.00 31.15  ? 92  VAL B CA  1 
ATOM   4817  C C   . VAL B  1 92  ? -15.122 -21.864 -2.427   1.00 28.94  ? 92  VAL B C   1 
ATOM   4818  O O   . VAL B  1 92  ? -14.587 -21.897 -3.543   1.00 28.52  ? 92  VAL B O   1 
ATOM   4819  C CB  . VAL B  1 92  ? -15.346 -19.723 -1.080   1.00 31.48  ? 92  VAL B CB  1 
ATOM   4820  C CG1 . VAL B  1 92  ? -14.074 -19.189 -1.726   1.00 31.65  ? 92  VAL B CG1 1 
ATOM   4821  C CG2 . VAL B  1 92  ? -16.263 -18.571 -0.761   1.00 33.95  ? 92  VAL B CG2 1 
ATOM   4822  N N   . GLU B  1 93  ? -14.909 -22.821 -1.521   1.00 30.35  ? 93  GLU B N   1 
ATOM   4823  C CA  . GLU B  1 93  ? -14.055 -23.956 -1.868   1.00 32.34  ? 93  GLU B CA  1 
ATOM   4824  C C   . GLU B  1 93  ? -14.569 -24.667 -3.119   1.00 35.31  ? 93  GLU B C   1 
ATOM   4825  O O   . GLU B  1 93  ? -13.802 -24.922 -4.058   1.00 31.29  ? 93  GLU B O   1 
ATOM   4826  C CB  . GLU B  1 93  ? -13.956 -24.921 -0.689   1.00 37.34  ? 93  GLU B CB  1 
ATOM   4827  C CG  . GLU B  1 93  ? -12.908 -24.515 0.352    1.00 48.63  ? 93  GLU B CG  1 
ATOM   4828  C CD  . GLU B  1 93  ? -13.117 -25.201 1.700    1.00 58.45  ? 93  GLU B CD  1 
ATOM   4829  O OE1 . GLU B  1 93  ? -12.894 -24.556 2.748    1.00 61.33  ? 93  GLU B OE1 1 
ATOM   4830  O OE2 . GLU B  1 93  ? -13.506 -26.386 1.709    1.00 61.76  ? 93  GLU B OE2 1 
ATOM   4831  N N   . LYS B  1 94  ? -15.876 -24.944 -3.170   1.00 34.67  ? 94  LYS B N   1 
ATOM   4832  C CA  . LYS B  1 94  ? -16.447 -25.637 -4.318   1.00 33.00  ? 94  LYS B CA  1 
ATOM   4833  C C   . LYS B  1 94  ? -16.264 -24.840 -5.602   1.00 33.52  ? 94  LYS B C   1 
ATOM   4834  O O   . LYS B  1 94  ? -16.026 -25.420 -6.667   1.00 30.58  ? 94  LYS B O   1 
ATOM   4835  C CB  . LYS B  1 94  ? -17.923 -25.918 -4.072   1.00 39.58  ? 94  LYS B CB  1 
ATOM   4836  C CG  . LYS B  1 94  ? -18.154 -27.196 -3.274   1.00 48.71  ? 94  LYS B CG  1 
ATOM   4837  C CD  . LYS B  1 94  ? -19.612 -27.632 -3.302   1.00 53.12  ? 94  LYS B CD  1 
ATOM   4838  C CE  . LYS B  1 94  ? -19.838 -28.907 -2.485   1.00 60.56  ? 94  LYS B CE  1 
ATOM   4839  N NZ  . LYS B  1 94  ? -20.508 -29.973 -3.302   1.00 65.35  ? 94  LYS B NZ  1 
ATOM   4840  N N   . LEU B  1 95  ? -16.374 -23.507 -5.521   1.00 28.36  ? 95  LEU B N   1 
ATOM   4841  C CA  . LEU B  1 95  ? -16.186 -22.665 -6.698   1.00 31.31  ? 95  LEU B CA  1 
ATOM   4842  C C   . LEU B  1 95  ? -14.739 -22.694 -7.167   1.00 30.16  ? 95  LEU B C   1 
ATOM   4843  O O   . LEU B  1 95  ? -14.467 -22.768 -8.374   1.00 27.65  ? 95  LEU B O   1 
ATOM   4844  C CB  . LEU B  1 95  ? -16.617 -21.239 -6.375   1.00 38.24  ? 95  LEU B CB  1 
ATOM   4845  C CG  . LEU B  1 95  ? -16.570 -20.272 -7.544   1.00 51.02  ? 95  LEU B CG  1 
ATOM   4846  C CD1 . LEU B  1 95  ? -17.518 -20.754 -8.631   1.00 52.18  ? 95  LEU B CD1 1 
ATOM   4847  C CD2 . LEU B  1 95  ? -16.908 -18.856 -7.095   1.00 55.28  ? 95  LEU B CD2 1 
ATOM   4848  N N   . ILE B  1 96  ? -13.802 -22.629 -6.217   1.00 28.14  ? 96  ILE B N   1 
ATOM   4849  C CA  . ILE B  1 96  ? -12.381 -22.770 -6.523   1.00 34.86  ? 96  ILE B CA  1 
ATOM   4850  C C   . ILE B  1 96  ? -12.086 -24.143 -7.128   1.00 36.46  ? 96  ILE B C   1 
ATOM   4851  O O   . ILE B  1 96  ? -11.395 -24.252 -8.149   1.00 35.83  ? 96  ILE B O   1 
ATOM   4852  C CB  . ILE B  1 96  ? -11.540 -22.527 -5.257   1.00 33.43  ? 96  ILE B CB  1 
ATOM   4853  C CG1 . ILE B  1 96  ? -11.529 -21.039 -4.901   1.00 32.85  ? 96  ILE B CG1 1 
ATOM   4854  C CG2 . ILE B  1 96  ? -10.127 -23.077 -5.445   1.00 37.67  ? 96  ILE B CG2 1 
ATOM   4855  C CD1 . ILE B  1 96  ? -11.110 -20.751 -3.482   1.00 33.78  ? 96  ILE B CD1 1 
ATOM   4856  N N   . GLU B  1 97  ? -12.584 -25.216 -6.499   1.00 36.33  ? 97  GLU B N   1 
ATOM   4857  C CA  . GLU B  1 97  ? -12.337 -26.559 -7.033   1.00 37.19  ? 97  GLU B CA  1 
ATOM   4858  C C   . GLU B  1 97  ? -12.903 -26.707 -8.438   1.00 32.44  ? 97  GLU B C   1 
ATOM   4859  O O   . GLU B  1 97  ? -12.250 -27.275 -9.317   1.00 32.43  ? 97  GLU B O   1 
ATOM   4860  C CB  . GLU B  1 97  ? -12.925 -27.636 -6.107   1.00 50.18  ? 97  GLU B CB  1 
ATOM   4861  C CG  . GLU B  1 97  ? -12.529 -27.524 -4.631   1.00 62.50  ? 97  GLU B CG  1 
ATOM   4862  C CD  . GLU B  1 97  ? -13.496 -28.259 -3.694   1.00 72.78  ? 97  GLU B CD  1 
ATOM   4863  O OE1 . GLU B  1 97  ? -13.317 -28.173 -2.455   1.00 70.23  ? 97  GLU B OE1 1 
ATOM   4864  O OE2 . GLU B  1 97  ? -14.436 -28.915 -4.198   1.00 76.63  ? 97  GLU B OE2 1 
ATOM   4865  N N   . PHE B  1 98  ? -14.113 -26.202 -8.667   1.00 29.50  ? 98  PHE B N   1 
ATOM   4866  C CA  . PHE B  1 98  ? -14.701 -26.270 -10.001  1.00 31.27  ? 98  PHE B CA  1 
ATOM   4867  C C   . PHE B  1 98  ? -13.835 -25.542 -11.025  1.00 31.35  ? 98  PHE B C   1 
ATOM   4868  O O   . PHE B  1 98  ? -13.569 -26.065 -12.116  1.00 33.63  ? 98  PHE B O   1 
ATOM   4869  C CB  . PHE B  1 98  ? -16.101 -25.673 -9.956   1.00 30.79  ? 98  PHE B CB  1 
ATOM   4870  C CG  . PHE B  1 98  ? -16.930 -25.937 -11.176  1.00 28.40  ? 98  PHE B CG  1 
ATOM   4871  C CD1 . PHE B  1 98  ? -17.608 -27.137 -11.325  1.00 34.57  ? 98  PHE B CD1 1 
ATOM   4872  C CD2 . PHE B  1 98  ? -17.055 -24.973 -12.151  1.00 33.32  ? 98  PHE B CD2 1 
ATOM   4873  C CE1 . PHE B  1 98  ? -18.381 -27.378 -12.462  1.00 38.01  ? 98  PHE B CE1 1 
ATOM   4874  C CE2 . PHE B  1 98  ? -17.823 -25.200 -13.280  1.00 35.33  ? 98  PHE B CE2 1 
ATOM   4875  C CZ  . PHE B  1 98  ? -18.485 -26.406 -13.435  1.00 35.08  ? 98  PHE B CZ  1 
ATOM   4876  N N   . THR B  1 99  ? -13.380 -24.335 -10.683  1.00 27.08  ? 99  THR B N   1 
ATOM   4877  C CA  . THR B  1 99  ? -12.510 -23.576 -11.576  1.00 32.77  ? 99  THR B CA  1 
ATOM   4878  C C   . THR B  1 99  ? -11.243 -24.352 -11.912  1.00 35.08  ? 99  THR B C   1 
ATOM   4879  O O   . THR B  1 99  ? -10.859 -24.464 -13.084  1.00 37.16  ? 99  THR B O   1 
ATOM   4880  C CB  . THR B  1 99  ? -12.160 -22.232 -10.939  1.00 34.14  ? 99  THR B CB  1 
ATOM   4881  O OG1 . THR B  1 99  ? -13.366 -21.507 -10.677  1.00 32.30  ? 99  THR B OG1 1 
ATOM   4882  C CG2 . THR B  1 99  ? -11.246 -21.425 -11.872  1.00 34.07  ? 99  THR B CG2 1 
ATOM   4883  N N   . LYS B  1 100 ? -10.575 -24.896 -10.890  1.00 32.42  ? 100 LYS B N   1 
ATOM   4884  C CA  . LYS B  1 100 ? -9.371  -25.686 -11.123  1.00 36.16  ? 100 LYS B CA  1 
ATOM   4885  C C   . LYS B  1 100 ? -9.654  -26.905 -11.990  1.00 35.10  ? 100 LYS B C   1 
ATOM   4886  O O   . LYS B  1 100 ? -8.787  -27.336 -12.762  1.00 30.71  ? 100 LYS B O   1 
ATOM   4887  C CB  . LYS B  1 100 ? -8.770  -26.133 -9.791   1.00 38.68  ? 100 LYS B CB  1 
ATOM   4888  C CG  . LYS B  1 100 ? -7.755  -25.177 -9.221   1.00 45.87  ? 100 LYS B CG  1 
ATOM   4889  C CD  . LYS B  1 100 ? -7.332  -25.597 -7.824   1.00 49.10  ? 100 LYS B CD  1 
ATOM   4890  C CE  . LYS B  1 100 ? -6.305  -24.634 -7.264   1.00 52.24  ? 100 LYS B CE  1 
ATOM   4891  N NZ  . LYS B  1 100 ? -6.278  -24.683 -5.777   1.00 50.24  ? 100 LYS B NZ  1 
ATOM   4892  N N   . LEU B  1 101 ? -10.840 -27.500 -11.851  1.00 32.51  ? 101 LEU B N   1 
ATOM   4893  C CA  . LEU B  1 101 ? -11.177 -28.650 -12.682  1.00 33.55  ? 101 LEU B CA  1 
ATOM   4894  C C   . LEU B  1 101 ? -11.231 -28.270 -14.155  1.00 28.56  ? 101 LEU B C   1 
ATOM   4895  O O   . LEU B  1 101 ? -10.847 -29.065 -15.016  1.00 28.35  ? 101 LEU B O   1 
ATOM   4896  C CB  . LEU B  1 101 ? -12.514 -29.238 -12.239  1.00 34.23  ? 101 LEU B CB  1 
ATOM   4897  C CG  . LEU B  1 101 ? -13.151 -30.342 -13.075  1.00 35.40  ? 101 LEU B CG  1 
ATOM   4898  C CD1 . LEU B  1 101 ? -12.310 -31.614 -13.008  1.00 38.41  ? 101 LEU B CD1 1 
ATOM   4899  C CD2 . LEU B  1 101 ? -14.562 -30.591 -12.562  1.00 33.16  ? 101 LEU B CD2 1 
ATOM   4900  N N   . ASN B  1 102 ? -11.693 -27.054 -14.462  1.00 28.61  ? 102 ASN B N   1 
ATOM   4901  C CA  . ASN B  1 102 ? -11.941 -26.612 -15.835  1.00 29.38  ? 102 ASN B CA  1 
ATOM   4902  C C   . ASN B  1 102 ? -10.857 -25.692 -16.379  1.00 32.11  ? 102 ASN B C   1 
ATOM   4903  O O   . ASN B  1 102 ? -10.910 -25.314 -17.561  1.00 26.36  ? 102 ASN B O   1 
ATOM   4904  C CB  . ASN B  1 102 ? -13.285 -25.896 -15.916  1.00 30.15  ? 102 ASN B CB  1 
ATOM   4905  C CG  . ASN B  1 102 ? -14.445 -26.822 -15.675  1.00 33.67  ? 102 ASN B CG  1 
ATOM   4906  O OD1 . ASN B  1 102 ? -14.661 -27.764 -16.443  1.00 34.73  ? 102 ASN B OD1 1 
ATOM   4907  N ND2 . ASN B  1 102 ? -15.199 -26.573 -14.606  1.00 24.95  ? 102 ASN B ND2 1 
ATOM   4908  N N   . TYR B  1 103 ? -9.846  -25.412 -15.558  1.00 29.76  ? 103 TYR B N   1 
ATOM   4909  C CA  . TYR B  1 103 ? -8.949  -24.273 -15.730  1.00 36.21  ? 103 TYR B CA  1 
ATOM   4910  C C   . TYR B  1 103 ? -8.214  -24.295 -17.067  1.00 34.87  ? 103 TYR B C   1 
ATOM   4911  O O   . TYR B  1 103 ? -7.903  -23.235 -17.628  1.00 35.83  ? 103 TYR B O   1 
ATOM   4912  C CB  . TYR B  1 103 ? -7.951  -24.279 -14.568  1.00 37.64  ? 103 TYR B CB  1 
ATOM   4913  C CG  . TYR B  1 103 ? -6.841  -23.281 -14.661  1.00 40.48  ? 103 TYR B CG  1 
ATOM   4914  C CD1 . TYR B  1 103 ? -7.028  -21.963 -14.270  1.00 46.44  ? 103 TYR B CD1 1 
ATOM   4915  C CD2 . TYR B  1 103 ? -5.596  -23.657 -15.125  1.00 46.50  ? 103 TYR B CD2 1 
ATOM   4916  C CE1 . TYR B  1 103 ? -5.992  -21.044 -14.348  1.00 50.42  ? 103 TYR B CE1 1 
ATOM   4917  C CE2 . TYR B  1 103 ? -4.563  -22.754 -15.210  1.00 52.61  ? 103 TYR B CE2 1 
ATOM   4918  C CZ  . TYR B  1 103 ? -4.762  -21.454 -14.820  1.00 55.11  ? 103 TYR B CZ  1 
ATOM   4919  O OH  . TYR B  1 103 ? -3.717  -20.570 -14.911  1.00 64.43  ? 103 TYR B OH  1 
ATOM   4920  N N   . GLU B  1 104 ? -7.874  -25.479 -17.560  1.00 32.65  ? 104 GLU B N   1 
ATOM   4921  C CA  . GLU B  1 104 ? -7.042  -25.590 -18.747  1.00 36.93  ? 104 GLU B CA  1 
ATOM   4922  C C   . GLU B  1 104 ? -7.855  -25.683 -20.027  1.00 34.72  ? 104 GLU B C   1 
ATOM   4923  O O   . GLU B  1 104 ? -7.268  -25.702 -21.108  1.00 35.43  ? 104 GLU B O   1 
ATOM   4924  C CB  . GLU B  1 104 ? -6.121  -26.801 -18.632  1.00 41.63  ? 104 GLU B CB  1 
ATOM   4925  C CG  . GLU B  1 104 ? -5.280  -26.819 -17.379  1.00 52.35  ? 104 GLU B CG  1 
ATOM   4926  C CD  . GLU B  1 104 ? -4.139  -25.824 -17.434  1.00 62.87  ? 104 GLU B CD  1 
ATOM   4927  O OE1 . GLU B  1 104 ? -3.757  -25.410 -18.549  1.00 66.52  ? 104 GLU B OE1 1 
ATOM   4928  O OE2 . GLU B  1 104 ? -3.611  -25.472 -16.361  1.00 67.79  ? 104 GLU B OE2 1 
ATOM   4929  N N   . LYS B  1 105 ? -9.181  -25.732 -19.924  1.00 30.92  ? 105 LYS B N   1 
ATOM   4930  C CA  . LYS B  1 105 ? -10.031 -25.780 -21.105  1.00 30.86  ? 105 LYS B CA  1 
ATOM   4931  C C   . LYS B  1 105 ? -10.007 -24.430 -21.819  1.00 29.95  ? 105 LYS B C   1 
ATOM   4932  O O   . LYS B  1 105 ? -9.981  -23.386 -21.162  1.00 34.30  ? 105 LYS B O   1 
ATOM   4933  C CB  . LYS B  1 105 ? -11.463 -26.157 -20.705  1.00 27.07  ? 105 LYS B CB  1 
ATOM   4934  C CG  . LYS B  1 105 ? -11.536 -27.533 -20.073  1.00 26.77  ? 105 LYS B CG  1 
ATOM   4935  C CD  . LYS B  1 105 ? -12.920 -27.910 -19.587  1.00 25.74  ? 105 LYS B CD  1 
ATOM   4936  C CE  . LYS B  1 105 ? -12.885 -29.268 -18.917  1.00 29.86  ? 105 LYS B CE  1 
ATOM   4937  N NZ  . LYS B  1 105 ? -14.253 -29.712 -18.512  1.00 30.97  ? 105 LYS B NZ  1 
ATOM   4938  N N   . PRO B  1 106 ? -9.987  -24.418 -23.155  1.00 32.03  ? 106 PRO B N   1 
ATOM   4939  C CA  . PRO B  1 106 ? -9.966  -23.133 -23.872  1.00 28.14  ? 106 PRO B CA  1 
ATOM   4940  C C   . PRO B  1 106 ? -11.109 -22.209 -23.513  1.00 26.48  ? 106 PRO B C   1 
ATOM   4941  O O   . PRO B  1 106 ? -10.923 -20.986 -23.519  1.00 26.62  ? 106 PRO B O   1 
ATOM   4942  C CB  . PRO B  1 106 ? -10.031 -23.558 -25.348  1.00 33.21  ? 106 PRO B CB  1 
ATOM   4943  C CG  . PRO B  1 106 ? -9.385  -24.877 -25.372  1.00 34.00  ? 106 PRO B CG  1 
ATOM   4944  C CD  . PRO B  1 106 ? -9.791  -25.556 -24.071  1.00 31.42  ? 106 PRO B CD  1 
ATOM   4945  N N   . ILE B  1 107 ? -12.294 -22.740 -23.208  1.00 27.23  ? 107 ILE B N   1 
ATOM   4946  C CA  . ILE B  1 107 ? -13.395 -21.869 -22.814  1.00 30.41  ? 107 ILE B CA  1 
ATOM   4947  C C   . ILE B  1 107 ? -13.151 -21.165 -21.485  1.00 34.02  ? 107 ILE B C   1 
ATOM   4948  O O   . ILE B  1 107 ? -13.869 -20.209 -21.160  1.00 30.22  ? 107 ILE B O   1 
ATOM   4949  C CB  . ILE B  1 107 ? -14.713 -22.669 -22.776  1.00 30.99  ? 107 ILE B CB  1 
ATOM   4950  C CG1 . ILE B  1 107 ? -14.632 -23.804 -21.762  1.00 23.31  ? 107 ILE B CG1 1 
ATOM   4951  C CG2 . ILE B  1 107 ? -15.032 -23.223 -24.193  1.00 24.24  ? 107 ILE B CG2 1 
ATOM   4952  C CD1 . ILE B  1 107 ? -16.004 -24.343 -21.360  1.00 27.12  ? 107 ILE B CD1 1 
ATOM   4953  N N   . TYR B  1 108 ? -12.153 -21.595 -20.713  1.00 34.02  ? 108 TYR B N   1 
ATOM   4954  C CA  . TYR B  1 108 ? -11.759 -20.901 -19.492  1.00 33.78  ? 108 TYR B CA  1 
ATOM   4955  C C   . TYR B  1 108 ? -10.535 -20.014 -19.688  1.00 37.67  ? 108 TYR B C   1 
ATOM   4956  O O   . TYR B  1 108 ? -9.983  -19.510 -18.705  1.00 39.29  ? 108 TYR B O   1 
ATOM   4957  C CB  . TYR B  1 108 ? -11.506 -21.912 -18.378  1.00 24.99  ? 108 TYR B CB  1 
ATOM   4958  C CG  . TYR B  1 108 ? -12.734 -22.202 -17.567  1.00 27.14  ? 108 TYR B CG  1 
ATOM   4959  C CD1 . TYR B  1 108 ? -13.784 -22.936 -18.107  1.00 29.14  ? 108 TYR B CD1 1 
ATOM   4960  C CD2 . TYR B  1 108 ? -12.840 -21.767 -16.249  1.00 28.03  ? 108 TYR B CD2 1 
ATOM   4961  C CE1 . TYR B  1 108 ? -14.911 -23.214 -17.371  1.00 28.52  ? 108 TYR B CE1 1 
ATOM   4962  C CE2 . TYR B  1 108 ? -13.962 -22.046 -15.498  1.00 27.33  ? 108 TYR B CE2 1 
ATOM   4963  C CZ  . TYR B  1 108 ? -14.994 -22.762 -16.070  1.00 30.92  ? 108 TYR B CZ  1 
ATOM   4964  O OH  . TYR B  1 108 ? -16.115 -23.050 -15.343  1.00 32.06  ? 108 TYR B OH  1 
ATOM   4965  N N   . ARG B  1 109 ? -10.104 -19.795 -20.934  1.00 41.14  ? 109 ARG B N   1 
ATOM   4966  C CA  . ARG B  1 109 ? -8.930  -18.964 -21.214  1.00 44.87  ? 109 ARG B CA  1 
ATOM   4967  C C   . ARG B  1 109 ? -9.279  -17.499 -20.964  1.00 42.98  ? 109 ARG B C   1 
ATOM   4968  O O   . ARG B  1 109 ? -9.597  -16.728 -21.872  1.00 40.50  ? 109 ARG B O   1 
ATOM   4969  C CB  . ARG B  1 109 ? -8.419  -19.171 -22.635  1.00 49.82  ? 109 ARG B CB  1 
ATOM   4970  C CG  . ARG B  1 109 ? -7.160  -18.361 -22.940  1.00 59.25  ? 109 ARG B CG  1 
ATOM   4971  C CD  . ARG B  1 109 ? -6.082  -19.196 -23.604  1.00 66.50  ? 109 ARG B CD  1 
ATOM   4972  N NE  . ARG B  1 109 ? -6.518  -19.749 -24.883  1.00 68.68  ? 109 ARG B NE  1 
ATOM   4973  C CZ  . ARG B  1 109 ? -6.584  -21.050 -25.153  1.00 68.08  ? 109 ARG B CZ  1 
ATOM   4974  N NH1 . ARG B  1 109 ? -6.247  -21.944 -24.233  1.00 71.37  ? 109 ARG B NH1 1 
ATOM   4975  N NH2 . ARG B  1 109 ? -6.987  -21.459 -26.344  1.00 66.73  ? 109 ARG B NH2 1 
ATOM   4976  N N   . PHE B  1 110 ? -9.212  -17.117 -19.691  1.00 38.25  ? 110 PHE B N   1 
ATOM   4977  C CA  . PHE B  1 110 ? -9.409  -15.742 -19.252  1.00 34.95  ? 110 PHE B CA  1 
ATOM   4978  C C   . PHE B  1 110 ? -8.232  -15.350 -18.376  1.00 39.04  ? 110 PHE B C   1 
ATOM   4979  O O   . PHE B  1 110 ? -7.972  -16.003 -17.354  1.00 36.18  ? 110 PHE B O   1 
ATOM   4980  C CB  . PHE B  1 110 ? -10.694 -15.577 -18.446  1.00 29.23  ? 110 PHE B CB  1 
ATOM   4981  C CG  . PHE B  1 110 ? -11.962 -15.675 -19.252  1.00 31.17  ? 110 PHE B CG  1 
ATOM   4982  C CD1 . PHE B  1 110 ? -12.463 -14.570 -19.917  1.00 30.80  ? 110 PHE B CD1 1 
ATOM   4983  C CD2 . PHE B  1 110 ? -12.699 -16.854 -19.263  1.00 34.11  ? 110 PHE B CD2 1 
ATOM   4984  C CE1 . PHE B  1 110 ? -13.658 -14.651 -20.607  1.00 36.57  ? 110 PHE B CE1 1 
ATOM   4985  C CE2 . PHE B  1 110 ? -13.893 -16.946 -19.951  1.00 32.60  ? 110 PHE B CE2 1 
ATOM   4986  C CZ  . PHE B  1 110 ? -14.377 -15.851 -20.619  1.00 34.72  ? 110 PHE B CZ  1 
ATOM   4987  N N   . GLU B  1 111 ? -7.541  -14.275 -18.767  1.00 39.66  ? 111 GLU B N   1 
ATOM   4988  C CA  . GLU B  1 111 ? -6.436  -13.757 -17.966  1.00 43.93  ? 111 GLU B CA  1 
ATOM   4989  C C   . GLU B  1 111 ? -6.846  -13.525 -16.513  1.00 43.39  ? 111 GLU B C   1 
ATOM   4990  O O   . GLU B  1 111 ? -6.045  -13.744 -15.596  1.00 48.67  ? 111 GLU B O   1 
ATOM   4991  C CB  . GLU B  1 111 ? -5.905  -12.467 -18.598  1.00 48.79  ? 111 GLU B CB  1 
ATOM   4992  C CG  . GLU B  1 111 ? -4.907  -11.715 -17.750  1.00 60.44  ? 111 GLU B CG  1 
ATOM   4993  C CD  . GLU B  1 111 ? -3.632  -12.504 -17.521  1.00 71.27  ? 111 GLU B CD  1 
ATOM   4994  O OE1 . GLU B  1 111 ? -3.290  -13.343 -18.385  1.00 75.51  ? 111 GLU B OE1 1 
ATOM   4995  O OE2 . GLU B  1 111 ? -2.970  -12.283 -16.481  1.00 73.98  ? 111 GLU B OE2 1 
ATOM   4996  N N   . ARG B  1 112 ? -8.089  -13.116 -16.274  1.00 38.81  ? 112 ARG B N   1 
ATOM   4997  C CA  . ARG B  1 112 ? -8.514  -12.871 -14.899  1.00 37.80  ? 112 ARG B CA  1 
ATOM   4998  C C   . ARG B  1 112 ? -8.562  -14.164 -14.090  1.00 33.97  ? 112 ARG B C   1 
ATOM   4999  O O   . ARG B  1 112 ? -8.216  -14.172 -12.904  1.00 37.34  ? 112 ARG B O   1 
ATOM   5000  C CB  . ARG B  1 112 ? -9.871  -12.175 -14.888  1.00 37.96  ? 112 ARG B CB  1 
ATOM   5001  C CG  . ARG B  1 112 ? -10.406 -11.835 -13.496  1.00 42.50  ? 112 ARG B CG  1 
ATOM   5002  C CD  . ARG B  1 112 ? -9.547  -10.824 -12.770  1.00 44.03  ? 112 ARG B CD  1 
ATOM   5003  N NE  . ARG B  1 112 ? -10.334 -10.097 -11.776  1.00 44.19  ? 112 ARG B NE  1 
ATOM   5004  C CZ  . ARG B  1 112 ? -9.835  -9.575  -10.661  1.00 45.03  ? 112 ARG B CZ  1 
ATOM   5005  N NH1 . ARG B  1 112 ? -8.545  -9.691  -10.398  1.00 47.28  ? 112 ARG B NH1 1 
ATOM   5006  N NH2 . ARG B  1 112 ? -10.629 -8.941  -9.810   1.00 45.96  ? 112 ARG B NH2 1 
ATOM   5007  N N   . ILE B  1 113 ? -8.986  -15.269 -14.706  1.00 36.02  ? 113 ILE B N   1 
ATOM   5008  C CA  . ILE B  1 113 ? -9.015  -16.541 -13.987  1.00 36.75  ? 113 ILE B CA  1 
ATOM   5009  C C   . ILE B  1 113 ? -7.606  -16.949 -13.577  1.00 39.16  ? 113 ILE B C   1 
ATOM   5010  O O   . ILE B  1 113 ? -7.394  -17.514 -12.496  1.00 36.76  ? 113 ILE B O   1 
ATOM   5011  C CB  . ILE B  1 113 ? -9.700  -17.625 -14.837  1.00 39.46  ? 113 ILE B CB  1 
ATOM   5012  C CG1 . ILE B  1 113 ? -11.188 -17.326 -14.961  1.00 39.46  ? 113 ILE B CG1 1 
ATOM   5013  C CG2 . ILE B  1 113 ? -9.515  -19.006 -14.214  1.00 41.31  ? 113 ILE B CG2 1 
ATOM   5014  C CD1 . ILE B  1 113 ? -11.837 -18.058 -16.092  1.00 40.88  ? 113 ILE B CD1 1 
ATOM   5015  N N   . ARG B  1 114 ? -6.616  -16.646 -14.417  1.00 42.67  ? 114 ARG B N   1 
ATOM   5016  C CA  . ARG B  1 114 ? -5.236  -16.948 -14.050  1.00 47.60  ? 114 ARG B CA  1 
ATOM   5017  C C   . ARG B  1 114 ? -4.827  -16.170 -12.807  1.00 50.32  ? 114 ARG B C   1 
ATOM   5018  O O   . ARG B  1 114 ? -4.215  -16.726 -11.886  1.00 53.74  ? 114 ARG B O   1 
ATOM   5019  C CB  . ARG B  1 114 ? -4.304  -16.643 -15.226  1.00 53.07  ? 114 ARG B CB  1 
ATOM   5020  C CG  . ARG B  1 114 ? -2.819  -16.539 -14.868  1.00 61.83  ? 114 ARG B CG  1 
ATOM   5021  C CD  . ARG B  1 114 ? -2.239  -17.894 -14.469  1.00 66.83  ? 114 ARG B CD  1 
ATOM   5022  N NE  . ARG B  1 114 ? -0.890  -17.808 -13.910  1.00 70.95  ? 114 ARG B NE  1 
ATOM   5023  C CZ  . ARG B  1 114 ? 0.139   -18.555 -14.310  1.00 71.30  ? 114 ARG B CZ  1 
ATOM   5024  N NH1 . ARG B  1 114 ? -0.019  -19.451 -15.278  1.00 68.77  ? 114 ARG B NH1 1 
ATOM   5025  N NH2 . ARG B  1 114 ? 1.329   -18.411 -13.735  1.00 72.55  ? 114 ARG B NH2 1 
ATOM   5026  N N   . GLU B  1 115 ? -5.192  -14.888 -12.747  1.00 47.30  ? 115 GLU B N   1 
ATOM   5027  C CA  . GLU B  1 115 ? -4.865  -14.080 -11.578  1.00 47.12  ? 115 GLU B CA  1 
ATOM   5028  C C   . GLU B  1 115 ? -5.620  -14.541 -10.343  1.00 45.22  ? 115 GLU B C   1 
ATOM   5029  O O   . GLU B  1 115 ? -5.043  -14.607 -9.251   1.00 48.64  ? 115 GLU B O   1 
ATOM   5030  C CB  . GLU B  1 115 ? -5.180  -12.617 -11.846  1.00 47.13  ? 115 GLU B CB  1 
ATOM   5031  C CG  . GLU B  1 115 ? -4.575  -12.098 -13.092  1.00 51.18  ? 115 GLU B CG  1 
ATOM   5032  C CD  . GLU B  1 115 ? -5.138  -10.757 -13.439  1.00 53.61  ? 115 GLU B CD  1 
ATOM   5033  O OE1 . GLU B  1 115 ? -5.823  -10.176 -12.572  1.00 54.40  ? 115 GLU B OE1 1 
ATOM   5034  O OE2 . GLU B  1 115 ? -4.902  -10.284 -14.569  1.00 54.59  ? 115 GLU B OE2 1 
ATOM   5035  N N   . LEU B  1 116 ? -6.917  -14.829 -10.488  1.00 42.88  ? 116 LEU B N   1 
ATOM   5036  C CA  . LEU B  1 116 ? -7.722  -15.202 -9.330   1.00 39.47  ? 116 LEU B CA  1 
ATOM   5037  C C   . LEU B  1 116 ? -7.189  -16.471 -8.684   1.00 45.77  ? 116 LEU B C   1 
ATOM   5038  O O   . LEU B  1 116 ? -7.135  -16.574 -7.456   1.00 43.27  ? 116 LEU B O   1 
ATOM   5039  C CB  . LEU B  1 116 ? -9.186  -15.376 -9.734   1.00 35.24  ? 116 LEU B CB  1 
ATOM   5040  C CG  . LEU B  1 116 ? -9.937  -14.102 -10.127  1.00 37.46  ? 116 LEU B CG  1 
ATOM   5041  C CD1 . LEU B  1 116 ? -11.269 -14.396 -10.795  1.00 38.32  ? 116 LEU B CD1 1 
ATOM   5042  C CD2 . LEU B  1 116 ? -10.164 -13.265 -8.912   1.00 37.20  ? 116 LEU B CD2 1 
ATOM   5043  N N   . MET B  1 117 ? -6.777  -17.446 -9.498   1.00 50.27  ? 117 MET B N   1 
ATOM   5044  C CA  . MET B  1 117 ? -6.217  -18.674 -8.946   1.00 52.62  ? 117 MET B CA  1 
ATOM   5045  C C   . MET B  1 117 ? -4.819  -18.481 -8.370   1.00 56.47  ? 117 MET B C   1 
ATOM   5046  O O   . MET B  1 117 ? -4.312  -19.392 -7.704   1.00 59.58  ? 117 MET B O   1 
ATOM   5047  C CB  . MET B  1 117 ? -6.210  -19.765 -10.018  1.00 54.34  ? 117 MET B CB  1 
ATOM   5048  C CG  . MET B  1 117 ? -7.601  -20.273 -10.381  1.00 54.08  ? 117 MET B CG  1 
ATOM   5049  S SD  . MET B  1 117 ? -8.718  -20.292 -8.954   1.00 56.39  ? 117 MET B SD  1 
ATOM   5050  C CE  . MET B  1 117 ? -9.195  -22.009 -8.899   1.00 56.75  ? 117 MET B CE  1 
ATOM   5051  N N   . ASN B  1 118 ? -4.203  -17.318 -8.583   1.00 56.18  ? 118 ASN B N   1 
ATOM   5052  C CA  . ASN B  1 118 ? -2.861  -17.029 -8.095   1.00 59.20  ? 118 ASN B CA  1 
ATOM   5053  C C   . ASN B  1 118 ? -2.853  -16.318 -6.748   1.00 56.38  ? 118 ASN B C   1 
ATOM   5054  O O   . ASN B  1 118 ? -1.775  -16.017 -6.228   1.00 57.95  ? 118 ASN B O   1 
ATOM   5055  C CB  . ASN B  1 118 ? -2.098  -16.179 -9.119   1.00 67.34  ? 118 ASN B CB  1 
ATOM   5056  C CG  . ASN B  1 118 ? -1.323  -17.023 -10.128  1.00 74.61  ? 118 ASN B CG  1 
ATOM   5057  O OD1 . ASN B  1 118 ? -1.468  -16.855 -11.344  1.00 77.86  ? 118 ASN B OD1 1 
ATOM   5058  N ND2 . ASN B  1 118 ? -0.490  -17.930 -9.625   1.00 74.61  ? 118 ASN B ND2 1 
ATOM   5059  N N   . LYS B  1 119 ? -4.012  -16.051 -6.161   1.00 53.09  ? 119 LYS B N   1 
ATOM   5060  C CA  . LYS B  1 119 ? -4.094  -15.285 -4.927   1.00 54.77  ? 119 LYS B CA  1 
ATOM   5061  C C   . LYS B  1 119 ? -4.445  -16.185 -3.750   1.00 56.28  ? 119 LYS B C   1 
ATOM   5062  O O   . LYS B  1 119 ? -5.240  -17.120 -3.883   1.00 56.49  ? 119 LYS B O   1 
ATOM   5063  C CB  . LYS B  1 119 ? -5.119  -14.169 -5.069   1.00 53.09  ? 119 LYS B CB  1 
ATOM   5064  C CG  . LYS B  1 119 ? -4.679  -13.123 -6.064   1.00 57.03  ? 119 LYS B CG  1 
ATOM   5065  C CD  . LYS B  1 119 ? -5.730  -12.063 -6.165   1.00 56.67  ? 119 LYS B CD  1 
ATOM   5066  C CE  . LYS B  1 119 ? -6.964  -12.629 -6.807   1.00 58.00  ? 119 LYS B CE  1 
ATOM   5067  N NZ  . LYS B  1 119 ? -7.087  -12.196 -8.218   1.00 61.77  ? 119 LYS B NZ  1 
ATOM   5068  N N   . GLU B  1 120 ? -3.845  -15.895 -2.591   1.00 56.78  ? 120 GLU B N   1 
ATOM   5069  C CA  . GLU B  1 120 ? -4.062  -16.746 -1.425   1.00 53.91  ? 120 GLU B CA  1 
ATOM   5070  C C   . GLU B  1 120 ? -5.467  -16.562 -0.864   1.00 53.21  ? 120 GLU B C   1 
ATOM   5071  O O   . GLU B  1 120 ? -6.128  -17.545 -0.508   1.00 55.84  ? 120 GLU B O   1 
ATOM   5072  C CB  . GLU B  1 120 ? -3.003  -16.462 -0.360   1.00 54.23  ? 120 GLU B CB  1 
ATOM   5073  N N   . LYS B  1 121 ? -5.943  -15.316 -0.792   1.00 50.41  ? 121 LYS B N   1 
ATOM   5074  C CA  . LYS B  1 121 ? -7.300  -15.003 -0.363   1.00 47.40  ? 121 LYS B CA  1 
ATOM   5075  C C   . LYS B  1 121 ? -7.991  -14.160 -1.428   1.00 50.41  ? 121 LYS B C   1 
ATOM   5076  O O   . LYS B  1 121 ? -7.345  -13.495 -2.241   1.00 53.94  ? 121 LYS B O   1 
ATOM   5077  C CB  . LYS B  1 121 ? -7.318  -14.259 0.977    1.00 44.76  ? 121 LYS B CB  1 
ATOM   5078  N N   . LEU B  1 122 ? -9.322  -14.186 -1.411   1.00 47.31  ? 122 LEU B N   1 
ATOM   5079  C CA  . LEU B  1 122 ? -10.143 -13.520 -2.417   1.00 43.57  ? 122 LEU B CA  1 
ATOM   5080  C C   . LEU B  1 122 ? -11.124 -12.571 -1.743   1.00 41.71  ? 122 LEU B C   1 
ATOM   5081  O O   . LEU B  1 122 ? -11.874 -12.981 -0.852   1.00 43.41  ? 122 LEU B O   1 
ATOM   5082  C CB  . LEU B  1 122 ? -10.913 -14.543 -3.259   1.00 39.15  ? 122 LEU B CB  1 
ATOM   5083  C CG  . LEU B  1 122 ? -10.101 -15.491 -4.137   1.00 40.78  ? 122 LEU B CG  1 
ATOM   5084  C CD1 . LEU B  1 122 ? -11.012 -16.480 -4.864   1.00 38.18  ? 122 LEU B CD1 1 
ATOM   5085  C CD2 . LEU B  1 122 ? -9.293  -14.679 -5.109   1.00 35.97  ? 122 LEU B CD2 1 
ATOM   5086  N N   . ASN B  1 123 ? -11.143 -11.315 -2.186   1.00 39.62  ? 123 ASN B N   1 
ATOM   5087  C CA  . ASN B  1 123 ? -12.088 -10.343 -1.652   1.00 37.82  ? 123 ASN B CA  1 
ATOM   5088  C C   . ASN B  1 123 ? -13.420 -10.438 -2.401   1.00 33.46  ? 123 ASN B C   1 
ATOM   5089  O O   . ASN B  1 123 ? -13.627 -11.308 -3.251   1.00 36.20  ? 123 ASN B O   1 
ATOM   5090  C CB  . ASN B  1 123 ? -11.496 -8.928  -1.688   1.00 33.71  ? 123 ASN B CB  1 
ATOM   5091  C CG  . ASN B  1 123 ? -11.225 -8.420  -3.110   1.00 36.18  ? 123 ASN B CG  1 
ATOM   5092  O OD1 . ASN B  1 123 ? -12.000 -8.663  -4.037   1.00 34.35  ? 123 ASN B OD1 1 
ATOM   5093  N ND2 . ASN B  1 123 ? -10.126 -7.683  -3.269   1.00 36.11  ? 123 ASN B ND2 1 
ATOM   5094  N N   . ARG B  1 124 ? -14.348 -9.529  -2.095   1.00 32.18  ? 124 ARG B N   1 
ATOM   5095  C CA  . ARG B  1 124 ? -15.676 -9.607  -2.692   1.00 31.78  ? 124 ARG B CA  1 
ATOM   5096  C C   . ARG B  1 124 ? -15.640 -9.355  -4.202   1.00 37.36  ? 124 ARG B C   1 
ATOM   5097  O O   . ARG B  1 124 ? -16.366 -10.014 -4.955   1.00 34.12  ? 124 ARG B O   1 
ATOM   5098  C CB  . ARG B  1 124 ? -16.615 -8.615  -2.013   1.00 36.40  ? 124 ARG B CB  1 
ATOM   5099  C CG  . ARG B  1 124 ? -18.045 -8.687  -2.529   1.00 37.18  ? 124 ARG B CG  1 
ATOM   5100  C CD  . ARG B  1 124 ? -18.851 -7.465  -2.114   1.00 42.56  ? 124 ARG B CD  1 
ATOM   5101  N NE  . ARG B  1 124 ? -20.189 -7.478  -2.697   1.00 42.63  ? 124 ARG B NE  1 
ATOM   5102  C CZ  . ARG B  1 124 ? -20.485 -6.954  -3.884   1.00 47.24  ? 124 ARG B CZ  1 
ATOM   5103  N NH1 . ARG B  1 124 ? -19.541 -6.376  -4.619   1.00 42.69  ? 124 ARG B NH1 1 
ATOM   5104  N NH2 . ARG B  1 124 ? -21.726 -7.014  -4.338   1.00 49.14  ? 124 ARG B NH2 1 
ATOM   5105  N N   . GLU B  1 125 ? -14.828 -8.392  -4.659   1.00 39.71  ? 125 GLU B N   1 
ATOM   5106  C CA  . GLU B  1 125 ? -14.749 -8.094  -6.092   1.00 43.11  ? 125 GLU B CA  1 
ATOM   5107  C C   . GLU B  1 125 ? -14.189 -9.279  -6.868   1.00 34.74  ? 125 GLU B C   1 
ATOM   5108  O O   . GLU B  1 125 ? -14.669 -9.607  -7.966   1.00 28.24  ? 125 GLU B O   1 
ATOM   5109  C CB  . GLU B  1 125 ? -13.886 -6.847  -6.327   1.00 50.98  ? 125 GLU B CB  1 
ATOM   5110  C CG  . GLU B  1 125 ? -14.208 -5.642  -5.432   1.00 63.18  ? 125 GLU B CG  1 
ATOM   5111  C CD  . GLU B  1 125 ? -13.320 -5.568  -4.176   1.00 72.34  ? 125 GLU B CD  1 
ATOM   5112  O OE1 . GLU B  1 125 ? -12.237 -4.942  -4.234   1.00 75.20  ? 125 GLU B OE1 1 
ATOM   5113  O OE2 . GLU B  1 125 ? -13.713 -6.130  -3.124   1.00 71.96  ? 125 GLU B OE2 1 
ATOM   5114  N N   . GLU B  1 126 ? -13.174 -9.932  -6.303   1.00 33.11  ? 126 GLU B N   1 
ATOM   5115  C CA  . GLU B  1 126 ? -12.545 -11.068 -6.955   1.00 34.33  ? 126 GLU B CA  1 
ATOM   5116  C C   . GLU B  1 126 ? -13.493 -12.260 -7.016   1.00 33.28  ? 126 GLU B C   1 
ATOM   5117  O O   . GLU B  1 126 ? -13.580 -12.947 -8.040   1.00 33.88  ? 126 GLU B O   1 
ATOM   5118  C CB  . GLU B  1 126 ? -11.247 -11.410 -6.223   1.00 33.18  ? 126 GLU B CB  1 
ATOM   5119  C CG  . GLU B  1 126 ? -10.311 -10.202 -6.233   1.00 43.55  ? 126 GLU B CG  1 
ATOM   5120  C CD  . GLU B  1 126 ? -9.139  -10.298 -5.273   1.00 55.17  ? 126 GLU B CD  1 
ATOM   5121  O OE1 . GLU B  1 126 ? -9.364  -10.696 -4.109   1.00 55.13  ? 126 GLU B OE1 1 
ATOM   5122  O OE2 . GLU B  1 126 ? -8.013  -9.900  -5.661   1.00 66.83  ? 126 GLU B OE2 1 
ATOM   5123  N N   . LEU B  1 127 ? -14.228 -12.507 -5.935   1.00 30.46  ? 127 LEU B N   1 
ATOM   5124  C CA  . LEU B  1 127 ? -15.228 -13.567 -5.953   1.00 27.72  ? 127 LEU B CA  1 
ATOM   5125  C C   . LEU B  1 127 ? -16.299 -13.297 -7.002   1.00 25.32  ? 127 LEU B C   1 
ATOM   5126  O O   . LEU B  1 127 ? -16.699 -14.210 -7.731   1.00 32.77  ? 127 LEU B O   1 
ATOM   5127  C CB  . LEU B  1 127 ? -15.843 -13.719 -4.560   1.00 26.32  ? 127 LEU B CB  1 
ATOM   5128  C CG  . LEU B  1 127 ? -14.916 -14.337 -3.513   1.00 28.80  ? 127 LEU B CG  1 
ATOM   5129  C CD1 . LEU B  1 127 ? -15.559 -14.323 -2.110   1.00 27.28  ? 127 LEU B CD1 1 
ATOM   5130  C CD2 . LEU B  1 127 ? -14.492 -15.751 -3.927   1.00 28.62  ? 127 LEU B CD2 1 
ATOM   5131  N N   . LEU B  1 128 ? -16.761 -12.045 -7.104   1.00 25.53  ? 128 LEU B N   1 
ATOM   5132  C CA  . LEU B  1 128 ? -17.727 -11.683 -8.139   1.00 31.91  ? 128 LEU B CA  1 
ATOM   5133  C C   . LEU B  1 128 ? -17.208 -12.024 -9.526   1.00 31.79  ? 128 LEU B C   1 
ATOM   5134  O O   . LEU B  1 128 ? -17.978 -12.450 -10.394  1.00 34.89  ? 128 LEU B O   1 
ATOM   5135  C CB  . LEU B  1 128 ? -18.052 -10.192 -8.068   1.00 33.82  ? 128 LEU B CB  1 
ATOM   5136  C CG  . LEU B  1 128 ? -19.308 -9.764  -7.310   1.00 37.61  ? 128 LEU B CG  1 
ATOM   5137  C CD1 . LEU B  1 128 ? -19.470 -8.251  -7.397   1.00 37.85  ? 128 LEU B CD1 1 
ATOM   5138  C CD2 . LEU B  1 128 ? -20.541 -10.465 -7.850   1.00 38.53  ? 128 LEU B CD2 1 
ATOM   5139  N N   . ASP B  1 129 ? -15.913 -11.805 -9.769   1.00 33.32  ? 129 ASP B N   1 
ATOM   5140  C CA  . ASP B  1 129 ? -15.343 -12.157 -11.066  1.00 32.39  ? 129 ASP B CA  1 
ATOM   5141  C C   . ASP B  1 129 ? -15.254 -13.663 -11.227  1.00 32.89  ? 129 ASP B C   1 
ATOM   5142  O O   . ASP B  1 129 ? -15.556 -14.193 -12.300  1.00 33.03  ? 129 ASP B O   1 
ATOM   5143  C CB  . ASP B  1 129 ? -13.965 -11.531 -11.240  1.00 34.63  ? 129 ASP B CB  1 
ATOM   5144  C CG  . ASP B  1 129 ? -14.039 -10.073 -11.620  1.00 40.21  ? 129 ASP B CG  1 
ATOM   5145  O OD1 . ASP B  1 129 ? -15.154 -9.507  -11.564  1.00 39.11  ? 129 ASP B OD1 1 
ATOM   5146  O OD2 . ASP B  1 129 ? -12.985 -9.495  -11.962  1.00 38.23  ? 129 ASP B OD2 1 
ATOM   5147  N N   . LEU B  1 130 ? -14.858 -14.366 -10.163  1.00 32.16  ? 130 LEU B N   1 
ATOM   5148  C CA  . LEU B  1 130 ? -14.746 -15.819 -10.229  1.00 32.63  ? 130 LEU B CA  1 
ATOM   5149  C C   . LEU B  1 130 ? -16.097 -16.457 -10.511  1.00 29.16  ? 130 LEU B C   1 
ATOM   5150  O O   . LEU B  1 130 ? -16.195 -17.399 -11.312  1.00 32.65  ? 130 LEU B O   1 
ATOM   5151  C CB  . LEU B  1 130 ? -14.162 -16.368 -8.924   1.00 34.08  ? 130 LEU B CB  1 
ATOM   5152  C CG  . LEU B  1 130 ? -13.856 -17.874 -8.959   1.00 36.06  ? 130 LEU B CG  1 
ATOM   5153  C CD1 . LEU B  1 130 ? -12.919 -18.221 -10.116  1.00 35.81  ? 130 LEU B CD1 1 
ATOM   5154  C CD2 . LEU B  1 130 ? -13.280 -18.367 -7.633   1.00 35.17  ? 130 LEU B CD2 1 
ATOM   5155  N N   . GLN B  1 131 ? -17.150 -15.968 -9.852   1.00 25.05  ? 131 GLN B N   1 
ATOM   5156  C CA  . GLN B  1 131 ? -18.487 -16.474 -10.130  1.00 28.46  ? 131 GLN B CA  1 
ATOM   5157  C C   . GLN B  1 131 ? -18.865 -16.217 -11.584  1.00 28.29  ? 131 GLN B C   1 
ATOM   5158  O O   . GLN B  1 131 ? -19.223 -17.143 -12.314  1.00 27.47  ? 131 GLN B O   1 
ATOM   5159  C CB  . GLN B  1 131 ? -19.518 -15.817 -9.218   1.00 26.25  ? 131 GLN B CB  1 
ATOM   5160  C CG  . GLN B  1 131 ? -19.426 -16.116 -7.736   1.00 23.57  ? 131 GLN B CG  1 
ATOM   5161  C CD  . GLN B  1 131 ? -20.331 -15.191 -6.962   1.00 28.75  ? 131 GLN B CD  1 
ATOM   5162  O OE1 . GLN B  1 131 ? -20.321 -13.979 -7.197   1.00 26.31  ? 131 GLN B OE1 1 
ATOM   5163  N NE2 . GLN B  1 131 ? -21.133 -15.744 -6.046   1.00 32.12  ? 131 GLN B NE2 1 
ATOM   5164  N N   . THR B  1 132 ? -18.780 -14.957 -12.011  1.00 30.49  ? 132 THR B N   1 
ATOM   5165  C CA  . THR B  1 132 ? -19.301 -14.567 -13.314  1.00 30.92  ? 132 THR B CA  1 
ATOM   5166  C C   . THR B  1 132 ? -18.476 -15.156 -14.455  1.00 34.88  ? 132 THR B C   1 
ATOM   5167  O O   . THR B  1 132 ? -19.020 -15.449 -15.527  1.00 33.57  ? 132 THR B O   1 
ATOM   5168  C CB  . THR B  1 132 ? -19.347 -13.038 -13.416  1.00 29.80  ? 132 THR B CB  1 
ATOM   5169  O OG1 . THR B  1 132 ? -19.956 -12.495 -12.237  1.00 29.40  ? 132 THR B OG1 1 
ATOM   5170  C CG2 . THR B  1 132 ? -20.151 -12.589 -14.644  1.00 27.15  ? 132 THR B CG2 1 
ATOM   5171  N N   . LEU B  1 133 ? -17.168 -15.320 -14.261  1.00 34.87  ? 133 LEU B N   1 
ATOM   5172  C CA  . LEU B  1 133 ? -16.360 -15.912 -15.319  1.00 33.05  ? 133 LEU B CA  1 
ATOM   5173  C C   . LEU B  1 133 ? -16.637 -17.403 -15.472  1.00 32.32  ? 133 LEU B C   1 
ATOM   5174  O O   . LEU B  1 133 ? -16.583 -17.927 -16.591  1.00 25.60  ? 133 LEU B O   1 
ATOM   5175  C CB  . LEU B  1 133 ? -14.875 -15.662 -15.058  1.00 35.12  ? 133 LEU B CB  1 
ATOM   5176  C CG  . LEU B  1 133 ? -14.419 -14.222 -15.298  1.00 39.67  ? 133 LEU B CG  1 
ATOM   5177  C CD1 . LEU B  1 133 ? -13.042 -13.977 -14.685  1.00 42.84  ? 133 LEU B CD1 1 
ATOM   5178  C CD2 . LEU B  1 133 ? -14.436 -13.924 -16.778  1.00 38.53  ? 133 LEU B CD2 1 
ATOM   5179  N N   . ASN B  1 134 ? -16.928 -18.108 -14.372  1.00 29.81  ? 134 ASN B N   1 
ATOM   5180  C CA  . ASN B  1 134 ? -17.374 -19.492 -14.509  1.00 30.06  ? 134 ASN B CA  1 
ATOM   5181  C C   . ASN B  1 134 ? -18.658 -19.551 -15.321  1.00 32.30  ? 134 ASN B C   1 
ATOM   5182  O O   . ASN B  1 134 ? -18.792 -20.386 -16.223  1.00 39.40  ? 134 ASN B O   1 
ATOM   5183  C CB  . ASN B  1 134 ? -17.572 -20.142 -13.136  1.00 29.70  ? 134 ASN B CB  1 
ATOM   5184  C CG  . ASN B  1 134 ? -16.286 -20.721 -12.576  1.00 28.05  ? 134 ASN B CG  1 
ATOM   5185  O OD1 . ASN B  1 134 ? -15.942 -21.876 -12.837  1.00 25.38  ? 134 ASN B OD1 1 
ATOM   5186  N ND2 . ASN B  1 134 ? -15.570 -19.919 -11.792  1.00 26.75  ? 134 ASN B ND2 1 
ATOM   5187  N N   . LEU B  1 135 ? -19.587 -18.636 -15.049  1.00 29.29  ? 135 LEU B N   1 
ATOM   5188  C CA  . LEU B  1 135 ? -20.804 -18.531 -15.853  1.00 35.15  ? 135 LEU B CA  1 
ATOM   5189  C C   . LEU B  1 135 ? -20.475 -18.275 -17.317  1.00 30.71  ? 135 LEU B C   1 
ATOM   5190  O O   . LEU B  1 135 ? -20.874 -19.037 -18.206  1.00 29.88  ? 135 LEU B O   1 
ATOM   5191  C CB  . LEU B  1 135 ? -21.688 -17.398 -15.336  1.00 35.71  ? 135 LEU B CB  1 
ATOM   5192  C CG  . LEU B  1 135 ? -22.596 -17.609 -14.134  1.00 45.81  ? 135 LEU B CG  1 
ATOM   5193  C CD1 . LEU B  1 135 ? -23.629 -16.499 -14.120  1.00 43.56  ? 135 LEU B CD1 1 
ATOM   5194  C CD2 . LEU B  1 135 ? -23.249 -18.978 -14.133  1.00 41.67  ? 135 LEU B CD2 1 
ATOM   5195  N N   . LEU B  1 136 ? -19.782 -17.167 -17.583  1.00 30.49  ? 136 LEU B N   1 
ATOM   5196  C CA  . LEU B  1 136 ? -19.489 -16.775 -18.962  1.00 27.96  ? 136 LEU B CA  1 
ATOM   5197  C C   . LEU B  1 136 ? -18.667 -17.825 -19.694  1.00 28.73  ? 136 LEU B C   1 
ATOM   5198  O O   . LEU B  1 136 ? -18.761 -17.935 -20.921  1.00 28.78  ? 136 LEU B O   1 
ATOM   5199  C CB  . LEU B  1 136 ? -18.766 -15.431 -18.969  1.00 26.77  ? 136 LEU B CB  1 
ATOM   5200  C CG  . LEU B  1 136 ? -19.673 -14.250 -18.595  1.00 28.83  ? 136 LEU B CG  1 
ATOM   5201  C CD1 . LEU B  1 136 ? -18.874 -12.973 -18.428  1.00 30.21  ? 136 LEU B CD1 1 
ATOM   5202  C CD2 . LEU B  1 136 ? -20.763 -14.052 -19.655  1.00 31.35  ? 136 LEU B CD2 1 
ATOM   5203  N N   . ALA B  1 137 ? -17.850 -18.601 -18.977  1.00 26.57  ? 137 ALA B N   1 
ATOM   5204  C CA  . ALA B  1 137 ? -17.049 -19.628 -19.644  1.00 30.99  ? 137 ALA B CA  1 
ATOM   5205  C C   . ALA B  1 137 ? -17.918 -20.632 -20.398  1.00 29.45  ? 137 ALA B C   1 
ATOM   5206  O O   . ALA B  1 137 ? -17.511 -21.142 -21.446  1.00 30.67  ? 137 ALA B O   1 
ATOM   5207  C CB  . ALA B  1 137 ? -16.168 -20.356 -18.633  1.00 31.78  ? 137 ALA B CB  1 
ATOM   5208  N N   . TRP B  1 138 ? -19.112 -20.923 -19.889  1.00 28.37  ? 138 TRP B N   1 
ATOM   5209  C CA  . TRP B  1 138 ? -20.028 -21.849 -20.537  1.00 29.70  ? 138 TRP B CA  1 
ATOM   5210  C C   . TRP B  1 138 ? -21.009 -21.149 -21.482  1.00 32.47  ? 138 TRP B C   1 
ATOM   5211  O O   . TRP B  1 138 ? -22.072 -21.701 -21.786  1.00 32.61  ? 138 TRP B O   1 
ATOM   5212  C CB  . TRP B  1 138 ? -20.776 -22.654 -19.469  1.00 27.48  ? 138 TRP B CB  1 
ATOM   5213  C CG  . TRP B  1 138 ? -19.831 -23.467 -18.674  1.00 26.63  ? 138 TRP B CG  1 
ATOM   5214  C CD1 . TRP B  1 138 ? -19.165 -23.081 -17.540  1.00 24.35  ? 138 TRP B CD1 1 
ATOM   5215  C CD2 . TRP B  1 138 ? -19.389 -24.798 -18.967  1.00 29.37  ? 138 TRP B CD2 1 
ATOM   5216  N NE1 . TRP B  1 138 ? -18.356 -24.107 -17.099  1.00 28.70  ? 138 TRP B NE1 1 
ATOM   5217  C CE2 . TRP B  1 138 ? -18.478 -25.171 -17.953  1.00 29.92  ? 138 TRP B CE2 1 
ATOM   5218  C CE3 . TRP B  1 138 ? -19.684 -25.719 -19.981  1.00 24.97  ? 138 TRP B CE3 1 
ATOM   5219  C CZ2 . TRP B  1 138 ? -17.853 -26.420 -17.930  1.00 29.80  ? 138 TRP B CZ2 1 
ATOM   5220  C CZ3 . TRP B  1 138 ? -19.064 -26.953 -19.959  1.00 28.13  ? 138 TRP B CZ3 1 
ATOM   5221  C CH2 . TRP B  1 138 ? -18.156 -27.295 -18.939  1.00 31.18  ? 138 TRP B CH2 1 
ATOM   5222  N N   . CYS B  1 139 ? -20.684 -19.950 -21.949  1.00 27.97  ? 139 CYS B N   1 
ATOM   5223  C CA  . CYS B  1 139 ? -21.616 -19.223 -22.794  1.00 24.42  ? 139 CYS B CA  1 
ATOM   5224  C C   . CYS B  1 139 ? -21.667 -19.857 -24.180  1.00 25.32  ? 139 CYS B C   1 
ATOM   5225  O O   . CYS B  1 139 ? -20.624 -20.182 -24.770  1.00 28.69  ? 139 CYS B O   1 
ATOM   5226  C CB  . CYS B  1 139 ? -21.209 -17.757 -22.874  1.00 28.47  ? 139 CYS B CB  1 
ATOM   5227  S SG  . CYS B  1 139 ? -22.305 -16.722 -23.851  1.00 33.35  ? 139 CYS B SG  1 
ATOM   5228  N N   . GLY B  1 140 ? -22.883 -20.045 -24.700  1.00 25.91  ? 140 GLY B N   1 
ATOM   5229  C CA  . GLY B  1 140 ? -23.066 -20.692 -25.989  1.00 27.26  ? 140 GLY B CA  1 
ATOM   5230  C C   . GLY B  1 140 ? -22.965 -19.731 -27.149  1.00 30.48  ? 140 GLY B C   1 
ATOM   5231  O O   . GLY B  1 140 ? -22.863 -18.516 -26.982  1.00 37.15  ? 140 GLY B O   1 
ATOM   5232  N N   . ARG B  1 141 ? -23.026 -20.305 -28.356  1.00 28.58  ? 141 ARG B N   1 
ATOM   5233  C CA  . ARG B  1 141 ? -22.840 -19.528 -29.580  1.00 28.21  ? 141 ARG B CA  1 
ATOM   5234  C C   . ARG B  1 141 ? -23.807 -18.345 -29.662  1.00 28.14  ? 141 ARG B C   1 
ATOM   5235  O O   . ARG B  1 141 ? -23.390 -17.217 -29.945  1.00 28.81  ? 141 ARG B O   1 
ATOM   5236  C CB  . ARG B  1 141 ? -23.000 -20.438 -30.793  1.00 27.45  ? 141 ARG B CB  1 
ATOM   5237  C CG  . ARG B  1 141 ? -22.506 -19.813 -32.077  1.00 34.36  ? 141 ARG B CG  1 
ATOM   5238  C CD  . ARG B  1 141 ? -22.608 -20.800 -33.207  1.00 44.44  ? 141 ARG B CD  1 
ATOM   5239  N NE  . ARG B  1 141 ? -23.999 -20.954 -33.578  1.00 49.99  ? 141 ARG B NE  1 
ATOM   5240  C CZ  . ARG B  1 141 ? -24.532 -20.421 -34.668  1.00 45.20  ? 141 ARG B CZ  1 
ATOM   5241  N NH1 . ARG B  1 141 ? -23.782 -19.707 -35.494  1.00 49.98  ? 141 ARG B NH1 1 
ATOM   5242  N NH2 . ARG B  1 141 ? -25.815 -20.598 -34.917  1.00 46.14  ? 141 ARG B NH2 1 
ATOM   5243  N N   . THR B  1 142 ? -25.098 -18.582 -29.399  1.00 28.28  ? 142 THR B N   1 
ATOM   5244  C CA  . THR B  1 142 ? -26.100 -17.518 -29.525  1.00 35.47  ? 142 THR B CA  1 
ATOM   5245  C C   . THR B  1 142 ? -25.790 -16.340 -28.606  1.00 33.68  ? 142 THR B C   1 
ATOM   5246  O O   . THR B  1 142 ? -25.723 -15.189 -29.050  1.00 34.54  ? 142 THR B O   1 
ATOM   5247  C CB  . THR B  1 142 ? -27.496 -18.069 -29.218  1.00 36.62  ? 142 THR B CB  1 
ATOM   5248  O OG1 . THR B  1 142 ? -27.814 -19.123 -30.134  1.00 37.76  ? 142 THR B OG1 1 
ATOM   5249  C CG2 . THR B  1 142 ? -28.554 -16.975 -29.303  1.00 32.30  ? 142 THR B CG2 1 
ATOM   5250  N N   . LEU B  1 143 ? -25.613 -16.609 -27.309  1.00 27.89  ? 143 LEU B N   1 
ATOM   5251  C CA  . LEU B  1 143 ? -25.340 -15.541 -26.355  1.00 32.77  ? 143 LEU B CA  1 
ATOM   5252  C C   . LEU B  1 143 ? -23.928 -14.973 -26.485  1.00 36.18  ? 143 LEU B C   1 
ATOM   5253  O O   . LEU B  1 143 ? -23.696 -13.827 -26.072  1.00 28.89  ? 143 LEU B O   1 
ATOM   5254  C CB  . LEU B  1 143 ? -25.585 -16.053 -24.932  1.00 27.13  ? 143 LEU B CB  1 
ATOM   5255  C CG  . LEU B  1 143 ? -27.059 -16.386 -24.693  1.00 27.05  ? 143 LEU B CG  1 
ATOM   5256  C CD1 . LEU B  1 143 ? -27.310 -16.735 -23.224  1.00 26.34  ? 143 LEU B CD1 1 
ATOM   5257  C CD2 . LEU B  1 143 ? -27.921 -15.200 -25.116  1.00 29.00  ? 143 LEU B CD2 1 
ATOM   5258  N N   . ARG B  1 144 ? -22.985 -15.721 -27.070  1.00 33.28  ? 144 ARG B N   1 
ATOM   5259  C CA  . ARG B  1 144 ? -21.658 -15.144 -27.270  1.00 33.85  ? 144 ARG B CA  1 
ATOM   5260  C C   . ARG B  1 144 ? -21.679 -13.925 -28.193  1.00 38.93  ? 144 ARG B C   1 
ATOM   5261  O O   . ARG B  1 144 ? -20.709 -13.156 -28.200  1.00 38.31  ? 144 ARG B O   1 
ATOM   5262  C CB  . ARG B  1 144 ? -20.691 -16.200 -27.794  1.00 37.88  ? 144 ARG B CB  1 
ATOM   5263  C CG  . ARG B  1 144 ? -19.934 -16.934 -26.671  1.00 33.72  ? 144 ARG B CG  1 
ATOM   5264  C CD  . ARG B  1 144 ? -19.209 -18.144 -27.227  1.00 36.54  ? 144 ARG B CD  1 
ATOM   5265  N NE  . ARG B  1 144 ? -18.583 -18.987 -26.214  1.00 38.53  ? 144 ARG B NE  1 
ATOM   5266  C CZ  . ARG B  1 144 ? -17.278 -18.996 -25.954  1.00 42.45  ? 144 ARG B CZ  1 
ATOM   5267  N NH1 . ARG B  1 144 ? -16.464 -18.201 -26.624  1.00 45.00  ? 144 ARG B NH1 1 
ATOM   5268  N NH2 . ARG B  1 144 ? -16.780 -19.800 -25.020  1.00 41.84  ? 144 ARG B NH2 1 
ATOM   5269  N N   . LYS B  1 145 ? -22.764 -13.702 -28.937  1.00 38.46  ? 145 LYS B N   1 
ATOM   5270  C CA  . LYS B  1 145 ? -22.900 -12.439 -29.651  1.00 42.76  ? 145 LYS B CA  1 
ATOM   5271  C C   . LYS B  1 145 ? -23.595 -11.376 -28.810  1.00 44.73  ? 145 LYS B C   1 
ATOM   5272  O O   . LYS B  1 145 ? -23.105 -10.248 -28.713  1.00 47.98  ? 145 LYS B O   1 
ATOM   5273  C CB  . LYS B  1 145 ? -23.659 -12.641 -30.964  1.00 52.46  ? 145 LYS B CB  1 
ATOM   5274  C CG  . LYS B  1 145 ? -22.844 -13.326 -32.023  1.00 59.29  ? 145 LYS B CG  1 
ATOM   5275  C CD  . LYS B  1 145 ? -23.138 -14.813 -31.997  1.00 63.94  ? 145 LYS B CD  1 
ATOM   5276  C CE  . LYS B  1 145 ? -22.133 -15.611 -32.820  1.00 64.24  ? 145 LYS B CE  1 
ATOM   5277  N NZ  . LYS B  1 145 ? -21.544 -16.735 -32.012  1.00 62.04  ? 145 LYS B NZ  1 
ATOM   5278  N N   . ASP B  1 146 ? -24.731 -11.720 -28.197  1.00 45.17  ? 146 ASP B N   1 
ATOM   5279  C CA  . ASP B  1 146 ? -25.463 -10.759 -27.373  1.00 51.08  ? 146 ASP B CA  1 
ATOM   5280  C C   . ASP B  1 146 ? -24.596 -10.211 -26.240  1.00 51.94  ? 146 ASP B C   1 
ATOM   5281  O O   . ASP B  1 146 ? -24.572 -8.999  -25.992  1.00 59.25  ? 146 ASP B O   1 
ATOM   5282  C CB  . ASP B  1 146 ? -26.729 -11.414 -26.812  1.00 56.93  ? 146 ASP B CB  1 
ATOM   5283  C CG  . ASP B  1 146 ? -27.632 -11.989 -27.906  1.00 63.12  ? 146 ASP B CG  1 
ATOM   5284  O OD1 . ASP B  1 146 ? -27.159 -12.186 -29.046  1.00 64.91  ? 146 ASP B OD1 1 
ATOM   5285  O OD2 . ASP B  1 146 ? -28.818 -12.255 -27.622  1.00 71.72  ? 146 ASP B OD2 1 
ATOM   5286  N N   . LEU B  1 147 ? -23.880 -11.089 -25.535  1.00 42.74  ? 147 LEU B N   1 
ATOM   5287  C CA  . LEU B  1 147 ? -23.089 -10.701 -24.372  1.00 43.62  ? 147 LEU B CA  1 
ATOM   5288  C C   . LEU B  1 147 ? -21.630 -10.425 -24.718  1.00 41.29  ? 147 LEU B C   1 
ATOM   5289  O O   . LEU B  1 147 ? -20.787 -10.375 -23.813  1.00 38.63  ? 147 LEU B O   1 
ATOM   5290  C CB  . LEU B  1 147 ? -23.171 -11.779 -23.288  1.00 39.16  ? 147 LEU B CB  1 
ATOM   5291  C CG  . LEU B  1 147 ? -24.576 -12.318 -23.013  1.00 39.59  ? 147 LEU B CG  1 
ATOM   5292  C CD1 . LEU B  1 147 ? -24.551 -13.528 -22.104  1.00 33.95  ? 147 LEU B CD1 1 
ATOM   5293  C CD2 . LEU B  1 147 ? -25.443 -11.208 -22.420  1.00 43.56  ? 147 LEU B CD2 1 
ATOM   5294  N N   . LYS B  1 148 ? -21.324 -10.236 -26.006  1.00 36.12  ? 148 LYS B N   1 
ATOM   5295  C CA  . LYS B  1 148 ? -19.939 -10.068 -26.441  1.00 37.00  ? 148 LYS B CA  1 
ATOM   5296  C C   . LYS B  1 148 ? -19.218 -8.986  -25.642  1.00 44.04  ? 148 LYS B C   1 
ATOM   5297  O O   . LYS B  1 148 ? -18.042 -9.141  -25.293  1.00 47.82  ? 148 LYS B O   1 
ATOM   5298  C CB  . LYS B  1 148 ? -19.902 -9.736  -27.938  1.00 36.30  ? 148 LYS B CB  1 
ATOM   5299  C CG  . LYS B  1 148 ? -18.583 -9.148  -28.432  1.00 36.58  ? 148 LYS B CG  1 
ATOM   5300  C CD  . LYS B  1 148 ? -18.584 -9.005  -29.969  1.00 45.16  ? 148 LYS B CD  1 
ATOM   5301  C CE  . LYS B  1 148 ? -17.209 -8.599  -30.505  1.00 51.24  ? 148 LYS B CE  1 
ATOM   5302  N NZ  . LYS B  1 148 ? -17.060 -8.887  -31.972  1.00 59.41  ? 148 LYS B NZ  1 
ATOM   5303  N N   . ASP B  1 149 ? -19.906 -7.883  -25.337  1.00 45.85  ? 149 ASP B N   1 
ATOM   5304  C CA  . ASP B  1 149 ? -19.253 -6.798  -24.606  1.00 48.28  ? 149 ASP B CA  1 
ATOM   5305  C C   . ASP B  1 149 ? -18.944 -7.188  -23.168  1.00 46.16  ? 149 ASP B C   1 
ATOM   5306  O O   . ASP B  1 149 ? -17.957 -6.704  -22.604  1.00 44.80  ? 149 ASP B O   1 
ATOM   5307  C CB  . ASP B  1 149 ? -20.113 -5.540  -24.635  1.00 54.45  ? 149 ASP B CB  1 
ATOM   5308  C CG  . ASP B  1 149 ? -20.505 -5.144  -26.041  1.00 61.67  ? 149 ASP B CG  1 
ATOM   5309  O OD1 . ASP B  1 149 ? -19.620 -5.134  -26.932  1.00 62.02  ? 149 ASP B OD1 1 
ATOM   5310  O OD2 . ASP B  1 149 ? -21.701 -4.850  -26.254  1.00 62.59  ? 149 ASP B OD2 1 
ATOM   5311  N N   . LEU B  1 150 ? -19.773 -8.048  -22.561  1.00 47.01  ? 150 LEU B N   1 
ATOM   5312  C CA  . LEU B  1 150 ? -19.484 -8.568  -21.223  1.00 43.72  ? 150 LEU B CA  1 
ATOM   5313  C C   . LEU B  1 150 ? -18.299 -9.511  -21.244  1.00 43.23  ? 150 LEU B C   1 
ATOM   5314  O O   . LEU B  1 150 ? -17.455 -9.481  -20.333  1.00 39.03  ? 150 LEU B O   1 
ATOM   5315  C CB  . LEU B  1 150 ? -20.698 -9.307  -20.644  1.00 44.00  ? 150 LEU B CB  1 
ATOM   5316  C CG  . LEU B  1 150 ? -21.892 -8.578  -20.048  1.00 47.25  ? 150 LEU B CG  1 
ATOM   5317  C CD1 . LEU B  1 150 ? -21.468 -7.847  -18.810  1.00 50.03  ? 150 LEU B CD1 1 
ATOM   5318  C CD2 . LEU B  1 150 ? -22.442 -7.615  -21.026  1.00 54.43  ? 150 LEU B CD2 1 
ATOM   5319  N N   . LEU B  1 151 ? -18.249 -10.385 -22.254  1.00 39.48  ? 151 LEU B N   1 
ATOM   5320  C CA  . LEU B  1 151 ? -17.176 -11.365 -22.334  1.00 41.97  ? 151 LEU B CA  1 
ATOM   5321  C C   . LEU B  1 151 ? -15.829 -10.700 -22.567  1.00 45.10  ? 151 LEU B C   1 
ATOM   5322  O O   . LEU B  1 151 ? -14.818 -11.119 -21.988  1.00 47.12  ? 151 LEU B O   1 
ATOM   5323  C CB  . LEU B  1 151 ? -17.464 -12.376 -23.441  1.00 40.70  ? 151 LEU B CB  1 
ATOM   5324  C CG  . LEU B  1 151 ? -18.628 -13.284 -23.053  1.00 40.84  ? 151 LEU B CG  1 
ATOM   5325  C CD1 . LEU B  1 151 ? -19.579 -13.444 -24.224  1.00 45.94  ? 151 LEU B CD1 1 
ATOM   5326  C CD2 . LEU B  1 151 ? -18.090 -14.621 -22.538  1.00 32.32  ? 151 LEU B CD2 1 
ATOM   5327  N N   . ASN B  1 152 ? -15.796 -9.668  -23.414  1.00 45.07  ? 152 ASN B N   1 
ATOM   5328  C CA  . ASN B  1 152 ? -14.551 -8.954  -23.669  1.00 50.18  ? 152 ASN B CA  1 
ATOM   5329  C C   . ASN B  1 152 ? -14.061 -8.185  -22.445  1.00 48.80  ? 152 ASN B C   1 
ATOM   5330  O O   . ASN B  1 152 ? -12.859 -7.912  -22.347  1.00 48.74  ? 152 ASN B O   1 
ATOM   5331  C CB  . ASN B  1 152 ? -14.718 -8.009  -24.863  1.00 58.87  ? 152 ASN B CB  1 
ATOM   5332  C CG  . ASN B  1 152 ? -15.056 -8.746  -26.157  1.00 70.03  ? 152 ASN B CG  1 
ATOM   5333  O OD1 . ASN B  1 152 ? -14.841 -9.954  -26.277  1.00 80.38  ? 152 ASN B OD1 1 
ATOM   5334  N ND2 . ASN B  1 152 ? -15.583 -8.014  -27.134  1.00 72.70  ? 152 ASN B ND2 1 
ATOM   5335  N N   . LYS B  1 153 ? -14.958 -7.823  -21.521  1.00 47.80  ? 153 LYS B N   1 
ATOM   5336  C CA  . LYS B  1 153 ? -14.532 -7.274  -20.236  1.00 49.59  ? 153 LYS B CA  1 
ATOM   5337  C C   . LYS B  1 153 ? -13.517 -8.186  -19.565  1.00 46.31  ? 153 LYS B C   1 
ATOM   5338  O O   . LYS B  1 153 ? -12.414 -7.759  -19.211  1.00 45.11  ? 153 LYS B O   1 
ATOM   5339  C CB  . LYS B  1 153 ? -15.733 -7.088  -19.305  1.00 53.13  ? 153 LYS B CB  1 
ATOM   5340  C CG  . LYS B  1 153 ? -16.659 -5.964  -19.662  1.00 51.98  ? 153 LYS B CG  1 
ATOM   5341  C CD  . LYS B  1 153 ? -17.966 -6.040  -18.879  1.00 48.81  ? 153 LYS B CD  1 
ATOM   5342  C CE  . LYS B  1 153 ? -17.762 -6.295  -17.381  1.00 45.76  ? 153 LYS B CE  1 
ATOM   5343  N NZ  . LYS B  1 153 ? -16.872 -5.359  -16.648  1.00 43.46  ? 153 LYS B NZ  1 
ATOM   5344  N N   . GLY B  1 154 ? -13.891 -9.446  -19.359  1.00 47.66  ? 154 GLY B N   1 
ATOM   5345  C CA  . GLY B  1 154 ? -13.038 -10.418 -18.702  1.00 46.58  ? 154 GLY B CA  1 
ATOM   5346  C C   . GLY B  1 154 ? -12.775 -10.154 -17.234  1.00 44.55  ? 154 GLY B C   1 
ATOM   5347  O O   . GLY B  1 154 ? -12.213 -11.016 -16.556  1.00 44.19  ? 154 GLY B O   1 
ATOM   5348  N N   . ARG B  1 155 ? -13.164 -8.978  -16.732  1.00 45.19  ? 155 ARG B N   1 
ATOM   5349  C CA  . ARG B  1 155 ? -12.828 -8.549  -15.379  1.00 45.76  ? 155 ARG B CA  1 
ATOM   5350  C C   . ARG B  1 155 ? -13.958 -7.693  -14.820  1.00 43.93  ? 155 ARG B C   1 
ATOM   5351  O O   . ARG B  1 155 ? -14.857 -7.247  -15.546  1.00 42.72  ? 155 ARG B O   1 
ATOM   5352  C CB  . ARG B  1 155 ? -11.534 -7.710  -15.323  1.00 45.70  ? 155 ARG B CB  1 
ATOM   5353  C CG  . ARG B  1 155 ? -10.620 -7.794  -16.530  1.00 49.15  ? 155 ARG B CG  1 
ATOM   5354  C CD  . ARG B  1 155 ? -9.341  -7.019  -16.295  1.00 50.61  ? 155 ARG B CD  1 
ATOM   5355  N NE  . ARG B  1 155 ? -8.632  -7.537  -15.133  1.00 53.70  ? 155 ARG B NE  1 
ATOM   5356  C CZ  . ARG B  1 155 ? -7.513  -8.252  -15.181  1.00 57.10  ? 155 ARG B CZ  1 
ATOM   5357  N NH1 . ARG B  1 155 ? -6.963  -8.657  -14.047  1.00 59.67  ? 155 ARG B NH1 1 
ATOM   5358  N NH2 . ARG B  1 155 ? -6.954  -8.577  -16.345  1.00 57.27  ? 155 ARG B NH2 1 
ATOM   5359  N N   . ASN B  1 156 ? -13.877 -7.449  -13.507  1.00 39.84  ? 156 ASN B N   1 
ATOM   5360  C CA  . ASN B  1 156 ? -14.621 -6.388  -12.825  1.00 38.84  ? 156 ASN B CA  1 
ATOM   5361  C C   . ASN B  1 156 ? -16.131 -6.506  -13.049  1.00 38.54  ? 156 ASN B C   1 
ATOM   5362  O O   . ASN B  1 156 ? -16.797 -5.557  -13.471  1.00 37.08  ? 156 ASN B O   1 
ATOM   5363  C CB  . ASN B  1 156 ? -14.127 -5.000  -13.260  1.00 42.41  ? 156 ASN B CB  1 
ATOM   5364  C CG  . ASN B  1 156 ? -12.614 -4.885  -13.293  1.00 42.21  ? 156 ASN B CG  1 
ATOM   5365  O OD1 . ASN B  1 156 ? -12.036 -4.475  -14.307  1.00 46.36  ? 156 ASN B OD1 1 
ATOM   5366  N ND2 . ASN B  1 156 ? -11.967 -5.217  -12.187  1.00 39.20  ? 156 ASN B ND2 1 
ATOM   5367  N N   . TYR B  1 157 ? -16.680 -7.673  -12.757  1.00 31.92  ? 157 TYR B N   1 
ATOM   5368  C CA  . TYR B  1 157 ? -18.105 -7.869  -12.971  1.00 29.05  ? 157 TYR B CA  1 
ATOM   5369  C C   . TYR B  1 157 ? -18.891 -7.421  -11.741  1.00 33.38  ? 157 TYR B C   1 
ATOM   5370  O O   . TYR B  1 157 ? -18.420 -7.518  -10.599  1.00 31.73  ? 157 TYR B O   1 
ATOM   5371  C CB  . TYR B  1 157 ? -18.391 -9.333  -13.321  1.00 27.47  ? 157 TYR B CB  1 
ATOM   5372  C CG  . TYR B  1 157 ? -17.841 -9.739  -14.681  1.00 34.35  ? 157 TYR B CG  1 
ATOM   5373  C CD1 . TYR B  1 157 ? -18.446 -9.298  -15.852  1.00 33.86  ? 157 TYR B CD1 1 
ATOM   5374  C CD2 . TYR B  1 157 ? -16.700 -10.535 -14.796  1.00 30.26  ? 157 TYR B CD2 1 
ATOM   5375  C CE1 . TYR B  1 157 ? -17.942 -9.658  -17.122  1.00 34.06  ? 157 TYR B CE1 1 
ATOM   5376  C CE2 . TYR B  1 157 ? -16.188 -10.889 -16.050  1.00 33.93  ? 157 TYR B CE2 1 
ATOM   5377  C CZ  . TYR B  1 157 ? -16.812 -10.451 -17.210  1.00 36.21  ? 157 TYR B CZ  1 
ATOM   5378  O OH  . TYR B  1 157 ? -16.308 -10.809 -18.456  1.00 36.76  ? 157 TYR B OH  1 
ATOM   5379  N N   . THR B  1 158 ? -20.085 -6.896  -11.985  1.00 32.35  ? 158 THR B N   1 
ATOM   5380  C CA  . THR B  1 158 ? -20.981 -6.511  -10.908  1.00 34.97  ? 158 THR B CA  1 
ATOM   5381  C C   . THR B  1 158 ? -22.062 -7.566  -10.754  1.00 33.65  ? 158 THR B C   1 
ATOM   5382  O O   . THR B  1 158 ? -22.310 -8.362  -11.658  1.00 31.28  ? 158 THR B O   1 
ATOM   5383  C CB  . THR B  1 158 ? -21.614 -5.134  -11.166  1.00 37.80  ? 158 THR B CB  1 
ATOM   5384  O OG1 . THR B  1 158 ? -22.397 -5.178  -12.369  1.00 36.32  ? 158 THR B OG1 1 
ATOM   5385  C CG2 . THR B  1 158 ? -20.540 -4.059  -11.290  1.00 35.28  ? 158 THR B CG2 1 
ATOM   5386  N N   . GLN B  1 159 ? -22.696 -7.578  -9.577   1.00 32.18  ? 159 GLN B N   1 
ATOM   5387  C CA  . GLN B  1 159 ? -23.784 -8.522  -9.348   1.00 31.47  ? 159 GLN B CA  1 
ATOM   5388  C C   . GLN B  1 159 ? -24.893 -8.349  -10.385  1.00 30.33  ? 159 GLN B C   1 
ATOM   5389  O O   . GLN B  1 159 ? -25.491 -9.336  -10.826  1.00 27.92  ? 159 GLN B O   1 
ATOM   5390  C CB  . GLN B  1 159 ? -24.331 -8.355  -7.923   1.00 33.21  ? 159 GLN B CB  1 
ATOM   5391  C CG  . GLN B  1 159 ? -25.513 -9.260  -7.572   1.00 34.16  ? 159 GLN B CG  1 
ATOM   5392  C CD  . GLN B  1 159 ? -25.102 -10.686 -7.235   1.00 38.62  ? 159 GLN B CD  1 
ATOM   5393  O OE1 . GLN B  1 159 ? -23.919 -10.980 -7.049   1.00 34.32  ? 159 GLN B OE1 1 
ATOM   5394  N NE2 . GLN B  1 159 ? -26.087 -11.578 -7.148   1.00 36.98  ? 159 GLN B NE2 1 
ATOM   5395  N N   . GLU B  1 160 ? -25.168 -7.099  -10.790  1.00 32.51  ? 160 GLU B N   1 
ATOM   5396  C CA  . GLU B  1 160 ? -26.204 -6.827  -11.788  1.00 37.01  ? 160 GLU B CA  1 
ATOM   5397  C C   . GLU B  1 160 ? -25.857 -7.435  -13.136  1.00 32.28  ? 160 GLU B C   1 
ATOM   5398  O O   . GLU B  1 160 ? -26.749 -7.887  -13.861  1.00 32.41  ? 160 GLU B O   1 
ATOM   5399  C CB  . GLU B  1 160 ? -26.417 -5.322  -11.959  1.00 41.39  ? 160 GLU B CB  1 
ATOM   5400  C CG  . GLU B  1 160 ? -27.409 -4.955  -13.061  1.00 51.07  ? 160 GLU B CG  1 
ATOM   5401  C CD  . GLU B  1 160 ? -28.857 -4.977  -12.582  1.00 63.20  ? 160 GLU B CD  1 
ATOM   5402  O OE1 . GLU B  1 160 ? -29.101 -5.312  -11.398  1.00 65.73  ? 160 GLU B OE1 1 
ATOM   5403  O OE2 . GLU B  1 160 ? -29.756 -4.656  -13.392  1.00 67.63  ? 160 GLU B OE2 1 
ATOM   5404  N N   . GLU B  1 161 ? -24.576 -7.415  -13.511  1.00 33.40  ? 161 GLU B N   1 
ATOM   5405  C CA  . GLU B  1 161 ? -24.184 -8.011  -14.785  1.00 32.44  ? 161 GLU B CA  1 
ATOM   5406  C C   . GLU B  1 161 ? -24.228 -9.532  -14.714  1.00 31.21  ? 161 GLU B C   1 
ATOM   5407  O O   . GLU B  1 161 ? -24.647 -10.191 -15.673  1.00 28.07  ? 161 GLU B O   1 
ATOM   5408  C CB  . GLU B  1 161 ? -22.789 -7.531  -15.184  1.00 31.48  ? 161 GLU B CB  1 
ATOM   5409  C CG  . GLU B  1 161 ? -22.724 -6.055  -15.499  1.00 37.47  ? 161 GLU B CG  1 
ATOM   5410  C CD  . GLU B  1 161 ? -21.296 -5.542  -15.558  1.00 43.26  ? 161 GLU B CD  1 
ATOM   5411  O OE1 . GLU B  1 161 ? -20.382 -6.294  -15.155  1.00 42.06  ? 161 GLU B OE1 1 
ATOM   5412  O OE2 . GLU B  1 161 ? -21.091 -4.393  -15.998  1.00 44.04  ? 161 GLU B OE2 1 
ATOM   5413  N N   . LYS B  1 162 ? -23.799 -10.104 -13.585  1.00 30.70  ? 162 LYS B N   1 
ATOM   5414  C CA  . LYS B  1 162 ? -23.907 -11.546 -13.379  1.00 30.81  ? 162 LYS B CA  1 
ATOM   5415  C C   . LYS B  1 162 ? -25.360 -12.002 -13.416  1.00 30.34  ? 162 LYS B C   1 
ATOM   5416  O O   . LYS B  1 162 ? -25.679 -13.029 -14.028  1.00 36.34  ? 162 LYS B O   1 
ATOM   5417  C CB  . LYS B  1 162 ? -23.256 -11.947 -12.049  1.00 27.17  ? 162 LYS B CB  1 
ATOM   5418  C CG  . LYS B  1 162 ? -23.400 -13.429 -11.682  1.00 28.41  ? 162 LYS B CG  1 
ATOM   5419  C CD  . LYS B  1 162 ? -22.764 -13.758 -10.320  1.00 26.57  ? 162 LYS B CD  1 
ATOM   5420  C CE  . LYS B  1 162 ? -23.524 -13.135 -9.179   1.00 27.02  ? 162 LYS B CE  1 
ATOM   5421  N NZ  . LYS B  1 162 ? -23.045 -13.505 -7.787   1.00 24.98  ? 162 LYS B NZ  1 
ATOM   5422  N N   . GLU B  1 163 ? -26.255 -11.259 -12.767  1.00 34.85  ? 163 GLU B N   1 
ATOM   5423  C CA  . GLU B  1 163 ? -27.670 -11.606 -12.841  1.00 34.50  ? 163 GLU B CA  1 
ATOM   5424  C C   . GLU B  1 163 ? -28.219 -11.388 -14.247  1.00 30.74  ? 163 GLU B C   1 
ATOM   5425  O O   . GLU B  1 163 ? -29.174 -12.058 -14.652  1.00 31.08  ? 163 GLU B O   1 
ATOM   5426  C CB  . GLU B  1 163 ? -28.451 -10.808 -11.797  1.00 39.79  ? 163 GLU B CB  1 
ATOM   5427  C CG  . GLU B  1 163 ? -27.975 -11.100 -10.363  1.00 44.67  ? 163 GLU B CG  1 
ATOM   5428  C CD  . GLU B  1 163 ? -28.651 -10.237 -9.308   1.00 51.50  ? 163 GLU B CD  1 
ATOM   5429  O OE1 . GLU B  1 163 ? -29.358 -9.281  -9.690   1.00 53.71  ? 163 GLU B OE1 1 
ATOM   5430  O OE2 . GLU B  1 163 ? -28.464 -10.502 -8.096   1.00 49.89  ? 163 GLU B OE2 1 
ATOM   5431  N N   . TYR B  1 164 ? -27.623 -10.473 -15.008  1.00 30.22  ? 164 TYR B N   1 
ATOM   5432  C CA  . TYR B  1 164 ? -28.079 -10.292 -16.385  1.00 38.20  ? 164 TYR B CA  1 
ATOM   5433  C C   . TYR B  1 164 ? -27.723 -11.507 -17.225  1.00 34.64  ? 164 TYR B C   1 
ATOM   5434  O O   . TYR B  1 164 ? -28.535 -11.964 -18.037  1.00 39.11  ? 164 TYR B O   1 
ATOM   5435  C CB  . TYR B  1 164 ? -27.495 -9.018  -16.997  1.00 39.16  ? 164 TYR B CB  1 
ATOM   5436  C CG  . TYR B  1 164 ? -27.945 -8.799  -18.431  1.00 42.42  ? 164 TYR B CG  1 
ATOM   5437  C CD1 . TYR B  1 164 ? -29.229 -8.346  -18.721  1.00 45.01  ? 164 TYR B CD1 1 
ATOM   5438  C CD2 . TYR B  1 164 ? -27.090 -9.068  -19.499  1.00 43.53  ? 164 TYR B CD2 1 
ATOM   5439  C CE1 . TYR B  1 164 ? -29.648 -8.150  -20.053  1.00 43.97  ? 164 TYR B CE1 1 
ATOM   5440  C CE2 . TYR B  1 164 ? -27.494 -8.875  -20.818  1.00 45.88  ? 164 TYR B CE2 1 
ATOM   5441  C CZ  . TYR B  1 164 ? -28.769 -8.415  -21.092  1.00 45.87  ? 164 TYR B CZ  1 
ATOM   5442  O OH  . TYR B  1 164 ? -29.153 -8.240  -22.409  1.00 46.23  ? 164 TYR B OH  1 
ATOM   5443  N N   . VAL B  1 165 ? -26.528 -12.065 -17.013  1.00 29.62  ? 165 VAL B N   1 
ATOM   5444  C CA  . VAL B  1 165 ? -26.122 -13.274 -17.726  1.00 32.21  ? 165 VAL B CA  1 
ATOM   5445  C C   . VAL B  1 165 ? -27.015 -14.451 -17.344  1.00 33.48  ? 165 VAL B C   1 
ATOM   5446  O O   . VAL B  1 165 ? -27.467 -15.208 -18.213  1.00 25.74  ? 165 VAL B O   1 
ATOM   5447  C CB  . VAL B  1 165 ? -24.639 -13.584 -17.443  1.00 32.25  ? 165 VAL B CB  1 
ATOM   5448  C CG1 . VAL B  1 165 ? -24.282 -14.982 -17.937  1.00 34.08  ? 165 VAL B CG1 1 
ATOM   5449  C CG2 . VAL B  1 165 ? -23.744 -12.542 -18.081  1.00 28.61  ? 165 VAL B CG2 1 
ATOM   5450  N N   . LEU B  1 166 ? -27.289 -14.622 -16.042  1.00 29.91  ? 166 LEU B N   1 
ATOM   5451  C CA  . LEU B  1 166 ? -28.121 -15.740 -15.599  1.00 28.42  ? 166 LEU B CA  1 
ATOM   5452  C C   . LEU B  1 166 ? -29.502 -15.690 -16.219  1.00 26.60  ? 166 LEU B C   1 
ATOM   5453  O O   . LEU B  1 166 ? -30.068 -16.734 -16.567  1.00 25.44  ? 166 LEU B O   1 
ATOM   5454  C CB  . LEU B  1 166 ? -28.273 -15.740 -14.080  1.00 30.03  ? 166 LEU B CB  1 
ATOM   5455  C CG  . LEU B  1 166 ? -27.172 -16.422 -13.309  1.00 34.47  ? 166 LEU B CG  1 
ATOM   5456  C CD1 . LEU B  1 166 ? -27.215 -15.953 -11.854  1.00 38.30  ? 166 LEU B CD1 1 
ATOM   5457  C CD2 . LEU B  1 166 ? -27.315 -17.952 -13.462  1.00 30.62  ? 166 LEU B CD2 1 
ATOM   5458  N N   . ASN B  1 167 ? -30.089 -14.491 -16.303  1.00 26.52  ? 167 ASN B N   1 
ATOM   5459  C CA  . ASN B  1 167 ? -31.420 -14.368 -16.865  1.00 30.95  ? 167 ASN B CA  1 
ATOM   5460  C C   . ASN B  1 167 ? -31.423 -14.751 -18.342  1.00 30.51  ? 167 ASN B C   1 
ATOM   5461  O O   . ASN B  1 167 ? -32.381 -15.368 -18.822  1.00 27.81  ? 167 ASN B O   1 
ATOM   5462  C CB  . ASN B  1 167 ? -31.950 -12.945 -16.661  1.00 38.62  ? 167 ASN B CB  1 
ATOM   5463  C CG  . ASN B  1 167 ? -32.503 -12.722 -15.257  1.00 51.23  ? 167 ASN B CG  1 
ATOM   5464  O OD1 . ASN B  1 167 ? -33.230 -13.563 -14.720  1.00 54.16  ? 167 ASN B OD1 1 
ATOM   5465  N ND2 . ASN B  1 167 ? -32.149 -11.590 -14.652  1.00 54.17  ? 167 ASN B ND2 1 
ATOM   5466  N N   . LYS B  1 168 ? -30.369 -14.378 -19.083  1.00 27.97  ? 168 LYS B N   1 
ATOM   5467  C CA  . LYS B  1 168 ? -30.305 -14.760 -20.486  1.00 29.32  ? 168 LYS B CA  1 
ATOM   5468  C C   . LYS B  1 168 ? -30.092 -16.260 -20.616  1.00 27.59  ? 168 LYS B C   1 
ATOM   5469  O O   . LYS B  1 168 ? -30.602 -16.885 -21.550  1.00 29.60  ? 168 LYS B O   1 
ATOM   5470  C CB  . LYS B  1 168 ? -29.186 -13.999 -21.210  1.00 32.46  ? 168 LYS B CB  1 
ATOM   5471  C CG  . LYS B  1 168 ? -29.240 -12.508 -21.080  1.00 35.26  ? 168 LYS B CG  1 
ATOM   5472  C CD  . LYS B  1 168 ? -30.518 -11.958 -21.669  1.00 46.81  ? 168 LYS B CD  1 
ATOM   5473  C CE  . LYS B  1 168 ? -30.504 -12.059 -23.188  1.00 52.37  ? 168 LYS B CE  1 
ATOM   5474  N NZ  . LYS B  1 168 ? -31.541 -11.184 -23.827  1.00 56.18  ? 168 LYS B NZ  1 
ATOM   5475  N N   . TYR B  1 169 ? -29.346 -16.857 -19.676  1.00 27.85  ? 169 TYR B N   1 
ATOM   5476  C CA  . TYR B  1 169 ? -29.104 -18.295 -19.733  1.00 26.19  ? 169 TYR B CA  1 
ATOM   5477  C C   . TYR B  1 169 ? -30.398 -19.070 -19.540  1.00 27.38  ? 169 TYR B C   1 
ATOM   5478  O O   . TYR B  1 169 ? -30.675 -20.026 -20.268  1.00 35.73  ? 169 TYR B O   1 
ATOM   5479  C CB  . TYR B  1 169 ? -28.064 -18.713 -18.687  1.00 30.06  ? 169 TYR B CB  1 
ATOM   5480  C CG  . TYR B  1 169 ? -26.619 -18.482 -19.084  1.00 26.24  ? 169 TYR B CG  1 
ATOM   5481  C CD1 . TYR B  1 169 ? -26.281 -17.616 -20.122  1.00 31.79  ? 169 TYR B CD1 1 
ATOM   5482  C CD2 . TYR B  1 169 ? -25.597 -19.129 -18.415  1.00 25.99  ? 169 TYR B CD2 1 
ATOM   5483  C CE1 . TYR B  1 169 ? -24.950 -17.396 -20.472  1.00 29.86  ? 169 TYR B CE1 1 
ATOM   5484  C CE2 . TYR B  1 169 ? -24.260 -18.914 -18.747  1.00 27.02  ? 169 TYR B CE2 1 
ATOM   5485  C CZ  . TYR B  1 169 ? -23.945 -18.058 -19.781  1.00 28.62  ? 169 TYR B CZ  1 
ATOM   5486  O OH  . TYR B  1 169 ? -22.616 -17.868 -20.101  1.00 25.84  ? 169 TYR B OH  1 
ATOM   5487  N N   . PHE B  1 170 ? -31.211 -18.675 -18.562  1.00 30.78  ? 170 PHE B N   1 
ATOM   5488  C CA  . PHE B  1 170 ? -32.494 -19.348 -18.410  1.00 32.72  ? 170 PHE B CA  1 
ATOM   5489  C C   . PHE B  1 170 ? -33.419 -19.075 -19.601  1.00 33.04  ? 170 PHE B C   1 
ATOM   5490  O O   . PHE B  1 170 ? -34.233 -19.931 -19.954  1.00 30.28  ? 170 PHE B O   1 
ATOM   5491  C CB  . PHE B  1 170 ? -33.140 -18.950 -17.086  1.00 33.76  ? 170 PHE B CB  1 
ATOM   5492  C CG  . PHE B  1 170 ? -32.606 -19.729 -15.915  1.00 36.92  ? 170 PHE B CG  1 
ATOM   5493  C CD1 . PHE B  1 170 ? -32.853 -21.096 -15.808  1.00 37.56  ? 170 PHE B CD1 1 
ATOM   5494  C CD2 . PHE B  1 170 ? -31.818 -19.116 -14.952  1.00 36.85  ? 170 PHE B CD2 1 
ATOM   5495  C CE1 . PHE B  1 170 ? -32.345 -21.835 -14.741  1.00 34.43  ? 170 PHE B CE1 1 
ATOM   5496  C CE2 . PHE B  1 170 ? -31.305 -19.854 -13.881  1.00 34.37  ? 170 PHE B CE2 1 
ATOM   5497  C CZ  . PHE B  1 170 ? -31.576 -21.211 -13.780  1.00 31.01  ? 170 PHE B CZ  1 
ATOM   5498  N N   . GLU B  1 171 ? -33.302 -17.913 -20.247  1.00 34.30  ? 171 GLU B N   1 
ATOM   5499  C CA  . GLU B  1 171 ? -34.032 -17.725 -21.499  1.00 36.03  ? 171 GLU B CA  1 
ATOM   5500  C C   . GLU B  1 171 ? -33.658 -18.799 -22.515  1.00 35.54  ? 171 GLU B C   1 
ATOM   5501  O O   . GLU B  1 171 ? -34.529 -19.353 -23.199  1.00 34.78  ? 171 GLU B O   1 
ATOM   5502  C CB  . GLU B  1 171 ? -33.778 -16.326 -22.059  1.00 40.91  ? 171 GLU B CB  1 
ATOM   5503  C CG  . GLU B  1 171 ? -34.468 -15.221 -21.277  1.00 47.81  ? 171 GLU B CG  1 
ATOM   5504  C CD  . GLU B  1 171 ? -34.254 -13.842 -21.880  1.00 55.42  ? 171 GLU B CD  1 
ATOM   5505  O OE1 . GLU B  1 171 ? -33.883 -13.747 -23.079  1.00 54.75  ? 171 GLU B OE1 1 
ATOM   5506  O OE2 . GLU B  1 171 ? -34.448 -12.853 -21.141  1.00 58.37  ? 171 GLU B OE2 1 
ATOM   5507  N N   . ILE B  1 172 ? -32.371 -19.133 -22.607  1.00 33.11  ? 172 ILE B N   1 
ATOM   5508  C CA  . ILE B  1 172 ? -31.943 -20.145 -23.563  1.00 32.08  ? 172 ILE B CA  1 
ATOM   5509  C C   . ILE B  1 172 ? -32.496 -21.517 -23.179  1.00 30.50  ? 172 ILE B C   1 
ATOM   5510  O O   . ILE B  1 172 ? -32.958 -22.285 -24.033  1.00 25.68  ? 172 ILE B O   1 
ATOM   5511  C CB  . ILE B  1 172 ? -30.407 -20.148 -23.661  1.00 31.30  ? 172 ILE B CB  1 
ATOM   5512  C CG1 . ILE B  1 172 ? -29.902 -18.883 -24.368  1.00 31.72  ? 172 ILE B CG1 1 
ATOM   5513  C CG2 . ILE B  1 172 ? -29.911 -21.389 -24.392  1.00 27.67  ? 172 ILE B CG2 1 
ATOM   5514  C CD1 . ILE B  1 172 ? -30.254 -18.808 -25.850  1.00 31.83  ? 172 ILE B CD1 1 
ATOM   5515  N N   . ILE B  1 173 ? -32.481 -21.840 -21.885  1.00 28.33  ? 173 ILE B N   1 
ATOM   5516  C CA  . ILE B  1 173 ? -32.976 -23.139 -21.460  1.00 30.90  ? 173 ILE B CA  1 
ATOM   5517  C C   . ILE B  1 173 ? -34.459 -23.289 -21.780  1.00 28.47  ? 173 ILE B C   1 
ATOM   5518  O O   . ILE B  1 173 ? -34.908 -24.359 -22.222  1.00 31.43  ? 173 ILE B O   1 
ATOM   5519  C CB  . ILE B  1 173 ? -32.687 -23.348 -19.963  1.00 30.83  ? 173 ILE B CB  1 
ATOM   5520  C CG1 . ILE B  1 173 ? -31.183 -23.554 -19.770  1.00 30.95  ? 173 ILE B CG1 1 
ATOM   5521  C CG2 . ILE B  1 173 ? -33.427 -24.561 -19.467  1.00 31.31  ? 173 ILE B CG2 1 
ATOM   5522  C CD1 . ILE B  1 173 ? -30.765 -23.724 -18.331  1.00 29.72  ? 173 ILE B CD1 1 
ATOM   5523  N N   . LYS B  1 174 ? -35.243 -22.230 -21.559  1.00 28.25  ? 174 LYS B N   1 
ATOM   5524  C CA  . LYS B  1 174 ? -36.685 -22.330 -21.758  1.00 36.08  ? 174 LYS B CA  1 
ATOM   5525  C C   . LYS B  1 174 ? -37.074 -22.525 -23.220  1.00 32.89  ? 174 LYS B C   1 
ATOM   5526  O O   . LYS B  1 174 ? -38.168 -23.029 -23.483  1.00 34.46  ? 174 LYS B O   1 
ATOM   5527  C CB  . LYS B  1 174 ? -37.408 -21.094 -21.199  1.00 43.20  ? 174 LYS B CB  1 
ATOM   5528  C CG  . LYS B  1 174 ? -37.209 -20.875 -19.700  1.00 48.60  ? 174 LYS B CG  1 
ATOM   5529  C CD  . LYS B  1 174 ? -37.335 -19.404 -19.324  1.00 53.28  ? 174 LYS B CD  1 
ATOM   5530  C CE  . LYS B  1 174 ? -37.707 -19.206 -17.855  1.00 56.07  ? 174 LYS B CE  1 
ATOM   5531  N NZ  . LYS B  1 174 ? -36.564 -19.483 -16.919  1.00 58.35  ? 174 LYS B NZ  1 
ATOM   5532  N N   . LYS B  1 175 ? -36.241 -22.123 -24.177  1.00 28.76  ? 175 LYS B N   1 
ATOM   5533  C CA  . LYS B  1 175 ? -36.604 -22.278 -25.589  1.00 33.49  ? 175 LYS B CA  1 
ATOM   5534  C C   . LYS B  1 175 ? -35.978 -23.511 -26.210  1.00 38.00  ? 175 LYS B C   1 
ATOM   5535  O O   . LYS B  1 175 ? -36.051 -23.688 -27.432  1.00 39.81  ? 175 LYS B O   1 
ATOM   5536  C CB  . LYS B  1 175 ? -36.217 -21.046 -26.421  1.00 39.95  ? 175 LYS B CB  1 
ATOM   5537  C CG  . LYS B  1 175 ? -36.173 -19.730 -25.692  1.00 49.70  ? 175 LYS B CG  1 
ATOM   5538  C CD  . LYS B  1 175 ? -37.513 -19.363 -25.035  1.00 61.39  ? 175 LYS B CD  1 
ATOM   5539  C CE  . LYS B  1 175 ? -37.345 -18.348 -23.884  1.00 60.87  ? 175 LYS B CE  1 
ATOM   5540  N NZ  . LYS B  1 175 ? -36.211 -17.394 -24.075  1.00 64.72  ? 175 LYS B NZ  1 
ATOM   5541  N N   . THR B  1 176 ? -35.389 -24.380 -25.386  1.00 31.93  ? 176 THR B N   1 
ATOM   5542  C CA  . THR B  1 176 ? -34.547 -25.453 -25.902  1.00 34.75  ? 176 THR B CA  1 
ATOM   5543  C C   . THR B  1 176 ? -35.373 -26.587 -26.493  1.00 35.98  ? 176 THR B C   1 
ATOM   5544  O O   . THR B  1 176 ? -35.097 -27.048 -27.605  1.00 36.00  ? 176 THR B O   1 
ATOM   5545  C CB  . THR B  1 176 ? -33.636 -25.961 -24.787  1.00 29.21  ? 176 THR B CB  1 
ATOM   5546  O OG1 . THR B  1 176 ? -32.625 -24.976 -24.555  1.00 25.11  ? 176 THR B OG1 1 
ATOM   5547  C CG2 . THR B  1 176 ? -32.992 -27.299 -25.162  1.00 29.21  ? 176 THR B CG2 1 
ATOM   5548  N N   . LEU B  1 177 ? -36.392 -27.055 -25.768  1.00 31.15  ? 177 LEU B N   1 
ATOM   5549  C CA  . LEU B  1 177 ? -37.241 -28.087 -26.347  1.00 27.38  ? 177 LEU B CA  1 
ATOM   5550  C C   . LEU B  1 177 ? -37.968 -27.556 -27.570  1.00 33.52  ? 177 LEU B C   1 
ATOM   5551  O O   . LEU B  1 177 ? -38.212 -28.314 -28.518  1.00 28.72  ? 177 LEU B O   1 
ATOM   5552  C CB  . LEU B  1 177 ? -38.236 -28.622 -25.315  1.00 28.73  ? 177 LEU B CB  1 
ATOM   5553  C CG  . LEU B  1 177 ? -37.580 -29.380 -24.157  1.00 29.48  ? 177 LEU B CG  1 
ATOM   5554  C CD1 . LEU B  1 177 ? -38.633 -29.815 -23.141  1.00 34.18  ? 177 LEU B CD1 1 
ATOM   5555  C CD2 . LEU B  1 177 ? -36.750 -30.572 -24.659  1.00 33.39  ? 177 LEU B CD2 1 
ATOM   5556  N N   . SER B  1 178 ? -38.291 -26.254 -27.575  1.00 27.94  ? 178 SER B N   1 
ATOM   5557  C CA  . SER B  1 178 ? -38.977 -25.659 -28.713  1.00 34.89  ? 178 SER B CA  1 
ATOM   5558  C C   . SER B  1 178 ? -38.156 -25.794 -29.984  1.00 28.87  ? 178 SER B C   1 
ATOM   5559  O O   . SER B  1 178 ? -38.706 -26.078 -31.050  1.00 29.51  ? 178 SER B O   1 
ATOM   5560  C CB  . SER B  1 178 ? -39.277 -24.180 -28.456  1.00 37.54  ? 178 SER B CB  1 
ATOM   5561  O OG  . SER B  1 178 ? -40.395 -24.031 -27.606  1.00 45.75  ? 178 SER B OG  1 
ATOM   5562  N N   . ILE B  1 179 ? -36.841 -25.577 -29.899  1.00 31.98  ? 179 ILE B N   1 
ATOM   5563  C CA  . ILE B  1 179 ? -36.063 -25.578 -31.130  1.00 37.16  ? 179 ILE B CA  1 
ATOM   5564  C C   . ILE B  1 179 ? -35.969 -26.986 -31.705  1.00 31.93  ? 179 ILE B C   1 
ATOM   5565  O O   . ILE B  1 179 ? -35.953 -27.150 -32.928  1.00 32.05  ? 179 ILE B O   1 
ATOM   5566  C CB  . ILE B  1 179 ? -34.678 -24.938 -30.920  1.00 37.98  ? 179 ILE B CB  1 
ATOM   5567  C CG1 . ILE B  1 179 ? -34.096 -24.516 -32.271  1.00 40.03  ? 179 ILE B CG1 1 
ATOM   5568  C CG2 . ILE B  1 179 ? -33.735 -25.886 -30.219  1.00 35.48  ? 179 ILE B CG2 1 
ATOM   5569  C CD1 . ILE B  1 179 ? -32.847 -23.713 -32.135  1.00 38.98  ? 179 ILE B CD1 1 
ATOM   5570  N N   . TYR B  1 180 ? -35.983 -28.018 -30.849  1.00 27.51  ? 180 TYR B N   1 
ATOM   5571  C CA  . TYR B  1 180 ? -35.992 -29.393 -31.338  1.00 30.60  ? 180 TYR B CA  1 
ATOM   5572  C C   . TYR B  1 180 ? -37.293 -29.705 -32.066  1.00 33.12  ? 180 TYR B C   1 
ATOM   5573  O O   . TYR B  1 180 ? -37.265 -30.294 -33.151  1.00 29.61  ? 180 TYR B O   1 
ATOM   5574  C CB  . TYR B  1 180 ? -35.748 -30.378 -30.184  1.00 29.58  ? 180 TYR B CB  1 
ATOM   5575  C CG  . TYR B  1 180 ? -34.293 -30.428 -29.758  1.00 27.98  ? 180 TYR B CG  1 
ATOM   5576  C CD1 . TYR B  1 180 ? -33.348 -31.132 -30.505  1.00 31.38  ? 180 TYR B CD1 1 
ATOM   5577  C CD2 . TYR B  1 180 ? -33.862 -29.753 -28.617  1.00 28.49  ? 180 TYR B CD2 1 
ATOM   5578  C CE1 . TYR B  1 180 ? -32.009 -31.166 -30.124  1.00 30.47  ? 180 TYR B CE1 1 
ATOM   5579  C CE2 . TYR B  1 180 ? -32.538 -29.773 -28.223  1.00 27.51  ? 180 TYR B CE2 1 
ATOM   5580  C CZ  . TYR B  1 180 ? -31.618 -30.488 -28.966  1.00 27.57  ? 180 TYR B CZ  1 
ATOM   5581  O OH  . TYR B  1 180 ? -30.311 -30.494 -28.569  1.00 23.48  ? 180 TYR B OH  1 
ATOM   5582  N N   . ARG B  1 181 ? -38.438 -29.302 -31.499  1.00 34.39  ? 181 ARG B N   1 
ATOM   5583  C CA  . ARG B  1 181 ? -39.692 -29.338 -32.257  1.00 34.77  ? 181 ARG B CA  1 
ATOM   5584  C C   . ARG B  1 181 ? -39.561 -28.553 -33.560  1.00 38.34  ? 181 ARG B C   1 
ATOM   5585  O O   . ARG B  1 181 ? -39.915 -29.044 -34.636  1.00 39.09  ? 181 ARG B O   1 
ATOM   5586  C CB  . ARG B  1 181 ? -40.835 -28.752 -31.422  1.00 32.25  ? 181 ARG B CB  1 
ATOM   5587  C CG  . ARG B  1 181 ? -41.225 -29.556 -30.190  1.00 35.41  ? 181 ARG B CG  1 
ATOM   5588  C CD  . ARG B  1 181 ? -42.464 -28.925 -29.519  1.00 39.92  ? 181 ARG B CD  1 
ATOM   5589  N NE  . ARG B  1 181 ? -42.677 -29.461 -28.180  1.00 45.09  ? 181 ARG B NE  1 
ATOM   5590  C CZ  . ARG B  1 181 ? -42.289 -28.864 -27.054  1.00 46.87  ? 181 ARG B CZ  1 
ATOM   5591  N NH1 . ARG B  1 181 ? -41.674 -27.689 -27.095  1.00 44.60  ? 181 ARG B NH1 1 
ATOM   5592  N NH2 . ARG B  1 181 ? -42.526 -29.447 -25.883  1.00 46.36  ? 181 ARG B NH2 1 
ATOM   5593  N N   . GLU B  1 182 ? -39.081 -27.309 -33.467  1.00 39.52  ? 182 GLU B N   1 
ATOM   5594  C CA  . GLU B  1 182 ? -38.827 -26.457 -34.632  1.00 43.92  ? 182 GLU B CA  1 
ATOM   5595  C C   . GLU B  1 182 ? -38.100 -27.184 -35.750  1.00 42.01  ? 182 GLU B C   1 
ATOM   5596  O O   . GLU B  1 182 ? -38.636 -27.313 -36.866  1.00 42.57  ? 182 GLU B O   1 
ATOM   5597  C CB  . GLU B  1 182 ? -38.038 -25.223 -34.189  1.00 54.09  ? 182 GLU B CB  1 
ATOM   5598  C CG  . GLU B  1 182 ? -37.472 -24.408 -35.336  1.00 60.17  ? 182 GLU B CG  1 
ATOM   5599  C CD  . GLU B  1 182 ? -37.723 -22.920 -35.214  1.00 61.49  ? 182 GLU B CD  1 
ATOM   5600  O OE1 . GLU B  1 182 ? -38.050 -22.309 -36.250  1.00 63.22  ? 182 GLU B OE1 1 
ATOM   5601  O OE2 . GLU B  1 182 ? -37.538 -22.361 -34.107  1.00 60.62  ? 182 GLU B OE2 1 
ATOM   5602  N N   . ILE B  1 183 ? -36.875 -27.650 -35.486  1.00 34.04  ? 183 ILE B N   1 
ATOM   5603  C CA  . ILE B  1 183 ? -36.081 -28.196 -36.581  1.00 39.55  ? 183 ILE B CA  1 
ATOM   5604  C C   . ILE B  1 183 ? -36.667 -29.511 -37.091  1.00 38.50  ? 183 ILE B C   1 
ATOM   5605  O O   . ILE B  1 183 ? -36.510 -29.868 -38.272  1.00 36.37  ? 183 ILE B O   1 
ATOM   5606  C CB  . ILE B  1 183 ? -34.623 -28.357 -36.137  1.00 39.64  ? 183 ILE B CB  1 
ATOM   5607  C CG1 . ILE B  1 183 ? -34.533 -29.348 -34.958  1.00 42.11  ? 183 ILE B CG1 1 
ATOM   5608  C CG2 . ILE B  1 183 ? -34.070 -27.008 -35.701  1.00 38.27  ? 183 ILE B CG2 1 
ATOM   5609  C CD1 . ILE B  1 183 ? -34.064 -30.740 -35.333  1.00 38.37  ? 183 ILE B CD1 1 
ATOM   5610  N N   . LYS B  1 184 ? -37.351 -30.244 -36.215  1.00 37.26  ? 184 LYS B N   1 
ATOM   5611  C CA  . LYS B  1 184 ? -37.986 -31.502 -36.597  1.00 36.11  ? 184 LYS B CA  1 
ATOM   5612  C C   . LYS B  1 184 ? -39.147 -31.274 -37.555  1.00 31.40  ? 184 LYS B C   1 
ATOM   5613  O O   . LYS B  1 184 ? -39.259 -31.937 -38.598  1.00 31.47  ? 184 LYS B O   1 
ATOM   5614  C CB  . LYS B  1 184 ? -38.465 -32.216 -35.337  1.00 38.35  ? 184 LYS B CB  1 
ATOM   5615  C CG  . LYS B  1 184 ? -39.429 -33.306 -35.592  1.00 41.23  ? 184 LYS B CG  1 
ATOM   5616  C CD  . LYS B  1 184 ? -39.809 -33.966 -34.288  1.00 43.39  ? 184 LYS B CD  1 
ATOM   5617  C CE  . LYS B  1 184 ? -39.786 -35.454 -34.467  1.00 45.38  ? 184 LYS B CE  1 
ATOM   5618  N NZ  . LYS B  1 184 ? -40.489 -35.858 -35.720  1.00 50.31  ? 184 LYS B NZ  1 
ATOM   5619  N N   . GLU B  1 185 ? -40.015 -30.317 -37.219  1.00 36.50  ? 185 GLU B N   1 
ATOM   5620  C CA  . GLU B  1 185 ? -41.192 -30.049 -38.022  1.00 40.55  ? 185 GLU B CA  1 
ATOM   5621  C C   . GLU B  1 185 ? -40.809 -29.463 -39.369  1.00 39.58  ? 185 GLU B C   1 
ATOM   5622  O O   . GLU B  1 185 ? -41.478 -29.732 -40.376  1.00 40.32  ? 185 GLU B O   1 
ATOM   5623  C CB  . GLU B  1 185 ? -42.131 -29.114 -37.255  1.00 49.36  ? 185 GLU B CB  1 
ATOM   5624  C CG  . GLU B  1 185 ? -42.950 -28.158 -38.108  1.00 57.40  ? 185 GLU B CG  1 
ATOM   5625  C CD  . GLU B  1 185 ? -44.119 -27.544 -37.343  1.00 66.07  ? 185 GLU B CD  1 
ATOM   5626  O OE1 . GLU B  1 185 ? -45.278 -27.927 -37.612  1.00 68.93  ? 185 GLU B OE1 1 
ATOM   5627  O OE2 . GLU B  1 185 ? -43.877 -26.684 -36.466  1.00 67.28  ? 185 GLU B OE2 1 
ATOM   5628  N N   . GLU B  1 186 ? -39.732 -28.681 -39.410  1.00 36.48  ? 186 GLU B N   1 
ATOM   5629  C CA  . GLU B  1 186 ? -39.251 -28.103 -40.657  1.00 39.25  ? 186 GLU B CA  1 
ATOM   5630  C C   . GLU B  1 186 ? -38.454 -29.106 -41.477  1.00 38.43  ? 186 GLU B C   1 
ATOM   5631  O O   . GLU B  1 186 ? -38.001 -28.766 -42.574  1.00 42.02  ? 186 GLU B O   1 
ATOM   5632  C CB  . GLU B  1 186 ? -38.399 -26.859 -40.376  1.00 34.15  ? 186 GLU B CB  1 
ATOM   5633  C CG  . GLU B  1 186 ? -39.161 -25.717 -39.741  1.00 42.70  ? 186 GLU B CG  1 
ATOM   5634  C CD  . GLU B  1 186 ? -38.290 -24.509 -39.440  1.00 46.21  ? 186 GLU B CD  1 
ATOM   5635  O OE1 . GLU B  1 186 ? -37.082 -24.692 -39.175  1.00 44.76  ? 186 GLU B OE1 1 
ATOM   5636  O OE2 . GLU B  1 186 ? -38.818 -23.373 -39.471  1.00 49.78  ? 186 GLU B OE2 1 
ATOM   5637  N N   . GLY B  1 187 ? -38.277 -30.327 -40.970  1.00 36.58  ? 187 GLY B N   1 
ATOM   5638  C CA  . GLY B  1 187 ? -37.521 -31.339 -41.668  1.00 34.72  ? 187 GLY B CA  1 
ATOM   5639  C C   . GLY B  1 187 ? -36.040 -31.070 -41.745  1.00 38.33  ? 187 GLY B C   1 
ATOM   5640  O O   . GLY B  1 187 ? -35.343 -31.732 -42.520  1.00 38.01  ? 187 GLY B O   1 
ATOM   5641  N N   . LYS B  1 188 ? -35.537 -30.109 -40.972  1.00 40.41  ? 188 LYS B N   1 
ATOM   5642  C CA  . LYS B  1 188 ? -34.106 -29.844 -40.920  1.00 39.86  ? 188 LYS B CA  1 
ATOM   5643  C C   . LYS B  1 188 ? -33.343 -30.901 -40.134  1.00 36.57  ? 188 LYS B C   1 
ATOM   5644  O O   . LYS B  1 188 ? -32.105 -30.908 -40.161  1.00 34.90  ? 188 LYS B O   1 
ATOM   5645  C CB  . LYS B  1 188 ? -33.872 -28.456 -40.326  1.00 35.58  ? 188 LYS B CB  1 
ATOM   5646  C CG  . LYS B  1 188 ? -34.338 -27.339 -41.259  1.00 39.13  ? 188 LYS B CG  1 
ATOM   5647  C CD  . LYS B  1 188 ? -34.212 -25.968 -40.613  1.00 41.66  ? 188 LYS B CD  1 
ATOM   5648  C CE  . LYS B  1 188 ? -34.234 -24.863 -41.649  1.00 45.21  ? 188 LYS B CE  1 
ATOM   5649  N NZ  . LYS B  1 188 ? -35.587 -24.262 -41.766  1.00 47.36  ? 188 LYS B NZ  1 
ATOM   5650  N N   . GLY B  1 189 ? -34.043 -31.797 -39.449  1.00 36.90  ? 189 GLY B N   1 
ATOM   5651  C CA  . GLY B  1 189 ? -33.392 -32.796 -38.630  1.00 33.24  ? 189 GLY B CA  1 
ATOM   5652  C C   . GLY B  1 189 ? -34.401 -33.738 -38.014  1.00 32.00  ? 189 GLY B C   1 
ATOM   5653  O O   . GLY B  1 189 ? -35.548 -33.351 -37.781  1.00 32.84  ? 189 GLY B O   1 
ATOM   5654  N N   . SER B  1 190 ? -34.005 -34.984 -37.791  1.00 31.06  ? 190 SER B N   1 
ATOM   5655  C CA  . SER B  1 190 ? -34.825 -35.924 -37.053  1.00 30.40  ? 190 SER B CA  1 
ATOM   5656  C C   . SER B  1 190 ? -34.345 -35.946 -35.610  1.00 30.79  ? 190 SER B C   1 
ATOM   5657  O O   . SER B  1 190 ? -33.178 -35.657 -35.324  1.00 27.51  ? 190 SER B O   1 
ATOM   5658  C CB  . SER B  1 190 ? -34.770 -37.317 -37.673  1.00 35.45  ? 190 SER B CB  1 
ATOM   5659  O OG  . SER B  1 190 ? -35.149 -37.281 -39.045  1.00 39.59  ? 190 SER B OG  1 
ATOM   5660  N N   . VAL B  1 191 ? -35.268 -36.229 -34.693  1.00 32.69  ? 191 VAL B N   1 
ATOM   5661  C CA  . VAL B  1 191 ? -34.947 -36.330 -33.271  1.00 28.79  ? 191 VAL B CA  1 
ATOM   5662  C C   . VAL B  1 191 ? -35.266 -37.745 -32.805  1.00 33.93  ? 191 VAL B C   1 
ATOM   5663  O O   . VAL B  1 191 ? -36.391 -38.228 -32.980  1.00 35.98  ? 191 VAL B O   1 
ATOM   5664  C CB  . VAL B  1 191 ? -35.708 -35.310 -32.402  1.00 27.31  ? 191 VAL B CB  1 
ATOM   5665  C CG1 . VAL B  1 191 ? -35.391 -35.565 -30.890  1.00 25.19  ? 191 VAL B CG1 1 
ATOM   5666  C CG2 . VAL B  1 191 ? -35.378 -33.877 -32.790  1.00 28.85  ? 191 VAL B CG2 1 
ATOM   5667  N N   . SER B  1 192 ? -34.287 -38.390 -32.196  1.00 27.51  ? 192 SER B N   1 
ATOM   5668  C CA  . SER B  1 192 ? -34.428 -39.703 -31.601  1.00 25.36  ? 192 SER B CA  1 
ATOM   5669  C C   . SER B  1 192 ? -34.341 -39.577 -30.081  1.00 28.16  ? 192 SER B C   1 
ATOM   5670  O O   . SER B  1 192 ? -34.095 -38.494 -29.528  1.00 27.88  ? 192 SER B O   1 
ATOM   5671  C CB  . SER B  1 192 ? -33.350 -40.633 -32.130  1.00 25.38  ? 192 SER B CB  1 
ATOM   5672  O OG  . SER B  1 192 ? -32.110 -40.248 -31.577  1.00 31.54  ? 192 SER B OG  1 
ATOM   5673  N N   . THR B  1 193 ? -34.548 -40.705 -29.407  1.00 30.37  ? 193 THR B N   1 
ATOM   5674  C CA  . THR B  1 193 ? -34.311 -40.813 -27.973  1.00 26.77  ? 193 THR B CA  1 
ATOM   5675  C C   . THR B  1 193 ? -33.580 -42.123 -27.707  1.00 26.12  ? 193 THR B C   1 
ATOM   5676  O O   . THR B  1 193 ? -33.287 -42.882 -28.631  1.00 25.61  ? 193 THR B O   1 
ATOM   5677  C CB  . THR B  1 193 ? -35.612 -40.732 -27.174  1.00 28.48  ? 193 THR B CB  1 
ATOM   5678  O OG1 . THR B  1 193 ? -35.287 -40.675 -25.779  1.00 33.92  ? 193 THR B OG1 1 
ATOM   5679  C CG2 . THR B  1 193 ? -36.496 -41.951 -27.435  1.00 27.12  ? 193 THR B CG2 1 
ATOM   5680  N N   . SER B  1 194 ? -33.307 -42.357 -26.438  1.00 23.94  ? 194 SER B N   1 
ATOM   5681  C CA  . SER B  1 194 ? -32.727 -43.580 -26.000  1.00 24.62  ? 194 SER B CA  1 
ATOM   5682  C C   . SER B  1 194 ? -33.562 -44.174 -24.859  1.00 29.57  ? 194 SER B C   1 
ATOM   5683  O O   . SER B  1 194 ? -34.387 -43.520 -24.318  1.00 23.61  ? 194 SER B O   1 
ATOM   5684  C CB  . SER B  1 194 ? -31.256 -43.393 -25.617  1.00 24.83  ? 194 SER B CB  1 
ATOM   5685  O OG  . SER B  1 194 ? -30.444 -42.875 -26.609  1.00 28.00  ? 194 SER B OG  1 
ATOM   5686  N N   . PRO B  1 195 ? -33.355 -45.462 -24.590  1.00 32.22  ? 195 PRO B N   1 
ATOM   5687  C CA  . PRO B  1 195 ? -33.979 -46.048 -23.418  1.00 34.96  ? 195 PRO B CA  1 
ATOM   5688  C C   . PRO B  1 195 ? -33.798 -45.097 -22.221  1.00 29.73  ? 195 PRO B C   1 
ATOM   5689  O O   . PRO B  1 195 ? -32.734 -44.677 -22.063  1.00 27.77  ? 195 PRO B O   1 
ATOM   5690  C CB  . PRO B  1 195 ? -33.305 -47.398 -23.335  1.00 32.82  ? 195 PRO B CB  1 
ATOM   5691  C CG  . PRO B  1 195 ? -33.138 -47.766 -24.750  1.00 35.70  ? 195 PRO B CG  1 
ATOM   5692  C CD  . PRO B  1 195 ? -32.729 -46.501 -25.422  1.00 33.44  ? 195 PRO B CD  1 
ATOM   5693  N N   . TYR B  1 196 ? -34.825 -44.866 -21.407  1.00 28.64  ? 196 TYR B N   1 
ATOM   5694  C CA  . TYR B  1 196 ? -34.919 -43.761 -20.430  1.00 24.06  ? 196 TYR B CA  1 
ATOM   5695  C C   . TYR B  1 196 ? -33.739 -43.257 -19.729  1.00 28.76  ? 196 TYR B C   1 
ATOM   5696  O O   . TYR B  1 196 ? -33.406 -42.153 -19.894  1.00 25.33  ? 196 TYR B O   1 
ATOM   5697  C CB  . TYR B  1 196 ? -36.051 -44.031 -19.419  1.00 26.87  ? 196 TYR B CB  1 
ATOM   5698  C CG  . TYR B  1 196 ? -36.796 -42.801 -19.005  1.00 28.10  ? 196 TYR B CG  1 
ATOM   5699  C CD1 . TYR B  1 196 ? -36.255 -41.914 -18.101  1.00 27.25  ? 196 TYR B CD1 1 
ATOM   5700  C CD2 . TYR B  1 196 ? -38.040 -42.525 -19.520  1.00 30.01  ? 196 TYR B CD2 1 
ATOM   5701  C CE1 . TYR B  1 196 ? -36.935 -40.783 -17.728  1.00 28.69  ? 196 TYR B CE1 1 
ATOM   5702  C CE2 . TYR B  1 196 ? -38.721 -41.400 -19.158  1.00 30.22  ? 196 TYR B CE2 1 
ATOM   5703  C CZ  . TYR B  1 196 ? -38.168 -40.534 -18.262  1.00 27.74  ? 196 TYR B CZ  1 
ATOM   5704  O OH  . TYR B  1 196 ? -38.858 -39.424 -17.910  1.00 32.51  ? 196 TYR B OH  1 
ATOM   5705  N N   . TYR B  1 197 ? -33.134 -44.134 -18.991  1.00 28.05  ? 197 TYR B N   1 
ATOM   5706  C CA  . TYR B  1 197 ? -32.032 -43.732 -18.167  1.00 29.90  ? 197 TYR B CA  1 
ATOM   5707  C C   . TYR B  1 197 ? -30.644 -44.055 -18.749  1.00 28.68  ? 197 TYR B C   1 
ATOM   5708  O O   . TYR B  1 197 ? -29.676 -44.074 -18.042  1.00 28.33  ? 197 TYR B O   1 
ATOM   5709  C CB  . TYR B  1 197 ? -32.223 -44.238 -16.744  1.00 27.92  ? 197 TYR B CB  1 
ATOM   5710  C CG  . TYR B  1 197 ? -33.383 -43.555 -16.080  1.00 30.06  ? 197 TYR B CG  1 
ATOM   5711  C CD1 . TYR B  1 197 ? -33.287 -42.235 -15.702  1.00 23.55  ? 197 TYR B CD1 1 
ATOM   5712  C CD2 . TYR B  1 197 ? -34.582 -44.209 -15.869  1.00 24.62  ? 197 TYR B CD2 1 
ATOM   5713  C CE1 . TYR B  1 197 ? -34.336 -41.583 -15.128  1.00 28.41  ? 197 TYR B CE1 1 
ATOM   5714  C CE2 . TYR B  1 197 ? -35.641 -43.558 -15.289  1.00 25.20  ? 197 TYR B CE2 1 
ATOM   5715  C CZ  . TYR B  1 197 ? -35.501 -42.237 -14.922  1.00 31.82  ? 197 TYR B CZ  1 
ATOM   5716  O OH  . TYR B  1 197 ? -36.511 -41.552 -14.339  1.00 33.10  ? 197 TYR B OH  1 
ATOM   5717  N N   . HIS B  1 198 ? -30.603 -44.252 -20.050  1.00 29.34  ? 198 HIS B N   1 
ATOM   5718  C CA  . HIS B  1 198 ? -29.352 -44.534 -20.739  1.00 25.77  ? 198 HIS B CA  1 
ATOM   5719  C C   . HIS B  1 198 ? -28.664 -45.772 -20.159  1.00 26.77  ? 198 HIS B C   1 
ATOM   5720  O O   . HIS B  1 198 ? -27.478 -45.697 -19.814  1.00 28.35  ? 198 HIS B O   1 
ATOM   5721  C CB  . HIS B  1 198 ? -28.438 -43.309 -20.629  1.00 26.05  ? 198 HIS B CB  1 
ATOM   5722  C CG  . HIS B  1 198 ? -27.353 -43.243 -21.659  1.00 25.89  ? 198 HIS B CG  1 
ATOM   5723  N ND1 . HIS B  1 198 ? -26.043 -43.561 -21.373  1.00 23.29  ? 198 HIS B ND1 1 
ATOM   5724  C CD2 . HIS B  1 198 ? -27.371 -42.856 -22.960  1.00 26.55  ? 198 HIS B CD2 1 
ATOM   5725  C CE1 . HIS B  1 198 ? -25.304 -43.406 -22.459  1.00 26.58  ? 198 HIS B CE1 1 
ATOM   5726  N NE2 . HIS B  1 198 ? -26.086 -42.979 -23.437  1.00 25.27  ? 198 HIS B NE2 1 
ATOM   5727  N N   . PRO B  1 199 ? -29.367 -46.920 -20.001  1.00 29.99  ? 199 PRO B N   1 
ATOM   5728  C CA  . PRO B  1 199 ? -28.705 -48.116 -19.460  1.00 30.22  ? 199 PRO B CA  1 
ATOM   5729  C C   . PRO B  1 199 ? -28.029 -48.951 -20.532  1.00 34.76  ? 199 PRO B C   1 
ATOM   5730  O O   . PRO B  1 199 ? -28.163 -48.661 -21.729  1.00 30.81  ? 199 PRO B O   1 
ATOM   5731  C CB  . PRO B  1 199 ? -29.865 -48.891 -18.838  1.00 32.00  ? 199 PRO B CB  1 
ATOM   5732  C CG  . PRO B  1 199 ? -30.992 -48.616 -19.764  1.00 35.60  ? 199 PRO B CG  1 
ATOM   5733  C CD  . PRO B  1 199 ? -30.791 -47.195 -20.283  1.00 33.74  ? 199 PRO B CD  1 
ATOM   5734  N N   . LEU B  1 200 ? -27.346 -50.027 -20.120  1.00 31.19  ? 200 LEU B N   1 
ATOM   5735  C CA  . LEU B  1 200 ? -26.774 -50.986 -21.063  1.00 34.67  ? 200 LEU B CA  1 
ATOM   5736  C C   . LEU B  1 200 ? -27.799 -52.093 -21.295  1.00 37.09  ? 200 LEU B C   1 
ATOM   5737  O O   . LEU B  1 200 ? -27.831 -53.097 -20.585  1.00 34.06  ? 200 LEU B O   1 
ATOM   5738  C CB  . LEU B  1 200 ? -25.449 -51.523 -20.537  1.00 35.73  ? 200 LEU B CB  1 
ATOM   5739  C CG  . LEU B  1 200 ? -24.293 -50.523 -20.538  1.00 36.86  ? 200 LEU B CG  1 
ATOM   5740  C CD1 . LEU B  1 200 ? -23.154 -51.113 -19.774  1.00 42.61  ? 200 LEU B CD1 1 
ATOM   5741  C CD2 . LEU B  1 200 ? -23.852 -50.186 -21.969  1.00 36.37  ? 200 LEU B CD2 1 
ATOM   5742  N N   . ILE B  1 201 ? -28.646 -51.904 -22.322  1.00 32.20  ? 201 ILE B N   1 
ATOM   5743  C CA  . ILE B  1 201 ? -29.741 -52.852 -22.572  1.00 28.44  ? 201 ILE B CA  1 
ATOM   5744  C C   . ILE B  1 201 ? -29.251 -54.284 -22.768  1.00 31.21  ? 201 ILE B C   1 
ATOM   5745  O O   . ILE B  1 201 ? -29.885 -55.208 -22.222  1.00 30.99  ? 201 ILE B O   1 
ATOM   5746  C CB  . ILE B  1 201 ? -30.618 -52.354 -23.733  1.00 31.91  ? 201 ILE B CB  1 
ATOM   5747  C CG1 . ILE B  1 201 ? -31.408 -51.074 -23.366  1.00 28.19  ? 201 ILE B CG1 1 
ATOM   5748  C CG2 . ILE B  1 201 ? -31.529 -53.452 -24.243  1.00 28.32  ? 201 ILE B CG2 1 
ATOM   5749  C CD1 . ILE B  1 201 ? -32.524 -51.243 -22.310  1.00 29.70  ? 201 ILE B CD1 1 
ATOM   5750  N N   . PRO B  1 202 ? -28.168 -54.566 -23.521  1.00 25.23  ? 202 PRO B N   1 
ATOM   5751  C CA  . PRO B  1 202 ? -27.757 -55.980 -23.676  1.00 24.42  ? 202 PRO B CA  1 
ATOM   5752  C C   . PRO B  1 202 ? -27.500 -56.688 -22.357  1.00 23.73  ? 202 PRO B C   1 
ATOM   5753  O O   . PRO B  1 202 ? -27.763 -57.890 -22.254  1.00 27.46  ? 202 PRO B O   1 
ATOM   5754  C CB  . PRO B  1 202 ? -26.485 -55.887 -24.530  1.00 26.23  ? 202 PRO B CB  1 
ATOM   5755  C CG  . PRO B  1 202 ? -26.718 -54.653 -25.376  1.00 31.04  ? 202 PRO B CG  1 
ATOM   5756  C CD  . PRO B  1 202 ? -27.392 -53.684 -24.417  1.00 30.07  ? 202 PRO B CD  1 
ATOM   5757  N N   . ILE B  1 203 ? -27.017 -55.966 -21.343  1.00 23.15  ? 203 ILE B N   1 
ATOM   5758  C CA  . ILE B  1 203 ? -26.724 -56.564 -20.045  1.00 23.32  ? 203 ILE B CA  1 
ATOM   5759  C C   . ILE B  1 203 ? -28.005 -56.807 -19.256  1.00 27.88  ? 203 ILE B C   1 
ATOM   5760  O O   . ILE B  1 203 ? -28.134 -57.817 -18.562  1.00 29.30  ? 203 ILE B O   1 
ATOM   5761  C CB  . ILE B  1 203 ? -25.747 -55.679 -19.253  1.00 25.40  ? 203 ILE B CB  1 
ATOM   5762  C CG1 . ILE B  1 203 ? -24.376 -55.676 -19.922  1.00 29.68  ? 203 ILE B CG1 1 
ATOM   5763  C CG2 . ILE B  1 203 ? -25.613 -56.172 -17.777  1.00 22.30  ? 203 ILE B CG2 1 
ATOM   5764  C CD1 . ILE B  1 203 ? -23.377 -54.816 -19.195  1.00 31.28  ? 203 ILE B CD1 1 
ATOM   5765  N N   . LEU B  1 204 ? -28.974 -55.897 -19.334  1.00 29.16  ? 204 LEU B N   1 
ATOM   5766  C CA  . LEU B  1 204 ? -30.204 -56.138 -18.588  1.00 25.87  ? 204 LEU B CA  1 
ATOM   5767  C C   . LEU B  1 204 ? -30.956 -57.317 -19.181  1.00 27.00  ? 204 LEU B C   1 
ATOM   5768  O O   . LEU B  1 204 ? -31.505 -58.143 -18.448  1.00 23.73  ? 204 LEU B O   1 
ATOM   5769  C CB  . LEU B  1 204 ? -31.079 -54.876 -18.560  1.00 21.30  ? 204 LEU B CB  1 
ATOM   5770  C CG  . LEU B  1 204 ? -30.478 -53.553 -18.059  1.00 24.06  ? 204 LEU B CG  1 
ATOM   5771  C CD1 . LEU B  1 204 ? -31.514 -52.393 -18.110  1.00 19.61  ? 204 LEU B CD1 1 
ATOM   5772  C CD2 . LEU B  1 204 ? -29.875 -53.667 -16.676  1.00 26.45  ? 204 LEU B CD2 1 
ATOM   5773  N N   . LEU B  1 205 ? -30.955 -57.437 -20.515  1.00 29.25  ? 205 LEU B N   1 
ATOM   5774  C CA  . LEU B  1 205 ? -31.574 -58.587 -21.157  1.00 31.28  ? 205 LEU B CA  1 
ATOM   5775  C C   . LEU B  1 205 ? -30.825 -59.874 -20.853  1.00 33.53  ? 205 LEU B C   1 
ATOM   5776  O O   . LEU B  1 205 ? -31.449 -60.933 -20.752  1.00 37.39  ? 205 LEU B O   1 
ATOM   5777  C CB  . LEU B  1 205 ? -31.646 -58.375 -22.676  1.00 28.12  ? 205 LEU B CB  1 
ATOM   5778  C CG  . LEU B  1 205 ? -32.710 -57.325 -23.039  1.00 30.96  ? 205 LEU B CG  1 
ATOM   5779  C CD1 . LEU B  1 205 ? -32.676 -56.892 -24.513  1.00 29.31  ? 205 LEU B CD1 1 
ATOM   5780  C CD2 . LEU B  1 205 ? -34.075 -57.845 -22.659  1.00 30.78  ? 205 LEU B CD2 1 
ATOM   5781  N N   . ASN B  1 206 ? -29.502 -59.813 -20.733  1.00 32.01  ? 206 ASN B N   1 
ATOM   5782  C CA  . ASN B  1 206 ? -28.687 -61.023 -20.653  1.00 37.74  ? 206 ASN B CA  1 
ATOM   5783  C C   . ASN B  1 206 ? -27.256 -60.686 -20.262  1.00 34.82  ? 206 ASN B C   1 
ATOM   5784  O O   . ASN B  1 206 ? -26.425 -60.405 -21.135  1.00 33.79  ? 206 ASN B O   1 
ATOM   5785  C CB  . ASN B  1 206 ? -28.696 -61.763 -21.992  1.00 46.93  ? 206 ASN B CB  1 
ATOM   5786  C CG  . ASN B  1 206 ? -28.141 -63.171 -21.888  1.00 53.04  ? 206 ASN B CG  1 
ATOM   5787  O OD1 . ASN B  1 206 ? -27.317 -63.478 -21.023  1.00 48.45  ? 206 ASN B OD1 1 
ATOM   5788  N ND2 . ASN B  1 206 ? -28.600 -64.038 -22.780  1.00 58.67  ? 206 ASN B ND2 1 
ATOM   5789  N N   . PRO B  1 207 ? -26.927 -60.701 -18.969  1.00 32.05  ? 207 PRO B N   1 
ATOM   5790  C CA  . PRO B  1 207 ? -25.564 -60.327 -18.558  1.00 28.71  ? 207 PRO B CA  1 
ATOM   5791  C C   . PRO B  1 207 ? -24.478 -61.217 -19.147  1.00 29.72  ? 207 PRO B C   1 
ATOM   5792  O O   . PRO B  1 207 ? -23.329 -60.777 -19.252  1.00 34.98  ? 207 PRO B O   1 
ATOM   5793  C CB  . PRO B  1 207 ? -25.615 -60.444 -17.021  1.00 29.67  ? 207 PRO B CB  1 
ATOM   5794  C CG  . PRO B  1 207 ? -27.064 -60.355 -16.676  1.00 26.97  ? 207 PRO B CG  1 
ATOM   5795  C CD  . PRO B  1 207 ? -27.807 -60.975 -17.819  1.00 31.14  ? 207 PRO B CD  1 
ATOM   5796  N N   . ASN B  1 208 ? -24.796 -62.453 -19.530  1.00 25.35  ? 208 ASN B N   1 
ATOM   5797  C CA  . ASN B  1 208 ? -23.792 -63.347 -20.086  1.00 29.08  ? 208 ASN B CA  1 
ATOM   5798  C C   . ASN B  1 208 ? -23.317 -62.911 -21.466  1.00 31.89  ? 208 ASN B C   1 
ATOM   5799  O O   . ASN B  1 208 ? -22.310 -63.436 -21.945  1.00 27.19  ? 208 ASN B O   1 
ATOM   5800  C CB  . ASN B  1 208 ? -24.339 -64.772 -20.140  1.00 29.82  ? 208 ASN B CB  1 
ATOM   5801  C CG  . ASN B  1 208 ? -24.722 -65.285 -18.766  1.00 35.97  ? 208 ASN B CG  1 
ATOM   5802  O OD1 . ASN B  1 208 ? -24.047 -64.990 -17.779  1.00 30.93  ? 208 ASN B OD1 1 
ATOM   5803  N ND2 . ASN B  1 208 ? -25.811 -66.038 -18.690  1.00 38.06  ? 208 ASN B ND2 1 
ATOM   5804  N N   . CYS B  1 209 ? -23.975 -61.926 -22.085  1.00 36.94  ? 209 CYS B N   1 
ATOM   5805  C CA  . CYS B  1 209 ? -23.543 -61.447 -23.392  1.00 33.67  ? 209 CYS B CA  1 
ATOM   5806  C C   . CYS B  1 209 ? -22.169 -60.788 -23.344  1.00 33.41  ? 209 CYS B C   1 
ATOM   5807  O O   . CYS B  1 209 ? -21.520 -60.651 -24.393  1.00 29.89  ? 209 CYS B O   1 
ATOM   5808  C CB  . CYS B  1 209 ? -24.582 -60.484 -23.966  1.00 34.11  ? 209 CYS B CB  1 
ATOM   5809  S SG  . CYS B  1 209 ? -24.542 -58.824 -23.324  1.00 36.18  ? 209 CYS B SG  1 
ATOM   5810  N N   . VAL B  1 210 ? -21.694 -60.410 -22.154  1.00 33.37  ? 210 VAL B N   1 
ATOM   5811  C CA  . VAL B  1 210 ? -20.344 -59.878 -22.041  1.00 32.47  ? 210 VAL B CA  1 
ATOM   5812  C C   . VAL B  1 210 ? -19.295 -60.911 -22.448  1.00 31.10  ? 210 VAL B C   1 
ATOM   5813  O O   . VAL B  1 210 ? -18.157 -60.546 -22.756  1.00 34.79  ? 210 VAL B O   1 
ATOM   5814  C CB  . VAL B  1 210 ? -20.099 -59.366 -20.603  1.00 31.44  ? 210 VAL B CB  1 
ATOM   5815  C CG1 . VAL B  1 210 ? -21.116 -58.290 -20.263  1.00 32.65  ? 210 VAL B CG1 1 
ATOM   5816  C CG2 . VAL B  1 210 ? -20.161 -60.506 -19.586  1.00 31.38  ? 210 VAL B CG2 1 
ATOM   5817  N N   . TYR B  1 211 ? -19.641 -62.201 -22.447  1.00 27.32  ? 211 TYR B N   1 
ATOM   5818  C CA  . TYR B  1 211 ? -18.667 -63.242 -22.756  1.00 30.01  ? 211 TYR B CA  1 
ATOM   5819  C C   . TYR B  1 211 ? -18.478 -63.464 -24.251  1.00 29.62  ? 211 TYR B C   1 
ATOM   5820  O O   . TYR B  1 211 ? -17.646 -64.291 -24.648  1.00 33.62  ? 211 TYR B O   1 
ATOM   5821  C CB  . TYR B  1 211 ? -19.083 -64.548 -22.094  1.00 32.49  ? 211 TYR B CB  1 
ATOM   5822  C CG  . TYR B  1 211 ? -19.135 -64.440 -20.602  1.00 33.23  ? 211 TYR B CG  1 
ATOM   5823  C CD1 . TYR B  1 211 ? -17.981 -64.201 -19.866  1.00 33.51  ? 211 TYR B CD1 1 
ATOM   5824  C CD2 . TYR B  1 211 ? -20.337 -64.546 -19.927  1.00 35.59  ? 211 TYR B CD2 1 
ATOM   5825  C CE1 . TYR B  1 211 ? -18.022 -64.104 -18.490  1.00 37.13  ? 211 TYR B CE1 1 
ATOM   5826  C CE2 . TYR B  1 211 ? -20.390 -64.432 -18.543  1.00 40.84  ? 211 TYR B CE2 1 
ATOM   5827  C CZ  . TYR B  1 211 ? -19.227 -64.215 -17.839  1.00 41.85  ? 211 TYR B CZ  1 
ATOM   5828  O OH  . TYR B  1 211 ? -19.261 -64.114 -16.474  1.00 48.41  ? 211 TYR B OH  1 
ATOM   5829  N N   . GLU B  1 212 ? -19.230 -62.758 -25.083  1.00 31.28  ? 212 GLU B N   1 
ATOM   5830  C CA  . GLU B  1 212 ? -18.996 -62.820 -26.518  1.00 37.35  ? 212 GLU B CA  1 
ATOM   5831  C C   . GLU B  1 212 ? -17.704 -62.121 -26.927  1.00 41.04  ? 212 GLU B C   1 
ATOM   5832  O O   . GLU B  1 212 ? -17.210 -62.370 -28.029  1.00 43.37  ? 212 GLU B O   1 
ATOM   5833  C CB  . GLU B  1 212 ? -20.188 -62.207 -27.247  1.00 37.22  ? 212 GLU B CB  1 
ATOM   5834  C CG  . GLU B  1 212 ? -21.481 -62.955 -27.007  1.00 44.33  ? 212 GLU B CG  1 
ATOM   5835  C CD  . GLU B  1 212 ? -22.662 -62.342 -27.739  1.00 50.47  ? 212 GLU B CD  1 
ATOM   5836  O OE1 . GLU B  1 212 ? -23.811 -62.605 -27.334  1.00 53.45  ? 212 GLU B OE1 1 
ATOM   5837  O OE2 . GLU B  1 212 ? -22.443 -61.593 -28.714  1.00 53.95  ? 212 GLU B OE2 1 
ATOM   5838  N N   . THR B  1 213 ? -17.145 -61.258 -26.072  1.00 44.53  ? 213 THR B N   1 
ATOM   5839  C CA  . THR B  1 213 ? -15.969 -60.467 -26.435  1.00 44.73  ? 213 THR B CA  1 
ATOM   5840  C C   . THR B  1 213 ? -14.867 -60.516 -25.378  1.00 43.36  ? 213 THR B C   1 
ATOM   5841  O O   . THR B  1 213 ? -13.692 -60.329 -25.701  1.00 40.44  ? 213 THR B O   1 
ATOM   5842  C CB  . THR B  1 213 ? -16.362 -59.010 -26.677  1.00 38.65  ? 213 THR B CB  1 
ATOM   5843  O OG1 . THR B  1 213 ? -17.052 -58.515 -25.525  1.00 39.43  ? 213 THR B OG1 1 
ATOM   5844  C CG2 . THR B  1 213 ? -17.269 -58.883 -27.925  1.00 37.95  ? 213 THR B CG2 1 
ATOM   5845  N N   . THR B  1 214 ? -15.220 -60.719 -24.111  1.00 40.26  ? 214 THR B N   1 
ATOM   5846  C CA  . THR B  1 214 ? -14.238 -60.823 -23.032  1.00 35.08  ? 214 THR B CA  1 
ATOM   5847  C C   . THR B  1 214 ? -14.564 -62.078 -22.237  1.00 33.12  ? 214 THR B C   1 
ATOM   5848  O O   . THR B  1 214 ? -15.262 -62.018 -21.212  1.00 31.84  ? 214 THR B O   1 
ATOM   5849  C CB  . THR B  1 214 ? -14.239 -59.587 -22.133  1.00 35.88  ? 214 THR B CB  1 
ATOM   5850  O OG1 . THR B  1 214 ? -15.560 -59.379 -21.622  1.00 33.18  ? 214 THR B OG1 1 
ATOM   5851  C CG2 . THR B  1 214 ? -13.779 -58.333 -22.921  1.00 33.18  ? 214 THR B CG2 1 
ATOM   5852  N N   . PRO B  1 215 ? -14.086 -63.240 -22.694  1.00 35.41  ? 215 PRO B N   1 
ATOM   5853  C CA  . PRO B  1 215 ? -14.438 -64.496 -22.012  1.00 40.10  ? 215 PRO B CA  1 
ATOM   5854  C C   . PRO B  1 215 ? -13.878 -64.607 -20.607  1.00 45.74  ? 215 PRO B C   1 
ATOM   5855  O O   . PRO B  1 215 ? -14.399 -65.396 -19.804  1.00 46.91  ? 215 PRO B O   1 
ATOM   5856  C CB  . PRO B  1 215 ? -13.855 -65.575 -22.940  1.00 43.68  ? 215 PRO B CB  1 
ATOM   5857  C CG  . PRO B  1 215 ? -12.857 -64.847 -23.821  1.00 38.64  ? 215 PRO B CG  1 
ATOM   5858  C CD  . PRO B  1 215 ? -13.390 -63.474 -23.981  1.00 32.93  ? 215 PRO B CD  1 
ATOM   5859  N N   . ASN B  1 216 ? -12.854 -63.829 -20.278  1.00 45.66  ? 216 ASN B N   1 
ATOM   5860  C CA  . ASN B  1 216 ? -12.177 -63.952 -19.000  1.00 49.73  ? 216 ASN B CA  1 
ATOM   5861  C C   . ASN B  1 216 ? -12.787 -63.099 -17.904  1.00 47.82  ? 216 ASN B C   1 
ATOM   5862  O O   . ASN B  1 216 ? -12.379 -63.230 -16.747  1.00 49.91  ? 216 ASN B O   1 
ATOM   5863  C CB  . ASN B  1 216 ? -10.705 -63.587 -19.161  1.00 49.66  ? 216 ASN B CB  1 
ATOM   5864  C CG  . ASN B  1 216 ? -9.870  -64.782 -19.511  1.00 51.33  ? 216 ASN B CG  1 
ATOM   5865  O OD1 . ASN B  1 216 ? -9.247  -64.832 -20.570  1.00 50.21  ? 216 ASN B OD1 1 
ATOM   5866  N ND2 . ASN B  1 216 ? -9.866  -65.769 -18.626  1.00 55.39  ? 216 ASN B ND2 1 
ATOM   5867  N N   . VAL B  1 217 ? -13.754 -62.241 -18.230  1.00 47.16  ? 217 VAL B N   1 
ATOM   5868  C CA  . VAL B  1 217 ? -14.247 -61.277 -17.258  1.00 41.26  ? 217 VAL B CA  1 
ATOM   5869  C C   . VAL B  1 217 ? -15.061 -61.982 -16.177  1.00 37.89  ? 217 VAL B C   1 
ATOM   5870  O O   . VAL B  1 217 ? -15.909 -62.844 -16.458  1.00 34.08  ? 217 VAL B O   1 
ATOM   5871  C CB  . VAL B  1 217 ? -15.064 -60.181 -17.971  1.00 39.40  ? 217 VAL B CB  1 
ATOM   5872  C CG1 . VAL B  1 217 ? -16.394 -60.717 -18.500  1.00 33.87  ? 217 VAL B CG1 1 
ATOM   5873  C CG2 . VAL B  1 217 ? -15.316 -59.047 -17.033  1.00 38.77  ? 217 VAL B CG2 1 
ATOM   5874  N N   . LYS B  1 218 ? -14.793 -61.632 -14.921  1.00 36.45  ? 218 LYS B N   1 
ATOM   5875  C CA  . LYS B  1 218 ? -15.649 -62.030 -13.812  1.00 31.25  ? 218 LYS B CA  1 
ATOM   5876  C C   . LYS B  1 218 ? -16.805 -61.043 -13.707  1.00 32.29  ? 218 LYS B C   1 
ATOM   5877  O O   . LYS B  1 218 ? -16.596 -59.830 -13.787  1.00 33.10  ? 218 LYS B O   1 
ATOM   5878  C CB  . LYS B  1 218 ? -14.857 -62.051 -12.499  1.00 36.38  ? 218 LYS B CB  1 
ATOM   5879  C CG  . LYS B  1 218 ? -13.455 -62.625 -12.655  1.00 49.60  ? 218 LYS B CG  1 
ATOM   5880  C CD  . LYS B  1 218 ? -12.514 -62.130 -11.563  1.00 56.49  ? 218 LYS B CD  1 
ATOM   5881  C CE  . LYS B  1 218 ? -12.796 -62.815 -10.241  1.00 58.95  ? 218 LYS B CE  1 
ATOM   5882  N NZ  . LYS B  1 218 ? -12.295 -64.221 -10.238  1.00 60.55  ? 218 LYS B NZ  1 
ATOM   5883  N N   . ILE B  1 219 ? -18.019 -61.558 -13.547  1.00 33.63  ? 219 ILE B N   1 
ATOM   5884  C CA  . ILE B  1 219 ? -19.180 -60.719 -13.253  1.00 30.62  ? 219 ILE B CA  1 
ATOM   5885  C C   . ILE B  1 219 ? -19.871 -61.285 -12.023  1.00 29.50  ? 219 ILE B C   1 
ATOM   5886  O O   . ILE B  1 219 ? -19.697 -62.470 -11.684  1.00 28.76  ? 219 ILE B O   1 
ATOM   5887  C CB  . ILE B  1 219 ? -20.169 -60.650 -14.441  1.00 29.82  ? 219 ILE B CB  1 
ATOM   5888  C CG1 . ILE B  1 219 ? -20.965 -61.956 -14.542  1.00 33.25  ? 219 ILE B CG1 1 
ATOM   5889  C CG2 . ILE B  1 219 ? -19.458 -60.263 -15.751  1.00 26.73  ? 219 ILE B CG2 1 
ATOM   5890  C CD1 . ILE B  1 219 ? -22.172 -61.867 -15.447  1.00 36.26  ? 219 ILE B CD1 1 
ATOM   5891  N N   . PRO B  1 220 ? -20.672 -60.471 -11.340  1.00 30.96  ? 220 PRO B N   1 
ATOM   5892  C CA  . PRO B  1 220 ? -21.382 -60.964 -10.154  1.00 34.51  ? 220 PRO B CA  1 
ATOM   5893  C C   . PRO B  1 220 ? -22.528 -61.885 -10.538  1.00 34.14  ? 220 PRO B C   1 
ATOM   5894  O O   . PRO B  1 220 ? -22.940 -61.972 -11.693  1.00 32.61  ? 220 PRO B O   1 
ATOM   5895  C CB  . PRO B  1 220 ? -21.887 -59.682 -9.473   1.00 35.08  ? 220 PRO B CB  1 
ATOM   5896  C CG  . PRO B  1 220 ? -21.912 -58.665 -10.520  1.00 30.72  ? 220 PRO B CG  1 
ATOM   5897  C CD  . PRO B  1 220 ? -20.786 -59.002 -11.470  1.00 31.12  ? 220 PRO B CD  1 
ATOM   5898  N N   . ASP B  1 221 ? -23.033 -62.592 -9.525   1.00 34.41  ? 221 ASP B N   1 
ATOM   5899  C CA  . ASP B  1 221 ? -24.131 -63.556 -9.642   1.00 30.09  ? 221 ASP B CA  1 
ATOM   5900  C C   . ASP B  1 221 ? -25.430 -62.788 -9.899   1.00 31.30  ? 221 ASP B C   1 
ATOM   5901  O O   . ASP B  1 221 ? -26.007 -62.204 -8.980   1.00 32.42  ? 221 ASP B O   1 
ATOM   5902  C CB  . ASP B  1 221 ? -24.203 -64.382 -8.359   1.00 35.35  ? 221 ASP B CB  1 
ATOM   5903  C CG  . ASP B  1 221 ? -25.283 -65.457 -8.383   1.00 39.71  ? 221 ASP B CG  1 
ATOM   5904  O OD1 . ASP B  1 221 ? -25.670 -65.929 -9.466   1.00 39.51  ? 221 ASP B OD1 1 
ATOM   5905  O OD2 . ASP B  1 221 ? -25.752 -65.842 -7.288   1.00 46.09  ? 221 ASP B OD2 1 
ATOM   5906  N N   . PHE B  1 222 ? -25.898 -62.772 -11.153  1.00 30.39  ? 222 PHE B N   1 
ATOM   5907  C CA  . PHE B  1 222 ? -27.114 -62.038 -11.520  1.00 29.07  ? 222 PHE B CA  1 
ATOM   5908  C C   . PHE B  1 222 ? -28.337 -62.852 -11.094  1.00 32.73  ? 222 PHE B C   1 
ATOM   5909  O O   . PHE B  1 222 ? -28.985 -63.543 -11.881  1.00 38.21  ? 222 PHE B O   1 
ATOM   5910  C CB  . PHE B  1 222 ? -27.111 -61.704 -13.012  1.00 29.00  ? 222 PHE B CB  1 
ATOM   5911  C CG  . PHE B  1 222 ? -26.402 -60.406 -13.325  1.00 27.05  ? 222 PHE B CG  1 
ATOM   5912  C CD1 . PHE B  1 222 ? -25.019 -60.358 -13.393  1.00 29.22  ? 222 PHE B CD1 1 
ATOM   5913  C CD2 . PHE B  1 222 ? -27.107 -59.231 -13.472  1.00 28.80  ? 222 PHE B CD2 1 
ATOM   5914  C CE1 . PHE B  1 222 ? -24.354 -59.170 -13.631  1.00 22.95  ? 222 PHE B CE1 1 
ATOM   5915  C CE2 . PHE B  1 222 ? -26.449 -58.026 -13.722  1.00 30.48  ? 222 PHE B CE2 1 
ATOM   5916  C CZ  . PHE B  1 222 ? -25.063 -58.003 -13.800  1.00 25.96  ? 222 PHE B CZ  1 
ATOM   5917  N N   . ALA B  1 223 ? -28.655 -62.755 -9.798   1.00 34.22  ? 223 ALA B N   1 
ATOM   5918  C CA  . ALA B  1 223 ? -29.668 -63.582 -9.155   1.00 35.48  ? 223 ALA B CA  1 
ATOM   5919  C C   . ALA B  1 223 ? -31.097 -63.124 -9.414   1.00 41.52  ? 223 ALA B C   1 
ATOM   5920  O O   . ALA B  1 223 ? -32.028 -63.837 -9.018   1.00 48.61  ? 223 ALA B O   1 
ATOM   5921  C CB  . ALA B  1 223 ? -29.427 -63.623 -7.640   1.00 33.12  ? 223 ALA B CB  1 
ATOM   5922  N N   . VAL B  1 224 ? -31.295 -61.950 -10.020  1.00 32.33  ? 224 VAL B N   1 
ATOM   5923  C CA  . VAL B  1 224 ? -32.609 -61.442 -10.400  1.00 37.22  ? 224 VAL B CA  1 
ATOM   5924  C C   . VAL B  1 224 ? -32.576 -61.103 -11.884  1.00 40.10  ? 224 VAL B C   1 
ATOM   5925  O O   . VAL B  1 224 ? -31.514 -60.984 -12.489  1.00 43.96  ? 224 VAL B O   1 
ATOM   5926  C CB  . VAL B  1 224 ? -33.024 -60.193 -9.596   1.00 34.41  ? 224 VAL B CB  1 
ATOM   5927  C CG1 . VAL B  1 224 ? -33.487 -60.575 -8.219   1.00 39.74  ? 224 VAL B CG1 1 
ATOM   5928  C CG2 . VAL B  1 224 ? -31.871 -59.195 -9.532   1.00 31.84  ? 224 VAL B CG2 1 
ATOM   5929  N N   . SER B  1 225 ? -33.760 -60.901 -12.456  1.00 39.84  ? 225 SER B N   1 
ATOM   5930  C CA  . SER B  1 225 ? -33.898 -60.557 -13.865  1.00 34.13  ? 225 SER B CA  1 
ATOM   5931  C C   . SER B  1 225 ? -34.114 -59.058 -14.068  1.00 35.59  ? 225 SER B C   1 
ATOM   5932  O O   . SER B  1 225 ? -34.902 -58.427 -13.355  1.00 32.12  ? 225 SER B O   1 
ATOM   5933  C CB  . SER B  1 225 ? -35.062 -61.326 -14.493  1.00 37.80  ? 225 SER B CB  1 
ATOM   5934  O OG  . SER B  1 225 ? -35.313 -60.868 -15.814  1.00 36.10  ? 225 SER B OG  1 
ATOM   5935  N N   . PHE B  1 226 ? -33.429 -58.497 -15.068  1.00 35.40  ? 226 PHE B N   1 
ATOM   5936  C CA  . PHE B  1 226 ? -33.639 -57.118 -15.489  1.00 35.00  ? 226 PHE B CA  1 
ATOM   5937  C C   . PHE B  1 226 ? -34.334 -57.034 -16.839  1.00 34.41  ? 226 PHE B C   1 
ATOM   5938  O O   . PHE B  1 226 ? -34.437 -55.942 -17.415  1.00 32.07  ? 226 PHE B O   1 
ATOM   5939  C CB  . PHE B  1 226 ? -32.305 -56.365 -15.519  1.00 32.23  ? 226 PHE B CB  1 
ATOM   5940  C CG  . PHE B  1 226 ? -31.683 -56.192 -14.141  1.00 30.72  ? 226 PHE B CG  1 
ATOM   5941  C CD1 . PHE B  1 226 ? -31.994 -55.094 -13.355  1.00 23.47  ? 226 PHE B CD1 1 
ATOM   5942  C CD2 . PHE B  1 226 ? -30.801 -57.131 -13.641  1.00 28.56  ? 226 PHE B CD2 1 
ATOM   5943  C CE1 . PHE B  1 226 ? -31.431 -54.927 -12.088  1.00 31.36  ? 226 PHE B CE1 1 
ATOM   5944  C CE2 . PHE B  1 226 ? -30.227 -56.972 -12.365  1.00 25.13  ? 226 PHE B CE2 1 
ATOM   5945  C CZ  . PHE B  1 226 ? -30.547 -55.877 -11.595  1.00 27.70  ? 226 PHE B CZ  1 
ATOM   5946  N N   . ARG B  1 227 ? -34.831 -58.159 -17.351  1.00 32.87  ? 227 ARG B N   1 
ATOM   5947  C CA  . ARG B  1 227 ? -35.396 -58.159 -18.698  1.00 34.06  ? 227 ARG B CA  1 
ATOM   5948  C C   . ARG B  1 227 ? -36.614 -57.252 -18.781  1.00 37.18  ? 227 ARG B C   1 
ATOM   5949  O O   . ARG B  1 227 ? -36.737 -56.456 -19.719  1.00 31.82  ? 227 ARG B O   1 
ATOM   5950  C CB  . ARG B  1 227 ? -35.739 -59.587 -19.132  1.00 32.99  ? 227 ARG B CB  1 
ATOM   5951  C CG  . ARG B  1 227 ? -34.507 -60.458 -19.322  1.00 35.90  ? 227 ARG B CG  1 
ATOM   5952  C CD  . ARG B  1 227 ? -34.845 -61.848 -19.802  1.00 38.89  ? 227 ARG B CD  1 
ATOM   5953  N NE  . ARG B  1 227 ? -35.576 -61.816 -21.057  1.00 42.55  ? 227 ARG B NE  1 
ATOM   5954  C CZ  . ARG B  1 227 ? -34.999 -61.692 -22.246  1.00 43.39  ? 227 ARG B CZ  1 
ATOM   5955  N NH1 . ARG B  1 227 ? -33.675 -61.593 -22.350  1.00 40.02  ? 227 ARG B NH1 1 
ATOM   5956  N NH2 . ARG B  1 227 ? -35.746 -61.670 -23.330  1.00 46.37  ? 227 ARG B NH2 1 
ATOM   5957  N N   . GLU B  1 228 ? -37.521 -57.334 -17.800  1.00 38.28  ? 228 GLU B N   1 
ATOM   5958  C CA  . GLU B  1 228 ? -38.687 -56.462 -17.868  1.00 41.23  ? 228 GLU B CA  1 
ATOM   5959  C C   . GLU B  1 228 ? -38.293 -55.002 -17.660  1.00 39.44  ? 228 GLU B C   1 
ATOM   5960  O O   . GLU B  1 228 ? -38.928 -54.098 -18.221  1.00 37.06  ? 228 GLU B O   1 
ATOM   5961  C CB  . GLU B  1 228 ? -39.755 -56.904 -16.866  1.00 47.07  ? 228 GLU B CB  1 
ATOM   5962  C CG  . GLU B  1 228 ? -40.428 -58.226 -17.258  1.00 59.05  ? 228 GLU B CG  1 
ATOM   5963  C CD  . GLU B  1 228 ? -41.527 -58.068 -18.322  1.00 71.17  ? 228 GLU B CD  1 
ATOM   5964  O OE1 . GLU B  1 228 ? -41.490 -58.802 -19.340  1.00 74.31  ? 228 GLU B OE1 1 
ATOM   5965  O OE2 . GLU B  1 228 ? -42.426 -57.216 -18.149  1.00 76.03  ? 228 GLU B OE2 1 
ATOM   5966  N N   . ASP B  1 229 ? -37.222 -54.753 -16.901  1.00 35.60  ? 229 ASP B N   1 
ATOM   5967  C CA  . ASP B  1 229 ? -36.720 -53.395 -16.753  1.00 31.31  ? 229 ASP B CA  1 
ATOM   5968  C C   . ASP B  1 229 ? -36.161 -52.862 -18.067  1.00 28.16  ? 229 ASP B C   1 
ATOM   5969  O O   . ASP B  1 229 ? -36.288 -51.664 -18.359  1.00 32.26  ? 229 ASP B O   1 
ATOM   5970  C CB  . ASP B  1 229 ? -35.662 -53.344 -15.646  1.00 28.56  ? 229 ASP B CB  1 
ATOM   5971  C CG  . ASP B  1 229 ? -36.292 -53.295 -14.244  1.00 32.93  ? 229 ASP B CG  1 
ATOM   5972  O OD1 . ASP B  1 229 ? -37.542 -53.321 -14.165  1.00 35.69  ? 229 ASP B OD1 1 
ATOM   5973  O OD2 . ASP B  1 229 ? -35.555 -53.193 -13.230  1.00 30.11  ? 229 ASP B OD2 1 
ATOM   5974  N N   . ALA B  1 230 ? -35.538 -53.720 -18.862  1.00 28.09  ? 230 ALA B N   1 
ATOM   5975  C CA  . ALA B  1 230 ? -35.060 -53.286 -20.170  1.00 30.67  ? 230 ALA B CA  1 
ATOM   5976  C C   . ALA B  1 230 ? -36.219 -52.786 -21.025  1.00 32.21  ? 230 ALA B C   1 
ATOM   5977  O O   . ALA B  1 230 ? -36.138 -51.719 -21.646  1.00 35.30  ? 230 ALA B O   1 
ATOM   5978  C CB  . ALA B  1 230 ? -34.326 -54.426 -20.863  1.00 29.16  ? 230 ALA B CB  1 
ATOM   5979  N N   . SER B  1 231 ? -37.322 -53.532 -21.042  1.00 30.94  ? 231 SER B N   1 
ATOM   5980  C CA  . SER B  1 231 ? -38.473 -53.112 -21.830  1.00 35.27  ? 231 SER B CA  1 
ATOM   5981  C C   . SER B  1 231 ? -39.021 -51.795 -21.315  1.00 34.20  ? 231 SER B C   1 
ATOM   5982  O O   . SER B  1 231 ? -39.481 -50.955 -22.097  1.00 26.09  ? 231 SER B O   1 
ATOM   5983  C CB  . SER B  1 231 ? -39.558 -54.185 -21.794  1.00 42.51  ? 231 SER B CB  1 
ATOM   5984  O OG  . SER B  1 231 ? -39.090 -55.383 -22.389  1.00 49.83  ? 231 SER B OG  1 
ATOM   5985  N N   . LYS B  1 232 ? -38.977 -51.607 -19.994  1.00 34.93  ? 232 LYS B N   1 
ATOM   5986  C CA  . LYS B  1 232 ? -39.542 -50.420 -19.379  1.00 30.27  ? 232 LYS B CA  1 
ATOM   5987  C C   . LYS B  1 232 ? -38.781 -49.178 -19.813  1.00 27.72  ? 232 LYS B C   1 
ATOM   5988  O O   . LYS B  1 232 ? -39.391 -48.162 -20.162  1.00 31.82  ? 232 LYS B O   1 
ATOM   5989  C CB  . LYS B  1 232 ? -39.529 -50.567 -17.855  1.00 33.04  ? 232 LYS B CB  1 
ATOM   5990  C CG  . LYS B  1 232 ? -40.727 -51.273 -17.263  1.00 38.11  ? 232 LYS B CG  1 
ATOM   5991  C CD  . LYS B  1 232 ? -40.929 -50.809 -15.840  1.00 46.57  ? 232 LYS B CD  1 
ATOM   5992  C CE  . LYS B  1 232 ? -41.578 -51.857 -14.976  1.00 55.70  ? 232 LYS B CE  1 
ATOM   5993  N NZ  . LYS B  1 232 ? -41.424 -51.446 -13.557  1.00 62.23  ? 232 LYS B NZ  1 
ATOM   5994  N N   . HIS B  1 233 ? -37.441 -49.244 -19.791  1.00 27.23  ? 233 HIS B N   1 
ATOM   5995  C CA  . HIS B  1 233 ? -36.624 -48.134 -20.273  1.00 26.94  ? 233 HIS B CA  1 
ATOM   5996  C C   . HIS B  1 233 ? -37.049 -47.738 -21.677  1.00 27.75  ? 233 HIS B C   1 
ATOM   5997  O O   . HIS B  1 233 ? -37.225 -46.550 -21.970  1.00 26.65  ? 233 HIS B O   1 
ATOM   5998  C CB  . HIS B  1 233 ? -35.135 -48.499 -20.281  1.00 26.76  ? 233 HIS B CB  1 
ATOM   5999  C CG  . HIS B  1 233 ? -34.474 -48.491 -18.929  1.00 27.54  ? 233 HIS B CG  1 
ATOM   6000  N ND1 . HIS B  1 233 ? -34.043 -47.337 -18.316  1.00 26.59  ? 233 HIS B ND1 1 
ATOM   6001  C CD2 . HIS B  1 233 ? -34.118 -49.509 -18.104  1.00 30.63  ? 233 HIS B CD2 1 
ATOM   6002  C CE1 . HIS B  1 233 ? -33.485 -47.635 -17.154  1.00 28.57  ? 233 HIS B CE1 1 
ATOM   6003  N NE2 . HIS B  1 233 ? -33.515 -48.947 -17.002  1.00 29.91  ? 233 HIS B NE2 1 
ATOM   6004  N N   . VAL B  1 234 ? -37.231 -48.734 -22.555  1.00 27.25  ? 234 VAL B N   1 
ATOM   6005  C CA  . VAL B  1 234 ? -37.610 -48.460 -23.940  1.00 25.03  ? 234 VAL B CA  1 
ATOM   6006  C C   . VAL B  1 234 ? -39.026 -47.899 -24.001  1.00 26.21  ? 234 VAL B C   1 
ATOM   6007  O O   . VAL B  1 234 ? -39.278 -46.886 -24.662  1.00 28.17  ? 234 VAL B O   1 
ATOM   6008  C CB  . VAL B  1 234 ? -37.478 -49.723 -24.823  1.00 27.37  ? 234 VAL B CB  1 
ATOM   6009  C CG1 . VAL B  1 234 ? -37.810 -49.393 -26.293  1.00 24.16  ? 234 VAL B CG1 1 
ATOM   6010  C CG2 . VAL B  1 234 ? -36.075 -50.373 -24.742  1.00 28.29  ? 234 VAL B CG2 1 
ATOM   6011  N N   . GLU B  1 235 ? -39.980 -48.549 -23.325  1.00 26.58  ? 235 GLU B N   1 
ATOM   6012  C CA  . GLU B  1 235 ? -41.365 -48.097 -23.442  1.00 34.02  ? 235 GLU B CA  1 
ATOM   6013  C C   . GLU B  1 235 ? -41.566 -46.731 -22.793  1.00 36.00  ? 235 GLU B C   1 
ATOM   6014  O O   . GLU B  1 235 ? -42.261 -45.868 -23.349  1.00 31.32  ? 235 GLU B O   1 
ATOM   6015  C CB  . GLU B  1 235 ? -42.328 -49.124 -22.848  1.00 41.97  ? 235 GLU B CB  1 
ATOM   6016  C CG  . GLU B  1 235 ? -43.756 -48.979 -23.376  1.00 50.12  ? 235 GLU B CG  1 
ATOM   6017  C CD  . GLU B  1 235 ? -43.908 -49.481 -24.807  1.00 57.17  ? 235 GLU B CD  1 
ATOM   6018  O OE1 . GLU B  1 235 ? -44.442 -48.726 -25.647  1.00 60.91  ? 235 GLU B OE1 1 
ATOM   6019  O OE2 . GLU B  1 235 ? -43.504 -50.632 -25.088  1.00 60.12  ? 235 GLU B OE2 1 
ATOM   6020  N N   . LEU B  1 236 ? -40.959 -46.504 -21.624  1.00 35.62  ? 236 LEU B N   1 
ATOM   6021  C CA  . LEU B  1 236 ? -41.091 -45.199 -20.984  1.00 32.39  ? 236 LEU B CA  1 
ATOM   6022  C C   . LEU B  1 236 ? -40.427 -44.116 -21.817  1.00 31.29  ? 236 LEU B C   1 
ATOM   6023  O O   . LEU B  1 236 ? -40.904 -42.976 -21.844  1.00 29.99  ? 236 LEU B O   1 
ATOM   6024  C CB  . LEU B  1 236 ? -40.503 -45.232 -19.563  1.00 28.65  ? 236 LEU B CB  1 
ATOM   6025  C CG  . LEU B  1 236 ? -41.285 -46.031 -18.511  1.00 34.24  ? 236 LEU B CG  1 
ATOM   6026  C CD1 . LEU B  1 236 ? -40.591 -46.030 -17.152  1.00 30.31  ? 236 LEU B CD1 1 
ATOM   6027  C CD2 . LEU B  1 236 ? -42.724 -45.541 -18.365  1.00 35.49  ? 236 LEU B CD2 1 
ATOM   6028  N N   . ALA B  1 237 ? -39.337 -44.446 -22.516  1.00 31.75  ? 237 ALA B N   1 
ATOM   6029  C CA  . ALA B  1 237 ? -38.747 -43.467 -23.424  1.00 29.10  ? 237 ALA B CA  1 
ATOM   6030  C C   . ALA B  1 237 ? -39.733 -43.101 -24.533  1.00 32.55  ? 237 ALA B C   1 
ATOM   6031  O O   . ALA B  1 237 ? -39.953 -41.916 -24.823  1.00 31.14  ? 237 ALA B O   1 
ATOM   6032  C CB  . ALA B  1 237 ? -37.445 -44.001 -24.008  1.00 25.99  ? 237 ALA B CB  1 
ATOM   6033  N N   . LYS B  1 238 ? -40.358 -44.114 -25.137  1.00 30.53  ? 238 LYS B N   1 
ATOM   6034  C CA  . LYS B  1 238 ? -41.418 -43.880 -26.118  1.00 34.13  ? 238 LYS B CA  1 
ATOM   6035  C C   . LYS B  1 238 ? -42.483 -42.922 -25.593  1.00 33.67  ? 238 LYS B C   1 
ATOM   6036  O O   . LYS B  1 238 ? -42.929 -42.022 -26.315  1.00 34.54  ? 238 LYS B O   1 
ATOM   6037  C CB  . LYS B  1 238 ? -42.053 -45.211 -26.519  1.00 35.07  ? 238 LYS B CB  1 
ATOM   6038  C CG  . LYS B  1 238 ? -41.183 -46.045 -27.426  1.00 37.54  ? 238 LYS B CG  1 
ATOM   6039  C CD  . LYS B  1 238 ? -41.821 -47.379 -27.745  1.00 37.06  ? 238 LYS B CD  1 
ATOM   6040  C CE  . LYS B  1 238 ? -43.085 -47.207 -28.568  1.00 42.40  ? 238 LYS B CE  1 
ATOM   6041  N NZ  . LYS B  1 238 ? -43.777 -48.518 -28.714  1.00 45.62  ? 238 LYS B NZ  1 
ATOM   6042  N N   . GLU B  1 239 ? -42.897 -43.092 -24.335  1.00 32.68  ? 239 GLU B N   1 
ATOM   6043  C CA  . GLU B  1 239 ? -43.926 -42.228 -23.768  1.00 31.87  ? 239 GLU B CA  1 
ATOM   6044  C C   . GLU B  1 239 ? -43.413 -40.810 -23.531  1.00 30.54  ? 239 GLU B C   1 
ATOM   6045  O O   . GLU B  1 239 ? -44.133 -39.843 -23.794  1.00 29.81  ? 239 GLU B O   1 
ATOM   6046  C CB  . GLU B  1 239 ? -44.462 -42.841 -22.478  1.00 33.52  ? 239 GLU B CB  1 
ATOM   6047  C CG  . GLU B  1 239 ? -45.121 -44.189 -22.713  1.00 37.77  ? 239 GLU B CG  1 
ATOM   6048  C CD  . GLU B  1 239 ? -45.748 -44.775 -21.464  1.00 50.71  ? 239 GLU B CD  1 
ATOM   6049  O OE1 . GLU B  1 239 ? -45.485 -44.259 -20.354  1.00 55.40  ? 239 GLU B OE1 1 
ATOM   6050  O OE2 . GLU B  1 239 ? -46.506 -45.761 -21.597  1.00 55.31  ? 239 GLU B OE2 1 
ATOM   6051  N N   . LYS B  1 240 ? -42.173 -40.654 -23.053  1.00 31.39  ? 240 LYS B N   1 
ATOM   6052  C CA  . LYS B  1 240 ? -41.642 -39.302 -22.867  1.00 32.71  ? 240 LYS B CA  1 
ATOM   6053  C C   . LYS B  1 240 ? -41.446 -38.588 -24.202  1.00 30.89  ? 240 LYS B C   1 
ATOM   6054  O O   . LYS B  1 240 ? -41.733 -37.389 -24.324  1.00 29.43  ? 240 LYS B O   1 
ATOM   6055  C CB  . LYS B  1 240 ? -40.321 -39.333 -22.097  1.00 29.68  ? 240 LYS B CB  1 
ATOM   6056  C CG  . LYS B  1 240 ? -39.753 -37.949 -21.796  1.00 27.91  ? 240 LYS B CG  1 
ATOM   6057  C CD  . LYS B  1 240 ? -40.523 -37.277 -20.670  1.00 30.25  ? 240 LYS B CD  1 
ATOM   6058  C CE  . LYS B  1 240 ? -40.039 -35.871 -20.412  1.00 31.75  ? 240 LYS B CE  1 
ATOM   6059  N NZ  . LYS B  1 240 ? -40.698 -35.342 -19.157  1.00 30.47  ? 240 LYS B NZ  1 
ATOM   6060  N N   . TYR B  1 241 ? -40.929 -39.293 -25.206  1.00 33.81  ? 241 TYR B N   1 
ATOM   6061  C CA  . TYR B  1 241 ? -40.809 -38.693 -26.533  1.00 31.48  ? 241 TYR B CA  1 
ATOM   6062  C C   . TYR B  1 241 ? -42.181 -38.265 -27.052  1.00 30.63  ? 241 TYR B C   1 
ATOM   6063  O O   . TYR B  1 241 ? -42.357 -37.135 -27.527  1.00 35.40  ? 241 TYR B O   1 
ATOM   6064  C CB  . TYR B  1 241 ? -40.134 -39.689 -27.472  1.00 31.06  ? 241 TYR B CB  1 
ATOM   6065  C CG  . TYR B  1 241 ? -39.773 -39.186 -28.864  1.00 30.66  ? 241 TYR B CG  1 
ATOM   6066  C CD1 . TYR B  1 241 ? -40.673 -39.285 -29.912  1.00 29.40  ? 241 TYR B CD1 1 
ATOM   6067  C CD2 . TYR B  1 241 ? -38.512 -38.663 -29.137  1.00 32.87  ? 241 TYR B CD2 1 
ATOM   6068  C CE1 . TYR B  1 241 ? -40.338 -38.845 -31.207  1.00 31.89  ? 241 TYR B CE1 1 
ATOM   6069  C CE2 . TYR B  1 241 ? -38.165 -38.234 -30.430  1.00 27.54  ? 241 TYR B CE2 1 
ATOM   6070  C CZ  . TYR B  1 241 ? -39.082 -38.327 -31.448  1.00 28.73  ? 241 TYR B CZ  1 
ATOM   6071  O OH  . TYR B  1 241 ? -38.738 -37.896 -32.707  1.00 32.59  ? 241 TYR B OH  1 
ATOM   6072  N N   . PHE B  1 242 ? -43.170 -39.164 -26.946  1.00 27.53  ? 242 PHE B N   1 
ATOM   6073  C CA  . PHE B  1 242 ? -44.556 -38.848 -27.275  1.00 30.34  ? 242 PHE B CA  1 
ATOM   6074  C C   . PHE B  1 242 ? -45.034 -37.574 -26.576  1.00 35.78  ? 242 PHE B C   1 
ATOM   6075  O O   . PHE B  1 242 ? -45.713 -36.740 -27.187  1.00 38.66  ? 242 PHE B O   1 
ATOM   6076  C CB  . PHE B  1 242 ? -45.436 -40.053 -26.913  1.00 26.15  ? 242 PHE B CB  1 
ATOM   6077  C CG  . PHE B  1 242 ? -46.901 -39.866 -27.202  1.00 30.85  ? 242 PHE B CG  1 
ATOM   6078  C CD1 . PHE B  1 242 ? -47.393 -40.007 -28.488  1.00 31.89  ? 242 PHE B CD1 1 
ATOM   6079  C CD2 . PHE B  1 242 ? -47.792 -39.563 -26.178  1.00 34.61  ? 242 PHE B CD2 1 
ATOM   6080  C CE1 . PHE B  1 242 ? -48.751 -39.832 -28.757  1.00 38.51  ? 242 PHE B CE1 1 
ATOM   6081  C CE2 . PHE B  1 242 ? -49.149 -39.389 -26.437  1.00 38.36  ? 242 PHE B CE2 1 
ATOM   6082  C CZ  . PHE B  1 242 ? -49.629 -39.528 -27.729  1.00 39.68  ? 242 PHE B CZ  1 
ATOM   6083  N N   . GLU B  1 243 ? -44.673 -37.392 -25.301  1.00 35.34  ? 243 GLU B N   1 
ATOM   6084  C CA  . GLU B  1 243 ? -45.084 -36.186 -24.583  1.00 41.69  ? 243 GLU B CA  1 
ATOM   6085  C C   . GLU B  1 243 ? -44.500 -34.921 -25.205  1.00 40.47  ? 243 GLU B C   1 
ATOM   6086  O O   . GLU B  1 243 ? -45.160 -33.874 -25.238  1.00 34.32  ? 243 GLU B O   1 
ATOM   6087  C CB  . GLU B  1 243 ? -44.666 -36.274 -23.115  1.00 47.07  ? 243 GLU B CB  1 
ATOM   6088  C CG  . GLU B  1 243 ? -45.531 -37.172 -22.252  1.00 55.14  ? 243 GLU B CG  1 
ATOM   6089  C CD  . GLU B  1 243 ? -44.984 -37.298 -20.840  1.00 62.13  ? 243 GLU B CD  1 
ATOM   6090  O OE1 . GLU B  1 243 ? -44.153 -36.445 -20.452  1.00 65.09  ? 243 GLU B OE1 1 
ATOM   6091  O OE2 . GLU B  1 243 ? -45.377 -38.245 -20.124  1.00 62.58  ? 243 GLU B OE2 1 
ATOM   6092  N N   . ILE B  1 244 ? -43.255 -34.986 -25.675  1.00 37.30  ? 244 ILE B N   1 
ATOM   6093  C CA  . ILE B  1 244 ? -42.575 -33.777 -26.129  1.00 35.59  ? 244 ILE B CA  1 
ATOM   6094  C C   . ILE B  1 244 ? -42.955 -33.447 -27.568  1.00 36.76  ? 244 ILE B C   1 
ATOM   6095  O O   . ILE B  1 244 ? -43.246 -32.289 -27.903  1.00 35.66  ? 244 ILE B O   1 
ATOM   6096  C CB  . ILE B  1 244 ? -41.051 -33.938 -25.975  1.00 39.50  ? 244 ILE B CB  1 
ATOM   6097  C CG1 . ILE B  1 244 ? -40.661 -34.152 -24.502  1.00 38.55  ? 244 ILE B CG1 1 
ATOM   6098  C CG2 . ILE B  1 244 ? -40.326 -32.763 -26.603  1.00 39.89  ? 244 ILE B CG2 1 
ATOM   6099  C CD1 . ILE B  1 244 ? -41.291 -33.180 -23.531  1.00 37.24  ? 244 ILE B CD1 1 
ATOM   6100  N N   . PHE B  1 245 ? -42.969 -34.460 -28.436  1.00 38.04  ? 245 PHE B N   1 
ATOM   6101  C CA  . PHE B  1 245 ? -43.059 -34.262 -29.877  1.00 38.65  ? 245 PHE B CA  1 
ATOM   6102  C C   . PHE B  1 245 ? -44.392 -34.673 -30.485  1.00 35.92  ? 245 PHE B C   1 
ATOM   6103  O O   . PHE B  1 245 ? -44.670 -34.286 -31.624  1.00 40.56  ? 245 PHE B O   1 
ATOM   6104  C CB  . PHE B  1 245 ? -41.918 -35.017 -30.575  1.00 36.70  ? 245 PHE B CB  1 
ATOM   6105  C CG  . PHE B  1 245 ? -40.553 -34.518 -30.196  1.00 35.12  ? 245 PHE B CG  1 
ATOM   6106  C CD1 . PHE B  1 245 ? -40.078 -33.317 -30.706  1.00 32.61  ? 245 PHE B CD1 1 
ATOM   6107  C CD2 . PHE B  1 245 ? -39.743 -35.245 -29.333  1.00 30.45  ? 245 PHE B CD2 1 
ATOM   6108  C CE1 . PHE B  1 245 ? -38.822 -32.846 -30.358  1.00 35.41  ? 245 PHE B CE1 1 
ATOM   6109  C CE2 . PHE B  1 245 ? -38.485 -34.781 -28.981  1.00 33.05  ? 245 PHE B CE2 1 
ATOM   6110  C CZ  . PHE B  1 245 ? -38.023 -33.577 -29.489  1.00 35.76  ? 245 PHE B CZ  1 
ATOM   6111  N N   . GLY B  1 246 ? -45.225 -35.417 -29.763  1.00 42.62  ? 246 GLY B N   1 
ATOM   6112  C CA  . GLY B  1 246 ? -46.507 -35.856 -30.274  1.00 43.33  ? 246 GLY B CA  1 
ATOM   6113  C C   . GLY B  1 246 ? -46.480 -37.097 -31.145  1.00 44.40  ? 246 GLY B C   1 
ATOM   6114  O O   . GLY B  1 246 ? -47.536 -37.479 -31.674  1.00 42.66  ? 246 GLY B O   1 
ATOM   6115  N N   . GLU B  1 247 ? -45.314 -37.717 -31.331  1.00 40.56  ? 247 GLU B N   1 
ATOM   6116  C CA  . GLU B  1 247 ? -45.142 -38.963 -32.069  1.00 46.32  ? 247 GLU B CA  1 
ATOM   6117  C C   . GLU B  1 247 ? -44.499 -39.990 -31.145  1.00 41.26  ? 247 GLU B C   1 
ATOM   6118  O O   . GLU B  1 247 ? -43.768 -39.637 -30.221  1.00 40.53  ? 247 GLU B O   1 
ATOM   6119  C CB  . GLU B  1 247 ? -44.213 -38.814 -33.292  1.00 49.21  ? 247 GLU B CB  1 
ATOM   6120  C CG  . GLU B  1 247 ? -44.428 -37.645 -34.197  1.00 62.23  ? 247 GLU B CG  1 
ATOM   6121  C CD  . GLU B  1 247 ? -43.104 -37.073 -34.693  1.00 73.50  ? 247 GLU B CD  1 
ATOM   6122  O OE1 . GLU B  1 247 ? -42.483 -37.655 -35.613  1.00 76.96  ? 247 GLU B OE1 1 
ATOM   6123  O OE2 . GLU B  1 247 ? -42.690 -36.027 -34.150  1.00 77.68  ? 247 GLU B OE2 1 
ATOM   6124  N N   . HIS B  1 248 ? -44.749 -41.259 -31.401  1.00 40.77  ? 248 HIS B N   1 
ATOM   6125  C CA  . HIS B  1 248 ? -43.851 -42.264 -30.862  1.00 41.38  ? 248 HIS B CA  1 
ATOM   6126  C C   . HIS B  1 248 ? -42.543 -42.206 -31.643  1.00 40.04  ? 248 HIS B C   1 
ATOM   6127  O O   . HIS B  1 248 ? -42.557 -41.911 -32.844  1.00 39.82  ? 248 HIS B O   1 
ATOM   6128  C CB  . HIS B  1 248 ? -44.466 -43.654 -30.956  1.00 48.95  ? 248 HIS B CB  1 
ATOM   6129  C CG  . HIS B  1 248 ? -45.529 -43.905 -29.937  1.00 57.86  ? 248 HIS B CG  1 
ATOM   6130  N ND1 . HIS B  1 248 ? -45.311 -43.750 -28.585  1.00 60.05  ? 248 HIS B ND1 1 
ATOM   6131  C CD2 . HIS B  1 248 ? -46.825 -44.273 -30.070  1.00 61.99  ? 248 HIS B CD2 1 
ATOM   6132  C CE1 . HIS B  1 248 ? -46.423 -44.022 -27.928  1.00 61.46  ? 248 HIS B CE1 1 
ATOM   6133  N NE2 . HIS B  1 248 ? -47.357 -44.343 -28.805  1.00 63.14  ? 248 HIS B NE2 1 
ATOM   6134  N N   . PRO B  1 249 ? -41.402 -42.433 -30.993  1.00 38.89  ? 249 PRO B N   1 
ATOM   6135  C CA  . PRO B  1 249 ? -40.133 -42.420 -31.727  1.00 37.43  ? 249 PRO B CA  1 
ATOM   6136  C C   . PRO B  1 249 ? -39.989 -43.659 -32.596  1.00 38.45  ? 249 PRO B C   1 
ATOM   6137  O O   . PRO B  1 249 ? -40.374 -44.763 -32.206  1.00 38.77  ? 249 PRO B O   1 
ATOM   6138  C CB  . PRO B  1 249 ? -39.077 -42.387 -30.613  1.00 33.30  ? 249 PRO B CB  1 
ATOM   6139  C CG  . PRO B  1 249 ? -39.748 -43.021 -29.444  1.00 32.93  ? 249 PRO B CG  1 
ATOM   6140  C CD  . PRO B  1 249 ? -41.207 -42.681 -29.549  1.00 36.72  ? 249 PRO B CD  1 
ATOM   6141  N N   . VAL B  1 250 ? -39.455 -43.458 -33.798  1.00 37.95  ? 250 VAL B N   1 
ATOM   6142  C CA  . VAL B  1 250 ? -39.171 -44.561 -34.712  1.00 33.98  ? 250 VAL B CA  1 
ATOM   6143  C C   . VAL B  1 250 ? -37.679 -44.840 -34.839  1.00 29.98  ? 250 VAL B C   1 
ATOM   6144  O O   . VAL B  1 250 ? -37.308 -45.921 -35.320  1.00 35.05  ? 250 VAL B O   1 
ATOM   6145  C CB  . VAL B  1 250 ? -39.804 -44.324 -36.104  1.00 40.11  ? 250 VAL B CB  1 
ATOM   6146  C CG1 . VAL B  1 250 ? -41.333 -44.331 -36.007  1.00 40.46  ? 250 VAL B CG1 1 
ATOM   6147  C CG2 . VAL B  1 250 ? -39.310 -43.024 -36.730  1.00 39.55  ? 250 VAL B CG2 1 
ATOM   6148  N N   . TYR B  1 251 ? -36.817 -43.919 -34.400  1.00 31.47  ? 251 TYR B N   1 
ATOM   6149  C CA  . TYR B  1 251 ? -35.375 -44.111 -34.320  1.00 33.20  ? 251 TYR B CA  1 
ATOM   6150  C C   . TYR B  1 251 ? -34.918 -44.006 -32.870  1.00 29.73  ? 251 TYR B C   1 
ATOM   6151  O O   . TYR B  1 251 ? -35.387 -43.141 -32.125  1.00 35.25  ? 251 TYR B O   1 
ATOM   6152  C CB  . TYR B  1 251 ? -34.642 -43.065 -35.166  1.00 34.89  ? 251 TYR B CB  1 
ATOM   6153  C CG  . TYR B  1 251 ? -35.343 -42.815 -36.477  1.00 38.11  ? 251 TYR B CG  1 
ATOM   6154  C CD1 . TYR B  1 251 ? -35.508 -43.846 -37.389  1.00 36.89  ? 251 TYR B CD1 1 
ATOM   6155  C CD2 . TYR B  1 251 ? -35.873 -41.564 -36.791  1.00 40.12  ? 251 TYR B CD2 1 
ATOM   6156  C CE1 . TYR B  1 251 ? -36.162 -43.647 -38.583  1.00 40.21  ? 251 TYR B CE1 1 
ATOM   6157  C CE2 . TYR B  1 251 ? -36.542 -41.350 -38.001  1.00 37.79  ? 251 TYR B CE2 1 
ATOM   6158  C CZ  . TYR B  1 251 ? -36.680 -42.398 -38.889  1.00 41.64  ? 251 TYR B CZ  1 
ATOM   6159  O OH  . TYR B  1 251 ? -37.332 -42.237 -40.094  1.00 46.27  ? 251 TYR B OH  1 
ATOM   6160  N N   . MET B  1 252 ? -33.985 -44.863 -32.474  1.00 25.45  ? 252 MET B N   1 
ATOM   6161  C CA  . MET B  1 252 ? -33.356 -44.719 -31.166  1.00 24.87  ? 252 MET B CA  1 
ATOM   6162  C C   . MET B  1 252 ? -31.849 -44.847 -31.310  1.00 26.46  ? 252 MET B C   1 
ATOM   6163  O O   . MET B  1 252 ? -31.355 -45.565 -32.180  1.00 32.82  ? 252 MET B O   1 
ATOM   6164  C CB  . MET B  1 252 ? -33.880 -45.764 -30.169  1.00 26.06  ? 252 MET B CB  1 
ATOM   6165  C CG  . MET B  1 252 ? -35.188 -45.380 -29.525  1.00 33.11  ? 252 MET B CG  1 
ATOM   6166  S SD  . MET B  1 252 ? -35.653 -46.425 -28.120  1.00 35.44  ? 252 MET B SD  1 
ATOM   6167  C CE  . MET B  1 252 ? -37.202 -45.654 -27.688  1.00 34.79  ? 252 MET B CE  1 
ATOM   6168  N N   . TRP B  1 253 ? -31.120 -44.135 -30.443  1.00 26.22  ? 253 TRP B N   1 
ATOM   6169  C CA  . TRP B  1 253 ? -29.698 -44.360 -30.278  1.00 24.23  ? 253 TRP B CA  1 
ATOM   6170  C C   . TRP B  1 253 ? -29.503 -45.277 -29.087  1.00 28.84  ? 253 TRP B C   1 
ATOM   6171  O O   . TRP B  1 253 ? -29.858 -44.892 -27.959  1.00 26.05  ? 253 TRP B O   1 
ATOM   6172  C CB  . TRP B  1 253 ? -28.961 -43.051 -30.051  1.00 26.08  ? 253 TRP B CB  1 
ATOM   6173  C CG  . TRP B  1 253 ? -27.557 -43.255 -29.543  1.00 26.25  ? 253 TRP B CG  1 
ATOM   6174  C CD1 . TRP B  1 253 ? -27.068 -43.006 -28.269  1.00 31.62  ? 253 TRP B CD1 1 
ATOM   6175  C CD2 . TRP B  1 253 ? -26.456 -43.748 -30.304  1.00 28.86  ? 253 TRP B CD2 1 
ATOM   6176  N NE1 . TRP B  1 253 ? -25.724 -43.333 -28.209  1.00 30.97  ? 253 TRP B NE1 1 
ATOM   6177  C CE2 . TRP B  1 253 ? -25.327 -43.784 -29.448  1.00 29.58  ? 253 TRP B CE2 1 
ATOM   6178  C CE3 . TRP B  1 253 ? -26.312 -44.161 -31.639  1.00 32.13  ? 253 TRP B CE3 1 
ATOM   6179  C CZ2 . TRP B  1 253 ? -24.076 -44.224 -29.884  1.00 29.95  ? 253 TRP B CZ2 1 
ATOM   6180  C CZ3 . TRP B  1 253 ? -25.073 -44.600 -32.070  1.00 33.35  ? 253 TRP B CZ3 1 
ATOM   6181  C CH2 . TRP B  1 253 ? -23.967 -44.621 -31.196  1.00 28.78  ? 253 TRP B CH2 1 
ATOM   6182  N N   . PRO B  1 254 ? -28.990 -46.486 -29.283  1.00 26.64  ? 254 PRO B N   1 
ATOM   6183  C CA  . PRO B  1 254 ? -28.685 -47.363 -28.160  1.00 25.49  ? 254 PRO B CA  1 
ATOM   6184  C C   . PRO B  1 254 ? -27.549 -46.794 -27.327  1.00 26.63  ? 254 PRO B C   1 
ATOM   6185  O O   . PRO B  1 254 ? -26.471 -46.497 -27.864  1.00 26.15  ? 254 PRO B O   1 
ATOM   6186  C CB  . PRO B  1 254 ? -28.273 -48.680 -28.846  1.00 26.87  ? 254 PRO B CB  1 
ATOM   6187  C CG  . PRO B  1 254 ? -27.834 -48.280 -30.213  1.00 23.67  ? 254 PRO B CG  1 
ATOM   6188  C CD  . PRO B  1 254 ? -28.683 -47.104 -30.588  1.00 25.07  ? 254 PRO B CD  1 
ATOM   6189  N N   . PRO B  1 255 ? -27.786 -46.653 -26.035  1.00 28.86  ? 255 PRO B N   1 
ATOM   6190  C CA  . PRO B  1 255 ? -26.676 -46.173 -25.236  1.00 22.75  ? 255 PRO B CA  1 
ATOM   6191  C C   . PRO B  1 255 ? -25.356 -46.945 -25.398  1.00 23.87  ? 255 PRO B C   1 
ATOM   6192  O O   . PRO B  1 255 ? -25.331 -48.107 -25.436  1.00 23.57  ? 255 PRO B O   1 
ATOM   6193  C CB  . PRO B  1 255 ? -27.236 -46.218 -23.813  1.00 27.14  ? 255 PRO B CB  1 
ATOM   6194  C CG  . PRO B  1 255 ? -28.682 -46.094 -23.946  1.00 29.12  ? 255 PRO B CG  1 
ATOM   6195  C CD  . PRO B  1 255 ? -29.038 -46.712 -25.252  1.00 29.10  ? 255 PRO B CD  1 
ATOM   6196  N N   . GLU B  1 256 ? -24.315 -46.199 -25.511  1.00 24.22  ? 256 GLU B N   1 
ATOM   6197  C CA  . GLU B  1 256 ? -22.997 -46.744 -25.692  1.00 26.80  ? 256 GLU B CA  1 
ATOM   6198  C C   . GLU B  1 256 ? -22.858 -47.487 -27.026  1.00 28.01  ? 256 GLU B C   1 
ATOM   6199  O O   . GLU B  1 256 ? -21.953 -48.234 -27.193  1.00 32.05  ? 256 GLU B O   1 
ATOM   6200  C CB  . GLU B  1 256 ? -22.604 -47.552 -24.445  1.00 21.08  ? 256 GLU B CB  1 
ATOM   6201  C CG  . GLU B  1 256 ? -22.670 -46.834 -23.124  1.00 22.82  ? 256 GLU B CG  1 
ATOM   6202  C CD  . GLU B  1 256 ? -22.001 -45.489 -23.106  1.00 27.50  ? 256 GLU B CD  1 
ATOM   6203  O OE1 . GLU B  1 256 ? -21.033 -45.251 -23.823  1.00 35.56  ? 256 GLU B OE1 1 
ATOM   6204  O OE2 . GLU B  1 256 ? -22.443 -44.657 -22.332  1.00 34.15  ? 256 GLU B OE2 1 
ATOM   6205  N N   . ALA B  1 257 ? -23.774 -47.254 -27.937  1.00 27.05  ? 257 ALA B N   1 
ATOM   6206  C CA  . ALA B  1 257 ? -23.812 -47.960 -29.205  1.00 28.65  ? 257 ALA B CA  1 
ATOM   6207  C C   . ALA B  1 257 ? -23.968 -49.474 -28.965  1.00 29.80  ? 257 ALA B C   1 
ATOM   6208  O O   . ALA B  1 257 ? -23.689 -50.270 -29.785  1.00 26.75  ? 257 ALA B O   1 
ATOM   6209  C CB  . ALA B  1 257 ? -22.632 -47.600 -30.024  1.00 29.28  ? 257 ALA B CB  1 
ATOM   6210  N N   . SER B  1 258 ? -24.584 -49.798 -27.833  1.00 32.54  ? 258 SER B N   1 
ATOM   6211  C CA  . SER B  1 258 ? -24.680 -51.170 -27.408  1.00 30.67  ? 258 SER B CA  1 
ATOM   6212  C C   . SER B  1 258 ? -25.789 -51.932 -27.952  1.00 27.32  ? 258 SER B C   1 
ATOM   6213  O O   . SER B  1 258 ? -26.887 -51.580 -27.824  1.00 28.56  ? 258 SER B O   1 
ATOM   6214  C CB  . SER B  1 258 ? -24.635 -51.328 -25.841  1.00 32.28  ? 258 SER B CB  1 
ATOM   6215  O OG  . SER B  1 258 ? -24.462 -52.654 -25.460  1.00 33.40  ? 258 SER B OG  1 
ATOM   6216  N N   . VAL B  1 259 ? -25.410 -52.999 -28.583  1.00 25.48  ? 259 VAL B N   1 
ATOM   6217  C CA  . VAL B  1 259 ? -26.336 -53.867 -29.160  1.00 21.83  ? 259 VAL B CA  1 
ATOM   6218  C C   . VAL B  1 259 ? -25.998 -55.305 -28.906  1.00 24.76  ? 259 VAL B C   1 
ATOM   6219  O O   . VAL B  1 259 ? -24.927 -55.623 -28.515  1.00 26.46  ? 259 VAL B O   1 
ATOM   6220  C CB  . VAL B  1 259 ? -26.412 -53.670 -30.702  1.00 27.55  ? 259 VAL B CB  1 
ATOM   6221  C CG1 . VAL B  1 259 ? -27.052 -52.323 -31.013  1.00 22.93  ? 259 VAL B CG1 1 
ATOM   6222  C CG2 . VAL B  1 259 ? -25.051 -53.783 -31.333  1.00 31.79  ? 259 VAL B CG2 1 
ATOM   6223  N N   . SER B  1 260 ? -26.971 -56.146 -29.178  1.00 31.01  ? 260 SER B N   1 
ATOM   6224  C CA  . SER B  1 260 ? -26.835 -57.583 -29.019  1.00 31.78  ? 260 SER B CA  1 
ATOM   6225  C C   . SER B  1 260 ? -27.981 -58.177 -29.807  1.00 27.96  ? 260 SER B C   1 
ATOM   6226  O O   . SER B  1 260 ? -28.913 -57.463 -30.181  1.00 32.75  ? 260 SER B O   1 
ATOM   6227  C CB  . SER B  1 260 ? -26.880 -57.993 -27.540  1.00 27.38  ? 260 SER B CB  1 
ATOM   6228  O OG  . SER B  1 260 ? -28.187 -57.837 -27.003  1.00 25.72  ? 260 SER B OG  1 
ATOM   6229  N N   . ASN B  1 261 ? -27.912 -59.482 -30.080  1.00 25.51  ? 261 ASN B N   1 
ATOM   6230  C CA  . ASN B  1 261 ? -29.030 -60.091 -30.792  1.00 30.48  ? 261 ASN B CA  1 
ATOM   6231  C C   . ASN B  1 261 ? -30.337 -59.882 -30.022  1.00 33.08  ? 261 ASN B C   1 
ATOM   6232  O O   . ASN B  1 261 ? -31.348 -59.454 -30.599  1.00 31.68  ? 261 ASN B O   1 
ATOM   6233  C CB  . ASN B  1 261 ? -28.745 -61.574 -31.059  1.00 32.40  ? 261 ASN B CB  1 
ATOM   6234  C CG  . ASN B  1 261 ? -27.636 -61.781 -32.088  1.00 33.36  ? 261 ASN B CG  1 
ATOM   6235  O OD1 . ASN B  1 261 ? -27.329 -60.883 -32.883  1.00 30.05  ? 261 ASN B OD1 1 
ATOM   6236  N ND2 . ASN B  1 261 ? -27.020 -62.966 -32.071  1.00 31.81  ? 261 ASN B ND2 1 
ATOM   6237  N N   . GLU B  1 262 ? -30.315 -60.077 -28.699  1.00 28.90  ? 262 GLU B N   1 
ATOM   6238  C CA  . GLU B  1 262 ? -31.549 -59.909 -27.939  1.00 31.66  ? 262 GLU B CA  1 
ATOM   6239  C C   . GLU B  1 262 ? -31.986 -58.452 -27.865  1.00 27.70  ? 262 GLU B C   1 
ATOM   6240  O O   . GLU B  1 262 ? -33.193 -58.168 -27.889  1.00 29.66  ? 262 GLU B O   1 
ATOM   6241  C CB  . GLU B  1 262 ? -31.381 -60.487 -26.539  1.00 33.09  ? 262 GLU B CB  1 
ATOM   6242  C CG  . GLU B  1 262 ? -31.284 -61.981 -26.537  1.00 33.95  ? 262 GLU B CG  1 
ATOM   6243  C CD  . GLU B  1 262 ? -31.182 -62.530 -25.133  1.00 41.91  ? 262 GLU B CD  1 
ATOM   6244  O OE1 . GLU B  1 262 ? -31.845 -61.963 -24.235  1.00 45.42  ? 262 GLU B OE1 1 
ATOM   6245  O OE2 . GLU B  1 262 ? -30.426 -63.510 -24.935  1.00 39.78  ? 262 GLU B OE2 1 
ATOM   6246  N N   . ALA B  1 263 ? -31.036 -57.513 -27.783  1.00 26.52  ? 263 ALA B N   1 
ATOM   6247  C CA  . ALA B  1 263 ? -31.415 -56.103 -27.719  1.00 25.78  ? 263 ALA B CA  1 
ATOM   6248  C C   . ALA B  1 263 ? -32.011 -55.632 -29.044  1.00 28.69  ? 263 ALA B C   1 
ATOM   6249  O O   . ALA B  1 263 ? -32.996 -54.887 -29.048  1.00 30.07  ? 263 ALA B O   1 
ATOM   6250  C CB  . ALA B  1 263 ? -30.217 -55.248 -27.317  1.00 25.81  ? 263 ALA B CB  1 
ATOM   6251  N N   . LEU B  1 264 ? -31.453 -56.080 -30.176  1.00 29.73  ? 264 LEU B N   1 
ATOM   6252  C CA  . LEU B  1 264 ? -32.025 -55.713 -31.472  1.00 29.57  ? 264 LEU B CA  1 
ATOM   6253  C C   . LEU B  1 264 ? -33.449 -56.237 -31.613  1.00 30.36  ? 264 LEU B C   1 
ATOM   6254  O O   . LEU B  1 264 ? -34.328 -55.536 -32.128  1.00 32.42  ? 264 LEU B O   1 
ATOM   6255  C CB  . LEU B  1 264 ? -31.146 -56.248 -32.602  1.00 32.46  ? 264 LEU B CB  1 
ATOM   6256  C CG  . LEU B  1 264 ? -29.808 -55.523 -32.708  1.00 34.09  ? 264 LEU B CG  1 
ATOM   6257  C CD1 . LEU B  1 264 ? -28.955 -56.118 -33.811  1.00 30.43  ? 264 LEU B CD1 1 
ATOM   6258  C CD2 . LEU B  1 264 ? -30.057 -54.030 -32.931  1.00 33.47  ? 264 LEU B CD2 1 
ATOM   6259  N N   . GLU B  1 265 ? -33.691 -57.468 -31.149  1.00 32.98  ? 265 GLU B N   1 
ATOM   6260  C CA  . GLU B  1 265 ? -35.047 -58.010 -31.099  1.00 35.03  ? 265 GLU B CA  1 
ATOM   6261  C C   . GLU B  1 265 ? -35.973 -57.126 -30.271  1.00 31.41  ? 265 GLU B C   1 
ATOM   6262  O O   . GLU B  1 265 ? -37.088 -56.815 -30.702  1.00 27.93  ? 265 GLU B O   1 
ATOM   6263  C CB  . GLU B  1 265 ? -35.029 -59.433 -30.537  1.00 36.88  ? 265 GLU B CB  1 
ATOM   6264  C CG  . GLU B  1 265 ? -34.518 -60.484 -31.513  1.00 47.62  ? 265 GLU B CG  1 
ATOM   6265  C CD  . GLU B  1 265 ? -35.499 -60.784 -32.633  1.00 55.34  ? 265 GLU B CD  1 
ATOM   6266  O OE1 . GLU B  1 265 ? -36.710 -60.490 -32.478  1.00 54.31  ? 265 GLU B OE1 1 
ATOM   6267  O OE2 . GLU B  1 265 ? -35.046 -61.316 -33.672  1.00 59.71  ? 265 GLU B OE2 1 
ATOM   6268  N N   . LEU B  1 266 ? -35.535 -56.737 -29.066  1.00 33.45  ? 266 LEU B N   1 
ATOM   6269  C CA  . LEU B  1 266 ? -36.352 -55.894 -28.189  1.00 34.10  ? 266 LEU B CA  1 
ATOM   6270  C C   . LEU B  1 266 ? -36.688 -54.566 -28.859  1.00 33.77  ? 266 LEU B C   1 
ATOM   6271  O O   . LEU B  1 266 ? -37.848 -54.138 -28.870  1.00 36.75  ? 266 LEU B O   1 
ATOM   6272  C CB  . LEU B  1 266 ? -35.634 -55.648 -26.855  1.00 31.78  ? 266 LEU B CB  1 
ATOM   6273  C CG  . LEU B  1 266 ? -36.320 -54.572 -26.004  1.00 29.73  ? 266 LEU B CG  1 
ATOM   6274  C CD1 . LEU B  1 266 ? -37.662 -55.098 -25.471  1.00 29.06  ? 266 LEU B CD1 1 
ATOM   6275  C CD2 . LEU B  1 266 ? -35.452 -54.031 -24.833  1.00 32.28  ? 266 LEU B CD2 1 
ATOM   6276  N N   . TYR B  1 267 ? -35.681 -53.903 -29.429  1.00 29.95  ? 267 TYR B N   1 
ATOM   6277  C CA  . TYR B  1 267 ? -35.929 -52.669 -30.169  1.00 33.35  ? 267 TYR B CA  1 
ATOM   6278  C C   . TYR B  1 267 ? -36.961 -52.871 -31.269  1.00 35.64  ? 267 TYR B C   1 
ATOM   6279  O O   . TYR B  1 267 ? -37.788 -51.988 -31.516  1.00 32.83  ? 267 TYR B O   1 
ATOM   6280  C CB  . TYR B  1 267 ? -34.629 -52.143 -30.767  1.00 32.62  ? 267 TYR B CB  1 
ATOM   6281  C CG  . TYR B  1 267 ? -33.779 -51.433 -29.757  1.00 31.62  ? 267 TYR B CG  1 
ATOM   6282  C CD1 . TYR B  1 267 ? -34.244 -50.298 -29.113  1.00 32.74  ? 267 TYR B CD1 1 
ATOM   6283  C CD2 . TYR B  1 267 ? -32.514 -51.893 -29.446  1.00 33.55  ? 267 TYR B CD2 1 
ATOM   6284  C CE1 . TYR B  1 267 ? -33.472 -49.648 -28.186  1.00 31.64  ? 267 TYR B CE1 1 
ATOM   6285  C CE2 . TYR B  1 267 ? -31.741 -51.257 -28.537  1.00 29.23  ? 267 TYR B CE2 1 
ATOM   6286  C CZ  . TYR B  1 267 ? -32.223 -50.128 -27.907  1.00 31.30  ? 267 TYR B CZ  1 
ATOM   6287  O OH  . TYR B  1 267 ? -31.440 -49.490 -26.985  1.00 25.62  ? 267 TYR B OH  1 
ATOM   6288  N N   . TYR B  1 268 ? -36.909 -54.021 -31.954  1.00 38.60  ? 268 TYR B N   1 
ATOM   6289  C CA  . TYR B  1 268 ? -37.853 -54.321 -33.025  1.00 35.35  ? 268 TYR B CA  1 
ATOM   6290  C C   . TYR B  1 268 ? -39.265 -54.509 -32.491  1.00 33.02  ? 268 TYR B C   1 
ATOM   6291  O O   . TYR B  1 268 ? -40.236 -54.035 -33.093  1.00 30.22  ? 268 TYR B O   1 
ATOM   6292  C CB  . TYR B  1 268 ? -37.414 -55.583 -33.765  1.00 39.48  ? 268 TYR B CB  1 
ATOM   6293  C CG  . TYR B  1 268 ? -38.523 -56.188 -34.590  1.00 44.27  ? 268 TYR B CG  1 
ATOM   6294  C CD1 . TYR B  1 268 ? -38.965 -55.554 -35.742  1.00 42.75  ? 268 TYR B CD1 1 
ATOM   6295  C CD2 . TYR B  1 268 ? -39.135 -57.380 -34.212  1.00 42.58  ? 268 TYR B CD2 1 
ATOM   6296  C CE1 . TYR B  1 268 ? -39.979 -56.080 -36.495  1.00 46.53  ? 268 TYR B CE1 1 
ATOM   6297  C CE2 . TYR B  1 268 ? -40.150 -57.917 -34.958  1.00 42.66  ? 268 TYR B CE2 1 
ATOM   6298  C CZ  . TYR B  1 268 ? -40.570 -57.260 -36.104  1.00 47.93  ? 268 TYR B CZ  1 
ATOM   6299  O OH  . TYR B  1 268 ? -41.582 -57.783 -36.873  1.00 48.15  ? 268 TYR B OH  1 
ATOM   6300  N N   . GLU B  1 269 ? -39.403 -55.246 -31.392  1.00 32.04  ? 269 GLU B N   1 
ATOM   6301  C CA  . GLU B  1 269 ? -40.709 -55.493 -30.799  1.00 41.15  ? 269 GLU B CA  1 
ATOM   6302  C C   . GLU B  1 269 ? -41.317 -54.232 -30.200  1.00 38.70  ? 269 GLU B C   1 
ATOM   6303  O O   . GLU B  1 269 ? -42.540 -54.171 -30.018  1.00 42.46  ? 269 GLU B O   1 
ATOM   6304  C CB  . GLU B  1 269 ? -40.592 -56.595 -29.739  1.00 46.93  ? 269 GLU B CB  1 
ATOM   6305  C CG  . GLU B  1 269 ? -40.054 -57.910 -30.296  1.00 55.17  ? 269 GLU B CG  1 
ATOM   6306  C CD  . GLU B  1 269 ? -39.668 -58.907 -29.215  1.00 62.71  ? 269 GLU B CD  1 
ATOM   6307  O OE1 . GLU B  1 269 ? -39.632 -58.512 -28.024  1.00 59.87  ? 269 GLU B OE1 1 
ATOM   6308  O OE2 . GLU B  1 269 ? -39.386 -60.079 -29.567  1.00 66.22  ? 269 GLU B OE2 1 
ATOM   6309  N N   . LYS B  1 270 ? -40.506 -53.219 -29.910  1.00 34.37  ? 270 LYS B N   1 
ATOM   6310  C CA  . LYS B  1 270 ? -41.018 -51.954 -29.413  1.00 32.65  ? 270 LYS B CA  1 
ATOM   6311  C C   . LYS B  1 270 ? -41.297 -50.938 -30.523  1.00 37.76  ? 270 LYS B C   1 
ATOM   6312  O O   . LYS B  1 270 ? -41.561 -49.766 -30.222  1.00 37.73  ? 270 LYS B O   1 
ATOM   6313  C CB  . LYS B  1 270 ? -40.046 -51.378 -28.395  1.00 33.60  ? 270 LYS B CB  1 
ATOM   6314  C CG  . LYS B  1 270 ? -40.032 -52.180 -27.093  1.00 31.20  ? 270 LYS B CG  1 
ATOM   6315  C CD  . LYS B  1 270 ? -41.462 -52.496 -26.622  1.00 40.94  ? 270 LYS B CD  1 
ATOM   6316  C CE  . LYS B  1 270 ? -41.465 -53.245 -25.286  1.00 47.69  ? 270 LYS B CE  1 
ATOM   6317  N NZ  . LYS B  1 270 ? -42.503 -54.326 -25.221  1.00 52.59  ? 270 LYS B NZ  1 
ATOM   6318  N N   . GLY B  1 271 ? -41.238 -51.352 -31.789  1.00 33.81  ? 271 GLY B N   1 
ATOM   6319  C CA  . GLY B  1 271 ? -41.591 -50.473 -32.890  1.00 31.78  ? 271 GLY B CA  1 
ATOM   6320  C C   . GLY B  1 271 ? -40.501 -49.540 -33.379  1.00 36.29  ? 271 GLY B C   1 
ATOM   6321  O O   . GLY B  1 271 ? -40.810 -48.586 -34.107  1.00 42.57  ? 271 GLY B O   1 
ATOM   6322  N N   . ILE B  1 272 ? -39.243 -49.767 -33.003  1.00 31.88  ? 272 ILE B N   1 
ATOM   6323  C CA  . ILE B  1 272 ? -38.139 -48.952 -33.506  1.00 31.88  ? 272 ILE B CA  1 
ATOM   6324  C C   . ILE B  1 272 ? -37.757 -49.462 -34.891  1.00 33.37  ? 272 ILE B C   1 
ATOM   6325  O O   . ILE B  1 272 ? -37.488 -50.660 -35.074  1.00 33.01  ? 272 ILE B O   1 
ATOM   6326  C CB  . ILE B  1 272 ? -36.940 -48.982 -32.537  1.00 30.43  ? 272 ILE B CB  1 
ATOM   6327  C CG1 . ILE B  1 272 ? -37.384 -48.726 -31.095  1.00 26.07  ? 272 ILE B CG1 1 
ATOM   6328  C CG2 . ILE B  1 272 ? -35.892 -47.950 -32.923  1.00 31.63  ? 272 ILE B CG2 1 
ATOM   6329  C CD1 . ILE B  1 272 ? -38.001 -47.352 -30.886  1.00 31.80  ? 272 ILE B CD1 1 
ATOM   6330  N N   . ASN B  1 273 ? -37.758 -48.557 -35.882  1.00 39.95  ? 273 ASN B N   1 
ATOM   6331  C CA  . ASN B  1 273 ? -37.474 -48.928 -37.266  1.00 40.90  ? 273 ASN B CA  1 
ATOM   6332  C C   . ASN B  1 273 ? -35.992 -48.956 -37.590  1.00 39.86  ? 273 ASN B C   1 
ATOM   6333  O O   . ASN B  1 273 ? -35.569 -49.747 -38.446  1.00 38.94  ? 273 ASN B O   1 
ATOM   6334  C CB  . ASN B  1 273 ? -38.152 -47.966 -38.245  1.00 50.88  ? 273 ASN B CB  1 
ATOM   6335  C CG  . ASN B  1 273 ? -39.646 -47.898 -38.056  1.00 62.79  ? 273 ASN B CG  1 
ATOM   6336  O OD1 . ASN B  1 273 ? -40.191 -46.846 -37.741  1.00 70.84  ? 273 ASN B OD1 1 
ATOM   6337  N ND2 . ASN B  1 273 ? -40.319 -49.020 -38.241  1.00 62.68  ? 273 ASN B ND2 1 
ATOM   6338  N N   . MET B  1 274 ? -35.195 -48.117 -36.932  1.00 36.54  ? 274 MET B N   1 
ATOM   6339  C CA  . MET B  1 274 ? -33.799 -47.942 -37.295  1.00 35.89  ? 274 MET B CA  1 
ATOM   6340  C C   . MET B  1 274 ? -33.013 -47.509 -36.070  1.00 30.96  ? 274 MET B C   1 
ATOM   6341  O O   . MET B  1 274 ? -33.520 -46.765 -35.226  1.00 34.63  ? 274 MET B O   1 
ATOM   6342  C CB  . MET B  1 274 ? -33.645 -46.908 -38.427  1.00 42.80  ? 274 MET B CB  1 
ATOM   6343  C CG  . MET B  1 274 ? -32.224 -46.715 -38.926  1.00 53.02  ? 274 MET B CG  1 
ATOM   6344  S SD  . MET B  1 274 ? -31.388 -45.334 -38.104  1.00 63.49  ? 274 MET B SD  1 
ATOM   6345  C CE  . MET B  1 274 ? -31.989 -43.974 -39.114  1.00 64.58  ? 274 MET B CE  1 
ATOM   6346  N N   . LEU B  1 275 ? -31.780 -48.000 -35.967  1.00 29.48  ? 275 LEU B N   1 
ATOM   6347  C CA  . LEU B  1 275 ? -30.841 -47.517 -34.963  1.00 33.80  ? 275 LEU B CA  1 
ATOM   6348  C C   . LEU B  1 275 ? -29.460 -47.478 -35.595  1.00 32.74  ? 275 LEU B C   1 
ATOM   6349  O O   . LEU B  1 275 ? -29.269 -47.875 -36.745  1.00 37.54  ? 275 LEU B O   1 
ATOM   6350  C CB  . LEU B  1 275 ? -30.857 -48.387 -33.700  1.00 35.88  ? 275 LEU B CB  1 
ATOM   6351  C CG  . LEU B  1 275 ? -30.727 -49.907 -33.794  1.00 43.32  ? 275 LEU B CG  1 
ATOM   6352  C CD1 . LEU B  1 275 ? -29.284 -50.343 -33.989  1.00 45.87  ? 275 LEU B CD1 1 
ATOM   6353  C CD2 . LEU B  1 275 ? -31.298 -50.555 -32.536  1.00 44.21  ? 275 LEU B CD2 1 
ATOM   6354  N N   . ALA B  1 276 ? -28.495 -46.989 -34.837  1.00 31.42  ? 276 ALA B N   1 
ATOM   6355  C CA  . ALA B  1 276 ? -27.105 -47.000 -35.246  1.00 32.88  ? 276 ALA B CA  1 
ATOM   6356  C C   . ALA B  1 276 ? -26.272 -47.647 -34.152  1.00 32.39  ? 276 ALA B C   1 
ATOM   6357  O O   . ALA B  1 276 ? -26.663 -47.705 -32.980  1.00 33.43  ? 276 ALA B O   1 
ATOM   6358  C CB  . ALA B  1 276 ? -26.583 -45.588 -35.545  1.00 35.27  ? 276 ALA B CB  1 
ATOM   6359  N N   . THR B  1 277 ? -25.115 -48.152 -34.552  1.00 29.00  ? 277 THR B N   1 
ATOM   6360  C CA  . THR B  1 277 ? -24.167 -48.685 -33.596  1.00 28.17  ? 277 THR B CA  1 
ATOM   6361  C C   . THR B  1 277 ? -22.773 -48.432 -34.164  1.00 30.52  ? 277 THR B C   1 
ATOM   6362  O O   . THR B  1 277 ? -22.602 -47.593 -35.056  1.00 32.35  ? 277 THR B O   1 
ATOM   6363  C CB  . THR B  1 277 ? -24.502 -50.156 -33.276  1.00 27.65  ? 277 THR B CB  1 
ATOM   6364  O OG1 . THR B  1 277 ? -23.572 -50.670 -32.309  1.00 27.67  ? 277 THR B OG1 1 
ATOM   6365  C CG2 . THR B  1 277 ? -24.509 -50.997 -34.534  1.00 28.12  ? 277 THR B CG2 1 
ATOM   6366  N N   . ASP B  1 278 ? -21.767 -49.124 -33.635  1.00 26.79  ? 278 ASP B N   1 
ATOM   6367  C CA  . ASP B  1 278 ? -20.373 -48.769 -33.897  1.00 32.36  ? 278 ASP B CA  1 
ATOM   6368  C C   . ASP B  1 278 ? -19.730 -49.664 -34.957  1.00 30.20  ? 278 ASP B C   1 
ATOM   6369  O O   . ASP B  1 278 ? -20.060 -50.845 -35.089  1.00 27.49  ? 278 ASP B O   1 
ATOM   6370  C CB  . ASP B  1 278 ? -19.545 -48.848 -32.601  1.00 30.69  ? 278 ASP B CB  1 
ATOM   6371  C CG  . ASP B  1 278 ? -18.127 -48.310 -32.774  1.00 33.09  ? 278 ASP B CG  1 
ATOM   6372  O OD1 . ASP B  1 278 ? -17.957 -47.273 -33.434  1.00 34.82  ? 278 ASP B OD1 1 
ATOM   6373  O OD2 . ASP B  1 278 ? -17.173 -48.924 -32.254  1.00 36.21  ? 278 ASP B OD2 1 
ATOM   6374  N N   . GLU B  1 279 ? -18.755 -49.089 -35.674  1.00 28.06  ? 279 GLU B N   1 
ATOM   6375  C CA  . GLU B  1 279 ? -17.991 -49.845 -36.654  1.00 28.49  ? 279 GLU B CA  1 
ATOM   6376  C C   . GLU B  1 279 ? -17.287 -51.049 -36.035  1.00 30.70  ? 279 GLU B C   1 
ATOM   6377  O O   . GLU B  1 279 ? -17.167 -52.093 -36.687  1.00 29.42  ? 279 GLU B O   1 
ATOM   6378  C CB  . GLU B  1 279 ? -16.978 -48.926 -37.332  1.00 37.19  ? 279 GLU B CB  1 
ATOM   6379  C CG  . GLU B  1 279 ? -16.446 -49.477 -38.644  1.00 45.48  ? 279 GLU B CG  1 
ATOM   6380  C CD  . GLU B  1 279 ? -15.619 -48.470 -39.407  1.00 50.68  ? 279 GLU B CD  1 
ATOM   6381  O OE1 . GLU B  1 279 ? -15.553 -47.290 -38.982  1.00 47.48  ? 279 GLU B OE1 1 
ATOM   6382  O OE2 . GLU B  1 279 ? -15.017 -48.875 -40.423  1.00 52.60  ? 279 GLU B OE2 1 
ATOM   6383  N N   . VAL B  1 280 ? -16.812 -50.934 -34.786  1.00 26.94  ? 280 VAL B N   1 
ATOM   6384  C CA  . VAL B  1 280 ? -16.148 -52.075 -34.161  1.00 27.77  ? 280 VAL B CA  1 
ATOM   6385  C C   . VAL B  1 280 ? -17.092 -53.269 -34.085  1.00 26.23  ? 280 VAL B C   1 
ATOM   6386  O O   . VAL B  1 280 ? -16.690 -54.407 -34.360  1.00 29.33  ? 280 VAL B O   1 
ATOM   6387  C CB  . VAL B  1 280 ? -15.598 -51.712 -32.769  1.00 30.74  ? 280 VAL B CB  1 
ATOM   6388  C CG1 . VAL B  1 280 ? -15.057 -52.951 -32.120  1.00 27.79  ? 280 VAL B CG1 1 
ATOM   6389  C CG2 . VAL B  1 280 ? -14.487 -50.662 -32.872  1.00 31.88  ? 280 VAL B CG2 1 
ATOM   6390  N N   . ILE B  1 281 ? -18.355 -53.036 -33.715  1.00 30.25  ? 281 ILE B N   1 
ATOM   6391  C CA  . ILE B  1 281 ? -19.341 -54.121 -33.680  1.00 30.74  ? 281 ILE B CA  1 
ATOM   6392  C C   . ILE B  1 281 ? -19.441 -54.792 -35.046  1.00 29.14  ? 281 ILE B C   1 
ATOM   6393  O O   . ILE B  1 281 ? -19.353 -56.024 -35.170  1.00 29.42  ? 281 ILE B O   1 
ATOM   6394  C CB  . ILE B  1 281 ? -20.715 -53.594 -33.228  1.00 32.65  ? 281 ILE B CB  1 
ATOM   6395  C CG1 . ILE B  1 281 ? -20.622 -52.833 -31.898  1.00 40.17  ? 281 ILE B CG1 1 
ATOM   6396  C CG2 . ILE B  1 281 ? -21.750 -54.728 -33.186  1.00 25.07  ? 281 ILE B CG2 1 
ATOM   6397  C CD1 . ILE B  1 281 ? -19.864 -53.534 -30.836  1.00 42.06  ? 281 ILE B CD1 1 
ATOM   6398  N N   . LEU B  1 282 ? -19.671 -53.993 -36.086  1.00 30.31  ? 282 LEU B N   1 
ATOM   6399  C CA  . LEU B  1 282 ? -19.701 -54.530 -37.444  1.00 30.29  ? 282 LEU B CA  1 
ATOM   6400  C C   . LEU B  1 282 ? -18.479 -55.395 -37.731  1.00 30.43  ? 282 LEU B C   1 
ATOM   6401  O O   . LEU B  1 282 ? -18.604 -56.502 -38.263  1.00 30.03  ? 282 LEU B O   1 
ATOM   6402  C CB  . LEU B  1 282 ? -19.799 -53.400 -38.467  1.00 31.36  ? 282 LEU B CB  1 
ATOM   6403  C CG  . LEU B  1 282 ? -20.053 -53.910 -39.897  1.00 27.88  ? 282 LEU B CG  1 
ATOM   6404  C CD1 . LEU B  1 282 ? -21.333 -54.738 -39.964  1.00 25.38  ? 282 LEU B CD1 1 
ATOM   6405  C CD2 . LEU B  1 282 ? -20.121 -52.762 -40.898  1.00 30.51  ? 282 LEU B CD2 1 
ATOM   6406  N N   . LYS B  1 283 ? -17.284 -54.899 -37.388  1.00 32.42  ? 283 LYS B N   1 
ATOM   6407  C CA  . LYS B  1 283 ? -16.060 -55.637 -37.685  1.00 36.00  ? 283 LYS B CA  1 
ATOM   6408  C C   . LYS B  1 283 ? -15.995 -56.954 -36.920  1.00 36.58  ? 283 LYS B C   1 
ATOM   6409  O O   . LYS B  1 283 ? -15.381 -57.915 -37.401  1.00 32.48  ? 283 LYS B O   1 
ATOM   6410  C CB  . LYS B  1 283 ? -14.829 -54.789 -37.358  1.00 40.11  ? 283 LYS B CB  1 
ATOM   6411  C CG  . LYS B  1 283 ? -14.586 -53.608 -38.304  1.00 49.66  ? 283 LYS B CG  1 
ATOM   6412  C CD  . LYS B  1 283 ? -13.359 -52.800 -37.871  1.00 56.36  ? 283 LYS B CD  1 
ATOM   6413  C CE  . LYS B  1 283 ? -12.930 -51.796 -38.932  1.00 62.19  ? 283 LYS B CE  1 
ATOM   6414  N NZ  . LYS B  1 283 ? -12.251 -52.450 -40.089  1.00 68.77  ? 283 LYS B NZ  1 
ATOM   6415  N N   . ASN B  1 284 ? -16.615 -57.016 -35.733  1.00 35.20  ? 284 ASN B N   1 
ATOM   6416  C CA  . ASN B  1 284 ? -16.633 -58.230 -34.926  1.00 33.95  ? 284 ASN B CA  1 
ATOM   6417  C C   . ASN B  1 284 ? -17.684 -59.234 -35.377  1.00 33.17  ? 284 ASN B C   1 
ATOM   6418  O O   . ASN B  1 284 ? -17.543 -60.427 -35.076  1.00 32.31  ? 284 ASN B O   1 
ATOM   6419  C CB  . ASN B  1 284 ? -16.895 -57.887 -33.455  1.00 38.28  ? 284 ASN B CB  1 
ATOM   6420  C CG  . ASN B  1 284 ? -15.721 -57.184 -32.793  1.00 40.65  ? 284 ASN B CG  1 
ATOM   6421  O OD1 . ASN B  1 284 ? -14.593 -57.232 -33.289  1.00 39.69  ? 284 ASN B OD1 1 
ATOM   6422  N ND2 . ASN B  1 284 ? -15.988 -56.519 -31.662  1.00 40.15  ? 284 ASN B ND2 1 
ATOM   6423  N N   . SER B  1 285 ? -18.714 -58.781 -36.107  1.00 31.55  ? 285 SER B N   1 
ATOM   6424  C CA  . SER B  1 285 ? -19.887 -59.578 -36.449  1.00 32.79  ? 285 SER B CA  1 
ATOM   6425  C C   . SER B  1 285 ? -19.925 -60.073 -37.893  1.00 34.98  ? 285 SER B C   1 
ATOM   6426  O O   . SER B  1 285 ? -20.640 -61.045 -38.167  1.00 35.33  ? 285 SER B O   1 
ATOM   6427  C CB  . SER B  1 285 ? -21.169 -58.766 -36.196  1.00 38.01  ? 285 SER B CB  1 
ATOM   6428  O OG  . SER B  1 285 ? -21.145 -58.096 -34.936  1.00 39.32  ? 285 SER B OG  1 
ATOM   6429  N N   . VAL B  1 286 ? -19.224 -59.414 -38.824  1.00 29.00  ? 286 VAL B N   1 
ATOM   6430  C CA  . VAL B  1 286 ? -19.195 -59.802 -40.236  1.00 38.98  ? 286 VAL B CA  1 
ATOM   6431  C C   . VAL B  1 286 ? -17.773 -59.630 -40.763  1.00 38.22  ? 286 VAL B C   1 
ATOM   6432  O O   . VAL B  1 286 ? -16.967 -58.874 -40.214  1.00 39.30  ? 286 VAL B O   1 
ATOM   6433  C CB  . VAL B  1 286 ? -20.193 -58.983 -41.110  1.00 44.54  ? 286 VAL B CB  1 
ATOM   6434  C CG1 . VAL B  1 286 ? -21.583 -58.934 -40.473  1.00 42.52  ? 286 VAL B CG1 1 
ATOM   6435  C CG2 . VAL B  1 286 ? -19.674 -57.562 -41.386  1.00 44.88  ? 286 VAL B CG2 1 
ATOM   6436  N N   . GLU B  1 287 ? -17.466 -60.336 -41.852  1.00 46.05  ? 287 GLU B N   1 
ATOM   6437  C CA  . GLU B  1 287 ? -16.120 -60.239 -42.416  1.00 47.69  ? 287 GLU B CA  1 
ATOM   6438  C C   . GLU B  1 287 ? -15.946 -58.967 -43.255  1.00 50.77  ? 287 GLU B C   1 
ATOM   6439  O O   . GLU B  1 287 ? -15.102 -58.118 -42.945  1.00 54.09  ? 287 GLU B O   1 
ATOM   6440  C CB  . GLU B  1 287 ? -15.806 -61.493 -43.228  1.00 52.84  ? 287 GLU B CB  1 
ATOM   6441  C CG  . GLU B  1 287 ? -16.070 -62.774 -42.452  1.00 55.49  ? 287 GLU B CG  1 
ATOM   6442  C CD  . GLU B  1 287 ? -15.804 -64.016 -43.282  1.00 63.67  ? 287 GLU B CD  1 
ATOM   6443  O OE1 . GLU B  1 287 ? -15.444 -65.067 -42.702  1.00 68.18  ? 287 GLU B OE1 1 
ATOM   6444  O OE2 . GLU B  1 287 ? -15.945 -63.932 -44.523  1.00 64.39  ? 287 GLU B OE2 1 
ATOM   6445  N N   . ARG B  1 288 ? -16.737 -58.815 -44.321  1.00 45.86  ? 288 ARG B N   1 
ATOM   6446  C CA  . ARG B  1 288 ? -16.704 -57.619 -45.171  1.00 49.01  ? 288 ARG B CA  1 
ATOM   6447  C C   . ARG B  1 288 ? -17.538 -56.546 -44.485  1.00 47.83  ? 288 ARG B C   1 
ATOM   6448  O O   . ARG B  1 288 ? -18.765 -56.566 -44.539  1.00 52.17  ? 288 ARG B O   1 
ATOM   6449  C CB  . ARG B  1 288 ? -17.212 -57.942 -46.581  1.00 52.59  ? 288 ARG B CB  1 
ATOM   6450  C CG  . ARG B  1 288 ? -16.143 -58.683 -47.429  1.00 57.10  ? 288 ARG B CG  1 
ATOM   6451  C CD  . ARG B  1 288 ? -16.667 -59.420 -48.694  1.00 59.56  ? 288 ARG B CD  1 
ATOM   6452  N NE  . ARG B  1 288 ? -17.948 -60.080 -48.465  1.00 65.58  ? 288 ARG B NE  1 
ATOM   6453  C CZ  . ARG B  1 288 ? -19.109 -59.558 -48.811  1.00 72.82  ? 288 ARG B CZ  1 
ATOM   6454  N NH1 . ARG B  1 288 ? -20.203 -60.240 -48.568  1.00 75.69  ? 288 ARG B NH1 1 
ATOM   6455  N NH2 . ARG B  1 288 ? -19.163 -58.347 -49.350  1.00 75.30  ? 288 ARG B NH2 1 
ATOM   6456  N N   . ALA B  1 289 ? -16.875 -55.594 -43.844  1.00 46.12  ? 289 ALA B N   1 
ATOM   6457  C CA  . ALA B  1 289 ? -17.497 -54.734 -42.837  1.00 47.74  ? 289 ALA B CA  1 
ATOM   6458  C C   . ALA B  1 289 ? -17.471 -53.286 -43.313  1.00 49.69  ? 289 ALA B C   1 
ATOM   6459  O O   . ALA B  1 289 ? -16.810 -52.437 -42.707  1.00 56.42  ? 289 ALA B O   1 
ATOM   6460  C CB  . ALA B  1 289 ? -16.779 -54.899 -41.465  1.00 39.22  ? 289 ALA B CB  1 
ATOM   6461  N N   . SER B  1 290 ? -18.203 -53.001 -44.376  1.00 45.30  ? 290 SER B N   1 
ATOM   6462  C CA  . SER B  1 290 ? -18.228 -51.615 -44.841  1.00 41.81  ? 290 SER B CA  1 
ATOM   6463  C C   . SER B  1 290 ? -19.320 -50.839 -44.118  1.00 36.40  ? 290 SER B C   1 
ATOM   6464  O O   . SER B  1 290 ? -20.477 -51.276 -44.101  1.00 36.87  ? 290 SER B O   1 
ATOM   6465  C CB  . SER B  1 290 ? -18.462 -51.545 -46.345  1.00 42.42  ? 290 SER B CB  1 
ATOM   6466  O OG  . SER B  1 290 ? -18.861 -50.238 -46.731  1.00 38.42  ? 290 SER B OG  1 
ATOM   6467  N N   . PRO B  1 291 ? -19.002 -49.693 -43.519  1.00 39.91  ? 291 PRO B N   1 
ATOM   6468  C CA  . PRO B  1 291 ? -20.025 -48.910 -42.816  1.00 39.83  ? 291 PRO B CA  1 
ATOM   6469  C C   . PRO B  1 291 ? -20.845 -48.016 -43.735  1.00 36.79  ? 291 PRO B C   1 
ATOM   6470  O O   . PRO B  1 291 ? -21.700 -47.262 -43.255  1.00 31.44  ? 291 PRO B O   1 
ATOM   6471  C CB  . PRO B  1 291 ? -19.183 -48.085 -41.833  1.00 42.14  ? 291 PRO B CB  1 
ATOM   6472  C CG  . PRO B  1 291 ? -17.889 -47.849 -42.602  1.00 40.76  ? 291 PRO B CG  1 
ATOM   6473  C CD  . PRO B  1 291 ? -17.670 -49.062 -43.462  1.00 41.92  ? 291 PRO B CD  1 
ATOM   6474  N N   . TYR B  1 292 ? -20.624 -48.080 -45.042  1.00 35.18  ? 292 TYR B N   1 
ATOM   6475  C CA  . TYR B  1 292 ? -21.266 -47.157 -45.964  1.00 33.15  ? 292 TYR B CA  1 
ATOM   6476  C C   . TYR B  1 292 ? -22.561 -47.715 -46.534  1.00 35.78  ? 292 TYR B C   1 
ATOM   6477  O O   . TYR B  1 292 ? -23.112 -47.137 -47.488  1.00 30.95  ? 292 TYR B O   1 
ATOM   6478  C CB  . TYR B  1 292 ? -20.277 -46.769 -47.080  1.00 38.83  ? 292 TYR B CB  1 
ATOM   6479  C CG  . TYR B  1 292 ? -18.992 -46.224 -46.480  1.00 43.68  ? 292 TYR B CG  1 
ATOM   6480  C CD1 . TYR B  1 292 ? -19.039 -45.349 -45.408  1.00 43.68  ? 292 TYR B CD1 1 
ATOM   6481  C CD2 . TYR B  1 292 ? -17.743 -46.599 -46.963  1.00 50.44  ? 292 TYR B CD2 1 
ATOM   6482  C CE1 . TYR B  1 292 ? -17.887 -44.855 -44.821  1.00 46.20  ? 292 TYR B CE1 1 
ATOM   6483  C CE2 . TYR B  1 292 ? -16.575 -46.107 -46.379  1.00 48.97  ? 292 TYR B CE2 1 
ATOM   6484  C CZ  . TYR B  1 292 ? -16.659 -45.235 -45.308  1.00 48.48  ? 292 TYR B CZ  1 
ATOM   6485  O OH  . TYR B  1 292 ? -15.522 -44.728 -44.716  1.00 46.81  ? 292 TYR B OH  1 
ATOM   6486  N N   . LEU B  1 293 ? -23.066 -48.802 -45.946  1.00 29.29  ? 293 LEU B N   1 
ATOM   6487  C CA  . LEU B  1 293 ? -24.274 -49.487 -46.387  1.00 34.38  ? 293 LEU B CA  1 
ATOM   6488  C C   . LEU B  1 293 ? -25.339 -49.429 -45.299  1.00 32.84  ? 293 LEU B C   1 
ATOM   6489  O O   . LEU B  1 293 ? -25.025 -49.465 -44.107  1.00 29.58  ? 293 LEU B O   1 
ATOM   6490  C CB  . LEU B  1 293 ? -24.002 -50.959 -46.700  1.00 30.32  ? 293 LEU B CB  1 
ATOM   6491  C CG  . LEU B  1 293 ? -23.410 -51.394 -48.040  1.00 40.32  ? 293 LEU B CG  1 
ATOM   6492  C CD1 . LEU B  1 293 ? -22.024 -50.807 -48.263  1.00 44.03  ? 293 LEU B CD1 1 
ATOM   6493  C CD2 . LEU B  1 293 ? -23.376 -52.907 -48.055  1.00 36.13  ? 293 LEU B CD2 1 
ATOM   6494  N N   . ARG B  1 294 ? -26.603 -49.366 -45.719  1.00 34.32  ? 294 ARG B N   1 
ATOM   6495  C CA  . ARG B  1 294 ? -27.714 -49.600 -44.805  1.00 36.20  ? 294 ARG B CA  1 
ATOM   6496  C C   . ARG B  1 294 ? -27.864 -51.098 -44.568  1.00 36.87  ? 294 ARG B C   1 
ATOM   6497  O O   . ARG B  1 294 ? -27.923 -51.883 -45.519  1.00 38.07  ? 294 ARG B O   1 
ATOM   6498  C CB  . ARG B  1 294 ? -29.015 -49.014 -45.359  1.00 35.43  ? 294 ARG B CB  1 
ATOM   6499  C CG  . ARG B  1 294 ? -30.215 -49.327 -44.469  1.00 36.59  ? 294 ARG B CG  1 
ATOM   6500  C CD  . ARG B  1 294 ? -31.421 -48.457 -44.795  1.00 37.04  ? 294 ARG B CD  1 
ATOM   6501  N NE  . ARG B  1 294 ? -32.002 -48.769 -46.089  1.00 38.56  ? 294 ARG B NE  1 
ATOM   6502  C CZ  . ARG B  1 294 ? -32.142 -47.888 -47.068  1.00 42.32  ? 294 ARG B CZ  1 
ATOM   6503  N NH1 . ARG B  1 294 ? -31.745 -46.633 -46.889  1.00 40.62  ? 294 ARG B NH1 1 
ATOM   6504  N NH2 . ARG B  1 294 ? -32.689 -48.260 -48.219  1.00 47.51  ? 294 ARG B NH2 1 
ATOM   6505  N N   . TYR B  1 295 ? -27.916 -51.500 -43.299  1.00 34.00  ? 295 TYR B N   1 
ATOM   6506  C CA  . TYR B  1 295 ? -28.024 -52.905 -42.943  1.00 29.13  ? 295 TYR B CA  1 
ATOM   6507  C C   . TYR B  1 295 ? -29.413 -53.201 -42.394  1.00 33.18  ? 295 TYR B C   1 
ATOM   6508  O O   . TYR B  1 295 ? -30.062 -52.334 -41.798  1.00 35.95  ? 295 TYR B O   1 
ATOM   6509  C CB  . TYR B  1 295 ? -26.952 -53.288 -41.923  1.00 31.44  ? 295 TYR B CB  1 
ATOM   6510  C CG  . TYR B  1 295 ? -25.569 -53.351 -42.508  1.00 29.73  ? 295 TYR B CG  1 
ATOM   6511  C CD1 . TYR B  1 295 ? -24.783 -52.214 -42.616  1.00 29.55  ? 295 TYR B CD1 1 
ATOM   6512  C CD2 . TYR B  1 295 ? -25.060 -54.548 -42.977  1.00 34.25  ? 295 TYR B CD2 1 
ATOM   6513  C CE1 . TYR B  1 295 ? -23.527 -52.269 -43.183  1.00 30.23  ? 295 TYR B CE1 1 
ATOM   6514  C CE2 . TYR B  1 295 ? -23.806 -54.621 -43.540  1.00 37.82  ? 295 TYR B CE2 1 
ATOM   6515  C CZ  . TYR B  1 295 ? -23.041 -53.488 -43.643  1.00 35.89  ? 295 TYR B CZ  1 
ATOM   6516  O OH  . TYR B  1 295 ? -21.791 -53.588 -44.211  1.00 32.11  ? 295 TYR B OH  1 
ATOM   6517  N N   . TYR B  1 296 ? -29.878 -54.425 -42.633  1.00 30.63  ? 296 TYR B N   1 
ATOM   6518  C CA  . TYR B  1 296 ? -31.126 -54.921 -42.066  1.00 34.51  ? 296 TYR B CA  1 
ATOM   6519  C C   . TYR B  1 296 ? -30.795 -56.129 -41.205  1.00 32.19  ? 296 TYR B C   1 
ATOM   6520  O O   . TYR B  1 296 ? -30.256 -57.120 -41.707  1.00 32.25  ? 296 TYR B O   1 
ATOM   6521  C CB  . TYR B  1 296 ? -32.144 -55.290 -43.153  1.00 40.42  ? 296 TYR B CB  1 
ATOM   6522  C CG  . TYR B  1 296 ? -32.408 -54.210 -44.191  1.00 44.96  ? 296 TYR B CG  1 
ATOM   6523  C CD1 . TYR B  1 296 ? -32.755 -52.912 -43.816  1.00 45.73  ? 296 TYR B CD1 1 
ATOM   6524  C CD2 . TYR B  1 296 ? -32.312 -54.493 -45.556  1.00 49.40  ? 296 TYR B CD2 1 
ATOM   6525  C CE1 . TYR B  1 296 ? -33.000 -51.924 -44.770  1.00 46.55  ? 296 TYR B CE1 1 
ATOM   6526  C CE2 . TYR B  1 296 ? -32.553 -53.507 -46.518  1.00 48.41  ? 296 TYR B CE2 1 
ATOM   6527  C CZ  . TYR B  1 296 ? -32.893 -52.222 -46.115  1.00 49.09  ? 296 TYR B CZ  1 
ATOM   6528  O OH  . TYR B  1 296 ? -33.139 -51.234 -47.055  1.00 49.05  ? 296 TYR B OH  1 
ATOM   6529  N N   . PHE B  1 297 ? -31.080 -56.032 -39.904  1.00 31.94  ? 297 PHE B N   1 
ATOM   6530  C CA  . PHE B  1 297 ? -30.859 -57.145 -38.991  1.00 30.51  ? 297 PHE B CA  1 
ATOM   6531  C C   . PHE B  1 297 ? -32.043 -58.090 -39.103  1.00 33.22  ? 297 PHE B C   1 
ATOM   6532  O O   . PHE B  1 297 ? -33.153 -57.751 -38.677  1.00 31.73  ? 297 PHE B O   1 
ATOM   6533  C CB  . PHE B  1 297 ? -30.670 -56.652 -37.554  1.00 31.81  ? 297 PHE B CB  1 
ATOM   6534  C CG  . PHE B  1 297 ? -30.458 -57.763 -36.547  1.00 30.81  ? 297 PHE B CG  1 
ATOM   6535  C CD1 . PHE B  1 297 ? -29.242 -58.438 -36.480  1.00 32.88  ? 297 PHE B CD1 1 
ATOM   6536  C CD2 . PHE B  1 297 ? -31.473 -58.131 -35.670  1.00 29.27  ? 297 PHE B CD2 1 
ATOM   6537  C CE1 . PHE B  1 297 ? -29.034 -59.456 -35.540  1.00 33.99  ? 297 PHE B CE1 1 
ATOM   6538  C CE2 . PHE B  1 297 ? -31.274 -59.146 -34.713  1.00 28.86  ? 297 PHE B CE2 1 
ATOM   6539  C CZ  . PHE B  1 297 ? -30.054 -59.816 -34.660  1.00 30.95  ? 297 PHE B CZ  1 
ATOM   6540  N N   . ARG B  1 298 ? -31.799 -59.269 -39.691  1.00 37.09  ? 298 ARG B N   1 
ATOM   6541  C CA  . ARG B  1 298 ? -32.798 -60.330 -39.850  1.00 39.54  ? 298 ARG B CA  1 
ATOM   6542  C C   . ARG B  1 298 ? -34.058 -59.833 -40.559  1.00 41.32  ? 298 ARG B C   1 
ATOM   6543  O O   . ARG B  1 298 ? -35.156 -60.348 -40.329  1.00 43.84  ? 298 ARG B O   1 
ATOM   6544  C CB  . ARG B  1 298 ? -33.157 -60.949 -38.496  1.00 39.16  ? 298 ARG B CB  1 
ATOM   6545  C CG  . ARG B  1 298 ? -31.958 -61.488 -37.744  1.00 34.40  ? 298 ARG B CG  1 
ATOM   6546  C CD  . ARG B  1 298 ? -32.331 -62.120 -36.408  1.00 37.27  ? 298 ARG B CD  1 
ATOM   6547  N NE  . ARG B  1 298 ? -31.168 -62.808 -35.850  1.00 40.15  ? 298 ARG B NE  1 
ATOM   6548  C CZ  . ARG B  1 298 ? -31.031 -63.165 -34.575  1.00 42.26  ? 298 ARG B CZ  1 
ATOM   6549  N NH1 . ARG B  1 298 ? -31.990 -62.900 -33.692  1.00 41.52  ? 298 ARG B NH1 1 
ATOM   6550  N NH2 . ARG B  1 298 ? -29.924 -63.790 -34.186  1.00 38.13  ? 298 ARG B NH2 1 
ATOM   6551  N N   . GLU B  1 299 ? -33.908 -58.833 -41.433  1.00 38.41  ? 299 GLU B N   1 
ATOM   6552  C CA  . GLU B  1 299 ? -35.045 -58.214 -42.119  1.00 38.70  ? 299 GLU B CA  1 
ATOM   6553  C C   . GLU B  1 299 ? -36.112 -57.750 -41.126  1.00 39.21  ? 299 GLU B C   1 
ATOM   6554  O O   . GLU B  1 299 ? -37.305 -57.737 -41.436  1.00 40.74  ? 299 GLU B O   1 
ATOM   6555  C CB  . GLU B  1 299 ? -35.659 -59.163 -43.156  1.00 45.96  ? 299 GLU B CB  1 
ATOM   6556  C CG  . GLU B  1 299 ? -34.683 -59.709 -44.183  1.00 51.02  ? 299 GLU B CG  1 
ATOM   6557  C CD  . GLU B  1 299 ? -34.393 -58.727 -45.299  1.00 57.13  ? 299 GLU B CD  1 
ATOM   6558  O OE1 . GLU B  1 299 ? -34.806 -57.551 -45.189  1.00 58.89  ? 299 GLU B OE1 1 
ATOM   6559  O OE2 . GLU B  1 299 ? -33.776 -59.141 -46.301  1.00 58.22  ? 299 GLU B OE2 1 
ATOM   6560  N N   . LEU B  1 300 ? -35.693 -57.393 -39.912  1.00 37.46  ? 300 LEU B N   1 
ATOM   6561  C CA  . LEU B  1 300 ? -36.587 -56.885 -38.876  1.00 39.34  ? 300 LEU B CA  1 
ATOM   6562  C C   . LEU B  1 300 ? -36.409 -55.402 -38.603  1.00 39.51  ? 300 LEU B C   1 
ATOM   6563  O O   . LEU B  1 300 ? -37.391 -54.686 -38.409  1.00 40.06  ? 300 LEU B O   1 
ATOM   6564  C CB  . LEU B  1 300 ? -36.381 -57.655 -37.562  1.00 37.90  ? 300 LEU B CB  1 
ATOM   6565  C CG  . LEU B  1 300 ? -36.777 -59.132 -37.606  1.00 43.22  ? 300 LEU B CG  1 
ATOM   6566  C CD1 . LEU B  1 300 ? -36.106 -59.903 -36.476  1.00 46.55  ? 300 LEU B CD1 1 
ATOM   6567  C CD2 . LEU B  1 300 ? -38.284 -59.294 -37.550  1.00 45.78  ? 300 LEU B CD2 1 
ATOM   6568  N N   . ILE B  1 301 ? -35.177 -54.918 -38.597  1.00 39.09  ? 301 ILE B N   1 
ATOM   6569  C CA  . ILE B  1 301 ? -34.901 -53.552 -38.190  1.00 40.07  ? 301 ILE B CA  1 
ATOM   6570  C C   . ILE B  1 301 ? -33.655 -53.101 -38.921  1.00 37.00  ? 301 ILE B C   1 
ATOM   6571  O O   . ILE B  1 301 ? -32.729 -53.889 -39.136  1.00 38.82  ? 301 ILE B O   1 
ATOM   6572  C CB  . ILE B  1 301 ? -34.722 -53.465 -36.657  1.00 41.61  ? 301 ILE B CB  1 
ATOM   6573  C CG1 . ILE B  1 301 ? -34.322 -52.053 -36.218  1.00 36.91  ? 301 ILE B CG1 1 
ATOM   6574  C CG2 . ILE B  1 301 ? -33.704 -54.503 -36.195  1.00 38.04  ? 301 ILE B CG2 1 
ATOM   6575  C CD1 . ILE B  1 301 ? -34.175 -51.916 -34.736  1.00 34.74  ? 301 ILE B CD1 1 
ATOM   6576  N N   . SER B  1 302 ? -33.627 -51.830 -39.290  1.00 35.61  ? 302 SER B N   1 
ATOM   6577  C CA  . SER B  1 302 ? -32.511 -51.280 -40.034  1.00 35.97  ? 302 SER B CA  1 
ATOM   6578  C C   . SER B  1 302 ? -31.443 -50.795 -39.070  1.00 37.50  ? 302 SER B C   1 
ATOM   6579  O O   . SER B  1 302 ? -31.748 -50.304 -37.979  1.00 40.41  ? 302 SER B O   1 
ATOM   6580  C CB  . SER B  1 302 ? -32.990 -50.149 -40.931  1.00 38.02  ? 302 SER B CB  1 
ATOM   6581  O OG  . SER B  1 302 ? -34.277 -50.488 -41.433  1.00 41.11  ? 302 SER B OG  1 
ATOM   6582  N N   . VAL B  1 303 ? -30.190 -50.968 -39.468  1.00 35.25  ? 303 VAL B N   1 
ATOM   6583  C CA  . VAL B  1 303 ? -29.044 -50.635 -38.635  1.00 35.50  ? 303 VAL B CA  1 
ATOM   6584  C C   . VAL B  1 303 ? -28.018 -49.929 -39.503  1.00 34.01  ? 303 VAL B C   1 
ATOM   6585  O O   . VAL B  1 303 ? -27.667 -50.415 -40.583  1.00 33.39  ? 303 VAL B O   1 
ATOM   6586  C CB  . VAL B  1 303 ? -28.409 -51.876 -37.977  1.00 31.63  ? 303 VAL B CB  1 
ATOM   6587  C CG1 . VAL B  1 303 ? -27.210 -51.455 -37.102  1.00 29.20  ? 303 VAL B CG1 1 
ATOM   6588  C CG2 . VAL B  1 303 ? -29.443 -52.648 -37.142  1.00 33.34  ? 303 VAL B CG2 1 
ATOM   6589  N N   . PHE B  1 304 ? -27.533 -48.791 -39.034  1.00 30.93  ? 304 PHE B N   1 
ATOM   6590  C CA  . PHE B  1 304 ? -26.363 -48.172 -39.622  1.00 32.86  ? 304 PHE B CA  1 
ATOM   6591  C C   . PHE B  1 304 ? -25.201 -48.299 -38.655  1.00 31.06  ? 304 PHE B C   1 
ATOM   6592  O O   . PHE B  1 304 ? -25.378 -48.306 -37.429  1.00 32.23  ? 304 PHE B O   1 
ATOM   6593  C CB  . PHE B  1 304 ? -26.612 -46.705 -39.970  1.00 33.35  ? 304 PHE B CB  1 
ATOM   6594  C CG  . PHE B  1 304 ? -27.451 -46.510 -41.196  1.00 32.12  ? 304 PHE B CG  1 
ATOM   6595  C CD1 . PHE B  1 304 ? -26.881 -46.562 -42.462  1.00 34.41  ? 304 PHE B CD1 1 
ATOM   6596  C CD2 . PHE B  1 304 ? -28.814 -46.275 -41.088  1.00 32.57  ? 304 PHE B CD2 1 
ATOM   6597  C CE1 . PHE B  1 304 ? -27.658 -46.363 -43.597  1.00 34.99  ? 304 PHE B CE1 1 
ATOM   6598  C CE2 . PHE B  1 304 ? -29.599 -46.085 -42.225  1.00 36.11  ? 304 PHE B CE2 1 
ATOM   6599  C CZ  . PHE B  1 304 ? -29.019 -46.126 -43.476  1.00 35.16  ? 304 PHE B CZ  1 
ATOM   6600  N N   . PHE B  1 305 ? -24.006 -48.427 -39.212  1.00 26.00  ? 305 PHE B N   1 
ATOM   6601  C CA  . PHE B  1 305 ? -22.799 -48.501 -38.405  1.00 26.59  ? 305 PHE B CA  1 
ATOM   6602  C C   . PHE B  1 305 ? -22.036 -47.209 -38.633  1.00 28.86  ? 305 PHE B C   1 
ATOM   6603  O O   . PHE B  1 305 ? -21.785 -46.824 -39.782  1.00 24.44  ? 305 PHE B O   1 
ATOM   6604  C CB  . PHE B  1 305 ? -21.983 -49.749 -38.754  1.00 28.49  ? 305 PHE B CB  1 
ATOM   6605  C CG  . PHE B  1 305 ? -22.718 -51.038 -38.455  1.00 30.99  ? 305 PHE B CG  1 
ATOM   6606  C CD1 . PHE B  1 305 ? -23.647 -51.545 -39.352  1.00 32.08  ? 305 PHE B CD1 1 
ATOM   6607  C CD2 . PHE B  1 305 ? -22.511 -51.722 -37.261  1.00 27.04  ? 305 PHE B CD2 1 
ATOM   6608  C CE1 . PHE B  1 305 ? -24.337 -52.715 -39.082  1.00 29.78  ? 305 PHE B CE1 1 
ATOM   6609  C CE2 . PHE B  1 305 ? -23.205 -52.899 -36.987  1.00 25.32  ? 305 PHE B CE2 1 
ATOM   6610  C CZ  . PHE B  1 305 ? -24.120 -53.390 -37.896  1.00 26.16  ? 305 PHE B CZ  1 
ATOM   6611  N N   . ARG B  1 306 ? -21.731 -46.505 -37.547  1.00 27.19  ? 306 ARG B N   1 
ATOM   6612  C CA  . ARG B  1 306 ? -21.179 -45.176 -37.725  1.00 30.61  ? 306 ARG B CA  1 
ATOM   6613  C C   . ARG B  1 306 ? -19.763 -45.298 -38.269  1.00 31.06  ? 306 ARG B C   1 
ATOM   6614  O O   . ARG B  1 306 ? -19.099 -46.326 -38.108  1.00 26.49  ? 306 ARG B O   1 
ATOM   6615  C CB  . ARG B  1 306 ? -21.202 -44.389 -36.414  1.00 30.64  ? 306 ARG B CB  1 
ATOM   6616  C CG  . ARG B  1 306 ? -20.281 -44.935 -35.369  1.00 32.66  ? 306 ARG B CG  1 
ATOM   6617  C CD  . ARG B  1 306 ? -20.118 -43.985 -34.197  1.00 30.60  ? 306 ARG B CD  1 
ATOM   6618  N NE  . ARG B  1 306 ? -18.933 -44.387 -33.477  1.00 32.41  ? 306 ARG B NE  1 
ATOM   6619  C CZ  . ARG B  1 306 ? -18.258 -43.637 -32.621  1.00 30.41  ? 306 ARG B CZ  1 
ATOM   6620  N NH1 . ARG B  1 306 ? -18.617 -42.399 -32.343  1.00 30.08  ? 306 ARG B NH1 1 
ATOM   6621  N NH2 . ARG B  1 306 ? -17.195 -44.150 -32.052  1.00 31.81  ? 306 ARG B NH2 1 
ATOM   6622  N N   . ASP B  1 307 ? -19.327 -44.260 -38.968  1.00 32.49  ? 307 ASP B N   1 
ATOM   6623  C CA  . ASP B  1 307 ? -17.941 -44.177 -39.429  1.00 34.15  ? 307 ASP B CA  1 
ATOM   6624  C C   . ASP B  1 307 ? -17.092 -43.765 -38.233  1.00 30.80  ? 307 ASP B C   1 
ATOM   6625  O O   . ASP B  1 307 ? -17.045 -42.589 -37.860  1.00 28.59  ? 307 ASP B O   1 
ATOM   6626  C CB  . ASP B  1 307 ? -17.821 -43.189 -40.580  1.00 35.34  ? 307 ASP B CB  1 
ATOM   6627  C CG  . ASP B  1 307 ? -16.416 -43.084 -41.124  1.00 37.17  ? 307 ASP B CG  1 
ATOM   6628  O OD1 . ASP B  1 307 ? -15.473 -42.859 -40.336  1.00 33.62  ? 307 ASP B OD1 1 
ATOM   6629  O OD2 . ASP B  1 307 ? -16.264 -43.189 -42.360  1.00 34.60  ? 307 ASP B OD2 1 
ATOM   6630  N N   . LYS B  1 308 ? -16.397 -44.738 -37.646  1.00 27.15  ? 308 LYS B N   1 
ATOM   6631  C CA  . LYS B  1 308 ? -15.747 -44.494 -36.361  1.00 28.59  ? 308 LYS B CA  1 
ATOM   6632  C C   . LYS B  1 308 ? -14.606 -43.480 -36.494  1.00 29.78  ? 308 LYS B C   1 
ATOM   6633  O O   . LYS B  1 308 ? -14.450 -42.603 -35.635  1.00 32.21  ? 308 LYS B O   1 
ATOM   6634  C CB  . LYS B  1 308 ? -15.266 -45.826 -35.779  1.00 28.79  ? 308 LYS B CB  1 
ATOM   6635  C CG  . LYS B  1 308 ? -14.499 -45.739 -34.464  1.00 33.65  ? 308 LYS B CG  1 
ATOM   6636  C CD  . LYS B  1 308 ? -14.042 -47.143 -34.049  1.00 36.91  ? 308 LYS B CD  1 
ATOM   6637  C CE  . LYS B  1 308 ? -12.628 -47.106 -33.489  1.00 42.79  ? 308 LYS B CE  1 
ATOM   6638  N NZ  . LYS B  1 308 ? -12.487 -46.021 -32.486  1.00 46.99  ? 308 LYS B NZ  1 
ATOM   6639  N N   . THR B  1 309 ? -13.829 -43.545 -37.581  1.00 31.44  ? 309 THR B N   1 
ATOM   6640  C CA  . THR B  1 309 ? -12.702 -42.618 -37.732  1.00 30.79  ? 309 THR B CA  1 
ATOM   6641  C C   . THR B  1 309 ? -13.171 -41.158 -37.801  1.00 28.82  ? 309 THR B C   1 
ATOM   6642  O O   . THR B  1 309 ? -12.619 -40.283 -37.131  1.00 35.55  ? 309 THR B O   1 
ATOM   6643  C CB  . THR B  1 309 ? -11.884 -42.970 -38.979  1.00 31.31  ? 309 THR B CB  1 
ATOM   6644  O OG1 . THR B  1 309 ? -12.694 -42.760 -40.130  1.00 41.66  ? 309 THR B OG1 1 
ATOM   6645  C CG2 . THR B  1 309 ? -11.404 -44.400 -38.967  1.00 25.77  ? 309 THR B CG2 1 
ATOM   6646  N N   . LEU B  1 310 ? -14.164 -40.871 -38.641  1.00 33.13  ? 310 LEU B N   1 
ATOM   6647  C CA  . LEU B  1 310 ? -14.648 -39.498 -38.777  1.00 31.61  ? 310 LEU B CA  1 
ATOM   6648  C C   . LEU B  1 310 ? -15.304 -39.009 -37.494  1.00 30.59  ? 310 LEU B C   1 
ATOM   6649  O O   . LEU B  1 310 ? -15.160 -37.837 -37.116  1.00 28.93  ? 310 LEU B O   1 
ATOM   6650  C CB  . LEU B  1 310 ? -15.649 -39.412 -39.920  1.00 26.28  ? 310 LEU B CB  1 
ATOM   6651  C CG  . LEU B  1 310 ? -15.182 -39.609 -41.366  1.00 26.66  ? 310 LEU B CG  1 
ATOM   6652  C CD1 . LEU B  1 310 ? -16.390 -39.460 -42.292  1.00 28.44  ? 310 LEU B CD1 1 
ATOM   6653  C CD2 . LEU B  1 310 ? -14.093 -38.610 -41.710  1.00 28.71  ? 310 LEU B CD2 1 
ATOM   6654  N N   . SER B  1 311 ? -16.082 -39.876 -36.851  1.00 30.14  ? 311 SER B N   1 
ATOM   6655  C CA  . SER B  1 311 ? -16.679 -39.536 -35.563  1.00 26.59  ? 311 SER B CA  1 
ATOM   6656  C C   . SER B  1 311 ? -15.610 -39.229 -34.525  1.00 29.59  ? 311 SER B C   1 
ATOM   6657  O O   . SER B  1 311 ? -15.711 -38.239 -33.794  1.00 31.37  ? 311 SER B O   1 
ATOM   6658  C CB  . SER B  1 311 ? -17.579 -40.672 -35.086  1.00 25.62  ? 311 SER B CB  1 
ATOM   6659  O OG  . SER B  1 311 ? -18.701 -40.828 -35.946  1.00 27.06  ? 311 SER B OG  1 
ATOM   6660  N N   . ASP B  1 312 ? -14.578 -40.072 -34.438  1.00 30.29  ? 312 ASP B N   1 
ATOM   6661  C CA  . ASP B  1 312 ? -13.529 -39.842 -33.444  1.00 28.73  ? 312 ASP B CA  1 
ATOM   6662  C C   . ASP B  1 312 ? -12.711 -38.586 -33.759  1.00 31.77  ? 312 ASP B C   1 
ATOM   6663  O O   . ASP B  1 312 ? -12.196 -37.931 -32.840  1.00 30.63  ? 312 ASP B O   1 
ATOM   6664  C CB  . ASP B  1 312 ? -12.603 -41.065 -33.348  1.00 30.73  ? 312 ASP B CB  1 
ATOM   6665  C CG  . ASP B  1 312 ? -13.258 -42.258 -32.639  1.00 34.07  ? 312 ASP B CG  1 
ATOM   6666  O OD1 . ASP B  1 312 ? -14.381 -42.110 -32.106  1.00 33.92  ? 312 ASP B OD1 1 
ATOM   6667  O OD2 . ASP B  1 312 ? -12.641 -43.349 -32.606  1.00 35.80  ? 312 ASP B OD2 1 
ATOM   6668  N N   . LEU B  1 313 ? -12.556 -38.248 -35.047  1.00 29.91  ? 313 LEU B N   1 
ATOM   6669  C CA  . LEU B  1 313 ? -11.794 -37.054 -35.416  1.00 29.32  ? 313 LEU B CA  1 
ATOM   6670  C C   . LEU B  1 313 ? -12.433 -35.784 -34.862  1.00 26.54  ? 313 LEU B C   1 
ATOM   6671  O O   . LEU B  1 313 ? -11.734 -34.899 -34.350  1.00 28.09  ? 313 LEU B O   1 
ATOM   6672  C CB  . LEU B  1 313 ? -11.680 -36.953 -36.941  1.00 29.06  ? 313 LEU B CB  1 
ATOM   6673  C CG  . LEU B  1 313 ? -10.540 -37.722 -37.604  1.00 30.21  ? 313 LEU B CG  1 
ATOM   6674  C CD1 . LEU B  1 313 ? -10.778 -37.799 -39.119  1.00 29.01  ? 313 LEU B CD1 1 
ATOM   6675  C CD2 . LEU B  1 313 ? -9.233  -37.025 -37.321  1.00 31.07  ? 313 LEU B CD2 1 
ATOM   6676  N N   . ILE B  1 314 ? -13.760 -35.668 -34.969  1.00 26.05  ? 314 ILE B N   1 
ATOM   6677  C CA  . ILE B  1 314 ? -14.459 -34.519 -34.399  1.00 25.18  ? 314 ILE B CA  1 
ATOM   6678  C C   . ILE B  1 314 ? -14.443 -34.588 -32.873  1.00 27.48  ? 314 ILE B C   1 
ATOM   6679  O O   . ILE B  1 314 ? -14.176 -33.589 -32.185  1.00 26.15  ? 314 ILE B O   1 
ATOM   6680  C CB  . ILE B  1 314 ? -15.895 -34.447 -34.952  1.00 23.89  ? 314 ILE B CB  1 
ATOM   6681  C CG1 . ILE B  1 314 ? -15.871 -34.012 -36.423  1.00 24.89  ? 314 ILE B CG1 1 
ATOM   6682  C CG2 . ILE B  1 314 ? -16.732 -33.487 -34.144  1.00 25.98  ? 314 ILE B CG2 1 
ATOM   6683  C CD1 . ILE B  1 314 ? -17.239 -34.055 -37.116  1.00 25.41  ? 314 ILE B CD1 1 
ATOM   6684  N N   . GLY B  1 315 ? -14.707 -35.772 -32.323  1.00 24.10  ? 315 GLY B N   1 
ATOM   6685  C CA  . GLY B  1 315 ? -14.871 -35.906 -30.890  1.00 22.52  ? 315 GLY B CA  1 
ATOM   6686  C C   . GLY B  1 315 ? -13.578 -35.854 -30.112  1.00 26.33  ? 315 GLY B C   1 
ATOM   6687  O O   . GLY B  1 315 ? -13.600 -35.489 -28.931  1.00 30.65  ? 315 GLY B O   1 
ATOM   6688  N N   . PHE B  1 316 ? -12.451 -36.187 -30.748  1.00 23.58  ? 316 PHE B N   1 
ATOM   6689  C CA  . PHE B  1 316 ? -11.194 -36.416 -30.032  1.00 29.29  ? 316 PHE B CA  1 
ATOM   6690  C C   . PHE B  1 316 ? -10.015 -35.655 -30.608  1.00 28.20  ? 316 PHE B C   1 
ATOM   6691  O O   . PHE B  1 316 ? -9.102  -35.277 -29.872  1.00 30.73  ? 316 PHE B O   1 
ATOM   6692  C CB  . PHE B  1 316 ? -10.819 -37.904 -30.033  1.00 34.92  ? 316 PHE B CB  1 
ATOM   6693  C CG  . PHE B  1 316 ? -11.723 -38.758 -29.200  1.00 42.64  ? 316 PHE B CG  1 
ATOM   6694  C CD1 . PHE B  1 316 ? -12.312 -38.244 -28.061  1.00 47.02  ? 316 PHE B CD1 1 
ATOM   6695  C CD2 . PHE B  1 316 ? -11.984 -40.076 -29.557  1.00 43.43  ? 316 PHE B CD2 1 
ATOM   6696  C CE1 . PHE B  1 316 ? -13.148 -39.017 -27.296  1.00 47.26  ? 316 PHE B CE1 1 
ATOM   6697  C CE2 . PHE B  1 316 ? -12.830 -40.852 -28.792  1.00 41.60  ? 316 PHE B CE2 1 
ATOM   6698  C CZ  . PHE B  1 316 ? -13.404 -40.323 -27.664  1.00 43.70  ? 316 PHE B CZ  1 
ATOM   6699  N N   . SER B  1 317 ? -9.997  -35.449 -31.923  1.00 28.00  ? 317 SER B N   1 
ATOM   6700  C CA  . SER B  1 317 ? -8.788  -34.953 -32.560  1.00 31.36  ? 317 SER B CA  1 
ATOM   6701  C C   . SER B  1 317 ? -8.838  -33.459 -32.892  1.00 33.94  ? 317 SER B C   1 
ATOM   6702  O O   . SER B  1 317 ? -7.889  -32.732 -32.579  1.00 34.70  ? 317 SER B O   1 
ATOM   6703  C CB  . SER B  1 317 ? -8.503  -35.794 -33.815  1.00 31.82  ? 317 SER B CB  1 
ATOM   6704  O OG  . SER B  1 317 ? -7.205  -35.533 -34.339  1.00 42.00  ? 317 SER B OG  1 
ATOM   6705  N N   . TYR B  1 318 ? -9.920  -32.969 -33.507  1.00 27.45  ? 318 TYR B N   1 
ATOM   6706  C CA  . TYR B  1 318 ? -9.868  -31.633 -34.110  1.00 27.90  ? 318 TYR B CA  1 
ATOM   6707  C C   . TYR B  1 318 ? -9.784  -30.490 -33.095  1.00 31.31  ? 318 TYR B C   1 
ATOM   6708  O O   . TYR B  1 318 ? -9.467  -29.359 -33.492  1.00 29.31  ? 318 TYR B O   1 
ATOM   6709  C CB  . TYR B  1 318 ? -11.080 -31.425 -35.024  1.00 29.25  ? 318 TYR B CB  1 
ATOM   6710  C CG  . TYR B  1 318 ? -11.013 -32.217 -36.311  1.00 31.22  ? 318 TYR B CG  1 
ATOM   6711  C CD1 . TYR B  1 318 ? -9.790  -32.538 -36.893  1.00 32.64  ? 318 TYR B CD1 1 
ATOM   6712  C CD2 . TYR B  1 318 ? -12.176 -32.633 -36.951  1.00 32.90  ? 318 TYR B CD2 1 
ATOM   6713  C CE1 . TYR B  1 318 ? -9.729  -33.246 -38.095  1.00 30.61  ? 318 TYR B CE1 1 
ATOM   6714  C CE2 . TYR B  1 318 ? -12.127 -33.345 -38.139  1.00 31.01  ? 318 TYR B CE2 1 
ATOM   6715  C CZ  . TYR B  1 318 ? -10.901 -33.652 -38.704  1.00 31.10  ? 318 TYR B CZ  1 
ATOM   6716  O OH  . TYR B  1 318 ? -10.859 -34.357 -39.888  1.00 34.89  ? 318 TYR B OH  1 
ATOM   6717  N N   . HIS B  1 319 ? -10.036 -30.743 -31.801  1.00 29.95  ? 319 HIS B N   1 
ATOM   6718  C CA  . HIS B  1 319 ? -9.844  -29.682 -30.818  1.00 34.68  ? 319 HIS B CA  1 
ATOM   6719  C C   . HIS B  1 319 ? -8.410  -29.169 -30.830  1.00 33.11  ? 319 HIS B C   1 
ATOM   6720  O O   . HIS B  1 319 ? -8.163  -28.006 -30.490  1.00 28.00  ? 319 HIS B O   1 
ATOM   6721  C CB  . HIS B  1 319 ? -10.208 -30.176 -29.414  1.00 34.36  ? 319 HIS B CB  1 
ATOM   6722  C CG  . HIS B  1 319 ? -9.210  -31.127 -28.824  1.00 34.64  ? 319 HIS B CG  1 
ATOM   6723  N ND1 . HIS B  1 319 ? -8.111  -30.708 -28.107  1.00 38.97  ? 319 HIS B ND1 1 
ATOM   6724  C CD2 . HIS B  1 319 ? -9.142  -32.479 -28.856  1.00 35.66  ? 319 HIS B CD2 1 
ATOM   6725  C CE1 . HIS B  1 319 ? -7.415  -31.761 -27.713  1.00 35.32  ? 319 HIS B CE1 1 
ATOM   6726  N NE2 . HIS B  1 319 ? -8.022  -32.848 -28.149  1.00 34.25  ? 319 HIS B NE2 1 
ATOM   6727  N N   . ALA B  1 320 ? -7.463  -30.023 -31.209  1.00 30.13  ? 320 ALA B N   1 
ATOM   6728  C CA  . ALA B  1 320 ? -6.047  -29.700 -31.230  1.00 32.74  ? 320 ALA B CA  1 
ATOM   6729  C C   . ALA B  1 320 ? -5.590  -29.192 -32.589  1.00 34.63  ? 320 ALA B C   1 
ATOM   6730  O O   . ALA B  1 320 ? -4.384  -29.032 -32.802  1.00 36.14  ? 320 ALA B O   1 
ATOM   6731  C CB  . ALA B  1 320 ? -5.222  -30.927 -30.834  1.00 35.58  ? 320 ALA B CB  1 
ATOM   6732  N N   . TRP B  1 321 ? -6.523  -28.936 -33.499  1.00 33.96  ? 321 TRP B N   1 
ATOM   6733  C CA  . TRP B  1 321 ? -6.238  -28.413 -34.825  1.00 41.89  ? 321 TRP B CA  1 
ATOM   6734  C C   . TRP B  1 321 ? -6.748  -26.986 -34.958  1.00 42.70  ? 321 TRP B C   1 
ATOM   6735  O O   . TRP B  1 321 ? -7.744  -26.602 -34.343  1.00 45.17  ? 321 TRP B O   1 
ATOM   6736  C CB  . TRP B  1 321 ? -6.916  -29.237 -35.926  1.00 40.41  ? 321 TRP B CB  1 
ATOM   6737  C CG  . TRP B  1 321 ? -6.497  -30.659 -36.050  1.00 42.77  ? 321 TRP B CG  1 
ATOM   6738  C CD1 . TRP B  1 321 ? -6.363  -31.577 -35.047  1.00 40.60  ? 321 TRP B CD1 1 
ATOM   6739  C CD2 . TRP B  1 321 ? -6.196  -31.345 -37.268  1.00 45.48  ? 321 TRP B CD2 1 
ATOM   6740  N NE1 . TRP B  1 321 ? -5.981  -32.789 -35.568  1.00 40.91  ? 321 TRP B NE1 1 
ATOM   6741  C CE2 . TRP B  1 321 ? -5.872  -32.673 -36.929  1.00 43.78  ? 321 TRP B CE2 1 
ATOM   6742  C CE3 . TRP B  1 321 ? -6.164  -30.962 -38.616  1.00 45.08  ? 321 TRP B CE3 1 
ATOM   6743  C CZ2 . TRP B  1 321 ? -5.519  -33.620 -37.887  1.00 43.49  ? 321 TRP B CZ2 1 
ATOM   6744  C CZ3 . TRP B  1 321 ? -5.814  -31.903 -39.567  1.00 43.66  ? 321 TRP B CZ3 1 
ATOM   6745  C CH2 . TRP B  1 321 ? -5.494  -33.216 -39.198  1.00 43.13  ? 321 TRP B CH2 1 
ATOM   6746  N N   . ASN B  1 322 ? -6.065  -26.216 -35.793  1.00 42.78  ? 322 ASN B N   1 
ATOM   6747  C CA  . ASN B  1 322 ? -6.660  -25.023 -36.374  1.00 48.07  ? 322 ASN B CA  1 
ATOM   6748  C C   . ASN B  1 322 ? -8.000  -25.387 -37.015  1.00 43.05  ? 322 ASN B C   1 
ATOM   6749  O O   . ASN B  1 322 ? -8.179  -26.498 -37.525  1.00 39.71  ? 322 ASN B O   1 
ATOM   6750  C CB  . ASN B  1 322 ? -5.660  -24.440 -37.389  1.00 59.14  ? 322 ASN B CB  1 
ATOM   6751  C CG  . ASN B  1 322 ? -6.249  -23.380 -38.288  1.00 68.20  ? 322 ASN B CG  1 
ATOM   6752  O OD1 . ASN B  1 322 ? -7.027  -23.676 -39.192  1.00 71.45  ? 322 ASN B OD1 1 
ATOM   6753  N ND2 . ASN B  1 322 ? -5.848  -22.130 -38.067  1.00 71.54  ? 322 ASN B ND2 1 
ATOM   6754  N N   . ALA B  1 323 ? -8.964  -24.461 -36.957  1.00 38.33  ? 323 ALA B N   1 
ATOM   6755  C CA  . ALA B  1 323 ? -10.283 -24.748 -37.523  1.00 36.53  ? 323 ALA B CA  1 
ATOM   6756  C C   . ALA B  1 323 ? -10.220 -24.943 -39.039  1.00 37.47  ? 323 ALA B C   1 
ATOM   6757  O O   . ALA B  1 323 ? -10.857 -25.854 -39.581  1.00 36.24  ? 323 ALA B O   1 
ATOM   6758  C CB  . ALA B  1 323 ? -11.273 -23.628 -37.179  1.00 32.46  ? 323 ALA B CB  1 
ATOM   6759  N N   . GLU B  1 324 ? -9.470  -24.091 -39.744  1.00 37.49  ? 324 GLU B N   1 
ATOM   6760  C CA  . GLU B  1 324 ? -9.391  -24.224 -41.195  1.00 41.17  ? 324 GLU B CA  1 
ATOM   6761  C C   . GLU B  1 324 ? -8.739  -25.547 -41.596  1.00 38.88  ? 324 GLU B C   1 
ATOM   6762  O O   . GLU B  1 324 ? -9.192  -26.207 -42.538  1.00 35.27  ? 324 GLU B O   1 
ATOM   6763  C CB  . GLU B  1 324 ? -8.639  -23.027 -41.790  1.00 50.46  ? 324 GLU B CB  1 
ATOM   6764  C CG  . GLU B  1 324 ? -9.395  -22.343 -42.930  1.00 66.57  ? 324 GLU B CG  1 
ATOM   6765  C CD  . GLU B  1 324 ? -9.045  -20.861 -43.114  1.00 77.35  ? 324 GLU B CD  1 
ATOM   6766  O OE1 . GLU B  1 324 ? -7.858  -20.534 -43.343  1.00 80.07  ? 324 GLU B OE1 1 
ATOM   6767  O OE2 . GLU B  1 324 ? -9.970  -20.019 -43.040  1.00 79.63  ? 324 GLU B OE2 1 
ATOM   6768  N N   . ASP B  1 325 ? -7.682  -25.960 -40.887  1.00 36.18  ? 325 ASP B N   1 
ATOM   6769  C CA  . ASP B  1 325 ? -7.023  -27.224 -41.207  1.00 34.71  ? 325 ASP B CA  1 
ATOM   6770  C C   . ASP B  1 325 ? -7.918  -28.420 -40.905  1.00 36.37  ? 325 ASP B C   1 
ATOM   6771  O O   . ASP B  1 325 ? -7.853  -29.438 -41.607  1.00 36.84  ? 325 ASP B O   1 
ATOM   6772  C CB  . ASP B  1 325 ? -5.711  -27.352 -40.433  1.00 37.22  ? 325 ASP B CB  1 
ATOM   6773  C CG  . ASP B  1 325 ? -4.658  -26.349 -40.874  1.00 50.74  ? 325 ASP B CG  1 
ATOM   6774  O OD1 . ASP B  1 325 ? -4.839  -25.684 -41.922  1.00 54.74  ? 325 ASP B OD1 1 
ATOM   6775  O OD2 . ASP B  1 325 ? -3.643  -26.218 -40.156  1.00 53.71  ? 325 ASP B OD2 1 
ATOM   6776  N N   . ALA B  1 326 ? -8.748  -28.329 -39.866  1.00 36.96  ? 326 ALA B N   1 
ATOM   6777  C CA  . ALA B  1 326 ? -9.578  -29.469 -39.494  1.00 32.17  ? 326 ALA B CA  1 
ATOM   6778  C C   . ALA B  1 326 ? -10.684 -29.707 -40.519  1.00 33.83  ? 326 ALA B C   1 
ATOM   6779  O O   . ALA B  1 326 ? -10.942 -30.854 -40.908  1.00 35.78  ? 326 ALA B O   1 
ATOM   6780  C CB  . ALA B  1 326 ? -10.164 -29.256 -38.101  1.00 30.18  ? 326 ALA B CB  1 
ATOM   6781  N N   . VAL B  1 327 ? -11.343 -28.641 -40.972  1.00 31.04  ? 327 VAL B N   1 
ATOM   6782  C CA  . VAL B  1 327 ? -12.408 -28.801 -41.964  1.00 35.94  ? 327 VAL B CA  1 
ATOM   6783  C C   . VAL B  1 327 ? -11.842 -29.346 -43.266  1.00 35.58  ? 327 VAL B C   1 
ATOM   6784  O O   . VAL B  1 327 ? -12.460 -30.198 -43.918  1.00 37.07  ? 327 VAL B O   1 
ATOM   6785  C CB  . VAL B  1 327 ? -13.162 -27.468 -42.173  1.00 41.05  ? 327 VAL B CB  1 
ATOM   6786  C CG1 . VAL B  1 327 ? -12.196 -26.321 -42.385  1.00 45.94  ? 327 VAL B CG1 1 
ATOM   6787  C CG2 . VAL B  1 327 ? -14.133 -27.568 -43.365  1.00 37.15  ? 327 VAL B CG2 1 
ATOM   6788  N N   . ARG B  1 328 ? -10.655 -28.879 -43.664  1.00 35.83  ? 328 ARG B N   1 
ATOM   6789  C CA  . ARG B  1 328 ? -10.063 -29.366 -44.905  1.00 38.01  ? 328 ARG B CA  1 
ATOM   6790  C C   . ARG B  1 328 ? -9.761  -30.858 -44.820  1.00 36.39  ? 328 ARG B C   1 
ATOM   6791  O O   . ARG B  1 328 ? -10.017 -31.608 -45.770  1.00 34.50  ? 328 ARG B O   1 
ATOM   6792  C CB  . ARG B  1 328 ? -8.791  -28.592 -45.234  1.00 43.40  ? 328 ARG B CB  1 
ATOM   6793  C CG  . ARG B  1 328 ? -7.854  -29.390 -46.140  1.00 54.59  ? 328 ARG B CG  1 
ATOM   6794  C CD  . ARG B  1 328 ? -6.708  -28.560 -46.674  1.00 63.38  ? 328 ARG B CD  1 
ATOM   6795  N NE  . ARG B  1 328 ? -5.871  -28.038 -45.601  1.00 69.99  ? 328 ARG B NE  1 
ATOM   6796  C CZ  . ARG B  1 328 ? -5.749  -26.744 -45.311  1.00 76.03  ? 328 ARG B CZ  1 
ATOM   6797  N NH1 . ARG B  1 328 ? -6.412  -25.830 -46.015  1.00 78.09  ? 328 ARG B NH1 1 
ATOM   6798  N NH2 . ARG B  1 328 ? -4.964  -26.360 -44.315  1.00 76.32  ? 328 ARG B NH2 1 
ATOM   6799  N N   . ASP B  1 329 ? -9.203  -31.302 -43.693  1.00 33.79  ? 329 ASP B N   1 
ATOM   6800  C CA  . ASP B  1 329 ? -8.968  -32.725 -43.481  1.00 35.08  ? 329 ASP B CA  1 
ATOM   6801  C C   . ASP B  1 329 ? -10.272 -33.515 -43.564  1.00 35.87  ? 329 ASP B C   1 
ATOM   6802  O O   . ASP B  1 329 ? -10.362 -34.511 -44.291  1.00 36.80  ? 329 ASP B O   1 
ATOM   6803  C CB  . ASP B  1 329 ? -8.280  -32.921 -42.127  1.00 37.76  ? 329 ASP B CB  1 
ATOM   6804  C CG  . ASP B  1 329 ? -7.847  -34.360 -41.879  1.00 37.70  ? 329 ASP B CG  1 
ATOM   6805  O OD1 . ASP B  1 329 ? -6.726  -34.707 -42.290  1.00 37.01  ? 329 ASP B OD1 1 
ATOM   6806  O OD2 . ASP B  1 329 ? -8.619  -35.142 -41.274  1.00 38.67  ? 329 ASP B OD2 1 
ATOM   6807  N N   . PHE B  1 330 ? -11.296 -33.076 -42.822  1.00 33.15  ? 330 PHE B N   1 
ATOM   6808  C CA  . PHE B  1 330 ? -12.596 -33.744 -42.851  1.00 30.93  ? 330 PHE B CA  1 
ATOM   6809  C C   . PHE B  1 330 ? -13.167 -33.788 -44.267  1.00 30.55  ? 330 PHE B C   1 
ATOM   6810  O O   . PHE B  1 330 ? -13.693 -34.818 -44.704  1.00 33.47  ? 330 PHE B O   1 
ATOM   6811  C CB  . PHE B  1 330 ? -13.566 -33.027 -41.914  1.00 29.77  ? 330 PHE B CB  1 
ATOM   6812  C CG  . PHE B  1 330 ? -14.810 -33.811 -41.598  1.00 38.47  ? 330 PHE B CG  1 
ATOM   6813  C CD1 . PHE B  1 330 ? -14.790 -34.803 -40.617  1.00 40.47  ? 330 PHE B CD1 1 
ATOM   6814  C CD2 . PHE B  1 330 ? -16.006 -33.535 -42.247  1.00 29.73  ? 330 PHE B CD2 1 
ATOM   6815  C CE1 . PHE B  1 330 ? -15.941 -35.525 -40.305  1.00 36.45  ? 330 PHE B CE1 1 
ATOM   6816  C CE2 . PHE B  1 330 ? -17.160 -34.245 -41.945  1.00 30.23  ? 330 PHE B CE2 1 
ATOM   6817  C CZ  . PHE B  1 330 ? -17.131 -35.248 -40.978  1.00 29.59  ? 330 PHE B CZ  1 
ATOM   6818  N N   . ILE B  1 331 ? -13.116 -32.666 -44.979  1.00 35.26  ? 331 ILE B N   1 
ATOM   6819  C CA  . ILE B  1 331 ? -13.647 -32.650 -46.339  1.00 40.30  ? 331 ILE B CA  1 
ATOM   6820  C C   . ILE B  1 331 ? -12.850 -33.601 -47.216  1.00 38.25  ? 331 ILE B C   1 
ATOM   6821  O O   . ILE B  1 331 ? -13.418 -34.397 -47.974  1.00 37.74  ? 331 ILE B O   1 
ATOM   6822  C CB  . ILE B  1 331 ? -13.650 -31.218 -46.905  1.00 38.94  ? 331 ILE B CB  1 
ATOM   6823  C CG1 . ILE B  1 331 ? -14.618 -30.335 -46.111  1.00 41.25  ? 331 ILE B CG1 1 
ATOM   6824  C CG2 . ILE B  1 331 ? -14.051 -31.225 -48.390  1.00 36.86  ? 331 ILE B CG2 1 
ATOM   6825  C CD1 . ILE B  1 331 ? -16.043 -30.850 -46.097  1.00 42.95  ? 331 ILE B CD1 1 
ATOM   6826  N N   . GLY B  1 332 ? -11.524 -33.556 -47.101  1.00 38.93  ? 332 GLY B N   1 
ATOM   6827  C CA  . GLY B  1 332 ? -10.681 -34.421 -47.906  1.00 39.84  ? 332 GLY B CA  1 
ATOM   6828  C C   . GLY B  1 332 ? -10.953 -35.898 -47.700  1.00 40.57  ? 332 GLY B C   1 
ATOM   6829  O O   . GLY B  1 332 ? -10.852 -36.687 -48.644  1.00 34.87  ? 332 GLY B O   1 
ATOM   6830  N N   . ARG B  1 333 ? -11.299 -36.299 -46.469  1.00 32.66  ? 333 ARG B N   1 
ATOM   6831  C CA  . ARG B  1 333 ? -11.597 -37.707 -46.228  1.00 42.23  ? 333 ARG B CA  1 
ATOM   6832  C C   . ARG B  1 333 ? -12.930 -38.099 -46.854  1.00 40.70  ? 333 ARG B C   1 
ATOM   6833  O O   . ARG B  1 333 ? -13.078 -39.218 -47.364  1.00 38.92  ? 333 ARG B O   1 
ATOM   6834  C CB  . ARG B  1 333 ? -11.589 -38.002 -44.726  1.00 42.17  ? 333 ARG B CB  1 
ATOM   6835  C CG  . ARG B  1 333 ? -10.202 -37.946 -44.092  1.00 37.18  ? 333 ARG B CG  1 
ATOM   6836  C CD  . ARG B  1 333 ? -10.327 -37.821 -42.586  1.00 32.27  ? 333 ARG B CD  1 
ATOM   6837  N NE  . ARG B  1 333 ? -9.050  -37.903 -41.896  1.00 30.13  ? 333 ARG B NE  1 
ATOM   6838  C CZ  . ARG B  1 333 ? -8.398  -39.038 -41.674  1.00 36.81  ? 333 ARG B CZ  1 
ATOM   6839  N NH1 . ARG B  1 333 ? -8.886  -40.181 -42.127  1.00 37.75  ? 333 ARG B NH1 1 
ATOM   6840  N NH2 . ARG B  1 333 ? -7.246  -39.026 -41.020  1.00 41.34  ? 333 ARG B NH2 1 
ATOM   6841  N N   . LEU B  1 334 ? -13.908 -37.191 -46.830  1.00 31.69  ? 334 LEU B N   1 
ATOM   6842  C CA  . LEU B  1 334 ? -15.185 -37.478 -47.466  1.00 34.83  ? 334 LEU B CA  1 
ATOM   6843  C C   . LEU B  1 334 ? -15.028 -37.606 -48.975  1.00 36.64  ? 334 LEU B C   1 
ATOM   6844  O O   . LEU B  1 334 ? -15.765 -38.362 -49.614  1.00 33.54  ? 334 LEU B O   1 
ATOM   6845  C CB  . LEU B  1 334 ? -16.204 -36.385 -47.130  1.00 31.39  ? 334 LEU B CB  1 
ATOM   6846  C CG  . LEU B  1 334 ? -16.673 -36.299 -45.673  1.00 30.08  ? 334 LEU B CG  1 
ATOM   6847  C CD1 . LEU B  1 334 ? -17.653 -35.147 -45.496  1.00 29.98  ? 334 LEU B CD1 1 
ATOM   6848  C CD2 . LEU B  1 334 ? -17.317 -37.601 -45.227  1.00 34.06  ? 334 LEU B CD2 1 
ATOM   6849  N N   . LYS B  1 335 ? -14.079 -36.877 -49.553  1.00 37.69  ? 335 LYS B N   1 
ATOM   6850  C CA  . LYS B  1 335 ? -13.819 -36.998 -50.983  1.00 38.72  ? 335 LYS B CA  1 
ATOM   6851  C C   . LYS B  1 335 ? -13.220 -38.358 -51.309  1.00 43.11  ? 335 LYS B C   1 
ATOM   6852  O O   . LYS B  1 335 ? -13.551 -38.962 -52.337  1.00 43.28  ? 335 LYS B O   1 
ATOM   6853  C CB  . LYS B  1 335 ? -12.893 -35.868 -51.439  1.00 44.80  ? 335 LYS B CB  1 
ATOM   6854  C CG  . LYS B  1 335 ? -12.922 -35.568 -52.943  1.00 57.98  ? 335 LYS B CG  1 
ATOM   6855  C CD  . LYS B  1 335 ? -13.682 -34.280 -53.239  1.00 63.24  ? 335 LYS B CD  1 
ATOM   6856  C CE  . LYS B  1 335 ? -14.047 -34.148 -54.712  1.00 67.30  ? 335 LYS B CE  1 
ATOM   6857  N NZ  . LYS B  1 335 ? -13.910 -32.745 -55.223  1.00 67.06  ? 335 LYS B NZ  1 
ATOM   6858  N N   . LYS B  1 336 ? -12.337 -38.857 -50.443  1.00 43.50  ? 336 LYS B N   1 
ATOM   6859  C CA  . LYS B  1 336 ? -11.741 -40.166 -50.676  1.00 46.48  ? 336 LYS B CA  1 
ATOM   6860  C C   . LYS B  1 336 ? -12.774 -41.278 -50.525  1.00 43.64  ? 336 LYS B C   1 
ATOM   6861  O O   . LYS B  1 336 ? -12.742 -42.264 -51.266  1.00 50.30  ? 336 LYS B O   1 
ATOM   6862  C CB  . LYS B  1 336 ? -10.553 -40.381 -49.732  1.00 50.53  ? 336 LYS B CB  1 
ATOM   6863  C CG  . LYS B  1 336 ? -9.285  -39.644 -50.174  1.00 57.69  ? 336 LYS B CG  1 
ATOM   6864  C CD  . LYS B  1 336 ? -8.059  -40.046 -49.355  1.00 60.54  ? 336 LYS B CD  1 
ATOM   6865  C CE  . LYS B  1 336 ? -7.419  -41.340 -49.887  1.00 65.12  ? 336 LYS B CE  1 
ATOM   6866  N NZ  . LYS B  1 336 ? -7.104  -41.292 -51.355  1.00 68.12  ? 336 LYS B NZ  1 
ATOM   6867  N N   . ILE B  1 337 ? -13.696 -41.143 -49.571  1.00 37.75  ? 337 ILE B N   1 
ATOM   6868  C CA  . ILE B  1 337 ? -14.820 -42.072 -49.504  1.00 36.34  ? 337 ILE B CA  1 
ATOM   6869  C C   . ILE B  1 337 ? -15.652 -41.980 -50.776  1.00 40.32  ? 337 ILE B C   1 
ATOM   6870  O O   . ILE B  1 337 ? -16.036 -42.996 -51.368  1.00 43.84  ? 337 ILE B O   1 
ATOM   6871  C CB  . ILE B  1 337 ? -15.675 -41.783 -48.261  1.00 35.25  ? 337 ILE B CB  1 
ATOM   6872  C CG1 . ILE B  1 337 ? -14.919 -42.184 -46.985  1.00 34.17  ? 337 ILE B CG1 1 
ATOM   6873  C CG2 . ILE B  1 337 ? -17.001 -42.505 -48.384  1.00 37.84  ? 337 ILE B CG2 1 
ATOM   6874  C CD1 . ILE B  1 337 ? -15.509 -41.617 -45.713  1.00 36.91  ? 337 ILE B CD1 1 
ATOM   6875  N N   . HIS B  1 338 ? -15.939 -40.753 -51.209  1.00 38.75  ? 338 HIS B N   1 
ATOM   6876  C CA  . HIS B  1 338 ? -16.777 -40.521 -52.381  1.00 40.46  ? 338 HIS B CA  1 
ATOM   6877  C C   . HIS B  1 338 ? -16.186 -41.166 -53.636  1.00 41.66  ? 338 HIS B C   1 
ATOM   6878  O O   . HIS B  1 338 ? -16.926 -41.680 -54.490  1.00 38.87  ? 338 HIS B O   1 
ATOM   6879  C CB  . HIS B  1 338 ? -16.954 -39.010 -52.550  1.00 38.31  ? 338 HIS B CB  1 
ATOM   6880  C CG  . HIS B  1 338 ? -17.730 -38.613 -53.765  1.00 42.40  ? 338 HIS B CG  1 
ATOM   6881  N ND1 . HIS B  1 338 ? -17.160 -37.925 -54.815  1.00 46.47  ? 338 HIS B ND1 1 
ATOM   6882  C CD2 . HIS B  1 338 ? -19.032 -38.787 -54.090  1.00 44.47  ? 338 HIS B CD2 1 
ATOM   6883  C CE1 . HIS B  1 338 ? -18.074 -37.709 -55.745  1.00 46.49  ? 338 HIS B CE1 1 
ATOM   6884  N NE2 . HIS B  1 338 ? -19.219 -38.222 -55.330  1.00 47.08  ? 338 HIS B NE2 1 
ATOM   6885  N N   . GLU B  1 339 ? -14.855 -41.171 -53.762  1.00 45.79  ? 339 GLU B N   1 
ATOM   6886  C CA  . GLU B  1 339 ? -14.210 -41.727 -54.952  1.00 48.45  ? 339 GLU B CA  1 
ATOM   6887  C C   . GLU B  1 339 ? -13.882 -43.211 -54.838  1.00 48.84  ? 339 GLU B C   1 
ATOM   6888  O O   . GLU B  1 339 ? -13.581 -43.841 -55.856  1.00 49.78  ? 339 GLU B O   1 
ATOM   6889  C CB  . GLU B  1 339 ? -12.915 -40.968 -55.267  1.00 52.69  ? 339 GLU B CB  1 
ATOM   6890  C CG  . GLU B  1 339 ? -13.074 -39.462 -55.380  1.00 56.74  ? 339 GLU B CG  1 
ATOM   6891  C CD  . GLU B  1 339 ? -11.745 -38.733 -55.302  1.00 61.67  ? 339 GLU B CD  1 
ATOM   6892  O OE1 . GLU B  1 339 ? -11.669 -37.574 -55.766  1.00 62.90  ? 339 GLU B OE1 1 
ATOM   6893  O OE2 . GLU B  1 339 ? -10.776 -39.320 -54.773  1.00 62.79  ? 339 GLU B OE2 1 
ATOM   6894  N N   . SER B  1 340 ? -13.922 -43.784 -53.633  1.00 47.32  ? 340 SER B N   1 
ATOM   6895  C CA  . SER B  1 340 ? -13.486 -45.162 -53.440  1.00 41.36  ? 340 SER B CA  1 
ATOM   6896  C C   . SER B  1 340 ? -14.555 -46.180 -53.801  1.00 39.64  ? 340 SER B C   1 
ATOM   6897  O O   . SER B  1 340 ? -14.243 -47.377 -53.924  1.00 40.98  ? 340 SER B O   1 
ATOM   6898  C CB  . SER B  1 340 ? -13.068 -45.368 -51.987  1.00 43.74  ? 340 SER B CB  1 
ATOM   6899  O OG  . SER B  1 340 ? -14.150 -45.029 -51.128  1.00 47.17  ? 340 SER B OG  1 
ATOM   6900  N N   . VAL B  1 341 ? -15.795 -45.733 -53.963  1.00 41.90  ? 341 VAL B N   1 
ATOM   6901  C CA  . VAL B  1 341 ? -16.943 -46.584 -54.232  1.00 46.41  ? 341 VAL B CA  1 
ATOM   6902  C C   . VAL B  1 341 ? -17.683 -45.996 -55.423  1.00 48.26  ? 341 VAL B C   1 
ATOM   6903  O O   . VAL B  1 341 ? -17.743 -44.774 -55.592  1.00 45.30  ? 341 VAL B O   1 
ATOM   6904  C CB  . VAL B  1 341 ? -17.896 -46.703 -53.012  1.00 44.18  ? 341 VAL B CB  1 
ATOM   6905  C CG1 . VAL B  1 341 ? -17.202 -47.398 -51.855  1.00 46.51  ? 341 VAL B CG1 1 
ATOM   6906  C CG2 . VAL B  1 341 ? -18.406 -45.339 -52.565  1.00 41.47  ? 341 VAL B CG2 1 
ATOM   6907  N N   . ASP B  1 342 ? -18.252 -46.872 -56.248  1.00 53.46  ? 342 ASP B N   1 
ATOM   6908  C CA  . ASP B  1 342 ? -19.044 -46.426 -57.387  1.00 58.56  ? 342 ASP B CA  1 
ATOM   6909  C C   . ASP B  1 342 ? -20.520 -46.260 -57.051  1.00 53.86  ? 342 ASP B C   1 
ATOM   6910  O O   . ASP B  1 342 ? -21.274 -45.756 -57.889  1.00 52.33  ? 342 ASP B O   1 
ATOM   6911  C CB  . ASP B  1 342 ? -18.883 -47.397 -58.563  1.00 68.98  ? 342 ASP B CB  1 
ATOM   6912  C CG  . ASP B  1 342 ? -19.480 -48.758 -58.282  1.00 75.60  ? 342 ASP B CG  1 
ATOM   6913  O OD1 . ASP B  1 342 ? -19.021 -49.436 -57.334  1.00 75.22  ? 342 ASP B OD1 1 
ATOM   6914  O OD2 . ASP B  1 342 ? -20.410 -49.149 -59.019  1.00 78.48  ? 342 ASP B OD2 1 
ATOM   6915  N N   . PHE B  1 343 ? -20.950 -46.660 -55.851  1.00 47.39  ? 343 PHE B N   1 
ATOM   6916  C CA  . PHE B  1 343 ? -22.313 -46.412 -55.400  1.00 43.65  ? 343 PHE B CA  1 
ATOM   6917  C C   . PHE B  1 343 ? -22.345 -45.157 -54.521  1.00 44.54  ? 343 PHE B C   1 
ATOM   6918  O O   . PHE B  1 343 ? -21.353 -44.442 -54.367  1.00 44.77  ? 343 PHE B O   1 
ATOM   6919  C CB  . PHE B  1 343 ? -22.882 -47.642 -54.675  1.00 42.64  ? 343 PHE B CB  1 
ATOM   6920  C CG  . PHE B  1 343 ? -22.105 -48.063 -53.441  1.00 41.67  ? 343 PHE B CG  1 
ATOM   6921  C CD1 . PHE B  1 343 ? -21.058 -48.964 -53.545  1.00 43.51  ? 343 PHE B CD1 1 
ATOM   6922  C CD2 . PHE B  1 343 ? -22.444 -47.577 -52.181  1.00 40.36  ? 343 PHE B CD2 1 
ATOM   6923  C CE1 . PHE B  1 343 ? -20.350 -49.365 -52.428  1.00 44.30  ? 343 PHE B CE1 1 
ATOM   6924  C CE2 . PHE B  1 343 ? -21.732 -47.969 -51.044  1.00 42.64  ? 343 PHE B CE2 1 
ATOM   6925  C CZ  . PHE B  1 343 ? -20.689 -48.864 -51.168  1.00 43.49  ? 343 PHE B CZ  1 
ATOM   6926  N N   . GLN B  1 344 ? -23.511 -44.864 -53.955  1.00 42.67  ? 344 GLN B N   1 
ATOM   6927  C CA  . GLN B  1 344 ? -23.619 -43.682 -53.115  1.00 40.39  ? 344 GLN B CA  1 
ATOM   6928  C C   . GLN B  1 344 ? -23.476 -44.105 -51.659  1.00 37.87  ? 344 GLN B C   1 
ATOM   6929  O O   . GLN B  1 344 ? -24.409 -44.690 -51.095  1.00 40.34  ? 344 GLN B O   1 
ATOM   6930  C CB  . GLN B  1 344 ? -24.949 -42.966 -53.353  1.00 37.07  ? 344 GLN B CB  1 
ATOM   6931  C CG  . GLN B  1 344 ? -25.093 -42.482 -54.832  1.00 38.65  ? 344 GLN B CG  1 
ATOM   6932  C CD  . GLN B  1 344 ? -26.231 -41.511 -55.029  1.00 39.98  ? 344 GLN B CD  1 
ATOM   6933  O OE1 . GLN B  1 344 ? -26.033 -40.380 -55.480  1.00 40.86  ? 344 GLN B OE1 1 
ATOM   6934  N NE2 . GLN B  1 344 ? -27.440 -41.952 -54.713  1.00 39.92  ? 344 GLN B NE2 1 
ATOM   6935  N N   . PRO B  1 345 ? -22.336 -43.865 -51.024  1.00 34.48  ? 345 PRO B N   1 
ATOM   6936  C CA  . PRO B  1 345 ? -22.166 -44.295 -49.629  1.00 37.30  ? 345 PRO B CA  1 
ATOM   6937  C C   . PRO B  1 345 ? -22.953 -43.413 -48.674  1.00 40.24  ? 345 PRO B C   1 
ATOM   6938  O O   . PRO B  1 345 ? -23.144 -42.218 -48.909  1.00 36.15  ? 345 PRO B O   1 
ATOM   6939  C CB  . PRO B  1 345 ? -20.661 -44.135 -49.400  1.00 37.10  ? 345 PRO B CB  1 
ATOM   6940  C CG  . PRO B  1 345 ? -20.296 -42.966 -50.266  1.00 37.63  ? 345 PRO B CG  1 
ATOM   6941  C CD  . PRO B  1 345 ? -21.201 -43.048 -51.492  1.00 35.67  ? 345 PRO B CD  1 
ATOM   6942  N N   . VAL B  1 346 ? -23.400 -44.005 -47.567  1.00 40.32  ? 346 VAL B N   1 
ATOM   6943  C CA  . VAL B  1 346 ? -24.024 -43.246 -46.488  1.00 39.88  ? 346 VAL B CA  1 
ATOM   6944  C C   . VAL B  1 346 ? -23.055 -43.226 -45.305  1.00 37.41  ? 346 VAL B C   1 
ATOM   6945  O O   . VAL B  1 346 ? -22.616 -44.280 -44.825  1.00 30.03  ? 346 VAL B O   1 
ATOM   6946  C CB  . VAL B  1 346 ? -25.394 -43.822 -46.100  1.00 43.59  ? 346 VAL B CB  1 
ATOM   6947  C CG1 . VAL B  1 346 ? -25.301 -45.313 -45.844  1.00 46.20  ? 346 VAL B CG1 1 
ATOM   6948  C CG2 . VAL B  1 346 ? -25.947 -43.087 -44.870  1.00 38.90  ? 346 VAL B CG2 1 
ATOM   6949  N N   . VAL B  1 347 ? -22.693 -42.032 -44.860  1.00 29.29  ? 347 VAL B N   1 
ATOM   6950  C CA  . VAL B  1 347 ? -21.624 -41.865 -43.883  1.00 32.51  ? 347 VAL B CA  1 
ATOM   6951  C C   . VAL B  1 347 ? -22.243 -41.297 -42.603  1.00 29.63  ? 347 VAL B C   1 
ATOM   6952  O O   . VAL B  1 347 ? -22.577 -40.107 -42.516  1.00 27.62  ? 347 VAL B O   1 
ATOM   6953  C CB  . VAL B  1 347 ? -20.504 -40.977 -44.437  1.00 33.63  ? 347 VAL B CB  1 
ATOM   6954  C CG1 . VAL B  1 347 ? -19.346 -40.927 -43.471  1.00 35.27  ? 347 VAL B CG1 1 
ATOM   6955  C CG2 . VAL B  1 347 ? -20.045 -41.500 -45.808  1.00 29.68  ? 347 VAL B CG2 1 
ATOM   6956  N N   . PHE B  1 348 ? -22.419 -42.154 -41.606  1.00 34.21  ? 348 PHE B N   1 
ATOM   6957  C CA  . PHE B  1 348 ? -22.988 -41.760 -40.319  1.00 31.78  ? 348 PHE B CA  1 
ATOM   6958  C C   . PHE B  1 348 ? -21.875 -41.255 -39.414  1.00 26.59  ? 348 PHE B C   1 
ATOM   6959  O O   . PHE B  1 348 ? -20.930 -41.988 -39.119  1.00 28.98  ? 348 PHE B O   1 
ATOM   6960  C CB  . PHE B  1 348 ? -23.697 -42.933 -39.645  1.00 32.75  ? 348 PHE B CB  1 
ATOM   6961  C CG  . PHE B  1 348 ? -25.179 -42.964 -39.867  1.00 33.46  ? 348 PHE B CG  1 
ATOM   6962  C CD1 . PHE B  1 348 ? -25.697 -43.201 -41.134  1.00 28.23  ? 348 PHE B CD1 1 
ATOM   6963  C CD2 . PHE B  1 348 ? -26.053 -42.795 -38.806  1.00 33.49  ? 348 PHE B CD2 1 
ATOM   6964  C CE1 . PHE B  1 348 ? -27.060 -43.250 -41.344  1.00 30.46  ? 348 PHE B CE1 1 
ATOM   6965  C CE2 . PHE B  1 348 ? -27.414 -42.844 -38.996  1.00 33.85  ? 348 PHE B CE2 1 
ATOM   6966  C CZ  . PHE B  1 348 ? -27.925 -43.070 -40.289  1.00 34.07  ? 348 PHE B CZ  1 
ATOM   6967  N N   . VAL B  1 349 ? -21.965 -39.999 -39.021  1.00 28.21  ? 349 VAL B N   1 
ATOM   6968  C CA  . VAL B  1 349 ? -21.059 -39.400 -38.059  1.00 29.89  ? 349 VAL B CA  1 
ATOM   6969  C C   . VAL B  1 349 ? -21.867 -39.248 -36.775  1.00 27.69  ? 349 VAL B C   1 
ATOM   6970  O O   . VAL B  1 349 ? -22.792 -38.420 -36.709  1.00 29.63  ? 349 VAL B O   1 
ATOM   6971  C CB  . VAL B  1 349 ? -20.505 -38.053 -38.552  1.00 28.46  ? 349 VAL B CB  1 
ATOM   6972  C CG1 . VAL B  1 349 ? -19.575 -37.448 -37.504  1.00 30.35  ? 349 VAL B CG1 1 
ATOM   6973  C CG2 . VAL B  1 349 ? -19.792 -38.213 -39.917  1.00 28.58  ? 349 VAL B CG2 1 
ATOM   6974  N N   . VAL B  1 350 ? -21.525 -40.042 -35.762  1.00 24.64  ? 350 VAL B N   1 
ATOM   6975  C CA  . VAL B  1 350 ? -22.316 -40.160 -34.536  1.00 25.32  ? 350 VAL B CA  1 
ATOM   6976  C C   . VAL B  1 350 ? -21.406 -40.078 -33.307  1.00 26.17  ? 350 VAL B C   1 
ATOM   6977  O O   . VAL B  1 350 ? -20.467 -40.871 -33.161  1.00 24.97  ? 350 VAL B O   1 
ATOM   6978  C CB  . VAL B  1 350 ? -23.122 -41.473 -34.506  1.00 24.96  ? 350 VAL B CB  1 
ATOM   6979  C CG1 . VAL B  1 350 ? -24.049 -41.503 -33.290  1.00 25.08  ? 350 VAL B CG1 1 
ATOM   6980  C CG2 . VAL B  1 350 ? -23.907 -41.649 -35.799  1.00 25.53  ? 350 VAL B CG2 1 
ATOM   6981  N N   . LEU B  1 351 ? -21.724 -39.157 -32.400  1.00 25.41  ? 351 LEU B N   1 
ATOM   6982  C CA  . LEU B  1 351 ? -20.925 -38.928 -31.206  1.00 28.64  ? 351 LEU B CA  1 
ATOM   6983  C C   . LEU B  1 351 ? -21.743 -38.060 -30.269  1.00 30.54  ? 351 LEU B C   1 
ATOM   6984  O O   . LEU B  1 351 ? -22.753 -37.470 -30.663  1.00 27.57  ? 351 LEU B O   1 
ATOM   6985  C CB  . LEU B  1 351 ? -19.588 -38.253 -31.546  1.00 26.14  ? 351 LEU B CB  1 
ATOM   6986  C CG  . LEU B  1 351 ? -19.624 -36.858 -32.188  1.00 23.51  ? 351 LEU B CG  1 
ATOM   6987  C CD1 . LEU B  1 351 ? -18.404 -36.062 -31.776  1.00 27.63  ? 351 LEU B CD1 1 
ATOM   6988  C CD2 . LEU B  1 351 ? -19.722 -36.912 -33.741  1.00 24.09  ? 351 LEU B CD2 1 
ATOM   6989  N N   . ASN B  1 352 ? -21.319 -37.934 -29.016  1.00 27.64  ? 352 ASN B N   1 
ATOM   6990  C CA  . ASN B  1 352 ? -21.927 -36.973 -28.135  1.00 24.36  ? 352 ASN B CA  1 
ATOM   6991  C C   . ASN B  1 352 ? -21.709 -35.607 -28.750  1.00 26.71  ? 352 ASN B C   1 
ATOM   6992  O O   . ASN B  1 352 ? -20.712 -35.359 -29.334  1.00 27.70  ? 352 ASN B O   1 
ATOM   6993  C CB  . ASN B  1 352 ? -21.298 -37.029 -26.775  1.00 29.62  ? 352 ASN B CB  1 
ATOM   6994  C CG  . ASN B  1 352 ? -21.911 -38.055 -25.889  1.00 31.69  ? 352 ASN B CG  1 
ATOM   6995  O OD1 . ASN B  1 352 ? -21.499 -39.189 -25.880  1.00 33.95  ? 352 ASN B OD1 1 
ATOM   6996  N ND2 . ASN B  1 352 ? -22.896 -37.646 -25.122  1.00 31.80  ? 352 ASN B ND2 1 
ATOM   6997  N N   . GLY B  1 353 ? -22.668 -34.735 -28.596  1.00 26.80  ? 353 GLY B N   1 
ATOM   6998  C CA  . GLY B  1 353 ? -22.503 -33.407 -29.148  1.00 30.61  ? 353 GLY B CA  1 
ATOM   6999  C C   . GLY B  1 353 ? -22.442 -32.271 -28.160  1.00 26.78  ? 353 GLY B C   1 
ATOM   7000  O O   . GLY B  1 353 ? -22.718 -31.126 -28.521  1.00 27.07  ? 353 GLY B O   1 
ATOM   7001  N N   . GLU B  1 354 ? -22.074 -32.552 -26.907  1.00 24.67  ? 354 GLU B N   1 
ATOM   7002  C CA  . GLU B  1 354 ? -21.959 -31.489 -25.918  1.00 30.88  ? 354 GLU B CA  1 
ATOM   7003  C C   . GLU B  1 354 ? -20.632 -31.519 -25.173  1.00 30.21  ? 354 GLU B C   1 
ATOM   7004  O O   . GLU B  1 354 ? -20.303 -30.545 -24.483  1.00 28.38  ? 354 GLU B O   1 
ATOM   7005  C CB  . GLU B  1 354 ? -23.122 -31.563 -24.911  1.00 32.44  ? 354 GLU B CB  1 
ATOM   7006  C CG  . GLU B  1 354 ? -22.962 -32.609 -23.795  1.00 24.93  ? 354 GLU B CG  1 
ATOM   7007  C CD  . GLU B  1 354 ? -23.507 -33.991 -24.181  1.00 24.90  ? 354 GLU B CD  1 
ATOM   7008  O OE1 . GLU B  1 354 ? -24.502 -34.456 -23.572  1.00 25.73  ? 354 GLU B OE1 1 
ATOM   7009  O OE2 . GLU B  1 354 ? -22.912 -34.638 -25.072  1.00 26.73  ? 354 GLU B OE2 1 
ATOM   7010  N N   . ASN B  1 355 ? -19.843 -32.574 -25.340  1.00 26.32  ? 355 ASN B N   1 
ATOM   7011  C CA  . ASN B  1 355 ? -18.668 -32.803 -24.523  1.00 25.50  ? 355 ASN B CA  1 
ATOM   7012  C C   . ASN B  1 355 ? -17.363 -32.386 -25.175  1.00 26.42  ? 355 ASN B C   1 
ATOM   7013  O O   . ASN B  1 355 ? -16.399 -32.097 -24.452  1.00 25.02  ? 355 ASN B O   1 
ATOM   7014  C CB  . ASN B  1 355 ? -18.597 -34.287 -24.141  1.00 27.18  ? 355 ASN B CB  1 
ATOM   7015  C CG  . ASN B  1 355 ? -19.677 -34.655 -23.168  1.00 27.45  ? 355 ASN B CG  1 
ATOM   7016  O OD1 . ASN B  1 355 ? -20.096 -33.816 -22.376  1.00 27.44  ? 355 ASN B OD1 1 
ATOM   7017  N ND2 . ASN B  1 355 ? -20.168 -35.887 -23.241  1.00 29.29  ? 355 ASN B ND2 1 
ATOM   7018  N N   . CYS B  1 356 ? -17.291 -32.348 -26.505  1.00 23.66  ? 356 CYS B N   1 
ATOM   7019  C CA  . CYS B  1 356 ? -16.002 -32.123 -27.140  1.00 23.74  ? 356 CYS B CA  1 
ATOM   7020  C C   . CYS B  1 356 ? -15.710 -30.654 -27.358  1.00 24.10  ? 356 CYS B C   1 
ATOM   7021  O O   . CYS B  1 356 ? -14.537 -30.279 -27.425  1.00 34.40  ? 356 CYS B O   1 
ATOM   7022  C CB  . CYS B  1 356 ? -15.922 -32.868 -28.478  1.00 28.78  ? 356 CYS B CB  1 
ATOM   7023  S SG  . CYS B  1 356 ? -17.222 -32.392 -29.665  1.00 25.83  ? 356 CYS B SG  1 
ATOM   7024  N N   . TRP B  1 357 ? -16.746 -29.812 -27.415  1.00 25.78  ? 357 TRP B N   1 
ATOM   7025  C CA  . TRP B  1 357 ? -16.567 -28.417 -27.816  1.00 26.84  ? 357 TRP B CA  1 
ATOM   7026  C C   . TRP B  1 357 ? -15.757 -27.619 -26.806  1.00 28.95  ? 357 TRP B C   1 
ATOM   7027  O O   . TRP B  1 357 ? -15.008 -26.724 -27.196  1.00 25.64  ? 357 TRP B O   1 
ATOM   7028  C CB  . TRP B  1 357 ? -17.932 -27.768 -28.045  1.00 26.16  ? 357 TRP B CB  1 
ATOM   7029  C CG  . TRP B  1 357 ? -18.775 -28.639 -28.883  1.00 27.74  ? 357 TRP B CG  1 
ATOM   7030  C CD1 . TRP B  1 357 ? -19.986 -29.186 -28.561  1.00 27.74  ? 357 TRP B CD1 1 
ATOM   7031  C CD2 . TRP B  1 357 ? -18.452 -29.110 -30.192  1.00 32.56  ? 357 TRP B CD2 1 
ATOM   7032  N NE1 . TRP B  1 357 ? -20.440 -29.965 -29.604  1.00 27.78  ? 357 TRP B NE1 1 
ATOM   7033  C CE2 . TRP B  1 357 ? -19.510 -29.938 -30.612  1.00 30.70  ? 357 TRP B CE2 1 
ATOM   7034  C CE3 . TRP B  1 357 ? -17.367 -28.906 -31.057  1.00 32.26  ? 357 TRP B CE3 1 
ATOM   7035  C CZ2 . TRP B  1 357 ? -19.514 -30.562 -31.859  1.00 30.53  ? 357 TRP B CZ2 1 
ATOM   7036  C CZ3 . TRP B  1 357 ? -17.373 -29.526 -32.285  1.00 30.14  ? 357 TRP B CZ3 1 
ATOM   7037  C CH2 . TRP B  1 357 ? -18.439 -30.341 -32.677  1.00 31.89  ? 357 TRP B CH2 1 
ATOM   7038  N N   . GLU B  1 358 ? -15.874 -27.933 -25.511  1.00 26.49  ? 358 GLU B N   1 
ATOM   7039  C CA  . GLU B  1 358 ? -15.168 -27.160 -24.488  1.00 25.52  ? 358 GLU B CA  1 
ATOM   7040  C C   . GLU B  1 358 ? -13.645 -27.241 -24.618  1.00 25.91  ? 358 GLU B C   1 
ATOM   7041  O O   . GLU B  1 358 ? -12.952 -26.365 -24.085  1.00 26.34  ? 358 GLU B O   1 
ATOM   7042  C CB  . GLU B  1 358 ? -15.582 -27.633 -23.097  1.00 25.48  ? 358 GLU B CB  1 
ATOM   7043  C CG  . GLU B  1 358 ? -15.448 -29.129 -22.928  1.00 32.36  ? 358 GLU B CG  1 
ATOM   7044  C CD  . GLU B  1 358 ? -16.195 -29.645 -21.724  1.00 28.17  ? 358 GLU B CD  1 
ATOM   7045  O OE1 . GLU B  1 358 ? -17.438 -29.562 -21.724  1.00 28.43  ? 358 GLU B OE1 1 
ATOM   7046  O OE2 . GLU B  1 358 ? -15.534 -30.147 -20.801  1.00 33.28  ? 358 GLU B OE2 1 
ATOM   7047  N N   . TYR B  1 359 ? -13.107 -28.270 -25.288  1.00 27.44  ? 359 TYR B N   1 
ATOM   7048  C CA  . TYR B  1 359 ? -11.680 -28.333 -25.592  1.00 29.92  ? 359 TYR B CA  1 
ATOM   7049  C C   . TYR B  1 359 ? -11.314 -27.615 -26.883  1.00 30.60  ? 359 TYR B C   1 
ATOM   7050  O O   . TYR B  1 359 ? -10.124 -27.412 -27.152  1.00 31.89  ? 359 TYR B O   1 
ATOM   7051  C CB  . TYR B  1 359 ? -11.196 -29.806 -25.641  1.00 33.01  ? 359 TYR B CB  1 
ATOM   7052  C CG  . TYR B  1 359 ? -11.461 -30.502 -24.316  1.00 29.88  ? 359 TYR B CG  1 
ATOM   7053  C CD1 . TYR B  1 359 ? -10.650 -30.267 -23.201  1.00 31.45  ? 359 TYR B CD1 1 
ATOM   7054  C CD2 . TYR B  1 359 ? -12.574 -31.323 -24.156  1.00 30.43  ? 359 TYR B CD2 1 
ATOM   7055  C CE1 . TYR B  1 359 ? -10.928 -30.867 -21.957  1.00 26.40  ? 359 TYR B CE1 1 
ATOM   7056  C CE2 . TYR B  1 359 ? -12.864 -31.924 -22.920  1.00 24.80  ? 359 TYR B CE2 1 
ATOM   7057  C CZ  . TYR B  1 359 ? -12.043 -31.692 -21.836  1.00 28.06  ? 359 TYR B CZ  1 
ATOM   7058  O OH  . TYR B  1 359 ? -12.364 -32.298 -20.641  1.00 30.51  ? 359 TYR B OH  1 
ATOM   7059  N N   . TYR B  1 360 ? -12.293 -27.226 -27.686  1.00 29.28  ? 360 TYR B N   1 
ATOM   7060  C CA  . TYR B  1 360 ? -12.001 -26.491 -28.901  1.00 33.40  ? 360 TYR B CA  1 
ATOM   7061  C C   . TYR B  1 360 ? -11.779 -25.016 -28.592  1.00 34.48  ? 360 TYR B C   1 
ATOM   7062  O O   . TYR B  1 360 ? -12.382 -24.456 -27.675  1.00 34.08  ? 360 TYR B O   1 
ATOM   7063  C CB  . TYR B  1 360 ? -13.154 -26.608 -29.889  1.00 31.98  ? 360 TYR B CB  1 
ATOM   7064  C CG  . TYR B  1 360 ? -13.229 -27.855 -30.739  1.00 31.99  ? 360 TYR B CG  1 
ATOM   7065  C CD1 . TYR B  1 360 ? -13.584 -29.084 -30.192  1.00 27.98  ? 360 TYR B CD1 1 
ATOM   7066  C CD2 . TYR B  1 360 ? -13.018 -27.780 -32.117  1.00 34.64  ? 360 TYR B CD2 1 
ATOM   7067  C CE1 . TYR B  1 360 ? -13.685 -30.215 -30.986  1.00 30.16  ? 360 TYR B CE1 1 
ATOM   7068  C CE2 . TYR B  1 360 ? -13.122 -28.899 -32.929  1.00 34.03  ? 360 TYR B CE2 1 
ATOM   7069  C CZ  . TYR B  1 360 ? -13.462 -30.106 -32.367  1.00 32.49  ? 360 TYR B CZ  1 
ATOM   7070  O OH  . TYR B  1 360 ? -13.559 -31.199 -33.183  1.00 31.42  ? 360 TYR B OH  1 
ATOM   7071  N N   . GLU B  1 361 ? -10.910 -24.388 -29.378  1.00 37.53  ? 361 GLU B N   1 
ATOM   7072  C CA  . GLU B  1 361 ? -10.831 -22.938 -29.399  1.00 40.74  ? 361 GLU B CA  1 
ATOM   7073  C C   . GLU B  1 361 ? -12.221 -22.350 -29.582  1.00 37.28  ? 361 GLU B C   1 
ATOM   7074  O O   . GLU B  1 361 ? -12.964 -22.749 -30.489  1.00 34.21  ? 361 GLU B O   1 
ATOM   7075  C CB  . GLU B  1 361 ? -9.906  -22.471 -30.531  1.00 49.01  ? 361 GLU B CB  1 
ATOM   7076  C CG  . GLU B  1 361 ? -9.183  -21.165 -30.216  1.00 56.54  ? 361 GLU B CG  1 
ATOM   7077  C CD  . GLU B  1 361 ? -8.463  -21.216 -28.870  1.00 63.36  ? 361 GLU B CD  1 
ATOM   7078  O OE1 . GLU B  1 361 ? -8.877  -20.500 -27.930  1.00 65.31  ? 361 GLU B OE1 1 
ATOM   7079  O OE2 . GLU B  1 361 ? -7.483  -21.981 -28.740  1.00 65.92  ? 361 GLU B OE2 1 
ATOM   7080  N N   . GLU B  1 362 ? -12.584 -21.432 -28.680  1.00 36.39  ? 362 GLU B N   1 
ATOM   7081  C CA  . GLU B  1 362 ? -13.830 -20.676 -28.788  1.00 35.02  ? 362 GLU B CA  1 
ATOM   7082  C C   . GLU B  1 362 ? -15.044 -21.599 -28.814  1.00 33.16  ? 362 GLU B C   1 
ATOM   7083  O O   . GLU B  1 362 ? -15.992 -21.382 -29.570  1.00 36.09  ? 362 GLU B O   1 
ATOM   7084  C CB  . GLU B  1 362 ? -13.812 -19.770 -30.022  1.00 39.33  ? 362 GLU B CB  1 
ATOM   7085  C CG  . GLU B  1 362 ? -13.425 -18.317 -29.733  1.00 54.11  ? 362 GLU B CG  1 
ATOM   7086  C CD  . GLU B  1 362 ? -13.305 -17.474 -30.997  1.00 66.94  ? 362 GLU B CD  1 
ATOM   7087  O OE1 . GLU B  1 362 ? -12.230 -16.873 -31.213  1.00 71.80  ? 362 GLU B OE1 1 
ATOM   7088  O OE2 . GLU B  1 362 ? -14.287 -17.406 -31.769  1.00 68.75  ? 362 GLU B OE2 1 
ATOM   7089  N N   . ASN B  1 363 ? -15.005 -22.658 -28.006  1.00 36.59  ? 363 ASN B N   1 
ATOM   7090  C CA  . ASN B  1 363 ? -16.135 -23.570 -27.837  1.00 33.93  ? 363 ASN B CA  1 
ATOM   7091  C C   . ASN B  1 363 ? -16.498 -24.282 -29.145  1.00 33.12  ? 363 ASN B C   1 
ATOM   7092  O O   . ASN B  1 363 ? -17.607 -24.805 -29.296  1.00 31.23  ? 363 ASN B O   1 
ATOM   7093  C CB  . ASN B  1 363 ? -17.341 -22.812 -27.267  1.00 26.55  ? 363 ASN B CB  1 
ATOM   7094  C CG  . ASN B  1 363 ? -18.408 -23.732 -26.687  1.00 22.83  ? 363 ASN B CG  1 
ATOM   7095  O OD1 . ASN B  1 363 ? -18.127 -24.848 -26.246  1.00 30.70  ? 363 ASN B OD1 1 
ATOM   7096  N ND2 . ASN B  1 363 ? -19.646 -23.260 -26.703  1.00 23.31  ? 363 ASN B ND2 1 
ATOM   7097  N N   . GLY B  1 364 ? -15.576 -24.315 -30.102  1.00 32.03  ? 364 GLY B N   1 
ATOM   7098  C CA  . GLY B  1 364 ? -15.806 -25.031 -31.336  1.00 32.64  ? 364 GLY B CA  1 
ATOM   7099  C C   . GLY B  1 364 ? -16.610 -24.280 -32.359  1.00 31.83  ? 364 GLY B C   1 
ATOM   7100  O O   . GLY B  1 364 ? -16.903 -24.833 -33.430  1.00 31.10  ? 364 GLY B O   1 
ATOM   7101  N N   . ILE B  1 365 ? -16.976 -23.035 -32.076  1.00 28.27  ? 365 ILE B N   1 
ATOM   7102  C CA  . ILE B  1 365 ? -17.809 -22.293 -33.004  1.00 29.12  ? 365 ILE B CA  1 
ATOM   7103  C C   . ILE B  1 365 ? -17.078 -22.037 -34.316  1.00 32.36  ? 365 ILE B C   1 
ATOM   7104  O O   . ILE B  1 365 ? -17.676 -22.263 -35.380  1.00 33.35  ? 365 ILE B O   1 
ATOM   7105  C CB  . ILE B  1 365 ? -18.337 -21.014 -32.333  1.00 30.49  ? 365 ILE B CB  1 
ATOM   7106  C CG1 . ILE B  1 365 ? -19.244 -21.396 -31.160  1.00 29.11  ? 365 ILE B CG1 1 
ATOM   7107  C CG2 . ILE B  1 365 ? -19.065 -20.154 -33.347  1.00 26.93  ? 365 ILE B CG2 1 
ATOM   7108  C CD1 . ILE B  1 365 ? -19.203 -20.438 -29.983  1.00 25.51  ? 365 ILE B CD1 1 
ATOM   7109  N N   . PRO B  1 366 ? -15.809 -21.595 -34.327  1.00 33.39  ? 366 PRO B N   1 
ATOM   7110  C CA  . PRO B  1 366 ? -15.122 -21.445 -35.617  1.00 34.04  ? 366 PRO B CA  1 
ATOM   7111  C C   . PRO B  1 366 ? -15.061 -22.741 -36.399  1.00 40.16  ? 366 PRO B C   1 
ATOM   7112  O O   . PRO B  1 366 ? -15.239 -22.719 -37.623  1.00 37.42  ? 366 PRO B O   1 
ATOM   7113  C CB  . PRO B  1 366 ? -13.724 -20.949 -35.216  1.00 30.70  ? 366 PRO B CB  1 
ATOM   7114  C CG  . PRO B  1 366 ? -13.926 -20.290 -33.913  1.00 33.87  ? 366 PRO B CG  1 
ATOM   7115  C CD  . PRO B  1 366 ? -14.969 -21.107 -33.217  1.00 30.92  ? 366 PRO B CD  1 
ATOM   7116  N N   . PHE B  1 367 ? -14.841 -23.877 -35.729  1.00 35.48  ? 367 PHE B N   1 
ATOM   7117  C CA  . PHE B  1 367 ? -14.812 -25.150 -36.438  1.00 34.67  ? 367 PHE B CA  1 
ATOM   7118  C C   . PHE B  1 367 ? -16.174 -25.481 -37.039  1.00 32.29  ? 367 PHE B C   1 
ATOM   7119  O O   . PHE B  1 367 ? -16.293 -25.711 -38.249  1.00 33.66  ? 367 PHE B O   1 
ATOM   7120  C CB  . PHE B  1 367 ? -14.365 -26.280 -35.514  1.00 32.77  ? 367 PHE B CB  1 
ATOM   7121  C CG  . PHE B  1 367 ? -14.561 -27.651 -36.115  1.00 31.11  ? 367 PHE B CG  1 
ATOM   7122  C CD1 . PHE B  1 367 ? -13.712 -28.113 -37.111  1.00 33.72  ? 367 PHE B CD1 1 
ATOM   7123  C CD2 . PHE B  1 367 ? -15.610 -28.457 -35.709  1.00 27.65  ? 367 PHE B CD2 1 
ATOM   7124  C CE1 . PHE B  1 367 ? -13.890 -29.364 -37.670  1.00 30.83  ? 367 PHE B CE1 1 
ATOM   7125  C CE2 . PHE B  1 367 ? -15.790 -29.717 -36.259  1.00 27.20  ? 367 PHE B CE2 1 
ATOM   7126  C CZ  . PHE B  1 367 ? -14.935 -30.164 -37.244  1.00 28.01  ? 367 PHE B CZ  1 
ATOM   7127  N N   . LEU B  1 368 ? -17.213 -25.547 -36.197  1.00 25.49  ? 368 LEU B N   1 
ATOM   7128  C CA  . LEU B  1 368 ? -18.539 -25.909 -36.699  1.00 29.03  ? 368 LEU B CA  1 
ATOM   7129  C C   . LEU B  1 368 ? -19.049 -24.916 -37.749  1.00 29.77  ? 368 LEU B C   1 
ATOM   7130  O O   . LEU B  1 368 ? -19.719 -25.307 -38.712  1.00 30.97  ? 368 LEU B O   1 
ATOM   7131  C CB  . LEU B  1 368 ? -19.530 -26.016 -35.538  1.00 27.17  ? 368 LEU B CB  1 
ATOM   7132  C CG  . LEU B  1 368 ? -19.493 -27.357 -34.788  1.00 28.52  ? 368 LEU B CG  1 
ATOM   7133  C CD1 . LEU B  1 368 ? -20.671 -27.472 -33.839  1.00 31.30  ? 368 LEU B CD1 1 
ATOM   7134  C CD2 . LEU B  1 368 ? -19.490 -28.505 -35.775  1.00 26.39  ? 368 LEU B CD2 1 
ATOM   7135  N N   . GLU B  1 369 ? -18.771 -23.629 -37.574  1.00 29.59  ? 369 GLU B N   1 
ATOM   7136  C CA  . GLU B  1 369 ? -19.264 -22.665 -38.543  1.00 33.22  ? 369 GLU B CA  1 
ATOM   7137  C C   . GLU B  1 369 ? -18.555 -22.837 -39.878  1.00 36.96  ? 369 GLU B C   1 
ATOM   7138  O O   . GLU B  1 369 ? -19.191 -22.770 -40.932  1.00 29.78  ? 369 GLU B O   1 
ATOM   7139  C CB  . GLU B  1 369 ? -19.106 -21.248 -38.011  1.00 35.46  ? 369 GLU B CB  1 
ATOM   7140  C CG  . GLU B  1 369 ? -20.208 -20.849 -37.076  1.00 38.33  ? 369 GLU B CG  1 
ATOM   7141  C CD  . GLU B  1 369 ? -20.033 -19.443 -36.580  1.00 40.24  ? 369 GLU B CD  1 
ATOM   7142  O OE1 . GLU B  1 369 ? -18.966 -18.860 -36.861  1.00 41.28  ? 369 GLU B OE1 1 
ATOM   7143  O OE2 . GLU B  1 369 ? -20.949 -18.923 -35.903  1.00 40.47  ? 369 GLU B OE2 1 
ATOM   7144  N N   . LYS B  1 370 ? -17.248 -23.106 -39.847  1.00 35.76  ? 370 LYS B N   1 
ATOM   7145  C CA  . LYS B  1 370 ? -16.522 -23.379 -41.080  1.00 40.96  ? 370 LYS B CA  1 
ATOM   7146  C C   . LYS B  1 370 ? -16.935 -24.718 -41.682  1.00 38.11  ? 370 LYS B C   1 
ATOM   7147  O O   . LYS B  1 370 ? -17.037 -24.843 -42.909  1.00 36.28  ? 370 LYS B O   1 
ATOM   7148  C CB  . LYS B  1 370 ? -15.017 -23.337 -40.823  1.00 45.98  ? 370 LYS B CB  1 
ATOM   7149  C CG  . LYS B  1 370 ? -14.505 -21.951 -40.459  1.00 54.97  ? 370 LYS B CG  1 
ATOM   7150  C CD  . LYS B  1 370 ? -13.072 -21.720 -40.928  1.00 62.47  ? 370 LYS B CD  1 
ATOM   7151  C CE  . LYS B  1 370 ? -12.997 -21.368 -42.417  1.00 67.34  ? 370 LYS B CE  1 
ATOM   7152  N NZ  . LYS B  1 370 ? -13.402 -22.488 -43.320  1.00 70.79  ? 370 LYS B NZ  1 
ATOM   7153  N N   . LEU B  1 371 ? -17.186 -25.725 -40.834  1.00 34.49  ? 371 LEU B N   1 
ATOM   7154  C CA  . LEU B  1 371 ? -17.604 -27.040 -41.317  1.00 33.30  ? 371 LEU B CA  1 
ATOM   7155  C C   . LEU B  1 371 ? -18.970 -26.965 -41.988  1.00 37.05  ? 371 LEU B C   1 
ATOM   7156  O O   . LEU B  1 371 ? -19.147 -27.427 -43.125  1.00 41.69  ? 371 LEU B O   1 
ATOM   7157  C CB  . LEU B  1 371 ? -17.632 -28.049 -40.159  1.00 32.76  ? 371 LEU B CB  1 
ATOM   7158  C CG  . LEU B  1 371 ? -18.130 -29.475 -40.443  1.00 31.02  ? 371 LEU B CG  1 
ATOM   7159  C CD1 . LEU B  1 371 ? -17.225 -30.172 -41.448  1.00 30.19  ? 371 LEU B CD1 1 
ATOM   7160  C CD2 . LEU B  1 371 ? -18.236 -30.311 -39.152  1.00 29.19  ? 371 LEU B CD2 1 
ATOM   7161  N N   . TYR B  1 372 ? -19.946 -26.367 -41.302  1.00 31.27  ? 372 TYR B N   1 
ATOM   7162  C CA  . TYR B  1 372 ? -21.302 -26.323 -41.831  1.00 28.32  ? 372 TYR B CA  1 
ATOM   7163  C C   . TYR B  1 372 ? -21.387 -25.441 -43.070  1.00 30.01  ? 372 TYR B C   1 
ATOM   7164  O O   . TYR B  1 372 ? -22.089 -25.777 -44.029  1.00 33.45  ? 372 TYR B O   1 
ATOM   7165  C CB  . TYR B  1 372 ? -22.256 -25.826 -40.760  1.00 31.81  ? 372 TYR B CB  1 
ATOM   7166  C CG  . TYR B  1 372 ? -22.463 -26.793 -39.619  1.00 29.77  ? 372 TYR B CG  1 
ATOM   7167  C CD1 . TYR B  1 372 ? -22.087 -28.143 -39.718  1.00 26.47  ? 372 TYR B CD1 1 
ATOM   7168  C CD2 . TYR B  1 372 ? -23.060 -26.363 -38.446  1.00 31.87  ? 372 TYR B CD2 1 
ATOM   7169  C CE1 . TYR B  1 372 ? -22.315 -29.037 -38.629  1.00 28.14  ? 372 TYR B CE1 1 
ATOM   7170  C CE2 . TYR B  1 372 ? -23.274 -27.221 -37.388  1.00 30.66  ? 372 TYR B CE2 1 
ATOM   7171  C CZ  . TYR B  1 372 ? -22.904 -28.552 -37.482  1.00 29.74  ? 372 TYR B CZ  1 
ATOM   7172  O OH  . TYR B  1 372 ? -23.155 -29.369 -36.402  1.00 25.88  ? 372 TYR B OH  1 
ATOM   7173  N N   . SER B  1 373 ? -20.692 -24.300 -43.054  1.00 30.53  ? 373 SER B N   1 
ATOM   7174  C CA  . SER B  1 373 ? -20.649 -23.425 -44.222  1.00 32.24  ? 373 SER B CA  1 
ATOM   7175  C C   . SER B  1 373 ? -20.019 -24.127 -45.421  1.00 35.74  ? 373 SER B C   1 
ATOM   7176  O O   . SER B  1 373 ? -20.465 -23.953 -46.565  1.00 36.71  ? 373 SER B O   1 
ATOM   7177  C CB  . SER B  1 373 ? -19.878 -22.153 -43.877  1.00 32.82  ? 373 SER B CB  1 
ATOM   7178  O OG  . SER B  1 373 ? -19.764 -21.315 -45.002  1.00 49.31  ? 373 SER B OG  1 
ATOM   7179  N N   . THR B  1 374 ? -18.969 -24.913 -45.187  1.00 41.83  ? 374 THR B N   1 
ATOM   7180  C CA  . THR B  1 374 ? -18.343 -25.633 -46.287  1.00 42.36  ? 374 THR B CA  1 
ATOM   7181  C C   . THR B  1 374 ? -19.238 -26.763 -46.775  1.00 40.81  ? 374 THR B C   1 
ATOM   7182  O O   . THR B  1 374 ? -19.442 -26.917 -47.984  1.00 35.66  ? 374 THR B O   1 
ATOM   7183  C CB  . THR B  1 374 ? -16.970 -26.152 -45.858  1.00 42.58  ? 374 THR B CB  1 
ATOM   7184  O OG1 . THR B  1 374 ? -16.178 -25.047 -45.400  1.00 33.95  ? 374 THR B OG1 1 
ATOM   7185  C CG2 . THR B  1 374 ? -16.262 -26.819 -47.034  1.00 46.01  ? 374 THR B CG2 1 
ATOM   7186  N N   . LEU B  1 375 ? -19.809 -27.541 -45.847  1.00 31.98  ? 375 LEU B N   1 
ATOM   7187  C CA  . LEU B  1 375 ? -20.679 -28.647 -46.239  1.00 34.37  ? 375 LEU B CA  1 
ATOM   7188  C C   . LEU B  1 375 ? -21.868 -28.161 -47.061  1.00 39.62  ? 375 LEU B C   1 
ATOM   7189  O O   . LEU B  1 375 ? -22.273 -28.820 -48.027  1.00 42.08  ? 375 LEU B O   1 
ATOM   7190  C CB  . LEU B  1 375 ? -21.165 -29.404 -44.997  1.00 32.06  ? 375 LEU B CB  1 
ATOM   7191  C CG  . LEU B  1 375 ? -20.209 -30.434 -44.399  1.00 30.98  ? 375 LEU B CG  1 
ATOM   7192  C CD1 . LEU B  1 375 ? -20.721 -31.030 -43.047  1.00 27.87  ? 375 LEU B CD1 1 
ATOM   7193  C CD2 . LEU B  1 375 ? -19.943 -31.534 -45.399  1.00 32.50  ? 375 LEU B CD2 1 
ATOM   7194  N N   . GLU B  1 376 ? -22.441 -27.011 -46.699  1.00 40.84  ? 376 GLU B N   1 
ATOM   7195  C CA  . GLU B  1 376 ? -23.649 -26.547 -47.358  1.00 41.04  ? 376 GLU B CA  1 
ATOM   7196  C C   . GLU B  1 376 ? -23.384 -26.030 -48.763  1.00 44.88  ? 376 GLU B C   1 
ATOM   7197  O O   . GLU B  1 376 ? -24.338 -25.685 -49.461  1.00 49.38  ? 376 GLU B O   1 
ATOM   7198  C CB  . GLU B  1 376 ? -24.325 -25.460 -46.521  1.00 39.66  ? 376 GLU B CB  1 
ATOM   7199  C CG  . GLU B  1 376 ? -23.823 -24.042 -46.765  1.00 43.87  ? 376 GLU B CG  1 
ATOM   7200  C CD  . GLU B  1 376 ? -24.602 -23.018 -45.965  1.00 52.25  ? 376 GLU B CD  1 
ATOM   7201  O OE1 . GLU B  1 376 ? -24.077 -21.913 -45.704  1.00 54.17  ? 376 GLU B OE1 1 
ATOM   7202  O OE2 . GLU B  1 376 ? -25.747 -23.328 -45.580  1.00 56.08  ? 376 GLU B OE2 1 
ATOM   7203  N N   . LYS B  1 377 ? -22.126 -25.981 -49.194  1.00 45.80  ? 377 LYS B N   1 
ATOM   7204  C CA  . LYS B  1 377 ? -21.787 -25.545 -50.537  1.00 50.56  ? 377 LYS B CA  1 
ATOM   7205  C C   . LYS B  1 377 ? -21.139 -26.635 -51.382  1.00 50.39  ? 377 LYS B C   1 
ATOM   7206  O O   . LYS B  1 377 ? -20.858 -26.390 -52.557  1.00 54.12  ? 377 LYS B O   1 
ATOM   7207  C CB  . LYS B  1 377 ? -20.870 -24.315 -50.471  1.00 51.43  ? 377 LYS B CB  1 
ATOM   7208  C CG  . LYS B  1 377 ? -21.505 -23.117 -49.778  1.00 50.20  ? 377 LYS B CG  1 
ATOM   7209  C CD  . LYS B  1 377 ? -20.476 -22.050 -49.473  1.00 49.08  ? 377 LYS B CD  1 
ATOM   7210  C CE  . LYS B  1 377 ? -21.117 -20.800 -48.910  1.00 45.82  ? 377 LYS B CE  1 
ATOM   7211  N NZ  . LYS B  1 377 ? -21.247 -20.897 -47.432  1.00 45.09  ? 377 LYS B NZ  1 
ATOM   7212  N N   . GLU B  1 378 ? -20.897 -27.825 -50.832  1.00 49.22  ? 378 GLU B N   1 
ATOM   7213  C CA  . GLU B  1 378 ? -20.375 -28.929 -51.629  1.00 53.77  ? 378 GLU B CA  1 
ATOM   7214  C C   . GLU B  1 378 ? -21.528 -29.594 -52.373  1.00 54.89  ? 378 GLU B C   1 
ATOM   7215  O O   . GLU B  1 378 ? -22.430 -30.171 -51.754  1.00 55.89  ? 378 GLU B O   1 
ATOM   7216  C CB  . GLU B  1 378 ? -19.629 -29.942 -50.762  1.00 54.24  ? 378 GLU B CB  1 
ATOM   7217  C CG  . GLU B  1 378 ? -18.246 -29.486 -50.287  1.00 57.99  ? 378 GLU B CG  1 
ATOM   7218  C CD  . GLU B  1 378 ? -17.262 -29.272 -51.432  1.00 68.13  ? 378 GLU B CD  1 
ATOM   7219  O OE1 . GLU B  1 378 ? -17.049 -28.108 -51.841  1.00 71.10  ? 378 GLU B OE1 1 
ATOM   7220  O OE2 . GLU B  1 378 ? -16.697 -30.270 -51.929  1.00 70.99  ? 378 GLU B OE2 1 
ATOM   7221  N N   . GLU B  1 379 ? -21.492 -29.509 -53.704  1.00 48.14  ? 379 GLU B N   1 
ATOM   7222  C CA  . GLU B  1 379 ? -22.571 -30.045 -54.528  1.00 49.72  ? 379 GLU B CA  1 
ATOM   7223  C C   . GLU B  1 379 ? -22.698 -31.555 -54.385  1.00 49.89  ? 379 GLU B C   1 
ATOM   7224  O O   . GLU B  1 379 ? -23.812 -32.093 -54.410  1.00 50.82  ? 379 GLU B O   1 
ATOM   7225  C CB  . GLU B  1 379 ? -22.335 -29.664 -55.996  1.00 50.56  ? 379 GLU B CB  1 
ATOM   7226  N N   . TRP B  1 380 ? -21.579 -32.253 -54.220  1.00 50.10  ? 380 TRP B N   1 
ATOM   7227  C CA  . TRP B  1 380 ? -21.580 -33.708 -54.195  1.00 49.75  ? 380 TRP B CA  1 
ATOM   7228  C C   . TRP B  1 380 ? -21.835 -34.287 -52.805  1.00 41.68  ? 380 TRP B C   1 
ATOM   7229  O O   . TRP B  1 380 ? -21.903 -35.512 -52.668  1.00 43.66  ? 380 TRP B O   1 
ATOM   7230  C CB  . TRP B  1 380 ? -20.252 -34.230 -54.748  1.00 47.14  ? 380 TRP B CB  1 
ATOM   7231  C CG  . TRP B  1 380 ? -19.087 -33.654 -54.030  1.00 47.46  ? 380 TRP B CG  1 
ATOM   7232  C CD1 . TRP B  1 380 ? -18.494 -32.445 -54.258  1.00 47.80  ? 380 TRP B CD1 1 
ATOM   7233  C CD2 . TRP B  1 380 ? -18.386 -34.245 -52.924  1.00 50.12  ? 380 TRP B CD2 1 
ATOM   7234  N NE1 . TRP B  1 380 ? -17.457 -32.253 -53.374  1.00 51.88  ? 380 TRP B NE1 1 
ATOM   7235  C CE2 . TRP B  1 380 ? -17.369 -33.345 -52.545  1.00 50.46  ? 380 TRP B CE2 1 
ATOM   7236  C CE3 . TRP B  1 380 ? -18.512 -35.454 -52.230  1.00 49.80  ? 380 TRP B CE3 1 
ATOM   7237  C CZ2 . TRP B  1 380 ? -16.482 -33.617 -51.503  1.00 48.58  ? 380 TRP B CZ2 1 
ATOM   7238  C CZ3 . TRP B  1 380 ? -17.629 -35.724 -51.197  1.00 47.20  ? 380 TRP B CZ3 1 
ATOM   7239  C CH2 . TRP B  1 380 ? -16.632 -34.807 -50.838  1.00 48.70  ? 380 TRP B CH2 1 
ATOM   7240  N N   . ILE B  1 381 ? -21.978 -33.452 -51.779  1.00 37.07  ? 381 ILE B N   1 
ATOM   7241  C CA  . ILE B  1 381 ? -22.327 -33.911 -50.431  1.00 35.95  ? 381 ILE B CA  1 
ATOM   7242  C C   . ILE B  1 381 ? -23.774 -33.528 -50.176  1.00 38.92  ? 381 ILE B C   1 
ATOM   7243  O O   . ILE B  1 381 ? -24.143 -32.359 -50.323  1.00 42.71  ? 381 ILE B O   1 
ATOM   7244  C CB  . ILE B  1 381 ? -21.409 -33.314 -49.351  1.00 37.22  ? 381 ILE B CB  1 
ATOM   7245  C CG1 . ILE B  1 381 ? -19.945 -33.656 -49.634  1.00 41.92  ? 381 ILE B CG1 1 
ATOM   7246  C CG2 . ILE B  1 381 ? -21.797 -33.833 -47.947  1.00 32.22  ? 381 ILE B CG2 1 
ATOM   7247  C CD1 . ILE B  1 381 ? -18.999 -33.215 -48.536  1.00 39.90  ? 381 ILE B CD1 1 
ATOM   7248  N N   . GLU B  1 382 ? -24.601 -34.506 -49.822  1.00 34.42  ? 382 GLU B N   1 
ATOM   7249  C CA  . GLU B  1 382 ? -25.958 -34.247 -49.361  1.00 40.60  ? 382 GLU B CA  1 
ATOM   7250  C C   . GLU B  1 382 ? -26.084 -34.752 -47.931  1.00 32.43  ? 382 GLU B C   1 
ATOM   7251  O O   . GLU B  1 382 ? -25.990 -35.959 -47.693  1.00 32.38  ? 382 GLU B O   1 
ATOM   7252  C CB  . GLU B  1 382 ? -26.997 -34.928 -50.248  1.00 47.03  ? 382 GLU B CB  1 
ATOM   7253  C CG  . GLU B  1 382 ? -28.351 -34.226 -50.225  1.00 56.28  ? 382 GLU B CG  1 
ATOM   7254  C CD  . GLU B  1 382 ? -29.494 -35.081 -50.762  1.00 62.82  ? 382 GLU B CD  1 
ATOM   7255  O OE1 . GLU B  1 382 ? -29.258 -35.891 -51.693  1.00 62.46  ? 382 GLU B OE1 1 
ATOM   7256  O OE2 . GLU B  1 382 ? -30.632 -34.928 -50.256  1.00 63.81  ? 382 GLU B OE2 1 
ATOM   7257  N N   . THR B  1 383 ? -26.314 -33.844 -46.989  1.00 36.32  ? 383 THR B N   1 
ATOM   7258  C CA  . THR B  1 383 ? -26.597 -34.272 -45.618  1.00 30.16  ? 383 THR B CA  1 
ATOM   7259  C C   . THR B  1 383 ? -28.055 -34.699 -45.513  1.00 32.02  ? 383 THR B C   1 
ATOM   7260  O O   . THR B  1 383 ? -28.931 -34.132 -46.170  1.00 31.82  ? 383 THR B O   1 
ATOM   7261  C CB  . THR B  1 383 ? -26.299 -33.164 -44.612  1.00 33.17  ? 383 THR B CB  1 
ATOM   7262  O OG1 . THR B  1 383 ? -27.024 -31.971 -44.963  1.00 31.10  ? 383 THR B OG1 1 
ATOM   7263  C CG2 . THR B  1 383 ? -24.811 -32.877 -44.582  1.00 37.25  ? 383 THR B CG2 1 
ATOM   7264  N N   . LEU B  1 384 ? -28.316 -35.713 -44.699  1.00 31.47  ? 384 LEU B N   1 
ATOM   7265  C CA  . LEU B  1 384 ? -29.658 -36.271 -44.580  1.00 32.32  ? 384 LEU B CA  1 
ATOM   7266  C C   . LEU B  1 384 ? -30.170 -36.205 -43.144  1.00 29.28  ? 384 LEU B C   1 
ATOM   7267  O O   . LEU B  1 384 ? -29.402 -36.297 -42.183  1.00 28.15  ? 384 LEU B O   1 
ATOM   7268  C CB  . LEU B  1 384 ? -29.689 -37.729 -45.045  1.00 30.79  ? 384 LEU B CB  1 
ATOM   7269  C CG  . LEU B  1 384 ? -29.053 -38.019 -46.409  1.00 34.16  ? 384 LEU B CG  1 
ATOM   7270  C CD1 . LEU B  1 384 ? -29.171 -39.498 -46.745  1.00 32.39  ? 384 LEU B CD1 1 
ATOM   7271  C CD2 . LEU B  1 384 ? -29.719 -37.147 -47.485  1.00 33.15  ? 384 LEU B CD2 1 
ATOM   7272  N N   . THR B  1 385 ? -31.488 -36.069 -43.010  1.00 33.21  ? 385 THR B N   1 
ATOM   7273  C CA  . THR B  1 385 ? -32.112 -36.419 -41.745  1.00 36.00  ? 385 THR B CA  1 
ATOM   7274  C C   . THR B  1 385 ? -32.083 -37.936 -41.569  1.00 33.06  ? 385 THR B C   1 
ATOM   7275  O O   . THR B  1 385 ? -31.826 -38.692 -42.512  1.00 31.60  ? 385 THR B O   1 
ATOM   7276  C CB  . THR B  1 385 ? -33.553 -35.908 -41.669  1.00 38.39  ? 385 THR B CB  1 
ATOM   7277  O OG1 . THR B  1 385 ? -34.399 -36.707 -42.516  1.00 36.80  ? 385 THR B OG1 1 
ATOM   7278  C CG2 . THR B  1 385 ? -33.625 -34.436 -42.108  1.00 37.97  ? 385 THR B CG2 1 
ATOM   7279  N N   . LEU B  1 386 ? -32.318 -38.382 -40.331  1.00 29.64  ? 386 LEU B N   1 
ATOM   7280  C CA  . LEU B  1 386 ? -32.390 -39.818 -40.077  1.00 31.30  ? 386 LEU B CA  1 
ATOM   7281  C C   . LEU B  1 386 ? -33.487 -40.465 -40.909  1.00 31.82  ? 386 LEU B C   1 
ATOM   7282  O O   . LEU B  1 386 ? -33.336 -41.602 -41.371  1.00 31.02  ? 386 LEU B O   1 
ATOM   7283  C CB  . LEU B  1 386 ? -32.639 -40.089 -38.593  1.00 28.43  ? 386 LEU B CB  1 
ATOM   7284  C CG  . LEU B  1 386 ? -31.592 -39.607 -37.587  1.00 27.11  ? 386 LEU B CG  1 
ATOM   7285  C CD1 . LEU B  1 386 ? -32.053 -39.951 -36.150  1.00 26.91  ? 386 LEU B CD1 1 
ATOM   7286  C CD2 . LEU B  1 386 ? -30.233 -40.211 -37.873  1.00 26.60  ? 386 LEU B CD2 1 
ATOM   7287  N N   . GLU B  1 387 ? -34.611 -39.765 -41.087  1.00 31.29  ? 387 GLU B N   1 
ATOM   7288  C CA  . GLU B  1 387 ? -35.709 -40.326 -41.867  1.00 37.56  ? 387 GLU B CA  1 
ATOM   7289  C C   . GLU B  1 387 ? -35.321 -40.472 -43.335  1.00 34.49  ? 387 GLU B C   1 
ATOM   7290  O O   . GLU B  1 387 ? -35.706 -41.445 -43.989  1.00 34.78  ? 387 GLU B O   1 
ATOM   7291  C CB  . GLU B  1 387 ? -36.964 -39.461 -41.730  1.00 46.68  ? 387 GLU B CB  1 
ATOM   7292  C CG  . GLU B  1 387 ? -38.006 -39.719 -42.816  1.00 58.75  ? 387 GLU B CG  1 
ATOM   7293  C CD  . GLU B  1 387 ? -39.413 -39.879 -42.270  1.00 69.53  ? 387 GLU B CD  1 
ATOM   7294  O OE1 . GLU B  1 387 ? -40.073 -40.884 -42.615  1.00 74.02  ? 387 GLU B OE1 1 
ATOM   7295  O OE2 . GLU B  1 387 ? -39.867 -39.003 -41.505  1.00 73.02  ? 387 GLU B OE2 1 
ATOM   7296  N N   . GLU B  1 388 ? -34.569 -39.512 -43.874  1.00 34.20  ? 388 GLU B N   1 
ATOM   7297  C CA  . GLU B  1 388 ? -34.141 -39.629 -45.270  1.00 36.01  ? 388 GLU B CA  1 
ATOM   7298  C C   . GLU B  1 388 ? -33.126 -40.742 -45.442  1.00 36.38  ? 388 GLU B C   1 
ATOM   7299  O O   . GLU B  1 388 ? -33.112 -41.404 -46.487  1.00 40.01  ? 388 GLU B O   1 
ATOM   7300  C CB  . GLU B  1 388 ? -33.563 -38.305 -45.764  1.00 33.85  ? 388 GLU B CB  1 
ATOM   7301  C CG  . GLU B  1 388 ? -34.610 -37.218 -45.951  1.00 34.70  ? 388 GLU B CG  1 
ATOM   7302  C CD  . GLU B  1 388 ? -34.010 -35.829 -45.935  1.00 43.63  ? 388 GLU B CD  1 
ATOM   7303  O OE1 . GLU B  1 388 ? -32.788 -35.692 -45.674  1.00 38.36  ? 388 GLU B OE1 1 
ATOM   7304  O OE2 . GLU B  1 388 ? -34.770 -34.870 -46.180  1.00 45.91  ? 388 GLU B OE2 1 
ATOM   7305  N N   . ALA B  1 389 ? -32.275 -40.950 -44.431  1.00 33.13  ? 389 ALA B N   1 
ATOM   7306  C CA  . ALA B  1 389 ? -31.321 -42.047 -44.452  1.00 33.27  ? 389 ALA B CA  1 
ATOM   7307  C C   . ALA B  1 389 ? -32.034 -43.385 -44.367  1.00 33.47  ? 389 ALA B C   1 
ATOM   7308  O O   . ALA B  1 389 ? -31.640 -44.351 -45.027  1.00 38.77  ? 389 ALA B O   1 
ATOM   7309  C CB  . ALA B  1 389 ? -30.324 -41.899 -43.303  1.00 30.53  ? 389 ALA B CB  1 
ATOM   7310  N N   . MET B  1 390 ? -33.097 -43.452 -43.571  1.00 38.37  ? 390 MET B N   1 
ATOM   7311  C CA  . MET B  1 390 ? -33.877 -44.677 -43.466  1.00 47.02  ? 390 MET B CA  1 
ATOM   7312  C C   . MET B  1 390 ? -34.552 -45.017 -44.792  1.00 44.95  ? 390 MET B C   1 
ATOM   7313  O O   . MET B  1 390 ? -34.510 -46.164 -45.245  1.00 45.08  ? 390 MET B O   1 
ATOM   7314  C CB  . MET B  1 390 ? -34.913 -44.533 -42.353  1.00 55.86  ? 390 MET B CB  1 
ATOM   7315  C CG  . MET B  1 390 ? -35.936 -45.649 -42.299  1.00 67.75  ? 390 MET B CG  1 
ATOM   7316  S SD  . MET B  1 390 ? -35.278 -47.175 -41.615  1.00 75.21  ? 390 MET B SD  1 
ATOM   7317  C CE  . MET B  1 390 ? -34.826 -48.089 -43.090  1.00 78.09  ? 390 MET B CE  1 
ATOM   7318  N N   . ARG B  1 391 ? -35.162 -44.027 -45.439  1.00 42.95  ? 391 ARG B N   1 
ATOM   7319  C CA  . ARG B  1 391 ? -36.004 -44.262 -46.604  1.00 48.30  ? 391 ARG B CA  1 
ATOM   7320  C C   . ARG B  1 391 ? -35.264 -44.167 -47.935  1.00 51.59  ? 391 ARG B C   1 
ATOM   7321  O O   . ARG B  1 391 ? -35.864 -44.458 -48.974  1.00 50.31  ? 391 ARG B O   1 
ATOM   7322  C CB  . ARG B  1 391 ? -37.179 -43.275 -46.608  1.00 53.88  ? 391 ARG B CB  1 
ATOM   7323  C CG  . ARG B  1 391 ? -38.260 -43.583 -45.583  1.00 58.66  ? 391 ARG B CG  1 
ATOM   7324  C CD  . ARG B  1 391 ? -38.922 -42.305 -45.091  1.00 65.30  ? 391 ARG B CD  1 
ATOM   7325  N NE  . ARG B  1 391 ? -40.316 -42.182 -45.518  1.00 75.75  ? 391 ARG B NE  1 
ATOM   7326  C CZ  . ARG B  1 391 ? -40.999 -41.039 -45.539  1.00 82.36  ? 391 ARG B CZ  1 
ATOM   7327  N NH1 . ARG B  1 391 ? -40.422 -39.905 -45.161  1.00 81.99  ? 391 ARG B NH1 1 
ATOM   7328  N NH2 . ARG B  1 391 ? -42.263 -41.027 -45.945  1.00 86.68  ? 391 ARG B NH2 1 
ATOM   7329  N N   . LYS B  1 392 ? -33.985 -43.794 -47.935  1.00 49.59  ? 392 LYS B N   1 
ATOM   7330  C CA  . LYS B  1 392 ? -33.262 -43.546 -49.181  1.00 48.53  ? 392 LYS B CA  1 
ATOM   7331  C C   . LYS B  1 392 ? -33.221 -44.784 -50.079  1.00 47.46  ? 392 LYS B C   1 
ATOM   7332  O O   . LYS B  1 392 ? -32.847 -45.876 -49.646  1.00 47.22  ? 392 LYS B O   1 
ATOM   7333  C CB  . LYS B  1 392 ? -31.845 -43.075 -48.855  1.00 45.42  ? 392 LYS B CB  1 
ATOM   7334  C CG  . LYS B  1 392 ? -31.121 -42.446 -50.013  1.00 44.76  ? 392 LYS B CG  1 
ATOM   7335  C CD  . LYS B  1 392 ? -31.827 -41.194 -50.485  1.00 49.35  ? 392 LYS B CD  1 
ATOM   7336  C CE  . LYS B  1 392 ? -31.400 -39.968 -49.710  1.00 48.17  ? 392 LYS B CE  1 
ATOM   7337  N NZ  . LYS B  1 392 ? -31.749 -38.747 -50.493  1.00 53.69  ? 392 LYS B NZ  1 
ATOM   7338  N N   . GLU B  1 393 ? -33.597 -44.611 -51.346  1.00 52.28  ? 393 GLU B N   1 
ATOM   7339  C CA  . GLU B  1 393 ? -33.664 -45.755 -52.249  1.00 56.77  ? 393 GLU B CA  1 
ATOM   7340  C C   . GLU B  1 393 ? -32.332 -46.062 -52.937  1.00 55.05  ? 393 GLU B C   1 
ATOM   7341  O O   . GLU B  1 393 ? -31.955 -47.233 -53.048  1.00 56.69  ? 393 GLU B O   1 
ATOM   7342  C CB  . GLU B  1 393 ? -34.765 -45.530 -53.295  1.00 61.93  ? 393 GLU B CB  1 
ATOM   7343  C CG  . GLU B  1 393 ? -36.151 -45.320 -52.684  1.00 66.20  ? 393 GLU B CG  1 
ATOM   7344  C CD  . GLU B  1 393 ? -37.199 -46.288 -53.216  1.00 72.98  ? 393 GLU B CD  1 
ATOM   7345  O OE1 . GLU B  1 393 ? -37.896 -46.916 -52.388  1.00 77.11  ? 393 GLU B OE1 1 
ATOM   7346  O OE2 . GLU B  1 393 ? -37.332 -46.415 -54.455  1.00 72.92  ? 393 GLU B OE2 1 
ATOM   7347  N N   . ASP B  1 394 ? -31.602 -45.043 -53.387  1.00 54.55  ? 394 ASP B N   1 
ATOM   7348  C CA  . ASP B  1 394 ? -30.420 -45.238 -54.234  1.00 54.76  ? 394 ASP B CA  1 
ATOM   7349  C C   . ASP B  1 394 ? -29.157 -45.491 -53.411  1.00 52.94  ? 394 ASP B C   1 
ATOM   7350  O O   . ASP B  1 394 ? -28.114 -44.860 -53.588  1.00 51.73  ? 394 ASP B O   1 
ATOM   7351  C CB  . ASP B  1 394 ? -30.244 -44.041 -55.165  1.00 63.91  ? 394 ASP B CB  1 
ATOM   7352  C CG  . ASP B  1 394 ? -30.536 -42.711 -54.484  1.00 66.86  ? 394 ASP B CG  1 
ATOM   7353  O OD1 . ASP B  1 394 ? -31.329 -42.690 -53.516  1.00 69.73  ? 394 ASP B OD1 1 
ATOM   7354  O OD2 . ASP B  1 394 ? -29.982 -41.681 -54.933  1.00 65.30  ? 394 ASP B OD2 1 
ATOM   7355  N N   . VAL B  1 395 ? -29.257 -46.467 -52.514  1.00 46.05  ? 395 VAL B N   1 
ATOM   7356  C CA  . VAL B  1 395 ? -28.225 -46.782 -51.541  1.00 41.53  ? 395 VAL B CA  1 
ATOM   7357  C C   . VAL B  1 395 ? -28.012 -48.293 -51.591  1.00 42.89  ? 395 VAL B C   1 
ATOM   7358  O O   . VAL B  1 395 ? -28.870 -49.044 -52.060  1.00 42.51  ? 395 VAL B O   1 
ATOM   7359  C CB  . VAL B  1 395 ? -28.639 -46.302 -50.129  1.00 39.58  ? 395 VAL B CB  1 
ATOM   7360  C CG1 . VAL B  1 395 ? -29.545 -47.310 -49.474  1.00 38.30  ? 395 VAL B CG1 1 
ATOM   7361  C CG2 . VAL B  1 395 ? -27.452 -46.012 -49.291  1.00 42.26  ? 395 VAL B CG2 1 
ATOM   7362  N N   . LYS B  1 396 ? -26.844 -48.745 -51.145  1.00 41.98  ? 396 LYS B N   1 
ATOM   7363  C CA  . LYS B  1 396 ? -26.602 -50.182 -51.130  1.00 47.17  ? 396 LYS B CA  1 
ATOM   7364  C C   . LYS B  1 396 ? -26.971 -50.768 -49.774  1.00 45.00  ? 396 LYS B C   1 
ATOM   7365  O O   . LYS B  1 396 ? -26.802 -50.127 -48.730  1.00 47.13  ? 396 LYS B O   1 
ATOM   7366  C CB  . LYS B  1 396 ? -25.150 -50.513 -51.470  1.00 53.97  ? 396 LYS B CB  1 
ATOM   7367  C CG  . LYS B  1 396 ? -24.941 -51.993 -51.761  1.00 62.73  ? 396 LYS B CG  1 
ATOM   7368  C CD  . LYS B  1 396 ? -23.661 -52.248 -52.534  1.00 68.74  ? 396 LYS B CD  1 
ATOM   7369  C CE  . LYS B  1 396 ? -23.946 -52.853 -53.902  1.00 72.81  ? 396 LYS B CE  1 
ATOM   7370  N NZ  . LYS B  1 396 ? -24.301 -51.807 -54.897  1.00 73.58  ? 396 LYS B NZ  1 
ATOM   7371  N N   . THR B  1 397 ? -27.487 -51.998 -49.799  1.00 42.83  ? 397 THR B N   1 
ATOM   7372  C CA  . THR B  1 397 ? -28.019 -52.635 -48.600  1.00 42.59  ? 397 THR B CA  1 
ATOM   7373  C C   . THR B  1 397 ? -27.435 -54.031 -48.431  1.00 41.72  ? 397 THR B C   1 
ATOM   7374  O O   . THR B  1 397 ? -27.006 -54.672 -49.393  1.00 39.61  ? 397 THR B O   1 
ATOM   7375  C CB  . THR B  1 397 ? -29.550 -52.735 -48.648  1.00 42.95  ? 397 THR B CB  1 
ATOM   7376  O OG1 . THR B  1 397 ? -29.933 -53.498 -49.792  1.00 49.53  ? 397 THR B OG1 1 
ATOM   7377  C CG2 . THR B  1 397 ? -30.167 -51.354 -48.758  1.00 42.62  ? 397 THR B CG2 1 
ATOM   7378  N N   . GLU B  1 398 ? -27.457 -54.507 -47.189  1.00 39.27  ? 398 GLU B N   1 
ATOM   7379  C CA  . GLU B  1 398 ? -26.980 -55.833 -46.844  1.00 44.25  ? 398 GLU B CA  1 
ATOM   7380  C C   . GLU B  1 398 ? -27.815 -56.349 -45.683  1.00 45.40  ? 398 GLU B C   1 
ATOM   7381  O O   . GLU B  1 398 ? -28.291 -55.571 -44.850  1.00 44.45  ? 398 GLU B O   1 
ATOM   7382  C CB  . GLU B  1 398 ? -25.491 -55.798 -46.471  1.00 51.99  ? 398 GLU B CB  1 
ATOM   7383  C CG  . GLU B  1 398 ? -24.860 -57.151 -46.234  1.00 60.32  ? 398 GLU B CG  1 
ATOM   7384  C CD  . GLU B  1 398 ? -24.962 -58.039 -47.441  1.00 74.21  ? 398 GLU B CD  1 
ATOM   7385  O OE1 . GLU B  1 398 ? -24.449 -57.638 -48.510  1.00 78.38  ? 398 GLU B OE1 1 
ATOM   7386  O OE2 . GLU B  1 398 ? -25.564 -59.129 -47.323  1.00 79.36  ? 398 GLU B OE2 1 
ATOM   7387  N N   . VAL B  1 399 ? -27.992 -57.661 -45.630  1.00 40.95  ? 399 VAL B N   1 
ATOM   7388  C CA  . VAL B  1 399 ? -28.702 -58.296 -44.527  1.00 44.22  ? 399 VAL B CA  1 
ATOM   7389  C C   . VAL B  1 399 ? -27.688 -58.814 -43.518  1.00 43.23  ? 399 VAL B C   1 
ATOM   7390  O O   . VAL B  1 399 ? -26.625 -59.330 -43.894  1.00 47.49  ? 399 VAL B O   1 
ATOM   7391  C CB  . VAL B  1 399 ? -29.613 -59.423 -45.044  1.00 49.10  ? 399 VAL B CB  1 
ATOM   7392  C CG1 . VAL B  1 399 ? -30.305 -60.156 -43.871  1.00 45.45  ? 399 VAL B CG1 1 
ATOM   7393  C CG2 . VAL B  1 399 ? -30.626 -58.843 -46.018  1.00 49.16  ? 399 VAL B CG2 1 
ATOM   7394  N N   . ILE B  1 400 ? -28.016 -58.672 -42.237  1.00 38.11  ? 400 ILE B N   1 
ATOM   7395  C CA  . ILE B  1 400 ? -27.219 -59.174 -41.120  1.00 44.98  ? 400 ILE B CA  1 
ATOM   7396  C C   . ILE B  1 400 ? -28.102 -60.098 -40.293  1.00 44.52  ? 400 ILE B C   1 
ATOM   7397  O O   . ILE B  1 400 ? -29.242 -59.743 -39.975  1.00 45.83  ? 400 ILE B O   1 
ATOM   7398  C CB  . ILE B  1 400 ? -26.688 -58.023 -40.242  1.00 43.30  ? 400 ILE B CB  1 
ATOM   7399  C CG1 . ILE B  1 400 ? -25.480 -57.357 -40.892  1.00 46.56  ? 400 ILE B CG1 1 
ATOM   7400  C CG2 . ILE B  1 400 ? -26.309 -58.519 -38.849  1.00 47.78  ? 400 ILE B CG2 1 
ATOM   7401  C CD1 . ILE B  1 400 ? -24.797 -56.341 -39.983  1.00 48.45  ? 400 ILE B CD1 1 
ATOM   7402  N N   . GLU B  1 401 ? -27.589 -61.280 -39.942  1.00 41.80  ? 401 GLU B N   1 
ATOM   7403  C CA  . GLU B  1 401 ? -28.376 -62.198 -39.129  1.00 39.44  ? 401 GLU B CA  1 
ATOM   7404  C C   . GLU B  1 401 ? -27.887 -62.333 -37.697  1.00 35.39  ? 401 GLU B C   1 
ATOM   7405  O O   . GLU B  1 401 ? -28.599 -62.928 -36.884  1.00 36.93  ? 401 GLU B O   1 
ATOM   7406  C CB  . GLU B  1 401 ? -28.443 -63.588 -39.772  1.00 40.04  ? 401 GLU B CB  1 
ATOM   7407  C CG  . GLU B  1 401 ? -28.852 -63.561 -41.260  1.00 47.19  ? 401 GLU B CG  1 
ATOM   7408  C CD  . GLU B  1 401 ? -30.328 -63.871 -41.483  1.00 53.09  ? 401 GLU B CD  1 
ATOM   7409  O OE1 . GLU B  1 401 ? -31.183 -63.153 -40.920  1.00 54.71  ? 401 GLU B OE1 1 
ATOM   7410  O OE2 . GLU B  1 401 ? -30.641 -64.812 -42.243  1.00 58.77  ? 401 GLU B OE2 1 
ATOM   7411  N N   . SER B  1 402 ? -26.731 -61.764 -37.354  1.00 33.18  ? 402 SER B N   1 
ATOM   7412  C CA  . SER B  1 402 ? -26.176 -61.885 -36.005  1.00 33.56  ? 402 SER B CA  1 
ATOM   7413  C C   . SER B  1 402 ? -25.173 -60.762 -35.765  1.00 31.45  ? 402 SER B C   1 
ATOM   7414  O O   . SER B  1 402 ? -24.447 -60.378 -36.686  1.00 30.79  ? 402 SER B O   1 
ATOM   7415  C CB  . SER B  1 402 ? -25.493 -63.251 -35.803  1.00 34.59  ? 402 SER B CB  1 
ATOM   7416  O OG  . SER B  1 402 ? -25.074 -63.396 -34.449  1.00 42.24  ? 402 SER B OG  1 
ATOM   7417  N N   . VAL B  1 403 ? -25.150 -60.308 -34.517  1.00 31.15  ? 403 VAL B N   1 
ATOM   7418  C CA  . VAL B  1 403 ? -24.190 -59.338 -34.077  1.00 30.52  ? 403 VAL B CA  1 
ATOM   7419  C C   . VAL B  1 403 ? -23.499 -59.781 -32.780  1.00 30.98  ? 403 VAL B C   1 
ATOM   7420  O O   . VAL B  1 403 ? -24.089 -60.379 -31.971  1.00 35.30  ? 403 VAL B O   1 
ATOM   7421  C CB  . VAL B  1 403 ? -24.839 -57.942 -33.831  1.00 29.62  ? 403 VAL B CB  1 
ATOM   7422  C CG1 . VAL B  1 403 ? -25.572 -57.476 -35.063  1.00 31.83  ? 403 VAL B CG1 1 
ATOM   7423  C CG2 . VAL B  1 403 ? -25.712 -57.942 -32.602  1.00 25.99  ? 403 VAL B CG2 1 
ATOM   7424  N N   . LYS B  1 404 ? -22.274 -59.406 -32.633  1.00 29.55  ? 404 LYS B N   1 
ATOM   7425  C CA  . LYS B  1 404 ? -21.517 -59.731 -31.426  1.00 31.54  ? 404 LYS B CA  1 
ATOM   7426  C C   . LYS B  1 404 ? -21.641 -58.615 -30.411  1.00 30.14  ? 404 LYS B C   1 
ATOM   7427  O O   . LYS B  1 404 ? -21.223 -57.536 -30.616  1.00 34.19  ? 404 LYS B O   1 
ATOM   7428  C CB  . LYS B  1 404 ? -20.092 -59.978 -31.706  1.00 35.99  ? 404 LYS B CB  1 
ATOM   7429  C CG  . LYS B  1 404 ? -19.390 -60.933 -30.778  1.00 47.85  ? 404 LYS B CG  1 
ATOM   7430  C CD  . LYS B  1 404 ? -19.171 -62.280 -31.425  1.00 55.86  ? 404 LYS B CD  1 
ATOM   7431  C CE  . LYS B  1 404 ? -18.130 -62.200 -32.523  1.00 59.09  ? 404 LYS B CE  1 
ATOM   7432  N NZ  . LYS B  1 404 ? -16.865 -62.910 -32.225  1.00 59.73  ? 404 LYS B NZ  1 
ATOM   7433  N N   . ALA B  1 405 ? -22.279 -58.919 -29.335  1.00 27.02  ? 405 ALA B N   1 
ATOM   7434  C CA  . ALA B  1 405 ? -22.512 -57.877 -28.377  1.00 31.86  ? 405 ALA B CA  1 
ATOM   7435  C C   . ALA B  1 405 ? -21.363 -57.047 -27.933  1.00 28.11  ? 405 ALA B C   1 
ATOM   7436  O O   . ALA B  1 405 ? -20.300 -57.477 -27.788  1.00 32.70  ? 405 ALA B O   1 
ATOM   7437  C CB  . ALA B  1 405 ? -23.236 -58.434 -27.181  1.00 31.37  ? 405 ALA B CB  1 
ATOM   7438  N N   . GLY B  1 406 ? -21.647 -55.786 -27.834  1.00 27.34  ? 406 GLY B N   1 
ATOM   7439  C CA  . GLY B  1 406 ? -20.681 -54.859 -27.368  1.00 24.82  ? 406 GLY B CA  1 
ATOM   7440  C C   . GLY B  1 406 ? -21.051 -53.414 -27.295  1.00 24.65  ? 406 GLY B C   1 
ATOM   7441  O O   . GLY B  1 406 ? -22.188 -53.121 -27.302  1.00 27.38  ? 406 GLY B O   1 
ATOM   7442  N N   . THR B  1 407 ? -20.064 -52.559 -27.228  1.00 22.70  ? 407 THR B N   1 
ATOM   7443  C CA  . THR B  1 407 ? -20.232 -51.173 -27.137  1.00 22.68  ? 407 THR B CA  1 
ATOM   7444  C C   . THR B  1 407 ? -19.270 -50.468 -28.028  1.00 25.95  ? 407 THR B C   1 
ATOM   7445  O O   . THR B  1 407 ? -18.430 -51.068 -28.564  1.00 27.21  ? 407 THR B O   1 
ATOM   7446  C CB  . THR B  1 407 ? -19.952 -50.647 -25.676  1.00 24.29  ? 407 THR B CB  1 
ATOM   7447  O OG1 . THR B  1 407 ? -18.563 -50.605 -25.391  1.00 22.15  ? 407 THR B OG1 1 
ATOM   7448  C CG2 . THR B  1 407 ? -20.704 -51.478 -24.659  1.00 21.77  ? 407 THR B CG2 1 
ATOM   7449  N N   . TRP B  1 408 ? -19.408 -49.153 -28.089  1.00 26.37  ? 408 TRP B N   1 
ATOM   7450  C CA  . TRP B  1 408 ? -18.440 -48.404 -28.871  1.00 30.07  ? 408 TRP B CA  1 
ATOM   7451  C C   . TRP B  1 408 ? -17.148 -48.138 -28.111  1.00 31.28  ? 408 TRP B C   1 
ATOM   7452  O O   . TRP B  1 408 ? -16.272 -47.456 -28.645  1.00 31.21  ? 408 TRP B O   1 
ATOM   7453  C CB  . TRP B  1 408 ? -19.048 -47.088 -29.385  1.00 24.98  ? 408 TRP B CB  1 
ATOM   7454  C CG  . TRP B  1 408 ? -19.517 -46.072 -28.345  1.00 26.88  ? 408 TRP B CG  1 
ATOM   7455  C CD1 . TRP B  1 408 ? -19.503 -46.194 -26.965  1.00 25.23  ? 408 TRP B CD1 1 
ATOM   7456  C CD2 . TRP B  1 408 ? -20.063 -44.780 -28.628  1.00 25.37  ? 408 TRP B CD2 1 
ATOM   7457  N NE1 . TRP B  1 408 ? -20.015 -45.034 -26.394  1.00 23.76  ? 408 TRP B NE1 1 
ATOM   7458  C CE2 . TRP B  1 408 ? -20.357 -44.159 -27.390  1.00 24.84  ? 408 TRP B CE2 1 
ATOM   7459  C CE3 . TRP B  1 408 ? -20.315 -44.075 -29.815  1.00 26.56  ? 408 TRP B CE3 1 
ATOM   7460  C CZ2 . TRP B  1 408 ? -20.911 -42.875 -27.311  1.00 25.21  ? 408 TRP B CZ2 1 
ATOM   7461  C CZ3 . TRP B  1 408 ? -20.864 -42.802 -29.731  1.00 31.53  ? 408 TRP B CZ3 1 
ATOM   7462  C CH2 . TRP B  1 408 ? -21.152 -42.217 -28.483  1.00 33.68  ? 408 TRP B CH2 1 
ATOM   7463  N N   . PHE B  1 409 ? -16.993 -48.661 -26.891  1.00 28.65  ? 409 PHE B N   1 
ATOM   7464  C CA  . PHE B  1 409 ? -15.684 -48.716 -26.242  1.00 32.40  ? 409 PHE B CA  1 
ATOM   7465  C C   . PHE B  1 409 ? -15.057 -50.092 -26.490  1.00 33.16  ? 409 PHE B C   1 
ATOM   7466  O O   . PHE B  1 409 ? -15.365 -51.065 -25.792  1.00 25.12  ? 409 PHE B O   1 
ATOM   7467  C CB  . PHE B  1 409 ? -15.790 -48.420 -24.750  1.00 33.38  ? 409 PHE B CB  1 
ATOM   7468  C CG  . PHE B  1 409 ? -14.461 -48.200 -24.109  1.00 37.84  ? 409 PHE B CG  1 
ATOM   7469  C CD1 . PHE B  1 409 ? -13.664 -49.277 -23.755  1.00 42.99  ? 409 PHE B CD1 1 
ATOM   7470  C CD2 . PHE B  1 409 ? -13.981 -46.917 -23.904  1.00 43.18  ? 409 PHE B CD2 1 
ATOM   7471  C CE1 . PHE B  1 409 ? -12.428 -49.080 -23.186  1.00 47.44  ? 409 PHE B CE1 1 
ATOM   7472  C CE2 . PHE B  1 409 ? -12.740 -46.713 -23.326  1.00 45.80  ? 409 PHE B CE2 1 
ATOM   7473  C CZ  . PHE B  1 409 ? -11.965 -47.793 -22.974  1.00 48.10  ? 409 PHE B CZ  1 
ATOM   7474  N N   . ASP B  1 410 ? -14.170 -50.166 -27.488  1.00 29.79  ? 410 ASP B N   1 
ATOM   7475  C CA  . ASP B  1 410 ? -13.423 -51.379 -27.826  1.00 34.88  ? 410 ASP B CA  1 
ATOM   7476  C C   . ASP B  1 410 ? -14.330 -52.561 -28.145  1.00 31.23  ? 410 ASP B C   1 
ATOM   7477  O O   . ASP B  1 410 ? -13.883 -53.707 -28.132  1.00 38.69  ? 410 ASP B O   1 
ATOM   7478  C CB  . ASP B  1 410 ? -12.452 -51.773 -26.703  1.00 45.65  ? 410 ASP B CB  1 
ATOM   7479  C CG  . ASP B  1 410 ? -11.334 -50.762 -26.502  1.00 53.92  ? 410 ASP B CG  1 
ATOM   7480  O OD1 . ASP B  1 410 ? -11.007 -50.021 -27.455  1.00 56.69  ? 410 ASP B OD1 1 
ATOM   7481  O OD2 . ASP B  1 410 ? -10.782 -50.712 -25.379  1.00 59.02  ? 410 ASP B OD2 1 
ATOM   7482  N N   . GLY B  1 411 ? -15.607 -52.327 -28.429  1.00 27.04  ? 411 GLY B N   1 
ATOM   7483  C CA  . GLY B  1 411 ? -16.477 -53.433 -28.769  1.00 27.32  ? 411 GLY B CA  1 
ATOM   7484  C C   . GLY B  1 411 ? -16.817 -54.361 -27.623  1.00 31.58  ? 411 GLY B C   1 
ATOM   7485  O O   . GLY B  1 411 ? -17.208 -55.515 -27.863  1.00 33.95  ? 411 GLY B O   1 
ATOM   7486  N N   . ASN B  1 412 ? -16.668 -53.912 -26.378  1.00 28.29  ? 412 ASN B N   1 
ATOM   7487  C CA  . ASN B  1 412 ? -16.906 -54.790 -25.237  1.00 26.42  ? 412 ASN B CA  1 
ATOM   7488  C C   . ASN B  1 412 ? -17.485 -53.962 -24.092  1.00 28.97  ? 412 ASN B C   1 
ATOM   7489  O O   . ASN B  1 412 ? -17.732 -52.758 -24.232  1.00 25.74  ? 412 ASN B O   1 
ATOM   7490  C CB  . ASN B  1 412 ? -15.626 -55.567 -24.860  1.00 27.11  ? 412 ASN B CB  1 
ATOM   7491  C CG  . ASN B  1 412 ? -14.498 -54.671 -24.337  1.00 30.82  ? 412 ASN B CG  1 
ATOM   7492  O OD1 . ASN B  1 412 ? -14.715 -53.802 -23.495  1.00 33.12  ? 412 ASN B OD1 1 
ATOM   7493  N ND2 . ASN B  1 412 ? -13.278 -54.932 -24.788  1.00 30.40  ? 412 ASN B ND2 1 
ATOM   7494  N N   . PHE B  1 413 ? -17.719 -54.610 -22.945  1.00 27.17  ? 413 PHE B N   1 
ATOM   7495  C CA  . PHE B  1 413 ? -18.439 -53.986 -21.838  1.00 22.27  ? 413 PHE B CA  1 
ATOM   7496  C C   . PHE B  1 413 ? -17.548 -53.678 -20.631  1.00 26.42  ? 413 PHE B C   1 
ATOM   7497  O O   . PHE B  1 413 ? -18.067 -53.325 -19.568  1.00 25.89  ? 413 PHE B O   1 
ATOM   7498  C CB  . PHE B  1 413 ? -19.611 -54.873 -21.405  1.00 20.84  ? 413 PHE B CB  1 
ATOM   7499  C CG  . PHE B  1 413 ? -20.722 -54.951 -22.417  1.00 24.21  ? 413 PHE B CG  1 
ATOM   7500  C CD1 . PHE B  1 413 ? -21.755 -54.015 -22.413  1.00 23.37  ? 413 PHE B CD1 1 
ATOM   7501  C CD2 . PHE B  1 413 ? -20.750 -55.978 -23.358  1.00 26.58  ? 413 PHE B CD2 1 
ATOM   7502  C CE1 . PHE B  1 413 ? -22.791 -54.104 -23.355  1.00 24.39  ? 413 PHE B CE1 1 
ATOM   7503  C CE2 . PHE B  1 413 ? -21.769 -56.059 -24.305  1.00 28.20  ? 413 PHE B CE2 1 
ATOM   7504  C CZ  . PHE B  1 413 ? -22.786 -55.125 -24.306  1.00 23.84  ? 413 PHE B CZ  1 
ATOM   7505  N N   . LEU B  1 414 ? -16.222 -53.737 -20.786  1.00 29.16  ? 414 LEU B N   1 
ATOM   7506  C CA  . LEU B  1 414 ? -15.299 -53.610 -19.659  1.00 35.57  ? 414 LEU B CA  1 
ATOM   7507  C C   . LEU B  1 414 ? -15.312 -52.232 -18.992  1.00 30.07  ? 414 LEU B C   1 
ATOM   7508  O O   . LEU B  1 414 ? -14.811 -52.107 -17.868  1.00 29.82  ? 414 LEU B O   1 
ATOM   7509  C CB  . LEU B  1 414 ? -13.882 -53.956 -20.120  1.00 36.72  ? 414 LEU B CB  1 
ATOM   7510  C CG  . LEU B  1 414 ? -13.685 -55.432 -20.470  1.00 38.42  ? 414 LEU B CG  1 
ATOM   7511  C CD1 . LEU B  1 414 ? -12.208 -55.748 -20.770  1.00 36.75  ? 414 LEU B CD1 1 
ATOM   7512  C CD2 . LEU B  1 414 ? -14.215 -56.326 -19.349  1.00 37.08  ? 414 LEU B CD2 1 
ATOM   7513  N N   . LYS B  1 415 ? -15.875 -51.203 -19.615  1.00 28.37  ? 415 LYS B N   1 
ATOM   7514  C CA  . LYS B  1 415 ? -15.901 -49.910 -18.936  1.00 31.84  ? 415 LYS B CA  1 
ATOM   7515  C C   . LYS B  1 415 ? -17.019 -49.802 -17.905  1.00 27.54  ? 415 LYS B C   1 
ATOM   7516  O O   . LYS B  1 415 ? -17.078 -48.805 -17.181  1.00 33.89  ? 415 LYS B O   1 
ATOM   7517  C CB  . LYS B  1 415 ? -16.042 -48.776 -19.957  1.00 36.74  ? 415 LYS B CB  1 
ATOM   7518  C CG  . LYS B  1 415 ? -14.724 -48.339 -20.587  1.00 42.99  ? 415 LYS B CG  1 
ATOM   7519  C CD  . LYS B  1 415 ? -13.786 -47.719 -19.568  1.00 51.50  ? 415 LYS B CD  1 
ATOM   7520  C CE  . LYS B  1 415 ? -12.464 -48.483 -19.492  1.00 58.09  ? 415 LYS B CE  1 
ATOM   7521  N NZ  . LYS B  1 415 ? -11.696 -48.171 -18.240  1.00 60.75  ? 415 LYS B NZ  1 
ATOM   7522  N N   . TRP B  1 416 ? -17.915 -50.779 -17.838  1.00 30.19  ? 416 TRP B N   1 
ATOM   7523  C CA  . TRP B  1 416 ? -19.055 -50.736 -16.933  1.00 24.85  ? 416 TRP B CA  1 
ATOM   7524  C C   . TRP B  1 416 ? -19.214 -51.984 -16.080  1.00 27.34  ? 416 TRP B C   1 
ATOM   7525  O O   . TRP B  1 416 ? -20.034 -51.974 -15.149  1.00 27.64  ? 416 TRP B O   1 
ATOM   7526  C CB  . TRP B  1 416 ? -20.350 -50.526 -17.732  1.00 24.54  ? 416 TRP B CB  1 
ATOM   7527  C CG  . TRP B  1 416 ? -20.294 -49.321 -18.612  1.00 32.02  ? 416 TRP B CG  1 
ATOM   7528  C CD1 . TRP B  1 416 ? -20.666 -48.043 -18.273  1.00 28.33  ? 416 TRP B CD1 1 
ATOM   7529  C CD2 . TRP B  1 416 ? -19.818 -49.253 -19.971  1.00 31.45  ? 416 TRP B CD2 1 
ATOM   7530  N NE1 . TRP B  1 416 ? -20.460 -47.199 -19.334  1.00 30.86  ? 416 TRP B NE1 1 
ATOM   7531  C CE2 . TRP B  1 416 ? -19.938 -47.907 -20.385  1.00 30.34  ? 416 TRP B CE2 1 
ATOM   7532  C CE3 . TRP B  1 416 ? -19.293 -50.196 -20.871  1.00 30.27  ? 416 TRP B CE3 1 
ATOM   7533  C CZ2 . TRP B  1 416 ? -19.560 -47.472 -21.675  1.00 27.28  ? 416 TRP B CZ2 1 
ATOM   7534  C CZ3 . TRP B  1 416 ? -18.917 -49.765 -22.155  1.00 27.76  ? 416 TRP B CZ3 1 
ATOM   7535  C CH2 . TRP B  1 416 ? -19.057 -48.414 -22.537  1.00 24.84  ? 416 TRP B CH2 1 
ATOM   7536  N N   . ILE B  1 417 ? -18.468 -53.052 -16.361  1.00 26.06  ? 417 ILE B N   1 
ATOM   7537  C CA  . ILE B  1 417 ? -18.563 -54.277 -15.582  1.00 31.62  ? 417 ILE B CA  1 
ATOM   7538  C C   . ILE B  1 417 ? -17.236 -55.010 -15.689  1.00 33.52  ? 417 ILE B C   1 
ATOM   7539  O O   . ILE B  1 417 ? -16.484 -54.825 -16.650  1.00 34.83  ? 417 ILE B O   1 
ATOM   7540  C CB  . ILE B  1 417 ? -19.752 -55.122 -16.086  1.00 31.51  ? 417 ILE B CB  1 
ATOM   7541  C CG1 . ILE B  1 417 ? -20.089 -56.248 -15.116  1.00 29.03  ? 417 ILE B CG1 1 
ATOM   7542  C CG2 . ILE B  1 417 ? -19.496 -55.583 -17.504  1.00 29.50  ? 417 ILE B CG2 1 
ATOM   7543  C CD1 . ILE B  1 417 ? -21.540 -56.626 -15.129  1.00 27.48  ? 417 ILE B CD1 1 
ATOM   7544  N N   . GLY B  1 418 ? -16.924 -55.820 -14.685  1.00 30.91  ? 418 GLY B N   1 
ATOM   7545  C CA  . GLY B  1 418 ? -15.695 -56.575 -14.779  1.00 33.47  ? 418 GLY B CA  1 
ATOM   7546  C C   . GLY B  1 418 ? -14.665 -56.434 -13.681  1.00 40.01  ? 418 GLY B C   1 
ATOM   7547  O O   . GLY B  1 418 ? -14.076 -57.447 -13.294  1.00 51.87  ? 418 GLY B O   1 
ATOM   7548  N N   . ASN B  1 419 ? -14.401 -55.233 -13.171  1.00 34.60  ? 419 ASN B N   1 
ATOM   7549  C CA  . ASN B  1 419 ? -13.440 -55.150 -12.078  1.00 35.80  ? 419 ASN B CA  1 
ATOM   7550  C C   . ASN B  1 419 ? -14.169 -55.152 -10.734  1.00 32.21  ? 419 ASN B C   1 
ATOM   7551  O O   . ASN B  1 419 ? -15.399 -55.132 -10.665  1.00 32.58  ? 419 ASN B O   1 
ATOM   7552  C CB  . ASN B  1 419 ? -12.510 -53.932 -12.228  1.00 40.40  ? 419 ASN B CB  1 
ATOM   7553  C CG  . ASN B  1 419 ? -13.210 -52.582 -12.030  1.00 44.17  ? 419 ASN B CG  1 
ATOM   7554  O OD1 . ASN B  1 419 ? -14.261 -52.474 -11.394  1.00 48.39  ? 419 ASN B OD1 1 
ATOM   7555  N ND2 . ASN B  1 419 ? -12.596 -51.535 -12.570  1.00 41.89  ? 419 ASN B ND2 1 
ATOM   7556  N N   . LYS B  1 420 ? -13.387 -55.180 -9.653   1.00 34.47  ? 420 LYS B N   1 
ATOM   7557  C CA  . LYS B  1 420 ? -13.979 -55.345 -8.331   1.00 32.99  ? 420 LYS B CA  1 
ATOM   7558  C C   . LYS B  1 420 ? -14.951 -54.218 -8.016   1.00 36.10  ? 420 LYS B C   1 
ATOM   7559  O O   . LYS B  1 420 ? -16.050 -54.459 -7.498   1.00 37.64  ? 420 LYS B O   1 
ATOM   7560  C CB  . LYS B  1 420 ? -12.873 -55.418 -7.273   1.00 38.49  ? 420 LYS B CB  1 
ATOM   7561  C CG  . LYS B  1 420 ? -13.343 -55.839 -5.895   1.00 46.69  ? 420 LYS B CG  1 
ATOM   7562  C CD  . LYS B  1 420 ? -12.224 -56.556 -5.129   1.00 52.45  ? 420 LYS B CD  1 
ATOM   7563  C CE  . LYS B  1 420 ? -12.174 -56.123 -3.670   1.00 57.47  ? 420 LYS B CE  1 
ATOM   7564  N NZ  . LYS B  1 420 ? -11.101 -56.849 -2.921   1.00 61.55  ? 420 LYS B NZ  1 
ATOM   7565  N N   . GLU B  1 421 ? -14.577 -52.979 -8.342   1.00 37.15  ? 421 GLU B N   1 
ATOM   7566  C CA  . GLU B  1 421 ? -15.393 -51.838 -7.940   1.00 36.59  ? 421 GLU B CA  1 
ATOM   7567  C C   . GLU B  1 421 ? -16.667 -51.751 -8.772   1.00 34.85  ? 421 GLU B C   1 
ATOM   7568  O O   . GLU B  1 421 ? -17.763 -51.551 -8.230   1.00 31.52  ? 421 GLU B O   1 
ATOM   7569  C CB  . GLU B  1 421 ? -14.580 -50.544 -8.045   1.00 41.48  ? 421 GLU B CB  1 
ATOM   7570  C CG  . GLU B  1 421 ? -13.640 -50.299 -6.873   1.00 52.38  ? 421 GLU B CG  1 
ATOM   7571  C CD  . GLU B  1 421 ? -12.309 -51.001 -7.046   1.00 59.80  ? 421 GLU B CD  1 
ATOM   7572  O OE1 . GLU B  1 421 ? -11.917 -51.264 -8.207   1.00 62.42  ? 421 GLU B OE1 1 
ATOM   7573  O OE2 . GLU B  1 421 ? -11.653 -51.289 -6.022   1.00 62.86  ? 421 GLU B OE2 1 
ATOM   7574  N N   . LYS B  1 422 ? -16.547 -51.890 -10.095  1.00 36.20  ? 422 LYS B N   1 
ATOM   7575  C CA  . LYS B  1 422 ? -17.731 -51.843 -10.945  1.00 28.53  ? 422 LYS B CA  1 
ATOM   7576  C C   . LYS B  1 422 ? -18.683 -52.984 -10.622  1.00 31.83  ? 422 LYS B C   1 
ATOM   7577  O O   . LYS B  1 422 ? -19.904 -52.788 -10.595  1.00 31.16  ? 422 LYS B O   1 
ATOM   7578  C CB  . LYS B  1 422 ? -17.328 -51.890 -12.415  1.00 27.85  ? 422 LYS B CB  1 
ATOM   7579  C CG  . LYS B  1 422 ? -16.544 -50.687 -12.881  1.00 31.18  ? 422 LYS B CG  1 
ATOM   7580  C CD  . LYS B  1 422 ? -16.227 -50.775 -14.372  1.00 30.00  ? 422 LYS B CD  1 
ATOM   7581  C CE  . LYS B  1 422 ? -15.279 -49.658 -14.812  1.00 31.38  ? 422 LYS B CE  1 
ATOM   7582  N NZ  . LYS B  1 422 ? -15.824 -48.269 -14.659  1.00 27.30  ? 422 LYS B NZ  1 
ATOM   7583  N N   . ASN B  1 423 ? -18.137 -54.186 -10.371  1.00 28.11  ? 423 ASN B N   1 
ATOM   7584  C CA  . ASN B  1 423 ? -18.968 -55.334 -10.025  1.00 29.84  ? 423 ASN B CA  1 
ATOM   7585  C C   . ASN B  1 423 ? -19.669 -55.129 -8.691   1.00 28.19  ? 423 ASN B C   1 
ATOM   7586  O O   . ASN B  1 423 ? -20.750 -55.688 -8.469   1.00 28.28  ? 423 ASN B O   1 
ATOM   7587  C CB  . ASN B  1 423 ? -18.131 -56.619 -9.969   1.00 30.68  ? 423 ASN B CB  1 
ATOM   7588  C CG  . ASN B  1 423 ? -17.826 -57.193 -11.346  1.00 31.32  ? 423 ASN B CG  1 
ATOM   7589  O OD1 . ASN B  1 423 ? -18.227 -56.645 -12.365  1.00 28.89  ? 423 ASN B OD1 1 
ATOM   7590  N ND2 . ASN B  1 423 ? -17.114 -58.311 -11.370  1.00 34.08  ? 423 ASN B ND2 1 
ATOM   7591  N N   . GLU B  1 424 ? -19.071 -54.349 -7.786   1.00 34.36  ? 424 GLU B N   1 
ATOM   7592  C CA  . GLU B  1 424 ? -19.755 -54.049 -6.527   1.00 38.17  ? 424 GLU B CA  1 
ATOM   7593  C C   . GLU B  1 424 ? -21.023 -53.251 -6.788   1.00 31.69  ? 424 GLU B C   1 
ATOM   7594  O O   . GLU B  1 424 ? -22.050 -53.471 -6.140   1.00 31.76  ? 424 GLU B O   1 
ATOM   7595  C CB  . GLU B  1 424 ? -18.829 -53.294 -5.570   1.00 44.88  ? 424 GLU B CB  1 
ATOM   7596  C CG  . GLU B  1 424 ? -19.499 -52.768 -4.281   1.00 51.24  ? 424 GLU B CG  1 
ATOM   7597  C CD  . GLU B  1 424 ? -19.953 -53.877 -3.319   1.00 57.92  ? 424 GLU B CD  1 
ATOM   7598  O OE1 . GLU B  1 424 ? -20.612 -53.557 -2.295   1.00 56.62  ? 424 GLU B OE1 1 
ATOM   7599  O OE2 . GLU B  1 424 ? -19.662 -55.068 -3.588   1.00 59.84  ? 424 GLU B OE2 1 
ATOM   7600  N N   . TYR B  1 425 ? -20.976 -52.342 -7.761   1.00 30.96  ? 425 TYR B N   1 
ATOM   7601  C CA  . TYR B  1 425 ? -22.172 -51.594 -8.134   1.00 32.63  ? 425 TYR B CA  1 
ATOM   7602  C C   . TYR B  1 425 ? -23.278 -52.526 -8.633   1.00 30.46  ? 425 TYR B C   1 
ATOM   7603  O O   . TYR B  1 425 ? -24.437 -52.413 -8.215   1.00 32.90  ? 425 TYR B O   1 
ATOM   7604  C CB  . TYR B  1 425 ? -21.816 -50.545 -9.187   1.00 29.46  ? 425 TYR B CB  1 
ATOM   7605  C CG  . TYR B  1 425 ? -21.535 -49.179 -8.612   1.00 28.61  ? 425 TYR B CG  1 
ATOM   7606  C CD1 . TYR B  1 425 ? -20.945 -49.027 -7.359   1.00 30.94  ? 425 TYR B CD1 1 
ATOM   7607  C CD2 . TYR B  1 425 ? -21.865 -48.042 -9.325   1.00 27.68  ? 425 TYR B CD2 1 
ATOM   7608  C CE1 . TYR B  1 425 ? -20.699 -47.759 -6.837   1.00 36.85  ? 425 TYR B CE1 1 
ATOM   7609  C CE2 . TYR B  1 425 ? -21.627 -46.780 -8.828   1.00 28.04  ? 425 TYR B CE2 1 
ATOM   7610  C CZ  . TYR B  1 425 ? -21.044 -46.638 -7.585   1.00 29.97  ? 425 TYR B CZ  1 
ATOM   7611  O OH  . TYR B  1 425 ? -20.815 -45.366 -7.121   1.00 29.59  ? 425 TYR B OH  1 
ATOM   7612  N N   . TRP B  1 426 ? -22.939 -53.463 -9.525   1.00 27.27  ? 426 TRP B N   1 
ATOM   7613  C CA  . TRP B  1 426 ? -23.940 -54.417 -9.994   1.00 29.55  ? 426 TRP B CA  1 
ATOM   7614  C C   . TRP B  1 426 ? -24.500 -55.255 -8.851   1.00 30.81  ? 426 TRP B C   1 
ATOM   7615  O O   . TRP B  1 426 ? -25.706 -55.518 -8.809   1.00 34.05  ? 426 TRP B O   1 
ATOM   7616  C CB  . TRP B  1 426 ? -23.348 -55.320 -11.077  1.00 29.19  ? 426 TRP B CB  1 
ATOM   7617  C CG  . TRP B  1 426 ? -23.145 -54.581 -12.343  1.00 23.75  ? 426 TRP B CG  1 
ATOM   7618  C CD1 . TRP B  1 426 ? -21.972 -54.118 -12.842  1.00 25.74  ? 426 TRP B CD1 1 
ATOM   7619  C CD2 . TRP B  1 426 ? -24.159 -54.210 -13.269  1.00 28.71  ? 426 TRP B CD2 1 
ATOM   7620  N NE1 . TRP B  1 426 ? -22.186 -53.481 -14.052  1.00 27.79  ? 426 TRP B NE1 1 
ATOM   7621  C CE2 . TRP B  1 426 ? -23.524 -53.539 -14.339  1.00 32.70  ? 426 TRP B CE2 1 
ATOM   7622  C CE3 . TRP B  1 426 ? -25.544 -54.400 -13.314  1.00 30.87  ? 426 TRP B CE3 1 
ATOM   7623  C CZ2 . TRP B  1 426 ? -24.228 -53.036 -15.424  1.00 36.10  ? 426 TRP B CZ2 1 
ATOM   7624  C CZ3 . TRP B  1 426 ? -26.243 -53.914 -14.412  1.00 36.98  ? 426 TRP B CZ3 1 
ATOM   7625  C CH2 . TRP B  1 426 ? -25.582 -53.235 -15.447  1.00 38.82  ? 426 TRP B CH2 1 
ATOM   7626  N N   . LYS B  1 427 ? -23.640 -55.706 -7.930   1.00 33.58  ? 427 LYS B N   1 
ATOM   7627  C CA  . LYS B  1 427 ? -24.122 -56.434 -6.752   1.00 32.89  ? 427 LYS B CA  1 
ATOM   7628  C C   . LYS B  1 427 ? -25.109 -55.604 -5.944   1.00 32.28  ? 427 LYS B C   1 
ATOM   7629  O O   . LYS B  1 427 ? -26.166 -56.103 -5.539   1.00 34.09  ? 427 LYS B O   1 
ATOM   7630  C CB  . LYS B  1 427 ? -22.950 -56.855 -5.867   1.00 39.71  ? 427 LYS B CB  1 
ATOM   7631  C CG  . LYS B  1 427 ? -22.467 -58.265 -6.165   1.00 47.87  ? 427 LYS B CG  1 
ATOM   7632  C CD  . LYS B  1 427 ? -20.950 -58.356 -6.152   1.00 52.11  ? 427 LYS B CD  1 
ATOM   7633  C CE  . LYS B  1 427 ? -20.399 -58.074 -4.766   1.00 56.42  ? 427 LYS B CE  1 
ATOM   7634  N NZ  . LYS B  1 427 ? -18.933 -58.340 -4.665   1.00 58.65  ? 427 LYS B NZ  1 
ATOM   7635  N N   . ILE B  1 428 ? -24.763 -54.340 -5.675   1.00 30.84  ? 428 ILE B N   1 
ATOM   7636  C CA  . ILE B  1 428 ? -25.689 -53.406 -5.029   1.00 33.99  ? 428 ILE B CA  1 
ATOM   7637  C C   . ILE B  1 428 ? -27.012 -53.362 -5.783   1.00 36.82  ? 428 ILE B C   1 
ATOM   7638  O O   . ILE B  1 428 ? -28.097 -53.424 -5.184   1.00 36.65  ? 428 ILE B O   1 
ATOM   7639  C CB  . ILE B  1 428 ? -25.054 -52.007 -4.931   1.00 36.28  ? 428 ILE B CB  1 
ATOM   7640  C CG1 . ILE B  1 428 ? -23.886 -52.027 -3.942   1.00 29.34  ? 428 ILE B CG1 1 
ATOM   7641  C CG2 . ILE B  1 428 ? -26.094 -50.949 -4.520   1.00 38.45  ? 428 ILE B CG2 1 
ATOM   7642  C CD1 . ILE B  1 428 ? -23.090 -50.760 -3.895   1.00 29.93  ? 428 ILE B CD1 1 
ATOM   7643  N N   . LEU B  1 429 ? -26.932 -53.248 -7.117   1.00 28.74  ? 429 LEU B N   1 
ATOM   7644  C CA  . LEU B  1 429 ? -28.123 -53.140 -7.953   1.00 24.86  ? 429 LEU B CA  1 
ATOM   7645  C C   . LEU B  1 429 ? -28.918 -54.430 -7.955   1.00 28.97  ? 429 LEU B C   1 
ATOM   7646  O O   . LEU B  1 429 ? -30.155 -54.403 -7.902   1.00 36.74  ? 429 LEU B O   1 
ATOM   7647  C CB  . LEU B  1 429 ? -27.721 -52.783 -9.380   1.00 25.55  ? 429 LEU B CB  1 
ATOM   7648  C CG  . LEU B  1 429 ? -28.892 -52.626 -10.349  1.00 27.71  ? 429 LEU B CG  1 
ATOM   7649  C CD1 . LEU B  1 429 ? -29.677 -51.347 -10.038  1.00 26.68  ? 429 LEU B CD1 1 
ATOM   7650  C CD2 . LEU B  1 429 ? -28.393 -52.621 -11.799  1.00 22.13  ? 429 LEU B CD2 1 
ATOM   7651  N N   . ILE B  1 430 ? -28.221 -55.569 -8.035   1.00 29.43  ? 430 ILE B N   1 
ATOM   7652  C CA  . ILE B  1 430 ? -28.881 -56.868 -7.965   1.00 30.30  ? 430 ILE B CA  1 
ATOM   7653  C C   . ILE B  1 430 ? -29.610 -57.009 -6.637   1.00 31.79  ? 430 ILE B C   1 
ATOM   7654  O O   . ILE B  1 430 ? -30.795 -57.356 -6.594   1.00 37.08  ? 430 ILE B O   1 
ATOM   7655  C CB  . ILE B  1 430 ? -27.862 -58.005 -8.174   1.00 30.29  ? 430 ILE B CB  1 
ATOM   7656  C CG1 . ILE B  1 430 ? -27.387 -58.048 -9.633   1.00 30.12  ? 430 ILE B CG1 1 
ATOM   7657  C CG2 . ILE B  1 430 ? -28.477 -59.349 -7.818   1.00 33.75  ? 430 ILE B CG2 1 
ATOM   7658  C CD1 . ILE B  1 430 ? -26.110 -58.813 -9.800   1.00 32.59  ? 430 ILE B CD1 1 
ATOM   7659  N N   . GLU B  1 431 ? -28.919 -56.735 -5.533   1.00 33.38  ? 431 GLU B N   1 
ATOM   7660  C CA  . GLU B  1 431 ? -29.576 -56.872 -4.232   1.00 39.02  ? 431 GLU B CA  1 
ATOM   7661  C C   . GLU B  1 431 ? -30.743 -55.901 -4.102   1.00 39.06  ? 431 GLU B C   1 
ATOM   7662  O O   . GLU B  1 431 ? -31.817 -56.270 -3.608   1.00 39.16  ? 431 GLU B O   1 
ATOM   7663  C CB  . GLU B  1 431 ? -28.577 -56.664 -3.093   1.00 46.58  ? 431 GLU B CB  1 
ATOM   7664  C CG  . GLU B  1 431 ? -27.637 -57.836 -2.843   1.00 59.71  ? 431 GLU B CG  1 
ATOM   7665  C CD  . GLU B  1 431 ? -28.321 -59.206 -2.933   1.00 65.93  ? 431 GLU B CD  1 
ATOM   7666  O OE1 . GLU B  1 431 ? -27.993 -59.980 -3.866   1.00 63.61  ? 431 GLU B OE1 1 
ATOM   7667  O OE2 . GLU B  1 431 ? -29.177 -59.506 -2.067   1.00 68.81  ? 431 GLU B OE2 1 
ATOM   7668  N N   . ALA B  1 432 ? -30.559 -54.657 -4.553   1.00 37.96  ? 432 ALA B N   1 
ATOM   7669  C CA  . ALA B  1 432 ? -31.638 -53.678 -4.462   1.00 39.42  ? 432 ALA B CA  1 
ATOM   7670  C C   . ALA B  1 432 ? -32.828 -54.061 -5.333   1.00 39.91  ? 432 ALA B C   1 
ATOM   7671  O O   . ALA B  1 432 ? -33.977 -53.793 -4.960   1.00 38.78  ? 432 ALA B O   1 
ATOM   7672  C CB  . ALA B  1 432 ? -31.131 -52.291 -4.851   1.00 38.74  ? 432 ALA B CB  1 
ATOM   7673  N N   . LYS B  1 433 ? -32.574 -54.677 -6.492   1.00 37.09  ? 433 LYS B N   1 
ATOM   7674  C CA  . LYS B  1 433 ? -33.657 -55.051 -7.392   1.00 36.71  ? 433 LYS B CA  1 
ATOM   7675  C C   . LYS B  1 433 ? -34.621 -56.028 -6.731   1.00 39.35  ? 433 LYS B C   1 
ATOM   7676  O O   . LYS B  1 433 ? -35.840 -55.919 -6.915   1.00 35.07  ? 433 LYS B O   1 
ATOM   7677  C CB  . LYS B  1 433 ? -33.081 -55.635 -8.684   1.00 37.41  ? 433 LYS B CB  1 
ATOM   7678  C CG  . LYS B  1 433 ? -34.107 -56.279 -9.598   1.00 34.32  ? 433 LYS B CG  1 
ATOM   7679  C CD  . LYS B  1 433 ? -35.086 -55.264 -10.138  1.00 36.17  ? 433 LYS B CD  1 
ATOM   7680  C CE  . LYS B  1 433 ? -36.059 -55.898 -11.129  1.00 32.36  ? 433 LYS B CE  1 
ATOM   7681  N NZ  . LYS B  1 433 ? -37.123 -54.947 -11.581  1.00 32.97  ? 433 LYS B NZ  1 
ATOM   7682  N N   . LYS B  1 434 ? -34.096 -56.972 -5.932   1.00 44.71  ? 434 LYS B N   1 
ATOM   7683  C CA  . LYS B  1 434 ? -34.953 -57.956 -5.266   1.00 45.46  ? 434 LYS B CA  1 
ATOM   7684  C C   . LYS B  1 434 ? -35.999 -57.314 -4.365   1.00 45.87  ? 434 LYS B C   1 
ATOM   7685  O O   . LYS B  1 434 ? -37.072 -57.894 -4.166   1.00 49.96  ? 434 LYS B O   1 
ATOM   7686  C CB  . LYS B  1 434 ? -34.128 -58.949 -4.441   1.00 48.46  ? 434 LYS B CB  1 
ATOM   7687  C CG  . LYS B  1 434 ? -32.842 -59.410 -5.090   1.00 47.58  ? 434 LYS B CG  1 
ATOM   7688  C CD  . LYS B  1 434 ? -31.922 -60.067 -4.081   1.00 50.40  ? 434 LYS B CD  1 
ATOM   7689  C CE  . LYS B  1 434 ? -30.828 -60.850 -4.782   1.00 50.24  ? 434 LYS B CE  1 
ATOM   7690  N NZ  . LYS B  1 434 ? -30.858 -62.283 -4.430   1.00 51.97  ? 434 LYS B NZ  1 
ATOM   7691  N N   . LYS B  1 435 ? -35.706 -56.141 -3.789   1.00 40.36  ? 435 LYS B N   1 
ATOM   7692  C CA  . LYS B  1 435 ? -36.637 -55.464 -2.892   1.00 40.91  ? 435 LYS B CA  1 
ATOM   7693  C C   . LYS B  1 435 ? -37.028 -54.088 -3.413   1.00 44.78  ? 435 LYS B C   1 
ATOM   7694  O O   . LYS B  1 435 ? -37.438 -53.225 -2.628   1.00 46.85  ? 435 LYS B O   1 
ATOM   7695  C CB  . LYS B  1 435 ? -36.053 -55.330 -1.483   1.00 43.25  ? 435 LYS B CB  1 
ATOM   7696  C CG  . LYS B  1 435 ? -34.789 -56.121 -1.247   1.00 45.14  ? 435 LYS B CG  1 
ATOM   7697  C CD  . LYS B  1 435 ? -34.343 -55.982 0.190    1.00 50.24  ? 435 LYS B CD  1 
ATOM   7698  C CE  . LYS B  1 435 ? -32.993 -56.651 0.435    1.00 54.63  ? 435 LYS B CE  1 
ATOM   7699  N NZ  . LYS B  1 435 ? -32.732 -56.849 1.900    1.00 61.34  ? 435 LYS B NZ  1 
ATOM   7700  N N   . ALA B  1 436 ? -36.888 -53.865 -4.715   1.00 39.69  ? 436 ALA B N   1 
ATOM   7701  C CA  . ALA B  1 436 ? -37.265 -52.603 -5.324   1.00 41.10  ? 436 ALA B CA  1 
ATOM   7702  C C   . ALA B  1 436 ? -38.783 -52.471 -5.367   1.00 42.05  ? 436 ALA B C   1 
ATOM   7703  O O   . ALA B  1 436 ? -39.509 -53.457 -5.518   1.00 42.27  ? 436 ALA B O   1 
ATOM   7704  C CB  . ALA B  1 436 ? -36.679 -52.504 -6.733   1.00 37.67  ? 436 ALA B CB  1 
ATOM   7705  N N   . LYS B  1 437 ? -39.266 -51.231 -5.210   1.00 42.75  ? 437 LYS B N   1 
ATOM   7706  C CA  . LYS B  1 437 ? -40.702 -50.977 -5.215   1.00 47.96  ? 437 LYS B CA  1 
ATOM   7707  C C   . LYS B  1 437 ? -41.102 -49.745 -6.027   1.00 48.30  ? 437 LYS B C   1 
ATOM   7708  O O   . LYS B  1 437 ? -42.274 -49.350 -5.982   1.00 47.99  ? 437 LYS B O   1 
ATOM   7709  C CB  . LYS B  1 437 ? -41.236 -50.833 -3.774   1.00 51.51  ? 437 LYS B CB  1 
ATOM   7710  C CG  . LYS B  1 437 ? -40.398 -51.522 -2.708   1.00 55.25  ? 437 LYS B CG  1 
ATOM   7711  C CD  . LYS B  1 437 ? -41.111 -51.565 -1.369   1.00 60.03  ? 437 LYS B CD  1 
ATOM   7712  C CE  . LYS B  1 437 ? -40.174 -52.000 -0.244   1.00 63.25  ? 437 LYS B CE  1 
ATOM   7713  N NZ  . LYS B  1 437 ? -40.699 -51.652 1.125    1.00 65.97  ? 437 LYS B NZ  1 
ATOM   7714  N N   . ASN B  1 438 ? -40.184 -49.120 -6.759   1.00 45.35  ? 438 ASN B N   1 
ATOM   7715  C CA  . ASN B  1 438 ? -40.548 -47.998 -7.614   1.00 46.10  ? 438 ASN B CA  1 
ATOM   7716  C C   . ASN B  1 438 ? -39.490 -47.862 -8.704   1.00 43.94  ? 438 ASN B C   1 
ATOM   7717  O O   . ASN B  1 438 ? -38.473 -48.564 -8.698   1.00 44.70  ? 438 ASN B O   1 
ATOM   7718  C CB  . ASN B  1 438 ? -40.718 -46.703 -6.803   1.00 43.91  ? 438 ASN B CB  1 
ATOM   7719  C CG  . ASN B  1 438 ? -39.484 -46.345 -6.002   1.00 42.37  ? 438 ASN B CG  1 
ATOM   7720  O OD1 . ASN B  1 438 ? -38.447 -46.002 -6.569   1.00 41.06  ? 438 ASN B OD1 1 
ATOM   7721  N ND2 . ASN B  1 438 ? -39.598 -46.390 -4.672   1.00 45.23  ? 438 ASN B ND2 1 
ATOM   7722  N N   . ASP B  1 439 ? -39.737 -46.935 -9.636   1.00 39.80  ? 439 ASP B N   1 
ATOM   7723  C CA  . ASP B  1 439 ? -38.934 -46.765 -10.842  1.00 37.99  ? 439 ASP B CA  1 
ATOM   7724  C C   . ASP B  1 439 ? -37.594 -46.093 -10.589  1.00 32.07  ? 439 ASP B C   1 
ATOM   7725  O O   . ASP B  1 439 ? -36.855 -45.838 -11.547  1.00 33.49  ? 439 ASP B O   1 
ATOM   7726  C CB  . ASP B  1 439 ? -39.709 -45.952 -11.887  1.00 45.83  ? 439 ASP B CB  1 
ATOM   7727  C CG  . ASP B  1 439 ? -40.767 -46.774 -12.608  1.00 52.25  ? 439 ASP B CG  1 
ATOM   7728  O OD1 . ASP B  1 439 ? -40.652 -48.019 -12.630  1.00 49.07  ? 439 ASP B OD1 1 
ATOM   7729  O OD2 . ASP B  1 439 ? -41.719 -46.165 -13.153  1.00 58.59  ? 439 ASP B OD2 1 
ATOM   7730  N N   . TYR B  1 440 ? -37.256 -45.783 -9.344   1.00 32.02  ? 440 TYR B N   1 
ATOM   7731  C CA  . TYR B  1 440 ? -35.907 -45.303 -9.083   1.00 32.23  ? 440 TYR B CA  1 
ATOM   7732  C C   . TYR B  1 440 ? -34.877 -46.399 -9.285   1.00 31.58  ? 440 TYR B C   1 
ATOM   7733  O O   . TYR B  1 440 ? -33.684 -46.099 -9.392   1.00 32.10  ? 440 TYR B O   1 
ATOM   7734  C CB  . TYR B  1 440 ? -35.800 -44.739 -7.671   1.00 35.05  ? 440 TYR B CB  1 
ATOM   7735  C CG  . TYR B  1 440 ? -36.007 -43.234 -7.616   1.00 41.63  ? 440 TYR B CG  1 
ATOM   7736  C CD1 . TYR B  1 440 ? -35.074 -42.362 -8.173   1.00 40.26  ? 440 TYR B CD1 1 
ATOM   7737  C CD2 . TYR B  1 440 ? -37.137 -42.687 -7.008   1.00 43.86  ? 440 TYR B CD2 1 
ATOM   7738  C CE1 . TYR B  1 440 ? -35.261 -40.984 -8.124   1.00 41.44  ? 440 TYR B CE1 1 
ATOM   7739  C CE2 . TYR B  1 440 ? -37.332 -41.316 -6.955   1.00 43.66  ? 440 TYR B CE2 1 
ATOM   7740  C CZ  . TYR B  1 440 ? -36.394 -40.468 -7.512   1.00 43.53  ? 440 TYR B CZ  1 
ATOM   7741  O OH  . TYR B  1 440 ? -36.591 -39.101 -7.458   1.00 47.95  ? 440 TYR B OH  1 
ATOM   7742  N N   . ILE B  1 441 ? -35.312 -47.661 -9.335   1.00 29.87  ? 441 ILE B N   1 
ATOM   7743  C CA  . ILE B  1 441 ? -34.383 -48.726 -9.700   1.00 33.37  ? 441 ILE B CA  1 
ATOM   7744  C C   . ILE B  1 441 ? -33.957 -48.563 -11.150  1.00 31.59  ? 441 ILE B C   1 
ATOM   7745  O O   . ILE B  1 441 ? -32.809 -48.860 -11.504  1.00 30.14  ? 441 ILE B O   1 
ATOM   7746  C CB  . ILE B  1 441 ? -35.001 -50.115 -9.434   1.00 32.71  ? 441 ILE B CB  1 
ATOM   7747  C CG1 . ILE B  1 441 ? -33.924 -51.205 -9.478   1.00 26.75  ? 441 ILE B CG1 1 
ATOM   7748  C CG2 . ILE B  1 441 ? -36.122 -50.433 -10.439  1.00 29.61  ? 441 ILE B CG2 1 
ATOM   7749  C CD1 . ILE B  1 441 ? -33.064 -51.256 -8.210   1.00 29.28  ? 441 ILE B CD1 1 
ATOM   7750  N N   . LEU B  1 442 ? -34.854 -48.053 -12.007  1.00 28.38  ? 442 LEU B N   1 
ATOM   7751  C CA  . LEU B  1 442 ? -34.466 -47.789 -13.383  1.00 27.17  ? 442 LEU B CA  1 
ATOM   7752  C C   . LEU B  1 442 ? -33.453 -46.657 -13.447  1.00 26.31  ? 442 LEU B C   1 
ATOM   7753  O O   . LEU B  1 442 ? -32.569 -46.670 -14.313  1.00 23.64  ? 442 LEU B O   1 
ATOM   7754  C CB  . LEU B  1 442 ? -35.704 -47.470 -14.222  1.00 23.73  ? 442 LEU B CB  1 
ATOM   7755  C CG  . LEU B  1 442 ? -36.845 -48.487 -14.120  1.00 25.90  ? 442 LEU B CG  1 
ATOM   7756  C CD1 . LEU B  1 442 ? -38.098 -47.967 -14.835  1.00 32.34  ? 442 LEU B CD1 1 
ATOM   7757  C CD2 . LEU B  1 442 ? -36.423 -49.842 -14.696  1.00 29.10  ? 442 LEU B CD2 1 
ATOM   7758  N N   . VAL B  1 443 ? -33.541 -45.692 -12.521  1.00 26.94  ? 443 VAL B N   1 
ATOM   7759  C CA  . VAL B  1 443 ? -32.579 -44.594 -12.521  1.00 29.80  ? 443 VAL B CA  1 
ATOM   7760  C C   . VAL B  1 443 ? -31.185 -45.132 -12.246  1.00 28.52  ? 443 VAL B C   1 
ATOM   7761  O O   . VAL B  1 443 ? -30.206 -44.726 -12.885  1.00 28.42  ? 443 VAL B O   1 
ATOM   7762  C CB  . VAL B  1 443 ? -32.965 -43.508 -11.495  1.00 29.66  ? 443 VAL B CB  1 
ATOM   7763  C CG1 . VAL B  1 443 ? -31.950 -42.363 -11.554  1.00 31.24  ? 443 VAL B CG1 1 
ATOM   7764  C CG2 . VAL B  1 443 ? -34.375 -42.985 -11.727  1.00 29.36  ? 443 VAL B CG2 1 
ATOM   7765  N N   . ALA B  1 444 ? -31.079 -46.051 -11.281  1.00 30.23  ? 444 ALA B N   1 
ATOM   7766  C CA  . ALA B  1 444 ? -29.812 -46.668 -10.895  1.00 30.90  ? 444 ALA B CA  1 
ATOM   7767  C C   . ALA B  1 444 ? -29.298 -47.655 -11.930  1.00 28.86  ? 444 ALA B C   1 
ATOM   7768  O O   . ALA B  1 444 ? -28.154 -48.112 -11.806  1.00 28.05  ? 444 ALA B O   1 
ATOM   7769  C CB  . ALA B  1 444 ? -29.948 -47.378 -9.540   1.00 29.14  ? 444 ALA B CB  1 
ATOM   7770  N N   . GLU B  1 445 ? -30.092 -47.987 -12.948  1.00 26.06  ? 445 GLU B N   1 
ATOM   7771  C CA  . GLU B  1 445 ? -29.593 -48.841 -14.014  1.00 26.23  ? 445 GLU B CA  1 
ATOM   7772  C C   . GLU B  1 445 ? -28.918 -48.043 -15.116  1.00 28.59  ? 445 GLU B C   1 
ATOM   7773  O O   . GLU B  1 445 ? -28.466 -48.630 -16.101  1.00 28.97  ? 445 GLU B O   1 
ATOM   7774  C CB  . GLU B  1 445 ? -30.731 -49.699 -14.576  1.00 29.55  ? 445 GLU B CB  1 
ATOM   7775  C CG  . GLU B  1 445 ? -31.161 -50.808 -13.601  1.00 30.43  ? 445 GLU B CG  1 
ATOM   7776  C CD  . GLU B  1 445 ? -32.583 -51.282 -13.839  1.00 33.59  ? 445 GLU B CD  1 
ATOM   7777  O OE1 . GLU B  1 445 ? -33.185 -50.860 -14.851  1.00 29.41  ? 445 GLU B OE1 1 
ATOM   7778  O OE2 . GLU B  1 445 ? -33.099 -52.077 -13.016  1.00 37.96  ? 445 GLU B OE2 1 
ATOM   7779  N N   . GLY B  1 446 ? -28.820 -46.725 -14.960  1.00 28.02  ? 446 GLY B N   1 
ATOM   7780  C CA  . GLY B  1 446 ? -28.115 -45.927 -15.941  1.00 30.51  ? 446 GLY B CA  1 
ATOM   7781  C C   . GLY B  1 446 ? -26.648 -46.298 -16.010  1.00 32.55  ? 446 GLY B C   1 
ATOM   7782  O O   . GLY B  1 446 ? -26.026 -46.684 -15.007  1.00 27.20  ? 446 GLY B O   1 
ATOM   7783  N N   . SER B  1 447 ? -26.096 -46.175 -17.226  1.00 27.31  ? 447 SER B N   1 
ATOM   7784  C CA  . SER B  1 447 ? -24.728 -46.604 -17.500  1.00 28.99  ? 447 SER B CA  1 
ATOM   7785  C C   . SER B  1 447 ? -23.714 -45.741 -16.768  1.00 29.29  ? 447 SER B C   1 
ATOM   7786  O O   . SER B  1 447 ? -22.663 -46.245 -16.342  1.00 26.20  ? 447 SER B O   1 
ATOM   7787  C CB  . SER B  1 447 ? -24.445 -46.546 -19.003  1.00 26.61  ? 447 SER B CB  1 
ATOM   7788  O OG  . SER B  1 447 ? -24.282 -45.181 -19.423  1.00 29.52  ? 447 SER B OG  1 
ATOM   7789  N N   . ASP B  1 448 ? -24.012 -44.435 -16.652  1.00 24.90  ? 448 ASP B N   1 
ATOM   7790  C CA  . ASP B  1 448 ? -23.075 -43.446 -16.122  1.00 21.68  ? 448 ASP B CA  1 
ATOM   7791  C C   . ASP B  1 448 ? -22.510 -43.822 -14.760  1.00 23.71  ? 448 ASP B C   1 
ATOM   7792  O O   . ASP B  1 448 ? -21.337 -43.535 -14.480  1.00 24.73  ? 448 ASP B O   1 
ATOM   7793  C CB  . ASP B  1 448 ? -23.757 -42.080 -15.999  1.00 21.07  ? 448 ASP B CB  1 
ATOM   7794  C CG  . ASP B  1 448 ? -24.450 -41.662 -17.275  1.00 28.23  ? 448 ASP B CG  1 
ATOM   7795  O OD1 . ASP B  1 448 ? -25.578 -42.141 -17.535  1.00 25.58  ? 448 ASP B OD1 1 
ATOM   7796  O OD2 . ASP B  1 448 ? -23.862 -40.842 -18.012  1.00 31.75  ? 448 ASP B OD2 1 
ATOM   7797  N N   . TRP B  1 449 ? -23.342 -44.384 -13.866  1.00 24.54  ? 449 TRP B N   1 
ATOM   7798  C CA  . TRP B  1 449 ? -22.850 -44.694 -12.522  1.00 27.06  ? 449 TRP B CA  1 
ATOM   7799  C C   . TRP B  1 449 ? -21.749 -45.744 -12.581  1.00 23.23  ? 449 TRP B C   1 
ATOM   7800  O O   . TRP B  1 449 ? -20.769 -45.679 -11.827  1.00 23.68  ? 449 TRP B O   1 
ATOM   7801  C CB  . TRP B  1 449 ? -23.994 -45.177 -11.607  1.00 27.06  ? 449 TRP B CB  1 
ATOM   7802  C CG  . TRP B  1 449 ? -25.281 -44.421 -11.807  1.00 25.54  ? 449 TRP B CG  1 
ATOM   7803  C CD1 . TRP B  1 449 ? -26.468 -44.923 -12.265  1.00 26.70  ? 449 TRP B CD1 1 
ATOM   7804  C CD2 . TRP B  1 449 ? -25.506 -43.019 -11.567  1.00 22.89  ? 449 TRP B CD2 1 
ATOM   7805  N NE1 . TRP B  1 449 ? -27.409 -43.924 -12.342  1.00 27.81  ? 449 TRP B NE1 1 
ATOM   7806  C CE2 . TRP B  1 449 ? -26.851 -42.748 -11.900  1.00 27.23  ? 449 TRP B CE2 1 
ATOM   7807  C CE3 . TRP B  1 449 ? -24.701 -41.970 -11.103  1.00 23.28  ? 449 TRP B CE3 1 
ATOM   7808  C CZ2 . TRP B  1 449 ? -27.408 -41.462 -11.799  1.00 28.37  ? 449 TRP B CZ2 1 
ATOM   7809  C CZ3 . TRP B  1 449 ? -25.260 -40.690 -10.995  1.00 23.44  ? 449 TRP B CZ3 1 
ATOM   7810  C CH2 . TRP B  1 449 ? -26.600 -40.455 -11.337  1.00 24.28  ? 449 TRP B CH2 1 
ATOM   7811  N N   . PHE B  1 450 ? -21.900 -46.723 -13.468  1.00 20.19  ? 450 PHE B N   1 
ATOM   7812  C CA  . PHE B  1 450 ? -20.883 -47.756 -13.583  1.00 20.49  ? 450 PHE B CA  1 
ATOM   7813  C C   . PHE B  1 450 ? -19.653 -47.240 -14.319  1.00 25.12  ? 450 PHE B C   1 
ATOM   7814  O O   . PHE B  1 450 ? -18.540 -47.700 -14.047  1.00 28.41  ? 450 PHE B O   1 
ATOM   7815  C CB  . PHE B  1 450 ? -21.483 -48.995 -14.261  1.00 24.33  ? 450 PHE B CB  1 
ATOM   7816  C CG  . PHE B  1 450 ? -22.736 -49.525 -13.580  1.00 25.36  ? 450 PHE B CG  1 
ATOM   7817  C CD1 . PHE B  1 450 ? -23.982 -48.969 -13.856  1.00 30.16  ? 450 PHE B CD1 1 
ATOM   7818  C CD2 . PHE B  1 450 ? -22.662 -50.546 -12.652  1.00 29.27  ? 450 PHE B CD2 1 
ATOM   7819  C CE1 . PHE B  1 450 ? -25.126 -49.435 -13.236  1.00 27.99  ? 450 PHE B CE1 1 
ATOM   7820  C CE2 . PHE B  1 450 ? -23.814 -51.023 -12.021  1.00 28.98  ? 450 PHE B CE2 1 
ATOM   7821  C CZ  . PHE B  1 450 ? -25.046 -50.461 -12.325  1.00 29.28  ? 450 PHE B CZ  1 
ATOM   7822  N N   . TRP B  1 451 ? -19.829 -46.239 -15.194  1.00 25.79  ? 451 TRP B N   1 
ATOM   7823  C CA  . TRP B  1 451 ? -18.698 -45.657 -15.918  1.00 24.18  ? 451 TRP B CA  1 
ATOM   7824  C C   . TRP B  1 451 ? -17.676 -45.050 -14.966  1.00 26.15  ? 451 TRP B C   1 
ATOM   7825  O O   . TRP B  1 451 ? -16.472 -45.286 -15.106  1.00 29.95  ? 451 TRP B O   1 
ATOM   7826  C CB  . TRP B  1 451 ? -19.198 -44.590 -16.896  1.00 25.66  ? 451 TRP B CB  1 
ATOM   7827  C CG  . TRP B  1 451 ? -18.111 -43.748 -17.485  1.00 35.62  ? 451 TRP B CG  1 
ATOM   7828  C CD1 . TRP B  1 451 ? -17.713 -42.502 -17.081  1.00 36.90  ? 451 TRP B CD1 1 
ATOM   7829  C CD2 . TRP B  1 451 ? -17.281 -44.094 -18.594  1.00 44.31  ? 451 TRP B CD2 1 
ATOM   7830  N NE1 . TRP B  1 451 ? -16.686 -42.053 -17.877  1.00 40.63  ? 451 TRP B NE1 1 
ATOM   7831  C CE2 . TRP B  1 451 ? -16.401 -43.011 -18.814  1.00 45.99  ? 451 TRP B CE2 1 
ATOM   7832  C CE3 . TRP B  1 451 ? -17.194 -45.217 -19.425  1.00 50.31  ? 451 TRP B CE3 1 
ATOM   7833  C CZ2 . TRP B  1 451 ? -15.443 -43.023 -19.823  1.00 51.47  ? 451 TRP B CZ2 1 
ATOM   7834  C CZ3 . TRP B  1 451 ? -16.244 -45.227 -20.426  1.00 57.15  ? 451 TRP B CZ3 1 
ATOM   7835  C CH2 . TRP B  1 451 ? -15.382 -44.133 -20.621  1.00 57.09  ? 451 TRP B CH2 1 
ATOM   7836  N N   . TRP B  1 452 ? -18.141 -44.234 -14.010  1.00 27.28  ? 452 TRP B N   1 
ATOM   7837  C CA  . TRP B  1 452 ? -17.247 -43.496 -13.124  1.00 28.29  ? 452 TRP B CA  1 
ATOM   7838  C C   . TRP B  1 452 ? -16.712 -44.345 -11.975  1.00 34.26  ? 452 TRP B C   1 
ATOM   7839  O O   . TRP B  1 452 ? -15.663 -44.007 -11.404  1.00 29.54  ? 452 TRP B O   1 
ATOM   7840  C CB  . TRP B  1 452 ? -17.962 -42.263 -12.566  1.00 26.95  ? 452 TRP B CB  1 
ATOM   7841  C CG  . TRP B  1 452 ? -18.374 -41.296 -13.627  1.00 30.56  ? 452 TRP B CG  1 
ATOM   7842  C CD1 . TRP B  1 452 ? -19.634 -41.074 -14.091  1.00 29.07  ? 452 TRP B CD1 1 
ATOM   7843  C CD2 . TRP B  1 452 ? -17.509 -40.438 -14.382  1.00 28.57  ? 452 TRP B CD2 1 
ATOM   7844  N NE1 . TRP B  1 452 ? -19.611 -40.117 -15.078  1.00 30.64  ? 452 TRP B NE1 1 
ATOM   7845  C CE2 . TRP B  1 452 ? -18.317 -39.712 -15.274  1.00 30.50  ? 452 TRP B CE2 1 
ATOM   7846  C CE3 . TRP B  1 452 ? -16.131 -40.207 -14.378  1.00 26.14  ? 452 TRP B CE3 1 
ATOM   7847  C CZ2 . TRP B  1 452 ? -17.794 -38.780 -16.162  1.00 28.74  ? 452 TRP B CZ2 1 
ATOM   7848  C CZ3 . TRP B  1 452 ? -15.614 -39.282 -15.258  1.00 31.36  ? 452 TRP B CZ3 1 
ATOM   7849  C CH2 . TRP B  1 452 ? -16.444 -38.577 -16.138  1.00 29.02  ? 452 TRP B CH2 1 
ATOM   7850  N N   . GLN B  1 453 ? -17.361 -45.413 -11.663  1.00 33.26  ? 453 GLN B N   1 
ATOM   7851  C CA  . GLN B  1 453 ? -16.927 -46.245 -10.592  1.00 33.90  ? 453 GLN B CA  1 
ATOM   7852  C C   . GLN B  1 453 ? -15.675 -46.944 -10.874  1.00 42.08  ? 453 GLN B C   1 
ATOM   7853  O O   . GLN B  1 453 ? -15.474 -47.493 -11.920  1.00 43.42  ? 453 GLN B O   1 
ATOM   7854  C CB  . GLN B  1 453 ? -17.950 -47.289 -10.260  1.00 31.16  ? 453 GLN B CB  1 
ATOM   7855  C CG  . GLN B  1 453 ? -17.511 -48.362 -9.300   1.00 31.93  ? 453 GLN B CG  1 
ATOM   7856  C CD  . GLN B  1 453 ? -17.547 -47.902 -7.864   1.00 33.85  ? 453 GLN B CD  1 
ATOM   7857  O OE1 . GLN B  1 453 ? -17.514 -46.717 -7.583   1.00 32.40  ? 453 GLN B OE1 1 
ATOM   7858  N NE2 . GLN B  1 453 ? -17.609 -48.846 -6.953   1.00 33.88  ? 453 GLN B NE2 1 
ATOM   7859  N N   . GLY B  1 454 ? -14.798 -46.891 -9.932   1.00 47.99  ? 454 GLY B N   1 
ATOM   7860  C CA  . GLY B  1 454 ? -13.617 -47.697 -10.042  1.00 56.65  ? 454 GLY B CA  1 
ATOM   7861  C C   . GLY B  1 454 ? -12.725 -47.288 -11.095  1.00 64.63  ? 454 GLY B C   1 
ATOM   7862  O O   . GLY B  1 454 ? -12.316 -48.083 -11.944  1.00 67.70  ? 454 GLY B O   1 
ATOM   7863  N N   . GLU B  1 455 ? -12.515 -46.003 -11.060  1.00 67.48  ? 455 GLU B N   1 
ATOM   7864  C CA  . GLU B  1 455 ? -11.676 -45.430 -12.010  1.00 66.50  ? 455 GLU B CA  1 
ATOM   7865  C C   . GLU B  1 455 ? -10.817 -44.739 -11.018  1.00 69.26  ? 455 GLU B C   1 
ATOM   7866  O O   . GLU B  1 455 ? -10.803 -45.071 -9.861   1.00 70.38  ? 455 GLU B O   1 
ATOM   7867  C CB  . GLU B  1 455 ? -12.507 -44.497 -12.866  1.00 60.59  ? 455 GLU B CB  1 
ATOM   7868  C CG  . GLU B  1 455 ? -13.532 -45.174 -13.743  1.00 55.55  ? 455 GLU B CG  1 
ATOM   7869  C CD  . GLU B  1 455 ? -12.913 -46.006 -14.837  1.00 56.86  ? 455 GLU B CD  1 
ATOM   7870  O OE1 . GLU B  1 455 ? -11.699 -45.897 -15.039  1.00 55.39  ? 455 GLU B OE1 1 
ATOM   7871  O OE2 . GLU B  1 455 ? -13.640 -46.757 -15.503  1.00 57.92  ? 455 GLU B OE2 1 
ATOM   7872  N N   . GLU B  1 456 ? -10.157 -43.711 -11.438  1.00 70.62  ? 456 GLU B N   1 
ATOM   7873  C CA  . GLU B  1 456 ? -9.245  -43.101 -10.581  1.00 72.53  ? 456 GLU B CA  1 
ATOM   7874  C C   . GLU B  1 456 ? -9.560  -41.796 -10.078  1.00 73.97  ? 456 GLU B C   1 
ATOM   7875  O O   . GLU B  1 456 ? -10.094 -40.992 -10.807  1.00 74.73  ? 456 GLU B O   1 
ATOM   7876  C CB  . GLU B  1 456 ? -7.958  -42.843 -11.365  1.00 72.57  ? 456 GLU B CB  1 
ATOM   7877  N N   . LYS B  1 457 ? -9.241  -41.571 -8.848   1.00 74.26  ? 457 LYS B N   1 
ATOM   7878  C CA  . LYS B  1 457 ? -9.259  -40.275 -8.309   1.00 73.71  ? 457 LYS B CA  1 
ATOM   7879  C C   . LYS B  1 457 ? -9.463  -39.181 -9.259   1.00 70.46  ? 457 LYS B C   1 
ATOM   7880  O O   . LYS B  1 457 ? -8.592  -38.880 -10.052  1.00 72.53  ? 457 LYS B O   1 
ATOM   7881  C CB  . LYS B  1 457 ? -7.836  -40.070 -7.760   1.00 77.59  ? 457 LYS B CB  1 
ATOM   7882  N N   . ALA B  1 458 ? -10.602 -38.559 -9.165   1.00 64.22  ? 458 ALA B N   1 
ATOM   7883  C CA  . ALA B  1 458 ? -10.897 -37.516 -10.028  1.00 57.94  ? 458 ALA B CA  1 
ATOM   7884  C C   . ALA B  1 458 ? -11.961 -36.762 -9.275   1.00 55.97  ? 458 ALA B C   1 
ATOM   7885  O O   . ALA B  1 458 ? -12.816 -37.361 -8.663   1.00 52.32  ? 458 ALA B O   1 
ATOM   7886  C CB  . ALA B  1 458 ? -11.378 -38.066 -11.325  1.00 53.16  ? 458 ALA B CB  1 
ATOM   7887  N N   . PRO B  1 459 ? -11.886 -35.428 -9.305   1.00 53.22  ? 459 PRO B N   1 
ATOM   7888  C CA  . PRO B  1 459 ? -12.804 -34.599 -8.545   1.00 47.45  ? 459 PRO B CA  1 
ATOM   7889  C C   . PRO B  1 459 ? -14.278 -34.812 -8.850   1.00 44.83  ? 459 PRO B C   1 
ATOM   7890  O O   . PRO B  1 459 ? -14.611 -35.100 -9.991   1.00 34.22  ? 459 PRO B O   1 
ATOM   7891  C CB  . PRO B  1 459 ? -12.359 -33.196 -8.882   1.00 47.23  ? 459 PRO B CB  1 
ATOM   7892  C CG  . PRO B  1 459 ? -11.030 -33.297 -9.532   1.00 50.10  ? 459 PRO B CG  1 
ATOM   7893  C CD  . PRO B  1 459 ? -10.936 -34.654 -10.114  1.00 52.62  ? 459 PRO B CD  1 
ATOM   7894  N N   . PHE B  1 460 ? -15.102 -34.683 -7.830   1.00 41.52  ? 460 PHE B N   1 
ATOM   7895  C CA  . PHE B  1 460 ? -16.535 -34.913 -7.929   1.00 36.67  ? 460 PHE B CA  1 
ATOM   7896  C C   . PHE B  1 460 ? -17.037 -36.297 -8.217   1.00 30.36  ? 460 PHE B C   1 
ATOM   7897  O O   . PHE B  1 460 ? -18.205 -36.520 -8.143   1.00 31.94  ? 460 PHE B O   1 
ATOM   7898  C CB  . PHE B  1 460 ? -17.173 -33.885 -8.840   1.00 42.26  ? 460 PHE B CB  1 
ATOM   7899  C CG  . PHE B  1 460 ? -16.783 -32.468 -8.530   1.00 43.80  ? 460 PHE B CG  1 
ATOM   7900  C CD1 . PHE B  1 460 ? -16.966 -31.944 -7.278   1.00 46.33  ? 460 PHE B CD1 1 
ATOM   7901  C CD2 . PHE B  1 460 ? -16.234 -31.663 -9.499   1.00 47.11  ? 460 PHE B CD2 1 
ATOM   7902  C CE1 . PHE B  1 460 ? -16.613 -30.640 -6.997   1.00 48.35  ? 460 PHE B CE1 1 
ATOM   7903  C CE2 . PHE B  1 460 ? -15.874 -30.365 -9.229   1.00 47.42  ? 460 PHE B CE2 1 
ATOM   7904  C CZ  . PHE B  1 460 ? -16.063 -29.851 -7.972   1.00 49.63  ? 460 PHE B CZ  1 
ATOM   7905  N N   . VAL B  1 461 ? -16.164 -37.242 -8.412   1.00 31.93  ? 461 VAL B N   1 
ATOM   7906  C CA  . VAL B  1 461 ? -16.610 -38.624 -8.599   1.00 37.24  ? 461 VAL B CA  1 
ATOM   7907  C C   . VAL B  1 461 ? -17.455 -39.096 -7.421   1.00 42.94  ? 461 VAL B C   1 
ATOM   7908  O O   . VAL B  1 461 ? -18.402 -39.872 -7.600   1.00 48.77  ? 461 VAL B O   1 
ATOM   7909  C CB  . VAL B  1 461 ? -15.397 -39.553 -8.835   1.00 46.81  ? 461 VAL B CB  1 
ATOM   7910  C CG1 . VAL B  1 461 ? -14.489 -39.588 -7.604   1.00 47.31  ? 461 VAL B CG1 1 
ATOM   7911  C CG2 . VAL B  1 461 ? -15.863 -40.968 -9.195   1.00 47.17  ? 461 VAL B CG2 1 
ATOM   7912  N N   . GLU B  1 462 ? -17.142 -38.633 -6.205   1.00 38.25  ? 462 GLU B N   1 
ATOM   7913  C CA  . GLU B  1 462 ? -17.970 -38.966 -5.049   1.00 42.74  ? 462 GLU B CA  1 
ATOM   7914  C C   . GLU B  1 462 ? -19.420 -38.577 -5.272   1.00 38.86  ? 462 GLU B C   1 
ATOM   7915  O O   . GLU B  1 462 ? -20.323 -39.229 -4.735   1.00 36.33  ? 462 GLU B O   1 
ATOM   7916  C CB  . GLU B  1 462 ? -17.452 -38.265 -3.791   1.00 49.05  ? 462 GLU B CB  1 
ATOM   7917  C CG  . GLU B  1 462 ? -16.117 -38.760 -3.292   1.00 61.38  ? 462 GLU B CG  1 
ATOM   7918  C CD  . GLU B  1 462 ? -14.961 -38.006 -3.913   1.00 71.15  ? 462 GLU B CD  1 
ATOM   7919  O OE1 . GLU B  1 462 ? -13.800 -38.409 -3.674   1.00 74.55  ? 462 GLU B OE1 1 
ATOM   7920  O OE2 . GLU B  1 462 ? -15.218 -37.016 -4.641   1.00 70.31  ? 462 GLU B OE2 1 
ATOM   7921  N N   . VAL B  1 463 ? -19.666 -37.513 -6.047   1.00 33.79  ? 463 VAL B N   1 
ATOM   7922  C CA  . VAL B  1 463 ? -21.043 -37.089 -6.245   1.00 32.44  ? 463 VAL B CA  1 
ATOM   7923  C C   . VAL B  1 463 ? -21.820 -38.159 -6.997   1.00 30.81  ? 463 VAL B C   1 
ATOM   7924  O O   . VAL B  1 463 ? -22.964 -38.465 -6.639   1.00 29.35  ? 463 VAL B O   1 
ATOM   7925  C CB  . VAL B  1 463 ? -21.110 -35.720 -6.947   1.00 32.90  ? 463 VAL B CB  1 
ATOM   7926  C CG1 . VAL B  1 463 ? -22.550 -35.309 -7.118   1.00 30.65  ? 463 VAL B CG1 1 
ATOM   7927  C CG2 . VAL B  1 463 ? -20.344 -34.650 -6.149   1.00 31.11  ? 463 VAL B CG2 1 
ATOM   7928  N N   . PHE B  1 464 ? -21.205 -38.771 -8.030   1.00 33.26  ? 464 PHE B N   1 
ATOM   7929  C CA  . PHE B  1 464 ? -21.882 -39.840 -8.766   1.00 28.89  ? 464 PHE B CA  1 
ATOM   7930  C C   . PHE B  1 464 ? -22.189 -41.021 -7.854   1.00 27.63  ? 464 PHE B C   1 
ATOM   7931  O O   . PHE B  1 464 ? -23.269 -41.621 -7.936   1.00 25.39  ? 464 PHE B O   1 
ATOM   7932  C CB  . PHE B  1 464 ? -21.040 -40.284 -9.978   1.00 29.44  ? 464 PHE B CB  1 
ATOM   7933  C CG  . PHE B  1 464 ? -20.921 -39.212 -11.050  1.00 28.15  ? 464 PHE B CG  1 
ATOM   7934  C CD1 . PHE B  1 464 ? -21.884 -39.094 -12.046  1.00 30.01  ? 464 PHE B CD1 1 
ATOM   7935  C CD2 . PHE B  1 464 ? -19.868 -38.301 -11.031  1.00 28.92  ? 464 PHE B CD2 1 
ATOM   7936  C CE1 . PHE B  1 464 ? -21.800 -38.088 -13.026  1.00 29.81  ? 464 PHE B CE1 1 
ATOM   7937  C CE2 . PHE B  1 464 ? -19.774 -37.293 -11.999  1.00 30.25  ? 464 PHE B CE2 1 
ATOM   7938  C CZ  . PHE B  1 464 ? -20.742 -37.194 -13.005  1.00 25.71  ? 464 PHE B CZ  1 
ATOM   7939  N N   . ASP B  1 465 ? -21.243 -41.369 -6.981   1.00 24.85  ? 465 ASP B N   1 
ATOM   7940  C CA  . ASP B  1 465 ? -21.461 -42.449 -6.026   1.00 28.91  ? 465 ASP B CA  1 
ATOM   7941  C C   . ASP B  1 465 ? -22.584 -42.118 -5.048   1.00 28.35  ? 465 ASP B C   1 
ATOM   7942  O O   . ASP B  1 465 ? -23.435 -42.968 -4.759   1.00 29.77  ? 465 ASP B O   1 
ATOM   7943  C CB  . ASP B  1 465 ? -20.168 -42.737 -5.263   1.00 28.07  ? 465 ASP B CB  1 
ATOM   7944  C CG  . ASP B  1 465 ? -20.368 -43.745 -4.162   1.00 28.58  ? 465 ASP B CG  1 
ATOM   7945  O OD1 . ASP B  1 465 ? -20.464 -44.954 -4.473   1.00 32.00  ? 465 ASP B OD1 1 
ATOM   7946  O OD2 . ASP B  1 465 ? -20.435 -43.314 -2.988   1.00 33.86  ? 465 ASP B OD2 1 
ATOM   7947  N N   . LYS B  1 466 ? -22.595 -40.894 -4.514   1.00 30.61  ? 466 LYS B N   1 
ATOM   7948  C CA  . LYS B  1 466 ? -23.701 -40.470 -3.658   1.00 32.27  ? 466 LYS B CA  1 
ATOM   7949  C C   . LYS B  1 466 ? -25.030 -40.573 -4.390   1.00 30.98  ? 466 LYS B C   1 
ATOM   7950  O O   . LYS B  1 466 ? -26.025 -41.059 -3.833   1.00 32.92  ? 466 LYS B O   1 
ATOM   7951  C CB  . LYS B  1 466 ? -23.479 -39.037 -3.178   1.00 34.77  ? 466 LYS B CB  1 
ATOM   7952  C CG  . LYS B  1 466 ? -24.557 -38.538 -2.230   1.00 41.16  ? 466 LYS B CG  1 
ATOM   7953  C CD  . LYS B  1 466 ? -24.240 -37.145 -1.728   1.00 44.30  ? 466 LYS B CD  1 
ATOM   7954  C CE  . LYS B  1 466 ? -24.926 -36.863 -0.403   1.00 50.49  ? 466 LYS B CE  1 
ATOM   7955  N NZ  . LYS B  1 466 ? -24.220 -35.791 0.347    1.00 55.84  ? 466 LYS B NZ  1 
ATOM   7956  N N   . LEU B  1 467 ? -25.064 -40.111 -5.639   1.00 25.25  ? 467 LEU B N   1 
ATOM   7957  C CA  . LEU B  1 467 ? -26.295 -40.178 -6.417   1.00 25.95  ? 467 LEU B CA  1 
ATOM   7958  C C   . LEU B  1 467 ? -26.734 -41.615 -6.635   1.00 26.41  ? 467 LEU B C   1 
ATOM   7959  O O   . LEU B  1 467 ? -27.880 -41.966 -6.340   1.00 29.64  ? 467 LEU B O   1 
ATOM   7960  C CB  . LEU B  1 467 ? -26.109 -39.479 -7.762   1.00 27.47  ? 467 LEU B CB  1 
ATOM   7961  C CG  . LEU B  1 467 ? -26.086 -37.952 -7.706   1.00 23.81  ? 467 LEU B CG  1 
ATOM   7962  C CD1 . LEU B  1 467 ? -25.632 -37.435 -9.040   1.00 24.95  ? 467 LEU B CD1 1 
ATOM   7963  C CD2 . LEU B  1 467 ? -27.457 -37.420 -7.366   1.00 27.25  ? 467 LEU B CD2 1 
ATOM   7964  N N   . PHE B  1 468 ? -25.841 -42.452 -7.190   1.00 22.36  ? 468 PHE B N   1 
ATOM   7965  C CA  . PHE B  1 468 ? -26.180 -43.854 -7.434   1.00 24.05  ? 468 PHE B CA  1 
ATOM   7966  C C   . PHE B  1 468 ? -26.793 -44.483 -6.184   1.00 24.59  ? 468 PHE B C   1 
ATOM   7967  O O   . PHE B  1 468 ? -27.898 -45.032 -6.224   1.00 26.92  ? 468 PHE B O   1 
ATOM   7968  C CB  . PHE B  1 468 ? -24.935 -44.631 -7.867   1.00 21.66  ? 468 PHE B CB  1 
ATOM   7969  C CG  . PHE B  1 468 ? -25.140 -46.136 -7.974   1.00 26.00  ? 468 PHE B CG  1 
ATOM   7970  C CD1 . PHE B  1 468 ? -25.869 -46.682 -9.032   1.00 23.30  ? 468 PHE B CD1 1 
ATOM   7971  C CD2 . PHE B  1 468 ? -24.568 -46.998 -7.046   1.00 28.34  ? 468 PHE B CD2 1 
ATOM   7972  C CE1 . PHE B  1 468 ? -26.040 -48.047 -9.146   1.00 29.59  ? 468 PHE B CE1 1 
ATOM   7973  C CE2 . PHE B  1 468 ? -24.739 -48.381 -7.156   1.00 26.78  ? 468 PHE B CE2 1 
ATOM   7974  C CZ  . PHE B  1 468 ? -25.476 -48.902 -8.203   1.00 30.25  ? 468 PHE B CZ  1 
ATOM   7975  N N   . ARG B  1 469 ? -26.093 -44.376 -5.059   1.00 22.46  ? 469 ARG B N   1 
ATOM   7976  C CA  . ARG B  1 469 ? -26.539 -45.052 -3.842   1.00 27.73  ? 469 ARG B CA  1 
ATOM   7977  C C   . ARG B  1 469 ? -27.792 -44.421 -3.248   1.00 29.54  ? 469 ARG B C   1 
ATOM   7978  O O   . ARG B  1 469 ? -28.568 -45.118 -2.577   1.00 32.16  ? 469 ARG B O   1 
ATOM   7979  C CB  . ARG B  1 469 ? -25.410 -45.072 -2.815   1.00 25.68  ? 469 ARG B CB  1 
ATOM   7980  C CG  . ARG B  1 469 ? -24.220 -45.919 -3.256   1.00 28.60  ? 469 ARG B CG  1 
ATOM   7981  C CD  . ARG B  1 469 ? -23.055 -45.742 -2.295   1.00 28.92  ? 469 ARG B CD  1 
ATOM   7982  N NE  . ARG B  1 469 ? -21.902 -46.577 -2.633   1.00 27.53  ? 469 ARG B NE  1 
ATOM   7983  C CZ  . ARG B  1 469 ? -21.717 -47.802 -2.162   1.00 30.51  ? 469 ARG B CZ  1 
ATOM   7984  N NH1 . ARG B  1 469 ? -22.614 -48.345 -1.339   1.00 29.81  ? 469 ARG B NH1 1 
ATOM   7985  N NH2 . ARG B  1 469 ? -20.628 -48.479 -2.488   1.00 31.09  ? 469 ARG B NH2 1 
ATOM   7986  N N   . SER B  1 470 ? -28.005 -43.118 -3.460   1.00 31.02  ? 470 SER B N   1 
ATOM   7987  C CA  . SER B  1 470 ? -29.256 -42.502 -3.027   1.00 32.67  ? 470 SER B CA  1 
ATOM   7988  C C   . SER B  1 470 ? -30.440 -43.050 -3.820   1.00 35.68  ? 470 SER B C   1 
ATOM   7989  O O   . SER B  1 470 ? -31.500 -43.321 -3.244   1.00 35.54  ? 470 SER B O   1 
ATOM   7990  C CB  . SER B  1 470 ? -29.178 -40.980 -3.167   1.00 34.55  ? 470 SER B CB  1 
ATOM   7991  O OG  . SER B  1 470 ? -28.425 -40.383 -2.118   1.00 40.40  ? 470 SER B OG  1 
ATOM   7992  N N   . PHE B  1 471 ? -30.273 -43.211 -5.145   1.00 33.16  ? 471 PHE B N   1 
ATOM   7993  C CA  . PHE B  1 471 ? -31.326 -43.764 -6.001   1.00 29.07  ? 471 PHE B CA  1 
ATOM   7994  C C   . PHE B  1 471 ? -31.613 -45.220 -5.660   1.00 29.71  ? 471 PHE B C   1 
ATOM   7995  O O   . PHE B  1 471 ? -32.768 -45.664 -5.711   1.00 31.22  ? 471 PHE B O   1 
ATOM   7996  C CB  . PHE B  1 471 ? -30.926 -43.655 -7.479   1.00 31.36  ? 471 PHE B CB  1 
ATOM   7997  C CG  . PHE B  1 471 ? -30.865 -42.244 -8.007   1.00 29.21  ? 471 PHE B CG  1 
ATOM   7998  C CD1 . PHE B  1 471 ? -31.893 -41.351 -7.776   1.00 28.99  ? 471 PHE B CD1 1 
ATOM   7999  C CD2 . PHE B  1 471 ? -29.771 -41.821 -8.750   1.00 32.07  ? 471 PHE B CD2 1 
ATOM   8000  C CE1 . PHE B  1 471 ? -31.837 -40.072 -8.260   1.00 32.97  ? 471 PHE B CE1 1 
ATOM   8001  C CE2 . PHE B  1 471 ? -29.703 -40.531 -9.240   1.00 34.93  ? 471 PHE B CE2 1 
ATOM   8002  C CZ  . PHE B  1 471 ? -30.740 -39.655 -9.000   1.00 30.90  ? 471 PHE B CZ  1 
ATOM   8003  N N   . VAL B  1 472 ? -30.564 -45.981 -5.340   1.00 27.12  ? 472 VAL B N   1 
ATOM   8004  C CA  . VAL B  1 472 ? -30.726 -47.369 -4.900   1.00 30.62  ? 472 VAL B CA  1 
ATOM   8005  C C   . VAL B  1 472 ? -31.534 -47.427 -3.606   1.00 35.36  ? 472 VAL B C   1 
ATOM   8006  O O   . VAL B  1 472 ? -32.435 -48.263 -3.441   1.00 32.29  ? 472 VAL B O   1 
ATOM   8007  C CB  . VAL B  1 472 ? -29.344 -48.029 -4.717   1.00 36.04  ? 472 VAL B CB  1 
ATOM   8008  C CG1 . VAL B  1 472 ? -29.438 -49.212 -3.788   1.00 40.81  ? 472 VAL B CG1 1 
ATOM   8009  C CG2 . VAL B  1 472 ? -28.727 -48.444 -6.074   1.00 34.21  ? 472 VAL B CG2 1 
ATOM   8010  N N   . ARG B  1 473 ? -31.200 -46.556 -2.657   1.00 36.49  ? 473 ARG B N   1 
ATOM   8011  C CA  . ARG B  1 473 ? -31.938 -46.512 -1.398   1.00 38.57  ? 473 ARG B CA  1 
ATOM   8012  C C   . ARG B  1 473 ? -33.393 -46.145 -1.645   1.00 35.39  ? 473 ARG B C   1 
ATOM   8013  O O   . ARG B  1 473 ? -34.307 -46.850 -1.211   1.00 37.51  ? 473 ARG B O   1 
ATOM   8014  C CB  . ARG B  1 473 ? -31.278 -45.519 -0.445   1.00 49.39  ? 473 ARG B CB  1 
ATOM   8015  C CG  . ARG B  1 473 ? -31.217 -45.962 1.013    1.00 62.31  ? 473 ARG B CG  1 
ATOM   8016  C CD  . ARG B  1 473 ? -29.856 -45.620 1.635    1.00 74.53  ? 473 ARG B CD  1 
ATOM   8017  N NE  . ARG B  1 473 ? -28.771 -46.487 1.155    1.00 81.46  ? 473 ARG B NE  1 
ATOM   8018  C CZ  . ARG B  1 473 ? -27.479 -46.156 1.163    1.00 83.62  ? 473 ARG B CZ  1 
ATOM   8019  N NH1 . ARG B  1 473 ? -27.095 -44.965 1.613    1.00 84.64  ? 473 ARG B NH1 1 
ATOM   8020  N NH2 . ARG B  1 473 ? -26.570 -47.017 0.712    1.00 81.13  ? 473 ARG B NH2 1 
ATOM   8021  N N   . ARG B  1 474 ? -33.624 -45.078 -2.408   1.00 36.78  ? 474 ARG B N   1 
ATOM   8022  C CA  . ARG B  1 474 ? -34.985 -44.596 -2.609   1.00 41.47  ? 474 ARG B CA  1 
ATOM   8023  C C   . ARG B  1 474 ? -35.841 -45.611 -3.358   1.00 39.14  ? 474 ARG B C   1 
ATOM   8024  O O   . ARG B  1 474 ? -37.067 -45.629 -3.189   1.00 36.84  ? 474 ARG B O   1 
ATOM   8025  C CB  . ARG B  1 474 ? -34.944 -43.248 -3.331   1.00 47.26  ? 474 ARG B CB  1 
ATOM   8026  C CG  . ARG B  1 474 ? -36.303 -42.656 -3.675   1.00 56.53  ? 474 ARG B CG  1 
ATOM   8027  C CD  . ARG B  1 474 ? -37.065 -42.112 -2.471   1.00 64.95  ? 474 ARG B CD  1 
ATOM   8028  N NE  . ARG B  1 474 ? -38.509 -42.268 -2.669   1.00 73.67  ? 474 ARG B NE  1 
ATOM   8029  C CZ  . ARG B  1 474 ? -39.244 -41.514 -3.487   1.00 77.33  ? 474 ARG B CZ  1 
ATOM   8030  N NH1 . ARG B  1 474 ? -38.680 -40.532 -4.178   1.00 80.17  ? 474 ARG B NH1 1 
ATOM   8031  N NH2 . ARG B  1 474 ? -40.548 -41.738 -3.613   1.00 76.15  ? 474 ARG B NH2 1 
ATOM   8032  N N   . ALA B  1 475 ? -35.218 -46.485 -4.152   1.00 34.85  ? 475 ALA B N   1 
ATOM   8033  C CA  . ALA B  1 475 ? -35.979 -47.477 -4.896   1.00 38.55  ? 475 ALA B CA  1 
ATOM   8034  C C   . ALA B  1 475 ? -36.557 -48.564 -4.002   1.00 41.60  ? 475 ALA B C   1 
ATOM   8035  O O   . ALA B  1 475 ? -37.432 -49.314 -4.450   1.00 41.73  ? 475 ALA B O   1 
ATOM   8036  C CB  . ALA B  1 475 ? -35.105 -48.123 -5.971   1.00 34.29  ? 475 ALA B CB  1 
ATOM   8037  N N   . GLN B  1 476 ? -36.080 -48.681 -2.764   1.00 45.31  ? 476 GLN B N   1 
ATOM   8038  C CA  . GLN B  1 476 ? -36.511 -49.739 -1.863   1.00 47.88  ? 476 GLN B CA  1 
ATOM   8039  C C   . GLN B  1 476 ? -37.499 -49.260 -0.813   1.00 51.75  ? 476 GLN B C   1 
ATOM   8040  O O   . GLN B  1 476 ? -37.819 -50.020 0.106    1.00 53.59  ? 476 GLN B O   1 
ATOM   8041  C CB  . GLN B  1 476 ? -35.297 -50.378 -1.189   1.00 46.14  ? 476 GLN B CB  1 
ATOM   8042  C CG  . GLN B  1 476 ? -34.260 -50.824 -2.196   1.00 41.94  ? 476 GLN B CG  1 
ATOM   8043  C CD  . GLN B  1 476 ? -33.035 -51.389 -1.541   1.00 40.74  ? 476 GLN B CD  1 
ATOM   8044  O OE1 . GLN B  1 476 ? -33.065 -52.493 -0.996   1.00 46.28  ? 476 GLN B OE1 1 
ATOM   8045  N NE2 . GLN B  1 476 ? -31.940 -50.646 -1.595   1.00 37.86  ? 476 GLN B NE2 1 
ATOM   8046  N N   . GLU B  1 477 ? -38.001 -48.033 -0.936   1.00 57.94  ? 477 GLU B N   1 
ATOM   8047  C CA  . GLU B  1 477 ? -38.941 -47.466 0.030    1.00 65.45  ? 477 GLU B CA  1 
ATOM   8048  C C   . GLU B  1 477 ? -40.357 -47.406 -0.539   1.00 68.69  ? 477 GLU B C   1 
ATOM   8049  O O   . GLU B  1 477 ? -40.542 -47.136 -1.727   1.00 69.72  ? 477 GLU B O   1 
ATOM   8050  C CB  . GLU B  1 477 ? -38.491 -46.064 0.450    1.00 67.82  ? 477 GLU B CB  1 
ATOM   8051  C CG  . GLU B  1 477 ? -36.985 -45.922 0.584    1.00 68.02  ? 477 GLU B CG  1 
ATOM   8052  C CD  . GLU B  1 477 ? -36.574 -44.864 1.581    1.00 69.99  ? 477 GLU B CD  1 
ATOM   8053  O OE1 . GLU B  1 477 ? -36.046 -45.256 2.638    1.00 73.97  ? 477 GLU B OE1 1 
ATOM   8054  O OE2 . GLU B  1 477 ? -36.763 -43.654 1.309    1.00 68.64  ? 477 GLU B OE2 1 
ATOM   8055  N N   . LYS C  1 2   ? -1.448  -14.433 -34.677  1.00 49.05  ? 2   LYS C N   1 
ATOM   8056  C CA  . LYS C  1 2   ? -1.194  -13.300 -35.550  1.00 53.21  ? 2   LYS C CA  1 
ATOM   8057  C C   . LYS C  1 2   ? -0.941  -13.780 -36.969  1.00 50.75  ? 2   LYS C C   1 
ATOM   8058  O O   . LYS C  1 2   ? 0.129   -14.297 -37.255  1.00 53.46  ? 2   LYS C O   1 
ATOM   8059  C CB  . LYS C  1 2   ? 0.004   -12.477 -35.057  1.00 60.73  ? 2   LYS C CB  1 
ATOM   8060  C CG  . LYS C  1 2   ? 0.198   -11.187 -35.867  1.00 64.20  ? 2   LYS C CG  1 
ATOM   8061  C CD  . LYS C  1 2   ? 1.601   -11.076 -36.464  1.00 65.81  ? 2   LYS C CD  1 
ATOM   8062  C CE  . LYS C  1 2   ? 2.594   -10.574 -35.426  1.00 70.20  ? 2   LYS C CE  1 
ATOM   8063  N NZ  . LYS C  1 2   ? 3.961   -10.348 -35.990  1.00 69.11  ? 2   LYS C NZ  1 
ATOM   8064  N N   . LYS C  1 3   ? -1.916  -13.589 -37.857  1.00 48.56  ? 3   LYS C N   1 
ATOM   8065  C CA  . LYS C  1 3   ? -1.872  -14.119 -39.212  1.00 44.81  ? 3   LYS C CA  1 
ATOM   8066  C C   . LYS C  1 3   ? -1.385  -13.065 -40.205  1.00 44.95  ? 3   LYS C C   1 
ATOM   8067  O O   . LYS C  1 3   ? -1.555  -11.860 -40.007  1.00 44.78  ? 3   LYS C O   1 
ATOM   8068  C CB  . LYS C  1 3   ? -3.256  -14.610 -39.659  1.00 43.56  ? 3   LYS C CB  1 
ATOM   8069  C CG  . LYS C  1 3   ? -4.033  -15.422 -38.651  1.00 48.36  ? 3   LYS C CG  1 
ATOM   8070  C CD  . LYS C  1 3   ? -3.778  -16.897 -38.816  1.00 52.65  ? 3   LYS C CD  1 
ATOM   8071  C CE  . LYS C  1 3   ? -4.743  -17.725 -37.984  1.00 58.23  ? 3   LYS C CE  1 
ATOM   8072  N NZ  . LYS C  1 3   ? -4.055  -18.794 -37.202  1.00 62.81  ? 3   LYS C NZ  1 
ATOM   8073  N N   . LEU C  1 4   ? -0.777  -13.541 -41.283  1.00 47.91  ? 4   LEU C N   1 
ATOM   8074  C CA  . LEU C  1 4   ? -0.569  -12.746 -42.483  1.00 43.36  ? 4   LEU C CA  1 
ATOM   8075  C C   . LEU C  1 4   ? -1.715  -13.071 -43.423  1.00 42.22  ? 4   LEU C C   1 
ATOM   8076  O O   . LEU C  1 4   ? -2.057  -14.246 -43.600  1.00 42.04  ? 4   LEU C O   1 
ATOM   8077  C CB  . LEU C  1 4   ? 0.779   -13.058 -43.141  1.00 44.69  ? 4   LEU C CB  1 
ATOM   8078  C CG  . LEU C  1 4   ? 1.098   -12.405 -44.498  1.00 39.51  ? 4   LEU C CG  1 
ATOM   8079  C CD1 . LEU C  1 4   ? 2.587   -12.094 -44.611  1.00 38.59  ? 4   LEU C CD1 1 
ATOM   8080  C CD2 . LEU C  1 4   ? 0.660   -13.300 -45.659  1.00 34.26  ? 4   LEU C CD2 1 
ATOM   8081  N N   . PHE C  1 5   ? -2.319  -12.036 -43.999  1.00 42.49  ? 5   PHE C N   1 
ATOM   8082  C CA  . PHE C  1 5   ? -3.456  -12.191 -44.896  1.00 37.68  ? 5   PHE C CA  1 
ATOM   8083  C C   . PHE C  1 5   ? -2.970  -12.060 -46.338  1.00 39.46  ? 5   PHE C C   1 
ATOM   8084  O O   . PHE C  1 5   ? -2.421  -11.023 -46.729  1.00 37.43  ? 5   PHE C O   1 
ATOM   8085  C CB  . PHE C  1 5   ? -4.544  -11.163 -44.576  1.00 36.84  ? 5   PHE C CB  1 
ATOM   8086  C CG  . PHE C  1 5   ? -5.198  -11.369 -43.213  1.00 42.86  ? 5   PHE C CG  1 
ATOM   8087  C CD1 . PHE C  1 5   ? -5.750  -12.590 -42.875  1.00 39.52  ? 5   PHE C CD1 1 
ATOM   8088  C CD2 . PHE C  1 5   ? -5.254  -10.346 -42.292  1.00 44.04  ? 5   PHE C CD2 1 
ATOM   8089  C CE1 . PHE C  1 5   ? -6.355  -12.789 -41.654  1.00 45.04  ? 5   PHE C CE1 1 
ATOM   8090  C CE2 . PHE C  1 5   ? -5.861  -10.535 -41.047  1.00 47.73  ? 5   PHE C CE2 1 
ATOM   8091  C CZ  . PHE C  1 5   ? -6.407  -11.761 -40.731  1.00 49.75  ? 5   PHE C CZ  1 
ATOM   8092  N N   . LEU C  1 6   ? -3.180  -13.110 -47.118  1.00 37.47  ? 6   LEU C N   1 
ATOM   8093  C CA  . LEU C  1 6   ? -2.662  -13.220 -48.472  1.00 34.41  ? 6   LEU C CA  1 
ATOM   8094  C C   . LEU C  1 6   ? -3.844  -13.186 -49.434  1.00 30.43  ? 6   LEU C C   1 
ATOM   8095  O O   . LEU C  1 6   ? -4.836  -13.889 -49.227  1.00 31.21  ? 6   LEU C O   1 
ATOM   8096  C CB  . LEU C  1 6   ? -1.840  -14.514 -48.617  1.00 32.34  ? 6   LEU C CB  1 
ATOM   8097  C CG  . LEU C  1 6   ? -1.139  -14.737 -49.972  1.00 35.08  ? 6   LEU C CG  1 
ATOM   8098  C CD1 . LEU C  1 6   ? -0.202  -13.587 -50.327  1.00 30.74  ? 6   LEU C CD1 1 
ATOM   8099  C CD2 . LEU C  1 6   ? -0.379  -16.044 -49.976  1.00 34.07  ? 6   LEU C CD2 1 
ATOM   8100  N N   . VAL C  1 7   ? -3.770  -12.343 -50.458  1.00 31.10  ? 7   VAL C N   1 
ATOM   8101  C CA  . VAL C  1 7   ? -4.885  -12.176 -51.380  1.00 30.67  ? 7   VAL C CA  1 
ATOM   8102  C C   . VAL C  1 7   ? -4.357  -12.330 -52.802  1.00 31.13  ? 7   VAL C C   1 
ATOM   8103  O O   . VAL C  1 7   ? -3.657  -11.446 -53.310  1.00 33.72  ? 7   VAL C O   1 
ATOM   8104  C CB  . VAL C  1 7   ? -5.589  -10.822 -51.193  1.00 29.49  ? 7   VAL C CB  1 
ATOM   8105  C CG1 . VAL C  1 7   ? -6.819  -10.714 -52.102  1.00 30.75  ? 7   VAL C CG1 1 
ATOM   8106  C CG2 . VAL C  1 7   ? -5.990  -10.611 -49.720  1.00 33.87  ? 7   VAL C CG2 1 
ATOM   8107  N N   . PHE C  1 8   ? -4.680  -13.448 -53.445  1.00 30.30  ? 8   PHE C N   1 
ATOM   8108  C CA  . PHE C  1 8   ? -4.365  -13.599 -54.864  1.00 29.80  ? 8   PHE C CA  1 
ATOM   8109  C C   . PHE C  1 8   ? -5.507  -13.022 -55.690  1.00 26.88  ? 8   PHE C C   1 
ATOM   8110  O O   . PHE C  1 8   ? -6.684  -13.260 -55.396  1.00 27.10  ? 8   PHE C O   1 
ATOM   8111  C CB  . PHE C  1 8   ? -4.146  -15.063 -55.244  1.00 29.37  ? 8   PHE C CB  1 
ATOM   8112  C CG  . PHE C  1 8   ? -2.848  -15.632 -54.748  1.00 32.30  ? 8   PHE C CG  1 
ATOM   8113  C CD1 . PHE C  1 8   ? -1.677  -15.476 -55.476  1.00 33.30  ? 8   PHE C CD1 1 
ATOM   8114  C CD2 . PHE C  1 8   ? -2.798  -16.307 -53.543  1.00 30.64  ? 8   PHE C CD2 1 
ATOM   8115  C CE1 . PHE C  1 8   ? -0.482  -15.991 -55.025  1.00 32.01  ? 8   PHE C CE1 1 
ATOM   8116  C CE2 . PHE C  1 8   ? -1.604  -16.829 -53.081  1.00 33.53  ? 8   PHE C CE2 1 
ATOM   8117  C CZ  . PHE C  1 8   ? -0.441  -16.668 -53.811  1.00 32.93  ? 8   PHE C CZ  1 
ATOM   8118  N N   . TRP C  1 9   ? -5.156  -12.265 -56.726  1.00 25.45  ? 9   TRP C N   1 
ATOM   8119  C CA  . TRP C  1 9   ? -6.148  -11.710 -57.652  1.00 26.46  ? 9   TRP C CA  1 
ATOM   8120  C C   . TRP C  1 9   ? -5.594  -11.898 -59.061  1.00 26.07  ? 9   TRP C C   1 
ATOM   8121  O O   . TRP C  1 9   ? -4.677  -11.184 -59.476  1.00 25.54  ? 9   TRP C O   1 
ATOM   8122  C CB  . TRP C  1 9   ? -6.426  -10.244 -57.323  1.00 24.28  ? 9   TRP C CB  1 
ATOM   8123  C CG  . TRP C  1 9   ? -7.698  -9.637  -57.879  1.00 23.11  ? 9   TRP C CG  1 
ATOM   8124  C CD1 . TRP C  1 9   ? -8.584  -10.200 -58.764  1.00 25.62  ? 9   TRP C CD1 1 
ATOM   8125  C CD2 . TRP C  1 9   ? -8.196  -8.316  -57.604  1.00 21.92  ? 9   TRP C CD2 1 
ATOM   8126  N NE1 . TRP C  1 9   ? -9.600  -9.309  -59.044  1.00 24.43  ? 9   TRP C NE1 1 
ATOM   8127  C CE2 . TRP C  1 9   ? -9.387  -8.153  -58.341  1.00 22.36  ? 9   TRP C CE2 1 
ATOM   8128  C CE3 . TRP C  1 9   ? -7.757  -7.266  -56.787  1.00 24.89  ? 9   TRP C CE3 1 
ATOM   8129  C CZ2 . TRP C  1 9   ? -10.136 -6.984  -58.294  1.00 23.63  ? 9   TRP C CZ2 1 
ATOM   8130  C CZ3 . TRP C  1 9   ? -8.507  -6.113  -56.734  1.00 29.57  ? 9   TRP C CZ3 1 
ATOM   8131  C CH2 . TRP C  1 9   ? -9.684  -5.978  -57.487  1.00 29.15  ? 9   TRP C CH2 1 
ATOM   8132  N N   . TRP C  1 10  ? -6.131  -12.884 -59.775  1.00 23.33  ? 10  TRP C N   1 
ATOM   8133  C CA  . TRP C  1 10  ? -5.627  -13.271 -61.085  1.00 25.25  ? 10  TRP C CA  1 
ATOM   8134  C C   . TRP C  1 10  ? -6.458  -12.567 -62.140  1.00 23.08  ? 10  TRP C C   1 
ATOM   8135  O O   . TRP C  1 10  ? -7.664  -12.803 -62.235  1.00 27.60  ? 10  TRP C O   1 
ATOM   8136  C CB  . TRP C  1 10  ? -5.719  -14.782 -61.286  1.00 21.85  ? 10  TRP C CB  1 
ATOM   8137  C CG  . TRP C  1 10  ? -4.938  -15.621 -60.342  1.00 28.90  ? 10  TRP C CG  1 
ATOM   8138  C CD1 . TRP C  1 10  ? -5.433  -16.462 -59.386  1.00 29.43  ? 10  TRP C CD1 1 
ATOM   8139  C CD2 . TRP C  1 10  ? -3.510  -15.745 -60.288  1.00 30.67  ? 10  TRP C CD2 1 
ATOM   8140  N NE1 . TRP C  1 10  ? -4.400  -17.094 -58.738  1.00 30.37  ? 10  TRP C NE1 1 
ATOM   8141  C CE2 . TRP C  1 10  ? -3.211  -16.672 -59.273  1.00 30.55  ? 10  TRP C CE2 1 
ATOM   8142  C CE3 . TRP C  1 10  ? -2.456  -15.155 -60.994  1.00 28.69  ? 10  TRP C CE3 1 
ATOM   8143  C CZ2 . TRP C  1 10  ? -1.898  -17.030 -58.946  1.00 31.80  ? 10  TRP C CZ2 1 
ATOM   8144  C CZ3 . TRP C  1 10  ? -1.144  -15.532 -60.674  1.00 27.17  ? 10  TRP C CZ3 1 
ATOM   8145  C CH2 . TRP C  1 10  ? -0.884  -16.442 -59.649  1.00 27.04  ? 10  TRP C CH2 1 
ATOM   8146  N N   . HIS C  1 11  ? -5.821  -11.728 -62.943  1.00 24.02  ? 11  HIS C N   1 
ATOM   8147  C CA  . HIS C  1 11  ? -6.525  -10.902 -63.921  1.00 25.78  ? 11  HIS C CA  1 
ATOM   8148  C C   . HIS C  1 11  ? -6.536  -11.599 -65.284  1.00 23.55  ? 11  HIS C C   1 
ATOM   8149  O O   . HIS C  1 11  ? -5.476  -11.919 -65.824  1.00 27.26  ? 11  HIS C O   1 
ATOM   8150  C CB  . HIS C  1 11  ? -5.856  -9.529  -63.999  1.00 23.64  ? 11  HIS C CB  1 
ATOM   8151  C CG  . HIS C  1 11  ? -6.231  -8.720  -65.206  1.00 28.45  ? 11  HIS C CG  1 
ATOM   8152  N ND1 . HIS C  1 11  ? -7.525  -8.335  -65.475  1.00 27.25  ? 11  HIS C ND1 1 
ATOM   8153  C CD2 . HIS C  1 11  ? -5.467  -8.190  -66.193  1.00 29.26  ? 11  HIS C CD2 1 
ATOM   8154  C CE1 . HIS C  1 11  ? -7.545  -7.611  -66.584  1.00 29.71  ? 11  HIS C CE1 1 
ATOM   8155  N NE2 . HIS C  1 11  ? -6.309  -7.506  -67.035  1.00 28.52  ? 11  HIS C NE2 1 
ATOM   8156  N N   . MET C  1 12  ? -7.731  -11.805 -65.848  1.00 26.91  ? 12  MET C N   1 
ATOM   8157  C CA  . MET C  1 12  ? -7.918  -12.478 -67.133  1.00 24.69  ? 12  MET C CA  1 
ATOM   8158  C C   . MET C  1 12  ? -8.544  -11.516 -68.135  1.00 25.36  ? 12  MET C C   1 
ATOM   8159  O O   . MET C  1 12  ? -9.573  -10.897 -67.843  1.00 22.81  ? 12  MET C O   1 
ATOM   8160  C CB  . MET C  1 12  ? -8.819  -13.705 -66.979  1.00 23.40  ? 12  MET C CB  1 
ATOM   8161  C CG  . MET C  1 12  ? -8.486  -14.601 -65.779  1.00 27.14  ? 12  MET C CG  1 
ATOM   8162  S SD  . MET C  1 12  ? -6.831  -15.297 -65.937  1.00 24.23  ? 12  MET C SD  1 
ATOM   8163  C CE  . MET C  1 12  ? -6.980  -16.726 -64.870  1.00 27.47  ? 12  MET C CE  1 
ATOM   8164  N N   . HIS C  1 13  ? -7.953  -11.415 -69.327  1.00 26.06  ? 13  HIS C N   1 
ATOM   8165  C CA  . HIS C  1 13  ? -8.418  -10.414 -70.272  1.00 22.33  ? 13  HIS C CA  1 
ATOM   8166  C C   . HIS C  1 13  ? -7.891  -10.744 -71.667  1.00 27.38  ? 13  HIS C C   1 
ATOM   8167  O O   . HIS C  1 13  ? -6.762  -11.223 -71.816  1.00 24.79  ? 13  HIS C O   1 
ATOM   8168  C CB  . HIS C  1 13  ? -7.978  -8.994  -69.849  1.00 21.20  ? 13  HIS C CB  1 
ATOM   8169  C CG  . HIS C  1 13  ? -8.093  -7.978  -70.950  1.00 26.55  ? 13  HIS C CG  1 
ATOM   8170  N ND1 . HIS C  1 13  ? -9.287  -7.717  -71.590  1.00 25.47  ? 13  HIS C ND1 1 
ATOM   8171  C CD2 . HIS C  1 13  ? -7.172  -7.158  -71.517  1.00 24.67  ? 13  HIS C CD2 1 
ATOM   8172  C CE1 . HIS C  1 13  ? -9.091  -6.799  -72.528  1.00 26.91  ? 13  HIS C CE1 1 
ATOM   8173  N NE2 . HIS C  1 13  ? -7.816  -6.445  -72.508  1.00 27.40  ? 13  HIS C NE2 1 
ATOM   8174  N N   . GLN C  1 14  ? -8.735  -10.517 -72.684  1.00 26.86  ? 14  GLN C N   1 
ATOM   8175  C CA  . GLN C  1 14  ? -8.294  -10.443 -74.081  1.00 28.69  ? 14  GLN C CA  1 
ATOM   8176  C C   . GLN C  1 14  ? -9.000  -9.264  -74.736  1.00 30.01  ? 14  GLN C C   1 
ATOM   8177  O O   . GLN C  1 14  ? -10.188 -9.037  -74.471  1.00 31.31  ? 14  GLN C O   1 
ATOM   8178  C CB  . GLN C  1 14  ? -8.613  -11.725 -74.869  1.00 29.14  ? 14  GLN C CB  1 
ATOM   8179  C CG  . GLN C  1 14  ? -7.859  -12.970 -74.377  1.00 26.96  ? 14  GLN C CG  1 
ATOM   8180  C CD  . GLN C  1 14  ? -6.357  -12.870 -74.587  1.00 27.80  ? 14  GLN C CD  1 
ATOM   8181  O OE1 . GLN C  1 14  ? -5.898  -12.204 -75.520  1.00 27.91  ? 14  GLN C OE1 1 
ATOM   8182  N NE2 . GLN C  1 14  ? -5.580  -13.545 -73.725  1.00 29.34  ? 14  GLN C NE2 1 
ATOM   8183  N N   . PRO C  1 15  ? -8.306  -8.493  -75.578  1.00 26.69  ? 15  PRO C N   1 
ATOM   8184  C CA  . PRO C  1 15  ? -9.005  -7.538  -76.451  1.00 31.89  ? 15  PRO C CA  1 
ATOM   8185  C C   . PRO C  1 15  ? -9.908  -8.272  -77.445  1.00 33.52  ? 15  PRO C C   1 
ATOM   8186  O O   . PRO C  1 15  ? -9.776  -9.473  -77.676  1.00 32.61  ? 15  PRO C O   1 
ATOM   8187  C CB  . PRO C  1 15  ? -7.861  -6.808  -77.174  1.00 27.33  ? 15  PRO C CB  1 
ATOM   8188  C CG  . PRO C  1 15  ? -6.722  -7.799  -77.191  1.00 23.93  ? 15  PRO C CG  1 
ATOM   8189  C CD  . PRO C  1 15  ? -6.858  -8.546  -75.850  1.00 25.53  ? 15  PRO C CD  1 
ATOM   8190  N N   . LEU C  1 16  ? -10.840 -7.537  -78.048  1.00 35.35  ? 16  LEU C N   1 
ATOM   8191  C CA  . LEU C  1 16  ? -11.823 -8.163  -78.927  1.00 38.19  ? 16  LEU C CA  1 
ATOM   8192  C C   . LEU C  1 16  ? -11.175 -8.511  -80.268  1.00 37.92  ? 16  LEU C C   1 
ATOM   8193  O O   . LEU C  1 16  ? -10.857 -7.618  -81.060  1.00 40.94  ? 16  LEU C O   1 
ATOM   8194  C CB  . LEU C  1 16  ? -13.023 -7.241  -79.112  1.00 38.74  ? 16  LEU C CB  1 
ATOM   8195  C CG  . LEU C  1 16  ? -14.130 -7.773  -80.019  1.00 40.69  ? 16  LEU C CG  1 
ATOM   8196  C CD1 . LEU C  1 16  ? -14.607 -9.148  -79.546  1.00 37.28  ? 16  LEU C CD1 1 
ATOM   8197  C CD2 . LEU C  1 16  ? -15.275 -6.767  -80.114  1.00 39.22  ? 16  LEU C CD2 1 
ATOM   8198  N N   . TYR C  1 17  ? -10.991 -9.808  -80.539  1.00 29.43  ? 17  TYR C N   1 
ATOM   8199  C CA  . TYR C  1 17  ? -10.341 -10.258 -81.765  1.00 37.06  ? 17  TYR C CA  1 
ATOM   8200  C C   . TYR C  1 17  ? -11.305 -10.403 -82.941  1.00 39.71  ? 17  TYR C C   1 
ATOM   8201  O O   . TYR C  1 17  ? -10.873 -10.755 -84.046  1.00 35.30  ? 17  TYR C O   1 
ATOM   8202  C CB  . TYR C  1 17  ? -9.633  -11.600 -81.532  1.00 39.09  ? 17  TYR C CB  1 
ATOM   8203  C CG  . TYR C  1 17  ? -8.504  -11.551 -80.533  1.00 37.51  ? 17  TYR C CG  1 
ATOM   8204  C CD1 . TYR C  1 17  ? -7.401  -10.737 -80.742  1.00 33.29  ? 17  TYR C CD1 1 
ATOM   8205  C CD2 . TYR C  1 17  ? -8.532  -12.342 -79.376  1.00 36.76  ? 17  TYR C CD2 1 
ATOM   8206  C CE1 . TYR C  1 17  ? -6.353  -10.702 -79.822  1.00 28.49  ? 17  TYR C CE1 1 
ATOM   8207  C CE2 . TYR C  1 17  ? -7.495  -12.312 -78.464  1.00 30.42  ? 17  TYR C CE2 1 
ATOM   8208  C CZ  . TYR C  1 17  ? -6.415  -11.485 -78.685  1.00 29.99  ? 17  TYR C CZ  1 
ATOM   8209  O OH  . TYR C  1 17  ? -5.391  -11.453 -77.768  1.00 29.83  ? 17  TYR C OH  1 
ATOM   8210  N N   . ARG C  1 18  ? -12.591 -10.136 -82.729  1.00 42.12  ? 18  ARG C N   1 
ATOM   8211  C CA  . ARG C  1 18  ? -13.631 -10.414 -83.715  1.00 45.30  ? 18  ARG C CA  1 
ATOM   8212  C C   . ARG C  1 18  ? -13.799 -9.199  -84.621  1.00 47.44  ? 18  ARG C C   1 
ATOM   8213  O O   . ARG C  1 18  ? -14.420 -8.206  -84.235  1.00 49.62  ? 18  ARG C O   1 
ATOM   8214  C CB  . ARG C  1 18  ? -14.936 -10.763 -83.013  1.00 45.20  ? 18  ARG C CB  1 
ATOM   8215  C CG  . ARG C  1 18  ? -16.042 -11.253 -83.925  1.00 47.76  ? 18  ARG C CG  1 
ATOM   8216  C CD  . ARG C  1 18  ? -17.334 -11.327 -83.145  1.00 44.36  ? 18  ARG C CD  1 
ATOM   8217  N NE  . ARG C  1 18  ? -18.370 -12.033 -83.874  1.00 44.01  ? 18  ARG C NE  1 
ATOM   8218  C CZ  . ARG C  1 18  ? -19.152 -11.466 -84.787  1.00 48.48  ? 18  ARG C CZ  1 
ATOM   8219  N NH1 . ARG C  1 18  ? -19.017 -10.176 -85.080  1.00 48.60  ? 18  ARG C NH1 1 
ATOM   8220  N NH2 . ARG C  1 18  ? -20.071 -12.193 -85.404  1.00 52.88  ? 18  ARG C NH2 1 
ATOM   8221  N N   . GLU C  1 19  ? -13.259 -9.288  -85.833  1.00 48.64  ? 19  GLU C N   1 
ATOM   8222  C CA  . GLU C  1 19  ? -13.401 -8.212  -86.805  1.00 46.18  ? 19  GLU C CA  1 
ATOM   8223  C C   . GLU C  1 19  ? -14.882 -7.983  -87.092  1.00 43.63  ? 19  GLU C C   1 
ATOM   8224  O O   . GLU C  1 19  ? -15.610 -8.945  -87.351  1.00 42.79  ? 19  GLU C O   1 
ATOM   8225  C CB  . GLU C  1 19  ? -12.644 -8.554  -88.084  1.00 53.57  ? 19  GLU C CB  1 
ATOM   8226  C CG  . GLU C  1 19  ? -12.311 -7.344  -88.927  1.00 61.34  ? 19  GLU C CG  1 
ATOM   8227  C CD  . GLU C  1 19  ? -13.351 -7.096  -89.992  1.00 64.35  ? 19  GLU C CD  1 
ATOM   8228  O OE1 . GLU C  1 19  ? -14.287 -7.920  -90.101  1.00 61.47  ? 19  GLU C OE1 1 
ATOM   8229  O OE2 . GLU C  1 19  ? -13.236 -6.076  -90.703  1.00 70.13  ? 19  GLU C OE2 1 
ATOM   8230  N N   . PRO C  1 20  ? -15.373 -6.739  -87.026  1.00 45.66  ? 20  PRO C N   1 
ATOM   8231  C CA  . PRO C  1 20  ? -16.828 -6.518  -87.059  1.00 50.36  ? 20  PRO C CA  1 
ATOM   8232  C C   . PRO C  1 20  ? -17.468 -6.641  -88.437  1.00 56.93  ? 20  PRO C C   1 
ATOM   8233  O O   . PRO C  1 20  ? -18.703 -6.699  -88.516  1.00 62.92  ? 20  PRO C O   1 
ATOM   8234  C CB  . PRO C  1 20  ? -16.974 -5.092  -86.512  1.00 49.79  ? 20  PRO C CB  1 
ATOM   8235  C CG  . PRO C  1 20  ? -15.693 -4.420  -86.868  1.00 47.74  ? 20  PRO C CG  1 
ATOM   8236  C CD  . PRO C  1 20  ? -14.622 -5.490  -86.808  1.00 43.57  ? 20  PRO C CD  1 
ATOM   8237  N N   . TYR C  1 21  ? -16.689 -6.691  -89.515  1.00 54.21  ? 21  TYR C N   1 
ATOM   8238  C CA  . TYR C  1 21  ? -17.267 -6.793  -90.852  1.00 59.52  ? 21  TYR C CA  1 
ATOM   8239  C C   . TYR C  1 21  ? -17.410 -8.247  -91.287  1.00 59.59  ? 21  TYR C C   1 
ATOM   8240  O O   . TYR C  1 21  ? -18.470 -8.652  -91.775  1.00 61.87  ? 21  TYR C O   1 
ATOM   8241  C CB  . TYR C  1 21  ? -16.411 -6.009  -91.852  1.00 62.43  ? 21  TYR C CB  1 
ATOM   8242  C CG  . TYR C  1 21  ? -16.462 -4.512  -91.638  1.00 69.68  ? 21  TYR C CG  1 
ATOM   8243  C CD1 . TYR C  1 21  ? -17.679 -3.836  -91.605  1.00 72.69  ? 21  TYR C CD1 1 
ATOM   8244  C CD2 . TYR C  1 21  ? -15.298 -3.776  -91.432  1.00 73.02  ? 21  TYR C CD2 1 
ATOM   8245  C CE1 . TYR C  1 21  ? -17.739 -2.465  -91.396  1.00 73.66  ? 21  TYR C CE1 1 
ATOM   8246  C CE2 . TYR C  1 21  ? -15.345 -2.398  -91.217  1.00 75.01  ? 21  TYR C CE2 1 
ATOM   8247  C CZ  . TYR C  1 21  ? -16.572 -1.750  -91.204  1.00 73.70  ? 21  TYR C CZ  1 
ATOM   8248  O OH  . TYR C  1 21  ? -16.642 -0.393  -90.997  1.00 70.24  ? 21  TYR C OH  1 
ATOM   8249  N N   . THR C  1 22  ? -16.353 -9.036  -91.105  1.00 54.61  ? 22  THR C N   1 
ATOM   8250  C CA  . THR C  1 22  ? -16.357 -10.452 -91.440  1.00 59.02  ? 22  THR C CA  1 
ATOM   8251  C C   . THR C  1 22  ? -16.768 -11.343 -90.272  1.00 57.71  ? 22  THR C C   1 
ATOM   8252  O O   . THR C  1 22  ? -17.042 -12.527 -90.486  1.00 57.20  ? 22  THR C O   1 
ATOM   8253  C CB  . THR C  1 22  ? -14.969 -10.889 -91.926  1.00 60.49  ? 22  THR C CB  1 
ATOM   8254  O OG1 . THR C  1 22  ? -14.065 -10.927 -90.810  1.00 55.63  ? 22  THR C OG1 1 
ATOM   8255  C CG2 . THR C  1 22  ? -14.434 -9.919  -92.980  1.00 61.14  ? 22  THR C CG2 1 
ATOM   8256  N N   . GLY C  1 23  ? -16.814 -10.815 -89.051  1.00 56.95  ? 23  GLY C N   1 
ATOM   8257  C CA  . GLY C  1 23  ? -17.101 -11.659 -87.908  1.00 56.50  ? 23  GLY C CA  1 
ATOM   8258  C C   . GLY C  1 23  ? -16.031 -12.681 -87.598  1.00 55.62  ? 23  GLY C C   1 
ATOM   8259  O O   . GLY C  1 23  ? -16.285 -13.617 -86.834  1.00 56.70  ? 23  GLY C O   1 
ATOM   8260  N N   . GLU C  1 24  ? -14.834 -12.528 -88.162  1.00 53.86  ? 24  GLU C N   1 
ATOM   8261  C CA  . GLU C  1 24  ? -13.770 -13.510 -88.003  1.00 54.49  ? 24  GLU C CA  1 
ATOM   8262  C C   . GLU C  1 24  ? -12.910 -13.161 -86.795  1.00 50.74  ? 24  GLU C C   1 
ATOM   8263  O O   . GLU C  1 24  ? -12.472 -12.014 -86.647  1.00 48.08  ? 24  GLU C O   1 
ATOM   8264  C CB  . GLU C  1 24  ? -12.897 -13.569 -89.257  1.00 60.41  ? 24  GLU C CB  1 
ATOM   8265  C CG  . GLU C  1 24  ? -13.557 -14.225 -90.467  1.00 69.12  ? 24  GLU C CG  1 
ATOM   8266  C CD  . GLU C  1 24  ? -12.823 -15.469 -90.915  1.00 75.05  ? 24  GLU C CD  1 
ATOM   8267  O OE1 . GLU C  1 24  ? -11.960 -15.956 -90.143  1.00 74.67  ? 24  GLU C OE1 1 
ATOM   8268  O OE2 . GLU C  1 24  ? -13.108 -15.953 -92.035  1.00 77.73  ? 24  GLU C OE2 1 
ATOM   8269  N N   . TYR C  1 25  ? -12.670 -14.148 -85.932  1.00 46.02  ? 25  TYR C N   1 
ATOM   8270  C CA  . TYR C  1 25  ? -11.630 -14.002 -84.924  1.00 40.77  ? 25  TYR C CA  1 
ATOM   8271  C C   . TYR C  1 25  ? -10.285 -14.059 -85.630  1.00 41.92  ? 25  TYR C C   1 
ATOM   8272  O O   . TYR C  1 25  ? -9.899  -15.104 -86.166  1.00 46.51  ? 25  TYR C O   1 
ATOM   8273  C CB  . TYR C  1 25  ? -11.756 -15.083 -83.856  1.00 42.64  ? 25  TYR C CB  1 
ATOM   8274  C CG  . TYR C  1 25  ? -12.834 -14.755 -82.863  1.00 42.49  ? 25  TYR C CG  1 
ATOM   8275  C CD1 . TYR C  1 25  ? -14.172 -14.808 -83.237  1.00 45.05  ? 25  TYR C CD1 1 
ATOM   8276  C CD2 . TYR C  1 25  ? -12.520 -14.360 -81.566  1.00 41.20  ? 25  TYR C CD2 1 
ATOM   8277  C CE1 . TYR C  1 25  ? -15.171 -14.497 -82.346  1.00 48.58  ? 25  TYR C CE1 1 
ATOM   8278  C CE2 . TYR C  1 25  ? -13.515 -14.042 -80.657  1.00 41.49  ? 25  TYR C CE2 1 
ATOM   8279  C CZ  . TYR C  1 25  ? -14.839 -14.115 -81.055  1.00 47.66  ? 25  TYR C CZ  1 
ATOM   8280  O OH  . TYR C  1 25  ? -15.844 -13.799 -80.175  1.00 49.99  ? 25  TYR C OH  1 
ATOM   8281  N N   . LEU C  1 26  ? -9.586  -12.926 -85.653  1.00 41.04  ? 26  LEU C N   1 
ATOM   8282  C CA  . LEU C  1 26  ? -8.374  -12.788 -86.452  1.00 42.77  ? 26  LEU C CA  1 
ATOM   8283  C C   . LEU C  1 26  ? -7.132  -13.296 -85.734  1.00 43.37  ? 26  LEU C C   1 
ATOM   8284  O O   . LEU C  1 26  ? -6.111  -13.534 -86.389  1.00 45.58  ? 26  LEU C O   1 
ATOM   8285  C CB  . LEU C  1 26  ? -8.188  -11.322 -86.875  1.00 42.54  ? 26  LEU C CB  1 
ATOM   8286  C CG  . LEU C  1 26  ? -9.320  -10.701 -87.707  1.00 41.72  ? 26  LEU C CG  1 
ATOM   8287  C CD1 . LEU C  1 26  ? -8.966  -9.287  -88.146  1.00 43.95  ? 26  LEU C CD1 1 
ATOM   8288  C CD2 . LEU C  1 26  ? -9.669  -11.546 -88.938  1.00 48.58  ? 26  LEU C CD2 1 
ATOM   8289  N N   . LEU C  1 27  ? -7.188  -13.450 -84.414  1.00 39.21  ? 27  LEU C N   1 
ATOM   8290  C CA  . LEU C  1 27  ? -6.138  -14.141 -83.691  1.00 40.06  ? 27  LEU C CA  1 
ATOM   8291  C C   . LEU C  1 27  ? -6.766  -15.185 -82.778  1.00 42.48  ? 27  LEU C C   1 
ATOM   8292  O O   . LEU C  1 27  ? -7.898  -15.008 -82.315  1.00 45.90  ? 27  LEU C O   1 
ATOM   8293  C CB  . LEU C  1 27  ? -5.285  -13.162 -82.874  1.00 42.84  ? 27  LEU C CB  1 
ATOM   8294  C CG  . LEU C  1 27  ? -4.279  -12.333 -83.677  1.00 43.96  ? 27  LEU C CG  1 
ATOM   8295  C CD1 . LEU C  1 27  ? -3.532  -11.372 -82.768  1.00 39.69  ? 27  LEU C CD1 1 
ATOM   8296  C CD2 . LEU C  1 27  ? -3.304  -13.215 -84.429  1.00 43.01  ? 27  LEU C CD2 1 
ATOM   8297  N N   . PRO C  1 28  ? -6.068  -16.288 -82.512  1.00 37.04  ? 28  PRO C N   1 
ATOM   8298  C CA  . PRO C  1 28  ? -6.655  -17.380 -81.720  1.00 36.48  ? 28  PRO C CA  1 
ATOM   8299  C C   . PRO C  1 28  ? -6.390  -17.313 -80.219  1.00 32.32  ? 28  PRO C C   1 
ATOM   8300  O O   . PRO C  1 28  ? -6.705  -18.278 -79.517  1.00 31.70  ? 28  PRO C O   1 
ATOM   8301  C CB  . PRO C  1 28  ? -5.957  -18.602 -82.321  1.00 36.99  ? 28  PRO C CB  1 
ATOM   8302  C CG  . PRO C  1 28  ? -4.565  -18.088 -82.579  1.00 34.61  ? 28  PRO C CG  1 
ATOM   8303  C CD  . PRO C  1 28  ? -4.716  -16.634 -82.987  1.00 35.73  ? 28  PRO C CD  1 
ATOM   8304  N N   . TRP C  1 29  ? -5.875  -16.202 -79.706  1.00 31.47  ? 29  TRP C N   1 
ATOM   8305  C CA  . TRP C  1 29  ? -5.383  -16.175 -78.327  1.00 35.53  ? 29  TRP C CA  1 
ATOM   8306  C C   . TRP C  1 29  ? -6.487  -16.432 -77.303  1.00 35.18  ? 29  TRP C C   1 
ATOM   8307  O O   . TRP C  1 29  ? -6.251  -17.092 -76.281  1.00 30.01  ? 29  TRP C O   1 
ATOM   8308  C CB  . TRP C  1 29  ? -4.709  -14.837 -78.061  1.00 34.25  ? 29  TRP C CB  1 
ATOM   8309  C CG  . TRP C  1 29  ? -3.517  -14.576 -78.953  1.00 38.58  ? 29  TRP C CG  1 
ATOM   8310  C CD1 . TRP C  1 29  ? -3.317  -13.490 -79.762  1.00 37.31  ? 29  TRP C CD1 1 
ATOM   8311  C CD2 . TRP C  1 29  ? -2.361  -15.413 -79.111  1.00 40.26  ? 29  TRP C CD2 1 
ATOM   8312  N NE1 . TRP C  1 29  ? -2.103  -13.594 -80.400  1.00 41.37  ? 29  TRP C NE1 1 
ATOM   8313  C CE2 . TRP C  1 29  ? -1.500  -14.767 -80.021  1.00 42.54  ? 29  TRP C CE2 1 
ATOM   8314  C CE3 . TRP C  1 29  ? -1.964  -16.639 -78.560  1.00 41.25  ? 29  TRP C CE3 1 
ATOM   8315  C CZ2 . TRP C  1 29  ? -0.274  -15.311 -80.400  1.00 43.41  ? 29  TRP C CZ2 1 
ATOM   8316  C CZ3 . TRP C  1 29  ? -0.749  -17.177 -78.937  1.00 38.26  ? 29  TRP C CZ3 1 
ATOM   8317  C CH2 . TRP C  1 29  ? 0.083   -16.512 -79.849  1.00 42.41  ? 29  TRP C CH2 1 
ATOM   8318  N N   . THR C  1 30  ? -7.691  -15.899 -77.532  1.00 33.90  ? 30  THR C N   1 
ATOM   8319  C CA  . THR C  1 30  ? -8.779  -16.164 -76.591  1.00 34.75  ? 30  THR C CA  1 
ATOM   8320  C C   . THR C  1 30  ? -9.030  -17.665 -76.457  1.00 33.34  ? 30  THR C C   1 
ATOM   8321  O O   . THR C  1 30  ? -9.130  -18.194 -75.338  1.00 30.56  ? 30  THR C O   1 
ATOM   8322  C CB  . THR C  1 30  ? -10.044 -15.421 -77.029  1.00 35.05  ? 30  THR C CB  1 
ATOM   8323  O OG1 . THR C  1 30  ? -9.827  -14.015 -76.885  1.00 37.21  ? 30  THR C OG1 1 
ATOM   8324  C CG2 . THR C  1 30  ? -11.243 -15.815 -76.175  1.00 33.11  ? 30  THR C CG2 1 
ATOM   8325  N N   . PHE C  1 31  ? -9.098  -18.370 -77.598  1.00 29.77  ? 31  PHE C N   1 
ATOM   8326  C CA  . PHE C  1 31  ? -9.280  -19.821 -77.601  1.00 23.45  ? 31  PHE C CA  1 
ATOM   8327  C C   . PHE C  1 31  ? -8.150  -20.526 -76.853  1.00 26.63  ? 31  PHE C C   1 
ATOM   8328  O O   . PHE C  1 31  ? -8.392  -21.382 -75.992  1.00 25.86  ? 31  PHE C O   1 
ATOM   8329  C CB  . PHE C  1 31  ? -9.367  -20.336 -79.054  1.00 28.12  ? 31  PHE C CB  1 
ATOM   8330  C CG  . PHE C  1 31  ? -9.413  -21.842 -79.166  1.00 28.92  ? 31  PHE C CG  1 
ATOM   8331  C CD1 . PHE C  1 31  ? -10.616 -22.520 -79.063  1.00 29.09  ? 31  PHE C CD1 1 
ATOM   8332  C CD2 . PHE C  1 31  ? -8.255  -22.579 -79.361  1.00 31.26  ? 31  PHE C CD2 1 
ATOM   8333  C CE1 . PHE C  1 31  ? -10.664 -23.905 -79.146  1.00 31.03  ? 31  PHE C CE1 1 
ATOM   8334  C CE2 . PHE C  1 31  ? -8.290  -23.968 -79.455  1.00 29.82  ? 31  PHE C CE2 1 
ATOM   8335  C CZ  . PHE C  1 31  ? -9.497  -24.632 -79.351  1.00 30.26  ? 31  PHE C CZ  1 
ATOM   8336  N N   . PHE C  1 32  ? -6.898  -20.185 -77.171  1.00 29.61  ? 32  PHE C N   1 
ATOM   8337  C CA  . PHE C  1 32  ? -5.785  -20.927 -76.578  1.00 31.29  ? 32  PHE C CA  1 
ATOM   8338  C C   . PHE C  1 32  ? -5.678  -20.685 -75.078  1.00 27.82  ? 32  PHE C C   1 
ATOM   8339  O O   . PHE C  1 32  ? -5.409  -21.618 -74.309  1.00 28.72  ? 32  PHE C O   1 
ATOM   8340  C CB  . PHE C  1 32  ? -4.479  -20.570 -77.279  1.00 33.75  ? 32  PHE C CB  1 
ATOM   8341  C CG  . PHE C  1 32  ? -4.266  -21.334 -78.542  1.00 35.99  ? 32  PHE C CG  1 
ATOM   8342  C CD1 . PHE C  1 32  ? -4.401  -22.709 -78.551  1.00 38.52  ? 32  PHE C CD1 1 
ATOM   8343  C CD2 . PHE C  1 32  ? -3.978  -20.678 -79.732  1.00 38.21  ? 32  PHE C CD2 1 
ATOM   8344  C CE1 . PHE C  1 32  ? -4.228  -23.435 -79.721  1.00 44.95  ? 32  PHE C CE1 1 
ATOM   8345  C CE2 . PHE C  1 32  ? -3.802  -21.389 -80.900  1.00 40.89  ? 32  PHE C CE2 1 
ATOM   8346  C CZ  . PHE C  1 32  ? -3.925  -22.775 -80.896  1.00 42.51  ? 32  PHE C CZ  1 
ATOM   8347  N N   . HIS C  1 33  ? -5.872  -19.448 -74.641  1.00 24.53  ? 33  HIS C N   1 
ATOM   8348  C CA  . HIS C  1 33  ? -5.809  -19.183 -73.210  1.00 24.96  ? 33  HIS C CA  1 
ATOM   8349  C C   . HIS C  1 33  ? -7.056  -19.661 -72.487  1.00 19.25  ? 33  HIS C C   1 
ATOM   8350  O O   . HIS C  1 33  ? -7.030  -19.815 -71.261  1.00 23.08  ? 33  HIS C O   1 
ATOM   8351  C CB  . HIS C  1 33  ? -5.571  -17.687 -72.971  1.00 18.75  ? 33  HIS C CB  1 
ATOM   8352  C CG  . HIS C  1 33  ? -4.140  -17.288 -73.154  1.00 27.04  ? 33  HIS C CG  1 
ATOM   8353  N ND1 . HIS C  1 33  ? -3.138  -17.694 -72.292  1.00 26.37  ? 33  HIS C ND1 1 
ATOM   8354  C CD2 . HIS C  1 33  ? -3.532  -16.560 -74.122  1.00 21.90  ? 33  HIS C CD2 1 
ATOM   8355  C CE1 . HIS C  1 33  ? -1.980  -17.211 -72.709  1.00 24.65  ? 33  HIS C CE1 1 
ATOM   8356  N NE2 . HIS C  1 33  ? -2.191  -16.527 -73.824  1.00 25.18  ? 33  HIS C NE2 1 
ATOM   8357  N N   . ALA C  1 34  ? -8.143  -19.920 -73.212  1.00 21.97  ? 34  ALA C N   1 
ATOM   8358  C CA  . ALA C  1 34  ? -9.323  -20.485 -72.563  1.00 25.98  ? 34  ALA C CA  1 
ATOM   8359  C C   . ALA C  1 34  ? -9.123  -21.967 -72.268  1.00 31.09  ? 34  ALA C C   1 
ATOM   8360  O O   . ALA C  1 34  ? -9.444  -22.443 -71.168  1.00 33.67  ? 34  ALA C O   1 
ATOM   8361  C CB  . ALA C  1 34  ? -10.562 -20.267 -73.435  1.00 26.02  ? 34  ALA C CB  1 
ATOM   8362  N N   . VAL C  1 35  ? -8.593  -22.712 -73.243  1.00 28.65  ? 35  VAL C N   1 
ATOM   8363  C CA  . VAL C  1 35  ? -8.371  -24.149 -73.064  1.00 29.55  ? 35  VAL C CA  1 
ATOM   8364  C C   . VAL C  1 35  ? -7.223  -24.413 -72.095  1.00 29.92  ? 35  VAL C C   1 
ATOM   8365  O O   . VAL C  1 35  ? -7.189  -25.454 -71.438  1.00 31.71  ? 35  VAL C O   1 
ATOM   8366  C CB  . VAL C  1 35  ? -8.112  -24.844 -74.419  1.00 27.31  ? 35  VAL C CB  1 
ATOM   8367  C CG1 . VAL C  1 35  ? -9.271  -24.603 -75.405  1.00 29.39  ? 35  VAL C CG1 1 
ATOM   8368  C CG2 . VAL C  1 35  ? -6.787  -24.369 -75.013  1.00 26.08  ? 35  VAL C CG2 1 
ATOM   8369  N N   . LYS C  1 36  ? -6.255  -23.503 -72.008  1.00 30.02  ? 36  LYS C N   1 
ATOM   8370  C CA  . LYS C  1 36  ? -5.107  -23.697 -71.138  1.00 28.65  ? 36  LYS C CA  1 
ATOM   8371  C C   . LYS C  1 36  ? -5.267  -23.051 -69.760  1.00 27.69  ? 36  LYS C C   1 
ATOM   8372  O O   . LYS C  1 36  ? -4.881  -23.659 -68.765  1.00 27.54  ? 36  LYS C O   1 
ATOM   8373  C CB  . LYS C  1 36  ? -3.837  -23.161 -71.810  1.00 30.49  ? 36  LYS C CB  1 
ATOM   8374  C CG  . LYS C  1 36  ? -2.544  -23.613 -71.118  1.00 26.65  ? 36  LYS C CG  1 
ATOM   8375  C CD  . LYS C  1 36  ? -1.298  -23.099 -71.858  1.00 31.95  ? 36  LYS C CD  1 
ATOM   8376  C CE  . LYS C  1 36  ? -1.040  -21.607 -71.626  1.00 28.96  ? 36  LYS C CE  1 
ATOM   8377  N NZ  . LYS C  1 36  ? -0.666  -21.288 -70.194  1.00 28.02  ? 36  LYS C NZ  1 
ATOM   8378  N N   . ASP C  1 37  ? -5.846  -21.849 -69.661  1.00 26.51  ? 37  ASP C N   1 
ATOM   8379  C CA  . ASP C  1 37  ? -5.716  -21.108 -68.409  1.00 27.50  ? 37  ASP C CA  1 
ATOM   8380  C C   . ASP C  1 37  ? -7.031  -20.654 -67.791  1.00 34.07  ? 37  ASP C C   1 
ATOM   8381  O O   . ASP C  1 37  ? -7.137  -20.621 -66.556  1.00 30.03  ? 37  ASP C O   1 
ATOM   8382  C CB  . ASP C  1 37  ? -4.850  -19.879 -68.605  1.00 27.76  ? 37  ASP C CB  1 
ATOM   8383  C CG  . ASP C  1 37  ? -3.533  -20.197 -69.258  1.00 27.83  ? 37  ASP C CG  1 
ATOM   8384  O OD1 . ASP C  1 37  ? -2.708  -20.915 -68.639  1.00 24.77  ? 37  ASP C OD1 1 
ATOM   8385  O OD2 . ASP C  1 37  ? -3.336  -19.730 -70.405  1.00 26.42  ? 37  ASP C OD2 1 
ATOM   8386  N N   . TYR C  1 38  ? -8.022  -20.264 -68.602  1.00 27.63  ? 38  TYR C N   1 
ATOM   8387  C CA  . TYR C  1 38  ? -9.180  -19.582 -68.029  1.00 27.17  ? 38  TYR C CA  1 
ATOM   8388  C C   . TYR C  1 38  ? -10.073 -20.536 -67.250  1.00 27.09  ? 38  TYR C C   1 
ATOM   8389  O O   . TYR C  1 38  ? -10.719 -20.126 -66.285  1.00 27.82  ? 38  TYR C O   1 
ATOM   8390  C CB  . TYR C  1 38  ? -9.970  -18.862 -69.118  1.00 27.76  ? 38  TYR C CB  1 
ATOM   8391  C CG  . TYR C  1 38  ? -9.204  -17.696 -69.701  1.00 27.45  ? 38  TYR C CG  1 
ATOM   8392  C CD1 . TYR C  1 38  ? -8.278  -17.002 -68.932  1.00 26.86  ? 38  TYR C CD1 1 
ATOM   8393  C CD2 . TYR C  1 38  ? -9.386  -17.307 -71.020  1.00 31.67  ? 38  TYR C CD2 1 
ATOM   8394  C CE1 . TYR C  1 38  ? -7.573  -15.944 -69.444  1.00 29.36  ? 38  TYR C CE1 1 
ATOM   8395  C CE2 . TYR C  1 38  ? -8.681  -16.250 -71.554  1.00 30.71  ? 38  TYR C CE2 1 
ATOM   8396  C CZ  . TYR C  1 38  ? -7.776  -15.572 -70.774  1.00 30.89  ? 38  TYR C CZ  1 
ATOM   8397  O OH  . TYR C  1 38  ? -7.073  -14.523 -71.314  1.00 28.36  ? 38  TYR C OH  1 
ATOM   8398  N N   . TYR C  1 39  ? -10.134 -21.797 -67.655  1.00 28.03  ? 39  TYR C N   1 
ATOM   8399  C CA  . TYR C  1 39  ? -10.851 -22.780 -66.858  1.00 32.05  ? 39  TYR C CA  1 
ATOM   8400  C C   . TYR C  1 39  ? -9.957  -23.340 -65.757  1.00 30.58  ? 39  TYR C C   1 
ATOM   8401  O O   . TYR C  1 39  ? -10.392 -23.482 -64.607  1.00 27.79  ? 39  TYR C O   1 
ATOM   8402  C CB  . TYR C  1 39  ? -11.364 -23.912 -67.745  1.00 35.96  ? 39  TYR C CB  1 
ATOM   8403  C CG  . TYR C  1 39  ? -11.980 -25.041 -66.953  1.00 36.77  ? 39  TYR C CG  1 
ATOM   8404  C CD1 . TYR C  1 39  ? -13.290 -24.960 -66.493  1.00 36.47  ? 39  TYR C CD1 1 
ATOM   8405  C CD2 . TYR C  1 39  ? -11.242 -26.183 -66.646  1.00 36.75  ? 39  TYR C CD2 1 
ATOM   8406  C CE1 . TYR C  1 39  ? -13.849 -25.982 -65.763  1.00 37.49  ? 39  TYR C CE1 1 
ATOM   8407  C CE2 . TYR C  1 39  ? -11.791 -27.204 -65.914  1.00 39.16  ? 39  TYR C CE2 1 
ATOM   8408  C CZ  . TYR C  1 39  ? -13.095 -27.101 -65.477  1.00 41.48  ? 39  TYR C CZ  1 
ATOM   8409  O OH  . TYR C  1 39  ? -13.651 -28.128 -64.754  1.00 45.85  ? 39  TYR C OH  1 
ATOM   8410  N N   . ASP C  1 40  ? -8.693  -23.599 -66.090  1.00 27.90  ? 40  ASP C N   1 
ATOM   8411  C CA  . ASP C  1 40  ? -7.801  -24.344 -65.216  1.00 27.11  ? 40  ASP C CA  1 
ATOM   8412  C C   . ASP C  1 40  ? -7.315  -23.539 -64.023  1.00 29.66  ? 40  ASP C C   1 
ATOM   8413  O O   . ASP C  1 40  ? -7.095  -24.115 -62.950  1.00 27.91  ? 40  ASP C O   1 
ATOM   8414  C CB  . ASP C  1 40  ? -6.630  -24.869 -66.033  1.00 28.02  ? 40  ASP C CB  1 
ATOM   8415  C CG  . ASP C  1 40  ? -6.962  -26.191 -66.666  1.00 34.56  ? 40  ASP C CG  1 
ATOM   8416  O OD1 . ASP C  1 40  ? -7.168  -27.144 -65.879  1.00 32.22  ? 40  ASP C OD1 1 
ATOM   8417  O OD2 . ASP C  1 40  ? -7.087  -26.273 -67.914  1.00 32.18  ? 40  ASP C OD2 1 
ATOM   8418  N N   . MET C  1 41  ? -7.175  -22.218 -64.162  1.00 27.99  ? 41  MET C N   1 
ATOM   8419  C CA  . MET C  1 41  ? -6.731  -21.425 -63.016  1.00 28.06  ? 41  MET C CA  1 
ATOM   8420  C C   . MET C  1 41  ? -7.754  -21.434 -61.883  1.00 29.08  ? 41  MET C C   1 
ATOM   8421  O O   . MET C  1 41  ? -7.361  -21.715 -60.734  1.00 32.83  ? 41  MET C O   1 
ATOM   8422  C CB  . MET C  1 41  ? -6.364  -20.014 -63.473  1.00 26.81  ? 41  MET C CB  1 
ATOM   8423  C CG  . MET C  1 41  ? -5.028  -19.992 -64.176  1.00 24.82  ? 41  MET C CG  1 
ATOM   8424  S SD  . MET C  1 41  ? -3.672  -20.146 -62.984  1.00 26.56  ? 41  MET C SD  1 
ATOM   8425  C CE  . MET C  1 41  ? -3.676  -18.476 -62.357  1.00 24.09  ? 41  MET C CE  1 
ATOM   8426  N N   . PRO C  1 42  ? -9.050  -21.161 -62.108  1.00 26.77  ? 42  PRO C N   1 
ATOM   8427  C CA  . PRO C  1 42  ? -10.025 -21.376 -61.016  1.00 26.13  ? 42  PRO C CA  1 
ATOM   8428  C C   . PRO C  1 42  ? -10.239 -22.848 -60.673  1.00 30.97  ? 42  PRO C C   1 
ATOM   8429  O O   . PRO C  1 42  ? -10.604 -23.150 -59.531  1.00 33.72  ? 42  PRO C O   1 
ATOM   8430  C CB  . PRO C  1 42  ? -11.311 -20.728 -61.544  1.00 24.98  ? 42  PRO C CB  1 
ATOM   8431  C CG  . PRO C  1 42  ? -11.144 -20.702 -63.063  1.00 25.19  ? 42  PRO C CG  1 
ATOM   8432  C CD  . PRO C  1 42  ? -9.675  -20.512 -63.289  1.00 23.66  ? 42  PRO C CD  1 
ATOM   8433  N N   . ALA C  1 43  ? -9.999  -23.768 -61.610  1.00 34.02  ? 43  ALA C N   1 
ATOM   8434  C CA  . ALA C  1 43  ? -10.139 -25.192 -61.319  1.00 33.36  ? 43  ALA C CA  1 
ATOM   8435  C C   . ALA C  1 43  ? -9.182  -25.669 -60.241  1.00 35.23  ? 43  ALA C C   1 
ATOM   8436  O O   . ALA C  1 43  ? -9.443  -26.710 -59.626  1.00 32.35  ? 43  ALA C O   1 
ATOM   8437  C CB  . ALA C  1 43  ? -9.929  -26.037 -62.582  1.00 32.98  ? 43  ALA C CB  1 
ATOM   8438  N N   . TYR C  1 44  ? -8.080  -24.946 -59.993  1.00 38.31  ? 44  TYR C N   1 
ATOM   8439  C CA  . TYR C  1 44  ? -7.198  -25.330 -58.886  1.00 33.74  ? 44  TYR C CA  1 
ATOM   8440  C C   . TYR C  1 44  ? -7.954  -25.408 -57.572  1.00 37.62  ? 44  TYR C C   1 
ATOM   8441  O O   . TYR C  1 44  ? -7.591  -26.196 -56.689  1.00 38.61  ? 44  TYR C O   1 
ATOM   8442  C CB  . TYR C  1 44  ? -6.039  -24.345 -58.739  1.00 29.65  ? 44  TYR C CB  1 
ATOM   8443  C CG  . TYR C  1 44  ? -4.867  -24.629 -59.665  1.00 31.75  ? 44  TYR C CG  1 
ATOM   8444  C CD1 . TYR C  1 44  ? -3.874  -25.529 -59.302  1.00 31.62  ? 44  TYR C CD1 1 
ATOM   8445  C CD2 . TYR C  1 44  ? -4.749  -23.984 -60.891  1.00 30.81  ? 44  TYR C CD2 1 
ATOM   8446  C CE1 . TYR C  1 44  ? -2.792  -25.786 -60.131  1.00 30.92  ? 44  TYR C CE1 1 
ATOM   8447  C CE2 . TYR C  1 44  ? -3.664  -24.241 -61.741  1.00 28.70  ? 44  TYR C CE2 1 
ATOM   8448  C CZ  . TYR C  1 44  ? -2.689  -25.151 -61.348  1.00 30.50  ? 44  TYR C CZ  1 
ATOM   8449  O OH  . TYR C  1 44  ? -1.602  -25.437 -62.163  1.00 31.81  ? 44  TYR C OH  1 
ATOM   8450  N N   . LEU C  1 45  ? -9.000  -24.600 -57.416  1.00 32.59  ? 45  LEU C N   1 
ATOM   8451  C CA  . LEU C  1 45  ? -9.754  -24.610 -56.170  1.00 32.47  ? 45  LEU C CA  1 
ATOM   8452  C C   . LEU C  1 45  ? -10.463 -25.938 -55.924  1.00 42.64  ? 45  LEU C C   1 
ATOM   8453  O O   . LEU C  1 45  ? -10.828 -26.221 -54.778  1.00 44.56  ? 45  LEU C O   1 
ATOM   8454  C CB  . LEU C  1 45  ? -10.756 -23.454 -56.167  1.00 31.10  ? 45  LEU C CB  1 
ATOM   8455  C CG  . LEU C  1 45  ? -10.064 -22.086 -56.178  1.00 31.01  ? 45  LEU C CG  1 
ATOM   8456  C CD1 . LEU C  1 45  ? -11.040 -20.967 -56.480  1.00 32.12  ? 45  LEU C CD1 1 
ATOM   8457  C CD2 . LEU C  1 45  ? -9.359  -21.824 -54.850  1.00 32.61  ? 45  LEU C CD2 1 
ATOM   8458  N N   . LYS C  1 46  ? -10.665 -26.760 -56.963  1.00 43.84  ? 46  LYS C N   1 
ATOM   8459  C CA  . LYS C  1 46  ? -11.253 -28.083 -56.749  1.00 49.01  ? 46  LYS C CA  1 
ATOM   8460  C C   . LYS C  1 46  ? -10.335 -28.996 -55.943  1.00 48.60  ? 46  LYS C C   1 
ATOM   8461  O O   . LYS C  1 46  ? -10.820 -29.876 -55.224  1.00 51.40  ? 46  LYS C O   1 
ATOM   8462  C CB  . LYS C  1 46  ? -11.586 -28.744 -58.087  1.00 52.54  ? 46  LYS C CB  1 
ATOM   8463  C CG  . LYS C  1 46  ? -12.650 -28.024 -58.892  1.00 54.06  ? 46  LYS C CG  1 
ATOM   8464  C CD  . LYS C  1 46  ? -13.721 -28.997 -59.359  1.00 55.72  ? 46  LYS C CD  1 
ATOM   8465  C CE  . LYS C  1 46  ? -14.411 -28.478 -60.604  1.00 57.84  ? 46  LYS C CE  1 
ATOM   8466  N NZ  . LYS C  1 46  ? -14.317 -29.450 -61.731  1.00 58.12  ? 46  LYS C NZ  1 
ATOM   8467  N N   . ASP C  1 47  ? -9.017  -28.818 -56.061  1.00 46.06  ? 47  ASP C N   1 
ATOM   8468  C CA  . ASP C  1 47  ? -8.043  -29.680 -55.407  1.00 45.72  ? 47  ASP C CA  1 
ATOM   8469  C C   . ASP C  1 47  ? -7.313  -29.032 -54.243  1.00 44.86  ? 47  ASP C C   1 
ATOM   8470  O O   . ASP C  1 47  ? -6.647  -29.744 -53.485  1.00 46.17  ? 47  ASP C O   1 
ATOM   8471  C CB  . ASP C  1 47  ? -6.992  -30.159 -56.415  1.00 45.44  ? 47  ASP C CB  1 
ATOM   8472  C CG  . ASP C  1 47  ? -7.599  -30.881 -57.584  1.00 46.20  ? 47  ASP C CG  1 
ATOM   8473  O OD1 . ASP C  1 47  ? -8.744  -31.368 -57.454  1.00 44.63  ? 47  ASP C OD1 1 
ATOM   8474  O OD2 . ASP C  1 47  ? -6.922  -30.977 -58.627  1.00 46.92  ? 47  ASP C OD2 1 
ATOM   8475  N N   . PHE C  1 48  ? -7.394  -27.714 -54.097  1.00 38.40  ? 48  PHE C N   1 
ATOM   8476  C CA  . PHE C  1 48  ? -6.683  -26.994 -53.050  1.00 35.48  ? 48  PHE C CA  1 
ATOM   8477  C C   . PHE C  1 48  ? -7.665  -26.056 -52.378  1.00 40.67  ? 48  PHE C C   1 
ATOM   8478  O O   . PHE C  1 48  ? -8.239  -25.178 -53.028  1.00 42.23  ? 48  PHE C O   1 
ATOM   8479  C CB  . PHE C  1 48  ? -5.487  -26.218 -53.603  1.00 39.57  ? 48  PHE C CB  1 
ATOM   8480  C CG  . PHE C  1 48  ? -4.456  -27.087 -54.251  1.00 42.10  ? 48  PHE C CG  1 
ATOM   8481  C CD1 . PHE C  1 48  ? -3.474  -27.695 -53.490  1.00 42.38  ? 48  PHE C CD1 1 
ATOM   8482  C CD2 . PHE C  1 48  ? -4.481  -27.315 -55.615  1.00 39.23  ? 48  PHE C CD2 1 
ATOM   8483  C CE1 . PHE C  1 48  ? -2.520  -28.505 -54.084  1.00 44.57  ? 48  PHE C CE1 1 
ATOM   8484  C CE2 . PHE C  1 48  ? -3.535  -28.115 -56.216  1.00 40.00  ? 48  PHE C CE2 1 
ATOM   8485  C CZ  . PHE C  1 48  ? -2.548  -28.714 -55.449  1.00 43.55  ? 48  PHE C CZ  1 
ATOM   8486  N N   . GLU C  1 49  ? -7.863  -26.253 -51.085  1.00 46.64  ? 49  GLU C N   1 
ATOM   8487  C CA  . GLU C  1 49  ? -8.900  -25.536 -50.356  1.00 52.46  ? 49  GLU C CA  1 
ATOM   8488  C C   . GLU C  1 49  ? -8.348  -24.232 -49.773  1.00 49.22  ? 49  GLU C C   1 
ATOM   8489  O O   . GLU C  1 49  ? -8.343  -23.997 -48.567  1.00 53.47  ? 49  GLU C O   1 
ATOM   8490  C CB  . GLU C  1 49  ? -9.475  -26.447 -49.284  1.00 60.24  ? 49  GLU C CB  1 
ATOM   8491  C CG  . GLU C  1 49  ? -10.801 -26.022 -48.763  1.00 69.54  ? 49  GLU C CG  1 
ATOM   8492  C CD  . GLU C  1 49  ? -10.796 -26.012 -47.262  1.00 81.60  ? 49  GLU C CD  1 
ATOM   8493  O OE1 . GLU C  1 49  ? -9.687  -25.946 -46.687  1.00 87.24  ? 49  GLU C OE1 1 
ATOM   8494  O OE2 . GLU C  1 49  ? -11.884 -26.077 -46.657  1.00 85.33  ? 49  GLU C OE2 1 
ATOM   8495  N N   . ILE C  1 50  ? -7.854  -23.382 -50.673  1.00 44.68  ? 50  ILE C N   1 
ATOM   8496  C CA  . ILE C  1 50  ? -7.441  -22.028 -50.324  1.00 42.48  ? 50  ILE C CA  1 
ATOM   8497  C C   . ILE C  1 50  ? -8.406  -21.063 -50.990  1.00 41.91  ? 50  ILE C C   1 
ATOM   8498  O O   . ILE C  1 50  ? -9.347  -21.474 -51.685  1.00 38.01  ? 50  ILE C O   1 
ATOM   8499  C CB  . ILE C  1 50  ? -6.006  -21.723 -50.781  1.00 41.22  ? 50  ILE C CB  1 
ATOM   8500  C CG1 . ILE C  1 50  ? -5.868  -22.075 -52.272  1.00 42.69  ? 50  ILE C CG1 1 
ATOM   8501  C CG2 . ILE C  1 50  ? -4.991  -22.439 -49.935  1.00 42.99  ? 50  ILE C CG2 1 
ATOM   8502  C CD1 . ILE C  1 50  ? -4.664  -21.471 -52.906  1.00 40.27  ? 50  ILE C CD1 1 
ATOM   8503  N N   . LYS C  1 51  ? -8.147  -19.772 -50.831  1.00 39.20  ? 51  LYS C N   1 
ATOM   8504  C CA  . LYS C  1 51  ? -8.918  -18.738 -51.505  1.00 34.43  ? 51  LYS C CA  1 
ATOM   8505  C C   . LYS C  1 51  ? -8.083  -18.128 -52.617  1.00 34.31  ? 51  LYS C C   1 
ATOM   8506  O O   . LYS C  1 51  ? -6.925  -17.752 -52.396  1.00 32.96  ? 51  LYS C O   1 
ATOM   8507  C CB  . LYS C  1 51  ? -9.360  -17.655 -50.532  1.00 28.95  ? 51  LYS C CB  1 
ATOM   8508  C CG  . LYS C  1 51  ? -9.962  -18.204 -49.256  1.00 32.93  ? 51  LYS C CG  1 
ATOM   8509  C CD  . LYS C  1 51  ? -11.358 -18.777 -49.448  1.00 32.23  ? 51  LYS C CD  1 
ATOM   8510  C CE  . LYS C  1 51  ? -11.990 -18.960 -48.056  1.00 33.42  ? 51  LYS C CE  1 
ATOM   8511  N NZ  . LYS C  1 51  ? -13.324 -19.610 -48.058  1.00 40.22  ? 51  LYS C NZ  1 
ATOM   8512  N N   . LEU C  1 52  ? -8.684  -18.028 -53.801  1.00 30.58  ? 52  LEU C N   1 
ATOM   8513  C CA  . LEU C  1 52  ? -8.088  -17.403 -54.975  1.00 32.20  ? 52  LEU C CA  1 
ATOM   8514  C C   . LEU C  1 52  ? -9.148  -16.521 -55.622  1.00 29.49  ? 52  LEU C C   1 
ATOM   8515  O O   . LEU C  1 52  ? -10.304 -16.933 -55.751  1.00 32.53  ? 52  LEU C O   1 
ATOM   8516  C CB  . LEU C  1 52  ? -7.585  -18.446 -55.988  1.00 34.12  ? 52  LEU C CB  1 
ATOM   8517  C CG  . LEU C  1 52  ? -6.540  -19.482 -55.547  1.00 36.57  ? 52  LEU C CG  1 
ATOM   8518  C CD1 . LEU C  1 52  ? -6.387  -20.574 -56.599  1.00 35.79  ? 52  LEU C CD1 1 
ATOM   8519  C CD2 . LEU C  1 52  ? -5.189  -18.832 -55.275  1.00 33.98  ? 52  LEU C CD2 1 
ATOM   8520  N N   . ASN C  1 53  ? -8.777  -15.307 -55.996  1.00 24.03  ? 53  ASN C N   1 
ATOM   8521  C CA  . ASN C  1 53  ? -9.725  -14.389 -56.612  1.00 25.88  ? 53  ASN C CA  1 
ATOM   8522  C C   . ASN C  1 53  ? -9.345  -14.164 -58.066  1.00 26.72  ? 53  ASN C C   1 
ATOM   8523  O O   . ASN C  1 53  ? -8.196  -14.385 -58.453  1.00 27.72  ? 53  ASN C O   1 
ATOM   8524  C CB  . ASN C  1 53  ? -9.762  -13.065 -55.852  1.00 23.70  ? 53  ASN C CB  1 
ATOM   8525  C CG  . ASN C  1 53  ? -9.856  -13.282 -54.362  1.00 30.18  ? 53  ASN C CG  1 
ATOM   8526  O OD1 . ASN C  1 53  ? -10.929 -13.603 -53.844  1.00 34.61  ? 53  ASN C OD1 1 
ATOM   8527  N ND2 . ASN C  1 53  ? -8.723  -13.164 -53.667  1.00 26.99  ? 53  ASN C ND2 1 
ATOM   8528  N N   . PHE C  1 54  ? -10.332 -13.721 -58.864  1.00 25.66  ? 54  PHE C N   1 
ATOM   8529  C CA  . PHE C  1 54  ? -10.187 -13.615 -60.313  1.00 29.87  ? 54  PHE C CA  1 
ATOM   8530  C C   . PHE C  1 54  ? -10.899 -12.382 -60.845  1.00 29.57  ? 54  PHE C C   1 
ATOM   8531  O O   . PHE C  1 54  ? -12.006 -12.054 -60.409  1.00 35.09  ? 54  PHE C O   1 
ATOM   8532  C CB  . PHE C  1 54  ? -10.744 -14.866 -61.014  1.00 30.66  ? 54  PHE C CB  1 
ATOM   8533  C CG  . PHE C  1 54  ? -10.054 -16.132 -60.603  1.00 29.98  ? 54  PHE C CG  1 
ATOM   8534  C CD1 . PHE C  1 54  ? -10.492 -16.855 -59.504  1.00 30.06  ? 54  PHE C CD1 1 
ATOM   8535  C CD2 . PHE C  1 54  ? -8.950  -16.585 -61.304  1.00 29.34  ? 54  PHE C CD2 1 
ATOM   8536  C CE1 . PHE C  1 54  ? -9.835  -18.023 -59.121  1.00 32.07  ? 54  PHE C CE1 1 
ATOM   8537  C CE2 . PHE C  1 54  ? -8.292  -17.738 -60.934  1.00 29.45  ? 54  PHE C CE2 1 
ATOM   8538  C CZ  . PHE C  1 54  ? -8.729  -18.457 -59.832  1.00 32.13  ? 54  PHE C CZ  1 
ATOM   8539  N N   . ASN C  1 55  ? -10.259 -11.704 -61.794  1.00 30.89  ? 55  ASN C N   1 
ATOM   8540  C CA  . ASN C  1 55  ? -10.902 -10.674 -62.605  1.00 29.76  ? 55  ASN C CA  1 
ATOM   8541  C C   . ASN C  1 55  ? -11.147 -11.219 -64.006  1.00 31.57  ? 55  ASN C C   1 
ATOM   8542  O O   . ASN C  1 55  ? -10.236 -11.795 -64.614  1.00 29.40  ? 55  ASN C O   1 
ATOM   8543  C CB  . ASN C  1 55  ? -10.047 -9.410  -62.679  1.00 29.02  ? 55  ASN C CB  1 
ATOM   8544  C CG  . ASN C  1 55  ? -10.796 -8.248  -63.276  1.00 32.00  ? 55  ASN C CG  1 
ATOM   8545  O OD1 . ASN C  1 55  ? -11.786 -7.794  -62.704  1.00 32.18  ? 55  ASN C OD1 1 
ATOM   8546  N ND2 . ASN C  1 55  ? -10.335 -7.753  -64.430  1.00 27.38  ? 55  ASN C ND2 1 
ATOM   8547  N N   . LEU C  1 56  ? -12.378 -11.046 -64.499  1.00 29.41  ? 56  LEU C N   1 
ATOM   8548  C CA  . LEU C  1 56  ? -12.782 -11.368 -65.867  1.00 31.94  ? 56  LEU C CA  1 
ATOM   8549  C C   . LEU C  1 56  ? -13.300 -10.094 -66.520  1.00 30.84  ? 56  LEU C C   1 
ATOM   8550  O O   . LEU C  1 56  ? -14.342 -9.572  -66.114  1.00 32.81  ? 56  LEU C O   1 
ATOM   8551  C CB  . LEU C  1 56  ? -13.881 -12.421 -65.894  1.00 33.71  ? 56  LEU C CB  1 
ATOM   8552  C CG  . LEU C  1 56  ? -13.616 -13.798 -65.333  1.00 32.32  ? 56  LEU C CG  1 
ATOM   8553  C CD1 . LEU C  1 56  ? -14.919 -14.565 -65.430  1.00 30.39  ? 56  LEU C CD1 1 
ATOM   8554  C CD2 . LEU C  1 56  ? -12.511 -14.459 -66.127  1.00 35.33  ? 56  LEU C CD2 1 
ATOM   8555  N N   . THR C  1 57  ? -12.583 -9.589  -67.518  1.00 26.49  ? 57  THR C N   1 
ATOM   8556  C CA  . THR C  1 57  ? -13.079 -8.427  -68.238  1.00 30.39  ? 57  THR C CA  1 
ATOM   8557  C C   . THR C  1 57  ? -14.293 -8.824  -69.074  1.00 32.61  ? 57  THR C C   1 
ATOM   8558  O O   . THR C  1 57  ? -14.350 -9.941  -69.605  1.00 26.83  ? 57  THR C O   1 
ATOM   8559  C CB  . THR C  1 57  ? -12.014 -7.820  -69.152  1.00 29.83  ? 57  THR C CB  1 
ATOM   8560  O OG1 . THR C  1 57  ? -11.671 -8.766  -70.175  1.00 30.69  ? 57  THR C OG1 1 
ATOM   8561  C CG2 . THR C  1 57  ? -10.767 -7.415  -68.349  1.00 28.79  ? 57  THR C CG2 1 
ATOM   8562  N N   . PRO C  1 58  ? -15.279 -7.938  -69.202  1.00 37.05  ? 58  PRO C N   1 
ATOM   8563  C CA  . PRO C  1 58  ? -16.486 -8.297  -69.960  1.00 37.57  ? 58  PRO C CA  1 
ATOM   8564  C C   . PRO C  1 58  ? -16.202 -8.606  -71.413  1.00 36.18  ? 58  PRO C C   1 
ATOM   8565  O O   . PRO C  1 58  ? -16.894 -9.443  -72.004  1.00 39.21  ? 58  PRO C O   1 
ATOM   8566  C CB  . PRO C  1 58  ? -17.371 -7.055  -69.808  1.00 37.61  ? 58  PRO C CB  1 
ATOM   8567  C CG  . PRO C  1 58  ? -16.832 -6.343  -68.576  1.00 38.49  ? 58  PRO C CG  1 
ATOM   8568  C CD  . PRO C  1 58  ? -15.363 -6.592  -68.614  1.00 36.97  ? 58  PRO C CD  1 
ATOM   8569  N N   . VAL C  1 59  ? -15.203 -7.955  -72.013  1.00 34.78  ? 59  VAL C N   1 
ATOM   8570  C CA  . VAL C  1 59  ? -14.897 -8.243  -73.411  1.00 29.10  ? 59  VAL C CA  1 
ATOM   8571  C C   . VAL C  1 59  ? -14.327 -9.653  -73.542  1.00 28.62  ? 59  VAL C C   1 
ATOM   8572  O O   . VAL C  1 59  ? -14.540 -10.319 -74.556  1.00 31.17  ? 59  VAL C O   1 
ATOM   8573  C CB  . VAL C  1 59  ? -13.960 -7.165  -74.003  1.00 26.01  ? 59  VAL C CB  1 
ATOM   8574  C CG1 . VAL C  1 59  ? -12.684 -7.031  -73.194  1.00 23.41  ? 59  VAL C CG1 1 
ATOM   8575  C CG2 . VAL C  1 59  ? -13.636 -7.447  -75.486  1.00 27.32  ? 59  VAL C CG2 1 
ATOM   8576  N N   . LEU C  1 60  ? -13.630 -10.148 -72.515  1.00 25.26  ? 60  LEU C N   1 
ATOM   8577  C CA  . LEU C  1 60  ? -13.206 -11.547 -72.544  1.00 26.29  ? 60  LEU C CA  1 
ATOM   8578  C C   . LEU C  1 60  ? -14.399 -12.481 -72.373  1.00 29.56  ? 60  LEU C C   1 
ATOM   8579  O O   . LEU C  1 60  ? -14.493 -13.513 -73.052  1.00 32.92  ? 60  LEU C O   1 
ATOM   8580  C CB  . LEU C  1 60  ? -12.162 -11.813 -71.454  1.00 25.74  ? 60  LEU C CB  1 
ATOM   8581  C CG  . LEU C  1 60  ? -11.845 -13.288 -71.191  1.00 22.04  ? 60  LEU C CG  1 
ATOM   8582  C CD1 . LEU C  1 60  ? -11.258 -13.886 -72.469  1.00 28.26  ? 60  LEU C CD1 1 
ATOM   8583  C CD2 . LEU C  1 60  ? -10.893 -13.495 -70.007  1.00 20.17  ? 60  LEU C CD2 1 
ATOM   8584  N N   . ILE C  1 61  ? -15.320 -12.130 -71.472  1.00 31.47  ? 61  ILE C N   1 
ATOM   8585  C CA  . ILE C  1 61  ? -16.507 -12.952 -71.245  1.00 34.04  ? 61  ILE C CA  1 
ATOM   8586  C C   . ILE C  1 61  ? -17.311 -13.105 -72.532  1.00 34.50  ? 61  ILE C C   1 
ATOM   8587  O O   . ILE C  1 61  ? -17.814 -14.193 -72.836  1.00 36.70  ? 61  ILE C O   1 
ATOM   8588  C CB  . ILE C  1 61  ? -17.362 -12.347 -70.117  1.00 33.21  ? 61  ILE C CB  1 
ATOM   8589  C CG1 . ILE C  1 61  ? -16.615 -12.425 -68.786  1.00 31.16  ? 61  ILE C CG1 1 
ATOM   8590  C CG2 . ILE C  1 61  ? -18.707 -13.039 -70.037  1.00 35.45  ? 61  ILE C CG2 1 
ATOM   8591  C CD1 . ILE C  1 61  ? -17.393 -11.871 -67.592  1.00 32.05  ? 61  ILE C CD1 1 
ATOM   8592  N N   . ASP C  1 62  ? -17.472 -12.016 -73.288  1.00 35.37  ? 62  ASP C N   1 
ATOM   8593  C CA  . ASP C  1 62  ? -18.187 -12.094 -74.561  1.00 41.19  ? 62  ASP C CA  1 
ATOM   8594  C C   . ASP C  1 62  ? -17.568 -13.152 -75.461  1.00 45.61  ? 62  ASP C C   1 
ATOM   8595  O O   . ASP C  1 62  ? -18.265 -14.026 -75.992  1.00 45.86  ? 62  ASP C O   1 
ATOM   8596  C CB  . ASP C  1 62  ? -18.165 -10.740 -75.274  1.00 43.24  ? 62  ASP C CB  1 
ATOM   8597  C CG  . ASP C  1 62  ? -19.111 -9.730  -74.661  1.00 45.20  ? 62  ASP C CG  1 
ATOM   8598  O OD1 . ASP C  1 62  ? -20.092 -10.139 -74.010  1.00 46.81  ? 62  ASP C OD1 1 
ATOM   8599  O OD2 . ASP C  1 62  ? -18.872 -8.516  -74.839  1.00 45.37  ? 62  ASP C OD2 1 
ATOM   8600  N N   . GLN C  1 63  ? -16.247 -13.089 -75.634  1.00 43.76  ? 63  GLN C N   1 
ATOM   8601  C CA  . GLN C  1 63  ? -15.589 -13.998 -76.561  1.00 43.87  ? 63  GLN C CA  1 
ATOM   8602  C C   . GLN C  1 63  ? -15.696 -15.438 -76.089  1.00 41.36  ? 63  GLN C C   1 
ATOM   8603  O O   . GLN C  1 63  ? -15.958 -16.343 -76.894  1.00 35.54  ? 63  GLN C O   1 
ATOM   8604  C CB  . GLN C  1 63  ? -14.130 -13.600 -76.734  1.00 37.76  ? 63  GLN C CB  1 
ATOM   8605  C CG  . GLN C  1 63  ? -13.956 -12.237 -77.320  1.00 40.48  ? 63  GLN C CG  1 
ATOM   8606  C CD  . GLN C  1 63  ? -12.503 -11.854 -77.376  1.00 39.99  ? 63  GLN C CD  1 
ATOM   8607  O OE1 . GLN C  1 63  ? -11.727 -12.433 -78.141  1.00 34.65  ? 63  GLN C OE1 1 
ATOM   8608  N NE2 . GLN C  1 63  ? -12.115 -10.891 -76.545  1.00 32.45  ? 63  GLN C NE2 1 
ATOM   8609  N N   . ILE C  1 64  ? -15.493 -15.669 -74.790  1.00 40.09  ? 64  ILE C N   1 
ATOM   8610  C CA  . ILE C  1 64  ? -15.643 -17.015 -74.255  1.00 39.64  ? 64  ILE C CA  1 
ATOM   8611  C C   . ILE C  1 64  ? -17.034 -17.554 -74.572  1.00 37.86  ? 64  ILE C C   1 
ATOM   8612  O O   . ILE C  1 64  ? -17.177 -18.695 -75.014  1.00 31.75  ? 64  ILE C O   1 
ATOM   8613  C CB  . ILE C  1 64  ? -15.335 -17.031 -72.744  1.00 36.85  ? 64  ILE C CB  1 
ATOM   8614  C CG1 . ILE C  1 64  ? -13.841 -16.805 -72.514  1.00 32.47  ? 64  ILE C CG1 1 
ATOM   8615  C CG2 . ILE C  1 64  ? -15.716 -18.354 -72.129  1.00 34.70  ? 64  ILE C CG2 1 
ATOM   8616  C CD1 . ILE C  1 64  ? -13.439 -16.727 -71.039  1.00 26.55  ? 64  ILE C CD1 1 
ATOM   8617  N N   . GLN C  1 65  ? -18.073 -16.731 -74.395  1.00 40.88  ? 65  GLN C N   1 
ATOM   8618  C CA  . GLN C  1 65  ? -19.433 -17.180 -74.705  1.00 43.12  ? 65  GLN C CA  1 
ATOM   8619  C C   . GLN C  1 65  ? -19.595 -17.505 -76.187  1.00 40.42  ? 65  GLN C C   1 
ATOM   8620  O O   . GLN C  1 65  ? -20.296 -18.460 -76.549  1.00 39.15  ? 65  GLN C O   1 
ATOM   8621  C CB  . GLN C  1 65  ? -20.449 -16.114 -74.302  1.00 49.84  ? 65  GLN C CB  1 
ATOM   8622  C CG  . GLN C  1 65  ? -20.775 -16.069 -72.823  1.00 54.81  ? 65  GLN C CG  1 
ATOM   8623  C CD  . GLN C  1 65  ? -21.644 -14.882 -72.478  1.00 56.94  ? 65  GLN C CD  1 
ATOM   8624  O OE1 . GLN C  1 65  ? -21.393 -13.769 -72.938  1.00 56.97  ? 65  GLN C OE1 1 
ATOM   8625  N NE2 . GLN C  1 65  ? -22.677 -15.110 -71.672  1.00 58.10  ? 65  GLN C NE2 1 
ATOM   8626  N N   . GLU C  1 66  ? -18.962 -16.718 -77.058  1.00 36.18  ? 66  GLU C N   1 
ATOM   8627  C CA  . GLU C  1 66  ? -19.073 -16.962 -78.495  1.00 42.25  ? 66  GLU C CA  1 
ATOM   8628  C C   . GLU C  1 66  ? -18.369 -18.253 -78.901  1.00 40.26  ? 66  GLU C C   1 
ATOM   8629  O O   . GLU C  1 66  ? -18.846 -18.977 -79.781  1.00 37.87  ? 66  GLU C O   1 
ATOM   8630  C CB  . GLU C  1 66  ? -18.502 -15.775 -79.270  1.00 46.55  ? 66  GLU C CB  1 
ATOM   8631  C CG  . GLU C  1 66  ? -18.935 -15.713 -80.723  1.00 55.54  ? 66  GLU C CG  1 
ATOM   8632  C CD  . GLU C  1 66  ? -19.260 -14.304 -81.163  1.00 61.18  ? 66  GLU C CD  1 
ATOM   8633  O OE1 . GLU C  1 66  ? -18.440 -13.396 -80.905  1.00 57.76  ? 66  GLU C OE1 1 
ATOM   8634  O OE2 . GLU C  1 66  ? -20.340 -14.106 -81.761  1.00 67.79  ? 66  GLU C OE2 1 
ATOM   8635  N N   . TYR C  1 67  ? -17.217 -18.545 -78.298  1.00 39.47  ? 67  TYR C N   1 
ATOM   8636  C CA  . TYR C  1 67  ? -16.560 -19.814 -78.588  1.00 39.85  ? 67  TYR C CA  1 
ATOM   8637  C C   . TYR C  1 67  ? -17.378 -20.965 -78.048  1.00 44.16  ? 67  TYR C C   1 
ATOM   8638  O O   . TYR C  1 67  ? -17.509 -22.011 -78.698  1.00 50.04  ? 67  TYR C O   1 
ATOM   8639  C CB  . TYR C  1 67  ? -15.173 -19.845 -77.966  1.00 37.65  ? 67  TYR C CB  1 
ATOM   8640  C CG  . TYR C  1 67  ? -14.110 -19.278 -78.856  1.00 33.26  ? 67  TYR C CG  1 
ATOM   8641  C CD1 . TYR C  1 67  ? -13.467 -20.074 -79.793  1.00 32.77  ? 67  TYR C CD1 1 
ATOM   8642  C CD2 . TYR C  1 67  ? -13.733 -17.950 -78.746  1.00 34.24  ? 67  TYR C CD2 1 
ATOM   8643  C CE1 . TYR C  1 67  ? -12.479 -19.555 -80.608  1.00 33.24  ? 67  TYR C CE1 1 
ATOM   8644  C CE2 . TYR C  1 67  ? -12.744 -17.420 -79.545  1.00 34.85  ? 67  TYR C CE2 1 
ATOM   8645  C CZ  . TYR C  1 67  ? -12.117 -18.222 -80.472  1.00 32.84  ? 67  TYR C CZ  1 
ATOM   8646  O OH  . TYR C  1 67  ? -11.142 -17.675 -81.277  1.00 32.94  ? 67  TYR C OH  1 
ATOM   8647  N N   . ALA C  1 68  ? -17.913 -20.782 -76.838  1.00 40.00  ? 68  ALA C N   1 
ATOM   8648  C CA  . ALA C  1 68  ? -18.748 -21.797 -76.221  1.00 38.31  ? 68  ALA C CA  1 
ATOM   8649  C C   . ALA C  1 68  ? -19.905 -22.177 -77.132  1.00 42.05  ? 68  ALA C C   1 
ATOM   8650  O O   . ALA C  1 68  ? -20.087 -23.359 -77.450  1.00 46.52  ? 68  ALA C O   1 
ATOM   8651  C CB  . ALA C  1 68  ? -19.251 -21.297 -74.861  1.00 35.81  ? 68  ALA C CB  1 
ATOM   8652  N N   . GLN C  1 69  ? -20.672 -21.193 -77.603  1.00 42.38  ? 69  GLN C N   1 
ATOM   8653  C CA  . GLN C  1 69  ? -21.816 -21.510 -78.455  1.00 46.99  ? 69  GLN C CA  1 
ATOM   8654  C C   . GLN C  1 69  ? -21.428 -22.113 -79.801  1.00 49.45  ? 69  GLN C C   1 
ATOM   8655  O O   . GLN C  1 69  ? -22.320 -22.568 -80.526  1.00 49.60  ? 69  GLN C O   1 
ATOM   8656  C CB  . GLN C  1 69  ? -22.655 -20.263 -78.696  1.00 52.38  ? 69  GLN C CB  1 
ATOM   8657  C CG  . GLN C  1 69  ? -23.487 -19.870 -77.512  1.00 60.10  ? 69  GLN C CG  1 
ATOM   8658  C CD  . GLN C  1 69  ? -24.301 -18.639 -77.789  1.00 68.01  ? 69  GLN C CD  1 
ATOM   8659  O OE1 . GLN C  1 69  ? -25.525 -18.655 -77.694  1.00 74.74  ? 69  GLN C OE1 1 
ATOM   8660  N NE2 . GLN C  1 69  ? -23.622 -17.554 -78.152  1.00 66.01  ? 69  GLN C NE2 1 
ATOM   8661  N N   . GLY C  1 70  ? -20.142 -22.139 -80.152  1.00 50.97  ? 70  GLY C N   1 
ATOM   8662  C CA  . GLY C  1 70  ? -19.740 -22.629 -81.455  1.00 53.50  ? 70  GLY C CA  1 
ATOM   8663  C C   . GLY C  1 70  ? -19.940 -21.643 -82.580  1.00 55.52  ? 70  GLY C C   1 
ATOM   8664  O O   . GLY C  1 70  ? -19.893 -22.030 -83.751  1.00 58.58  ? 70  GLY C O   1 
ATOM   8665  N N   . LYS C  1 71  ? -20.171 -20.373 -82.259  1.00 56.01  ? 71  LYS C N   1 
ATOM   8666  C CA  . LYS C  1 71  ? -20.391 -19.333 -83.249  1.00 53.28  ? 71  LYS C CA  1 
ATOM   8667  C C   . LYS C  1 71  ? -19.141 -18.505 -83.508  1.00 52.79  ? 71  LYS C C   1 
ATOM   8668  O O   . LYS C  1 71  ? -19.234 -17.441 -84.126  1.00 56.09  ? 71  LYS C O   1 
ATOM   8669  C CB  . LYS C  1 71  ? -21.543 -18.428 -82.808  1.00 53.73  ? 71  LYS C CB  1 
ATOM   8670  N N   . ALA C  1 72  ? -17.976 -18.963 -83.055  1.00 45.97  ? 72  ALA C N   1 
ATOM   8671  C CA  . ALA C  1 72  ? -16.729 -18.229 -83.224  1.00 44.87  ? 72  ALA C CA  1 
ATOM   8672  C C   . ALA C  1 72  ? -16.014 -18.733 -84.472  1.00 46.82  ? 72  ALA C C   1 
ATOM   8673  O O   . ALA C  1 72  ? -15.680 -19.922 -84.567  1.00 45.44  ? 72  ALA C O   1 
ATOM   8674  C CB  . ALA C  1 72  ? -15.839 -18.374 -81.990  1.00 47.41  ? 72  ALA C CB  1 
ATOM   8675  N N   . LYS C  1 73  ? -15.780 -17.827 -85.424  1.00 43.94  ? 73  LYS C N   1 
ATOM   8676  C CA  . LYS C  1 73  ? -15.081 -18.137 -86.671  1.00 40.91  ? 73  LYS C CA  1 
ATOM   8677  C C   . LYS C  1 73  ? -13.638 -17.667 -86.531  1.00 37.24  ? 73  LYS C C   1 
ATOM   8678  O O   . LYS C  1 73  ? -13.334 -16.489 -86.728  1.00 42.55  ? 73  LYS C O   1 
ATOM   8679  C CB  . LYS C  1 73  ? -15.775 -17.472 -87.857  1.00 38.56  ? 73  LYS C CB  1 
ATOM   8680  C CG  . LYS C  1 73  ? -17.288 -17.592 -87.808  1.00 44.11  ? 73  LYS C CG  1 
ATOM   8681  C CD  . LYS C  1 73  ? -17.935 -17.289 -89.174  1.00 53.32  ? 73  LYS C CD  1 
ATOM   8682  C CE  . LYS C  1 73  ? -18.681 -15.958 -89.146  1.00 57.08  ? 73  LYS C CE  1 
ATOM   8683  N NZ  . LYS C  1 73  ? -19.930 -16.007 -89.962  1.00 65.07  ? 73  LYS C NZ  1 
ATOM   8684  N N   . ASP C  1 74  ? -12.735 -18.589 -86.240  1.00 34.62  ? 74  ASP C N   1 
ATOM   8685  C CA  . ASP C  1 74  ? -11.346 -18.293 -85.955  1.00 35.89  ? 74  ASP C CA  1 
ATOM   8686  C C   . ASP C  1 74  ? -10.489 -18.790 -87.018  1.00 39.88  ? 74  ASP C C   1 
ATOM   8687  O O   . ASP C  1 74  ? -10.387 -19.946 -87.239  1.00 44.19  ? 74  ASP C O   1 
ATOM   8688  C CB  . ASP C  1 74  ? -10.996 -18.852 -84.553  1.00 38.77  ? 74  ASP C CB  1 
ATOM   8689  C CG  . ASP C  1 74  ? -9.561  -18.711 -84.173  1.00 43.10  ? 74  ASP C CG  1 
ATOM   8690  O OD1 . ASP C  1 74  ? -8.663  -18.910 -84.988  1.00 45.37  ? 74  ASP C OD1 1 
ATOM   8691  O OD2 . ASP C  1 74  ? -9.336  -18.435 -82.995  1.00 42.68  ? 74  ASP C OD2 1 
ATOM   8692  N N   . VAL C  1 75  ? -9.755  -17.912 -87.602  1.00 44.66  ? 75  VAL C N   1 
ATOM   8693  C CA  . VAL C  1 75  ? -9.016  -18.208 -88.753  1.00 45.22  ? 75  VAL C CA  1 
ATOM   8694  C C   . VAL C  1 75  ? -7.883  -19.135 -88.565  1.00 42.35  ? 75  VAL C C   1 
ATOM   8695  O O   . VAL C  1 75  ? -7.809  -20.066 -89.308  1.00 39.31  ? 75  VAL C O   1 
ATOM   8696  C CB  . VAL C  1 75  ? -8.604  -16.896 -89.400  1.00 48.64  ? 75  VAL C CB  1 
ATOM   8697  C CG1 . VAL C  1 75  ? -7.942  -15.970 -88.412  1.00 52.61  ? 75  VAL C CG1 1 
ATOM   8698  C CG2 . VAL C  1 75  ? -7.695  -17.139 -90.583  1.00 51.32  ? 75  VAL C CG2 1 
ATOM   8699  N N   . PHE C  1 76  ? -7.050  -18.940 -87.557  1.00 41.84  ? 76  PHE C N   1 
ATOM   8700  C CA  . PHE C  1 76  ? -5.997  -19.897 -87.266  1.00 38.79  ? 76  PHE C CA  1 
ATOM   8701  C C   . PHE C  1 76  ? -6.598  -21.255 -86.983  1.00 40.14  ? 76  PHE C C   1 
ATOM   8702  O O   . PHE C  1 76  ? -6.177  -22.210 -87.506  1.00 43.07  ? 76  PHE C O   1 
ATOM   8703  C CB  . PHE C  1 76  ? -5.092  -19.401 -86.149  1.00 42.62  ? 76  PHE C CB  1 
ATOM   8704  C CG  . PHE C  1 76  ? -3.860  -20.166 -85.983  1.00 51.60  ? 76  PHE C CG  1 
ATOM   8705  C CD1 . PHE C  1 76  ? -2.748  -19.841 -86.698  1.00 57.60  ? 76  PHE C CD1 1 
ATOM   8706  C CD2 . PHE C  1 76  ? -3.811  -21.221 -85.096  1.00 59.74  ? 76  PHE C CD2 1 
ATOM   8707  C CE1 . PHE C  1 76  ? -1.595  -20.572 -86.560  1.00 62.82  ? 76  PHE C CE1 1 
ATOM   8708  C CE2 . PHE C  1 76  ? -2.661  -21.961 -84.949  1.00 63.47  ? 76  PHE C CE2 1 
ATOM   8709  C CZ  . PHE C  1 76  ? -1.551  -21.636 -85.689  1.00 64.44  ? 76  PHE C CZ  1 
ATOM   8710  N N   . LEU C  1 77  ? -7.611  -21.312 -86.180  1.00 39.01  ? 77  LEU C N   1 
ATOM   8711  C CA  . LEU C  1 77  ? -8.209  -22.552 -85.864  1.00 39.02  ? 77  LEU C CA  1 
ATOM   8712  C C   . LEU C  1 77  ? -8.770  -23.294 -87.089  1.00 43.85  ? 77  LEU C C   1 
ATOM   8713  O O   . LEU C  1 77  ? -8.557  -24.468 -87.215  1.00 44.00  ? 77  LEU C O   1 
ATOM   8714  C CB  . LEU C  1 77  ? -9.272  -22.393 -84.836  1.00 41.82  ? 77  LEU C CB  1 
ATOM   8715  C CG  . LEU C  1 77  ? -9.415  -23.338 -83.662  1.00 43.44  ? 77  LEU C CG  1 
ATOM   8716  C CD1 . LEU C  1 77  ? -8.063  -23.732 -83.101  1.00 42.20  ? 77  LEU C CD1 1 
ATOM   8717  C CD2 . LEU C  1 77  ? -10.243 -22.632 -82.617  1.00 43.80  ? 77  LEU C CD2 1 
ATOM   8718  N N   . GLU C  1 78  ? -9.512  -22.616 -87.937  1.00 40.52  ? 78  GLU C N   1 
ATOM   8719  C CA  . GLU C  1 78  ? -9.931  -23.285 -89.167  1.00 45.78  ? 78  GLU C CA  1 
ATOM   8720  C C   . GLU C  1 78  ? -8.739  -23.928 -89.861  1.00 48.31  ? 78  GLU C C   1 
ATOM   8721  O O   . GLU C  1 78  ? -8.845  -25.030 -90.414  1.00 53.37  ? 78  GLU C O   1 
ATOM   8722  C CB  . GLU C  1 78  ? -10.624 -22.304 -90.120  1.00 54.15  ? 78  GLU C CB  1 
ATOM   8723  C CG  . GLU C  1 78  ? -11.713 -21.437 -89.502  1.00 64.33  ? 78  GLU C CG  1 
ATOM   8724  C CD  . GLU C  1 78  ? -12.012 -20.181 -90.327  1.00 74.42  ? 78  GLU C CD  1 
ATOM   8725  O OE1 . GLU C  1 78  ? -11.400 -20.005 -91.406  1.00 76.92  ? 78  GLU C OE1 1 
ATOM   8726  O OE2 . GLU C  1 78  ? -12.851 -19.361 -89.890  1.00 76.73  ? 78  GLU C OE2 1 
ATOM   8727  N N   . ALA C  1 79  ? -7.584  -23.258 -89.824  1.00 43.61  ? 79  ALA C N   1 
ATOM   8728  C CA  . ALA C  1 79  ? -6.374  -23.823 -90.408  1.00 39.81  ? 79  ALA C CA  1 
ATOM   8729  C C   . ALA C  1 79  ? -5.842  -25.017 -89.628  1.00 41.71  ? 79  ALA C C   1 
ATOM   8730  O O   . ALA C  1 79  ? -5.113  -25.835 -90.203  1.00 43.83  ? 79  ALA C O   1 
ATOM   8731  C CB  . ALA C  1 79  ? -5.287  -22.760 -90.506  1.00 37.35  ? 79  ALA C CB  1 
ATOM   8732  N N   . ILE C  1 80  ? -6.152  -25.118 -88.332  1.00 37.72  ? 80  ILE C N   1 
ATOM   8733  C CA  . ILE C  1 80  ? -5.796  -26.311 -87.581  1.00 35.18  ? 80  ILE C CA  1 
ATOM   8734  C C   . ILE C  1 80  ? -6.746  -27.453 -87.901  1.00 34.11  ? 80  ILE C C   1 
ATOM   8735  O O   . ILE C  1 80  ? -6.308  -28.573 -88.179  1.00 34.04  ? 80  ILE C O   1 
ATOM   8736  C CB  . ILE C  1 80  ? -5.778  -26.024 -86.067  1.00 36.72  ? 80  ILE C CB  1 
ATOM   8737  C CG1 . ILE C  1 80  ? -4.663  -25.045 -85.719  1.00 41.19  ? 80  ILE C CG1 1 
ATOM   8738  C CG2 . ILE C  1 80  ? -5.634  -27.334 -85.308  1.00 35.72  ? 80  ILE C CG2 1 
ATOM   8739  C CD1 . ILE C  1 80  ? -3.304  -25.673 -85.691  1.00 44.57  ? 80  ILE C CD1 1 
ATOM   8740  N N   . ARG C  1 81  ? -8.059  -27.185 -87.864  1.00 40.76  ? 81  ARG C N   1 
ATOM   8741  C CA  . ARG C  1 81  ? -9.056  -28.242 -88.050  1.00 48.45  ? 81  ARG C CA  1 
ATOM   8742  C C   . ARG C  1 81  ? -8.963  -28.901 -89.424  1.00 51.26  ? 81  ARG C C   1 
ATOM   8743  O O   . ARG C  1 81  ? -9.240  -30.100 -89.545  1.00 54.86  ? 81  ARG C O   1 
ATOM   8744  C CB  . ARG C  1 81  ? -10.470 -27.687 -87.837  1.00 54.46  ? 81  ARG C CB  1 
ATOM   8745  C CG  . ARG C  1 81  ? -11.479 -28.712 -87.301  1.00 60.61  ? 81  ARG C CG  1 
ATOM   8746  C CD  . ARG C  1 81  ? -12.826 -28.064 -86.955  1.00 65.69  ? 81  ARG C CD  1 
ATOM   8747  N NE  . ARG C  1 81  ? -13.538 -28.752 -85.869  1.00 69.24  ? 81  ARG C NE  1 
ATOM   8748  C CZ  . ARG C  1 81  ? -13.949 -28.166 -84.744  1.00 68.56  ? 81  ARG C CZ  1 
ATOM   8749  N NH1 . ARG C  1 81  ? -13.726 -26.876 -84.545  1.00 65.32  ? 81  ARG C NH1 1 
ATOM   8750  N NH2 . ARG C  1 81  ? -14.594 -28.867 -83.818  1.00 71.43  ? 81  ARG C NH2 1 
ATOM   8751  N N   . LYS C  1 82  ? -8.575  -28.148 -90.455  1.00 47.32  ? 82  LYS C N   1 
ATOM   8752  C CA  . LYS C  1 82  ? -8.563  -28.651 -91.830  1.00 48.11  ? 82  LYS C CA  1 
ATOM   8753  C C   . LYS C  1 82  ? -7.641  -29.858 -91.999  1.00 50.01  ? 82  LYS C C   1 
ATOM   8754  O O   . LYS C  1 82  ? -6.565  -29.936 -91.402  1.00 50.02  ? 82  LYS C O   1 
ATOM   8755  C CB  . LYS C  1 82  ? -8.090  -27.553 -92.787  1.00 45.62  ? 82  LYS C CB  1 
ATOM   8756  C CG  . LYS C  1 82  ? -9.174  -26.697 -93.404  1.00 43.00  ? 82  LYS C CG  1 
ATOM   8757  C CD  . LYS C  1 82  ? -8.546  -25.553 -94.196  1.00 44.00  ? 82  LYS C CD  1 
ATOM   8758  C CE  . LYS C  1 82  ? -9.608  -24.753 -94.945  1.00 49.63  ? 82  LYS C CE  1 
ATOM   8759  N NZ  . LYS C  1 82  ? -9.035  -23.610 -95.711  1.00 51.66  ? 82  LYS C NZ  1 
ATOM   8760  N N   . ASP C  1 83  ? -8.061  -30.790 -92.849  1.00 51.80  ? 83  ASP C N   1 
ATOM   8761  C CA  . ASP C  1 83  ? -7.127  -31.759 -93.399  1.00 50.94  ? 83  ASP C CA  1 
ATOM   8762  C C   . ASP C  1 83  ? -5.977  -31.016 -94.079  1.00 48.33  ? 83  ASP C C   1 
ATOM   8763  O O   . ASP C  1 83  ? -6.213  -30.039 -94.803  1.00 45.37  ? 83  ASP C O   1 
ATOM   8764  C CB  . ASP C  1 83  ? -7.836  -32.670 -94.409  1.00 55.27  ? 83  ASP C CB  1 
ATOM   8765  C CG  . ASP C  1 83  ? -7.031  -33.929 -94.750  1.00 52.78  ? 83  ASP C CG  1 
ATOM   8766  O OD1 . ASP C  1 83  ? -5.918  -33.810 -95.306  1.00 51.03  ? 83  ASP C OD1 1 
ATOM   8767  O OD2 . ASP C  1 83  ? -7.522  -35.047 -94.466  1.00 52.34  ? 83  ASP C OD2 1 
ATOM   8768  N N   . PRO C  1 84  ? -4.725  -31.426 -93.850  1.00 43.42  ? 84  PRO C N   1 
ATOM   8769  C CA  . PRO C  1 84  ? -3.590  -30.719 -94.474  1.00 42.38  ? 84  PRO C CA  1 
ATOM   8770  C C   . PRO C  1 84  ? -3.659  -30.610 -95.986  1.00 47.51  ? 84  PRO C C   1 
ATOM   8771  O O   . PRO C  1 84  ? -3.022  -29.713 -96.546  1.00 48.37  ? 84  PRO C O   1 
ATOM   8772  C CB  . PRO C  1 84  ? -2.380  -31.552 -94.038  1.00 42.10  ? 84  PRO C CB  1 
ATOM   8773  C CG  . PRO C  1 84  ? -2.797  -32.094 -92.697  1.00 40.06  ? 84  PRO C CG  1 
ATOM   8774  C CD  . PRO C  1 84  ? -4.281  -32.390 -92.823  1.00 43.32  ? 84  PRO C CD  1 
ATOM   8775  N N   . ASP C  1 85  ? -4.370  -31.508 -96.668  1.00 49.66  ? 85  ASP C N   1 
ATOM   8776  C CA  . ASP C  1 85  ? -4.474  -31.424 -98.119  1.00 49.99  ? 85  ASP C CA  1 
ATOM   8777  C C   . ASP C  1 85  ? -5.299  -30.227 -98.568  1.00 50.23  ? 85  ASP C C   1 
ATOM   8778  O O   . ASP C  1 85  ? -5.146  -29.786 -99.712  1.00 51.63  ? 85  ASP C O   1 
ATOM   8779  C CB  . ASP C  1 85  ? -5.086  -32.702 -98.681  1.00 54.03  ? 85  ASP C CB  1 
ATOM   8780  C CG  . ASP C  1 85  ? -4.113  -33.875 -98.689  1.00 54.53  ? 85  ASP C CG  1 
ATOM   8781  O OD1 . ASP C  1 85  ? -2.881  -33.644 -98.730  1.00 52.54  ? 85  ASP C OD1 1 
ATOM   8782  O OD2 . ASP C  1 85  ? -4.594  -35.033 -98.682  1.00 53.47  ? 85  ASP C OD2 1 
ATOM   8783  N N   . ASP C  1 86  ? -6.165  -29.699 -97.699  1.00 49.21  ? 86  ASP C N   1 
ATOM   8784  C CA  . ASP C  1 86  ? -6.981  -28.521 -97.981  1.00 49.87  ? 86  ASP C CA  1 
ATOM   8785  C C   . ASP C  1 86  ? -6.304  -27.222 -97.584  1.00 44.48  ? 86  ASP C C   1 
ATOM   8786  O O   . ASP C  1 86  ? -6.870  -26.152 -97.814  1.00 47.92  ? 86  ASP C O   1 
ATOM   8787  C CB  . ASP C  1 86  ? -8.331  -28.607 -97.251  1.00 59.21  ? 86  ASP C CB  1 
ATOM   8788  C CG  . ASP C  1 86  ? -9.084  -29.890 -97.553  1.00 68.65  ? 86  ASP C CG  1 
ATOM   8789  O OD1 . ASP C  1 86  ? -8.901  -30.441 -98.661  1.00 67.94  ? 86  ASP C OD1 1 
ATOM   8790  O OD2 . ASP C  1 86  ? -9.857  -30.346 -96.680  1.00 73.71  ? 86  ASP C OD2 1 
ATOM   8791  N N   . LEU C  1 87  ? -5.133  -27.283 -96.964  1.00 43.38  ? 87  LEU C N   1 
ATOM   8792  C CA  . LEU C  1 87  ? -4.461  -26.065 -96.537  1.00 43.22  ? 87  LEU C CA  1 
ATOM   8793  C C   . LEU C  1 87  ? -4.019  -25.241 -97.743  1.00 43.40  ? 87  LEU C C   1 
ATOM   8794  O O   . LEU C  1 87  ? -3.471  -25.780 -98.709  1.00 42.83  ? 87  LEU C O   1 
ATOM   8795  C CB  . LEU C  1 87  ? -3.256  -26.407 -95.672  1.00 38.28  ? 87  LEU C CB  1 
ATOM   8796  C CG  . LEU C  1 87  ? -3.590  -26.827 -94.248  1.00 38.80  ? 87  LEU C CG  1 
ATOM   8797  C CD1 . LEU C  1 87  ? -2.334  -27.360 -93.616  1.00 41.65  ? 87  LEU C CD1 1 
ATOM   8798  C CD2 . LEU C  1 87  ? -4.124  -25.623 -93.467  1.00 36.15  ? 87  LEU C CD2 1 
ATOM   8799  N N   . GLU C  1 88  ? -4.267  -23.932 -97.678  1.00 46.27  ? 88  GLU C N   1 
ATOM   8800  C CA  . GLU C  1 88  ? -3.635  -22.985 -98.581  1.00 47.28  ? 88  GLU C CA  1 
ATOM   8801  C C   . GLU C  1 88  ? -2.202  -22.716 -98.138  1.00 47.27  ? 88  GLU C C   1 
ATOM   8802  O O   . GLU C  1 88  ? -1.845  -22.867 -96.960  1.00 39.87  ? 88  GLU C O   1 
ATOM   8803  C CB  . GLU C  1 88  ? -4.398  -21.659 -98.618  1.00 48.72  ? 88  GLU C CB  1 
ATOM   8804  C CG  . GLU C  1 88  ? -5.894  -21.777 -98.827  1.00 52.57  ? 88  GLU C CG  1 
ATOM   8805  C CD  . GLU C  1 88  ? -6.608  -20.459 -98.576  1.00 55.87  ? 88  GLU C CD  1 
ATOM   8806  O OE1 . GLU C  1 88  ? -7.714  -20.254 -99.118  1.00 62.70  ? 88  GLU C OE1 1 
ATOM   8807  O OE2 . GLU C  1 88  ? -6.050  -19.612 -97.857  1.00 54.45  ? 88  GLU C OE2 1 
ATOM   8808  N N   . LYS C  1 89  ? -1.379  -22.302 -99.102  1.00 42.55  ? 89  LYS C N   1 
ATOM   8809  C CA  . LYS C  1 89  ? -0.002  -21.932 -98.790  1.00 52.17  ? 89  LYS C CA  1 
ATOM   8810  C C   . LYS C  1 89  ? 0.045   -20.844 -97.714  1.00 47.60  ? 89  LYS C C   1 
ATOM   8811  O O   . LYS C  1 89  ? 0.854   -20.916 -96.779  1.00 48.58  ? 89  LYS C O   1 
ATOM   8812  C CB  . LYS C  1 89  ? 0.705   -21.476 -100.071 1.00 55.74  ? 89  LYS C CB  1 
ATOM   8813  C CG  . LYS C  1 89  ? 2.160   -21.884 -100.153 1.00 57.08  ? 89  LYS C CG  1 
ATOM   8814  C CD  . LYS C  1 89  ? 2.695   -21.687 -101.564 1.00 64.56  ? 89  LYS C CD  1 
ATOM   8815  C CE  . LYS C  1 89  ? 3.059   -20.231 -101.808 1.00 70.03  ? 89  LYS C CE  1 
ATOM   8816  N NZ  . LYS C  1 89  ? 3.628   -19.601 -100.571 1.00 66.41  ? 89  LYS C NZ  1 
ATOM   8817  N N   . GLU C  1 90  ? -0.836  -19.842 -97.816  1.00 46.29  ? 90  GLU C N   1 
ATOM   8818  C CA  . GLU C  1 90  ? -0.938  -18.818 -96.778  1.00 50.44  ? 90  GLU C CA  1 
ATOM   8819  C C   . GLU C  1 90  ? -1.172  -19.440 -95.407  1.00 42.77  ? 90  GLU C C   1 
ATOM   8820  O O   . GLU C  1 90  ? -0.587  -18.998 -94.411  1.00 42.13  ? 90  GLU C O   1 
ATOM   8821  C CB  . GLU C  1 90  ? -2.066  -17.843 -97.120  1.00 59.86  ? 90  GLU C CB  1 
ATOM   8822  C CG  . GLU C  1 90  ? -1.965  -16.491 -96.431  1.00 71.13  ? 90  GLU C CG  1 
ATOM   8823  C CD  . GLU C  1 90  ? -2.959  -16.330 -95.293  1.00 80.73  ? 90  GLU C CD  1 
ATOM   8824  O OE1 . GLU C  1 90  ? -3.314  -17.343 -94.649  1.00 84.10  ? 90  GLU C OE1 1 
ATOM   8825  O OE2 . GLU C  1 90  ? -3.389  -15.184 -95.043  1.00 84.01  ? 90  GLU C OE2 1 
ATOM   8826  N N   . GLU C  1 91  ? -2.020  -20.469 -95.338  1.00 41.43  ? 91  GLU C N   1 
ATOM   8827  C CA  . GLU C  1 91  ? -2.351  -21.080 -94.050  1.00 40.61  ? 91  GLU C CA  1 
ATOM   8828  C C   . GLU C  1 91  ? -1.199  -21.923 -93.510  1.00 41.26  ? 91  GLU C C   1 
ATOM   8829  O O   . GLU C  1 91  ? -0.994  -22.010 -92.284  1.00 34.72  ? 91  GLU C O   1 
ATOM   8830  C CB  . GLU C  1 91  ? -3.600  -21.948 -94.183  1.00 42.29  ? 91  GLU C CB  1 
ATOM   8831  C CG  . GLU C  1 91  ? -4.868  -21.199 -94.511  1.00 45.56  ? 91  GLU C CG  1 
ATOM   8832  C CD  . GLU C  1 91  ? -6.058  -22.131 -94.617  1.00 50.14  ? 91  GLU C CD  1 
ATOM   8833  O OE1 . GLU C  1 91  ? -6.062  -23.000 -95.521  1.00 50.98  ? 91  GLU C OE1 1 
ATOM   8834  O OE2 . GLU C  1 91  ? -6.978  -22.015 -93.775  1.00 48.88  ? 91  GLU C OE2 1 
ATOM   8835  N N   . VAL C  1 92  ? -0.470  -22.535 -94.390  1.00 40.02  ? 92  VAL C N   1 
ATOM   8836  C CA  . VAL C  1 92  ? 0.644   -23.297 -93.961  1.00 44.02  ? 92  VAL C CA  1 
ATOM   8837  C C   . VAL C  1 92  ? 1.672   -22.366 -93.358  1.00 44.02  ? 92  VAL C C   1 
ATOM   8838  O O   . VAL C  1 92  ? 2.151   -22.607 -92.293  1.00 41.21  ? 92  VAL C O   1 
ATOM   8839  C CB  . VAL C  1 92  ? 1.221   -24.218 -95.081  1.00 41.97  ? 92  VAL C CB  1 
ATOM   8840  C CG1 . VAL C  1 92  ? 2.484   -24.915 -94.629  1.00 40.74  ? 92  VAL C CG1 1 
ATOM   8841  C CG2 . VAL C  1 92  ? 0.169   -25.181 -95.569  1.00 40.84  ? 92  VAL C CG2 1 
ATOM   8842  N N   . GLU C  1 93  ? 1.951   -21.284 -94.017  1.00 42.13  ? 93  GLU C N   1 
ATOM   8843  C CA  . GLU C  1 93  ? 2.925   -20.327 -93.509  1.00 45.58  ? 93  GLU C CA  1 
ATOM   8844  C C   . GLU C  1 93  ? 2.510   -19.705 -92.139  1.00 39.41  ? 93  GLU C C   1 
ATOM   8845  O O   . GLU C  1 93  ? 3.302   -19.424 -91.334  1.00 38.89  ? 93  GLU C O   1 
ATOM   8846  C CB  . GLU C  1 93  ? 3.256   -19.303 -94.572  1.00 48.65  ? 93  GLU C CB  1 
ATOM   8847  C CG  . GLU C  1 93  ? 4.497   -19.678 -95.379  1.00 60.33  ? 93  GLU C CG  1 
ATOM   8848  C CD  . GLU C  1 93  ? 5.563   -18.579 -95.504  1.00 68.40  ? 93  GLU C CD  1 
ATOM   8849  O OE1 . GLU C  1 93  ? 5.922   -18.236 -96.645  1.00 71.46  ? 93  GLU C OE1 1 
ATOM   8850  O OE2 . GLU C  1 93  ? 6.088   -18.084 -94.483  1.00 70.35  ? 93  GLU C OE2 1 
ATOM   8851  N N   . LYS C  1 94  ? 1.260   -19.582 -91.940  1.00 37.19  ? 94  LYS C N   1 
ATOM   8852  C CA  . LYS C  1 94  ? 0.772   -19.085 -90.704  1.00 40.43  ? 94  LYS C CA  1 
ATOM   8853  C C   . LYS C  1 94  ? 1.016   -20.093 -89.594  1.00 37.19  ? 94  LYS C C   1 
ATOM   8854  O O   . LYS C  1 94  ? 1.480   -19.727 -88.565  1.00 35.79  ? 94  LYS C O   1 
ATOM   8855  C CB  . LYS C  1 94  ? -0.654  -18.789 -90.941  1.00 46.68  ? 94  LYS C CB  1 
ATOM   8856  C CG  . LYS C  1 94  ? -1.501  -18.568 -89.734  1.00 56.73  ? 94  LYS C CG  1 
ATOM   8857  C CD  . LYS C  1 94  ? -2.954  -18.568 -90.169  1.00 61.29  ? 94  LYS C CD  1 
ATOM   8858  C CE  . LYS C  1 94  ? -3.583  -19.926 -89.945  1.00 57.58  ? 94  LYS C CE  1 
ATOM   8859  N NZ  . LYS C  1 94  ? -2.601  -21.015 -90.166  1.00 56.02  ? 94  LYS C NZ  1 
ATOM   8860  N N   . LEU C  1 95  ? 0.737   -21.352 -89.846  1.00 40.56  ? 95  LEU C N   1 
ATOM   8861  C CA  . LEU C  1 95  ? 1.037   -22.417 -88.913  1.00 39.67  ? 95  LEU C CA  1 
ATOM   8862  C C   . LEU C  1 95  ? 2.469   -22.451 -88.521  1.00 35.96  ? 95  LEU C C   1 
ATOM   8863  O O   . LEU C  1 95  ? 2.789   -22.552 -87.388  1.00 30.10  ? 95  LEU C O   1 
ATOM   8864  C CB  . LEU C  1 95  ? 0.691   -23.714 -89.553  1.00 38.00  ? 95  LEU C CB  1 
ATOM   8865  C CG  . LEU C  1 95  ? 0.216   -24.861 -88.692  1.00 46.61  ? 95  LEU C CG  1 
ATOM   8866  C CD1 . LEU C  1 95  ? -0.997  -24.409 -87.917  1.00 49.49  ? 95  LEU C CD1 1 
ATOM   8867  C CD2 . LEU C  1 95  ? -0.146  -26.012 -89.598  1.00 47.39  ? 95  LEU C CD2 1 
ATOM   8868  N N   . ILE C  1 96  ? 3.340   -22.326 -89.491  1.00 33.46  ? 96  ILE C N   1 
ATOM   8869  C CA  . ILE C  1 96  ? 4.725   -22.368 -89.208  1.00 36.00  ? 96  ILE C CA  1 
ATOM   8870  C C   . ILE C  1 96  ? 5.221   -21.126 -88.444  1.00 37.70  ? 96  ILE C C   1 
ATOM   8871  O O   . ILE C  1 96  ? 6.018   -21.272 -87.559  1.00 37.71  ? 96  ILE C O   1 
ATOM   8872  C CB  . ILE C  1 96  ? 5.533   -22.621 -90.503  1.00 42.78  ? 96  ILE C CB  1 
ATOM   8873  C CG1 . ILE C  1 96  ? 5.038   -23.878 -91.199  1.00 43.57  ? 96  ILE C CG1 1 
ATOM   8874  C CG2 . ILE C  1 96  ? 7.011   -22.751 -90.210  1.00 44.88  ? 96  ILE C CG2 1 
ATOM   8875  C CD1 . ILE C  1 96  ? 5.554   -24.013 -92.605  1.00 49.13  ? 96  ILE C CD1 1 
ATOM   8876  N N   . GLU C  1 97  ? 4.710   -19.946 -88.764  1.00 36.00  ? 97  GLU C N   1 
ATOM   8877  C CA  . GLU C  1 97  ? 5.061   -18.738 -88.062  1.00 35.58  ? 97  GLU C CA  1 
ATOM   8878  C C   . GLU C  1 97  ? 4.623   -18.826 -86.613  1.00 38.88  ? 97  GLU C C   1 
ATOM   8879  O O   . GLU C  1 97  ? 5.355   -18.482 -85.755  1.00 38.24  ? 97  GLU C O   1 
ATOM   8880  C CB  . GLU C  1 97  ? 4.401   -17.553 -88.691  1.00 50.96  ? 97  GLU C CB  1 
ATOM   8881  C CG  . GLU C  1 97  ? 4.858   -16.210 -88.109  1.00 66.08  ? 97  GLU C CG  1 
ATOM   8882  C CD  . GLU C  1 97  ? 4.159   -14.981 -88.681  1.00 78.30  ? 97  GLU C CD  1 
ATOM   8883  O OE1 . GLU C  1 97  ? 3.047   -15.105 -89.225  1.00 82.37  ? 97  GLU C OE1 1 
ATOM   8884  O OE2 . GLU C  1 97  ? 4.722   -13.869 -88.590  1.00 81.89  ? 97  GLU C OE2 1 
ATOM   8885  N N   . PHE C  1 98  ? 3.415   -19.265 -86.421  1.00 36.37  ? 98  PHE C N   1 
ATOM   8886  C CA  . PHE C  1 98  ? 2.896   -19.458 -85.102  1.00 33.03  ? 98  PHE C CA  1 
ATOM   8887  C C   . PHE C  1 98  ? 3.737   -20.435 -84.309  1.00 32.54  ? 98  PHE C C   1 
ATOM   8888  O O   . PHE C  1 98  ? 3.957   -20.218 -83.158  1.00 38.21  ? 98  PHE C O   1 
ATOM   8889  C CB  . PHE C  1 98  ? 1.515   -19.959 -85.229  1.00 32.67  ? 98  PHE C CB  1 
ATOM   8890  C CG  . PHE C  1 98  ? 0.756   -19.981 -83.941  1.00 35.16  ? 98  PHE C CG  1 
ATOM   8891  C CD1 . PHE C  1 98  ? 0.193   -18.841 -83.442  1.00 39.30  ? 98  PHE C CD1 1 
ATOM   8892  C CD2 . PHE C  1 98  ? 0.595   -21.146 -83.244  1.00 36.38  ? 98  PHE C CD2 1 
ATOM   8893  C CE1 . PHE C  1 98  ? -0.515  -18.857 -82.260  1.00 37.67  ? 98  PHE C CE1 1 
ATOM   8894  C CE2 . PHE C  1 98  ? -0.121  -21.176 -82.068  1.00 30.27  ? 98  PHE C CE2 1 
ATOM   8895  C CZ  . PHE C  1 98  ? -0.674  -20.035 -81.576  1.00 34.42  ? 98  PHE C CZ  1 
ATOM   8896  N N   . THR C  1 99  ? 4.207   -21.493 -84.929  1.00 31.82  ? 99  THR C N   1 
ATOM   8897  C CA  . THR C  1 99  ? 5.004   -22.435 -84.288  1.00 32.85  ? 99  THR C CA  1 
ATOM   8898  C C   . THR C  1 99  ? 6.344   -21.777 -83.903  1.00 34.79  ? 99  THR C C   1 
ATOM   8899  O O   . THR C  1 99  ? 6.784   -21.861 -82.811  1.00 32.20  ? 99  THR C O   1 
ATOM   8900  C CB  . THR C  1 99  ? 5.108   -23.771 -85.114  1.00 36.29  ? 99  THR C CB  1 
ATOM   8901  O OG1 . THR C  1 99  ? 3.821   -24.341 -85.305  1.00 38.85  ? 99  THR C OG1 1 
ATOM   8902  C CG2 . THR C  1 99  ? 6.007   -24.767 -84.433  1.00 36.89  ? 99  THR C CG2 1 
ATOM   8903  N N   . LYS C  1 100 ? 7.001   -21.145 -84.831  1.00 38.28  ? 100 LYS C N   1 
ATOM   8904  C CA  . LYS C  1 100 ? 8.286   -20.538 -84.502  1.00 45.09  ? 100 LYS C CA  1 
ATOM   8905  C C   . LYS C  1 100 ? 8.144   -19.438 -83.456  1.00 40.72  ? 100 LYS C C   1 
ATOM   8906  O O   . LYS C  1 100 ? 9.065   -19.230 -82.657  1.00 39.38  ? 100 LYS C O   1 
ATOM   8907  C CB  . LYS C  1 100 ? 8.961   -20.005 -85.768  1.00 51.41  ? 100 LYS C CB  1 
ATOM   8908  C CG  . LYS C  1 100 ? 9.972   -20.983 -86.374  1.00 56.44  ? 100 LYS C CG  1 
ATOM   8909  C CD  . LYS C  1 100 ? 10.942  -21.545 -85.323  1.00 63.26  ? 100 LYS C CD  1 
ATOM   8910  C CE  . LYS C  1 100 ? 12.097  -22.312 -85.968  1.00 68.10  ? 100 LYS C CE  1 
ATOM   8911  N NZ  . LYS C  1 100 ? 13.245  -22.495 -85.034  1.00 68.76  ? 100 LYS C NZ  1 
ATOM   8912  N N   . LEU C  1 101 ? 7.001   -18.742 -83.432  1.00 34.51  ? 101 LEU C N   1 
ATOM   8913  C CA  . LEU C  1 101 ? 6.779   -17.706 -82.426  1.00 39.83  ? 101 LEU C CA  1 
ATOM   8914  C C   . LEU C  1 101 ? 6.736   -18.299 -81.021  1.00 36.86  ? 101 LEU C C   1 
ATOM   8915  O O   . LEU C  1 101 ? 7.174   -17.661 -80.056  1.00 34.80  ? 101 LEU C O   1 
ATOM   8916  C CB  . LEU C  1 101 ? 5.482   -16.957 -82.730  1.00 43.33  ? 101 LEU C CB  1 
ATOM   8917  C CG  . LEU C  1 101 ? 5.093   -15.822 -81.790  1.00 48.79  ? 101 LEU C CG  1 
ATOM   8918  C CD1 . LEU C  1 101 ? 5.997   -14.617 -82.009  1.00 50.90  ? 101 LEU C CD1 1 
ATOM   8919  C CD2 . LEU C  1 101 ? 3.636   -15.457 -81.999  1.00 51.96  ? 101 LEU C CD2 1 
ATOM   8920  N N   . ASN C  1 102 ? 6.192   -19.509 -80.894  1.00 38.46  ? 102 ASN C N   1 
ATOM   8921  C CA  . ASN C  1 102 ? 6.037   -20.217 -79.628  1.00 37.40  ? 102 ASN C CA  1 
ATOM   8922  C C   . ASN C  1 102 ? 7.123   -21.267 -79.401  1.00 38.82  ? 102 ASN C C   1 
ATOM   8923  O O   . ASN C  1 102 ? 7.140   -21.921 -78.344  1.00 33.48  ? 102 ASN C O   1 
ATOM   8924  C CB  . ASN C  1 102 ? 4.657   -20.875 -79.584  1.00 36.81  ? 102 ASN C CB  1 
ATOM   8925  C CG  . ASN C  1 102 ? 3.518   -19.859 -79.630  1.00 37.73  ? 102 ASN C CG  1 
ATOM   8926  O OD1 . ASN C  1 102 ? 3.431   -18.962 -78.783  1.00 34.36  ? 102 ASN C OD1 1 
ATOM   8927  N ND2 . ASN C  1 102 ? 2.628   -20.011 -80.609  1.00 30.46  ? 102 ASN C ND2 1 
ATOM   8928  N N   . TYR C  1 103 ? 8.057   -21.382 -80.348  1.00 36.78  ? 103 TYR C N   1 
ATOM   8929  C CA  . TYR C  1 103 ? 9.003   -22.491 -80.410  1.00 38.38  ? 103 TYR C CA  1 
ATOM   8930  C C   . TYR C  1 103 ? 9.813   -22.648 -79.123  1.00 36.14  ? 103 TYR C C   1 
ATOM   8931  O O   . TYR C  1 103 ? 10.107  -23.774 -78.705  1.00 36.70  ? 103 TYR C O   1 
ATOM   8932  C CB  . TYR C  1 103 ? 9.926   -22.271 -81.618  1.00 43.09  ? 103 TYR C CB  1 
ATOM   8933  C CG  . TYR C  1 103 ? 10.935  -23.365 -81.857  1.00 51.16  ? 103 TYR C CG  1 
ATOM   8934  C CD1 . TYR C  1 103 ? 10.611  -24.472 -82.625  1.00 53.50  ? 103 TYR C CD1 1 
ATOM   8935  C CD2 . TYR C  1 103 ? 12.216  -23.288 -81.326  1.00 55.47  ? 103 TYR C CD2 1 
ATOM   8936  C CE1 . TYR C  1 103 ? 11.532  -25.474 -82.855  1.00 58.89  ? 103 TYR C CE1 1 
ATOM   8937  C CE2 . TYR C  1 103 ? 13.144  -24.286 -81.549  1.00 60.12  ? 103 TYR C CE2 1 
ATOM   8938  C CZ  . TYR C  1 103 ? 12.796  -25.377 -82.314  1.00 65.36  ? 103 TYR C CZ  1 
ATOM   8939  O OH  . TYR C  1 103 ? 13.718  -26.373 -82.540  1.00 78.85  ? 103 TYR C OH  1 
ATOM   8940  N N   . GLU C  1 104 ? 10.209  -21.543 -78.494  1.00 37.22  ? 104 GLU C N   1 
ATOM   8941  C CA  . GLU C  1 104 ? 11.129  -21.612 -77.364  1.00 39.74  ? 104 GLU C CA  1 
ATOM   8942  C C   . GLU C  1 104 ? 10.421  -21.660 -76.018  1.00 38.36  ? 104 GLU C C   1 
ATOM   8943  O O   . GLU C  1 104 ? 11.079  -21.549 -74.979  1.00 40.08  ? 104 GLU C O   1 
ATOM   8944  C CB  . GLU C  1 104 ? 12.108  -20.437 -77.394  1.00 39.18  ? 104 GLU C CB  1 
ATOM   8945  C CG  . GLU C  1 104 ? 12.977  -20.395 -78.657  1.00 39.87  ? 104 GLU C CG  1 
ATOM   8946  C CD  . GLU C  1 104 ? 14.086  -21.448 -78.695  1.00 48.46  ? 104 GLU C CD  1 
ATOM   8947  O OE1 . GLU C  1 104 ? 14.361  -22.109 -77.670  1.00 55.06  ? 104 GLU C OE1 1 
ATOM   8948  O OE2 . GLU C  1 104 ? 14.693  -21.611 -79.772  1.00 56.19  ? 104 GLU C OE2 1 
ATOM   8949  N N   . LYS C  1 105 ? 9.146   -21.824 -76.012  1.00 37.41  ? 105 LYS C N   1 
ATOM   8950  C CA  . LYS C  1 105 ? 8.467   -21.941 -74.731  1.00 31.66  ? 105 LYS C CA  1 
ATOM   8951  C C   . LYS C  1 105 ? 8.478   -23.395 -74.262  1.00 31.81  ? 105 LYS C C   1 
ATOM   8952  O O   . LYS C  1 105 ? 8.449   -24.315 -75.079  1.00 27.87  ? 105 LYS C O   1 
ATOM   8953  C CB  . LYS C  1 105 ? 7.032   -21.432 -74.847  1.00 29.23  ? 105 LYS C CB  1 
ATOM   8954  C CG  . LYS C  1 105 ? 6.960   -19.954 -75.221  1.00 30.11  ? 105 LYS C CG  1 
ATOM   8955  C CD  . LYS C  1 105 ? 5.624   -19.558 -75.820  1.00 26.23  ? 105 LYS C CD  1 
ATOM   8956  C CE  . LYS C  1 105 ? 5.616   -18.062 -76.134  1.00 31.12  ? 105 LYS C CE  1 
ATOM   8957  N NZ  . LYS C  1 105 ? 4.286   -17.587 -76.623  1.00 34.26  ? 105 LYS C NZ  1 
ATOM   8958  N N   . PRO C  1 106 ? 8.546   -23.642 -72.949  1.00 29.72  ? 106 PRO C N   1 
ATOM   8959  C CA  . PRO C  1 106 ? 8.548   -25.033 -72.471  1.00 28.71  ? 106 PRO C CA  1 
ATOM   8960  C C   . PRO C  1 106 ? 7.316   -25.823 -72.881  1.00 27.57  ? 106 PRO C C   1 
ATOM   8961  O O   . PRO C  1 106 ? 7.400   -27.046 -73.029  1.00 32.73  ? 106 PRO C O   1 
ATOM   8962  C CB  . PRO C  1 106 ? 8.637   -24.875 -70.941  1.00 33.88  ? 106 PRO C CB  1 
ATOM   8963  C CG  . PRO C  1 106 ? 9.329   -23.565 -70.746  1.00 32.86  ? 106 PRO C CG  1 
ATOM   8964  C CD  . PRO C  1 106 ? 8.838   -22.680 -71.871  1.00 30.92  ? 106 PRO C CD  1 
ATOM   8965  N N   . ILE C  1 107 ? 6.170   -25.172 -73.077  1.00 29.62  ? 107 ILE C N   1 
ATOM   8966  C CA  . ILE C  1 107 ? 4.975   -25.934 -73.407  1.00 30.69  ? 107 ILE C CA  1 
ATOM   8967  C C   . ILE C  1 107 ? 5.025   -26.458 -74.835  1.00 33.51  ? 107 ILE C C   1 
ATOM   8968  O O   . ILE C  1 107 ? 4.248   -27.350 -75.198  1.00 31.15  ? 107 ILE C O   1 
ATOM   8969  C CB  . ILE C  1 107 ? 3.711   -25.087 -73.179  1.00 27.61  ? 107 ILE C CB  1 
ATOM   8970  C CG1 . ILE C  1 107 ? 3.847   -23.721 -73.845  1.00 25.24  ? 107 ILE C CG1 1 
ATOM   8971  C CG2 . ILE C  1 107 ? 3.413   -24.935 -71.691  1.00 26.21  ? 107 ILE C CG2 1 
ATOM   8972  C CD1 . ILE C  1 107 ? 2.487   -23.092 -74.145  1.00 30.19  ? 107 ILE C CD1 1 
ATOM   8973  N N   . TYR C  1 108 ? 5.932   -25.932 -75.652  1.00 33.14  ? 108 TYR C N   1 
ATOM   8974  C CA  . TYR C  1 108 ? 6.152   -26.412 -77.006  1.00 34.48  ? 108 TYR C CA  1 
ATOM   8975  C C   . TYR C  1 108 ? 7.299   -27.408 -77.099  1.00 36.14  ? 108 TYR C C   1 
ATOM   8976  O O   . TYR C  1 108 ? 7.637   -27.838 -78.197  1.00 36.39  ? 108 TYR C O   1 
ATOM   8977  C CB  . TYR C  1 108 ? 6.404   -25.228 -77.937  1.00 32.62  ? 108 TYR C CB  1 
ATOM   8978  C CG  . TYR C  1 108 ? 5.129   -24.724 -78.558  1.00 34.15  ? 108 TYR C CG  1 
ATOM   8979  C CD1 . TYR C  1 108 ? 4.204   -23.996 -77.812  1.00 29.86  ? 108 TYR C CD1 1 
ATOM   8980  C CD2 . TYR C  1 108 ? 4.833   -24.999 -79.888  1.00 32.58  ? 108 TYR C CD2 1 
ATOM   8981  C CE1 . TYR C  1 108 ? 3.023   -23.539 -78.390  1.00 27.09  ? 108 TYR C CE1 1 
ATOM   8982  C CE2 . TYR C  1 108 ? 3.667   -24.556 -80.462  1.00 33.34  ? 108 TYR C CE2 1 
ATOM   8983  C CZ  . TYR C  1 108 ? 2.766   -23.827 -79.716  1.00 31.18  ? 108 TYR C CZ  1 
ATOM   8984  O OH  . TYR C  1 108 ? 1.605   -23.396 -80.313  1.00 30.66  ? 108 TYR C OH  1 
ATOM   8985  N N   . ARG C  1 109 ? 7.892   -27.803 -75.971  1.00 38.24  ? 109 ARG C N   1 
ATOM   8986  C CA  . ARG C  1 109 ? 9.045   -28.700 -75.978  1.00 44.35  ? 109 ARG C CA  1 
ATOM   8987  C C   . ARG C  1 109 ? 8.569   -30.100 -76.362  1.00 45.33  ? 109 ARG C C   1 
ATOM   8988  O O   . ARG C  1 109 ? 8.278   -30.957 -75.521  1.00 42.42  ? 109 ARG C O   1 
ATOM   8989  C CB  . ARG C  1 109 ? 9.745   -28.689 -74.619  1.00 51.22  ? 109 ARG C CB  1 
ATOM   8990  C CG  . ARG C  1 109 ? 10.916  -29.655 -74.515  1.00 59.99  ? 109 ARG C CG  1 
ATOM   8991  C CD  . ARG C  1 109 ? 11.502  -29.681 -73.103  1.00 65.68  ? 109 ARG C CD  1 
ATOM   8992  N NE  . ARG C  1 109 ? 10.977  -30.775 -72.278  1.00 68.57  ? 109 ARG C NE  1 
ATOM   8993  C CZ  . ARG C  1 109 ? 11.127  -32.075 -72.539  1.00 71.18  ? 109 ARG C CZ  1 
ATOM   8994  N NH1 . ARG C  1 109 ? 11.798  -32.480 -73.614  1.00 71.01  ? 109 ARG C NH1 1 
ATOM   8995  N NH2 . ARG C  1 109 ? 10.605  -32.980 -71.716  1.00 71.85  ? 109 ARG C NH2 1 
ATOM   8996  N N   . PHE C  1 110 ? 8.455   -30.314 -77.671  1.00 45.57  ? 110 PHE C N   1 
ATOM   8997  C CA  . PHE C  1 110 ? 8.142   -31.611 -78.260  1.00 43.96  ? 110 PHE C CA  1 
ATOM   8998  C C   . PHE C  1 110 ? 9.241   -31.970 -79.247  1.00 43.91  ? 110 PHE C C   1 
ATOM   8999  O O   . PHE C  1 110 ? 9.578   -31.160 -80.117  1.00 44.68  ? 110 PHE C O   1 
ATOM   9000  C CB  . PHE C  1 110 ? 6.805   -31.595 -79.007  1.00 40.62  ? 110 PHE C CB  1 
ATOM   9001  C CG  . PHE C  1 110 ? 5.601   -31.495 -78.123  1.00 32.98  ? 110 PHE C CG  1 
ATOM   9002  C CD1 . PHE C  1 110 ? 5.093   -32.622 -77.499  1.00 29.91  ? 110 PHE C CD1 1 
ATOM   9003  C CD2 . PHE C  1 110 ? 4.949   -30.280 -77.955  1.00 29.10  ? 110 PHE C CD2 1 
ATOM   9004  C CE1 . PHE C  1 110 ? 3.969   -32.540 -76.703  1.00 32.41  ? 110 PHE C CE1 1 
ATOM   9005  C CE2 . PHE C  1 110 ? 3.830   -30.190 -77.167  1.00 30.02  ? 110 PHE C CE2 1 
ATOM   9006  C CZ  . PHE C  1 110 ? 3.338   -31.325 -76.529  1.00 32.26  ? 110 PHE C CZ  1 
ATOM   9007  N N   . GLU C  1 111 ? 9.778   -33.188 -79.128  1.00 46.13  ? 111 GLU C N   1 
ATOM   9008  C CA  . GLU C  1 111 ? 10.798  -33.645 -80.068  1.00 52.50  ? 111 GLU C CA  1 
ATOM   9009  C C   . GLU C  1 111 ? 10.346  -33.462 -81.512  1.00 46.77  ? 111 GLU C C   1 
ATOM   9010  O O   . GLU C  1 111 ? 11.130  -33.034 -82.367  1.00 45.42  ? 111 GLU C O   1 
ATOM   9011  C CB  . GLU C  1 111 ? 11.133  -35.115 -79.809  1.00 66.17  ? 111 GLU C CB  1 
ATOM   9012  C CG  . GLU C  1 111 ? 11.149  -35.495 -78.337  1.00 77.05  ? 111 GLU C CG  1 
ATOM   9013  C CD  . GLU C  1 111 ? 11.823  -36.832 -78.083  1.00 84.91  ? 111 GLU C CD  1 
ATOM   9014  O OE1 . GLU C  1 111 ? 11.166  -37.879 -78.274  1.00 87.84  ? 111 GLU C OE1 1 
ATOM   9015  O OE2 . GLU C  1 111 ? 13.013  -36.836 -77.696  1.00 86.20  ? 111 GLU C OE2 1 
ATOM   9016  N N   . ARG C  1 112 ? 9.077   -33.760 -81.797  1.00 42.33  ? 112 ARG C N   1 
ATOM   9017  C CA  . ARG C  1 112 ? 8.602   -33.727 -83.175  1.00 46.17  ? 112 ARG C CA  1 
ATOM   9018  C C   . ARG C  1 112 ? 8.541   -32.305 -83.732  1.00 43.53  ? 112 ARG C C   1 
ATOM   9019  O O   . ARG C  1 112 ? 8.750   -32.108 -84.935  1.00 42.64  ? 112 ARG C O   1 
ATOM   9020  C CB  . ARG C  1 112 ? 7.235   -34.401 -83.260  1.00 45.89  ? 112 ARG C CB  1 
ATOM   9021  C CG  . ARG C  1 112 ? 6.639   -34.468 -84.657  1.00 42.30  ? 112 ARG C CG  1 
ATOM   9022  C CD  . ARG C  1 112 ? 7.395   -35.431 -85.560  1.00 45.12  ? 112 ARG C CD  1 
ATOM   9023  N NE  . ARG C  1 112 ? 6.526   -35.962 -86.609  1.00 45.30  ? 112 ARG C NE  1 
ATOM   9024  C CZ  . ARG C  1 112 ? 6.923   -36.265 -87.841  1.00 46.35  ? 112 ARG C CZ  1 
ATOM   9025  N NH1 . ARG C  1 112 ? 8.192   -36.089 -88.200  1.00 47.52  ? 112 ARG C NH1 1 
ATOM   9026  N NH2 . ARG C  1 112 ? 6.043   -36.735 -88.723  1.00 48.04  ? 112 ARG C NH2 1 
ATOM   9027  N N   . ILE C  1 113 ? 8.251   -31.311 -82.889  1.00 39.54  ? 113 ILE C N   1 
ATOM   9028  C CA  . ILE C  1 113 ? 8.232   -29.924 -83.353  1.00 40.96  ? 113 ILE C CA  1 
ATOM   9029  C C   . ILE C  1 113 ? 9.625   -29.499 -83.803  1.00 47.47  ? 113 ILE C C   1 
ATOM   9030  O O   . ILE C  1 113 ? 9.780   -28.784 -84.800  1.00 49.27  ? 113 ILE C O   1 
ATOM   9031  C CB  . ILE C  1 113 ? 7.665   -29.008 -82.250  1.00 39.73  ? 113 ILE C CB  1 
ATOM   9032  C CG1 . ILE C  1 113 ? 6.189   -29.316 -82.033  1.00 42.18  ? 113 ILE C CG1 1 
ATOM   9033  C CG2 . ILE C  1 113 ? 7.815   -27.534 -82.595  1.00 36.99  ? 113 ILE C CG2 1 
ATOM   9034  C CD1 . ILE C  1 113 ? 5.510   -28.342 -81.114  1.00 43.80  ? 113 ILE C CD1 1 
ATOM   9035  N N   . ARG C  1 114 ? 10.661  -29.963 -83.095  1.00 51.87  ? 114 ARG C N   1 
ATOM   9036  C CA  . ARG C  1 114 ? 12.035  -29.705 -83.516  1.00 55.30  ? 114 ARG C CA  1 
ATOM   9037  C C   . ARG C  1 114 ? 12.288  -30.245 -84.913  1.00 53.50  ? 114 ARG C C   1 
ATOM   9038  O O   . ARG C  1 114 ? 13.013  -29.631 -85.701  1.00 52.68  ? 114 ARG C O   1 
ATOM   9039  C CB  . ARG C  1 114 ? 13.022  -30.340 -82.535  1.00 60.88  ? 114 ARG C CB  1 
ATOM   9040  C CG  . ARG C  1 114 ? 12.914  -29.836 -81.107  1.00 66.16  ? 114 ARG C CG  1 
ATOM   9041  C CD  . ARG C  1 114 ? 14.109  -30.283 -80.277  1.00 72.42  ? 114 ARG C CD  1 
ATOM   9042  N NE  . ARG C  1 114 ? 14.338  -29.393 -79.141  1.00 77.85  ? 114 ARG C NE  1 
ATOM   9043  C CZ  . ARG C  1 114 ? 13.782  -29.549 -77.943  1.00 80.38  ? 114 ARG C CZ  1 
ATOM   9044  N NH1 . ARG C  1 114 ? 12.961  -30.567 -77.721  1.00 81.00  ? 114 ARG C NH1 1 
ATOM   9045  N NH2 . ARG C  1 114 ? 14.047  -28.688 -76.967  1.00 80.71  ? 114 ARG C NH2 1 
ATOM   9046  N N   . GLU C  1 115 ? 11.702  -31.399 -85.235  1.00 55.38  ? 115 GLU C N   1 
ATOM   9047  C CA  . GLU C  1 115 ? 11.944  -32.020 -86.533  1.00 54.26  ? 115 GLU C CA  1 
ATOM   9048  C C   . GLU C  1 115 ? 11.190  -31.306 -87.641  1.00 51.86  ? 115 GLU C C   1 
ATOM   9049  O O   . GLU C  1 115 ? 11.740  -31.075 -88.721  1.00 54.87  ? 115 GLU C O   1 
ATOM   9050  C CB  . GLU C  1 115 ? 11.539  -33.488 -86.491  1.00 55.54  ? 115 GLU C CB  1 
ATOM   9051  C CG  . GLU C  1 115 ? 12.464  -34.369 -85.684  1.00 59.41  ? 115 GLU C CG  1 
ATOM   9052  C CD  . GLU C  1 115 ? 11.766  -35.612 -85.185  1.00 62.85  ? 115 GLU C CD  1 
ATOM   9053  O OE1 . GLU C  1 115 ? 12.310  -36.281 -84.282  1.00 63.31  ? 115 GLU C OE1 1 
ATOM   9054  O OE2 . GLU C  1 115 ? 10.664  -35.915 -85.692  1.00 65.02  ? 115 GLU C OE2 1 
ATOM   9055  N N   . LEU C  1 116 ? 9.923   -30.968 -87.399  1.00 53.33  ? 116 LEU C N   1 
ATOM   9056  C CA  . LEU C  1 116 ? 9.123   -30.297 -88.419  1.00 52.43  ? 116 LEU C CA  1 
ATOM   9057  C C   . LEU C  1 116 ? 9.724   -28.954 -88.810  1.00 54.08  ? 116 LEU C C   1 
ATOM   9058  O O   . LEU C  1 116 ? 9.814   -28.630 -90.001  1.00 55.71  ? 116 LEU C O   1 
ATOM   9059  C CB  . LEU C  1 116 ? 7.694   -30.119 -87.915  1.00 48.65  ? 116 LEU C CB  1 
ATOM   9060  C CG  . LEU C  1 116 ? 7.011   -31.433 -87.530  1.00 46.77  ? 116 LEU C CG  1 
ATOM   9061  C CD1 . LEU C  1 116 ? 5.634   -31.182 -86.933  1.00 45.06  ? 116 LEU C CD1 1 
ATOM   9062  C CD2 . LEU C  1 116 ? 6.913   -32.349 -88.733  1.00 48.18  ? 116 LEU C CD2 1 
ATOM   9063  N N   . MET C  1 117 ? 10.143  -28.160 -87.824  1.00 51.48  ? 117 MET C N   1 
ATOM   9064  C CA  . MET C  1 117 ? 10.741  -26.856 -88.087  1.00 54.68  ? 117 MET C CA  1 
ATOM   9065  C C   . MET C  1 117 ? 12.141  -26.956 -88.676  1.00 62.13  ? 117 MET C C   1 
ATOM   9066  O O   . MET C  1 117 ? 12.690  -25.933 -89.102  1.00 66.78  ? 117 MET C O   1 
ATOM   9067  C CB  . MET C  1 117 ? 10.759  -26.038 -86.796  1.00 55.66  ? 117 MET C CB  1 
ATOM   9068  C CG  . MET C  1 117 ? 9.388   -25.880 -86.160  1.00 53.46  ? 117 MET C CG  1 
ATOM   9069  S SD  . MET C  1 117 ? 8.236   -24.968 -87.203  1.00 51.47  ? 117 MET C SD  1 
ATOM   9070  C CE  . MET C  1 117 ? 7.354   -26.288 -88.048  1.00 51.45  ? 117 MET C CE  1 
ATOM   9071  N N   . ASN C  1 118 ? 12.726  -28.151 -88.705  1.00 61.44  ? 118 ASN C N   1 
ATOM   9072  C CA  . ASN C  1 118 ? 13.974  -28.386 -89.414  1.00 67.57  ? 118 ASN C CA  1 
ATOM   9073  C C   . ASN C  1 118 ? 13.760  -28.819 -90.852  1.00 68.48  ? 118 ASN C C   1 
ATOM   9074  O O   . ASN C  1 118 ? 14.740  -28.948 -91.593  1.00 70.92  ? 118 ASN C O   1 
ATOM   9075  C CB  . ASN C  1 118 ? 14.803  -29.469 -88.717  1.00 73.55  ? 118 ASN C CB  1 
ATOM   9076  C CG  . ASN C  1 118 ? 15.300  -29.041 -87.361  1.00 79.54  ? 118 ASN C CG  1 
ATOM   9077  O OD1 . ASN C  1 118 ? 15.253  -27.861 -87.014  1.00 81.19  ? 118 ASN C OD1 1 
ATOM   9078  N ND2 . ASN C  1 118 ? 15.766  -30.007 -86.569  1.00 81.70  ? 118 ASN C ND2 1 
ATOM   9079  N N   . LYS C  1 119 ? 12.520  -29.061 -91.260  1.00 66.60  ? 119 LYS C N   1 
ATOM   9080  C CA  . LYS C  1 119 ? 12.239  -29.688 -92.541  1.00 66.07  ? 119 LYS C CA  1 
ATOM   9081  C C   . LYS C  1 119 ? 11.902  -28.645 -93.597  1.00 67.96  ? 119 LYS C C   1 
ATOM   9082  O O   . LYS C  1 119 ? 11.138  -27.708 -93.344  1.00 68.78  ? 119 LYS C O   1 
ATOM   9083  C CB  . LYS C  1 119 ? 11.108  -30.706 -92.404  1.00 62.26  ? 119 LYS C CB  1 
ATOM   9084  C CG  . LYS C  1 119 ? 11.631  -32.055 -91.951  1.00 63.03  ? 119 LYS C CG  1 
ATOM   9085  C CD  . LYS C  1 119 ? 10.526  -33.069 -91.728  1.00 63.13  ? 119 LYS C CD  1 
ATOM   9086  C CE  . LYS C  1 119 ? 11.085  -34.488 -91.731  1.00 64.40  ? 119 LYS C CE  1 
ATOM   9087  N NZ  . LYS C  1 119 ? 12.168  -34.690 -90.723  1.00 64.83  ? 119 LYS C NZ  1 
ATOM   9088  N N   . GLU C  1 120 ? 12.474  -28.837 -94.790  1.00 69.34  ? 120 GLU C N   1 
ATOM   9089  C CA  . GLU C  1 120 ? 12.391  -27.838 -95.854  1.00 70.86  ? 120 GLU C CA  1 
ATOM   9090  C C   . GLU C  1 120 ? 11.009  -27.811 -96.497  1.00 69.76  ? 120 GLU C C   1 
ATOM   9091  O O   . GLU C  1 120 ? 10.495  -26.737 -96.833  1.00 73.73  ? 120 GLU C O   1 
ATOM   9092  C CB  . GLU C  1 120 ? 13.470  -28.117 -96.898  1.00 71.69  ? 120 GLU C CB  1 
ATOM   9093  N N   . LYS C  1 121 ? 10.401  -28.979 -96.692  1.00 64.81  ? 121 LYS C N   1 
ATOM   9094  C CA  . LYS C  1 121 ? 9.037   -29.098 -97.185  1.00 63.34  ? 121 LYS C CA  1 
ATOM   9095  C C   . LYS C  1 121 ? 8.281   -30.074 -96.293  1.00 63.88  ? 121 LYS C C   1 
ATOM   9096  O O   . LYS C  1 121 ? 8.825   -31.110 -95.898  1.00 64.04  ? 121 LYS C O   1 
ATOM   9097  C CB  . LYS C  1 121 ? 9.009   -29.573 -98.648  1.00 63.47  ? 121 LYS C CB  1 
ATOM   9098  N N   . LEU C  1 122 ? 7.035   -29.741 -95.967  1.00 60.44  ? 122 LEU C N   1 
ATOM   9099  C CA  . LEU C  1 122 ? 6.208   -30.551 -95.081  1.00 57.74  ? 122 LEU C CA  1 
ATOM   9100  C C   . LEU C  1 122 ? 5.148   -31.282 -95.891  1.00 58.07  ? 122 LEU C C   1 
ATOM   9101  O O   . LEU C  1 122 ? 4.400   -30.651 -96.647  1.00 57.79  ? 122 LEU C O   1 
ATOM   9102  C CB  . LEU C  1 122 ? 5.533   -29.689 -94.011  1.00 49.94  ? 122 LEU C CB  1 
ATOM   9103  C CG  . LEU C  1 122 ? 6.367   -29.246 -92.809  1.00 50.98  ? 122 LEU C CG  1 
ATOM   9104  C CD1 . LEU C  1 122 ? 5.451   -28.842 -91.676  1.00 47.25  ? 122 LEU C CD1 1 
ATOM   9105  C CD2 . LEU C  1 122 ? 7.321   -30.345 -92.356  1.00 52.76  ? 122 LEU C CD2 1 
ATOM   9106  N N   . ASN C  1 123 ? 5.074   -32.604 -95.717  1.00 57.90  ? 123 ASN C N   1 
ATOM   9107  C CA  . ASN C  1 123 ? 4.036   -33.405 -96.350  1.00 53.66  ? 123 ASN C CA  1 
ATOM   9108  C C   . ASN C  1 123 ? 2.784   -33.408 -95.471  1.00 48.64  ? 123 ASN C C   1 
ATOM   9109  O O   . ASN C  1 123 ? 2.711   -32.718 -94.452  1.00 46.80  ? 123 ASN C O   1 
ATOM   9110  C CB  . ASN C  1 123 ? 4.540   -34.820 -96.653  1.00 53.33  ? 123 ASN C CB  1 
ATOM   9111  C CG  . ASN C  1 123 ? 4.942   -35.608 -95.402  1.00 52.46  ? 123 ASN C CG  1 
ATOM   9112  O OD1 . ASN C  1 123 ? 4.442   -35.380 -94.294  1.00 47.06  ? 123 ASN C OD1 1 
ATOM   9113  N ND2 . ASN C  1 123 ? 5.852   -36.561 -95.591  1.00 52.01  ? 123 ASN C ND2 1 
ATOM   9114  N N   . ARG C  1 124 ? 1.785   -34.204 -95.859  1.00 48.38  ? 124 ARG C N   1 
ATOM   9115  C CA  . ARG C  1 124 ? 0.495   -34.163 -95.177  1.00 43.25  ? 124 ARG C CA  1 
ATOM   9116  C C   . ARG C  1 124 ? 0.606   -34.663 -93.746  1.00 44.24  ? 124 ARG C C   1 
ATOM   9117  O O   . ARG C  1 124 ? 0.053   -34.058 -92.824  1.00 39.55  ? 124 ARG C O   1 
ATOM   9118  C CB  . ARG C  1 124 ? -0.537  -34.996 -95.932  1.00 45.75  ? 124 ARG C CB  1 
ATOM   9119  C CG  . ARG C  1 124 ? -1.846  -35.131 -95.178  1.00 46.73  ? 124 ARG C CG  1 
ATOM   9120  C CD  . ARG C  1 124 ? -2.813  -36.092 -95.858  1.00 52.80  ? 124 ARG C CD  1 
ATOM   9121  N NE  . ARG C  1 124 ? -4.075  -36.164 -95.125  1.00 56.55  ? 124 ARG C NE  1 
ATOM   9122  C CZ  . ARG C  1 124 ? -4.315  -37.002 -94.120  1.00 56.05  ? 124 ARG C CZ  1 
ATOM   9123  N NH1 . ARG C  1 124 ? -3.380  -37.851 -93.711  1.00 55.29  ? 124 ARG C NH1 1 
ATOM   9124  N NH2 . ARG C  1 124 ? -5.495  -36.985 -93.516  1.00 53.88  ? 124 ARG C NH2 1 
ATOM   9125  N N   . GLU C  1 125 ? 1.296   -35.781 -93.543  1.00 41.44  ? 125 GLU C N   1 
ATOM   9126  C CA  . GLU C  1 125 ? 1.302   -36.383 -92.223  1.00 48.54  ? 125 GLU C CA  1 
ATOM   9127  C C   . GLU C  1 125 ? 2.132   -35.546 -91.257  1.00 42.90  ? 125 GLU C C   1 
ATOM   9128  O O   . GLU C  1 125 ? 1.821   -35.468 -90.067  1.00 40.33  ? 125 GLU C O   1 
ATOM   9129  C CB  . GLU C  1 125 ? 1.829   -37.806 -92.334  1.00 57.24  ? 125 GLU C CB  1 
ATOM   9130  C CG  . GLU C  1 125 ? 0.851   -38.843 -92.906  1.00 68.13  ? 125 GLU C CG  1 
ATOM   9131  C CD  . GLU C  1 125 ? 0.226   -38.464 -94.278  1.00 74.24  ? 125 GLU C CD  1 
ATOM   9132  O OE1 . GLU C  1 125 ? -1.006  -38.202 -94.289  1.00 78.49  ? 125 GLU C OE1 1 
ATOM   9133  O OE2 . GLU C  1 125 ? 0.898   -38.444 -95.317  1.00 76.36  ? 125 GLU C OE2 1 
ATOM   9134  N N   . GLU C  1 126 ? 3.182   -34.899 -91.769  1.00 43.23  ? 126 GLU C N   1 
ATOM   9135  C CA  . GLU C  1 126 ? 3.946   -33.939 -90.979  1.00 42.99  ? 126 GLU C CA  1 
ATOM   9136  C C   . GLU C  1 126 ? 3.117   -32.707 -90.630  1.00 43.31  ? 126 GLU C C   1 
ATOM   9137  O O   . GLU C  1 126 ? 3.234   -32.170 -89.520  1.00 37.71  ? 126 GLU C O   1 
ATOM   9138  C CB  . GLU C  1 126 ? 5.215   -33.525 -91.728  1.00 44.39  ? 126 GLU C CB  1 
ATOM   9139  C CG  . GLU C  1 126 ? 6.250   -34.616 -91.778  1.00 45.87  ? 126 GLU C CG  1 
ATOM   9140  C CD  . GLU C  1 126 ? 7.179   -34.508 -92.963  1.00 52.17  ? 126 GLU C CD  1 
ATOM   9141  O OE1 . GLU C  1 126 ? 6.957   -33.648 -93.844  1.00 51.31  ? 126 GLU C OE1 1 
ATOM   9142  O OE2 . GLU C  1 126 ? 8.129   -35.315 -93.020  1.00 55.52  ? 126 GLU C OE2 1 
ATOM   9143  N N   . LEU C  1 127 ? 2.285   -32.235 -91.563  1.00 41.51  ? 127 LEU C N   1 
ATOM   9144  C CA  . LEU C  1 127 ? 1.410   -31.106 -91.255  1.00 38.05  ? 127 LEU C CA  1 
ATOM   9145  C C   . LEU C  1 127 ? 0.377   -31.481 -90.200  1.00 37.83  ? 127 LEU C C   1 
ATOM   9146  O O   . LEU C  1 127 ? 0.031   -30.657 -89.343  1.00 37.24  ? 127 LEU C O   1 
ATOM   9147  C CB  . LEU C  1 127 ? 0.711   -30.609 -92.521  1.00 35.57  ? 127 LEU C CB  1 
ATOM   9148  C CG  . LEU C  1 127 ? 1.552   -29.722 -93.441  1.00 38.64  ? 127 LEU C CG  1 
ATOM   9149  C CD1 . LEU C  1 127 ? 0.848   -29.425 -94.773  1.00 38.58  ? 127 LEU C CD1 1 
ATOM   9150  C CD2 . LEU C  1 127 ? 1.883   -28.446 -92.728  1.00 34.68  ? 127 LEU C CD2 1 
ATOM   9151  N N   . LEU C  1 128 ? -0.149  -32.706 -90.270  1.00 40.19  ? 128 LEU C N   1 
ATOM   9152  C CA  . LEU C  1 128 ? -1.087  -33.169 -89.257  1.00 40.22  ? 128 LEU C CA  1 
ATOM   9153  C C   . LEU C  1 128 ? -0.448  -33.127 -87.878  1.00 37.70  ? 128 LEU C C   1 
ATOM   9154  O O   . LEU C  1 128 ? -1.109  -32.790 -86.887  1.00 30.60  ? 128 LEU C O   1 
ATOM   9155  C CB  . LEU C  1 128 ? -1.553  -34.587 -89.588  1.00 43.03  ? 128 LEU C CB  1 
ATOM   9156  C CG  . LEU C  1 128 ? -2.929  -34.753 -90.238  1.00 48.06  ? 128 LEU C CG  1 
ATOM   9157  C CD1 . LEU C  1 128 ? -3.166  -36.206 -90.622  1.00 52.21  ? 128 LEU C CD1 1 
ATOM   9158  C CD2 . LEU C  1 128 ? -4.031  -34.256 -89.329  1.00 49.01  ? 128 LEU C CD2 1 
ATOM   9159  N N   . ASP C  1 129 ? 0.840   -33.475 -87.801  1.00 36.59  ? 129 ASP C N   1 
ATOM   9160  C CA  . ASP C  1 129 ? 1.560   -33.412 -86.536  1.00 41.47  ? 129 ASP C CA  1 
ATOM   9161  C C   . ASP C  1 129 ? 1.741   -31.972 -86.087  1.00 41.79  ? 129 ASP C C   1 
ATOM   9162  O O   . ASP C  1 129 ? 1.639   -31.672 -84.890  1.00 38.16  ? 129 ASP C O   1 
ATOM   9163  C CB  . ASP C  1 129 ? 2.916   -34.101 -86.668  1.00 44.82  ? 129 ASP C CB  1 
ATOM   9164  C CG  . ASP C  1 129 ? 2.815   -35.608 -86.587  1.00 45.86  ? 129 ASP C CG  1 
ATOM   9165  O OD1 . ASP C  1 129 ? 1.684   -36.143 -86.620  1.00 41.17  ? 129 ASP C OD1 1 
ATOM   9166  O OD2 . ASP C  1 129 ? 3.878   -36.258 -86.471  1.00 51.29  ? 129 ASP C OD2 1 
ATOM   9167  N N   . LEU C  1 130 ? 1.999   -31.067 -87.037  1.00 35.32  ? 130 LEU C N   1 
ATOM   9168  C CA  . LEU C  1 130 ? 2.161   -29.658 -86.694  1.00 36.24  ? 130 LEU C CA  1 
ATOM   9169  C C   . LEU C  1 130 ? 0.856   -29.073 -86.163  1.00 34.95  ? 130 LEU C C   1 
ATOM   9170  O O   . LEU C  1 130 ? 0.842   -28.393 -85.130  1.00 34.08  ? 130 LEU C O   1 
ATOM   9171  C CB  . LEU C  1 130 ? 2.658   -28.877 -87.913  1.00 35.38  ? 130 LEU C CB  1 
ATOM   9172  C CG  . LEU C  1 130 ? 3.124   -27.442 -87.659  1.00 34.96  ? 130 LEU C CG  1 
ATOM   9173  C CD1 . LEU C  1 130 ? 4.301   -27.409 -86.715  1.00 34.56  ? 130 LEU C CD1 1 
ATOM   9174  C CD2 . LEU C  1 130 ? 3.464   -26.720 -88.981  1.00 35.21  ? 130 LEU C CD2 1 
ATOM   9175  N N   . GLN C  1 131 ? -0.259  -29.355 -86.842  1.00 32.25  ? 131 GLN C N   1 
ATOM   9176  C CA  . GLN C  1 131 ? -1.557  -28.912 -86.342  1.00 28.77  ? 131 GLN C CA  1 
ATOM   9177  C C   . GLN C  1 131 ? -1.827  -29.485 -84.954  1.00 30.83  ? 131 GLN C C   1 
ATOM   9178  O O   . GLN C  1 131 ? -2.204  -28.762 -84.030  1.00 29.17  ? 131 GLN C O   1 
ATOM   9179  C CB  . GLN C  1 131 ? -2.661  -29.330 -87.306  1.00 28.65  ? 131 GLN C CB  1 
ATOM   9180  C CG  . GLN C  1 131 ? -2.490  -28.833 -88.744  1.00 30.93  ? 131 GLN C CG  1 
ATOM   9181  C CD  . GLN C  1 131 ? -3.491  -29.489 -89.664  1.00 32.16  ? 131 GLN C CD  1 
ATOM   9182  O OE1 . GLN C  1 131 ? -3.692  -30.707 -89.613  1.00 33.25  ? 131 GLN C OE1 1 
ATOM   9183  N NE2 . GLN C  1 131 ? -4.158  -28.689 -90.483  1.00 36.74  ? 131 GLN C NE2 1 
ATOM   9184  N N   . THR C  1 132 ? -1.625  -30.787 -84.785  1.00 33.78  ? 132 THR C N   1 
ATOM   9185  C CA  . THR C  1 132 ? -2.032  -31.404 -83.533  1.00 37.47  ? 132 THR C CA  1 
ATOM   9186  C C   . THR C  1 132 ? -1.121  -30.986 -82.385  1.00 41.02  ? 132 THR C C   1 
ATOM   9187  O O   . THR C  1 132 ? -1.598  -30.703 -81.282  1.00 38.55  ? 132 THR C O   1 
ATOM   9188  C CB  . THR C  1 132 ? -2.059  -32.915 -83.675  1.00 34.65  ? 132 THR C CB  1 
ATOM   9189  O OG1 . THR C  1 132 ? -2.789  -33.266 -84.862  1.00 36.68  ? 132 THR C OG1 1 
ATOM   9190  C CG2 . THR C  1 132 ? -2.745  -33.527 -82.457  1.00 34.38  ? 132 THR C CG2 1 
ATOM   9191  N N   . LEU C  1 133 ? 0.190   -30.928 -82.630  1.00 39.69  ? 133 LEU C N   1 
ATOM   9192  C CA  . LEU C  1 133 ? 1.121   -30.572 -81.567  1.00 35.00  ? 133 LEU C CA  1 
ATOM   9193  C C   . LEU C  1 133 ? 0.970   -29.117 -81.143  1.00 32.32  ? 133 LEU C C   1 
ATOM   9194  O O   . LEU C  1 133 ? 1.207   -28.787 -79.974  1.00 32.16  ? 133 LEU C O   1 
ATOM   9195  C CB  . LEU C  1 133 ? 2.549   -30.860 -82.008  1.00 32.99  ? 133 LEU C CB  1 
ATOM   9196  C CG  . LEU C  1 133 ? 2.920   -32.340 -81.875  1.00 30.91  ? 133 LEU C CG  1 
ATOM   9197  C CD1 . LEU C  1 133 ? 4.170   -32.631 -82.700  1.00 34.52  ? 133 LEU C CD1 1 
ATOM   9198  C CD2 . LEU C  1 133 ? 3.129   -32.709 -80.415  1.00 31.92  ? 133 LEU C CD2 1 
ATOM   9199  N N   . ASN C  1 134 ? 0.569   -28.235 -82.056  1.00 28.72  ? 134 ASN C N   1 
ATOM   9200  C CA  . ASN C  1 134 ? 0.211   -26.892 -81.626  1.00 30.98  ? 134 ASN C CA  1 
ATOM   9201  C C   . ASN C  1 134 ? -0.952  -26.955 -80.645  1.00 32.34  ? 134 ASN C C   1 
ATOM   9202  O O   . ASN C  1 134 ? -0.887  -26.376 -79.558  1.00 37.79  ? 134 ASN C O   1 
ATOM   9203  C CB  . ASN C  1 134 ? -0.111  -26.002 -82.832  1.00 32.78  ? 134 ASN C CB  1 
ATOM   9204  C CG  . ASN C  1 134 ? 1.104   -25.220 -83.330  1.00 31.48  ? 134 ASN C CG  1 
ATOM   9205  O OD1 . ASN C  1 134 ? 1.515   -24.219 -82.724  1.00 37.00  ? 134 ASN C OD1 1 
ATOM   9206  N ND2 . ASN C  1 134 ? 1.672   -25.661 -84.443  1.00 31.44  ? 134 ASN C ND2 1 
ATOM   9207  N N   . LEU C  1 135 ? -2.005  -27.702 -80.991  1.00 28.63  ? 135 LEU C N   1 
ATOM   9208  C CA  . LEU C  1 135 ? -3.118  -27.877 -80.059  1.00 28.93  ? 135 LEU C CA  1 
ATOM   9209  C C   . LEU C  1 135 ? -2.632  -28.440 -78.730  1.00 28.45  ? 135 LEU C C   1 
ATOM   9210  O O   . LEU C  1 135 ? -2.886  -27.858 -77.678  1.00 26.64  ? 135 LEU C O   1 
ATOM   9211  C CB  . LEU C  1 135 ? -4.178  -28.802 -80.649  1.00 31.29  ? 135 LEU C CB  1 
ATOM   9212  C CG  . LEU C  1 135 ? -5.035  -28.264 -81.795  1.00 31.72  ? 135 LEU C CG  1 
ATOM   9213  C CD1 . LEU C  1 135 ? -6.009  -29.337 -82.228  1.00 28.23  ? 135 LEU C CD1 1 
ATOM   9214  C CD2 . LEU C  1 135 ? -5.771  -26.973 -81.390  1.00 35.47  ? 135 LEU C CD2 1 
ATOM   9215  N N   . LEU C  1 136 ? -1.906  -29.568 -78.771  1.00 28.40  ? 136 LEU C N   1 
ATOM   9216  C CA  . LEU C  1 136 ? -1.496  -30.247 -77.543  1.00 29.77  ? 136 LEU C CA  1 
ATOM   9217  C C   . LEU C  1 136 ? -0.594  -29.382 -76.667  1.00 25.76  ? 136 LEU C C   1 
ATOM   9218  O O   . LEU C  1 136 ? -0.606  -29.536 -75.439  1.00 23.63  ? 136 LEU C O   1 
ATOM   9219  C CB  . LEU C  1 136 ? -0.798  -31.576 -77.880  1.00 23.87  ? 136 LEU C CB  1 
ATOM   9220  C CG  . LEU C  1 136 ? -1.743  -32.687 -78.344  1.00 30.30  ? 136 LEU C CG  1 
ATOM   9221  C CD1 . LEU C  1 136 ? -1.009  -34.007 -78.651  1.00 27.27  ? 136 LEU C CD1 1 
ATOM   9222  C CD2 . LEU C  1 136 ? -2.858  -32.916 -77.330  1.00 29.41  ? 136 LEU C CD2 1 
ATOM   9223  N N   . ALA C  1 137 ? 0.215   -28.498 -77.259  1.00 29.74  ? 137 ALA C N   1 
ATOM   9224  C CA  . ALA C  1 137 ? 1.068   -27.623 -76.446  1.00 33.49  ? 137 ALA C CA  1 
ATOM   9225  C C   . ALA C  1 137 ? 0.262   -26.767 -75.479  1.00 30.44  ? 137 ALA C C   1 
ATOM   9226  O O   . ALA C  1 137 ? 0.742   -26.441 -74.390  1.00 24.63  ? 137 ALA C O   1 
ATOM   9227  C CB  . ALA C  1 137 ? 1.903   -26.703 -77.338  1.00 32.78  ? 137 ALA C CB  1 
ATOM   9228  N N   . TRP C  1 138 ? -0.935  -26.348 -75.875  1.00 31.98  ? 138 TRP C N   1 
ATOM   9229  C CA  . TRP C  1 138 ? -1.761  -25.489 -75.045  1.00 31.62  ? 138 TRP C CA  1 
ATOM   9230  C C   . TRP C  1 138 ? -2.721  -26.283 -74.181  1.00 32.84  ? 138 TRP C C   1 
ATOM   9231  O O   . TRP C  1 138 ? -3.715  -25.730 -73.700  1.00 30.52  ? 138 TRP C O   1 
ATOM   9232  C CB  . TRP C  1 138 ? -2.522  -24.494 -75.918  1.00 32.65  ? 138 TRP C CB  1 
ATOM   9233  C CG  . TRP C  1 138 ? -1.606  -23.545 -76.622  1.00 34.73  ? 138 TRP C CG  1 
ATOM   9234  C CD1 . TRP C  1 138 ? -0.947  -23.765 -77.797  1.00 35.46  ? 138 TRP C CD1 1 
ATOM   9235  C CD2 . TRP C  1 138 ? -1.227  -22.231 -76.190  1.00 35.96  ? 138 TRP C CD2 1 
ATOM   9236  N NE1 . TRP C  1 138 ? -0.182  -22.669 -78.123  1.00 33.34  ? 138 TRP C NE1 1 
ATOM   9237  C CE2 . TRP C  1 138 ? -0.345  -21.710 -77.162  1.00 38.01  ? 138 TRP C CE2 1 
ATOM   9238  C CE3 . TRP C  1 138 ? -1.559  -21.437 -75.087  1.00 33.55  ? 138 TRP C CE3 1 
ATOM   9239  C CZ2 . TRP C  1 138 ? 0.216   -20.436 -77.059  1.00 41.65  ? 138 TRP C CZ2 1 
ATOM   9240  C CZ3 . TRP C  1 138 ? -1.004  -20.176 -74.986  1.00 37.71  ? 138 TRP C CZ3 1 
ATOM   9241  C CH2 . TRP C  1 138 ? -0.122  -19.685 -75.967  1.00 38.22  ? 138 TRP C CH2 1 
ATOM   9242  N N   . CYS C  1 139 ? -2.458  -27.571 -73.994  1.00 30.28  ? 139 CYS C N   1 
ATOM   9243  C CA  . CYS C  1 139 ? -3.316  -28.382 -73.143  1.00 30.45  ? 139 CYS C CA  1 
ATOM   9244  C C   . CYS C  1 139 ? -3.283  -27.851 -71.717  1.00 29.38  ? 139 CYS C C   1 
ATOM   9245  O O   . CYS C  1 139 ? -2.217  -27.515 -71.183  1.00 26.68  ? 139 CYS C O   1 
ATOM   9246  C CB  . CYS C  1 139 ? -2.872  -29.846 -73.180  1.00 26.96  ? 139 CYS C CB  1 
ATOM   9247  S SG  . CYS C  1 139 ? -3.953  -30.950 -72.239  1.00 35.41  ? 139 CYS C SG  1 
ATOM   9248  N N   . GLY C  1 140 ? -4.468  -27.765 -71.102  1.00 28.42  ? 140 GLY C N   1 
ATOM   9249  C CA  . GLY C  1 140 ? -4.568  -27.288 -69.737  1.00 24.03  ? 140 GLY C CA  1 
ATOM   9250  C C   . GLY C  1 140 ? -4.397  -28.388 -68.720  1.00 27.89  ? 140 GLY C C   1 
ATOM   9251  O O   . GLY C  1 140 ? -4.394  -29.576 -69.053  1.00 35.77  ? 140 GLY C O   1 
ATOM   9252  N N   . ARG C  1 141 ? -4.275  -27.964 -67.452  1.00 27.94  ? 141 ARG C N   1 
ATOM   9253  C CA  . ARG C  1 141 ? -3.998  -28.896 -66.364  1.00 25.88  ? 141 ARG C CA  1 
ATOM   9254  C C   . ARG C  1 141 ? -5.037  -30.006 -66.299  1.00 29.94  ? 141 ARG C C   1 
ATOM   9255  O O   . ARG C  1 141 ? -4.687  -31.190 -66.175  1.00 24.94  ? 141 ARG C O   1 
ATOM   9256  C CB  . ARG C  1 141 ? -3.936  -28.145 -65.037  1.00 28.91  ? 141 ARG C CB  1 
ATOM   9257  C CG  . ARG C  1 141 ? -3.494  -29.026 -63.892  1.00 35.02  ? 141 ARG C CG  1 
ATOM   9258  C CD  . ARG C  1 141 ? -3.387  -28.256 -62.604  1.00 44.01  ? 141 ARG C CD  1 
ATOM   9259  N NE  . ARG C  1 141 ? -4.707  -28.041 -62.048  1.00 50.31  ? 141 ARG C NE  1 
ATOM   9260  C CZ  . ARG C  1 141 ? -5.188  -28.702 -61.006  1.00 46.37  ? 141 ARG C CZ  1 
ATOM   9261  N NH1 . ARG C  1 141 ? -4.456  -29.620 -60.401  1.00 47.63  ? 141 ARG C NH1 1 
ATOM   9262  N NH2 . ARG C  1 141 ? -6.411  -28.443 -60.580  1.00 49.32  ? 141 ARG C NH2 1 
ATOM   9263  N N   . THR C  1 142 ? -6.319  -29.646 -66.408  1.00 31.06  ? 142 THR C N   1 
ATOM   9264  C CA  . THR C  1 142 ? -7.378  -30.645 -66.320  1.00 37.70  ? 142 THR C CA  1 
ATOM   9265  C C   . THR C  1 142 ? -7.214  -31.718 -67.393  1.00 45.49  ? 142 THR C C   1 
ATOM   9266  O O   . THR C  1 142 ? -7.282  -32.915 -67.102  1.00 59.06  ? 142 THR C O   1 
ATOM   9267  C CB  . THR C  1 142 ? -8.751  -29.976 -66.437  1.00 40.57  ? 142 THR C CB  1 
ATOM   9268  O OG1 . THR C  1 142 ? -8.895  -28.970 -65.426  1.00 45.27  ? 142 THR C OG1 1 
ATOM   9269  C CG2 . THR C  1 142 ? -9.851  -31.004 -66.258  1.00 42.86  ? 142 THR C CG2 1 
ATOM   9270  N N   . LEU C  1 143 ? -6.977  -31.311 -68.644  1.00 40.81  ? 143 LEU C N   1 
ATOM   9271  C CA  . LEU C  1 143 ? -7.050  -32.267 -69.739  1.00 36.66  ? 143 LEU C CA  1 
ATOM   9272  C C   . LEU C  1 143 ? -5.822  -33.160 -69.873  1.00 35.51  ? 143 LEU C C   1 
ATOM   9273  O O   . LEU C  1 143 ? -5.865  -34.102 -70.673  1.00 34.44  ? 143 LEU C O   1 
ATOM   9274  C CB  . LEU C  1 143 ? -7.296  -31.531 -71.056  1.00 36.60  ? 143 LEU C CB  1 
ATOM   9275  C CG  . LEU C  1 143 ? -8.773  -31.286 -71.352  1.00 34.54  ? 143 LEU C CG  1 
ATOM   9276  C CD1 . LEU C  1 143 ? -8.982  -30.958 -72.816  1.00 25.83  ? 143 LEU C CD1 1 
ATOM   9277  C CD2 . LEU C  1 143 ? -9.602  -32.486 -70.972  1.00 35.43  ? 143 LEU C CD2 1 
ATOM   9278  N N   . ARG C  1 144 ? -4.741  -32.914 -69.116  1.00 40.03  ? 144 ARG C N   1 
ATOM   9279  C CA  . ARG C  1 144 ? -3.551  -33.752 -69.259  1.00 44.14  ? 144 ARG C CA  1 
ATOM   9280  C C   . ARG C  1 144 ? -3.849  -35.214 -68.957  1.00 43.91  ? 144 ARG C C   1 
ATOM   9281  O O   . ARG C  1 144 ? -3.185  -36.106 -69.494  1.00 47.07  ? 144 ARG C O   1 
ATOM   9282  C CB  . ARG C  1 144 ? -2.418  -33.281 -68.349  1.00 47.66  ? 144 ARG C CB  1 
ATOM   9283  C CG  . ARG C  1 144 ? -2.368  -31.820 -68.041  1.00 51.61  ? 144 ARG C CG  1 
ATOM   9284  C CD  . ARG C  1 144 ? -1.515  -31.602 -66.792  1.00 54.56  ? 144 ARG C CD  1 
ATOM   9285  N NE  . ARG C  1 144 ? -2.181  -31.992 -65.541  1.00 52.28  ? 144 ARG C NE  1 
ATOM   9286  C CZ  . ARG C  1 144 ? -1.555  -32.104 -64.371  1.00 52.66  ? 144 ARG C CZ  1 
ATOM   9287  N NH1 . ARG C  1 144 ? -0.252  -31.863 -64.305  1.00 55.37  ? 144 ARG C NH1 1 
ATOM   9288  N NH2 . ARG C  1 144 ? -2.215  -32.460 -63.268  1.00 46.43  ? 144 ARG C NH2 1 
ATOM   9289  N N   . LYS C  1 145 ? -4.826  -35.479 -68.089  1.00 40.74  ? 145 LYS C N   1 
ATOM   9290  C CA  . LYS C  1 145 ? -5.177  -36.856 -67.764  1.00 43.81  ? 145 LYS C CA  1 
ATOM   9291  C C   . LYS C  1 145 ? -5.789  -37.564 -68.971  1.00 43.12  ? 145 LYS C C   1 
ATOM   9292  O O   . LYS C  1 145 ? -5.306  -38.614 -69.412  1.00 41.08  ? 145 LYS C O   1 
ATOM   9293  C CB  . LYS C  1 145 ? -6.142  -36.865 -66.577  1.00 54.51  ? 145 LYS C CB  1 
ATOM   9294  C CG  . LYS C  1 145 ? -5.882  -35.755 -65.532  1.00 65.36  ? 145 LYS C CG  1 
ATOM   9295  C CD  . LYS C  1 145 ? -4.414  -35.678 -65.070  1.00 71.22  ? 145 LYS C CD  1 
ATOM   9296  C CE  . LYS C  1 145 ? -4.295  -35.181 -63.629  1.00 73.99  ? 145 LYS C CE  1 
ATOM   9297  N NZ  . LYS C  1 145 ? -4.935  -33.843 -63.450  1.00 75.77  ? 145 LYS C NZ  1 
ATOM   9298  N N   . ASP C  1 146 ? -6.859  -36.996 -69.526  1.00 37.72  ? 146 ASP C N   1 
ATOM   9299  C CA  . ASP C  1 146 ? -7.579  -37.657 -70.605  1.00 44.72  ? 146 ASP C CA  1 
ATOM   9300  C C   . ASP C  1 146 ? -6.816  -37.635 -71.921  1.00 40.35  ? 146 ASP C C   1 
ATOM   9301  O O   . ASP C  1 146 ? -7.108  -38.457 -72.793  1.00 43.11  ? 146 ASP C O   1 
ATOM   9302  C CB  . ASP C  1 146 ? -8.951  -37.006 -70.804  1.00 58.51  ? 146 ASP C CB  1 
ATOM   9303  C CG  . ASP C  1 146 ? -9.695  -36.794 -69.495  1.00 72.09  ? 146 ASP C CG  1 
ATOM   9304  O OD1 . ASP C  1 146 ? -10.118 -37.796 -68.881  1.00 76.66  ? 146 ASP C OD1 1 
ATOM   9305  O OD2 . ASP C  1 146 ? -9.850  -35.625 -69.076  1.00 74.70  ? 146 ASP C OD2 1 
ATOM   9306  N N   . LEU C  1 147 ? -5.871  -36.708 -72.097  1.00 36.04  ? 147 LEU C N   1 
ATOM   9307  C CA  . LEU C  1 147 ? -5.122  -36.562 -73.338  1.00 32.84  ? 147 LEU C CA  1 
ATOM   9308  C C   . LEU C  1 147 ? -3.724  -37.163 -73.255  1.00 37.88  ? 147 LEU C C   1 
ATOM   9309  O O   . LEU C  1 147 ? -2.928  -36.971 -74.181  1.00 37.64  ? 147 LEU C O   1 
ATOM   9310  C CB  . LEU C  1 147 ? -5.016  -35.084 -73.724  1.00 30.65  ? 147 LEU C CB  1 
ATOM   9311  C CG  . LEU C  1 147 ? -6.300  -34.368 -74.138  1.00 31.77  ? 147 LEU C CG  1 
ATOM   9312  C CD1 . LEU C  1 147 ? -5.976  -32.946 -74.534  1.00 31.58  ? 147 LEU C CD1 1 
ATOM   9313  C CD2 . LEU C  1 147 ? -6.989  -35.120 -75.283  1.00 34.66  ? 147 LEU C CD2 1 
ATOM   9314  N N   . LYS C  1 148 ? -3.393  -37.878 -72.185  1.00 39.48  ? 148 LYS C N   1 
ATOM   9315  C CA  . LYS C  1 148 ? -2.029  -38.463 -71.979  1.00 40.05  ? 148 LYS C CA  1 
ATOM   9316  C C   . LYS C  1 148 ? -1.580  -39.412 -73.033  1.00 38.78  ? 148 LYS C C   1 
ATOM   9317  O O   . LYS C  1 148 ? -0.454  -39.452 -73.393  1.00 39.10  ? 148 LYS C O   1 
ATOM   9318  C CB  . LYS C  1 148 ? -1.869  -39.166 -70.599  1.00 36.19  ? 148 LYS C CB  1 
ATOM   9319  C CG  . LYS C  1 148 ? -0.514  -39.765 -70.341  1.00 39.34  ? 148 LYS C CG  1 
ATOM   9320  C CD  . LYS C  1 148 ? -0.289  -39.985 -68.864  1.00 44.73  ? 148 LYS C CD  1 
ATOM   9321  C CE  . LYS C  1 148 ? -1.615  -40.034 -68.134  1.00 52.69  ? 148 LYS C CE  1 
ATOM   9322  N NZ  . LYS C  1 148 ? -1.535  -39.801 -66.667  1.00 55.21  ? 148 LYS C NZ  1 
ATOM   9323  N N   . ASP C  1 149 ? -2.485  -40.173 -73.488  1.00 36.85  ? 149 ASP C N   1 
ATOM   9324  C CA  . ASP C  1 149 ? -2.166  -41.036 -74.587  1.00 47.93  ? 149 ASP C CA  1 
ATOM   9325  C C   . ASP C  1 149 ? -1.688  -40.299 -75.824  1.00 39.34  ? 149 ASP C C   1 
ATOM   9326  O O   . ASP C  1 149 ? -0.711  -40.639 -76.405  1.00 38.58  ? 149 ASP C O   1 
ATOM   9327  C CB  . ASP C  1 149 ? -3.397  -41.827 -74.864  1.00 62.84  ? 149 ASP C CB  1 
ATOM   9328  C CG  . ASP C  1 149 ? -3.254  -42.779 -76.040  1.00 76.39  ? 149 ASP C CG  1 
ATOM   9329  O OD1 . ASP C  1 149 ? -2.139  -43.264 -76.310  1.00 79.09  ? 149 ASP C OD1 1 
ATOM   9330  O OD2 . ASP C  1 149 ? -4.279  -43.054 -76.696  1.00 80.67  ? 149 ASP C OD2 1 
ATOM   9331  N N   . LEU C  1 150 ? -2.362  -39.253 -76.155  1.00 37.72  ? 150 LEU C N   1 
ATOM   9332  C CA  . LEU C  1 150 ? -1.938  -38.433 -77.255  1.00 36.11  ? 150 LEU C CA  1 
ATOM   9333  C C   . LEU C  1 150 ? -0.677  -37.650 -76.910  1.00 39.64  ? 150 LEU C C   1 
ATOM   9334  O O   . LEU C  1 150 ? 0.161   -37.458 -77.742  1.00 38.20  ? 150 LEU C O   1 
ATOM   9335  C CB  . LEU C  1 150 ? -3.099  -37.550 -77.709  1.00 33.85  ? 150 LEU C CB  1 
ATOM   9336  C CG  . LEU C  1 150 ? -4.327  -38.275 -78.203  1.00 37.75  ? 150 LEU C CG  1 
ATOM   9337  C CD1 . LEU C  1 150 ? -5.428  -37.300 -78.529  1.00 38.50  ? 150 LEU C CD1 1 
ATOM   9338  C CD2 . LEU C  1 150 ? -3.988  -39.175 -79.375  1.00 38.39  ? 150 LEU C CD2 1 
ATOM   9339  N N   . LEU C  1 151 ? -0.544  -37.189 -75.681  1.00 38.55  ? 151 LEU C N   1 
ATOM   9340  C CA  . LEU C  1 151 ? 0.620   -36.399 -75.294  1.00 41.54  ? 151 LEU C CA  1 
ATOM   9341  C C   . LEU C  1 151 ? 1.898   -37.228 -75.355  1.00 46.15  ? 151 LEU C C   1 
ATOM   9342  O O   . LEU C  1 151 ? 2.943   -36.732 -75.791  1.00 46.74  ? 151 LEU C O   1 
ATOM   9343  C CB  . LEU C  1 151 ? 0.412   -35.812 -73.895  1.00 41.39  ? 151 LEU C CB  1 
ATOM   9344  C CG  . LEU C  1 151 ? -0.572  -34.634 -73.848  1.00 35.97  ? 151 LEU C CG  1 
ATOM   9345  C CD1 . LEU C  1 151 ? -0.996  -34.280 -72.420  1.00 36.42  ? 151 LEU C CD1 1 
ATOM   9346  C CD2 . LEU C  1 151 ? 0.001   -33.404 -74.565  1.00 34.69  ? 151 LEU C CD2 1 
ATOM   9347  N N   . ASN C  1 152 ? 1.828   -38.499 -74.941  1.00 47.89  ? 152 ASN C N   1 
ATOM   9348  C CA  . ASN C  1 152 ? 2.984   -39.391 -74.977  1.00 50.67  ? 152 ASN C CA  1 
ATOM   9349  C C   . ASN C  1 152 ? 3.280   -39.929 -76.372  1.00 52.38  ? 152 ASN C C   1 
ATOM   9350  O O   . ASN C  1 152 ? 4.410   -40.361 -76.630  1.00 53.97  ? 152 ASN C O   1 
ATOM   9351  C CB  . ASN C  1 152 ? 2.772   -40.573 -74.033  1.00 53.63  ? 152 ASN C CB  1 
ATOM   9352  C CG  . ASN C  1 152 ? 2.658   -40.152 -72.572  1.00 52.67  ? 152 ASN C CG  1 
ATOM   9353  O OD1 . ASN C  1 152 ? 3.201   -39.129 -72.159  1.00 49.69  ? 152 ASN C OD1 1 
ATOM   9354  N ND2 . ASN C  1 152 ? 1.957   -40.955 -71.786  1.00 54.30  ? 152 ASN C ND2 1 
ATOM   9355  N N   . LYS C  1 153 ? 2.285   -39.940 -77.260  1.00 47.99  ? 153 LYS C N   1 
ATOM   9356  C CA  . LYS C  1 153 ? 2.513   -40.353 -78.641  1.00 47.81  ? 153 LYS C CA  1 
ATOM   9357  C C   . LYS C  1 153 ? 3.566   -39.475 -79.297  1.00 44.89  ? 153 LYS C C   1 
ATOM   9358  O O   . LYS C  1 153 ? 4.578   -39.970 -79.812  1.00 49.17  ? 153 LYS C O   1 
ATOM   9359  C CB  . LYS C  1 153 ? 1.196   -40.298 -79.415  1.00 43.19  ? 153 LYS C CB  1 
ATOM   9360  C CG  . LYS C  1 153 ? 1.269   -40.865 -80.803  1.00 46.70  ? 153 LYS C CG  1 
ATOM   9361  C CD  . LYS C  1 153 ? -0.119  -41.090 -81.376  1.00 47.34  ? 153 LYS C CD  1 
ATOM   9362  C CE  . LYS C  1 153 ? -0.040  -41.549 -82.817  1.00 51.01  ? 153 LYS C CE  1 
ATOM   9363  N NZ  . LYS C  1 153 ? -1.347  -42.009 -83.379  1.00 51.06  ? 153 LYS C NZ  1 
ATOM   9364  N N   . GLY C  1 154 ? 3.343   -38.163 -79.270  1.00 41.66  ? 154 GLY C N   1 
ATOM   9365  C CA  . GLY C  1 154 ? 4.303   -37.173 -79.697  1.00 40.95  ? 154 GLY C CA  1 
ATOM   9366  C C   . GLY C  1 154 ? 4.435   -36.982 -81.188  1.00 45.86  ? 154 GLY C C   1 
ATOM   9367  O O   . GLY C  1 154 ? 5.076   -36.015 -81.607  1.00 46.82  ? 154 GLY C O   1 
ATOM   9368  N N   . ARG C  1 155 ? 3.854   -37.856 -82.004  1.00 48.30  ? 155 ARG C N   1 
ATOM   9369  C CA  . ARG C  1 155 ? 4.070   -37.785 -83.443  1.00 50.58  ? 155 ARG C CA  1 
ATOM   9370  C C   . ARG C  1 155 ? 3.063   -38.686 -84.143  1.00 49.03  ? 155 ARG C C   1 
ATOM   9371  O O   . ARG C  1 155 ? 2.415   -39.535 -83.524  1.00 47.64  ? 155 ARG C O   1 
ATOM   9372  C CB  . ARG C  1 155 ? 5.496   -38.191 -83.826  1.00 50.13  ? 155 ARG C CB  1 
ATOM   9373  C CG  . ARG C  1 155 ? 5.867   -39.616 -83.467  1.00 50.95  ? 155 ARG C CG  1 
ATOM   9374  C CD  . ARG C  1 155 ? 7.294   -39.936 -83.893  1.00 54.19  ? 155 ARG C CD  1 
ATOM   9375  N NE  . ARG C  1 155 ? 8.269   -39.062 -83.243  1.00 56.12  ? 155 ARG C NE  1 
ATOM   9376  C CZ  . ARG C  1 155 ? 9.190   -38.351 -83.888  1.00 60.61  ? 155 ARG C CZ  1 
ATOM   9377  N NH1 . ARG C  1 155 ? 10.032  -37.583 -83.203  1.00 59.17  ? 155 ARG C NH1 1 
ATOM   9378  N NH2 . ARG C  1 155 ? 9.282   -38.416 -85.217  1.00 63.25  ? 155 ARG C NH2 1 
ATOM   9379  N N   . ASN C  1 156 ? 2.957   -38.484 -85.455  1.00 47.23  ? 156 ASN C N   1 
ATOM   9380  C CA  . ASN C  1 156 ? 2.145   -39.302 -86.347  1.00 51.24  ? 156 ASN C CA  1 
ATOM   9381  C C   . ASN C  1 156 ? 0.694   -39.393 -85.872  1.00 36.43  ? 156 ASN C C   1 
ATOM   9382  O O   . ASN C  1 156 ? 0.133   -40.468 -85.675  1.00 43.83  ? 156 ASN C O   1 
ATOM   9383  C CB  . ASN C  1 156 ? 2.789   -40.685 -86.553  1.00 56.63  ? 156 ASN C CB  1 
ATOM   9384  C CG  . ASN C  1 156 ? 4.187   -40.593 -87.164  1.00 65.08  ? 156 ASN C CG  1 
ATOM   9385  O OD1 . ASN C  1 156 ? 4.538   -39.585 -87.787  1.00 68.66  ? 156 ASN C OD1 1 
ATOM   9386  N ND2 . ASN C  1 156 ? 4.976   -41.651 -87.012  1.00 69.34  ? 156 ASN C ND2 1 
ATOM   9387  N N   . TYR C  1 157 ? 0.084   -38.226 -85.764  1.00 34.90  ? 157 TYR C N   1 
ATOM   9388  C CA  . TYR C  1 157 ? -1.311  -38.053 -85.409  1.00 42.39  ? 157 TYR C CA  1 
ATOM   9389  C C   . TYR C  1 157 ? -2.207  -38.129 -86.643  1.00 45.61  ? 157 TYR C C   1 
ATOM   9390  O O   . TYR C  1 157 ? -1.791  -37.832 -87.769  1.00 45.76  ? 157 TYR C O   1 
ATOM   9391  C CB  . TYR C  1 157 ? -1.517  -36.707 -84.717  1.00 39.22  ? 157 TYR C CB  1 
ATOM   9392  C CG  . TYR C  1 157 ? -0.763  -36.584 -83.415  1.00 40.06  ? 157 TYR C CG  1 
ATOM   9393  C CD1 . TYR C  1 157 ? -1.260  -37.155 -82.254  1.00 35.33  ? 157 TYR C CD1 1 
ATOM   9394  C CD2 . TYR C  1 157 ? 0.449   -35.903 -83.350  1.00 40.49  ? 157 TYR C CD2 1 
ATOM   9395  C CE1 . TYR C  1 157 ? -0.579  -37.050 -81.063  1.00 34.56  ? 157 TYR C CE1 1 
ATOM   9396  C CE2 . TYR C  1 157 ? 1.136   -35.792 -82.166  1.00 37.70  ? 157 TYR C CE2 1 
ATOM   9397  C CZ  . TYR C  1 157 ? 0.614   -36.369 -81.023  1.00 35.45  ? 157 TYR C CZ  1 
ATOM   9398  O OH  . TYR C  1 157 ? 1.296   -36.273 -79.835  1.00 29.36  ? 157 TYR C OH  1 
ATOM   9399  N N   . THR C  1 158 ? -3.457  -38.526 -86.413  1.00 44.08  ? 158 THR C N   1 
ATOM   9400  C CA  . THR C  1 158 ? -4.464  -38.607 -87.458  1.00 46.02  ? 158 THR C CA  1 
ATOM   9401  C C   . THR C  1 158 ? -5.422  -37.426 -87.370  1.00 42.59  ? 158 THR C C   1 
ATOM   9402  O O   . THR C  1 158 ? -5.518  -36.744 -86.345  1.00 41.98  ? 158 THR C O   1 
ATOM   9403  C CB  . THR C  1 158 ? -5.271  -39.904 -87.359  1.00 45.86  ? 158 THR C CB  1 
ATOM   9404  O OG1 . THR C  1 158 ? -6.024  -39.879 -86.139  1.00 42.31  ? 158 THR C OG1 1 
ATOM   9405  C CG2 . THR C  1 158 ? -4.357  -41.127 -87.384  1.00 45.52  ? 158 THR C CG2 1 
ATOM   9406  N N   . GLN C  1 159 ? -6.146  -37.207 -88.472  1.00 37.44  ? 159 GLN C N   1 
ATOM   9407  C CA  . GLN C  1 159 ? -7.233  -36.237 -88.475  1.00 39.20  ? 159 GLN C CA  1 
ATOM   9408  C C   . GLN C  1 159 ? -8.238  -36.521 -87.363  1.00 41.05  ? 159 GLN C C   1 
ATOM   9409  O O   . GLN C  1 159 ? -8.689  -35.597 -86.678  1.00 40.11  ? 159 GLN C O   1 
ATOM   9410  C CB  . GLN C  1 159 ? -7.925  -36.236 -89.839  1.00 42.33  ? 159 GLN C CB  1 
ATOM   9411  C CG  . GLN C  1 159 ? -9.084  -35.262 -89.923  1.00 48.49  ? 159 GLN C CG  1 
ATOM   9412  C CD  . GLN C  1 159 ? -8.638  -33.807 -89.851  1.00 45.94  ? 159 GLN C CD  1 
ATOM   9413  O OE1 . GLN C  1 159 ? -7.505  -33.469 -90.196  1.00 49.31  ? 159 GLN C OE1 1 
ATOM   9414  N NE2 . GLN C  1 159 ? -9.539  -32.937 -89.413  1.00 40.31  ? 159 GLN C NE2 1 
ATOM   9415  N N   . GLU C  1 160 ? -8.585  -37.794 -87.152  1.00 46.44  ? 160 GLU C N   1 
ATOM   9416  C CA  . GLU C  1 160 ? -9.545  -38.125 -86.102  1.00 48.43  ? 160 GLU C CA  1 
ATOM   9417  C C   . GLU C  1 160 ? -9.042  -37.689 -84.731  1.00 44.69  ? 160 GLU C C   1 
ATOM   9418  O O   . GLU C  1 160 ? -9.796  -37.112 -83.937  1.00 45.19  ? 160 GLU C O   1 
ATOM   9419  C CB  . GLU C  1 160 ? -9.838  -39.626 -86.108  1.00 53.73  ? 160 GLU C CB  1 
ATOM   9420  C CG  . GLU C  1 160 ? -10.518 -40.122 -87.371  1.00 63.92  ? 160 GLU C CG  1 
ATOM   9421  C CD  . GLU C  1 160 ? -9.539  -40.484 -88.485  1.00 69.43  ? 160 GLU C CD  1 
ATOM   9422  O OE1 . GLU C  1 160 ? -9.263  -39.637 -89.361  1.00 70.10  ? 160 GLU C OE1 1 
ATOM   9423  O OE2 . GLU C  1 160 ? -9.047  -41.633 -88.483  1.00 74.21  ? 160 GLU C OE2 1 
ATOM   9424  N N   . GLU C  1 161 ? -7.768  -37.953 -84.436  1.00 41.69  ? 161 GLU C N   1 
ATOM   9425  C CA  . GLU C  1 161 ? -7.236  -37.614 -83.120  1.00 36.93  ? 161 GLU C CA  1 
ATOM   9426  C C   . GLU C  1 161 ? -7.171  -36.109 -82.931  1.00 41.79  ? 161 GLU C C   1 
ATOM   9427  O O   . GLU C  1 161 ? -7.439  -35.601 -81.833  1.00 40.02  ? 161 GLU C O   1 
ATOM   9428  C CB  . GLU C  1 161 ? -5.861  -38.239 -82.932  1.00 38.03  ? 161 GLU C CB  1 
ATOM   9429  C CG  . GLU C  1 161 ? -5.899  -39.758 -82.874  1.00 39.72  ? 161 GLU C CG  1 
ATOM   9430  C CD  . GLU C  1 161 ? -4.526  -40.365 -82.943  1.00 44.48  ? 161 GLU C CD  1 
ATOM   9431  O OE1 . GLU C  1 161 ? -3.629  -39.759 -83.574  1.00 46.05  ? 161 GLU C OE1 1 
ATOM   9432  O OE2 . GLU C  1 161 ? -4.347  -41.449 -82.353  1.00 54.78  ? 161 GLU C OE2 1 
ATOM   9433  N N   . LYS C  1 162 ? -6.822  -35.377 -83.991  1.00 44.35  ? 162 LYS C N   1 
ATOM   9434  C CA  . LYS C  1 162 ? -6.855  -33.920 -83.919  1.00 39.32  ? 162 LYS C CA  1 
ATOM   9435  C C   . LYS C  1 162 ? -8.254  -33.432 -83.570  1.00 38.03  ? 162 LYS C C   1 
ATOM   9436  O O   . LYS C  1 162 ? -8.420  -32.530 -82.737  1.00 38.42  ? 162 LYS C O   1 
ATOM   9437  C CB  . LYS C  1 162 ? -6.391  -33.321 -85.249  1.00 34.60  ? 162 LYS C CB  1 
ATOM   9438  C CG  . LYS C  1 162 ? -6.192  -31.833 -85.226  1.00 29.79  ? 162 LYS C CG  1 
ATOM   9439  C CD  . LYS C  1 162 ? -5.623  -31.351 -86.561  1.00 30.95  ? 162 LYS C CD  1 
ATOM   9440  C CE  . LYS C  1 162 ? -6.566  -31.666 -87.712  1.00 32.53  ? 162 LYS C CE  1 
ATOM   9441  N NZ  . LYS C  1 162 ? -6.162  -30.961 -88.984  1.00 33.97  ? 162 LYS C NZ  1 
ATOM   9442  N N   . GLU C  1 163 ? -9.273  -34.025 -84.199  1.00 41.07  ? 163 GLU C N   1 
ATOM   9443  C CA  . GLU C  1 163 ? -10.654 -33.651 -83.921  1.00 44.71  ? 163 GLU C CA  1 
ATOM   9444  C C   . GLU C  1 163 ? -11.070 -34.031 -82.505  1.00 43.97  ? 163 GLU C C   1 
ATOM   9445  O O   . GLU C  1 163 ? -11.908 -33.349 -81.908  1.00 46.31  ? 163 GLU C O   1 
ATOM   9446  C CB  . GLU C  1 163 ? -11.587 -34.292 -84.952  1.00 44.96  ? 163 GLU C CB  1 
ATOM   9447  C CG  . GLU C  1 163 ? -11.630 -33.537 -86.267  1.00 46.75  ? 163 GLU C CG  1 
ATOM   9448  C CD  . GLU C  1 163 ? -12.134 -34.384 -87.427  1.00 52.27  ? 163 GLU C CD  1 
ATOM   9449  O OE1 . GLU C  1 163 ? -11.978 -33.946 -88.586  1.00 48.98  ? 163 GLU C OE1 1 
ATOM   9450  O OE2 . GLU C  1 163 ? -12.684 -35.479 -87.185  1.00 52.98  ? 163 GLU C OE2 1 
ATOM   9451  N N   . TYR C  1 164 ? -10.509 -35.104 -81.950  1.00 44.62  ? 164 TYR C N   1 
ATOM   9452  C CA  . TYR C  1 164 ? -10.836 -35.451 -80.572  1.00 43.79  ? 164 TYR C CA  1 
ATOM   9453  C C   . TYR C  1 164 ? -10.331 -34.389 -79.608  1.00 43.41  ? 164 TYR C C   1 
ATOM   9454  O O   . TYR C  1 164 ? -11.001 -34.074 -78.617  1.00 41.13  ? 164 TYR C O   1 
ATOM   9455  C CB  . TYR C  1 164 ? -10.258 -36.817 -80.202  1.00 43.42  ? 164 TYR C CB  1 
ATOM   9456  C CG  . TYR C  1 164 ? -10.499 -37.169 -78.749  1.00 46.03  ? 164 TYR C CG  1 
ATOM   9457  C CD1 . TYR C  1 164 ? -11.706 -37.718 -78.339  1.00 51.08  ? 164 TYR C CD1 1 
ATOM   9458  C CD2 . TYR C  1 164 ? -9.530  -36.933 -77.785  1.00 46.29  ? 164 TYR C CD2 1 
ATOM   9459  C CE1 . TYR C  1 164 ? -11.938 -38.027 -77.012  1.00 52.33  ? 164 TYR C CE1 1 
ATOM   9460  C CE2 . TYR C  1 164 ? -9.757  -37.236 -76.452  1.00 49.32  ? 164 TYR C CE2 1 
ATOM   9461  C CZ  . TYR C  1 164 ? -10.961 -37.784 -76.071  1.00 51.99  ? 164 TYR C CZ  1 
ATOM   9462  O OH  . TYR C  1 164 ? -11.184 -38.089 -74.744  1.00 50.88  ? 164 TYR C OH  1 
ATOM   9463  N N   . VAL C  1 165 ? -9.138  -33.849 -79.865  1.00 39.35  ? 165 VAL C N   1 
ATOM   9464  C CA  . VAL C  1 165 ? -8.583  -32.822 -78.993  1.00 34.50  ? 165 VAL C CA  1 
ATOM   9465  C C   . VAL C  1 165 ? -9.395  -31.544 -79.101  1.00 34.18  ? 165 VAL C C   1 
ATOM   9466  O O   . VAL C  1 165 ? -9.646  -30.857 -78.102  1.00 29.21  ? 165 VAL C O   1 
ATOM   9467  C CB  . VAL C  1 165 ? -7.103  -32.576 -79.335  1.00 32.37  ? 165 VAL C CB  1 
ATOM   9468  C CG1 . VAL C  1 165 ? -6.556  -31.388 -78.536  1.00 25.11  ? 165 VAL C CG1 1 
ATOM   9469  C CG2 . VAL C  1 165 ? -6.287  -33.836 -79.084  1.00 28.95  ? 165 VAL C CG2 1 
ATOM   9470  N N   . LEU C  1 166 ? -9.811  -31.199 -80.322  1.00 33.26  ? 166 LEU C N   1 
ATOM   9471  C CA  . LEU C  1 166 ? -10.622 -30.006 -80.503  1.00 34.89  ? 166 LEU C CA  1 
ATOM   9472  C C   . LEU C  1 166 ? -11.939 -30.137 -79.760  1.00 37.54  ? 166 LEU C C   1 
ATOM   9473  O O   . LEU C  1 166 ? -12.405 -29.175 -79.137  1.00 40.53  ? 166 LEU C O   1 
ATOM   9474  C CB  . LEU C  1 166 ? -10.856 -29.748 -81.994  1.00 34.42  ? 166 LEU C CB  1 
ATOM   9475  C CG  . LEU C  1 166 ? -9.655  -29.136 -82.721  1.00 32.68  ? 166 LEU C CG  1 
ATOM   9476  C CD1 . LEU C  1 166 ? -9.828  -29.282 -84.221  1.00 35.76  ? 166 LEU C CD1 1 
ATOM   9477  C CD2 . LEU C  1 166 ? -9.485  -27.684 -82.343  1.00 35.53  ? 166 LEU C CD2 1 
ATOM   9478  N N   . ASN C  1 167 ? -12.544 -31.324 -79.805  1.00 36.88  ? 167 ASN C N   1 
ATOM   9479  C CA  . ASN C  1 167 ? -13.794 -31.554 -79.090  1.00 41.76  ? 167 ASN C CA  1 
ATOM   9480  C C   . ASN C  1 167 ? -13.603 -31.392 -77.589  1.00 40.31  ? 167 ASN C C   1 
ATOM   9481  O O   . ASN C  1 167 ? -14.377 -30.697 -76.924  1.00 40.75  ? 167 ASN C O   1 
ATOM   9482  C CB  . ASN C  1 167 ? -14.333 -32.947 -79.425  1.00 45.57  ? 167 ASN C CB  1 
ATOM   9483  C CG  . ASN C  1 167 ? -14.973 -32.994 -80.797  1.00 54.43  ? 167 ASN C CG  1 
ATOM   9484  O OD1 . ASN C  1 167 ? -15.478 -31.976 -81.283  1.00 54.00  ? 167 ASN C OD1 1 
ATOM   9485  N ND2 . ASN C  1 167 ? -14.959 -34.170 -81.432  1.00 56.50  ? 167 ASN C ND2 1 
ATOM   9486  N N   . LYS C  1 168 ? -12.562 -32.018 -77.040  1.00 39.46  ? 168 LYS C N   1 
ATOM   9487  C CA  . LYS C  1 168 ? -12.299 -31.879 -75.614  1.00 39.05  ? 168 LYS C CA  1 
ATOM   9488  C C   . LYS C  1 168 ? -12.037 -30.427 -75.248  1.00 37.66  ? 168 LYS C C   1 
ATOM   9489  O O   . LYS C  1 168 ? -12.470 -29.959 -74.188  1.00 40.05  ? 168 LYS C O   1 
ATOM   9490  C CB  . LYS C  1 168 ? -11.119 -32.757 -75.206  1.00 33.57  ? 168 LYS C CB  1 
ATOM   9491  C CG  . LYS C  1 168 ? -11.336 -34.240 -75.474  1.00 34.22  ? 168 LYS C CG  1 
ATOM   9492  C CD  . LYS C  1 168 ? -12.523 -34.784 -74.679  1.00 41.36  ? 168 LYS C CD  1 
ATOM   9493  C CE  . LYS C  1 168 ? -12.250 -34.775 -73.178  1.00 47.99  ? 168 LYS C CE  1 
ATOM   9494  N NZ  . LYS C  1 168 ? -13.384 -35.338 -72.382  1.00 54.63  ? 168 LYS C NZ  1 
ATOM   9495  N N   . TYR C  1 169 ? -11.342 -29.694 -76.122  1.00 35.13  ? 169 TYR C N   1 
ATOM   9496  C CA  . TYR C  1 169 ? -11.035 -28.295 -75.834  1.00 29.60  ? 169 TYR C CA  1 
ATOM   9497  C C   . TYR C  1 169 ? -12.301 -27.456 -75.799  1.00 35.28  ? 169 TYR C C   1 
ATOM   9498  O O   . TYR C  1 169 ? -12.479 -26.618 -74.907  1.00 35.10  ? 169 TYR C O   1 
ATOM   9499  C CB  . TYR C  1 169 ? -10.058 -27.739 -76.866  1.00 25.04  ? 169 TYR C CB  1 
ATOM   9500  C CG  . TYR C  1 169 ? -8.609  -28.087 -76.612  1.00 24.33  ? 169 TYR C CG  1 
ATOM   9501  C CD1 . TYR C  1 169 ? -8.246  -28.996 -75.620  1.00 26.89  ? 169 TYR C CD1 1 
ATOM   9502  C CD2 . TYR C  1 169 ? -7.598  -27.499 -77.362  1.00 24.76  ? 169 TYR C CD2 1 
ATOM   9503  C CE1 . TYR C  1 169 ? -6.909  -29.312 -75.399  1.00 26.73  ? 169 TYR C CE1 1 
ATOM   9504  C CE2 . TYR C  1 169 ? -6.268  -27.808 -77.148  1.00 25.37  ? 169 TYR C CE2 1 
ATOM   9505  C CZ  . TYR C  1 169 ? -5.930  -28.709 -76.170  1.00 26.62  ? 169 TYR C CZ  1 
ATOM   9506  O OH  . TYR C  1 169 ? -4.602  -29.010 -75.973  1.00 30.39  ? 169 TYR C OH  1 
ATOM   9507  N N   . PHE C  1 170 ? -13.188 -27.647 -76.777  1.00 36.01  ? 170 PHE C N   1 
ATOM   9508  C CA  . PHE C  1 170 ? -14.429 -26.885 -76.755  1.00 36.73  ? 170 PHE C CA  1 
ATOM   9509  C C   . PHE C  1 170 ? -15.296 -27.286 -75.567  1.00 35.73  ? 170 PHE C C   1 
ATOM   9510  O O   . PHE C  1 170 ? -16.008 -26.441 -75.014  1.00 39.52  ? 170 PHE C O   1 
ATOM   9511  C CB  . PHE C  1 170 ? -15.171 -27.050 -78.084  1.00 38.91  ? 170 PHE C CB  1 
ATOM   9512  C CG  . PHE C  1 170 ? -14.695 -26.094 -79.151  1.00 43.76  ? 170 PHE C CG  1 
ATOM   9513  C CD1 . PHE C  1 170 ? -15.185 -24.795 -79.205  1.00 44.53  ? 170 PHE C CD1 1 
ATOM   9514  C CD2 . PHE C  1 170 ? -13.722 -26.477 -80.069  1.00 45.16  ? 170 PHE C CD2 1 
ATOM   9515  C CE1 . PHE C  1 170 ? -14.743 -23.903 -80.169  1.00 44.45  ? 170 PHE C CE1 1 
ATOM   9516  C CE2 . PHE C  1 170 ? -13.267 -25.584 -81.033  1.00 47.03  ? 170 PHE C CE2 1 
ATOM   9517  C CZ  . PHE C  1 170 ? -13.785 -24.294 -81.082  1.00 46.87  ? 170 PHE C CZ  1 
ATOM   9518  N N   . GLU C  1 171 ? -15.245 -28.555 -75.156  1.00 32.69  ? 171 GLU C N   1 
ATOM   9519  C CA  . GLU C  1 171 ? -15.890 -28.947 -73.903  1.00 42.22  ? 171 GLU C CA  1 
ATOM   9520  C C   . GLU C  1 171 ? -15.400 -28.085 -72.747  1.00 43.55  ? 171 GLU C C   1 
ATOM   9521  O O   . GLU C  1 171 ? -16.196 -27.605 -71.928  1.00 50.05  ? 171 GLU C O   1 
ATOM   9522  C CB  . GLU C  1 171 ? -15.624 -30.424 -73.598  1.00 49.51  ? 171 GLU C CB  1 
ATOM   9523  C CG  . GLU C  1 171 ? -16.247 -31.418 -74.561  1.00 59.48  ? 171 GLU C CG  1 
ATOM   9524  C CD  . GLU C  1 171 ? -15.977 -32.863 -74.156  1.00 66.18  ? 171 GLU C CD  1 
ATOM   9525  O OE1 . GLU C  1 171 ? -16.680 -33.770 -74.654  1.00 69.09  ? 171 GLU C OE1 1 
ATOM   9526  O OE2 . GLU C  1 171 ? -15.067 -33.088 -73.326  1.00 67.96  ? 171 GLU C OE2 1 
ATOM   9527  N N   . ILE C  1 172 ? -14.083 -27.888 -72.660  1.00 38.37  ? 172 ILE C N   1 
ATOM   9528  C CA  . ILE C  1 172 ? -13.513 -27.087 -71.581  1.00 36.28  ? 172 ILE C CA  1 
ATOM   9529  C C   . ILE C  1 172 ? -14.026 -25.656 -71.661  1.00 37.79  ? 172 ILE C C   1 
ATOM   9530  O O   . ILE C  1 172 ? -14.358 -25.038 -70.643  1.00 36.40  ? 172 ILE C O   1 
ATOM   9531  C CB  . ILE C  1 172 ? -11.974 -27.148 -71.639  1.00 34.79  ? 172 ILE C CB  1 
ATOM   9532  C CG1 . ILE C  1 172 ? -11.467 -28.480 -71.094  1.00 35.58  ? 172 ILE C CG1 1 
ATOM   9533  C CG2 . ILE C  1 172 ? -11.342 -25.985 -70.878  1.00 31.71  ? 172 ILE C CG2 1 
ATOM   9534  C CD1 . ILE C  1 172 ? -11.591 -28.611 -69.573  1.00 37.08  ? 172 ILE C CD1 1 
ATOM   9535  N N   . ILE C  1 173 ? -14.127 -25.111 -72.875  1.00 38.92  ? 173 ILE C N   1 
ATOM   9536  C CA  . ILE C  1 173 ? -14.585 -23.733 -73.022  1.00 34.81  ? 173 ILE C CA  1 
ATOM   9537  C C   . ILE C  1 173 ? -16.022 -23.601 -72.536  1.00 35.13  ? 173 ILE C C   1 
ATOM   9538  O O   . ILE C  1 173 ? -16.371 -22.669 -71.795  1.00 38.59  ? 173 ILE C O   1 
ATOM   9539  C CB  . ILE C  1 173 ? -14.436 -23.273 -74.484  1.00 34.08  ? 173 ILE C CB  1 
ATOM   9540  C CG1 . ILE C  1 173 ? -12.969 -23.335 -74.907  1.00 35.55  ? 173 ILE C CG1 1 
ATOM   9541  C CG2 . ILE C  1 173 ? -14.937 -21.866 -74.638  1.00 30.94  ? 173 ILE C CG2 1 
ATOM   9542  C CD1 . ILE C  1 173 ? -12.716 -22.811 -76.322  1.00 36.63  ? 173 ILE C CD1 1 
ATOM   9543  N N   . LYS C  1 174 ? -16.872 -24.547 -72.932  1.00 35.31  ? 174 LYS C N   1 
ATOM   9544  C CA  . LYS C  1 174 ? -18.279 -24.538 -72.551  1.00 42.70  ? 174 LYS C CA  1 
ATOM   9545  C C   . LYS C  1 174 ? -18.508 -24.649 -71.057  1.00 37.30  ? 174 LYS C C   1 
ATOM   9546  O O   . LYS C  1 174 ? -19.650 -24.472 -70.623  1.00 40.02  ? 174 LYS C O   1 
ATOM   9547  C CB  . LYS C  1 174 ? -19.043 -25.679 -73.216  1.00 45.44  ? 174 LYS C CB  1 
ATOM   9548  C CG  . LYS C  1 174 ? -19.448 -25.389 -74.640  1.00 49.66  ? 174 LYS C CG  1 
ATOM   9549  C CD  . LYS C  1 174 ? -20.680 -24.431 -74.689  1.00 59.73  ? 174 LYS C CD  1 
ATOM   9550  C CE  . LYS C  1 174 ? -21.780 -24.598 -73.611  1.00 60.23  ? 174 LYS C CE  1 
ATOM   9551  N NZ  . LYS C  1 174 ? -22.527 -23.299 -73.658  1.00 59.77  ? 174 LYS C NZ  1 
ATOM   9552  N N   . LYS C  1 175 ? -17.479 -24.973 -70.284  1.00 41.36  ? 175 LYS C N   1 
ATOM   9553  C CA  . LYS C  1 175 ? -17.569 -25.136 -68.839  1.00 45.72  ? 175 LYS C CA  1 
ATOM   9554  C C   . LYS C  1 175 ? -16.946 -23.978 -68.078  1.00 38.39  ? 175 LYS C C   1 
ATOM   9555  O O   . LYS C  1 175 ? -17.015 -23.956 -66.844  1.00 35.45  ? 175 LYS C O   1 
ATOM   9556  C CB  . LYS C  1 175 ? -16.880 -26.437 -68.403  1.00 47.89  ? 175 LYS C CB  1 
ATOM   9557  C CG  . LYS C  1 175 ? -17.549 -27.719 -68.837  1.00 52.85  ? 175 LYS C CG  1 
ATOM   9558  C CD  . LYS C  1 175 ? -17.162 -28.841 -67.886  1.00 58.35  ? 175 LYS C CD  1 
ATOM   9559  C CE  . LYS C  1 175 ? -17.055 -30.180 -68.598  1.00 62.69  ? 175 LYS C CE  1 
ATOM   9560  N NZ  . LYS C  1 175 ? -15.998 -31.035 -67.983  1.00 65.57  ? 175 LYS C NZ  1 
ATOM   9561  N N   . THR C  1 176 ? -16.365 -23.011 -68.784  1.00 32.29  ? 176 THR C N   1 
ATOM   9562  C CA  . THR C  1 176 ? -15.439 -22.073 -68.159  1.00 35.42  ? 176 THR C CA  1 
ATOM   9563  C C   . THR C  1 176 ? -16.163 -21.034 -67.310  1.00 39.86  ? 176 THR C C   1 
ATOM   9564  O O   . THR C  1 176 ? -15.815 -20.823 -66.144  1.00 39.00  ? 176 THR C O   1 
ATOM   9565  C CB  . THR C  1 176 ? -14.595 -21.396 -69.231  1.00 31.13  ? 176 THR C CB  1 
ATOM   9566  O OG1 . THR C  1 176 ? -13.743 -22.375 -69.829  1.00 31.65  ? 176 THR C OG1 1 
ATOM   9567  C CG2 . THR C  1 176 ? -13.745 -20.281 -68.616  1.00 28.53  ? 176 THR C CG2 1 
ATOM   9568  N N   . LEU C  1 177 ? -17.155 -20.349 -67.878  1.00 40.06  ? 177 LEU C N   1 
ATOM   9569  C CA  . LEU C  1 177 ? -17.902 -19.412 -67.049  1.00 41.92  ? 177 LEU C CA  1 
ATOM   9570  C C   . LEU C  1 177 ? -18.598 -20.135 -65.906  1.00 42.81  ? 177 LEU C C   1 
ATOM   9571  O O   . LEU C  1 177 ? -18.784 -19.562 -64.824  1.00 37.32  ? 177 LEU C O   1 
ATOM   9572  C CB  . LEU C  1 177 ? -18.910 -18.630 -67.894  1.00 42.24  ? 177 LEU C CB  1 
ATOM   9573  C CG  . LEU C  1 177 ? -18.267 -17.802 -69.007  1.00 40.69  ? 177 LEU C CG  1 
ATOM   9574  C CD1 . LEU C  1 177 ? -19.328 -17.086 -69.795  1.00 42.75  ? 177 LEU C CD1 1 
ATOM   9575  C CD2 . LEU C  1 177 ? -17.262 -16.811 -68.447  1.00 39.97  ? 177 LEU C CD2 1 
ATOM   9576  N N   . SER C  1 178 ? -18.961 -21.402 -66.111  1.00 47.73  ? 178 SER C N   1 
ATOM   9577  C CA  . SER C  1 178 ? -19.664 -22.130 -65.060  1.00 49.42  ? 178 SER C CA  1 
ATOM   9578  C C   . SER C  1 178 ? -18.766 -22.394 -63.856  1.00 44.57  ? 178 SER C C   1 
ATOM   9579  O O   . SER C  1 178 ? -19.253 -22.411 -62.722  1.00 46.02  ? 178 SER C O   1 
ATOM   9580  C CB  . SER C  1 178 ? -20.225 -23.438 -65.618  1.00 52.76  ? 178 SER C CB  1 
ATOM   9581  O OG  . SER C  1 178 ? -21.396 -23.194 -66.380  1.00 56.54  ? 178 SER C OG  1 
ATOM   9582  N N   . ILE C  1 179 ? -17.459 -22.587 -64.069  1.00 42.21  ? 179 ILE C N   1 
ATOM   9583  C CA  . ILE C  1 179 ? -16.583 -22.811 -62.920  1.00 43.95  ? 179 ILE C CA  1 
ATOM   9584  C C   . ILE C  1 179 ? -16.365 -21.510 -62.145  1.00 40.10  ? 179 ILE C C   1 
ATOM   9585  O O   . ILE C  1 179 ? -16.263 -21.530 -60.912  1.00 37.11  ? 179 ILE C O   1 
ATOM   9586  C CB  . ILE C  1 179 ? -15.248 -23.472 -63.339  1.00 40.81  ? 179 ILE C CB  1 
ATOM   9587  C CG1 . ILE C  1 179 ? -14.556 -24.069 -62.106  1.00 43.13  ? 179 ILE C CG1 1 
ATOM   9588  C CG2 . ILE C  1 179 ? -14.309 -22.494 -64.023  1.00 37.45  ? 179 ILE C CG2 1 
ATOM   9589  C CD1 . ILE C  1 179 ? -13.475 -25.076 -62.425  1.00 39.46  ? 179 ILE C CD1 1 
ATOM   9590  N N   . TYR C  1 180 ? -16.323 -20.362 -62.833  1.00 31.27  ? 180 TYR C N   1 
ATOM   9591  C CA  . TYR C  1 180 ? -16.265 -19.084 -62.120  1.00 34.87  ? 180 TYR C CA  1 
ATOM   9592  C C   . TYR C  1 180 ? -17.505 -18.872 -61.262  1.00 42.01  ? 180 TYR C C   1 
ATOM   9593  O O   . TYR C  1 180 ? -17.400 -18.466 -60.098  1.00 41.60  ? 180 TYR C O   1 
ATOM   9594  C CB  . TYR C  1 180 ? -16.086 -17.932 -63.105  1.00 32.33  ? 180 TYR C CB  1 
ATOM   9595  C CG  . TYR C  1 180 ? -14.683 -17.888 -63.650  1.00 31.20  ? 180 TYR C CG  1 
ATOM   9596  C CD1 . TYR C  1 180 ? -13.650 -17.323 -62.914  1.00 31.95  ? 180 TYR C CD1 1 
ATOM   9597  C CD2 . TYR C  1 180 ? -14.380 -18.442 -64.893  1.00 33.21  ? 180 TYR C CD2 1 
ATOM   9598  C CE1 . TYR C  1 180 ? -12.351 -17.302 -63.403  1.00 29.05  ? 180 TYR C CE1 1 
ATOM   9599  C CE2 . TYR C  1 180 ? -13.091 -18.421 -65.388  1.00 26.77  ? 180 TYR C CE2 1 
ATOM   9600  C CZ  . TYR C  1 180 ? -12.081 -17.850 -64.637  1.00 25.66  ? 180 TYR C CZ  1 
ATOM   9601  O OH  . TYR C  1 180 ? -10.799 -17.830 -65.129  1.00 24.33  ? 180 TYR C OH  1 
ATOM   9602  N N   . ARG C  1 181 ? -18.689 -19.144 -61.819  1.00 46.00  ? 181 ARG C N   1 
ATOM   9603  C CA  . ARG C  1 181 ? -19.908 -19.127 -61.014  1.00 47.93  ? 181 ARG C CA  1 
ATOM   9604  C C   . ARG C  1 181 ? -19.791 -20.060 -59.815  1.00 47.19  ? 181 ARG C C   1 
ATOM   9605  O O   . ARG C  1 181 ? -20.232 -19.725 -58.708  1.00 45.99  ? 181 ARG C O   1 
ATOM   9606  C CB  . ARG C  1 181 ? -21.108 -19.527 -61.873  1.00 48.91  ? 181 ARG C CB  1 
ATOM   9607  C CG  . ARG C  1 181 ? -21.661 -18.426 -62.761  1.00 52.94  ? 181 ARG C CG  1 
ATOM   9608  C CD  . ARG C  1 181 ? -22.977 -18.860 -63.389  1.00 56.58  ? 181 ARG C CD  1 
ATOM   9609  N NE  . ARG C  1 181 ? -23.292 -18.093 -64.589  1.00 59.17  ? 181 ARG C NE  1 
ATOM   9610  C CZ  . ARG C  1 181 ? -23.068 -18.515 -65.828  1.00 60.06  ? 181 ARG C CZ  1 
ATOM   9611  N NH1 . ARG C  1 181 ? -22.518 -19.706 -66.040  1.00 59.43  ? 181 ARG C NH1 1 
ATOM   9612  N NH2 . ARG C  1 181 ? -23.396 -17.744 -66.857  1.00 61.76  ? 181 ARG C NH2 1 
ATOM   9613  N N   . GLU C  1 182 ? -19.194 -21.236 -60.020  1.00 47.90  ? 182 GLU C N   1 
ATOM   9614  C CA  . GLU C  1 182 ? -19.175 -22.261 -58.984  1.00 50.35  ? 182 GLU C CA  1 
ATOM   9615  C C   . GLU C  1 182 ? -18.308 -21.848 -57.796  1.00 49.94  ? 182 GLU C C   1 
ATOM   9616  O O   . GLU C  1 182 ? -18.741 -21.939 -56.643  1.00 52.03  ? 182 GLU C O   1 
ATOM   9617  C CB  . GLU C  1 182 ? -18.692 -23.588 -59.571  1.00 52.56  ? 182 GLU C CB  1 
ATOM   9618  C CG  . GLU C  1 182 ? -18.686 -24.713 -58.548  1.00 58.20  ? 182 GLU C CG  1 
ATOM   9619  C CD  . GLU C  1 182 ? -18.132 -26.023 -59.081  1.00 59.17  ? 182 GLU C CD  1 
ATOM   9620  O OE1 . GLU C  1 182 ? -17.455 -26.006 -60.130  1.00 57.97  ? 182 GLU C OE1 1 
ATOM   9621  O OE2 . GLU C  1 182 ? -18.365 -27.070 -58.436  1.00 60.99  ? 182 GLU C OE2 1 
ATOM   9622  N N   . ILE C  1 183 ? -17.073 -21.404 -58.054  1.00 46.24  ? 183 ILE C N   1 
ATOM   9623  C CA  . ILE C  1 183 ? -16.197 -21.001 -56.958  1.00 46.20  ? 183 ILE C CA  1 
ATOM   9624  C C   . ILE C  1 183 ? -16.699 -19.741 -56.269  1.00 46.95  ? 183 ILE C C   1 
ATOM   9625  O O   . ILE C  1 183 ? -16.370 -19.505 -55.102  1.00 49.57  ? 183 ILE C O   1 
ATOM   9626  C CB  . ILE C  1 183 ? -14.746 -20.802 -57.446  1.00 47.33  ? 183 ILE C CB  1 
ATOM   9627  C CG1 . ILE C  1 183 ? -14.638 -19.605 -58.402  1.00 51.47  ? 183 ILE C CG1 1 
ATOM   9628  C CG2 . ILE C  1 183 ? -14.219 -22.074 -58.089  1.00 39.97  ? 183 ILE C CG2 1 
ATOM   9629  C CD1 . ILE C  1 183 ? -14.063 -18.350 -57.762  1.00 52.17  ? 183 ILE C CD1 1 
ATOM   9630  N N   . LYS C  1 184 ? -17.486 -18.919 -56.961  1.00 43.32  ? 184 LYS C N   1 
ATOM   9631  C CA  . LYS C  1 184 ? -18.062 -17.743 -56.320  1.00 48.76  ? 184 LYS C CA  1 
ATOM   9632  C C   . LYS C  1 184 ? -19.156 -18.138 -55.330  1.00 53.24  ? 184 LYS C C   1 
ATOM   9633  O O   . LYS C  1 184 ? -19.155 -17.692 -54.176  1.00 54.11  ? 184 LYS C O   1 
ATOM   9634  C CB  . LYS C  1 184 ? -18.605 -16.795 -57.382  1.00 46.88  ? 184 LYS C CB  1 
ATOM   9635  C CG  . LYS C  1 184 ? -19.151 -15.502 -56.840  1.00 48.45  ? 184 LYS C CG  1 
ATOM   9636  C CD  . LYS C  1 184 ? -19.440 -14.565 -57.989  1.00 52.64  ? 184 LYS C CD  1 
ATOM   9637  C CE  . LYS C  1 184 ? -20.693 -13.757 -57.730  1.00 56.80  ? 184 LYS C CE  1 
ATOM   9638  N NZ  . LYS C  1 184 ? -20.432 -12.699 -56.727  1.00 59.43  ? 184 LYS C NZ  1 
ATOM   9639  N N   . GLU C  1 185 ? -20.098 -18.980 -55.768  1.00 55.93  ? 185 GLU C N   1 
ATOM   9640  C CA  . GLU C  1 185 ? -21.160 -19.442 -54.876  1.00 56.87  ? 185 GLU C CA  1 
ATOM   9641  C C   . GLU C  1 185 ? -20.587 -20.217 -53.699  1.00 54.48  ? 185 GLU C C   1 
ATOM   9642  O O   . GLU C  1 185 ? -21.089 -20.116 -52.572  1.00 59.82  ? 185 GLU C O   1 
ATOM   9643  C CB  . GLU C  1 185 ? -22.162 -20.307 -55.647  1.00 61.98  ? 185 GLU C CB  1 
ATOM   9644  C CG  . GLU C  1 185 ? -23.016 -21.234 -54.768  1.00 72.66  ? 185 GLU C CG  1 
ATOM   9645  C CD  . GLU C  1 185 ? -22.487 -22.669 -54.723  1.00 78.50  ? 185 GLU C CD  1 
ATOM   9646  O OE1 . GLU C  1 185 ? -21.749 -23.062 -55.657  1.00 78.54  ? 185 GLU C OE1 1 
ATOM   9647  O OE2 . GLU C  1 185 ? -22.808 -23.401 -53.756  1.00 80.57  ? 185 GLU C OE2 1 
ATOM   9648  N N   . GLU C  1 186 ? -19.538 -20.994 -53.939  1.00 46.91  ? 186 GLU C N   1 
ATOM   9649  C CA  . GLU C  1 186 ? -18.923 -21.818 -52.907  1.00 48.85  ? 186 GLU C CA  1 
ATOM   9650  C C   . GLU C  1 186 ? -17.982 -21.040 -52.000  1.00 48.77  ? 186 GLU C C   1 
ATOM   9651  O O   . GLU C  1 186 ? -17.347 -21.648 -51.129  1.00 51.66  ? 186 GLU C O   1 
ATOM   9652  C CB  . GLU C  1 186 ? -18.176 -22.991 -53.543  1.00 51.42  ? 186 GLU C CB  1 
ATOM   9653  C CG  . GLU C  1 186 ? -19.088 -24.129 -53.919  1.00 60.56  ? 186 GLU C CG  1 
ATOM   9654  C CD  . GLU C  1 186 ? -18.520 -24.999 -55.010  1.00 67.31  ? 186 GLU C CD  1 
ATOM   9655  O OE1 . GLU C  1 186 ? -17.277 -25.068 -55.129  1.00 66.63  ? 186 GLU C OE1 1 
ATOM   9656  O OE2 . GLU C  1 186 ? -19.322 -25.640 -55.724  1.00 72.01  ? 186 GLU C OE2 1 
ATOM   9657  N N   . GLY C  1 187 ? -17.875 -19.724 -52.179  1.00 43.76  ? 187 GLY C N   1 
ATOM   9658  C CA  . GLY C  1 187 ? -17.054 -18.922 -51.298  1.00 42.41  ? 187 GLY C CA  1 
ATOM   9659  C C   . GLY C  1 187 ? -15.573 -19.197 -51.434  1.00 45.46  ? 187 GLY C C   1 
ATOM   9660  O O   . GLY C  1 187 ? -14.779 -18.739 -50.609  1.00 50.70  ? 187 GLY C O   1 
ATOM   9661  N N   . LYS C  1 188 ? -15.180 -19.943 -52.471  1.00 40.87  ? 188 LYS C N   1 
ATOM   9662  C CA  . LYS C  1 188 ? -13.773 -20.259 -52.652  1.00 40.80  ? 188 LYS C CA  1 
ATOM   9663  C C   . LYS C  1 188 ? -12.988 -19.089 -53.230  1.00 42.92  ? 188 LYS C C   1 
ATOM   9664  O O   . LYS C  1 188 ? -11.753 -19.076 -53.139  1.00 42.55  ? 188 LYS C O   1 
ATOM   9665  C CB  . LYS C  1 188 ? -13.625 -21.490 -53.552  1.00 44.25  ? 188 LYS C CB  1 
ATOM   9666  C CG  . LYS C  1 188 ? -13.579 -22.811 -52.799  1.00 46.08  ? 188 LYS C CG  1 
ATOM   9667  C CD  . LYS C  1 188 ? -14.269 -23.923 -53.566  1.00 50.64  ? 188 LYS C CD  1 
ATOM   9668  C CE  . LYS C  1 188 ? -14.060 -25.290 -52.903  1.00 55.29  ? 188 LYS C CE  1 
ATOM   9669  N NZ  . LYS C  1 188 ? -13.816 -25.190 -51.432  1.00 60.14  ? 188 LYS C NZ  1 
ATOM   9670  N N   . GLY C  1 189 ? -13.676 -18.123 -53.825  1.00 38.29  ? 189 GLY C N   1 
ATOM   9671  C CA  . GLY C  1 189 ? -13.028 -16.937 -54.329  1.00 35.27  ? 189 GLY C CA  1 
ATOM   9672  C C   . GLY C  1 189 ? -14.054 -15.907 -54.733  1.00 36.13  ? 189 GLY C C   1 
ATOM   9673  O O   . GLY C  1 189 ? -15.222 -16.225 -54.985  1.00 38.30  ? 189 GLY C O   1 
ATOM   9674  N N   . SER C  1 190 ? -13.605 -14.661 -54.771  1.00 33.32  ? 190 SER C N   1 
ATOM   9675  C CA  . SER C  1 190 ? -14.400 -13.573 -55.306  1.00 30.75  ? 190 SER C CA  1 
ATOM   9676  C C   . SER C  1 190 ? -14.035 -13.379 -56.766  1.00 36.81  ? 190 SER C C   1 
ATOM   9677  O O   . SER C  1 190 ? -12.892 -13.603 -57.172  1.00 40.31  ? 190 SER C O   1 
ATOM   9678  C CB  . SER C  1 190 ? -14.161 -12.278 -54.530  1.00 33.36  ? 190 SER C CB  1 
ATOM   9679  O OG  . SER C  1 190 ? -14.478 -12.439 -53.154  1.00 35.08  ? 190 SER C OG  1 
ATOM   9680  N N   . VAL C  1 191 ? -15.023 -12.984 -57.557  1.00 34.62  ? 191 VAL C N   1 
ATOM   9681  C CA  . VAL C  1 191 ? -14.831 -12.696 -58.971  1.00 36.47  ? 191 VAL C CA  1 
ATOM   9682  C C   . VAL C  1 191 ? -15.201 -11.239 -59.202  1.00 36.59  ? 191 VAL C C   1 
ATOM   9683  O O   . VAL C  1 191 ? -16.282 -10.797 -58.801  1.00 42.64  ? 191 VAL C O   1 
ATOM   9684  C CB  . VAL C  1 191 ? -15.665 -13.635 -59.855  1.00 34.47  ? 191 VAL C CB  1 
ATOM   9685  C CG1 . VAL C  1 191 ? -15.371 -13.375 -61.335  1.00 40.48  ? 191 VAL C CG1 1 
ATOM   9686  C CG2 . VAL C  1 191 ? -15.358 -15.060 -59.503  1.00 30.91  ? 191 VAL C CG2 1 
ATOM   9687  N N   . SER C  1 192 ? -14.292 -10.490 -59.811  1.00 34.95  ? 192 SER C N   1 
ATOM   9688  C CA  . SER C  1 192 ? -14.512 -9.091  -60.143  1.00 33.73  ? 192 SER C CA  1 
ATOM   9689  C C   . SER C  1 192 ? -14.554 -8.911  -61.658  1.00 34.20  ? 192 SER C C   1 
ATOM   9690  O O   . SER C  1 192 ? -14.411 -9.859  -62.435  1.00 32.73  ? 192 SER C O   1 
ATOM   9691  C CB  . SER C  1 192 ? -13.418 -8.215  -59.542  1.00 28.15  ? 192 SER C CB  1 
ATOM   9692  O OG  . SER C  1 192 ? -12.170 -8.497  -60.149  1.00 31.60  ? 192 SER C OG  1 
ATOM   9693  N N   . THR C  1 193 ? -14.654 -7.648  -62.044  1.00 32.11  ? 193 THR C N   1 
ATOM   9694  C CA  . THR C  1 193 ? -14.597 -7.289  -63.422  1.00 26.08  ? 193 THR C CA  1 
ATOM   9695  C C   . THR C  1 193 ? -13.927 -6.005  -63.611  1.00 30.32  ? 193 THR C C   1 
ATOM   9696  O O   . THR C  1 193 ? -13.522 -5.389  -62.672  1.00 32.45  ? 193 THR C O   1 
ATOM   9697  C CB  . THR C  1 193 ? -15.989 -7.224  -64.078  1.00 38.55  ? 193 THR C CB  1 
ATOM   9698  O OG1 . THR C  1 193 ? -15.869 -7.489  -65.477  1.00 39.68  ? 193 THR C OG1 1 
ATOM   9699  C CG2 . THR C  1 193 ? -16.628 -5.877  -63.873  1.00 39.06  ? 193 THR C CG2 1 
ATOM   9700  N N   . SER C  1 194 ? -13.717 -5.624  -64.840  1.00 32.49  ? 194 SER C N   1 
ATOM   9701  C CA  . SER C  1 194 ? -13.145 -4.375  -65.206  1.00 36.10  ? 194 SER C CA  1 
ATOM   9702  C C   . SER C  1 194 ? -14.081 -3.588  -66.196  1.00 35.44  ? 194 SER C C   1 
ATOM   9703  O O   . SER C  1 194 ? -14.928 -4.155  -66.780  1.00 30.70  ? 194 SER C O   1 
ATOM   9704  C CB  . SER C  1 194 ? -11.736 -4.517  -65.797  1.00 35.33  ? 194 SER C CB  1 
ATOM   9705  O OG  . SER C  1 194 ? -10.809 -5.194  -65.023  1.00 34.36  ? 194 SER C OG  1 
ATOM   9706  N N   . PRO C  1 195 ? -13.952 -2.276  -66.231  1.00 36.57  ? 195 PRO C N   1 
ATOM   9707  C CA  . PRO C  1 195 ? -14.670 -1.490  -67.250  1.00 34.40  ? 195 PRO C CA  1 
ATOM   9708  C C   . PRO C  1 195 ? -14.632 -2.257  -68.551  1.00 34.63  ? 195 PRO C C   1 
ATOM   9709  O O   . PRO C  1 195 ? -13.582 -2.769  -68.858  1.00 36.05  ? 195 PRO C O   1 
ATOM   9710  C CB  . PRO C  1 195 ? -13.922 -0.207  -67.278  1.00 32.12  ? 195 PRO C CB  1 
ATOM   9711  C CG  . PRO C  1 195 ? -13.397 -0.052  -65.891  1.00 39.29  ? 195 PRO C CG  1 
ATOM   9712  C CD  . PRO C  1 195 ? -13.211 -1.417  -65.307  1.00 36.80  ? 195 PRO C CD  1 
ATOM   9713  N N   . TYR C  1 196 ? -15.701 -2.251  -69.337  1.00 34.17  ? 196 TYR C N   1 
ATOM   9714  C CA  . TYR C  1 196 ? -15.893 -3.221  -70.451  1.00 35.64  ? 196 TYR C CA  1 
ATOM   9715  C C   . TYR C  1 196 ? -14.784 -3.627  -71.361  1.00 37.73  ? 196 TYR C C   1 
ATOM   9716  O O   . TYR C  1 196 ? -14.480 -4.774  -71.427  1.00 36.96  ? 196 TYR C O   1 
ATOM   9717  C CB  . TYR C  1 196 ? -17.175 -2.887  -71.225  1.00 36.14  ? 196 TYR C CB  1 
ATOM   9718  C CG  . TYR C  1 196 ? -17.916 -4.031  -71.762  1.00 36.67  ? 196 TYR C CG  1 
ATOM   9719  C CD1 . TYR C  1 196 ? -17.439 -4.731  -72.842  1.00 37.85  ? 196 TYR C CD1 1 
ATOM   9720  C CD2 . TYR C  1 196 ? -19.104 -4.399  -71.213  1.00 37.01  ? 196 TYR C CD2 1 
ATOM   9721  C CE1 . TYR C  1 196 ? -18.131 -5.779  -73.355  1.00 40.28  ? 196 TYR C CE1 1 
ATOM   9722  C CE2 . TYR C  1 196 ? -19.812 -5.444  -71.715  1.00 43.55  ? 196 TYR C CE2 1 
ATOM   9723  C CZ  . TYR C  1 196 ? -19.318 -6.124  -72.791  1.00 43.94  ? 196 TYR C CZ  1 
ATOM   9724  O OH  . TYR C  1 196 ? -20.026 -7.154  -73.277  1.00 45.94  ? 196 TYR C OH  1 
ATOM   9725  N N   . TYR C  1 197 ? -14.222 -2.706  -72.056  1.00 37.96  ? 197 TYR C N   1 
ATOM   9726  C CA  . TYR C  1 197 ? -13.211 -3.035  -72.996  1.00 35.53  ? 197 TYR C CA  1 
ATOM   9727  C C   . TYR C  1 197 ? -11.794 -2.780  -72.522  1.00 31.36  ? 197 TYR C C   1 
ATOM   9728  O O   . TYR C  1 197 ? -10.926 -2.630  -73.290  1.00 34.05  ? 197 TYR C O   1 
ATOM   9729  C CB  . TYR C  1 197 ? -13.543 -2.313  -74.290  1.00 36.91  ? 197 TYR C CB  1 
ATOM   9730  C CG  . TYR C  1 197 ? -14.795 -2.814  -74.906  1.00 38.38  ? 197 TYR C CG  1 
ATOM   9731  C CD1 . TYR C  1 197 ? -14.805 -3.953  -75.682  1.00 38.72  ? 197 TYR C CD1 1 
ATOM   9732  C CD2 . TYR C  1 197 ? -15.972 -2.171  -74.685  1.00 38.04  ? 197 TYR C CD2 1 
ATOM   9733  C CE1 . TYR C  1 197 ? -15.970 -4.421  -76.221  1.00 36.01  ? 197 TYR C CE1 1 
ATOM   9734  C CE2 . TYR C  1 197 ? -17.134 -2.630  -75.223  1.00 42.26  ? 197 TYR C CE2 1 
ATOM   9735  C CZ  . TYR C  1 197 ? -17.125 -3.745  -75.993  1.00 38.99  ? 197 TYR C CZ  1 
ATOM   9736  O OH  . TYR C  1 197 ? -18.310 -4.169  -76.494  1.00 46.82  ? 197 TYR C OH  1 
ATOM   9737  N N   . HIS C  1 198 ? -11.629 -2.771  -71.199  1.00 32.49  ? 198 HIS C N   1 
ATOM   9738  C CA  . HIS C  1 198 ? -10.305 -2.609  -70.601  1.00 31.21  ? 198 HIS C CA  1 
ATOM   9739  C C   . HIS C  1 198 ? -9.632  -1.304  -71.042  1.00 32.84  ? 198 HIS C C   1 
ATOM   9740  O O   . HIS C  1 198 ? -8.478  -1.336  -71.480  1.00 37.05  ? 198 HIS C O   1 
ATOM   9741  C CB  . HIS C  1 198 ? -9.452  -3.838  -70.968  1.00 30.92  ? 198 HIS C CB  1 
ATOM   9742  C CG  . HIS C  1 198 ? -8.272  -4.073  -70.080  1.00 25.51  ? 198 HIS C CG  1 
ATOM   9743  N ND1 . HIS C  1 198 ? -7.004  -3.655  -70.416  1.00 27.19  ? 198 HIS C ND1 1 
ATOM   9744  C CD2 . HIS C  1 198 ? -8.153  -4.716  -68.890  1.00 26.26  ? 198 HIS C CD2 1 
ATOM   9745  C CE1 . HIS C  1 198 ? -6.157  -4.003  -69.460  1.00 30.67  ? 198 HIS C CE1 1 
ATOM   9746  N NE2 . HIS C  1 198 ? -6.828  -4.652  -68.525  1.00 25.18  ? 198 HIS C NE2 1 
ATOM   9747  N N   . PRO C  1 199 ? -10.279 -0.142  -70.913  1.00 32.59  ? 199 PRO C N   1 
ATOM   9748  C CA  . PRO C  1 199 ? -9.636  1.116   -71.300  1.00 38.40  ? 199 PRO C CA  1 
ATOM   9749  C C   . PRO C  1 199 ? -8.881  1.761   -70.141  1.00 44.31  ? 199 PRO C C   1 
ATOM   9750  O O   . PRO C  1 199 ? -8.938  1.318   -68.991  1.00 42.09  ? 199 PRO C O   1 
ATOM   9751  C CB  . PRO C  1 199 ? -10.831 1.989   -71.696  1.00 37.15  ? 199 PRO C CB  1 
ATOM   9752  C CG  . PRO C  1 199 ? -11.861 1.604   -70.670  1.00 35.87  ? 199 PRO C CG  1 
ATOM   9753  C CD  . PRO C  1 199 ? -11.632 0.111   -70.381  1.00 33.20  ? 199 PRO C CD  1 
ATOM   9754  N N   . LEU C  1 200 ? -8.186  2.852   -70.469  1.00 44.45  ? 200 LEU C N   1 
ATOM   9755  C CA  . LEU C  1 200 ? -7.491  3.676   -69.482  1.00 36.71  ? 200 LEU C CA  1 
ATOM   9756  C C   . LEU C  1 200 ? -8.473  4.725   -68.991  1.00 38.15  ? 200 LEU C C   1 
ATOM   9757  O O   . LEU C  1 200 ? -8.568  5.826   -69.537  1.00 38.77  ? 200 LEU C O   1 
ATOM   9758  C CB  . LEU C  1 200 ? -6.244  4.312   -70.080  1.00 31.16  ? 200 LEU C CB  1 
ATOM   9759  C CG  . LEU C  1 200 ? -5.091  3.339   -70.309  1.00 33.22  ? 200 LEU C CG  1 
ATOM   9760  C CD1 . LEU C  1 200 ? -3.967  4.009   -71.094  1.00 38.30  ? 200 LEU C CD1 1 
ATOM   9761  C CD2 . LEU C  1 200 ? -4.586  2.763   -68.969  1.00 31.76  ? 200 LEU C CD2 1 
ATOM   9762  N N   . ILE C  1 201 ? -9.213  4.373   -67.941  1.00 34.31  ? 201 ILE C N   1 
ATOM   9763  C CA  . ILE C  1 201 ? -10.244 5.269   -67.418  1.00 30.90  ? 201 ILE C CA  1 
ATOM   9764  C C   . ILE C  1 201 ? -9.710  6.666   -67.108  1.00 30.46  ? 201 ILE C C   1 
ATOM   9765  O O   . ILE C  1 201 ? -10.363 7.646   -67.495  1.00 31.63  ? 201 ILE C O   1 
ATOM   9766  C CB  . ILE C  1 201 ? -10.949 4.623   -66.218  1.00 30.22  ? 201 ILE C CB  1 
ATOM   9767  C CG1 . ILE C  1 201 ? -11.757 3.414   -66.691  1.00 30.50  ? 201 ILE C CG1 1 
ATOM   9768  C CG2 . ILE C  1 201 ? -11.856 5.639   -65.537  1.00 31.71  ? 201 ILE C CG2 1 
ATOM   9769  C CD1 . ILE C  1 201 ? -12.778 3.753   -67.789  1.00 33.49  ? 201 ILE C CD1 1 
ATOM   9770  N N   . PRO C  1 202 ? -8.555  6.836   -66.442  1.00 31.98  ? 202 PRO C N   1 
ATOM   9771  C CA  . PRO C  1 202 ? -8.132  8.204   -66.087  1.00 34.63  ? 202 PRO C CA  1 
ATOM   9772  C C   . PRO C  1 202 ? -7.844  9.070   -67.302  1.00 34.65  ? 202 PRO C C   1 
ATOM   9773  O O   . PRO C  1 202 ? -8.066  10.287  -67.256  1.00 35.28  ? 202 PRO C O   1 
ATOM   9774  C CB  . PRO C  1 202 ? -6.874  7.979   -65.228  1.00 30.55  ? 202 PRO C CB  1 
ATOM   9775  C CG  . PRO C  1 202 ? -7.008  6.537   -64.707  1.00 30.92  ? 202 PRO C CG  1 
ATOM   9776  C CD  . PRO C  1 202 ? -7.647  5.818   -65.869  1.00 30.03  ? 202 PRO C CD  1 
ATOM   9777  N N   . ILE C  1 203 ? -7.371  8.474   -68.396  1.00 32.72  ? 203 ILE C N   1 
ATOM   9778  C CA  . ILE C  1 203 ? -7.131  9.254   -69.607  1.00 36.67  ? 203 ILE C CA  1 
ATOM   9779  C C   . ILE C  1 203 ? -8.451  9.695   -70.234  1.00 39.96  ? 203 ILE C C   1 
ATOM   9780  O O   . ILE C  1 203 ? -8.593  10.848  -70.662  1.00 43.91  ? 203 ILE C O   1 
ATOM   9781  C CB  . ILE C  1 203 ? -6.258  8.446   -70.585  1.00 37.33  ? 203 ILE C CB  1 
ATOM   9782  C CG1 . ILE C  1 203 ? -4.846  8.335   -70.015  1.00 36.07  ? 203 ILE C CG1 1 
ATOM   9783  C CG2 . ILE C  1 203 ? -6.224  9.109   -71.990  1.00 41.88  ? 203 ILE C CG2 1 
ATOM   9784  C CD1 . ILE C  1 203 ? -3.845  7.805   -70.997  1.00 40.61  ? 203 ILE C CD1 1 
ATOM   9785  N N   . LEU C  1 204 ? -9.448  8.802   -70.268  1.00 38.26  ? 204 LEU C N   1 
ATOM   9786  C CA  . LEU C  1 204 ? -10.752 9.170   -70.814  1.00 39.54  ? 204 LEU C CA  1 
ATOM   9787  C C   . LEU C  1 204 ? -11.399 10.292  -70.006  1.00 41.96  ? 204 LEU C C   1 
ATOM   9788  O O   . LEU C  1 204 ? -12.021 11.194  -70.574  1.00 42.58  ? 204 LEU C O   1 
ATOM   9789  C CB  . LEU C  1 204 ? -11.667 7.948   -70.850  1.00 39.23  ? 204 LEU C CB  1 
ATOM   9790  C CG  . LEU C  1 204 ? -11.239 6.750   -71.691  1.00 39.02  ? 204 LEU C CG  1 
ATOM   9791  C CD1 . LEU C  1 204 ? -12.336 5.685   -71.685  1.00 38.23  ? 204 LEU C CD1 1 
ATOM   9792  C CD2 . LEU C  1 204 ? -10.899 7.182   -73.118  1.00 35.53  ? 204 LEU C CD2 1 
ATOM   9793  N N   . LEU C  1 205 ? -11.269 10.252  -68.676  1.00 38.05  ? 205 LEU C N   1 
ATOM   9794  C CA  . LEU C  1 205 ? -11.888 11.280  -67.842  1.00 35.90  ? 205 LEU C CA  1 
ATOM   9795  C C   . LEU C  1 205 ? -11.182 12.620  -67.981  1.00 37.37  ? 205 LEU C C   1 
ATOM   9796  O O   . LEU C  1 205 ? -11.836 13.670  -68.011  1.00 38.83  ? 205 LEU C O   1 
ATOM   9797  C CB  . LEU C  1 205 ? -11.887 10.848  -66.375  1.00 34.99  ? 205 LEU C CB  1 
ATOM   9798  C CG  . LEU C  1 205 ? -12.897 9.763   -66.012  1.00 36.66  ? 205 LEU C CG  1 
ATOM   9799  C CD1 . LEU C  1 205 ? -12.685 9.338   -64.571  1.00 33.46  ? 205 LEU C CD1 1 
ATOM   9800  C CD2 . LEU C  1 205 ? -14.306 10.265  -66.217  1.00 40.50  ? 205 LEU C CD2 1 
ATOM   9801  N N   . ASN C  1 206 ? -9.861  12.618  -68.030  1.00 37.19  ? 206 ASN C N   1 
ATOM   9802  C CA  . ASN C  1 206 ? -9.127  13.867  -68.194  1.00 39.54  ? 206 ASN C CA  1 
ATOM   9803  C C   . ASN C  1 206 ? -7.709  13.576  -68.659  1.00 38.76  ? 206 ASN C C   1 
ATOM   9804  O O   . ASN C  1 206 ? -6.844  13.248  -67.839  1.00 39.11  ? 206 ASN C O   1 
ATOM   9805  C CB  . ASN C  1 206 ? -9.113  14.671  -66.891  1.00 45.41  ? 206 ASN C CB  1 
ATOM   9806  C CG  . ASN C  1 206 ? -8.290  15.949  -66.993  1.00 48.66  ? 206 ASN C CG  1 
ATOM   9807  O OD1 . ASN C  1 206 ? -8.050  16.467  -68.080  1.00 50.48  ? 206 ASN C OD1 1 
ATOM   9808  N ND2 . ASN C  1 206 ? -7.880  16.472  -65.847  1.00 51.43  ? 206 ASN C ND2 1 
ATOM   9809  N N   . PRO C  1 207 ? -7.436  13.695  -69.962  1.00 43.31  ? 207 PRO C N   1 
ATOM   9810  C CA  . PRO C  1 207 ? -6.094  13.370  -70.473  1.00 42.59  ? 207 PRO C CA  1 
ATOM   9811  C C   . PRO C  1 207 ? -4.974  14.174  -69.838  1.00 43.56  ? 207 PRO C C   1 
ATOM   9812  O O   . PRO C  1 207 ? -3.813  13.754  -69.925  1.00 50.79  ? 207 PRO C O   1 
ATOM   9813  C CB  . PRO C  1 207 ? -6.207  13.677  -71.973  1.00 45.92  ? 207 PRO C CB  1 
ATOM   9814  C CG  . PRO C  1 207 ? -7.659  13.561  -72.271  1.00 49.78  ? 207 PRO C CG  1 
ATOM   9815  C CD  . PRO C  1 207 ? -8.361  14.069  -71.042  1.00 48.75  ? 207 PRO C CD  1 
ATOM   9816  N N   . ASN C  1 208 ? -5.276  15.315  -69.217  1.00 44.82  ? 208 ASN C N   1 
ATOM   9817  C CA  . ASN C  1 208 ? -4.247  16.114  -68.561  1.00 47.82  ? 208 ASN C CA  1 
ATOM   9818  C C   . ASN C  1 208 ? -3.674  15.445  -67.322  1.00 44.27  ? 208 ASN C C   1 
ATOM   9819  O O   . ASN C  1 208 ? -2.707  15.965  -66.756  1.00 42.06  ? 208 ASN C O   1 
ATOM   9820  C CB  . ASN C  1 208 ? -4.804  17.485  -68.208  1.00 47.91  ? 208 ASN C CB  1 
ATOM   9821  C CG  . ASN C  1 208 ? -5.098  18.315  -69.442  1.00 56.90  ? 208 ASN C CG  1 
ATOM   9822  O OD1 . ASN C  1 208 ? -4.183  18.783  -70.118  1.00 56.46  ? 208 ASN C OD1 1 
ATOM   9823  N ND2 . ASN C  1 208 ? -6.377  18.486  -69.754  1.00 63.29  ? 208 ASN C ND2 1 
ATOM   9824  N N   . CYS C  1 209 ? -4.229  14.303  -66.908  1.00 44.50  ? 209 CYS C N   1 
ATOM   9825  C CA  . CYS C  1 209 ? -3.697  13.565  -65.767  1.00 44.79  ? 209 CYS C CA  1 
ATOM   9826  C C   . CYS C  1 209 ? -2.343  12.930  -66.065  1.00 44.27  ? 209 CYS C C   1 
ATOM   9827  O O   . CYS C  1 209 ? -1.606  12.603  -65.124  1.00 44.35  ? 209 CYS C O   1 
ATOM   9828  C CB  . CYS C  1 209 ? -4.687  12.484  -65.335  1.00 42.53  ? 209 CYS C CB  1 
ATOM   9829  S SG  . CYS C  1 209 ? -4.772  11.105  -66.490  1.00 48.23  ? 209 CYS C SG  1 
ATOM   9830  N N   . VAL C  1 210 ? -1.992  12.756  -67.344  1.00 46.02  ? 210 VAL C N   1 
ATOM   9831  C CA  . VAL C  1 210 ? -0.680  12.212  -67.688  1.00 46.03  ? 210 VAL C CA  1 
ATOM   9832  C C   . VAL C  1 210 ? 0.434   13.160  -67.264  1.00 45.75  ? 210 VAL C C   1 
ATOM   9833  O O   . VAL C  1 210 ? 1.585   12.746  -67.114  1.00 47.82  ? 210 VAL C O   1 
ATOM   9834  C CB  . VAL C  1 210 ? -0.584  11.878  -69.203  1.00 43.20  ? 210 VAL C CB  1 
ATOM   9835  C CG1 . VAL C  1 210 ? -1.688  10.904  -69.613  1.00 39.80  ? 210 VAL C CG1 1 
ATOM   9836  C CG2 . VAL C  1 210 ? -0.611  13.143  -70.052  1.00 44.80  ? 210 VAL C CG2 1 
ATOM   9837  N N   . TYR C  1 211 ? 0.115   14.425  -67.037  1.00 49.64  ? 211 TYR C N   1 
ATOM   9838  C CA  . TYR C  1 211 ? 1.119   15.378  -66.594  1.00 52.45  ? 211 TYR C CA  1 
ATOM   9839  C C   . TYR C  1 211 ? 1.560   15.179  -65.152  1.00 52.51  ? 211 TYR C C   1 
ATOM   9840  O O   . TYR C  1 211 ? 2.577   15.757  -64.755  1.00 54.48  ? 211 TYR C O   1 
ATOM   9841  C CB  . TYR C  1 211 ? 0.578   16.782  -66.766  1.00 54.29  ? 211 TYR C CB  1 
ATOM   9842  C CG  . TYR C  1 211 ? 0.540   17.157  -68.204  1.00 58.59  ? 211 TYR C CG  1 
ATOM   9843  C CD1 . TYR C  1 211 ? 1.580   16.795  -69.044  1.00 61.06  ? 211 TYR C CD1 1 
ATOM   9844  C CD2 . TYR C  1 211 ? -0.537  17.839  -68.735  1.00 59.67  ? 211 TYR C CD2 1 
ATOM   9845  C CE1 . TYR C  1 211 ? 1.563   17.119  -70.369  1.00 66.10  ? 211 TYR C CE1 1 
ATOM   9846  C CE2 . TYR C  1 211 ? -0.566  18.171  -70.060  1.00 63.64  ? 211 TYR C CE2 1 
ATOM   9847  C CZ  . TYR C  1 211 ? 0.491   17.807  -70.876  1.00 70.13  ? 211 TYR C CZ  1 
ATOM   9848  O OH  . TYR C  1 211 ? 0.486   18.130  -72.211  1.00 83.56  ? 211 TYR C OH  1 
ATOM   9849  N N   . GLU C  1 212 ? 0.837   14.380  -64.362  1.00 51.91  ? 212 GLU C N   1 
ATOM   9850  C CA  . GLU C  1 212 ? 1.149   14.289  -62.940  1.00 48.60  ? 212 GLU C CA  1 
ATOM   9851  C C   . GLU C  1 212 ? 2.426   13.509  -62.673  1.00 50.60  ? 212 GLU C C   1 
ATOM   9852  O O   . GLU C  1 212 ? 3.051   13.708  -61.626  1.00 54.39  ? 212 GLU C O   1 
ATOM   9853  C CB  . GLU C  1 212 ? -0.028  13.669  -62.193  1.00 43.42  ? 212 GLU C CB  1 
ATOM   9854  C CG  . GLU C  1 212 ? -1.285  14.510  -62.301  1.00 42.32  ? 212 GLU C CG  1 
ATOM   9855  C CD  . GLU C  1 212 ? -2.455  13.894  -61.578  1.00 49.85  ? 212 GLU C CD  1 
ATOM   9856  O OE1 . GLU C  1 212 ? -3.604  14.301  -61.849  1.00 54.47  ? 212 GLU C OE1 1 
ATOM   9857  O OE2 . GLU C  1 212 ? -2.228  12.997  -60.740  1.00 51.29  ? 212 GLU C OE2 1 
ATOM   9858  N N   . THR C  1 213 ? 2.835   12.641  -63.595  1.00 49.96  ? 213 THR C N   1 
ATOM   9859  C CA  . THR C  1 213 ? 4.084   11.910  -63.472  1.00 48.44  ? 213 THR C CA  1 
ATOM   9860  C C   . THR C  1 213 ? 5.036   12.134  -64.639  1.00 49.86  ? 213 THR C C   1 
ATOM   9861  O O   . THR C  1 213 ? 6.247   11.969  -64.464  1.00 52.01  ? 213 THR C O   1 
ATOM   9862  C CB  . THR C  1 213 ? 3.812   10.406  -63.339  1.00 45.68  ? 213 THR C CB  1 
ATOM   9863  O OG1 . THR C  1 213 ? 2.960   9.996   -64.414  1.00 47.51  ? 213 THR C OG1 1 
ATOM   9864  C CG2 . THR C  1 213 ? 3.121   10.106  -62.004  1.00 41.48  ? 213 THR C CG2 1 
ATOM   9865  N N   . THR C  1 214 ? 4.536   12.509  -65.812  1.00 51.41  ? 214 THR C N   1 
ATOM   9866  C CA  . THR C  1 214 ? 5.376   12.840  -66.965  1.00 57.06  ? 214 THR C CA  1 
ATOM   9867  C C   . THR C  1 214 ? 4.953   14.219  -67.460  1.00 60.90  ? 214 THR C C   1 
ATOM   9868  O O   . THR C  1 214 ? 4.206   14.345  -68.439  1.00 61.88  ? 214 THR C O   1 
ATOM   9869  C CB  . THR C  1 214 ? 5.264   11.781  -68.063  1.00 59.25  ? 214 THR C CB  1 
ATOM   9870  O OG1 . THR C  1 214 ? 3.908   11.710  -68.524  1.00 62.45  ? 214 THR C OG1 1 
ATOM   9871  C CG2 . THR C  1 214 ? 5.694   10.409  -67.535  1.00 56.49  ? 214 THR C CG2 1 
ATOM   9872  N N   . PRO C  1 215 ? 5.410   15.283  -66.797  1.00 60.41  ? 215 PRO C N   1 
ATOM   9873  C CA  . PRO C  1 215 ? 4.900   16.624  -67.124  1.00 60.40  ? 215 PRO C CA  1 
ATOM   9874  C C   . PRO C  1 215 ? 5.279   17.131  -68.511  1.00 65.36  ? 215 PRO C C   1 
ATOM   9875  O O   . PRO C  1 215 ? 4.643   18.078  -68.989  1.00 66.73  ? 215 PRO C O   1 
ATOM   9876  C CB  . PRO C  1 215 ? 5.509   17.507  -66.027  1.00 59.47  ? 215 PRO C CB  1 
ATOM   9877  C CG  . PRO C  1 215 ? 6.681   16.737  -65.511  1.00 59.39  ? 215 PRO C CG  1 
ATOM   9878  C CD  . PRO C  1 215 ? 6.285   15.299  -65.613  1.00 60.73  ? 215 PRO C CD  1 
ATOM   9879  N N   . ASN C  1 216 ? 6.272   16.550  -69.183  1.00 66.88  ? 216 ASN C N   1 
ATOM   9880  C CA  . ASN C  1 216 ? 6.739   17.092  -70.454  1.00 68.72  ? 216 ASN C CA  1 
ATOM   9881  C C   . ASN C  1 216 ? 6.369   16.229  -71.653  1.00 66.20  ? 216 ASN C C   1 
ATOM   9882  O O   . ASN C  1 216 ? 6.814   16.513  -72.770  1.00 67.66  ? 216 ASN C O   1 
ATOM   9883  C CB  . ASN C  1 216 ? 8.250   17.305  -70.404  1.00 71.80  ? 216 ASN C CB  1 
ATOM   9884  C CG  . ASN C  1 216 ? 8.651   18.293  -69.342  1.00 74.79  ? 216 ASN C CG  1 
ATOM   9885  O OD1 . ASN C  1 216 ? 9.585   18.056  -68.576  1.00 76.22  ? 216 ASN C OD1 1 
ATOM   9886  N ND2 . ASN C  1 216 ? 7.937   19.413  -69.281  1.00 75.72  ? 216 ASN C ND2 1 
ATOM   9887  N N   . VAL C  1 217 ? 5.561   15.191  -71.455  1.00 64.07  ? 217 VAL C N   1 
ATOM   9888  C CA  . VAL C  1 217 ? 5.128   14.370  -72.574  1.00 63.06  ? 217 VAL C CA  1 
ATOM   9889  C C   . VAL C  1 217 ? 4.208   15.190  -73.467  1.00 60.39  ? 217 VAL C C   1 
ATOM   9890  O O   . VAL C  1 217 ? 3.385   15.983  -72.991  1.00 57.75  ? 217 VAL C O   1 
ATOM   9891  C CB  . VAL C  1 217 ? 4.432   13.095  -72.063  1.00 62.59  ? 217 VAL C CB  1 
ATOM   9892  C CG1 . VAL C  1 217 ? 3.246   13.444  -71.176  1.00 62.30  ? 217 VAL C CG1 1 
ATOM   9893  C CG2 . VAL C  1 217 ? 3.994   12.220  -73.209  1.00 59.89  ? 217 VAL C CG2 1 
ATOM   9894  N N   . LYS C  1 218 ? 4.353   15.021  -74.772  1.00 58.44  ? 218 LYS C N   1 
ATOM   9895  C CA  . LYS C  1 218 ? 3.471   15.667  -75.727  1.00 60.39  ? 218 LYS C CA  1 
ATOM   9896  C C   . LYS C  1 218 ? 2.407   14.661  -76.146  1.00 62.10  ? 218 LYS C C   1 
ATOM   9897  O O   . LYS C  1 218 ? 2.732   13.582  -76.651  1.00 68.43  ? 218 LYS C O   1 
ATOM   9898  C CB  . LYS C  1 218 ? 4.271   16.192  -76.919  1.00 62.97  ? 218 LYS C CB  1 
ATOM   9899  C CG  . LYS C  1 218 ? 5.569   16.882  -76.495  1.00 66.07  ? 218 LYS C CG  1 
ATOM   9900  C CD  . LYS C  1 218 ? 6.474   17.196  -77.675  1.00 70.80  ? 218 LYS C CD  1 
ATOM   9901  C CE  . LYS C  1 218 ? 5.859   18.248  -78.584  1.00 75.11  ? 218 LYS C CE  1 
ATOM   9902  N NZ  . LYS C  1 218 ? 6.667   18.479  -79.833  1.00 78.14  ? 218 LYS C NZ  1 
ATOM   9903  N N   . ILE C  1 219 ? 1.148   14.993  -75.895  1.00 59.62  ? 219 ILE C N   1 
ATOM   9904  C CA  . ILE C  1 219 ? 0.019   14.149  -76.279  1.00 58.95  ? 219 ILE C CA  1 
ATOM   9905  C C   . ILE C  1 219 ? -0.854  14.962  -77.224  1.00 62.34  ? 219 ILE C C   1 
ATOM   9906  O O   . ILE C  1 219 ? -0.821  16.204  -77.200  1.00 61.95  ? 219 ILE C O   1 
ATOM   9907  C CB  . ILE C  1 219 ? -0.777  13.659  -75.049  1.00 59.27  ? 219 ILE C CB  1 
ATOM   9908  C CG1 . ILE C  1 219 ? -1.484  14.835  -74.377  1.00 61.45  ? 219 ILE C CG1 1 
ATOM   9909  C CG2 . ILE C  1 219 ? 0.140   12.952  -74.057  1.00 56.78  ? 219 ILE C CG2 1 
ATOM   9910  C CD1 . ILE C  1 219 ? -2.428  14.417  -73.289  1.00 62.21  ? 219 ILE C CD1 1 
ATOM   9911  N N   . PRO C  1 220 ? -1.653  14.294  -78.087  1.00 65.18  ? 220 PRO C N   1 
ATOM   9912  C CA  . PRO C  1 220 ? -2.443  15.045  -79.075  1.00 69.02  ? 220 PRO C CA  1 
ATOM   9913  C C   . PRO C  1 220 ? -3.475  15.953  -78.433  1.00 70.23  ? 220 PRO C C   1 
ATOM   9914  O O   . PRO C  1 220 ? -3.627  15.979  -77.207  1.00 68.74  ? 220 PRO C O   1 
ATOM   9915  C CB  . PRO C  1 220 ? -3.112  13.942  -79.910  1.00 69.86  ? 220 PRO C CB  1 
ATOM   9916  C CG  . PRO C  1 220 ? -3.089  12.738  -79.048  1.00 65.17  ? 220 PRO C CG  1 
ATOM   9917  C CD  . PRO C  1 220 ? -1.820  12.840  -78.256  1.00 64.18  ? 220 PRO C CD  1 
ATOM   9918  N N   . ASP C  1 221 ? -4.189  16.709  -79.257  1.00 74.70  ? 221 ASP C N   1 
ATOM   9919  C CA  . ASP C  1 221 ? -5.195  17.640  -78.766  1.00 72.56  ? 221 ASP C CA  1 
ATOM   9920  C C   . ASP C  1 221 ? -6.503  16.882  -78.588  1.00 62.24  ? 221 ASP C C   1 
ATOM   9921  O O   . ASP C  1 221 ? -7.130  16.471  -79.568  1.00 55.71  ? 221 ASP C O   1 
ATOM   9922  C CB  . ASP C  1 221 ? -5.355  18.816  -79.724  1.00 80.07  ? 221 ASP C CB  1 
ATOM   9923  C CG  . ASP C  1 221 ? -6.221  19.909  -79.149  1.00 86.32  ? 221 ASP C CG  1 
ATOM   9924  O OD1 . ASP C  1 221 ? -6.088  20.182  -77.935  1.00 85.07  ? 221 ASP C OD1 1 
ATOM   9925  O OD2 . ASP C  1 221 ? -7.017  20.503  -79.909  1.00 92.90  ? 221 ASP C OD2 1 
ATOM   9926  N N   . PHE C  1 222 ? -6.907  16.674  -77.338  1.00 58.21  ? 222 PHE C N   1 
ATOM   9927  C CA  . PHE C  1 222 ? -8.171  15.994  -77.076  1.00 55.57  ? 222 PHE C CA  1 
ATOM   9928  C C   . PHE C  1 222 ? -9.283  17.026  -77.225  1.00 62.20  ? 222 PHE C C   1 
ATOM   9929  O O   . PHE C  1 222 ? -9.713  17.664  -76.261  1.00 61.60  ? 222 PHE C O   1 
ATOM   9930  C CB  . PHE C  1 222 ? -8.164  15.342  -75.702  1.00 50.19  ? 222 PHE C CB  1 
ATOM   9931  C CG  . PHE C  1 222 ? -7.445  14.015  -75.661  1.00 48.57  ? 222 PHE C CG  1 
ATOM   9932  C CD1 . PHE C  1 222 ? -6.063  13.966  -75.610  1.00 49.30  ? 222 PHE C CD1 1 
ATOM   9933  C CD2 . PHE C  1 222 ? -8.150  12.828  -75.642  1.00 45.23  ? 222 PHE C CD2 1 
ATOM   9934  C CE1 . PHE C  1 222 ? -5.397  12.767  -75.567  1.00 50.86  ? 222 PHE C CE1 1 
ATOM   9935  C CE2 . PHE C  1 222 ? -7.489  11.622  -75.581  1.00 50.05  ? 222 PHE C CE2 1 
ATOM   9936  C CZ  . PHE C  1 222 ? -6.109  11.588  -75.546  1.00 51.80  ? 222 PHE C CZ  1 
ATOM   9937  N N   . ALA C  1 223 ? -9.749  17.187  -78.468  1.00 65.22  ? 223 ALA C N   1 
ATOM   9938  C CA  . ALA C  1 223 ? -10.793 18.133  -78.843  1.00 68.01  ? 223 ALA C CA  1 
ATOM   9939  C C   . ALA C  1 223 ? -12.207 17.608  -78.615  1.00 69.42  ? 223 ALA C C   1 
ATOM   9940  O O   . ALA C  1 223 ? -13.169 18.318  -78.935  1.00 71.04  ? 223 ALA C O   1 
ATOM   9941  C CB  . ALA C  1 223 ? -10.633 18.523  -80.313  1.00 69.01  ? 223 ALA C CB  1 
ATOM   9942  N N   . VAL C  1 224 ? -12.360 16.387  -78.099  1.00 65.92  ? 224 VAL C N   1 
ATOM   9943  C CA  . VAL C  1 224 ? -13.657 15.798  -77.790  1.00 64.51  ? 224 VAL C CA  1 
ATOM   9944  C C   . VAL C  1 224 ? -13.606 15.302  -76.352  1.00 60.39  ? 224 VAL C C   1 
ATOM   9945  O O   . VAL C  1 224 ? -12.537 15.176  -75.757  1.00 61.04  ? 224 VAL C O   1 
ATOM   9946  C CB  . VAL C  1 224 ? -14.025 14.646  -78.751  1.00 68.53  ? 224 VAL C CB  1 
ATOM   9947  C CG1 . VAL C  1 224 ? -15.530 14.407  -78.772  1.00 70.89  ? 224 VAL C CG1 1 
ATOM   9948  C CG2 . VAL C  1 224 ? -13.527 14.949  -80.150  1.00 70.68  ? 224 VAL C CG2 1 
ATOM   9949  N N   . SER C  1 225 ? -14.781 15.028  -75.792  1.00 55.44  ? 225 SER C N   1 
ATOM   9950  C CA  . SER C  1 225 ? -14.899 14.519  -74.431  1.00 55.03  ? 225 SER C CA  1 
ATOM   9951  C C   . SER C  1 225 ? -15.167 13.021  -74.452  1.00 54.59  ? 225 SER C C   1 
ATOM   9952  O O   . SER C  1 225 ? -16.077 12.557  -75.148  1.00 58.77  ? 225 SER C O   1 
ATOM   9953  C CB  . SER C  1 225 ? -16.016 15.218  -73.666  1.00 53.01  ? 225 SER C CB  1 
ATOM   9954  O OG  . SER C  1 225 ? -16.125 14.653  -72.367  1.00 53.38  ? 225 SER C OG  1 
ATOM   9955  N N   . PHE C  1 226 ? -14.382 12.275  -73.682  1.00 45.38  ? 226 PHE C N   1 
ATOM   9956  C CA  . PHE C  1 226 ? -14.571 10.841  -73.514  1.00 44.46  ? 226 PHE C CA  1 
ATOM   9957  C C   . PHE C  1 226 ? -15.194 10.493  -72.165  1.00 40.10  ? 226 PHE C C   1 
ATOM   9958  O O   . PHE C  1 226 ? -15.267 9.316   -71.815  1.00 39.85  ? 226 PHE C O   1 
ATOM   9959  C CB  . PHE C  1 226 ? -13.234 10.111  -73.679  1.00 45.36  ? 226 PHE C CB  1 
ATOM   9960  C CG  . PHE C  1 226 ? -12.721 10.095  -75.101  1.00 52.71  ? 226 PHE C CG  1 
ATOM   9961  C CD1 . PHE C  1 226 ? -13.163 9.136   -76.004  1.00 55.15  ? 226 PHE C CD1 1 
ATOM   9962  C CD2 . PHE C  1 226 ? -11.805 11.044  -75.535  1.00 55.04  ? 226 PHE C CD2 1 
ATOM   9963  C CE1 . PHE C  1 226 ? -12.695 9.119   -77.321  1.00 57.07  ? 226 PHE C CE1 1 
ATOM   9964  C CE2 . PHE C  1 226 ? -11.334 11.034  -76.847  1.00 58.06  ? 226 PHE C CE2 1 
ATOM   9965  C CZ  . PHE C  1 226 ? -11.781 10.068  -77.738  1.00 57.20  ? 226 PHE C CZ  1 
ATOM   9966  N N   . ARG C  1 227 ? -15.680 11.491  -71.419  1.00 37.35  ? 227 ARG C N   1 
ATOM   9967  C CA  . ARG C  1 227 ? -16.019 11.266  -70.016  1.00 45.24  ? 227 ARG C CA  1 
ATOM   9968  C C   . ARG C  1 227 ? -17.302 10.463  -69.847  1.00 48.05  ? 227 ARG C C   1 
ATOM   9969  O O   . ARG C  1 227 ? -17.404 9.675   -68.903  1.00 50.08  ? 227 ARG C O   1 
ATOM   9970  C CB  . ARG C  1 227 ? -16.103 12.598  -69.275  1.00 50.18  ? 227 ARG C CB  1 
ATOM   9971  C CG  . ARG C  1 227 ? -14.811 13.396  -69.388  1.00 54.62  ? 227 ARG C CG  1 
ATOM   9972  C CD  . ARG C  1 227 ? -14.922 14.755  -68.741  1.00 55.66  ? 227 ARG C CD  1 
ATOM   9973  N NE  . ARG C  1 227 ? -15.667 14.685  -67.493  1.00 57.63  ? 227 ARG C NE  1 
ATOM   9974  C CZ  . ARG C  1 227 ? -15.114 14.539  -66.290  1.00 59.35  ? 227 ARG C CZ  1 
ATOM   9975  N NH1 . ARG C  1 227 ? -13.795 14.445  -66.154  1.00 57.70  ? 227 ARG C NH1 1 
ATOM   9976  N NH2 . ARG C  1 227 ? -15.885 14.483  -65.216  1.00 60.62  ? 227 ARG C NH2 1 
ATOM   9977  N N   . GLU C  1 228 ? -18.273 10.603  -70.754  1.00 46.56  ? 228 GLU C N   1 
ATOM   9978  C CA  . GLU C  1 228 ? -19.433 9.726   -70.670  1.00 48.85  ? 228 GLU C CA  1 
ATOM   9979  C C   . GLU C  1 228 ? -19.093 8.309   -71.134  1.00 50.60  ? 228 GLU C C   1 
ATOM   9980  O O   . GLU C  1 228 ? -19.684 7.339   -70.646  1.00 50.77  ? 228 GLU C O   1 
ATOM   9981  C CB  . GLU C  1 228 ? -20.594 10.316  -71.469  1.00 59.50  ? 228 GLU C CB  1 
ATOM   9982  C CG  . GLU C  1 228 ? -21.905 9.530   -71.381  1.00 71.90  ? 228 GLU C CG  1 
ATOM   9983  C CD  . GLU C  1 228 ? -22.437 9.378   -69.944  1.00 83.07  ? 228 GLU C CD  1 
ATOM   9984  O OE1 . GLU C  1 228 ? -23.013 8.306   -69.647  1.00 87.25  ? 228 GLU C OE1 1 
ATOM   9985  O OE2 . GLU C  1 228 ? -22.284 10.303  -69.113  1.00 85.67  ? 228 GLU C OE2 1 
ATOM   9986  N N   . ASP C  1 229 ? -18.137 8.164   -72.053  1.00 45.15  ? 229 ASP C N   1 
ATOM   9987  C CA  . ASP C  1 229 ? -17.680 6.829   -72.416  1.00 44.20  ? 229 ASP C CA  1 
ATOM   9988  C C   . ASP C  1 229 ? -17.020 6.133   -71.229  1.00 43.72  ? 229 ASP C C   1 
ATOM   9989  O O   . ASP C  1 229 ? -17.148 4.914   -71.072  1.00 44.00  ? 229 ASP C O   1 
ATOM   9990  C CB  . ASP C  1 229 ? -16.712 6.894   -73.591  1.00 41.38  ? 229 ASP C CB  1 
ATOM   9991  C CG  . ASP C  1 229 ? -17.420 6.963   -74.930  1.00 45.25  ? 229 ASP C CG  1 
ATOM   9992  O OD1 . ASP C  1 229 ? -18.647 7.224   -74.970  1.00 38.83  ? 229 ASP C OD1 1 
ATOM   9993  O OD2 . ASP C  1 229 ? -16.733 6.715   -75.942  1.00 47.47  ? 229 ASP C OD2 1 
ATOM   9994  N N   . ALA C  1 230 ? -16.302 6.888   -70.393  1.00 38.72  ? 230 ALA C N   1 
ATOM   9995  C CA  . ALA C  1 230 ? -15.732 6.304   -69.179  1.00 40.74  ? 230 ALA C CA  1 
ATOM   9996  C C   . ALA C  1 230 ? -16.832 5.721   -68.301  1.00 37.42  ? 230 ALA C C   1 
ATOM   9997  O O   . ALA C  1 230 ? -16.735 4.577   -67.841  1.00 31.81  ? 230 ALA C O   1 
ATOM   9998  C CB  . ALA C  1 230 ? -14.914 7.345   -68.416  1.00 36.98  ? 230 ALA C CB  1 
ATOM   9999  N N   . SER C  1 231 ? -17.920 6.475   -68.121  1.00 39.83  ? 231 SER C N   1 
ATOM   10000 C CA  . SER C  1 231 ? -19.074 5.969   -67.385  1.00 40.11  ? 231 SER C CA  1 
ATOM   10001 C C   . SER C  1 231 ? -19.613 4.698   -68.017  1.00 41.26  ? 231 SER C C   1 
ATOM   10002 O O   . SER C  1 231 ? -19.942 3.735   -67.316  1.00 41.51  ? 231 SER C O   1 
ATOM   10003 C CB  . SER C  1 231 ? -20.171 7.029   -67.330  1.00 42.81  ? 231 SER C CB  1 
ATOM   10004 O OG  . SER C  1 231 ? -19.937 7.956   -66.298  1.00 44.89  ? 231 SER C OG  1 
ATOM   10005 N N   . LYS C  1 232 ? -19.710 4.677   -69.351  1.00 42.82  ? 232 LYS C N   1 
ATOM   10006 C CA  . LYS C  1 232 ? -20.336 3.546   -70.022  1.00 41.19  ? 232 LYS C CA  1 
ATOM   10007 C C   . LYS C  1 232 ? -19.533 2.277   -69.828  1.00 36.29  ? 232 LYS C C   1 
ATOM   10008 O O   . LYS C  1 232 ? -20.105 1.198   -69.633  1.00 40.15  ? 232 LYS C O   1 
ATOM   10009 C CB  . LYS C  1 232 ? -20.528 3.852   -71.512  1.00 45.21  ? 232 LYS C CB  1 
ATOM   10010 C CG  . LYS C  1 232 ? -21.570 4.929   -71.800  1.00 55.51  ? 232 LYS C CG  1 
ATOM   10011 C CD  . LYS C  1 232 ? -22.906 4.704   -71.031  1.00 65.67  ? 232 LYS C CD  1 
ATOM   10012 C CE  . LYS C  1 232 ? -22.939 5.444   -69.657  1.00 70.58  ? 232 LYS C CE  1 
ATOM   10013 N NZ  . LYS C  1 232 ? -24.006 5.089   -68.655  1.00 70.38  ? 232 LYS C NZ  1 
ATOM   10014 N N   . HIS C  1 233 ? -18.202 2.380   -69.887  1.00 33.26  ? 233 HIS C N   1 
ATOM   10015 C CA  . HIS C  1 233 ? -17.359 1.212   -69.675  1.00 35.25  ? 233 HIS C CA  1 
ATOM   10016 C C   . HIS C  1 233 ? -17.661 0.577   -68.328  1.00 35.02  ? 233 HIS C C   1 
ATOM   10017 O O   . HIS C  1 233 ? -17.800 -0.645  -68.222  1.00 37.22  ? 233 HIS C O   1 
ATOM   10018 C CB  . HIS C  1 233 ? -15.886 1.611   -69.760  1.00 38.98  ? 233 HIS C CB  1 
ATOM   10019 C CG  . HIS C  1 233 ? -15.384 1.816   -71.159  1.00 43.62  ? 233 HIS C CG  1 
ATOM   10020 N ND1 . HIS C  1 233 ? -15.075 0.768   -71.996  1.00 42.32  ? 233 HIS C ND1 1 
ATOM   10021 C CD2 . HIS C  1 233 ? -15.107 2.945   -71.853  1.00 43.09  ? 233 HIS C CD2 1 
ATOM   10022 C CE1 . HIS C  1 233 ? -14.640 1.241   -73.149  1.00 45.17  ? 233 HIS C CE1 1 
ATOM   10023 N NE2 . HIS C  1 233 ? -14.645 2.559   -73.087  1.00 43.61  ? 233 HIS C NE2 1 
ATOM   10024 N N   . VAL C  1 234 ? -17.800 1.401   -67.291  1.00 38.39  ? 234 VAL C N   1 
ATOM   10025 C CA  . VAL C  1 234 ? -18.095 0.889   -65.958  1.00 38.55  ? 234 VAL C CA  1 
ATOM   10026 C C   . VAL C  1 234 ? -19.540 0.414   -65.876  1.00 41.53  ? 234 VAL C C   1 
ATOM   10027 O O   . VAL C  1 234 ? -19.839 -0.631  -65.280  1.00 37.16  ? 234 VAL C O   1 
ATOM   10028 C CB  . VAL C  1 234 ? -17.783 1.978   -64.916  1.00 38.86  ? 234 VAL C CB  1 
ATOM   10029 C CG1 . VAL C  1 234 ? -17.931 1.444   -63.490  1.00 31.05  ? 234 VAL C CG1 1 
ATOM   10030 C CG2 . VAL C  1 234 ? -16.371 2.501   -65.156  1.00 41.85  ? 234 VAL C CG2 1 
ATOM   10031 N N   . GLU C  1 235 ? -20.456 1.163   -66.487  1.00 46.16  ? 235 GLU C N   1 
ATOM   10032 C CA  . GLU C  1 235 ? -21.873 0.844   -66.374  1.00 54.52  ? 235 GLU C CA  1 
ATOM   10033 C C   . GLU C  1 235 ? -22.206 -0.451  -67.103  1.00 53.42  ? 235 GLU C C   1 
ATOM   10034 O O   . GLU C  1 235 ? -22.912 -1.315  -66.566  1.00 53.55  ? 235 GLU C O   1 
ATOM   10035 C CB  . GLU C  1 235 ? -22.712 1.998   -66.918  1.00 60.08  ? 235 GLU C CB  1 
ATOM   10036 C CG  . GLU C  1 235 ? -24.155 1.968   -66.466  1.00 70.58  ? 235 GLU C CG  1 
ATOM   10037 C CD  . GLU C  1 235 ? -24.298 2.065   -64.960  1.00 76.45  ? 235 GLU C CD  1 
ATOM   10038 O OE1 . GLU C  1 235 ? -24.310 3.201   -64.430  1.00 80.65  ? 235 GLU C OE1 1 
ATOM   10039 O OE2 . GLU C  1 235 ? -24.404 1.004   -64.309  1.00 75.48  ? 235 GLU C OE2 1 
ATOM   10040 N N   . LEU C  1 236 ? -21.722 -0.597  -68.339  1.00 47.47  ? 236 LEU C N   1 
ATOM   10041 C CA  . LEU C  1 236 ? -21.971 -1.830  -69.073  1.00 45.97  ? 236 LEU C CA  1 
ATOM   10042 C C   . LEU C  1 236 ? -21.291 -3.013  -68.397  1.00 45.33  ? 236 LEU C C   1 
ATOM   10043 O O   . LEU C  1 236 ? -21.862 -4.106  -68.329  1.00 47.11  ? 236 LEU C O   1 
ATOM   10044 C CB  . LEU C  1 236 ? -21.503 -1.683  -70.517  1.00 41.96  ? 236 LEU C CB  1 
ATOM   10045 C CG  . LEU C  1 236 ? -22.243 -0.610  -71.303  1.00 43.38  ? 236 LEU C CG  1 
ATOM   10046 C CD1 . LEU C  1 236 ? -21.676 -0.498  -72.706  1.00 45.11  ? 236 LEU C CD1 1 
ATOM   10047 C CD2 . LEU C  1 236 ? -23.747 -0.895  -71.338  1.00 43.13  ? 236 LEU C CD2 1 
ATOM   10048 N N   . ALA C  1 237 ? -20.073 -2.812  -67.881  1.00 43.40  ? 237 ALA C N   1 
ATOM   10049 C CA  . ALA C  1 237 ? -19.417 -3.865  -67.110  1.00 44.57  ? 237 ALA C CA  1 
ATOM   10050 C C   . ALA C  1 237 ? -20.292 -4.326  -65.953  1.00 43.14  ? 237 ALA C C   1 
ATOM   10051 O O   . ALA C  1 237 ? -20.468 -5.532  -65.740  1.00 47.96  ? 237 ALA C O   1 
ATOM   10052 C CB  . ALA C  1 237 ? -18.065 -3.377  -66.592  1.00 43.14  ? 237 ALA C CB  1 
ATOM   10053 N N   . LYS C  1 238 ? -20.861 -3.376  -65.208  1.00 42.93  ? 238 LYS C N   1 
ATOM   10054 C CA  . LYS C  1 238 ? -21.747 -3.711  -64.097  1.00 46.85  ? 238 LYS C CA  1 
ATOM   10055 C C   . LYS C  1 238 ? -22.938 -4.550  -64.555  1.00 52.09  ? 238 LYS C C   1 
ATOM   10056 O O   . LYS C  1 238 ? -23.330 -5.508  -63.878  1.00 53.75  ? 238 LYS C O   1 
ATOM   10057 C CB  . LYS C  1 238 ? -22.232 -2.430  -63.421  1.00 43.69  ? 238 LYS C CB  1 
ATOM   10058 C CG  . LYS C  1 238 ? -21.190 -1.734  -62.544  1.00 41.20  ? 238 LYS C CG  1 
ATOM   10059 C CD  . LYS C  1 238 ? -21.761 -0.443  -61.943  1.00 41.48  ? 238 LYS C CD  1 
ATOM   10060 C CE  . LYS C  1 238 ? -23.034 -0.707  -61.156  1.00 40.40  ? 238 LYS C CE  1 
ATOM   10061 N NZ  . LYS C  1 238 ? -23.795 0.550   -60.920  1.00 43.09  ? 238 LYS C NZ  1 
ATOM   10062 N N   . GLU C  1 239 ? -23.541 -4.196  -65.689  1.00 53.76  ? 239 GLU C N   1 
ATOM   10063 C CA  . GLU C  1 239 ? -24.711 -4.939  -66.152  1.00 62.02  ? 239 GLU C CA  1 
ATOM   10064 C C   . GLU C  1 239 ? -24.327 -6.354  -66.572  1.00 62.06  ? 239 GLU C C   1 
ATOM   10065 O O   . GLU C  1 239 ? -25.007 -7.325  -66.216  1.00 63.81  ? 239 GLU C O   1 
ATOM   10066 C CB  . GLU C  1 239 ? -25.389 -4.192  -67.305  1.00 66.13  ? 239 GLU C CB  1 
ATOM   10067 C CG  . GLU C  1 239 ? -26.886 -3.937  -67.105  1.00 74.37  ? 239 GLU C CG  1 
ATOM   10068 C CD  . GLU C  1 239 ? -27.747 -5.175  -67.348  1.00 82.49  ? 239 GLU C CD  1 
ATOM   10069 O OE1 . GLU C  1 239 ? -28.971 -5.114  -67.090  1.00 87.14  ? 239 GLU C OE1 1 
ATOM   10070 O OE2 . GLU C  1 239 ? -27.204 -6.208  -67.798  1.00 84.90  ? 239 GLU C OE2 1 
ATOM   10071 N N   . LYS C  1 240 ? -23.232 -6.484  -67.324  1.00 59.52  ? 240 LYS C N   1 
ATOM   10072 C CA  . LYS C  1 240 ? -22.770 -7.795  -67.769  1.00 58.69  ? 240 LYS C CA  1 
ATOM   10073 C C   . LYS C  1 240 ? -22.421 -8.689  -66.586  1.00 58.99  ? 240 LYS C C   1 
ATOM   10074 O O   . LYS C  1 240 ? -22.744 -9.882  -66.587  1.00 62.23  ? 240 LYS C O   1 
ATOM   10075 C CB  . LYS C  1 240 ? -21.568 -7.626  -68.702  1.00 53.84  ? 240 LYS C CB  1 
ATOM   10076 C CG  . LYS C  1 240 ? -20.964 -8.923  -69.217  1.00 53.13  ? 240 LYS C CG  1 
ATOM   10077 C CD  . LYS C  1 240 ? -21.271 -9.119  -70.700  1.00 52.61  ? 240 LYS C CD  1 
ATOM   10078 C CE  . LYS C  1 240 ? -21.173 -10.584 -71.095  1.00 49.31  ? 240 LYS C CE  1 
ATOM   10079 N NZ  . LYS C  1 240 ? -21.893 -10.870 -72.376  1.00 47.46  ? 240 LYS C NZ  1 
ATOM   10080 N N   . TYR C  1 241 ? -21.781 -8.123  -65.557  1.00 57.15  ? 241 TYR C N   1 
ATOM   10081 C CA  . TYR C  1 241 ? -21.416 -8.915  -64.385  1.00 58.87  ? 241 TYR C CA  1 
ATOM   10082 C C   . TYR C  1 241 ? -22.649 -9.484  -63.691  1.00 62.54  ? 241 TYR C C   1 
ATOM   10083 O O   . TYR C  1 241 ? -22.669 -10.663 -63.319  1.00 63.95  ? 241 TYR C O   1 
ATOM   10084 C CB  . TYR C  1 241 ? -20.593 -8.069  -63.409  1.00 57.69  ? 241 TYR C CB  1 
ATOM   10085 C CG  . TYR C  1 241 ? -20.106 -8.837  -62.196  1.00 55.28  ? 241 TYR C CG  1 
ATOM   10086 C CD1 . TYR C  1 241 ? -20.930 -9.026  -61.093  1.00 54.32  ? 241 TYR C CD1 1 
ATOM   10087 C CD2 . TYR C  1 241 ? -18.824 -9.377  -62.156  1.00 53.69  ? 241 TYR C CD2 1 
ATOM   10088 C CE1 . TYR C  1 241 ? -20.500 -9.730  -59.989  1.00 54.75  ? 241 TYR C CE1 1 
ATOM   10089 C CE2 . TYR C  1 241 ? -18.382 -10.087 -61.049  1.00 51.93  ? 241 TYR C CE2 1 
ATOM   10090 C CZ  . TYR C  1 241 ? -19.228 -10.259 -59.970  1.00 53.77  ? 241 TYR C CZ  1 
ATOM   10091 O OH  . TYR C  1 241 ? -18.807 -10.958 -58.866  1.00 55.92  ? 241 TYR C OH  1 
ATOM   10092 N N   . PHE C  1 242 ? -23.682 -8.656  -63.499  1.00 64.61  ? 242 PHE C N   1 
ATOM   10093 C CA  . PHE C  1 242 ? -24.914 -9.130  -62.871  1.00 67.32  ? 242 PHE C CA  1 
ATOM   10094 C C   . PHE C  1 242 ? -25.555 -10.260 -63.672  1.00 68.17  ? 242 PHE C C   1 
ATOM   10095 O O   . PHE C  1 242 ? -26.042 -11.239 -63.094  1.00 68.09  ? 242 PHE C O   1 
ATOM   10096 C CB  . PHE C  1 242 ? -25.900 -7.973  -62.710  1.00 66.84  ? 242 PHE C CB  1 
ATOM   10097 C CG  . PHE C  1 242 ? -27.177 -8.366  -62.037  1.00 70.42  ? 242 PHE C CG  1 
ATOM   10098 C CD1 . PHE C  1 242 ? -27.255 -8.416  -60.655  1.00 71.74  ? 242 PHE C CD1 1 
ATOM   10099 C CD2 . PHE C  1 242 ? -28.299 -8.696  -62.781  1.00 72.93  ? 242 PHE C CD2 1 
ATOM   10100 C CE1 . PHE C  1 242 ? -28.429 -8.784  -60.027  1.00 74.28  ? 242 PHE C CE1 1 
ATOM   10101 C CE2 . PHE C  1 242 ? -29.474 -9.067  -62.159  1.00 75.93  ? 242 PHE C CE2 1 
ATOM   10102 C CZ  . PHE C  1 242 ? -29.539 -9.112  -60.780  1.00 76.36  ? 242 PHE C CZ  1 
ATOM   10103 N N   . GLU C  1 243 ? -25.581 -10.130 -65.003  1.00 69.14  ? 243 GLU C N   1 
ATOM   10104 C CA  . GLU C  1 243 ? -26.142 -11.181 -65.848  1.00 74.02  ? 243 GLU C CA  1 
ATOM   10105 C C   . GLU C  1 243 ? -25.405 -12.500 -65.649  1.00 73.90  ? 243 GLU C C   1 
ATOM   10106 O O   . GLU C  1 243 ? -26.032 -13.563 -65.544  1.00 77.59  ? 243 GLU C O   1 
ATOM   10107 C CB  . GLU C  1 243 ? -26.087 -10.758 -67.316  1.00 76.83  ? 243 GLU C CB  1 
ATOM   10108 C CG  . GLU C  1 243 ? -26.308 -11.892 -68.307  1.00 82.68  ? 243 GLU C CG  1 
ATOM   10109 C CD  . GLU C  1 243 ? -25.428 -11.768 -69.539  1.00 85.52  ? 243 GLU C CD  1 
ATOM   10110 O OE1 . GLU C  1 243 ? -24.984 -12.813 -70.065  1.00 87.17  ? 243 GLU C OE1 1 
ATOM   10111 O OE2 . GLU C  1 243 ? -25.175 -10.626 -69.977  1.00 85.84  ? 243 GLU C OE2 1 
ATOM   10112 N N   . ILE C  1 244 ? -24.074 -12.450 -65.582  1.00 67.17  ? 244 ILE C N   1 
ATOM   10113 C CA  . ILE C  1 244 ? -23.297 -13.674 -65.436  1.00 61.70  ? 244 ILE C CA  1 
ATOM   10114 C C   . ILE C  1 244 ? -23.375 -14.210 -64.012  1.00 61.30  ? 244 ILE C C   1 
ATOM   10115 O O   . ILE C  1 244 ? -23.435 -15.426 -63.807  1.00 63.19  ? 244 ILE C O   1 
ATOM   10116 C CB  . ILE C  1 244 ? -21.837 -13.437 -65.865  1.00 55.85  ? 244 ILE C CB  1 
ATOM   10117 C CG1 . ILE C  1 244 ? -21.779 -12.835 -67.271  1.00 54.59  ? 244 ILE C CG1 1 
ATOM   10118 C CG2 . ILE C  1 244 ? -21.044 -14.738 -65.813  1.00 54.02  ? 244 ILE C CG2 1 
ATOM   10119 C CD1 . ILE C  1 244 ? -22.279 -13.768 -68.374  1.00 54.12  ? 244 ILE C CD1 1 
ATOM   10120 N N   . PHE C  1 245 ? -23.390 -13.325 -63.005  1.00 59.66  ? 245 PHE C N   1 
ATOM   10121 C CA  . PHE C  1 245 ? -23.104 -13.736 -61.636  1.00 60.73  ? 245 PHE C CA  1 
ATOM   10122 C C   . PHE C  1 245 ? -24.197 -13.451 -60.612  1.00 68.93  ? 245 PHE C C   1 
ATOM   10123 O O   . PHE C  1 245 ? -24.174 -14.063 -59.540  1.00 72.66  ? 245 PHE C O   1 
ATOM   10124 C CB  . PHE C  1 245 ? -21.803 -13.084 -61.143  1.00 55.33  ? 245 PHE C CB  1 
ATOM   10125 C CG  . PHE C  1 245 ? -20.575 -13.583 -61.847  1.00 53.58  ? 245 PHE C CG  1 
ATOM   10126 C CD1 . PHE C  1 245 ? -20.130 -14.885 -61.657  1.00 53.24  ? 245 PHE C CD1 1 
ATOM   10127 C CD2 . PHE C  1 245 ? -19.864 -12.752 -62.702  1.00 50.66  ? 245 PHE C CD2 1 
ATOM   10128 C CE1 . PHE C  1 245 ? -19.004 -15.351 -62.307  1.00 52.33  ? 245 PHE C CE1 1 
ATOM   10129 C CE2 . PHE C  1 245 ? -18.732 -13.212 -63.355  1.00 48.10  ? 245 PHE C CE2 1 
ATOM   10130 C CZ  . PHE C  1 245 ? -18.301 -14.512 -63.158  1.00 49.68  ? 245 PHE C CZ  1 
ATOM   10131 N N   . GLY C  1 246 ? -25.133 -12.551 -60.882  1.00 74.08  ? 246 GLY C N   1 
ATOM   10132 C CA  . GLY C  1 246 ? -26.229 -12.377 -59.948  1.00 79.32  ? 246 GLY C CA  1 
ATOM   10133 C C   . GLY C  1 246 ? -25.973 -11.455 -58.778  1.00 80.12  ? 246 GLY C C   1 
ATOM   10134 O O   . GLY C  1 246 ? -26.622 -11.593 -57.737  1.00 85.18  ? 246 GLY C O   1 
ATOM   10135 N N   . GLU C  1 247 ? -25.019 -10.540 -58.901  1.00 75.23  ? 247 GLU C N   1 
ATOM   10136 C CA  . GLU C  1 247 ? -24.928 -9.396  -58.010  1.00 73.64  ? 247 GLU C CA  1 
ATOM   10137 C C   . GLU C  1 247 ? -24.352 -8.245  -58.812  1.00 72.22  ? 247 GLU C C   1 
ATOM   10138 O O   . GLU C  1 247 ? -23.712 -8.445  -59.847  1.00 71.26  ? 247 GLU C O   1 
ATOM   10139 C CB  . GLU C  1 247 ? -24.050 -9.657  -56.775  1.00 75.11  ? 247 GLU C CB  1 
ATOM   10140 C CG  . GLU C  1 247 ? -23.963 -11.095 -56.287  1.00 79.41  ? 247 GLU C CG  1 
ATOM   10141 C CD  . GLU C  1 247 ? -22.859 -11.295 -55.269  1.00 81.90  ? 247 GLU C CD  1 
ATOM   10142 O OE1 . GLU C  1 247 ? -22.552 -10.333 -54.532  1.00 82.16  ? 247 GLU C OE1 1 
ATOM   10143 O OE2 . GLU C  1 247 ? -22.300 -12.411 -55.201  1.00 83.01  ? 247 GLU C OE2 1 
ATOM   10144 N N   . HIS C  1 248 ? -24.585 -7.046  -58.341  1.00 71.24  ? 248 HIS C N   1 
ATOM   10145 C CA  . HIS C  1 248 ? -23.830 -5.947  -58.914  1.00 68.72  ? 248 HIS C CA  1 
ATOM   10146 C C   . HIS C  1 248 ? -22.426 -5.968  -58.318  1.00 63.22  ? 248 HIS C C   1 
ATOM   10147 O O   . HIS C  1 248 ? -22.283 -6.045  -57.093  1.00 61.91  ? 248 HIS C O   1 
ATOM   10148 C CB  . HIS C  1 248 ? -24.532 -4.611  -58.656  1.00 72.53  ? 248 HIS C CB  1 
ATOM   10149 C CG  . HIS C  1 248 ? -25.392 -4.150  -59.796  1.00 74.29  ? 248 HIS C CG  1 
ATOM   10150 N ND1 . HIS C  1 248 ? -26.444 -3.275  -59.631  1.00 76.79  ? 248 HIS C ND1 1 
ATOM   10151 C CD2 . HIS C  1 248 ? -25.352 -4.443  -61.118  1.00 74.63  ? 248 HIS C CD2 1 
ATOM   10152 C CE1 . HIS C  1 248 ? -27.015 -3.048  -60.802  1.00 77.80  ? 248 HIS C CE1 1 
ATOM   10153 N NE2 . HIS C  1 248 ? -26.371 -3.744  -61.721  1.00 76.51  ? 248 HIS C NE2 1 
ATOM   10154 N N   . PRO C  1 249 ? -21.375 -5.948  -59.142  1.00 57.84  ? 249 PRO C N   1 
ATOM   10155 C CA  . PRO C  1 249 ? -20.016 -6.109  -58.604  1.00 53.10  ? 249 PRO C CA  1 
ATOM   10156 C C   . PRO C  1 249 ? -19.635 -4.923  -57.733  1.00 51.66  ? 249 PRO C C   1 
ATOM   10157 O O   . PRO C  1 249 ? -19.821 -3.765  -58.116  1.00 55.01  ? 249 PRO C O   1 
ATOM   10158 C CB  . PRO C  1 249 ? -19.140 -6.196  -59.859  1.00 50.43  ? 249 PRO C CB  1 
ATOM   10159 C CG  . PRO C  1 249 ? -19.908 -5.443  -60.897  1.00 51.63  ? 249 PRO C CG  1 
ATOM   10160 C CD  . PRO C  1 249 ? -21.372 -5.667  -60.589  1.00 55.89  ? 249 PRO C CD  1 
ATOM   10161 N N   . VAL C  1 250 ? -19.120 -5.223  -56.542  1.00 47.11  ? 250 VAL C N   1 
ATOM   10162 C CA  . VAL C  1 250 ? -18.692 -4.176  -55.619  1.00 46.77  ? 250 VAL C CA  1 
ATOM   10163 C C   . VAL C  1 250 ? -17.178 -3.991  -55.611  1.00 43.15  ? 250 VAL C C   1 
ATOM   10164 O O   . VAL C  1 250 ? -16.683 -3.056  -54.962  1.00 41.70  ? 250 VAL C O   1 
ATOM   10165 C CB  . VAL C  1 250 ? -19.212 -4.447  -54.189  1.00 50.52  ? 250 VAL C CB  1 
ATOM   10166 C CG1 . VAL C  1 250 ? -20.692 -4.814  -54.231  1.00 53.15  ? 250 VAL C CG1 1 
ATOM   10167 C CG2 . VAL C  1 250 ? -18.404 -5.550  -53.522  1.00 48.30  ? 250 VAL C CG2 1 
ATOM   10168 N N   . TYR C  1 251 ? -16.430 -4.845  -56.308  1.00 41.00  ? 251 TYR C N   1 
ATOM   10169 C CA  . TYR C  1 251 ? -15.009 -4.636  -56.514  1.00 41.51  ? 251 TYR C CA  1 
ATOM   10170 C C   . TYR C  1 251 ? -14.684 -4.741  -57.998  1.00 42.72  ? 251 TYR C C   1 
ATOM   10171 O O   . TYR C  1 251 ? -15.361 -5.444  -58.755  1.00 38.42  ? 251 TYR C O   1 
ATOM   10172 C CB  . TYR C  1 251 ? -14.160 -5.627  -55.708  1.00 46.02  ? 251 TYR C CB  1 
ATOM   10173 C CG  . TYR C  1 251 ? -14.860 -6.919  -55.389  1.00 50.54  ? 251 TYR C CG  1 
ATOM   10174 C CD1 . TYR C  1 251 ? -14.974 -7.915  -56.346  1.00 53.26  ? 251 TYR C CD1 1 
ATOM   10175 C CD2 . TYR C  1 251 ? -15.390 -7.151  -54.126  1.00 53.26  ? 251 TYR C CD2 1 
ATOM   10176 C CE1 . TYR C  1 251 ? -15.610 -9.104  -56.057  1.00 59.11  ? 251 TYR C CE1 1 
ATOM   10177 C CE2 . TYR C  1 251 ? -16.028 -8.332  -53.823  1.00 57.74  ? 251 TYR C CE2 1 
ATOM   10178 C CZ  . TYR C  1 251 ? -16.136 -9.307  -54.789  1.00 62.27  ? 251 TYR C CZ  1 
ATOM   10179 O OH  . TYR C  1 251 ? -16.775 -10.484 -54.476  1.00 67.41  ? 251 TYR C OH  1 
ATOM   10180 N N   . MET C  1 252 ? -13.647 -4.017  -58.409  1.00 36.96  ? 252 MET C N   1 
ATOM   10181 C CA  . MET C  1 252 ? -13.253 -3.958  -59.806  1.00 36.98  ? 252 MET C CA  1 
ATOM   10182 C C   . MET C  1 252 ? -11.741 -3.872  -59.884  1.00 37.18  ? 252 MET C C   1 
ATOM   10183 O O   . MET C  1 252 ? -11.087 -3.318  -58.994  1.00 30.85  ? 252 MET C O   1 
ATOM   10184 C CB  . MET C  1 252 ? -13.899 -2.763  -60.539  1.00 32.65  ? 252 MET C CB  1 
ATOM   10185 C CG  . MET C  1 252 ? -15.304 -3.030  -61.048  1.00 32.82  ? 252 MET C CG  1 
ATOM   10186 S SD  . MET C  1 252 ? -15.806 -1.841  -62.328  1.00 42.33  ? 252 MET C SD  1 
ATOM   10187 C CE  . MET C  1 252 ? -17.510 -2.326  -62.588  1.00 42.36  ? 252 MET C CE  1 
ATOM   10188 N N   . TRP C  1 253 ? -11.188 -4.457  -60.946  1.00 27.35  ? 253 TRP C N   1 
ATOM   10189 C CA  . TRP C  1 253 ? -9.775  -4.283  -61.227  1.00 30.04  ? 253 TRP C CA  1 
ATOM   10190 C C   . TRP C  1 253 ? -9.631  -3.169  -62.244  1.00 33.65  ? 253 TRP C C   1 
ATOM   10191 O O   . TRP C  1 253 ? -10.080 -3.333  -63.390  1.00 35.53  ? 253 TRP C O   1 
ATOM   10192 C CB  . TRP C  1 253 ? -9.143  -5.567  -61.763  1.00 26.78  ? 253 TRP C CB  1 
ATOM   10193 C CG  . TRP C  1 253 ? -7.776  -5.304  -62.345  1.00 26.97  ? 253 TRP C CG  1 
ATOM   10194 C CD1 . TRP C  1 253 ? -7.402  -5.383  -63.661  1.00 27.18  ? 253 TRP C CD1 1 
ATOM   10195 C CD2 . TRP C  1 253 ? -6.611  -4.917  -61.619  1.00 25.11  ? 253 TRP C CD2 1 
ATOM   10196 N NE1 . TRP C  1 253 ? -6.066  -5.063  -63.792  1.00 25.79  ? 253 TRP C NE1 1 
ATOM   10197 C CE2 . TRP C  1 253 ? -5.562  -4.771  -62.549  1.00 25.48  ? 253 TRP C CE2 1 
ATOM   10198 C CE3 . TRP C  1 253 ? -6.353  -4.677  -60.266  1.00 27.66  ? 253 TRP C CE3 1 
ATOM   10199 C CZ2 . TRP C  1 253 ? -4.280  -4.401  -62.168  1.00 21.61  ? 253 TRP C CZ2 1 
ATOM   10200 C CZ3 . TRP C  1 253 ? -5.084  -4.320  -59.886  1.00 25.37  ? 253 TRP C CZ3 1 
ATOM   10201 C CH2 . TRP C  1 253 ? -4.061  -4.188  -60.826  1.00 26.01  ? 253 TRP C CH2 1 
ATOM   10202 N N   . PRO C  1 254 ? -9.023  -2.042  -61.897  1.00 35.78  ? 254 PRO C N   1 
ATOM   10203 C CA  . PRO C  1 254 ? -8.805  -0.984  -62.889  1.00 33.97  ? 254 PRO C CA  1 
ATOM   10204 C C   . PRO C  1 254 ? -7.768  -1.414  -63.909  1.00 28.64  ? 254 PRO C C   1 
ATOM   10205 O O   . PRO C  1 254 ? -6.642  -1.784  -63.536  1.00 24.38  ? 254 PRO C O   1 
ATOM   10206 C CB  . PRO C  1 254 ? -8.301  0.201   -62.051  1.00 28.68  ? 254 PRO C CB  1 
ATOM   10207 C CG  . PRO C  1 254 ? -7.717  -0.439  -60.829  1.00 35.50  ? 254 PRO C CG  1 
ATOM   10208 C CD  . PRO C  1 254 ? -8.527  -1.671  -60.559  1.00 36.08  ? 254 PRO C CD  1 
ATOM   10209 N N   . PRO C  1 255 ? -8.101  -1.351  -65.199  1.00 29.82  ? 255 PRO C N   1 
ATOM   10210 C CA  . PRO C  1 255 ? -7.170  -1.821  -66.234  1.00 27.91  ? 255 PRO C CA  1 
ATOM   10211 C C   . PRO C  1 255 ? -5.810  -1.172  -66.070  1.00 24.81  ? 255 PRO C C   1 
ATOM   10212 O O   . PRO C  1 255 ? -5.703  0.032   -65.854  1.00 28.67  ? 255 PRO C O   1 
ATOM   10213 C CB  . PRO C  1 255 ? -7.847  -1.401  -67.548  1.00 27.20  ? 255 PRO C CB  1 
ATOM   10214 C CG  . PRO C  1 255 ? -9.303  -1.347  -67.210  1.00 33.52  ? 255 PRO C CG  1 
ATOM   10215 C CD  . PRO C  1 255 ? -9.362  -0.844  -65.771  1.00 29.05  ? 255 PRO C CD  1 
ATOM   10216 N N   . GLU C  1 256 ? -4.778  -1.916  -66.146  1.00 29.15  ? 256 GLU C N   1 
ATOM   10217 C CA  . GLU C  1 256 ? -3.442  -1.401  -65.994  1.00 32.24  ? 256 GLU C CA  1 
ATOM   10218 C C   . GLU C  1 256 ? -3.223  -0.842  -64.576  1.00 31.77  ? 256 GLU C C   1 
ATOM   10219 O O   . GLU C  1 256 ? -2.307  -0.095  -64.382  1.00 33.54  ? 256 GLU C O   1 
ATOM   10220 C CB  . GLU C  1 256 ? -3.094  -0.432  -67.131  1.00 32.08  ? 256 GLU C CB  1 
ATOM   10221 C CG  . GLU C  1 256 ? -3.280  -0.976  -68.521  1.00 30.68  ? 256 GLU C CG  1 
ATOM   10222 C CD  . GLU C  1 256 ? -2.514  -2.251  -68.753  1.00 33.66  ? 256 GLU C CD  1 
ATOM   10223 O OE1 . GLU C  1 256 ? -1.521  -2.504  -68.068  1.00 32.85  ? 256 GLU C OE1 1 
ATOM   10224 O OE2 . GLU C  1 256 ? -2.904  -2.995  -69.639  1.00 32.84  ? 256 GLU C OE2 1 
ATOM   10225 N N   . ALA C  1 257 ? -3.967  -1.349  -63.608  1.00 30.50  ? 257 ALA C N   1 
ATOM   10226 C CA  . ALA C  1 257 ? -3.931  -0.784  -62.252  1.00 26.13  ? 257 ALA C CA  1 
ATOM   10227 C C   . ALA C  1 257 ? -4.053  0.732   -62.293  1.00 29.00  ? 257 ALA C C   1 
ATOM   10228 O O   . ALA C  1 257 ? -3.599  1.420   -61.382  1.00 30.12  ? 257 ALA C O   1 
ATOM   10229 C CB  . ALA C  1 257 ? -2.650  -1.185  -61.510  1.00 22.91  ? 257 ALA C CB  1 
ATOM   10230 N N   A SER C  1 258 ? -4.645  1.270   -63.361  0.28 31.75  ? 258 SER C N   1 
ATOM   10231 N N   B SER C  1 258 ? -4.656  1.262   -63.356  0.72 31.82  ? 258 SER C N   1 
ATOM   10232 C CA  A SER C  1 258 ? -4.621  2.706   -63.603  0.28 33.13  ? 258 SER C CA  1 
ATOM   10233 C CA  B SER C  1 258 ? -4.643  2.696   -63.593  0.72 33.69  ? 258 SER C CA  1 
ATOM   10234 C C   A SER C  1 258 ? -5.684  3.405   -62.770  0.28 31.59  ? 258 SER C C   1 
ATOM   10235 C C   B SER C  1 258 ? -5.690  3.390   -62.743  0.72 31.34  ? 258 SER C C   1 
ATOM   10236 O O   A SER C  1 258 ? -6.867  3.061   -62.838  0.28 32.43  ? 258 SER C O   1 
ATOM   10237 O O   B SER C  1 258 ? -6.873  3.045   -62.791  0.72 32.92  ? 258 SER C O   1 
ATOM   10238 C CB  A SER C  1 258 ? -4.827  3.013   -65.090  0.28 35.51  ? 258 SER C CB  1 
ATOM   10239 C CB  B SER C  1 258 ? -4.891  3.008   -65.067  0.72 35.48  ? 258 SER C CB  1 
ATOM   10240 O OG  A SER C  1 258 ? -6.169  2.804   -65.491  0.28 39.57  ? 258 SER C OG  1 
ATOM   10241 O OG  B SER C  1 258 ? -4.677  4.382   -65.286  0.72 36.06  ? 258 SER C OG  1 
ATOM   10242 N N   . VAL C  1 259 ? -5.255  4.392   -61.986  1.00 27.88  ? 259 VAL C N   1 
ATOM   10243 C CA  . VAL C  1 259 ? -6.144  5.169   -61.139  1.00 32.32  ? 259 VAL C CA  1 
ATOM   10244 C C   . VAL C  1 259 ? -5.775  6.632   -61.279  1.00 32.86  ? 259 VAL C C   1 
ATOM   10245 O O   . VAL C  1 259 ? -4.674  6.985   -61.706  1.00 41.71  ? 259 VAL C O   1 
ATOM   10246 C CB  . VAL C  1 259 ? -6.071  4.745   -59.649  1.00 30.73  ? 259 VAL C CB  1 
ATOM   10247 C CG1 . VAL C  1 259 ? -6.651  3.348   -59.459  1.00 33.71  ? 259 VAL C CG1 1 
ATOM   10248 C CG2 . VAL C  1 259 ? -4.633  4.820   -59.127  1.00 30.65  ? 259 VAL C CG2 1 
ATOM   10249 N N   . SER C  1 260 ? -6.733  7.483   -60.942  1.00 33.43  ? 260 SER C N   1 
ATOM   10250 C CA  . SER C  1 260 ? -6.508  8.901   -60.714  1.00 32.73  ? 260 SER C CA  1 
ATOM   10251 C C   . SER C  1 260 ? -7.554  9.332   -59.700  1.00 31.57  ? 260 SER C C   1 
ATOM   10252 O O   . SER C  1 260 ? -8.430  8.547   -59.334  1.00 29.66  ? 260 SER C O   1 
ATOM   10253 C CB  . SER C  1 260 ? -6.609  9.710   -62.011  1.00 26.98  ? 260 SER C CB  1 
ATOM   10254 O OG  . SER C  1 260 ? -7.918  9.609   -62.541  1.00 28.14  ? 260 SER C OG  1 
ATOM   10255 N N   . ASN C  1 261 ? -7.466  10.587  -59.247  1.00 30.11  ? 261 ASN C N   1 
ATOM   10256 C CA  . ASN C  1 261 ? -8.479  11.094  -58.325  1.00 35.24  ? 261 ASN C CA  1 
ATOM   10257 C C   . ASN C  1 261 ? -9.859  11.062  -58.979  1.00 34.78  ? 261 ASN C C   1 
ATOM   10258 O O   . ASN C  1 261 ? -10.847 10.645  -58.356  1.00 31.45  ? 261 ASN C O   1 
ATOM   10259 C CB  . ASN C  1 261 ? -8.136  12.518  -57.865  1.00 34.13  ? 261 ASN C CB  1 
ATOM   10260 C CG  . ASN C  1 261 ? -6.889  12.583  -56.983  1.00 37.68  ? 261 ASN C CG  1 
ATOM   10261 O OD1 . ASN C  1 261 ? -6.575  11.651  -56.244  1.00 36.55  ? 261 ASN C OD1 1 
ATOM   10262 N ND2 . ASN C  1 261 ? -6.173  13.701  -57.065  1.00 39.15  ? 261 ASN C ND2 1 
ATOM   10263 N N   . GLU C  1 262 ? -9.942  11.468  -60.248  1.00 34.05  ? 262 GLU C N   1 
ATOM   10264 C CA  . GLU C  1 262 ? -11.235 11.460  -60.916  1.00 34.82  ? 262 GLU C CA  1 
ATOM   10265 C C   . GLU C  1 262 ? -11.705 10.044  -61.189  1.00 31.04  ? 262 GLU C C   1 
ATOM   10266 O O   . GLU C  1 262 ? -12.894 9.748   -61.045  1.00 36.37  ? 262 GLU C O   1 
ATOM   10267 C CB  . GLU C  1 262 ? -11.171 12.272  -62.204  1.00 43.69  ? 262 GLU C CB  1 
ATOM   10268 C CG  . GLU C  1 262 ? -11.050 13.759  -61.939  1.00 49.82  ? 262 GLU C CG  1 
ATOM   10269 C CD  . GLU C  1 262 ? -11.113 14.564  -63.207  1.00 54.62  ? 262 GLU C CD  1 
ATOM   10270 O OE1 . GLU C  1 262 ? -11.907 14.193  -64.101  1.00 54.66  ? 262 GLU C OE1 1 
ATOM   10271 O OE2 . GLU C  1 262 ? -10.365 15.558  -63.308  1.00 56.07  ? 262 GLU C OE2 1 
ATOM   10272 N N   . ALA C  1 263 ? -10.790 9.150   -61.560  1.00 32.49  ? 263 ALA C N   1 
ATOM   10273 C CA  . ALA C  1 263 ? -11.174 7.759   -61.783  1.00 32.89  ? 263 ALA C CA  1 
ATOM   10274 C C   . ALA C  1 263 ? -11.689 7.118   -60.495  1.00 32.26  ? 263 ALA C C   1 
ATOM   10275 O O   . ALA C  1 263 ? -12.685 6.386   -60.510  1.00 32.56  ? 263 ALA C O   1 
ATOM   10276 C CB  . ALA C  1 263 ? -9.997  6.974   -62.359  1.00 29.71  ? 263 ALA C CB  1 
ATOM   10277 N N   . LEU C  1 264 ? -11.034 7.389   -59.367  1.00 32.27  ? 264 LEU C N   1 
ATOM   10278 C CA  . LEU C  1 264 ? -11.526 6.857   -58.100  1.00 31.53  ? 264 LEU C CA  1 
ATOM   10279 C C   . LEU C  1 264 ? -12.917 7.390   -57.784  1.00 37.15  ? 264 LEU C C   1 
ATOM   10280 O O   . LEU C  1 264 ? -13.787 6.635   -57.335  1.00 40.54  ? 264 LEU C O   1 
ATOM   10281 C CB  . LEU C  1 264 ? -10.552 7.195   -56.979  1.00 32.32  ? 264 LEU C CB  1 
ATOM   10282 C CG  . LEU C  1 264 ? -9.185  6.526   -57.130  1.00 33.89  ? 264 LEU C CG  1 
ATOM   10283 C CD1 . LEU C  1 264 ? -8.156  7.238   -56.263  1.00 31.26  ? 264 LEU C CD1 1 
ATOM   10284 C CD2 . LEU C  1 264 ? -9.235  5.017   -56.821  1.00 34.37  ? 264 LEU C CD2 1 
ATOM   10285 N N   . GLU C  1 265 ? -13.153 8.689   -58.025  1.00 36.49  ? 265 GLU C N   1 
ATOM   10286 C CA  . GLU C  1 265 ? -14.487 9.236   -57.807  1.00 43.89  ? 265 GLU C CA  1 
ATOM   10287 C C   . GLU C  1 265 ? -15.511 8.518   -58.676  1.00 43.13  ? 265 GLU C C   1 
ATOM   10288 O O   . GLU C  1 265 ? -16.627 8.229   -58.227  1.00 47.87  ? 265 GLU C O   1 
ATOM   10289 C CB  . GLU C  1 265 ? -14.506 10.746  -58.085  1.00 46.83  ? 265 GLU C CB  1 
ATOM   10290 C CG  . GLU C  1 265 ? -13.774 11.602  -57.046  1.00 49.81  ? 265 GLU C CG  1 
ATOM   10291 C CD  . GLU C  1 265 ? -13.654 13.059  -57.468  1.00 52.22  ? 265 GLU C CD  1 
ATOM   10292 O OE1 . GLU C  1 265 ? -13.814 13.354  -58.674  1.00 57.25  ? 265 GLU C OE1 1 
ATOM   10293 O OE2 . GLU C  1 265 ? -13.400 13.915  -56.599  1.00 53.12  ? 265 GLU C OE2 1 
ATOM   10294 N N   . LEU C  1 266 ? -15.142 8.205   -59.918  1.00 38.82  ? 266 LEU C N   1 
ATOM   10295 C CA  . LEU C  1 266 ? -16.080 7.565   -60.832  1.00 35.04  ? 266 LEU C CA  1 
ATOM   10296 C C   . LEU C  1 266 ? -16.464 6.183   -60.336  1.00 35.77  ? 266 LEU C C   1 
ATOM   10297 O O   . LEU C  1 266 ? -17.655 5.855   -60.257  1.00 34.23  ? 266 LEU C O   1 
ATOM   10298 C CB  . LEU C  1 266 ? -15.482 7.477   -62.234  1.00 34.00  ? 266 LEU C CB  1 
ATOM   10299 C CG  . LEU C  1 266 ? -16.307 6.697   -63.258  1.00 37.15  ? 266 LEU C CG  1 
ATOM   10300 C CD1 . LEU C  1 266 ? -17.735 7.221   -63.316  1.00 43.20  ? 266 LEU C CD1 1 
ATOM   10301 C CD2 . LEU C  1 266 ? -15.676 6.813   -64.623  1.00 38.38  ? 266 LEU C CD2 1 
ATOM   10302 N N   . TYR C  1 267 ? -15.461 5.353   -60.017  1.00 34.82  ? 267 TYR C N   1 
ATOM   10303 C CA  . TYR C  1 267 ? -15.712 4.023   -59.465  1.00 39.03  ? 267 TYR C CA  1 
ATOM   10304 C C   . TYR C  1 267 ? -16.621 4.093   -58.250  1.00 36.61  ? 267 TYR C C   1 
ATOM   10305 O O   . TYR C  1 267 ? -17.593 3.337   -58.145  1.00 34.35  ? 267 TYR C O   1 
ATOM   10306 C CB  . TYR C  1 267 ? -14.391 3.342   -59.095  1.00 41.01  ? 267 TYR C CB  1 
ATOM   10307 C CG  . TYR C  1 267 ? -13.606 2.819   -60.284  1.00 37.80  ? 267 TYR C CG  1 
ATOM   10308 C CD1 . TYR C  1 267 ? -14.143 1.852   -61.121  1.00 35.97  ? 267 TYR C CD1 1 
ATOM   10309 C CD2 . TYR C  1 267 ? -12.320 3.280   -60.551  1.00 36.56  ? 267 TYR C CD2 1 
ATOM   10310 C CE1 . TYR C  1 267 ? -13.427 1.363   -62.206  1.00 37.66  ? 267 TYR C CE1 1 
ATOM   10311 C CE2 . TYR C  1 267 ? -11.595 2.800   -61.621  1.00 37.83  ? 267 TYR C CE2 1 
ATOM   10312 C CZ  . TYR C  1 267 ? -12.151 1.843   -62.453  1.00 36.66  ? 267 TYR C CZ  1 
ATOM   10313 O OH  . TYR C  1 267 ? -11.419 1.366   -63.518  1.00 31.71  ? 267 TYR C OH  1 
ATOM   10314 N N   . TYR C  1 268 ? -16.326 5.014   -57.324  1.00 37.69  ? 268 TYR C N   1 
ATOM   10315 C CA  . TYR C  1 268 ? -17.191 5.206   -56.162  1.00 36.06  ? 268 TYR C CA  1 
ATOM   10316 C C   . TYR C  1 268 ? -18.618 5.525   -56.582  1.00 35.16  ? 268 TYR C C   1 
ATOM   10317 O O   . TYR C  1 268 ? -19.576 4.938   -56.067  1.00 35.12  ? 268 TYR C O   1 
ATOM   10318 C CB  . TYR C  1 268 ? -16.663 6.326   -55.272  1.00 37.93  ? 268 TYR C CB  1 
ATOM   10319 C CG  . TYR C  1 268 ? -17.657 6.726   -54.208  1.00 42.03  ? 268 TYR C CG  1 
ATOM   10320 C CD1 . TYR C  1 268 ? -17.996 5.841   -53.198  1.00 46.02  ? 268 TYR C CD1 1 
ATOM   10321 C CD2 . TYR C  1 268 ? -18.281 7.966   -54.229  1.00 44.20  ? 268 TYR C CD2 1 
ATOM   10322 C CE1 . TYR C  1 268 ? -18.905 6.178   -52.221  1.00 50.87  ? 268 TYR C CE1 1 
ATOM   10323 C CE2 . TYR C  1 268 ? -19.204 8.315   -53.259  1.00 51.61  ? 268 TYR C CE2 1 
ATOM   10324 C CZ  . TYR C  1 268 ? -19.510 7.413   -52.249  1.00 56.98  ? 268 TYR C CZ  1 
ATOM   10325 O OH  . TYR C  1 268 ? -20.419 7.731   -51.253  1.00 62.90  ? 268 TYR C OH  1 
ATOM   10326 N N   . GLU C  1 269 ? -18.789 6.479   -57.496  1.00 35.78  ? 269 GLU C N   1 
ATOM   10327 C CA  . GLU C  1 269 ? -20.145 6.873   -57.854  1.00 41.04  ? 269 GLU C CA  1 
ATOM   10328 C C   . GLU C  1 269 ? -20.907 5.720   -58.485  1.00 42.52  ? 269 GLU C C   1 
ATOM   10329 O O   . GLU C  1 269 ? -22.130 5.637   -58.344  1.00 45.72  ? 269 GLU C O   1 
ATOM   10330 C CB  . GLU C  1 269 ? -20.121 8.083   -58.784  1.00 46.86  ? 269 GLU C CB  1 
ATOM   10331 C CG  . GLU C  1 269 ? -19.702 9.368   -58.089  1.00 57.39  ? 269 GLU C CG  1 
ATOM   10332 C CD  . GLU C  1 269 ? -20.793 9.961   -57.196  1.00 65.40  ? 269 GLU C CD  1 
ATOM   10333 O OE1 . GLU C  1 269 ? -20.677 11.150  -56.835  1.00 66.80  ? 269 GLU C OE1 1 
ATOM   10334 O OE2 . GLU C  1 269 ? -21.764 9.250   -56.854  1.00 68.92  ? 269 GLU C OE2 1 
ATOM   10335 N N   . LYS C  1 270 ? -20.209 4.802   -59.145  1.00 43.92  ? 270 LYS C N   1 
ATOM   10336 C CA  . LYS C  1 270 ? -20.864 3.662   -59.773  1.00 49.42  ? 270 LYS C CA  1 
ATOM   10337 C C   . LYS C  1 270 ? -20.980 2.466   -58.841  1.00 47.35  ? 270 LYS C C   1 
ATOM   10338 O O   . LYS C  1 270 ? -21.274 1.358   -59.303  1.00 45.70  ? 270 LYS C O   1 
ATOM   10339 C CB  . LYS C  1 270 ? -20.137 3.258   -61.062  1.00 48.60  ? 270 LYS C CB  1 
ATOM   10340 C CG  . LYS C  1 270 ? -19.723 4.417   -61.999  1.00 53.64  ? 270 LYS C CG  1 
ATOM   10341 C CD  . LYS C  1 270 ? -20.708 5.612   -62.052  1.00 58.29  ? 270 LYS C CD  1 
ATOM   10342 C CE  . LYS C  1 270 ? -22.093 5.235   -62.542  1.00 63.28  ? 270 LYS C CE  1 
ATOM   10343 N NZ  . LYS C  1 270 ? -22.033 4.287   -63.676  1.00 66.05  ? 270 LYS C NZ  1 
ATOM   10344 N N   . GLY C  1 271 ? -20.762 2.669   -57.546  1.00 47.11  ? 271 GLY C N   1 
ATOM   10345 C CA  . GLY C  1 271 ? -21.007 1.648   -56.551  1.00 43.67  ? 271 GLY C CA  1 
ATOM   10346 C C   . GLY C  1 271 ? -19.863 0.706   -56.272  1.00 41.12  ? 271 GLY C C   1 
ATOM   10347 O O   . GLY C  1 271 ? -20.074 -0.309  -55.596  1.00 48.03  ? 271 GLY C O   1 
ATOM   10348 N N   . ILE C  1 272 ? -18.660 0.989   -56.762  1.00 36.66  ? 272 ILE C N   1 
ATOM   10349 C CA  . ILE C  1 272 ? -17.528 0.098   -56.513  1.00 39.95  ? 272 ILE C CA  1 
ATOM   10350 C C   . ILE C  1 272 ? -16.938 0.442   -55.149  1.00 42.21  ? 272 ILE C C   1 
ATOM   10351 O O   . ILE C  1 272 ? -16.529 1.583   -54.911  1.00 45.53  ? 272 ILE C O   1 
ATOM   10352 C CB  . ILE C  1 272 ? -16.474 0.210   -57.626  1.00 37.01  ? 272 ILE C CB  1 
ATOM   10353 C CG1 . ILE C  1 272 ? -17.095 -0.071  -58.999  1.00 40.22  ? 272 ILE C CG1 1 
ATOM   10354 C CG2 . ILE C  1 272 ? -15.323 -0.720  -57.361  1.00 34.16  ? 272 ILE C CG2 1 
ATOM   10355 C CD1 . ILE C  1 272 ? -17.883 -1.359  -59.078  1.00 41.51  ? 272 ILE C CD1 1 
ATOM   10356 N N   . ASN C  1 273 ? -16.906 -0.537  -54.244  1.00 38.78  ? 273 ASN C N   1 
ATOM   10357 C CA  . ASN C  1 273 ? -16.479 -0.279  -52.871  1.00 40.38  ? 273 ASN C CA  1 
ATOM   10358 C C   . ASN C  1 273 ? -15.008 -0.560  -52.635  1.00 40.83  ? 273 ASN C C   1 
ATOM   10359 O O   . ASN C  1 273 ? -14.431 -0.036  -51.677  1.00 42.51  ? 273 ASN C O   1 
ATOM   10360 C CB  . ASN C  1 273 ? -17.289 -1.123  -51.890  1.00 42.97  ? 273 ASN C CB  1 
ATOM   10361 C CG  . ASN C  1 273 ? -18.722 -0.711  -51.833  1.00 47.26  ? 273 ASN C CG  1 
ATOM   10362 O OD1 . ASN C  1 273 ? -19.036 0.475   -51.710  1.00 53.58  ? 273 ASN C OD1 1 
ATOM   10363 N ND2 . ASN C  1 273 ? -19.614 -1.681  -51.944  1.00 49.35  ? 273 ASN C ND2 1 
ATOM   10364 N N   . MET C  1 274 ? -14.391 -1.375  -53.477  1.00 39.59  ? 274 MET C N   1 
ATOM   10365 C CA  . MET C  1 274 ? -13.003 -1.738  -53.269  1.00 41.85  ? 274 MET C CA  1 
ATOM   10366 C C   . MET C  1 274 ? -12.368 -1.999  -54.622  1.00 35.79  ? 274 MET C C   1 
ATOM   10367 O O   . MET C  1 274 ? -12.987 -2.599  -55.504  1.00 35.94  ? 274 MET C O   1 
ATOM   10368 C CB  . MET C  1 274 ? -12.884 -2.961  -52.352  1.00 45.89  ? 274 MET C CB  1 
ATOM   10369 C CG  . MET C  1 274 ? -11.465 -3.269  -51.909  1.00 54.74  ? 274 MET C CG  1 
ATOM   10370 S SD  . MET C  1 274 ? -10.725 -4.546  -52.944  1.00 60.79  ? 274 MET C SD  1 
ATOM   10371 C CE  . MET C  1 274 ? -11.221 -6.011  -52.052  1.00 62.03  ? 274 MET C CE  1 
ATOM   10372 N N   . LEU C  1 275 ? -11.149 -1.508  -54.791  1.00 33.44  ? 275 LEU C N   1 
ATOM   10373 C CA  . LEU C  1 275 ? -10.305 -1.897  -55.906  1.00 32.90  ? 275 LEU C CA  1 
ATOM   10374 C C   . LEU C  1 275 ? -8.862  -1.943  -55.428  1.00 32.54  ? 275 LEU C C   1 
ATOM   10375 O O   . LEU C  1 275 ? -8.542  -1.560  -54.297  1.00 27.84  ? 275 LEU C O   1 
ATOM   10376 C CB  . LEU C  1 275 ? -10.456 -0.943  -57.095  1.00 35.36  ? 275 LEU C CB  1 
ATOM   10377 C CG  . LEU C  1 275 ? -10.177 0.536   -56.870  1.00 35.10  ? 275 LEU C CG  1 
ATOM   10378 C CD1 . LEU C  1 275 ? -8.693  0.865   -56.953  1.00 35.32  ? 275 LEU C CD1 1 
ATOM   10379 C CD2 . LEU C  1 275 ? -10.963 1.325   -57.893  1.00 36.64  ? 275 LEU C CD2 1 
ATOM   10380 N N   . ALA C  1 276 ? -7.988  -2.391  -56.320  1.00 31.59  ? 276 ALA C N   1 
ATOM   10381 C CA  . ALA C  1 276 ? -6.562  -2.415  -56.064  1.00 29.76  ? 276 ALA C CA  1 
ATOM   10382 C C   . ALA C  1 276 ? -5.819  -1.705  -57.188  1.00 27.20  ? 276 ALA C C   1 
ATOM   10383 O O   . ALA C  1 276 ? -6.324  -1.541  -58.301  1.00 31.51  ? 276 ALA C O   1 
ATOM   10384 C CB  . ALA C  1 276 ? -6.033  -3.850  -55.904  1.00 24.32  ? 276 ALA C CB  1 
ATOM   10385 N N   . THR C  1 277 ? -4.611  -1.267  -56.871  1.00 30.30  ? 277 THR C N   1 
ATOM   10386 C CA  . THR C  1 277 ? -3.720  -0.691  -57.862  1.00 34.32  ? 277 THR C CA  1 
ATOM   10387 C C   . THR C  1 277 ? -2.290  -1.042  -57.460  1.00 33.61  ? 277 THR C C   1 
ATOM   10388 O O   . THR C  1 277 ? -2.060  -1.995  -56.708  1.00 36.51  ? 277 THR C O   1 
ATOM   10389 C CB  . THR C  1 277 ? -3.975  0.819   -58.002  1.00 35.66  ? 277 THR C CB  1 
ATOM   10390 O OG1 . THR C  1 277 ? -3.030  1.383   -58.926  1.00 29.12  ? 277 THR C OG1 1 
ATOM   10391 C CG2 . THR C  1 277 ? -3.849  1.494   -56.655  1.00 38.37  ? 277 THR C CG2 1 
ATOM   10392 N N   . ASP C  1 278 ? -1.327  -0.273  -57.952  1.00 31.55  ? 278 ASP C N   1 
ATOM   10393 C CA  . ASP C  1 278 ? 0.067   -0.682  -57.914  1.00 31.57  ? 278 ASP C CA  1 
ATOM   10394 C C   . ASP C  1 278 ? 0.830   0.030   -56.801  1.00 34.78  ? 278 ASP C C   1 
ATOM   10395 O O   . ASP C  1 278 ? 0.534   1.175   -56.450  1.00 40.64  ? 278 ASP C O   1 
ATOM   10396 C CB  . ASP C  1 278 ? 0.741   -0.411  -59.263  1.00 30.55  ? 278 ASP C CB  1 
ATOM   10397 C CG  . ASP C  1 278 ? 2.120   -1.017  -59.352  1.00 36.13  ? 278 ASP C CG  1 
ATOM   10398 O OD1 . ASP C  1 278 ? 2.287   -2.203  -58.983  1.00 37.09  ? 278 ASP C OD1 1 
ATOM   10399 O OD2 . ASP C  1 278 ? 3.042   -0.298  -59.780  1.00 40.03  ? 278 ASP C OD2 1 
ATOM   10400 N N   . GLU C  1 279 ? 1.839   -0.666  -56.271  1.00 36.87  ? 279 GLU C N   1 
ATOM   10401 C CA  . GLU C  1 279 ? 2.725   -0.092  -55.262  1.00 36.77  ? 279 GLU C CA  1 
ATOM   10402 C C   . GLU C  1 279 ? 3.430   1.169   -55.759  1.00 38.82  ? 279 GLU C C   1 
ATOM   10403 O O   . GLU C  1 279 ? 3.668   2.094   -54.972  1.00 41.04  ? 279 GLU C O   1 
ATOM   10404 C CB  . GLU C  1 279 ? 3.753   -1.142  -54.817  1.00 37.43  ? 279 GLU C CB  1 
ATOM   10405 C CG  . GLU C  1 279 ? 4.547   -0.774  -53.557  1.00 42.08  ? 279 GLU C CG  1 
ATOM   10406 C CD  . GLU C  1 279 ? 5.447   -1.908  -53.065  1.00 44.11  ? 279 GLU C CD  1 
ATOM   10407 O OE1 . GLU C  1 279 ? 5.414   -3.012  -53.651  1.00 44.56  ? 279 GLU C OE1 1 
ATOM   10408 O OE2 . GLU C  1 279 ? 6.207   -1.687  -52.098  1.00 47.86  ? 279 GLU C OE2 1 
ATOM   10409 N N   . VAL C  1 280 ? 3.777   1.236   -57.049  1.00 37.24  ? 280 VAL C N   1 
ATOM   10410 C CA  . VAL C  1 280 ? 4.466   2.424   -57.556  1.00 39.69  ? 280 VAL C CA  1 
ATOM   10411 C C   . VAL C  1 280 ? 3.565   3.647   -57.445  1.00 38.23  ? 280 VAL C C   1 
ATOM   10412 O O   . VAL C  1 280 ? 4.020   4.746   -57.108  1.00 40.14  ? 280 VAL C O   1 
ATOM   10413 C CB  . VAL C  1 280 ? 4.942   2.206   -59.005  1.00 45.55  ? 280 VAL C CB  1 
ATOM   10414 C CG1 . VAL C  1 280 ? 5.516   3.502   -59.572  1.00 41.87  ? 280 VAL C CG1 1 
ATOM   10415 C CG2 . VAL C  1 280 ? 5.976   1.077   -59.069  1.00 49.03  ? 280 VAL C CG2 1 
ATOM   10416 N N   . ILE C  1 281 ? 2.271   3.475   -57.710  1.00 33.64  ? 281 ILE C N   1 
ATOM   10417 C CA  . ILE C  1 281 ? 1.335   4.574   -57.511  1.00 31.25  ? 281 ILE C CA  1 
ATOM   10418 C C   . ILE C  1 281 ? 1.273   4.951   -56.033  1.00 37.47  ? 281 ILE C C   1 
ATOM   10419 O O   . ILE C  1 281 ? 1.218   6.135   -55.679  1.00 33.49  ? 281 ILE C O   1 
ATOM   10420 C CB  . ILE C  1 281 ? -0.045  4.193   -58.075  1.00 32.13  ? 281 ILE C CB  1 
ATOM   10421 C CG1 . ILE C  1 281 ? 0.070   3.953   -59.591  1.00 36.15  ? 281 ILE C CG1 1 
ATOM   10422 C CG2 . ILE C  1 281 ? -1.099  5.247   -57.728  1.00 25.85  ? 281 ILE C CG2 1 
ATOM   10423 C CD1 . ILE C  1 281 ? -1.231  4.116   -60.375  1.00 39.45  ? 281 ILE C CD1 1 
ATOM   10424 N N   . LEU C  1 282 ? 1.316   3.953   -55.146  1.00 38.00  ? 282 LEU C N   1 
ATOM   10425 C CA  . LEU C  1 282 ? 1.358   4.238   -53.717  1.00 38.42  ? 282 LEU C CA  1 
ATOM   10426 C C   . LEU C  1 282 ? 2.591   5.054   -53.362  1.00 35.84  ? 282 LEU C C   1 
ATOM   10427 O O   . LEU C  1 282 ? 2.493   6.075   -52.675  1.00 36.75  ? 282 LEU C O   1 
ATOM   10428 C CB  . LEU C  1 282 ? 1.331   2.940   -52.922  1.00 39.28  ? 282 LEU C CB  1 
ATOM   10429 C CG  . LEU C  1 282 ? 1.401   3.153   -51.411  1.00 38.74  ? 282 LEU C CG  1 
ATOM   10430 C CD1 . LEU C  1 282 ? 0.173   3.916   -50.930  1.00 39.45  ? 282 LEU C CD1 1 
ATOM   10431 C CD2 . LEU C  1 282 ? 1.492   1.814   -50.741  1.00 39.45  ? 282 LEU C CD2 1 
ATOM   10432 N N   . LYS C  1 283 ? 3.761   4.634   -53.853  1.00 34.49  ? 283 LYS C N   1 
ATOM   10433 C CA  . LYS C  1 283 ? 4.999   5.342   -53.533  1.00 43.54  ? 283 LYS C CA  1 
ATOM   10434 C C   . LYS C  1 283 ? 5.017   6.760   -54.101  1.00 43.34  ? 283 LYS C C   1 
ATOM   10435 O O   . LYS C  1 283 ? 5.678   7.638   -53.538  1.00 43.69  ? 283 LYS C O   1 
ATOM   10436 C CB  . LYS C  1 283 ? 6.204   4.548   -54.038  1.00 46.41  ? 283 LYS C CB  1 
ATOM   10437 C CG  . LYS C  1 283 ? 6.272   3.125   -53.501  1.00 53.45  ? 283 LYS C CG  1 
ATOM   10438 C CD  . LYS C  1 283 ? 6.518   3.089   -52.005  1.00 61.64  ? 283 LYS C CD  1 
ATOM   10439 C CE  . LYS C  1 283 ? 6.963   1.713   -51.511  1.00 65.73  ? 283 LYS C CE  1 
ATOM   10440 N NZ  . LYS C  1 283 ? 8.162   1.195   -52.232  1.00 66.32  ? 283 LYS C NZ  1 
ATOM   10441 N N   . ASN C  1 284 ? 4.306   7.005   -55.203  1.00 42.18  ? 284 ASN C N   1 
ATOM   10442 C CA  . ASN C  1 284 ? 4.230   8.341   -55.785  1.00 43.97  ? 284 ASN C CA  1 
ATOM   10443 C C   . ASN C  1 284 ? 3.249   9.244   -55.062  1.00 44.28  ? 284 ASN C C   1 
ATOM   10444 O O   . ASN C  1 284 ? 3.371   10.471  -55.154  1.00 48.50  ? 284 ASN C O   1 
ATOM   10445 C CB  . ASN C  1 284 ? 3.810   8.266   -57.256  1.00 44.31  ? 284 ASN C CB  1 
ATOM   10446 C CG  . ASN C  1 284 ? 4.874   7.670   -58.140  1.00 44.66  ? 284 ASN C CG  1 
ATOM   10447 O OD1 . ASN C  1 284 ? 6.053   7.648   -57.786  1.00 45.84  ? 284 ASN C OD1 1 
ATOM   10448 N ND2 . ASN C  1 284 ? 4.463   7.179   -59.306  1.00 44.07  ? 284 ASN C ND2 1 
ATOM   10449 N N   . SER C  1 285 ? 2.280   8.666   -54.359  1.00 41.72  ? 285 SER C N   1 
ATOM   10450 C CA  . SER C  1 285 ? 1.171   9.414   -53.789  1.00 43.18  ? 285 SER C CA  1 
ATOM   10451 C C   . SER C  1 285 ? 1.307   9.673   -52.297  1.00 43.84  ? 285 SER C C   1 
ATOM   10452 O O   . SER C  1 285 ? 0.770   10.674  -51.809  1.00 39.95  ? 285 SER C O   1 
ATOM   10453 C CB  . SER C  1 285 ? -0.140  8.668   -54.034  1.00 39.58  ? 285 SER C CB  1 
ATOM   10454 O OG  . SER C  1 285 ? -0.328  8.409   -55.404  1.00 36.20  ? 285 SER C OG  1 
ATOM   10455 N N   . VAL C  1 286 ? 1.981   8.786   -51.558  1.00 43.88  ? 286 VAL C N   1 
ATOM   10456 C CA  . VAL C  1 286 ? 2.086   8.896   -50.108  1.00 49.45  ? 286 VAL C CA  1 
ATOM   10457 C C   . VAL C  1 286 ? 3.539   8.729   -49.684  1.00 50.90  ? 286 VAL C C   1 
ATOM   10458 O O   . VAL C  1 286 ? 4.341   8.074   -50.354  1.00 50.23  ? 286 VAL C O   1 
ATOM   10459 C CB  . VAL C  1 286 ? 1.213   7.856   -49.372  1.00 51.18  ? 286 VAL C CB  1 
ATOM   10460 C CG1 . VAL C  1 286 ? -0.156  7.744   -50.004  1.00 49.31  ? 286 VAL C CG1 1 
ATOM   10461 C CG2 . VAL C  1 286 ? 1.892   6.514   -49.378  1.00 55.61  ? 286 VAL C CG2 1 
ATOM   10462 N N   . GLU C  1 287 ? 3.805   9.305   -48.520  1.00 54.39  ? 287 GLU C N   1 
ATOM   10463 C CA  . GLU C  1 287 ? 5.139   9.214   -47.967  1.00 61.25  ? 287 GLU C CA  1 
ATOM   10464 C C   . GLU C  1 287 ? 5.321   7.998   -47.139  1.00 65.60  ? 287 GLU C C   1 
ATOM   10465 O O   . GLU C  1 287 ? 6.275   7.327   -47.304  1.00 71.34  ? 287 GLU C O   1 
ATOM   10466 C CB  . GLU C  1 287 ? 5.425   10.440  -47.130  1.00 61.60  ? 287 GLU C CB  1 
ATOM   10467 C CG  . GLU C  1 287 ? 5.294   11.765  -47.826  1.00 62.94  ? 287 GLU C CG  1 
ATOM   10468 C CD  . GLU C  1 287 ? 5.358   12.904  -46.839  1.00 66.31  ? 287 GLU C CD  1 
ATOM   10469 O OE1 . GLU C  1 287 ? 5.850   13.976  -47.208  1.00 67.00  ? 287 GLU C OE1 1 
ATOM   10470 O OE2 . GLU C  1 287 ? 4.926   12.709  -45.690  1.00 68.17  ? 287 GLU C OE2 1 
ATOM   10471 N N   . ARG C  1 288 ? 4.393   7.733   -46.249  1.00 67.05  ? 288 ARG C N   1 
ATOM   10472 C CA  . ARG C  1 288 ? 4.433   6.511   -45.379  1.00 70.29  ? 288 ARG C CA  1 
ATOM   10473 C C   . ARG C  1 288 ? 3.978   5.299   -46.148  1.00 68.36  ? 288 ARG C C   1 
ATOM   10474 O O   . ARG C  1 288 ? 3.030   4.687   -45.820  1.00 70.31  ? 288 ARG C O   1 
ATOM   10475 C CB  . ARG C  1 288 ? 3.468   6.771   -44.255  1.00 70.83  ? 288 ARG C CB  1 
ATOM   10476 C CG  . ARG C  1 288 ? 3.560   5.895   -43.034  1.00 71.03  ? 288 ARG C CG  1 
ATOM   10477 C CD  . ARG C  1 288 ? 3.165   6.700   -41.815  1.00 66.34  ? 288 ARG C CD  1 
ATOM   10478 N NE  . ARG C  1 288 ? 4.258   7.576   -41.427  1.00 65.48  ? 288 ARG C NE  1 
ATOM   10479 C CZ  . ARG C  1 288 ? 4.149   8.891   -41.332  1.00 62.66  ? 288 ARG C CZ  1 
ATOM   10480 N NH1 . ARG C  1 288 ? 5.183   9.627   -40.973  1.00 56.07  ? 288 ARG C NH1 1 
ATOM   10481 N NH2 . ARG C  1 288 ? 2.986   9.462   -41.591  1.00 63.52  ? 288 ARG C NH2 1 
ATOM   10482 N N   . ALA C  1 289 ? 4.645   4.957   -47.190  1.00 64.74  ? 289 ALA C N   1 
ATOM   10483 C CA  . ALA C  1 289 ? 4.107   3.964   -48.097  1.00 63.87  ? 289 ALA C CA  1 
ATOM   10484 C C   . ALA C  1 289 ? 4.153   2.509   -47.799  1.00 61.64  ? 289 ALA C C   1 
ATOM   10485 O O   . ALA C  1 289 ? 4.915   1.794   -48.348  1.00 66.99  ? 289 ALA C O   1 
ATOM   10486 C CB  . ALA C  1 289 ? 4.746   4.237   -49.439  1.00 62.28  ? 289 ALA C CB  1 
ATOM   10487 N N   . SER C  1 290 ? 3.237   2.060   -47.029  1.00 53.20  ? 290 SER C N   1 
ATOM   10488 C CA  . SER C  1 290 ? 3.177   0.646   -46.677  1.00 46.08  ? 290 SER C CA  1 
ATOM   10489 C C   . SER C  1 290 ? 2.071   -0.043  -47.457  1.00 40.07  ? 290 SER C C   1 
ATOM   10490 O O   . SER C  1 290 ? 0.887   0.277   -47.253  1.00 36.85  ? 290 SER C O   1 
ATOM   10491 C CB  . SER C  1 290 ? 2.945   0.463   -45.185  1.00 44.03  ? 290 SER C CB  1 
ATOM   10492 O OG  . SER C  1 290 ? 2.639   -0.893  -44.910  1.00 40.07  ? 290 SER C OG  1 
ATOM   10493 N N   . PRO C  1 291 ? 2.395   -1.000  -48.327  1.00 39.06  ? 291 PRO C N   1 
ATOM   10494 C CA  . PRO C  1 291 ? 1.364   -1.696  -49.105  1.00 37.79  ? 291 PRO C CA  1 
ATOM   10495 C C   . PRO C  1 291 ? 0.584   -2.748  -48.332  1.00 39.51  ? 291 PRO C C   1 
ATOM   10496 O O   . PRO C  1 291 ? -0.183  -3.490  -48.947  1.00 38.21  ? 291 PRO C O   1 
ATOM   10497 C CB  . PRO C  1 291 ? 2.185   -2.352  -50.227  1.00 41.67  ? 291 PRO C CB  1 
ATOM   10498 C CG  . PRO C  1 291 ? 3.501   -2.657  -49.579  1.00 40.10  ? 291 PRO C CG  1 
ATOM   10499 C CD  . PRO C  1 291 ? 3.752   -1.503  -48.615  1.00 39.49  ? 291 PRO C CD  1 
ATOM   10500 N N   . TYR C  1 292 ? 0.730   -2.842  -47.008  1.00 37.77  ? 292 TYR C N   1 
ATOM   10501 C CA  . TYR C  1 292 ? 0.075   -3.903  -46.257  1.00 36.06  ? 292 TYR C CA  1 
ATOM   10502 C C   . TYR C  1 292 ? -1.163  -3.424  -45.516  1.00 32.55  ? 292 TYR C C   1 
ATOM   10503 O O   . TYR C  1 292 ? -1.762  -4.199  -44.762  1.00 30.44  ? 292 TYR C O   1 
ATOM   10504 C CB  . TYR C  1 292 ? 1.078   -4.539  -45.301  1.00 38.86  ? 292 TYR C CB  1 
ATOM   10505 C CG  . TYR C  1 292 ? 2.299   -4.976  -46.062  1.00 44.17  ? 292 TYR C CG  1 
ATOM   10506 C CD1 . TYR C  1 292 ? 2.173   -5.808  -47.174  1.00 46.40  ? 292 TYR C CD1 1 
ATOM   10507 C CD2 . TYR C  1 292 ? 3.566   -4.522  -45.723  1.00 43.99  ? 292 TYR C CD2 1 
ATOM   10508 C CE1 . TYR C  1 292 ? 3.271   -6.206  -47.902  1.00 48.36  ? 292 TYR C CE1 1 
ATOM   10509 C CE2 . TYR C  1 292 ? 4.682   -4.919  -46.452  1.00 49.94  ? 292 TYR C CE2 1 
ATOM   10510 C CZ  . TYR C  1 292 ? 4.522   -5.765  -47.544  1.00 52.44  ? 292 TYR C CZ  1 
ATOM   10511 O OH  . TYR C  1 292 ? 5.605   -6.175  -48.292  1.00 56.08  ? 292 TYR C OH  1 
ATOM   10512 N N   . LEU C  1 293 ? -1.567  -2.179  -45.737  1.00 30.21  ? 293 LEU C N   1 
ATOM   10513 C CA  . LEU C  1 293 ? -2.723  -1.567  -45.103  1.00 34.22  ? 293 LEU C CA  1 
ATOM   10514 C C   . LEU C  1 293 ? -3.913  -1.562  -46.054  1.00 34.91  ? 293 LEU C C   1 
ATOM   10515 O O   . LEU C  1 293 ? -3.745  -1.576  -47.277  1.00 33.36  ? 293 LEU C O   1 
ATOM   10516 C CB  . LEU C  1 293 ? -2.404  -0.131  -44.697  1.00 36.49  ? 293 LEU C CB  1 
ATOM   10517 C CG  . LEU C  1 293 ? -1.603  0.164   -43.422  1.00 41.40  ? 293 LEU C CG  1 
ATOM   10518 C CD1 . LEU C  1 293 ? -0.421  -0.767  -43.199  1.00 40.19  ? 293 LEU C CD1 1 
ATOM   10519 C CD2 . LEU C  1 293 ? -1.136  1.611   -43.455  1.00 44.56  ? 293 LEU C CD2 1 
ATOM   10520 N N   . ARG C  1 294 ? -5.121  -1.548  -45.486  1.00 32.16  ? 294 ARG C N   1 
ATOM   10521 C CA  . ARG C  1 294 ? -6.310  -1.203  -46.257  1.00 31.39  ? 294 ARG C CA  1 
ATOM   10522 C C   . ARG C  1 294 ? -6.446  0.315   -46.254  1.00 31.74  ? 294 ARG C C   1 
ATOM   10523 O O   . ARG C  1 294 ? -6.560  0.934   -45.190  1.00 33.03  ? 294 ARG C O   1 
ATOM   10524 C CB  . ARG C  1 294 ? -7.580  -1.859  -45.707  1.00 30.61  ? 294 ARG C CB  1 
ATOM   10525 C CG  . ARG C  1 294 ? -8.864  -1.414  -46.445  1.00 33.40  ? 294 ARG C CG  1 
ATOM   10526 C CD  . ARG C  1 294 ? -10.044 -2.357  -46.205  1.00 37.70  ? 294 ARG C CD  1 
ATOM   10527 N NE  . ARG C  1 294 ? -10.566 -2.228  -44.848  1.00 41.46  ? 294 ARG C NE  1 
ATOM   10528 C CZ  . ARG C  1 294 ? -10.645 -3.219  -43.963  1.00 43.98  ? 294 ARG C CZ  1 
ATOM   10529 N NH1 . ARG C  1 294 ? -10.239 -4.451  -44.276  1.00 40.90  ? 294 ARG C NH1 1 
ATOM   10530 N NH2 . ARG C  1 294 ? -11.135 -2.972  -42.754  1.00 45.55  ? 294 ARG C NH2 1 
ATOM   10531 N N   . TYR C  1 295 ? -6.401  0.916   -47.434  1.00 31.20  ? 295 TYR C N   1 
ATOM   10532 C CA  . TYR C  1 295 ? -6.499  2.360   -47.541  1.00 35.46  ? 295 TYR C CA  1 
ATOM   10533 C C   . TYR C  1 295 ? -7.923  2.754   -47.883  1.00 36.73  ? 295 TYR C C   1 
ATOM   10534 O O   . TYR C  1 295 ? -8.639  2.033   -48.581  1.00 33.58  ? 295 TYR C O   1 
ATOM   10535 C CB  . TYR C  1 295 ? -5.541  2.910   -48.596  1.00 36.52  ? 295 TYR C CB  1 
ATOM   10536 C CG  . TYR C  1 295 ? -4.108  2.907   -48.141  1.00 32.60  ? 295 TYR C CG  1 
ATOM   10537 C CD1 . TYR C  1 295 ? -3.320  1.768   -48.273  1.00 30.49  ? 295 TYR C CD1 1 
ATOM   10538 C CD2 . TYR C  1 295 ? -3.541  4.036   -47.565  1.00 37.89  ? 295 TYR C CD2 1 
ATOM   10539 C CE1 . TYR C  1 295 ? -2.003  1.753   -47.858  1.00 30.98  ? 295 TYR C CE1 1 
ATOM   10540 C CE2 . TYR C  1 295 ? -2.218  4.032   -47.131  1.00 37.79  ? 295 TYR C CE2 1 
ATOM   10541 C CZ  . TYR C  1 295 ? -1.456  2.887   -47.285  1.00 37.83  ? 295 TYR C CZ  1 
ATOM   10542 O OH  . TYR C  1 295 ? -0.148  2.895   -46.866  1.00 35.30  ? 295 TYR C OH  1 
ATOM   10543 N N   . TYR C  1 296 ? -8.329  3.906   -47.364  1.00 38.13  ? 296 TYR C N   1 
ATOM   10544 C CA  . TYR C  1 296 ? -9.630  4.489   -47.655  1.00 35.09  ? 296 TYR C CA  1 
ATOM   10545 C C   . TYR C  1 296 ? -9.367  5.776   -48.422  1.00 34.37  ? 296 TYR C C   1 
ATOM   10546 O O   . TYR C  1 296 ? -8.813  6.735   -47.872  1.00 33.90  ? 296 TYR C O   1 
ATOM   10547 C CB  . TYR C  1 296 ? -10.426 4.758   -46.378  1.00 35.64  ? 296 TYR C CB  1 
ATOM   10548 C CG  . TYR C  1 296 ? -10.705 3.533   -45.529  1.00 35.78  ? 296 TYR C CG  1 
ATOM   10549 C CD1 . TYR C  1 296 ? -11.280 2.396   -46.082  1.00 38.26  ? 296 TYR C CD1 1 
ATOM   10550 C CD2 . TYR C  1 296 ? -10.397 3.515   -44.176  1.00 41.34  ? 296 TYR C CD2 1 
ATOM   10551 C CE1 . TYR C  1 296 ? -11.540 1.273   -45.311  1.00 37.79  ? 296 TYR C CE1 1 
ATOM   10552 C CE2 . TYR C  1 296 ? -10.653 2.385   -43.390  1.00 36.55  ? 296 TYR C CE2 1 
ATOM   10553 C CZ  . TYR C  1 296 ? -11.224 1.273   -43.964  1.00 37.50  ? 296 TYR C CZ  1 
ATOM   10554 O OH  . TYR C  1 296 ? -11.485 0.152   -43.205  1.00 40.08  ? 296 TYR C OH  1 
ATOM   10555 N N   . PHE C  1 297 ? -9.730  5.791   -49.696  1.00 33.43  ? 297 PHE C N   1 
ATOM   10556 C CA  . PHE C  1 297 ? -9.542  6.997   -50.489  1.00 33.91  ? 297 PHE C CA  1 
ATOM   10557 C C   . PHE C  1 297 ? -10.682 7.964   -50.180  1.00 33.06  ? 297 PHE C C   1 
ATOM   10558 O O   . PHE C  1 297 ? -11.834 7.725   -50.565  1.00 31.79  ? 297 PHE C O   1 
ATOM   10559 C CB  . PHE C  1 297 ? -9.463  6.683   -51.981  1.00 31.84  ? 297 PHE C CB  1 
ATOM   10560 C CG  . PHE C  1 297 ? -9.365  7.916   -52.824  1.00 32.40  ? 297 PHE C CG  1 
ATOM   10561 C CD1 . PHE C  1 297 ? -8.162  8.594   -52.939  1.00 35.85  ? 297 PHE C CD1 1 
ATOM   10562 C CD2 . PHE C  1 297 ? -10.492 8.446   -53.435  1.00 32.87  ? 297 PHE C CD2 1 
ATOM   10563 C CE1 . PHE C  1 297 ? -8.075  9.762   -53.696  1.00 36.40  ? 297 PHE C CE1 1 
ATOM   10564 C CE2 . PHE C  1 297 ? -10.409 9.614   -54.194  1.00 31.84  ? 297 PHE C CE2 1 
ATOM   10565 C CZ  . PHE C  1 297 ? -9.195  10.269  -54.319  1.00 32.14  ? 297 PHE C CZ  1 
ATOM   10566 N N   . ARG C  1 298 ? -10.350 9.053   -49.480  1.00 35.07  ? 298 ARG C N   1 
ATOM   10567 C CA  . ARG C  1 298 ? -11.311 10.089  -49.087  1.00 37.50  ? 298 ARG C CA  1 
ATOM   10568 C C   . ARG C  1 298 ? -12.496 9.491   -48.333  1.00 40.75  ? 298 ARG C C   1 
ATOM   10569 O O   . ARG C  1 298 ? -13.627 9.984   -48.433  1.00 37.17  ? 298 ARG C O   1 
ATOM   10570 C CB  . ARG C  1 298 ? -11.774 10.903  -50.301  1.00 39.68  ? 298 ARG C CB  1 
ATOM   10571 C CG  . ARG C  1 298 ? -10.600 11.526  -51.063  1.00 38.56  ? 298 ARG C CG  1 
ATOM   10572 C CD  . ARG C  1 298 ? -11.023 12.487  -52.158  1.00 39.41  ? 298 ARG C CD  1 
ATOM   10573 N NE  . ARG C  1 298 ? -9.857  13.071  -52.827  1.00 35.66  ? 298 ARG C NE  1 
ATOM   10574 C CZ  . ARG C  1 298 ? -9.873  13.636  -54.032  1.00 38.58  ? 298 ARG C CZ  1 
ATOM   10575 N NH1 . ARG C  1 298 ? -11.000 13.708  -54.731  1.00 37.90  ? 298 ARG C NH1 1 
ATOM   10576 N NH2 . ARG C  1 298 ? -8.749  14.134  -54.539  1.00 35.63  ? 298 ARG C NH2 1 
ATOM   10577 N N   . GLU C  1 299 ? -12.225 8.418   -47.575  1.00 39.44  ? 299 GLU C N   1 
ATOM   10578 C CA  . GLU C  1 299 ? -13.231 7.682   -46.807  1.00 38.74  ? 299 GLU C CA  1 
ATOM   10579 C C   . GLU C  1 299 ? -14.413 7.254   -47.669  1.00 43.69  ? 299 GLU C C   1 
ATOM   10580 O O   . GLU C  1 299 ? -15.504 7.000   -47.149  1.00 46.86  ? 299 GLU C O   1 
ATOM   10581 C CB  . GLU C  1 299 ? -13.718 8.493   -45.599  1.00 39.43  ? 299 GLU C CB  1 
ATOM   10582 C CG  . GLU C  1 299 ? -12.692 8.629   -44.482  1.00 43.70  ? 299 GLU C CG  1 
ATOM   10583 C CD  . GLU C  1 299 ? -12.506 7.355   -43.671  1.00 51.96  ? 299 GLU C CD  1 
ATOM   10584 O OE1 . GLU C  1 299 ? -11.949 7.443   -42.551  1.00 58.86  ? 299 GLU C OE1 1 
ATOM   10585 O OE2 . GLU C  1 299 ? -12.906 6.266   -44.140  1.00 52.90  ? 299 GLU C OE2 1 
ATOM   10586 N N   . LEU C  1 300 ? -14.199 7.142   -48.981  1.00 41.42  ? 300 LEU C N   1 
ATOM   10587 C CA  . LEU C  1 300 ? -15.253 6.839   -49.944  1.00 43.39  ? 300 LEU C CA  1 
ATOM   10588 C C   . LEU C  1 300 ? -15.082 5.506   -50.661  1.00 37.42  ? 300 LEU C C   1 
ATOM   10589 O O   . LEU C  1 300 ? -16.084 4.865   -50.965  1.00 41.54  ? 300 LEU C O   1 
ATOM   10590 C CB  . LEU C  1 300 ? -15.356 7.953   -50.994  1.00 46.18  ? 300 LEU C CB  1 
ATOM   10591 C CG  . LEU C  1 300 ? -16.023 9.249   -50.519  1.00 47.60  ? 300 LEU C CG  1 
ATOM   10592 C CD1 . LEU C  1 300 ? -16.116 10.227  -51.658  1.00 54.01  ? 300 LEU C CD1 1 
ATOM   10593 C CD2 . LEU C  1 300 ? -17.399 8.992   -49.939  1.00 49.44  ? 300 LEU C CD2 1 
ATOM   10594 N N   . ILE C  1 301 ? -13.857 5.061   -50.924  1.00 35.58  ? 301 ILE C N   1 
ATOM   10595 C CA  . ILE C  1 301 ? -13.624 3.773   -51.581  1.00 33.11  ? 301 ILE C CA  1 
ATOM   10596 C C   . ILE C  1 301 ? -12.396 3.113   -50.971  1.00 35.98  ? 301 ILE C C   1 
ATOM   10597 O O   . ILE C  1 301 ? -11.372 3.768   -50.738  1.00 35.86  ? 301 ILE C O   1 
ATOM   10598 C CB  . ILE C  1 301 ? -13.460 3.943   -53.111  1.00 29.10  ? 301 ILE C CB  1 
ATOM   10599 C CG1 . ILE C  1 301 ? -13.299 2.592   -53.822  1.00 27.06  ? 301 ILE C CG1 1 
ATOM   10600 C CG2 . ILE C  1 301 ? -12.281 4.835   -53.427  1.00 27.76  ? 301 ILE C CG2 1 
ATOM   10601 C CD1 . ILE C  1 301 ? -13.407 2.704   -55.383  1.00 27.88  ? 301 ILE C CD1 1 
ATOM   10602 N N   . SER C  1 302 ? -12.489 1.809   -50.727  1.00 33.29  ? 302 SER C N   1 
ATOM   10603 C CA  . SER C  1 302 ? -11.348 1.074   -50.203  1.00 36.29  ? 302 SER C CA  1 
ATOM   10604 C C   . SER C  1 302 ? -10.365 0.779   -51.324  1.00 34.33  ? 302 SER C C   1 
ATOM   10605 O O   . SER C  1 302 ? -10.757 0.469   -52.454  1.00 32.18  ? 302 SER C O   1 
ATOM   10606 C CB  . SER C  1 302 ? -11.788 -0.228  -49.545  1.00 37.38  ? 302 SER C CB  1 
ATOM   10607 O OG  . SER C  1 302 ? -12.620 0.040   -48.443  1.00 36.64  ? 302 SER C OG  1 
ATOM   10608 N N   . VAL C  1 303 ? -9.081  0.893   -51.006  1.00 32.13  ? 303 VAL C N   1 
ATOM   10609 C CA  . VAL C  1 303 ? -8.018  0.740   -51.986  1.00 30.55  ? 303 VAL C CA  1 
ATOM   10610 C C   . VAL C  1 303 ? -6.922  -0.105  -51.362  1.00 28.85  ? 303 VAL C C   1 
ATOM   10611 O O   . VAL C  1 303 ? -6.413  0.224   -50.287  1.00 25.53  ? 303 VAL C O   1 
ATOM   10612 C CB  . VAL C  1 303 ? -7.448  2.096   -52.447  1.00 30.27  ? 303 VAL C CB  1 
ATOM   10613 C CG1 . VAL C  1 303 ? -6.239  1.864   -53.371  1.00 32.27  ? 303 VAL C CG1 1 
ATOM   10614 C CG2 . VAL C  1 303 ? -8.508  2.927   -53.168  1.00 28.04  ? 303 VAL C CG2 1 
ATOM   10615 N N   . PHE C  1 304 ? -6.563  -1.189  -52.029  1.00 27.20  ? 304 PHE C N   1 
ATOM   10616 C CA  . PHE C  1 304 ? -5.385  -1.953  -51.684  1.00 24.76  ? 304 PHE C CA  1 
ATOM   10617 C C   . PHE C  1 304 ? -4.321  -1.720  -52.749  1.00 32.53  ? 304 PHE C C   1 
ATOM   10618 O O   . PHE C  1 304 ? -4.628  -1.495  -53.929  1.00 26.68  ? 304 PHE C O   1 
ATOM   10619 C CB  . PHE C  1 304 ? -5.707  -3.446  -51.577  1.00 25.72  ? 304 PHE C CB  1 
ATOM   10620 C CG  . PHE C  1 304 ? -6.397  -3.840  -50.290  1.00 26.13  ? 304 PHE C CG  1 
ATOM   10621 C CD1 . PHE C  1 304 ? -5.695  -3.927  -49.117  1.00 27.60  ? 304 PHE C CD1 1 
ATOM   10622 C CD2 . PHE C  1 304 ? -7.748  -4.160  -50.276  1.00 32.82  ? 304 PHE C CD2 1 
ATOM   10623 C CE1 . PHE C  1 304 ? -6.319  -4.311  -47.937  1.00 26.72  ? 304 PHE C CE1 1 
ATOM   10624 C CE2 . PHE C  1 304 ? -8.376  -4.546  -49.089  1.00 32.42  ? 304 PHE C CE2 1 
ATOM   10625 C CZ  . PHE C  1 304 ? -7.649  -4.629  -47.927  1.00 27.89  ? 304 PHE C CZ  1 
ATOM   10626 N N   . PHE C  1 305 ? -3.068  -1.748  -52.325  1.00 35.74  ? 305 PHE C N   1 
ATOM   10627 C CA  . PHE C  1 305 ? -1.944  -1.615  -53.238  1.00 32.67  ? 305 PHE C CA  1 
ATOM   10628 C C   . PHE C  1 305 ? -1.195  -2.936  -53.238  1.00 31.54  ? 305 PHE C C   1 
ATOM   10629 O O   . PHE C  1 305 ? -0.764  -3.411  -52.180  1.00 33.69  ? 305 PHE C O   1 
ATOM   10630 C CB  . PHE C  1 305 ? -1.038  -0.455  -52.834  1.00 34.58  ? 305 PHE C CB  1 
ATOM   10631 C CG  . PHE C  1 305 ? -1.733  0.869   -52.829  1.00 39.64  ? 305 PHE C CG  1 
ATOM   10632 C CD1 . PHE C  1 305 ? -2.421  1.303   -51.701  1.00 38.56  ? 305 PHE C CD1 1 
ATOM   10633 C CD2 . PHE C  1 305 ? -1.715  1.681   -53.957  1.00 38.94  ? 305 PHE C CD2 1 
ATOM   10634 C CE1 . PHE C  1 305 ? -3.064  2.516   -51.695  1.00 36.55  ? 305 PHE C CE1 1 
ATOM   10635 C CE2 . PHE C  1 305 ? -2.356  2.898   -53.951  1.00 36.39  ? 305 PHE C CE2 1 
ATOM   10636 C CZ  . PHE C  1 305 ? -3.037  3.316   -52.821  1.00 37.20  ? 305 PHE C CZ  1 
ATOM   10637 N N   . ARG C  1 306 ? -1.081  -3.540  -54.419  1.00 27.08  ? 306 ARG C N   1 
ATOM   10638 C CA  . ARG C  1 306 ? -0.469  -4.845  -54.555  1.00 27.53  ? 306 ARG C CA  1 
ATOM   10639 C C   . ARG C  1 306 ? 1.005   -4.788  -54.175  1.00 36.30  ? 306 ARG C C   1 
ATOM   10640 O O   . ARG C  1 306 ? 1.655   -3.735  -54.233  1.00 32.90  ? 306 ARG C O   1 
ATOM   10641 C CB  . ARG C  1 306 ? -0.613  -5.349  -55.994  1.00 33.33  ? 306 ARG C CB  1 
ATOM   10642 C CG  . ARG C  1 306 ? 0.396   -4.718  -56.940  1.00 35.24  ? 306 ARG C CG  1 
ATOM   10643 C CD  . ARG C  1 306 ? 0.399   -5.369  -58.320  1.00 34.80  ? 306 ARG C CD  1 
ATOM   10644 N NE  . ARG C  1 306 ? 1.424   -4.746  -59.152  1.00 30.49  ? 306 ARG C NE  1 
ATOM   10645 C CZ  . ARG C  1 306 ? 2.086   -5.357  -60.119  1.00 31.99  ? 306 ARG C CZ  1 
ATOM   10646 N NH1 . ARG C  1 306 ? 1.838   -6.634  -60.409  1.00 31.55  ? 306 ARG C NH1 1 
ATOM   10647 N NH2 . ARG C  1 306 ? 3.008   -4.684  -60.790  1.00 36.14  ? 306 ARG C NH2 1 
ATOM   10648 N N   . ASP C  1 307 ? 1.529   -5.949  -53.773  1.00 36.84  ? 307 ASP C N   1 
ATOM   10649 C CA  . ASP C  1 307 ? 2.959   -6.132  -53.566  1.00 36.83  ? 307 ASP C CA  1 
ATOM   10650 C C   . ASP C  1 307 ? 3.587   -6.365  -54.931  1.00 34.30  ? 307 ASP C C   1 
ATOM   10651 O O   . ASP C  1 307 ? 3.507   -7.460  -55.492  1.00 31.21  ? 307 ASP C O   1 
ATOM   10652 C CB  . ASP C  1 307 ? 3.228   -7.296  -52.619  1.00 36.23  ? 307 ASP C CB  1 
ATOM   10653 C CG  . ASP C  1 307 ? 4.659   -7.330  -52.132  1.00 40.39  ? 307 ASP C CG  1 
ATOM   10654 O OD1 . ASP C  1 307 ? 5.589   -7.238  -52.963  1.00 41.38  ? 307 ASP C OD1 1 
ATOM   10655 O OD2 . ASP C  1 307 ? 4.851   -7.435  -50.905  1.00 42.30  ? 307 ASP C OD2 1 
ATOM   10656 N N   . LYS C  1 308 ? 4.224   -5.323  -55.461  1.00 37.18  ? 308 LYS C N   1 
ATOM   10657 C CA  . LYS C  1 308 ? 4.797   -5.397  -56.798  1.00 33.33  ? 308 LYS C CA  1 
ATOM   10658 C C   . LYS C  1 308 ? 5.894   -6.451  -56.874  1.00 34.74  ? 308 LYS C C   1 
ATOM   10659 O O   . LYS C  1 308 ? 6.032   -7.150  -57.886  1.00 30.34  ? 308 LYS C O   1 
ATOM   10660 C CB  . LYS C  1 308 ? 5.338   -4.024  -57.194  1.00 31.13  ? 308 LYS C CB  1 
ATOM   10661 C CG  . LYS C  1 308 ? 5.895   -3.962  -58.591  1.00 35.37  ? 308 LYS C CG  1 
ATOM   10662 C CD  . LYS C  1 308 ? 6.783   -2.760  -58.783  1.00 41.33  ? 308 LYS C CD  1 
ATOM   10663 C CE  . LYS C  1 308 ? 7.719   -2.974  -59.964  1.00 43.72  ? 308 LYS C CE  1 
ATOM   10664 N NZ  . LYS C  1 308 ? 7.014   -3.533  -61.151  1.00 42.21  ? 308 LYS C NZ  1 
ATOM   10665 N N   . THR C  1 309 ? 6.692   -6.584  -55.816  1.00 34.34  ? 309 THR C N   1 
ATOM   10666 C CA  . THR C  1 309 ? 7.798   -7.524  -55.878  1.00 35.43  ? 309 THR C CA  1 
ATOM   10667 C C   . THR C  1 309 ? 7.294   -8.964  -55.929  1.00 33.80  ? 309 THR C C   1 
ATOM   10668 O O   . THR C  1 309 ? 7.766   -9.770  -56.738  1.00 32.57  ? 309 THR C O   1 
ATOM   10669 C CB  . THR C  1 309 ? 8.730   -7.305  -54.692  1.00 41.04  ? 309 THR C CB  1 
ATOM   10670 O OG1 . THR C  1 309 ? 9.310   -5.998  -54.789  1.00 43.03  ? 309 THR C OG1 1 
ATOM   10671 C CG2 . THR C  1 309 ? 9.833   -8.341  -54.693  1.00 41.47  ? 309 THR C CG2 1 
ATOM   10672 N N   . LEU C  1 310 ? 6.326   -9.306  -55.080  1.00 33.02  ? 310 LEU C N   1 
ATOM   10673 C CA  . LEU C  1 310 ? 5.804   -10.671 -55.090  1.00 34.29  ? 310 LEU C CA  1 
ATOM   10674 C C   . LEU C  1 310 ? 5.044   -10.959 -56.375  1.00 32.58  ? 310 LEU C C   1 
ATOM   10675 O O   . LEU C  1 310 ? 5.095   -12.077 -56.899  1.00 31.29  ? 310 LEU C O   1 
ATOM   10676 C CB  . LEU C  1 310 ? 4.900   -10.895 -53.885  1.00 33.50  ? 310 LEU C CB  1 
ATOM   10677 C CG  . LEU C  1 310 ? 5.594   -10.744 -52.537  1.00 33.50  ? 310 LEU C CG  1 
ATOM   10678 C CD1 . LEU C  1 310 ? 4.552   -10.862 -51.467  1.00 31.14  ? 310 LEU C CD1 1 
ATOM   10679 C CD2 . LEU C  1 310 ? 6.681   -11.798 -52.384  1.00 34.30  ? 310 LEU C CD2 1 
ATOM   10680 N N   . SER C  1 311 ? 4.334   -9.961  -56.891  1.00 36.22  ? 311 SER C N   1 
ATOM   10681 C CA  . SER C  1 311 ? 3.587   -10.151 -58.122  1.00 36.12  ? 311 SER C CA  1 
ATOM   10682 C C   . SER C  1 311 ? 4.521   -10.344 -59.313  1.00 34.56  ? 311 SER C C   1 
ATOM   10683 O O   . SER C  1 311 ? 4.298   -11.233 -60.141  1.00 34.74  ? 311 SER C O   1 
ATOM   10684 C CB  . SER C  1 311 ? 2.658   -8.962  -58.337  1.00 36.65  ? 311 SER C CB  1 
ATOM   10685 O OG  . SER C  1 311 ? 1.630   -8.951  -57.360  1.00 37.72  ? 311 SER C OG  1 
ATOM   10686 N N   . ASP C  1 312 ? 5.572   -9.522  -59.411  1.00 36.29  ? 312 ASP C N   1 
ATOM   10687 C CA  . ASP C  1 312 ? 6.516   -9.625  -60.523  1.00 36.88  ? 312 ASP C CA  1 
ATOM   10688 C C   . ASP C  1 312 ? 7.313   -10.920 -60.461  1.00 38.56  ? 312 ASP C C   1 
ATOM   10689 O O   . ASP C  1 312 ? 7.664   -11.488 -61.503  1.00 37.62  ? 312 ASP C O   1 
ATOM   10690 C CB  . ASP C  1 312 ? 7.475   -8.434  -60.523  1.00 35.51  ? 312 ASP C CB  1 
ATOM   10691 C CG  . ASP C  1 312 ? 6.808   -7.145  -60.935  1.00 34.63  ? 312 ASP C CG  1 
ATOM   10692 O OD1 . ASP C  1 312 ? 5.646   -7.193  -61.391  1.00 35.15  ? 312 ASP C OD1 1 
ATOM   10693 O OD2 . ASP C  1 312 ? 7.452   -6.084  -60.807  1.00 36.37  ? 312 ASP C OD2 1 
ATOM   10694 N N   . LEU C  1 313 ? 7.642   -11.379 -59.251  1.00 39.89  ? 313 LEU C N   1 
ATOM   10695 C CA  . LEU C  1 313 ? 8.345   -12.649 -59.111  1.00 38.52  ? 313 LEU C CA  1 
ATOM   10696 C C   . LEU C  1 313 ? 7.567   -13.772 -59.782  1.00 37.95  ? 313 LEU C C   1 
ATOM   10697 O O   . LEU C  1 313 ? 8.126   -14.548 -60.565  1.00 37.66  ? 313 LEU C O   1 
ATOM   10698 C CB  . LEU C  1 313 ? 8.580   -12.966 -57.634  1.00 38.12  ? 313 LEU C CB  1 
ATOM   10699 C CG  . LEU C  1 313 ? 9.751   -12.239 -56.962  1.00 37.58  ? 313 LEU C CG  1 
ATOM   10700 C CD1 . LEU C  1 313 ? 9.686   -12.369 -55.455  1.00 35.53  ? 313 LEU C CD1 1 
ATOM   10701 C CD2 . LEU C  1 313 ? 11.098  -12.714 -57.489  1.00 39.18  ? 313 LEU C CD2 1 
ATOM   10702 N N   . ILE C  1 314 ? 6.271   -13.877 -59.484  1.00 33.47  ? 314 ILE C N   1 
ATOM   10703 C CA  . ILE C  1 314 ? 5.470   -14.903 -60.133  1.00 33.76  ? 314 ILE C CA  1 
ATOM   10704 C C   . ILE C  1 314 ? 5.386   -14.621 -61.627  1.00 36.12  ? 314 ILE C C   1 
ATOM   10705 O O   . ILE C  1 314 ? 5.549   -15.526 -62.456  1.00 35.65  ? 314 ILE C O   1 
ATOM   10706 C CB  . ILE C  1 314 ? 4.074   -14.996 -59.487  1.00 29.80  ? 314 ILE C CB  1 
ATOM   10707 C CG1 . ILE C  1 314 ? 4.148   -15.597 -58.080  1.00 33.14  ? 314 ILE C CG1 1 
ATOM   10708 C CG2 . ILE C  1 314 ? 3.138   -15.847 -60.353  1.00 30.85  ? 314 ILE C CG2 1 
ATOM   10709 C CD1 . ILE C  1 314 ? 2.772   -15.724 -57.422  1.00 29.98  ? 314 ILE C CD1 1 
ATOM   10710 N N   . GLY C  1 315 ? 5.188   -13.354 -61.998  1.00 35.79  ? 315 GLY C N   1 
ATOM   10711 C CA  . GLY C  1 315 ? 4.961   -13.035 -63.399  1.00 37.17  ? 315 GLY C CA  1 
ATOM   10712 C C   . GLY C  1 315 ? 6.204   -13.024 -64.269  1.00 37.49  ? 315 GLY C C   1 
ATOM   10713 O O   . GLY C  1 315 ? 6.122   -13.323 -65.464  1.00 39.71  ? 315 GLY C O   1 
ATOM   10714 N N   . PHE C  1 316 ? 7.365   -12.678 -63.701  1.00 35.73  ? 316 PHE C N   1 
ATOM   10715 C CA  . PHE C  1 316 ? 8.556   -12.411 -64.502  1.00 34.31  ? 316 PHE C CA  1 
ATOM   10716 C C   . PHE C  1 316 ? 9.713   -13.365 -64.260  1.00 38.67  ? 316 PHE C C   1 
ATOM   10717 O O   . PHE C  1 316 ? 10.511  -13.575 -65.177  1.00 40.84  ? 316 PHE C O   1 
ATOM   10718 C CB  . PHE C  1 316 ? 9.066   -10.981 -64.260  1.00 37.67  ? 316 PHE C CB  1 
ATOM   10719 C CG  . PHE C  1 316 ? 8.130   -9.914  -64.750  1.00 41.74  ? 316 PHE C CG  1 
ATOM   10720 C CD1 . PHE C  1 316 ? 7.304   -10.146 -65.840  1.00 44.55  ? 316 PHE C CD1 1 
ATOM   10721 C CD2 . PHE C  1 316 ? 8.080   -8.672  -64.127  1.00 43.98  ? 316 PHE C CD2 1 
ATOM   10722 C CE1 . PHE C  1 316 ? 6.439   -9.165  -66.303  1.00 44.23  ? 316 PHE C CE1 1 
ATOM   10723 C CE2 . PHE C  1 316 ? 7.221   -7.680  -64.593  1.00 46.27  ? 316 PHE C CE2 1 
ATOM   10724 C CZ  . PHE C  1 316 ? 6.401   -7.928  -65.679  1.00 44.15  ? 316 PHE C CZ  1 
ATOM   10725 N N   . SER C  1 317 ? 9.836   -13.949 -63.068  1.00 36.81  ? 317 SER C N   1 
ATOM   10726 C CA  . SER C  1 317 ? 11.103  -14.583 -62.728  1.00 42.20  ? 317 SER C CA  1 
ATOM   10727 C C   . SER C  1 317 ? 11.033  -16.068 -62.403  1.00 37.48  ? 317 SER C C   1 
ATOM   10728 O O   . SER C  1 317 ? 11.916  -16.822 -62.816  1.00 35.93  ? 317 SER C O   1 
ATOM   10729 C CB  . SER C  1 317 ? 11.749  -13.829 -61.570  1.00 54.00  ? 317 SER C CB  1 
ATOM   10730 O OG  . SER C  1 317 ? 12.633  -12.868 -62.103  1.00 62.57  ? 317 SER C OG  1 
ATOM   10731 N N   . TYR C  1 318 ? 10.011  -16.494 -61.658  1.00 37.23  ? 318 TYR C N   1 
ATOM   10732 C CA  . TYR C  1 318 ? 9.972   -17.863 -61.148  1.00 38.32  ? 318 TYR C CA  1 
ATOM   10733 C C   . TYR C  1 318 ? 9.925   -18.913 -62.259  1.00 36.74  ? 318 TYR C C   1 
ATOM   10734 O O   . TYR C  1 318 ? 10.260  -20.079 -62.009  1.00 36.33  ? 318 TYR C O   1 
ATOM   10735 C CB  . TYR C  1 318 ? 8.770   -18.026 -60.211  1.00 35.78  ? 318 TYR C CB  1 
ATOM   10736 C CG  . TYR C  1 318 ? 8.981   -17.457 -58.823  1.00 36.14  ? 318 TYR C CG  1 
ATOM   10737 C CD1 . TYR C  1 318 ? 10.260  -17.128 -58.365  1.00 38.08  ? 318 TYR C CD1 1 
ATOM   10738 C CD2 . TYR C  1 318 ? 7.905   -17.254 -57.968  1.00 35.59  ? 318 TYR C CD2 1 
ATOM   10739 C CE1 . TYR C  1 318 ? 10.462  -16.613 -57.075  1.00 35.24  ? 318 TYR C CE1 1 
ATOM   10740 C CE2 . TYR C  1 318 ? 8.091   -16.736 -56.677  1.00 37.95  ? 318 TYR C CE2 1 
ATOM   10741 C CZ  . TYR C  1 318 ? 9.376   -16.418 -56.242  1.00 38.92  ? 318 TYR C CZ  1 
ATOM   10742 O OH  . TYR C  1 318 ? 9.580   -15.906 -54.979  1.00 40.72  ? 318 TYR C OH  1 
ATOM   10743 N N   . HIS C  1 319 ? 9.532   -18.529 -63.479  1.00 36.68  ? 319 HIS C N   1 
ATOM   10744 C CA  . HIS C  1 319 ? 9.533   -19.476 -64.593  1.00 36.56  ? 319 HIS C CA  1 
ATOM   10745 C C   . HIS C  1 319 ? 10.899  -20.134 -64.773  1.00 38.85  ? 319 HIS C C   1 
ATOM   10746 O O   . HIS C  1 319 ? 10.981  -21.294 -65.198  1.00 37.24  ? 319 HIS C O   1 
ATOM   10747 C CB  . HIS C  1 319 ? 9.118   -18.775 -65.896  1.00 31.70  ? 319 HIS C CB  1 
ATOM   10748 C CG  . HIS C  1 319 ? 10.190  -17.903 -66.467  1.00 34.89  ? 319 HIS C CG  1 
ATOM   10749 N ND1 . HIS C  1 319 ? 10.355  -16.588 -66.095  1.00 37.12  ? 319 HIS C ND1 1 
ATOM   10750 C CD2 . HIS C  1 319 ? 11.177  -18.168 -67.355  1.00 38.72  ? 319 HIS C CD2 1 
ATOM   10751 C CE1 . HIS C  1 319 ? 11.387  -16.075 -66.740  1.00 38.91  ? 319 HIS C CE1 1 
ATOM   10752 N NE2 . HIS C  1 319 ? 11.905  -17.015 -67.510  1.00 38.07  ? 319 HIS C NE2 1 
ATOM   10753 N N   . ALA C  1 320 ? 11.976  -19.421 -64.449  1.00 34.17  ? 320 ALA C N   1 
ATOM   10754 C CA  . ALA C  1 320 ? 13.321  -19.933 -64.652  1.00 39.13  ? 320 ALA C CA  1 
ATOM   10755 C C   . ALA C  1 320 ? 13.847  -20.700 -63.451  1.00 44.10  ? 320 ALA C C   1 
ATOM   10756 O O   . ALA C  1 320 ? 14.960  -21.236 -63.516  1.00 45.57  ? 320 ALA C O   1 
ATOM   10757 C CB  . ALA C  1 320 ? 14.277  -18.787 -64.990  1.00 41.92  ? 320 ALA C CB  1 
ATOM   10758 N N   . TRP C  1 321 ? 13.075  -20.767 -62.371  1.00 46.12  ? 321 TRP C N   1 
ATOM   10759 C CA  . TRP C  1 321 ? 13.483  -21.405 -61.130  1.00 47.40  ? 321 TRP C CA  1 
ATOM   10760 C C   . TRP C  1 321 ? 12.926  -22.815 -61.039  1.00 44.45  ? 321 TRP C C   1 
ATOM   10761 O O   . TRP C  1 321 ? 11.855  -23.123 -61.577  1.00 44.09  ? 321 TRP C O   1 
ATOM   10762 C CB  . TRP C  1 321 ? 12.990  -20.624 -59.907  1.00 49.84  ? 321 TRP C CB  1 
ATOM   10763 C CG  . TRP C  1 321 ? 13.500  -19.232 -59.747  1.00 52.09  ? 321 TRP C CG  1 
ATOM   10764 C CD1 . TRP C  1 321 ? 13.719  -18.312 -60.729  1.00 52.98  ? 321 TRP C CD1 1 
ATOM   10765 C CD2 . TRP C  1 321 ? 13.833  -18.592 -58.513  1.00 53.89  ? 321 TRP C CD2 1 
ATOM   10766 N NE1 . TRP C  1 321 ? 14.174  -17.136 -60.182  1.00 55.15  ? 321 TRP C NE1 1 
ATOM   10767 C CE2 . TRP C  1 321 ? 14.255  -17.284 -58.821  1.00 56.55  ? 321 TRP C CE2 1 
ATOM   10768 C CE3 . TRP C  1 321 ? 13.823  -19.001 -57.177  1.00 54.72  ? 321 TRP C CE3 1 
ATOM   10769 C CZ2 . TRP C  1 321 ? 14.663  -16.381 -57.841  1.00 57.97  ? 321 TRP C CZ2 1 
ATOM   10770 C CZ3 . TRP C  1 321 ? 14.228  -18.106 -56.204  1.00 55.82  ? 321 TRP C CZ3 1 
ATOM   10771 C CH2 . TRP C  1 321 ? 14.639  -16.810 -56.540  1.00 57.53  ? 321 TRP C CH2 1 
ATOM   10772 N N   . ASN C  1 322 ? 13.658  -23.665 -60.329  1.00 44.54  ? 322 ASN C N   1 
ATOM   10773 C CA  . ASN C  1 322 ? 13.062  -24.875 -59.795  1.00 48.51  ? 322 ASN C CA  1 
ATOM   10774 C C   . ASN C  1 322 ? 11.837  -24.510 -58.961  1.00 48.84  ? 322 ASN C C   1 
ATOM   10775 O O   . ASN C  1 322 ? 11.812  -23.468 -58.299  1.00 51.38  ? 322 ASN C O   1 
ATOM   10776 C CB  . ASN C  1 322 ? 14.100  -25.628 -58.961  1.00 53.49  ? 322 ASN C CB  1 
ATOM   10777 C CG  . ASN C  1 322 ? 13.587  -26.939 -58.442  1.00 59.27  ? 322 ASN C CG  1 
ATOM   10778 O OD1 . ASN C  1 322 ? 13.069  -27.014 -57.332  1.00 62.16  ? 322 ASN C OD1 1 
ATOM   10779 N ND2 . ASN C  1 322 ? 13.711  -27.985 -59.248  1.00 65.43  ? 322 ASN C ND2 1 
ATOM   10780 N N   . ALA C  1 323 ? 10.801  -25.355 -59.018  1.00 52.13  ? 323 ALA C N   1 
ATOM   10781 C CA  . ALA C  1 323 ? 9.546   -25.022 -58.348  1.00 47.48  ? 323 ALA C CA  1 
ATOM   10782 C C   . ALA C  1 323 ? 9.706   -24.981 -56.829  1.00 51.99  ? 323 ALA C C   1 
ATOM   10783 O O   . ALA C  1 323 ? 9.165   -24.085 -56.169  1.00 52.15  ? 323 ALA C O   1 
ATOM   10784 C CB  . ALA C  1 323 ? 8.457   -26.016 -58.737  1.00 41.11  ? 323 ALA C CB  1 
ATOM   10785 N N   . GLU C  1 324 ? 10.429  -25.941 -56.248  1.00 55.20  ? 324 GLU C N   1 
ATOM   10786 C CA  . GLU C  1 324 ? 10.584  -25.942 -54.795  1.00 57.49  ? 324 GLU C CA  1 
ATOM   10787 C C   . GLU C  1 324 ? 11.403  -24.744 -54.325  1.00 51.78  ? 324 GLU C C   1 
ATOM   10788 O O   . GLU C  1 324 ? 11.099  -24.149 -53.282  1.00 49.19  ? 324 GLU C O   1 
ATOM   10789 C CB  . GLU C  1 324 ? 11.206  -27.256 -54.331  1.00 68.99  ? 324 GLU C CB  1 
ATOM   10790 C CG  . GLU C  1 324 ? 10.443  -28.472 -54.814  1.00 75.84  ? 324 GLU C CG  1 
ATOM   10791 C CD  . GLU C  1 324 ? 10.120  -29.458 -53.710  1.00 83.81  ? 324 GLU C CD  1 
ATOM   10792 O OE1 . GLU C  1 324 ? 10.585  -30.618 -53.807  1.00 87.06  ? 324 GLU C OE1 1 
ATOM   10793 O OE2 . GLU C  1 324 ? 9.396   -29.081 -52.760  1.00 84.85  ? 324 GLU C OE2 1 
ATOM   10794 N N   . ASP C  1 325 ? 12.427  -24.359 -55.089  1.00 48.63  ? 325 ASP C N   1 
ATOM   10795 C CA  . ASP C  1 325 ? 13.176  -23.148 -54.758  1.00 50.61  ? 325 ASP C CA  1 
ATOM   10796 C C   . ASP C  1 325 ? 12.299  -21.905 -54.861  1.00 48.69  ? 325 ASP C C   1 
ATOM   10797 O O   . ASP C  1 325 ? 12.368  -21.011 -54.005  1.00 42.95  ? 325 ASP C O   1 
ATOM   10798 C CB  . ASP C  1 325 ? 14.385  -23.013 -55.677  1.00 55.23  ? 325 ASP C CB  1 
ATOM   10799 C CG  . ASP C  1 325 ? 15.291  -24.210 -55.615  1.00 66.02  ? 325 ASP C CG  1 
ATOM   10800 O OD1 . ASP C  1 325 ? 15.192  -24.968 -54.628  1.00 72.65  ? 325 ASP C OD1 1 
ATOM   10801 O OD2 . ASP C  1 325 ? 16.092  -24.398 -56.554  1.00 67.62  ? 325 ASP C OD2 1 
ATOM   10802 N N   . ALA C  1 326 ? 11.478  -21.825 -55.913  1.00 44.40  ? 326 ALA C N   1 
ATOM   10803 C CA  . ALA C  1 326 ? 10.598  -20.676 -56.078  1.00 42.54  ? 326 ALA C CA  1 
ATOM   10804 C C   . ALA C  1 326 ? 9.634   -20.542 -54.905  1.00 41.65  ? 326 ALA C C   1 
ATOM   10805 O O   . ALA C  1 326 ? 9.434   -19.441 -54.375  1.00 41.58  ? 326 ALA C O   1 
ATOM   10806 C CB  . ALA C  1 326 ? 9.830   -20.787 -57.399  1.00 41.78  ? 326 ALA C CB  1 
ATOM   10807 N N   . VAL C  1 327 ? 9.010   -21.647 -54.491  1.00 42.33  ? 327 VAL C N   1 
ATOM   10808 C CA  . VAL C  1 327 ? 8.008   -21.560 -53.429  1.00 42.61  ? 327 VAL C CA  1 
ATOM   10809 C C   . VAL C  1 327 ? 8.673   -21.251 -52.090  1.00 43.00  ? 327 VAL C C   1 
ATOM   10810 O O   . VAL C  1 327 ? 8.126   -20.503 -51.269  1.00 40.61  ? 327 VAL C O   1 
ATOM   10811 C CB  . VAL C  1 327 ? 7.161   -22.847 -53.373  1.00 46.12  ? 327 VAL C CB  1 
ATOM   10812 C CG1 . VAL C  1 327 ? 6.260   -22.858 -52.130  1.00 48.24  ? 327 VAL C CG1 1 
ATOM   10813 C CG2 . VAL C  1 327 ? 6.312   -22.985 -54.642  1.00 44.88  ? 327 VAL C CG2 1 
ATOM   10814 N N   . ARG C  1 328 ? 9.867   -21.806 -51.850  1.00 45.08  ? 328 ARG C N   1 
ATOM   10815 C CA  . ARG C  1 328 ? 10.589  -21.474 -50.624  1.00 44.98  ? 328 ARG C CA  1 
ATOM   10816 C C   . ARG C  1 328 ? 10.912  -19.986 -50.577  1.00 49.50  ? 328 ARG C C   1 
ATOM   10817 O O   . ARG C  1 328 ? 10.759  -19.341 -49.531  1.00 47.83  ? 328 ARG C O   1 
ATOM   10818 C CB  . ARG C  1 328 ? 11.865  -22.308 -50.512  1.00 49.17  ? 328 ARG C CB  1 
ATOM   10819 C CG  . ARG C  1 328 ? 12.792  -21.883 -49.372  1.00 57.66  ? 328 ARG C CG  1 
ATOM   10820 C CD  . ARG C  1 328 ? 14.106  -22.638 -49.420  1.00 61.03  ? 328 ARG C CD  1 
ATOM   10821 N NE  . ARG C  1 328 ? 13.947  -23.898 -50.136  1.00 67.38  ? 328 ARG C NE  1 
ATOM   10822 C CZ  . ARG C  1 328 ? 14.631  -24.233 -51.226  1.00 68.64  ? 328 ARG C CZ  1 
ATOM   10823 N NH1 . ARG C  1 328 ? 15.538  -23.400 -51.725  1.00 68.64  ? 328 ARG C NH1 1 
ATOM   10824 N NH2 . ARG C  1 328 ? 14.415  -25.405 -51.808  1.00 67.27  ? 328 ARG C NH2 1 
ATOM   10825 N N   . ASP C  1 329 ? 11.318  -19.415 -51.717  1.00 46.74  ? 329 ASP C N   1 
ATOM   10826 C CA  . ASP C  1 329 ? 11.630  -17.991 -51.774  1.00 45.43  ? 329 ASP C CA  1 
ATOM   10827 C C   . ASP C  1 329 ? 10.387  -17.153 -51.505  1.00 44.71  ? 329 ASP C C   1 
ATOM   10828 O O   . ASP C  1 329 ? 10.447  -16.124 -50.816  1.00 41.18  ? 329 ASP C O   1 
ATOM   10829 C CB  . ASP C  1 329 ? 12.230  -17.655 -53.144  1.00 45.42  ? 329 ASP C CB  1 
ATOM   10830 C CG  . ASP C  1 329 ? 12.685  -16.204 -53.256  1.00 50.17  ? 329 ASP C CG  1 
ATOM   10831 O OD1 . ASP C  1 329 ? 11.862  -15.347 -53.645  1.00 47.50  ? 329 ASP C OD1 1 
ATOM   10832 O OD2 . ASP C  1 329 ? 13.863  -15.916 -52.957  1.00 52.26  ? 329 ASP C OD2 1 
ATOM   10833 N N   . PHE C  1 330 ? 9.246   -17.588 -52.037  1.00 46.39  ? 330 PHE C N   1 
ATOM   10834 C CA  . PHE C  1 330 ? 8.007   -16.831 -51.897  1.00 43.02  ? 330 PHE C CA  1 
ATOM   10835 C C   . PHE C  1 330 ? 7.507   -16.877 -50.460  1.00 42.15  ? 330 PHE C C   1 
ATOM   10836 O O   . PHE C  1 330 ? 7.187   -15.839 -49.873  1.00 41.95  ? 330 PHE C O   1 
ATOM   10837 C CB  . PHE C  1 330 ? 6.966   -17.398 -52.859  1.00 36.25  ? 330 PHE C CB  1 
ATOM   10838 C CG  . PHE C  1 330 ? 5.717   -16.587 -52.964  1.00 34.82  ? 330 PHE C CG  1 
ATOM   10839 C CD1 . PHE C  1 330 ? 5.625   -15.548 -53.877  1.00 34.27  ? 330 PHE C CD1 1 
ATOM   10840 C CD2 . PHE C  1 330 ? 4.621   -16.885 -52.172  1.00 36.55  ? 330 PHE C CD2 1 
ATOM   10841 C CE1 . PHE C  1 330 ? 4.456   -14.801 -53.993  1.00 36.82  ? 330 PHE C CE1 1 
ATOM   10842 C CE2 . PHE C  1 330 ? 3.456   -16.149 -52.266  1.00 38.42  ? 330 PHE C CE2 1 
ATOM   10843 C CZ  . PHE C  1 330 ? 3.367   -15.096 -53.185  1.00 36.75  ? 330 PHE C CZ  1 
ATOM   10844 N N   . ILE C  1 331 ? 7.432   -18.082 -49.880  1.00 45.17  ? 331 ILE C N   1 
ATOM   10845 C CA  . ILE C  1 331 ? 7.048   -18.232 -48.478  1.00 50.54  ? 331 ILE C CA  1 
ATOM   10846 C C   . ILE C  1 331 ? 8.035   -17.515 -47.572  1.00 50.96  ? 331 ILE C C   1 
ATOM   10847 O O   . ILE C  1 331 ? 7.651   -16.959 -46.534  1.00 47.37  ? 331 ILE C O   1 
ATOM   10848 C CB  . ILE C  1 331 ? 6.939   -19.724 -48.102  1.00 56.74  ? 331 ILE C CB  1 
ATOM   10849 C CG1 . ILE C  1 331 ? 5.939   -20.449 -49.010  1.00 55.68  ? 331 ILE C CG1 1 
ATOM   10850 C CG2 . ILE C  1 331 ? 6.541   -19.876 -46.642  1.00 59.94  ? 331 ILE C CG2 1 
ATOM   10851 C CD1 . ILE C  1 331 ? 4.511   -20.087 -48.753  1.00 51.40  ? 331 ILE C CD1 1 
ATOM   10852 N N   . GLY C  1 332 ? 9.317   -17.513 -47.942  1.00 53.48  ? 332 GLY C N   1 
ATOM   10853 C CA  . GLY C  1 332 ? 10.311  -16.823 -47.139  1.00 56.26  ? 332 GLY C CA  1 
ATOM   10854 C C   . GLY C  1 332 ? 10.111  -15.322 -47.111  1.00 51.25  ? 332 GLY C C   1 
ATOM   10855 O O   . GLY C  1 332 ? 10.384  -14.677 -46.093  1.00 45.23  ? 332 GLY C O   1 
ATOM   10856 N N   . ARG C  1 333 ? 9.646   -14.742 -48.221  1.00 46.26  ? 333 ARG C N   1 
ATOM   10857 C CA  . ARG C  1 333 ? 9.341   -13.313 -48.234  1.00 46.60  ? 333 ARG C CA  1 
ATOM   10858 C C   . ARG C  1 333 ? 8.089   -13.003 -47.421  1.00 44.72  ? 333 ARG C C   1 
ATOM   10859 O O   . ARG C  1 333 ? 8.028   -11.973 -46.739  1.00 44.99  ? 333 ARG C O   1 
ATOM   10860 C CB  . ARG C  1 333 ? 9.186   -12.817 -49.670  1.00 47.46  ? 333 ARG C CB  1 
ATOM   10861 C CG  . ARG C  1 333 ? 10.456  -12.928 -50.475  1.00 47.60  ? 333 ARG C CG  1 
ATOM   10862 C CD  . ARG C  1 333 ? 10.266  -12.378 -51.852  1.00 44.99  ? 333 ARG C CD  1 
ATOM   10863 N NE  . ARG C  1 333 ? 11.382  -12.742 -52.712  1.00 48.09  ? 333 ARG C NE  1 
ATOM   10864 C CZ  . ARG C  1 333 ? 12.406  -11.943 -52.975  1.00 49.73  ? 333 ARG C CZ  1 
ATOM   10865 N NH1 . ARG C  1 333 ? 12.445  -10.726 -52.437  1.00 47.41  ? 333 ARG C NH1 1 
ATOM   10866 N NH2 . ARG C  1 333 ? 13.382  -12.357 -53.776  1.00 52.15  ? 333 ARG C NH2 1 
ATOM   10867 N N   . LEU C  1 334 ? 7.076   -13.869 -47.498  1.00 39.41  ? 334 LEU C N   1 
ATOM   10868 C CA  . LEU C  1 334 ? 5.898   -13.715 -46.652  1.00 38.95  ? 334 LEU C CA  1 
ATOM   10869 C C   . LEU C  1 334 ? 6.264   -13.846 -45.179  1.00 46.88  ? 334 LEU C C   1 
ATOM   10870 O O   . LEU C  1 334 ? 5.727   -13.122 -44.332  1.00 49.27  ? 334 LEU C O   1 
ATOM   10871 C CB  . LEU C  1 334 ? 4.844   -14.752 -47.036  1.00 37.87  ? 334 LEU C CB  1 
ATOM   10872 C CG  . LEU C  1 334 ? 4.230   -14.626 -48.430  1.00 35.85  ? 334 LEU C CG  1 
ATOM   10873 C CD1 . LEU C  1 334 ? 3.206   -15.731 -48.649  1.00 36.67  ? 334 LEU C CD1 1 
ATOM   10874 C CD2 . LEU C  1 334 ? 3.591   -13.265 -48.598  1.00 34.66  ? 334 LEU C CD2 1 
ATOM   10875 N N   . LYS C  1 335 ? 7.170   -14.774 -44.856  1.00 48.56  ? 335 LYS C N   1 
ATOM   10876 C CA  . LYS C  1 335 ? 7.698   -14.872 -43.494  1.00 55.55  ? 335 LYS C CA  1 
ATOM   10877 C C   . LYS C  1 335 ? 8.287   -13.539 -43.044  1.00 54.94  ? 335 LYS C C   1 
ATOM   10878 O O   . LYS C  1 335 ? 7.978   -13.041 -41.953  1.00 54.78  ? 335 LYS C O   1 
ATOM   10879 C CB  . LYS C  1 335 ? 8.765   -15.974 -43.411  1.00 61.68  ? 335 LYS C CB  1 
ATOM   10880 C CG  . LYS C  1 335 ? 8.242   -17.398 -43.183  1.00 68.54  ? 335 LYS C CG  1 
ATOM   10881 C CD  . LYS C  1 335 ? 9.386   -18.416 -42.991  1.00 74.03  ? 335 LYS C CD  1 
ATOM   10882 C CE  . LYS C  1 335 ? 9.252   -19.646 -43.907  1.00 72.99  ? 335 LYS C CE  1 
ATOM   10883 N NZ  . LYS C  1 335 ? 8.236   -20.643 -43.457  1.00 71.87  ? 335 LYS C NZ  1 
ATOM   10884 N N   . LYS C  1 336 ? 9.133   -12.944 -43.889  1.00 54.44  ? 336 LYS C N   1 
ATOM   10885 C CA  . LYS C  1 336 ? 9.789   -11.688 -43.546  1.00 53.72  ? 336 LYS C CA  1 
ATOM   10886 C C   . LYS C  1 336 ? 8.776   -10.554 -43.405  1.00 52.52  ? 336 LYS C C   1 
ATOM   10887 O O   . LYS C  1 336 ? 8.929   -9.678  -42.545  1.00 54.27  ? 336 LYS C O   1 
ATOM   10888 C CB  . LYS C  1 336 ? 10.845  -11.365 -44.607  1.00 52.15  ? 336 LYS C CB  1 
ATOM   10889 C CG  . LYS C  1 336 ? 11.494  -10.001 -44.482  1.00 56.23  ? 336 LYS C CG  1 
ATOM   10890 C CD  . LYS C  1 336 ? 12.155  -9.605  -45.790  1.00 61.32  ? 336 LYS C CD  1 
ATOM   10891 C CE  . LYS C  1 336 ? 11.251  -9.955  -46.976  1.00 61.48  ? 336 LYS C CE  1 
ATOM   10892 N NZ  . LYS C  1 336 ? 11.936  -9.887  -48.303  1.00 63.29  ? 336 LYS C NZ  1 
ATOM   10893 N N   . ILE C  1 337 ? 7.726   -10.558 -44.231  1.00 47.24  ? 337 ILE C N   1 
ATOM   10894 C CA  . ILE C  1 337 ? 6.675   -9.555  -44.072  1.00 47.07  ? 337 ILE C CA  1 
ATOM   10895 C C   . ILE C  1 337 ? 5.921   -9.770  -42.764  1.00 44.06  ? 337 ILE C C   1 
ATOM   10896 O O   . ILE C  1 337 ? 5.616   -8.814  -42.048  1.00 42.26  ? 337 ILE C O   1 
ATOM   10897 C CB  . ILE C  1 337 ? 5.709   -9.572  -45.270  1.00 42.48  ? 337 ILE C CB  1 
ATOM   10898 C CG1 . ILE C  1 337 ? 6.423   -9.158  -46.566  1.00 39.87  ? 337 ILE C CG1 1 
ATOM   10899 C CG2 . ILE C  1 337 ? 4.501   -8.676  -44.969  1.00 39.77  ? 337 ILE C CG2 1 
ATOM   10900 C CD1 . ILE C  1 337 ? 5.613   -9.431  -47.851  1.00 36.83  ? 337 ILE C CD1 1 
ATOM   10901 N N   . HIS C  1 338 ? 5.575   -11.024 -42.459  1.00 47.49  ? 338 HIS C N   1 
ATOM   10902 C CA  . HIS C  1 338 ? 4.837   -11.339 -41.241  1.00 51.15  ? 338 HIS C CA  1 
ATOM   10903 C C   . HIS C  1 338 ? 5.649   -10.999 -39.999  1.00 55.30  ? 338 HIS C C   1 
ATOM   10904 O O   . HIS C  1 338 ? 5.080   -10.640 -38.960  1.00 60.00  ? 338 HIS C O   1 
ATOM   10905 C CB  . HIS C  1 338 ? 4.452   -12.819 -41.269  1.00 53.13  ? 338 HIS C CB  1 
ATOM   10906 C CG  . HIS C  1 338 ? 3.854   -13.331 -39.997  1.00 52.88  ? 338 HIS C CG  1 
ATOM   10907 N ND1 . HIS C  1 338 ? 4.520   -14.206 -39.165  1.00 54.29  ? 338 HIS C ND1 1 
ATOM   10908 C CD2 . HIS C  1 338 ? 2.637   -13.131 -39.438  1.00 51.20  ? 338 HIS C CD2 1 
ATOM   10909 C CE1 . HIS C  1 338 ? 3.748   -14.504 -38.136  1.00 54.78  ? 338 HIS C CE1 1 
ATOM   10910 N NE2 . HIS C  1 338 ? 2.601   -13.865 -38.277  1.00 53.47  ? 338 HIS C NE2 1 
ATOM   10911 N N   . GLU C  1 339 ? 6.974   -11.075 -40.100  1.00 57.92  ? 339 GLU C N   1 
ATOM   10912 C CA  . GLU C  1 339 ? 7.873   -10.752 -39.002  1.00 64.20  ? 339 GLU C CA  1 
ATOM   10913 C C   . GLU C  1 339 ? 8.233   -9.270  -38.937  1.00 64.54  ? 339 GLU C C   1 
ATOM   10914 O O   . GLU C  1 339 ? 8.863   -8.847  -37.965  1.00 67.32  ? 339 GLU C O   1 
ATOM   10915 C CB  . GLU C  1 339 ? 9.162   -11.576 -39.120  1.00 72.21  ? 339 GLU C CB  1 
ATOM   10916 C CG  . GLU C  1 339 ? 9.043   -13.027 -38.674  1.00 81.31  ? 339 GLU C CG  1 
ATOM   10917 C CD  . GLU C  1 339 ? 10.222  -13.864 -39.136  1.00 92.11  ? 339 GLU C CD  1 
ATOM   10918 O OE1 . GLU C  1 339 ? 11.267  -13.270 -39.478  1.00 95.95  ? 339 GLU C OE1 1 
ATOM   10919 O OE2 . GLU C  1 339 ? 10.109  -15.110 -39.159  1.00 95.99  ? 339 GLU C OE2 1 
ATOM   10920 N N   . SER C  1 340 ? 7.852   -8.467  -39.932  1.00 60.66  ? 340 SER C N   1 
ATOM   10921 C CA  . SER C  1 340 ? 8.320   -7.086  -39.995  1.00 58.44  ? 340 SER C CA  1 
ATOM   10922 C C   . SER C  1 340 ? 7.366   -6.075  -39.363  1.00 58.35  ? 340 SER C C   1 
ATOM   10923 O O   . SER C  1 340 ? 7.769   -4.927  -39.142  1.00 59.89  ? 340 SER C O   1 
ATOM   10924 C CB  . SER C  1 340 ? 8.581   -6.684  -41.446  1.00 52.88  ? 340 SER C CB  1 
ATOM   10925 O OG  . SER C  1 340 ? 7.394   -6.801  -42.206  1.00 54.31  ? 340 SER C OG  1 
ATOM   10926 N N   . VAL C  1 341 ? 6.121   -6.458  -39.082  1.00 53.80  ? 341 VAL C N   1 
ATOM   10927 C CA  . VAL C  1 341 ? 5.133   -5.568  -38.492  1.00 52.81  ? 341 VAL C CA  1 
ATOM   10928 C C   . VAL C  1 341 ? 4.477   -6.291  -37.325  1.00 58.69  ? 341 VAL C C   1 
ATOM   10929 O O   . VAL C  1 341 ? 4.501   -7.520  -37.233  1.00 61.03  ? 341 VAL C O   1 
ATOM   10930 C CB  . VAL C  1 341 ? 4.058   -5.124  -39.512  1.00 46.77  ? 341 VAL C CB  1 
ATOM   10931 C CG1 . VAL C  1 341 ? 4.674   -4.315  -40.650  1.00 42.35  ? 341 VAL C CG1 1 
ATOM   10932 C CG2 . VAL C  1 341 ? 3.343   -6.339  -40.055  1.00 43.76  ? 341 VAL C CG2 1 
ATOM   10933 N N   . ASP C  1 342 ? 3.870   -5.510  -36.430  1.00 65.60  ? 342 ASP C N   1 
ATOM   10934 C CA  . ASP C  1 342 ? 3.184   -6.085  -35.281  1.00 73.56  ? 342 ASP C CA  1 
ATOM   10935 C C   . ASP C  1 342 ? 1.686   -6.260  -35.509  1.00 71.33  ? 342 ASP C C   1 
ATOM   10936 O O   . ASP C  1 342 ? 1.037   -6.975  -34.734  1.00 77.08  ? 342 ASP C O   1 
ATOM   10937 C CB  . ASP C  1 342 ? 3.432   -5.231  -34.027  1.00 80.44  ? 342 ASP C CB  1 
ATOM   10938 C CG  . ASP C  1 342 ? 2.843   -3.846  -34.142  1.00 83.22  ? 342 ASP C CG  1 
ATOM   10939 O OD1 . ASP C  1 342 ? 2.736   -3.345  -35.284  1.00 80.83  ? 342 ASP C OD1 1 
ATOM   10940 O OD2 . ASP C  1 342 ? 2.505   -3.255  -33.089  1.00 86.89  ? 342 ASP C OD2 1 
ATOM   10941 N N   . PHE C  1 343 ? 1.129   -5.643  -36.552  1.00 59.37  ? 343 PHE C N   1 
ATOM   10942 C CA  . PHE C  1 343 ? -0.256  -5.866  -36.931  1.00 50.70  ? 343 PHE C CA  1 
ATOM   10943 C C   . PHE C  1 343 ? -0.333  -6.981  -37.974  1.00 47.10  ? 343 PHE C C   1 
ATOM   10944 O O   . PHE C  1 343 ? 0.671   -7.588  -38.353  1.00 48.94  ? 343 PHE C O   1 
ATOM   10945 C CB  . PHE C  1 343 ? -0.884  -4.576  -37.457  1.00 48.02  ? 343 PHE C CB  1 
ATOM   10946 C CG  . PHE C  1 343 ? -0.180  -4.020  -38.661  1.00 46.14  ? 343 PHE C CG  1 
ATOM   10947 C CD1 . PHE C  1 343 ? 0.872   -3.133  -38.511  1.00 46.51  ? 343 PHE C CD1 1 
ATOM   10948 C CD2 . PHE C  1 343 ? -0.564  -4.389  -39.942  1.00 45.95  ? 343 PHE C CD2 1 
ATOM   10949 C CE1 . PHE C  1 343 ? 1.532   -2.624  -39.611  1.00 43.26  ? 343 PHE C CE1 1 
ATOM   10950 C CE2 . PHE C  1 343 ? 0.094   -3.886  -41.054  1.00 45.05  ? 343 PHE C CE2 1 
ATOM   10951 C CZ  . PHE C  1 343 ? 1.142   -2.998  -40.889  1.00 43.72  ? 343 PHE C CZ  1 
ATOM   10952 N N   . GLN C  1 344 ? -1.543  -7.249  -38.460  1.00 42.53  ? 344 GLN C N   1 
ATOM   10953 C CA  . GLN C  1 344 ? -1.759  -8.326  -39.417  1.00 40.43  ? 344 GLN C CA  1 
ATOM   10954 C C   . GLN C  1 344 ? -1.748  -7.768  -40.841  1.00 40.56  ? 344 GLN C C   1 
ATOM   10955 O O   . GLN C  1 344 ? -2.729  -7.131  -41.262  1.00 40.89  ? 344 GLN C O   1 
ATOM   10956 C CB  . GLN C  1 344 ? -3.074  -9.058  -39.121  1.00 39.77  ? 344 GLN C CB  1 
ATOM   10957 C CG  . GLN C  1 344 ? -3.056  -9.795  -37.751  1.00 46.47  ? 344 GLN C CG  1 
ATOM   10958 C CD  . GLN C  1 344 ? -4.247  -10.709 -37.556  1.00 47.69  ? 344 GLN C CD  1 
ATOM   10959 O OE1 . GLN C  1 344 ? -4.081  -11.894 -37.279  1.00 53.79  ? 344 GLN C OE1 1 
ATOM   10960 N NE2 . GLN C  1 344 ? -5.450  -10.169 -37.695  1.00 46.49  ? 344 GLN C NE2 1 
ATOM   10961 N N   . PRO C  1 345 ? -0.671  -7.959  -41.606  1.00 39.75  ? 345 PRO C N   1 
ATOM   10962 C CA  . PRO C  1 345 ? -0.597  -7.358  -42.944  1.00 41.18  ? 345 PRO C CA  1 
ATOM   10963 C C   . PRO C  1 345 ? -1.520  -8.021  -43.949  1.00 39.84  ? 345 PRO C C   1 
ATOM   10964 O O   . PRO C  1 345 ? -1.831  -9.213  -43.870  1.00 35.59  ? 345 PRO C O   1 
ATOM   10965 C CB  . PRO C  1 345 ? 0.873   -7.555  -43.342  1.00 40.91  ? 345 PRO C CB  1 
ATOM   10966 C CG  . PRO C  1 345 ? 1.315   -8.729  -42.577  1.00 42.08  ? 345 PRO C CG  1 
ATOM   10967 C CD  . PRO C  1 345 ? 0.563   -8.688  -41.266  1.00 38.80  ? 345 PRO C CD  1 
ATOM   10968 N N   . VAL C  1 346 ? -1.935  -7.224  -44.928  1.00 41.73  ? 346 VAL C N   1 
ATOM   10969 C CA  . VAL C  1 346 ? -2.692  -7.706  -46.074  1.00 36.88  ? 346 VAL C CA  1 
ATOM   10970 C C   . VAL C  1 346 ? -1.786  -7.604  -47.296  1.00 40.17  ? 346 VAL C C   1 
ATOM   10971 O O   . VAL C  1 346 ? -1.313  -6.513  -47.643  1.00 39.19  ? 346 VAL C O   1 
ATOM   10972 C CB  . VAL C  1 346 ? -3.999  -6.924  -46.252  1.00 34.62  ? 346 VAL C CB  1 
ATOM   10973 C CG1 . VAL C  1 346 ? -4.754  -7.422  -47.451  1.00 30.79  ? 346 VAL C CG1 1 
ATOM   10974 C CG2 . VAL C  1 346 ? -4.853  -7.086  -45.017  1.00 33.32  ? 346 VAL C CG2 1 
ATOM   10975 N N   . VAL C  1 347 ? -1.526  -8.748  -47.926  1.00 36.77  ? 347 VAL C N   1 
ATOM   10976 C CA  . VAL C  1 347 ? -0.562  -8.876  -49.012  1.00 38.14  ? 347 VAL C CA  1 
ATOM   10977 C C   . VAL C  1 347 ? -1.344  -9.187  -50.277  1.00 34.48  ? 347 VAL C C   1 
ATOM   10978 O O   . VAL C  1 347 ? -1.825  -10.312 -50.462  1.00 31.47  ? 347 VAL C O   1 
ATOM   10979 C CB  . VAL C  1 347 ? 0.476   -9.973  -48.737  1.00 37.76  ? 347 VAL C CB  1 
ATOM   10980 C CG1 . VAL C  1 347 ? 1.553   -9.948  -49.795  1.00 35.41  ? 347 VAL C CG1 1 
ATOM   10981 C CG2 . VAL C  1 347 ? 1.077   -9.811  -47.354  1.00 40.43  ? 347 VAL C CG2 1 
ATOM   10982 N N   . PHE C  1 348 ? -1.484  -8.189  -51.138  1.00 30.40  ? 348 PHE C N   1 
ATOM   10983 C CA  . PHE C  1 348 ? -2.169  -8.364  -52.410  1.00 32.44  ? 348 PHE C CA  1 
ATOM   10984 C C   . PHE C  1 348 ? -1.146  -8.774  -53.463  1.00 32.22  ? 348 PHE C C   1 
ATOM   10985 O O   . PHE C  1 348 ? -0.155  -8.070  -53.683  1.00 34.77  ? 348 PHE C O   1 
ATOM   10986 C CB  . PHE C  1 348 ? -2.902  -7.087  -52.801  1.00 28.51  ? 348 PHE C CB  1 
ATOM   10987 C CG  . PHE C  1 348 ? -4.373  -7.108  -52.456  1.00 28.94  ? 348 PHE C CG  1 
ATOM   10988 C CD1 . PHE C  1 348 ? -4.791  -7.071  -51.129  1.00 27.88  ? 348 PHE C CD1 1 
ATOM   10989 C CD2 . PHE C  1 348 ? -5.335  -7.179  -53.466  1.00 28.41  ? 348 PHE C CD2 1 
ATOM   10990 C CE1 . PHE C  1 348 ? -6.142  -7.098  -50.809  1.00 28.65  ? 348 PHE C CE1 1 
ATOM   10991 C CE2 . PHE C  1 348 ? -6.685  -7.208  -53.162  1.00 27.82  ? 348 PHE C CE2 1 
ATOM   10992 C CZ  . PHE C  1 348 ? -7.095  -7.162  -51.830  1.00 29.26  ? 348 PHE C CZ  1 
ATOM   10993 N N   . VAL C  1 349 ? -1.356  -9.939  -54.063  1.00 27.97  ? 349 VAL C N   1 
ATOM   10994 C CA  . VAL C  1 349 ? -0.560  -10.402 -55.191  1.00 30.07  ? 349 VAL C CA  1 
ATOM   10995 C C   . VAL C  1 349 ? -1.476  -10.377 -56.406  1.00 32.36  ? 349 VAL C C   1 
ATOM   10996 O O   . VAL C  1 349 ? -2.425  -11.171 -56.500  1.00 30.48  ? 349 VAL C O   1 
ATOM   10997 C CB  . VAL C  1 349 ? 0.027   -11.802 -54.952  1.00 31.30  ? 349 VAL C CB  1 
ATOM   10998 C CG1 . VAL C  1 349 ? 0.677   -12.323 -56.217  1.00 28.17  ? 349 VAL C CG1 1 
ATOM   10999 C CG2 . VAL C  1 349 ? 1.042   -11.766 -53.806  1.00 34.25  ? 349 VAL C CG2 1 
ATOM   11000 N N   . VAL C  1 350 ? -1.193  -9.468  -57.340  1.00 31.92  ? 350 VAL C N   1 
ATOM   11001 C CA  . VAL C  1 350 ? -2.083  -9.177  -58.458  1.00 31.72  ? 350 VAL C CA  1 
ATOM   11002 C C   . VAL C  1 350 ? -1.276  -9.172  -59.747  1.00 30.69  ? 350 VAL C C   1 
ATOM   11003 O O   . VAL C  1 350 ? -0.282  -8.445  -59.858  1.00 33.17  ? 350 VAL C O   1 
ATOM   11004 C CB  . VAL C  1 350 ? -2.798  -7.826  -58.270  1.00 28.29  ? 350 VAL C CB  1 
ATOM   11005 C CG1 . VAL C  1 350 ? -3.888  -7.644  -59.333  1.00 31.63  ? 350 VAL C CG1 1 
ATOM   11006 C CG2 . VAL C  1 350 ? -3.389  -7.738  -56.867  1.00 29.80  ? 350 VAL C CG2 1 
ATOM   11007 N N   . LEU C  1 351 ? -1.705  -9.979  -60.714  1.00 27.22  ? 351 LEU C N   1 
ATOM   11008 C CA  . LEU C  1 351 ? -1.053  -10.053 -62.017  1.00 22.87  ? 351 LEU C CA  1 
ATOM   11009 C C   . LEU C  1 351 ? -1.978  -10.805 -62.961  1.00 23.05  ? 351 LEU C C   1 
ATOM   11010 O O   . LEU C  1 351 ? -2.939  -11.458 -62.542  1.00 25.52  ? 351 LEU C O   1 
ATOM   11011 C CB  . LEU C  1 351 ? 0.314   -10.741 -61.930  1.00 23.54  ? 351 LEU C CB  1 
ATOM   11012 C CG  . LEU C  1 351 ? 0.330   -12.228 -61.544  1.00 24.11  ? 351 LEU C CG  1 
ATOM   11013 C CD1 . LEU C  1 351 ? 1.583   -12.897 -62.080  1.00 25.83  ? 351 LEU C CD1 1 
ATOM   11014 C CD2 . LEU C  1 351 ? 0.239   -12.431 -60.014  1.00 26.67  ? 351 LEU C CD2 1 
ATOM   11015 N N   . ASN C  1 352 ? -1.676  -10.787 -64.233  1.00 22.01  ? 352 ASN C N   1 
ATOM   11016 C CA  . ASN C  1 352 ? -2.407  -11.530 -65.201  1.00 21.51  ? 352 ASN C CA  1 
ATOM   11017 C C   . ASN C  1 352 ? -2.325  -12.997 -64.839  1.00 21.63  ? 352 ASN C C   1 
ATOM   11018 O O   . ASN C  1 352 ? -1.355  -13.462 -64.373  1.00 22.16  ? 352 ASN C O   1 
ATOM   11019 C CB  . ASN C  1 352 ? -1.867  -11.202 -66.604  1.00 22.45  ? 352 ASN C CB  1 
ATOM   11020 C CG  . ASN C  1 352 ? -2.584  -10.057 -67.245  1.00 31.96  ? 352 ASN C CG  1 
ATOM   11021 O OD1 . ASN C  1 352 ? -2.242  -8.912  -67.027  1.00 30.74  ? 352 ASN C OD1 1 
ATOM   11022 N ND2 . ASN C  1 352 ? -3.601  -10.366 -68.030  1.00 28.54  ? 352 ASN C ND2 1 
ATOM   11023 N N   . GLY C  1 353 ? -3.445  -13.665 -64.983  1.00 23.49  ? 353 GLY C N   1 
ATOM   11024 C CA  . GLY C  1 353 ? -3.433  -15.062 -64.603  1.00 22.86  ? 353 GLY C CA  1 
ATOM   11025 C C   . GLY C  1 353 ? -3.266  -16.073 -65.708  1.00 23.37  ? 353 GLY C C   1 
ATOM   11026 O O   . GLY C  1 353 ? -3.416  -17.274 -65.450  1.00 30.02  ? 353 GLY C O   1 
ATOM   11027 N N   . GLU C  1 354 ? -2.906  -15.641 -66.925  1.00 21.28  ? 354 GLU C N   1 
ATOM   11028 C CA  . GLU C  1 354 ? -2.886  -16.538 -68.061  1.00 23.47  ? 354 GLU C CA  1 
ATOM   11029 C C   . GLU C  1 354 ? -1.651  -16.406 -68.947  1.00 22.76  ? 354 GLU C C   1 
ATOM   11030 O O   . GLU C  1 354 ? -1.466  -17.258 -69.818  1.00 23.04  ? 354 GLU C O   1 
ATOM   11031 C CB  . GLU C  1 354 ? -4.148  -16.311 -68.915  1.00 30.02  ? 354 GLU C CB  1 
ATOM   11032 C CG  . GLU C  1 354 ? -4.036  -15.157 -69.905  1.00 32.58  ? 354 GLU C CG  1 
ATOM   11033 C CD  . GLU C  1 354 ? -4.432  -13.804 -69.321  1.00 30.06  ? 354 GLU C CD  1 
ATOM   11034 O OE1 . GLU C  1 354 ? -5.422  -13.200 -69.796  1.00 29.00  ? 354 GLU C OE1 1 
ATOM   11035 O OE2 . GLU C  1 354 ? -3.733  -13.328 -68.413  1.00 26.39  ? 354 GLU C OE2 1 
ATOM   11036 N N   . ASN C  1 355 ? -0.777  -15.419 -68.732  1.00 25.30  ? 355 ASN C N   1 
ATOM   11037 C CA  . ASN C  1 355 ? 0.309   -15.141 -69.670  1.00 28.03  ? 355 ASN C CA  1 
ATOM   11038 C C   . ASN C  1 355 ? 1.659   -15.717 -69.255  1.00 26.19  ? 355 ASN C C   1 
ATOM   11039 O O   . ASN C  1 355 ? 2.502   -15.959 -70.118  1.00 25.12  ? 355 ASN C O   1 
ATOM   11040 C CB  . ASN C  1 355 ? 0.454   -13.628 -69.858  1.00 29.68  ? 355 ASN C CB  1 
ATOM   11041 C CG  . ASN C  1 355 ? -0.739  -13.021 -70.549  1.00 31.80  ? 355 ASN C CG  1 
ATOM   11042 O OD1 . ASN C  1 355 ? -1.333  -13.638 -71.439  1.00 31.86  ? 355 ASN C OD1 1 
ATOM   11043 N ND2 . ASN C  1 355 ? -1.122  -11.820 -70.128  1.00 27.24  ? 355 ASN C ND2 1 
ATOM   11044 N N   . CYS C  1 356 ? 1.905   -15.935 -67.964  1.00 23.14  ? 356 CYS C N   1 
ATOM   11045 C CA  . CYS C  1 356 ? 3.245   -16.292 -67.526  1.00 24.51  ? 356 CYS C CA  1 
ATOM   11046 C C   . CYS C  1 356 ? 3.485   -17.788 -67.561  1.00 25.62  ? 356 CYS C C   1 
ATOM   11047 O O   . CYS C  1 356 ? 4.637   -18.217 -67.669  1.00 34.40  ? 356 CYS C O   1 
ATOM   11048 C CB  . CYS C  1 356 ? 3.502   -15.757 -66.105  1.00 29.30  ? 356 CYS C CB  1 
ATOM   11049 S SG  . CYS C  1 356 ? 2.325   -16.360 -64.860  1.00 27.61  ? 356 CYS C SG  1 
ATOM   11050 N N   . TRP C  1 357 ? 2.426   -18.590 -67.523  1.00 26.68  ? 357 TRP C N   1 
ATOM   11051 C CA  . TRP C  1 357 ? 2.605   -20.019 -67.285  1.00 32.03  ? 357 TRP C CA  1 
ATOM   11052 C C   . TRP C  1 357 ? 3.261   -20.725 -68.455  1.00 32.86  ? 357 TRP C C   1 
ATOM   11053 O O   . TRP C  1 357 ? 3.981   -21.709 -68.250  1.00 31.46  ? 357 TRP C O   1 
ATOM   11054 C CB  . TRP C  1 357 ? 1.260   -20.656 -66.956  1.00 31.51  ? 357 TRP C CB  1 
ATOM   11055 C CG  . TRP C  1 357 ? 0.558   -19.891 -65.916  1.00 30.64  ? 357 TRP C CG  1 
ATOM   11056 C CD1 . TRP C  1 357 ? -0.651  -19.285 -66.025  1.00 31.73  ? 357 TRP C CD1 1 
ATOM   11057 C CD2 . TRP C  1 357 ? 1.036   -19.608 -64.589  1.00 34.52  ? 357 TRP C CD2 1 
ATOM   11058 N NE1 . TRP C  1 357 ? -0.970  -18.646 -64.844  1.00 31.95  ? 357 TRP C NE1 1 
ATOM   11059 C CE2 . TRP C  1 357 ? 0.050   -18.829 -63.948  1.00 31.49  ? 357 TRP C CE2 1 
ATOM   11060 C CE3 . TRP C  1 357 ? 2.199   -19.941 -63.880  1.00 36.04  ? 357 TRP C CE3 1 
ATOM   11061 C CZ2 . TRP C  1 357 ? 0.185   -18.383 -62.630  1.00 34.66  ? 357 TRP C CZ2 1 
ATOM   11062 C CZ3 . TRP C  1 357 ? 2.331   -19.491 -62.564  1.00 36.10  ? 357 TRP C CZ3 1 
ATOM   11063 C CH2 . TRP C  1 357 ? 1.330   -18.721 -61.961  1.00 32.74  ? 357 TRP C CH2 1 
ATOM   11064 N N   . GLU C  1 358 ? 3.032   -20.244 -69.681  1.00 33.64  ? 358 GLU C N   1 
ATOM   11065 C CA  . GLU C  1 358 ? 3.612   -20.884 -70.860  1.00 30.10  ? 358 GLU C CA  1 
ATOM   11066 C C   . GLU C  1 358 ? 5.133   -20.866 -70.838  1.00 26.27  ? 358 GLU C C   1 
ATOM   11067 O O   . GLU C  1 358 ? 5.759   -21.612 -71.600  1.00 27.23  ? 358 GLU C O   1 
ATOM   11068 C CB  . GLU C  1 358 ? 3.103   -20.204 -72.139  1.00 29.89  ? 358 GLU C CB  1 
ATOM   11069 C CG  . GLU C  1 358 ? 3.481   -18.736 -72.222  1.00 29.41  ? 358 GLU C CG  1 
ATOM   11070 C CD  . GLU C  1 358 ? 2.527   -17.919 -73.074  1.00 37.01  ? 358 GLU C CD  1 
ATOM   11071 O OE1 . GLU C  1 358 ? 2.961   -17.459 -74.154  1.00 37.51  ? 358 GLU C OE1 1 
ATOM   11072 O OE2 . GLU C  1 358 ? 1.359   -17.725 -72.665  1.00 34.79  ? 358 GLU C OE2 1 
ATOM   11073 N N   . TYR C  1 359 ? 5.744   -20.042 -69.987  1.00 26.14  ? 359 TYR C N   1 
ATOM   11074 C CA  . TYR C  1 359 ? 7.192   -20.017 -69.840  1.00 29.94  ? 359 TYR C CA  1 
ATOM   11075 C C   . TYR C  1 359 ? 7.691   -20.881 -68.687  1.00 31.77  ? 359 TYR C C   1 
ATOM   11076 O O   . TYR C  1 359 ? 8.897   -21.124 -68.593  1.00 30.47  ? 359 TYR C O   1 
ATOM   11077 C CB  . TYR C  1 359 ? 7.676   -18.570 -69.662  1.00 30.41  ? 359 TYR C CB  1 
ATOM   11078 C CG  . TYR C  1 359 ? 7.316   -17.668 -70.828  1.00 32.35  ? 359 TYR C CG  1 
ATOM   11079 C CD1 . TYR C  1 359 ? 8.098   -17.638 -71.984  1.00 37.80  ? 359 TYR C CD1 1 
ATOM   11080 C CD2 . TYR C  1 359 ? 6.185   -16.869 -70.787  1.00 30.37  ? 359 TYR C CD2 1 
ATOM   11081 C CE1 . TYR C  1 359 ? 7.764   -16.818 -73.058  1.00 38.68  ? 359 TYR C CE1 1 
ATOM   11082 C CE2 . TYR C  1 359 ? 5.840   -16.049 -71.846  1.00 33.79  ? 359 TYR C CE2 1 
ATOM   11083 C CZ  . TYR C  1 359 ? 6.634   -16.022 -72.981  1.00 39.43  ? 359 TYR C CZ  1 
ATOM   11084 O OH  . TYR C  1 359 ? 6.284   -15.199 -74.032  1.00 39.56  ? 359 TYR C OH  1 
ATOM   11085 N N   . TYR C  1 360 ? 6.800   -21.354 -67.822  1.00 28.12  ? 360 TYR C N   1 
ATOM   11086 C CA  . TYR C  1 360 ? 7.169   -22.294 -66.775  1.00 35.62  ? 360 TYR C CA  1 
ATOM   11087 C C   . TYR C  1 360 ? 7.273   -23.710 -67.321  1.00 34.97  ? 360 TYR C C   1 
ATOM   11088 O O   . TYR C  1 360 ? 6.585   -24.085 -68.276  1.00 33.76  ? 360 TYR C O   1 
ATOM   11089 C CB  . TYR C  1 360 ? 6.127   -22.320 -65.662  1.00 33.75  ? 360 TYR C CB  1 
ATOM   11090 C CG  . TYR C  1 360 ? 6.130   -21.164 -64.710  1.00 32.57  ? 360 TYR C CG  1 
ATOM   11091 C CD1 . TYR C  1 360 ? 5.782   -19.891 -65.129  1.00 32.44  ? 360 TYR C CD1 1 
ATOM   11092 C CD2 . TYR C  1 360 ? 6.426   -21.363 -63.358  1.00 36.21  ? 360 TYR C CD2 1 
ATOM   11093 C CE1 . TYR C  1 360 ? 5.745   -18.830 -64.225  1.00 30.70  ? 360 TYR C CE1 1 
ATOM   11094 C CE2 . TYR C  1 360 ? 6.413   -20.326 -62.467  1.00 29.73  ? 360 TYR C CE2 1 
ATOM   11095 C CZ  . TYR C  1 360 ? 6.067   -19.059 -62.903  1.00 29.37  ? 360 TYR C CZ  1 
ATOM   11096 O OH  . TYR C  1 360 ? 6.037   -18.020 -62.006  1.00 29.43  ? 360 TYR C OH  1 
ATOM   11097 N N   . GLU C  1 361 ? 8.104   -24.510 -66.657  1.00 34.07  ? 361 GLU C N   1 
ATOM   11098 C CA  . GLU C  1 361 ? 8.123   -25.951 -66.860  1.00 38.69  ? 361 GLU C CA  1 
ATOM   11099 C C   . GLU C  1 361 ? 6.734   -26.538 -66.631  1.00 36.76  ? 361 GLU C C   1 
ATOM   11100 O O   . GLU C  1 361 ? 6.101   -26.274 -65.604  1.00 34.95  ? 361 GLU C O   1 
ATOM   11101 C CB  . GLU C  1 361 ? 9.126   -26.579 -65.888  1.00 46.34  ? 361 GLU C CB  1 
ATOM   11102 C CG  . GLU C  1 361 ? 9.464   -28.020 -66.172  1.00 58.72  ? 361 GLU C CG  1 
ATOM   11103 C CD  . GLU C  1 361 ? 10.619  -28.163 -67.145  1.00 67.47  ? 361 GLU C CD  1 
ATOM   11104 O OE1 . GLU C  1 361 ? 10.900  -27.199 -67.894  1.00 66.12  ? 361 GLU C OE1 1 
ATOM   11105 O OE2 . GLU C  1 361 ? 11.245  -29.245 -67.161  1.00 73.54  ? 361 GLU C OE2 1 
ATOM   11106 N N   . GLU C  1 362 ? 6.253   -27.320 -67.602  1.00 36.81  ? 362 GLU C N   1 
ATOM   11107 C CA  . GLU C  1 362 ? 4.966   -28.019 -67.501  1.00 37.64  ? 362 GLU C CA  1 
ATOM   11108 C C   . GLU C  1 362 ? 3.814   -27.053 -67.230  1.00 31.91  ? 362 GLU C C   1 
ATOM   11109 O O   . GLU C  1 362 ? 2.900   -27.340 -66.450  1.00 29.41  ? 362 GLU C O   1 
ATOM   11110 C CB  . GLU C  1 362 ? 5.007   -29.125 -66.442  1.00 41.54  ? 362 GLU C CB  1 
ATOM   11111 C CG  . GLU C  1 362 ? 6.136   -30.114 -66.649  1.00 52.14  ? 362 GLU C CG  1 
ATOM   11112 C CD  . GLU C  1 362 ? 6.141   -31.215 -65.607  1.00 61.52  ? 362 GLU C CD  1 
ATOM   11113 O OE1 . GLU C  1 362 ? 7.238   -31.574 -65.121  1.00 62.82  ? 362 GLU C OE1 1 
ATOM   11114 O OE2 . GLU C  1 362 ? 5.044   -31.719 -65.275  1.00 65.63  ? 362 GLU C OE2 1 
ATOM   11115 N N   . ASN C  1 363 ? 3.860   -25.890 -67.874  1.00 30.94  ? 363 ASN C N   1 
ATOM   11116 C CA  . ASN C  1 363 ? 2.742   -24.954 -67.838  1.00 26.76  ? 363 ASN C CA  1 
ATOM   11117 C C   . ASN C  1 363 ? 2.446   -24.480 -66.413  1.00 27.98  ? 363 ASN C C   1 
ATOM   11118 O O   . ASN C  1 363 ? 1.296   -24.202 -66.075  1.00 27.80  ? 363 ASN C O   1 
ATOM   11119 C CB  . ASN C  1 363 ? 1.490   -25.583 -68.476  1.00 28.60  ? 363 ASN C CB  1 
ATOM   11120 C CG  . ASN C  1 363 ? 0.431   -24.553 -68.833  1.00 27.32  ? 363 ASN C CG  1 
ATOM   11121 O OD1 . ASN C  1 363 ? 0.747   -23.401 -69.111  1.00 29.16  ? 363 ASN C OD1 1 
ATOM   11122 N ND2 . ASN C  1 363 ? -0.836  -24.960 -68.784  1.00 27.30  ? 363 ASN C ND2 1 
ATOM   11123 N N   . GLY C  1 364 ? 3.476   -24.378 -65.571  1.00 26.88  ? 364 GLY C N   1 
ATOM   11124 C CA  . GLY C  1 364 ? 3.298   -23.827 -64.237  1.00 25.85  ? 364 GLY C CA  1 
ATOM   11125 C C   . GLY C  1 364 ? 2.631   -24.746 -63.249  1.00 29.32  ? 364 GLY C C   1 
ATOM   11126 O O   . GLY C  1 364 ? 2.416   -24.348 -62.089  1.00 27.25  ? 364 GLY C O   1 
ATOM   11127 N N   . ILE C  1 365 ? 2.319   -25.970 -63.655  1.00 27.45  ? 365 ILE C N   1 
ATOM   11128 C CA  . ILE C  1 365 ? 1.546   -26.856 -62.797  1.00 33.24  ? 365 ILE C CA  1 
ATOM   11129 C C   . ILE C  1 365 ? 2.387   -27.275 -61.595  1.00 35.65  ? 365 ILE C C   1 
ATOM   11130 O O   . ILE C  1 365 ? 1.865   -27.245 -60.471  1.00 35.97  ? 365 ILE C O   1 
ATOM   11131 C CB  . ILE C  1 365 ? 0.999   -28.059 -63.573  1.00 37.38  ? 365 ILE C CB  1 
ATOM   11132 C CG1 . ILE C  1 365 ? -0.100  -27.580 -64.524  1.00 34.55  ? 365 ILE C CG1 1 
ATOM   11133 C CG2 . ILE C  1 365 ? 0.466   -29.113 -62.592  1.00 29.40  ? 365 ILE C CG2 1 
ATOM   11134 C CD1 . ILE C  1 365 ? -0.108  -28.259 -65.857  1.00 34.47  ? 365 ILE C CD1 1 
ATOM   11135 N N   . PRO C  1 366 ? 3.664   -27.661 -61.751  1.00 36.87  ? 366 PRO C N   1 
ATOM   11136 C CA  . PRO C  1 366 ? 4.464   -27.932 -60.541  1.00 40.39  ? 366 PRO C CA  1 
ATOM   11137 C C   . PRO C  1 366 ? 4.546   -26.733 -59.611  1.00 38.15  ? 366 PRO C C   1 
ATOM   11138 O O   . PRO C  1 366 ? 4.334   -26.869 -58.396  1.00 40.07  ? 366 PRO C O   1 
ATOM   11139 C CB  . PRO C  1 366 ? 5.834   -28.336 -61.111  1.00 31.63  ? 366 PRO C CB  1 
ATOM   11140 C CG  . PRO C  1 366 ? 5.496   -28.959 -62.447  1.00 36.11  ? 366 PRO C CG  1 
ATOM   11141 C CD  . PRO C  1 366 ? 4.359   -28.122 -62.977  1.00 36.97  ? 366 PRO C CD  1 
ATOM   11142 N N   . PHE C  1 367 ? 4.811   -25.546 -60.154  1.00 35.75  ? 367 PHE C N   1 
ATOM   11143 C CA  . PHE C  1 367 ? 4.937   -24.371 -59.305  1.00 34.62  ? 367 PHE C CA  1 
ATOM   11144 C C   . PHE C  1 367 ? 3.647   -24.091 -58.544  1.00 33.25  ? 367 PHE C C   1 
ATOM   11145 O O   . PHE C  1 367 ? 3.672   -23.857 -57.332  1.00 29.43  ? 367 PHE C O   1 
ATOM   11146 C CB  . PHE C  1 367 ? 5.337   -23.150 -60.122  1.00 29.98  ? 367 PHE C CB  1 
ATOM   11147 C CG  . PHE C  1 367 ? 5.305   -21.886 -59.325  1.00 30.89  ? 367 PHE C CG  1 
ATOM   11148 C CD1 . PHE C  1 367 ? 6.273   -21.644 -58.361  1.00 33.66  ? 367 PHE C CD1 1 
ATOM   11149 C CD2 . PHE C  1 367 ? 4.292   -20.962 -59.506  1.00 30.97  ? 367 PHE C CD2 1 
ATOM   11150 C CE1 . PHE C  1 367 ? 6.232   -20.479 -57.593  1.00 34.60  ? 367 PHE C CE1 1 
ATOM   11151 C CE2 . PHE C  1 367 ? 4.250   -19.801 -58.749  1.00 33.29  ? 367 PHE C CE2 1 
ATOM   11152 C CZ  . PHE C  1 367 ? 5.221   -19.564 -57.794  1.00 33.30  ? 367 PHE C CZ  1 
ATOM   11153 N N   . LEU C  1 368 ? 2.509   -24.103 -59.237  1.00 33.13  ? 368 LEU C N   1 
ATOM   11154 C CA  . LEU C  1 368 ? 1.259   -23.725 -58.585  1.00 30.12  ? 368 LEU C CA  1 
ATOM   11155 C C   . LEU C  1 368 ? 0.784   -24.799 -57.615  1.00 29.83  ? 368 LEU C C   1 
ATOM   11156 O O   . LEU C  1 368 ? 0.237   -24.484 -56.548  1.00 33.00  ? 368 LEU C O   1 
ATOM   11157 C CB  . LEU C  1 368 ? 0.188   -23.440 -59.636  1.00 26.76  ? 368 LEU C CB  1 
ATOM   11158 C CG  . LEU C  1 368 ? 0.301   -22.095 -60.356  1.00 25.62  ? 368 LEU C CG  1 
ATOM   11159 C CD1 . LEU C  1 368 ? -0.822  -21.948 -61.396  1.00 24.88  ? 368 LEU C CD1 1 
ATOM   11160 C CD2 . LEU C  1 368 ? 0.289   -20.941 -59.362  1.00 36.69  ? 368 LEU C CD2 1 
ATOM   11161 N N   . GLU C  1 369 ? 0.963   -26.071 -57.968  1.00 30.12  ? 369 GLU C N   1 
ATOM   11162 C CA  . GLU C  1 369 ? 0.532   -27.133 -57.066  1.00 32.55  ? 369 GLU C CA  1 
ATOM   11163 C C   . GLU C  1 369 ? 1.381   -27.139 -55.806  1.00 36.81  ? 369 GLU C C   1 
ATOM   11164 O O   . GLU C  1 369 ? 0.851   -27.274 -54.696  1.00 35.97  ? 369 GLU C O   1 
ATOM   11165 C CB  . GLU C  1 369 ? 0.577   -28.486 -57.776  1.00 34.80  ? 369 GLU C CB  1 
ATOM   11166 C CG  . GLU C  1 369 ? -0.649  -28.714 -58.648  1.00 34.11  ? 369 GLU C CG  1 
ATOM   11167 C CD  . GLU C  1 369 ? -0.623  -30.029 -59.390  1.00 36.19  ? 369 GLU C CD  1 
ATOM   11168 O OE1 . GLU C  1 369 ? 0.418   -30.727 -59.356  1.00 39.28  ? 369 GLU C OE1 1 
ATOM   11169 O OE2 . GLU C  1 369 ? -1.661  -30.375 -59.993  1.00 33.37  ? 369 GLU C OE2 1 
ATOM   11170 N N   . LYS C  1 370 ? 2.689   -26.931 -55.952  1.00 34.94  ? 370 LYS C N   1 
ATOM   11171 C CA  . LYS C  1 370 ? 3.547   -26.802 -54.780  1.00 33.41  ? 370 LYS C CA  1 
ATOM   11172 C C   . LYS C  1 370 ? 3.167   -25.577 -53.957  1.00 40.57  ? 370 LYS C C   1 
ATOM   11173 O O   . LYS C  1 370 ? 3.043   -25.657 -52.725  1.00 36.93  ? 370 LYS C O   1 
ATOM   11174 C CB  . LYS C  1 370 ? 5.014   -26.729 -55.200  1.00 36.89  ? 370 LYS C CB  1 
ATOM   11175 C CG  . LYS C  1 370 ? 5.985   -27.028 -54.052  1.00 48.56  ? 370 LYS C CG  1 
ATOM   11176 C CD  . LYS C  1 370 ? 6.264   -28.523 -53.949  1.00 58.97  ? 370 LYS C CD  1 
ATOM   11177 C CE  . LYS C  1 370 ? 6.971   -29.044 -55.207  1.00 65.25  ? 370 LYS C CE  1 
ATOM   11178 N NZ  . LYS C  1 370 ? 6.632   -30.460 -55.564  1.00 68.71  ? 370 LYS C NZ  1 
ATOM   11179 N N   . LEU C  1 371 ? 2.975   -24.435 -54.632  1.00 37.63  ? 371 LEU C N   1 
ATOM   11180 C CA  . LEU C  1 371 ? 2.654   -23.184 -53.950  1.00 37.67  ? 371 LEU C CA  1 
ATOM   11181 C C   . LEU C  1 371 ? 1.368   -23.311 -53.139  1.00 37.83  ? 371 LEU C C   1 
ATOM   11182 O O   . LEU C  1 371 ? 1.351   -23.049 -51.930  1.00 35.82  ? 371 LEU C O   1 
ATOM   11183 C CB  . LEU C  1 371 ? 2.541   -22.054 -54.978  1.00 35.55  ? 371 LEU C CB  1 
ATOM   11184 C CG  . LEU C  1 371 ? 2.077   -20.682 -54.488  1.00 32.57  ? 371 LEU C CG  1 
ATOM   11185 C CD1 . LEU C  1 371 ? 3.143   -20.091 -53.585  1.00 36.76  ? 371 LEU C CD1 1 
ATOM   11186 C CD2 . LEU C  1 371 ? 1.786   -19.762 -55.680  1.00 36.32  ? 371 LEU C CD2 1 
ATOM   11187 N N   . TYR C  1 372 ? 0.285   -23.744 -53.789  1.00 38.08  ? 372 TYR C N   1 
ATOM   11188 C CA  . TYR C  1 372 ? -1.009  -23.809 -53.123  1.00 39.38  ? 372 TYR C CA  1 
ATOM   11189 C C   . TYR C  1 372 ? -0.991  -24.802 -51.966  1.00 45.10  ? 372 TYR C C   1 
ATOM   11190 O O   . TYR C  1 372 ? -1.568  -24.539 -50.904  1.00 42.28  ? 372 TYR C O   1 
ATOM   11191 C CB  . TYR C  1 372 ? -2.085  -24.176 -54.141  1.00 36.69  ? 372 TYR C CB  1 
ATOM   11192 C CG  . TYR C  1 372 ? -2.385  -23.076 -55.140  1.00 31.24  ? 372 TYR C CG  1 
ATOM   11193 C CD1 . TYR C  1 372 ? -2.016  -21.763 -54.889  1.00 33.48  ? 372 TYR C CD1 1 
ATOM   11194 C CD2 . TYR C  1 372 ? -3.021  -23.362 -56.349  1.00 28.91  ? 372 TYR C CD2 1 
ATOM   11195 C CE1 . TYR C  1 372 ? -2.303  -20.736 -55.809  1.00 33.30  ? 372 TYR C CE1 1 
ATOM   11196 C CE2 . TYR C  1 372 ? -3.299  -22.362 -57.273  1.00 27.34  ? 372 TYR C CE2 1 
ATOM   11197 C CZ  . TYR C  1 372 ? -2.940  -21.049 -56.995  1.00 30.91  ? 372 TYR C CZ  1 
ATOM   11198 O OH  . TYR C  1 372 ? -3.231  -20.059 -57.901  1.00 26.36  ? 372 TYR C OH  1 
ATOM   11199 N N   . SER C  1 373 ? -0.330  -25.947 -52.154  1.00 45.43  ? 373 SER C N   1 
ATOM   11200 C CA  . SER C  1 373 ? -0.253  -26.940 -51.092  1.00 44.99  ? 373 SER C CA  1 
ATOM   11201 C C   . SER C  1 373 ? 0.565   -26.427 -49.914  1.00 43.65  ? 373 SER C C   1 
ATOM   11202 O O   . SER C  1 373 ? 0.168   -26.603 -48.758  1.00 46.90  ? 373 SER C O   1 
ATOM   11203 C CB  . SER C  1 373 ? 0.345   -28.234 -51.632  1.00 46.25  ? 373 SER C CB  1 
ATOM   11204 O OG  . SER C  1 373 ? 1.693   -28.027 -52.006  1.00 49.59  ? 373 SER C OG  1 
ATOM   11205 N N   . THR C  1 374 ? 1.714   -25.798 -50.185  1.00 42.69  ? 374 THR C N   1 
ATOM   11206 C CA  . THR C  1 374 ? 2.525   -25.243 -49.104  1.00 47.12  ? 374 THR C CA  1 
ATOM   11207 C C   . THR C  1 374 ? 1.771   -24.144 -48.361  1.00 46.67  ? 374 THR C C   1 
ATOM   11208 O O   . THR C  1 374 ? 1.811   -24.082 -47.124  1.00 47.44  ? 374 THR C O   1 
ATOM   11209 C CB  . THR C  1 374 ? 3.851   -24.707 -49.651  1.00 47.10  ? 374 THR C CB  1 
ATOM   11210 O OG1 . THR C  1 374 ? 4.488   -25.720 -50.430  1.00 45.52  ? 374 THR C OG1 1 
ATOM   11211 C CG2 . THR C  1 374 ? 4.794   -24.318 -48.510  1.00 51.92  ? 374 THR C CG2 1 
ATOM   11212 N N   . LEU C  1 375 ? 1.069   -23.278 -49.091  1.00 38.64  ? 375 LEU C N   1 
ATOM   11213 C CA  . LEU C  1 375 ? 0.264   -22.252 -48.434  1.00 40.01  ? 375 LEU C CA  1 
ATOM   11214 C C   . LEU C  1 375 ? -0.831  -22.880 -47.582  1.00 42.23  ? 375 LEU C C   1 
ATOM   11215 O O   . LEU C  1 375 ? -1.155  -22.377 -46.497  1.00 40.11  ? 375 LEU C O   1 
ATOM   11216 C CB  . LEU C  1 375 ? -0.352  -21.308 -49.472  1.00 37.67  ? 375 LEU C CB  1 
ATOM   11217 C CG  . LEU C  1 375 ? 0.554   -20.262 -50.135  1.00 37.51  ? 375 LEU C CG  1 
ATOM   11218 C CD1 . LEU C  1 375 ? -0.145  -19.579 -51.333  1.00 35.66  ? 375 LEU C CD1 1 
ATOM   11219 C CD2 . LEU C  1 375 ? 1.003   -19.232 -49.130  1.00 37.64  ? 375 LEU C CD2 1 
ATOM   11220 N N   . GLU C  1 376 ? -1.406  -23.989 -48.056  1.00 41.43  ? 376 GLU C N   1 
ATOM   11221 C CA  . GLU C  1 376 ? -2.482  -24.646 -47.323  1.00 49.24  ? 376 GLU C CA  1 
ATOM   11222 C C   . GLU C  1 376 ? -2.017  -25.115 -45.951  1.00 52.31  ? 376 GLU C C   1 
ATOM   11223 O O   . GLU C  1 376 ? -2.827  -25.237 -45.024  1.00 55.08  ? 376 GLU C O   1 
ATOM   11224 C CB  . GLU C  1 376 ? -3.008  -25.833 -48.132  1.00 54.70  ? 376 GLU C CB  1 
ATOM   11225 C CG  . GLU C  1 376 ? -4.424  -25.687 -48.665  1.00 57.16  ? 376 GLU C CG  1 
ATOM   11226 C CD  . GLU C  1 376 ? -4.907  -26.963 -49.322  1.00 60.24  ? 376 GLU C CD  1 
ATOM   11227 O OE1 . GLU C  1 376 ? -4.045  -27.810 -49.628  1.00 60.05  ? 376 GLU C OE1 1 
ATOM   11228 O OE2 . GLU C  1 376 ? -6.131  -27.127 -49.529  1.00 62.89  ? 376 GLU C OE2 1 
ATOM   11229 N N   . LYS C  1 377 ? -0.722  -25.376 -45.799  1.00 54.26  ? 377 LYS C N   1 
ATOM   11230 C CA  . LYS C  1 377 ? -0.177  -25.954 -44.582  1.00 57.10  ? 377 LYS C CA  1 
ATOM   11231 C C   . LYS C  1 377 ? 0.563   -24.939 -43.723  1.00 60.78  ? 377 LYS C C   1 
ATOM   11232 O O   . LYS C  1 377 ? 1.289   -25.336 -42.806  1.00 66.12  ? 377 LYS C O   1 
ATOM   11233 C CB  . LYS C  1 377 ? 0.748   -27.122 -44.929  1.00 57.85  ? 377 LYS C CB  1 
ATOM   11234 C CG  . LYS C  1 377 ? 0.011   -28.383 -45.367  1.00 60.51  ? 377 LYS C CG  1 
ATOM   11235 C CD  . LYS C  1 377 ? 0.982   -29.506 -45.677  1.00 63.25  ? 377 LYS C CD  1 
ATOM   11236 C CE  . LYS C  1 377 ? 1.747   -29.239 -46.965  1.00 63.67  ? 377 LYS C CE  1 
ATOM   11237 N NZ  . LYS C  1 377 ? 3.057   -29.951 -46.967  1.00 67.72  ? 377 LYS C NZ  1 
ATOM   11238 N N   . GLU C  1 378 ? 0.393   -23.649 -43.980  1.00 55.55  ? 378 GLU C N   1 
ATOM   11239 C CA  . GLU C  1 378 ? 1.012   -22.609 -43.163  1.00 50.01  ? 378 GLU C CA  1 
ATOM   11240 C C   . GLU C  1 378 ? -0.090  -21.988 -42.306  1.00 46.70  ? 378 GLU C C   1 
ATOM   11241 O O   . GLU C  1 378 ? -0.915  -21.222 -42.804  1.00 49.83  ? 378 GLU C O   1 
ATOM   11242 C CB  . GLU C  1 378 ? 1.726   -21.583 -44.044  1.00 46.73  ? 378 GLU C CB  1 
ATOM   11243 C CG  . GLU C  1 378 ? 2.889   -22.167 -44.853  1.00 51.91  ? 378 GLU C CG  1 
ATOM   11244 C CD  . GLU C  1 378 ? 4.213   -22.192 -44.094  1.00 61.89  ? 378 GLU C CD  1 
ATOM   11245 O OE1 . GLU C  1 378 ? 5.259   -22.399 -44.746  1.00 64.30  ? 378 GLU C OE1 1 
ATOM   11246 O OE2 . GLU C  1 378 ? 4.216   -22.005 -42.855  1.00 61.56  ? 378 GLU C OE2 1 
ATOM   11247 N N   . GLU C  1 379 ? -0.114  -22.333 -41.012  1.00 47.60  ? 379 GLU C N   1 
ATOM   11248 C CA  . GLU C  1 379 ? -1.205  -21.872 -40.153  1.00 47.22  ? 379 GLU C CA  1 
ATOM   11249 C C   . GLU C  1 379 ? -1.202  -20.354 -39.976  1.00 50.32  ? 379 GLU C C   1 
ATOM   11250 O O   . GLU C  1 379 ? -2.246  -19.767 -39.666  1.00 51.66  ? 379 GLU C O   1 
ATOM   11251 C CB  . GLU C  1 379 ? -1.137  -22.563 -38.789  1.00 48.00  ? 379 GLU C CB  1 
ATOM   11252 N N   . TRP C  1 380 ? -0.053  -19.703 -40.165  1.00 47.28  ? 380 TRP C N   1 
ATOM   11253 C CA  . TRP C  1 380 ? 0.059   -18.264 -39.947  1.00 46.36  ? 380 TRP C CA  1 
ATOM   11254 C C   . TRP C  1 380 ? -0.324  -17.450 -41.173  1.00 46.67  ? 380 TRP C C   1 
ATOM   11255 O O   . TRP C  1 380 ? -0.296  -16.216 -41.108  1.00 47.83  ? 380 TRP C O   1 
ATOM   11256 C CB  . TRP C  1 380 ? 1.481   -17.899 -39.517  1.00 46.01  ? 380 TRP C CB  1 
ATOM   11257 C CG  . TRP C  1 380 ? 2.504   -18.438 -40.443  1.00 48.76  ? 380 TRP C CG  1 
ATOM   11258 C CD1 . TRP C  1 380 ? 2.956   -19.723 -40.507  1.00 52.91  ? 380 TRP C CD1 1 
ATOM   11259 C CD2 . TRP C  1 380 ? 3.199   -17.718 -41.462  1.00 49.97  ? 380 TRP C CD2 1 
ATOM   11260 N NE1 . TRP C  1 380 ? 3.897   -19.848 -41.500  1.00 54.66  ? 380 TRP C NE1 1 
ATOM   11261 C CE2 . TRP C  1 380 ? 4.063   -18.629 -42.103  1.00 53.03  ? 380 TRP C CE2 1 
ATOM   11262 C CE3 . TRP C  1 380 ? 3.174   -16.393 -41.896  1.00 50.03  ? 380 TRP C CE3 1 
ATOM   11263 C CZ2 . TRP C  1 380 ? 4.892   -18.256 -43.151  1.00 49.85  ? 380 TRP C CZ2 1 
ATOM   11264 C CZ3 . TRP C  1 380 ? 4.000   -16.024 -42.927  1.00 50.61  ? 380 TRP C CZ3 1 
ATOM   11265 C CH2 . TRP C  1 380 ? 4.848   -16.952 -43.546  1.00 51.24  ? 380 TRP C CH2 1 
ATOM   11266 N N   . ILE C  1 381 ? -0.662  -18.109 -42.278  1.00 44.03  ? 381 ILE C N   1 
ATOM   11267 C CA  . ILE C  1 381 ? -1.139  -17.455 -43.492  1.00 41.53  ? 381 ILE C CA  1 
ATOM   11268 C C   . ILE C  1 381 ? -2.609  -17.797 -43.670  1.00 43.60  ? 381 ILE C C   1 
ATOM   11269 O O   . ILE C  1 381 ? -2.989  -18.972 -43.641  1.00 45.28  ? 381 ILE C O   1 
ATOM   11270 C CB  . ILE C  1 381 ? -0.324  -17.878 -44.725  1.00 36.94  ? 381 ILE C CB  1 
ATOM   11271 C CG1 . ILE C  1 381 ? 1.090   -17.309 -44.618  1.00 42.31  ? 381 ILE C CG1 1 
ATOM   11272 C CG2 . ILE C  1 381 ? -0.999  -17.403 -46.020  1.00 35.12  ? 381 ILE C CG2 1 
ATOM   11273 C CD1 . ILE C  1 381 ? 2.051   -17.837 -45.644  1.00 40.37  ? 381 ILE C CD1 1 
ATOM   11274 N N   . GLU C  1 382 ? -3.433  -16.768 -43.847  1.00 45.89  ? 382 GLU C N   1 
ATOM   11275 C CA  . GLU C  1 382 ? -4.839  -16.933 -44.194  1.00 46.15  ? 382 GLU C CA  1 
ATOM   11276 C C   . GLU C  1 382 ? -5.084  -16.293 -45.555  1.00 42.22  ? 382 GLU C C   1 
ATOM   11277 O O   . GLU C  1 382 ? -5.015  -15.062 -45.688  1.00 39.91  ? 382 GLU C O   1 
ATOM   11278 C CB  . GLU C  1 382 ? -5.735  -16.308 -43.136  1.00 46.45  ? 382 GLU C CB  1 
ATOM   11279 C CG  . GLU C  1 382 ? -7.209  -16.552 -43.363  1.00 51.92  ? 382 GLU C CG  1 
ATOM   11280 C CD  . GLU C  1 382 ? -8.053  -16.000 -42.234  1.00 59.97  ? 382 GLU C CD  1 
ATOM   11281 O OE1 . GLU C  1 382 ? -9.250  -15.725 -42.473  1.00 63.02  ? 382 GLU C OE1 1 
ATOM   11282 O OE2 . GLU C  1 382 ? -7.521  -15.855 -41.107  1.00 59.90  ? 382 GLU C OE2 1 
ATOM   11283 N N   . THR C  1 383 ? -5.370  -17.114 -46.558  1.00 36.19  ? 383 THR C N   1 
ATOM   11284 C CA  . THR C  1 383 ? -5.765  -16.560 -47.840  1.00 36.21  ? 383 THR C CA  1 
ATOM   11285 C C   . THR C  1 383 ? -7.206  -16.084 -47.734  1.00 36.57  ? 383 THR C C   1 
ATOM   11286 O O   . THR C  1 383 ? -8.037  -16.710 -47.072  1.00 38.57  ? 383 THR C O   1 
ATOM   11287 C CB  . THR C  1 383 ? -5.594  -17.565 -48.993  1.00 35.25  ? 383 THR C CB  1 
ATOM   11288 O OG1 . THR C  1 383 ? -6.374  -18.747 -48.765  1.00 36.93  ? 383 THR C OG1 1 
ATOM   11289 C CG2 . THR C  1 383 ? -4.143  -17.955 -49.149  1.00 32.09  ? 383 THR C CG2 1 
ATOM   11290 N N   . LEU C  1 384 ? -7.483  -14.951 -48.358  1.00 32.69  ? 384 LEU C N   1 
ATOM   11291 C CA  . LEU C  1 384 ? -8.776  -14.299 -48.268  1.00 33.14  ? 384 LEU C CA  1 
ATOM   11292 C C   . LEU C  1 384 ? -9.394  -14.175 -49.652  1.00 32.01  ? 384 LEU C C   1 
ATOM   11293 O O   . LEU C  1 384 ? -8.686  -14.039 -50.653  1.00 31.66  ? 384 LEU C O   1 
ATOM   11294 C CB  . LEU C  1 384 ? -8.636  -12.902 -47.651  1.00 33.40  ? 384 LEU C CB  1 
ATOM   11295 C CG  . LEU C  1 384 ? -7.971  -12.810 -46.275  1.00 34.60  ? 384 LEU C CG  1 
ATOM   11296 C CD1 . LEU C  1 384 ? -7.772  -11.350 -45.882  1.00 34.68  ? 384 LEU C CD1 1 
ATOM   11297 C CD2 . LEU C  1 384 ? -8.851  -13.519 -45.259  1.00 36.34  ? 384 LEU C CD2 1 
ATOM   11298 N N   . THR C  1 385 ? -10.722 -14.220 -49.701  1.00 33.67  ? 385 THR C N   1 
ATOM   11299 C CA  . THR C  1 385 ? -11.421 -13.673 -50.851  1.00 34.95  ? 385 THR C CA  1 
ATOM   11300 C C   . THR C  1 385 ? -11.327 -12.149 -50.834  1.00 36.24  ? 385 THR C C   1 
ATOM   11301 O O   . THR C  1 385 ? -10.928 -11.537 -49.839  1.00 36.80  ? 385 THR C O   1 
ATOM   11302 C CB  . THR C  1 385 ? -12.887 -14.100 -50.863  1.00 33.31  ? 385 THR C CB  1 
ATOM   11303 O OG1 . THR C  1 385 ? -13.561 -13.497 -49.751  1.00 34.86  ? 385 THR C OG1 1 
ATOM   11304 C CG2 . THR C  1 385 ? -13.004 -15.630 -50.788  1.00 35.98  ? 385 THR C CG2 1 
ATOM   11305 N N   . LEU C  1 386 ? -11.691 -11.533 -51.969  1.00 33.86  ? 386 LEU C N   1 
ATOM   11306 C CA  . LEU C  1 386 ? -11.787 -10.076 -52.028  1.00 30.67  ? 386 LEU C CA  1 
ATOM   11307 C C   . LEU C  1 386 ? -12.802 -9.548  -51.023  1.00 32.24  ? 386 LEU C C   1 
ATOM   11308 O O   . LEU C  1 386 ? -12.590 -8.500  -50.399  1.00 34.36  ? 386 LEU C O   1 
ATOM   11309 C CB  . LEU C  1 386 ? -12.175 -9.625  -53.441  1.00 29.79  ? 386 LEU C CB  1 
ATOM   11310 C CG  . LEU C  1 386 ? -11.151 -9.909  -54.548  1.00 28.81  ? 386 LEU C CG  1 
ATOM   11311 C CD1 . LEU C  1 386 ? -11.665 -9.465  -55.921  1.00 27.68  ? 386 LEU C CD1 1 
ATOM   11312 C CD2 . LEU C  1 386 ? -9.819  -9.243  -54.230  1.00 33.16  ? 386 LEU C CD2 1 
ATOM   11313 N N   . GLU C  1 387 ? -13.929 -10.245 -50.884  1.00 33.32  ? 387 GLU C N   1 
ATOM   11314 C CA  . GLU C  1 387 ? -14.960 -9.821  -49.943  1.00 38.86  ? 387 GLU C CA  1 
ATOM   11315 C C   . GLU C  1 387 ? -14.448 -9.873  -48.512  1.00 37.50  ? 387 GLU C C   1 
ATOM   11316 O O   . GLU C  1 387 ? -14.747 -8.988  -47.705  1.00 37.77  ? 387 GLU C O   1 
ATOM   11317 C CB  . GLU C  1 387 ? -16.189 -10.708 -50.100  1.00 51.70  ? 387 GLU C CB  1 
ATOM   11318 C CG  . GLU C  1 387 ? -17.508 -10.009 -49.895  1.00 68.36  ? 387 GLU C CG  1 
ATOM   11319 C CD  . GLU C  1 387 ? -18.673 -10.973 -49.986  1.00 81.89  ? 387 GLU C CD  1 
ATOM   11320 O OE1 . GLU C  1 387 ? -19.134 -11.240 -51.120  1.00 83.82  ? 387 GLU C OE1 1 
ATOM   11321 O OE2 . GLU C  1 387 ? -19.126 -11.458 -48.924  1.00 90.02  ? 387 GLU C OE2 1 
ATOM   11322 N N   . GLU C  1 388 ? -13.685 -10.919 -48.175  1.00 39.85  ? 388 GLU C N   1 
ATOM   11323 C CA  . GLU C  1 388 ? -13.098 -11.013 -46.841  1.00 39.73  ? 388 GLU C CA  1 
ATOM   11324 C C   . GLU C  1 388 ? -12.046 -9.932  -46.630  1.00 39.01  ? 388 GLU C C   1 
ATOM   11325 O O   . GLU C  1 388 ? -11.970 -9.339  -45.549  1.00 40.93  ? 388 GLU C O   1 
ATOM   11326 C CB  . GLU C  1 388 ? -12.499 -12.406 -46.628  1.00 38.97  ? 388 GLU C CB  1 
ATOM   11327 C CG  . GLU C  1 388 ? -13.539 -13.519 -46.644  1.00 44.26  ? 388 GLU C CG  1 
ATOM   11328 C CD  . GLU C  1 388 ? -12.943 -14.926 -46.648  1.00 51.59  ? 388 GLU C CD  1 
ATOM   11329 O OE1 . GLU C  1 388 ? -11.831 -15.129 -47.192  1.00 46.69  ? 388 GLU C OE1 1 
ATOM   11330 O OE2 . GLU C  1 388 ? -13.598 -15.833 -46.079  1.00 55.47  ? 388 GLU C OE2 1 
ATOM   11331 N N   . ALA C  1 389 ? -11.238 -9.648  -47.661  1.00 37.92  ? 389 ALA C N   1 
ATOM   11332 C CA  . ALA C  1 389 ? -10.243 -8.589  -47.539  1.00 38.02  ? 389 ALA C CA  1 
ATOM   11333 C C   . ALA C  1 389 ? -10.901 -7.227  -47.374  1.00 43.35  ? 389 ALA C C   1 
ATOM   11334 O O   . ALA C  1 389 ? -10.378 -6.366  -46.653  1.00 43.26  ? 389 ALA C O   1 
ATOM   11335 C CB  . ALA C  1 389 ? -9.310  -8.588  -48.753  1.00 38.55  ? 389 ALA C CB  1 
ATOM   11336 N N   . MET C  1 390 ? -12.049 -7.014  -48.017  1.00 45.25  ? 390 MET C N   1 
ATOM   11337 C CA  . MET C  1 390 ? -12.720 -5.728  -47.884  1.00 45.50  ? 390 MET C CA  1 
ATOM   11338 C C   . MET C  1 390 ? -13.271 -5.540  -46.479  1.00 49.76  ? 390 MET C C   1 
ATOM   11339 O O   . MET C  1 390 ? -13.233 -4.431  -45.935  1.00 51.28  ? 390 MET C O   1 
ATOM   11340 C CB  . MET C  1 390 ? -13.843 -5.614  -48.907  1.00 49.87  ? 390 MET C CB  1 
ATOM   11341 C CG  . MET C  1 390 ? -14.445 -4.221  -49.000  1.00 57.01  ? 390 MET C CG  1 
ATOM   11342 S SD  . MET C  1 390 ? -15.945 -4.188  -49.994  1.00 62.56  ? 390 MET C SD  1 
ATOM   11343 C CE  . MET C  1 390 ? -15.633 -5.569  -51.094  1.00 63.07  ? 390 MET C CE  1 
ATOM   11344 N N   . ARG C  1 391 ? -13.741 -6.620  -45.929  1.00 45.66  ? 391 ARG C N   1 
ATOM   11345 C CA  . ARG C  1 391 ? -14.446 -6.512  -44.672  1.00 46.94  ? 391 ARG C CA  1 
ATOM   11346 C C   . ARG C  1 391 ? -13.723 -6.871  -43.396  1.00 46.93  ? 391 ARG C C   1 
ATOM   11347 O O   . ARG C  1 391 ? -14.255 -6.691  -42.339  1.00 49.49  ? 391 ARG C O   1 
ATOM   11348 C CB  . ARG C  1 391 ? -15.739 -7.317  -44.793  1.00 50.15  ? 391 ARG C CB  1 
ATOM   11349 C CG  . ARG C  1 391 ? -16.722 -6.883  -45.838  1.00 55.22  ? 391 ARG C CG  1 
ATOM   11350 C CD  . ARG C  1 391 ? -18.101 -7.288  -45.376  1.00 62.60  ? 391 ARG C CD  1 
ATOM   11351 N NE  . ARG C  1 391 ? -18.836 -8.049  -46.367  1.00 70.19  ? 391 ARG C NE  1 
ATOM   11352 C CZ  . ARG C  1 391 ? -20.148 -8.255  -46.311  1.00 76.41  ? 391 ARG C CZ  1 
ATOM   11353 N NH1 . ARG C  1 391 ? -20.851 -7.764  -45.302  1.00 78.17  ? 391 ARG C NH1 1 
ATOM   11354 N NH2 . ARG C  1 391 ? -20.757 -8.962  -47.251  1.00 79.21  ? 391 ARG C NH2 1 
ATOM   11355 N N   . LYS C  1 392 ? -12.520 -7.331  -43.489  1.00 44.36  ? 392 LYS C N   1 
ATOM   11356 C CA  . LYS C  1 392 ? -11.841 -7.801  -42.344  1.00 47.67  ? 392 LYS C CA  1 
ATOM   11357 C C   . LYS C  1 392 ? -11.513 -6.658  -41.415  1.00 53.87  ? 392 LYS C C   1 
ATOM   11358 O O   . LYS C  1 392 ? -11.046 -5.653  -41.854  1.00 55.33  ? 392 LYS C O   1 
ATOM   11359 C CB  . LYS C  1 392 ? -10.616 -8.582  -42.756  1.00 43.69  ? 392 LYS C CB  1 
ATOM   11360 C CG  . LYS C  1 392 ? -9.597  -8.808  -41.672  1.00 50.71  ? 392 LYS C CG  1 
ATOM   11361 C CD  . LYS C  1 392 ? -9.332  -10.285 -41.436  1.00 56.67  ? 392 LYS C CD  1 
ATOM   11362 C CE  . LYS C  1 392 ? -10.138 -11.184 -42.347  1.00 54.47  ? 392 LYS C CE  1 
ATOM   11363 N NZ  . LYS C  1 392 ? -10.639 -12.368 -41.619  1.00 54.88  ? 392 LYS C NZ  1 
ATOM   11364 N N   . GLU C  1 393 ? -11.754 -6.828  -40.121  1.00 57.34  ? 393 GLU C N   1 
ATOM   11365 C CA  . GLU C  1 393 ? -11.534 -5.747  -39.136  1.00 57.54  ? 393 GLU C CA  1 
ATOM   11366 C C   . GLU C  1 393 ? -10.197 -5.662  -38.500  1.00 56.91  ? 393 GLU C C   1 
ATOM   11367 O O   . GLU C  1 393 ? -9.670  -4.614  -38.294  1.00 54.77  ? 393 GLU C O   1 
ATOM   11368 C CB  . GLU C  1 393 ? -12.579 -5.872  -38.057  1.00 65.93  ? 393 GLU C CB  1 
ATOM   11369 C CG  . GLU C  1 393 ? -13.777 -6.724  -38.421  1.00 76.21  ? 393 GLU C CG  1 
ATOM   11370 C CD  . GLU C  1 393 ? -15.099 -6.006  -38.205  1.00 81.71  ? 393 GLU C CD  1 
ATOM   11371 O OE1 . GLU C  1 393 ? -15.058 -4.803  -37.902  1.00 83.20  ? 393 GLU C OE1 1 
ATOM   11372 O OE2 . GLU C  1 393 ? -16.173 -6.634  -38.337  1.00 80.23  ? 393 GLU C OE2 1 
ATOM   11373 N N   . ASP C  1 394 ? -9.634  -6.786  -38.230  1.00 60.71  ? 394 ASP C N   1 
ATOM   11374 C CA  . ASP C  1 394 ? -8.380  -6.851  -37.594  1.00 63.04  ? 394 ASP C CA  1 
ATOM   11375 C C   . ASP C  1 394 ? -7.210  -6.588  -38.500  1.00 59.89  ? 394 ASP C C   1 
ATOM   11376 O O   . ASP C  1 394 ? -6.265  -7.303  -38.487  1.00 60.60  ? 394 ASP C O   1 
ATOM   11377 C CB  . ASP C  1 394 ? -8.289  -8.154  -36.924  1.00 70.36  ? 394 ASP C CB  1 
ATOM   11378 C CG  . ASP C  1 394 ? -8.756  -9.311  -37.766  1.00 75.68  ? 394 ASP C CG  1 
ATOM   11379 O OD1 . ASP C  1 394 ? -9.686  -9.146  -38.570  1.00 76.61  ? 394 ASP C OD1 1 
ATOM   11380 O OD2 . ASP C  1 394 ? -8.214  -10.418 -37.572  1.00 76.77  ? 394 ASP C OD2 1 
ATOM   11381 N N   . VAL C  1 395 ? -7.264  -5.502  -39.208  1.00 54.41  ? 395 VAL C N   1 
ATOM   11382 C CA  . VAL C  1 395 ? -6.233  -5.091  -40.127  1.00 50.19  ? 395 VAL C CA  1 
ATOM   11383 C C   . VAL C  1 395 ? -5.963  -3.662  -39.916  1.00 49.89  ? 395 VAL C C   1 
ATOM   11384 O O   . VAL C  1 395 ? -6.787  -2.986  -39.416  1.00 53.40  ? 395 VAL C O   1 
ATOM   11385 C CB  . VAL C  1 395 ? -6.731  -5.272  -41.595  1.00 43.03  ? 395 VAL C CB  1 
ATOM   11386 C CG1 . VAL C  1 395 ? -6.973  -6.727  -41.912  1.00 45.25  ? 395 VAL C CG1 1 
ATOM   11387 C CG2 . VAL C  1 395 ? -7.943  -4.426  -41.892  1.00 39.09  ? 395 VAL C CG2 1 
ATOM   11388 N N   . LYS C  1 396 ? -4.846  -3.182  -40.358  1.00 46.48  ? 396 LYS C N   1 
ATOM   11389 C CA  . LYS C  1 396 ? -4.525  -1.782  -40.241  1.00 45.51  ? 396 LYS C CA  1 
ATOM   11390 C C   . LYS C  1 396 ? -5.142  -0.963  -41.347  1.00 46.69  ? 396 LYS C C   1 
ATOM   11391 O O   . LYS C  1 396 ? -5.271  -1.440  -42.442  1.00 41.57  ? 396 LYS C O   1 
ATOM   11392 C CB  . LYS C  1 396 ? -3.081  -1.509  -40.159  1.00 44.40  ? 396 LYS C CB  1 
ATOM   11393 C CG  . LYS C  1 396 ? -2.708  -0.115  -39.757  1.00 46.39  ? 396 LYS C CG  1 
ATOM   11394 C CD  . LYS C  1 396 ? -1.419  -0.090  -38.970  1.00 45.13  ? 396 LYS C CD  1 
ATOM   11395 C CE  . LYS C  1 396 ? -0.458  0.915   -39.554  1.00 43.47  ? 396 LYS C CE  1 
ATOM   11396 N NZ  . LYS C  1 396 ? 0.147   1.788   -38.540  1.00 45.88  ? 396 LYS C NZ  1 
ATOM   11397 N N   . THR C  1 397 ? -5.299  0.316   -41.116  1.00 38.25  ? 397 THR C N   1 
ATOM   11398 C CA  . THR C  1 397 ? -6.139  1.167   -41.957  1.00 41.85  ? 397 THR C CA  1 
ATOM   11399 C C   . THR C  1 397 ? -5.514  2.553   -42.080  1.00 40.52  ? 397 THR C C   1 
ATOM   11400 O O   . THR C  1 397 ? -4.859  3.033   -41.154  1.00 41.19  ? 397 THR C O   1 
ATOM   11401 C CB  . THR C  1 397 ? -7.543  1.256   -41.336  1.00 49.90  ? 397 THR C CB  1 
ATOM   11402 O OG1 . THR C  1 397 ? -8.290  0.078   -41.657  1.00 51.93  ? 397 THR C OG1 1 
ATOM   11403 C CG2 . THR C  1 397 ? -8.295  2.527   -41.762  1.00 52.62  ? 397 THR C CG2 1 
ATOM   11404 N N   . GLU C  1 398 ? -5.706  3.193   -43.233  1.00 42.04  ? 398 GLU C N   1 
ATOM   11405 C CA  . GLU C  1 398 ? -5.205  4.547   -43.438  1.00 41.74  ? 398 GLU C CA  1 
ATOM   11406 C C   . GLU C  1 398 ? -6.099  5.279   -44.428  1.00 36.71  ? 398 GLU C C   1 
ATOM   11407 O O   . GLU C  1 398 ? -6.592  4.684   -45.388  1.00 36.84  ? 398 GLU C O   1 
ATOM   11408 C CB  . GLU C  1 398 ? -3.757  4.541   -43.942  1.00 44.80  ? 398 GLU C CB  1 
ATOM   11409 C CG  . GLU C  1 398 ? -3.126  5.919   -44.021  1.00 53.14  ? 398 GLU C CG  1 
ATOM   11410 C CD  . GLU C  1 398 ? -3.000  6.566   -42.651  1.00 69.11  ? 398 GLU C CD  1 
ATOM   11411 O OE1 . GLU C  1 398 ? -2.279  6.006   -41.792  1.00 74.78  ? 398 GLU C OE1 1 
ATOM   11412 O OE2 . GLU C  1 398 ? -3.634  7.625   -42.427  1.00 72.28  ? 398 GLU C OE2 1 
ATOM   11413 N N   . VAL C  1 399 ? -6.312  6.569   -44.198  1.00 35.77  ? 399 VAL C N   1 
ATOM   11414 C CA  . VAL C  1 399 ? -7.068  7.404   -45.129  1.00 37.58  ? 399 VAL C CA  1 
ATOM   11415 C C   . VAL C  1 399 ? -6.079  8.121   -46.036  1.00 40.41  ? 399 VAL C C   1 
ATOM   11416 O O   . VAL C  1 399 ? -5.074  8.668   -45.560  1.00 45.79  ? 399 VAL C O   1 
ATOM   11417 C CB  . VAL C  1 399 ? -7.958  8.412   -44.387  1.00 40.77  ? 399 VAL C CB  1 
ATOM   11418 C CG1 . VAL C  1 399 ? -8.656  9.321   -45.385  1.00 37.45  ? 399 VAL C CG1 1 
ATOM   11419 C CG2 . VAL C  1 399 ? -8.975  7.695   -43.517  1.00 39.26  ? 399 VAL C CG2 1 
ATOM   11420 N N   . ILE C  1 400 ? -6.354  8.111   -47.336  1.00 37.38  ? 400 ILE C N   1 
ATOM   11421 C CA  . ILE C  1 400 ? -5.534  8.781   -48.338  1.00 43.30  ? 400 ILE C CA  1 
ATOM   11422 C C   . ILE C  1 400 ? -6.406  9.809   -49.058  1.00 39.91  ? 400 ILE C C   1 
ATOM   11423 O O   . ILE C  1 400 ? -7.579  9.551   -49.344  1.00 40.39  ? 400 ILE C O   1 
ATOM   11424 C CB  . ILE C  1 400 ? -4.904  7.763   -49.320  1.00 45.16  ? 400 ILE C CB  1 
ATOM   11425 C CG1 . ILE C  1 400 ? -4.094  8.464   -50.407  1.00 52.84  ? 400 ILE C CG1 1 
ATOM   11426 C CG2 . ILE C  1 400 ? -5.948  6.877   -49.965  1.00 41.68  ? 400 ILE C CG2 1 
ATOM   11427 C CD1 . ILE C  1 400 ? -3.450  7.499   -51.381  1.00 55.18  ? 400 ILE C CD1 1 
ATOM   11428 N N   . GLU C  1 401 ? -5.854  10.994  -49.301  1.00 36.39  ? 401 GLU C N   1 
ATOM   11429 C CA  . GLU C  1 401 ? -6.654  12.076  -49.867  1.00 41.17  ? 401 GLU C CA  1 
ATOM   11430 C C   . GLU C  1 401 ? -6.447  12.276  -51.365  1.00 43.23  ? 401 GLU C C   1 
ATOM   11431 O O   . GLU C  1 401 ? -7.359  12.763  -52.043  1.00 42.65  ? 401 GLU C O   1 
ATOM   11432 C CB  . GLU C  1 401 ? -6.361  13.393  -49.145  1.00 42.43  ? 401 GLU C CB  1 
ATOM   11433 C CG  . GLU C  1 401 ? -6.844  13.430  -47.700  1.00 51.70  ? 401 GLU C CG  1 
ATOM   11434 C CD  . GLU C  1 401 ? -8.352  13.275  -47.590  1.00 57.67  ? 401 GLU C CD  1 
ATOM   11435 O OE1 . GLU C  1 401 ? -9.081  14.129  -48.134  1.00 61.89  ? 401 GLU C OE1 1 
ATOM   11436 O OE2 . GLU C  1 401 ? -8.809  12.286  -46.978  1.00 59.36  ? 401 GLU C OE2 1 
ATOM   11437 N N   . SER C  1 402 ? -5.281  11.911  -51.898  1.00 43.36  ? 402 SER C N   1 
ATOM   11438 C CA  . SER C  1 402 ? -4.959  12.176  -53.294  1.00 39.38  ? 402 SER C CA  1 
ATOM   11439 C C   . SER C  1 402 ? -4.022  11.091  -53.815  1.00 41.39  ? 402 SER C C   1 
ATOM   11440 O O   . SER C  1 402 ? -3.159  10.604  -53.079  1.00 39.67  ? 402 SER C O   1 
ATOM   11441 C CB  . SER C  1 402 ? -4.304  13.550  -53.445  1.00 41.28  ? 402 SER C CB  1 
ATOM   11442 O OG  . SER C  1 402 ? -4.042  13.839  -54.807  1.00 46.63  ? 402 SER C OG  1 
ATOM   11443 N N   . VAL C  1 403 ? -4.204  10.699  -55.077  1.00 37.69  ? 403 VAL C N   1 
ATOM   11444 C CA  . VAL C  1 403 ? -3.224  9.855   -55.749  1.00 40.85  ? 403 VAL C CA  1 
ATOM   11445 C C   . VAL C  1 403 ? -2.670  10.619  -56.941  1.00 42.67  ? 403 VAL C C   1 
ATOM   11446 O O   . VAL C  1 403 ? -3.275  11.573  -57.439  1.00 45.84  ? 403 VAL C O   1 
ATOM   11447 C CB  . VAL C  1 403 ? -3.785  8.483   -56.193  1.00 39.53  ? 403 VAL C CB  1 
ATOM   11448 C CG1 . VAL C  1 403 ? -4.294  7.699   -55.000  1.00 35.68  ? 403 VAL C CG1 1 
ATOM   11449 C CG2 . VAL C  1 403 ? -4.874  8.651   -57.257  1.00 42.77  ? 403 VAL C CG2 1 
ATOM   11450 N N   . LYS C  1 404 ? -1.484  10.206  -57.377  1.00 42.08  ? 404 LYS C N   1 
ATOM   11451 C CA  . LYS C  1 404 ? -0.896  10.702  -58.614  1.00 45.69  ? 404 LYS C CA  1 
ATOM   11452 C C   . LYS C  1 404 ? -1.206  9.698   -59.718  1.00 40.83  ? 404 LYS C C   1 
ATOM   11453 O O   . LYS C  1 404 ? -0.871  8.514   -59.596  1.00 36.90  ? 404 LYS C O   1 
ATOM   11454 C CB  . LYS C  1 404 ? 0.609   10.930  -58.468  1.00 50.81  ? 404 LYS C CB  1 
ATOM   11455 C CG  . LYS C  1 404 ? 0.962   12.077  -57.529  1.00 54.70  ? 404 LYS C CG  1 
ATOM   11456 C CD  . LYS C  1 404 ? 2.219   12.814  -57.962  1.00 57.68  ? 404 LYS C CD  1 
ATOM   11457 C CE  . LYS C  1 404 ? 2.504   13.983  -57.027  1.00 58.84  ? 404 LYS C CE  1 
ATOM   11458 N NZ  . LYS C  1 404 ? 3.891   14.511  -57.182  1.00 60.84  ? 404 LYS C NZ  1 
ATOM   11459 N N   . ALA C  1 405 ? -1.857  10.168  -60.780  1.00 42.90  ? 405 ALA C N   1 
ATOM   11460 C CA  . ALA C  1 405 ? -2.360  9.272   -61.820  1.00 41.51  ? 405 ALA C CA  1 
ATOM   11461 C C   . ALA C  1 405 ? -1.236  8.479   -62.472  1.00 40.05  ? 405 ALA C C   1 
ATOM   11462 O O   . ALA C  1 405 ? -0.143  8.999   -62.709  1.00 46.47  ? 405 ALA C O   1 
ATOM   11463 C CB  . ALA C  1 405 ? -3.110  10.070  -62.886  1.00 42.32  ? 405 ALA C CB  1 
ATOM   11464 N N   . GLY C  1 406 ? -1.520  7.219   -62.781  1.00 36.70  ? 406 GLY C N   1 
ATOM   11465 C CA  . GLY C  1 406 ? -0.533  6.374   -63.422  1.00 38.87  ? 406 GLY C CA  1 
ATOM   11466 C C   . GLY C  1 406 ? -1.081  4.989   -63.687  1.00 37.22  ? 406 GLY C C   1 
ATOM   11467 O O   . GLY C  1 406 ? -2.288  4.746   -63.622  1.00 37.07  ? 406 GLY C O   1 
ATOM   11468 N N   . THR C  1 407 ? -0.161  4.082   -63.994  1.00 32.58  ? 407 THR C N   1 
ATOM   11469 C CA  . THR C  1 407 ? -0.455  2.680   -64.248  1.00 36.39  ? 407 THR C CA  1 
ATOM   11470 C C   . THR C  1 407 ? 0.595   1.849   -63.540  1.00 37.67  ? 407 THR C C   1 
ATOM   11471 O O   . THR C  1 407 ? 1.592   2.380   -63.047  1.00 41.56  ? 407 THR C O   1 
ATOM   11472 C CB  . THR C  1 407 ? -0.382  2.343   -65.728  1.00 36.09  ? 407 THR C CB  1 
ATOM   11473 O OG1 . THR C  1 407 ? 0.983   2.494   -66.134  1.00 31.93  ? 407 THR C OG1 1 
ATOM   11474 C CG2 . THR C  1 407 ? -1.263  3.281   -66.548  1.00 43.57  ? 407 THR C CG2 1 
ATOM   11475 N N   . TRP C  1 408 ? 0.408   0.528   -63.548  1.00 34.31  ? 408 TRP C N   1 
ATOM   11476 C CA  . TRP C  1 408 ? 1.434   -0.341  -62.987  1.00 34.39  ? 408 TRP C CA  1 
ATOM   11477 C C   . TRP C  1 408 ? 2.634   -0.487  -63.900  1.00 37.68  ? 408 TRP C C   1 
ATOM   11478 O O   . TRP C  1 408 ? 3.500   -1.321  -63.625  1.00 40.66  ? 408 TRP C O   1 
ATOM   11479 C CB  . TRP C  1 408 ? 0.872   -1.725  -62.641  1.00 36.11  ? 408 TRP C CB  1 
ATOM   11480 C CG  . TRP C  1 408 ? 0.243   -2.514  -63.766  1.00 38.62  ? 408 TRP C CG  1 
ATOM   11481 C CD1 . TRP C  1 408 ? 0.091   -2.135  -65.081  1.00 36.32  ? 408 TRP C CD1 1 
ATOM   11482 C CD2 . TRP C  1 408 ? -0.327  -3.825  -63.661  1.00 38.80  ? 408 TRP C CD2 1 
ATOM   11483 N NE1 . TRP C  1 408 ? -0.542  -3.128  -65.783  1.00 35.93  ? 408 TRP C NE1 1 
ATOM   11484 C CE2 . TRP C  1 408 ? -0.807  -4.177  -64.939  1.00 39.00  ? 408 TRP C CE2 1 
ATOM   11485 C CE3 . TRP C  1 408 ? -0.490  -4.732  -62.604  1.00 37.99  ? 408 TRP C CE3 1 
ATOM   11486 C CZ2 . TRP C  1 408 ? -1.436  -5.400  -65.190  1.00 34.45  ? 408 TRP C CZ2 1 
ATOM   11487 C CZ3 . TRP C  1 408 ? -1.110  -5.943  -62.856  1.00 37.02  ? 408 TRP C CZ3 1 
ATOM   11488 C CH2 . TRP C  1 408 ? -1.578  -6.266  -64.140  1.00 37.00  ? 408 TRP C CH2 1 
ATOM   11489 N N   . PHE C  1 409 ? 2.692   0.282   -64.985  1.00 37.87  ? 409 PHE C N   1 
ATOM   11490 C CA  . PHE C  1 409 ? 3.890   0.372   -65.809  1.00 41.23  ? 409 PHE C CA  1 
ATOM   11491 C C   . PHE C  1 409 ? 4.577   1.686   -65.454  1.00 43.08  ? 409 PHE C C   1 
ATOM   11492 O O   . PHE C  1 409 ? 4.173   2.757   -65.913  1.00 39.04  ? 409 PHE C O   1 
ATOM   11493 C CB  . PHE C  1 409 ? 3.558   0.283   -67.292  1.00 40.22  ? 409 PHE C CB  1 
ATOM   11494 C CG  . PHE C  1 409 ? 4.746   -0.053  -68.148  1.00 46.10  ? 409 PHE C CG  1 
ATOM   11495 C CD1 . PHE C  1 409 ? 5.738   0.886   -68.376  1.00 50.49  ? 409 PHE C CD1 1 
ATOM   11496 C CD2 . PHE C  1 409 ? 4.880   -1.312  -68.711  1.00 49.81  ? 409 PHE C CD2 1 
ATOM   11497 C CE1 . PHE C  1 409 ? 6.838   0.581   -69.157  1.00 53.79  ? 409 PHE C CE1 1 
ATOM   11498 C CE2 . PHE C  1 409 ? 5.977   -1.623  -69.496  1.00 53.28  ? 409 PHE C CE2 1 
ATOM   11499 C CZ  . PHE C  1 409 ? 6.957   -0.674  -69.718  1.00 55.20  ? 409 PHE C CZ  1 
ATOM   11500 N N   . ASP C  1 410 ? 5.597   1.598   -64.601  1.00 47.37  ? 410 ASP C N   1 
ATOM   11501 C CA  . ASP C  1 410 ? 6.447   2.716   -64.201  1.00 52.81  ? 410 ASP C CA  1 
ATOM   11502 C C   . ASP C  1 410 ? 5.669   3.847   -63.533  1.00 49.77  ? 410 ASP C C   1 
ATOM   11503 O O   . ASP C  1 410 ? 6.218   4.938   -63.341  1.00 52.19  ? 410 ASP C O   1 
ATOM   11504 C CB  . ASP C  1 410 ? 7.251   3.266   -65.395  1.00 56.77  ? 410 ASP C CB  1 
ATOM   11505 C CG  . ASP C  1 410 ? 8.303   2.278   -65.906  1.00 63.42  ? 410 ASP C CG  1 
ATOM   11506 O OD1 . ASP C  1 410 ? 8.245   1.094   -65.509  1.00 64.44  ? 410 ASP C OD1 1 
ATOM   11507 O OD2 . ASP C  1 410 ? 9.179   2.675   -66.713  1.00 65.80  ? 410 ASP C OD2 1 
ATOM   11508 N N   . GLY C  1 411 ? 4.409   3.621   -63.168  1.00 43.63  ? 411 GLY C N   1 
ATOM   11509 C CA  . GLY C  1 411 ? 3.613   4.675   -62.573  1.00 42.95  ? 411 GLY C CA  1 
ATOM   11510 C C   . GLY C  1 411 ? 3.157   5.771   -63.516  1.00 44.70  ? 411 GLY C C   1 
ATOM   11511 O O   . GLY C  1 411 ? 2.758   6.841   -63.045  1.00 48.33  ? 411 GLY C O   1 
ATOM   11512 N N   . ASN C  1 412 ? 3.196   5.545   -64.829  1.00 42.83  ? 412 ASN C N   1 
ATOM   11513 C CA  . ASN C  1 412 ? 2.805   6.569   -65.798  1.00 43.71  ? 412 ASN C CA  1 
ATOM   11514 C C   . ASN C  1 412 ? 2.096   5.897   -66.977  1.00 41.43  ? 412 ASN C C   1 
ATOM   11515 O O   . ASN C  1 412 ? 1.838   4.690   -66.971  1.00 42.19  ? 412 ASN C O   1 
ATOM   11516 C CB  . ASN C  1 412 ? 4.019   7.408   -66.236  1.00 46.02  ? 412 ASN C CB  1 
ATOM   11517 C CG  . ASN C  1 412 ? 5.116   6.575   -66.887  1.00 46.89  ? 412 ASN C CG  1 
ATOM   11518 O OD1 . ASN C  1 412 ? 4.885   5.870   -67.874  1.00 49.71  ? 412 ASN C OD1 1 
ATOM   11519 N ND2 . ASN C  1 412 ? 6.322   6.664   -66.339  1.00 44.67  ? 412 ASN C ND2 1 
ATOM   11520 N N   . PHE C  1 413 ? 1.782   6.699   -68.001  1.00 39.57  ? 413 PHE C N   1 
ATOM   11521 C CA  . PHE C  1 413 ? 0.969   6.287   -69.141  1.00 35.38  ? 413 PHE C CA  1 
ATOM   11522 C C   . PHE C  1 413 ? 1.775   6.216   -70.433  1.00 36.58  ? 413 PHE C C   1 
ATOM   11523 O O   . PHE C  1 413 ? 1.192   6.186   -71.518  1.00 38.52  ? 413 PHE C O   1 
ATOM   11524 C CB  . PHE C  1 413 ? -0.211  7.246   -69.335  1.00 38.59  ? 413 PHE C CB  1 
ATOM   11525 C CG  . PHE C  1 413 ? -1.196  7.255   -68.194  1.00 39.59  ? 413 PHE C CG  1 
ATOM   11526 C CD1 . PHE C  1 413 ? -2.231  6.333   -68.147  1.00 39.38  ? 413 PHE C CD1 1 
ATOM   11527 C CD2 . PHE C  1 413 ? -1.093  8.190   -67.175  1.00 41.33  ? 413 PHE C CD2 1 
ATOM   11528 C CE1 . PHE C  1 413 ? -3.140  6.339   -67.098  1.00 38.72  ? 413 PHE C CE1 1 
ATOM   11529 C CE2 . PHE C  1 413 ? -2.001  8.194   -66.114  1.00 38.02  ? 413 PHE C CE2 1 
ATOM   11530 C CZ  . PHE C  1 413 ? -3.025  7.272   -66.085  1.00 36.05  ? 413 PHE C CZ  1 
ATOM   11531 N N   . LEU C  1 414 ? 3.103   6.186   -70.342  1.00 37.91  ? 414 LEU C N   1 
ATOM   11532 C CA  . LEU C  1 414 ? 3.916   6.347   -71.540  1.00 48.65  ? 414 LEU C CA  1 
ATOM   11533 C C   . LEU C  1 414 ? 3.825   5.149   -72.478  1.00 48.89  ? 414 LEU C C   1 
ATOM   11534 O O   . LEU C  1 414 ? 4.114   5.294   -73.671  1.00 48.90  ? 414 LEU C O   1 
ATOM   11535 C CB  . LEU C  1 414 ? 5.368   6.614   -71.148  1.00 48.85  ? 414 LEU C CB  1 
ATOM   11536 C CG  . LEU C  1 414 ? 5.590   7.980   -70.492  1.00 49.05  ? 414 LEU C CG  1 
ATOM   11537 C CD1 . LEU C  1 414 ? 7.066   8.302   -70.368  1.00 51.06  ? 414 LEU C CD1 1 
ATOM   11538 C CD2 . LEU C  1 414 ? 4.871   9.071   -71.265  1.00 46.68  ? 414 LEU C CD2 1 
ATOM   11539 N N   . LYS C  1 415 ? 3.417   3.979   -71.983  1.00 42.81  ? 415 LYS C N   1 
ATOM   11540 C CA  . LYS C  1 415 ? 3.273   2.851   -72.886  1.00 46.55  ? 415 LYS C CA  1 
ATOM   11541 C C   . LYS C  1 415 ? 1.973   2.898   -73.690  1.00 47.20  ? 415 LYS C C   1 
ATOM   11542 O O   . LYS C  1 415 ? 1.730   1.992   -74.490  1.00 37.51  ? 415 LYS C O   1 
ATOM   11543 C CB  . LYS C  1 415 ? 3.396   1.527   -72.112  1.00 47.13  ? 415 LYS C CB  1 
ATOM   11544 C CG  . LYS C  1 415 ? 4.840   0.997   -72.024  1.00 52.29  ? 415 LYS C CG  1 
ATOM   11545 C CD  . LYS C  1 415 ? 5.353   0.504   -73.387  1.00 61.50  ? 415 LYS C CD  1 
ATOM   11546 C CE  . LYS C  1 415 ? 6.828   0.846   -73.632  1.00 67.20  ? 415 LYS C CE  1 
ATOM   11547 N NZ  . LYS C  1 415 ? 7.768   -0.146  -73.038  1.00 68.55  ? 415 LYS C NZ  1 
ATOM   11548 N N   . TRP C  1 416 ? 1.139   3.926   -73.521  1.00 42.37  ? 416 TRP C N   1 
ATOM   11549 C CA  . TRP C  1 416 ? -0.084  4.046   -74.307  1.00 43.10  ? 416 TRP C CA  1 
ATOM   11550 C C   . TRP C  1 416 ? -0.264  5.417   -74.946  1.00 43.35  ? 416 TRP C C   1 
ATOM   11551 O O   . TRP C  1 416 ? -1.205  5.592   -75.730  1.00 42.25  ? 416 TRP C O   1 
ATOM   11552 C CB  . TRP C  1 416 ? -1.322  3.732   -73.439  1.00 36.37  ? 416 TRP C CB  1 
ATOM   11553 C CG  . TRP C  1 416 ? -1.274  2.372   -72.794  1.00 37.25  ? 416 TRP C CG  1 
ATOM   11554 C CD1 . TRP C  1 416 ? -1.795  1.200   -73.292  1.00 36.66  ? 416 TRP C CD1 1 
ATOM   11555 C CD2 . TRP C  1 416 ? -0.658  2.035   -71.547  1.00 37.00  ? 416 TRP C CD2 1 
ATOM   11556 N NE1 . TRP C  1 416 ? -1.551  0.162   -72.416  1.00 31.99  ? 416 TRP C NE1 1 
ATOM   11557 C CE2 . TRP C  1 416 ? -0.846  0.643   -71.346  1.00 33.02  ? 416 TRP C CE2 1 
ATOM   11558 C CE3 . TRP C  1 416 ? 0.028   2.772   -70.569  1.00 35.38  ? 416 TRP C CE3 1 
ATOM   11559 C CZ2 . TRP C  1 416 ? -0.370  -0.020  -70.214  1.00 30.77  ? 416 TRP C CZ2 1 
ATOM   11560 C CZ3 . TRP C  1 416 ? 0.505   2.103   -69.443  1.00 32.42  ? 416 TRP C CZ3 1 
ATOM   11561 C CH2 . TRP C  1 416 ? 0.304   0.724   -69.280  1.00 33.92  ? 416 TRP C CH2 1 
ATOM   11562 N N   . ILE C  1 417 ? 0.600   6.385   -74.644  1.00 44.92  ? 417 ILE C N   1 
ATOM   11563 C CA  . ILE C  1 417 ? 0.451   7.744   -75.144  1.00 49.37  ? 417 ILE C CA  1 
ATOM   11564 C C   . ILE C  1 417 ? 1.786   8.453   -74.980  1.00 51.26  ? 417 ILE C C   1 
ATOM   11565 O O   . ILE C  1 417 ? 2.537   8.177   -74.045  1.00 54.16  ? 417 ILE C O   1 
ATOM   11566 C CB  . ILE C  1 417 ? -0.698  8.483   -74.412  1.00 47.40  ? 417 ILE C CB  1 
ATOM   11567 C CG1 . ILE C  1 417 ? -1.060  9.774   -75.141  1.00 50.49  ? 417 ILE C CG1 1 
ATOM   11568 C CG2 . ILE C  1 417 ? -0.362  8.726   -72.930  1.00 45.43  ? 417 ILE C CG2 1 
ATOM   11569 C CD1 . ILE C  1 417 ? -2.506  10.162  -74.988  1.00 52.19  ? 417 ILE C CD1 1 
ATOM   11570 N N   . GLY C  1 418 ? 2.097   9.351   -75.908  1.00 52.15  ? 418 GLY C N   1 
ATOM   11571 C CA  . GLY C  1 418 ? 3.256   10.206  -75.757  1.00 53.20  ? 418 GLY C CA  1 
ATOM   11572 C C   . GLY C  1 418 ? 4.344   10.056  -76.795  1.00 62.21  ? 418 GLY C C   1 
ATOM   11573 O O   . GLY C  1 418 ? 5.291   10.854  -76.778  1.00 68.30  ? 418 GLY C O   1 
ATOM   11574 N N   . ASN C  1 419 ? 4.284   9.080   -77.693  1.00 62.88  ? 419 ASN C N   1 
ATOM   11575 C CA  . ASN C  1 419 ? 5.197   9.049   -78.822  1.00 66.47  ? 419 ASN C CA  1 
ATOM   11576 C C   . ASN C  1 419 ? 4.386   9.190   -80.103  1.00 67.17  ? 419 ASN C C   1 
ATOM   11577 O O   . ASN C  1 419 ? 3.156   9.091   -80.093  1.00 64.39  ? 419 ASN C O   1 
ATOM   11578 C CB  . ASN C  1 419 ? 6.069   7.778   -78.819  1.00 68.16  ? 419 ASN C CB  1 
ATOM   11579 C CG  . ASN C  1 419 ? 5.292   6.498   -79.107  1.00 67.92  ? 419 ASN C CG  1 
ATOM   11580 O OD1 . ASN C  1 419 ? 4.168   6.514   -79.612  1.00 66.42  ? 419 ASN C OD1 1 
ATOM   11581 N ND2 . ASN C  1 419 ? 5.921   5.367   -78.810  1.00 70.30  ? 419 ASN C ND2 1 
ATOM   11582 N N   . LYS C  1 420 ? 5.098   9.422   -81.210  1.00 69.61  ? 420 LYS C N   1 
ATOM   11583 C CA  . LYS C  1 420 ? 4.453   9.750   -82.479  1.00 73.27  ? 420 LYS C CA  1 
ATOM   11584 C C   . LYS C  1 420 ? 3.342   8.761   -82.818  1.00 70.23  ? 420 LYS C C   1 
ATOM   11585 O O   . LYS C  1 420 ? 2.208   9.148   -83.122  1.00 67.51  ? 420 LYS C O   1 
ATOM   11586 C CB  . LYS C  1 420 ? 5.505   9.779   -83.593  1.00 80.38  ? 420 LYS C CB  1 
ATOM   11587 C CG  . LYS C  1 420 ? 6.894   10.245  -83.139  1.00 85.07  ? 420 LYS C CG  1 
ATOM   11588 C CD  . LYS C  1 420 ? 8.001   9.258   -83.526  1.00 86.99  ? 420 LYS C CD  1 
ATOM   11589 C CE  . LYS C  1 420 ? 9.317   9.598   -82.824  1.00 87.81  ? 420 LYS C CE  1 
ATOM   11590 N NZ  . LYS C  1 420 ? 10.449  8.729   -83.258  1.00 88.05  ? 420 LYS C NZ  1 
ATOM   11591 N N   . GLU C  1 421 ? 3.650   7.474   -82.737  1.00 72.97  ? 421 GLU C N   1 
ATOM   11592 C CA  . GLU C  1 421 ? 2.782   6.442   -83.289  1.00 77.21  ? 421 GLU C CA  1 
ATOM   11593 C C   . GLU C  1 421 ? 1.592   6.144   -82.379  1.00 71.77  ? 421 GLU C C   1 
ATOM   11594 O O   . GLU C  1 421 ? 0.464   5.990   -82.863  1.00 73.99  ? 421 GLU C O   1 
ATOM   11595 C CB  . GLU C  1 421 ? 3.619   5.192   -83.535  1.00 85.17  ? 421 GLU C CB  1 
ATOM   11596 C CG  . GLU C  1 421 ? 4.498   4.877   -82.343  1.00 92.34  ? 421 GLU C CG  1 
ATOM   11597 C CD  . GLU C  1 421 ? 5.872   5.534   -82.370  1.00 100.79 ? 421 GLU C CD  1 
ATOM   11598 O OE1 . GLU C  1 421 ? 5.952   6.768   -82.548  1.00 103.79 ? 421 GLU C OE1 1 
ATOM   11599 O OE2 . GLU C  1 421 ? 6.875   4.810   -82.190  1.00 103.76 ? 421 GLU C OE2 1 
ATOM   11600 N N   . LYS C  1 422 ? 1.818   6.049   -81.063  1.00 62.36  ? 422 LYS C N   1 
ATOM   11601 C CA  . LYS C  1 422 ? 0.701   5.894   -80.135  1.00 56.55  ? 422 LYS C CA  1 
ATOM   11602 C C   . LYS C  1 422 ? -0.174  7.141   -80.095  1.00 54.90  ? 422 LYS C C   1 
ATOM   11603 O O   . LYS C  1 422 ? -1.397  7.031   -79.969  1.00 54.13  ? 422 LYS C O   1 
ATOM   11604 C CB  . LYS C  1 422 ? 1.209   5.550   -78.733  1.00 54.40  ? 422 LYS C CB  1 
ATOM   11605 C CG  . LYS C  1 422 ? 1.992   4.236   -78.664  1.00 56.97  ? 422 LYS C CG  1 
ATOM   11606 C CD  . LYS C  1 422 ? 3.128   4.298   -77.649  1.00 54.48  ? 422 LYS C CD  1 
ATOM   11607 C CE  . LYS C  1 422 ? 3.201   3.058   -76.784  1.00 50.39  ? 422 LYS C CE  1 
ATOM   11608 N NZ  . LYS C  1 422 ? 3.509   1.787   -77.488  1.00 52.06  ? 422 LYS C NZ  1 
ATOM   11609 N N   . ASN C  1 423 ? 0.424   8.330   -80.222  1.00 53.79  ? 423 ASN C N   1 
ATOM   11610 C CA  . ASN C  1 423 ? -0.374  9.546   -80.329  1.00 53.11  ? 423 ASN C CA  1 
ATOM   11611 C C   . ASN C  1 423 ? -1.291  9.510   -81.547  1.00 58.78  ? 423 ASN C C   1 
ATOM   11612 O O   . ASN C  1 423 ? -2.400  10.057  -81.502  1.00 61.03  ? 423 ASN C O   1 
ATOM   11613 C CB  . ASN C  1 423 ? 0.535   10.776  -80.407  1.00 55.54  ? 423 ASN C CB  1 
ATOM   11614 C CG  . ASN C  1 423 ? 1.041   11.228  -79.050  1.00 55.02  ? 423 ASN C CG  1 
ATOM   11615 O OD1 . ASN C  1 423 ? 0.533   10.812  -78.011  1.00 56.80  ? 423 ASN C OD1 1 
ATOM   11616 N ND2 . ASN C  1 423 ? 2.052   12.087  -79.057  1.00 53.60  ? 423 ASN C ND2 1 
ATOM   11617 N N   . GLU C  1 424 ? -0.843  8.891   -82.647  1.00 58.44  ? 424 GLU C N   1 
ATOM   11618 C CA  . GLU C  1 424 ? -1.669  8.841   -83.851  1.00 60.15  ? 424 GLU C CA  1 
ATOM   11619 C C   . GLU C  1 424 ? -2.929  8.019   -83.623  1.00 55.42  ? 424 GLU C C   1 
ATOM   11620 O O   . GLU C  1 424 ? -3.995  8.360   -84.145  1.00 50.67  ? 424 GLU C O   1 
ATOM   11621 C CB  . GLU C  1 424 ? -0.867  8.283   -85.031  1.00 67.49  ? 424 GLU C CB  1 
ATOM   11622 C CG  . GLU C  1 424 ? -1.541  8.462   -86.402  1.00 74.71  ? 424 GLU C CG  1 
ATOM   11623 C CD  . GLU C  1 424 ? -1.477  9.904   -86.918  1.00 87.73  ? 424 GLU C CD  1 
ATOM   11624 O OE1 . GLU C  1 424 ? -0.768  10.726  -86.297  1.00 91.02  ? 424 GLU C OE1 1 
ATOM   11625 O OE2 . GLU C  1 424 ? -2.126  10.216  -87.947  1.00 91.84  ? 424 GLU C OE2 1 
ATOM   11626 N N   . TYR C  1 425 ? -2.841  6.959   -82.821  1.00 53.93  ? 425 TYR C N   1 
ATOM   11627 C CA  . TYR C  1 425 ? -4.040  6.199   -82.495  1.00 52.01  ? 425 TYR C CA  1 
ATOM   11628 C C   . TYR C  1 425 ? -5.029  7.053   -81.730  1.00 53.33  ? 425 TYR C C   1 
ATOM   11629 O O   . TYR C  1 425 ? -6.235  7.021   -82.000  1.00 54.34  ? 425 TYR C O   1 
ATOM   11630 C CB  . TYR C  1 425 ? -3.674  4.962   -81.692  1.00 46.98  ? 425 TYR C CB  1 
ATOM   11631 C CG  . TYR C  1 425 ? -3.528  3.767   -82.561  1.00 51.57  ? 425 TYR C CG  1 
ATOM   11632 C CD1 . TYR C  1 425 ? -3.268  3.908   -83.921  1.00 56.32  ? 425 TYR C CD1 1 
ATOM   11633 C CD2 . TYR C  1 425 ? -3.639  2.499   -82.036  1.00 55.33  ? 425 TYR C CD2 1 
ATOM   11634 C CE1 . TYR C  1 425 ? -3.148  2.819   -84.723  1.00 59.22  ? 425 TYR C CE1 1 
ATOM   11635 C CE2 . TYR C  1 425 ? -3.505  1.405   -82.823  1.00 60.52  ? 425 TYR C CE2 1 
ATOM   11636 C CZ  . TYR C  1 425 ? -3.257  1.564   -84.162  1.00 62.07  ? 425 TYR C CZ  1 
ATOM   11637 O OH  . TYR C  1 425 ? -3.124  0.422   -84.900  1.00 61.92  ? 425 TYR C OH  1 
ATOM   11638 N N   . TRP C  1 426 ? -4.535  7.821   -80.761  1.00 53.27  ? 426 TRP C N   1 
ATOM   11639 C CA  . TRP C  1 426 ? -5.411  8.717   -80.023  1.00 51.43  ? 426 TRP C CA  1 
ATOM   11640 C C   . TRP C  1 426 ? -6.043  9.747   -80.955  1.00 50.57  ? 426 TRP C C   1 
ATOM   11641 O O   . TRP C  1 426 ? -7.256  9.978   -80.904  1.00 50.52  ? 426 TRP C O   1 
ATOM   11642 C CB  . TRP C  1 426 ? -4.634  9.374   -78.883  1.00 49.79  ? 426 TRP C CB  1 
ATOM   11643 C CG  . TRP C  1 426 ? -4.373  8.410   -77.777  1.00 44.63  ? 426 TRP C CG  1 
ATOM   11644 C CD1 . TRP C  1 426 ? -3.221  7.714   -77.545  1.00 44.44  ? 426 TRP C CD1 1 
ATOM   11645 C CD2 . TRP C  1 426 ? -5.301  7.996   -76.774  1.00 39.14  ? 426 TRP C CD2 1 
ATOM   11646 N NE1 . TRP C  1 426 ? -3.369  6.906   -76.447  1.00 41.47  ? 426 TRP C NE1 1 
ATOM   11647 C CE2 . TRP C  1 426 ? -4.638  7.059   -75.953  1.00 43.77  ? 426 TRP C CE2 1 
ATOM   11648 C CE3 . TRP C  1 426 ? -6.626  8.342   -76.474  1.00 38.61  ? 426 TRP C CE3 1 
ATOM   11649 C CZ2 . TRP C  1 426 ? -5.255  6.461   -74.849  1.00 45.90  ? 426 TRP C CZ2 1 
ATOM   11650 C CZ3 . TRP C  1 426 ? -7.242  7.748   -75.377  1.00 41.84  ? 426 TRP C CZ3 1 
ATOM   11651 C CH2 . TRP C  1 426 ? -6.553  6.819   -74.577  1.00 44.07  ? 426 TRP C CH2 1 
ATOM   11652 N N   . LYS C  1 427 ? -5.246  10.342  -81.849  1.00 50.07  ? 427 LYS C N   1 
ATOM   11653 C CA  . LYS C  1 427 ? -5.800  11.296  -82.804  1.00 55.13  ? 427 LYS C CA  1 
ATOM   11654 C C   . LYS C  1 427 ? -6.832  10.633  -83.712  1.00 56.41  ? 427 LYS C C   1 
ATOM   11655 O O   . LYS C  1 427 ? -7.912  11.189  -83.945  1.00 61.26  ? 427 LYS C O   1 
ATOM   11656 C CB  . LYS C  1 427 ? -4.684  11.936  -83.628  1.00 59.88  ? 427 LYS C CB  1 
ATOM   11657 C CG  . LYS C  1 427 ? -4.947  13.400  -83.935  1.00 67.00  ? 427 LYS C CG  1 
ATOM   11658 C CD  . LYS C  1 427 ? -3.759  14.058  -84.613  1.00 75.55  ? 427 LYS C CD  1 
ATOM   11659 C CE  . LYS C  1 427 ? -2.477  13.796  -83.842  1.00 77.20  ? 427 LYS C CE  1 
ATOM   11660 N NZ  . LYS C  1 427 ? -1.306  14.396  -84.535  1.00 80.83  ? 427 LYS C NZ  1 
ATOM   11661 N N   . ILE C  1 428 ? -6.513  9.443   -84.239  1.00 56.81  ? 428 ILE C N   1 
ATOM   11662 C CA  . ILE C  1 428 ? -7.501  8.657   -84.981  1.00 55.10  ? 428 ILE C CA  1 
ATOM   11663 C C   . ILE C  1 428 ? -8.751  8.460   -84.135  1.00 52.79  ? 428 ILE C C   1 
ATOM   11664 O O   . ILE C  1 428 ? -9.883  8.608   -84.612  1.00 51.93  ? 428 ILE C O   1 
ATOM   11665 C CB  . ILE C  1 428 ? -6.905  7.300   -85.415  1.00 54.72  ? 428 ILE C CB  1 
ATOM   11666 C CG1 . ILE C  1 428 ? -5.829  7.475   -86.490  1.00 55.88  ? 428 ILE C CG1 1 
ATOM   11667 C CG2 . ILE C  1 428 ? -7.995  6.373   -85.925  1.00 51.73  ? 428 ILE C CG2 1 
ATOM   11668 C CD1 . ILE C  1 428 ? -4.847  6.303   -86.561  1.00 53.46  ? 428 ILE C CD1 1 
ATOM   11669 N N   . LEU C  1 429 ? -8.563  8.135   -82.859  1.00 52.13  ? 429 LEU C N   1 
ATOM   11670 C CA  . LEU C  1 429 ? -9.704  7.873   -81.996  1.00 49.89  ? 429 LEU C CA  1 
ATOM   11671 C C   . LEU C  1 429 ? -10.473 9.152   -81.702  1.00 48.59  ? 429 LEU C C   1 
ATOM   11672 O O   . LEU C  1 429 ? -11.707 9.139   -81.643  1.00 49.99  ? 429 LEU C O   1 
ATOM   11673 C CB  . LEU C  1 429 ? -9.227  7.205   -80.705  1.00 48.61  ? 429 LEU C CB  1 
ATOM   11674 C CG  . LEU C  1 429 ? -10.303 6.829   -79.690  1.00 47.90  ? 429 LEU C CG  1 
ATOM   11675 C CD1 . LEU C  1 429 ? -11.173 5.702   -80.225  1.00 52.12  ? 429 LEU C CD1 1 
ATOM   11676 C CD2 . LEU C  1 429 ? -9.652  6.461   -78.357  1.00 49.14  ? 429 LEU C CD2 1 
ATOM   11677 N N   . ILE C  1 430 ? -9.758  10.264  -81.510  1.00 46.82  ? 430 ILE C N   1 
ATOM   11678 C CA  . ILE C  1 430 ? -10.405 11.537  -81.210  1.00 51.58  ? 430 ILE C CA  1 
ATOM   11679 C C   . ILE C  1 430 ? -11.253 12.008  -82.391  1.00 59.56  ? 430 ILE C C   1 
ATOM   11680 O O   . ILE C  1 430 ? -12.379 12.493  -82.212  1.00 61.96  ? 430 ILE C O   1 
ATOM   11681 C CB  . ILE C  1 430 ? -9.347  12.586  -80.825  1.00 49.21  ? 430 ILE C CB  1 
ATOM   11682 C CG1 . ILE C  1 430 ? -8.718  12.249  -79.472  1.00 45.43  ? 430 ILE C CG1 1 
ATOM   11683 C CG2 . ILE C  1 430 ? -9.967  13.973  -80.804  1.00 48.98  ? 430 ILE C CG2 1 
ATOM   11684 C CD1 . ILE C  1 430 ? -7.263  12.684  -79.371  1.00 47.81  ? 430 ILE C CD1 1 
ATOM   11685 N N   . GLU C  1 431 ? -10.732 11.888  -83.614  1.00 59.88  ? 431 GLU C N   1 
ATOM   11686 C CA  . GLU C  1 431 ? -11.530 12.290  -84.767  1.00 63.68  ? 431 GLU C CA  1 
ATOM   11687 C C   . GLU C  1 431 ? -12.723 11.361  -84.950  1.00 64.01  ? 431 GLU C C   1 
ATOM   11688 O O   . GLU C  1 431 ? -13.822 11.813  -85.286  1.00 65.99  ? 431 GLU C O   1 
ATOM   11689 C CB  . GLU C  1 431 ? -10.667 12.330  -86.027  1.00 67.80  ? 431 GLU C CB  1 
ATOM   11690 C CG  . GLU C  1 431 ? -9.387  13.139  -85.875  1.00 73.04  ? 431 GLU C CG  1 
ATOM   11691 C CD  . GLU C  1 431 ? -9.609  14.640  -85.960  1.00 76.50  ? 431 GLU C CD  1 
ATOM   11692 O OE1 . GLU C  1 431 ? -10.198 15.222  -85.021  1.00 75.36  ? 431 GLU C OE1 1 
ATOM   11693 O OE2 . GLU C  1 431 ? -9.183  15.239  -86.971  1.00 78.79  ? 431 GLU C OE2 1 
ATOM   11694 N N   . ALA C  1 432 ? -12.537 10.064  -84.691  1.00 62.94  ? 432 ALA C N   1 
ATOM   11695 C CA  . ALA C  1 432 ? -13.634 9.113   -84.842  1.00 62.13  ? 432 ALA C CA  1 
ATOM   11696 C C   . ALA C  1 432 ? -14.729 9.329   -83.803  1.00 60.65  ? 432 ALA C C   1 
ATOM   11697 O O   . ALA C  1 432 ? -15.908 9.103   -84.098  1.00 61.19  ? 432 ALA C O   1 
ATOM   11698 C CB  . ALA C  1 432 ? -13.106 7.684   -84.750  1.00 61.50  ? 432 ALA C CB  1 
ATOM   11699 N N   . LYS C  1 433 ? -14.359 9.750   -82.586  1.00 54.43  ? 433 LYS C N   1 
ATOM   11700 C CA  . LYS C  1 433 ? -15.349 10.037  -81.555  1.00 53.30  ? 433 LYS C CA  1 
ATOM   11701 C C   . LYS C  1 433 ? -16.285 11.173  -81.959  1.00 58.47  ? 433 LYS C C   1 
ATOM   11702 O O   . LYS C  1 433 ? -17.463 11.169  -81.578  1.00 55.62  ? 433 LYS C O   1 
ATOM   11703 C CB  . LYS C  1 433 ? -14.643 10.383  -80.242  1.00 54.26  ? 433 LYS C CB  1 
ATOM   11704 C CG  . LYS C  1 433 ? -15.578 10.758  -79.105  1.00 53.74  ? 433 LYS C CG  1 
ATOM   11705 C CD  . LYS C  1 433 ? -16.372 9.561   -78.615  1.00 50.24  ? 433 LYS C CD  1 
ATOM   11706 C CE  . LYS C  1 433 ? -17.276 9.943   -77.456  1.00 45.38  ? 433 LYS C CE  1 
ATOM   11707 N NZ  . LYS C  1 433 ? -18.226 8.845   -77.145  1.00 44.65  ? 433 LYS C NZ  1 
ATOM   11708 N N   . LYS C  1 434 ? -15.778 12.165  -82.698  1.00 62.25  ? 434 LYS C N   1 
ATOM   11709 C CA  . LYS C  1 434 ? -16.635 13.234  -83.203  1.00 66.72  ? 434 LYS C CA  1 
ATOM   11710 C C   . LYS C  1 434 ? -17.811 12.666  -83.988  1.00 70.58  ? 434 LYS C C   1 
ATOM   11711 O O   . LYS C  1 434 ? -18.961 13.087  -83.813  1.00 72.20  ? 434 LYS C O   1 
ATOM   11712 C CB  . LYS C  1 434 ? -15.831 14.190  -84.090  1.00 71.62  ? 434 LYS C CB  1 
ATOM   11713 C CG  . LYS C  1 434 ? -14.758 14.996  -83.380  1.00 71.69  ? 434 LYS C CG  1 
ATOM   11714 C CD  . LYS C  1 434 ? -13.788 15.633  -84.373  1.00 74.63  ? 434 LYS C CD  1 
ATOM   11715 C CE  . LYS C  1 434 ? -14.148 17.090  -84.665  1.00 76.09  ? 434 LYS C CE  1 
ATOM   11716 N NZ  . LYS C  1 434 ? -14.934 17.280  -85.930  1.00 79.50  ? 434 LYS C NZ  1 
ATOM   11717 N N   . LYS C  1 435 ? -17.537 11.700  -84.862  1.00 74.80  ? 435 LYS C N   1 
ATOM   11718 C CA  . LYS C  1 435 ? -18.538 11.172  -85.777  1.00 76.78  ? 435 LYS C CA  1 
ATOM   11719 C C   . LYS C  1 435 ? -18.951 9.751   -85.420  1.00 72.99  ? 435 LYS C C   1 
ATOM   11720 O O   . LYS C  1 435 ? -19.297 8.969   -86.307  1.00 74.70  ? 435 LYS C O   1 
ATOM   11721 C CB  . LYS C  1 435 ? -18.031 11.198  -87.214  1.00 78.63  ? 435 LYS C CB  1 
ATOM   11722 C CG  . LYS C  1 435 ? -16.961 12.208  -87.511  1.00 81.04  ? 435 LYS C CG  1 
ATOM   11723 C CD  . LYS C  1 435 ? -16.844 12.361  -89.016  1.00 85.80  ? 435 LYS C CD  1 
ATOM   11724 C CE  . LYS C  1 435 ? -16.045 13.603  -89.356  1.00 89.94  ? 435 LYS C CE  1 
ATOM   11725 N NZ  . LYS C  1 435 ? -16.542 14.301  -90.559  1.00 94.09  ? 435 LYS C NZ  1 
ATOM   11726 N N   . ALA C  1 436 ? -18.903 9.398   -84.139  1.00 65.17  ? 436 ALA C N   1 
ATOM   11727 C CA  . ALA C  1 436 ? -19.235 8.045   -83.720  1.00 63.52  ? 436 ALA C CA  1 
ATOM   11728 C C   . ALA C  1 436 ? -20.728 7.928   -83.447  1.00 65.41  ? 436 ALA C C   1 
ATOM   11729 O O   . ALA C  1 436 ? -21.355 8.856   -82.927  1.00 58.13  ? 436 ALA C O   1 
ATOM   11730 C CB  . ALA C  1 436 ? -18.444 7.650   -82.472  1.00 61.05  ? 436 ALA C CB  1 
ATOM   11731 N N   . LYS C  1 437 ? -21.290 6.761   -83.787  1.00 64.65  ? 437 LYS C N   1 
ATOM   11732 C CA  . LYS C  1 437 ? -22.728 6.534   -83.690  1.00 69.15  ? 437 LYS C CA  1 
ATOM   11733 C C   . LYS C  1 437 ? -23.133 5.271   -82.948  1.00 64.46  ? 437 LYS C C   1 
ATOM   11734 O O   . LYS C  1 437 ? -24.334 5.068   -82.741  1.00 63.77  ? 437 LYS C O   1 
ATOM   11735 C CB  . LYS C  1 437 ? -23.368 6.477   -85.087  1.00 76.01  ? 437 LYS C CB  1 
ATOM   11736 C CG  . LYS C  1 437 ? -23.303 7.773   -85.865  1.00 82.65  ? 437 LYS C CG  1 
ATOM   11737 C CD  . LYS C  1 437 ? -22.027 7.831   -86.679  1.00 83.45  ? 437 LYS C CD  1 
ATOM   11738 C CE  . LYS C  1 437 ? -22.247 8.360   -88.088  1.00 84.20  ? 437 LYS C CE  1 
ATOM   11739 N NZ  . LYS C  1 437 ? -20.990 8.951   -88.652  1.00 80.88  ? 437 LYS C NZ  1 
ATOM   11740 N N   . ASN C  1 438 ? -22.199 4.411   -82.558  1.00 61.86  ? 438 ASN C N   1 
ATOM   11741 C CA  . ASN C  1 438 ? -22.552 3.163   -81.903  1.00 59.03  ? 438 ASN C CA  1 
ATOM   11742 C C   . ASN C  1 438 ? -21.456 2.821   -80.910  1.00 55.34  ? 438 ASN C C   1 
ATOM   11743 O O   . ASN C  1 438 ? -20.460 3.540   -80.784  1.00 55.76  ? 438 ASN C O   1 
ATOM   11744 C CB  . ASN C  1 438 ? -22.752 2.033   -82.920  1.00 62.96  ? 438 ASN C CB  1 
ATOM   11745 C CG  . ASN C  1 438 ? -21.540 1.830   -83.806  1.00 62.54  ? 438 ASN C CG  1 
ATOM   11746 O OD1 . ASN C  1 438 ? -20.496 1.365   -83.349  1.00 60.77  ? 438 ASN C OD1 1 
ATOM   11747 N ND2 . ASN C  1 438 ? -21.670 2.182   -85.079  1.00 64.22  ? 438 ASN C ND2 1 
ATOM   11748 N N   . ASP C  1 439 ? -21.631 1.691   -80.225  1.00 50.56  ? 439 ASP C N   1 
ATOM   11749 C CA  . ASP C  1 439 ? -20.770 1.354   -79.098  1.00 52.68  ? 439 ASP C CA  1 
ATOM   11750 C C   . ASP C  1 439 ? -19.439 0.756   -79.521  1.00 52.22  ? 439 ASP C C   1 
ATOM   11751 O O   . ASP C  1 439 ? -18.650 0.377   -78.648  1.00 48.70  ? 439 ASP C O   1 
ATOM   11752 C CB  . ASP C  1 439 ? -21.493 0.393   -78.147  1.00 57.32  ? 439 ASP C CB  1 
ATOM   11753 C CG  . ASP C  1 439 ? -22.339 1.122   -77.113  1.00 64.84  ? 439 ASP C CG  1 
ATOM   11754 O OD1 . ASP C  1 439 ? -22.227 2.363   -77.020  1.00 67.56  ? 439 ASP C OD1 1 
ATOM   11755 O OD2 . ASP C  1 439 ? -23.115 0.457   -76.389  1.00 68.28  ? 439 ASP C OD2 1 
ATOM   11756 N N   . TYR C  1 440 ? -19.164 0.655   -80.825  1.00 52.81  ? 440 TYR C N   1 
ATOM   11757 C CA  . TYR C  1 440 ? -17.856 0.170   -81.241  1.00 54.02  ? 440 TYR C CA  1 
ATOM   11758 C C   . TYR C  1 440 ? -16.755 1.181   -80.959  1.00 49.83  ? 440 TYR C C   1 
ATOM   11759 O O   . TYR C  1 440 ? -15.574 0.818   -80.994  1.00 43.94  ? 440 TYR C O   1 
ATOM   11760 C CB  . TYR C  1 440 ? -17.863 -0.196  -82.721  1.00 52.82  ? 440 TYR C CB  1 
ATOM   11761 C CG  . TYR C  1 440 ? -18.244 -1.635  -82.962  1.00 57.59  ? 440 TYR C CG  1 
ATOM   11762 C CD1 . TYR C  1 440 ? -17.296 -2.645  -82.867  1.00 55.52  ? 440 TYR C CD1 1 
ATOM   11763 C CD2 . TYR C  1 440 ? -19.550 -1.988  -83.286  1.00 60.77  ? 440 TYR C CD2 1 
ATOM   11764 C CE1 . TYR C  1 440 ? -17.636 -3.964  -83.084  1.00 58.13  ? 440 TYR C CE1 1 
ATOM   11765 C CE2 . TYR C  1 440 ? -19.898 -3.308  -83.514  1.00 62.25  ? 440 TYR C CE2 1 
ATOM   11766 C CZ  . TYR C  1 440 ? -18.938 -4.291  -83.409  1.00 62.93  ? 440 TYR C CZ  1 
ATOM   11767 O OH  . TYR C  1 440 ? -19.284 -5.607  -83.628  1.00 64.95  ? 440 TYR C OH  1 
ATOM   11768 N N   . ILE C  1 441 ? -17.119 2.438   -80.698  1.00 46.32  ? 441 ILE C N   1 
ATOM   11769 C CA  . ILE C  1 441 ? -16.135 3.426   -80.279  1.00 47.00  ? 441 ILE C CA  1 
ATOM   11770 C C   . ILE C  1 441 ? -15.558 3.047   -78.918  1.00 43.17  ? 441 ILE C C   1 
ATOM   11771 O O   . ILE C  1 441 ? -14.398 3.359   -78.621  1.00 40.98  ? 441 ILE C O   1 
ATOM   11772 C CB  . ILE C  1 441 ? -16.758 4.838   -80.268  1.00 50.21  ? 441 ILE C CB  1 
ATOM   11773 C CG1 . ILE C  1 441 ? -15.666 5.908   -80.303  1.00 51.68  ? 441 ILE C CG1 1 
ATOM   11774 C CG2 . ILE C  1 441 ? -17.665 5.042   -79.049  1.00 49.99  ? 441 ILE C CG2 1 
ATOM   11775 C CD1 . ILE C  1 441 ? -15.017 6.077   -81.655  1.00 55.56  ? 441 ILE C CD1 1 
ATOM   11776 N N   . LEU C  1 442 ? -16.349 2.365   -78.078  1.00 42.81  ? 442 LEU C N   1 
ATOM   11777 C CA  . LEU C  1 442 ? -15.840 1.862   -76.804  1.00 43.44  ? 442 LEU C CA  1 
ATOM   11778 C C   . LEU C  1 442 ? -14.849 0.727   -77.005  1.00 41.29  ? 442 LEU C C   1 
ATOM   11779 O O   . LEU C  1 442 ? -13.900 0.600   -76.226  1.00 39.91  ? 442 LEU C O   1 
ATOM   11780 C CB  . LEU C  1 442 ? -16.982 1.375   -75.911  1.00 42.82  ? 442 LEU C CB  1 
ATOM   11781 C CG  . LEU C  1 442 ? -18.168 2.305   -75.696  1.00 47.22  ? 442 LEU C CG  1 
ATOM   11782 C CD1 . LEU C  1 442 ? -19.110 1.735   -74.644  1.00 44.90  ? 442 LEU C CD1 1 
ATOM   11783 C CD2 . LEU C  1 442 ? -17.677 3.677   -75.302  1.00 49.67  ? 442 LEU C CD2 1 
ATOM   11784 N N   . VAL C  1 443 ? -15.058 -0.115  -78.026  1.00 45.02  ? 443 VAL C N   1 
ATOM   11785 C CA  . VAL C  1 443 ? -14.110 -1.197  -78.293  1.00 43.64  ? 443 VAL C CA  1 
ATOM   11786 C C   . VAL C  1 443 ? -12.750 -0.623  -78.666  1.00 44.81  ? 443 VAL C C   1 
ATOM   11787 O O   . VAL C  1 443 ? -11.706 -1.151  -78.261  1.00 42.15  ? 443 VAL C O   1 
ATOM   11788 C CB  . VAL C  1 443 ? -14.640 -2.138  -79.399  1.00 45.65  ? 443 VAL C CB  1 
ATOM   11789 C CG1 . VAL C  1 443 ? -13.787 -3.396  -79.475  1.00 41.71  ? 443 VAL C CG1 1 
ATOM   11790 C CG2 . VAL C  1 443 ? -16.077 -2.514  -79.147  1.00 48.01  ? 443 VAL C CG2 1 
ATOM   11791 N N   . ALA C  1 444 ? -12.741 0.463   -79.455  1.00 43.32  ? 444 ALA C N   1 
ATOM   11792 C CA  . ALA C  1 444 ? -11.507 1.114   -79.885  1.00 45.26  ? 444 ALA C CA  1 
ATOM   11793 C C   . ALA C  1 444 ? -10.807 1.867   -78.762  1.00 45.86  ? 444 ALA C C   1 
ATOM   11794 O O   . ALA C  1 444 ? -9.652  2.275   -78.936  1.00 44.09  ? 444 ALA C O   1 
ATOM   11795 C CB  . ALA C  1 444 ? -11.784 2.077   -81.052  1.00 41.97  ? 444 ALA C CB  1 
ATOM   11796 N N   . GLU C  1 445 ? -11.466 2.062   -77.626  1.00 44.37  ? 445 GLU C N   1 
ATOM   11797 C CA  . GLU C  1 445 ? -10.836 2.698   -76.478  1.00 43.09  ? 445 GLU C CA  1 
ATOM   11798 C C   . GLU C  1 445 ? -10.118 1.708   -75.573  1.00 41.36  ? 445 GLU C C   1 
ATOM   11799 O O   . GLU C  1 445 ? -9.491  2.130   -74.598  1.00 39.16  ? 445 GLU C O   1 
ATOM   11800 C CB  . GLU C  1 445 ? -11.878 3.481   -75.684  1.00 44.79  ? 445 GLU C CB  1 
ATOM   11801 C CG  . GLU C  1 445 ? -12.357 4.719   -76.418  1.00 47.31  ? 445 GLU C CG  1 
ATOM   11802 C CD  . GLU C  1 445 ? -13.711 5.175   -75.946  1.00 54.68  ? 445 GLU C CD  1 
ATOM   11803 O OE1 . GLU C  1 445 ? -14.250 4.544   -75.010  1.00 53.48  ? 445 GLU C OE1 1 
ATOM   11804 O OE2 . GLU C  1 445 ? -14.231 6.170   -76.504  1.00 60.72  ? 445 GLU C OE2 1 
ATOM   11805 N N   . GLY C  1 446 ? -10.177 0.415   -75.884  1.00 44.85  ? 446 GLY C N   1 
ATOM   11806 C CA  . GLY C  1 446 ? -9.429  -0.558  -75.107  1.00 43.85  ? 446 GLY C CA  1 
ATOM   11807 C C   . GLY C  1 446 ? -7.936  -0.285  -75.165  1.00 40.58  ? 446 GLY C C   1 
ATOM   11808 O O   . GLY C  1 446 ? -7.386  0.058   -76.215  1.00 38.46  ? 446 GLY C O   1 
ATOM   11809 N N   . SER C  1 447 ? -7.277  -0.455  -74.015  1.00 37.24  ? 447 SER C N   1 
ATOM   11810 C CA  . SER C  1 447 ? -5.866  -0.104  -73.896  1.00 37.34  ? 447 SER C CA  1 
ATOM   11811 C C   . SER C  1 447 ? -4.980  -0.931  -74.817  1.00 35.86  ? 447 SER C C   1 
ATOM   11812 O O   . SER C  1 447 ? -3.919  -0.458  -75.238  1.00 35.75  ? 447 SER C O   1 
ATOM   11813 C CB  . SER C  1 447 ? -5.407  -0.291  -72.448  1.00 35.39  ? 447 SER C CB  1 
ATOM   11814 O OG  . SER C  1 447 ? -5.327  -1.677  -72.155  1.00 33.67  ? 447 SER C OG  1 
ATOM   11815 N N   . ASP C  1 448 ? -5.387  -2.170  -75.123  1.00 33.55  ? 448 ASP C N   1 
ATOM   11816 C CA  . ASP C  1 448 ? -4.533  -3.095  -75.869  1.00 35.82  ? 448 ASP C CA  1 
ATOM   11817 C C   . ASP C  1 448 ? -4.062  -2.510  -77.195  1.00 37.74  ? 448 ASP C C   1 
ATOM   11818 O O   . ASP C  1 448 ? -2.910  -2.721  -77.595  1.00 33.99  ? 448 ASP C O   1 
ATOM   11819 C CB  . ASP C  1 448 ? -5.278  -4.393  -76.146  1.00 34.00  ? 448 ASP C CB  1 
ATOM   11820 C CG  . ASP C  1 448 ? -5.762  -5.056  -74.888  1.00 32.86  ? 448 ASP C CG  1 
ATOM   11821 O OD1 . ASP C  1 448 ? -6.828  -4.650  -74.377  1.00 31.53  ? 448 ASP C OD1 1 
ATOM   11822 O OD2 . ASP C  1 448 ? -5.064  -5.977  -74.425  1.00 34.90  ? 448 ASP C OD2 1 
ATOM   11823 N N   . TRP C  1 449 ? -4.955  -1.834  -77.918  1.00 36.57  ? 449 TRP C N   1 
ATOM   11824 C CA  . TRP C  1 449 ? -4.587  -1.295  -79.224  1.00 39.97  ? 449 TRP C CA  1 
ATOM   11825 C C   . TRP C  1 449 ? -3.402  -0.347  -79.099  1.00 41.79  ? 449 TRP C C   1 
ATOM   11826 O O   . TRP C  1 449 ? -2.470  -0.389  -79.913  1.00 39.72  ? 449 TRP C O   1 
ATOM   11827 C CB  . TRP C  1 449 ? -5.787  -0.582  -79.863  1.00 41.74  ? 449 TRP C CB  1 
ATOM   11828 C CG  . TRP C  1 449 ? -7.102  -1.305  -79.677  1.00 41.15  ? 449 TRP C CG  1 
ATOM   11829 C CD1 . TRP C  1 449 ? -8.232  -0.818  -79.074  1.00 42.59  ? 449 TRP C CD1 1 
ATOM   11830 C CD2 . TRP C  1 449 ? -7.411  -2.649  -80.077  1.00 38.66  ? 449 TRP C CD2 1 
ATOM   11831 N NE1 . TRP C  1 449 ? -9.221  -1.781  -79.074  1.00 39.91  ? 449 TRP C NE1 1 
ATOM   11832 C CE2 . TRP C  1 449 ? -8.744  -2.906  -79.695  1.00 37.20  ? 449 TRP C CE2 1 
ATOM   11833 C CE3 . TRP C  1 449 ? -6.692  -3.658  -80.734  1.00 38.28  ? 449 TRP C CE3 1 
ATOM   11834 C CZ2 . TRP C  1 449 ? -9.370  -4.132  -79.941  1.00 37.05  ? 449 TRP C CZ2 1 
ATOM   11835 C CZ3 . TRP C  1 449 ? -7.314  -4.875  -80.970  1.00 38.55  ? 449 TRP C CZ3 1 
ATOM   11836 C CH2 . TRP C  1 449 ? -8.642  -5.098  -80.581  1.00 36.63  ? 449 TRP C CH2 1 
ATOM   11837 N N   . PHE C  1 450 ? -3.399  0.476   -78.051  1.00 45.22  ? 450 PHE C N   1 
ATOM   11838 C CA  . PHE C  1 450 ? -2.339  1.455   -77.840  1.00 45.29  ? 450 PHE C CA  1 
ATOM   11839 C C   . PHE C  1 450 ? -1.062  0.792   -77.349  1.00 42.27  ? 450 PHE C C   1 
ATOM   11840 O O   . PHE C  1 450 ? 0.039   1.216   -77.722  1.00 44.63  ? 450 PHE C O   1 
ATOM   11841 C CB  . PHE C  1 450 ? -2.822  2.527   -76.861  1.00 43.15  ? 450 PHE C CB  1 
ATOM   11842 C CG  . PHE C  1 450 ? -4.116  3.164   -77.276  1.00 41.94  ? 450 PHE C CG  1 
ATOM   11843 C CD1 . PHE C  1 450 ? -5.330  2.578   -76.954  1.00 37.83  ? 450 PHE C CD1 1 
ATOM   11844 C CD2 . PHE C  1 450 ? -4.116  4.319   -78.027  1.00 42.46  ? 450 PHE C CD2 1 
ATOM   11845 C CE1 . PHE C  1 450 ? -6.517  3.155   -77.362  1.00 42.05  ? 450 PHE C CE1 1 
ATOM   11846 C CE2 . PHE C  1 450 ? -5.301  4.903   -78.438  1.00 42.54  ? 450 PHE C CE2 1 
ATOM   11847 C CZ  . PHE C  1 450 ? -6.499  4.321   -78.111  1.00 42.97  ? 450 PHE C CZ  1 
ATOM   11848 N N   . TRP C  1 451 ? -1.094  -0.266  -76.578  1.00 40.83  ? 451 TRP C N   1 
ATOM   11849 C CA  . TRP C  1 451 ? 0.092   -0.963  -76.132  1.00 36.38  ? 451 TRP C CA  1 
ATOM   11850 C C   . TRP C  1 451 ? 0.989   -1.436  -77.273  1.00 39.00  ? 451 TRP C C   1 
ATOM   11851 O O   . TRP C  1 451 ? 2.151   -1.269  -77.254  1.00 39.50  ? 451 TRP C O   1 
ATOM   11852 C CB  . TRP C  1 451 ? -0.326  -2.182  -75.266  1.00 36.50  ? 451 TRP C CB  1 
ATOM   11853 C CG  . TRP C  1 451 ? 0.713   -3.148  -74.987  1.00 37.78  ? 451 TRP C CG  1 
ATOM   11854 C CD1 . TRP C  1 451 ? 0.892   -4.356  -75.576  1.00 36.70  ? 451 TRP C CD1 1 
ATOM   11855 C CD2 . TRP C  1 451 ? 1.747   -3.010  -74.032  1.00 47.06  ? 451 TRP C CD2 1 
ATOM   11856 N NE1 . TRP C  1 451 ? 1.986   -4.968  -75.063  1.00 39.41  ? 451 TRP C NE1 1 
ATOM   11857 C CE2 . TRP C  1 451 ? 2.534   -4.162  -74.108  1.00 46.04  ? 451 TRP C CE2 1 
ATOM   11858 C CE3 . TRP C  1 451 ? 2.102   -2.007  -73.135  1.00 51.13  ? 451 TRP C CE3 1 
ATOM   11859 C CZ2 . TRP C  1 451 ? 3.635   -4.349  -73.310  1.00 47.87  ? 451 TRP C CZ2 1 
ATOM   11860 C CZ3 . TRP C  1 451 ? 3.195   -2.188  -72.355  1.00 52.85  ? 451 TRP C CZ3 1 
ATOM   11861 C CH2 . TRP C  1 451 ? 3.953   -3.350  -72.440  1.00 52.68  ? 451 TRP C CH2 1 
ATOM   11862 N N   . TRP C  1 452 ? 0.380   -2.061  -78.225  1.00 41.42  ? 452 TRP C N   1 
ATOM   11863 C CA  . TRP C  1 452 ? 1.078   -2.584  -79.337  1.00 44.63  ? 452 TRP C CA  1 
ATOM   11864 C C   . TRP C  1 452 ? 1.432   -1.606  -80.411  1.00 49.19  ? 452 TRP C C   1 
ATOM   11865 O O   . TRP C  1 452 ? 2.247   -1.888  -81.211  1.00 47.68  ? 452 TRP C O   1 
ATOM   11866 C CB  . TRP C  1 452 ? 0.159   -3.623  -79.928  1.00 46.38  ? 452 TRP C CB  1 
ATOM   11867 C CG  . TRP C  1 452 ? -0.082  -4.831  -79.072  1.00 44.22  ? 452 TRP C CG  1 
ATOM   11868 C CD1 . TRP C  1 452 ? -1.261  -5.219  -78.550  1.00 45.64  ? 452 TRP C CD1 1 
ATOM   11869 C CD2 . TRP C  1 452 ? 0.874   -5.811  -78.665  1.00 44.67  ? 452 TRP C CD2 1 
ATOM   11870 N NE1 . TRP C  1 452 ? -1.110  -6.364  -77.838  1.00 44.77  ? 452 TRP C NE1 1 
ATOM   11871 C CE2 . TRP C  1 452 ? 0.196   -6.747  -77.889  1.00 42.59  ? 452 TRP C CE2 1 
ATOM   11872 C CE3 . TRP C  1 452 ? 2.241   -5.978  -78.871  1.00 46.99  ? 452 TRP C CE3 1 
ATOM   11873 C CZ2 . TRP C  1 452 ? 0.827   -7.829  -77.322  1.00 42.64  ? 452 TRP C CZ2 1 
ATOM   11874 C CZ3 . TRP C  1 452 ? 2.861   -7.051  -78.313  1.00 44.65  ? 452 TRP C CZ3 1 
ATOM   11875 C CH2 . TRP C  1 452 ? 2.160   -7.961  -77.541  1.00 43.46  ? 452 TRP C CH2 1 
ATOM   11876 N N   . GLN C  1 453 ? 0.772   -0.460  -80.448  1.00 52.28  ? 453 GLN C N   1 
ATOM   11877 C CA  . GLN C  1 453 ? 1.122   0.571   -81.409  1.00 54.55  ? 453 GLN C CA  1 
ATOM   11878 C C   . GLN C  1 453 ? 2.476   1.036   -81.231  1.00 60.17  ? 453 GLN C C   1 
ATOM   11879 O O   . GLN C  1 453 ? 2.972   1.188   -80.168  1.00 57.06  ? 453 GLN C O   1 
ATOM   11880 C CB  . GLN C  1 453 ? 0.231   1.763   -81.338  1.00 57.32  ? 453 GLN C CB  1 
ATOM   11881 C CG  . GLN C  1 453 ? 0.298   2.698   -82.541  1.00 66.87  ? 453 GLN C CG  1 
ATOM   11882 C CD  . GLN C  1 453 ? 0.388   1.992   -83.894  1.00 74.92  ? 453 GLN C CD  1 
ATOM   11883 O OE1 . GLN C  1 453 ? -0.610  1.566   -84.451  1.00 79.26  ? 453 GLN C OE1 1 
ATOM   11884 N NE2 . GLN C  1 453 ? 1.584   1.898   -84.433  1.00 76.90  ? 453 GLN C NE2 1 
ATOM   11885 N N   . GLY C  1 454 ? 3.105   1.151   -82.352  1.00 68.08  ? 454 GLY C N   1 
ATOM   11886 C CA  . GLY C  1 454 ? 4.370   1.761   -82.355  1.00 76.24  ? 454 GLY C CA  1 
ATOM   11887 C C   . GLY C  1 454 ? 5.466   1.056   -81.767  1.00 81.93  ? 454 GLY C C   1 
ATOM   11888 O O   . GLY C  1 454 ? 6.296   1.674   -81.125  1.00 81.25  ? 454 GLY C O   1 
ATOM   11889 N N   . GLU C  1 455 ? 5.474   -0.251  -81.924  1.00 87.02  ? 455 GLU C N   1 
ATOM   11890 C CA  . GLU C  1 455 ? 6.628   -0.926  -81.446  1.00 84.97  ? 455 GLU C CA  1 
ATOM   11891 C C   . GLU C  1 455 ? 7.087   -1.556  -82.654  1.00 86.34  ? 455 GLU C C   1 
ATOM   11892 O O   . GLU C  1 455 ? 8.300   -1.644  -82.851  1.00 87.25  ? 455 GLU C O   1 
ATOM   11893 C CB  . GLU C  1 455 ? 6.297   -1.871  -80.361  1.00 83.48  ? 455 GLU C CB  1 
ATOM   11894 C CG  . GLU C  1 455 ? 4.899   -2.435  -80.426  1.00 84.74  ? 455 GLU C CG  1 
ATOM   11895 C CD  . GLU C  1 455 ? 4.895   -3.938  -80.570  1.00 85.60  ? 455 GLU C CD  1 
ATOM   11896 O OE1 . GLU C  1 455 ? 3.852   -4.490  -80.987  1.00 83.05  ? 455 GLU C OE1 1 
ATOM   11897 O OE2 . GLU C  1 455 ? 5.935   -4.563  -80.279  1.00 87.96  ? 455 GLU C OE2 1 
ATOM   11898 N N   . GLU C  1 456 ? 6.166   -2.039  -83.489  1.00 87.09  ? 456 GLU C N   1 
ATOM   11899 C CA  . GLU C  1 456 ? 6.594   -2.525  -84.791  1.00 84.59  ? 456 GLU C CA  1 
ATOM   11900 C C   . GLU C  1 456 ? 7.509   -3.754  -84.816  1.00 79.06  ? 456 GLU C C   1 
ATOM   11901 O O   . GLU C  1 456 ? 7.579   -4.460  -85.805  1.00 76.40  ? 456 GLU C O   1 
ATOM   11902 C CB  . GLU C  1 456 ? 7.338   -1.367  -85.544  1.00 82.70  ? 456 GLU C CB  1 
ATOM   11903 N N   . LYS C  1 457 ? 8.134   -4.045  -83.729  1.00 76.69  ? 457 LYS C N   1 
ATOM   11904 C CA  . LYS C  1 457 ? 9.122   -5.087  -83.731  1.00 76.56  ? 457 LYS C CA  1 
ATOM   11905 C C   . LYS C  1 457 ? 8.694   -6.617  -83.628  1.00 79.70  ? 457 LYS C C   1 
ATOM   11906 O O   . LYS C  1 457 ? 9.412   -7.340  -82.949  1.00 83.27  ? 457 LYS C O   1 
ATOM   11907 C CB  . LYS C  1 457 ? 10.065  -4.665  -82.575  1.00 77.10  ? 457 LYS C CB  1 
ATOM   11908 N N   . ALA C  1 458 ? 7.652   -7.132  -84.345  1.00 76.34  ? 458 ALA C N   1 
ATOM   11909 C CA  . ALA C  1 458 ? 7.122   -8.529  -84.090  1.00 69.93  ? 458 ALA C CA  1 
ATOM   11910 C C   . ALA C  1 458 ? 5.942   -9.104  -84.828  1.00 64.89  ? 458 ALA C C   1 
ATOM   11911 O O   . ALA C  1 458 ? 5.083   -8.399  -85.262  1.00 66.01  ? 458 ALA C O   1 
ATOM   11912 C CB  . ALA C  1 458 ? 6.756   -8.613  -82.631  1.00 67.20  ? 458 ALA C CB  1 
ATOM   11913 N N   . PRO C  1 459 ? 5.851   -10.414 -84.855  1.00 59.66  ? 459 PRO C N   1 
ATOM   11914 C CA  . PRO C  1 459 ? 4.797   -11.045 -85.615  1.00 59.67  ? 459 PRO C CA  1 
ATOM   11915 C C   . PRO C  1 459 ? 3.318   -10.846 -85.219  1.00 60.15  ? 459 PRO C C   1 
ATOM   11916 O O   . PRO C  1 459 ? 2.996   -10.805 -84.066  1.00 51.72  ? 459 PRO C O   1 
ATOM   11917 C CB  . PRO C  1 459 ? 5.197   -12.520 -85.534  1.00 60.90  ? 459 PRO C CB  1 
ATOM   11918 C CG  . PRO C  1 459 ? 6.643   -12.536 -85.286  1.00 60.62  ? 459 PRO C CG  1 
ATOM   11919 C CD  . PRO C  1 459 ? 6.873   -11.361 -84.406  1.00 60.07  ? 459 PRO C CD  1 
ATOM   11920 N N   . PHE C  1 460 ? 2.437   -10.696 -86.202  1.00 63.46  ? 460 PHE C N   1 
ATOM   11921 C CA  . PHE C  1 460 ? 0.994   -10.560 -85.997  1.00 62.92  ? 460 PHE C CA  1 
ATOM   11922 C C   . PHE C  1 460 ? 0.561   -9.267  -85.312  1.00 58.62  ? 460 PHE C C   1 
ATOM   11923 O O   . PHE C  1 460 ? -0.613  -9.156  -84.939  1.00 59.25  ? 460 PHE C O   1 
ATOM   11924 C CB  . PHE C  1 460 ? 0.407   -11.724 -85.190  1.00 59.84  ? 460 PHE C CB  1 
ATOM   11925 C CG  . PHE C  1 460 ? 0.644   -13.075 -85.793  1.00 60.98  ? 460 PHE C CG  1 
ATOM   11926 C CD1 . PHE C  1 460 ? 0.128   -13.403 -87.039  1.00 65.37  ? 460 PHE C CD1 1 
ATOM   11927 C CD2 . PHE C  1 460 ? 1.358   -14.038 -85.097  1.00 57.19  ? 460 PHE C CD2 1 
ATOM   11928 C CE1 . PHE C  1 460 ? 0.344   -14.667 -87.586  1.00 61.91  ? 460 PHE C CE1 1 
ATOM   11929 C CE2 . PHE C  1 460 ? 1.569   -15.296 -85.635  1.00 58.04  ? 460 PHE C CE2 1 
ATOM   11930 C CZ  . PHE C  1 460 ? 1.055   -15.615 -86.875  1.00 58.82  ? 460 PHE C CZ  1 
ATOM   11931 N N   . VAL C  1 461 ? 1.448   -8.286  -85.124  1.00 57.96  ? 461 VAL C N   1 
ATOM   11932 C CA  . VAL C  1 461 ? 0.973   -7.031  -84.543  1.00 58.09  ? 461 VAL C CA  1 
ATOM   11933 C C   . VAL C  1 461 ? 0.088   -6.282  -85.525  1.00 59.43  ? 461 VAL C C   1 
ATOM   11934 O O   . VAL C  1 461 ? -0.798  -5.525  -85.110  1.00 62.79  ? 461 VAL C O   1 
ATOM   11935 C CB  . VAL C  1 461 ? 2.133   -6.134  -84.070  1.00 63.14  ? 461 VAL C CB  1 
ATOM   11936 C CG1 . VAL C  1 461 ? 2.935   -6.822  -82.971  1.00 63.39  ? 461 VAL C CG1 1 
ATOM   11937 C CG2 . VAL C  1 461 ? 3.018   -5.714  -85.249  1.00 68.69  ? 461 VAL C CG2 1 
ATOM   11938 N N   . GLU C  1 462 ? 0.310   -6.465  -86.834  1.00 55.12  ? 462 GLU C N   1 
ATOM   11939 C CA  . GLU C  1 462 ? -0.535  -5.814  -87.828  1.00 56.22  ? 462 GLU C CA  1 
ATOM   11940 C C   . GLU C  1 462 ? -2.000  -6.190  -87.647  1.00 51.21  ? 462 GLU C C   1 
ATOM   11941 O O   . GLU C  1 462 ? -2.893  -5.407  -88.005  1.00 45.71  ? 462 GLU C O   1 
ATOM   11942 C CB  . GLU C  1 462 ? -0.048  -6.170  -89.243  1.00 62.12  ? 462 GLU C CB  1 
ATOM   11943 C CG  . GLU C  1 462 ? -0.656  -7.450  -89.834  1.00 71.02  ? 462 GLU C CG  1 
ATOM   11944 C CD  . GLU C  1 462 ? 0.320   -8.630  -89.852  1.00 79.11  ? 462 GLU C CD  1 
ATOM   11945 O OE1 . GLU C  1 462 ? 1.067   -8.802  -88.861  1.00 77.38  ? 462 GLU C OE1 1 
ATOM   11946 O OE2 . GLU C  1 462 ? 0.345   -9.380  -90.860  1.00 84.12  ? 462 GLU C OE2 1 
ATOM   11947 N N   . VAL C  1 463 ? -2.266  -7.379  -87.091  1.00 50.13  ? 463 VAL C N   1 
ATOM   11948 C CA  . VAL C  1 463 ? -3.642  -7.781  -86.819  1.00 48.69  ? 463 VAL C CA  1 
ATOM   11949 C C   . VAL C  1 463 ? -4.275  -6.848  -85.794  1.00 48.38  ? 463 VAL C C   1 
ATOM   11950 O O   . VAL C  1 463 ? -5.447  -6.476  -85.914  1.00 50.85  ? 463 VAL C O   1 
ATOM   11951 C CB  . VAL C  1 463 ? -3.693  -9.248  -86.360  1.00 49.03  ? 463 VAL C CB  1 
ATOM   11952 C CG1 . VAL C  1 463 ? -5.111  -9.750  -86.407  1.00 49.73  ? 463 VAL C CG1 1 
ATOM   11953 C CG2 . VAL C  1 463 ? -2.793  -10.101 -87.226  1.00 52.69  ? 463 VAL C CG2 1 
ATOM   11954 N N   . PHE C  1 464 ? -3.513  -6.463  -84.763  1.00 43.09  ? 464 PHE C N   1 
ATOM   11955 C CA  . PHE C  1 464 ? -4.021  -5.508  -83.786  1.00 36.96  ? 464 PHE C CA  1 
ATOM   11956 C C   . PHE C  1 464 ? -4.332  -4.160  -84.438  1.00 41.97  ? 464 PHE C C   1 
ATOM   11957 O O   . PHE C  1 464 ? -5.337  -3.518  -84.105  1.00 41.11  ? 464 PHE C O   1 
ATOM   11958 C CB  . PHE C  1 464 ? -3.018  -5.352  -82.636  1.00 35.89  ? 464 PHE C CB  1 
ATOM   11959 C CG  . PHE C  1 464 ? -2.964  -6.552  -81.706  1.00 35.25  ? 464 PHE C CG  1 
ATOM   11960 C CD1 . PHE C  1 464 ? -3.899  -6.711  -80.689  1.00 36.21  ? 464 PHE C CD1 1 
ATOM   11961 C CD2 . PHE C  1 464 ? -1.985  -7.525  -81.861  1.00 34.99  ? 464 PHE C CD2 1 
ATOM   11962 C CE1 . PHE C  1 464 ? -3.853  -7.832  -79.831  1.00 34.17  ? 464 PHE C CE1 1 
ATOM   11963 C CE2 . PHE C  1 464 ? -1.935  -8.634  -81.019  1.00 36.97  ? 464 PHE C CE2 1 
ATOM   11964 C CZ  . PHE C  1 464 ? -2.869  -8.785  -79.996  1.00 32.22  ? 464 PHE C CZ  1 
ATOM   11965 N N   . ASP C  1 465 ? -3.501  -3.723  -85.392  1.00 42.72  ? 465 ASP C N   1 
ATOM   11966 C CA  . ASP C  1 465 ? -3.784  -2.458  -86.065  1.00 42.84  ? 465 ASP C CA  1 
ATOM   11967 C C   . ASP C  1 465 ? -5.034  -2.573  -86.928  1.00 44.93  ? 465 ASP C C   1 
ATOM   11968 O O   . ASP C  1 465 ? -5.850  -1.642  -86.985  1.00 47.73  ? 465 ASP C O   1 
ATOM   11969 C CB  . ASP C  1 465 ? -2.581  -2.019  -86.902  1.00 44.60  ? 465 ASP C CB  1 
ATOM   11970 C CG  . ASP C  1 465 ? -2.899  -0.832  -87.805  1.00 55.42  ? 465 ASP C CG  1 
ATOM   11971 O OD1 . ASP C  1 465 ? -2.755  0.316   -87.331  1.00 56.70  ? 465 ASP C OD1 1 
ATOM   11972 O OD2 . ASP C  1 465 ? -3.329  -1.045  -88.964  1.00 58.53  ? 465 ASP C OD2 1 
ATOM   11973 N N   . LYS C  1 466 ? -5.214  -3.721  -87.581  1.00 44.07  ? 466 LYS C N   1 
ATOM   11974 C CA  . LYS C  1 466 ? -6.379  -3.918  -88.435  1.00 48.65  ? 466 LYS C CA  1 
ATOM   11975 C C   . LYS C  1 466 ? -7.658  -3.948  -87.618  1.00 44.94  ? 466 LYS C C   1 
ATOM   11976 O O   . LYS C  1 466 ? -8.656  -3.337  -88.004  1.00 44.53  ? 466 LYS C O   1 
ATOM   11977 C CB  . LYS C  1 466 ? -6.238  -5.209  -89.243  1.00 52.68  ? 466 LYS C CB  1 
ATOM   11978 C CG  . LYS C  1 466 ? -7.572  -5.782  -89.735  1.00 59.87  ? 466 LYS C CG  1 
ATOM   11979 C CD  . LYS C  1 466 ? -7.472  -6.420  -91.124  1.00 62.45  ? 466 LYS C CD  1 
ATOM   11980 C CE  . LYS C  1 466 ? -6.278  -7.360  -91.243  1.00 59.16  ? 466 LYS C CE  1 
ATOM   11981 N NZ  . LYS C  1 466 ? -5.880  -7.563  -92.678  1.00 63.83  ? 466 LYS C NZ  1 
ATOM   11982 N N   . LEU C  1 467 ? -7.647  -4.673  -86.496  1.00 41.61  ? 467 LEU C N   1 
ATOM   11983 C CA  . LEU C  1 467 ? -8.807  -4.719  -85.611  1.00 43.20  ? 467 LEU C CA  1 
ATOM   11984 C C   . LEU C  1 467 ? -9.175  -3.321  -85.137  1.00 45.61  ? 467 LEU C C   1 
ATOM   11985 O O   . LEU C  1 467 ? -10.333 -2.895  -85.248  1.00 44.82  ? 467 LEU C O   1 
ATOM   11986 C CB  . LEU C  1 467 ? -8.514  -5.642  -84.413  1.00 39.04  ? 467 LEU C CB  1 
ATOM   11987 C CG  . LEU C  1 467 ? -8.479  -7.147  -84.757  1.00 40.98  ? 467 LEU C CG  1 
ATOM   11988 C CD1 . LEU C  1 467 ? -7.803  -8.008  -83.676  1.00 41.46  ? 467 LEU C CD1 1 
ATOM   11989 C CD2 . LEU C  1 467 ? -9.878  -7.663  -85.037  1.00 40.32  ? 467 LEU C CD2 1 
ATOM   11990 N N   . PHE C  1 468 ? -8.191  -2.587  -84.617  1.00 42.24  ? 468 PHE C N   1 
ATOM   11991 C CA  . PHE C  1 468 ? -8.454  -1.246  -84.117  1.00 47.31  ? 468 PHE C CA  1 
ATOM   11992 C C   . PHE C  1 468 ? -9.095  -0.392  -85.200  1.00 45.84  ? 468 PHE C C   1 
ATOM   11993 O O   . PHE C  1 468 ? -10.202 0.123   -85.026  1.00 49.61  ? 468 PHE C O   1 
ATOM   11994 C CB  . PHE C  1 468 ? -7.160  -0.612  -83.614  1.00 45.56  ? 468 PHE C CB  1 
ATOM   11995 C CG  . PHE C  1 468 ? -7.289  0.845   -83.288  1.00 44.95  ? 468 PHE C CG  1 
ATOM   11996 C CD1 . PHE C  1 468 ? -7.964  1.256   -82.152  1.00 42.18  ? 468 PHE C CD1 1 
ATOM   11997 C CD2 . PHE C  1 468 ? -6.736  1.805   -84.124  1.00 43.72  ? 468 PHE C CD2 1 
ATOM   11998 C CE1 . PHE C  1 468 ? -8.079  2.602   -81.844  1.00 44.86  ? 468 PHE C CE1 1 
ATOM   11999 C CE2 . PHE C  1 468 ? -6.848  3.144   -83.828  1.00 48.14  ? 468 PHE C CE2 1 
ATOM   12000 C CZ  . PHE C  1 468 ? -7.519  3.545   -82.683  1.00 49.80  ? 468 PHE C CZ  1 
ATOM   12001 N N   . ARG C  1 469 ? -8.436  -0.281  -86.353  1.00 44.79  ? 469 ARG C N   1 
ATOM   12002 C CA  . ARG C  1 469 ? -8.980  0.552   -87.421  1.00 47.88  ? 469 ARG C CA  1 
ATOM   12003 C C   . ARG C  1 469 ? -10.315 0.025   -87.932  1.00 48.75  ? 469 ARG C C   1 
ATOM   12004 O O   . ARG C  1 469 ? -11.152 0.808   -88.387  1.00 51.07  ? 469 ARG C O   1 
ATOM   12005 C CB  . ARG C  1 469 ? -7.961  0.679   -88.550  1.00 47.26  ? 469 ARG C CB  1 
ATOM   12006 C CG  . ARG C  1 469 ? -6.774  1.543   -88.154  1.00 51.67  ? 469 ARG C CG  1 
ATOM   12007 C CD  . ARG C  1 469 ? -5.678  1.456   -89.170  1.00 54.60  ? 469 ARG C CD  1 
ATOM   12008 N NE  . ARG C  1 469 ? -4.500  2.267   -88.860  1.00 55.29  ? 469 ARG C NE  1 
ATOM   12009 C CZ  . ARG C  1 469 ? -4.391  3.580   -89.061  1.00 55.31  ? 469 ARG C CZ  1 
ATOM   12010 N NH1 . ARG C  1 469 ? -5.410  4.297   -89.527  1.00 57.21  ? 469 ARG C NH1 1 
ATOM   12011 N NH2 . ARG C  1 469 ? -3.251  4.186   -88.767  1.00 55.17  ? 469 ARG C NH2 1 
ATOM   12012 N N   . SER C  1 470 ? -10.553 -1.284  -87.839  1.00 49.35  ? 470 SER C N   1 
ATOM   12013 C CA  . SER C  1 470 ? -11.863 -1.810  -88.212  1.00 53.65  ? 470 SER C CA  1 
ATOM   12014 C C   . SER C  1 470 ? -12.937 -1.370  -87.223  1.00 52.99  ? 470 SER C C   1 
ATOM   12015 O O   . SER C  1 470 ? -14.036 -0.973  -87.630  1.00 56.57  ? 470 SER C O   1 
ATOM   12016 C CB  . SER C  1 470 ? -11.818 -3.333  -88.306  1.00 57.82  ? 470 SER C CB  1 
ATOM   12017 O OG  . SER C  1 470 ? -10.990 -3.748  -89.377  1.00 64.55  ? 470 SER C OG  1 
ATOM   12018 N N   . PHE C  1 471 ? -12.640 -1.437  -85.921  1.00 45.67  ? 471 PHE C N   1 
ATOM   12019 C CA  . PHE C  1 471 ? -13.597 -0.975  -84.921  1.00 44.10  ? 471 PHE C CA  1 
ATOM   12020 C C   . PHE C  1 471 ? -13.847 0.520   -85.067  1.00 45.40  ? 471 PHE C C   1 
ATOM   12021 O O   . PHE C  1 471 ? -14.991 0.980   -84.977  1.00 47.95  ? 471 PHE C O   1 
ATOM   12022 C CB  . PHE C  1 471 ? -13.093 -1.297  -83.500  1.00 41.76  ? 471 PHE C CB  1 
ATOM   12023 C CG  . PHE C  1 471 ? -13.011 -2.769  -83.196  1.00 46.08  ? 471 PHE C CG  1 
ATOM   12024 C CD1 . PHE C  1 471 ? -14.047 -3.620  -83.543  1.00 49.57  ? 471 PHE C CD1 1 
ATOM   12025 C CD2 . PHE C  1 471 ? -11.893 -3.307  -82.576  1.00 38.93  ? 471 PHE C CD2 1 
ATOM   12026 C CE1 . PHE C  1 471 ? -13.972 -4.977  -83.275  1.00 49.22  ? 471 PHE C CE1 1 
ATOM   12027 C CE2 . PHE C  1 471 ? -11.812 -4.658  -82.315  1.00 40.91  ? 471 PHE C CE2 1 
ATOM   12028 C CZ  . PHE C  1 471 ? -12.854 -5.497  -82.660  1.00 42.86  ? 471 PHE C CZ  1 
ATOM   12029 N N   . VAL C  1 472 ? -12.776 1.293   -85.272  1.00 45.40  ? 472 VAL C N   1 
ATOM   12030 C CA  . VAL C  1 472 ? -12.897 2.737   -85.448  1.00 48.03  ? 472 VAL C CA  1 
ATOM   12031 C C   . VAL C  1 472 ? -13.800 3.049   -86.630  1.00 54.20  ? 472 VAL C C   1 
ATOM   12032 O O   . VAL C  1 472 ? -14.634 3.963   -86.576  1.00 57.80  ? 472 VAL C O   1 
ATOM   12033 C CB  . VAL C  1 472 ? -11.498 3.363   -85.615  1.00 50.36  ? 472 VAL C CB  1 
ATOM   12034 C CG1 . VAL C  1 472 ? -11.595 4.802   -86.057  1.00 55.73  ? 472 VAL C CG1 1 
ATOM   12035 C CG2 . VAL C  1 472 ? -10.685 3.245   -84.299  1.00 48.33  ? 472 VAL C CG2 1 
ATOM   12036 N N   . ARG C  1 473 ? -13.665 2.289   -87.711  1.00 52.34  ? 473 ARG C N   1 
ATOM   12037 C CA  . ARG C  1 473 ? -14.498 2.567   -88.876  1.00 63.86  ? 473 ARG C CA  1 
ATOM   12038 C C   . ARG C  1 473 ? -15.949 2.200   -88.598  1.00 62.51  ? 473 ARG C C   1 
ATOM   12039 O O   . ARG C  1 473 ? -16.860 3.001   -88.834  1.00 59.23  ? 473 ARG C O   1 
ATOM   12040 C CB  . ARG C  1 473 ? -13.963 1.825   -90.100  1.00 69.16  ? 473 ARG C CB  1 
ATOM   12041 C CG  . ARG C  1 473 ? -12.735 2.476   -90.726  1.00 74.47  ? 473 ARG C CG  1 
ATOM   12042 C CD  . ARG C  1 473 ? -12.545 2.036   -92.173  1.00 80.27  ? 473 ARG C CD  1 
ATOM   12043 N NE  . ARG C  1 473 ? -12.613 0.582   -92.318  1.00 81.98  ? 473 ARG C NE  1 
ATOM   12044 C CZ  . ARG C  1 473 ? -11.566 -0.232  -92.207  1.00 82.30  ? 473 ARG C CZ  1 
ATOM   12045 N NH1 . ARG C  1 473 ? -10.363 0.265   -91.952  1.00 80.30  ? 473 ARG C NH1 1 
ATOM   12046 N NH2 . ARG C  1 473 ? -11.720 -1.544  -92.347  1.00 83.60  ? 473 ARG C NH2 1 
ATOM   12047 N N   . ARG C  1 474 ? -16.179 0.998   -88.066  1.00 60.11  ? 474 ARG C N   1 
ATOM   12048 C CA  . ARG C  1 474 ? -17.543 0.545   -87.825  1.00 61.97  ? 474 ARG C CA  1 
ATOM   12049 C C   . ARG C  1 474 ? -18.267 1.445   -86.828  1.00 64.67  ? 474 ARG C C   1 
ATOM   12050 O O   . ARG C  1 474 ? -19.494 1.595   -86.901  1.00 66.08  ? 474 ARG C O   1 
ATOM   12051 C CB  . ARG C  1 474 ? -17.516 -0.910  -87.351  1.00 58.82  ? 474 ARG C CB  1 
ATOM   12052 C CG  . ARG C  1 474 ? -18.795 -1.395  -86.710  1.00 64.30  ? 474 ARG C CG  1 
ATOM   12053 C CD  . ARG C  1 474 ? -19.916 -1.576  -87.718  1.00 71.39  ? 474 ARG C CD  1 
ATOM   12054 N NE  . ARG C  1 474 ? -19.604 -2.575  -88.736  1.00 81.83  ? 474 ARG C NE  1 
ATOM   12055 C CZ  . ARG C  1 474 ? -20.189 -3.768  -88.797  1.00 86.89  ? 474 ARG C CZ  1 
ATOM   12056 N NH1 . ARG C  1 474 ? -21.093 -4.094  -87.881  1.00 86.14  ? 474 ARG C NH1 1 
ATOM   12057 N NH2 . ARG C  1 474 ? -19.870 -4.635  -89.755  1.00 85.85  ? 474 ARG C NH2 1 
ATOM   12058 N N   . ALA C  1 475 ? -17.523 2.079   -85.915  1.00 64.96  ? 475 ALA C N   1 
ATOM   12059 C CA  . ALA C  1 475 ? -18.130 2.961   -84.927  1.00 62.54  ? 475 ALA C CA  1 
ATOM   12060 C C   . ALA C  1 475 ? -18.758 4.202   -85.554  1.00 65.19  ? 475 ALA C C   1 
ATOM   12061 O O   . ALA C  1 475 ? -19.617 4.833   -84.925  1.00 59.38  ? 475 ALA C O   1 
ATOM   12062 C CB  . ALA C  1 475 ? -17.086 3.365   -83.884  1.00 63.82  ? 475 ALA C CB  1 
ATOM   12063 N N   . GLN C  1 476 ? -18.365 4.557   -86.778  1.00 68.42  ? 476 GLN C N   1 
ATOM   12064 C CA  . GLN C  1 476 ? -18.864 5.746   -87.452  1.00 72.56  ? 476 GLN C CA  1 
ATOM   12065 C C   . GLN C  1 476 ? -19.926 5.431   -88.494  1.00 78.77  ? 476 GLN C C   1 
ATOM   12066 O O   . GLN C  1 476 ? -20.248 6.295   -89.313  1.00 84.43  ? 476 GLN C O   1 
ATOM   12067 C CB  . GLN C  1 476 ? -17.708 6.498   -88.111  1.00 72.02  ? 476 GLN C CB  1 
ATOM   12068 C CG  . GLN C  1 476 ? -16.556 6.809   -87.182  1.00 69.86  ? 476 GLN C CG  1 
ATOM   12069 C CD  . GLN C  1 476 ? -15.327 7.276   -87.931  1.00 70.38  ? 476 GLN C CD  1 
ATOM   12070 O OE1 . GLN C  1 476 ? -15.236 8.435   -88.336  1.00 71.52  ? 476 GLN C OE1 1 
ATOM   12071 N NE2 . GLN C  1 476 ? -14.372 6.372   -88.121  1.00 68.76  ? 476 GLN C NE2 1 
ATOM   12072 N N   . GLU C  1 477 ? -20.468 4.221   -88.493  1.00 82.54  ? 477 GLU C N   1 
ATOM   12073 C CA  . GLU C  1 477 ? -21.423 3.820   -89.522  1.00 88.09  ? 477 GLU C CA  1 
ATOM   12074 C C   . GLU C  1 477 ? -22.771 3.425   -88.925  1.00 87.08  ? 477 GLU C C   1 
ATOM   12075 O O   . GLU C  1 477 ? -22.839 2.880   -87.825  1.00 83.29  ? 477 GLU C O   1 
ATOM   12076 C CB  . GLU C  1 477 ? -20.856 2.665   -90.356  1.00 89.76  ? 477 GLU C CB  1 
ATOM   12077 C CG  . GLU C  1 477 ? -19.678 3.059   -91.236  1.00 92.05  ? 477 GLU C CG  1 
ATOM   12078 C CD  . GLU C  1 477 ? -19.022 1.869   -91.907  1.00 93.44  ? 477 GLU C CD  1 
ATOM   12079 O OE1 . GLU C  1 477 ? -18.178 2.085   -92.804  1.00 95.30  ? 477 GLU C OE1 1 
ATOM   12080 O OE2 . GLU C  1 477 ? -19.345 0.720   -91.536  1.00 92.04  ? 477 GLU C OE2 1 
ATOM   12081 N N   . MET D  1 1   ? 5.203   -47.205 37.277   1.00 62.17  ? 1   MET D N   1 
ATOM   12082 C CA  . MET D  1 1   ? 6.322   -47.595 38.101   1.00 66.27  ? 1   MET D CA  1 
ATOM   12083 C C   . MET D  1 1   ? 6.093   -48.848 38.773   1.00 65.41  ? 1   MET D C   1 
ATOM   12084 O O   . MET D  1 1   ? 4.966   -49.230 39.003   1.00 73.00  ? 1   MET D O   1 
ATOM   12085 C CB  . MET D  1 1   ? 6.506   -46.644 39.280   1.00 71.10  ? 1   MET D CB  1 
ATOM   12086 C CG  . MET D  1 1   ? 6.236   -45.185 39.061   1.00 75.83  ? 1   MET D CG  1 
ATOM   12087 S SD  . MET D  1 1   ? 7.044   -44.257 40.373   1.00 80.49  ? 1   MET D SD  1 
ATOM   12088 C CE  . MET D  1 1   ? 6.296   -42.664 40.078   1.00 77.37  ? 1   MET D CE  1 
ATOM   12089 N N   . LYS D  1 2   ? 7.142   -49.574 39.000   1.00 54.58  ? 2   LYS D N   1 
ATOM   12090 C CA  . LYS D  1 2   ? 7.035   -50.654 39.840   1.00 50.12  ? 2   LYS D CA  1 
ATOM   12091 C C   . LYS D  1 2   ? 6.910   -49.817 41.137   1.00 44.98  ? 2   LYS D C   1 
ATOM   12092 O O   . LYS D  1 2   ? 7.728   -48.975 41.406   1.00 47.38  ? 2   LYS D O   1 
ATOM   12093 C CB  . LYS D  1 2   ? 8.285   -51.439 39.893   1.00 45.96  ? 2   LYS D CB  1 
ATOM   12094 C CG  . LYS D  1 2   ? 8.186   -52.750 40.616   1.00 48.01  ? 2   LYS D CG  1 
ATOM   12095 C CD  . LYS D  1 2   ? 9.481   -53.518 40.535   1.00 55.91  ? 2   LYS D CD  1 
ATOM   12096 C CE  . LYS D  1 2   ? 10.605  -52.739 41.161   1.00 57.21  ? 2   LYS D CE  1 
ATOM   12097 N NZ  . LYS D  1 2   ? 11.884  -53.200 40.587   1.00 57.35  ? 2   LYS D NZ  1 
ATOM   12098 N N   . LYS D  1 3   ? 5.856   -49.999 41.898   1.00 37.66  ? 3   LYS D N   1 
ATOM   12099 C CA  . LYS D  1 3   ? 5.789   -49.347 43.188   1.00 31.71  ? 3   LYS D CA  1 
ATOM   12100 C C   . LYS D  1 3   ? 6.158   -50.282 44.323   1.00 33.19  ? 3   LYS D C   1 
ATOM   12101 O O   . LYS D  1 3   ? 6.188   -51.466 44.124   1.00 34.29  ? 3   LYS D O   1 
ATOM   12102 C CB  . LYS D  1 3   ? 4.416   -48.859 43.464   1.00 29.97  ? 3   LYS D CB  1 
ATOM   12103 C CG  . LYS D  1 3   ? 3.830   -47.918 42.457   1.00 41.11  ? 3   LYS D CG  1 
ATOM   12104 C CD  . LYS D  1 3   ? 3.856   -46.509 42.985   1.00 49.91  ? 3   LYS D CD  1 
ATOM   12105 C CE  . LYS D  1 3   ? 3.573   -45.527 41.872   1.00 55.91  ? 3   LYS D CE  1 
ATOM   12106 N NZ  . LYS D  1 3   ? 2.269   -44.863 42.071   1.00 59.79  ? 3   LYS D NZ  1 
ATOM   12107 N N   . LEU D  1 4   ? 6.571   -49.736 45.439   1.00 33.57  ? 4   LEU D N   1 
ATOM   12108 C CA  . LEU D  1 4   ? 6.700   -50.470 46.651   1.00 30.13  ? 4   LEU D CA  1 
ATOM   12109 C C   . LEU D  1 4   ? 5.397   -50.202 47.498   1.00 30.39  ? 4   LEU D C   1 
ATOM   12110 O O   . LEU D  1 4   ? 5.039   -49.087 47.706   1.00 33.67  ? 4   LEU D O   1 
ATOM   12111 C CB  . LEU D  1 4   ? 7.891   -50.073 47.426   1.00 32.07  ? 4   LEU D CB  1 
ATOM   12112 C CG  . LEU D  1 4   ? 8.131   -50.815 48.736   1.00 30.96  ? 4   LEU D CG  1 
ATOM   12113 C CD1 . LEU D  1 4   ? 9.600   -51.080 48.969   1.00 34.97  ? 4   LEU D CD1 1 
ATOM   12114 C CD2 . LEU D  1 4   ? 7.533   -50.099 49.929   1.00 23.75  ? 4   LEU D CD2 1 
ATOM   12115 N N   . PHE D  1 5   ? 4.748   -51.239 47.964   1.00 28.85  ? 5   PHE D N   1 
ATOM   12116 C CA  . PHE D  1 5   ? 3.537   -51.115 48.776   1.00 22.70  ? 5   PHE D CA  1 
ATOM   12117 C C   . PHE D  1 5   ? 3.898   -51.258 50.255   1.00 26.89  ? 5   PHE D C   1 
ATOM   12118 O O   . PHE D  1 5   ? 4.399   -52.302 50.673   1.00 30.38  ? 5   PHE D O   1 
ATOM   12119 C CB  . PHE D  1 5   ? 2.499   -52.161 48.371   1.00 23.10  ? 5   PHE D CB  1 
ATOM   12120 C CG  . PHE D  1 5   ? 1.952   -51.954 46.964   1.00 30.40  ? 5   PHE D CG  1 
ATOM   12121 C CD1 . PHE D  1 5   ? 1.429   -50.721 46.589   1.00 31.72  ? 5   PHE D CD1 1 
ATOM   12122 C CD2 . PHE D  1 5   ? 1.988   -52.978 46.020   1.00 28.21  ? 5   PHE D CD2 1 
ATOM   12123 C CE1 . PHE D  1 5   ? 0.928   -50.512 45.287   1.00 30.90  ? 5   PHE D CE1 1 
ATOM   12124 C CE2 . PHE D  1 5   ? 1.483   -52.779 44.720   1.00 28.99  ? 5   PHE D CE2 1 
ATOM   12125 C CZ  . PHE D  1 5   ? 0.955   -51.532 44.367   1.00 26.45  ? 5   PHE D CZ  1 
ATOM   12126 N N   . LEU D  1 6   ? 3.640   -50.208 51.032   1.00 24.32  ? 6   LEU D N   1 
ATOM   12127 C CA  . LEU D  1 6   ? 4.012   -50.127 52.443   1.00 20.03  ? 6   LEU D CA  1 
ATOM   12128 C C   . LEU D  1 6   ? 2.744   -50.132 53.288   1.00 23.29  ? 6   LEU D C   1 
ATOM   12129 O O   . LEU D  1 6   ? 1.800   -49.397 52.990   1.00 21.17  ? 6   LEU D O   1 
ATOM   12130 C CB  . LEU D  1 6   ? 4.820   -48.851 52.704   1.00 23.21  ? 6   LEU D CB  1 
ATOM   12131 C CG  . LEU D  1 6   ? 5.441   -48.632 54.093   1.00 24.91  ? 6   LEU D CG  1 
ATOM   12132 C CD1 . LEU D  1 6   ? 6.407   -49.722 54.452   1.00 25.53  ? 6   LEU D CD1 1 
ATOM   12133 C CD2 . LEU D  1 6   ? 6.159   -47.306 54.132   1.00 24.87  ? 6   LEU D CD2 1 
ATOM   12134 N N   . VAL D  1 7   ? 2.716   -50.949 54.342   1.00 26.35  ? 7   VAL D N   1 
ATOM   12135 C CA  . VAL D  1 7   ? 1.511   -51.149 55.154   1.00 23.46  ? 7   VAL D CA  1 
ATOM   12136 C C   . VAL D  1 7   ? 1.918   -51.033 56.626   1.00 23.41  ? 7   VAL D C   1 
ATOM   12137 O O   . VAL D  1 7   ? 2.514   -51.956 57.181   1.00 21.15  ? 7   VAL D O   1 
ATOM   12138 C CB  . VAL D  1 7   ? 0.843   -52.505 54.874   1.00 25.23  ? 7   VAL D CB  1 
ATOM   12139 C CG1 . VAL D  1 7   ? -0.564  -52.551 55.452   1.00 25.72  ? 7   VAL D CG1 1 
ATOM   12140 C CG2 . VAL D  1 7   ? 0.815   -52.840 53.337   1.00 30.58  ? 7   VAL D CG2 1 
ATOM   12141 N N   . PHE D  1 8   ? 1.619   -49.904 57.260   1.00 19.65  ? 8   PHE D N   1 
ATOM   12142 C CA  . PHE D  1 8   ? 1.817   -49.813 58.708   1.00 20.66  ? 8   PHE D CA  1 
ATOM   12143 C C   . PHE D  1 8   ? 0.621   -50.423 59.421   1.00 24.19  ? 8   PHE D C   1 
ATOM   12144 O O   . PHE D  1 8   ? -0.527  -50.069 59.123   1.00 19.14  ? 8   PHE D O   1 
ATOM   12145 C CB  . PHE D  1 8   ? 1.987   -48.360 59.145   1.00 25.78  ? 8   PHE D CB  1 
ATOM   12146 C CG  . PHE D  1 8   ? 3.292   -47.752 58.726   1.00 28.08  ? 8   PHE D CG  1 
ATOM   12147 C CD1 . PHE D  1 8   ? 4.424   -47.900 59.514   1.00 30.09  ? 8   PHE D CD1 1 
ATOM   12148 C CD2 . PHE D  1 8   ? 3.390   -47.053 57.532   1.00 22.90  ? 8   PHE D CD2 1 
ATOM   12149 C CE1 . PHE D  1 8   ? 5.637   -47.346 59.124   1.00 29.26  ? 8   PHE D CE1 1 
ATOM   12150 C CE2 . PHE D  1 8   ? 4.593   -46.498 57.134   1.00 25.12  ? 8   PHE D CE2 1 
ATOM   12151 C CZ  . PHE D  1 8   ? 5.726   -46.645 57.938   1.00 25.97  ? 8   PHE D CZ  1 
ATOM   12152 N N   . TRP D  1 9   ? 0.877   -51.318 60.388   1.00 20.00  ? 9   TRP D N   1 
ATOM   12153 C CA  . TRP D  1 9   ? -0.184  -51.872 61.232   1.00 19.40  ? 9   TRP D CA  1 
ATOM   12154 C C   . TRP D  1 9   ? 0.224   -51.689 62.701   1.00 20.40  ? 9   TRP D C   1 
ATOM   12155 O O   . TRP D  1 9   ? 1.028   -52.462 63.226   1.00 21.95  ? 9   TRP D O   1 
ATOM   12156 C CB  . TRP D  1 9   ? -0.424  -53.338 60.883   1.00 19.87  ? 9   TRP D CB  1 
ATOM   12157 C CG  . TRP D  1 9   ? -1.753  -53.925 61.327   1.00 20.88  ? 9   TRP D CG  1 
ATOM   12158 C CD1 . TRP D  1 9   ? -2.689  -53.359 62.146   1.00 24.46  ? 9   TRP D CD1 1 
ATOM   12159 C CD2 . TRP D  1 9   ? -2.260  -55.212 60.974   1.00 22.62  ? 9   TRP D CD2 1 
ATOM   12160 N NE1 . TRP D  1 9   ? -3.758  -54.217 62.306   1.00 20.90  ? 9   TRP D NE1 1 
ATOM   12161 C CE2 . TRP D  1 9   ? -3.508  -55.365 61.604   1.00 21.81  ? 9   TRP D CE2 1 
ATOM   12162 C CE3 . TRP D  1 9   ? -1.779  -56.251 60.179   1.00 19.80  ? 9   TRP D CE3 1 
ATOM   12163 C CZ2 . TRP D  1 9   ? -4.279  -56.507 61.447   1.00 22.69  ? 9   TRP D CZ2 1 
ATOM   12164 C CZ3 . TRP D  1 9   ? -2.550  -57.380 60.032   1.00 24.79  ? 9   TRP D CZ3 1 
ATOM   12165 C CH2 . TRP D  1 9   ? -3.780  -57.503 60.660   1.00 22.08  ? 9   TRP D CH2 1 
ATOM   12166 N N   . TRP D  1 10  ? -0.308  -50.659 63.355   1.00 21.94  ? 10  TRP D N   1 
ATOM   12167 C CA  . TRP D  1 10  ? 0.058   -50.336 64.737   1.00 22.01  ? 10  TRP D CA  1 
ATOM   12168 C C   . TRP D  1 10  ? -0.872  -51.067 65.698   1.00 19.95  ? 10  TRP D C   1 
ATOM   12169 O O   . TRP D  1 10  ? -2.093  -50.875 65.650   1.00 22.12  ? 10  TRP D O   1 
ATOM   12170 C CB  . TRP D  1 10  ? -0.018  -48.830 64.984   1.00 18.58  ? 10  TRP D CB  1 
ATOM   12171 C CG  . TRP D  1 10  ? 0.839   -47.961 64.100   1.00 22.54  ? 10  TRP D CG  1 
ATOM   12172 C CD1 . TRP D  1 10  ? 0.404   -47.113 63.125   1.00 18.06  ? 10  TRP D CD1 1 
ATOM   12173 C CD2 . TRP D  1 10  ? 2.270   -47.816 64.150   1.00 23.26  ? 10  TRP D CD2 1 
ATOM   12174 N NE1 . TRP D  1 10  ? 1.474   -46.479 62.542   1.00 22.00  ? 10  TRP D NE1 1 
ATOM   12175 C CE2 . TRP D  1 10  ? 2.629   -46.888 63.156   1.00 21.93  ? 10  TRP D CE2 1 
ATOM   12176 C CE3 . TRP D  1 10  ? 3.281   -48.401 64.922   1.00 22.61  ? 10  TRP D CE3 1 
ATOM   12177 C CZ2 . TRP D  1 10  ? 3.954   -46.510 62.926   1.00 21.31  ? 10  TRP D CZ2 1 
ATOM   12178 C CZ3 . TRP D  1 10  ? 4.597   -48.024 64.692   1.00 24.59  ? 10  TRP D CZ3 1 
ATOM   12179 C CH2 . TRP D  1 10  ? 4.922   -47.093 63.701   1.00 24.49  ? 10  TRP D CH2 1 
ATOM   12180 N N   . HIS D  1 11  ? -0.297  -51.886 66.586   1.00 20.65  ? 11  HIS D N   1 
ATOM   12181 C CA  . HIS D  1 11  ? -1.064  -52.711 67.507   1.00 21.17  ? 11  HIS D CA  1 
ATOM   12182 C C   . HIS D  1 11  ? -1.194  -52.021 68.874   1.00 24.70  ? 11  HIS D C   1 
ATOM   12183 O O   . HIS D  1 11  ? -0.193  -51.609 69.477   1.00 21.33  ? 11  HIS D O   1 
ATOM   12184 C CB  . HIS D  1 11  ? -0.391  -54.093 67.608   1.00 21.47  ? 11  HIS D CB  1 
ATOM   12185 C CG  . HIS D  1 11  ? -0.870  -54.934 68.745   1.00 22.18  ? 11  HIS D CG  1 
ATOM   12186 N ND1 . HIS D  1 11  ? -2.200  -55.251 68.938   1.00 15.90  ? 11  HIS D ND1 1 
ATOM   12187 C CD2 . HIS D  1 11  ? -0.184  -55.546 69.741   1.00 19.55  ? 11  HIS D CD2 1 
ATOM   12188 C CE1 . HIS D  1 11  ? -2.311  -56.006 70.018   1.00 22.75  ? 11  HIS D CE1 1 
ATOM   12189 N NE2 . HIS D  1 11  ? -1.105  -56.195 70.523   1.00 20.74  ? 11  HIS D NE2 1 
ATOM   12190 N N   . MET D  1 12  ? -2.434  -51.896 69.360   1.00 23.22  ? 12  MET D N   1 
ATOM   12191 C CA  . MET D  1 12  ? -2.735  -51.203 70.608   1.00 21.48  ? 12  MET D CA  1 
ATOM   12192 C C   . MET D  1 12  ? -3.438  -52.164 71.559   1.00 19.86  ? 12  MET D C   1 
ATOM   12193 O O   . MET D  1 12  ? -4.493  -52.721 71.227   1.00 17.09  ? 12  MET D O   1 
ATOM   12194 C CB  . MET D  1 12  ? -3.610  -49.977 70.341   1.00 23.45  ? 12  MET D CB  1 
ATOM   12195 C CG  . MET D  1 12  ? -3.128  -49.107 69.209   1.00 28.21  ? 12  MET D CG  1 
ATOM   12196 S SD  . MET D  1 12  ? -1.532  -48.385 69.469   1.00 43.20  ? 12  MET D SD  1 
ATOM   12197 C CE  . MET D  1 12  ? -1.730  -46.839 68.575   1.00 41.68  ? 12  MET D CE  1 
ATOM   12198 N N   . HIS D  1 13  ? -2.861  -52.351 72.739   1.00 23.39  ? 13  HIS D N   1 
ATOM   12199 C CA  . HIS D  1 13  ? -3.392  -53.328 73.673   1.00 20.88  ? 13  HIS D CA  1 
ATOM   12200 C C   . HIS D  1 13  ? -3.019  -52.927 75.098   1.00 21.03  ? 13  HIS D C   1 
ATOM   12201 O O   . HIS D  1 13  ? -1.906  -52.459 75.335   1.00 17.07  ? 13  HIS D O   1 
ATOM   12202 C CB  . HIS D  1 13  ? -2.848  -54.731 73.372   1.00 18.74  ? 13  HIS D CB  1 
ATOM   12203 C CG  . HIS D  1 13  ? -3.136  -55.731 74.452   1.00 23.98  ? 13  HIS D CG  1 
ATOM   12204 N ND1 . HIS D  1 13  ? -4.419  -56.029 74.869   1.00 21.91  ? 13  HIS D ND1 1 
ATOM   12205 C CD2 . HIS D  1 13  ? -2.311  -56.499 75.201   1.00 24.56  ? 13  HIS D CD2 1 
ATOM   12206 C CE1 . HIS D  1 13  ? -4.371  -56.940 75.823   1.00 22.72  ? 13  HIS D CE1 1 
ATOM   12207 N NE2 . HIS D  1 13  ? -3.105  -57.241 76.048   1.00 26.57  ? 13  HIS D NE2 1 
ATOM   12208 N N   . GLN D  1 14  ? -3.951  -53.131 76.037   1.00 23.10  ? 14  GLN D N   1 
ATOM   12209 C CA  . GLN D  1 14  ? -3.638  -53.222 77.477   1.00 21.72  ? 14  GLN D CA  1 
ATOM   12210 C C   . GLN D  1 14  ? -4.412  -54.387 78.074   1.00 24.96  ? 14  GLN D C   1 
ATOM   12211 O O   . GLN D  1 14  ? -5.598  -54.570 77.745   1.00 19.66  ? 14  GLN D O   1 
ATOM   12212 C CB  . GLN D  1 14  ? -4.006  -51.946 78.244   1.00 21.76  ? 14  GLN D CB  1 
ATOM   12213 C CG  . GLN D  1 14  ? -3.238  -50.683 77.789   1.00 19.80  ? 14  GLN D CG  1 
ATOM   12214 C CD  . GLN D  1 14  ? -1.762  -50.796 78.091   1.00 25.07  ? 14  GLN D CD  1 
ATOM   12215 O OE1 . GLN D  1 14  ? -1.371  -51.425 79.085   1.00 23.05  ? 14  GLN D OE1 1 
ATOM   12216 N NE2 . GLN D  1 14  ? -0.929  -50.203 77.239   1.00 22.38  ? 14  GLN D NE2 1 
ATOM   12217 N N   . PRO D  1 15  ? -3.784  -55.176 78.957   1.00 26.54  ? 15  PRO D N   1 
ATOM   12218 C CA  . PRO D  1 15  ? -4.554  -56.125 79.781   1.00 25.87  ? 15  PRO D CA  1 
ATOM   12219 C C   . PRO D  1 15  ? -5.509  -55.374 80.697   1.00 25.45  ? 15  PRO D C   1 
ATOM   12220 O O   . PRO D  1 15  ? -5.339  -54.181 80.963   1.00 23.10  ? 15  PRO D O   1 
ATOM   12221 C CB  . PRO D  1 15  ? -3.476  -56.867 80.586   1.00 26.30  ? 15  PRO D CB  1 
ATOM   12222 C CG  . PRO D  1 15  ? -2.334  -55.909 80.661   1.00 24.45  ? 15  PRO D CG  1 
ATOM   12223 C CD  . PRO D  1 15  ? -2.357  -55.146 79.332   1.00 25.06  ? 15  PRO D CD  1 
ATOM   12224 N N   . LEU D  1 16  ? -6.525  -56.090 81.193   1.00 26.18  ? 16  LEU D N   1 
ATOM   12225 C CA  . LEU D  1 16  ? -7.538  -55.497 82.067   1.00 31.16  ? 16  LEU D CA  1 
ATOM   12226 C C   . LEU D  1 16  ? -6.954  -55.184 83.448   1.00 30.71  ? 16  LEU D C   1 
ATOM   12227 O O   . LEU D  1 16  ? -6.733  -56.100 84.249   1.00 25.57  ? 16  LEU D O   1 
ATOM   12228 C CB  . LEU D  1 16  ? -8.729  -56.447 82.197   1.00 32.97  ? 16  LEU D CB  1 
ATOM   12229 C CG  . LEU D  1 16  ? -9.881  -55.898 83.040   1.00 29.59  ? 16  LEU D CG  1 
ATOM   12230 C CD1 . LEU D  1 16  ? -10.382 -54.578 82.435   1.00 30.91  ? 16  LEU D CD1 1 
ATOM   12231 C CD2 . LEU D  1 16  ? -11.004 -56.907 83.151   1.00 31.23  ? 16  LEU D CD2 1 
ATOM   12232 N N   . TYR D  1 17  ? -6.738  -53.894 83.750   1.00 27.57  ? 17  TYR D N   1 
ATOM   12233 C CA  . TYR D  1 17  ? -6.182  -53.468 85.030   1.00 25.89  ? 17  TYR D CA  1 
ATOM   12234 C C   . TYR D  1 17  ? -7.243  -53.318 86.118   1.00 30.75  ? 17  TYR D C   1 
ATOM   12235 O O   . TYR D  1 17  ? -6.926  -52.921 87.250   1.00 25.82  ? 17  TYR D O   1 
ATOM   12236 C CB  . TYR D  1 17  ? -5.428  -52.140 84.872   1.00 28.58  ? 17  TYR D CB  1 
ATOM   12237 C CG  . TYR D  1 17  ? -4.229  -52.224 83.945   1.00 28.31  ? 17  TYR D CG  1 
ATOM   12238 C CD1 . TYR D  1 17  ? -3.119  -52.991 84.287   1.00 31.23  ? 17  TYR D CD1 1 
ATOM   12239 C CD2 . TYR D  1 17  ? -4.206  -51.535 82.727   1.00 23.79  ? 17  TYR D CD2 1 
ATOM   12240 C CE1 . TYR D  1 17  ? -2.015  -53.083 83.435   1.00 31.33  ? 17  TYR D CE1 1 
ATOM   12241 C CE2 . TYR D  1 17  ? -3.096  -51.610 81.874   1.00 26.01  ? 17  TYR D CE2 1 
ATOM   12242 C CZ  . TYR D  1 17  ? -2.011  -52.399 82.226   1.00 28.86  ? 17  TYR D CZ  1 
ATOM   12243 O OH  . TYR D  1 17  ? -0.908  -52.504 81.398   1.00 26.00  ? 17  TYR D OH  1 
ATOM   12244 N N   . ARG D  1 18  ? -8.487  -53.630 85.807   1.00 33.08  ? 18  ARG D N   1 
ATOM   12245 C CA  . ARG D  1 18  ? -9.598  -53.335 86.693   1.00 34.66  ? 18  ARG D CA  1 
ATOM   12246 C C   . ARG D  1 18  ? -9.826  -54.547 87.586   1.00 35.75  ? 18  ARG D C   1 
ATOM   12247 O O   . ARG D  1 18  ? -10.328 -55.579 87.126   1.00 35.08  ? 18  ARG D O   1 
ATOM   12248 C CB  . ARG D  1 18  ? -10.834 -52.977 85.873   1.00 34.60  ? 18  ARG D CB  1 
ATOM   12249 C CG  . ARG D  1 18  ? -11.979 -52.444 86.676   1.00 35.51  ? 18  ARG D CG  1 
ATOM   12250 C CD  . ARG D  1 18  ? -13.220 -52.339 85.813   1.00 35.49  ? 18  ARG D CD  1 
ATOM   12251 N NE  . ARG D  1 18  ? -14.378 -51.840 86.551   1.00 40.29  ? 18  ARG D NE  1 
ATOM   12252 C CZ  . ARG D  1 18  ? -15.057 -52.554 87.442   1.00 41.21  ? 18  ARG D CZ  1 
ATOM   12253 N NH1 . ARG D  1 18  ? -14.684 -53.796 87.717   1.00 44.75  ? 18  ARG D NH1 1 
ATOM   12254 N NH2 . ARG D  1 18  ? -16.103 -52.030 88.064   1.00 45.81  ? 18  ARG D NH2 1 
ATOM   12255 N N   . GLU D  1 19  ? -9.439  -54.419 88.856   1.00 30.57  ? 19  GLU D N   1 
ATOM   12256 C CA  . GLU D  1 19  ? -9.613  -55.495 89.826   1.00 34.28  ? 19  GLU D CA  1 
ATOM   12257 C C   . GLU D  1 19  ? -11.102 -55.762 90.018   1.00 34.08  ? 19  GLU D C   1 
ATOM   12258 O O   . GLU D  1 19  ? -11.868 -54.820 90.257   1.00 35.28  ? 19  GLU D O   1 
ATOM   12259 C CB  . GLU D  1 19  ? -8.960  -55.128 91.162   1.00 35.16  ? 19  GLU D CB  1 
ATOM   12260 C CG  . GLU D  1 19  ? -8.471  -56.337 91.947   1.00 34.51  ? 19  GLU D CG  1 
ATOM   12261 C CD  . GLU D  1 19  ? -9.529  -56.874 92.885   1.00 46.46  ? 19  GLU D CD  1 
ATOM   12262 O OE1 . GLU D  1 19  ? -10.605 -56.247 93.000   1.00 47.78  ? 19  GLU D OE1 1 
ATOM   12263 O OE2 . GLU D  1 19  ? -9.278  -57.924 93.513   1.00 53.20  ? 19  GLU D OE2 1 
ATOM   12264 N N   . PRO D  1 20  ? -11.557 -57.011 89.893   1.00 31.98  ? 20  PRO D N   1 
ATOM   12265 C CA  . PRO D  1 20  ? -13.004 -57.251 89.810   1.00 37.19  ? 20  PRO D CA  1 
ATOM   12266 C C   . PRO D  1 20  ? -13.747 -57.156 91.138   1.00 43.28  ? 20  PRO D C   1 
ATOM   12267 O O   . PRO D  1 20  ? -14.982 -57.071 91.117   1.00 48.14  ? 20  PRO D O   1 
ATOM   12268 C CB  . PRO D  1 20  ? -13.089 -58.669 89.220   1.00 38.08  ? 20  PRO D CB  1 
ATOM   12269 C CG  . PRO D  1 20  ? -11.800 -59.316 89.583   1.00 34.45  ? 20  PRO D CG  1 
ATOM   12270 C CD  . PRO D  1 20  ? -10.765 -58.231 89.647   1.00 30.25  ? 20  PRO D CD  1 
ATOM   12271 N N   . TYR D  1 21  ? -13.059 -57.155 92.281   1.00 44.06  ? 21  TYR D N   1 
ATOM   12272 C CA  . TYR D  1 21  ? -13.762 -57.043 93.559   1.00 46.54  ? 21  TYR D CA  1 
ATOM   12273 C C   . TYR D  1 21  ? -13.885 -55.597 94.030   1.00 48.51  ? 21  TYR D C   1 
ATOM   12274 O O   . TYR D  1 21  ? -14.900 -55.224 94.626   1.00 52.91  ? 21  TYR D O   1 
ATOM   12275 C CB  . TYR D  1 21  ? -13.070 -57.904 94.624   1.00 41.38  ? 21  TYR D CB  1 
ATOM   12276 C CG  . TYR D  1 21  ? -13.260 -59.373 94.349   1.00 42.90  ? 21  TYR D CG  1 
ATOM   12277 C CD1 . TYR D  1 21  ? -14.420 -60.028 94.741   1.00 46.89  ? 21  TYR D CD1 1 
ATOM   12278 C CD2 . TYR D  1 21  ? -12.300 -60.098 93.655   1.00 36.86  ? 21  TYR D CD2 1 
ATOM   12279 C CE1 . TYR D  1 21  ? -14.608 -61.367 94.464   1.00 46.98  ? 21  TYR D CE1 1 
ATOM   12280 C CE2 . TYR D  1 21  ? -12.478 -61.432 93.373   1.00 38.33  ? 21  TYR D CE2 1 
ATOM   12281 C CZ  . TYR D  1 21  ? -13.632 -62.060 93.772   1.00 43.07  ? 21  TYR D CZ  1 
ATOM   12282 O OH  . TYR D  1 21  ? -13.802 -63.391 93.492   1.00 39.94  ? 21  TYR D OH  1 
ATOM   12283 N N   . THR D  1 22  ? -12.873 -54.774 93.774   1.00 47.27  ? 22  THR D N   1 
ATOM   12284 C CA  . THR D  1 22  ? -12.935 -53.363 94.121   1.00 45.59  ? 22  THR D CA  1 
ATOM   12285 C C   . THR D  1 22  ? -13.330 -52.491 92.942   1.00 46.73  ? 22  THR D C   1 
ATOM   12286 O O   . THR D  1 22  ? -13.739 -51.341 93.142   1.00 49.56  ? 22  THR D O   1 
ATOM   12287 C CB  . THR D  1 22  ? -11.584 -52.888 94.674   1.00 43.76  ? 22  THR D CB  1 
ATOM   12288 O OG1 . THR D  1 22  ? -10.564 -53.038 93.677   1.00 42.89  ? 22  THR D OG1 1 
ATOM   12289 C CG2 . THR D  1 22  ? -11.203 -53.700 95.920   1.00 43.60  ? 22  THR D CG2 1 
ATOM   12290 N N   . GLY D  1 23  ? -13.239 -53.015 91.726   1.00 42.53  ? 23  GLY D N   1 
ATOM   12291 C CA  . GLY D  1 23  ? -13.494 -52.176 90.577   1.00 44.58  ? 23  GLY D CA  1 
ATOM   12292 C C   . GLY D  1 23  ? -12.481 -51.077 90.393   1.00 45.34  ? 23  GLY D C   1 
ATOM   12293 O O   . GLY D  1 23  ? -12.773 -50.080 89.727   1.00 51.92  ? 23  GLY D O   1 
ATOM   12294 N N   . GLU D  1 24  ? -11.291 -51.226 90.963   1.00 38.76  ? 24  GLU D N   1 
ATOM   12295 C CA  . GLU D  1 24  ? -10.246 -50.223 90.841   1.00 38.60  ? 24  GLU D CA  1 
ATOM   12296 C C   . GLU D  1 24  ? -9.232  -50.657 89.790   1.00 38.29  ? 24  GLU D C   1 
ATOM   12297 O O   . GLU D  1 24  ? -8.850  -51.832 89.714   1.00 34.18  ? 24  GLU D O   1 
ATOM   12298 C CB  . GLU D  1 24  ? -9.555  -49.977 92.187   1.00 41.53  ? 24  GLU D CB  1 
ATOM   12299 C CG  . GLU D  1 24  ? -10.484 -49.392 93.224   1.00 48.52  ? 24  GLU D CG  1 
ATOM   12300 C CD  . GLU D  1 24  ? -9.903  -49.391 94.629   1.00 55.88  ? 24  GLU D CD  1 
ATOM   12301 O OE1 . GLU D  1 24  ? -10.665 -49.093 95.570   1.00 61.95  ? 24  GLU D OE1 1 
ATOM   12302 O OE2 . GLU D  1 24  ? -8.702  -49.684 94.801   1.00 58.73  ? 24  GLU D OE2 1 
ATOM   12303 N N   . TYR D  1 25  ? -8.834  -49.705 88.959   1.00 32.41  ? 25  TYR D N   1 
ATOM   12304 C CA  . TYR D  1 25  ? -7.707  -49.892 88.070   1.00 30.33  ? 25  TYR D CA  1 
ATOM   12305 C C   . TYR D  1 25  ? -6.415  -49.813 88.871   1.00 26.54  ? 25  TYR D C   1 
ATOM   12306 O O   . TYR D  1 25  ? -6.066  -48.749 89.396   1.00 27.06  ? 25  TYR D O   1 
ATOM   12307 C CB  . TYR D  1 25  ? -7.731  -48.840 86.965   1.00 30.53  ? 25  TYR D CB  1 
ATOM   12308 C CG  . TYR D  1 25  ? -8.703  -49.179 85.861   1.00 34.63  ? 25  TYR D CG  1 
ATOM   12309 C CD1 . TYR D  1 25  ? -10.081 -49.062 86.061   1.00 34.47  ? 25  TYR D CD1 1 
ATOM   12310 C CD2 . TYR D  1 25  ? -8.246  -49.626 84.614   1.00 30.27  ? 25  TYR D CD2 1 
ATOM   12311 C CE1 . TYR D  1 25  ? -10.975 -49.374 85.039   1.00 31.40  ? 25  TYR D CE1 1 
ATOM   12312 C CE2 . TYR D  1 25  ? -9.131  -49.942 83.600   1.00 29.71  ? 25  TYR D CE2 1 
ATOM   12313 C CZ  . TYR D  1 25  ? -10.490 -49.812 83.818   1.00 29.93  ? 25  TYR D CZ  1 
ATOM   12314 O OH  . TYR D  1 25  ? -11.367 -50.120 82.802   1.00 29.17  ? 25  TYR D OH  1 
ATOM   12315 N N   . LEU D  1 26  ? -5.681  -50.930 88.928   1.00 26.25  ? 26  LEU D N   1 
ATOM   12316 C CA  . LEU D  1 26  ? -4.539  -51.025 89.827   1.00 32.37  ? 26  LEU D CA  1 
ATOM   12317 C C   . LEU D  1 26  ? -3.256  -50.476 89.221   1.00 33.63  ? 26  LEU D C   1 
ATOM   12318 O O   . LEU D  1 26  ? -2.302  -50.214 89.959   1.00 37.00  ? 26  LEU D O   1 
ATOM   12319 C CB  . LEU D  1 26  ? -4.340  -52.474 90.271   1.00 34.69  ? 26  LEU D CB  1 
ATOM   12320 C CG  . LEU D  1 26  ? -5.584  -53.087 90.924   1.00 34.62  ? 26  LEU D CG  1 
ATOM   12321 C CD1 . LEU D  1 26  ? -5.273  -54.444 91.512   1.00 34.58  ? 26  LEU D CD1 1 
ATOM   12322 C CD2 . LEU D  1 26  ? -6.177  -52.165 91.994   1.00 38.17  ? 26  LEU D CD2 1 
ATOM   12323 N N   . LEU D  1 27  ? -3.211  -50.298 87.908   1.00 33.10  ? 27  LEU D N   1 
ATOM   12324 C CA  . LEU D  1 27  ? -2.143  -49.605 87.208   1.00 31.37  ? 27  LEU D CA  1 
ATOM   12325 C C   . LEU D  1 27  ? -2.762  -48.568 86.282   1.00 32.91  ? 27  LEU D C   1 
ATOM   12326 O O   . LEU D  1 27  ? -3.895  -48.738 85.828   1.00 33.61  ? 27  LEU D O   1 
ATOM   12327 C CB  . LEU D  1 27  ? -1.290  -50.577 86.393   1.00 31.84  ? 27  LEU D CB  1 
ATOM   12328 C CG  . LEU D  1 27  ? -0.434  -51.506 87.249   1.00 35.41  ? 27  LEU D CG  1 
ATOM   12329 C CD1 . LEU D  1 27  ? 0.198   -52.605 86.387   1.00 33.10  ? 27  LEU D CD1 1 
ATOM   12330 C CD2 . LEU D  1 27  ? 0.620   -50.698 87.985   1.00 34.87  ? 27  LEU D CD2 1 
ATOM   12331 N N   . PRO D  1 28  ? -2.059  -47.468 86.016   1.00 29.68  ? 28  PRO D N   1 
ATOM   12332 C CA  . PRO D  1 28  ? -2.623  -46.388 85.188   1.00 27.97  ? 28  PRO D CA  1 
ATOM   12333 C C   . PRO D  1 28  ? -2.244  -46.465 83.709   1.00 26.49  ? 28  PRO D C   1 
ATOM   12334 O O   . PRO D  1 28  ? -2.476  -45.491 82.995   1.00 27.30  ? 28  PRO D O   1 
ATOM   12335 C CB  . PRO D  1 28  ? -2.009  -45.138 85.831   1.00 23.56  ? 28  PRO D CB  1 
ATOM   12336 C CG  . PRO D  1 28  ? -0.648  -45.590 86.281   1.00 27.47  ? 28  PRO D CG  1 
ATOM   12337 C CD  . PRO D  1 28  ? -0.795  -47.065 86.658   1.00 29.88  ? 28  PRO D CD  1 
ATOM   12338 N N   . TRP D  1 29  ? -1.703  -47.591 83.250   1.00 26.53  ? 29  TRP D N   1 
ATOM   12339 C CA  . TRP D  1 29  ? -1.100  -47.651 81.926   1.00 28.07  ? 29  TRP D CA  1 
ATOM   12340 C C   . TRP D  1 29  ? -2.115  -47.429 80.814   1.00 22.89  ? 29  TRP D C   1 
ATOM   12341 O O   . TRP D  1 29  ? -1.777  -46.826 79.795   1.00 28.42  ? 29  TRP D O   1 
ATOM   12342 C CB  . TRP D  1 29  ? -0.375  -48.989 81.765   1.00 27.15  ? 29  TRP D CB  1 
ATOM   12343 C CG  . TRP D  1 29  ? 0.796   -49.162 82.738   1.00 30.25  ? 29  TRP D CG  1 
ATOM   12344 C CD1 . TRP D  1 29  ? 1.031   -50.238 83.558   1.00 31.58  ? 29  TRP D CD1 1 
ATOM   12345 C CD2 . TRP D  1 29  ? 1.884   -48.245 82.964   1.00 33.27  ? 29  TRP D CD2 1 
ATOM   12346 N NE1 . TRP D  1 29  ? 2.187   -50.043 84.278   1.00 36.11  ? 29  TRP D NE1 1 
ATOM   12347 C CE2 . TRP D  1 29  ? 2.734   -48.834 83.929   1.00 37.27  ? 29  TRP D CE2 1 
ATOM   12348 C CE3 . TRP D  1 29  ? 2.235   -46.993 82.429   1.00 33.28  ? 29  TRP D CE3 1 
ATOM   12349 C CZ2 . TRP D  1 29  ? 3.901   -48.209 84.382   1.00 36.35  ? 29  TRP D CZ2 1 
ATOM   12350 C CZ3 . TRP D  1 29  ? 3.391   -46.373 82.879   1.00 33.02  ? 29  TRP D CZ3 1 
ATOM   12351 C CH2 . TRP D  1 29  ? 4.212   -46.986 83.844   1.00 35.99  ? 29  TRP D CH2 1 
ATOM   12352 N N   . THR D  1 30  ? -3.357  -47.903 80.972   1.00 23.70  ? 30  THR D N   1 
ATOM   12353 C CA  . THR D  1 30  ? -4.353  -47.588 79.951   1.00 28.10  ? 30  THR D CA  1 
ATOM   12354 C C   . THR D  1 30  ? -4.586  -46.082 79.873   1.00 29.90  ? 30  THR D C   1 
ATOM   12355 O O   . THR D  1 30  ? -4.696  -45.518 78.774   1.00 28.58  ? 30  THR D O   1 
ATOM   12356 C CB  . THR D  1 30  ? -5.672  -48.311 80.210   1.00 26.85  ? 30  THR D CB  1 
ATOM   12357 O OG1 . THR D  1 30  ? -5.474  -49.726 80.148   1.00 26.28  ? 30  THR D OG1 1 
ATOM   12358 C CG2 . THR D  1 30  ? -6.708  -47.930 79.146   1.00 23.49  ? 30  THR D CG2 1 
ATOM   12359 N N   . PHE D  1 31  ? -4.664  -45.409 81.027   1.00 26.70  ? 31  PHE D N   1 
ATOM   12360 C CA  . PHE D  1 31  ? -4.866  -43.958 81.011   1.00 26.39  ? 31  PHE D CA  1 
ATOM   12361 C C   . PHE D  1 31  ? -3.705  -43.248 80.321   1.00 30.17  ? 31  PHE D C   1 
ATOM   12362 O O   . PHE D  1 31  ? -3.909  -42.379 79.462   1.00 33.32  ? 31  PHE D O   1 
ATOM   12363 C CB  . PHE D  1 31  ? -5.029  -43.421 82.436   1.00 25.48  ? 31  PHE D CB  1 
ATOM   12364 C CG  . PHE D  1 31  ? -5.096  -41.900 82.525   1.00 23.95  ? 31  PHE D CG  1 
ATOM   12365 C CD1 . PHE D  1 31  ? -6.300  -41.228 82.351   1.00 25.20  ? 31  PHE D CD1 1 
ATOM   12366 C CD2 . PHE D  1 31  ? -3.963  -41.152 82.833   1.00 22.54  ? 31  PHE D CD2 1 
ATOM   12367 C CE1 . PHE D  1 31  ? -6.375  -39.820 82.464   1.00 26.31  ? 31  PHE D CE1 1 
ATOM   12368 C CE2 . PHE D  1 31  ? -4.034  -39.753 82.947   1.00 23.04  ? 31  PHE D CE2 1 
ATOM   12369 C CZ  . PHE D  1 31  ? -5.240  -39.095 82.757   1.00 23.42  ? 31  PHE D CZ  1 
ATOM   12370 N N   . PHE D  1 32  ? -2.475  -43.590 80.709   1.00 27.65  ? 32  PHE D N   1 
ATOM   12371 C CA  . PHE D  1 32  ? -1.325  -42.825 80.254   1.00 25.12  ? 32  PHE D CA  1 
ATOM   12372 C C   . PHE D  1 32  ? -1.092  -43.020 78.759   1.00 24.60  ? 32  PHE D C   1 
ATOM   12373 O O   . PHE D  1 32  ? -0.847  -42.049 78.036   1.00 27.94  ? 32  PHE D O   1 
ATOM   12374 C CB  . PHE D  1 32  ? -0.093  -43.210 81.082   1.00 26.17  ? 32  PHE D CB  1 
ATOM   12375 C CG  . PHE D  1 32  ? 0.026   -42.446 82.394   1.00 29.94  ? 32  PHE D CG  1 
ATOM   12376 C CD1 . PHE D  1 32  ? 0.000   -41.059 82.410   1.00 33.30  ? 32  PHE D CD1 1 
ATOM   12377 C CD2 . PHE D  1 32  ? 0.171   -43.121 83.605   1.00 29.55  ? 32  PHE D CD2 1 
ATOM   12378 C CE1 . PHE D  1 32  ? 0.114   -40.352 83.614   1.00 35.63  ? 32  PHE D CE1 1 
ATOM   12379 C CE2 . PHE D  1 32  ? 0.289   -42.430 84.801   1.00 33.40  ? 32  PHE D CE2 1 
ATOM   12380 C CZ  . PHE D  1 32  ? 0.264   -41.042 84.806   1.00 33.60  ? 32  PHE D CZ  1 
ATOM   12381 N N   . HIS D  1 33  ? -1.178  -44.259 78.268   1.00 27.02  ? 33  HIS D N   1 
ATOM   12382 C CA  . HIS D  1 33  ? -1.034  -44.477 76.835   1.00 24.90  ? 33  HIS D CA  1 
ATOM   12383 C C   . HIS D  1 33  ? -2.245  -43.960 76.064   1.00 27.81  ? 33  HIS D C   1 
ATOM   12384 O O   . HIS D  1 33  ? -2.127  -43.647 74.868   1.00 21.07  ? 33  HIS D O   1 
ATOM   12385 C CB  . HIS D  1 33  ? -0.782  -45.970 76.535   1.00 17.98  ? 33  HIS D CB  1 
ATOM   12386 C CG  . HIS D  1 33  ? 0.597   -46.427 76.912   1.00 22.42  ? 33  HIS D CG  1 
ATOM   12387 N ND1 . HIS D  1 33  ? 1.730   -45.992 76.259   1.00 26.99  ? 33  HIS D ND1 1 
ATOM   12388 C CD2 . HIS D  1 33  ? 1.028   -47.261 77.891   1.00 26.71  ? 33  HIS D CD2 1 
ATOM   12389 C CE1 . HIS D  1 33  ? 2.799   -46.539 76.812   1.00 23.44  ? 33  HIS D CE1 1 
ATOM   12390 N NE2 . HIS D  1 33  ? 2.400   -47.313 77.806   1.00 27.38  ? 33  HIS D NE2 1 
ATOM   12391 N N   . ALA D  1 34  ? -3.407  -43.849 76.712   1.00 21.99  ? 34  ALA D N   1 
ATOM   12392 C CA  . ALA D  1 34  ? -4.535  -43.219 76.036   1.00 25.25  ? 34  ALA D CA  1 
ATOM   12393 C C   . ALA D  1 34  ? -4.248  -41.746 75.770   1.00 26.86  ? 34  ALA D C   1 
ATOM   12394 O O   . ALA D  1 34  ? -4.380  -41.271 74.635   1.00 23.15  ? 34  ALA D O   1 
ATOM   12395 C CB  . ALA D  1 34  ? -5.820  -43.384 76.854   1.00 26.71  ? 34  ALA D CB  1 
ATOM   12396 N N   . VAL D  1 35  ? -3.800  -41.011 76.792   1.00 22.41  ? 35  VAL D N   1 
ATOM   12397 C CA  . VAL D  1 35  ? -3.562  -39.587 76.564   1.00 24.19  ? 35  VAL D CA  1 
ATOM   12398 C C   . VAL D  1 35  ? -2.324  -39.364 75.691   1.00 25.32  ? 35  VAL D C   1 
ATOM   12399 O O   . VAL D  1 35  ? -2.227  -38.332 75.004   1.00 26.42  ? 35  VAL D O   1 
ATOM   12400 C CB  . VAL D  1 35  ? -3.467  -38.817 77.902   1.00 25.36  ? 35  VAL D CB  1 
ATOM   12401 C CG1 . VAL D  1 35  ? -4.581  -39.269 78.848   1.00 21.39  ? 35  VAL D CG1 1 
ATOM   12402 C CG2 . VAL D  1 35  ? -2.084  -38.968 78.542   1.00 29.56  ? 35  VAL D CG2 1 
ATOM   12403 N N   . LYS D  1 36  ? -1.406  -40.332 75.641   1.00 26.20  ? 36  LYS D N   1 
ATOM   12404 C CA  . LYS D  1 36  ? -0.152  -40.153 74.910   1.00 25.79  ? 36  LYS D CA  1 
ATOM   12405 C C   . LYS D  1 36  ? -0.193  -40.719 73.497   1.00 25.37  ? 36  LYS D C   1 
ATOM   12406 O O   . LYS D  1 36  ? 0.329   -40.095 72.565   1.00 28.88  ? 36  LYS D O   1 
ATOM   12407 C CB  . LYS D  1 36  ? 1.015   -40.787 75.684   1.00 21.36  ? 36  LYS D CB  1 
ATOM   12408 C CG  . LYS D  1 36  ? 2.366   -40.279 75.215   1.00 23.74  ? 36  LYS D CG  1 
ATOM   12409 C CD  . LYS D  1 36  ? 3.511   -40.787 76.062   1.00 19.88  ? 36  LYS D CD  1 
ATOM   12410 C CE  . LYS D  1 36  ? 3.840   -42.254 75.766   1.00 21.56  ? 36  LYS D CE  1 
ATOM   12411 N NZ  . LYS D  1 36  ? 4.210   -42.477 74.321   1.00 24.48  ? 36  LYS D NZ  1 
ATOM   12412 N N   . ASP D  1 37  ? -0.821  -41.846 73.310   1.00 23.87  ? 37  ASP D N   1 
ATOM   12413 C CA  . ASP D  1 37  ? -0.637  -42.576 72.065   1.00 29.25  ? 37  ASP D CA  1 
ATOM   12414 C C   . ASP D  1 37  ? -1.942  -42.946 71.378   1.00 29.79  ? 37  ASP D C   1 
ATOM   12415 O O   . ASP D  1 37  ? -2.047  -42.766 70.167   1.00 24.74  ? 37  ASP D O   1 
ATOM   12416 C CB  . ASP D  1 37  ? 0.190   -43.844 72.321   1.00 22.20  ? 37  ASP D CB  1 
ATOM   12417 C CG  . ASP D  1 37  ? 1.435   -43.556 73.116   1.00 25.72  ? 37  ASP D CG  1 
ATOM   12418 O OD1 . ASP D  1 37  ? 2.346   -42.894 72.562   1.00 24.13  ? 37  ASP D OD1 1 
ATOM   12419 O OD2 . ASP D  1 37  ? 1.483   -43.936 74.312   1.00 25.21  ? 37  ASP D OD2 1 
ATOM   12420 N N   . TYR D  1 38  ? -2.942  -43.440 72.115   1.00 20.45  ? 38  TYR D N   1 
ATOM   12421 C CA  . TYR D  1 38  ? -4.071  -44.085 71.444   1.00 26.09  ? 38  TYR D CA  1 
ATOM   12422 C C   . TYR D  1 38  ? -4.920  -43.112 70.630   1.00 24.01  ? 38  TYR D C   1 
ATOM   12423 O O   . TYR D  1 38  ? -5.465  -43.499 69.591   1.00 22.38  ? 38  TYR D O   1 
ATOM   12424 C CB  . TYR D  1 38  ? -4.927  -44.826 72.467   1.00 24.83  ? 38  TYR D CB  1 
ATOM   12425 C CG  . TYR D  1 38  ? -4.204  -46.022 73.077   1.00 25.72  ? 38  TYR D CG  1 
ATOM   12426 C CD1 . TYR D  1 38  ? -3.253  -46.728 72.354   1.00 24.79  ? 38  TYR D CD1 1 
ATOM   12427 C CD2 . TYR D  1 38  ? -4.445  -46.405 74.391   1.00 24.52  ? 38  TYR D CD2 1 
ATOM   12428 C CE1 . TYR D  1 38  ? -2.582  -47.816 72.915   1.00 31.98  ? 38  TYR D CE1 1 
ATOM   12429 C CE2 . TYR D  1 38  ? -3.781  -47.484 74.963   1.00 28.07  ? 38  TYR D CE2 1 
ATOM   12430 C CZ  . TYR D  1 38  ? -2.855  -48.180 74.240   1.00 30.37  ? 38  TYR D CZ  1 
ATOM   12431 O OH  . TYR D  1 38  ? -2.213  -49.249 74.832   1.00 29.84  ? 38  TYR D OH  1 
ATOM   12432 N N   . TYR D  1 39  ? -5.070  -41.868 71.072   1.00 21.79  ? 39  TYR D N   1 
ATOM   12433 C CA  . TYR D  1 39  ? -5.726  -40.872 70.232   1.00 20.50  ? 39  TYR D CA  1 
ATOM   12434 C C   . TYR D  1 39  ? -4.758  -40.343 69.190   1.00 24.76  ? 39  TYR D C   1 
ATOM   12435 O O   . TYR D  1 39  ? -5.121  -40.107 68.017   1.00 21.79  ? 39  TYR D O   1 
ATOM   12436 C CB  . TYR D  1 39  ? -6.246  -39.709 71.101   1.00 20.65  ? 39  TYR D CB  1 
ATOM   12437 C CG  . TYR D  1 39  ? -6.787  -38.558 70.286   1.00 20.90  ? 39  TYR D CG  1 
ATOM   12438 C CD1 . TYR D  1 39  ? -8.106  -38.556 69.861   1.00 23.78  ? 39  TYR D CD1 1 
ATOM   12439 C CD2 . TYR D  1 39  ? -5.974  -37.487 69.905   1.00 18.39  ? 39  TYR D CD2 1 
ATOM   12440 C CE1 . TYR D  1 39  ? -8.607  -37.521 69.104   1.00 27.46  ? 39  TYR D CE1 1 
ATOM   12441 C CE2 . TYR D  1 39  ? -6.461  -36.460 69.137   1.00 19.76  ? 39  TYR D CE2 1 
ATOM   12442 C CZ  . TYR D  1 39  ? -7.786  -36.478 68.736   1.00 27.91  ? 39  TYR D CZ  1 
ATOM   12443 O OH  . TYR D  1 39  ? -8.326  -35.457 67.976   1.00 31.49  ? 39  TYR D OH  1 
ATOM   12444 N N   . ASP D  1 40  ? -3.507  -40.185 69.595   1.00 20.44  ? 40  ASP D N   1 
ATOM   12445 C CA  . ASP D  1 40  ? -2.642  -39.392 68.759   1.00 22.46  ? 40  ASP D CA  1 
ATOM   12446 C C   . ASP D  1 40  ? -1.992  -40.134 67.635   1.00 24.73  ? 40  ASP D C   1 
ATOM   12447 O O   . ASP D  1 40  ? -1.626  -39.492 66.644   1.00 29.26  ? 40  ASP D O   1 
ATOM   12448 C CB  . ASP D  1 40  ? -1.607  -38.777 69.631   1.00 19.84  ? 40  ASP D CB  1 
ATOM   12449 C CG  . ASP D  1 40  ? -2.108  -37.512 70.179   1.00 30.86  ? 40  ASP D CG  1 
ATOM   12450 O OD1 . ASP D  1 40  ? -2.175  -36.549 69.392   1.00 29.72  ? 40  ASP D OD1 1 
ATOM   12451 O OD2 . ASP D  1 40  ? -2.443  -37.492 71.385   1.00 27.82  ? 40  ASP D OD2 1 
ATOM   12452 N N   . MET D  1 41  ? -1.781  -41.439 67.784   1.00 18.91  ? 41  MET D N   1 
ATOM   12453 C CA  . MET D  1 41  ? -1.261  -42.196 66.658   1.00 21.72  ? 41  MET D CA  1 
ATOM   12454 C C   . MET D  1 41  ? -2.200  -42.116 65.465   1.00 21.37  ? 41  MET D C   1 
ATOM   12455 O O   . MET D  1 41  ? -1.735  -41.765 64.368   1.00 19.23  ? 41  MET D O   1 
ATOM   12456 C CB  . MET D  1 41  ? -0.960  -43.640 67.097   1.00 19.24  ? 41  MET D CB  1 
ATOM   12457 C CG  . MET D  1 41  ? 0.331   -43.761 67.914   1.00 23.85  ? 41  MET D CG  1 
ATOM   12458 S SD  . MET D  1 41  ? 1.826   -43.433 66.905   1.00 29.19  ? 41  MET D SD  1 
ATOM   12459 C CE  . MET D  1 41  ? 2.048   -45.072 66.215   1.00 18.26  ? 41  MET D CE  1 
ATOM   12460 N N   . PRO D  1 42  ? -3.504  -42.392 65.584   1.00 17.84  ? 42  PRO D N   1 
ATOM   12461 C CA  . PRO D  1 42  ? -4.390  -42.157 64.429   1.00 16.35  ? 42  PRO D CA  1 
ATOM   12462 C C   . PRO D  1 42  ? -4.586  -40.687 64.074   1.00 26.23  ? 42  PRO D C   1 
ATOM   12463 O O   . PRO D  1 42  ? -4.909  -40.392 62.913   1.00 22.02  ? 42  PRO D O   1 
ATOM   12464 C CB  . PRO D  1 42  ? -5.714  -42.816 64.854   1.00 20.69  ? 42  PRO D CB  1 
ATOM   12465 C CG  . PRO D  1 42  ? -5.662  -42.854 66.349   1.00 16.56  ? 42  PRO D CG  1 
ATOM   12466 C CD  . PRO D  1 42  ? -4.220  -43.063 66.691   1.00 20.79  ? 42  PRO D CD  1 
ATOM   12467 N N   . ALA D  1 43  ? -4.383  -39.755 65.006   1.00 21.41  ? 43  ALA D N   1 
ATOM   12468 C CA  . ALA D  1 43  ? -4.582  -38.348 64.666   1.00 24.07  ? 43  ALA D CA  1 
ATOM   12469 C C   . ALA D  1 43  ? -3.513  -37.820 63.716   1.00 23.58  ? 43  ALA D C   1 
ATOM   12470 O O   . ALA D  1 43  ? -3.701  -36.751 63.119   1.00 21.59  ? 43  ALA D O   1 
ATOM   12471 C CB  . ALA D  1 43  ? -4.614  -37.479 65.927   1.00 20.82  ? 43  ALA D CB  1 
ATOM   12472 N N   . TYR D  1 44  ? -2.392  -38.524 63.581   1.00 19.98  ? 44  TYR D N   1 
ATOM   12473 C CA  . TYR D  1 44  ? -1.413  -38.146 62.564   1.00 24.02  ? 44  TYR D CA  1 
ATOM   12474 C C   . TYR D  1 44  ? -2.032  -38.138 61.175   1.00 26.61  ? 44  TYR D C   1 
ATOM   12475 O O   . TYR D  1 44  ? -1.564  -37.414 60.292   1.00 29.10  ? 44  TYR D O   1 
ATOM   12476 C CB  . TYR D  1 44  ? -0.252  -39.126 62.551   1.00 19.12  ? 44  TYR D CB  1 
ATOM   12477 C CG  . TYR D  1 44  ? 0.838   -38.889 63.559   1.00 21.64  ? 44  TYR D CG  1 
ATOM   12478 C CD1 . TYR D  1 44  ? 1.928   -38.086 63.252   1.00 22.61  ? 44  TYR D CD1 1 
ATOM   12479 C CD2 . TYR D  1 44  ? 0.787   -39.491 64.803   1.00 18.92  ? 44  TYR D CD2 1 
ATOM   12480 C CE1 . TYR D  1 44  ? 2.951   -37.892 64.163   1.00 20.99  ? 44  TYR D CE1 1 
ATOM   12481 C CE2 . TYR D  1 44  ? 1.805   -39.293 65.739   1.00 20.64  ? 44  TYR D CE2 1 
ATOM   12482 C CZ  . TYR D  1 44  ? 2.883   -38.494 65.397   1.00 19.81  ? 44  TYR D CZ  1 
ATOM   12483 O OH  . TYR D  1 44  ? 3.907   -38.287 66.279   1.00 20.07  ? 44  TYR D OH  1 
ATOM   12484 N N   . LEU D  1 45  ? -3.053  -38.967 60.958   1.00 24.36  ? 45  LEU D N   1 
ATOM   12485 C CA  . LEU D  1 45  ? -3.699  -39.067 59.651   1.00 24.15  ? 45  LEU D CA  1 
ATOM   12486 C C   . LEU D  1 45  ? -4.465  -37.803 59.287   1.00 22.94  ? 45  LEU D C   1 
ATOM   12487 O O   . LEU D  1 45  ? -4.759  -37.593 58.102   1.00 26.55  ? 45  LEU D O   1 
ATOM   12488 C CB  . LEU D  1 45  ? -4.634  -40.285 59.625   1.00 24.24  ? 45  LEU D CB  1 
ATOM   12489 C CG  . LEU D  1 45  ? -3.916  -41.645 59.587   1.00 23.49  ? 45  LEU D CG  1 
ATOM   12490 C CD1 . LEU D  1 45  ? -4.832  -42.804 59.957   1.00 20.98  ? 45  LEU D CD1 1 
ATOM   12491 C CD2 . LEU D  1 45  ? -3.305  -41.847 58.204   1.00 20.92  ? 45  LEU D CD2 1 
ATOM   12492 N N   . LYS D  1 46  ? -4.793  -36.965 60.275   1.00 19.95  ? 46  LYS D N   1 
ATOM   12493 C CA  . LYS D  1 46  ? -5.406  -35.664 60.006   1.00 29.52  ? 46  LYS D CA  1 
ATOM   12494 C C   . LYS D  1 46  ? -4.451  -34.729 59.276   1.00 29.45  ? 46  LYS D C   1 
ATOM   12495 O O   . LYS D  1 46  ? -4.899  -33.804 58.587   1.00 23.67  ? 46  LYS D O   1 
ATOM   12496 C CB  . LYS D  1 46  ? -5.851  -34.999 61.314   1.00 30.27  ? 46  LYS D CB  1 
ATOM   12497 C CG  . LYS D  1 46  ? -6.977  -35.722 62.055   1.00 32.91  ? 46  LYS D CG  1 
ATOM   12498 C CD  . LYS D  1 46  ? -8.308  -35.023 61.825   1.00 42.35  ? 46  LYS D CD  1 
ATOM   12499 C CE  . LYS D  1 46  ? -9.362  -35.486 62.823   1.00 45.66  ? 46  LYS D CE  1 
ATOM   12500 N NZ  . LYS D  1 46  ? -8.915  -35.218 64.207   1.00 49.62  ? 46  LYS D NZ  1 
ATOM   12501 N N   . ASP D  1 47  ? -3.139  -34.926 59.441   1.00 26.38  ? 47  ASP D N   1 
ATOM   12502 C CA  . ASP D  1 47  ? -2.156  -33.972 58.948   1.00 29.95  ? 47  ASP D CA  1 
ATOM   12503 C C   . ASP D  1 47  ? -1.299  -34.512 57.818   1.00 29.67  ? 47  ASP D C   1 
ATOM   12504 O O   . ASP D  1 47  ? -0.553  -33.739 57.220   1.00 32.89  ? 47  ASP D O   1 
ATOM   12505 C CB  . ASP D  1 47  ? -1.217  -33.514 60.077   1.00 28.84  ? 47  ASP D CB  1 
ATOM   12506 C CG  . ASP D  1 47  ? -1.942  -32.816 61.196   1.00 39.57  ? 47  ASP D CG  1 
ATOM   12507 O OD1 . ASP D  1 47  ? -2.810  -31.966 60.910   1.00 42.47  ? 47  ASP D OD1 1 
ATOM   12508 O OD2 . ASP D  1 47  ? -1.628  -33.105 62.369   1.00 42.03  ? 47  ASP D OD2 1 
ATOM   12509 N N   . PHE D  1 48  ? -1.350  -35.812 57.544   1.00 30.06  ? 48  PHE D N   1 
ATOM   12510 C CA  . PHE D  1 48  ? -0.427  -36.459 56.627   1.00 25.33  ? 48  PHE D CA  1 
ATOM   12511 C C   . PHE D  1 48  ? -1.220  -37.322 55.664   1.00 25.07  ? 48  PHE D C   1 
ATOM   12512 O O   . PHE D  1 48  ? -2.100  -38.076 56.087   1.00 29.16  ? 48  PHE D O   1 
ATOM   12513 C CB  . PHE D  1 48  ? 0.620   -37.279 57.391   1.00 24.77  ? 48  PHE D CB  1 
ATOM   12514 C CG  . PHE D  1 48  ? 1.580   -36.429 58.161   1.00 25.87  ? 48  PHE D CG  1 
ATOM   12515 C CD1 . PHE D  1 48  ? 2.571   -35.726 57.508   1.00 26.84  ? 48  PHE D CD1 1 
ATOM   12516 C CD2 . PHE D  1 48  ? 1.477   -36.311 59.541   1.00 29.66  ? 48  PHE D CD2 1 
ATOM   12517 C CE1 . PHE D  1 48  ? 3.451   -34.913 58.215   1.00 29.41  ? 48  PHE D CE1 1 
ATOM   12518 C CE2 . PHE D  1 48  ? 2.356   -35.507 60.255   1.00 29.54  ? 48  PHE D CE2 1 
ATOM   12519 C CZ  . PHE D  1 48  ? 3.342   -34.804 59.589   1.00 25.10  ? 48  PHE D CZ  1 
ATOM   12520 N N   . GLU D  1 49  ? -0.929  -37.186 54.370   1.00 26.30  ? 49  GLU D N   1 
ATOM   12521 C CA  . GLU D  1 49  ? -1.699  -37.858 53.319   1.00 28.98  ? 49  GLU D CA  1 
ATOM   12522 C C   . GLU D  1 49  ? -1.106  -39.241 53.047   1.00 25.78  ? 49  GLU D C   1 
ATOM   12523 O O   . GLU D  1 49  ? -0.527  -39.514 51.997   1.00 28.31  ? 49  GLU D O   1 
ATOM   12524 C CB  . GLU D  1 49  ? -1.719  -37.008 52.051   1.00 36.14  ? 49  GLU D CB  1 
ATOM   12525 C CG  . GLU D  1 49  ? -3.098  -36.856 51.426   1.00 49.64  ? 49  GLU D CG  1 
ATOM   12526 C CD  . GLU D  1 49  ? -4.092  -36.258 52.399   1.00 60.20  ? 49  GLU D CD  1 
ATOM   12527 O OE1 . GLU D  1 49  ? -3.810  -35.167 52.934   1.00 62.86  ? 49  GLU D OE1 1 
ATOM   12528 O OE2 . GLU D  1 49  ? -5.138  -36.896 52.653   1.00 66.59  ? 49  GLU D OE2 1 
ATOM   12529 N N   . ILE D  1 50  ? -1.229  -40.114 54.039   1.00 22.48  ? 50  ILE D N   1 
ATOM   12530 C CA  . ILE D  1 50  ? -0.815  -41.508 53.924   1.00 22.06  ? 50  ILE D CA  1 
ATOM   12531 C C   . ILE D  1 50  ? -1.896  -42.386 54.538   1.00 25.83  ? 50  ILE D C   1 
ATOM   12532 O O   . ILE D  1 50  ? -2.867  -41.901 55.124   1.00 22.51  ? 50  ILE D O   1 
ATOM   12533 C CB  . ILE D  1 50  ? 0.548   -41.786 54.601   1.00 20.96  ? 50  ILE D CB  1 
ATOM   12534 C CG1 . ILE D  1 50  ? 0.482   -41.465 56.099   1.00 21.57  ? 50  ILE D CG1 1 
ATOM   12535 C CG2 . ILE D  1 50  ? 1.683   -41.021 53.894   1.00 20.23  ? 50  ILE D CG2 1 
ATOM   12536 C CD1 . ILE D  1 50  ? 1.684   -41.960 56.852   1.00 20.15  ? 50  ILE D CD1 1 
ATOM   12537 N N   . LYS D  1 51  ? -1.720  -43.701 54.385   1.00 23.98  ? 51  LYS D N   1 
ATOM   12538 C CA  . LYS D  1 51  ? -2.573  -44.689 55.032   1.00 18.33  ? 51  LYS D CA  1 
ATOM   12539 C C   . LYS D  1 51  ? -1.852  -45.267 56.246   1.00 25.49  ? 51  LYS D C   1 
ATOM   12540 O O   . LYS D  1 51  ? -0.672  -45.634 56.156   1.00 18.76  ? 51  LYS D O   1 
ATOM   12541 C CB  . LYS D  1 51  ? -2.948  -45.821 54.080   1.00 25.63  ? 51  LYS D CB  1 
ATOM   12542 C CG  . LYS D  1 51  ? -3.548  -45.337 52.770   1.00 27.75  ? 51  LYS D CG  1 
ATOM   12543 C CD  . LYS D  1 51  ? -4.927  -44.705 53.022   1.00 26.40  ? 51  LYS D CD  1 
ATOM   12544 C CE  . LYS D  1 51  ? -5.533  -44.118 51.721   1.00 31.17  ? 51  LYS D CE  1 
ATOM   12545 N NZ  . LYS D  1 51  ? -4.772  -44.409 50.463   1.00 28.94  ? 51  LYS D NZ  1 
ATOM   12546 N N   . LEU D  1 52  ? -2.567  -45.371 57.369   1.00 21.07  ? 52  LEU D N   1 
ATOM   12547 C CA  . LEU D  1 52  ? -2.023  -46.063 58.532   1.00 18.78  ? 52  LEU D CA  1 
ATOM   12548 C C   . LEU D  1 52  ? -3.114  -46.940 59.126   1.00 25.29  ? 52  LEU D C   1 
ATOM   12549 O O   . LEU D  1 52  ? -4.253  -46.505 59.257   1.00 25.61  ? 52  LEU D O   1 
ATOM   12550 C CB  . LEU D  1 52  ? -1.513  -45.087 59.595   1.00 21.88  ? 52  LEU D CB  1 
ATOM   12551 C CG  . LEU D  1 52  ? -0.368  -44.128 59.289   1.00 26.18  ? 52  LEU D CG  1 
ATOM   12552 C CD1 . LEU D  1 52  ? -0.240  -43.133 60.431   1.00 24.35  ? 52  LEU D CD1 1 
ATOM   12553 C CD2 . LEU D  1 52  ? 0.952   -44.846 59.028   1.00 22.74  ? 52  LEU D CD2 1 
ATOM   12554 N N   . ASN D  1 53  ? -2.764  -48.174 59.472   1.00 26.38  ? 53  ASN D N   1 
ATOM   12555 C CA  . ASN D  1 53  ? -3.703  -49.130 60.026   1.00 16.67  ? 53  ASN D CA  1 
ATOM   12556 C C   . ASN D  1 53  ? -3.416  -49.339 61.503   1.00 23.05  ? 53  ASN D C   1 
ATOM   12557 O O   . ASN D  1 53  ? -2.310  -49.081 61.978   1.00 24.77  ? 53  ASN D O   1 
ATOM   12558 C CB  . ASN D  1 53  ? -3.612  -50.451 59.279   1.00 17.40  ? 53  ASN D CB  1 
ATOM   12559 C CG  . ASN D  1 53  ? -3.630  -50.234 57.810   1.00 24.28  ? 53  ASN D CG  1 
ATOM   12560 O OD1 . ASN D  1 53  ? -4.674  -49.894 57.258   1.00 23.61  ? 53  ASN D OD1 1 
ATOM   12561 N ND2 . ASN D  1 53  ? -2.465  -50.341 57.168   1.00 23.44  ? 53  ASN D ND2 1 
ATOM   12562 N N   . PHE D  1 54  ? -4.444  -49.802 62.213   1.00 22.73  ? 54  PHE D N   1 
ATOM   12563 C CA  . PHE D  1 54  ? -4.426  -49.943 63.667   1.00 18.11  ? 54  PHE D CA  1 
ATOM   12564 C C   . PHE D  1 54  ? -5.127  -51.222 64.080   1.00 19.02  ? 54  PHE D C   1 
ATOM   12565 O O   . PHE D  1 54  ? -6.156  -51.592 63.511   1.00 24.17  ? 54  PHE D O   1 
ATOM   12566 C CB  . PHE D  1 54  ? -5.103  -48.739 64.346   1.00 17.70  ? 54  PHE D CB  1 
ATOM   12567 C CG  . PHE D  1 54  ? -4.426  -47.445 64.041   1.00 24.96  ? 54  PHE D CG  1 
ATOM   12568 C CD1 . PHE D  1 54  ? -4.792  -46.706 62.921   1.00 30.32  ? 54  PHE D CD1 1 
ATOM   12569 C CD2 . PHE D  1 54  ? -3.362  -47.002 64.816   1.00 25.96  ? 54  PHE D CD2 1 
ATOM   12570 C CE1 . PHE D  1 54  ? -4.127  -45.513 62.598   1.00 31.79  ? 54  PHE D CE1 1 
ATOM   12571 C CE2 . PHE D  1 54  ? -2.700  -45.818 64.505   1.00 27.94  ? 54  PHE D CE2 1 
ATOM   12572 C CZ  . PHE D  1 54  ? -3.081  -45.074 63.390   1.00 27.93  ? 54  PHE D CZ  1 
ATOM   12573 N N   . ASN D  1 55  ? -4.583  -51.884 65.100   1.00 19.09  ? 55  ASN D N   1 
ATOM   12574 C CA  . ASN D  1 55  ? -5.288  -52.934 65.806   1.00 22.33  ? 55  ASN D CA  1 
ATOM   12575 C C   . ASN D  1 55  ? -5.680  -52.420 67.188   1.00 22.53  ? 55  ASN D C   1 
ATOM   12576 O O   . ASN D  1 55  ? -4.843  -51.843 67.889   1.00 23.74  ? 55  ASN D O   1 
ATOM   12577 C CB  . ASN D  1 55  ? -4.420  -54.186 65.948   1.00 25.19  ? 55  ASN D CB  1 
ATOM   12578 C CG  . ASN D  1 55  ? -5.186  -55.331 66.556   1.00 22.70  ? 55  ASN D CG  1 
ATOM   12579 O OD1 . ASN D  1 55  ? -6.145  -55.813 65.955   1.00 23.29  ? 55  ASN D OD1 1 
ATOM   12580 N ND2 . ASN D  1 55  ? -4.791  -55.761 67.743   1.00 21.09  ? 55  ASN D ND2 1 
ATOM   12581 N N   . LEU D  1 56  ? -6.930  -52.649 67.582   1.00 22.10  ? 56  LEU D N   1 
ATOM   12582 C CA  . LEU D  1 56  ? -7.403  -52.351 68.938   1.00 22.52  ? 56  LEU D CA  1 
ATOM   12583 C C   . LEU D  1 56  ? -7.971  -53.618 69.553   1.00 20.96  ? 56  LEU D C   1 
ATOM   12584 O O   . LEU D  1 56  ? -8.997  -54.107 69.084   1.00 23.74  ? 56  LEU D O   1 
ATOM   12585 C CB  . LEU D  1 56  ? -8.502  -51.283 68.919   1.00 26.80  ? 56  LEU D CB  1 
ATOM   12586 C CG  . LEU D  1 56  ? -8.235  -49.892 68.354   1.00 27.19  ? 56  LEU D CG  1 
ATOM   12587 C CD1 . LEU D  1 56  ? -9.530  -49.089 68.383   1.00 30.03  ? 56  LEU D CD1 1 
ATOM   12588 C CD2 . LEU D  1 56  ? -7.165  -49.214 69.160   1.00 28.43  ? 56  LEU D CD2 1 
ATOM   12589 N N   . THR D  1 57  ? -7.355  -54.119 70.642   1.00 26.73  ? 57  THR D N   1 
ATOM   12590 C CA  . THR D  1 57  ? -7.945  -55.277 71.310   1.00 27.25  ? 57  THR D CA  1 
ATOM   12591 C C   . THR D  1 57  ? -9.237  -54.866 72.026   1.00 30.03  ? 57  THR D C   1 
ATOM   12592 O O   . THR D  1 57  ? -9.351  -53.737 72.524   1.00 18.22  ? 57  THR D O   1 
ATOM   12593 C CB  . THR D  1 57  ? -6.973  -55.927 72.305   1.00 25.62  ? 57  THR D CB  1 
ATOM   12594 O OG1 . THR D  1 57  ? -6.756  -55.048 73.413   1.00 21.48  ? 57  THR D OG1 1 
ATOM   12595 C CG2 . THR D  1 57  ? -5.648  -56.219 71.628   1.00 24.16  ? 57  THR D CG2 1 
ATOM   12596 N N   . PRO D  1 58  ? -10.246 -55.735 72.049   1.00 18.70  ? 58  PRO D N   1 
ATOM   12597 C CA  . PRO D  1 58  ? -11.503 -55.364 72.710   1.00 19.93  ? 58  PRO D CA  1 
ATOM   12598 C C   . PRO D  1 58  ? -11.328 -55.034 74.188   1.00 23.47  ? 58  PRO D C   1 
ATOM   12599 O O   . PRO D  1 58  ? -12.047 -54.169 74.705   1.00 23.39  ? 58  PRO D O   1 
ATOM   12600 C CB  . PRO D  1 58  ? -12.381 -56.608 72.511   1.00 20.24  ? 58  PRO D CB  1 
ATOM   12601 C CG  . PRO D  1 58  ? -11.819 -57.287 71.295   1.00 21.28  ? 58  PRO D CG  1 
ATOM   12602 C CD  . PRO D  1 58  ? -10.328 -57.047 71.395   1.00 22.91  ? 58  PRO D CD  1 
ATOM   12603 N N   . VAL D  1 59  ? -10.402 -55.705 74.884   1.00 24.02  ? 59  VAL D N   1 
ATOM   12604 C CA  . VAL D  1 59  ? -10.212 -55.395 76.305   1.00 24.01  ? 59  VAL D CA  1 
ATOM   12605 C C   . VAL D  1 59  ? -9.665  -53.979 76.462   1.00 25.05  ? 59  VAL D C   1 
ATOM   12606 O O   . VAL D  1 59  ? -9.978  -53.291 77.435   1.00 20.71  ? 59  VAL D O   1 
ATOM   12607 C CB  . VAL D  1 59  ? -9.301  -56.437 76.985   1.00 19.75  ? 59  VAL D CB  1 
ATOM   12608 C CG1 . VAL D  1 59  ? -7.898  -56.403 76.391   1.00 26.31  ? 59  VAL D CG1 1 
ATOM   12609 C CG2 . VAL D  1 59  ? -9.284  -56.218 78.539   1.00 20.38  ? 59  VAL D CG2 1 
ATOM   12610 N N   . LEU D  1 60  ? -8.859  -53.500 75.501   1.00 18.83  ? 60  LEU D N   1 
ATOM   12611 C CA  . LEU D  1 60  ? -8.454  -52.107 75.582   1.00 18.66  ? 60  LEU D CA  1 
ATOM   12612 C C   . LEU D  1 60  ? -9.642  -51.189 75.335   1.00 19.08  ? 60  LEU D C   1 
ATOM   12613 O O   . LEU D  1 60  ? -9.797  -50.173 76.020   1.00 22.73  ? 60  LEU D O   1 
ATOM   12614 C CB  . LEU D  1 60  ? -7.333  -51.806 74.590   1.00 18.87  ? 60  LEU D CB  1 
ATOM   12615 C CG  . LEU D  1 60  ? -6.943  -50.345 74.428   1.00 21.63  ? 60  LEU D CG  1 
ATOM   12616 C CD1 . LEU D  1 60  ? -6.350  -49.782 75.721   1.00 26.66  ? 60  LEU D CD1 1 
ATOM   12617 C CD2 . LEU D  1 60  ? -5.963  -50.186 73.253   1.00 19.71  ? 60  LEU D CD2 1 
ATOM   12618 N N   . ILE D  1 61  ? -10.480 -51.521 74.349   1.00 26.03  ? 61  ILE D N   1 
ATOM   12619 C CA  . ILE D  1 61  ? -11.653 -50.704 74.060   1.00 21.16  ? 61  ILE D CA  1 
ATOM   12620 C C   . ILE D  1 61  ? -12.514 -50.557 75.314   1.00 20.57  ? 61  ILE D C   1 
ATOM   12621 O O   . ILE D  1 61  ? -12.960 -49.452 75.649   1.00 22.93  ? 61  ILE D O   1 
ATOM   12622 C CB  . ILE D  1 61  ? -12.439 -51.316 72.886   1.00 23.39  ? 61  ILE D CB  1 
ATOM   12623 C CG1 . ILE D  1 61  ? -11.580 -51.277 71.608   1.00 24.47  ? 61  ILE D CG1 1 
ATOM   12624 C CG2 . ILE D  1 61  ? -13.743 -50.574 72.658   1.00 26.53  ? 61  ILE D CG2 1 
ATOM   12625 C CD1 . ILE D  1 61  ? -12.217 -51.960 70.430   1.00 21.48  ? 61  ILE D CD1 1 
ATOM   12626 N N   . ASP D  1 62  ? -12.730 -51.661 76.031   1.00 22.49  ? 62  ASP D N   1 
ATOM   12627 C CA  . ASP D  1 62  ? -13.578 -51.638 77.226   1.00 29.25  ? 62  ASP D CA  1 
ATOM   12628 C C   . ASP D  1 62  ? -13.062 -50.626 78.230   1.00 28.24  ? 62  ASP D C   1 
ATOM   12629 O O   . ASP D  1 62  ? -13.833 -49.848 78.799   1.00 33.32  ? 62  ASP D O   1 
ATOM   12630 C CB  . ASP D  1 62  ? -13.627 -53.018 77.874   1.00 28.19  ? 62  ASP D CB  1 
ATOM   12631 C CG  . ASP D  1 62  ? -14.596 -53.951 77.192   1.00 32.91  ? 62  ASP D CG  1 
ATOM   12632 O OD1 . ASP D  1 62  ? -15.605 -53.469 76.639   1.00 36.32  ? 62  ASP D OD1 1 
ATOM   12633 O OD2 . ASP D  1 62  ? -14.344 -55.175 77.218   1.00 35.99  ? 62  ASP D OD2 1 
ATOM   12634 N N   . GLN D  1 63  ? -11.743 -50.623 78.444   1.00 30.94  ? 63  GLN D N   1 
ATOM   12635 C CA  . GLN D  1 63  ? -11.132 -49.718 79.409   1.00 28.92  ? 63  GLN D CA  1 
ATOM   12636 C C   . GLN D  1 63  ? -11.219 -48.269 78.947   1.00 26.20  ? 63  GLN D C   1 
ATOM   12637 O O   . GLN D  1 63  ? -11.553 -47.384 79.738   1.00 27.91  ? 63  GLN D O   1 
ATOM   12638 C CB  . GLN D  1 63  ? -9.677  -50.111 79.637   1.00 27.50  ? 63  GLN D CB  1 
ATOM   12639 C CG  . GLN D  1 63  ? -9.491  -51.498 80.233   1.00 30.22  ? 63  GLN D CG  1 
ATOM   12640 C CD  . GLN D  1 63  ? -8.038  -51.814 80.412   1.00 30.12  ? 63  GLN D CD  1 
ATOM   12641 O OE1 . GLN D  1 63  ? -7.388  -51.275 81.310   1.00 29.15  ? 63  GLN D OE1 1 
ATOM   12642 N NE2 . GLN D  1 63  ? -7.500  -52.675 79.541   1.00 24.19  ? 63  GLN D NE2 1 
ATOM   12643 N N   . ILE D  1 64  ? -10.892 -48.001 77.680   1.00 27.56  ? 64  ILE D N   1 
ATOM   12644 C CA  . ILE D  1 64  ? -11.054 -46.643 77.160   1.00 25.48  ? 64  ILE D CA  1 
ATOM   12645 C C   . ILE D  1 64  ? -12.487 -46.165 77.354   1.00 21.77  ? 64  ILE D C   1 
ATOM   12646 O O   . ILE D  1 64  ? -12.727 -45.022 77.763   1.00 29.11  ? 64  ILE D O   1 
ATOM   12647 C CB  . ILE D  1 64  ? -10.646 -46.578 75.676   1.00 26.46  ? 64  ILE D CB  1 
ATOM   12648 C CG1 . ILE D  1 64  ? -9.123  -46.718 75.519   1.00 21.94  ? 64  ILE D CG1 1 
ATOM   12649 C CG2 . ILE D  1 64  ? -11.212 -45.297 75.068   1.00 23.85  ? 64  ILE D CG2 1 
ATOM   12650 C CD1 . ILE D  1 64  ? -8.658  -46.873 74.043   1.00 24.07  ? 64  ILE D CD1 1 
ATOM   12651 N N   . GLN D  1 65  ? -13.463 -47.019 77.040   1.00 22.11  ? 65  GLN D N   1 
ATOM   12652 C CA  . GLN D  1 65  ? -14.863 -46.651 77.245   1.00 23.17  ? 65  GLN D CA  1 
ATOM   12653 C C   . GLN D  1 65  ? -15.133 -46.278 78.695   1.00 28.92  ? 65  GLN D C   1 
ATOM   12654 O O   . GLN D  1 65  ? -15.878 -45.324 78.972   1.00 24.98  ? 65  GLN D O   1 
ATOM   12655 C CB  . GLN D  1 65  ? -15.776 -47.798 76.821   1.00 25.53  ? 65  GLN D CB  1 
ATOM   12656 C CG  . GLN D  1 65  ? -15.975 -47.869 75.306   1.00 32.03  ? 65  GLN D CG  1 
ATOM   12657 C CD  . GLN D  1 65  ? -16.901 -48.984 74.895   1.00 32.81  ? 65  GLN D CD  1 
ATOM   12658 O OE1 . GLN D  1 65  ? -16.663 -50.146 75.222   1.00 29.61  ? 65  GLN D OE1 1 
ATOM   12659 N NE2 . GLN D  1 65  ? -17.980 -48.637 74.181   1.00 30.60  ? 65  GLN D NE2 1 
ATOM   12660 N N   . GLU D  1 66  ? -14.530 -47.013 79.633   1.00 26.54  ? 66  GLU D N   1 
ATOM   12661 C CA  . GLU D  1 66  ? -14.791 -46.764 81.055   1.00 30.68  ? 66  GLU D CA  1 
ATOM   12662 C C   . GLU D  1 66  ? -14.184 -45.438 81.495   1.00 31.35  ? 66  GLU D C   1 
ATOM   12663 O O   . GLU D  1 66  ? -14.853 -44.628 82.146   1.00 27.32  ? 66  GLU D O   1 
ATOM   12664 C CB  . GLU D  1 66  ? -14.252 -47.914 81.908   1.00 30.61  ? 66  GLU D CB  1 
ATOM   12665 C CG  . GLU D  1 66  ? -14.551 -47.772 83.395   1.00 38.69  ? 66  GLU D CG  1 
ATOM   12666 C CD  . GLU D  1 66  ? -14.358 -49.069 84.175   1.00 43.76  ? 66  GLU D CD  1 
ATOM   12667 O OE1 . GLU D  1 66  ? -14.756 -49.109 85.363   1.00 44.63  ? 66  GLU D OE1 1 
ATOM   12668 O OE2 . GLU D  1 66  ? -13.814 -50.047 83.612   1.00 39.01  ? 66  GLU D OE2 1 
ATOM   12669 N N   . TYR D  1 67  ? -12.914 -45.197 81.130   1.00 29.02  ? 67  TYR D N   1 
ATOM   12670 C CA  . TYR D  1 67  ? -12.287 -43.907 81.412   1.00 33.90  ? 67  TYR D CA  1 
ATOM   12671 C C   . TYR D  1 67  ? -13.071 -42.757 80.783   1.00 34.96  ? 67  TYR D C   1 
ATOM   12672 O O   . TYR D  1 67  ? -13.305 -41.729 81.430   1.00 36.88  ? 67  TYR D O   1 
ATOM   12673 C CB  . TYR D  1 67  ? -10.840 -43.901 80.905   1.00 33.50  ? 67  TYR D CB  1 
ATOM   12674 C CG  . TYR D  1 67  ? -9.832  -44.550 81.839   1.00 31.72  ? 67  TYR D CG  1 
ATOM   12675 C CD1 . TYR D  1 67  ? -9.323  -43.858 82.943   1.00 25.06  ? 67  TYR D CD1 1 
ATOM   12676 C CD2 . TYR D  1 67  ? -9.392  -45.861 81.621   1.00 27.54  ? 67  TYR D CD2 1 
ATOM   12677 C CE1 . TYR D  1 67  ? -8.395  -44.438 83.781   1.00 25.48  ? 67  TYR D CE1 1 
ATOM   12678 C CE2 . TYR D  1 67  ? -8.469  -46.466 82.488   1.00 22.85  ? 67  TYR D CE2 1 
ATOM   12679 C CZ  . TYR D  1 67  ? -7.969  -45.746 83.548   1.00 26.69  ? 67  TYR D CZ  1 
ATOM   12680 O OH  . TYR D  1 67  ? -7.052  -46.338 84.387   1.00 26.91  ? 67  TYR D OH  1 
ATOM   12681 N N   . ALA D  1 68  ? -13.485 -42.912 79.519   1.00 32.36  ? 68  ALA D N   1 
ATOM   12682 C CA  . ALA D  1 68  ? -14.202 -41.840 78.833   1.00 30.82  ? 68  ALA D CA  1 
ATOM   12683 C C   . ALA D  1 68  ? -15.538 -41.535 79.492   1.00 31.40  ? 68  ALA D C   1 
ATOM   12684 O O   . ALA D  1 68  ? -15.996 -40.386 79.464   1.00 37.84  ? 68  ALA D O   1 
ATOM   12685 C CB  . ALA D  1 68  ? -14.414 -42.195 77.353   1.00 31.07  ? 68  ALA D CB  1 
ATOM   12686 N N   . GLN D  1 69  ? -16.182 -42.531 80.085   1.00 36.93  ? 69  GLN D N   1 
ATOM   12687 C CA  . GLN D  1 69  ? -17.408 -42.263 80.832   1.00 41.75  ? 69  GLN D CA  1 
ATOM   12688 C C   . GLN D  1 69  ? -17.145 -41.732 82.235   1.00 41.27  ? 69  GLN D C   1 
ATOM   12689 O O   . GLN D  1 69  ? -18.106 -41.417 82.943   1.00 41.63  ? 69  GLN D O   1 
ATOM   12690 C CB  . GLN D  1 69  ? -18.274 -43.523 80.918   1.00 46.73  ? 69  GLN D CB  1 
ATOM   12691 C CG  . GLN D  1 69  ? -18.844 -43.970 79.572   1.00 54.69  ? 69  GLN D CG  1 
ATOM   12692 C CD  . GLN D  1 69  ? -19.106 -45.462 79.528   1.00 63.56  ? 69  GLN D CD  1 
ATOM   12693 O OE1 . GLN D  1 69  ? -19.190 -46.061 78.452   1.00 66.35  ? 69  GLN D OE1 1 
ATOM   12694 N NE2 . GLN D  1 69  ? -19.241 -46.073 80.702   1.00 67.17  ? 69  GLN D NE2 1 
ATOM   12695 N N   . GLY D  1 70  ? -15.883 -41.610 82.647   1.00 41.03  ? 70  GLY D N   1 
ATOM   12696 C CA  . GLY D  1 70  ? -15.564 -41.166 83.990   1.00 41.81  ? 70  GLY D CA  1 
ATOM   12697 C C   . GLY D  1 70  ? -15.842 -42.176 85.075   1.00 44.47  ? 70  GLY D C   1 
ATOM   12698 O O   . GLY D  1 70  ? -15.838 -41.815 86.255   1.00 47.51  ? 70  GLY D O   1 
ATOM   12699 N N   . LYS D  1 71  ? -16.080 -43.435 84.712   1.00 44.90  ? 71  LYS D N   1 
ATOM   12700 C CA  . LYS D  1 71  ? -16.405 -44.494 85.656   1.00 47.27  ? 71  LYS D CA  1 
ATOM   12701 C C   . LYS D  1 71  ? -15.183 -45.303 86.081   1.00 48.34  ? 71  LYS D C   1 
ATOM   12702 O O   . LYS D  1 71  ? -15.337 -46.310 86.776   1.00 52.08  ? 71  LYS D O   1 
ATOM   12703 C CB  . LYS D  1 71  ? -17.460 -45.424 85.048   1.00 44.27  ? 71  LYS D CB  1 
ATOM   12704 N N   . ALA D  1 72  ? -13.981 -44.892 85.678   1.00 41.56  ? 72  ALA D N   1 
ATOM   12705 C CA  . ALA D  1 72  ? -12.756 -45.626 85.979   1.00 36.95  ? 72  ALA D CA  1 
ATOM   12706 C C   . ALA D  1 72  ? -12.132 -45.071 87.251   1.00 40.74  ? 72  ALA D C   1 
ATOM   12707 O O   . ALA D  1 72  ? -11.793 -43.884 87.313   1.00 40.71  ? 72  ALA D O   1 
ATOM   12708 C CB  . ALA D  1 72  ? -11.760 -45.530 84.826   1.00 35.67  ? 72  ALA D CB  1 
ATOM   12709 N N   . LYS D  1 73  ? -11.987 -45.920 88.267   1.00 41.57  ? 73  LYS D N   1 
ATOM   12710 C CA  . LYS D  1 73  ? -11.356 -45.525 89.526   1.00 40.32  ? 73  LYS D CA  1 
ATOM   12711 C C   . LYS D  1 73  ? -9.915  -46.013 89.485   1.00 40.33  ? 73  LYS D C   1 
ATOM   12712 O O   . LYS D  1 73  ? -9.637  -47.193 89.689   1.00 44.09  ? 73  LYS D O   1 
ATOM   12713 C CB  . LYS D  1 73  ? -12.129 -46.068 90.722   1.00 46.92  ? 73  LYS D CB  1 
ATOM   12714 C CG  . LYS D  1 73  ? -13.606 -46.263 90.439   1.00 52.42  ? 73  LYS D CG  1 
ATOM   12715 C CD  . LYS D  1 73  ? -14.311 -46.939 91.596   1.00 62.56  ? 73  LYS D CD  1 
ATOM   12716 C CE  . LYS D  1 73  ? -15.463 -47.785 91.094   1.00 66.74  ? 73  LYS D CE  1 
ATOM   12717 N NZ  . LYS D  1 73  ? -15.896 -48.741 92.146   1.00 69.13  ? 73  LYS D NZ  1 
ATOM   12718 N N   . ASP D  1 74  ? -9.004  -45.098 89.207   1.00 38.00  ? 74  ASP D N   1 
ATOM   12719 C CA  . ASP D  1 74  ? -7.612  -45.414 88.920   1.00 33.70  ? 74  ASP D CA  1 
ATOM   12720 C C   . ASP D  1 74  ? -6.800  -45.013 90.138   1.00 32.28  ? 74  ASP D C   1 
ATOM   12721 O O   . ASP D  1 74  ? -6.667  -43.822 90.426   1.00 33.75  ? 74  ASP D O   1 
ATOM   12722 C CB  . ASP D  1 74  ? -7.175  -44.654 87.668   1.00 29.78  ? 74  ASP D CB  1 
ATOM   12723 C CG  . ASP D  1 74  ? -5.739  -44.945 87.239   1.00 35.76  ? 74  ASP D CG  1 
ATOM   12724 O OD1 . ASP D  1 74  ? -4.828  -45.057 88.093   1.00 36.24  ? 74  ASP D OD1 1 
ATOM   12725 O OD2 . ASP D  1 74  ? -5.523  -45.024 86.006   1.00 36.31  ? 74  ASP D OD2 1 
ATOM   12726 N N   . VAL D  1 75  ? -6.269  -45.999 90.866   1.00 36.92  ? 75  VAL D N   1 
ATOM   12727 C CA  . VAL D  1 75  ? -5.711  -45.686 92.180   1.00 40.97  ? 75  VAL D CA  1 
ATOM   12728 C C   . VAL D  1 75  ? -4.540  -44.721 92.040   1.00 40.08  ? 75  VAL D C   1 
ATOM   12729 O O   . VAL D  1 75  ? -4.400  -43.771 92.821   1.00 38.34  ? 75  VAL D O   1 
ATOM   12730 C CB  . VAL D  1 75  ? -5.327  -46.974 92.947   1.00 41.15  ? 75  VAL D CB  1 
ATOM   12731 C CG1 . VAL D  1 75  ? -6.506  -47.942 93.022   1.00 42.60  ? 75  VAL D CG1 1 
ATOM   12732 C CG2 . VAL D  1 75  ? -4.130  -47.661 92.351   1.00 37.98  ? 75  VAL D CG2 1 
ATOM   12733 N N   . PHE D  1 76  ? -3.706  -44.916 91.021   1.00 39.47  ? 76  PHE D N   1 
ATOM   12734 C CA  . PHE D  1 76  ? -2.562  -44.028 90.865   1.00 41.17  ? 76  PHE D CA  1 
ATOM   12735 C C   . PHE D  1 76  ? -3.008  -42.637 90.438   1.00 37.45  ? 76  PHE D C   1 
ATOM   12736 O O   . PHE D  1 76  ? -2.443  -41.631 90.881   1.00 37.26  ? 76  PHE D O   1 
ATOM   12737 C CB  . PHE D  1 76  ? -1.574  -44.615 89.866   1.00 46.25  ? 76  PHE D CB  1 
ATOM   12738 C CG  . PHE D  1 76  ? -0.302  -43.844 89.770   1.00 54.14  ? 76  PHE D CG  1 
ATOM   12739 C CD1 . PHE D  1 76  ? 0.714   -44.052 90.690   1.00 58.19  ? 76  PHE D CD1 1 
ATOM   12740 C CD2 . PHE D  1 76  ? -0.128  -42.893 88.774   1.00 56.71  ? 76  PHE D CD2 1 
ATOM   12741 C CE1 . PHE D  1 76  ? 1.884   -43.328 90.615   1.00 61.00  ? 76  PHE D CE1 1 
ATOM   12742 C CE2 . PHE D  1 76  ? 1.042   -42.164 88.688   1.00 58.82  ? 76  PHE D CE2 1 
ATOM   12743 C CZ  . PHE D  1 76  ? 2.049   -42.379 89.610   1.00 61.41  ? 76  PHE D CZ  1 
ATOM   12744 N N   . LEU D  1 77  ? -4.048  -42.564 89.608   1.00 36.14  ? 77  LEU D N   1 
ATOM   12745 C CA  . LEU D  1 77  ? -4.527  -41.279 89.123   1.00 37.25  ? 77  LEU D CA  1 
ATOM   12746 C C   . LEU D  1 77  ? -5.181  -40.450 90.224   1.00 40.76  ? 77  LEU D C   1 
ATOM   12747 O O   . LEU D  1 77  ? -5.118  -39.214 90.176   1.00 45.82  ? 77  LEU D O   1 
ATOM   12748 C CB  . LEU D  1 77  ? -5.490  -41.509 87.957   1.00 38.44  ? 77  LEU D CB  1 
ATOM   12749 C CG  . LEU D  1 77  ? -5.766  -40.326 87.047   1.00 39.38  ? 77  LEU D CG  1 
ATOM   12750 C CD1 . LEU D  1 77  ? -4.476  -39.584 86.689   1.00 36.75  ? 77  LEU D CD1 1 
ATOM   12751 C CD2 . LEU D  1 77  ? -6.486  -40.830 85.808   1.00 40.68  ? 77  LEU D CD2 1 
ATOM   12752 N N   . GLU D  1 78  ? -5.810  -41.095 91.220   1.00 41.49  ? 78  GLU D N   1 
ATOM   12753 C CA  . GLU D  1 78  ? -6.334  -40.342 92.360   1.00 47.11  ? 78  GLU D CA  1 
ATOM   12754 C C   . GLU D  1 78  ? -5.192  -39.795 93.215   1.00 43.40  ? 78  GLU D C   1 
ATOM   12755 O O   . GLU D  1 78  ? -5.274  -38.685 93.748   1.00 44.46  ? 78  GLU D O   1 
ATOM   12756 C CB  . GLU D  1 78  ? -7.267  -41.209 93.214   1.00 56.80  ? 78  GLU D CB  1 
ATOM   12757 C CG  . GLU D  1 78  ? -8.738  -41.088 92.803   1.00 65.71  ? 78  GLU D CG  1 
ATOM   12758 C CD  . GLU D  1 78  ? -9.459  -42.429 92.733   1.00 74.93  ? 78  GLU D CD  1 
ATOM   12759 O OE1 . GLU D  1 78  ? -8.897  -43.440 93.222   1.00 77.08  ? 78  GLU D OE1 1 
ATOM   12760 O OE2 . GLU D  1 78  ? -10.575 -42.481 92.164   1.00 77.30  ? 78  GLU D OE2 1 
ATOM   12761 N N   . ALA D  1 79  ? -4.110  -40.562 93.355   1.00 41.36  ? 79  ALA D N   1 
ATOM   12762 C CA  . ALA D  1 79  ? -2.910  -40.025 93.994   1.00 40.37  ? 79  ALA D CA  1 
ATOM   12763 C C   . ALA D  1 79  ? -2.385  -38.816 93.234   1.00 39.81  ? 79  ALA D C   1 
ATOM   12764 O O   . ALA D  1 79  ? -1.850  -37.883 93.843   1.00 42.49  ? 79  ALA D O   1 
ATOM   12765 C CB  . ALA D  1 79  ? -1.842  -41.116 94.099   1.00 36.95  ? 79  ALA D CB  1 
ATOM   12766 N N   . ILE D  1 80  ? -2.548  -38.803 91.908   1.00 40.95  ? 80  ILE D N   1 
ATOM   12767 C CA  . ILE D  1 80  ? -2.187  -37.624 91.131   1.00 38.05  ? 80  ILE D CA  1 
ATOM   12768 C C   . ILE D  1 80  ? -3.150  -36.483 91.410   1.00 36.13  ? 80  ILE D C   1 
ATOM   12769 O O   . ILE D  1 80  ? -2.731  -35.338 91.609   1.00 41.11  ? 80  ILE D O   1 
ATOM   12770 C CB  . ILE D  1 80  ? -2.155  -37.947 89.624   1.00 37.58  ? 80  ILE D CB  1 
ATOM   12771 C CG1 . ILE D  1 80  ? -1.017  -38.920 89.301   1.00 39.13  ? 80  ILE D CG1 1 
ATOM   12772 C CG2 . ILE D  1 80  ? -2.135  -36.624 88.796   1.00 31.65  ? 80  ILE D CG2 1 
ATOM   12773 C CD1 . ILE D  1 80  ? 0.342   -38.314 89.381   1.00 38.91  ? 80  ILE D CD1 1 
ATOM   12774 N N   . ARG D  1 81  ? -4.453  -36.773 91.417   1.00 35.20  ? 81  ARG D N   1 
ATOM   12775 C CA  . ARG D  1 81  ? -5.449  -35.703 91.447   1.00 42.90  ? 81  ARG D CA  1 
ATOM   12776 C C   . ARG D  1 81  ? -5.452  -34.965 92.780   1.00 47.52  ? 81  ARG D C   1 
ATOM   12777 O O   . ARG D  1 81  ? -5.651  -33.742 92.820   1.00 49.25  ? 81  ARG D O   1 
ATOM   12778 C CB  . ARG D  1 81  ? -6.834  -36.279 91.147   1.00 46.57  ? 81  ARG D CB  1 
ATOM   12779 C CG  . ARG D  1 81  ? -7.927  -35.232 90.983   1.00 53.26  ? 81  ARG D CG  1 
ATOM   12780 C CD  . ARG D  1 81  ? -9.274  -35.896 90.753   1.00 59.70  ? 81  ARG D CD  1 
ATOM   12781 N NE  . ARG D  1 81  ? -9.164  -37.083 89.901   1.00 63.40  ? 81  ARG D NE  1 
ATOM   12782 C CZ  . ARG D  1 81  ? -9.259  -37.087 88.571   1.00 66.08  ? 81  ARG D CZ  1 
ATOM   12783 N NH1 . ARG D  1 81  ? -9.468  -35.958 87.901   1.00 67.37  ? 81  ARG D NH1 1 
ATOM   12784 N NH2 . ARG D  1 81  ? -9.142  -38.234 87.903   1.00 63.38  ? 81  ARG D NH2 1 
ATOM   12785 N N   . LYS D  1 82  ? -5.221  -35.691 93.875   1.00 46.28  ? 82  LYS D N   1 
ATOM   12786 C CA  . LYS D  1 82  ? -5.374  -35.148 95.218   1.00 45.80  ? 82  LYS D CA  1 
ATOM   12787 C C   . LYS D  1 82  ? -4.471  -33.943 95.448   1.00 44.97  ? 82  LYS D C   1 
ATOM   12788 O O   . LYS D  1 82  ? -3.370  -33.839 94.897   1.00 41.63  ? 82  LYS D O   1 
ATOM   12789 C CB  . LYS D  1 82  ? -5.036  -36.212 96.257   1.00 46.49  ? 82  LYS D CB  1 
ATOM   12790 C CG  . LYS D  1 82  ? -6.042  -37.309 96.410   1.00 49.68  ? 82  LYS D CG  1 
ATOM   12791 C CD  . LYS D  1 82  ? -5.725  -38.089 97.672   1.00 48.02  ? 82  LYS D CD  1 
ATOM   12792 C CE  . LYS D  1 82  ? -6.492  -39.390 97.766   1.00 47.82  ? 82  LYS D CE  1 
ATOM   12793 N NZ  . LYS D  1 82  ? -6.250  -39.967 99.122   1.00 46.31  ? 82  LYS D NZ  1 
ATOM   12794 N N   . ASP D  1 83  ? -4.949  -33.031 96.280   1.00 43.27  ? 83  ASP D N   1 
ATOM   12795 C CA  . ASP D  1 83  ? -4.059  -32.060 96.884   1.00 45.95  ? 83  ASP D CA  1 
ATOM   12796 C C   . ASP D  1 83  ? -2.995  -32.810 97.682   1.00 45.49  ? 83  ASP D C   1 
ATOM   12797 O O   . ASP D  1 83  ? -3.331  -33.728 98.444   1.00 46.61  ? 83  ASP D O   1 
ATOM   12798 C CB  . ASP D  1 83  ? -4.843  -31.112 97.786   1.00 50.92  ? 83  ASP D CB  1 
ATOM   12799 C CG  . ASP D  1 83  ? -4.043  -29.898 98.199   1.00 55.27  ? 83  ASP D CG  1 
ATOM   12800 O OD1 . ASP D  1 83  ? -3.015  -30.055 98.892   1.00 56.08  ? 83  ASP D OD1 1 
ATOM   12801 O OD2 . ASP D  1 83  ? -4.451  -28.775 97.832   1.00 60.03  ? 83  ASP D OD2 1 
ATOM   12802 N N   . PRO D  1 84  ? -1.716  -32.469 97.527   1.00 44.97  ? 84  PRO D N   1 
ATOM   12803 C CA  . PRO D  1 84  ? -0.658  -33.222 98.225   1.00 46.65  ? 84  PRO D CA  1 
ATOM   12804 C C   . PRO D  1 84  ? -0.815  -33.285 99.746   1.00 52.27  ? 84  PRO D C   1 
ATOM   12805 O O   . PRO D  1 84  ? -0.313  -34.234 100.360  1.00 55.33  ? 84  PRO D O   1 
ATOM   12806 C CB  . PRO D  1 84  ? 0.617   -32.475 97.817   1.00 47.20  ? 84  PRO D CB  1 
ATOM   12807 C CG  . PRO D  1 84  ? 0.274   -31.914 96.432   1.00 41.04  ? 84  PRO D CG  1 
ATOM   12808 C CD  . PRO D  1 84  ? -1.179  -31.537 96.514   1.00 40.10  ? 84  PRO D CD  1 
ATOM   12809 N N   . ASP D  1 85  ? -1.502  -32.328 100.376  1.00 53.90  ? 85  ASP D N   1 
ATOM   12810 C CA  . ASP D  1 85  ? -1.720  -32.414 101.819  1.00 55.02  ? 85  ASP D CA  1 
ATOM   12811 C C   . ASP D  1 85  ? -2.629  -33.572 102.201  1.00 52.72  ? 85  ASP D C   1 
ATOM   12812 O O   . ASP D  1 85  ? -2.675  -33.946 103.382  1.00 51.04  ? 85  ASP D O   1 
ATOM   12813 C CB  . ASP D  1 85  ? -2.323  -31.114 102.353  1.00 56.05  ? 85  ASP D CB  1 
ATOM   12814 C CG  . ASP D  1 85  ? -1.352  -29.968 102.305  1.00 57.18  ? 85  ASP D CG  1 
ATOM   12815 O OD1 . ASP D  1 85  ? -0.133  -30.226 102.236  1.00 58.74  ? 85  ASP D OD1 1 
ATOM   12816 O OD2 . ASP D  1 85  ? -1.810  -28.809 102.330  1.00 59.59  ? 85  ASP D OD2 1 
ATOM   12817 N N   . ASP D  1 86  ? -3.373  -34.118 101.243  1.00 49.58  ? 86  ASP D N   1 
ATOM   12818 C CA  . ASP D  1 86  ? -4.256  -35.253 101.468  1.00 52.40  ? 86  ASP D CA  1 
ATOM   12819 C C   . ASP D  1 86  ? -3.610  -36.589 101.120  1.00 50.09  ? 86  ASP D C   1 
ATOM   12820 O O   . ASP D  1 86  ? -4.246  -37.632 101.300  1.00 49.52  ? 86  ASP D O   1 
ATOM   12821 C CB  . ASP D  1 86  ? -5.548  -35.088 100.656  1.00 55.00  ? 86  ASP D CB  1 
ATOM   12822 C CG  . ASP D  1 86  ? -6.215  -33.741 100.880  1.00 56.79  ? 86  ASP D CG  1 
ATOM   12823 O OD1 . ASP D  1 86  ? -6.039  -33.159 101.971  1.00 57.35  ? 86  ASP D OD1 1 
ATOM   12824 O OD2 . ASP D  1 86  ? -6.927  -33.270 99.963   1.00 57.48  ? 86  ASP D OD2 1 
ATOM   12825 N N   . LEU D  1 87  ? -2.371  -36.584 100.629  1.00 47.87  ? 87  LEU D N   1 
ATOM   12826 C CA  . LEU D  1 87  ? -1.705  -37.814 100.215  1.00 45.34  ? 87  LEU D CA  1 
ATOM   12827 C C   . LEU D  1 87  ? -1.236  -38.630 101.411  1.00 45.91  ? 87  LEU D C   1 
ATOM   12828 O O   . LEU D  1 87  ? -0.564  -38.108 102.304  1.00 45.49  ? 87  LEU D O   1 
ATOM   12829 C CB  . LEU D  1 87  ? -0.498  -37.500 99.345   1.00 43.98  ? 87  LEU D CB  1 
ATOM   12830 C CG  . LEU D  1 87  ? -0.786  -36.829 98.004   1.00 44.48  ? 87  LEU D CG  1 
ATOM   12831 C CD1 . LEU D  1 87  ? 0.522   -36.627 97.282   1.00 43.11  ? 87  LEU D CD1 1 
ATOM   12832 C CD2 . LEU D  1 87  ? -1.753  -37.672 97.182   1.00 44.06  ? 87  LEU D CD2 1 
ATOM   12833 N N   . GLU D  1 88  ? -1.530  -39.924 101.378  1.00 45.86  ? 88  GLU D N   1 
ATOM   12834 C CA  . GLU D  1 88  ? -0.920  -40.866 102.299  1.00 51.67  ? 88  GLU D CA  1 
ATOM   12835 C C   . GLU D  1 88  ? 0.553   -41.076 101.963  1.00 54.24  ? 88  GLU D C   1 
ATOM   12836 O O   . GLU D  1 88  ? 1.026   -40.784 100.853  1.00 50.47  ? 88  GLU D O   1 
ATOM   12837 C CB  . GLU D  1 88  ? -1.646  -42.206 102.245  1.00 49.56  ? 88  GLU D CB  1 
ATOM   12838 C CG  . GLU D  1 88  ? -3.143  -42.078 102.388  1.00 51.61  ? 88  GLU D CG  1 
ATOM   12839 C CD  . GLU D  1 88  ? -3.892  -43.293 101.876  1.00 59.06  ? 88  GLU D CD  1 
ATOM   12840 O OE1 . GLU D  1 88  ? -5.100  -43.394 102.169  1.00 62.85  ? 88  GLU D OE1 1 
ATOM   12841 O OE2 . GLU D  1 88  ? -3.285  -44.143 101.185  1.00 57.86  ? 88  GLU D OE2 1 
ATOM   12842 N N   . LYS D  1 89  ? 1.279   -41.601 102.953  1.00 47.52  ? 89  LYS D N   1 
ATOM   12843 C CA  . LYS D  1 89  ? 2.685   -41.932 102.759  1.00 49.81  ? 89  LYS D CA  1 
ATOM   12844 C C   . LYS D  1 89  ? 2.862   -42.925 101.622  1.00 49.93  ? 89  LYS D C   1 
ATOM   12845 O O   . LYS D  1 89  ? 3.754   -42.768 100.782  1.00 52.89  ? 89  LYS D O   1 
ATOM   12846 C CB  . LYS D  1 89  ? 3.280   -42.501 104.051  1.00 52.60  ? 89  LYS D CB  1 
ATOM   12847 C CG  . LYS D  1 89  ? 3.694   -41.473 105.070  1.00 56.69  ? 89  LYS D CG  1 
ATOM   12848 C CD  . LYS D  1 89  ? 4.502   -42.120 106.192  1.00 59.60  ? 89  LYS D CD  1 
ATOM   12849 C CE  . LYS D  1 89  ? 4.957   -41.098 107.223  1.00 62.39  ? 89  LYS D CE  1 
ATOM   12850 N NZ  . LYS D  1 89  ? 5.593   -41.755 108.404  1.00 67.45  ? 89  LYS D NZ  1 
ATOM   12851 N N   . GLU D  1 90  ? 2.015   -43.954 101.578  1.00 48.37  ? 90  GLU D N   1 
ATOM   12852 C CA  . GLU D  1 90  ? 2.122   -44.944 100.517  1.00 50.01  ? 90  GLU D CA  1 
ATOM   12853 C C   . GLU D  1 90  ? 1.806   -44.338 99.157   1.00 46.71  ? 90  GLU D C   1 
ATOM   12854 O O   . GLU D  1 90  ? 2.362   -44.783 98.151   1.00 44.42  ? 90  GLU D O   1 
ATOM   12855 C CB  . GLU D  1 90  ? 1.203   -46.133 100.790  1.00 60.03  ? 90  GLU D CB  1 
ATOM   12856 C CG  . GLU D  1 90  ? -0.072  -45.773 101.501  1.00 73.95  ? 90  GLU D CG  1 
ATOM   12857 C CD  . GLU D  1 90  ? 0.085   -45.743 103.018  1.00 87.87  ? 90  GLU D CD  1 
ATOM   12858 O OE1 . GLU D  1 90  ? 0.919   -44.942 103.519  1.00 91.23  ? 90  GLU D OE1 1 
ATOM   12859 O OE2 . GLU D  1 90  ? -0.601  -46.515 103.692  1.00 92.42  ? 90  GLU D OE2 1 
ATOM   12860 N N   . GLU D  1 91  ? 0.932   -43.326 99.106   1.00 45.61  ? 91  GLU D N   1 
ATOM   12861 C CA  . GLU D  1 91  ? 0.640   -42.671 97.833   1.00 40.92  ? 91  GLU D CA  1 
ATOM   12862 C C   . GLU D  1 91  ? 1.827   -41.845 97.359   1.00 41.01  ? 91  GLU D C   1 
ATOM   12863 O O   . GLU D  1 91  ? 2.184   -41.869 96.173   1.00 38.65  ? 91  GLU D O   1 
ATOM   12864 C CB  . GLU D  1 91  ? -0.602  -41.795 97.960   1.00 40.68  ? 91  GLU D CB  1 
ATOM   12865 C CG  . GLU D  1 91  ? -1.904  -42.553 97.988   1.00 41.17  ? 91  GLU D CG  1 
ATOM   12866 C CD  . GLU D  1 91  ? -3.083  -41.618 98.064   1.00 51.12  ? 91  GLU D CD  1 
ATOM   12867 O OE1 . GLU D  1 91  ? -3.004  -40.633 98.837   1.00 55.87  ? 91  GLU D OE1 1 
ATOM   12868 O OE2 . GLU D  1 91  ? -4.079  -41.851 97.344   1.00 50.64  ? 91  GLU D OE2 1 
ATOM   12869 N N   . VAL D  1 92  ? 2.430   -41.081 98.271   1.00 43.01  ? 92  VAL D N   1 
ATOM   12870 C CA  . VAL D  1 92  ? 3.685   -40.395 97.976   1.00 45.66  ? 92  VAL D CA  1 
ATOM   12871 C C   . VAL D  1 92  ? 4.746   -41.402 97.553   1.00 45.69  ? 92  VAL D C   1 
ATOM   12872 O O   . VAL D  1 92  ? 5.486   -41.180 96.583   1.00 48.13  ? 92  VAL D O   1 
ATOM   12873 C CB  . VAL D  1 92  ? 4.143   -39.576 99.201   1.00 48.72  ? 92  VAL D CB  1 
ATOM   12874 C CG1 . VAL D  1 92  ? 5.507   -38.957 98.953   1.00 46.55  ? 92  VAL D CG1 1 
ATOM   12875 C CG2 . VAL D  1 92  ? 3.111   -38.511 99.558   1.00 48.12  ? 92  VAL D CG2 1 
ATOM   12876 N N   . GLU D  1 93  ? 4.827   -42.528 98.272   1.00 44.86  ? 93  GLU D N   1 
ATOM   12877 C CA  . GLU D  1 93  ? 5.791   -43.573 97.935   1.00 46.43  ? 93  GLU D CA  1 
ATOM   12878 C C   . GLU D  1 93  ? 5.616   -44.036 96.490   1.00 46.84  ? 93  GLU D C   1 
ATOM   12879 O O   . GLU D  1 93  ? 6.568   -44.008 95.705   1.00 45.11  ? 93  GLU D O   1 
ATOM   12880 C CB  . GLU D  1 93  ? 5.655   -44.754 98.900   1.00 49.94  ? 93  GLU D CB  1 
ATOM   12881 C CG  . GLU D  1 93  ? 6.810   -44.890 99.899   1.00 57.96  ? 93  GLU D CG  1 
ATOM   12882 C CD  . GLU D  1 93  ? 6.414   -45.650 101.159  1.00 66.08  ? 93  GLU D CD  1 
ATOM   12883 O OE1 . GLU D  1 93  ? 6.852   -45.264 102.272  1.00 68.50  ? 93  GLU D OE1 1 
ATOM   12884 O OE2 . GLU D  1 93  ? 5.654   -46.637 101.031  1.00 67.07  ? 93  GLU D OE2 1 
ATOM   12885 N N   . LYS D  1 94  ? 4.397   -44.446 96.116   1.00 48.68  ? 94  LYS D N   1 
ATOM   12886 C CA  . LYS D  1 94  ? 4.159   -44.939 94.758   1.00 50.28  ? 94  LYS D CA  1 
ATOM   12887 C C   . LYS D  1 94  ? 4.327   -43.845 93.709   1.00 44.81  ? 94  LYS D C   1 
ATOM   12888 O O   . LYS D  1 94  ? 4.731   -44.133 92.577   1.00 39.87  ? 94  LYS D O   1 
ATOM   12889 C CB  . LYS D  1 94  ? 2.766   -45.564 94.651   1.00 58.23  ? 94  LYS D CB  1 
ATOM   12890 C CG  . LYS D  1 94  ? 2.441   -46.540 95.762   1.00 67.90  ? 94  LYS D CG  1 
ATOM   12891 C CD  . LYS D  1 94  ? 0.982   -46.969 95.750   1.00 71.71  ? 94  LYS D CD  1 
ATOM   12892 C CE  . LYS D  1 94  ? 0.764   -48.206 96.618   1.00 75.12  ? 94  LYS D CE  1 
ATOM   12893 N NZ  . LYS D  1 94  ? 2.039   -48.901 96.952   1.00 73.92  ? 94  LYS D NZ  1 
ATOM   12894 N N   . LEU D  1 95  ? 4.015   -42.593 94.044   1.00 45.02  ? 95  LEU D N   1 
ATOM   12895 C CA  . LEU D  1 95  ? 4.269   -41.514 93.099   1.00 43.71  ? 95  LEU D CA  1 
ATOM   12896 C C   . LEU D  1 95  ? 5.764   -41.295 92.897   1.00 41.09  ? 95  LEU D C   1 
ATOM   12897 O O   . LEU D  1 95  ? 6.206   -41.015 91.775   1.00 39.86  ? 95  LEU D O   1 
ATOM   12898 C CB  . LEU D  1 95  ? 3.573   -40.248 93.582   1.00 48.08  ? 95  LEU D CB  1 
ATOM   12899 C CG  . LEU D  1 95  ? 3.542   -39.065 92.640   1.00 55.96  ? 95  LEU D CG  1 
ATOM   12900 C CD1 . LEU D  1 95  ? 2.136   -38.503 92.597   1.00 59.67  ? 95  LEU D CD1 1 
ATOM   12901 C CD2 . LEU D  1 95  ? 4.496   -38.039 93.176   1.00 59.09  ? 95  LEU D CD2 1 
ATOM   12902 N N   . ILE D  1 96  ? 6.565   -41.458 93.953   1.00 38.40  ? 96  ILE D N   1 
ATOM   12903 C CA  . ILE D  1 96  ? 8.014   -41.418 93.789   1.00 40.77  ? 96  ILE D CA  1 
ATOM   12904 C C   . ILE D  1 96  ? 8.498   -42.638 93.012   1.00 42.10  ? 96  ILE D C   1 
ATOM   12905 O O   . ILE D  1 96  ? 9.299   -42.513 92.079   1.00 43.12  ? 96  ILE D O   1 
ATOM   12906 C CB  . ILE D  1 96  ? 8.715   -41.312 95.155   1.00 41.62  ? 96  ILE D CB  1 
ATOM   12907 C CG1 . ILE D  1 96  ? 8.587   -39.888 95.703   1.00 42.82  ? 96  ILE D CG1 1 
ATOM   12908 C CG2 . ILE D  1 96  ? 10.171  -41.700 95.020   1.00 42.79  ? 96  ILE D CG2 1 
ATOM   12909 C CD1 . ILE D  1 96  ? 9.165   -39.713 97.083   1.00 45.94  ? 96  ILE D CD1 1 
ATOM   12910 N N   . GLU D  1 97  ? 8.046   -43.835 93.415   1.00 44.10  ? 97  GLU D N   1 
ATOM   12911 C CA  . GLU D  1 97  ? 8.312   -45.081 92.693   1.00 49.26  ? 97  GLU D CA  1 
ATOM   12912 C C   . GLU D  1 97  ? 8.121   -44.905 91.195   1.00 45.84  ? 97  GLU D C   1 
ATOM   12913 O O   . GLU D  1 97  ? 8.979   -45.267 90.375   1.00 36.46  ? 97  GLU D O   1 
ATOM   12914 C CB  . GLU D  1 97  ? 7.355   -46.179 93.187   1.00 59.80  ? 97  GLU D CB  1 
ATOM   12915 C CG  . GLU D  1 97  ? 7.712   -46.835 94.490   1.00 75.08  ? 97  GLU D CG  1 
ATOM   12916 C CD  . GLU D  1 97  ? 9.184   -46.774 94.766   1.00 87.36  ? 97  GLU D CD  1 
ATOM   12917 O OE1 . GLU D  1 97  ? 9.914   -47.601 94.179   1.00 91.67  ? 97  GLU D OE1 1 
ATOM   12918 O OE2 . GLU D  1 97  ? 9.609   -45.907 95.561   1.00 91.68  ? 97  GLU D OE2 1 
ATOM   12919 N N   . PHE D  1 98  ? 6.968   -44.360 90.836   1.00 40.49  ? 98  PHE D N   1 
ATOM   12920 C CA  . PHE D  1 98  ? 6.587   -44.240 89.438   1.00 34.36  ? 98  PHE D CA  1 
ATOM   12921 C C   . PHE D  1 98  ? 7.497   -43.267 88.697   1.00 35.73  ? 98  PHE D C   1 
ATOM   12922 O O   . PHE D  1 98  ? 7.821   -43.483 87.520   1.00 38.25  ? 98  PHE D O   1 
ATOM   12923 C CB  . PHE D  1 98  ? 5.134   -43.807 89.382   1.00 32.25  ? 98  PHE D CB  1 
ATOM   12924 C CG  . PHE D  1 98  ? 4.520   -43.851 88.009   1.00 34.84  ? 98  PHE D CG  1 
ATOM   12925 C CD1 . PHE D  1 98  ? 3.945   -45.013 87.531   1.00 33.60  ? 98  PHE D CD1 1 
ATOM   12926 C CD2 . PHE D  1 98  ? 4.464   -42.709 87.229   1.00 35.92  ? 98  PHE D CD2 1 
ATOM   12927 C CE1 . PHE D  1 98  ? 3.350   -45.038 86.285   1.00 33.57  ? 98  PHE D CE1 1 
ATOM   12928 C CE2 . PHE D  1 98  ? 3.865   -42.728 85.989   1.00 36.63  ? 98  PHE D CE2 1 
ATOM   12929 C CZ  . PHE D  1 98  ? 3.318   -43.904 85.514   1.00 36.60  ? 98  PHE D CZ  1 
ATOM   12930 N N   . THR D  1 99  ? 7.919   -42.190 89.366   1.00 37.23  ? 99  THR D N   1 
ATOM   12931 C CA  . THR D  1 99  ? 8.883   -41.278 88.761   1.00 39.52  ? 99  THR D CA  1 
ATOM   12932 C C   . THR D  1 99  ? 10.207  -41.983 88.497   1.00 41.54  ? 99  THR D C   1 
ATOM   12933 O O   . THR D  1 99  ? 10.773  -41.877 87.403   1.00 40.73  ? 99  THR D O   1 
ATOM   12934 C CB  . THR D  1 99  ? 9.107   -40.064 89.661   1.00 39.82  ? 99  THR D CB  1 
ATOM   12935 O OG1 . THR D  1 99  ? 7.867   -39.378 89.858   1.00 39.12  ? 99  THR D OG1 1 
ATOM   12936 C CG2 . THR D  1 99  ? 10.123  -39.128 89.027   1.00 35.60  ? 99  THR D CG2 1 
ATOM   12937 N N   . LYS D  1 100 ? 10.723  -42.692 89.505   1.00 40.45  ? 100 LYS D N   1 
ATOM   12938 C CA  . LYS D  1 100 ? 11.992  -43.405 89.364   1.00 42.20  ? 100 LYS D CA  1 
ATOM   12939 C C   . LYS D  1 100 ? 11.955  -44.384 88.205   1.00 37.28  ? 100 LYS D C   1 
ATOM   12940 O O   . LYS D  1 100 ? 12.922  -44.489 87.438   1.00 37.07  ? 100 LYS D O   1 
ATOM   12941 C CB  . LYS D  1 100 ? 12.320  -44.153 90.659   1.00 39.79  ? 100 LYS D CB  1 
ATOM   12942 C CG  . LYS D  1 100 ? 12.591  -43.280 91.854   1.00 53.41  ? 100 LYS D CG  1 
ATOM   12943 C CD  . LYS D  1 100 ? 12.943  -44.158 93.062   1.00 55.42  ? 100 LYS D CD  1 
ATOM   12944 C CE  . LYS D  1 100 ? 14.038  -43.552 93.924   1.00 59.27  ? 100 LYS D CE  1 
ATOM   12945 N NZ  . LYS D  1 100 ? 14.099  -44.167 95.296   1.00 57.23  ? 100 LYS D NZ  1 
ATOM   12946 N N   . LEU D  1 101 ? 10.859  -45.137 88.096   1.00 36.97  ? 101 LEU D N   1 
ATOM   12947 C CA  . LEU D  1 101 ? 10.685  -46.092 87.009   1.00 40.62  ? 101 LEU D CA  1 
ATOM   12948 C C   . LEU D  1 101 ? 10.824  -45.422 85.644   1.00 39.79  ? 101 LEU D C   1 
ATOM   12949 O O   . LEU D  1 101 ? 11.433  -45.985 84.729   1.00 40.81  ? 101 LEU D O   1 
ATOM   12950 C CB  . LEU D  1 101 ? 9.318   -46.763 87.149   1.00 42.50  ? 101 LEU D CB  1 
ATOM   12951 C CG  . LEU D  1 101 ? 8.887   -47.874 86.196   1.00 45.32  ? 101 LEU D CG  1 
ATOM   12952 C CD1 . LEU D  1 101 ? 9.699   -49.130 86.444   1.00 46.96  ? 101 LEU D CD1 1 
ATOM   12953 C CD2 . LEU D  1 101 ? 7.398   -48.141 86.359   1.00 43.34  ? 101 LEU D CD2 1 
ATOM   12954 N N   . ASN D  1 102 ? 10.283  -44.214 85.491   1.00 40.70  ? 102 ASN D N   1 
ATOM   12955 C CA  . ASN D  1 102 ? 10.235  -43.533 84.200   1.00 38.45  ? 102 ASN D CA  1 
ATOM   12956 C C   . ASN D  1 102 ? 11.316  -42.476 84.039   1.00 38.61  ? 102 ASN D C   1 
ATOM   12957 O O   . ASN D  1 102 ? 11.388  -41.828 82.990   1.00 32.32  ? 102 ASN D O   1 
ATOM   12958 C CB  . ASN D  1 102 ? 8.872   -42.889 84.001   1.00 32.43  ? 102 ASN D CB  1 
ATOM   12959 C CG  . ASN D  1 102 ? 7.772   -43.894 83.896   1.00 40.75  ? 102 ASN D CG  1 
ATOM   12960 O OD1 . ASN D  1 102 ? 7.701   -44.649 82.921   1.00 50.78  ? 102 ASN D OD1 1 
ATOM   12961 N ND2 . ASN D  1 102 ? 6.892   -43.915 84.886   1.00 34.97  ? 102 ASN D ND2 1 
ATOM   12962 N N   . TYR D  1 103 ? 12.184  -42.338 85.037   1.00 40.72  ? 103 TYR D N   1 
ATOM   12963 C CA  . TYR D  1 103 ? 13.057  -41.179 85.181   1.00 43.40  ? 103 TYR D CA  1 
ATOM   12964 C C   . TYR D  1 103 ? 14.027  -41.016 84.017   1.00 40.62  ? 103 TYR D C   1 
ATOM   12965 O O   . TYR D  1 103 ? 14.382  -39.881 83.668   1.00 39.34  ? 103 TYR D O   1 
ATOM   12966 C CB  . TYR D  1 103 ? 13.817  -41.319 86.509   1.00 49.67  ? 103 TYR D CB  1 
ATOM   12967 C CG  . TYR D  1 103 ? 14.841  -40.255 86.801   1.00 56.17  ? 103 TYR D CG  1 
ATOM   12968 C CD1 . TYR D  1 103 ? 16.167  -40.411 86.417   1.00 60.95  ? 103 TYR D CD1 1 
ATOM   12969 C CD2 . TYR D  1 103 ? 14.490  -39.107 87.493   1.00 62.04  ? 103 TYR D CD2 1 
ATOM   12970 C CE1 . TYR D  1 103 ? 17.111  -39.442 86.695   1.00 65.67  ? 103 TYR D CE1 1 
ATOM   12971 C CE2 . TYR D  1 103 ? 15.424  -38.132 87.779   1.00 66.74  ? 103 TYR D CE2 1 
ATOM   12972 C CZ  . TYR D  1 103 ? 16.734  -38.304 87.378   1.00 69.68  ? 103 TYR D CZ  1 
ATOM   12973 O OH  . TYR D  1 103 ? 17.667  -37.331 87.661   1.00 74.05  ? 103 TYR D OH  1 
ATOM   12974 N N   . GLU D  1 104 ? 14.479  -42.121 83.415   1.00 34.12  ? 104 GLU D N   1 
ATOM   12975 C CA  . GLU D  1 104 ? 15.518  -42.070 82.394   1.00 38.34  ? 104 GLU D CA  1 
ATOM   12976 C C   . GLU D  1 104 ? 14.973  -41.965 80.976   1.00 36.13  ? 104 GLU D C   1 
ATOM   12977 O O   . GLU D  1 104 ? 15.764  -41.845 80.038   1.00 36.33  ? 104 GLU D O   1 
ATOM   12978 C CB  . GLU D  1 104 ? 16.427  -43.301 82.486   1.00 45.57  ? 104 GLU D CB  1 
ATOM   12979 C CG  . GLU D  1 104 ? 17.395  -43.286 83.658   1.00 56.25  ? 104 GLU D CG  1 
ATOM   12980 C CD  . GLU D  1 104 ? 16.903  -44.111 84.838   1.00 65.57  ? 104 GLU D CD  1 
ATOM   12981 O OE1 . GLU D  1 104 ? 17.563  -44.094 85.900   1.00 69.89  ? 104 GLU D OE1 1 
ATOM   12982 O OE2 . GLU D  1 104 ? 15.854  -44.779 84.704   1.00 67.38  ? 104 GLU D OE2 1 
ATOM   12983 N N   . LYS D  1 105 ? 13.659  -42.023 80.796   1.00 34.03  ? 105 LYS D N   1 
ATOM   12984 C CA  . LYS D  1 105 ? 13.040  -41.899 79.482   1.00 33.64  ? 105 LYS D CA  1 
ATOM   12985 C C   . LYS D  1 105 ? 13.015  -40.435 79.045   1.00 36.30  ? 105 LYS D C   1 
ATOM   12986 O O   . LYS D  1 105 ? 12.790  -39.541 79.867   1.00 34.32  ? 105 LYS D O   1 
ATOM   12987 C CB  . LYS D  1 105 ? 11.621  -42.467 79.505   1.00 31.04  ? 105 LYS D CB  1 
ATOM   12988 C CG  . LYS D  1 105 ? 11.572  -43.938 79.969   1.00 29.19  ? 105 LYS D CG  1 
ATOM   12989 C CD  . LYS D  1 105 ? 10.148  -44.360 80.305   1.00 32.93  ? 105 LYS D CD  1 
ATOM   12990 C CE  . LYS D  1 105 ? 10.077  -45.842 80.692   1.00 32.86  ? 105 LYS D CE  1 
ATOM   12991 N NZ  . LYS D  1 105 ? 8.668   -46.220 81.062   1.00 33.95  ? 105 LYS D NZ  1 
ATOM   12992 N N   . PRO D  1 106 ? 13.259  -40.166 77.762   1.00 35.43  ? 106 PRO D N   1 
ATOM   12993 C CA  . PRO D  1 106 ? 13.356  -38.770 77.320   1.00 35.21  ? 106 PRO D CA  1 
ATOM   12994 C C   . PRO D  1 106 ? 12.100  -37.956 77.572   1.00 31.35  ? 106 PRO D C   1 
ATOM   12995 O O   . PRO D  1 106 ? 12.205  -36.741 77.756   1.00 32.23  ? 106 PRO D O   1 
ATOM   12996 C CB  . PRO D  1 106 ? 13.663  -38.904 75.822   1.00 35.07  ? 106 PRO D CB  1 
ATOM   12997 C CG  . PRO D  1 106 ? 14.382  -40.207 75.717   1.00 34.39  ? 106 PRO D CG  1 
ATOM   12998 C CD  . PRO D  1 106 ? 13.700  -41.108 76.717   1.00 33.37  ? 106 PRO D CD  1 
ATOM   12999 N N   . ILE D  1 107 ? 10.915  -38.576 77.605   1.00 28.30  ? 107 ILE D N   1 
ATOM   13000 C CA  . ILE D  1 107 ? 9.701   -37.810 77.872   1.00 27.00  ? 107 ILE D CA  1 
ATOM   13001 C C   . ILE D  1 107 ? 9.628   -37.321 79.315   1.00 32.85  ? 107 ILE D C   1 
ATOM   13002 O O   . ILE D  1 107 ? 8.805   -36.446 79.630   1.00 25.69  ? 107 ILE D O   1 
ATOM   13003 C CB  . ILE D  1 107 ? 8.438   -38.629 77.526   1.00 25.05  ? 107 ILE D CB  1 
ATOM   13004 C CG1 . ILE D  1 107 ? 8.440   -39.990 78.222   1.00 27.65  ? 107 ILE D CG1 1 
ATOM   13005 C CG2 . ILE D  1 107 ? 8.312   -38.829 76.018   1.00 25.90  ? 107 ILE D CG2 1 
ATOM   13006 C CD1 . ILE D  1 107 ? 7.050   -40.595 78.311   1.00 23.34  ? 107 ILE D CD1 1 
ATOM   13007 N N   . TYR D  1 108 ? 10.475  -37.854 80.197   1.00 33.18  ? 108 TYR D N   1 
ATOM   13008 C CA  . TYR D  1 108 ? 10.599  -37.366 81.561   1.00 36.17  ? 108 TYR D CA  1 
ATOM   13009 C C   . TYR D  1 108 ? 11.736  -36.361 81.734   1.00 39.58  ? 108 TYR D C   1 
ATOM   13010 O O   . TYR D  1 108 ? 12.100  -36.043 82.873   1.00 35.17  ? 108 TYR D O   1 
ATOM   13011 C CB  . TYR D  1 108 ? 10.789  -38.545 82.519   1.00 36.64  ? 108 TYR D CB  1 
ATOM   13012 C CG  . TYR D  1 108 ? 9.476   -39.053 83.064   1.00 35.06  ? 108 TYR D CG  1 
ATOM   13013 C CD1 . TYR D  1 108 ? 8.579   -39.737 82.242   1.00 31.21  ? 108 TYR D CD1 1 
ATOM   13014 C CD2 . TYR D  1 108 ? 9.119   -38.834 84.392   1.00 31.18  ? 108 TYR D CD2 1 
ATOM   13015 C CE1 . TYR D  1 108 ? 7.364   -40.200 82.736   1.00 31.53  ? 108 TYR D CE1 1 
ATOM   13016 C CE2 . TYR D  1 108 ? 7.910   -39.288 84.895   1.00 30.50  ? 108 TYR D CE2 1 
ATOM   13017 C CZ  . TYR D  1 108 ? 7.036   -39.974 84.070   1.00 33.38  ? 108 TYR D CZ  1 
ATOM   13018 O OH  . TYR D  1 108 ? 5.830   -40.435 84.558   1.00 33.92  ? 108 TYR D OH  1 
ATOM   13019 N N   . ARG D  1 109 ? 12.309  -35.848 80.643   1.00 39.63  ? 109 ARG D N   1 
ATOM   13020 C CA  . ARG D  1 109 ? 13.458  -34.954 80.779   1.00 45.50  ? 109 ARG D CA  1 
ATOM   13021 C C   . ARG D  1 109 ? 12.963  -33.534 81.071   1.00 43.86  ? 109 ARG D C   1 
ATOM   13022 O O   . ARG D  1 109 ? 12.826  -32.682 80.190   1.00 38.58  ? 109 ARG D O   1 
ATOM   13023 C CB  . ARG D  1 109 ? 14.357  -35.014 79.550   1.00 47.52  ? 109 ARG D CB  1 
ATOM   13024 C CG  . ARG D  1 109 ? 15.826  -34.797 79.908   1.00 53.88  ? 109 ARG D CG  1 
ATOM   13025 C CD  . ARG D  1 109 ? 16.744  -34.984 78.727   1.00 58.53  ? 109 ARG D CD  1 
ATOM   13026 N NE  . ARG D  1 109 ? 16.019  -34.869 77.472   1.00 61.21  ? 109 ARG D NE  1 
ATOM   13027 C CZ  . ARG D  1 109 ? 16.011  -35.802 76.526   1.00 63.09  ? 109 ARG D CZ  1 
ATOM   13028 N NH1 . ARG D  1 109 ? 16.694  -36.929 76.696   1.00 60.35  ? 109 ARG D NH1 1 
ATOM   13029 N NH2 . ARG D  1 109 ? 15.314  -35.610 75.412   1.00 64.49  ? 109 ARG D NH2 1 
ATOM   13030 N N   . PHE D  1 110 ? 12.673  -33.301 82.353   1.00 44.31  ? 110 PHE D N   1 
ATOM   13031 C CA  . PHE D  1 110 ? 12.428  -31.980 82.917   1.00 44.73  ? 110 PHE D CA  1 
ATOM   13032 C C   . PHE D  1 110 ? 13.454  -31.717 84.011   1.00 44.25  ? 110 PHE D C   1 
ATOM   13033 O O   . PHE D  1 110 ? 13.724  -32.594 84.838   1.00 40.75  ? 110 PHE D O   1 
ATOM   13034 C CB  . PHE D  1 110 ? 11.021  -31.860 83.515   1.00 41.20  ? 110 PHE D CB  1 
ATOM   13035 C CG  . PHE D  1 110 ? 9.917   -32.085 82.527   1.00 36.75  ? 110 PHE D CG  1 
ATOM   13036 C CD1 . PHE D  1 110 ? 9.555   -33.368 82.158   1.00 34.89  ? 110 PHE D CD1 1 
ATOM   13037 C CD2 . PHE D  1 110 ? 9.224   -31.017 81.982   1.00 36.44  ? 110 PHE D CD2 1 
ATOM   13038 C CE1 . PHE D  1 110 ? 8.535   -33.584 81.254   1.00 33.93  ? 110 PHE D CE1 1 
ATOM   13039 C CE2 . PHE D  1 110 ? 8.194   -31.227 81.078   1.00 31.29  ? 110 PHE D CE2 1 
ATOM   13040 C CZ  . PHE D  1 110 ? 7.854   -32.515 80.714   1.00 31.13  ? 110 PHE D CZ  1 
ATOM   13041 N N   . GLU D  1 111 ? 14.024  -30.508 84.012   1.00 46.12  ? 111 GLU D N   1 
ATOM   13042 C CA  . GLU D  1 111 ? 15.036  -30.171 85.008   1.00 54.19  ? 111 GLU D CA  1 
ATOM   13043 C C   . GLU D  1 111 ? 14.465  -30.220 86.419   1.00 55.26  ? 111 GLU D C   1 
ATOM   13044 O O   . GLU D  1 111 ? 15.183  -30.536 87.378   1.00 55.36  ? 111 GLU D O   1 
ATOM   13045 C CB  . GLU D  1 111 ? 15.622  -28.788 84.709   1.00 64.32  ? 111 GLU D CB  1 
ATOM   13046 C CG  . GLU D  1 111 ? 16.785  -28.365 85.605   1.00 78.75  ? 111 GLU D CG  1 
ATOM   13047 C CD  . GLU D  1 111 ? 17.943  -29.348 85.580   1.00 89.48  ? 111 GLU D CD  1 
ATOM   13048 O OE1 . GLU D  1 111 ? 17.853  -30.381 86.270   1.00 92.62  ? 111 GLU D OE1 1 
ATOM   13049 O OE2 . GLU D  1 111 ? 18.942  -29.090 84.875   1.00 93.89  ? 111 GLU D OE2 1 
ATOM   13050 N N   . ARG D  1 112 ? 13.174  -29.931 86.563   1.00 53.12  ? 112 ARG D N   1 
ATOM   13051 C CA  . ARG D  1 112 ? 12.557  -29.945 87.880   1.00 53.97  ? 112 ARG D CA  1 
ATOM   13052 C C   . ARG D  1 112 ? 12.458  -31.362 88.433   1.00 54.12  ? 112 ARG D C   1 
ATOM   13053 O O   . ARG D  1 112 ? 12.564  -31.569 89.648   1.00 50.80  ? 112 ARG D O   1 
ATOM   13054 C CB  . ARG D  1 112 ? 11.181  -29.290 87.808   1.00 50.61  ? 112 ARG D CB  1 
ATOM   13055 C CG  . ARG D  1 112 ? 10.419  -29.269 89.117   1.00 49.85  ? 112 ARG D CG  1 
ATOM   13056 C CD  . ARG D  1 112 ? 11.120  -28.427 90.164   1.00 48.44  ? 112 ARG D CD  1 
ATOM   13057 N NE  . ARG D  1 112 ? 10.183  -28.006 91.197   1.00 48.34  ? 112 ARG D NE  1 
ATOM   13058 C CZ  . ARG D  1 112 ? 10.544  -27.610 92.413   1.00 54.71  ? 112 ARG D CZ  1 
ATOM   13059 N NH1 . ARG D  1 112 ? 11.830  -27.572 92.737   1.00 57.59  ? 112 ARG D NH1 1 
ATOM   13060 N NH2 . ARG D  1 112 ? 9.622   -27.239 93.298   1.00 53.36  ? 112 ARG D NH2 1 
ATOM   13061 N N   . ILE D  1 113 ? 12.263  -32.353 87.561   1.00 52.74  ? 113 ILE D N   1 
ATOM   13062 C CA  . ILE D  1 113 ? 12.181  -33.732 88.036   1.00 53.90  ? 113 ILE D CA  1 
ATOM   13063 C C   . ILE D  1 113 ? 13.519  -34.180 88.610   1.00 56.82  ? 113 ILE D C   1 
ATOM   13064 O O   . ILE D  1 113 ? 13.567  -34.900 89.616   1.00 59.63  ? 113 ILE D O   1 
ATOM   13065 C CB  . ILE D  1 113 ? 11.694  -34.663 86.911   1.00 51.08  ? 113 ILE D CB  1 
ATOM   13066 C CG1 . ILE D  1 113 ? 10.183  -34.521 86.746   1.00 47.99  ? 113 ILE D CG1 1 
ATOM   13067 C CG2 . ILE D  1 113 ? 12.052  -36.115 87.209   1.00 52.58  ? 113 ILE D CG2 1 
ATOM   13068 C CD1 . ILE D  1 113 ? 9.658   -35.108 85.473   1.00 45.76  ? 113 ILE D CD1 1 
ATOM   13069 N N   . ARG D  1 114 ? 14.626  -33.741 88.002   1.00 56.18  ? 114 ARG D N   1 
ATOM   13070 C CA  . ARG D  1 114 ? 15.939  -34.127 88.511   1.00 58.70  ? 114 ARG D CA  1 
ATOM   13071 C C   . ARG D  1 114 ? 16.146  -33.628 89.935   1.00 60.49  ? 114 ARG D C   1 
ATOM   13072 O O   . ARG D  1 114 ? 16.850  -34.268 90.724   1.00 59.62  ? 114 ARG D O   1 
ATOM   13073 C CB  . ARG D  1 114 ? 17.049  -33.606 87.587   1.00 59.92  ? 114 ARG D CB  1 
ATOM   13074 C CG  . ARG D  1 114 ? 18.458  -33.660 88.193   1.00 65.52  ? 114 ARG D CG  1 
ATOM   13075 C CD  . ARG D  1 114 ? 19.355  -32.526 87.693   1.00 71.73  ? 114 ARG D CD  1 
ATOM   13076 N NE  . ARG D  1 114 ? 20.297  -32.029 88.706   1.00 78.84  ? 114 ARG D NE  1 
ATOM   13077 C CZ  . ARG D  1 114 ? 20.052  -31.024 89.547   1.00 80.30  ? 114 ARG D CZ  1 
ATOM   13078 N NH1 . ARG D  1 114 ? 18.891  -30.383 89.516   1.00 77.50  ? 114 ARG D NH1 1 
ATOM   13079 N NH2 . ARG D  1 114 ? 20.977  -30.655 90.422   1.00 84.06  ? 114 ARG D NH2 1 
ATOM   13080 N N   . GLU D  1 115 ? 15.511  -32.510 90.293   1.00 61.87  ? 115 GLU D N   1 
ATOM   13081 C CA  . GLU D  1 115 ? 15.696  -31.930 91.618   1.00 65.52  ? 115 GLU D CA  1 
ATOM   13082 C C   . GLU D  1 115 ? 14.912  -32.688 92.676   1.00 66.52  ? 115 GLU D C   1 
ATOM   13083 O O   . GLU D  1 115 ? 15.453  -33.030 93.735   1.00 69.82  ? 115 GLU D O   1 
ATOM   13084 C CB  . GLU D  1 115 ? 15.274  -30.464 91.608   1.00 66.16  ? 115 GLU D CB  1 
ATOM   13085 C CG  . GLU D  1 115 ? 15.999  -29.626 90.585   1.00 67.12  ? 115 GLU D CG  1 
ATOM   13086 C CD  . GLU D  1 115 ? 15.394  -28.248 90.440   1.00 67.90  ? 115 GLU D CD  1 
ATOM   13087 O OE1 . GLU D  1 115 ? 14.557  -27.874 91.293   1.00 64.53  ? 115 GLU D OE1 1 
ATOM   13088 O OE2 . GLU D  1 115 ? 15.758  -27.542 89.474   1.00 69.55  ? 115 GLU D OE2 1 
ATOM   13089 N N   . LEU D  1 116 ? 13.627  -32.940 92.417   1.00 63.55  ? 116 LEU D N   1 
ATOM   13090 C CA  . LEU D  1 116 ? 12.805  -33.623 93.410   1.00 65.68  ? 116 LEU D CA  1 
ATOM   13091 C C   . LEU D  1 116 ? 13.309  -35.033 93.685   1.00 66.80  ? 116 LEU D C   1 
ATOM   13092 O O   . LEU D  1 116 ? 13.158  -35.538 94.805   1.00 71.41  ? 116 LEU D O   1 
ATOM   13093 C CB  . LEU D  1 116 ? 11.346  -33.644 92.956   1.00 61.60  ? 116 LEU D CB  1 
ATOM   13094 C CG  . LEU D  1 116 ? 10.862  -32.321 92.364   1.00 59.33  ? 116 LEU D CG  1 
ATOM   13095 C CD1 . LEU D  1 116 ? 9.555   -32.502 91.610   1.00 56.63  ? 116 LEU D CD1 1 
ATOM   13096 C CD2 . LEU D  1 116 ? 10.720  -31.268 93.455   1.00 58.29  ? 116 LEU D CD2 1 
ATOM   13097 N N   . MET D  1 117 ? 13.925  -35.673 92.691   1.00 64.07  ? 117 MET D N   1 
ATOM   13098 C CA  . MET D  1 117 ? 14.459  -37.016 92.882   1.00 66.26  ? 117 MET D CA  1 
ATOM   13099 C C   . MET D  1 117 ? 15.746  -37.026 93.686   1.00 69.53  ? 117 MET D C   1 
ATOM   13100 O O   . MET D  1 117 ? 16.180  -38.105 94.111   1.00 68.76  ? 117 MET D O   1 
ATOM   13101 C CB  . MET D  1 117 ? 14.675  -37.686 91.528   1.00 63.91  ? 117 MET D CB  1 
ATOM   13102 C CG  . MET D  1 117 ? 13.375  -37.968 90.811   1.00 65.93  ? 117 MET D CG  1 
ATOM   13103 S SD  . MET D  1 117 ? 12.264  -38.938 91.851   1.00 69.47  ? 117 MET D SD  1 
ATOM   13104 C CE  . MET D  1 117 ? 11.053  -37.723 92.349   1.00 65.51  ? 117 MET D CE  1 
ATOM   13105 N N   . ASN D  1 118 ? 16.356  -35.859 93.899   1.00 73.89  ? 118 ASN D N   1 
ATOM   13106 C CA  . ASN D  1 118 ? 17.517  -35.728 94.763   1.00 78.18  ? 118 ASN D CA  1 
ATOM   13107 C C   . ASN D  1 118 ? 17.148  -35.282 96.168   1.00 80.60  ? 118 ASN D C   1 
ATOM   13108 O O   . ASN D  1 118 ? 17.978  -35.405 97.070   1.00 85.05  ? 118 ASN D O   1 
ATOM   13109 C CB  . ASN D  1 118 ? 18.530  -34.736 94.164   1.00 80.10  ? 118 ASN D CB  1 
ATOM   13110 C CG  . ASN D  1 118 ? 19.392  -35.349 93.090   1.00 82.30  ? 118 ASN D CG  1 
ATOM   13111 O OD1 . ASN D  1 118 ? 19.784  -36.528 93.143   1.00 84.41  ? 118 ASN D OD1 1 
ATOM   13112 N ND2 . ASN D  1 118 ? 19.692  -34.543 92.093   1.00 81.64  ? 118 ASN D ND2 1 
ATOM   13113 N N   . LYS D  1 119 ? 15.923  -34.807 96.379   1.00 75.89  ? 119 LYS D N   1 
ATOM   13114 C CA  . LYS D  1 119 ? 15.517  -34.291 97.683   1.00 73.27  ? 119 LYS D CA  1 
ATOM   13115 C C   . LYS D  1 119 ? 15.109  -35.421 98.626   1.00 72.49  ? 119 LYS D C   1 
ATOM   13116 O O   . LYS D  1 119 ? 14.408  -36.367 98.237   1.00 67.28  ? 119 LYS D O   1 
ATOM   13117 C CB  . LYS D  1 119 ? 14.349  -33.304 97.555   1.00 66.96  ? 119 LYS D CB  1 
ATOM   13118 C CG  . LYS D  1 119 ? 14.663  -32.010 96.806   1.00 64.59  ? 119 LYS D CG  1 
ATOM   13119 C CD  . LYS D  1 119 ? 13.660  -30.847 97.039   1.00 63.88  ? 119 LYS D CD  1 
ATOM   13120 C CE  . LYS D  1 119 ? 14.021  -29.664 96.113   1.00 64.54  ? 119 LYS D CE  1 
ATOM   13121 N NZ  . LYS D  1 119 ? 15.293  -28.967 96.497   1.00 67.67  ? 119 LYS D NZ  1 
ATOM   13122 N N   . GLU D  1 120 ? 15.531  -35.302 99.890   1.00 75.87  ? 120 GLU D N   1 
ATOM   13123 C CA  . GLU D  1 120 ? 15.190  -36.322 100.877  1.00 77.82  ? 120 GLU D CA  1 
ATOM   13124 C C   . GLU D  1 120 ? 13.709  -36.272 101.223  1.00 77.78  ? 120 GLU D C   1 
ATOM   13125 O O   . GLU D  1 120 ? 13.045  -37.314 101.288  1.00 78.51  ? 120 GLU D O   1 
ATOM   13126 C CB  . GLU D  1 120 ? 16.053  -36.146 102.128  1.00 81.32  ? 120 GLU D CB  1 
ATOM   13127 N N   . LYS D  1 121 ? 13.175  -35.070 101.440  1.00 76.09  ? 121 LYS D N   1 
ATOM   13128 C CA  . LYS D  1 121 ? 11.760  -34.861 101.709  1.00 74.12  ? 121 LYS D CA  1 
ATOM   13129 C C   . LYS D  1 121 ? 11.219  -33.801 100.756  1.00 70.75  ? 121 LYS D C   1 
ATOM   13130 O O   . LYS D  1 121 ? 11.953  -32.920 100.299  1.00 73.00  ? 121 LYS D O   1 
ATOM   13131 C CB  . LYS D  1 121 ? 11.519  -34.437 103.166  1.00 75.68  ? 121 LYS D CB  1 
ATOM   13132 N N   . LEU D  1 122 ? 9.924   -33.899 100.457  1.00 61.55  ? 122 LEU D N   1 
ATOM   13133 C CA  . LEU D  1 122 ? 9.266   -33.010 99.511   1.00 56.17  ? 122 LEU D CA  1 
ATOM   13134 C C   . LEU D  1 122 ? 8.081   -32.342 100.194  1.00 53.91  ? 122 LEU D C   1 
ATOM   13135 O O   . LEU D  1 122 ? 7.252   -33.017 100.808  1.00 58.26  ? 122 LEU D O   1 
ATOM   13136 C CB  . LEU D  1 122 ? 8.813   -33.782 98.254   1.00 48.15  ? 122 LEU D CB  1 
ATOM   13137 C CG  . LEU D  1 122 ? 9.951   -34.303 97.375   1.00 50.67  ? 122 LEU D CG  1 
ATOM   13138 C CD1 . LEU D  1 122 ? 9.429   -35.196 96.266   1.00 54.45  ? 122 LEU D CD1 1 
ATOM   13139 C CD2 . LEU D  1 122 ? 10.746  -33.143 96.788   1.00 52.13  ? 122 LEU D CD2 1 
ATOM   13140 N N   . ASN D  1 123 ? 7.997   -31.022 100.088  1.00 51.52  ? 123 ASN D N   1 
ATOM   13141 C CA  . ASN D  1 123 ? 6.862   -30.303 100.649  1.00 54.75  ? 123 ASN D CA  1 
ATOM   13142 C C   . ASN D  1 123 ? 5.716   -30.257 99.632   1.00 49.72  ? 123 ASN D C   1 
ATOM   13143 O O   . ASN D  1 123 ? 5.783   -30.845 98.551   1.00 50.62  ? 123 ASN D O   1 
ATOM   13144 C CB  . ASN D  1 123 ? 7.283   -28.906 101.126  1.00 56.76  ? 123 ASN D CB  1 
ATOM   13145 C CG  . ASN D  1 123 ? 7.631   -27.951 99.981   1.00 56.99  ? 123 ASN D CG  1 
ATOM   13146 O OD1 . ASN D  1 123 ? 7.046   -27.997 98.901   1.00 53.61  ? 123 ASN D OD1 1 
ATOM   13147 N ND2 . ASN D  1 123 ? 8.577   -27.059 100.236  1.00 60.92  ? 123 ASN D ND2 1 
ATOM   13148 N N   . ARG D  1 124 ? 4.660   -29.517 99.972   1.00 42.66  ? 124 ARG D N   1 
ATOM   13149 C CA  . ARG D  1 124 ? 3.435   -29.536 99.181   1.00 47.23  ? 124 ARG D CA  1 
ATOM   13150 C C   . ARG D  1 124 ? 3.668   -29.000 97.771   1.00 50.24  ? 124 ARG D C   1 
ATOM   13151 O O   . ARG D  1 124 ? 3.219   -29.597 96.783   1.00 50.49  ? 124 ARG D O   1 
ATOM   13152 C CB  . ARG D  1 124 ? 2.361   -28.728 99.899   1.00 46.32  ? 124 ARG D CB  1 
ATOM   13153 C CG  . ARG D  1 124 ? 1.023   -28.754 99.230   1.00 44.70  ? 124 ARG D CG  1 
ATOM   13154 C CD  . ARG D  1 124 ? 0.153   -27.594 99.675   1.00 43.62  ? 124 ARG D CD  1 
ATOM   13155 N NE  . ARG D  1 124 ? -1.034  -27.531 98.833   1.00 46.07  ? 124 ARG D NE  1 
ATOM   13156 C CZ  . ARG D  1 124 ? -1.127  -26.800 97.729   1.00 45.09  ? 124 ARG D CZ  1 
ATOM   13157 N NH1 . ARG D  1 124 ? -0.114  -26.030 97.359   1.00 43.51  ? 124 ARG D NH1 1 
ATOM   13158 N NH2 . ARG D  1 124 ? -2.243  -26.820 97.011   1.00 42.62  ? 124 ARG D NH2 1 
ATOM   13159 N N   . GLU D  1 125 ? 4.358   -27.863 97.656   1.00 49.81  ? 125 GLU D N   1 
ATOM   13160 C CA  . GLU D  1 125 ? 4.600   -27.294 96.336   1.00 49.21  ? 125 GLU D CA  1 
ATOM   13161 C C   . GLU D  1 125 ? 5.452   -28.225 95.479   1.00 49.90  ? 125 GLU D C   1 
ATOM   13162 O O   . GLU D  1 125 ? 5.259   -28.300 94.257   1.00 45.63  ? 125 GLU D O   1 
ATOM   13163 C CB  . GLU D  1 125 ? 5.253   -25.919 96.471   1.00 53.51  ? 125 GLU D CB  1 
ATOM   13164 C CG  . GLU D  1 125 ? 5.494   -25.176 95.145   1.00 62.86  ? 125 GLU D CG  1 
ATOM   13165 C CD  . GLU D  1 125 ? 4.216   -24.877 94.345   1.00 71.03  ? 125 GLU D CD  1 
ATOM   13166 O OE1 . GLU D  1 125 ? 3.707   -25.796 93.654   1.00 68.69  ? 125 GLU D OE1 1 
ATOM   13167 O OE2 . GLU D  1 125 ? 3.735   -23.714 94.393   1.00 74.76  ? 125 GLU D OE2 1 
ATOM   13168 N N   . GLU D  1 126 ? 6.365   -28.970 96.109   1.00 52.08  ? 126 GLU D N   1 
ATOM   13169 C CA  . GLU D  1 126 ? 7.214   -29.899 95.370   1.00 50.87  ? 126 GLU D CA  1 
ATOM   13170 C C   . GLU D  1 126 ? 6.442   -31.146 94.949   1.00 49.08  ? 126 GLU D C   1 
ATOM   13171 O O   . GLU D  1 126 ? 6.601   -31.625 93.817   1.00 47.86  ? 126 GLU D O   1 
ATOM   13172 C CB  . GLU D  1 126 ? 8.437   -30.263 96.214   1.00 52.24  ? 126 GLU D CB  1 
ATOM   13173 C CG  . GLU D  1 126 ? 9.412   -29.104 96.344   1.00 54.56  ? 126 GLU D CG  1 
ATOM   13174 C CD  . GLU D  1 126 ? 10.286  -29.192 97.571   1.00 57.90  ? 126 GLU D CD  1 
ATOM   13175 O OE1 . GLU D  1 126 ? 9.925   -29.924 98.516   1.00 58.43  ? 126 GLU D OE1 1 
ATOM   13176 O OE2 . GLU D  1 126 ? 11.334  -28.515 97.587   1.00 58.99  ? 126 GLU D OE2 1 
ATOM   13177 N N   . LEU D  1 127 ? 5.598   -31.686 95.838   1.00 42.84  ? 127 LEU D N   1 
ATOM   13178 C CA  . LEU D  1 127 ? 4.726   -32.788 95.433   1.00 39.17  ? 127 LEU D CA  1 
ATOM   13179 C C   . LEU D  1 127 ? 3.792   -32.352 94.311   1.00 38.05  ? 127 LEU D C   1 
ATOM   13180 O O   . LEU D  1 127 ? 3.466   -33.144 93.412   1.00 33.93  ? 127 LEU D O   1 
ATOM   13181 C CB  . LEU D  1 127 ? 3.922   -33.300 96.626   1.00 41.96  ? 127 LEU D CB  1 
ATOM   13182 C CG  . LEU D  1 127 ? 4.729   -33.875 97.792   1.00 40.50  ? 127 LEU D CG  1 
ATOM   13183 C CD1 . LEU D  1 127 ? 3.855   -34.112 99.030   1.00 38.12  ? 127 LEU D CD1 1 
ATOM   13184 C CD2 . LEU D  1 127 ? 5.427   -35.158 97.354   1.00 40.03  ? 127 LEU D CD2 1 
ATOM   13185 N N   . LEU D  1 128 ? 3.352   -31.091 94.348   1.00 33.36  ? 128 LEU D N   1 
ATOM   13186 C CA  . LEU D  1 128 ? 2.485   -30.586 93.302   1.00 32.74  ? 128 LEU D CA  1 
ATOM   13187 C C   . LEU D  1 128 ? 3.207   -30.591 91.965   1.00 36.34  ? 128 LEU D C   1 
ATOM   13188 O O   . LEU D  1 128 ? 2.603   -30.895 90.933   1.00 32.96  ? 128 LEU D O   1 
ATOM   13189 C CB  . LEU D  1 128 ? 1.990   -29.181 93.652   1.00 38.53  ? 128 LEU D CB  1 
ATOM   13190 C CG  . LEU D  1 128 ? 0.513   -29.076 94.039   1.00 39.40  ? 128 LEU D CG  1 
ATOM   13191 C CD1 . LEU D  1 128 ? 0.113   -27.627 94.338   1.00 39.61  ? 128 LEU D CD1 1 
ATOM   13192 C CD2 . LEU D  1 128 ? -0.372  -29.660 92.960   1.00 42.59  ? 128 LEU D CD2 1 
ATOM   13193 N N   . ASP D  1 129 ? 4.511   -30.287 91.968   1.00 35.97  ? 129 ASP D N   1 
ATOM   13194 C CA  . ASP D  1 129 ? 5.294   -30.371 90.734   1.00 36.50  ? 129 ASP D CA  1 
ATOM   13195 C C   . ASP D  1 129 ? 5.490   -31.819 90.302   1.00 36.93  ? 129 ASP D C   1 
ATOM   13196 O O   . ASP D  1 129 ? 5.449   -32.128 89.102   1.00 30.83  ? 129 ASP D O   1 
ATOM   13197 C CB  . ASP D  1 129 ? 6.649   -29.680 90.912   1.00 39.54  ? 129 ASP D CB  1 
ATOM   13198 C CG  . ASP D  1 129 ? 6.552   -28.168 90.799   1.00 43.12  ? 129 ASP D CG  1 
ATOM   13199 O OD1 . ASP D  1 129 ? 5.420   -27.674 90.624   1.00 46.68  ? 129 ASP D OD1 1 
ATOM   13200 O OD2 . ASP D  1 129 ? 7.589   -27.469 90.891   1.00 45.63  ? 129 ASP D OD2 1 
ATOM   13201 N N   . LEU D  1 130 ? 5.680   -32.727 91.262   1.00 31.45  ? 130 LEU D N   1 
ATOM   13202 C CA  . LEU D  1 130 ? 5.873   -34.128 90.902   1.00 33.51  ? 130 LEU D CA  1 
ATOM   13203 C C   . LEU D  1 130 ? 4.608   -34.715 90.289   1.00 40.84  ? 130 LEU D C   1 
ATOM   13204 O O   . LEU D  1 130 ? 4.682   -35.486 89.321   1.00 43.22  ? 130 LEU D O   1 
ATOM   13205 C CB  . LEU D  1 130 ? 6.305   -34.946 92.114   1.00 33.50  ? 130 LEU D CB  1 
ATOM   13206 C CG  . LEU D  1 130 ? 6.969   -36.306 91.850   1.00 33.36  ? 130 LEU D CG  1 
ATOM   13207 C CD1 . LEU D  1 130 ? 8.073   -36.192 90.809   1.00 35.48  ? 130 LEU D CD1 1 
ATOM   13208 C CD2 . LEU D  1 130 ? 7.516   -36.898 93.160   1.00 38.28  ? 130 LEU D CD2 1 
ATOM   13209 N N   . GLN D  1 131 ? 3.435   -34.345 90.820   1.00 36.69  ? 131 GLN D N   1 
ATOM   13210 C CA  . GLN D  1 131 ? 2.188   -34.840 90.245   1.00 33.90  ? 131 GLN D CA  1 
ATOM   13211 C C   . GLN D  1 131 ? 1.990   -34.301 88.836   1.00 36.59  ? 131 GLN D C   1 
ATOM   13212 O O   . GLN D  1 131 ? 1.620   -35.044 87.923   1.00 39.56  ? 131 GLN D O   1 
ATOM   13213 C CB  . GLN D  1 131 ? 0.994   -34.450 91.107   1.00 31.40  ? 131 GLN D CB  1 
ATOM   13214 C CG  . GLN D  1 131 ? 1.009   -34.970 92.529   1.00 30.56  ? 131 GLN D CG  1 
ATOM   13215 C CD  . GLN D  1 131 ? -0.039  -34.282 93.358   1.00 33.18  ? 131 GLN D CD  1 
ATOM   13216 O OE1 . GLN D  1 131 ? -0.235  -33.061 93.248   1.00 33.48  ? 131 GLN D OE1 1 
ATOM   13217 N NE2 . GLN D  1 131 ? -0.747  -35.053 94.179   1.00 32.72  ? 131 GLN D NE2 1 
ATOM   13218 N N   . THR D  1 132 ? 2.222   -33.007 88.648   1.00 31.60  ? 132 THR D N   1 
ATOM   13219 C CA  . THR D  1 132 ? 1.879   -32.391 87.377   1.00 36.01  ? 132 THR D CA  1 
ATOM   13220 C C   . THR D  1 132 ? 2.877   -32.774 86.298   1.00 35.19  ? 132 THR D C   1 
ATOM   13221 O O   . THR D  1 132 ? 2.490   -33.042 85.156   1.00 36.33  ? 132 THR D O   1 
ATOM   13222 C CB  . THR D  1 132 ? 1.797   -30.870 87.540   1.00 29.76  ? 132 THR D CB  1 
ATOM   13223 O OG1 . THR D  1 132 ? 0.922   -30.573 88.636   1.00 31.30  ? 132 THR D OG1 1 
ATOM   13224 C CG2 . THR D  1 132 ? 1.252   -30.230 86.272   1.00 29.28  ? 132 THR D CG2 1 
ATOM   13225 N N   . LEU D  1 133 ? 4.167   -32.812 86.641   1.00 33.91  ? 133 LEU D N   1 
ATOM   13226 C CA  . LEU D  1 133 ? 5.166   -33.181 85.648   1.00 33.19  ? 133 LEU D CA  1 
ATOM   13227 C C   . LEU D  1 133 ? 5.037   -34.649 85.255   1.00 31.74  ? 133 LEU D C   1 
ATOM   13228 O O   . LEU D  1 133 ? 5.358   -35.020 84.117   1.00 29.91  ? 133 LEU D O   1 
ATOM   13229 C CB  . LEU D  1 133 ? 6.565   -32.865 86.175   1.00 30.68  ? 133 LEU D CB  1 
ATOM   13230 C CG  . LEU D  1 133 ? 6.903   -31.372 86.242   1.00 34.69  ? 133 LEU D CG  1 
ATOM   13231 C CD1 . LEU D  1 133 ? 8.256   -31.146 86.913   1.00 29.47  ? 133 LEU D CD1 1 
ATOM   13232 C CD2 . LEU D  1 133 ? 6.867   -30.741 84.854   1.00 34.59  ? 133 LEU D CD2 1 
ATOM   13233 N N   . ASN D  1 134 ? 4.543   -35.495 86.157   1.00 29.19  ? 134 ASN D N   1 
ATOM   13234 C CA  . ASN D  1 134 ? 4.245   -36.865 85.750   1.00 29.00  ? 134 ASN D CA  1 
ATOM   13235 C C   . ASN D  1 134 ? 3.124   -36.882 84.715   1.00 32.24  ? 134 ASN D C   1 
ATOM   13236 O O   . ASN D  1 134 ? 3.233   -37.554 83.682   1.00 35.19  ? 134 ASN D O   1 
ATOM   13237 C CB  . ASN D  1 134 ? 3.898   -37.722 86.968   1.00 36.55  ? 134 ASN D CB  1 
ATOM   13238 C CG  . ASN D  1 134 ? 5.115   -38.422 87.551   1.00 36.36  ? 134 ASN D CG  1 
ATOM   13239 O OD1 . ASN D  1 134 ? 5.588   -39.422 87.014   1.00 32.68  ? 134 ASN D OD1 1 
ATOM   13240 N ND2 . ASN D  1 134 ? 5.637   -37.886 88.645   1.00 40.18  ? 134 ASN D ND2 1 
ATOM   13241 N N   . LEU D  1 135 ? 2.061   -36.115 84.962   1.00 29.21  ? 135 LEU D N   1 
ATOM   13242 C CA  . LEU D  1 135 ? 1.028   -35.894 83.949   1.00 26.35  ? 135 LEU D CA  1 
ATOM   13243 C C   . LEU D  1 135 ? 1.625   -35.398 82.638   1.00 28.18  ? 135 LEU D C   1 
ATOM   13244 O O   . LEU D  1 135 ? 1.402   -35.991 81.576   1.00 23.07  ? 135 LEU D O   1 
ATOM   13245 C CB  . LEU D  1 135 ? 0.014   -34.872 84.462   1.00 27.30  ? 135 LEU D CB  1 
ATOM   13246 C CG  . LEU D  1 135 ? -1.041  -35.300 85.468   1.00 34.01  ? 135 LEU D CG  1 
ATOM   13247 C CD1 . LEU D  1 135 ? -2.093  -34.195 85.602   1.00 41.09  ? 135 LEU D CD1 1 
ATOM   13248 C CD2 . LEU D  1 135 ? -1.654  -36.582 84.983   1.00 32.06  ? 135 LEU D CD2 1 
ATOM   13249 N N   . LEU D  1 136 ? 2.366   -34.284 82.697   1.00 32.30  ? 136 LEU D N   1 
ATOM   13250 C CA  . LEU D  1 136 ? 2.857   -33.624 81.494   1.00 24.24  ? 136 LEU D CA  1 
ATOM   13251 C C   . LEU D  1 136 ? 3.879   -34.457 80.733   1.00 26.42  ? 136 LEU D C   1 
ATOM   13252 O O   . LEU D  1 136 ? 4.039   -34.279 79.510   1.00 23.29  ? 136 LEU D O   1 
ATOM   13253 C CB  . LEU D  1 136 ? 3.458   -32.279 81.871   1.00 28.07  ? 136 LEU D CB  1 
ATOM   13254 C CG  . LEU D  1 136 ? 2.432   -31.234 82.300   1.00 25.79  ? 136 LEU D CG  1 
ATOM   13255 C CD1 . LEU D  1 136 ? 3.133   -30.034 82.903   1.00 26.81  ? 136 LEU D CD1 1 
ATOM   13256 C CD2 . LEU D  1 136 ? 1.523   -30.823 81.092   1.00 25.43  ? 136 LEU D CD2 1 
ATOM   13257 N N   . ALA D  1 137 ? 4.601   -35.345 81.417   1.00 25.25  ? 137 ALA D N   1 
ATOM   13258 C CA  . ALA D  1 137 ? 5.548   -36.204 80.710   1.00 33.47  ? 137 ALA D CA  1 
ATOM   13259 C C   . ALA D  1 137 ? 4.845   -37.088 79.687   1.00 31.02  ? 137 ALA D C   1 
ATOM   13260 O O   . ALA D  1 137 ? 5.437   -37.455 78.673   1.00 31.04  ? 137 ALA D O   1 
ATOM   13261 C CB  . ALA D  1 137 ? 6.333   -37.061 81.700   1.00 32.61  ? 137 ALA D CB  1 
ATOM   13262 N N   . TRP D  1 138 ? 3.585   -37.427 79.933   1.00 30.39  ? 138 TRP D N   1 
ATOM   13263 C CA  . TRP D  1 138 ? 2.803   -38.299 79.072   1.00 27.62  ? 138 TRP D CA  1 
ATOM   13264 C C   . TRP D  1 138 ? 1.929   -37.517 78.098   1.00 28.13  ? 138 TRP D C   1 
ATOM   13265 O O   . TRP D  1 138 ? 1.025   -38.083 77.480   1.00 23.59  ? 138 TRP D O   1 
ATOM   13266 C CB  . TRP D  1 138 ? 1.960   -39.219 79.937   1.00 24.08  ? 138 TRP D CB  1 
ATOM   13267 C CG  . TRP D  1 138 ? 2.810   -40.170 80.690   1.00 26.53  ? 138 TRP D CG  1 
ATOM   13268 C CD1 . TRP D  1 138 ? 3.427   -39.959 81.894   1.00 29.87  ? 138 TRP D CD1 1 
ATOM   13269 C CD2 . TRP D  1 138 ? 3.191   -41.477 80.269   1.00 24.24  ? 138 TRP D CD2 1 
ATOM   13270 N NE1 . TRP D  1 138 ? 4.150   -41.078 82.261   1.00 25.97  ? 138 TRP D NE1 1 
ATOM   13271 C CE2 . TRP D  1 138 ? 4.011   -42.026 81.283   1.00 29.10  ? 138 TRP D CE2 1 
ATOM   13272 C CE3 . TRP D  1 138 ? 2.888   -42.259 79.151   1.00 21.93  ? 138 TRP D CE3 1 
ATOM   13273 C CZ2 . TRP D  1 138 ? 4.543   -43.312 81.197   1.00 23.47  ? 138 TRP D CZ2 1 
ATOM   13274 C CZ3 . TRP D  1 138 ? 3.421   -43.526 79.066   1.00 21.03  ? 138 TRP D CZ3 1 
ATOM   13275 C CH2 . TRP D  1 138 ? 4.237   -44.041 80.076   1.00 23.88  ? 138 TRP D CH2 1 
ATOM   13276 N N   . CYS D  1 139 ? 2.149   -36.261 77.938   1.00 22.29  ? 139 CYS D N   1 
ATOM   13277 C CA  . CYS D  1 139 ? 1.400   -35.471 77.021   1.00 24.73  ? 139 CYS D CA  1 
ATOM   13278 C C   . CYS D  1 139 ? 1.685   -35.836 75.595   1.00 24.32  ? 139 CYS D C   1 
ATOM   13279 O O   . CYS D  1 139 ? 2.757   -35.983 75.187   1.00 23.43  ? 139 CYS D O   1 
ATOM   13280 C CB  . CYS D  1 139 ? 1.700   -33.944 77.196   1.00 27.42  ? 139 CYS D CB  1 
ATOM   13281 S SG  . CYS D  1 139 ? 0.768   -32.815 76.247   1.00 34.03  ? 139 CYS D SG  1 
ATOM   13282 N N   . GLY D  1 140 ? 0.641   -35.996 74.902   1.00 25.07  ? 140 GLY D N   1 
ATOM   13283 C CA  . GLY D  1 140 ? 0.804   -36.207 73.529   1.00 24.59  ? 140 GLY D CA  1 
ATOM   13284 C C   . GLY D  1 140 ? 0.918   -35.044 72.574   1.00 35.02  ? 140 GLY D C   1 
ATOM   13285 O O   . GLY D  1 140 ? 0.665   -33.936 72.907   1.00 33.57  ? 140 GLY D O   1 
ATOM   13286 N N   . ARG D  1 141 ? 1.280   -35.358 71.340   1.00 54.72  ? 141 ARG D N   1 
ATOM   13287 C CA  . ARG D  1 141 ? 1.367   -34.402 70.266   1.00 30.18  ? 141 ARG D CA  1 
ATOM   13288 C C   . ARG D  1 141 ? 0.259   -33.431 70.167   1.00 21.17  ? 141 ARG D C   1 
ATOM   13289 O O   . ARG D  1 141 ? 0.543   -32.310 70.076   1.00 26.26  ? 141 ARG D O   1 
ATOM   13290 C CB  . ARG D  1 141 ? 1.487   -35.142 68.938   1.00 24.24  ? 141 ARG D CB  1 
ATOM   13291 C CG  . ARG D  1 141 ? 2.129   -34.301 67.846   1.00 26.74  ? 141 ARG D CG  1 
ATOM   13292 C CD  . ARG D  1 141 ? 2.262   -35.019 66.516   1.00 33.95  ? 141 ARG D CD  1 
ATOM   13293 N NE  . ARG D  1 141 ? 0.958   -35.134 65.927   1.00 41.77  ? 141 ARG D NE  1 
ATOM   13294 C CZ  . ARG D  1 141 ? 0.561   -34.577 64.795   1.00 36.07  ? 141 ARG D CZ  1 
ATOM   13295 N NH1 . ARG D  1 141 ? 1.373   -33.869 64.043   1.00 35.53  ? 141 ARG D NH1 1 
ATOM   13296 N NH2 . ARG D  1 141 ? -0.665  -34.754 64.421   1.00 35.38  ? 141 ARG D NH2 1 
ATOM   13297 N N   . THR D  1 142 ? -0.967  -33.887 70.200   1.00 21.03  ? 142 THR D N   1 
ATOM   13298 C CA  . THR D  1 142 ? -2.053  -32.921 69.974   1.00 24.75  ? 142 THR D CA  1 
ATOM   13299 C C   . THR D  1 142 ? -2.082  -31.855 71.060   1.00 28.23  ? 142 THR D C   1 
ATOM   13300 O O   . THR D  1 142 ? -2.158  -30.650 70.776   1.00 29.73  ? 142 THR D O   1 
ATOM   13301 C CB  . THR D  1 142 ? -3.411  -33.639 69.910   1.00 29.31  ? 142 THR D CB  1 
ATOM   13302 O OG1 . THR D  1 142 ? -3.431  -34.568 68.821   1.00 28.36  ? 142 THR D OG1 1 
ATOM   13303 C CG2 . THR D  1 142 ? -4.556  -32.642 69.727   1.00 31.60  ? 142 THR D CG2 1 
ATOM   13304 N N   . LEU D  1 143 ? -2.050  -32.284 72.318   1.00 32.43  ? 143 LEU D N   1 
ATOM   13305 C CA  . LEU D  1 143 ? -2.100  -31.356 73.433   1.00 33.73  ? 143 LEU D CA  1 
ATOM   13306 C C   . LEU D  1 143 ? -0.781  -30.636 73.683   1.00 32.04  ? 143 LEU D C   1 
ATOM   13307 O O   . LEU D  1 143 ? -0.772  -29.622 74.388   1.00 35.24  ? 143 LEU D O   1 
ATOM   13308 C CB  . LEU D  1 143 ? -2.524  -32.101 74.695   1.00 22.83  ? 143 LEU D CB  1 
ATOM   13309 C CG  . LEU D  1 143 ? -4.015  -32.407 74.808   1.00 27.35  ? 143 LEU D CG  1 
ATOM   13310 C CD1 . LEU D  1 143 ? -4.294  -33.074 76.163   1.00 23.01  ? 143 LEU D CD1 1 
ATOM   13311 C CD2 . LEU D  1 143 ? -4.812  -31.131 74.693   1.00 27.81  ? 143 LEU D CD2 1 
ATOM   13312 N N   . ARG D  1 144 ? 0.329   -31.125 73.137   1.00 40.10  ? 144 ARG D N   1 
ATOM   13313 C CA  . ARG D  1 144 ? 1.598   -30.445 73.359   1.00 44.71  ? 144 ARG D CA  1 
ATOM   13314 C C   . ARG D  1 144 ? 1.606   -29.017 72.822   1.00 49.86  ? 144 ARG D C   1 
ATOM   13315 O O   . ARG D  1 144 ? 2.538   -28.266 73.136   1.00 52.09  ? 144 ARG D O   1 
ATOM   13316 C CB  . ARG D  1 144 ? 2.742   -31.255 72.743   1.00 45.38  ? 144 ARG D CB  1 
ATOM   13317 C CG  . ARG D  1 144 ? 3.335   -32.310 73.692   1.00 45.37  ? 144 ARG D CG  1 
ATOM   13318 C CD  . ARG D  1 144 ? 4.482   -33.086 73.037   1.00 46.61  ? 144 ARG D CD  1 
ATOM   13319 N NE  . ARG D  1 144 ? 4.931   -34.219 73.843   1.00 47.90  ? 144 ARG D NE  1 
ATOM   13320 C CZ  . ARG D  1 144 ? 6.117   -34.284 74.447   1.00 49.38  ? 144 ARG D CZ  1 
ATOM   13321 N NH1 . ARG D  1 144 ? 6.980   -33.281 74.325   1.00 50.12  ? 144 ARG D NH1 1 
ATOM   13322 N NH2 . ARG D  1 144 ? 6.446   -35.351 75.170   1.00 45.82  ? 144 ARG D NH2 1 
ATOM   13323 N N   . LYS D  1 145 ? 0.593   -28.608 72.052   1.00 50.54  ? 145 LYS D N   1 
ATOM   13324 C CA  . LYS D  1 145 ? 0.488   -27.206 71.660   1.00 48.78  ? 145 LYS D CA  1 
ATOM   13325 C C   . LYS D  1 145 ? -0.393  -26.394 72.613   1.00 55.45  ? 145 LYS D C   1 
ATOM   13326 O O   . LYS D  1 145 ? -0.043  -25.258 72.963   1.00 58.73  ? 145 LYS D O   1 
ATOM   13327 C CB  . LYS D  1 145 ? -0.015  -27.108 70.216   1.00 52.23  ? 145 LYS D CB  1 
ATOM   13328 C CG  . LYS D  1 145 ? -1.432  -26.615 70.035   1.00 53.54  ? 145 LYS D CG  1 
ATOM   13329 C CD  . LYS D  1 145 ? -1.706  -26.256 68.582   1.00 55.30  ? 145 LYS D CD  1 
ATOM   13330 C CE  . LYS D  1 145 ? -3.178  -25.923 68.386   1.00 59.51  ? 145 LYS D CE  1 
ATOM   13331 N NZ  . LYS D  1 145 ? -3.656  -24.900 69.373   1.00 62.47  ? 145 LYS D NZ  1 
ATOM   13332 N N   . ASP D  1 146 ? -1.512  -26.957 73.081   1.00 51.10  ? 146 ASP D N   1 
ATOM   13333 C CA  . ASP D  1 146 ? -2.368  -26.223 74.007   1.00 49.25  ? 146 ASP D CA  1 
ATOM   13334 C C   . ASP D  1 146 ? -1.735  -26.126 75.391   1.00 47.62  ? 146 ASP D C   1 
ATOM   13335 O O   . ASP D  1 146 ? -2.014  -25.188 76.144   1.00 41.74  ? 146 ASP D O   1 
ATOM   13336 C CB  . ASP D  1 146 ? -3.731  -26.906 74.100   1.00 54.61  ? 146 ASP D CB  1 
ATOM   13337 C CG  . ASP D  1 146 ? -4.285  -27.307 72.736   1.00 59.33  ? 146 ASP D CG  1 
ATOM   13338 O OD1 . ASP D  1 146 ? -3.562  -27.976 71.954   1.00 53.13  ? 146 ASP D OD1 1 
ATOM   13339 O OD2 . ASP D  1 146 ? -5.458  -26.972 72.461   1.00 64.49  ? 146 ASP D OD2 1 
ATOM   13340 N N   . LEU D  1 147 ? -0.883  -27.082 75.744   1.00 44.17  ? 147 LEU D N   1 
ATOM   13341 C CA  . LEU D  1 147 ? -0.214  -27.086 77.034   1.00 41.34  ? 147 LEU D CA  1 
ATOM   13342 C C   . LEU D  1 147 ? 1.209   -26.548 76.943   1.00 43.47  ? 147 LEU D C   1 
ATOM   13343 O O   . LEU D  1 147 ? 2.024   -26.802 77.839   1.00 49.97  ? 147 LEU D O   1 
ATOM   13344 C CB  . LEU D  1 147 ? -0.238  -28.496 77.619   1.00 37.96  ? 147 LEU D CB  1 
ATOM   13345 C CG  . LEU D  1 147 ? -1.640  -29.109 77.674   1.00 38.07  ? 147 LEU D CG  1 
ATOM   13346 C CD1 . LEU D  1 147 ? -1.572  -30.559 78.114   1.00 36.05  ? 147 LEU D CD1 1 
ATOM   13347 C CD2 . LEU D  1 147 ? -2.543  -28.302 78.604   1.00 42.30  ? 147 LEU D CD2 1 
ATOM   13348 N N   . LYS D  1 148 ? 1.510   -25.783 75.888   1.00 39.73  ? 148 LYS D N   1 
ATOM   13349 C CA  . LYS D  1 148 ? 2.868   -25.297 75.665   1.00 39.10  ? 148 LYS D CA  1 
ATOM   13350 C C   . LYS D  1 148 ? 3.366   -24.419 76.809   1.00 38.50  ? 148 LYS D C   1 
ATOM   13351 O O   . LYS D  1 148 ? 4.523   -24.542 77.225   1.00 39.60  ? 148 LYS D O   1 
ATOM   13352 C CB  . LYS D  1 148 ? 2.939   -24.534 74.345   1.00 40.46  ? 148 LYS D CB  1 
ATOM   13353 C CG  . LYS D  1 148 ? 4.301   -23.906 74.086   1.00 43.74  ? 148 LYS D CG  1 
ATOM   13354 C CD  . LYS D  1 148 ? 4.546   -23.675 72.592   1.00 46.25  ? 148 LYS D CD  1 
ATOM   13355 C CE  . LYS D  1 148 ? 6.024   -23.413 72.308   1.00 46.14  ? 148 LYS D CE  1 
ATOM   13356 N NZ  . LYS D  1 148 ? 6.272   -23.125 70.864   1.00 45.83  ? 148 LYS D NZ  1 
ATOM   13357 N N   . ASP D  1 149 ? 2.515   -23.519 77.326   1.00 39.66  ? 149 ASP D N   1 
ATOM   13358 C CA  . ASP D  1 149 ? 2.933   -22.664 78.435   1.00 47.21  ? 149 ASP D CA  1 
ATOM   13359 C C   . ASP D  1 149 ? 3.132   -23.464 79.713   1.00 44.79  ? 149 ASP D C   1 
ATOM   13360 O O   . ASP D  1 149 ? 4.054   -23.180 80.490   1.00 43.19  ? 149 ASP D O   1 
ATOM   13361 C CB  . ASP D  1 149 ? 1.913   -21.555 78.678   1.00 54.99  ? 149 ASP D CB  1 
ATOM   13362 C CG  . ASP D  1 149 ? 1.744   -20.661 77.491   1.00 63.56  ? 149 ASP D CG  1 
ATOM   13363 O OD1 . ASP D  1 149 ? 2.761   -20.383 76.821   1.00 69.07  ? 149 ASP D OD1 1 
ATOM   13364 O OD2 . ASP D  1 149 ? 0.601   -20.233 77.230   1.00 64.93  ? 149 ASP D OD2 1 
ATOM   13365 N N   . LEU D  1 150 ? 2.261   -24.445 79.965   1.00 42.72  ? 150 LEU D N   1 
ATOM   13366 C CA  . LEU D  1 150 ? 2.433   -25.295 81.140   1.00 42.64  ? 150 LEU D CA  1 
ATOM   13367 C C   . LEU D  1 150 ? 3.642   -26.202 80.997   1.00 45.20  ? 150 LEU D C   1 
ATOM   13368 O O   . LEU D  1 150 ? 4.300   -26.522 81.997   1.00 49.56  ? 150 LEU D O   1 
ATOM   13369 C CB  . LEU D  1 150 ? 1.176   -26.135 81.374   1.00 42.25  ? 150 LEU D CB  1 
ATOM   13370 C CG  . LEU D  1 150 ? 0.006   -25.421 82.040   1.00 42.54  ? 150 LEU D CG  1 
ATOM   13371 C CD1 . LEU D  1 150 ? -1.228  -26.312 82.025   1.00 35.84  ? 150 LEU D CD1 1 
ATOM   13372 C CD2 . LEU D  1 150 ? 0.374   -24.999 83.475   1.00 45.61  ? 150 LEU D CD2 1 
ATOM   13373 N N   . LEU D  1 151 ? 3.933   -26.644 79.770   1.00 38.73  ? 151 LEU D N   1 
ATOM   13374 C CA  . LEU D  1 151 ? 5.098   -27.485 79.536   1.00 36.47  ? 151 LEU D CA  1 
ATOM   13375 C C   . LEU D  1 151 ? 6.393   -26.688 79.654   1.00 38.06  ? 151 LEU D C   1 
ATOM   13376 O O   . LEU D  1 151 ? 7.396   -27.205 80.159   1.00 42.20  ? 151 LEU D O   1 
ATOM   13377 C CB  . LEU D  1 151 ? 4.993   -28.147 78.158   1.00 38.64  ? 151 LEU D CB  1 
ATOM   13378 C CG  . LEU D  1 151 ? 4.130   -29.408 78.013   1.00 36.58  ? 151 LEU D CG  1 
ATOM   13379 C CD1 . LEU D  1 151 ? 3.788   -29.698 76.523   1.00 33.85  ? 151 LEU D CD1 1 
ATOM   13380 C CD2 . LEU D  1 151 ? 4.846   -30.580 78.619   1.00 32.46  ? 151 LEU D CD2 1 
ATOM   13381 N N   . ASN D  1 152 ? 6.400   -25.431 79.186   1.00 37.43  ? 152 ASN D N   1 
ATOM   13382 C CA  . ASN D  1 152 ? 7.606   -24.613 79.284   1.00 41.92  ? 152 ASN D CA  1 
ATOM   13383 C C   . ASN D  1 152 ? 7.774   -23.966 80.654   1.00 44.11  ? 152 ASN D C   1 
ATOM   13384 O O   . ASN D  1 152 ? 8.871   -23.495 80.972   1.00 46.59  ? 152 ASN D O   1 
ATOM   13385 C CB  . ASN D  1 152 ? 7.605   -23.517 78.225   1.00 44.36  ? 152 ASN D CB  1 
ATOM   13386 C CG  . ASN D  1 152 ? 7.663   -24.066 76.827   1.00 47.04  ? 152 ASN D CG  1 
ATOM   13387 O OD1 . ASN D  1 152 ? 8.208   -25.142 76.594   1.00 48.76  ? 152 ASN D OD1 1 
ATOM   13388 N ND2 . ASN D  1 152 ? 7.094   -23.328 75.880   1.00 47.28  ? 152 ASN D ND2 1 
ATOM   13389 N N   . LYS D  1 153 ? 6.704   -23.893 81.445   1.00 44.52  ? 153 LYS D N   1 
ATOM   13390 C CA  . LYS D  1 153 ? 6.828   -23.458 82.834   1.00 47.76  ? 153 LYS D CA  1 
ATOM   13391 C C   . LYS D  1 153 ? 7.804   -24.345 83.594   1.00 49.00  ? 153 LYS D C   1 
ATOM   13392 O O   . LYS D  1 153 ? 8.751   -23.856 84.223   1.00 54.35  ? 153 LYS D O   1 
ATOM   13393 C CB  . LYS D  1 153 ? 5.454   -23.478 83.496   1.00 46.88  ? 153 LYS D CB  1 
ATOM   13394 C CG  . LYS D  1 153 ? 5.380   -22.737 84.797   1.00 50.52  ? 153 LYS D CG  1 
ATOM   13395 C CD  . LYS D  1 153 ? 3.941   -22.614 85.241   1.00 50.92  ? 153 LYS D CD  1 
ATOM   13396 C CE  . LYS D  1 153 ? 3.856   -22.020 86.631   1.00 53.75  ? 153 LYS D CE  1 
ATOM   13397 N NZ  . LYS D  1 153 ? 2.456   -21.985 87.131   1.00 55.25  ? 153 LYS D NZ  1 
ATOM   13398 N N   . GLY D  1 154 ? 7.581   -25.659 83.553   1.00 46.90  ? 154 GLY D N   1 
ATOM   13399 C CA  . GLY D  1 154 ? 8.526   -26.619 84.077   1.00 46.62  ? 154 GLY D CA  1 
ATOM   13400 C C   . GLY D  1 154 ? 8.576   -26.740 85.583   1.00 45.82  ? 154 GLY D C   1 
ATOM   13401 O O   . GLY D  1 154 ? 9.183   -27.692 86.084   1.00 47.20  ? 154 GLY D O   1 
ATOM   13402 N N   . ARG D  1 155 ? 7.959   -25.821 86.323   1.00 43.30  ? 155 ARG D N   1 
ATOM   13403 C CA  . ARG D  1 155 ? 8.006   -25.860 87.776   1.00 46.54  ? 155 ARG D CA  1 
ATOM   13404 C C   . ARG D  1 155 ? 6.929   -24.942 88.331   1.00 48.60  ? 155 ARG D C   1 
ATOM   13405 O O   . ARG D  1 155 ? 6.379   -24.097 87.621   1.00 50.30  ? 155 ARG D O   1 
ATOM   13406 C CB  . ARG D  1 155 ? 9.388   -25.454 88.303   1.00 47.78  ? 155 ARG D CB  1 
ATOM   13407 C CG  . ARG D  1 155 ? 9.823   -24.049 87.925   1.00 50.47  ? 155 ARG D CG  1 
ATOM   13408 C CD  . ARG D  1 155 ? 11.185  -23.708 88.540   1.00 55.24  ? 155 ARG D CD  1 
ATOM   13409 N NE  . ARG D  1 155 ? 12.261  -24.528 87.987   1.00 60.58  ? 155 ARG D NE  1 
ATOM   13410 C CZ  . ARG D  1 155 ? 13.016  -25.363 88.697   1.00 64.33  ? 155 ARG D CZ  1 
ATOM   13411 N NH1 . ARG D  1 155 ? 13.971  -26.067 88.098   1.00 61.54  ? 155 ARG D NH1 1 
ATOM   13412 N NH2 . ARG D  1 155 ? 12.826  -25.490 90.006   1.00 70.33  ? 155 ARG D NH2 1 
ATOM   13413 N N   . ASN D  1 156 ? 6.622   -25.146 89.612   1.00 49.91  ? 156 ASN D N   1 
ATOM   13414 C CA  . ASN D  1 156 ? 5.708   -24.308 90.389   1.00 48.69  ? 156 ASN D CA  1 
ATOM   13415 C C   . ASN D  1 156 ? 4.279   -24.362 89.848   1.00 45.08  ? 156 ASN D C   1 
ATOM   13416 O O   . ASN D  1 156 ? 3.639   -23.343 89.591   1.00 47.43  ? 156 ASN D O   1 
ATOM   13417 C CB  . ASN D  1 156 ? 6.225   -22.872 90.464   1.00 50.61  ? 156 ASN D CB  1 
ATOM   13418 C CG  . ASN D  1 156 ? 7.505   -22.779 91.244   1.00 55.77  ? 156 ASN D CG  1 
ATOM   13419 O OD1 . ASN D  1 156 ? 8.496   -22.226 90.772   1.00 59.30  ? 156 ASN D OD1 1 
ATOM   13420 N ND2 . ASN D  1 156 ? 7.505   -23.353 92.442   1.00 60.32  ? 156 ASN D ND2 1 
ATOM   13421 N N   . TYR D  1 157 ? 3.770   -25.579 89.737   1.00 39.94  ? 157 TYR D N   1 
ATOM   13422 C CA  . TYR D  1 157 ? 2.412   -25.815 89.272   1.00 41.25  ? 157 TYR D CA  1 
ATOM   13423 C C   . TYR D  1 157 ? 1.422   -25.799 90.429   1.00 43.12  ? 157 TYR D C   1 
ATOM   13424 O O   . TYR D  1 157 ? 1.721   -26.253 91.535   1.00 43.63  ? 157 TYR D O   1 
ATOM   13425 C CB  . TYR D  1 157 ? 2.323   -27.157 88.561   1.00 40.01  ? 157 TYR D CB  1 
ATOM   13426 C CG  . TYR D  1 157 ? 3.177   -27.247 87.330   1.00 40.58  ? 157 TYR D CG  1 
ATOM   13427 C CD1 . TYR D  1 157 ? 2.699   -26.813 86.099   1.00 42.83  ? 157 TYR D CD1 1 
ATOM   13428 C CD2 . TYR D  1 157 ? 4.460   -27.781 87.395   1.00 38.22  ? 157 TYR D CD2 1 
ATOM   13429 C CE1 . TYR D  1 157 ? 3.479   -26.912 84.958   1.00 39.13  ? 157 TYR D CE1 1 
ATOM   13430 C CE2 . TYR D  1 157 ? 5.247   -27.881 86.275   1.00 38.27  ? 157 TYR D CE2 1 
ATOM   13431 C CZ  . TYR D  1 157 ? 4.753   -27.444 85.055   1.00 37.05  ? 157 TYR D CZ  1 
ATOM   13432 O OH  . TYR D  1 157 ? 5.537   -27.539 83.936   1.00 39.91  ? 157 TYR D OH  1 
ATOM   13433 N N   . THR D  1 158 ? 0.225   -25.294 90.153   1.00 40.97  ? 158 THR D N   1 
ATOM   13434 C CA  . THR D  1 158 ? -0.842  -25.226 91.136   1.00 36.58  ? 158 THR D CA  1 
ATOM   13435 C C   . THR D  1 158 ? -1.806  -26.392 90.970   1.00 36.35  ? 158 THR D C   1 
ATOM   13436 O O   . THR D  1 158 ? -1.842  -27.054 89.931   1.00 38.21  ? 158 THR D O   1 
ATOM   13437 C CB  . THR D  1 158 ? -1.619  -23.914 91.010   1.00 39.68  ? 158 THR D CB  1 
ATOM   13438 O OG1 . THR D  1 158 ? -2.307  -23.896 89.751   1.00 40.00  ? 158 THR D OG1 1 
ATOM   13439 C CG2 . THR D  1 158 ? -0.678  -22.715 91.121   1.00 36.24  ? 158 THR D CG2 1 
ATOM   13440 N N   . GLN D  1 159 ? -2.598  -26.632 92.022   1.00 34.26  ? 159 GLN D N   1 
ATOM   13441 C CA  . GLN D  1 159 ? -3.673  -27.618 91.943   1.00 35.58  ? 159 GLN D CA  1 
ATOM   13442 C C   . GLN D  1 159 ? -4.591  -27.344 90.752   1.00 33.54  ? 159 GLN D C   1 
ATOM   13443 O O   . GLN D  1 159 ? -4.992  -28.272 90.034   1.00 33.66  ? 159 GLN D O   1 
ATOM   13444 C CB  . GLN D  1 159 ? -4.464  -27.626 93.256   1.00 40.04  ? 159 GLN D CB  1 
ATOM   13445 C CG  . GLN D  1 159 ? -5.665  -28.558 93.267   1.00 43.11  ? 159 GLN D CG  1 
ATOM   13446 C CD  . GLN D  1 159 ? -5.265  -30.007 93.410   1.00 39.59  ? 159 GLN D CD  1 
ATOM   13447 O OE1 . GLN D  1 159 ? -4.156  -30.315 93.858   1.00 41.52  ? 159 GLN D OE1 1 
ATOM   13448 N NE2 . GLN D  1 159 ? -6.158  -30.914 93.015   1.00 36.15  ? 159 GLN D NE2 1 
ATOM   13449 N N   . GLU D  1 160 ? -4.915  -26.069 90.516   1.00 34.62  ? 160 GLU D N   1 
ATOM   13450 C CA  . GLU D  1 160 ? -5.822  -25.714 89.429   1.00 37.06  ? 160 GLU D CA  1 
ATOM   13451 C C   . GLU D  1 160 ? -5.230  -26.070 88.078   1.00 38.04  ? 160 GLU D C   1 
ATOM   13452 O O   . GLU D  1 160 ? -5.955  -26.469 87.161   1.00 39.45  ? 160 GLU D O   1 
ATOM   13453 C CB  . GLU D  1 160 ? -6.145  -24.219 89.478   1.00 34.84  ? 160 GLU D CB  1 
ATOM   13454 C CG  . GLU D  1 160 ? -7.513  -23.862 88.909   1.00 52.95  ? 160 GLU D CG  1 
ATOM   13455 C CD  . GLU D  1 160 ? -7.569  -22.456 88.325   1.00 68.73  ? 160 GLU D CD  1 
ATOM   13456 O OE1 . GLU D  1 160 ? -8.686  -21.908 88.168   1.00 74.35  ? 160 GLU D OE1 1 
ATOM   13457 O OE2 . GLU D  1 160 ? -6.494  -21.897 88.022   1.00 74.98  ? 160 GLU D OE2 1 
ATOM   13458 N N   . GLU D  1 161 ? -3.915  -25.909 87.928   1.00 37.57  ? 161 GLU D N   1 
ATOM   13459 C CA  . GLU D  1 161 ? -3.295  -26.204 86.642   1.00 40.72  ? 161 GLU D CA  1 
ATOM   13460 C C   . GLU D  1 161 ? -3.224  -27.706 86.411   1.00 37.11  ? 161 GLU D C   1 
ATOM   13461 O O   . GLU D  1 161 ? -3.429  -28.174 85.287   1.00 29.88  ? 161 GLU D O   1 
ATOM   13462 C CB  . GLU D  1 161 ? -1.907  -25.566 86.568   1.00 42.87  ? 161 GLU D CB  1 
ATOM   13463 C CG  . GLU D  1 161 ? -1.935  -24.035 86.550   1.00 44.90  ? 161 GLU D CG  1 
ATOM   13464 C CD  . GLU D  1 161 ? -0.553  -23.417 86.635   1.00 49.70  ? 161 GLU D CD  1 
ATOM   13465 O OE1 . GLU D  1 161 ? 0.361   -24.055 87.200   1.00 52.64  ? 161 GLU D OE1 1 
ATOM   13466 O OE2 . GLU D  1 161 ? -0.383  -22.282 86.149   1.00 52.24  ? 161 GLU D OE2 1 
ATOM   13467 N N   . LYS D  1 162 ? -2.967  -28.476 87.472   1.00 30.17  ? 162 LYS D N   1 
ATOM   13468 C CA  . LYS D  1 162 ? -2.985  -29.928 87.356   1.00 31.97  ? 162 LYS D CA  1 
ATOM   13469 C C   . LYS D  1 162 ? -4.386  -30.424 87.018   1.00 34.34  ? 162 LYS D C   1 
ATOM   13470 O O   . LYS D  1 162 ? -4.551  -31.375 86.241   1.00 31.71  ? 162 LYS D O   1 
ATOM   13471 C CB  . LYS D  1 162 ? -2.474  -30.564 88.661   1.00 33.77  ? 162 LYS D CB  1 
ATOM   13472 C CG  . LYS D  1 162 ? -2.639  -32.081 88.741   1.00 34.44  ? 162 LYS D CG  1 
ATOM   13473 C CD  . LYS D  1 162 ? -2.118  -32.643 90.071   1.00 31.30  ? 162 LYS D CD  1 
ATOM   13474 C CE  . LYS D  1 162 ? -2.806  -31.973 91.266   1.00 32.21  ? 162 LYS D CE  1 
ATOM   13475 N NZ  . LYS D  1 162 ? -2.767  -32.847 92.499   1.00 30.99  ? 162 LYS D NZ  1 
ATOM   13476 N N   . GLU D  1 163 ? -5.413  -29.781 87.582   1.00 32.17  ? 163 GLU D N   1 
ATOM   13477 C CA  . GLU D  1 163 ? -6.775  -30.177 87.256   1.00 32.05  ? 163 GLU D CA  1 
ATOM   13478 C C   . GLU D  1 163 ? -7.115  -29.829 85.815   1.00 34.21  ? 163 GLU D C   1 
ATOM   13479 O O   . GLU D  1 163 ? -7.898  -30.536 85.174   1.00 33.49  ? 163 GLU D O   1 
ATOM   13480 C CB  . GLU D  1 163 ? -7.762  -29.516 88.200   1.00 31.13  ? 163 GLU D CB  1 
ATOM   13481 C CG  . GLU D  1 163 ? -7.830  -30.222 89.544   1.00 38.35  ? 163 GLU D CG  1 
ATOM   13482 C CD  . GLU D  1 163 ? -8.388  -29.338 90.630   1.00 47.70  ? 163 GLU D CD  1 
ATOM   13483 O OE1 . GLU D  1 163 ? -8.408  -29.783 91.802   1.00 42.71  ? 163 GLU D OE1 1 
ATOM   13484 O OE2 . GLU D  1 163 ? -8.800  -28.196 90.306   1.00 53.79  ? 163 GLU D OE2 1 
ATOM   13485 N N   . TYR D  1 164 ? -6.538  -28.743 85.308   1.00 35.56  ? 164 TYR D N   1 
ATOM   13486 C CA  . TYR D  1 164 ? -6.780  -28.340 83.930   1.00 36.23  ? 164 TYR D CA  1 
ATOM   13487 C C   . TYR D  1 164 ? -6.183  -29.356 82.973   1.00 34.38  ? 164 TYR D C   1 
ATOM   13488 O O   . TYR D  1 164 ? -6.815  -29.747 81.983   1.00 31.94  ? 164 TYR D O   1 
ATOM   13489 C CB  . TYR D  1 164 ? -6.202  -26.943 83.690   1.00 37.71  ? 164 TYR D CB  1 
ATOM   13490 C CG  . TYR D  1 164 ? -6.275  -26.516 82.246   1.00 41.04  ? 164 TYR D CG  1 
ATOM   13491 C CD1 . TYR D  1 164 ? -7.464  -26.058 81.707   1.00 44.96  ? 164 TYR D CD1 1 
ATOM   13492 C CD2 . TYR D  1 164 ? -5.164  -26.598 81.416   1.00 44.21  ? 164 TYR D CD2 1 
ATOM   13493 C CE1 . TYR D  1 164 ? -7.549  -25.685 80.377   1.00 46.31  ? 164 TYR D CE1 1 
ATOM   13494 C CE2 . TYR D  1 164 ? -5.236  -26.223 80.090   1.00 46.68  ? 164 TYR D CE2 1 
ATOM   13495 C CZ  . TYR D  1 164 ? -6.433  -25.768 79.576   1.00 47.15  ? 164 TYR D CZ  1 
ATOM   13496 O OH  . TYR D  1 164 ? -6.519  -25.396 78.257   1.00 48.46  ? 164 TYR D OH  1 
ATOM   13497 N N   . VAL D  1 165 ? -4.961  -29.798 83.268   1.00 32.16  ? 165 VAL D N   1 
ATOM   13498 C CA  . VAL D  1 165 ? -4.331  -30.856 82.496   1.00 26.45  ? 165 VAL D CA  1 
ATOM   13499 C C   . VAL D  1 165 ? -5.177  -32.114 82.537   1.00 29.55  ? 165 VAL D C   1 
ATOM   13500 O O   . VAL D  1 165 ? -5.388  -32.769 81.508   1.00 28.42  ? 165 VAL D O   1 
ATOM   13501 C CB  . VAL D  1 165 ? -2.900  -31.106 83.006   1.00 26.30  ? 165 VAL D CB  1 
ATOM   13502 C CG1 . VAL D  1 165 ? -2.257  -32.292 82.276   1.00 26.48  ? 165 VAL D CG1 1 
ATOM   13503 C CG2 . VAL D  1 165 ? -2.077  -29.838 82.832   1.00 28.76  ? 165 VAL D CG2 1 
ATOM   13504 N N   . LEU D  1 166 ? -5.685  -32.473 83.721   1.00 27.55  ? 166 LEU D N   1 
ATOM   13505 C CA  . LEU D  1 166 ? -6.520  -33.661 83.818   1.00 28.22  ? 166 LEU D CA  1 
ATOM   13506 C C   . LEU D  1 166 ? -7.773  -33.527 82.966   1.00 26.23  ? 166 LEU D C   1 
ATOM   13507 O O   . LEU D  1 166 ? -8.201  -34.499 82.331   1.00 34.49  ? 166 LEU D O   1 
ATOM   13508 C CB  . LEU D  1 166 ? -6.895  -33.921 85.276   1.00 29.39  ? 166 LEU D CB  1 
ATOM   13509 C CG  . LEU D  1 166 ? -5.801  -34.608 86.090   1.00 33.05  ? 166 LEU D CG  1 
ATOM   13510 C CD1 . LEU D  1 166 ? -6.153  -34.613 87.584   1.00 37.26  ? 166 LEU D CD1 1 
ATOM   13511 C CD2 . LEU D  1 166 ? -5.540  -36.018 85.602   1.00 32.59  ? 166 LEU D CD2 1 
ATOM   13512 N N   . ASN D  1 167 ? -8.397  -32.345 82.979   1.00 28.04  ? 167 ASN D N   1 
ATOM   13513 C CA  . ASN D  1 167 ? -9.572  -32.104 82.148   1.00 31.17  ? 167 ASN D CA  1 
ATOM   13514 C C   . ASN D  1 167 ? -9.241  -32.306 80.674   1.00 28.25  ? 167 ASN D C   1 
ATOM   13515 O O   . ASN D  1 167 ? -9.995  -32.951 79.941   1.00 28.21  ? 167 ASN D O   1 
ATOM   13516 C CB  . ASN D  1 167 ? -10.112 -30.684 82.370   1.00 35.22  ? 167 ASN D CB  1 
ATOM   13517 C CG  . ASN D  1 167 ? -10.824 -30.513 83.711   1.00 49.29  ? 167 ASN D CG  1 
ATOM   13518 O OD1 . ASN D  1 167 ? -11.386 -31.463 84.262   1.00 52.07  ? 167 ASN D OD1 1 
ATOM   13519 N ND2 . ASN D  1 167 ? -10.815 -29.284 84.233   1.00 51.62  ? 167 ASN D ND2 1 
ATOM   13520 N N   . LYS D  1 168 ? -8.109  -31.761 80.225   1.00 26.09  ? 168 LYS D N   1 
ATOM   13521 C CA  . LYS D  1 168 ? -7.759  -31.880 78.809   1.00 28.28  ? 168 LYS D CA  1 
ATOM   13522 C C   . LYS D  1 168 ? -7.473  -33.329 78.434   1.00 27.72  ? 168 LYS D C   1 
ATOM   13523 O O   . LYS D  1 168 ? -7.817  -33.775 77.337   1.00 24.00  ? 168 LYS D O   1 
ATOM   13524 C CB  . LYS D  1 168 ? -6.560  -30.990 78.493   1.00 26.10  ? 168 LYS D CB  1 
ATOM   13525 C CG  . LYS D  1 168 ? -6.807  -29.503 78.740   1.00 28.94  ? 168 LYS D CG  1 
ATOM   13526 C CD  . LYS D  1 168 ? -7.985  -29.009 77.919   1.00 35.95  ? 168 LYS D CD  1 
ATOM   13527 C CE  . LYS D  1 168 ? -7.776  -29.241 76.432   1.00 40.62  ? 168 LYS D CE  1 
ATOM   13528 N NZ  . LYS D  1 168 ? -8.981  -28.772 75.711   1.00 41.04  ? 168 LYS D NZ  1 
ATOM   13529 N N   . TYR D  1 169 ? -6.869  -34.085 79.353   1.00 31.49  ? 169 TYR D N   1 
ATOM   13530 C CA  . TYR D  1 169 ? -6.542  -35.479 79.075   1.00 27.69  ? 169 TYR D CA  1 
ATOM   13531 C C   . TYR D  1 169 ? -7.802  -36.307 78.899   1.00 31.08  ? 169 TYR D C   1 
ATOM   13532 O O   . TYR D  1 169 ? -7.894  -37.121 77.973   1.00 32.55  ? 169 TYR D O   1 
ATOM   13533 C CB  . TYR D  1 169 ? -5.675  -36.042 80.203   1.00 27.85  ? 169 TYR D CB  1 
ATOM   13534 C CG  . TYR D  1 169 ? -4.215  -35.672 80.073   1.00 26.36  ? 169 TYR D CG  1 
ATOM   13535 C CD1 . TYR D  1 169 ? -3.794  -34.711 79.147   1.00 24.69  ? 169 TYR D CD1 1 
ATOM   13536 C CD2 . TYR D  1 169 ? -3.260  -36.286 80.865   1.00 25.61  ? 169 TYR D CD2 1 
ATOM   13537 C CE1 . TYR D  1 169 ? -2.463  -34.380 79.030   1.00 24.02  ? 169 TYR D CE1 1 
ATOM   13538 C CE2 . TYR D  1 169 ? -1.936  -35.968 80.758   1.00 25.38  ? 169 TYR D CE2 1 
ATOM   13539 C CZ  . TYR D  1 169 ? -1.533  -35.029 79.838   1.00 25.09  ? 169 TYR D CZ  1 
ATOM   13540 O OH  . TYR D  1 169 ? -0.193  -34.726 79.759   1.00 27.46  ? 169 TYR D OH  1 
ATOM   13541 N N   . PHE D  1 170 ? -8.791  -36.109 79.783   1.00 31.96  ? 170 PHE D N   1 
ATOM   13542 C CA  . PHE D  1 170 ? -10.041 -36.850 79.658   1.00 31.10  ? 170 PHE D CA  1 
ATOM   13543 C C   . PHE D  1 170 ? -10.810 -36.443 78.411   1.00 30.07  ? 170 PHE D C   1 
ATOM   13544 O O   . PHE D  1 170 ? -11.540 -37.263 77.846   1.00 32.40  ? 170 PHE D O   1 
ATOM   13545 C CB  . PHE D  1 170 ? -10.899 -36.682 80.915   1.00 25.28  ? 170 PHE D CB  1 
ATOM   13546 C CG  . PHE D  1 170 ? -10.505 -37.637 82.010   1.00 25.37  ? 170 PHE D CG  1 
ATOM   13547 C CD1 . PHE D  1 170 ? -10.695 -39.002 81.839   1.00 28.99  ? 170 PHE D CD1 1 
ATOM   13548 C CD2 . PHE D  1 170 ? -9.870  -37.196 83.159   1.00 31.34  ? 170 PHE D CD2 1 
ATOM   13549 C CE1 . PHE D  1 170 ? -10.297 -39.923 82.815   1.00 25.59  ? 170 PHE D CE1 1 
ATOM   13550 C CE2 . PHE D  1 170 ? -9.459  -38.111 84.149   1.00 31.32  ? 170 PHE D CE2 1 
ATOM   13551 C CZ  . PHE D  1 170 ? -9.677  -39.468 83.982   1.00 27.07  ? 170 PHE D CZ  1 
ATOM   13552 N N   . GLU D  1 171 ? -10.668 -35.193 77.970   1.00 35.79  ? 171 GLU D N   1 
ATOM   13553 C CA  . GLU D  1 171 ? -11.242 -34.800 76.683   1.00 36.54  ? 171 GLU D CA  1 
ATOM   13554 C C   . GLU D  1 171 ? -10.640 -35.620 75.552   1.00 33.74  ? 171 GLU D C   1 
ATOM   13555 O O   . GLU D  1 171 ? -11.338 -36.010 74.603   1.00 32.58  ? 171 GLU D O   1 
ATOM   13556 C CB  . GLU D  1 171 ? -11.003 -33.318 76.421   1.00 37.81  ? 171 GLU D CB  1 
ATOM   13557 C CG  . GLU D  1 171 ? -11.750 -32.356 77.321   1.00 48.49  ? 171 GLU D CG  1 
ATOM   13558 C CD  . GLU D  1 171 ? -11.450 -30.911 76.944   1.00 52.10  ? 171 GLU D CD  1 
ATOM   13559 O OE1 . GLU D  1 171 ? -10.793 -30.713 75.899   1.00 52.15  ? 171 GLU D OE1 1 
ATOM   13560 O OE2 . GLU D  1 171 ? -11.867 -29.984 77.671   1.00 54.05  ? 171 GLU D OE2 1 
ATOM   13561 N N   . ILE D  1 172 ? -9.332  -35.866 75.623   1.00 25.36  ? 172 ILE D N   1 
ATOM   13562 C CA  . ILE D  1 172 ? -8.656  -36.635 74.594   1.00 22.35  ? 172 ILE D CA  1 
ATOM   13563 C C   . ILE D  1 172 ? -9.112  -38.090 74.633   1.00 28.07  ? 172 ILE D C   1 
ATOM   13564 O O   . ILE D  1 172 ? -9.360  -38.713 73.588   1.00 26.80  ? 172 ILE D O   1 
ATOM   13565 C CB  . ILE D  1 172 ? -7.129  -36.503 74.761   1.00 25.71  ? 172 ILE D CB  1 
ATOM   13566 C CG1 . ILE D  1 172 ? -6.632  -35.170 74.194   1.00 28.92  ? 172 ILE D CG1 1 
ATOM   13567 C CG2 . ILE D  1 172 ? -6.404  -37.638 74.080   1.00 26.58  ? 172 ILE D CG2 1 
ATOM   13568 C CD1 . ILE D  1 172 ? -6.659  -35.086 72.640   1.00 30.88  ? 172 ILE D CD1 1 
ATOM   13569 N N   . ILE D  1 173 ? -9.244  -38.649 75.836   1.00 23.06  ? 173 ILE D N   1 
ATOM   13570 C CA  . ILE D  1 173 ? -9.755  -40.011 75.980   1.00 26.39  ? 173 ILE D CA  1 
ATOM   13571 C C   . ILE D  1 173 ? -11.174 -40.108 75.436   1.00 28.62  ? 173 ILE D C   1 
ATOM   13572 O O   . ILE D  1 173 ? -11.541 -41.094 74.779   1.00 32.43  ? 173 ILE D O   1 
ATOM   13573 C CB  . ILE D  1 173 ? -9.690  -40.450 77.459   1.00 27.59  ? 173 ILE D CB  1 
ATOM   13574 C CG1 . ILE D  1 173 ? -8.230  -40.534 77.929   1.00 22.07  ? 173 ILE D CG1 1 
ATOM   13575 C CG2 . ILE D  1 173 ? -10.443 -41.757 77.659   1.00 23.56  ? 173 ILE D CG2 1 
ATOM   13576 C CD1 . ILE D  1 173 ? -8.069  -41.015 79.403   1.00 23.56  ? 173 ILE D CD1 1 
ATOM   13577 N N   . LYS D  1 174 ? -11.991 -39.087 75.700   1.00 23.27  ? 174 LYS D N   1 
ATOM   13578 C CA  . LYS D  1 174 ? -13.376 -39.097 75.241   1.00 23.95  ? 174 LYS D CA  1 
ATOM   13579 C C   . LYS D  1 174 ? -13.470 -39.103 73.721   1.00 26.57  ? 174 LYS D C   1 
ATOM   13580 O O   . LYS D  1 174 ? -14.484 -39.542 73.161   1.00 29.33  ? 174 LYS D O   1 
ATOM   13581 C CB  . LYS D  1 174 ? -14.116 -37.881 75.793   1.00 25.15  ? 174 LYS D CB  1 
ATOM   13582 C CG  . LYS D  1 174 ? -14.609 -38.021 77.240   1.00 27.85  ? 174 LYS D CG  1 
ATOM   13583 C CD  . LYS D  1 174 ? -15.472 -36.797 77.634   1.00 39.20  ? 174 LYS D CD  1 
ATOM   13584 C CE  . LYS D  1 174 ? -15.850 -36.821 79.106   1.00 49.47  ? 174 LYS D CE  1 
ATOM   13585 N NZ  . LYS D  1 174 ? -16.497 -35.555 79.552   1.00 54.90  ? 174 LYS D NZ  1 
ATOM   13586 N N   . LYS D  1 175 ? -12.450 -38.592 73.039   1.00 25.52  ? 175 LYS D N   1 
ATOM   13587 C CA  . LYS D  1 175 ? -12.483 -38.506 71.589   1.00 29.51  ? 175 LYS D CA  1 
ATOM   13588 C C   . LYS D  1 175 ? -11.738 -39.656 70.924   1.00 32.01  ? 175 LYS D C   1 
ATOM   13589 O O   . LYS D  1 175 ? -11.564 -39.649 69.702   1.00 36.61  ? 175 LYS D O   1 
ATOM   13590 C CB  . LYS D  1 175 ? -11.924 -37.149 71.137   1.00 29.51  ? 175 LYS D CB  1 
ATOM   13591 C CG  . LYS D  1 175 ? -12.713 -35.985 71.679   1.00 38.23  ? 175 LYS D CG  1 
ATOM   13592 C CD  . LYS D  1 175 ? -12.197 -34.631 71.202   1.00 47.52  ? 175 LYS D CD  1 
ATOM   13593 C CE  . LYS D  1 175 ? -12.957 -33.502 71.902   1.00 53.56  ? 175 LYS D CE  1 
ATOM   13594 N NZ  . LYS D  1 175 ? -12.816 -32.177 71.232   1.00 56.43  ? 175 LYS D NZ  1 
ATOM   13595 N N   . THR D  1 176 ? -11.335 -40.668 71.687   1.00 28.47  ? 176 THR D N   1 
ATOM   13596 C CA  . THR D  1 176 ? -10.404 -41.652 71.139   1.00 27.85  ? 176 THR D CA  1 
ATOM   13597 C C   . THR D  1 176 ? -11.096 -42.650 70.215   1.00 31.33  ? 176 THR D C   1 
ATOM   13598 O O   . THR D  1 176 ? -10.656 -42.864 69.082   1.00 29.11  ? 176 THR D O   1 
ATOM   13599 C CB  . THR D  1 176 ? -9.689  -42.368 72.269   1.00 28.48  ? 176 THR D CB  1 
ATOM   13600 O OG1 . THR D  1 176 ? -8.848  -41.419 72.929   1.00 28.23  ? 176 THR D OG1 1 
ATOM   13601 C CG2 . THR D  1 176 ? -8.849  -43.530 71.727   1.00 24.68  ? 176 THR D CG2 1 
ATOM   13602 N N   . LEU D  1 177 ? -12.182 -43.267 70.668   1.00 26.74  ? 177 LEU D N   1 
ATOM   13603 C CA  . LEU D  1 177 ? -12.839 -44.236 69.799   1.00 26.41  ? 177 LEU D CA  1 
ATOM   13604 C C   . LEU D  1 177 ? -13.440 -43.552 68.584   1.00 23.78  ? 177 LEU D C   1 
ATOM   13605 O O   . LEU D  1 177 ? -13.559 -44.170 67.518   1.00 25.17  ? 177 LEU D O   1 
ATOM   13606 C CB  . LEU D  1 177 ? -13.908 -45.006 70.579   1.00 28.44  ? 177 LEU D CB  1 
ATOM   13607 C CG  . LEU D  1 177 ? -13.348 -45.896 71.693   1.00 27.12  ? 177 LEU D CG  1 
ATOM   13608 C CD1 . LEU D  1 177 ? -14.484 -46.597 72.403   1.00 29.03  ? 177 LEU D CD1 1 
ATOM   13609 C CD2 . LEU D  1 177 ? -12.353 -46.913 71.133   1.00 23.09  ? 177 LEU D CD2 1 
ATOM   13610 N N   . SER D  1 178 ? -13.806 -42.274 68.725   1.00 22.40  ? 178 SER D N   1 
ATOM   13611 C CA  . SER D  1 178 ? -14.344 -41.524 67.601   1.00 22.83  ? 178 SER D CA  1 
ATOM   13612 C C   . SER D  1 178 ? -13.290 -41.324 66.530   1.00 26.43  ? 178 SER D C   1 
ATOM   13613 O O   . SER D  1 178 ? -13.603 -41.356 65.333   1.00 27.93  ? 178 SER D O   1 
ATOM   13614 C CB  . SER D  1 178 ? -14.880 -40.173 68.067   1.00 34.93  ? 178 SER D CB  1 
ATOM   13615 O OG  . SER D  1 178 ? -16.190 -40.317 68.582   1.00 40.12  ? 178 SER D OG  1 
ATOM   13616 N N   . ILE D  1 179 ? -12.034 -41.118 66.920   1.00 21.54  ? 179 ILE D N   1 
ATOM   13617 C CA  . ILE D  1 179 ? -11.090 -40.823 65.850   1.00 22.50  ? 179 ILE D CA  1 
ATOM   13618 C C   . ILE D  1 179 ? -10.777 -42.092 65.066   1.00 27.60  ? 179 ILE D C   1 
ATOM   13619 O O   . ILE D  1 179 ? -10.535 -42.031 63.851   1.00 25.94  ? 179 ILE D O   1 
ATOM   13620 C CB  . ILE D  1 179 ? -9.821  -40.111 66.353   1.00 25.21  ? 179 ILE D CB  1 
ATOM   13621 C CG1 . ILE D  1 179 ? -9.018  -39.611 65.139   1.00 34.96  ? 179 ILE D CG1 1 
ATOM   13622 C CG2 . ILE D  1 179 ? -8.966  -41.033 67.165   1.00 29.24  ? 179 ILE D CG2 1 
ATOM   13623 C CD1 . ILE D  1 179 ? -8.231  -38.356 65.389   1.00 40.86  ? 179 ILE D CD1 1 
ATOM   13624 N N   . TYR D  1 180 ? -10.826 -43.259 65.721   1.00 22.15  ? 180 TYR D N   1 
ATOM   13625 C CA  . TYR D  1 180 ? -10.686 -44.516 64.990   1.00 21.09  ? 180 TYR D CA  1 
ATOM   13626 C C   . TYR D  1 180 ? -11.862 -44.742 64.055   1.00 24.31  ? 180 TYR D C   1 
ATOM   13627 O O   . TYR D  1 180 ? -11.667 -45.179 62.916   1.00 24.77  ? 180 TYR D O   1 
ATOM   13628 C CB  . TYR D  1 180 ? -10.538 -45.701 65.950   1.00 20.26  ? 180 TYR D CB  1 
ATOM   13629 C CG  . TYR D  1 180 ? -9.188  -45.741 66.617   1.00 23.84  ? 180 TYR D CG  1 
ATOM   13630 C CD1 . TYR D  1 180 ? -8.076  -46.283 65.968   1.00 22.20  ? 180 TYR D CD1 1 
ATOM   13631 C CD2 . TYR D  1 180 ? -9.015  -45.214 67.896   1.00 25.34  ? 180 TYR D CD2 1 
ATOM   13632 C CE1 . TYR D  1 180 ? -6.833  -46.302 66.583   1.00 24.59  ? 180 TYR D CE1 1 
ATOM   13633 C CE2 . TYR D  1 180 ? -7.786  -45.241 68.516   1.00 22.73  ? 180 TYR D CE2 1 
ATOM   13634 C CZ  . TYR D  1 180 ? -6.703  -45.778 67.864   1.00 22.20  ? 180 TYR D CZ  1 
ATOM   13635 O OH  . TYR D  1 180 ? -5.474  -45.769 68.485   1.00 17.74  ? 180 TYR D OH  1 
ATOM   13636 N N   . ARG D  1 181 ? -13.092 -44.486 64.521   1.00 24.79  ? 181 ARG D N   1 
ATOM   13637 C CA  . ARG D  1 181 ? -14.238 -44.558 63.616   1.00 24.02  ? 181 ARG D CA  1 
ATOM   13638 C C   . ARG D  1 181 ? -14.040 -43.630 62.430   1.00 29.45  ? 181 ARG D C   1 
ATOM   13639 O O   . ARG D  1 181 ? -14.353 -43.987 61.283   1.00 27.73  ? 181 ARG D O   1 
ATOM   13640 C CB  . ARG D  1 181 ? -15.534 -44.169 64.332   1.00 25.51  ? 181 ARG D CB  1 
ATOM   13641 C CG  . ARG D  1 181 ? -16.118 -45.176 65.331   1.00 32.23  ? 181 ARG D CG  1 
ATOM   13642 C CD  . ARG D  1 181 ? -17.516 -44.694 65.794   1.00 32.03  ? 181 ARG D CD  1 
ATOM   13643 N NE  . ARG D  1 181 ? -18.084 -45.529 66.851   1.00 39.61  ? 181 ARG D NE  1 
ATOM   13644 C CZ  . ARG D  1 181 ? -17.997 -45.266 68.153   1.00 45.57  ? 181 ARG D CZ  1 
ATOM   13645 N NH1 . ARG D  1 181 ? -17.348 -44.190 68.581   1.00 45.05  ? 181 ARG D NH1 1 
ATOM   13646 N NH2 . ARG D  1 181 ? -18.554 -46.089 69.034   1.00 49.11  ? 181 ARG D NH2 1 
ATOM   13647 N N   . GLU D  1 182 ? -13.554 -42.414 62.700   1.00 29.66  ? 182 GLU D N   1 
ATOM   13648 C CA  . GLU D  1 182 ? -13.419 -41.414 61.654   1.00 30.33  ? 182 GLU D CA  1 
ATOM   13649 C C   . GLU D  1 182 ? -12.441 -41.876 60.576   1.00 28.16  ? 182 GLU D C   1 
ATOM   13650 O O   . GLU D  1 182 ? -12.764 -41.844 59.383   1.00 25.68  ? 182 GLU D O   1 
ATOM   13651 C CB  . GLU D  1 182 ? -12.992 -40.068 62.260   1.00 33.47  ? 182 GLU D CB  1 
ATOM   13652 C CG  . GLU D  1 182 ? -14.137 -39.305 62.936   1.00 42.08  ? 182 GLU D CG  1 
ATOM   13653 C CD  . GLU D  1 182 ? -13.667 -38.263 63.951   1.00 51.90  ? 182 GLU D CD  1 
ATOM   13654 O OE1 . GLU D  1 182 ? -14.513 -37.762 64.735   1.00 52.93  ? 182 GLU D OE1 1 
ATOM   13655 O OE2 . GLU D  1 182 ? -12.459 -37.937 63.957   1.00 54.29  ? 182 GLU D OE2 1 
ATOM   13656 N N   . ILE D  1 183 ? -11.240 -42.309 60.970   1.00 25.06  ? 183 ILE D N   1 
ATOM   13657 C CA  . ILE D  1 183 ? -10.255 -42.680 59.955   1.00 29.38  ? 183 ILE D CA  1 
ATOM   13658 C C   . ILE D  1 183 ? -10.651 -43.974 59.257   1.00 30.19  ? 183 ILE D C   1 
ATOM   13659 O O   . ILE D  1 183 ? -10.273 -44.195 58.098   1.00 33.55  ? 183 ILE D O   1 
ATOM   13660 C CB  . ILE D  1 183 ? -8.834  -42.769 60.552   1.00 30.56  ? 183 ILE D CB  1 
ATOM   13661 C CG1 . ILE D  1 183 ? -8.721  -43.913 61.558   1.00 31.69  ? 183 ILE D CG1 1 
ATOM   13662 C CG2 . ILE D  1 183 ? -8.447  -41.443 61.203   1.00 27.10  ? 183 ILE D CG2 1 
ATOM   13663 C CD1 . ILE D  1 183 ? -7.885  -45.053 61.078   1.00 31.00  ? 183 ILE D CD1 1 
ATOM   13664 N N   . LYS D  1 184 ? -11.470 -44.802 59.901   1.00 24.73  ? 184 LYS D N   1 
ATOM   13665 C CA  . LYS D  1 184 ? -11.984 -45.983 59.226   1.00 25.25  ? 184 LYS D CA  1 
ATOM   13666 C C   . LYS D  1 184 ? -12.975 -45.595 58.141   1.00 29.41  ? 184 LYS D C   1 
ATOM   13667 O O   . LYS D  1 184 ? -12.874 -46.050 56.992   1.00 24.82  ? 184 LYS D O   1 
ATOM   13668 C CB  . LYS D  1 184 ? -12.640 -46.912 60.244   1.00 29.69  ? 184 LYS D CB  1 
ATOM   13669 C CG  . LYS D  1 184 ? -13.163 -48.191 59.642   1.00 34.42  ? 184 LYS D CG  1 
ATOM   13670 C CD  . LYS D  1 184 ? -13.983 -48.956 60.655   1.00 37.76  ? 184 LYS D CD  1 
ATOM   13671 C CE  . LYS D  1 184 ? -14.785 -50.067 59.991   1.00 41.24  ? 184 LYS D CE  1 
ATOM   13672 N NZ  . LYS D  1 184 ? -13.913 -51.131 59.412   1.00 43.90  ? 184 LYS D NZ  1 
ATOM   13673 N N   . GLU D  1 185 ? -13.949 -44.749 58.497   1.00 33.26  ? 185 GLU D N   1 
ATOM   13674 C CA  . GLU D  1 185 ? -14.989 -44.357 57.560   1.00 33.39  ? 185 GLU D CA  1 
ATOM   13675 C C   . GLU D  1 185 ? -14.417 -43.533 56.414   1.00 33.72  ? 185 GLU D C   1 
ATOM   13676 O O   . GLU D  1 185 ? -14.900 -43.626 55.278   1.00 33.26  ? 185 GLU D O   1 
ATOM   13677 C CB  . GLU D  1 185 ? -16.082 -43.576 58.291   1.00 37.10  ? 185 GLU D CB  1 
ATOM   13678 C CG  . GLU D  1 185 ? -16.783 -44.359 59.395   1.00 44.92  ? 185 GLU D CG  1 
ATOM   13679 C CD  . GLU D  1 185 ? -17.636 -45.504 58.866   1.00 52.46  ? 185 GLU D CD  1 
ATOM   13680 O OE1 . GLU D  1 185 ? -18.763 -45.237 58.397   1.00 54.91  ? 185 GLU D OE1 1 
ATOM   13681 O OE2 . GLU D  1 185 ? -17.179 -46.669 58.911   1.00 54.94  ? 185 GLU D OE2 1 
ATOM   13682 N N   . GLU D  1 186 ? -13.406 -42.708 56.693   1.00 27.86  ? 186 GLU D N   1 
ATOM   13683 C CA  . GLU D  1 186 ? -12.756 -41.929 55.645   1.00 32.66  ? 186 GLU D CA  1 
ATOM   13684 C C   . GLU D  1 186 ? -11.746 -42.748 54.855   1.00 33.80  ? 186 GLU D C   1 
ATOM   13685 O O   . GLU D  1 186 ? -11.058 -42.188 54.002   1.00 38.51  ? 186 GLU D O   1 
ATOM   13686 C CB  . GLU D  1 186 ? -12.074 -40.692 56.244   1.00 33.98  ? 186 GLU D CB  1 
ATOM   13687 C CG  . GLU D  1 186 ? -13.040 -39.721 56.911   1.00 41.89  ? 186 GLU D CG  1 
ATOM   13688 C CD  . GLU D  1 186 ? -12.355 -38.810 57.913   1.00 47.62  ? 186 GLU D CD  1 
ATOM   13689 O OE1 . GLU D  1 186 ? -11.105 -38.793 57.940   1.00 48.94  ? 186 GLU D OE1 1 
ATOM   13690 O OE2 . GLU D  1 186 ? -13.066 -38.139 58.694   1.00 47.78  ? 186 GLU D OE2 1 
ATOM   13691 N N   . GLY D  1 187 ? -11.627 -44.047 55.132   1.00 31.76  ? 187 GLY D N   1 
ATOM   13692 C CA  . GLY D  1 187 ? -10.670 -44.884 54.440   1.00 28.56  ? 187 GLY D CA  1 
ATOM   13693 C C   . GLY D  1 187 ? -9.244  -44.401 54.511   1.00 30.19  ? 187 GLY D C   1 
ATOM   13694 O O   . GLY D  1 187 ? -8.459  -44.680 53.601   1.00 28.89  ? 187 GLY D O   1 
ATOM   13695 N N   . LYS D  1 188 ? -8.875  -43.664 55.564   1.00 22.94  ? 188 LYS D N   1 
ATOM   13696 C CA  . LYS D  1 188 ? -7.463  -43.355 55.748   1.00 23.77  ? 188 LYS D CA  1 
ATOM   13697 C C   . LYS D  1 188 ? -6.704  -44.511 56.369   1.00 27.66  ? 188 LYS D C   1 
ATOM   13698 O O   . LYS D  1 188 ? -5.472  -44.464 56.428   1.00 24.09  ? 188 LYS D O   1 
ATOM   13699 C CB  . LYS D  1 188 ? -7.280  -42.114 56.618   1.00 26.95  ? 188 LYS D CB  1 
ATOM   13700 C CG  . LYS D  1 188 ? -8.061  -40.894 56.109   1.00 26.71  ? 188 LYS D CG  1 
ATOM   13701 C CD  . LYS D  1 188 ? -7.551  -39.578 56.687   1.00 34.12  ? 188 LYS D CD  1 
ATOM   13702 C CE  . LYS D  1 188 ? -8.102  -38.403 55.885   1.00 35.93  ? 188 LYS D CE  1 
ATOM   13703 N NZ  . LYS D  1 188 ? -7.586  -38.398 54.459   1.00 42.26  ? 188 LYS D NZ  1 
ATOM   13704 N N   . GLY D  1 189 ? -7.414  -45.523 56.853   1.00 29.99  ? 189 GLY D N   1 
ATOM   13705 C CA  . GLY D  1 189 ? -6.808  -46.632 57.554   1.00 27.14  ? 189 GLY D CA  1 
ATOM   13706 C C   . GLY D  1 189 ? -7.824  -47.714 57.824   1.00 28.57  ? 189 GLY D C   1 
ATOM   13707 O O   . GLY D  1 189 ? -9.021  -47.436 57.942   1.00 29.23  ? 189 GLY D O   1 
ATOM   13708 N N   . SER D  1 190 ? -7.367  -48.956 57.886   1.00 24.94  ? 190 SER D N   1 
ATOM   13709 C CA  . SER D  1 190 ? -8.211  -50.044 58.333   1.00 22.30  ? 190 SER D CA  1 
ATOM   13710 C C   . SER D  1 190 ? -7.966  -50.255 59.827   1.00 18.63  ? 190 SER D C   1 
ATOM   13711 O O   . SER D  1 190 ? -6.880  -49.970 60.333   1.00 25.33  ? 190 SER D O   1 
ATOM   13712 C CB  . SER D  1 190 ? -7.933  -51.306 57.516   1.00 23.04  ? 190 SER D CB  1 
ATOM   13713 O OG  . SER D  1 190 ? -8.340  -51.117 56.159   1.00 28.32  ? 190 SER D OG  1 
ATOM   13714 N N   . VAL D  1 191 ? -9.010  -50.652 60.545   1.00 24.32  ? 191 VAL D N   1 
ATOM   13715 C CA  . VAL D  1 191 ? -8.909  -50.960 61.976   1.00 22.08  ? 191 VAL D CA  1 
ATOM   13716 C C   . VAL D  1 191 ? -9.229  -52.441 62.141   1.00 21.49  ? 191 VAL D C   1 
ATOM   13717 O O   . VAL D  1 191 ? -10.311 -52.891 61.746   1.00 27.95  ? 191 VAL D O   1 
ATOM   13718 C CB  . VAL D  1 191 ? -9.845  -50.093 62.846   1.00 21.39  ? 191 VAL D CB  1 
ATOM   13719 C CG1 . VAL D  1 191 ? -9.718  -50.503 64.319   1.00 24.29  ? 191 VAL D CG1 1 
ATOM   13720 C CG2 . VAL D  1 191 ? -9.535  -48.592 62.725   1.00 22.27  ? 191 VAL D CG2 1 
ATOM   13721 N N   . SER D  1 192 ? -8.287  -53.203 62.686   1.00 21.30  ? 192 SER D N   1 
ATOM   13722 C CA  . SER D  1 192 ? -8.522  -54.600 63.016   1.00 18.50  ? 192 SER D CA  1 
ATOM   13723 C C   . SER D  1 192 ? -8.781  -54.744 64.517   1.00 24.02  ? 192 SER D C   1 
ATOM   13724 O O   . SER D  1 192 ? -8.702  -53.778 65.280   1.00 21.71  ? 192 SER D O   1 
ATOM   13725 C CB  . SER D  1 192 ? -7.336  -55.470 62.601   1.00 20.11  ? 192 SER D CB  1 
ATOM   13726 O OG  . SER D  1 192 ? -6.152  -55.090 63.306   1.00 19.38  ? 192 SER D OG  1 
ATOM   13727 N N   . THR D  1 193 ? -9.099  -55.971 64.946   1.00 19.73  ? 193 THR D N   1 
ATOM   13728 C CA  . THR D  1 193 ? -9.085  -56.293 66.372   1.00 22.40  ? 193 THR D CA  1 
ATOM   13729 C C   . THR D  1 193 ? -8.405  -57.646 66.571   1.00 25.96  ? 193 THR D C   1 
ATOM   13730 O O   . THR D  1 193 ? -7.916  -58.264 65.624   1.00 21.34  ? 193 THR D O   1 
ATOM   13731 C CB  . THR D  1 193 ? -10.493 -56.272 66.979   1.00 25.05  ? 193 THR D CB  1 
ATOM   13732 O OG1 . THR D  1 193 ? -10.387 -56.322 68.411   1.00 28.36  ? 193 THR D OG1 1 
ATOM   13733 C CG2 . THR D  1 193 ? -11.340 -57.436 66.486   1.00 24.51  ? 193 THR D CG2 1 
ATOM   13734 N N   . SER D  1 194 ? -8.343  -58.085 67.820   1.00 23.62  ? 194 SER D N   1 
ATOM   13735 C CA  . SER D  1 194 ? -7.806  -59.368 68.230   1.00 23.45  ? 194 SER D CA  1 
ATOM   13736 C C   . SER D  1 194 ? -8.860  -60.140 69.002   1.00 23.48  ? 194 SER D C   1 
ATOM   13737 O O   . SER D  1 194 ? -9.836  -59.552 69.487   1.00 22.24  ? 194 SER D O   1 
ATOM   13738 C CB  . SER D  1 194 ? -6.578  -59.189 69.135   1.00 21.77  ? 194 SER D CB  1 
ATOM   13739 O OG  . SER D  1 194 ? -5.574  -58.436 68.513   1.00 21.78  ? 194 SER D OG  1 
ATOM   13740 N N   . PRO D  1 195 ? -8.701  -61.455 69.138   1.00 25.32  ? 195 PRO D N   1 
ATOM   13741 C CA  . PRO D  1 195 ? -9.473  -62.189 70.148   1.00 29.57  ? 195 PRO D CA  1 
ATOM   13742 C C   . PRO D  1 195 ? -9.451  -61.444 71.484   1.00 22.11  ? 195 PRO D C   1 
ATOM   13743 O O   . PRO D  1 195 ? -8.425  -60.894 71.884   1.00 18.98  ? 195 PRO D O   1 
ATOM   13744 C CB  . PRO D  1 195 ? -8.746  -63.535 70.230   1.00 33.11  ? 195 PRO D CB  1 
ATOM   13745 C CG  . PRO D  1 195 ? -8.123  -63.701 68.860   1.00 31.14  ? 195 PRO D CG  1 
ATOM   13746 C CD  . PRO D  1 195 ? -7.756  -62.321 68.401   1.00 28.37  ? 195 PRO D CD  1 
ATOM   13747 N N   . TYR D  1 196 ? -10.588 -61.495 72.190   1.00 19.95  ? 196 TYR D N   1 
ATOM   13748 C CA  . TYR D  1 196 ? -11.018 -60.449 73.130   1.00 21.86  ? 196 TYR D CA  1 
ATOM   13749 C C   . TYR D  1 196 ? -9.943  -60.018 74.135   1.00 25.83  ? 196 TYR D C   1 
ATOM   13750 O O   . TYR D  1 196 ? -9.689  -58.817 74.295   1.00 20.58  ? 196 TYR D O   1 
ATOM   13751 C CB  . TYR D  1 196 ? -12.282 -60.910 73.878   1.00 21.33  ? 196 TYR D CB  1 
ATOM   13752 C CG  . TYR D  1 196 ? -13.143 -59.747 74.336   1.00 26.69  ? 196 TYR D CG  1 
ATOM   13753 C CD1 . TYR D  1 196 ? -12.799 -58.993 75.465   1.00 26.44  ? 196 TYR D CD1 1 
ATOM   13754 C CD2 . TYR D  1 196 ? -14.287 -59.386 73.631   1.00 29.29  ? 196 TYR D CD2 1 
ATOM   13755 C CE1 . TYR D  1 196 ? -13.575 -57.908 75.870   1.00 30.07  ? 196 TYR D CE1 1 
ATOM   13756 C CE2 . TYR D  1 196 ? -15.073 -58.312 74.029   1.00 29.20  ? 196 TYR D CE2 1 
ATOM   13757 C CZ  . TYR D  1 196 ? -14.712 -57.576 75.149   1.00 30.41  ? 196 TYR D CZ  1 
ATOM   13758 O OH  . TYR D  1 196 ? -15.501 -56.519 75.539   1.00 25.17  ? 196 TYR D OH  1 
ATOM   13759 N N   . TYR D  1 197 ? -9.358  -60.965 74.888   1.00 22.49  ? 197 TYR D N   1 
ATOM   13760 C CA  . TYR D  1 197 ? -8.426  -60.596 75.954   1.00 19.49  ? 197 TYR D CA  1 
ATOM   13761 C C   . TYR D  1 197 ? -6.972  -60.839 75.577   1.00 26.07  ? 197 TYR D C   1 
ATOM   13762 O O   . TYR D  1 197 ? -6.122  -60.967 76.467   1.00 23.37  ? 197 TYR D O   1 
ATOM   13763 C CB  . TYR D  1 197 ? -8.777  -61.319 77.269   1.00 20.08  ? 197 TYR D CB  1 
ATOM   13764 C CG  . TYR D  1 197 ? -10.077 -60.826 77.786   1.00 22.92  ? 197 TYR D CG  1 
ATOM   13765 C CD1 . TYR D  1 197 ? -10.172 -59.560 78.329   1.00 21.83  ? 197 TYR D CD1 1 
ATOM   13766 C CD2 . TYR D  1 197 ? -11.236 -61.577 77.641   1.00 26.73  ? 197 TYR D CD2 1 
ATOM   13767 C CE1 . TYR D  1 197 ? -11.364 -59.069 78.762   1.00 21.78  ? 197 TYR D CE1 1 
ATOM   13768 C CE2 . TYR D  1 197 ? -12.447 -61.089 78.075   1.00 27.40  ? 197 TYR D CE2 1 
ATOM   13769 C CZ  . TYR D  1 197 ? -12.490 -59.833 78.634   1.00 22.17  ? 197 TYR D CZ  1 
ATOM   13770 O OH  . TYR D  1 197 ? -13.662 -59.308 79.056   1.00 25.79  ? 197 TYR D OH  1 
ATOM   13771 N N   . HIS D  1 198 ? -6.666  -60.890 74.256   1.00 18.50  ? 198 HIS D N   1 
ATOM   13772 C CA  . HIS D  1 198 ? -5.305  -61.062 73.755   1.00 23.30  ? 198 HIS D CA  1 
ATOM   13773 C C   . HIS D  1 198 ? -4.722  -62.390 74.252   1.00 24.48  ? 198 HIS D C   1 
ATOM   13774 O O   . HIS D  1 198 ? -3.620  -62.404 74.808   1.00 28.27  ? 198 HIS D O   1 
ATOM   13775 C CB  . HIS D  1 198 ? -4.467  -59.842 74.186   1.00 18.47  ? 198 HIS D CB  1 
ATOM   13776 C CG  . HIS D  1 198 ? -3.249  -59.564 73.348   1.00 21.73  ? 198 HIS D CG  1 
ATOM   13777 N ND1 . HIS D  1 198 ? -1.981  -59.941 73.742   1.00 20.16  ? 198 HIS D ND1 1 
ATOM   13778 C CD2 . HIS D  1 198 ? -3.090  -58.870 72.192   1.00 18.14  ? 198 HIS D CD2 1 
ATOM   13779 C CE1 . HIS D  1 198 ? -1.101  -59.536 72.840   1.00 20.67  ? 198 HIS D CE1 1 
ATOM   13780 N NE2 . HIS D  1 198 ? -1.747  -58.877 71.895   1.00 17.69  ? 198 HIS D NE2 1 
ATOM   13781 N N   . PRO D  1 199 ? -5.419  -63.520 74.083   1.00 26.32  ? 199 PRO D N   1 
ATOM   13782 C CA  . PRO D  1 199 ? -4.842  -64.818 74.460   1.00 29.07  ? 199 PRO D CA  1 
ATOM   13783 C C   . PRO D  1 199 ? -3.912  -65.367 73.388   1.00 33.23  ? 199 PRO D C   1 
ATOM   13784 O O   . PRO D  1 199 ? -3.803  -64.842 72.279   1.00 31.95  ? 199 PRO D O   1 
ATOM   13785 C CB  . PRO D  1 199 ? -6.065  -65.727 74.588   1.00 24.48  ? 199 PRO D CB  1 
ATOM   13786 C CG  . PRO D  1 199 ? -6.970  -65.206 73.488   1.00 21.03  ? 199 PRO D CG  1 
ATOM   13787 C CD  . PRO D  1 199 ? -6.766  -63.689 73.496   1.00 22.95  ? 199 PRO D CD  1 
ATOM   13788 N N   . LEU D  1 200 ? -3.266  -66.480 73.740   1.00 31.55  ? 200 LEU D N   1 
ATOM   13789 C CA  . LEU D  1 200 ? -2.456  -67.248 72.800   1.00 29.10  ? 200 LEU D CA  1 
ATOM   13790 C C   . LEU D  1 200 ? -3.363  -68.319 72.214   1.00 31.59  ? 200 LEU D C   1 
ATOM   13791 O O   . LEU D  1 200 ? -3.426  -69.443 72.716   1.00 28.45  ? 200 LEU D O   1 
ATOM   13792 C CB  . LEU D  1 200 ? -1.245  -67.856 73.502   1.00 29.11  ? 200 LEU D CB  1 
ATOM   13793 C CG  . LEU D  1 200 ? -0.097  -66.908 73.838   1.00 25.92  ? 200 LEU D CG  1 
ATOM   13794 C CD1 . LEU D  1 200 ? 0.967   -67.574 74.674   1.00 25.96  ? 200 LEU D CD1 1 
ATOM   13795 C CD2 . LEU D  1 200 ? 0.515   -66.368 72.543   1.00 26.04  ? 200 LEU D CD2 1 
ATOM   13796 N N   . ILE D  1 201 ? -4.073  -67.956 71.129   1.00 21.73  ? 201 ILE D N   1 
ATOM   13797 C CA  . ILE D  1 201 ? -5.063  -68.863 70.537   1.00 20.53  ? 201 ILE D CA  1 
ATOM   13798 C C   . ILE D  1 201 ? -4.501  -70.256 70.220   1.00 25.35  ? 201 ILE D C   1 
ATOM   13799 O O   . ILE D  1 201 ? -5.185  -71.246 70.506   1.00 23.41  ? 201 ILE D O   1 
ATOM   13800 C CB  . ILE D  1 201 ? -5.718  -68.201 69.314   1.00 21.34  ? 201 ILE D CB  1 
ATOM   13801 C CG1 . ILE D  1 201 ? -6.522  -66.948 69.708   1.00 23.92  ? 201 ILE D CG1 1 
ATOM   13802 C CG2 . ILE D  1 201 ? -6.602  -69.198 68.543   1.00 24.06  ? 201 ILE D CG2 1 
ATOM   13803 C CD1 . ILE D  1 201 ? -7.832  -67.238 70.448   1.00 29.53  ? 201 ILE D CD1 1 
ATOM   13804 N N   . PRO D  1 202 ? -3.331  -70.407 69.585   1.00 25.22  ? 202 PRO D N   1 
ATOM   13805 C CA  . PRO D  1 202 ? -2.864  -71.781 69.291   1.00 26.92  ? 202 PRO D CA  1 
ATOM   13806 C C   . PRO D  1 202 ? -2.751  -72.686 70.525   1.00 26.85  ? 202 PRO D C   1 
ATOM   13807 O O   . PRO D  1 202 ? -2.969  -73.907 70.416   1.00 22.49  ? 202 PRO D O   1 
ATOM   13808 C CB  . PRO D  1 202 ? -1.499  -71.551 68.619   1.00 25.07  ? 202 PRO D CB  1 
ATOM   13809 C CG  . PRO D  1 202 ? -1.599  -70.140 68.029   1.00 24.65  ? 202 PRO D CG  1 
ATOM   13810 C CD  . PRO D  1 202 ? -2.402  -69.387 69.063   1.00 16.87  ? 202 PRO D CD  1 
ATOM   13811 N N   . ILE D  1 203 ? -2.425  -72.141 71.701   1.00 18.19  ? 203 ILE D N   1 
ATOM   13812 C CA  . ILE D  1 203 ? -2.305  -73.002 72.875   1.00 24.42  ? 203 ILE D CA  1 
ATOM   13813 C C   . ILE D  1 203 ? -3.683  -73.407 73.365   1.00 28.84  ? 203 ILE D C   1 
ATOM   13814 O O   . ILE D  1 203 ? -3.922  -74.574 73.682   1.00 32.40  ? 203 ILE D O   1 
ATOM   13815 C CB  . ILE D  1 203 ? -1.499  -72.304 73.985   1.00 30.00  ? 203 ILE D CB  1 
ATOM   13816 C CG1 . ILE D  1 203 ? -0.049  -72.129 73.535   1.00 32.95  ? 203 ILE D CG1 1 
ATOM   13817 C CG2 . ILE D  1 203 ? -1.552  -73.131 75.290   1.00 29.36  ? 203 ILE D CG2 1 
ATOM   13818 C CD1 . ILE D  1 203 ? 0.825   -71.512 74.597   1.00 36.33  ? 203 ILE D CD1 1 
ATOM   13819 N N   . LEU D  1 204 ? -4.615  -72.454 73.409   1.00 29.47  ? 204 LEU D N   1 
ATOM   13820 C CA  . LEU D  1 204 ? -5.979  -72.776 73.820   1.00 28.09  ? 204 LEU D CA  1 
ATOM   13821 C C   . LEU D  1 204 ? -6.597  -73.835 72.917   1.00 24.94  ? 204 LEU D C   1 
ATOM   13822 O O   . LEU D  1 204 ? -7.355  -74.690 73.385   1.00 26.25  ? 204 LEU D O   1 
ATOM   13823 C CB  . LEU D  1 204 ? -6.831  -71.508 73.817   1.00 25.43  ? 204 LEU D CB  1 
ATOM   13824 C CG  . LEU D  1 204 ? -6.354  -70.395 74.746   1.00 24.81  ? 204 LEU D CG  1 
ATOM   13825 C CD1 . LEU D  1 204 ? -7.382  -69.299 74.789   1.00 23.49  ? 204 LEU D CD1 1 
ATOM   13826 C CD2 . LEU D  1 204 ? -6.116  -70.955 76.137   1.00 22.38  ? 204 LEU D CD2 1 
ATOM   13827 N N   . LEU D  1 205 ? -6.293  -73.788 71.613   1.00 25.12  ? 205 LEU D N   1 
ATOM   13828 C CA  . LEU D  1 205 ? -6.825  -74.789 70.693   1.00 24.16  ? 205 LEU D CA  1 
ATOM   13829 C C   . LEU D  1 205 ? -6.119  -76.128 70.856   1.00 26.62  ? 205 LEU D C   1 
ATOM   13830 O O   . LEU D  1 205 ? -6.735  -77.185 70.691   1.00 28.92  ? 205 LEU D O   1 
ATOM   13831 C CB  . LEU D  1 205 ? -6.676  -74.303 69.242   1.00 26.56  ? 205 LEU D CB  1 
ATOM   13832 C CG  . LEU D  1 205 ? -7.626  -73.224 68.737   1.00 20.78  ? 205 LEU D CG  1 
ATOM   13833 C CD1 . LEU D  1 205 ? -7.257  -72.891 67.286   1.00 20.61  ? 205 LEU D CD1 1 
ATOM   13834 C CD2 . LEU D  1 205 ? -9.061  -73.739 68.846   1.00 24.60  ? 205 LEU D CD2 1 
ATOM   13835 N N   . ASN D  1 206 ? -4.819  -76.103 71.119   1.00 27.01  ? 206 ASN D N   1 
ATOM   13836 C CA  . ASN D  1 206 ? -4.032  -77.328 71.123   1.00 28.27  ? 206 ASN D CA  1 
ATOM   13837 C C   . ASN D  1 206 ? -2.704  -77.063 71.811   1.00 27.35  ? 206 ASN D C   1 
ATOM   13838 O O   . ASN D  1 206 ? -1.739  -76.652 71.158   1.00 25.30  ? 206 ASN D O   1 
ATOM   13839 C CB  . ASN D  1 206 ? -3.780  -77.843 69.703   1.00 27.82  ? 206 ASN D CB  1 
ATOM   13840 C CG  . ASN D  1 206 ? -3.280  -79.275 69.696   1.00 38.75  ? 206 ASN D CG  1 
ATOM   13841 O OD1 . ASN D  1 206 ? -2.748  -79.778 70.698   1.00 38.09  ? 206 ASN D OD1 1 
ATOM   13842 N ND2 . ASN D  1 206 ? -3.433  -79.939 68.562   1.00 43.74  ? 206 ASN D ND2 1 
ATOM   13843 N N   . PRO D  1 207 ? -2.610  -77.283 73.122   1.00 28.35  ? 207 PRO D N   1 
ATOM   13844 C CA  . PRO D  1 207 ? -1.353  -76.972 73.827   1.00 28.81  ? 207 PRO D CA  1 
ATOM   13845 C C   . PRO D  1 207 ? -0.151  -77.746 73.302   1.00 27.29  ? 207 PRO D C   1 
ATOM   13846 O O   . PRO D  1 207 ? 0.994   -77.310 73.489   1.00 32.76  ? 207 PRO D O   1 
ATOM   13847 C CB  . PRO D  1 207 ? -1.670  -77.338 75.284   1.00 31.70  ? 207 PRO D CB  1 
ATOM   13848 C CG  . PRO D  1 207 ? -3.162  -77.279 75.371   1.00 29.84  ? 207 PRO D CG  1 
ATOM   13849 C CD  . PRO D  1 207 ? -3.667  -77.744 74.033   1.00 29.96  ? 207 PRO D CD  1 
ATOM   13850 N N   . ASN D  1 208 ? -0.371  -78.857 72.618   1.00 25.70  ? 208 ASN D N   1 
ATOM   13851 C CA  . ASN D  1 208 ? 0.747   -79.612 72.076   1.00 29.76  ? 208 ASN D CA  1 
ATOM   13852 C C   . ASN D  1 208 ? 1.451   -78.899 70.925   1.00 28.44  ? 208 ASN D C   1 
ATOM   13853 O O   . ASN D  1 208 ? 2.582   -79.268 70.604   1.00 29.04  ? 208 ASN D O   1 
ATOM   13854 C CB  . ASN D  1 208 ? 0.262   -80.999 71.646   1.00 36.70  ? 208 ASN D CB  1 
ATOM   13855 C CG  . ASN D  1 208 ? 0.089   -81.955 72.832   1.00 44.09  ? 208 ASN D CG  1 
ATOM   13856 O OD1 . ASN D  1 208 ? 0.022   -81.533 73.986   1.00 45.93  ? 208 ASN D OD1 1 
ATOM   13857 N ND2 . ASN D  1 208 ? 0.029   -83.250 72.542   1.00 51.66  ? 208 ASN D ND2 1 
ATOM   13858 N N   . CYS D  1 209 ? 0.853   -77.848 70.343   1.00 29.66  ? 209 CYS D N   1 
ATOM   13859 C CA  . CYS D  1 209 ? 1.533   -77.135 69.263   1.00 31.06  ? 209 CYS D CA  1 
ATOM   13860 C C   . CYS D  1 209 ? 2.851   -76.496 69.713   1.00 30.93  ? 209 CYS D C   1 
ATOM   13861 O O   . CYS D  1 209 ? 3.659   -76.130 68.852   1.00 25.58  ? 209 CYS D O   1 
ATOM   13862 C CB  . CYS D  1 209 ? 0.611   -76.068 68.669   1.00 33.24  ? 209 CYS D CB  1 
ATOM   13863 S SG  . CYS D  1 209 ? 0.379   -74.635 69.736   1.00 38.58  ? 209 CYS D SG  1 
ATOM   13864 N N   . VAL D  1 210 ? 3.106   -76.380 71.026   1.00 28.86  ? 210 VAL D N   1 
ATOM   13865 C CA  . VAL D  1 210 ? 4.409   -75.902 71.493   1.00 29.93  ? 210 VAL D CA  1 
ATOM   13866 C C   . VAL D  1 210 ? 5.532   -76.870 71.116   1.00 27.04  ? 210 VAL D C   1 
ATOM   13867 O O   . VAL D  1 210 ? 6.691   -76.456 70.969   1.00 30.71  ? 210 VAL D O   1 
ATOM   13868 C CB  . VAL D  1 210 ? 4.403   -75.646 73.022   1.00 34.07  ? 210 VAL D CB  1 
ATOM   13869 C CG1 . VAL D  1 210 ? 3.193   -74.835 73.421   1.00 37.11  ? 210 VAL D CG1 1 
ATOM   13870 C CG2 . VAL D  1 210 ? 4.420   -76.938 73.784   1.00 37.28  ? 210 VAL D CG2 1 
ATOM   13871 N N   . TYR D  1 211 ? 5.220   -78.149 70.913   1.00 25.54  ? 211 TYR D N   1 
ATOM   13872 C CA  . TYR D  1 211 ? 6.286   -79.087 70.567   1.00 32.58  ? 211 TYR D CA  1 
ATOM   13873 C C   . TYR D  1 211 ? 6.809   -78.905 69.150   1.00 32.90  ? 211 TYR D C   1 
ATOM   13874 O O   . TYR D  1 211 ? 7.847   -79.483 68.815   1.00 31.04  ? 211 TYR D O   1 
ATOM   13875 C CB  . TYR D  1 211 ? 5.801   -80.516 70.730   1.00 35.43  ? 211 TYR D CB  1 
ATOM   13876 C CG  . TYR D  1 211 ? 5.421   -80.861 72.150   1.00 36.18  ? 211 TYR D CG  1 
ATOM   13877 C CD1 . TYR D  1 211 ? 6.204   -80.452 73.225   1.00 33.36  ? 211 TYR D CD1 1 
ATOM   13878 C CD2 . TYR D  1 211 ? 4.277   -81.596 72.413   1.00 37.89  ? 211 TYR D CD2 1 
ATOM   13879 C CE1 . TYR D  1 211 ? 5.859   -80.788 74.530   1.00 34.41  ? 211 TYR D CE1 1 
ATOM   13880 C CE2 . TYR D  1 211 ? 3.917   -81.920 73.707   1.00 36.35  ? 211 TYR D CE2 1 
ATOM   13881 C CZ  . TYR D  1 211 ? 4.709   -81.524 74.758   1.00 34.69  ? 211 TYR D CZ  1 
ATOM   13882 O OH  . TYR D  1 211 ? 4.337   -81.876 76.036   1.00 35.88  ? 211 TYR D OH  1 
ATOM   13883 N N   . GLU D  1 212 ? 6.123   -78.116 68.324   1.00 39.11  ? 212 GLU D N   1 
ATOM   13884 C CA  . GLU D  1 212 ? 6.527   -77.993 66.932   1.00 39.22  ? 212 GLU D CA  1 
ATOM   13885 C C   . GLU D  1 212 ? 7.832   -77.222 66.790   1.00 41.02  ? 212 GLU D C   1 
ATOM   13886 O O   . GLU D  1 212 ? 8.610   -77.489 65.868   1.00 43.28  ? 212 GLU D O   1 
ATOM   13887 C CB  . GLU D  1 212 ? 5.408   -77.338 66.133   1.00 32.47  ? 212 GLU D CB  1 
ATOM   13888 C CG  . GLU D  1 212 ? 4.157   -78.200 66.023   1.00 35.39  ? 212 GLU D CG  1 
ATOM   13889 C CD  . GLU D  1 212 ? 3.033   -77.513 65.238   1.00 41.50  ? 212 GLU D CD  1 
ATOM   13890 O OE1 . GLU D  1 212 ? 1.855   -77.878 65.438   1.00 43.64  ? 212 GLU D OE1 1 
ATOM   13891 O OE2 . GLU D  1 212 ? 3.330   -76.609 64.432   1.00 40.40  ? 212 GLU D OE2 1 
ATOM   13892 N N   . THR D  1 213 ? 8.105   -76.286 67.696   1.00 37.43  ? 213 THR D N   1 
ATOM   13893 C CA  . THR D  1 213 ? 9.356   -75.543 67.671   1.00 37.28  ? 213 THR D CA  1 
ATOM   13894 C C   . THR D  1 213 ? 10.204  -75.715 68.925   1.00 40.64  ? 213 THR D C   1 
ATOM   13895 O O   . THR D  1 213 ? 11.414  -75.471 68.864   1.00 45.58  ? 213 THR D O   1 
ATOM   13896 C CB  . THR D  1 213 ? 9.086   -74.044 67.454   1.00 37.69  ? 213 THR D CB  1 
ATOM   13897 O OG1 . THR D  1 213 ? 8.142   -73.588 68.431   1.00 42.73  ? 213 THR D OG1 1 
ATOM   13898 C CG2 . THR D  1 213 ? 8.538   -73.791 66.033   1.00 35.90  ? 213 THR D CG2 1 
ATOM   13899 N N   . THR D  1 214 ? 9.618   -76.131 70.050   1.00 38.58  ? 214 THR D N   1 
ATOM   13900 C CA  . THR D  1 214 ? 10.364  -76.466 71.264   1.00 34.85  ? 214 THR D CA  1 
ATOM   13901 C C   . THR D  1 214 ? 10.046  -77.907 71.650   1.00 37.08  ? 214 THR D C   1 
ATOM   13902 O O   . THR D  1 214 ? 9.297   -78.151 72.607   1.00 41.03  ? 214 THR D O   1 
ATOM   13903 C CB  . THR D  1 214 ? 10.023  -75.516 72.406   1.00 33.92  ? 214 THR D CB  1 
ATOM   13904 O OG1 . THR D  1 214 ? 8.601   -75.486 72.584   1.00 33.64  ? 214 THR D OG1 1 
ATOM   13905 C CG2 . THR D  1 214 ? 10.518  -74.123 72.087   1.00 34.44  ? 214 THR D CG2 1 
ATOM   13906 N N   . PRO D  1 215 ? 10.598  -78.891 70.938   1.00 35.68  ? 215 PRO D N   1 
ATOM   13907 C CA  . PRO D  1 215 ? 10.231  -80.282 71.240   1.00 35.23  ? 215 PRO D CA  1 
ATOM   13908 C C   . PRO D  1 215 ? 10.582  -80.696 72.658   1.00 39.57  ? 215 PRO D C   1 
ATOM   13909 O O   . PRO D  1 215 ? 9.908   -81.572 73.209   1.00 41.16  ? 215 PRO D O   1 
ATOM   13910 C CB  . PRO D  1 215 ? 11.001  -81.094 70.187   1.00 36.31  ? 215 PRO D CB  1 
ATOM   13911 C CG  . PRO D  1 215 ? 12.102  -80.197 69.732   1.00 37.78  ? 215 PRO D CG  1 
ATOM   13912 C CD  . PRO D  1 215 ? 11.574  -78.796 69.839   1.00 37.65  ? 215 PRO D CD  1 
ATOM   13913 N N   . ASN D  1 216 ? 11.560  -80.050 73.292   1.00 38.30  ? 216 ASN D N   1 
ATOM   13914 C CA  . ASN D  1 216 ? 12.029  -80.462 74.606   1.00 43.32  ? 216 ASN D CA  1 
ATOM   13915 C C   . ASN D  1 216 ? 11.405  -79.666 75.747   1.00 41.21  ? 216 ASN D C   1 
ATOM   13916 O O   . ASN D  1 216 ? 11.823  -79.827 76.896   1.00 38.80  ? 216 ASN D O   1 
ATOM   13917 C CB  . ASN D  1 216 ? 13.553  -80.360 74.679   1.00 46.16  ? 216 ASN D CB  1 
ATOM   13918 C CG  . ASN D  1 216 ? 14.247  -81.281 73.700   1.00 49.98  ? 216 ASN D CG  1 
ATOM   13919 O OD1 . ASN D  1 216 ? 15.220  -80.890 73.053   1.00 49.92  ? 216 ASN D OD1 1 
ATOM   13920 N ND2 . ASN D  1 216 ? 13.756  -82.514 73.587   1.00 51.38  ? 216 ASN D ND2 1 
ATOM   13921 N N   . VAL D  1 217 ? 10.420  -78.811 75.464   1.00 39.36  ? 217 VAL D N   1 
ATOM   13922 C CA  . VAL D  1 217 ? 9.771   -78.062 76.528   1.00 40.70  ? 217 VAL D CA  1 
ATOM   13923 C C   . VAL D  1 217 ? 8.946   -78.999 77.407   1.00 37.16  ? 217 VAL D C   1 
ATOM   13924 O O   . VAL D  1 217 ? 8.410   -80.018 76.949   1.00 39.19  ? 217 VAL D O   1 
ATOM   13925 C CB  . VAL D  1 217 ? 8.892   -76.941 75.945   1.00 42.92  ? 217 VAL D CB  1 
ATOM   13926 C CG1 . VAL D  1 217 ? 7.678   -77.517 75.194   1.00 39.32  ? 217 VAL D CG1 1 
ATOM   13927 C CG2 . VAL D  1 217 ? 8.453   -76.016 77.050   1.00 41.50  ? 217 VAL D CG2 1 
ATOM   13928 N N   . LYS D  1 218 ? 8.854   -78.660 78.691   1.00 33.54  ? 218 LYS D N   1 
ATOM   13929 C CA  . LYS D  1 218 ? 7.920   -79.297 79.609   1.00 39.03  ? 218 LYS D CA  1 
ATOM   13930 C C   . LYS D  1 218 ? 6.766   -78.340 79.867   1.00 36.45  ? 218 LYS D C   1 
ATOM   13931 O O   . LYS D  1 218 ? 6.975   -77.200 80.308   1.00 41.89  ? 218 LYS D O   1 
ATOM   13932 C CB  . LYS D  1 218 ? 8.593   -79.688 80.929   1.00 44.79  ? 218 LYS D CB  1 
ATOM   13933 C CG  . LYS D  1 218 ? 7.916   -80.865 81.677   1.00 53.83  ? 218 LYS D CG  1 
ATOM   13934 C CD  . LYS D  1 218 ? 6.633   -80.424 82.407   1.00 61.71  ? 218 LYS D CD  1 
ATOM   13935 C CE  . LYS D  1 218 ? 6.491   -81.037 83.806   1.00 65.45  ? 218 LYS D CE  1 
ATOM   13936 N NZ  . LYS D  1 218 ? 5.346   -80.430 84.567   1.00 64.98  ? 218 LYS D NZ  1 
ATOM   13937 N N   . ILE D  1 219 ? 5.555   -78.802 79.596   1.00 35.47  ? 219 ILE D N   1 
ATOM   13938 C CA  . ILE D  1 219 ? 4.355   -77.997 79.796   1.00 40.09  ? 219 ILE D CA  1 
ATOM   13939 C C   . ILE D  1 219 ? 3.445   -78.758 80.747   1.00 36.85  ? 219 ILE D C   1 
ATOM   13940 O O   . ILE D  1 219 ? 3.558   -79.990 80.887   1.00 39.86  ? 219 ILE D O   1 
ATOM   13941 C CB  . ILE D  1 219 ? 3.651   -77.670 78.459   1.00 40.68  ? 219 ILE D CB  1 
ATOM   13942 C CG1 . ILE D  1 219 ? 3.183   -78.949 77.769   1.00 42.09  ? 219 ILE D CG1 1 
ATOM   13943 C CG2 . ILE D  1 219 ? 4.593   -76.914 77.560   1.00 42.49  ? 219 ILE D CG2 1 
ATOM   13944 C CD1 . ILE D  1 219 ? 2.058   -78.709 76.802   1.00 43.19  ? 219 ILE D CD1 1 
ATOM   13945 N N   . PRO D  1 220 ? 2.552   -78.055 81.441   1.00 35.80  ? 220 PRO D N   1 
ATOM   13946 C CA  . PRO D  1 220 ? 1.640   -78.729 82.371   1.00 37.64  ? 220 PRO D CA  1 
ATOM   13947 C C   . PRO D  1 220 ? 0.690   -79.670 81.649   1.00 39.09  ? 220 PRO D C   1 
ATOM   13948 O O   . PRO D  1 220 ? 0.545   -79.661 80.425   1.00 34.96  ? 220 PRO D O   1 
ATOM   13949 C CB  . PRO D  1 220 ? 0.874   -77.576 83.030   1.00 33.97  ? 220 PRO D CB  1 
ATOM   13950 C CG  . PRO D  1 220 ? 1.058   -76.429 82.137   1.00 36.55  ? 220 PRO D CG  1 
ATOM   13951 C CD  . PRO D  1 220 ? 2.416   -76.590 81.527   1.00 35.97  ? 220 PRO D CD  1 
ATOM   13952 N N   . ASP D  1 221 ? 0.023   -80.486 82.452   1.00 39.09  ? 221 ASP D N   1 
ATOM   13953 C CA  . ASP D  1 221 ? -1.007  -81.383 81.952   1.00 40.35  ? 221 ASP D CA  1 
ATOM   13954 C C   . ASP D  1 221 ? -2.285  -80.574 81.774   1.00 38.38  ? 221 ASP D C   1 
ATOM   13955 O O   . ASP D  1 221 ? -2.943  -80.202 82.753   1.00 37.91  ? 221 ASP D O   1 
ATOM   13956 C CB  . ASP D  1 221 ? -1.193  -82.558 82.908   1.00 44.95  ? 221 ASP D CB  1 
ATOM   13957 C CG  . ASP D  1 221 ? -2.509  -83.292 82.703   1.00 47.49  ? 221 ASP D CG  1 
ATOM   13958 O OD1 . ASP D  1 221 ? -3.068  -83.269 81.584   1.00 45.31  ? 221 ASP D OD1 1 
ATOM   13959 O OD2 . ASP D  1 221 ? -2.995  -83.888 83.689   1.00 48.72  ? 221 ASP D OD2 1 
ATOM   13960 N N   . PHE D  1 222 ? -2.632  -80.305 80.514   1.00 32.60  ? 222 PHE D N   1 
ATOM   13961 C CA  . PHE D  1 222 ? -3.830  -79.546 80.155   1.00 34.36  ? 222 PHE D CA  1 
ATOM   13962 C C   . PHE D  1 222 ? -5.037  -80.474 80.277   1.00 39.80  ? 222 PHE D C   1 
ATOM   13963 O O   . PHE D  1 222 ? -5.584  -80.985 79.298   1.00 45.02  ? 222 PHE D O   1 
ATOM   13964 C CB  . PHE D  1 222 ? -3.668  -78.956 78.753   1.00 27.66  ? 222 PHE D CB  1 
ATOM   13965 C CG  . PHE D  1 222 ? -2.910  -77.655 78.744   1.00 25.74  ? 222 PHE D CG  1 
ATOM   13966 C CD1 . PHE D  1 222 ? -1.528  -77.639 78.794   1.00 25.06  ? 222 PHE D CD1 1 
ATOM   13967 C CD2 . PHE D  1 222 ? -3.581  -76.451 78.734   1.00 25.53  ? 222 PHE D CD2 1 
ATOM   13968 C CE1 . PHE D  1 222 ? -0.826  -76.441 78.815   1.00 30.68  ? 222 PHE D CE1 1 
ATOM   13969 C CE2 . PHE D  1 222 ? -2.882  -75.241 78.745   1.00 31.65  ? 222 PHE D CE2 1 
ATOM   13970 C CZ  . PHE D  1 222 ? -1.508  -75.237 78.786   1.00 32.66  ? 222 PHE D CZ  1 
ATOM   13971 N N   . ALA D  1 223 ? -5.454  -80.704 81.524   1.00 40.29  ? 223 ALA D N   1 
ATOM   13972 C CA  . ALA D  1 223 ? -6.511  -81.670 81.809   1.00 43.85  ? 223 ALA D CA  1 
ATOM   13973 C C   . ALA D  1 223 ? -7.890  -81.185 81.395   1.00 44.56  ? 223 ALA D C   1 
ATOM   13974 O O   . ALA D  1 223 ? -8.859  -81.936 81.544   1.00 48.37  ? 223 ALA D O   1 
ATOM   13975 C CB  . ALA D  1 223 ? -6.516  -82.024 83.303   1.00 45.29  ? 223 ALA D CB  1 
ATOM   13976 N N   . VAL D  1 224 ? -8.003  -79.956 80.896   1.00 42.67  ? 224 VAL D N   1 
ATOM   13977 C CA  . VAL D  1 224 ? -9.268  -79.346 80.525   1.00 39.87  ? 224 VAL D CA  1 
ATOM   13978 C C   . VAL D  1 224 ? -9.113  -78.810 79.102   1.00 33.56  ? 224 VAL D C   1 
ATOM   13979 O O   . VAL D  1 224 ? -8.005  -78.540 78.643   1.00 32.28  ? 224 VAL D O   1 
ATOM   13980 C CB  . VAL D  1 224 ? -9.660  -78.226 81.519   1.00 42.12  ? 224 VAL D CB  1 
ATOM   13981 C CG1 . VAL D  1 224 ? -8.852  -76.958 81.256   1.00 40.42  ? 224 VAL D CG1 1 
ATOM   13982 C CG2 . VAL D  1 224 ? -11.146 -77.945 81.468   1.00 49.08  ? 224 VAL D CG2 1 
ATOM   13983 N N   . SER D  1 225 ? -10.236 -78.669 78.398   1.00 34.53  ? 225 SER D N   1 
ATOM   13984 C CA  . SER D  1 225 ? -10.237 -78.188 77.018   1.00 34.64  ? 225 SER D CA  1 
ATOM   13985 C C   . SER D  1 225 ? -10.509 -76.685 76.957   1.00 36.79  ? 225 SER D C   1 
ATOM   13986 O O   . SER D  1 225 ? -11.511 -76.207 77.493   1.00 40.38  ? 225 SER D O   1 
ATOM   13987 C CB  . SER D  1 225 ? -11.278 -78.943 76.186   1.00 32.59  ? 225 SER D CB  1 
ATOM   13988 O OG  . SER D  1 225 ? -11.326 -78.455 74.848   1.00 33.64  ? 225 SER D OG  1 
ATOM   13989 N N   . PHE D  1 226 ? -9.635  -75.945 76.270   1.00 33.52  ? 226 PHE D N   1 
ATOM   13990 C CA  . PHE D  1 226 ? -9.807  -74.511 76.077   1.00 29.15  ? 226 PHE D CA  1 
ATOM   13991 C C   . PHE D  1 226 ? -10.288 -74.169 74.674   1.00 27.77  ? 226 PHE D C   1 
ATOM   13992 O O   . PHE D  1 226 ? -10.182 -73.010 74.254   1.00 26.88  ? 226 PHE D O   1 
ATOM   13993 C CB  . PHE D  1 226 ? -8.500  -73.779 76.374   1.00 26.82  ? 226 PHE D CB  1 
ATOM   13994 C CG  . PHE D  1 226 ? -8.162  -73.719 77.845   1.00 27.45  ? 226 PHE D CG  1 
ATOM   13995 C CD1 . PHE D  1 226 ? -8.775  -72.791 78.669   1.00 31.57  ? 226 PHE D CD1 1 
ATOM   13996 C CD2 . PHE D  1 226 ? -7.239  -74.592 78.395   1.00 30.85  ? 226 PHE D CD2 1 
ATOM   13997 C CE1 . PHE D  1 226 ? -8.475  -72.732 80.043   1.00 29.91  ? 226 PHE D CE1 1 
ATOM   13998 C CE2 . PHE D  1 226 ? -6.924  -74.540 79.759   1.00 29.08  ? 226 PHE D CE2 1 
ATOM   13999 C CZ  . PHE D  1 226 ? -7.543  -73.612 80.577   1.00 33.81  ? 226 PHE D CZ  1 
ATOM   14000 N N   . ARG D  1 227 ? -10.804 -75.155 73.938   1.00 32.88  ? 227 ARG D N   1 
ATOM   14001 C CA  . ARG D  1 227 ? -11.136 -74.927 72.535   1.00 29.90  ? 227 ARG D CA  1 
ATOM   14002 C C   . ARG D  1 227 ? -12.334 -73.998 72.387   1.00 29.61  ? 227 ARG D C   1 
ATOM   14003 O O   . ARG D  1 227 ? -12.312 -73.077 71.562   1.00 25.69  ? 227 ARG D O   1 
ATOM   14004 C CB  . ARG D  1 227 ? -11.382 -76.257 71.826   1.00 33.65  ? 227 ARG D CB  1 
ATOM   14005 C CG  . ARG D  1 227 ? -10.149 -77.137 71.736   1.00 42.09  ? 227 ARG D CG  1 
ATOM   14006 C CD  . ARG D  1 227 ? -10.374 -78.288 70.769   1.00 50.02  ? 227 ARG D CD  1 
ATOM   14007 N NE  . ARG D  1 227 ? -10.701 -77.796 69.433   1.00 53.86  ? 227 ARG D NE  1 
ATOM   14008 C CZ  . ARG D  1 227 ? -9.802  -77.558 68.485   1.00 52.87  ? 227 ARG D CZ  1 
ATOM   14009 N NH1 . ARG D  1 227 ? -8.515  -77.768 68.722   1.00 45.76  ? 227 ARG D NH1 1 
ATOM   14010 N NH2 . ARG D  1 227 ? -10.188 -77.108 67.299   1.00 57.82  ? 227 ARG D NH2 1 
ATOM   14011 N N   . GLU D  1 228 ? -13.388 -74.208 73.186   1.00 30.19  ? 228 GLU D N   1 
ATOM   14012 C CA  . GLU D  1 228 ? -14.562 -73.350 73.058   1.00 33.29  ? 228 GLU D CA  1 
ATOM   14013 C C   . GLU D  1 228 ? -14.276 -71.920 73.532   1.00 31.64  ? 228 GLU D C   1 
ATOM   14014 O O   . GLU D  1 228 ? -14.851 -70.970 72.992   1.00 33.13  ? 228 GLU D O   1 
ATOM   14015 C CB  . GLU D  1 228 ? -15.753 -73.947 73.818   1.00 45.15  ? 228 GLU D CB  1 
ATOM   14016 C CG  . GLU D  1 228 ? -17.099 -73.269 73.504   1.00 61.40  ? 228 GLU D CG  1 
ATOM   14017 C CD  . GLU D  1 228 ? -17.296 -72.986 72.006   1.00 71.53  ? 228 GLU D CD  1 
ATOM   14018 O OE1 . GLU D  1 228 ? -17.486 -73.945 71.223   1.00 76.21  ? 228 GLU D OE1 1 
ATOM   14019 O OE2 . GLU D  1 228 ? -17.253 -71.798 71.613   1.00 71.41  ? 228 GLU D OE2 1 
ATOM   14020 N N   . ASP D  1 229 ? -13.380 -71.742 74.519   1.00 24.33  ? 229 ASP D N   1 
ATOM   14021 C CA  . ASP D  1 229 ? -12.933 -70.400 74.907   1.00 25.72  ? 229 ASP D CA  1 
ATOM   14022 C C   . ASP D  1 229 ? -12.224 -69.695 73.755   1.00 26.92  ? 229 ASP D C   1 
ATOM   14023 O O   . ASP D  1 229 ? -12.382 -68.476 73.562   1.00 28.91  ? 229 ASP D O   1 
ATOM   14024 C CB  . ASP D  1 229 ? -12.000 -70.470 76.121   1.00 24.41  ? 229 ASP D CB  1 
ATOM   14025 C CG  . ASP D  1 229 ? -12.752 -70.715 77.441   1.00 29.17  ? 229 ASP D CG  1 
ATOM   14026 O OD1 . ASP D  1 229 ? -14.003 -70.713 77.443   1.00 26.18  ? 229 ASP D OD1 1 
ATOM   14027 O OD2 . ASP D  1 229 ? -12.080 -70.920 78.477   1.00 27.54  ? 229 ASP D OD2 1 
ATOM   14028 N N   . ALA D  1 230 ? -11.409 -70.426 72.998   1.00 29.47  ? 230 ALA D N   1 
ATOM   14029 C CA  . ALA D  1 230 ? -10.725 -69.792 71.876   1.00 30.46  ? 230 ALA D CA  1 
ATOM   14030 C C   . ALA D  1 230 ? -11.737 -69.232 70.878   1.00 27.17  ? 230 ALA D C   1 
ATOM   14031 O O   . ALA D  1 230 ? -11.634 -68.074 70.469   1.00 24.02  ? 230 ALA D O   1 
ATOM   14032 C CB  . ALA D  1 230 ? -9.767  -70.779 71.216   1.00 31.90  ? 230 ALA D CB  1 
ATOM   14033 N N   . SER D  1 231 ? -12.786 -69.998 70.566   1.00 27.86  ? 231 SER D N   1 
ATOM   14034 C CA  . SER D  1 231 ? -13.852 -69.453 69.728   1.00 28.99  ? 231 SER D CA  1 
ATOM   14035 C C   . SER D  1 231 ? -14.514 -68.249 70.381   1.00 27.66  ? 231 SER D C   1 
ATOM   14036 O O   . SER D  1 231 ? -14.846 -67.275 69.704   1.00 27.18  ? 231 SER D O   1 
ATOM   14037 C CB  . SER D  1 231 ? -14.892 -70.526 69.420   1.00 36.69  ? 231 SER D CB  1 
ATOM   14038 O OG  . SER D  1 231 ? -14.345 -71.519 68.570   1.00 43.90  ? 231 SER D OG  1 
ATOM   14039 N N   . LYS D  1 232 ? -14.707 -68.285 71.704   1.00 25.71  ? 232 LYS D N   1 
ATOM   14040 C CA  . LYS D  1 232 ? -15.434 -67.195 72.337   1.00 23.15  ? 232 LYS D CA  1 
ATOM   14041 C C   . LYS D  1 232 ? -14.613 -65.916 72.342   1.00 21.44  ? 232 LYS D C   1 
ATOM   14042 O O   . LYS D  1 232 ? -15.159 -64.815 72.164   1.00 24.30  ? 232 LYS D O   1 
ATOM   14043 C CB  . LYS D  1 232 ? -15.844 -67.584 73.764   1.00 32.60  ? 232 LYS D CB  1 
ATOM   14044 C CG  . LYS D  1 232 ? -17.277 -67.210 74.086   1.00 39.53  ? 232 LYS D CG  1 
ATOM   14045 C CD  . LYS D  1 232 ? -17.712 -67.695 75.463   1.00 40.95  ? 232 LYS D CD  1 
ATOM   14046 C CE  . LYS D  1 232 ? -18.660 -66.693 76.107   1.00 44.38  ? 232 LYS D CE  1 
ATOM   14047 N NZ  . LYS D  1 232 ? -19.457 -67.298 77.225   1.00 44.26  ? 232 LYS D NZ  1 
ATOM   14048 N N   . HIS D  1 233 ? -13.304 -66.024 72.572   1.00 20.38  ? 233 HIS D N   1 
ATOM   14049 C CA  . HIS D  1 233 ? -12.457 -64.846 72.428   1.00 21.64  ? 233 HIS D CA  1 
ATOM   14050 C C   . HIS D  1 233 ? -12.656 -64.199 71.059   1.00 19.98  ? 233 HIS D C   1 
ATOM   14051 O O   . HIS D  1 233 ? -12.712 -62.968 70.945   1.00 22.32  ? 233 HIS D O   1 
ATOM   14052 C CB  . HIS D  1 233 ? -10.980 -65.210 72.623   1.00 23.08  ? 233 HIS D CB  1 
ATOM   14053 C CG  . HIS D  1 233 ? -10.559 -65.331 74.064   1.00 22.63  ? 233 HIS D CG  1 
ATOM   14054 N ND1 . HIS D  1 233 ? -10.423 -64.243 74.900   1.00 22.28  ? 233 HIS D ND1 1 
ATOM   14055 C CD2 . HIS D  1 233 ? -10.216 -66.414 74.800   1.00 24.08  ? 233 HIS D CD2 1 
ATOM   14056 C CE1 . HIS D  1 233 ? -10.028 -64.652 76.091   1.00 25.18  ? 233 HIS D CE1 1 
ATOM   14057 N NE2 . HIS D  1 233 ? -9.900  -65.968 76.058   1.00 23.05  ? 233 HIS D NE2 1 
ATOM   14058 N N   . VAL D  1 234 ? -12.789 -65.014 70.011   1.00 22.90  ? 234 VAL D N   1 
ATOM   14059 C CA  . VAL D  1 234 ? -12.934 -64.460 68.659   1.00 23.67  ? 234 VAL D CA  1 
ATOM   14060 C C   . VAL D  1 234 ? -14.346 -63.930 68.421   1.00 24.04  ? 234 VAL D C   1 
ATOM   14061 O O   . VAL D  1 234 ? -14.532 -62.842 67.847   1.00 23.40  ? 234 VAL D O   1 
ATOM   14062 C CB  . VAL D  1 234 ? -12.556 -65.510 67.607   1.00 20.60  ? 234 VAL D CB  1 
ATOM   14063 C CG1 . VAL D  1 234 ? -12.750 -64.919 66.175   1.00 19.59  ? 234 VAL D CG1 1 
ATOM   14064 C CG2 . VAL D  1 234 ? -11.135 -65.985 67.832   1.00 20.84  ? 234 VAL D CG2 1 
ATOM   14065 N N   . GLU D  1 235 ? -15.356 -64.692 68.838   1.00 24.15  ? 235 GLU D N   1 
ATOM   14066 C CA  . GLU D  1 235 ? -16.740 -64.293 68.619   1.00 27.03  ? 235 GLU D CA  1 
ATOM   14067 C C   . GLU D  1 235 ? -17.077 -63.037 69.412   1.00 30.15  ? 235 GLU D C   1 
ATOM   14068 O O   . GLU D  1 235 ? -17.723 -62.119 68.887   1.00 26.57  ? 235 GLU D O   1 
ATOM   14069 C CB  . GLU D  1 235 ? -17.678 -65.441 68.988   1.00 37.73  ? 235 GLU D CB  1 
ATOM   14070 C CG  . GLU D  1 235 ? -18.980 -65.441 68.206   1.00 49.52  ? 235 GLU D CG  1 
ATOM   14071 C CD  . GLU D  1 235 ? -18.771 -65.789 66.738   1.00 59.13  ? 235 GLU D CD  1 
ATOM   14072 O OE1 . GLU D  1 235 ? -18.365 -66.934 66.443   1.00 61.19  ? 235 GLU D OE1 1 
ATOM   14073 O OE2 . GLU D  1 235 ? -19.009 -64.912 65.880   1.00 61.58  ? 235 GLU D OE2 1 
ATOM   14074 N N   . LEU D  1 236 ? -16.636 -62.975 70.673   1.00 28.01  ? 236 LEU D N   1 
ATOM   14075 C CA  . LEU D  1 236 ? -16.870 -61.787 71.483   1.00 29.42  ? 236 LEU D CA  1 
ATOM   14076 C C   . LEU D  1 236 ? -16.156 -60.582 70.905   1.00 29.76  ? 236 LEU D C   1 
ATOM   14077 O O   . LEU D  1 236 ? -16.677 -59.464 70.971   1.00 27.57  ? 236 LEU D O   1 
ATOM   14078 C CB  . LEU D  1 236 ? -16.420 -62.030 72.927   1.00 23.73  ? 236 LEU D CB  1 
ATOM   14079 C CG  . LEU D  1 236 ? -17.349 -62.979 73.686   1.00 25.81  ? 236 LEU D CG  1 
ATOM   14080 C CD1 . LEU D  1 236 ? -16.767 -63.260 75.057   1.00 29.16  ? 236 LEU D CD1 1 
ATOM   14081 C CD2 . LEU D  1 236 ? -18.747 -62.393 73.766   1.00 28.08  ? 236 LEU D CD2 1 
ATOM   14082 N N   . ALA D  1 237 ? -14.967 -60.783 70.333   1.00 28.74  ? 237 ALA D N   1 
ATOM   14083 C CA  . ALA D  1 237 ? -14.282 -59.667 69.695   1.00 25.26  ? 237 ALA D CA  1 
ATOM   14084 C C   . ALA D  1 237 ? -15.101 -59.132 68.531   1.00 26.64  ? 237 ALA D C   1 
ATOM   14085 O O   . ALA D  1 237 ? -15.276 -57.909 68.384   1.00 22.23  ? 237 ALA D O   1 
ATOM   14086 C CB  . ALA D  1 237 ? -12.897 -60.090 69.211   1.00 22.54  ? 237 ALA D CB  1 
ATOM   14087 N N   . LYS D  1 238 ? -15.627 -60.038 67.708   1.00 22.18  ? 238 LYS D N   1 
ATOM   14088 C CA  . LYS D  1 238 ? -16.413 -59.614 66.553   1.00 26.78  ? 238 LYS D CA  1 
ATOM   14089 C C   . LYS D  1 238 ? -17.606 -58.789 66.990   1.00 28.82  ? 238 LYS D C   1 
ATOM   14090 O O   . LYS D  1 238 ? -17.925 -57.773 66.361   1.00 28.76  ? 238 LYS D O   1 
ATOM   14091 C CB  . LYS D  1 238 ? -16.863 -60.837 65.746   1.00 23.50  ? 238 LYS D CB  1 
ATOM   14092 C CG  . LYS D  1 238 ? -15.715 -61.574 65.070   1.00 21.05  ? 238 LYS D CG  1 
ATOM   14093 C CD  . LYS D  1 238 ? -16.169 -62.935 64.520   1.00 29.13  ? 238 LYS D CD  1 
ATOM   14094 C CE  . LYS D  1 238 ? -17.261 -62.775 63.472   1.00 38.23  ? 238 LYS D CE  1 
ATOM   14095 N NZ  . LYS D  1 238 ? -17.796 -64.089 63.028   1.00 41.48  ? 238 LYS D NZ  1 
ATOM   14096 N N   . GLU D  1 239 ? -18.266 -59.198 68.088   1.00 27.92  ? 239 GLU D N   1 
ATOM   14097 C CA  . GLU D  1 239 ? -19.425 -58.461 68.576   1.00 27.40  ? 239 GLU D CA  1 
ATOM   14098 C C   . GLU D  1 239 ? -19.035 -57.075 69.071   1.00 29.12  ? 239 GLU D C   1 
ATOM   14099 O O   . GLU D  1 239 ? -19.734 -56.093 68.796   1.00 23.63  ? 239 GLU D O   1 
ATOM   14100 C CB  . GLU D  1 239 ? -20.120 -59.242 69.691   1.00 37.12  ? 239 GLU D CB  1 
ATOM   14101 C CG  . GLU D  1 239 ? -20.774 -60.523 69.234   1.00 49.54  ? 239 GLU D CG  1 
ATOM   14102 C CD  . GLU D  1 239 ? -21.041 -61.480 70.384   1.00 60.94  ? 239 GLU D CD  1 
ATOM   14103 O OE1 . GLU D  1 239 ? -21.048 -62.707 70.135   1.00 65.14  ? 239 GLU D OE1 1 
ATOM   14104 O OE2 . GLU D  1 239 ? -21.243 -61.004 71.527   1.00 58.50  ? 239 GLU D OE2 1 
ATOM   14105 N N   . LYS D  1 240 ? -17.943 -56.978 69.832   1.00 27.56  ? 240 LYS D N   1 
ATOM   14106 C CA  . LYS D  1 240 ? -17.511 -55.681 70.336   1.00 29.61  ? 240 LYS D CA  1 
ATOM   14107 C C   . LYS D  1 240 ? -17.059 -54.780 69.196   1.00 27.78  ? 240 LYS D C   1 
ATOM   14108 O O   . LYS D  1 240 ? -17.329 -53.568 69.197   1.00 26.32  ? 240 LYS D O   1 
ATOM   14109 C CB  . LYS D  1 240 ? -16.375 -55.867 71.335   1.00 26.55  ? 240 LYS D CB  1 
ATOM   14110 C CG  . LYS D  1 240 ? -15.952 -54.609 72.055   1.00 31.95  ? 240 LYS D CG  1 
ATOM   14111 C CD  . LYS D  1 240 ? -16.979 -54.232 73.100   1.00 39.16  ? 240 LYS D CD  1 
ATOM   14112 C CE  . LYS D  1 240 ? -16.656 -52.886 73.707   1.00 40.34  ? 240 LYS D CE  1 
ATOM   14113 N NZ  . LYS D  1 240 ? -17.658 -52.458 74.718   1.00 38.44  ? 240 LYS D NZ  1 
ATOM   14114 N N   . TYR D  1 241 ? -16.327 -55.349 68.240   1.00 21.04  ? 241 TYR D N   1 
ATOM   14115 C CA  . TYR D  1 241 ? -15.918 -54.573 67.077   1.00 22.52  ? 241 TYR D CA  1 
ATOM   14116 C C   . TYR D  1 241 ? -17.138 -54.022 66.353   1.00 24.67  ? 241 TYR D C   1 
ATOM   14117 O O   . TYR D  1 241 ? -17.173 -52.843 65.978   1.00 24.40  ? 241 TYR D O   1 
ATOM   14118 C CB  . TYR D  1 241 ? -15.077 -55.449 66.159   1.00 24.62  ? 241 TYR D CB  1 
ATOM   14119 C CG  . TYR D  1 241 ? -14.500 -54.737 64.964   1.00 20.30  ? 241 TYR D CG  1 
ATOM   14120 C CD1 . TYR D  1 241 ? -15.264 -54.552 63.813   1.00 20.26  ? 241 TYR D CD1 1 
ATOM   14121 C CD2 . TYR D  1 241 ? -13.192 -54.288 64.968   1.00 21.05  ? 241 TYR D CD2 1 
ATOM   14122 C CE1 . TYR D  1 241 ? -14.738 -53.904 62.698   1.00 28.08  ? 241 TYR D CE1 1 
ATOM   14123 C CE2 . TYR D  1 241 ? -12.655 -53.650 63.857   1.00 25.45  ? 241 TYR D CE2 1 
ATOM   14124 C CZ  . TYR D  1 241 ? -13.434 -53.458 62.728   1.00 29.48  ? 241 TYR D CZ  1 
ATOM   14125 O OH  . TYR D  1 241 ? -12.893 -52.835 61.623   1.00 26.68  ? 241 TYR D OH  1 
ATOM   14126 N N   . PHE D  1 242 ? -18.179 -54.846 66.220   1.00 25.96  ? 242 PHE D N   1 
ATOM   14127 C CA  . PHE D  1 242 ? -19.398 -54.407 65.553   1.00 28.00  ? 242 PHE D CA  1 
ATOM   14128 C C   . PHE D  1 242 ? -20.049 -53.240 66.283   1.00 27.56  ? 242 PHE D C   1 
ATOM   14129 O O   . PHE D  1 242 ? -20.565 -52.317 65.646   1.00 24.77  ? 242 PHE D O   1 
ATOM   14130 C CB  . PHE D  1 242 ? -20.398 -55.550 65.441   1.00 24.57  ? 242 PHE D CB  1 
ATOM   14131 C CG  . PHE D  1 242 ? -21.638 -55.159 64.688   1.00 30.04  ? 242 PHE D CG  1 
ATOM   14132 C CD1 . PHE D  1 242 ? -22.711 -54.569 65.343   1.00 28.90  ? 242 PHE D CD1 1 
ATOM   14133 C CD2 . PHE D  1 242 ? -21.701 -55.325 63.308   1.00 29.38  ? 242 PHE D CD2 1 
ATOM   14134 C CE1 . PHE D  1 242 ? -23.840 -54.178 64.650   1.00 31.04  ? 242 PHE D CE1 1 
ATOM   14135 C CE2 . PHE D  1 242 ? -22.839 -54.944 62.606   1.00 28.55  ? 242 PHE D CE2 1 
ATOM   14136 C CZ  . PHE D  1 242 ? -23.903 -54.368 63.278   1.00 30.40  ? 242 PHE D CZ  1 
ATOM   14137 N N   . GLU D  1 243 ? -20.077 -53.290 67.621   1.00 29.75  ? 243 GLU D N   1 
ATOM   14138 C CA  . GLU D  1 243 ? -20.691 -52.214 68.392   1.00 32.83  ? 243 GLU D CA  1 
ATOM   14139 C C   . GLU D  1 243 ? -20.002 -50.883 68.123   1.00 28.60  ? 243 GLU D C   1 
ATOM   14140 O O   . GLU D  1 243 ? -20.658 -49.836 68.053   1.00 26.22  ? 243 GLU D O   1 
ATOM   14141 C CB  . GLU D  1 243 ? -20.640 -52.545 69.889   1.00 35.15  ? 243 GLU D CB  1 
ATOM   14142 C CG  . GLU D  1 243 ? -21.049 -51.408 70.812   1.00 44.05  ? 243 GLU D CG  1 
ATOM   14143 C CD  . GLU D  1 243 ? -20.561 -51.611 72.252   1.00 53.39  ? 243 GLU D CD  1 
ATOM   14144 O OE1 . GLU D  1 243 ? -20.384 -50.603 72.975   1.00 54.38  ? 243 GLU D OE1 1 
ATOM   14145 O OE2 . GLU D  1 243 ? -20.352 -52.778 72.655   1.00 53.68  ? 243 GLU D OE2 1 
ATOM   14146 N N   . ILE D  1 244 ? -18.680 -50.905 67.980   1.00 23.53  ? 244 ILE D N   1 
ATOM   14147 C CA  . ILE D  1 244 ? -17.941 -49.665 67.805   1.00 26.71  ? 244 ILE D CA  1 
ATOM   14148 C C   . ILE D  1 244 ? -17.966 -49.243 66.352   1.00 24.83  ? 244 ILE D C   1 
ATOM   14149 O O   . ILE D  1 244 ? -18.120 -48.060 66.043   1.00 23.70  ? 244 ILE D O   1 
ATOM   14150 C CB  . ILE D  1 244 ? -16.495 -49.814 68.310   1.00 27.77  ? 244 ILE D CB  1 
ATOM   14151 C CG1 . ILE D  1 244 ? -16.472 -50.199 69.796   1.00 27.80  ? 244 ILE D CG1 1 
ATOM   14152 C CG2 . ILE D  1 244 ? -15.679 -48.546 68.025   1.00 23.11  ? 244 ILE D CG2 1 
ATOM   14153 C CD1 . ILE D  1 244 ? -16.991 -49.135 70.718   1.00 29.42  ? 244 ILE D CD1 1 
ATOM   14154 N N   . PHE D  1 245 ? -17.840 -50.196 65.440   1.00 22.52  ? 245 PHE D N   1 
ATOM   14155 C CA  . PHE D  1 245 ? -17.530 -49.850 64.060   1.00 25.20  ? 245 PHE D CA  1 
ATOM   14156 C C   . PHE D  1 245 ? -18.625 -50.205 63.082   1.00 24.53  ? 245 PHE D C   1 
ATOM   14157 O O   . PHE D  1 245 ? -18.580 -49.742 61.937   1.00 29.99  ? 245 PHE D O   1 
ATOM   14158 C CB  . PHE D  1 245 ? -16.206 -50.499 63.643   1.00 23.41  ? 245 PHE D CB  1 
ATOM   14159 C CG  . PHE D  1 245 ? -15.009 -49.961 64.398   1.00 22.91  ? 245 PHE D CG  1 
ATOM   14160 C CD1 . PHE D  1 245 ? -14.547 -48.652 64.169   1.00 24.55  ? 245 PHE D CD1 1 
ATOM   14161 C CD2 . PHE D  1 245 ? -14.344 -50.750 65.321   1.00 23.23  ? 245 PHE D CD2 1 
ATOM   14162 C CE1 . PHE D  1 245 ? -13.440 -48.153 64.873   1.00 26.11  ? 245 PHE D CE1 1 
ATOM   14163 C CE2 . PHE D  1 245 ? -13.241 -50.263 66.036   1.00 22.50  ? 245 PHE D CE2 1 
ATOM   14164 C CZ  . PHE D  1 245 ? -12.797 -48.973 65.829   1.00 28.77  ? 245 PHE D CZ  1 
ATOM   14165 N N   . GLY D  1 246 ? -19.627 -50.961 63.500   1.00 27.54  ? 246 GLY D N   1 
ATOM   14166 C CA  . GLY D  1 246 ? -20.764 -51.192 62.643   1.00 33.51  ? 246 GLY D CA  1 
ATOM   14167 C C   . GLY D  1 246 ? -20.555 -52.212 61.549   1.00 33.64  ? 246 GLY D C   1 
ATOM   14168 O O   . GLY D  1 246 ? -21.343 -52.242 60.597   1.00 35.25  ? 246 GLY D O   1 
ATOM   14169 N N   . GLU D  1 247 ? -19.521 -53.042 61.655   1.00 32.42  ? 247 GLU D N   1 
ATOM   14170 C CA  . GLU D  1 247 ? -19.292 -54.164 60.761   1.00 32.15  ? 247 GLU D CA  1 
ATOM   14171 C C   . GLU D  1 247 ? -18.637 -55.277 61.565   1.00 29.17  ? 247 GLU D C   1 
ATOM   14172 O O   . GLU D  1 247 ? -18.000 -55.032 62.589   1.00 24.92  ? 247 GLU D O   1 
ATOM   14173 C CB  . GLU D  1 247 ? -18.391 -53.773 59.568   1.00 39.88  ? 247 GLU D CB  1 
ATOM   14174 C CG  . GLU D  1 247 ? -16.877 -53.864 59.860   1.00 47.19  ? 247 GLU D CG  1 
ATOM   14175 C CD  . GLU D  1 247 ? -15.998 -53.456 58.670   1.00 56.21  ? 247 GLU D CD  1 
ATOM   14176 O OE1 . GLU D  1 247 ? -16.557 -52.986 57.658   1.00 57.39  ? 247 GLU D OE1 1 
ATOM   14177 O OE2 . GLU D  1 247 ? -14.754 -53.613 58.744   1.00 57.88  ? 247 GLU D OE2 1 
ATOM   14178 N N   . HIS D  1 248 ? -18.795 -56.502 61.095   1.00 30.21  ? 248 HIS D N   1 
ATOM   14179 C CA  . HIS D  1 248 ? -17.952 -57.591 61.586   1.00 29.56  ? 248 HIS D CA  1 
ATOM   14180 C C   . HIS D  1 248 ? -16.531 -57.397 61.065   1.00 28.30  ? 248 HIS D C   1 
ATOM   14181 O O   . HIS D  1 248 ? -16.352 -57.101 59.873   1.00 27.55  ? 248 HIS D O   1 
ATOM   14182 C CB  . HIS D  1 248 ? -18.499 -58.939 61.117   1.00 40.48  ? 248 HIS D CB  1 
ATOM   14183 C CG  . HIS D  1 248 ? -19.846 -59.285 61.677   1.00 54.95  ? 248 HIS D CG  1 
ATOM   14184 N ND1 . HIS D  1 248 ? -20.062 -59.512 63.021   1.00 58.72  ? 248 HIS D ND1 1 
ATOM   14185 C CD2 . HIS D  1 248 ? -21.047 -59.454 61.071   1.00 60.15  ? 248 HIS D CD2 1 
ATOM   14186 C CE1 . HIS D  1 248 ? -21.336 -59.805 63.219   1.00 59.85  ? 248 HIS D CE1 1 
ATOM   14187 N NE2 . HIS D  1 248 ? -21.956 -59.776 62.053   1.00 60.74  ? 248 HIS D NE2 1 
ATOM   14188 N N   . PRO D  1 249 ? -15.502 -57.571 61.900   1.00 26.61  ? 249 PRO D N   1 
ATOM   14189 C CA  . PRO D  1 249 ? -14.127 -57.363 61.419   1.00 25.05  ? 249 PRO D CA  1 
ATOM   14190 C C   . PRO D  1 249 ? -13.716 -58.458 60.458   1.00 28.20  ? 249 PRO D C   1 
ATOM   14191 O O   . PRO D  1 249 ? -13.981 -59.641 60.689   1.00 32.56  ? 249 PRO D O   1 
ATOM   14192 C CB  . PRO D  1 249 ? -13.284 -57.409 62.705   1.00 26.92  ? 249 PRO D CB  1 
ATOM   14193 C CG  . PRO D  1 249 ? -14.100 -58.316 63.638   1.00 21.34  ? 249 PRO D CG  1 
ATOM   14194 C CD  . PRO D  1 249 ? -15.545 -58.046 63.301   1.00 25.47  ? 249 PRO D CD  1 
ATOM   14195 N N   . VAL D  1 250 ? -13.056 -58.057 59.368   1.00 25.70  ? 250 VAL D N   1 
ATOM   14196 C CA  . VAL D  1 250 ? -12.548 -59.027 58.402   1.00 26.62  ? 250 VAL D CA  1 
ATOM   14197 C C   . VAL D  1 250 ? -11.046 -59.202 58.499   1.00 25.37  ? 250 VAL D C   1 
ATOM   14198 O O   . VAL D  1 250 ? -10.503 -60.116 57.853   1.00 24.03  ? 250 VAL D O   1 
ATOM   14199 C CB  . VAL D  1 250 ? -12.933 -58.665 56.949   1.00 31.32  ? 250 VAL D CB  1 
ATOM   14200 C CG1 . VAL D  1 250 ? -14.406 -58.920 56.721   1.00 34.68  ? 250 VAL D CG1 1 
ATOM   14201 C CG2 . VAL D  1 250 ? -12.573 -57.236 56.639   1.00 32.01  ? 250 VAL D CG2 1 
ATOM   14202 N N   . TYR D  1 251 ? -10.358 -58.358 59.279   1.00 21.90  ? 251 TYR D N   1 
ATOM   14203 C CA  . TYR D  1 251 ? -8.941  -58.496 59.571   1.00 22.21  ? 251 TYR D CA  1 
ATOM   14204 C C   . TYR D  1 251 ? -8.756  -58.622 61.075   1.00 25.26  ? 251 TYR D C   1 
ATOM   14205 O O   . TYR D  1 251 ? -9.414  -57.923 61.855   1.00 21.74  ? 251 TYR D O   1 
ATOM   14206 C CB  . TYR D  1 251 ? -8.144  -57.298 59.041   1.00 27.98  ? 251 TYR D CB  1 
ATOM   14207 C CG  . TYR D  1 251 ? -8.603  -56.902 57.651   1.00 34.17  ? 251 TYR D CG  1 
ATOM   14208 C CD1 . TYR D  1 251 ? -8.500  -57.800 56.595   1.00 37.34  ? 251 TYR D CD1 1 
ATOM   14209 C CD2 . TYR D  1 251 ? -9.208  -55.671 57.409   1.00 31.16  ? 251 TYR D CD2 1 
ATOM   14210 C CE1 . TYR D  1 251 ? -8.943  -57.474 55.328   1.00 42.02  ? 251 TYR D CE1 1 
ATOM   14211 C CE2 . TYR D  1 251 ? -9.665  -55.340 56.126   1.00 32.09  ? 251 TYR D CE2 1 
ATOM   14212 C CZ  . TYR D  1 251 ? -9.522  -56.249 55.098   1.00 37.43  ? 251 TYR D CZ  1 
ATOM   14213 O OH  . TYR D  1 251 ? -9.962  -55.958 53.826   1.00 40.13  ? 251 TYR D OH  1 
ATOM   14214 N N   . MET D  1 252 ? -7.859  -59.503 61.480   1.00 22.40  ? 252 MET D N   1 
ATOM   14215 C CA  . MET D  1 252 ? -7.469  -59.571 62.882   1.00 25.24  ? 252 MET D CA  1 
ATOM   14216 C C   . MET D  1 252 ? -5.958  -59.619 62.994   1.00 27.30  ? 252 MET D C   1 
ATOM   14217 O O   . MET D  1 252 ? -5.270  -60.143 62.111   1.00 25.58  ? 252 MET D O   1 
ATOM   14218 C CB  . MET D  1 252 ? -8.078  -60.792 63.587   1.00 27.74  ? 252 MET D CB  1 
ATOM   14219 C CG  . MET D  1 252 ? -9.512  -60.608 63.973   1.00 31.36  ? 252 MET D CG  1 
ATOM   14220 S SD  . MET D  1 252 ? -10.092 -61.865 65.125   1.00 29.01  ? 252 MET D SD  1 
ATOM   14221 C CE  . MET D  1 252 ? -11.783 -61.312 65.358   1.00 28.99  ? 252 MET D CE  1 
ATOM   14222 N N   . TRP D  1 253 ? -5.445  -59.038 64.083   1.00 25.77  ? 253 TRP D N   1 
ATOM   14223 C CA  . TRP D  1 253 ? -4.061  -59.252 64.478   1.00 25.41  ? 253 TRP D CA  1 
ATOM   14224 C C   . TRP D  1 253 ? -4.017  -60.394 65.482   1.00 28.22  ? 253 TRP D C   1 
ATOM   14225 O O   . TRP D  1 253 ? -4.641  -60.289 66.555   1.00 21.91  ? 253 TRP D O   1 
ATOM   14226 C CB  . TRP D  1 253 ? -3.465  -57.984 65.079   1.00 22.02  ? 253 TRP D CB  1 
ATOM   14227 C CG  . TRP D  1 253 ? -2.154  -58.220 65.750   1.00 18.59  ? 253 TRP D CG  1 
ATOM   14228 C CD1 . TRP D  1 253 ? -1.895  -58.153 67.094   1.00 21.54  ? 253 TRP D CD1 1 
ATOM   14229 C CD2 . TRP D  1 253 ? -0.921  -58.554 65.113   1.00 18.63  ? 253 TRP D CD2 1 
ATOM   14230 N NE1 . TRP D  1 253 ? -0.564  -58.436 67.335   1.00 23.28  ? 253 TRP D NE1 1 
ATOM   14231 C CE2 . TRP D  1 253 ? 0.054   -58.691 66.132   1.00 20.49  ? 253 TRP D CE2 1 
ATOM   14232 C CE3 . TRP D  1 253 ? -0.541  -58.758 63.766   1.00 21.07  ? 253 TRP D CE3 1 
ATOM   14233 C CZ2 . TRP D  1 253 ? 1.389   -59.027 65.856   1.00 20.49  ? 253 TRP D CZ2 1 
ATOM   14234 C CZ3 . TRP D  1 253 ? 0.791   -59.111 63.489   1.00 20.14  ? 253 TRP D CZ3 1 
ATOM   14235 C CH2 . TRP D  1 253 ? 1.744   -59.225 64.533   1.00 23.57  ? 253 TRP D CH2 1 
ATOM   14236 N N   . PRO D  1 254 ? -3.383  -61.521 65.163   1.00 30.00  ? 254 PRO D N   1 
ATOM   14237 C CA  . PRO D  1 254 ? -3.308  -62.612 66.127   1.00 26.90  ? 254 PRO D CA  1 
ATOM   14238 C C   . PRO D  1 254 ? -2.339  -62.235 67.232   1.00 22.84  ? 254 PRO D C   1 
ATOM   14239 O O   . PRO D  1 254 ? -1.215  -61.790 66.955   1.00 25.45  ? 254 PRO D O   1 
ATOM   14240 C CB  . PRO D  1 254 ? -2.804  -63.798 65.290   1.00 26.89  ? 254 PRO D CB  1 
ATOM   14241 C CG  . PRO D  1 254 ? -2.015  -63.147 64.184   1.00 26.83  ? 254 PRO D CG  1 
ATOM   14242 C CD  . PRO D  1 254 ? -2.661  -61.823 63.913   1.00 27.21  ? 254 PRO D CD  1 
ATOM   14243 N N   . PRO D  1 255 ? -2.763  -62.318 68.491   1.00 22.09  ? 255 PRO D N   1 
ATOM   14244 C CA  . PRO D  1 255 ? -1.910  -61.832 69.588   1.00 18.72  ? 255 PRO D CA  1 
ATOM   14245 C C   . PRO D  1 255 ? -0.534  -62.473 69.543   1.00 22.24  ? 255 PRO D C   1 
ATOM   14246 O O   . PRO D  1 255 ? -0.396  -63.673 69.281   1.00 19.45  ? 255 PRO D O   1 
ATOM   14247 C CB  . PRO D  1 255 ? -2.690  -62.231 70.850   1.00 21.39  ? 255 PRO D CB  1 
ATOM   14248 C CG  . PRO D  1 255 ? -4.143  -62.194 70.394   1.00 21.11  ? 255 PRO D CG  1 
ATOM   14249 C CD  . PRO D  1 255 ? -4.110  -62.709 68.949   1.00 22.03  ? 255 PRO D CD  1 
ATOM   14250 N N   . GLU D  1 256 ? 0.488   -61.647 69.768   1.00 19.01  ? 256 GLU D N   1 
ATOM   14251 C CA  . GLU D  1 256 ? 1.886   -62.059 69.636   1.00 23.96  ? 256 GLU D CA  1 
ATOM   14252 C C   . GLU D  1 256 ? 2.178   -62.632 68.257   1.00 25.89  ? 256 GLU D C   1 
ATOM   14253 O O   . GLU D  1 256 ? 3.053   -63.494 68.110   1.00 21.76  ? 256 GLU D O   1 
ATOM   14254 C CB  . GLU D  1 256 ? 2.287   -63.077 70.710   1.00 24.16  ? 256 GLU D CB  1 
ATOM   14255 C CG  . GLU D  1 256 ? 1.831   -62.732 72.112   1.00 22.13  ? 256 GLU D CG  1 
ATOM   14256 C CD  . GLU D  1 256 ? 2.360   -61.397 72.601   1.00 24.95  ? 256 GLU D CD  1 
ATOM   14257 O OE1 . GLU D  1 256 ? 3.440   -60.955 72.137   1.00 23.28  ? 256 GLU D OE1 1 
ATOM   14258 O OE2 . GLU D  1 256 ? 1.699   -60.800 73.476   1.00 26.03  ? 256 GLU D OE2 1 
ATOM   14259 N N   . ALA D  1 257 ? 1.426   -62.195 67.236   1.00 20.96  ? 257 ALA D N   1 
ATOM   14260 C CA  . ALA D  1 257 ? 1.577   -62.758 65.898   1.00 18.77  ? 257 ALA D CA  1 
ATOM   14261 C C   . ALA D  1 257 ? 1.406   -64.268 65.902   1.00 22.12  ? 257 ALA D C   1 
ATOM   14262 O O   . ALA D  1 257 ? 1.865   -64.942 64.987   1.00 20.73  ? 257 ALA D O   1 
ATOM   14263 C CB  . ALA D  1 257 ? 2.944   -62.413 65.297   1.00 20.75  ? 257 ALA D CB  1 
ATOM   14264 N N   A SER D  1 258 ? 0.763   -64.823 66.927   0.27 25.58  ? 258 SER D N   1 
ATOM   14265 N N   B SER D  1 258 ? 0.737   -64.815 66.916   0.73 26.23  ? 258 SER D N   1 
ATOM   14266 C CA  A SER D  1 258 ? 0.803   -66.262 67.146   0.27 26.09  ? 258 SER D CA  1 
ATOM   14267 C CA  B SER D  1 258 ? 0.780   -66.255 67.140   0.73 26.51  ? 258 SER D CA  1 
ATOM   14268 C C   A SER D  1 258 ? -0.181  -66.977 66.234   0.27 25.60  ? 258 SER D C   1 
ATOM   14269 C C   B SER D  1 258 ? -0.192  -66.979 66.224   0.73 25.76  ? 258 SER D C   1 
ATOM   14270 O O   A SER D  1 258 ? -1.371  -66.646 66.206   0.27 25.65  ? 258 SER D O   1 
ATOM   14271 O O   B SER D  1 258 ? -1.385  -66.661 66.190   0.73 25.68  ? 258 SER D O   1 
ATOM   14272 C CB  A SER D  1 258 ? 0.505   -66.587 68.609   0.27 25.69  ? 258 SER D CB  1 
ATOM   14273 C CB  B SER D  1 258 ? 0.469   -66.595 68.597   0.73 24.58  ? 258 SER D CB  1 
ATOM   14274 O OG  A SER D  1 258 ? -0.759  -66.082 68.987   0.27 30.28  ? 258 SER D OG  1 
ATOM   14275 O OG  B SER D  1 258 ? 0.630   -67.990 68.794   0.73 22.34  ? 258 SER D OG  1 
ATOM   14276 N N   . VAL D  1 259 ? 0.319   -67.962 65.486   1.00 22.98  ? 259 VAL D N   1 
ATOM   14277 C CA  . VAL D  1 259 ? -0.501  -68.736 64.570   1.00 25.39  ? 259 VAL D CA  1 
ATOM   14278 C C   . VAL D  1 259 ? -0.117  -70.200 64.686   1.00 25.06  ? 259 VAL D C   1 
ATOM   14279 O O   . VAL D  1 259 ? 0.976   -70.560 65.130   1.00 22.24  ? 259 VAL D O   1 
ATOM   14280 C CB  . VAL D  1 259 ? -0.395  -68.269 63.090   1.00 27.04  ? 259 VAL D CB  1 
ATOM   14281 C CG1 . VAL D  1 259 ? -0.967  -66.855 62.919   1.00 25.27  ? 259 VAL D CG1 1 
ATOM   14282 C CG2 . VAL D  1 259 ? 1.033   -68.347 62.579   1.00 26.65  ? 259 VAL D CG2 1 
ATOM   14283 N N   . SER D  1 260 ? -1.068  -71.040 64.306   1.00 23.12  ? 260 SER D N   1 
ATOM   14284 C CA  . SER D  1 260 ? -0.854  -72.456 64.067   1.00 27.44  ? 260 SER D CA  1 
ATOM   14285 C C   . SER D  1 260 ? -1.816  -72.826 62.955   1.00 27.06  ? 260 SER D C   1 
ATOM   14286 O O   . SER D  1 260 ? -2.673  -72.024 62.572   1.00 27.86  ? 260 SER D O   1 
ATOM   14287 C CB  . SER D  1 260 ? -1.108  -73.290 65.327   1.00 22.55  ? 260 SER D CB  1 
ATOM   14288 O OG  . SER D  1 260 ? -2.476  -73.232 65.715   1.00 28.13  ? 260 SER D OG  1 
ATOM   14289 N N   . ASN D  1 261 ? -1.678  -74.047 62.442   1.00 22.44  ? 261 ASN D N   1 
ATOM   14290 C CA  . ASN D  1 261 ? -2.611  -74.515 61.426   1.00 24.55  ? 261 ASN D CA  1 
ATOM   14291 C C   . ASN D  1 261 ? -4.044  -74.447 61.938   1.00 25.56  ? 261 ASN D C   1 
ATOM   14292 O O   . ASN D  1 261 ? -4.948  -73.994 61.223   1.00 24.76  ? 261 ASN D O   1 
ATOM   14293 C CB  . ASN D  1 261 ? -2.248  -75.939 60.992   1.00 27.54  ? 261 ASN D CB  1 
ATOM   14294 C CG  . ASN D  1 261 ? -1.017  -75.977 60.120   1.00 27.77  ? 261 ASN D CG  1 
ATOM   14295 O OD1 . ASN D  1 261 ? -0.746  -75.032 59.393   1.00 26.64  ? 261 ASN D OD1 1 
ATOM   14296 N ND2 . ASN D  1 261 ? -0.260  -77.066 60.194   1.00 27.10  ? 261 ASN D ND2 1 
ATOM   14297 N N   . GLU D  1 262 ? -4.261  -74.866 63.188   1.00 23.88  ? 262 GLU D N   1 
ATOM   14298 C CA  . GLU D  1 262 ? -5.598  -74.832 63.775   1.00 24.66  ? 262 GLU D CA  1 
ATOM   14299 C C   . GLU D  1 262 ? -6.068  -73.414 64.084   1.00 21.65  ? 262 GLU D C   1 
ATOM   14300 O O   . GLU D  1 262 ? -7.272  -73.146 64.033   1.00 26.77  ? 262 GLU D O   1 
ATOM   14301 C CB  . GLU D  1 262 ? -5.639  -75.673 65.054   1.00 28.96  ? 262 GLU D CB  1 
ATOM   14302 C CG  . GLU D  1 262 ? -5.315  -77.124 64.831   1.00 35.27  ? 262 GLU D CG  1 
ATOM   14303 C CD  . GLU D  1 262 ? -5.503  -77.959 66.076   1.00 41.34  ? 262 GLU D CD  1 
ATOM   14304 O OE1 . GLU D  1 262 ? -6.433  -77.650 66.850   1.00 41.80  ? 262 GLU D OE1 1 
ATOM   14305 O OE2 . GLU D  1 262 ? -4.724  -78.919 66.275   1.00 45.94  ? 262 GLU D OE2 1 
ATOM   14306 N N   . ALA D  1 263 ? -5.167  -72.505 64.457   1.00 20.71  ? 263 ALA D N   1 
ATOM   14307 C CA  . ALA D  1 263 ? -5.610  -71.127 64.677   1.00 25.84  ? 263 ALA D CA  1 
ATOM   14308 C C   . ALA D  1 263 ? -6.034  -70.466 63.366   1.00 23.73  ? 263 ALA D C   1 
ATOM   14309 O O   . ALA D  1 263 ? -7.046  -69.755 63.310   1.00 24.88  ? 263 ALA D O   1 
ATOM   14310 C CB  . ALA D  1 263 ? -4.513  -70.323 65.373   1.00 25.72  ? 263 ALA D CB  1 
ATOM   14311 N N   . LEU D  1 264 ? -5.293  -70.709 62.294   1.00 21.80  ? 264 LEU D N   1 
ATOM   14312 C CA  . LEU D  1 264 ? -5.660  -70.129 61.009   1.00 24.53  ? 264 LEU D CA  1 
ATOM   14313 C C   . LEU D  1 264 ? -7.005  -70.664 60.521   1.00 29.01  ? 264 LEU D C   1 
ATOM   14314 O O   . LEU D  1 264 ? -7.835  -69.902 59.999   1.00 27.00  ? 264 LEU D O   1 
ATOM   14315 C CB  . LEU D  1 264 ? -4.551  -70.411 60.007   1.00 22.18  ? 264 LEU D CB  1 
ATOM   14316 C CG  . LEU D  1 264 ? -3.222  -69.748 60.373   1.00 24.98  ? 264 LEU D CG  1 
ATOM   14317 C CD1 . LEU D  1 264 ? -2.083  -70.276 59.516   1.00 25.96  ? 264 LEU D CD1 1 
ATOM   14318 C CD2 . LEU D  1 264 ? -3.361  -68.231 60.225   1.00 31.54  ? 264 LEU D CD2 1 
ATOM   14319 N N   . GLU D  1 265 ? -7.237  -71.974 60.680   1.00 25.51  ? 265 GLU D N   1 
ATOM   14320 C CA  . GLU D  1 265 ? -8.548  -72.543 60.382   1.00 30.91  ? 265 GLU D CA  1 
ATOM   14321 C C   . GLU D  1 265 ? -9.659  -71.869 61.190   1.00 28.87  ? 265 GLU D C   1 
ATOM   14322 O O   . GLU D  1 265 ? -10.758 -71.645 60.671   1.00 27.53  ? 265 GLU D O   1 
ATOM   14323 C CB  . GLU D  1 265 ? -8.533  -74.049 60.661   1.00 33.05  ? 265 GLU D CB  1 
ATOM   14324 C CG  . GLU D  1 265 ? -9.885  -74.729 60.558   1.00 40.79  ? 265 GLU D CG  1 
ATOM   14325 C CD  . GLU D  1 265 ? -10.342 -74.881 59.116   1.00 45.47  ? 265 GLU D CD  1 
ATOM   14326 O OE1 . GLU D  1 265 ? -11.566 -75.000 58.874   1.00 44.57  ? 265 GLU D OE1 1 
ATOM   14327 O OE2 . GLU D  1 265 ? -9.460  -74.880 58.227   1.00 41.40  ? 265 GLU D OE2 1 
ATOM   14328 N N   . LEU D  1 266 ? -9.404  -71.565 62.470   1.00 26.48  ? 266 LEU D N   1 
ATOM   14329 C CA  . LEU D  1 266 ? -10.445 -70.974 63.315   1.00 26.65  ? 266 LEU D CA  1 
ATOM   14330 C C   . LEU D  1 266 ? -10.757 -69.544 62.894   1.00 28.10  ? 266 LEU D C   1 
ATOM   14331 O O   . LEU D  1 266 ? -11.929 -69.147 62.836   1.00 22.82  ? 266 LEU D O   1 
ATOM   14332 C CB  . LEU D  1 266 ? -10.027 -71.000 64.785   1.00 22.37  ? 266 LEU D CB  1 
ATOM   14333 C CG  . LEU D  1 266 ? -10.938 -70.233 65.760   1.00 22.56  ? 266 LEU D CG  1 
ATOM   14334 C CD1 . LEU D  1 266 ? -12.351 -70.806 65.837   1.00 23.79  ? 266 LEU D CD1 1 
ATOM   14335 C CD2 . LEU D  1 266 ? -10.339 -70.169 67.186   1.00 22.25  ? 266 LEU D CD2 1 
ATOM   14336 N N   . TYR D  1 267 ? -9.720  -68.757 62.603   1.00 23.05  ? 267 TYR D N   1 
ATOM   14337 C CA  . TYR D  1 267 ? -9.922  -67.393 62.125   1.00 23.85  ? 267 TYR D CA  1 
ATOM   14338 C C   . TYR D  1 267 ? -10.728 -67.396 60.833   1.00 28.79  ? 267 TYR D C   1 
ATOM   14339 O O   . TYR D  1 267 ? -11.665 -66.607 60.674   1.00 24.72  ? 267 TYR D O   1 
ATOM   14340 C CB  . TYR D  1 267 ? -8.575  -66.696 61.912   1.00 20.92  ? 267 TYR D CB  1 
ATOM   14341 C CG  . TYR D  1 267 ? -7.866  -66.265 63.197   1.00 26.84  ? 267 TYR D CG  1 
ATOM   14342 C CD1 . TYR D  1 267 ? -8.413  -65.292 64.043   1.00 28.60  ? 267 TYR D CD1 1 
ATOM   14343 C CD2 . TYR D  1 267 ? -6.647  -66.821 63.547   1.00 29.39  ? 267 TYR D CD2 1 
ATOM   14344 C CE1 . TYR D  1 267 ? -7.752  -64.890 65.204   1.00 31.54  ? 267 TYR D CE1 1 
ATOM   14345 C CE2 . TYR D  1 267 ? -5.981  -66.442 64.702   1.00 33.56  ? 267 TYR D CE2 1 
ATOM   14346 C CZ  . TYR D  1 267 ? -6.532  -65.479 65.532   1.00 34.90  ? 267 TYR D CZ  1 
ATOM   14347 O OH  . TYR D  1 267 ? -5.845  -65.124 66.681   1.00 29.93  ? 267 TYR D OH  1 
ATOM   14348 N N   . TYR D  1 268 ? -10.387 -68.299 59.905   1.00 29.24  ? 268 TYR D N   1 
ATOM   14349 C CA  . TYR D  1 268 ? -11.167 -68.430 58.677   1.00 25.65  ? 268 TYR D CA  1 
ATOM   14350 C C   . TYR D  1 268 ? -12.621 -68.776 58.991   1.00 27.68  ? 268 TYR D C   1 
ATOM   14351 O O   . TYR D  1 268 ? -13.549 -68.136 58.482   1.00 24.43  ? 268 TYR D O   1 
ATOM   14352 C CB  . TYR D  1 268 ? -10.548 -69.498 57.768   1.00 29.66  ? 268 TYR D CB  1 
ATOM   14353 C CG  . TYR D  1 268 ? -11.559 -70.177 56.867   1.00 30.98  ? 268 TYR D CG  1 
ATOM   14354 C CD1 . TYR D  1 268 ? -12.110 -69.505 55.773   1.00 33.55  ? 268 TYR D CD1 1 
ATOM   14355 C CD2 . TYR D  1 268 ? -11.978 -71.485 57.111   1.00 35.98  ? 268 TYR D CD2 1 
ATOM   14356 C CE1 . TYR D  1 268 ? -13.050 -70.118 54.944   1.00 26.44  ? 268 TYR D CE1 1 
ATOM   14357 C CE2 . TYR D  1 268 ? -12.911 -72.108 56.285   1.00 34.88  ? 268 TYR D CE2 1 
ATOM   14358 C CZ  . TYR D  1 268 ? -13.447 -71.414 55.208   1.00 33.84  ? 268 TYR D CZ  1 
ATOM   14359 O OH  . TYR D  1 268 ? -14.379 -72.008 54.386   1.00 36.47  ? 268 TYR D OH  1 
ATOM   14360 N N   . GLU D  1 269 ? -12.836 -69.788 59.843   1.00 24.31  ? 269 GLU D N   1 
ATOM   14361 C CA  . GLU D  1 269 ? -14.194 -70.233 60.135   1.00 28.84  ? 269 GLU D CA  1 
ATOM   14362 C C   . GLU D  1 269 ? -15.035 -69.122 60.751   1.00 30.00  ? 269 GLU D C   1 
ATOM   14363 O O   . GLU D  1 269 ? -16.262 -69.138 60.630   1.00 36.76  ? 269 GLU D O   1 
ATOM   14364 C CB  . GLU D  1 269 ? -14.159 -71.450 61.058   1.00 31.56  ? 269 GLU D CB  1 
ATOM   14365 C CG  . GLU D  1 269 ? -13.940 -72.738 60.322   1.00 39.10  ? 269 GLU D CG  1 
ATOM   14366 C CD  . GLU D  1 269 ? -13.953 -73.929 61.248   1.00 52.19  ? 269 GLU D CD  1 
ATOM   14367 O OE1 . GLU D  1 269 ? -13.412 -74.983 60.856   1.00 55.35  ? 269 GLU D OE1 1 
ATOM   14368 O OE2 . GLU D  1 269 ? -14.501 -73.808 62.371   1.00 55.91  ? 269 GLU D OE2 1 
ATOM   14369 N N   . LYS D  1 270 ? -14.399 -68.157 61.404   1.00 26.76  ? 270 LYS D N   1 
ATOM   14370 C CA  . LYS D  1 270 ? -15.083 -67.036 62.022   1.00 29.06  ? 270 LYS D CA  1 
ATOM   14371 C C   . LYS D  1 270 ? -15.161 -65.821 61.105   1.00 30.65  ? 270 LYS D C   1 
ATOM   14372 O O   . LYS D  1 270 ? -15.499 -64.735 61.570   1.00 23.76  ? 270 LYS D O   1 
ATOM   14373 C CB  . LYS D  1 270 ? -14.378 -66.666 63.331   1.00 30.36  ? 270 LYS D CB  1 
ATOM   14374 C CG  . LYS D  1 270 ? -14.438 -67.754 64.380   1.00 30.45  ? 270 LYS D CG  1 
ATOM   14375 C CD  . LYS D  1 270 ? -15.845 -67.907 64.910   1.00 38.87  ? 270 LYS D CD  1 
ATOM   14376 C CE  . LYS D  1 270 ? -15.985 -69.087 65.853   1.00 45.20  ? 270 LYS D CE  1 
ATOM   14377 N NZ  . LYS D  1 270 ? -17.412 -69.510 65.987   1.00 48.92  ? 270 LYS D NZ  1 
ATOM   14378 N N   . GLY D  1 271 ? -14.851 -65.976 59.821   1.00 31.67  ? 271 GLY D N   1 
ATOM   14379 C CA  . GLY D  1 271 ? -15.026 -64.907 58.866   1.00 28.06  ? 271 GLY D CA  1 
ATOM   14380 C C   . GLY D  1 271 ? -13.850 -63.973 58.734   1.00 29.62  ? 271 GLY D C   1 
ATOM   14381 O O   . GLY D  1 271 ? -13.986 -62.919 58.101   1.00 30.03  ? 271 GLY D O   1 
ATOM   14382 N N   . ILE D  1 272 ? -12.700 -64.314 59.308   1.00 26.64  ? 272 ILE D N   1 
ATOM   14383 C CA  . ILE D  1 272 ? -11.526 -63.463 59.163   1.00 26.43  ? 272 ILE D CA  1 
ATOM   14384 C C   . ILE D  1 272 ? -10.887 -63.773 57.818   1.00 27.01  ? 272 ILE D C   1 
ATOM   14385 O O   . ILE D  1 272 ? -10.547 -64.924 57.525   1.00 31.75  ? 272 ILE D O   1 
ATOM   14386 C CB  . ILE D  1 272 ? -10.527 -63.656 60.314   1.00 25.63  ? 272 ILE D CB  1 
ATOM   14387 C CG1 . ILE D  1 272 ? -11.201 -63.397 61.664   1.00 29.07  ? 272 ILE D CG1 1 
ATOM   14388 C CG2 . ILE D  1 272 ? -9.296  -62.765 60.094   1.00 24.01  ? 272 ILE D CG2 1 
ATOM   14389 C CD1 . ILE D  1 272 ? -12.007 -62.092 61.739   1.00 32.03  ? 272 ILE D CD1 1 
ATOM   14390 N N   . ASN D  1 273 ? -10.728 -62.746 57.003   1.00 23.53  ? 273 ASN D N   1 
ATOM   14391 C CA  . ASN D  1 273 ? -10.257 -62.890 55.635   1.00 24.88  ? 273 ASN D CA  1 
ATOM   14392 C C   . ASN D  1 273 ? -8.763  -62.681 55.504   1.00 27.35  ? 273 ASN D C   1 
ATOM   14393 O O   . ASN D  1 273 ? -8.159  -63.201 54.556   1.00 29.02  ? 273 ASN D O   1 
ATOM   14394 C CB  . ASN D  1 273 ? -10.982 -61.886 54.731   1.00 31.89  ? 273 ASN D CB  1 
ATOM   14395 C CG  . ASN D  1 273 ? -12.378 -62.331 54.365   1.00 43.81  ? 273 ASN D CG  1 
ATOM   14396 O OD1 . ASN D  1 273 ? -12.627 -63.516 54.141   1.00 50.93  ? 273 ASN D OD1 1 
ATOM   14397 N ND2 . ASN D  1 273 ? -13.303 -61.379 54.293   1.00 46.49  ? 273 ASN D ND2 1 
ATOM   14398 N N   . MET D  1 274 ? -8.156  -61.932 56.426   1.00 25.32  ? 274 MET D N   1 
ATOM   14399 C CA  . MET D  1 274 ? -6.728  -61.668 56.373   1.00 24.99  ? 274 MET D CA  1 
ATOM   14400 C C   . MET D  1 274 ? -6.190  -61.418 57.774   1.00 29.35  ? 274 MET D C   1 
ATOM   14401 O O   . MET D  1 274 ? -6.853  -60.807 58.616   1.00 29.71  ? 274 MET D O   1 
ATOM   14402 C CB  . MET D  1 274 ? -6.409  -60.471 55.468   1.00 28.19  ? 274 MET D CB  1 
ATOM   14403 C CG  . MET D  1 274 ? -4.927  -60.269 55.217   1.00 37.81  ? 274 MET D CG  1 
ATOM   14404 S SD  . MET D  1 274 ? -4.214  -59.113 56.417   1.00 50.22  ? 274 MET D SD  1 
ATOM   14405 C CE  . MET D  1 274 ? -4.678  -57.569 55.626   1.00 48.21  ? 274 MET D CE  1 
ATOM   14406 N N   . LEU D  1 275 ? -4.984  -61.909 58.014   1.00 32.07  ? 275 LEU D N   1 
ATOM   14407 C CA  . LEU D  1 275 ? -4.230  -61.550 59.196   1.00 31.13  ? 275 LEU D CA  1 
ATOM   14408 C C   . LEU D  1 275 ? -2.774  -61.386 58.784   1.00 30.49  ? 275 LEU D C   1 
ATOM   14409 O O   . LEU D  1 275 ? -2.396  -61.608 57.627   1.00 27.51  ? 275 LEU D O   1 
ATOM   14410 C CB  . LEU D  1 275 ? -4.425  -62.589 60.307   1.00 29.32  ? 275 LEU D CB  1 
ATOM   14411 C CG  . LEU D  1 275 ? -4.264  -64.060 59.949   1.00 30.98  ? 275 LEU D CG  1 
ATOM   14412 C CD1 . LEU D  1 275 ? -2.805  -64.430 59.988   1.00 26.12  ? 275 LEU D CD1 1 
ATOM   14413 C CD2 . LEU D  1 275 ? -5.073  -64.949 60.908   1.00 35.38  ? 275 LEU D CD2 1 
ATOM   14414 N N   . ALA D  1 276 ? -1.953  -60.973 59.735   1.00 26.55  ? 276 ALA D N   1 
ATOM   14415 C CA  . ALA D  1 276 ? -0.516  -60.978 59.553   1.00 23.85  ? 276 ALA D CA  1 
ATOM   14416 C C   . ALA D  1 276 ? 0.107   -61.739 60.706   1.00 23.85  ? 276 ALA D C   1 
ATOM   14417 O O   . ALA D  1 276 ? -0.516  -61.935 61.751   1.00 21.83  ? 276 ALA D O   1 
ATOM   14418 C CB  . ALA D  1 276 ? 0.070   -59.563 59.485   1.00 23.67  ? 276 ALA D CB  1 
ATOM   14419 N N   . THR D  1 277 ? 1.340   -62.173 60.492   1.00 22.38  ? 277 THR D N   1 
ATOM   14420 C CA  . THR D  1 277 ? 2.132   -62.862 61.504   1.00 26.56  ? 277 THR D CA  1 
ATOM   14421 C C   . THR D  1 277 ? 3.594   -62.534 61.213   1.00 26.50  ? 277 THR D C   1 
ATOM   14422 O O   . THR D  1 277 ? 3.884   -61.578 60.490   1.00 26.89  ? 277 THR D O   1 
ATOM   14423 C CB  . THR D  1 277 ? 1.822   -64.378 61.538   1.00 25.45  ? 277 THR D CB  1 
ATOM   14424 O OG1 . THR D  1 277 ? 2.641   -64.995 62.533   1.00 26.16  ? 277 THR D OG1 1 
ATOM   14425 C CG2 . THR D  1 277 ? 2.084   -65.055 60.204   1.00 27.00  ? 277 THR D CG2 1 
ATOM   14426 N N   . ASP D  1 278 ? 4.517   -63.309 61.782   1.00 27.68  ? 278 ASP D N   1 
ATOM   14427 C CA  . ASP D  1 278 ? 5.913   -62.907 61.808   1.00 25.54  ? 278 ASP D CA  1 
ATOM   14428 C C   . ASP D  1 278 ? 6.769   -63.614 60.758   1.00 23.86  ? 278 ASP D C   1 
ATOM   14429 O O   . ASP D  1 278 ? 6.521   -64.762 60.375   1.00 23.04  ? 278 ASP D O   1 
ATOM   14430 C CB  . ASP D  1 278 ? 6.511   -63.153 63.189   1.00 25.64  ? 278 ASP D CB  1 
ATOM   14431 C CG  . ASP D  1 278 ? 7.870   -62.516 63.344   1.00 30.95  ? 278 ASP D CG  1 
ATOM   14432 O OD1 . ASP D  1 278 ? 7.997   -61.306 63.068   1.00 35.78  ? 278 ASP D OD1 1 
ATOM   14433 O OD2 . ASP D  1 278 ? 8.813   -63.220 63.742   1.00 33.74  ? 278 ASP D OD2 1 
ATOM   14434 N N   . GLU D  1 279 ? 7.818   -62.905 60.342   1.00 25.17  ? 279 GLU D N   1 
ATOM   14435 C CA  . GLU D  1 279 ? 8.798   -63.435 59.411   1.00 26.45  ? 279 GLU D CA  1 
ATOM   14436 C C   . GLU D  1 279 ? 9.487   -64.669 59.965   1.00 29.58  ? 279 GLU D C   1 
ATOM   14437 O O   . GLU D  1 279 ? 9.852   -65.562 59.198   1.00 34.46  ? 279 GLU D O   1 
ATOM   14438 C CB  . GLU D  1 279 ? 9.825   -62.341 59.074   1.00 29.08  ? 279 GLU D CB  1 
ATOM   14439 C CG  . GLU D  1 279 ? 10.425  -62.489 57.698   1.00 34.21  ? 279 GLU D CG  1 
ATOM   14440 C CD  . GLU D  1 279 ? 11.447  -61.419 57.341   1.00 39.45  ? 279 GLU D CD  1 
ATOM   14441 O OE1 . GLU D  1 279 ? 11.485  -60.331 57.966   1.00 38.78  ? 279 GLU D OE1 1 
ATOM   14442 O OE2 . GLU D  1 279 ? 12.238  -61.694 56.417   1.00 43.71  ? 279 GLU D OE2 1 
ATOM   14443 N N   . VAL D  1 280 ? 9.670   -64.749 61.289   1.00 30.50  ? 280 VAL D N   1 
ATOM   14444 C CA  . VAL D  1 280 ? 10.323  -65.924 61.861   1.00 31.36  ? 280 VAL D CA  1 
ATOM   14445 C C   . VAL D  1 280 ? 9.464   -67.165 61.643   1.00 29.72  ? 280 VAL D C   1 
ATOM   14446 O O   . VAL D  1 280 ? 9.982   -68.261 61.391   1.00 23.78  ? 280 VAL D O   1 
ATOM   14447 C CB  . VAL D  1 280 ? 10.642  -65.704 63.354   1.00 34.27  ? 280 VAL D CB  1 
ATOM   14448 C CG1 . VAL D  1 280 ? 11.152  -66.994 63.980   1.00 37.96  ? 280 VAL D CG1 1 
ATOM   14449 C CG2 . VAL D  1 280 ? 11.680  -64.609 63.525   1.00 34.37  ? 280 VAL D CG2 1 
ATOM   14450 N N   . ILE D  1 281 ? 8.139   -67.013 61.750   1.00 29.73  ? 281 ILE D N   1 
ATOM   14451 C CA  . ILE D  1 281 ? 7.224   -68.114 61.458   1.00 25.55  ? 281 ILE D CA  1 
ATOM   14452 C C   . ILE D  1 281 ? 7.350   -68.530 60.002   1.00 26.47  ? 281 ILE D C   1 
ATOM   14453 O O   . ILE D  1 281 ? 7.441   -69.724 59.682   1.00 32.00  ? 281 ILE D O   1 
ATOM   14454 C CB  . ILE D  1 281 ? 5.774   -67.726 61.791   1.00 27.60  ? 281 ILE D CB  1 
ATOM   14455 C CG1 . ILE D  1 281 ? 5.637   -67.241 63.236   1.00 31.49  ? 281 ILE D CG1 1 
ATOM   14456 C CG2 . ILE D  1 281 ? 4.862   -68.903 61.515   1.00 28.97  ? 281 ILE D CG2 1 
ATOM   14457 C CD1 . ILE D  1 281 ? 6.060   -68.225 64.217   1.00 35.68  ? 281 ILE D CD1 1 
ATOM   14458 N N   . LEU D  1 282 ? 7.342   -67.550 59.094   1.00 27.88  ? 282 LEU D N   1 
ATOM   14459 C CA  . LEU D  1 282 ? 7.588   -67.849 57.685   1.00 27.38  ? 282 LEU D CA  1 
ATOM   14460 C C   . LEU D  1 282 ? 8.870   -68.659 57.504   1.00 27.00  ? 282 LEU D C   1 
ATOM   14461 O O   . LEU D  1 282 ? 8.848   -69.737 56.903   1.00 24.14  ? 282 LEU D O   1 
ATOM   14462 C CB  . LEU D  1 282 ? 7.651   -66.560 56.867   1.00 28.55  ? 282 LEU D CB  1 
ATOM   14463 C CG  . LEU D  1 282 ? 7.785   -66.793 55.358   1.00 26.46  ? 282 LEU D CG  1 
ATOM   14464 C CD1 . LEU D  1 282 ? 6.656   -67.646 54.802   1.00 26.51  ? 282 LEU D CD1 1 
ATOM   14465 C CD2 . LEU D  1 282 ? 7.845   -65.465 54.624   1.00 30.09  ? 282 LEU D CD2 1 
ATOM   14466 N N   . LYS D  1 283 ? 9.993   -68.170 58.046   1.00 31.31  ? 283 LYS D N   1 
ATOM   14467 C CA  . LYS D  1 283 ? 11.267  -68.872 57.862   1.00 35.85  ? 283 LYS D CA  1 
ATOM   14468 C C   . LYS D  1 283 ? 11.200  -70.301 58.389   1.00 36.60  ? 283 LYS D C   1 
ATOM   14469 O O   . LYS D  1 283 ? 11.771  -71.225 57.794   1.00 36.22  ? 283 LYS D O   1 
ATOM   14470 C CB  . LYS D  1 283 ? 12.403  -68.110 58.552   1.00 40.94  ? 283 LYS D CB  1 
ATOM   14471 C CG  . LYS D  1 283 ? 12.598  -66.666 58.090   1.00 49.18  ? 283 LYS D CG  1 
ATOM   14472 C CD  . LYS D  1 283 ? 12.646  -66.572 56.573   1.00 56.33  ? 283 LYS D CD  1 
ATOM   14473 C CE  . LYS D  1 283 ? 11.948  -65.320 56.067   1.00 58.96  ? 283 LYS D CE  1 
ATOM   14474 N NZ  . LYS D  1 283 ? 12.915  -64.226 55.810   1.00 60.63  ? 283 LYS D NZ  1 
ATOM   14475 N N   . ASN D  1 284 ? 10.509  -70.498 59.513   1.00 37.02  ? 284 ASN D N   1 
ATOM   14476 C CA  . ASN D  1 284 ? 10.363  -71.821 60.094   1.00 31.30  ? 284 ASN D CA  1 
ATOM   14477 C C   . ASN D  1 284 ? 9.490   -72.745 59.253   1.00 31.20  ? 284 ASN D C   1 
ATOM   14478 O O   . ASN D  1 284 ? 9.610   -73.971 59.376   1.00 34.81  ? 284 ASN D O   1 
ATOM   14479 C CB  . ASN D  1 284 ? 9.762   -71.704 61.501   1.00 30.32  ? 284 ASN D CB  1 
ATOM   14480 C CG  . ASN D  1 284 ? 10.767  -71.243 62.538   1.00 27.24  ? 284 ASN D CG  1 
ATOM   14481 O OD1 . ASN D  1 284 ? 11.967  -71.159 62.280   1.00 24.44  ? 284 ASN D OD1 1 
ATOM   14482 N ND2 . ASN D  1 284 ? 10.278  -70.967 63.734   1.00 28.26  ? 284 ASN D ND2 1 
ATOM   14483 N N   . SER D  1 285 ? 8.600   -72.193 58.428   1.00 29.57  ? 285 SER D N   1 
ATOM   14484 C CA  . SER D  1 285 ? 7.580   -72.987 57.752   1.00 30.15  ? 285 SER D CA  1 
ATOM   14485 C C   . SER D  1 285 ? 7.919   -73.311 56.307   1.00 30.79  ? 285 SER D C   1 
ATOM   14486 O O   . SER D  1 285 ? 7.525   -74.376 55.823   1.00 27.23  ? 285 SER D O   1 
ATOM   14487 C CB  . SER D  1 285 ? 6.228   -72.269 57.797   1.00 27.48  ? 285 SER D CB  1 
ATOM   14488 O OG  . SER D  1 285 ? 5.879   -71.947 59.135   1.00 36.14  ? 285 SER D OG  1 
ATOM   14489 N N   . VAL D  1 286 ? 8.639   -72.430 55.612   1.00 31.09  ? 286 VAL D N   1 
ATOM   14490 C CA  . VAL D  1 286 ? 8.984   -72.654 54.212   1.00 37.32  ? 286 VAL D CA  1 
ATOM   14491 C C   . VAL D  1 286 ? 10.447  -72.306 53.980   1.00 44.29  ? 286 VAL D C   1 
ATOM   14492 O O   . VAL D  1 286 ? 11.028  -71.461 54.670   1.00 42.88  ? 286 VAL D O   1 
ATOM   14493 C CB  . VAL D  1 286 ? 8.088   -71.848 53.247   1.00 35.83  ? 286 VAL D CB  1 
ATOM   14494 C CG1 . VAL D  1 286 ? 6.612   -72.085 53.537   1.00 35.11  ? 286 VAL D CG1 1 
ATOM   14495 C CG2 . VAL D  1 286 ? 8.402   -70.392 53.339   1.00 37.89  ? 286 VAL D CG2 1 
ATOM   14496 N N   . GLU D  1 287 ? 11.036  -72.975 52.984   1.00 53.30  ? 287 GLU D N   1 
ATOM   14497 C CA  . GLU D  1 287 ? 12.385  -72.698 52.496   1.00 56.23  ? 287 GLU D CA  1 
ATOM   14498 C C   . GLU D  1 287 ? 12.482  -71.328 51.833   1.00 48.86  ? 287 GLU D C   1 
ATOM   14499 O O   . GLU D  1 287 ? 13.162  -70.439 52.358   1.00 45.49  ? 287 GLU D O   1 
ATOM   14500 C CB  . GLU D  1 287 ? 12.823  -73.773 51.501   1.00 64.79  ? 287 GLU D CB  1 
ATOM   14501 C CG  . GLU D  1 287 ? 12.649  -75.191 51.999   1.00 73.20  ? 287 GLU D CG  1 
ATOM   14502 C CD  . GLU D  1 287 ? 12.231  -76.155 50.897   1.00 78.28  ? 287 GLU D CD  1 
ATOM   14503 O OE1 . GLU D  1 287 ? 11.772  -75.693 49.827   1.00 79.06  ? 287 GLU D OE1 1 
ATOM   14504 O OE2 . GLU D  1 287 ? 12.358  -77.380 51.110   1.00 79.91  ? 287 GLU D OE2 1 
ATOM   14505 N N   . ARG D  1 288 ? 11.820  -71.161 50.678   1.00 54.54  ? 288 ARG D N   1 
ATOM   14506 C CA  . ARG D  1 288 ? 11.856  -69.930 49.871   1.00 63.68  ? 288 ARG D CA  1 
ATOM   14507 C C   . ARG D  1 288 ? 10.907  -68.905 50.485   1.00 61.55  ? 288 ARG D C   1 
ATOM   14508 O O   . ARG D  1 288 ? 9.738   -68.790 50.108   1.00 64.52  ? 288 ARG D O   1 
ATOM   14509 C CB  . ARG D  1 288 ? 11.481  -70.218 48.419   1.00 70.89  ? 288 ARG D CB  1 
ATOM   14510 C CG  . ARG D  1 288 ? 12.009  -71.533 47.853   1.00 77.96  ? 288 ARG D CG  1 
ATOM   14511 C CD  . ARG D  1 288 ? 11.425  -71.837 46.469   1.00 83.25  ? 288 ARG D CD  1 
ATOM   14512 N NE  . ARG D  1 288 ? 10.049  -72.330 46.536   1.00 87.07  ? 288 ARG D NE  1 
ATOM   14513 C CZ  . ARG D  1 288 ? 8.962   -71.572 46.384   1.00 90.64  ? 288 ARG D CZ  1 
ATOM   14514 N NH1 . ARG D  1 288 ? 7.756   -72.122 46.464   1.00 91.35  ? 288 ARG D NH1 1 
ATOM   14515 N NH2 . ARG D  1 288 ? 9.073   -70.265 46.156   1.00 90.94  ? 288 ARG D NH2 1 
ATOM   14516 N N   . ALA D  1 289 ? 11.414  -68.134 51.434   1.00 54.08  ? 289 ALA D N   1 
ATOM   14517 C CA  . ALA D  1 289 ? 10.557  -67.394 52.349   1.00 53.61  ? 289 ALA D CA  1 
ATOM   14518 C C   . ALA D  1 289 ? 10.730  -65.897 52.113   1.00 51.10  ? 289 ALA D C   1 
ATOM   14519 O O   . ALA D  1 289 ? 11.551  -65.246 52.760   1.00 54.28  ? 289 ALA D O   1 
ATOM   14520 C CB  . ALA D  1 289 ? 10.883  -67.782 53.789   1.00 53.79  ? 289 ALA D CB  1 
ATOM   14521 N N   . SER D  1 290 ? 9.936   -65.347 51.196   1.00 41.93  ? 290 SER D N   1 
ATOM   14522 C CA  . SER D  1 290 ? 9.933   -63.907 50.994   1.00 37.72  ? 290 SER D CA  1 
ATOM   14523 C C   . SER D  1 290 ? 8.726   -63.304 51.685   1.00 33.22  ? 290 SER D C   1 
ATOM   14524 O O   . SER D  1 290 ? 7.591   -63.711 51.391   1.00 35.26  ? 290 SER D O   1 
ATOM   14525 C CB  . SER D  1 290 ? 9.915   -63.559 49.512   1.00 33.74  ? 290 SER D CB  1 
ATOM   14526 O OG  . SER D  1 290 ? 9.624   -62.180 49.341   1.00 34.59  ? 290 SER D OG  1 
ATOM   14527 N N   . PRO D  1 291 ? 8.910   -62.333 52.582   1.00 35.78  ? 291 PRO D N   1 
ATOM   14528 C CA  . PRO D  1 291 ? 7.768   -61.694 53.247   1.00 32.84  ? 291 PRO D CA  1 
ATOM   14529 C C   . PRO D  1 291 ? 7.028   -60.691 52.377   1.00 27.71  ? 291 PRO D C   1 
ATOM   14530 O O   . PRO D  1 291 ? 6.108   -60.037 52.873   1.00 25.12  ? 291 PRO D O   1 
ATOM   14531 C CB  . PRO D  1 291 ? 8.431   -60.981 54.430   1.00 30.24  ? 291 PRO D CB  1 
ATOM   14532 C CG  . PRO D  1 291 ? 9.782   -60.575 53.858   1.00 32.72  ? 291 PRO D CG  1 
ATOM   14533 C CD  . PRO D  1 291 ? 10.190  -61.697 52.943   1.00 34.63  ? 291 PRO D CD  1 
ATOM   14534 N N   . TYR D  1 292 ? 7.392   -60.534 51.109   1.00 31.37  ? 292 TYR D N   1 
ATOM   14535 C CA  . TYR D  1 292 ? 6.846   -59.457 50.294   1.00 26.92  ? 292 TYR D CA  1 
ATOM   14536 C C   . TYR D  1 292 ? 5.653   -59.898 49.470   1.00 24.85  ? 292 TYR D C   1 
ATOM   14537 O O   . TYR D  1 292 ? 5.176   -59.139 48.619   1.00 26.10  ? 292 TYR D O   1 
ATOM   14538 C CB  . TYR D  1 292 ? 7.945   -58.882 49.399   1.00 27.84  ? 292 TYR D CB  1 
ATOM   14539 C CG  . TYR D  1 292 ? 9.148   -58.410 50.195   1.00 27.83  ? 292 TYR D CG  1 
ATOM   14540 C CD1 . TYR D  1 292 ? 8.985   -57.696 51.378   1.00 32.09  ? 292 TYR D CD1 1 
ATOM   14541 C CD2 . TYR D  1 292 ? 10.440  -58.677 49.764   1.00 29.31  ? 292 TYR D CD2 1 
ATOM   14542 C CE1 . TYR D  1 292 ? 10.073  -57.268 52.103   1.00 30.46  ? 292 TYR D CE1 1 
ATOM   14543 C CE2 . TYR D  1 292 ? 11.533  -58.248 50.480   1.00 31.54  ? 292 TYR D CE2 1 
ATOM   14544 C CZ  . TYR D  1 292 ? 11.342  -57.545 51.647   1.00 34.42  ? 292 TYR D CZ  1 
ATOM   14545 O OH  . TYR D  1 292 ? 12.436  -57.128 52.360   1.00 43.32  ? 292 TYR D OH  1 
ATOM   14546 N N   . LEU D  1 293 ? 5.174   -61.112 49.692   1.00 28.33  ? 293 LEU D N   1 
ATOM   14547 C CA  . LEU D  1 293 ? 4.096   -61.709 48.924   1.00 23.48  ? 293 LEU D CA  1 
ATOM   14548 C C   . LEU D  1 293 ? 2.846   -61.699 49.781   1.00 22.56  ? 293 LEU D C   1 
ATOM   14549 O O   . LEU D  1 293 ? 2.933   -61.702 51.011   1.00 24.28  ? 293 LEU D O   1 
ATOM   14550 C CB  . LEU D  1 293 ? 4.426   -63.155 48.529   1.00 29.12  ? 293 LEU D CB  1 
ATOM   14551 C CG  . LEU D  1 293 ? 5.346   -63.439 47.343   1.00 37.24  ? 293 LEU D CG  1 
ATOM   14552 C CD1 . LEU D  1 293 ? 6.645   -62.651 47.425   1.00 41.54  ? 293 LEU D CD1 1 
ATOM   14553 C CD2 . LEU D  1 293 ? 5.626   -64.920 47.257   1.00 38.27  ? 293 LEU D CD2 1 
ATOM   14554 N N   . ARG D  1 294 ? 1.687   -61.683 49.126   1.00 25.68  ? 294 ARG D N   1 
ATOM   14555 C CA  . ARG D  1 294 ? 0.429   -62.013 49.779   1.00 23.86  ? 294 ARG D CA  1 
ATOM   14556 C C   . ARG D  1 294 ? 0.284   -63.525 49.737   1.00 24.51  ? 294 ARG D C   1 
ATOM   14557 O O   . ARG D  1 294 ? 0.251   -64.114 48.649   1.00 25.04  ? 294 ARG D O   1 
ATOM   14558 C CB  . ARG D  1 294 ? -0.766  -61.349 49.092   1.00 20.71  ? 294 ARG D CB  1 
ATOM   14559 C CG  . ARG D  1 294 ? -2.113  -61.685 49.805   1.00 24.95  ? 294 ARG D CG  1 
ATOM   14560 C CD  . ARG D  1 294 ? -3.233  -60.747 49.358   1.00 22.92  ? 294 ARG D CD  1 
ATOM   14561 N NE  . ARG D  1 294 ? -3.515  -60.920 47.932   1.00 25.21  ? 294 ARG D NE  1 
ATOM   14562 C CZ  . ARG D  1 294 ? -3.561  -59.937 47.045   1.00 25.26  ? 294 ARG D CZ  1 
ATOM   14563 N NH1 . ARG D  1 294 ? -3.367  -58.682 47.422   1.00 31.77  ? 294 ARG D NH1 1 
ATOM   14564 N NH2 . ARG D  1 294 ? -3.814  -60.204 45.774   1.00 32.55  ? 294 ARG D NH2 1 
ATOM   14565 N N   . TYR D  1 295 ? 0.222   -64.153 50.906   1.00 20.24  ? 295 TYR D N   1 
ATOM   14566 C CA  . TYR D  1 295 ? 0.109   -65.605 50.990   1.00 25.46  ? 295 TYR D CA  1 
ATOM   14567 C C   . TYR D  1 295 ? -1.344  -65.996 51.199   1.00 24.89  ? 295 TYR D C   1 
ATOM   14568 O O   . TYR D  1 295 ? -2.118  -65.260 51.816   1.00 26.78  ? 295 TYR D O   1 
ATOM   14569 C CB  . TYR D  1 295 ? 0.972   -66.183 52.127   1.00 25.38  ? 295 TYR D CB  1 
ATOM   14570 C CG  . TYR D  1 295 ? 2.460   -66.162 51.813   1.00 23.39  ? 295 TYR D CG  1 
ATOM   14571 C CD1 . TYR D  1 295 ? 3.214   -65.021 52.038   1.00 22.41  ? 295 TYR D CD1 1 
ATOM   14572 C CD2 . TYR D  1 295 ? 3.102   -67.280 51.278   1.00 26.43  ? 295 TYR D CD2 1 
ATOM   14573 C CE1 . TYR D  1 295 ? 4.584   -64.973 51.731   1.00 20.67  ? 295 TYR D CE1 1 
ATOM   14574 C CE2 . TYR D  1 295 ? 4.475   -67.248 50.975   1.00 24.79  ? 295 TYR D CE2 1 
ATOM   14575 C CZ  . TYR D  1 295 ? 5.204   -66.080 51.207   1.00 25.31  ? 295 TYR D CZ  1 
ATOM   14576 O OH  . TYR D  1 295 ? 6.558   -66.001 50.924   1.00 32.20  ? 295 TYR D OH  1 
ATOM   14577 N N   . TYR D  1 296 ? -1.714  -67.159 50.662   1.00 24.11  ? 296 TYR D N   1 
ATOM   14578 C CA  . TYR D  1 296 ? -3.047  -67.724 50.846   1.00 27.27  ? 296 TYR D CA  1 
ATOM   14579 C C   . TYR D  1 296 ? -2.879  -69.040 51.587   1.00 30.31  ? 296 TYR D C   1 
ATOM   14580 O O   . TYR D  1 296 ? -2.352  -70.008 51.026   1.00 27.43  ? 296 TYR D O   1 
ATOM   14581 C CB  . TYR D  1 296 ? -3.772  -67.939 49.510   1.00 30.06  ? 296 TYR D CB  1 
ATOM   14582 C CG  . TYR D  1 296 ? -4.101  -66.673 48.748   1.00 38.24  ? 296 TYR D CG  1 
ATOM   14583 C CD1 . TYR D  1 296 ? -4.453  -65.508 49.406   1.00 38.06  ? 296 TYR D CD1 1 
ATOM   14584 C CD2 . TYR D  1 296 ? -4.053  -66.644 47.353   1.00 44.25  ? 296 TYR D CD2 1 
ATOM   14585 C CE1 . TYR D  1 296 ? -4.755  -64.343 48.702   1.00 39.47  ? 296 TYR D CE1 1 
ATOM   14586 C CE2 . TYR D  1 296 ? -4.353  -65.480 46.644   1.00 45.55  ? 296 TYR D CE2 1 
ATOM   14587 C CZ  . TYR D  1 296 ? -4.699  -64.334 47.328   1.00 43.27  ? 296 TYR D CZ  1 
ATOM   14588 O OH  . TYR D  1 296 ? -4.995  -63.175 46.636   1.00 42.17  ? 296 TYR D OH  1 
ATOM   14589 N N   . PHE D  1 297 ? -3.333  -69.087 52.841   1.00 31.67  ? 297 PHE D N   1 
ATOM   14590 C CA  . PHE D  1 297 ? -3.188  -70.302 53.636   1.00 20.38  ? 297 PHE D CA  1 
ATOM   14591 C C   . PHE D  1 297 ? -4.284  -71.264 53.242   1.00 27.58  ? 297 PHE D C   1 
ATOM   14592 O O   . PHE D  1 297 ? -5.464  -71.021 53.530   1.00 25.09  ? 297 PHE D O   1 
ATOM   14593 C CB  . PHE D  1 297 ? -3.242  -70.004 55.130   1.00 19.93  ? 297 PHE D CB  1 
ATOM   14594 C CG  . PHE D  1 297 ? -3.148  -71.230 55.993   1.00 22.55  ? 297 PHE D CG  1 
ATOM   14595 C CD1 . PHE D  1 297 ? -1.912  -71.797 56.283   1.00 27.75  ? 297 PHE D CD1 1 
ATOM   14596 C CD2 . PHE D  1 297 ? -4.296  -71.824 56.522   1.00 21.26  ? 297 PHE D CD2 1 
ATOM   14597 C CE1 . PHE D  1 297 ? -1.822  -72.938 57.112   1.00 20.76  ? 297 PHE D CE1 1 
ATOM   14598 C CE2 . PHE D  1 297 ? -4.213  -72.958 57.335   1.00 25.06  ? 297 PHE D CE2 1 
ATOM   14599 C CZ  . PHE D  1 297 ? -2.975  -73.511 57.631   1.00 22.00  ? 297 PHE D CZ  1 
ATOM   14600 N N   . ARG D  1 298 ? -3.885  -72.354 52.571   1.00 25.61  ? 298 ARG D N   1 
ATOM   14601 C CA  . ARG D  1 298 ? -4.782  -73.407 52.115   1.00 25.05  ? 298 ARG D CA  1 
ATOM   14602 C C   . ARG D  1 298 ? -5.917  -72.852 51.246   1.00 27.40  ? 298 ARG D C   1 
ATOM   14603 O O   . ARG D  1 298 ? -6.996  -73.434 51.174   1.00 28.95  ? 298 ARG D O   1 
ATOM   14604 C CB  . ARG D  1 298 ? -5.313  -74.205 53.307   1.00 24.39  ? 298 ARG D CB  1 
ATOM   14605 C CG  . ARG D  1 298 ? -4.173  -74.874 54.080   1.00 29.56  ? 298 ARG D CG  1 
ATOM   14606 C CD  . ARG D  1 298 ? -4.621  -75.687 55.292   1.00 25.53  ? 298 ARG D CD  1 
ATOM   14607 N NE  . ARG D  1 298 ? -3.467  -76.352 55.899   1.00 27.77  ? 298 ARG D NE  1 
ATOM   14608 C CZ  . ARG D  1 298 ? -3.539  -77.217 56.900   1.00 29.44  ? 298 ARG D CZ  1 
ATOM   14609 N NH1 . ARG D  1 298 ? -4.717  -77.528 57.415   1.00 28.68  ? 298 ARG D NH1 1 
ATOM   14610 N NH2 . ARG D  1 298 ? -2.436  -77.785 57.371   1.00 31.62  ? 298 ARG D NH2 1 
ATOM   14611 N N   . GLU D  1 299 ? -5.672  -71.723 50.572   1.00 24.20  ? 299 GLU D N   1 
ATOM   14612 C CA  . GLU D  1 299 ? -6.682  -71.029 49.766   1.00 26.36  ? 299 GLU D CA  1 
ATOM   14613 C C   . GLU D  1 299 ? -7.925  -70.680 50.595   1.00 31.30  ? 299 GLU D C   1 
ATOM   14614 O O   . GLU D  1 299 ? -9.030  -70.573 50.059   1.00 32.38  ? 299 GLU D O   1 
ATOM   14615 C CB  . GLU D  1 299 ? -7.078  -71.847 48.527   1.00 31.25  ? 299 GLU D CB  1 
ATOM   14616 C CG  . GLU D  1 299 ? -5.911  -72.365 47.687   1.00 46.34  ? 299 GLU D CG  1 
ATOM   14617 C CD  . GLU D  1 299 ? -5.423  -71.384 46.626   1.00 63.88  ? 299 GLU D CD  1 
ATOM   14618 O OE1 . GLU D  1 299 ? -5.333  -70.171 46.906   1.00 71.76  ? 299 GLU D OE1 1 
ATOM   14619 O OE2 . GLU D  1 299 ? -5.137  -71.830 45.496   1.00 71.61  ? 299 GLU D OE2 1 
ATOM   14620 N N   . LEU D  1 300 ? -7.760  -70.492 51.907   1.00 25.98  ? 300 LEU D N   1 
ATOM   14621 C CA  . LEU D  1 300 ? -8.852  -70.110 52.801   1.00 27.73  ? 300 LEU D CA  1 
ATOM   14622 C C   . LEU D  1 300 ? -8.765  -68.670 53.289   1.00 31.46  ? 300 LEU D C   1 
ATOM   14623 O O   . LEU D  1 300 ? -9.771  -67.964 53.315   1.00 30.97  ? 300 LEU D O   1 
ATOM   14624 C CB  . LEU D  1 300 ? -8.881  -71.025 54.027   1.00 26.51  ? 300 LEU D CB  1 
ATOM   14625 C CG  . LEU D  1 300 ? -8.971  -72.525 53.816   1.00 21.84  ? 300 LEU D CG  1 
ATOM   14626 C CD1 . LEU D  1 300 ? -8.959  -73.218 55.161   1.00 21.71  ? 300 LEU D CD1 1 
ATOM   14627 C CD2 . LEU D  1 300 ? -10.234 -72.878 53.040   1.00 29.79  ? 300 LEU D CD2 1 
ATOM   14628 N N   . ILE D  1 301 ? -7.585  -68.218 53.691   1.00 35.01  ? 301 ILE D N   1 
ATOM   14629 C CA  . ILE D  1 301 ? -7.432  -66.928 54.347   1.00 26.54  ? 301 ILE D CA  1 
ATOM   14630 C C   . ILE D  1 301 ? -6.094  -66.362 53.917   1.00 26.40  ? 301 ILE D C   1 
ATOM   14631 O O   . ILE D  1 301 ? -5.133  -67.104 53.693   1.00 31.23  ? 301 ILE D O   1 
ATOM   14632 C CB  . ILE D  1 301 ? -7.532  -67.087 55.881   1.00 23.42  ? 301 ILE D CB  1 
ATOM   14633 C CG1 . ILE D  1 301 ? -7.248  -65.783 56.625   1.00 21.98  ? 301 ILE D CG1 1 
ATOM   14634 C CG2 . ILE D  1 301 ? -6.548  -68.141 56.346   1.00 21.75  ? 301 ILE D CG2 1 
ATOM   14635 C CD1 . ILE D  1 301 ? -7.505  -65.905 58.173   1.00 21.00  ? 301 ILE D CD1 1 
ATOM   14636 N N   . SER D  1 302 ? -6.046  -65.041 53.777   1.00 25.99  ? 302 SER D N   1 
ATOM   14637 C CA  . SER D  1 302 ? -4.833  -64.350 53.366   1.00 27.34  ? 302 SER D CA  1 
ATOM   14638 C C   . SER D  1 302 ? -3.925  -64.103 54.557   1.00 26.87  ? 302 SER D C   1 
ATOM   14639 O O   . SER D  1 302 ? -4.389  -63.840 55.674   1.00 24.12  ? 302 SER D O   1 
ATOM   14640 C CB  . SER D  1 302 ? -5.175  -63.025 52.689   1.00 24.16  ? 302 SER D CB  1 
ATOM   14641 O OG  . SER D  1 302 ? -5.927  -63.263 51.522   1.00 27.24  ? 302 SER D OG  1 
ATOM   14642 N N   . VAL D  1 303 ? -2.619  -64.205 54.310   1.00 26.14  ? 303 VAL D N   1 
ATOM   14643 C CA  . VAL D  1 303 ? -1.611  -64.096 55.358   1.00 24.68  ? 303 VAL D CA  1 
ATOM   14644 C C   . VAL D  1 303 ? -0.469  -63.245 54.818   1.00 24.11  ? 303 VAL D C   1 
ATOM   14645 O O   . VAL D  1 303 ? 0.144   -63.582 53.796   1.00 24.62  ? 303 VAL D O   1 
ATOM   14646 C CB  . VAL D  1 303 ? -1.082  -65.469 55.829   1.00 29.62  ? 303 VAL D CB  1 
ATOM   14647 C CG1 . VAL D  1 303 ? -0.035  -65.281 56.924   1.00 26.07  ? 303 VAL D CG1 1 
ATOM   14648 C CG2 . VAL D  1 303 ? -2.218  -66.366 56.365   1.00 25.18  ? 303 VAL D CG2 1 
ATOM   14649 N N   . PHE D  1 304 ? -0.212  -62.128 55.476   1.00 23.07  ? 304 PHE D N   1 
ATOM   14650 C CA  . PHE D  1 304 ? 0.983   -61.349 55.242   1.00 18.98  ? 304 PHE D CA  1 
ATOM   14651 C C   . PHE D  1 304 ? 1.979   -61.595 56.365   1.00 25.68  ? 304 PHE D C   1 
ATOM   14652 O O   . PHE D  1 304 ? 1.598   -61.790 57.522   1.00 29.12  ? 304 PHE D O   1 
ATOM   14653 C CB  . PHE D  1 304 ? 0.633   -59.867 55.150   1.00 18.54  ? 304 PHE D CB  1 
ATOM   14654 C CG  . PHE D  1 304 ? 0.067   -59.489 53.839   1.00 19.23  ? 304 PHE D CG  1 
ATOM   14655 C CD1 . PHE D  1 304 ? 0.901   -59.333 52.745   1.00 21.68  ? 304 PHE D CD1 1 
ATOM   14656 C CD2 . PHE D  1 304 ? -1.291  -59.289 53.688   1.00 20.92  ? 304 PHE D CD2 1 
ATOM   14657 C CE1 . PHE D  1 304 ? 0.396   -58.980 51.522   1.00 25.05  ? 304 PHE D CE1 1 
ATOM   14658 C CE2 . PHE D  1 304 ? -1.811  -58.923 52.452   1.00 24.64  ? 304 PHE D CE2 1 
ATOM   14659 C CZ  . PHE D  1 304 ? -0.966  -58.775 51.373   1.00 25.89  ? 304 PHE D CZ  1 
ATOM   14660 N N   . PHE D  1 305 ? 3.255   -61.616 56.024   1.00 27.45  ? 305 PHE D N   1 
ATOM   14661 C CA  . PHE D  1 305 ? 4.302   -61.811 57.016   1.00 24.52  ? 305 PHE D CA  1 
ATOM   14662 C C   . PHE D  1 305 ? 5.038   -60.495 57.165   1.00 26.36  ? 305 PHE D C   1 
ATOM   14663 O O   . PHE D  1 305 ? 5.542   -59.960 56.175   1.00 27.10  ? 305 PHE D O   1 
ATOM   14664 C CB  . PHE D  1 305 ? 5.255   -62.931 56.604   1.00 19.82  ? 305 PHE D CB  1 
ATOM   14665 C CG  . PHE D  1 305 ? 4.611   -64.277 56.572   1.00 23.56  ? 305 PHE D CG  1 
ATOM   14666 C CD1 . PHE D  1 305 ? 4.533   -65.051 57.736   1.00 25.90  ? 305 PHE D CD1 1 
ATOM   14667 C CD2 . PHE D  1 305 ? 4.041   -64.763 55.404   1.00 23.03  ? 305 PHE D CD2 1 
ATOM   14668 C CE1 . PHE D  1 305 ? 3.924   -66.305 57.715   1.00 27.41  ? 305 PHE D CE1 1 
ATOM   14669 C CE2 . PHE D  1 305 ? 3.432   -66.019 55.378   1.00 26.22  ? 305 PHE D CE2 1 
ATOM   14670 C CZ  . PHE D  1 305 ? 3.358   -66.779 56.527   1.00 30.31  ? 305 PHE D CZ  1 
ATOM   14671 N N   . ARG D  1 306 ? 5.080   -59.967 58.387   1.00 23.33  ? 306 ARG D N   1 
ATOM   14672 C CA  . ARG D  1 306 ? 5.698   -58.665 58.591   1.00 23.80  ? 306 ARG D CA  1 
ATOM   14673 C C   . ARG D  1 306 ? 7.182   -58.726 58.265   1.00 22.94  ? 306 ARG D C   1 
ATOM   14674 O O   . ARG D  1 306 ? 7.830   -59.772 58.370   1.00 32.68  ? 306 ARG D O   1 
ATOM   14675 C CB  . ARG D  1 306 ? 5.494   -58.174 60.030   1.00 25.98  ? 306 ARG D CB  1 
ATOM   14676 C CG  . ARG D  1 306 ? 6.417   -58.789 61.048   1.00 27.04  ? 306 ARG D CG  1 
ATOM   14677 C CD  . ARG D  1 306 ? 6.297   -58.109 62.410   1.00 28.01  ? 306 ARG D CD  1 
ATOM   14678 N NE  . ARG D  1 306 ? 7.227   -58.741 63.336   1.00 25.14  ? 306 ARG D NE  1 
ATOM   14679 C CZ  . ARG D  1 306 ? 7.801   -58.148 64.373   1.00 24.43  ? 306 ARG D CZ  1 
ATOM   14680 N NH1 . ARG D  1 306 ? 7.554   -56.876 64.658   1.00 28.30  ? 306 ARG D NH1 1 
ATOM   14681 N NH2 . ARG D  1 306 ? 8.634   -58.839 65.127   1.00 30.38  ? 306 ARG D NH2 1 
ATOM   14682 N N   . ASP D  1 307 ? 7.706   -57.594 57.832   1.00 22.24  ? 307 ASP D N   1 
ATOM   14683 C CA  . ASP D  1 307 ? 9.141   -57.404 57.678   1.00 25.74  ? 307 ASP D CA  1 
ATOM   14684 C C   . ASP D  1 307 ? 9.716   -57.154 59.068   1.00 27.24  ? 307 ASP D C   1 
ATOM   14685 O O   . ASP D  1 307 ? 9.611   -56.048 59.606   1.00 23.84  ? 307 ASP D O   1 
ATOM   14686 C CB  . ASP D  1 307 ? 9.424   -56.247 56.739   1.00 25.99  ? 307 ASP D CB  1 
ATOM   14687 C CG  . ASP D  1 307 ? 10.894  -56.083 56.453   1.00 34.81  ? 307 ASP D CG  1 
ATOM   14688 O OD1 . ASP D  1 307 ? 11.702  -56.073 57.416   1.00 35.75  ? 307 ASP D OD1 1 
ATOM   14689 O OD2 . ASP D  1 307 ? 11.239  -55.960 55.259   1.00 28.96  ? 307 ASP D OD2 1 
ATOM   14690 N N   . LYS D  1 308 ? 10.334  -58.191 59.638   1.00 27.82  ? 308 LYS D N   1 
ATOM   14691 C CA  . LYS D  1 308 ? 10.814  -58.129 61.015   1.00 24.83  ? 308 LYS D CA  1 
ATOM   14692 C C   . LYS D  1 308 ? 11.828  -57.013 61.190   1.00 22.98  ? 308 LYS D C   1 
ATOM   14693 O O   . LYS D  1 308 ? 11.734  -56.217 62.134   1.00 22.14  ? 308 LYS D O   1 
ATOM   14694 C CB  . LYS D  1 308 ? 11.424  -59.480 61.416   1.00 20.81  ? 308 LYS D CB  1 
ATOM   14695 C CG  . LYS D  1 308 ? 11.840  -59.594 62.912   1.00 24.74  ? 308 LYS D CG  1 
ATOM   14696 C CD  . LYS D  1 308 ? 12.771  -60.791 63.120   1.00 31.07  ? 308 LYS D CD  1 
ATOM   14697 C CE  . LYS D  1 308 ? 13.084  -61.054 64.600   1.00 35.13  ? 308 LYS D CE  1 
ATOM   14698 N NZ  . LYS D  1 308 ? 12.872  -59.829 65.413   1.00 32.16  ? 308 LYS D NZ  1 
ATOM   14699 N N   . THR D  1 309 ? 12.825  -56.963 60.297   1.00 23.93  ? 309 THR D N   1 
ATOM   14700 C CA  . THR D  1 309 ? 13.888  -55.964 60.370   1.00 25.88  ? 309 THR D CA  1 
ATOM   14701 C C   . THR D  1 309 ? 13.334  -54.546 60.447   1.00 26.47  ? 309 THR D C   1 
ATOM   14702 O O   . THR D  1 309 ? 13.757  -53.754 61.295   1.00 26.28  ? 309 THR D O   1 
ATOM   14703 C CB  . THR D  1 309 ? 14.805  -56.104 59.151   1.00 34.69  ? 309 THR D CB  1 
ATOM   14704 O OG1 . THR D  1 309 ? 15.468  -57.371 59.198   1.00 38.14  ? 309 THR D OG1 1 
ATOM   14705 C CG2 . THR D  1 309 ? 15.841  -54.988 59.104   1.00 38.27  ? 309 THR D CG2 1 
ATOM   14706 N N   . LEU D  1 310 ? 12.413  -54.192 59.537   1.00 22.62  ? 310 LEU D N   1 
ATOM   14707 C CA  . LEU D  1 310 ? 11.902  -52.824 59.501   1.00 22.95  ? 310 LEU D CA  1 
ATOM   14708 C C   . LEU D  1 310 ? 11.098  -52.504 60.755   1.00 23.55  ? 310 LEU D C   1 
ATOM   14709 O O   . LEU D  1 310 ? 11.224  -51.414 61.329   1.00 23.26  ? 310 LEU D O   1 
ATOM   14710 C CB  . LEU D  1 310 ? 11.040  -52.614 58.251   1.00 21.53  ? 310 LEU D CB  1 
ATOM   14711 C CG  . LEU D  1 310 ? 11.786  -52.512 56.913   1.00 29.77  ? 310 LEU D CG  1 
ATOM   14712 C CD1 . LEU D  1 310 ? 10.795  -52.344 55.775   1.00 32.64  ? 310 LEU D CD1 1 
ATOM   14713 C CD2 . LEU D  1 310 ? 12.803  -51.374 56.913   1.00 25.65  ? 310 LEU D CD2 1 
ATOM   14714 N N   . SER D  1 311 ? 10.238  -53.432 61.163   1.00 20.16  ? 311 SER D N   1 
ATOM   14715 C CA  . SER D  1 311 ? 9.469   -53.260 62.389   1.00 20.01  ? 311 SER D CA  1 
ATOM   14716 C C   . SER D  1 311 ? 10.386  -53.091 63.598   1.00 20.53  ? 311 SER D C   1 
ATOM   14717 O O   . SER D  1 311 ? 10.126  -52.250 64.463   1.00 22.49  ? 311 SER D O   1 
ATOM   14718 C CB  . SER D  1 311 ? 8.552   -54.470 62.584   1.00 25.61  ? 311 SER D CB  1 
ATOM   14719 O OG  . SER D  1 311 ? 7.729   -54.696 61.451   1.00 26.73  ? 311 SER D OG  1 
ATOM   14720 N N   . ASP D  1 312 ? 11.458  -53.890 63.679   1.00 28.19  ? 312 ASP D N   1 
ATOM   14721 C CA  . ASP D  1 312 ? 12.348  -53.821 64.839   1.00 27.90  ? 312 ASP D CA  1 
ATOM   14722 C C   . ASP D  1 312 ? 13.170  -52.540 64.835   1.00 28.70  ? 312 ASP D C   1 
ATOM   14723 O O   . ASP D  1 312 ? 13.610  -52.083 65.901   1.00 32.63  ? 312 ASP D O   1 
ATOM   14724 C CB  . ASP D  1 312 ? 13.295  -55.023 64.891   1.00 22.00  ? 312 ASP D CB  1 
ATOM   14725 C CG  . ASP D  1 312 ? 12.598  -56.326 65.314   1.00 27.76  ? 312 ASP D CG  1 
ATOM   14726 O OD1 . ASP D  1 312 ? 11.446  -56.315 65.792   1.00 29.09  ? 312 ASP D OD1 1 
ATOM   14727 O OD2 . ASP D  1 312 ? 13.230  -57.378 65.168   1.00 26.74  ? 312 ASP D OD2 1 
ATOM   14728 N N   . LEU D  1 313 ? 13.417  -51.963 63.656   1.00 25.47  ? 313 LEU D N   1 
ATOM   14729 C CA  . LEU D  1 313 ? 14.131  -50.693 63.591   1.00 27.00  ? 313 LEU D CA  1 
ATOM   14730 C C   . LEU D  1 313 ? 13.392  -49.616 64.363   1.00 27.98  ? 313 LEU D C   1 
ATOM   14731 O O   . LEU D  1 313 ? 13.983  -48.874 65.155   1.00 30.48  ? 313 LEU D O   1 
ATOM   14732 C CB  . LEU D  1 313 ? 14.298  -50.255 62.142   1.00 26.63  ? 313 LEU D CB  1 
ATOM   14733 C CG  . LEU D  1 313 ? 15.512  -50.811 61.428   1.00 25.35  ? 313 LEU D CG  1 
ATOM   14734 C CD1 . LEU D  1 313 ? 15.386  -50.487 59.940   1.00 25.59  ? 313 LEU D CD1 1 
ATOM   14735 C CD2 . LEU D  1 313 ? 16.800  -50.263 61.997   1.00 23.80  ? 313 LEU D CD2 1 
ATOM   14736 N N   . ILE D  1 314 ? 12.092  -49.503 64.119   1.00 24.80  ? 314 ILE D N   1 
ATOM   14737 C CA  . ILE D  1 314 ? 11.296  -48.511 64.823   1.00 26.15  ? 314 ILE D CA  1 
ATOM   14738 C C   . ILE D  1 314 ? 11.187  -48.878 66.297   1.00 29.79  ? 314 ILE D C   1 
ATOM   14739 O O   . ILE D  1 314 ? 11.387  -48.034 67.176   1.00 29.02  ? 314 ILE D O   1 
ATOM   14740 C CB  . ILE D  1 314 ? 9.918   -48.393 64.151   1.00 22.94  ? 314 ILE D CB  1 
ATOM   14741 C CG1 . ILE D  1 314 ? 10.095  -47.917 62.700   1.00 21.11  ? 314 ILE D CG1 1 
ATOM   14742 C CG2 . ILE D  1 314 ? 8.974   -47.493 64.952   1.00 24.77  ? 314 ILE D CG2 1 
ATOM   14743 C CD1 . ILE D  1 314 ? 8.782   -47.839 61.965   1.00 23.13  ? 314 ILE D CD1 1 
ATOM   14744 N N   . GLY D  1 315 ? 10.922  -50.154 66.589   1.00 26.90  ? 315 GLY D N   1 
ATOM   14745 C CA  . GLY D  1 315 ? 10.678  -50.546 67.969   1.00 31.35  ? 315 GLY D CA  1 
ATOM   14746 C C   . GLY D  1 315 ? 11.907  -50.619 68.852   1.00 28.78  ? 315 GLY D C   1 
ATOM   14747 O O   . GLY D  1 315 ? 11.801  -50.437 70.076   1.00 30.13  ? 315 GLY D O   1 
ATOM   14748 N N   . PHE D  1 316 ? 13.081  -50.882 68.271   1.00 25.99  ? 316 PHE D N   1 
ATOM   14749 C CA  . PHE D  1 316 ? 14.274  -51.170 69.063   1.00 27.71  ? 316 PHE D CA  1 
ATOM   14750 C C   . PHE D  1 316 ? 15.449  -50.251 68.807   1.00 29.92  ? 316 PHE D C   1 
ATOM   14751 O O   . PHE D  1 316 ? 16.260  -50.035 69.726   1.00 28.43  ? 316 PHE D O   1 
ATOM   14752 C CB  . PHE D  1 316 ? 14.777  -52.602 68.812   1.00 34.98  ? 316 PHE D CB  1 
ATOM   14753 C CG  . PHE D  1 316 ? 13.810  -53.668 69.198   1.00 44.28  ? 316 PHE D CG  1 
ATOM   14754 C CD1 . PHE D  1 316 ? 12.892  -53.461 70.213   1.00 49.19  ? 316 PHE D CD1 1 
ATOM   14755 C CD2 . PHE D  1 316 ? 13.825  -54.892 68.552   1.00 47.53  ? 316 PHE D CD2 1 
ATOM   14756 C CE1 . PHE D  1 316 ? 12.004  -54.452 70.574   1.00 50.61  ? 316 PHE D CE1 1 
ATOM   14757 C CE2 . PHE D  1 316 ? 12.934  -55.891 68.909   1.00 49.65  ? 316 PHE D CE2 1 
ATOM   14758 C CZ  . PHE D  1 316 ? 12.025  -55.669 69.918   1.00 49.98  ? 316 PHE D CZ  1 
ATOM   14759 N N   . SER D  1 317 ? 15.613  -49.741 67.591   1.00 24.37  ? 317 SER D N   1 
ATOM   14760 C CA  . SER D  1 317 ? 16.854  -49.050 67.260   1.00 31.09  ? 317 SER D CA  1 
ATOM   14761 C C   . SER D  1 317 ? 16.717  -47.534 67.202   1.00 32.60  ? 317 SER D C   1 
ATOM   14762 O O   . SER D  1 317 ? 17.463  -46.823 67.887   1.00 32.11  ? 317 SER D O   1 
ATOM   14763 C CB  . SER D  1 317 ? 17.405  -49.590 65.932   1.00 32.07  ? 317 SER D CB  1 
ATOM   14764 O OG  . SER D  1 317 ? 18.805  -49.380 65.867   1.00 37.17  ? 317 SER D OG  1 
ATOM   14765 N N   . TYR D  1 318 ? 15.752  -47.022 66.431   1.00 29.83  ? 318 TYR D N   1 
ATOM   14766 C CA  . TYR D  1 318 ? 15.720  -45.614 66.037   1.00 24.68  ? 318 TYR D CA  1 
ATOM   14767 C C   . TYR D  1 318 ? 15.605  -44.635 67.197   1.00 30.60  ? 318 TYR D C   1 
ATOM   14768 O O   . TYR D  1 318 ? 15.970  -43.466 67.028   1.00 25.70  ? 318 TYR D O   1 
ATOM   14769 C CB  . TYR D  1 318 ? 14.553  -45.378 65.088   1.00 31.05  ? 318 TYR D CB  1 
ATOM   14770 C CG  . TYR D  1 318 ? 14.837  -45.842 63.694   1.00 23.64  ? 318 TYR D CG  1 
ATOM   14771 C CD1 . TYR D  1 318 ? 16.150  -46.034 63.252   1.00 29.33  ? 318 TYR D CD1 1 
ATOM   14772 C CD2 . TYR D  1 318 ? 13.800  -46.093 62.806   1.00 23.47  ? 318 TYR D CD2 1 
ATOM   14773 C CE1 . TYR D  1 318 ? 16.411  -46.452 61.952   1.00 30.55  ? 318 TYR D CE1 1 
ATOM   14774 C CE2 . TYR D  1 318 ? 14.058  -46.507 61.516   1.00 25.06  ? 318 TYR D CE2 1 
ATOM   14775 C CZ  . TYR D  1 318 ? 15.357  -46.683 61.090   1.00 29.11  ? 318 TYR D CZ  1 
ATOM   14776 O OH  . TYR D  1 318 ? 15.586  -47.109 59.791   1.00 33.19  ? 318 TYR D OH  1 
ATOM   14777 N N   . HIS D  1 319 ? 15.107  -45.071 68.362   1.00 30.80  ? 319 HIS D N   1 
ATOM   14778 C CA  . HIS D  1 319 ? 14.947  -44.160 69.495   1.00 35.16  ? 319 HIS D CA  1 
ATOM   14779 C C   . HIS D  1 319 ? 16.231  -43.420 69.838   1.00 36.99  ? 319 HIS D C   1 
ATOM   14780 O O   . HIS D  1 319 ? 16.171  -42.312 70.379   1.00 47.79  ? 319 HIS D O   1 
ATOM   14781 C CB  . HIS D  1 319 ? 14.443  -44.919 70.732   1.00 32.07  ? 319 HIS D CB  1 
ATOM   14782 C CG  . HIS D  1 319 ? 15.468  -45.818 71.353   1.00 37.15  ? 319 HIS D CG  1 
ATOM   14783 N ND1 . HIS D  1 319 ? 16.348  -45.390 72.326   1.00 37.98  ? 319 HIS D ND1 1 
ATOM   14784 C CD2 . HIS D  1 319 ? 15.747  -47.128 71.145   1.00 37.70  ? 319 HIS D CD2 1 
ATOM   14785 C CE1 . HIS D  1 319 ? 17.130  -46.393 72.683   1.00 37.32  ? 319 HIS D CE1 1 
ATOM   14786 N NE2 . HIS D  1 319 ? 16.783  -47.461 71.985   1.00 39.51  ? 319 HIS D NE2 1 
ATOM   14787 N N   . ALA D  1 320 ? 17.388  -43.996 69.525   1.00 36.28  ? 320 ALA D N   1 
ATOM   14788 C CA  . ALA D  1 320 ? 18.676  -43.382 69.803   1.00 36.55  ? 320 ALA D CA  1 
ATOM   14789 C C   . ALA D  1 320 ? 19.265  -42.671 68.592   1.00 39.45  ? 320 ALA D C   1 
ATOM   14790 O O   . ALA D  1 320 ? 20.416  -42.223 68.650   1.00 43.55  ? 320 ALA D O   1 
ATOM   14791 C CB  . ALA D  1 320 ? 19.660  -44.437 70.316   1.00 40.94  ? 320 ALA D CB  1 
ATOM   14792 N N   . TRP D  1 321 ? 18.512  -42.563 67.501   1.00 37.59  ? 321 TRP D N   1 
ATOM   14793 C CA  . TRP D  1 321 ? 18.986  -41.916 66.285   1.00 39.60  ? 321 TRP D CA  1 
ATOM   14794 C C   . TRP D  1 321 ? 18.396  -40.519 66.169   1.00 38.07  ? 321 TRP D C   1 
ATOM   14795 O O   . TRP D  1 321 ? 17.243  -40.291 66.539   1.00 41.29  ? 321 TRP D O   1 
ATOM   14796 C CB  . TRP D  1 321 ? 18.588  -42.697 65.037   1.00 38.71  ? 321 TRP D CB  1 
ATOM   14797 C CG  . TRP D  1 321 ? 19.138  -44.075 64.888   1.00 41.85  ? 321 TRP D CG  1 
ATOM   14798 C CD1 . TRP D  1 321 ? 19.276  -45.032 65.859   1.00 40.98  ? 321 TRP D CD1 1 
ATOM   14799 C CD2 . TRP D  1 321 ? 19.591  -44.669 63.668   1.00 40.17  ? 321 TRP D CD2 1 
ATOM   14800 N NE1 . TRP D  1 321 ? 19.798  -46.183 65.312   1.00 43.40  ? 321 TRP D NE1 1 
ATOM   14801 C CE2 . TRP D  1 321 ? 20.003  -45.984 63.970   1.00 42.50  ? 321 TRP D CE2 1 
ATOM   14802 C CE3 . TRP D  1 321 ? 19.692  -44.212 62.348   1.00 41.84  ? 321 TRP D CE3 1 
ATOM   14803 C CZ2 . TRP D  1 321 ? 20.509  -46.845 63.001   1.00 45.56  ? 321 TRP D CZ2 1 
ATOM   14804 C CZ3 . TRP D  1 321 ? 20.196  -45.067 61.387   1.00 43.07  ? 321 TRP D CZ3 1 
ATOM   14805 C CH2 . TRP D  1 321 ? 20.599  -46.371 61.718   1.00 45.43  ? 321 TRP D CH2 1 
ATOM   14806 N N   . ASN D  1 322 ? 19.190  -39.596 65.635   1.00 38.28  ? 322 ASN D N   1 
ATOM   14807 C CA  . ASN D  1 322 ? 18.645  -38.353 65.106   1.00 38.49  ? 322 ASN D CA  1 
ATOM   14808 C C   . ASN D  1 322 ? 17.515  -38.670 64.138   1.00 36.75  ? 322 ASN D C   1 
ATOM   14809 O O   . ASN D  1 322 ? 17.632  -39.577 63.310   1.00 43.21  ? 322 ASN D O   1 
ATOM   14810 C CB  . ASN D  1 322 ? 19.746  -37.559 64.394   1.00 45.99  ? 322 ASN D CB  1 
ATOM   14811 C CG  . ASN D  1 322 ? 19.235  -36.275 63.763   1.00 49.21  ? 322 ASN D CG  1 
ATOM   14812 O OD1 . ASN D  1 322 ? 18.808  -36.261 62.605   1.00 50.56  ? 322 ASN D OD1 1 
ATOM   14813 N ND2 . ASN D  1 322 ? 19.275  -35.185 64.525   1.00 48.84  ? 322 ASN D ND2 1 
ATOM   14814 N N   . ALA D  1 323 ? 16.406  -37.931 64.257   1.00 33.22  ? 323 ALA D N   1 
ATOM   14815 C CA  . ALA D  1 323 ? 15.203  -38.274 63.500   1.00 32.43  ? 323 ALA D CA  1 
ATOM   14816 C C   . ALA D  1 323 ? 15.471  -38.301 61.998   1.00 34.92  ? 323 ALA D C   1 
ATOM   14817 O O   . ALA D  1 323 ? 15.024  -39.219 61.298   1.00 33.69  ? 323 ALA D O   1 
ATOM   14818 C CB  . ALA D  1 323 ? 14.071  -37.296 63.819   1.00 31.21  ? 323 ALA D CB  1 
ATOM   14819 N N   . GLU D  1 324 ? 16.202  -37.310 61.486   1.00 35.07  ? 324 GLU D N   1 
ATOM   14820 C CA  . GLU D  1 324 ? 16.418  -37.231 60.046   1.00 42.30  ? 324 GLU D CA  1 
ATOM   14821 C C   . GLU D  1 324 ? 17.240  -38.411 59.553   1.00 38.09  ? 324 GLU D C   1 
ATOM   14822 O O   . GLU D  1 324 ? 16.928  -38.994 58.508   1.00 35.03  ? 324 GLU D O   1 
ATOM   14823 C CB  . GLU D  1 324 ? 17.089  -35.905 59.686   1.00 51.01  ? 324 GLU D CB  1 
ATOM   14824 C CG  . GLU D  1 324 ? 16.250  -34.697 60.072   1.00 61.84  ? 324 GLU D CG  1 
ATOM   14825 C CD  . GLU D  1 324 ? 16.832  -33.384 59.587   1.00 71.62  ? 324 GLU D CD  1 
ATOM   14826 O OE1 . GLU D  1 324 ? 17.513  -32.708 60.389   1.00 76.09  ? 324 GLU D OE1 1 
ATOM   14827 O OE2 . GLU D  1 324 ? 16.602  -33.028 58.409   1.00 73.93  ? 324 GLU D OE2 1 
ATOM   14828 N N   . ASP D  1 325 ? 18.277  -38.788 60.308   1.00 36.06  ? 325 ASP D N   1 
ATOM   14829 C CA  . ASP D  1 325 ? 19.106  -39.932 59.943   1.00 39.74  ? 325 ASP D CA  1 
ATOM   14830 C C   . ASP D  1 325 ? 18.301  -41.228 59.931   1.00 39.53  ? 325 ASP D C   1 
ATOM   14831 O O   . ASP D  1 325 ? 18.487  -42.074 59.048   1.00 39.99  ? 325 ASP D O   1 
ATOM   14832 C CB  . ASP D  1 325 ? 20.286  -40.054 60.913   1.00 47.45  ? 325 ASP D CB  1 
ATOM   14833 C CG  . ASP D  1 325 ? 21.168  -38.815 60.933   1.00 55.20  ? 325 ASP D CG  1 
ATOM   14834 O OD1 . ASP D  1 325 ? 21.154  -38.055 59.946   1.00 58.12  ? 325 ASP D OD1 1 
ATOM   14835 O OD2 . ASP D  1 325 ? 21.894  -38.611 61.933   1.00 59.65  ? 325 ASP D OD2 1 
ATOM   14836 N N   . ALA D  1 326 ? 17.408  -41.409 60.912   1.00 33.70  ? 326 ALA D N   1 
ATOM   14837 C CA  . ALA D  1 326 ? 16.615  -42.629 60.971   1.00 29.71  ? 326 ALA D CA  1 
ATOM   14838 C C   . ALA D  1 326 ? 15.643  -42.722 59.800   1.00 27.85  ? 326 ALA D C   1 
ATOM   14839 O O   . ALA D  1 326 ? 15.458  -43.804 59.232   1.00 26.85  ? 326 ALA D O   1 
ATOM   14840 C CB  . ALA D  1 326 ? 15.869  -42.706 62.300   1.00 28.86  ? 326 ALA D CB  1 
ATOM   14841 N N   . VAL D  1 327 ? 14.997  -41.605 59.439   1.00 24.15  ? 327 VAL D N   1 
ATOM   14842 C CA  . VAL D  1 327 ? 14.091  -41.605 58.290   1.00 29.19  ? 327 VAL D CA  1 
ATOM   14843 C C   . VAL D  1 327 ? 14.867  -41.893 57.008   1.00 29.88  ? 327 VAL D C   1 
ATOM   14844 O O   . VAL D  1 327 ? 14.436  -42.694 56.167   1.00 32.05  ? 327 VAL D O   1 
ATOM   14845 C CB  . VAL D  1 327 ? 13.322  -40.269 58.196   1.00 29.23  ? 327 VAL D CB  1 
ATOM   14846 C CG1 . VAL D  1 327 ? 12.438  -40.251 56.942   1.00 30.74  ? 327 VAL D CG1 1 
ATOM   14847 C CG2 . VAL D  1 327 ? 12.473  -40.039 59.441   1.00 28.54  ? 327 VAL D CG2 1 
ATOM   14848 N N   . ARG D  1 328 ? 16.034  -41.263 56.850   1.00 31.88  ? 328 ARG D N   1 
ATOM   14849 C CA  . ARG D  1 328 ? 16.871  -41.564 55.695   1.00 37.10  ? 328 ARG D CA  1 
ATOM   14850 C C   . ARG D  1 328 ? 17.223  -43.044 55.650   1.00 35.92  ? 328 ARG D C   1 
ATOM   14851 O O   . ARG D  1 328 ? 17.113  -43.684 54.595   1.00 29.84  ? 328 ARG D O   1 
ATOM   14852 C CB  . ARG D  1 328 ? 18.138  -40.710 55.724   1.00 46.34  ? 328 ARG D CB  1 
ATOM   14853 C CG  . ARG D  1 328 ? 18.825  -40.594 54.364   1.00 54.73  ? 328 ARG D CG  1 
ATOM   14854 C CD  . ARG D  1 328 ? 19.925  -39.549 54.398   1.00 61.41  ? 328 ARG D CD  1 
ATOM   14855 N NE  . ARG D  1 328 ? 19.521  -38.367 55.155   1.00 65.84  ? 328 ARG D NE  1 
ATOM   14856 C CZ  . ARG D  1 328 ? 19.079  -37.241 54.603   1.00 70.40  ? 328 ARG D CZ  1 
ATOM   14857 N NH1 . ARG D  1 328 ? 18.988  -37.138 53.280   1.00 70.17  ? 328 ARG D NH1 1 
ATOM   14858 N NH2 . ARG D  1 328 ? 18.731  -36.215 55.375   1.00 71.09  ? 328 ARG D NH2 1 
ATOM   14859 N N   . ASP D  1 329 ? 17.619  -43.614 56.793   1.00 34.69  ? 329 ASP D N   1 
ATOM   14860 C CA  . ASP D  1 329 ? 17.947  -45.036 56.830   1.00 33.37  ? 329 ASP D CA  1 
ATOM   14861 C C   . ASP D  1 329 ? 16.737  -45.897 56.489   1.00 31.26  ? 329 ASP D C   1 
ATOM   14862 O O   . ASP D  1 329 ? 16.848  -46.858 55.719   1.00 34.49  ? 329 ASP D O   1 
ATOM   14863 C CB  . ASP D  1 329 ? 18.495  -45.423 58.206   1.00 32.14  ? 329 ASP D CB  1 
ATOM   14864 C CG  . ASP D  1 329 ? 18.843  -46.896 58.286   1.00 33.84  ? 329 ASP D CG  1 
ATOM   14865 O OD1 . ASP D  1 329 ? 19.960  -47.261 57.862   1.00 36.01  ? 329 ASP D OD1 1 
ATOM   14866 O OD2 . ASP D  1 329 ? 17.992  -47.685 58.738   1.00 30.61  ? 329 ASP D OD2 1 
ATOM   14867 N N   . PHE D  1 330 ? 15.584  -45.597 57.091   1.00 27.14  ? 330 PHE D N   1 
ATOM   14868 C CA  . PHE D  1 330 ? 14.370  -46.346 56.792   1.00 25.88  ? 330 PHE D CA  1 
ATOM   14869 C C   . PHE D  1 330 ? 14.037  -46.302 55.301   1.00 30.26  ? 330 PHE D C   1 
ATOM   14870 O O   . PHE D  1 330 ? 13.769  -47.340 54.686   1.00 30.54  ? 330 PHE D O   1 
ATOM   14871 C CB  . PHE D  1 330 ? 13.205  -45.790 57.599   1.00 23.43  ? 330 PHE D CB  1 
ATOM   14872 C CG  . PHE D  1 330 ? 12.046  -46.724 57.696   1.00 26.31  ? 330 PHE D CG  1 
ATOM   14873 C CD1 . PHE D  1 330 ? 12.069  -47.786 58.592   1.00 29.72  ? 330 PHE D CD1 1 
ATOM   14874 C CD2 . PHE D  1 330 ? 10.934  -46.548 56.897   1.00 25.30  ? 330 PHE D CD2 1 
ATOM   14875 C CE1 . PHE D  1 330 ? 10.992  -48.645 58.695   1.00 28.53  ? 330 PHE D CE1 1 
ATOM   14876 C CE2 . PHE D  1 330 ? 9.854   -47.395 56.997   1.00 29.43  ? 330 PHE D CE2 1 
ATOM   14877 C CZ  . PHE D  1 330 ? 9.885   -48.454 57.893   1.00 29.63  ? 330 PHE D CZ  1 
ATOM   14878 N N   . ILE D  1 331 ? 14.012  -45.098 54.717   1.00 32.20  ? 331 ILE D N   1 
ATOM   14879 C CA  . ILE D  1 331 ? 13.694  -44.962 53.295   1.00 35.72  ? 331 ILE D CA  1 
ATOM   14880 C C   . ILE D  1 331 ? 14.774  -45.615 52.451   1.00 36.40  ? 331 ILE D C   1 
ATOM   14881 O O   . ILE D  1 331 ? 14.489  -46.164 51.378   1.00 40.59  ? 331 ILE D O   1 
ATOM   14882 C CB  . ILE D  1 331 ? 13.508  -43.479 52.902   1.00 40.52  ? 331 ILE D CB  1 
ATOM   14883 C CG1 . ILE D  1 331 ? 12.398  -42.812 53.719   1.00 38.31  ? 331 ILE D CG1 1 
ATOM   14884 C CG2 . ILE D  1 331 ? 13.239  -43.340 51.389   1.00 42.53  ? 331 ILE D CG2 1 
ATOM   14885 C CD1 . ILE D  1 331 ? 11.011  -43.389 53.509   1.00 36.57  ? 331 ILE D CD1 1 
ATOM   14886 N N   . GLY D  1 332 ? 16.024  -45.576 52.913   1.00 36.07  ? 332 GLY D N   1 
ATOM   14887 C CA  . GLY D  1 332 ? 17.080  -46.280 52.205   1.00 35.42  ? 332 GLY D CA  1 
ATOM   14888 C C   . GLY D  1 332 ? 16.841  -47.777 52.139   1.00 38.12  ? 332 GLY D C   1 
ATOM   14889 O O   . GLY D  1 332 ? 17.141  -48.423 51.130   1.00 34.68  ? 332 GLY D O   1 
ATOM   14890 N N   . ARG D  1 333 ? 16.294  -48.354 53.211   1.00 36.95  ? 333 ARG D N   1 
ATOM   14891 C CA  . ARG D  1 333 ? 16.020  -49.787 53.178   1.00 36.56  ? 333 ARG D CA  1 
ATOM   14892 C C   . ARG D  1 333 ? 14.848  -50.105 52.264   1.00 32.22  ? 333 ARG D C   1 
ATOM   14893 O O   . ARG D  1 333 ? 14.857  -51.130 51.575   1.00 31.36  ? 333 ARG D O   1 
ATOM   14894 C CB  . ARG D  1 333 ? 15.769  -50.313 54.587   1.00 36.81  ? 333 ARG D CB  1 
ATOM   14895 C CG  . ARG D  1 333 ? 17.046  -50.383 55.394   1.00 40.44  ? 333 ARG D CG  1 
ATOM   14896 C CD  . ARG D  1 333 ? 16.730  -50.448 56.851   1.00 42.69  ? 333 ARG D CD  1 
ATOM   14897 N NE  . ARG D  1 333 ? 17.855  -49.998 57.661   1.00 45.94  ? 333 ARG D NE  1 
ATOM   14898 C CZ  . ARG D  1 333 ? 18.858  -50.772 58.035   1.00 46.37  ? 333 ARG D CZ  1 
ATOM   14899 N NH1 . ARG D  1 333 ? 18.876  -52.052 57.675   1.00 50.95  ? 333 ARG D NH1 1 
ATOM   14900 N NH2 . ARG D  1 333 ? 19.844  -50.264 58.759   1.00 47.66  ? 333 ARG D NH2 1 
ATOM   14901 N N   . LEU D  1 334 ? 13.833  -49.237 52.248   1.00 32.55  ? 334 LEU D N   1 
ATOM   14902 C CA  . LEU D  1 334 ? 12.732  -49.396 51.301   1.00 26.68  ? 334 LEU D CA  1 
ATOM   14903 C C   . LEU D  1 334 ? 13.233  -49.284 49.874   1.00 27.98  ? 334 LEU D C   1 
ATOM   14904 O O   . LEU D  1 334 ? 12.753  -49.990 48.981   1.00 29.85  ? 334 LEU D O   1 
ATOM   14905 C CB  . LEU D  1 334 ? 11.648  -48.348 51.567   1.00 24.92  ? 334 LEU D CB  1 
ATOM   14906 C CG  . LEU D  1 334 ? 10.935  -48.507 52.914   1.00 23.78  ? 334 LEU D CG  1 
ATOM   14907 C CD1 . LEU D  1 334 ? 9.813   -47.485 53.041   1.00 20.27  ? 334 LEU D CD1 1 
ATOM   14908 C CD2 . LEU D  1 334 ? 10.447  -49.944 53.102   1.00 22.21  ? 334 LEU D CD2 1 
ATOM   14909 N N   . LYS D  1 335 ? 14.207  -48.407 49.641   1.00 29.42  ? 335 LYS D N   1 
ATOM   14910 C CA  . LYS D  1 335 ? 14.820  -48.336 48.318   1.00 32.31  ? 335 LYS D CA  1 
ATOM   14911 C C   . LYS D  1 335 ? 15.498  -49.653 47.956   1.00 34.07  ? 335 LYS D C   1 
ATOM   14912 O O   . LYS D  1 335 ? 15.383  -50.128 46.817   1.00 28.47  ? 335 LYS D O   1 
ATOM   14913 C CB  . LYS D  1 335 ? 15.826  -47.193 48.257   1.00 32.58  ? 335 LYS D CB  1 
ATOM   14914 C CG  . LYS D  1 335 ? 16.375  -46.938 46.847   1.00 39.92  ? 335 LYS D CG  1 
ATOM   14915 C CD  . LYS D  1 335 ? 17.887  -46.798 46.856   1.00 40.66  ? 335 LYS D CD  1 
ATOM   14916 C CE  . LYS D  1 335 ? 18.404  -46.193 45.555   1.00 43.18  ? 335 LYS D CE  1 
ATOM   14917 N NZ  . LYS D  1 335 ? 18.540  -47.172 44.437   1.00 44.68  ? 335 LYS D NZ  1 
ATOM   14918 N N   . LYS D  1 336 ? 16.212  -50.256 48.910   1.00 33.37  ? 336 LYS D N   1 
ATOM   14919 C CA  . LYS D  1 336 ? 16.920  -51.498 48.610   1.00 38.90  ? 336 LYS D CA  1 
ATOM   14920 C C   . LYS D  1 336 ? 15.948  -52.637 48.343   1.00 35.49  ? 336 LYS D C   1 
ATOM   14921 O O   . LYS D  1 336 ? 16.210  -53.484 47.483   1.00 36.95  ? 336 LYS D O   1 
ATOM   14922 C CB  . LYS D  1 336 ? 17.877  -51.866 49.744   1.00 44.32  ? 336 LYS D CB  1 
ATOM   14923 C CG  . LYS D  1 336 ? 19.325  -51.495 49.458   1.00 51.51  ? 336 LYS D CG  1 
ATOM   14924 C CD  . LYS D  1 336 ? 19.615  -50.060 49.870   1.00 53.22  ? 336 LYS D CD  1 
ATOM   14925 C CE  . LYS D  1 336 ? 21.077  -49.886 50.268   1.00 57.39  ? 336 LYS D CE  1 
ATOM   14926 N NZ  . LYS D  1 336 ? 21.262  -48.795 51.268   1.00 58.99  ? 336 LYS D NZ  1 
ATOM   14927 N N   . ILE D  1 337 ? 14.829  -52.674 49.075   1.00 34.85  ? 337 ILE D N   1 
ATOM   14928 C CA  . ILE D  1 337 ? 13.764  -53.625 48.775   1.00 32.35  ? 337 ILE D CA  1 
ATOM   14929 C C   . ILE D  1 337 ? 13.227  -53.383 47.365   1.00 31.06  ? 337 ILE D C   1 
ATOM   14930 O O   . ILE D  1 337 ? 13.129  -54.307 46.547   1.00 29.12  ? 337 ILE D O   1 
ATOM   14931 C CB  . ILE D  1 337 ? 12.639  -53.519 49.822   1.00 30.32  ? 337 ILE D CB  1 
ATOM   14932 C CG1 . ILE D  1 337 ? 13.149  -53.876 51.230   1.00 31.51  ? 337 ILE D CG1 1 
ATOM   14933 C CG2 . ILE D  1 337 ? 11.462  -54.384 49.428   1.00 31.91  ? 337 ILE D CG2 1 
ATOM   14934 C CD1 . ILE D  1 337 ? 12.109  -53.698 52.361   1.00 27.50  ? 337 ILE D CD1 1 
ATOM   14935 N N   . HIS D  1 338 ? 12.849  -52.138 47.076   1.00 28.55  ? 338 HIS D N   1 
ATOM   14936 C CA  . HIS D  1 338 ? 12.268  -51.798 45.782   1.00 37.87  ? 338 HIS D CA  1 
ATOM   14937 C C   . HIS D  1 338 ? 13.161  -52.230 44.623   1.00 40.54  ? 338 HIS D C   1 
ATOM   14938 O O   . HIS D  1 338 ? 12.660  -52.625 43.564   1.00 44.52  ? 338 HIS D O   1 
ATOM   14939 C CB  . HIS D  1 338 ? 12.012  -50.290 45.718   1.00 39.57  ? 338 HIS D CB  1 
ATOM   14940 C CG  . HIS D  1 338 ? 11.396  -49.828 44.433   1.00 45.65  ? 338 HIS D CG  1 
ATOM   14941 N ND1 . HIS D  1 338 ? 12.091  -49.094 43.500   1.00 48.75  ? 338 HIS D ND1 1 
ATOM   14942 C CD2 . HIS D  1 338 ? 10.145  -49.978 43.939   1.00 45.99  ? 338 HIS D CD2 1 
ATOM   14943 C CE1 . HIS D  1 338 ? 11.299  -48.820 42.480   1.00 51.17  ? 338 HIS D CE1 1 
ATOM   14944 N NE2 . HIS D  1 338 ? 10.112  -49.345 42.722   1.00 47.87  ? 338 HIS D NE2 1 
ATOM   14945 N N   . GLU D  1 339 ? 14.479  -52.183 44.811   1.00 39.96  ? 339 GLU D N   1 
ATOM   14946 C CA  . GLU D  1 339 ? 15.408  -52.495 43.738   1.00 49.73  ? 339 GLU D CA  1 
ATOM   14947 C C   . GLU D  1 339 ? 15.714  -53.979 43.609   1.00 52.28  ? 339 GLU D C   1 
ATOM   14948 O O   . GLU D  1 339 ? 16.172  -54.404 42.543   1.00 57.84  ? 339 GLU D O   1 
ATOM   14949 C CB  . GLU D  1 339 ? 16.726  -51.730 43.930   1.00 56.87  ? 339 GLU D CB  1 
ATOM   14950 C CG  . GLU D  1 339 ? 16.613  -50.197 43.936   1.00 64.54  ? 339 GLU D CG  1 
ATOM   14951 C CD  . GLU D  1 339 ? 16.053  -49.583 42.646   1.00 76.44  ? 339 GLU D CD  1 
ATOM   14952 O OE1 . GLU D  1 339 ? 15.481  -50.299 41.792   1.00 80.60  ? 339 GLU D OE1 1 
ATOM   14953 O OE2 . GLU D  1 339 ? 16.188  -48.350 42.482   1.00 80.84  ? 339 GLU D OE2 1 
ATOM   14954 N N   . SER D  1 340 ? 15.468  -54.777 44.649   1.00 49.89  ? 340 SER D N   1 
ATOM   14955 C CA  . SER D  1 340 ? 15.864  -56.181 44.656   1.00 50.34  ? 340 SER D CA  1 
ATOM   14956 C C   . SER D  1 340 ? 14.802  -57.126 44.105   1.00 49.45  ? 340 SER D C   1 
ATOM   14957 O O   . SER D  1 340 ? 15.043  -58.338 44.054   1.00 53.96  ? 340 SER D O   1 
ATOM   14958 C CB  . SER D  1 340 ? 16.220  -56.611 46.077   1.00 51.48  ? 340 SER D CB  1 
ATOM   14959 O OG  . SER D  1 340 ? 15.088  -56.475 46.925   1.00 50.32  ? 340 SER D OG  1 
ATOM   14960 N N   . VAL D  1 341 ? 13.642  -56.619 43.702   1.00 44.74  ? 341 VAL D N   1 
ATOM   14961 C CA  . VAL D  1 341 ? 12.560  -57.443 43.179   1.00 45.63  ? 341 VAL D CA  1 
ATOM   14962 C C   . VAL D  1 341 ? 12.097  -56.845 41.859   1.00 46.12  ? 341 VAL D C   1 
ATOM   14963 O O   . VAL D  1 341 ? 12.082  -55.619 41.702   1.00 46.74  ? 341 VAL D O   1 
ATOM   14964 C CB  . VAL D  1 341 ? 11.384  -57.535 44.178   1.00 44.78  ? 341 VAL D CB  1 
ATOM   14965 C CG1 . VAL D  1 341 ? 11.790  -58.331 45.390   1.00 47.32  ? 341 VAL D CG1 1 
ATOM   14966 C CG2 . VAL D  1 341 ? 10.930  -56.153 44.593   1.00 40.66  ? 341 VAL D CG2 1 
ATOM   14967 N N   . ASP D  1 342 ? 11.738  -57.706 40.902   1.00 49.50  ? 342 ASP D N   1 
ATOM   14968 C CA  . ASP D  1 342 ? 11.164  -57.253 39.639   1.00 54.98  ? 342 ASP D CA  1 
ATOM   14969 C C   . ASP D  1 342 ? 9.654   -57.073 39.720   1.00 52.22  ? 342 ASP D C   1 
ATOM   14970 O O   . ASP D  1 342 ? 9.038   -56.633 38.744   1.00 54.43  ? 342 ASP D O   1 
ATOM   14971 C CB  . ASP D  1 342 ? 11.509  -58.232 38.510   1.00 65.48  ? 342 ASP D CB  1 
ATOM   14972 C CG  . ASP D  1 342 ? 10.616  -59.446 38.507   1.00 73.07  ? 342 ASP D CG  1 
ATOM   14973 O OD1 . ASP D  1 342 ? 10.522  -60.117 39.560   1.00 73.91  ? 342 ASP D OD1 1 
ATOM   14974 O OD2 . ASP D  1 342 ? 9.997   -59.718 37.454   1.00 77.20  ? 342 ASP D OD2 1 
ATOM   14975 N N   . PHE D  1 343 ? 9.046   -57.390 40.857   1.00 45.38  ? 343 PHE D N   1 
ATOM   14976 C CA  . PHE D  1 343 ? 7.618   -57.219 41.060   1.00 40.00  ? 343 PHE D CA  1 
ATOM   14977 C C   . PHE D  1 343 ? 7.391   -56.142 42.118   1.00 40.44  ? 343 PHE D C   1 
ATOM   14978 O O   . PHE D  1 343 ? 8.334   -55.582 42.682   1.00 42.73  ? 343 PHE D O   1 
ATOM   14979 C CB  . PHE D  1 343 ? 6.981   -58.548 41.459   1.00 34.58  ? 343 PHE D CB  1 
ATOM   14980 C CG  . PHE D  1 343 ? 7.477   -59.082 42.780   1.00 33.20  ? 343 PHE D CG  1 
ATOM   14981 C CD1 . PHE D  1 343 ? 8.641   -59.849 42.844   1.00 33.93  ? 343 PHE D CD1 1 
ATOM   14982 C CD2 . PHE D  1 343 ? 6.786   -58.810 43.955   1.00 28.81  ? 343 PHE D CD2 1 
ATOM   14983 C CE1 . PHE D  1 343 ? 9.096   -60.351 44.067   1.00 36.77  ? 343 PHE D CE1 1 
ATOM   14984 C CE2 . PHE D  1 343 ? 7.232   -59.311 45.188   1.00 32.34  ? 343 PHE D CE2 1 
ATOM   14985 C CZ  . PHE D  1 343 ? 8.385   -60.082 45.242   1.00 34.23  ? 343 PHE D CZ  1 
ATOM   14986 N N   . GLN D  1 344 ? 6.123   -55.841 42.388   1.00 37.16  ? 344 GLN D N   1 
ATOM   14987 C CA  . GLN D  1 344 ? 5.797   -54.820 43.369   1.00 31.13  ? 344 GLN D CA  1 
ATOM   14988 C C   . GLN D  1 344 ? 5.699   -55.473 44.737   1.00 29.79  ? 344 GLN D C   1 
ATOM   14989 O O   . GLN D  1 344 ? 4.722   -56.192 44.995   1.00 26.32  ? 344 GLN D O   1 
ATOM   14990 C CB  . GLN D  1 344 ? 4.494   -54.122 43.017   1.00 23.93  ? 344 GLN D CB  1 
ATOM   14991 C CG  . GLN D  1 344 ? 4.532   -53.519 41.611   1.00 26.18  ? 344 GLN D CG  1 
ATOM   14992 C CD  . GLN D  1 344 ? 3.408   -52.558 41.377   1.00 27.65  ? 344 GLN D CD  1 
ATOM   14993 O OE1 . GLN D  1 344 ? 3.628   -51.356 41.245   1.00 32.70  ? 344 GLN D OE1 1 
ATOM   14994 N NE2 . GLN D  1 344 ? 2.182   -53.078 41.323   1.00 27.35  ? 344 GLN D NE2 1 
ATOM   14995 N N   . PRO D  1 345 ? 6.645   -55.231 45.642   1.00 28.72  ? 345 PRO D N   1 
ATOM   14996 C CA  . PRO D  1 345 ? 6.609   -55.874 46.955   1.00 27.00  ? 345 PRO D CA  1 
ATOM   14997 C C   . PRO D  1 345 ? 5.606   -55.234 47.899   1.00 23.85  ? 345 PRO D C   1 
ATOM   14998 O O   . PRO D  1 345 ? 5.395   -54.018 47.891   1.00 26.24  ? 345 PRO D O   1 
ATOM   14999 C CB  . PRO D  1 345 ? 8.037   -55.665 47.475   1.00 29.18  ? 345 PRO D CB  1 
ATOM   15000 C CG  . PRO D  1 345 ? 8.430   -54.347 46.904   1.00 25.41  ? 345 PRO D CG  1 
ATOM   15001 C CD  . PRO D  1 345 ? 7.777   -54.295 45.520   1.00 29.20  ? 345 PRO D CD  1 
ATOM   15002 N N   . VAL D  1 346 ? 5.017   -56.070 48.757   1.00 30.90  ? 346 VAL D N   1 
ATOM   15003 C CA  . VAL D  1 346 ? 4.177   -55.606 49.860   1.00 27.59  ? 346 VAL D CA  1 
ATOM   15004 C C   . VAL D  1 346 ? 4.986   -55.754 51.146   1.00 27.51  ? 346 VAL D C   1 
ATOM   15005 O O   . VAL D  1 346 ? 5.437   -56.861 51.485   1.00 24.84  ? 346 VAL D O   1 
ATOM   15006 C CB  . VAL D  1 346 ? 2.851   -56.382 49.934   1.00 25.28  ? 346 VAL D CB  1 
ATOM   15007 C CG1 . VAL D  1 346 ? 1.947   -55.812 51.041   1.00 28.66  ? 346 VAL D CG1 1 
ATOM   15008 C CG2 . VAL D  1 346 ? 2.140   -56.330 48.603   1.00 25.14  ? 346 VAL D CG2 1 
ATOM   15009 N N   . VAL D  1 347 ? 5.181   -54.641 51.851   1.00 27.57  ? 347 VAL D N   1 
ATOM   15010 C CA  . VAL D  1 347 ? 6.047   -54.575 53.032   1.00 25.89  ? 347 VAL D CA  1 
ATOM   15011 C C   . VAL D  1 347 ? 5.192   -54.234 54.247   1.00 25.86  ? 347 VAL D C   1 
ATOM   15012 O O   . VAL D  1 347 ? 4.771   -53.079 54.413   1.00 21.90  ? 347 VAL D O   1 
ATOM   15013 C CB  . VAL D  1 347 ? 7.168   -53.546 52.862   1.00 21.91  ? 347 VAL D CB  1 
ATOM   15014 C CG1 . VAL D  1 347 ? 8.113   -53.612 54.042   1.00 27.88  ? 347 VAL D CG1 1 
ATOM   15015 C CG2 . VAL D  1 347 ? 7.924   -53.768 51.550   1.00 23.06  ? 347 VAL D CG2 1 
ATOM   15016 N N   . PHE D  1 348 ? 4.954   -55.222 55.107   1.00 28.55  ? 348 PHE D N   1 
ATOM   15017 C CA  . PHE D  1 348 ? 4.180   -55.002 56.324   1.00 25.20  ? 348 PHE D CA  1 
ATOM   15018 C C   . PHE D  1 348 ? 5.114   -54.608 57.462   1.00 21.78  ? 348 PHE D C   1 
ATOM   15019 O O   . PHE D  1 348 ? 6.019   -55.373 57.827   1.00 24.02  ? 348 PHE D O   1 
ATOM   15020 C CB  . PHE D  1 348 ? 3.378   -56.248 56.697   1.00 20.69  ? 348 PHE D CB  1 
ATOM   15021 C CG  . PHE D  1 348 ? 1.990   -56.234 56.170   1.00 22.60  ? 348 PHE D CG  1 
ATOM   15022 C CD1 . PHE D  1 348 ? 1.767   -56.260 54.794   1.00 21.99  ? 348 PHE D CD1 1 
ATOM   15023 C CD2 . PHE D  1 348 ? 0.904   -56.202 57.029   1.00 22.56  ? 348 PHE D CD2 1 
ATOM   15024 C CE1 . PHE D  1 348 ? 0.481   -56.259 54.287   1.00 22.06  ? 348 PHE D CE1 1 
ATOM   15025 C CE2 . PHE D  1 348 ? -0.372  -56.216 56.535   1.00 27.27  ? 348 PHE D CE2 1 
ATOM   15026 C CZ  . PHE D  1 348 ? -0.589  -56.240 55.152   1.00 25.74  ? 348 PHE D CZ  1 
ATOM   15027 N N   . VAL D  1 349 ? 4.904   -53.407 57.995   1.00 19.75  ? 349 VAL D N   1 
ATOM   15028 C CA  . VAL D  1 349 ? 5.575   -52.918 59.194   1.00 21.99  ? 349 VAL D CA  1 
ATOM   15029 C C   . VAL D  1 349 ? 4.560   -53.002 60.329   1.00 23.32  ? 349 VAL D C   1 
ATOM   15030 O O   . VAL D  1 349 ? 3.626   -52.190 60.393   1.00 25.07  ? 349 VAL D O   1 
ATOM   15031 C CB  . VAL D  1 349 ? 6.090   -51.489 59.006   1.00 21.81  ? 349 VAL D CB  1 
ATOM   15032 C CG1 . VAL D  1 349 ? 6.719   -50.959 60.304   1.00 27.17  ? 349 VAL D CG1 1 
ATOM   15033 C CG2 . VAL D  1 349 ? 7.105   -51.437 57.830   1.00 22.12  ? 349 VAL D CG2 1 
ATOM   15034 N N   . VAL D  1 350 ? 4.729   -53.982 61.219   1.00 22.84  ? 350 VAL D N   1 
ATOM   15035 C CA  . VAL D  1 350 ? 3.761   -54.274 62.275   1.00 24.62  ? 350 VAL D CA  1 
ATOM   15036 C C   . VAL D  1 350 ? 4.474   -54.293 63.629   1.00 27.30  ? 350 VAL D C   1 
ATOM   15037 O O   . VAL D  1 350 ? 5.393   -55.098 63.840   1.00 24.62  ? 350 VAL D O   1 
ATOM   15038 C CB  . VAL D  1 350 ? 3.040   -55.616 62.054   1.00 20.37  ? 350 VAL D CB  1 
ATOM   15039 C CG1 . VAL D  1 350 ? 1.899   -55.776 63.118   1.00 18.02  ? 350 VAL D CG1 1 
ATOM   15040 C CG2 . VAL D  1 350 ? 2.476   -55.744 60.644   1.00 16.40  ? 350 VAL D CG2 1 
ATOM   15041 N N   . LEU D  1 351 ? 4.026   -53.442 64.555   1.00 26.62  ? 351 LEU D N   1 
ATOM   15042 C CA  . LEU D  1 351 ? 4.571   -53.449 65.911   1.00 24.86  ? 351 LEU D CA  1 
ATOM   15043 C C   . LEU D  1 351 ? 3.574   -52.780 66.843   1.00 22.65  ? 351 LEU D C   1 
ATOM   15044 O O   . LEU D  1 351 ? 2.543   -52.252 66.414   1.00 20.42  ? 351 LEU D O   1 
ATOM   15045 C CB  . LEU D  1 351 ? 5.936   -52.760 65.963   1.00 22.91  ? 351 LEU D CB  1 
ATOM   15046 C CG  . LEU D  1 351 ? 5.983   -51.297 65.539   1.00 26.67  ? 351 LEU D CG  1 
ATOM   15047 C CD1 . LEU D  1 351 ? 7.120   -50.564 66.251   1.00 28.39  ? 351 LEU D CD1 1 
ATOM   15048 C CD2 . LEU D  1 351 ? 6.133   -51.147 63.998   1.00 20.83  ? 351 LEU D CD2 1 
ATOM   15049 N N   . ASN D  1 352 ? 3.886   -52.806 68.135   1.00 21.20  ? 352 ASN D N   1 
ATOM   15050 C CA  . ASN D  1 352 ? 3.035   -52.094 69.070   1.00 19.60  ? 352 ASN D CA  1 
ATOM   15051 C C   . ASN D  1 352 ? 3.095   -50.607 68.761   1.00 20.75  ? 352 ASN D C   1 
ATOM   15052 O O   . ASN D  1 352 ? 4.150   -50.074 68.393   1.00 20.40  ? 352 ASN D O   1 
ATOM   15053 C CB  . ASN D  1 352 ? 3.467   -52.361 70.515   1.00 20.29  ? 352 ASN D CB  1 
ATOM   15054 C CG  . ASN D  1 352 ? 2.779   -53.537 71.096   1.00 20.83  ? 352 ASN D CG  1 
ATOM   15055 O OD1 . ASN D  1 352 ? 3.231   -54.683 70.937   1.00 21.80  ? 352 ASN D OD1 1 
ATOM   15056 N ND2 . ASN D  1 352 ? 1.657   -53.286 71.773   1.00 20.06  ? 352 ASN D ND2 1 
ATOM   15057 N N   . GLY D  1 353 ? 1.948   -49.950 68.843   1.00 16.31  ? 353 GLY D N   1 
ATOM   15058 C CA  . GLY D  1 353 ? 1.873   -48.542 68.509   1.00 17.00  ? 353 GLY D CA  1 
ATOM   15059 C C   . GLY D  1 353 ? 1.997   -47.562 69.650   1.00 22.23  ? 353 GLY D C   1 
ATOM   15060 O O   . GLY D  1 353 ? 1.814   -46.356 69.435   1.00 24.16  ? 353 GLY D O   1 
ATOM   15061 N N   . GLU D  1 354 ? 2.318   -48.023 70.853   1.00 25.38  ? 354 GLU D N   1 
ATOM   15062 C CA  . GLU D  1 354 ? 2.320   -47.126 72.000   1.00 24.54  ? 354 GLU D CA  1 
ATOM   15063 C C   . GLU D  1 354 ? 3.495   -47.327 72.945   1.00 26.43  ? 354 GLU D C   1 
ATOM   15064 O O   . GLU D  1 354 ? 3.660   -46.505 73.851   1.00 26.03  ? 354 GLU D O   1 
ATOM   15065 C CB  . GLU D  1 354 ? 1.005   -47.289 72.784   1.00 24.81  ? 354 GLU D CB  1 
ATOM   15066 C CG  . GLU D  1 354 ? 0.963   -48.496 73.752   1.00 18.40  ? 354 GLU D CG  1 
ATOM   15067 C CD  . GLU D  1 354 ? 0.596   -49.831 73.086   1.00 21.18  ? 354 GLU D CD  1 
ATOM   15068 O OE1 . GLU D  1 354 ? -0.488  -50.386 73.384   1.00 19.49  ? 354 GLU D OE1 1 
ATOM   15069 O OE2 . GLU D  1 354 ? 1.391   -50.327 72.259   1.00 22.39  ? 354 GLU D OE2 1 
ATOM   15070 N N   . ASN D  1 355 ? 4.330   -48.361 72.766   1.00 24.46  ? 355 ASN D N   1 
ATOM   15071 C CA  . ASN D  1 355 ? 5.364   -48.656 73.749   1.00 23.54  ? 355 ASN D CA  1 
ATOM   15072 C C   . ASN D  1 355 ? 6.748   -48.141 73.388   1.00 25.42  ? 355 ASN D C   1 
ATOM   15073 O O   . ASN D  1 355 ? 7.596   -48.025 74.283   1.00 26.44  ? 355 ASN D O   1 
ATOM   15074 C CB  . ASN D  1 355 ? 5.433   -50.171 73.991   1.00 24.06  ? 355 ASN D CB  1 
ATOM   15075 C CG  . ASN D  1 355 ? 4.171   -50.690 74.639   1.00 25.61  ? 355 ASN D CG  1 
ATOM   15076 O OD1 . ASN D  1 355 ? 3.536   -49.968 75.412   1.00 26.03  ? 355 ASN D OD1 1 
ATOM   15077 N ND2 . ASN D  1 355 ? 3.768   -51.922 74.299   1.00 23.30  ? 355 ASN D ND2 1 
ATOM   15078 N N   . CYS D  1 356 ? 7.021   -47.811 72.126   1.00 23.07  ? 356 CYS D N   1 
ATOM   15079 C CA  . CYS D  1 356 ? 8.388   -47.420 71.811   1.00 18.97  ? 356 CYS D CA  1 
ATOM   15080 C C   . CYS D  1 356 ? 8.620   -45.917 71.903   1.00 17.76  ? 356 CYS D C   1 
ATOM   15081 O O   . CYS D  1 356 ? 9.763   -45.502 72.069   1.00 23.95  ? 356 CYS D O   1 
ATOM   15082 C CB  . CYS D  1 356 ? 8.785   -47.922 70.422   1.00 27.43  ? 356 CYS D CB  1 
ATOM   15083 S SG  . CYS D  1 356 ? 7.704   -47.348 69.064   1.00 27.33  ? 356 CYS D SG  1 
ATOM   15084 N N   . TRP D  1 357 ? 7.562   -45.104 71.837   1.00 20.25  ? 357 TRP D N   1 
ATOM   15085 C CA  . TRP D  1 357 ? 7.720   -43.659 71.661   1.00 22.82  ? 357 TRP D CA  1 
ATOM   15086 C C   . TRP D  1 357 ? 8.289   -42.976 72.897   1.00 25.05  ? 357 TRP D C   1 
ATOM   15087 O O   . TRP D  1 357 ? 9.038   -42.001 72.767   1.00 31.50  ? 357 TRP D O   1 
ATOM   15088 C CB  . TRP D  1 357 ? 6.380   -43.044 71.269   1.00 22.56  ? 357 TRP D CB  1 
ATOM   15089 C CG  . TRP D  1 357 ? 5.726   -43.802 70.116   1.00 22.44  ? 357 TRP D CG  1 
ATOM   15090 C CD1 . TRP D  1 357 ? 4.502   -44.396 70.114   1.00 19.99  ? 357 TRP D CD1 1 
ATOM   15091 C CD2 . TRP D  1 357 ? 6.296   -44.057 68.827   1.00 23.65  ? 357 TRP D CD2 1 
ATOM   15092 N NE1 . TRP D  1 357 ? 4.265   -44.996 68.902   1.00 24.79  ? 357 TRP D NE1 1 
ATOM   15093 C CE2 . TRP D  1 357 ? 5.356   -44.805 68.096   1.00 23.37  ? 357 TRP D CE2 1 
ATOM   15094 C CE3 . TRP D  1 357 ? 7.506   -43.716 68.217   1.00 25.45  ? 357 TRP D CE3 1 
ATOM   15095 C CZ2 . TRP D  1 357 ? 5.586   -45.216 66.789   1.00 24.69  ? 357 TRP D CZ2 1 
ATOM   15096 C CZ3 . TRP D  1 357 ? 7.737   -44.134 66.913   1.00 23.18  ? 357 TRP D CZ3 1 
ATOM   15097 C CH2 . TRP D  1 357 ? 6.780   -44.871 66.217   1.00 24.89  ? 357 TRP D CH2 1 
ATOM   15098 N N   . GLU D  1 358 ? 7.984   -43.478 74.094   1.00 24.17  ? 358 GLU D N   1 
ATOM   15099 C CA  . GLU D  1 358 ? 8.475   -42.831 75.310   1.00 24.29  ? 358 GLU D CA  1 
ATOM   15100 C C   . GLU D  1 358 ? 10.000  -42.816 75.390   1.00 27.72  ? 358 GLU D C   1 
ATOM   15101 O O   . GLU D  1 358 ? 10.561  -42.054 76.191   1.00 28.00  ? 358 GLU D O   1 
ATOM   15102 C CB  . GLU D  1 358 ? 7.888   -43.524 76.547   1.00 23.42  ? 358 GLU D CB  1 
ATOM   15103 C CG  . GLU D  1 358 ? 8.218   -45.030 76.627   1.00 24.57  ? 358 GLU D CG  1 
ATOM   15104 C CD  . GLU D  1 358 ? 7.248   -45.821 77.513   1.00 29.23  ? 358 GLU D CD  1 
ATOM   15105 O OE1 . GLU D  1 358 ? 7.687   -46.333 78.565   1.00 32.19  ? 358 GLU D OE1 1 
ATOM   15106 O OE2 . GLU D  1 358 ? 6.053   -45.942 77.156   1.00 29.44  ? 358 GLU D OE2 1 
ATOM   15107 N N   . TYR D  1 359 ? 10.686  -43.640 74.593   1.00 25.11  ? 359 TYR D N   1 
ATOM   15108 C CA  . TYR D  1 359 ? 12.145  -43.657 74.554   1.00 26.08  ? 359 TYR D CA  1 
ATOM   15109 C C   . TYR D  1 359 ? 12.725  -42.739 73.486   1.00 26.82  ? 359 TYR D C   1 
ATOM   15110 O O   . TYR D  1 359 ? 13.946  -42.540 73.450   1.00 26.94  ? 359 TYR D O   1 
ATOM   15111 C CB  . TYR D  1 359 ? 12.645  -45.091 74.332   1.00 30.65  ? 359 TYR D CB  1 
ATOM   15112 C CG  . TYR D  1 359 ? 12.182  -46.024 75.425   1.00 35.20  ? 359 TYR D CG  1 
ATOM   15113 C CD1 . TYR D  1 359 ? 12.863  -46.084 76.641   1.00 37.92  ? 359 TYR D CD1 1 
ATOM   15114 C CD2 . TYR D  1 359 ? 11.049  -46.814 75.270   1.00 35.06  ? 359 TYR D CD2 1 
ATOM   15115 C CE1 . TYR D  1 359 ? 12.442  -46.921 77.669   1.00 40.27  ? 359 TYR D CE1 1 
ATOM   15116 C CE2 . TYR D  1 359 ? 10.617  -47.665 76.305   1.00 38.77  ? 359 TYR D CE2 1 
ATOM   15117 C CZ  . TYR D  1 359 ? 11.318  -47.711 77.504   1.00 40.00  ? 359 TYR D CZ  1 
ATOM   15118 O OH  . TYR D  1 359 ? 10.916  -48.539 78.553   1.00 38.69  ? 359 TYR D OH  1 
ATOM   15119 N N   . TYR D  1 360 ? 11.890  -42.185 72.615   1.00 23.51  ? 360 TYR D N   1 
ATOM   15120 C CA  . TYR D  1 360 ? 12.355  -41.269 71.585   1.00 31.88  ? 360 TYR D CA  1 
ATOM   15121 C C   . TYR D  1 360 ? 12.339  -39.863 72.146   1.00 32.39  ? 360 TYR D C   1 
ATOM   15122 O O   . TYR D  1 360 ? 11.517  -39.534 72.999   1.00 33.70  ? 360 TYR D O   1 
ATOM   15123 C CB  . TYR D  1 360 ? 11.459  -41.282 70.342   1.00 24.57  ? 360 TYR D CB  1 
ATOM   15124 C CG  . TYR D  1 360 ? 11.557  -42.436 69.374   1.00 26.04  ? 360 TYR D CG  1 
ATOM   15125 C CD1 . TYR D  1 360 ? 11.234  -43.723 69.766   1.00 26.37  ? 360 TYR D CD1 1 
ATOM   15126 C CD2 . TYR D  1 360 ? 11.891  -42.219 68.032   1.00 24.15  ? 360 TYR D CD2 1 
ATOM   15127 C CE1 . TYR D  1 360 ? 11.287  -44.779 68.878   1.00 26.76  ? 360 TYR D CE1 1 
ATOM   15128 C CE2 . TYR D  1 360 ? 11.951  -43.276 67.128   1.00 27.24  ? 360 TYR D CE2 1 
ATOM   15129 C CZ  . TYR D  1 360 ? 11.647  -44.550 67.556   1.00 29.90  ? 360 TYR D CZ  1 
ATOM   15130 O OH  . TYR D  1 360 ? 11.692  -45.601 66.674   1.00 30.96  ? 360 TYR D OH  1 
ATOM   15131 N N   . GLU D  1 361 ? 13.238  -39.028 71.636   1.00 30.42  ? 361 GLU D N   1 
ATOM   15132 C CA  . GLU D  1 361 ? 13.160  -37.594 71.887   1.00 34.76  ? 361 GLU D CA  1 
ATOM   15133 C C   . GLU D  1 361 ? 11.782  -37.071 71.500   1.00 35.04  ? 361 GLU D C   1 
ATOM   15134 O O   . GLU D  1 361 ? 11.207  -37.469 70.481   1.00 28.68  ? 361 GLU D O   1 
ATOM   15135 C CB  . GLU D  1 361 ? 14.232  -36.842 71.092   1.00 45.08  ? 361 GLU D CB  1 
ATOM   15136 C CG  . GLU D  1 361 ? 14.351  -35.353 71.433   1.00 61.07  ? 361 GLU D CG  1 
ATOM   15137 C CD  . GLU D  1 361 ? 15.478  -35.065 72.413   1.00 71.76  ? 361 GLU D CD  1 
ATOM   15138 O OE1 . GLU D  1 361 ? 15.815  -33.903 72.667   1.00 77.99  ? 361 GLU D OE1 1 
ATOM   15139 O OE2 . GLU D  1 361 ? 16.048  -36.084 72.911   1.00 73.32  ? 361 GLU D OE2 1 
ATOM   15140 N N   . GLU D  1 362 ? 11.253  -36.176 72.340   1.00 39.09  ? 362 GLU D N   1 
ATOM   15141 C CA  . GLU D  1 362 ? 9.956   -35.529 72.128   1.00 37.63  ? 362 GLU D CA  1 
ATOM   15142 C C   . GLU D  1 362 ? 8.869   -36.544 71.806   1.00 31.84  ? 362 GLU D C   1 
ATOM   15143 O O   . GLU D  1 362 ? 7.982   -36.284 70.989   1.00 30.90  ? 362 GLU D O   1 
ATOM   15144 C CB  . GLU D  1 362 ? 10.044  -34.488 71.025   1.00 40.95  ? 362 GLU D CB  1 
ATOM   15145 C CG  . GLU D  1 362 ? 10.618  -33.163 71.454   1.00 48.49  ? 362 GLU D CG  1 
ATOM   15146 C CD  . GLU D  1 362 ? 10.639  -32.179 70.310   1.00 58.15  ? 362 GLU D CD  1 
ATOM   15147 O OE1 . GLU D  1 362 ? 9.688   -32.195 69.490   1.00 57.92  ? 362 GLU D OE1 1 
ATOM   15148 O OE2 . GLU D  1 362 ? 11.619  -31.410 70.215   1.00 64.43  ? 362 GLU D OE2 1 
ATOM   15149 N N   . ASN D  1 363 ? 8.946   -37.713 72.437   1.00 29.58  ? 363 ASN D N   1 
ATOM   15150 C CA  . ASN D  1 363 ? 7.915   -38.738 72.326   1.00 28.98  ? 363 ASN D CA  1 
ATOM   15151 C C   . ASN D  1 363 ? 7.761   -39.243 70.891   1.00 28.21  ? 363 ASN D C   1 
ATOM   15152 O O   . ASN D  1 363 ? 6.686   -39.687 70.491   1.00 24.73  ? 363 ASN D O   1 
ATOM   15153 C CB  . ASN D  1 363 ? 6.579   -38.226 72.868   1.00 26.34  ? 363 ASN D CB  1 
ATOM   15154 C CG  . ASN D  1 363 ? 5.570   -39.325 73.044   1.00 23.50  ? 363 ASN D CG  1 
ATOM   15155 O OD1 . ASN D  1 363 ? 5.909   -40.460 73.428   1.00 24.96  ? 363 ASN D OD1 1 
ATOM   15156 N ND2 . ASN D  1 363 ? 4.315   -39.010 72.744   1.00 22.78  ? 363 ASN D ND2 1 
ATOM   15157 N N   . GLY D  1 364 ? 8.830   -39.186 70.101   1.00 28.33  ? 364 GLY D N   1 
ATOM   15158 C CA  . GLY D  1 364 ? 8.781   -39.727 68.757   1.00 28.24  ? 364 GLY D CA  1 
ATOM   15159 C C   . GLY D  1 364 ? 8.111   -38.842 67.741   1.00 28.06  ? 364 GLY D C   1 
ATOM   15160 O O   . GLY D  1 364 ? 7.977   -39.243 66.574   1.00 29.20  ? 364 GLY D O   1 
ATOM   15161 N N   . ILE D  1 365 ? 7.697   -37.646 68.148   1.00 29.16  ? 365 ILE D N   1 
ATOM   15162 C CA  . ILE D  1 365 ? 7.047   -36.729 67.216   1.00 29.09  ? 365 ILE D CA  1 
ATOM   15163 C C   . ILE D  1 365 ? 7.986   -36.294 66.095   1.00 27.09  ? 365 ILE D C   1 
ATOM   15164 O O   . ILE D  1 365 ? 7.582   -36.358 64.924   1.00 27.34  ? 365 ILE D O   1 
ATOM   15165 C CB  . ILE D  1 365 ? 6.436   -35.546 67.988   1.00 27.18  ? 365 ILE D CB  1 
ATOM   15166 C CG1 . ILE D  1 365 ? 5.342   -36.051 68.940   1.00 27.16  ? 365 ILE D CG1 1 
ATOM   15167 C CG2 . ILE D  1 365 ? 5.859   -34.533 67.027   1.00 21.78  ? 365 ILE D CG2 1 
ATOM   15168 C CD1 . ILE D  1 365 ? 5.016   -35.074 70.085   1.00 27.22  ? 365 ILE D CD1 1 
ATOM   15169 N N   . PRO D  1 366 ? 9.214   -35.829 66.361   1.00 25.48  ? 366 PRO D N   1 
ATOM   15170 C CA  . PRO D  1 366 ? 10.118  -35.529 65.229   1.00 26.06  ? 366 PRO D CA  1 
ATOM   15171 C C   . PRO D  1 366 ? 10.254  -36.701 64.273   1.00 31.10  ? 366 PRO D C   1 
ATOM   15172 O O   . PRO D  1 366 ? 10.094  -36.538 63.051   1.00 29.50  ? 366 PRO D O   1 
ATOM   15173 C CB  . PRO D  1 366 ? 11.440  -35.185 65.931   1.00 29.17  ? 366 PRO D CB  1 
ATOM   15174 C CG  . PRO D  1 366 ? 11.013  -34.631 67.268   1.00 27.95  ? 366 PRO D CG  1 
ATOM   15175 C CD  . PRO D  1 366 ? 9.807   -35.433 67.657   1.00 26.24  ? 366 PRO D CD  1 
ATOM   15176 N N   . PHE D  1 367 ? 10.488  -37.903 64.808   1.00 23.57  ? 367 PHE D N   1 
ATOM   15177 C CA  . PHE D  1 367 ? 10.656  -39.067 63.957   1.00 21.49  ? 367 PHE D CA  1 
ATOM   15178 C C   . PHE D  1 367 ? 9.424   -39.289 63.083   1.00 22.69  ? 367 PHE D C   1 
ATOM   15179 O O   . PHE D  1 367 ? 9.514   -39.314 61.849   1.00 25.24  ? 367 PHE D O   1 
ATOM   15180 C CB  . PHE D  1 367 ? 10.955  -40.308 64.804   1.00 18.88  ? 367 PHE D CB  1 
ATOM   15181 C CG  . PHE D  1 367 ? 10.948  -41.563 64.010   1.00 23.46  ? 367 PHE D CG  1 
ATOM   15182 C CD1 . PHE D  1 367 ? 11.976  -41.826 63.107   1.00 25.58  ? 367 PHE D CD1 1 
ATOM   15183 C CD2 . PHE D  1 367 ? 9.891   -42.453 64.106   1.00 24.58  ? 367 PHE D CD2 1 
ATOM   15184 C CE1 . PHE D  1 367 ? 11.969  -42.986 62.331   1.00 29.26  ? 367 PHE D CE1 1 
ATOM   15185 C CE2 . PHE D  1 367 ? 9.874   -43.609 63.334   1.00 30.01  ? 367 PHE D CE2 1 
ATOM   15186 C CZ  . PHE D  1 367 ? 10.920  -43.873 62.438   1.00 28.60  ? 367 PHE D CZ  1 
ATOM   15187 N N   . LEU D  1 368 ? 8.251   -39.400 63.705   1.00 21.87  ? 368 LEU D N   1 
ATOM   15188 C CA  . LEU D  1 368 ? 7.053   -39.751 62.951   1.00 21.65  ? 368 LEU D CA  1 
ATOM   15189 C C   . LEU D  1 368 ? 6.649   -38.650 61.987   1.00 23.90  ? 368 LEU D C   1 
ATOM   15190 O O   . LEU D  1 368 ? 6.197   -38.938 60.873   1.00 22.45  ? 368 LEU D O   1 
ATOM   15191 C CB  . LEU D  1 368 ? 5.903   -40.079 63.904   1.00 22.70  ? 368 LEU D CB  1 
ATOM   15192 C CG  . LEU D  1 368 ? 5.985   -41.506 64.494   1.00 22.04  ? 368 LEU D CG  1 
ATOM   15193 C CD1 . LEU D  1 368 ? 4.791   -41.795 65.436   1.00 17.97  ? 368 LEU D CD1 1 
ATOM   15194 C CD2 . LEU D  1 368 ? 6.107   -42.565 63.403   1.00 25.41  ? 368 LEU D CD2 1 
ATOM   15195 N N   . GLU D  1 369 ? 6.784   -37.382 62.398   1.00 23.24  ? 369 GLU D N   1 
ATOM   15196 C CA  . GLU D  1 369 ? 6.433   -36.284 61.506   1.00 25.71  ? 369 GLU D CA  1 
ATOM   15197 C C   . GLU D  1 369 ? 7.372   -36.233 60.307   1.00 26.39  ? 369 GLU D C   1 
ATOM   15198 O O   . GLU D  1 369 ? 6.944   -35.932 59.190   1.00 24.35  ? 369 GLU D O   1 
ATOM   15199 C CB  . GLU D  1 369 ? 6.469   -34.955 62.262   1.00 25.13  ? 369 GLU D CB  1 
ATOM   15200 C CG  . GLU D  1 369 ? 5.284   -34.723 63.167   1.00 27.12  ? 369 GLU D CG  1 
ATOM   15201 C CD  . GLU D  1 369 ? 5.275   -33.334 63.781   1.00 31.21  ? 369 GLU D CD  1 
ATOM   15202 O OE1 . GLU D  1 369 ? 6.319   -32.635 63.736   1.00 30.44  ? 369 GLU D OE1 1 
ATOM   15203 O OE2 . GLU D  1 369 ? 4.210   -32.946 64.309   1.00 30.83  ? 369 GLU D OE2 1 
ATOM   15204 N N   . LYS D  1 370 ? 8.659   -36.503 60.527   1.00 27.01  ? 370 LYS D N   1 
ATOM   15205 C CA  . LYS D  1 370 ? 9.598   -36.556 59.416   1.00 26.59  ? 370 LYS D CA  1 
ATOM   15206 C C   . LYS D  1 370 ? 9.357   -37.795 58.558   1.00 29.70  ? 370 LYS D C   1 
ATOM   15207 O O   . LYS D  1 370 ? 9.418   -37.724 57.320   1.00 28.72  ? 370 LYS D O   1 
ATOM   15208 C CB  . LYS D  1 370 ? 11.025  -36.537 59.943   1.00 28.60  ? 370 LYS D CB  1 
ATOM   15209 C CG  . LYS D  1 370 ? 12.076  -36.479 58.843   1.00 38.44  ? 370 LYS D CG  1 
ATOM   15210 C CD  . LYS D  1 370 ? 12.290  -35.051 58.362   1.00 43.82  ? 370 LYS D CD  1 
ATOM   15211 C CE  . LYS D  1 370 ? 13.005  -34.999 57.013   1.00 47.90  ? 370 LYS D CE  1 
ATOM   15212 N NZ  . LYS D  1 370 ? 12.717  -33.714 56.297   1.00 47.55  ? 370 LYS D NZ  1 
ATOM   15213 N N   . LEU D  1 371 ? 9.070   -38.937 59.191   1.00 23.60  ? 371 LEU D N   1 
ATOM   15214 C CA  . LEU D  1 371 ? 8.762   -40.139 58.424   1.00 24.18  ? 371 LEU D CA  1 
ATOM   15215 C C   . LEU D  1 371 ? 7.527   -39.924 57.559   1.00 24.72  ? 371 LEU D C   1 
ATOM   15216 O O   . LEU D  1 371 ? 7.580   -40.091 56.338   1.00 23.10  ? 371 LEU D O   1 
ATOM   15217 C CB  . LEU D  1 371 ? 8.566   -41.337 59.350   1.00 26.26  ? 371 LEU D CB  1 
ATOM   15218 C CG  . LEU D  1 371 ? 8.141   -42.655 58.687   1.00 26.31  ? 371 LEU D CG  1 
ATOM   15219 C CD1 . LEU D  1 371 ? 9.149   -43.080 57.607   1.00 24.34  ? 371 LEU D CD1 1 
ATOM   15220 C CD2 . LEU D  1 371 ? 7.993   -43.751 59.720   1.00 25.76  ? 371 LEU D CD2 1 
ATOM   15221 N N   . TYR D  1 372 ? 6.417   -39.516 58.175   1.00 19.98  ? 372 TYR D N   1 
ATOM   15222 C CA  . TYR D  1 372 ? 5.155   -39.369 57.444   1.00 22.96  ? 372 TYR D CA  1 
ATOM   15223 C C   . TYR D  1 372 ? 5.231   -38.263 56.389   1.00 25.55  ? 372 TYR D C   1 
ATOM   15224 O O   . TYR D  1 372 ? 4.674   -38.399 55.288   1.00 26.06  ? 372 TYR D O   1 
ATOM   15225 C CB  . TYR D  1 372 ? 4.021   -39.112 58.446   1.00 21.95  ? 372 TYR D CB  1 
ATOM   15226 C CG  . TYR D  1 372 ? 3.723   -40.311 59.349   1.00 23.31  ? 372 TYR D CG  1 
ATOM   15227 C CD1 . TYR D  1 372 ? 4.194   -41.594 59.033   1.00 21.46  ? 372 TYR D CD1 1 
ATOM   15228 C CD2 . TYR D  1 372 ? 2.966   -40.166 60.519   1.00 24.71  ? 372 TYR D CD2 1 
ATOM   15229 C CE1 . TYR D  1 372 ? 3.906   -42.690 59.848   1.00 22.71  ? 372 TYR D CE1 1 
ATOM   15230 C CE2 . TYR D  1 372 ? 2.679   -41.246 61.325   1.00 21.09  ? 372 TYR D CE2 1 
ATOM   15231 C CZ  . TYR D  1 372 ? 3.149   -42.498 61.001   1.00 25.44  ? 372 TYR D CZ  1 
ATOM   15232 O OH  . TYR D  1 372 ? 2.842   -43.564 61.831   1.00 22.20  ? 372 TYR D OH  1 
ATOM   15233 N N   . SER D  1 373 ? 5.926   -37.167 56.701   1.00 23.80  ? 373 SER D N   1 
ATOM   15234 C CA  . SER D  1 373 ? 6.112   -36.095 55.732   1.00 24.69  ? 373 SER D CA  1 
ATOM   15235 C C   . SER D  1 373 ? 6.933   -36.560 54.532   1.00 24.22  ? 373 SER D C   1 
ATOM   15236 O O   . SER D  1 373 ? 6.655   -36.185 53.389   1.00 24.81  ? 373 SER D O   1 
ATOM   15237 C CB  . SER D  1 373 ? 6.786   -34.901 56.411   1.00 29.51  ? 373 SER D CB  1 
ATOM   15238 O OG  . SER D  1 373 ? 7.159   -33.948 55.439   1.00 41.72  ? 373 SER D OG  1 
ATOM   15239 N N   . THR D  1 374 ? 7.941   -37.388 54.777   1.00 30.21  ? 374 THR D N   1 
ATOM   15240 C CA  . THR D  1 374 ? 8.681   -38.011 53.694   1.00 31.66  ? 374 THR D CA  1 
ATOM   15241 C C   . THR D  1 374 ? 7.804   -38.985 52.908   1.00 32.44  ? 374 THR D C   1 
ATOM   15242 O O   . THR D  1 374 ? 7.718   -38.901 51.675   1.00 30.38  ? 374 THR D O   1 
ATOM   15243 C CB  . THR D  1 374 ? 9.905   -38.705 54.270   1.00 30.27  ? 374 THR D CB  1 
ATOM   15244 O OG1 . THR D  1 374 ? 10.708  -37.720 54.936   1.00 24.25  ? 374 THR D OG1 1 
ATOM   15245 C CG2 . THR D  1 374 ? 10.722  -39.382 53.154   1.00 34.51  ? 374 THR D CG2 1 
ATOM   15246 N N   . LEU D  1 375 ? 7.128   -39.899 53.610   1.00 29.30  ? 375 LEU D N   1 
ATOM   15247 C CA  . LEU D  1 375 ? 6.320   -40.916 52.941   1.00 25.00  ? 375 LEU D CA  1 
ATOM   15248 C C   . LEU D  1 375 ? 5.258   -40.295 52.046   1.00 33.09  ? 375 LEU D C   1 
ATOM   15249 O O   . LEU D  1 375 ? 5.036   -40.770 50.921   1.00 36.87  ? 375 LEU D O   1 
ATOM   15250 C CB  . LEU D  1 375 ? 5.679   -41.838 53.982   1.00 28.74  ? 375 LEU D CB  1 
ATOM   15251 C CG  . LEU D  1 375 ? 6.680   -42.769 54.669   1.00 28.11  ? 375 LEU D CG  1 
ATOM   15252 C CD1 . LEU D  1 375 ? 5.972   -43.666 55.700   1.00 27.29  ? 375 LEU D CD1 1 
ATOM   15253 C CD2 . LEU D  1 375 ? 7.447   -43.569 53.629   1.00 24.92  ? 375 LEU D CD2 1 
ATOM   15254 N N   . GLU D  1 376 ? 4.620   -39.202 52.503   1.00 26.41  ? 376 GLU D N   1 
ATOM   15255 C CA  . GLU D  1 376 ? 3.522   -38.636 51.733   1.00 26.31  ? 376 GLU D CA  1 
ATOM   15256 C C   . GLU D  1 376 ? 3.999   -38.007 50.423   1.00 27.39  ? 376 GLU D C   1 
ATOM   15257 O O   . GLU D  1 376 ? 3.185   -37.849 49.509   1.00 27.66  ? 376 GLU D O   1 
ATOM   15258 C CB  . GLU D  1 376 ? 2.726   -37.629 52.577   1.00 26.59  ? 376 GLU D CB  1 
ATOM   15259 C CG  . GLU D  1 376 ? 3.372   -36.272 52.763   1.00 25.31  ? 376 GLU D CG  1 
ATOM   15260 C CD  . GLU D  1 376 ? 2.493   -35.269 53.499   1.00 32.81  ? 376 GLU D CD  1 
ATOM   15261 O OE1 . GLU D  1 376 ? 2.982   -34.138 53.699   1.00 32.20  ? 376 GLU D OE1 1 
ATOM   15262 O OE2 . GLU D  1 376 ? 1.337   -35.589 53.880   1.00 34.47  ? 376 GLU D OE2 1 
ATOM   15263 N N   . LYS D  1 377 ? 5.289   -37.682 50.305   1.00 23.69  ? 377 LYS D N   1 
ATOM   15264 C CA  . LYS D  1 377 ? 5.862   -37.110 49.084   1.00 29.13  ? 377 LYS D CA  1 
ATOM   15265 C C   . LYS D  1 377 ? 6.468   -38.140 48.146   1.00 31.12  ? 377 LYS D C   1 
ATOM   15266 O O   . LYS D  1 377 ? 6.536   -37.889 46.935   1.00 33.51  ? 377 LYS D O   1 
ATOM   15267 C CB  . LYS D  1 377 ? 6.953   -36.086 49.429   1.00 32.82  ? 377 LYS D CB  1 
ATOM   15268 C CG  . LYS D  1 377 ? 6.431   -34.806 50.059   1.00 39.96  ? 377 LYS D CG  1 
ATOM   15269 C CD  . LYS D  1 377 ? 7.563   -33.927 50.599   1.00 47.63  ? 377 LYS D CD  1 
ATOM   15270 C CE  . LYS D  1 377 ? 7.200   -33.316 51.961   1.00 55.04  ? 377 LYS D CE  1 
ATOM   15271 N NZ  . LYS D  1 377 ? 8.035   -33.863 53.080   1.00 57.05  ? 377 LYS D NZ  1 
ATOM   15272 N N   . GLU D  1 378 ? 6.956   -39.268 48.660   1.00 31.87  ? 378 GLU D N   1 
ATOM   15273 C CA  . GLU D  1 378 ? 7.575   -40.280 47.802   1.00 33.27  ? 378 GLU D CA  1 
ATOM   15274 C C   . GLU D  1 378 ? 6.524   -40.929 46.917   1.00 34.33  ? 378 GLU D C   1 
ATOM   15275 O O   . GLU D  1 378 ? 5.535   -41.472 47.415   1.00 36.07  ? 378 GLU D O   1 
ATOM   15276 C CB  . GLU D  1 378 ? 8.290   -41.341 48.638   1.00 29.00  ? 378 GLU D CB  1 
ATOM   15277 C CG  . GLU D  1 378 ? 9.311   -40.778 49.616   1.00 31.00  ? 378 GLU D CG  1 
ATOM   15278 C CD  . GLU D  1 378 ? 10.544  -40.227 48.922   1.00 42.89  ? 378 GLU D CD  1 
ATOM   15279 O OE1 . GLU D  1 378 ? 10.561  -40.175 47.669   1.00 45.50  ? 378 GLU D OE1 1 
ATOM   15280 O OE2 . GLU D  1 378 ? 11.496  -39.831 49.630   1.00 45.88  ? 378 GLU D OE2 1 
ATOM   15281 N N   . GLU D  1 379 ? 6.735   -40.871 45.600   1.00 31.20  ? 379 GLU D N   1 
ATOM   15282 C CA  . GLU D  1 379 ? 5.764   -41.403 44.651   1.00 29.96  ? 379 GLU D CA  1 
ATOM   15283 C C   . GLU D  1 379 ? 5.969   -42.879 44.337   1.00 31.47  ? 379 GLU D C   1 
ATOM   15284 O O   . GLU D  1 379 ? 5.014   -43.537 43.917   1.00 35.14  ? 379 GLU D O   1 
ATOM   15285 C CB  . GLU D  1 379 ? 5.800   -40.604 43.342   1.00 27.59  ? 379 GLU D CB  1 
ATOM   15286 N N   . TRP D  1 380 ? 7.176   -43.414 44.533   1.00 26.84  ? 380 TRP D N   1 
ATOM   15287 C CA  . TRP D  1 380 ? 7.437   -44.835 44.341   1.00 25.45  ? 380 TRP D CA  1 
ATOM   15288 C C   . TRP D  1 380 ? 7.026   -45.692 45.538   1.00 24.65  ? 380 TRP D C   1 
ATOM   15289 O O   . TRP D  1 380 ? 7.146   -46.925 45.466   1.00 27.78  ? 380 TRP D O   1 
ATOM   15290 C CB  . TRP D  1 380 ? 8.923   -45.047 44.044   1.00 30.97  ? 380 TRP D CB  1 
ATOM   15291 C CG  . TRP D  1 380 ? 9.788   -44.510 45.102   1.00 32.26  ? 380 TRP D CG  1 
ATOM   15292 C CD1 . TRP D  1 380 ? 10.103  -43.205 45.320   1.00 34.85  ? 380 TRP D CD1 1 
ATOM   15293 C CD2 . TRP D  1 380 ? 10.426  -45.260 46.132   1.00 36.17  ? 380 TRP D CD2 1 
ATOM   15294 N NE1 . TRP D  1 380 ? 10.916  -43.093 46.422   1.00 36.40  ? 380 TRP D NE1 1 
ATOM   15295 C CE2 . TRP D  1 380 ? 11.133  -44.345 46.937   1.00 35.75  ? 380 TRP D CE2 1 
ATOM   15296 C CE3 . TRP D  1 380 ? 10.489  -46.625 46.439   1.00 36.46  ? 380 TRP D CE3 1 
ATOM   15297 C CZ2 . TRP D  1 380 ? 11.888  -44.745 48.032   1.00 34.51  ? 380 TRP D CZ2 1 
ATOM   15298 C CZ3 . TRP D  1 380 ? 11.238  -47.021 47.525   1.00 35.94  ? 380 TRP D CZ3 1 
ATOM   15299 C CH2 . TRP D  1 380 ? 11.924  -46.086 48.312   1.00 33.70  ? 380 TRP D CH2 1 
ATOM   15300 N N   . ILE D  1 381 ? 6.562   -45.075 46.622   1.00 23.62  ? 381 ILE D N   1 
ATOM   15301 C CA  . ILE D  1 381 ? 5.995   -45.763 47.787   1.00 23.52  ? 381 ILE D CA  1 
ATOM   15302 C C   . ILE D  1 381 ? 4.512   -45.431 47.843   1.00 23.26  ? 381 ILE D C   1 
ATOM   15303 O O   . ILE D  1 381 ? 4.135   -44.256 47.886   1.00 27.76  ? 381 ILE D O   1 
ATOM   15304 C CB  . ILE D  1 381 ? 6.685   -45.330 49.094   1.00 23.48  ? 381 ILE D CB  1 
ATOM   15305 C CG1 . ILE D  1 381 ? 8.190   -45.571 49.043   1.00 31.79  ? 381 ILE D CG1 1 
ATOM   15306 C CG2 . ILE D  1 381 ? 6.045   -46.016 50.324   1.00 21.40  ? 381 ILE D CG2 1 
ATOM   15307 C CD1 . ILE D  1 381 ? 8.895   -45.188 50.349   1.00 31.28  ? 381 ILE D CD1 1 
ATOM   15308 N N   . GLU D  1 382 ? 3.668   -46.443 47.858   1.00 23.50  ? 382 GLU D N   1 
ATOM   15309 C CA  . GLU D  1 382 ? 2.244   -46.245 48.103   1.00 21.32  ? 382 GLU D CA  1 
ATOM   15310 C C   . GLU D  1 382 ? 1.915   -46.922 49.429   1.00 20.73  ? 382 GLU D C   1 
ATOM   15311 O O   . GLU D  1 382 ? 2.000   -48.152 49.531   1.00 18.84  ? 382 GLU D O   1 
ATOM   15312 C CB  . GLU D  1 382 ? 1.396   -46.829 46.982   1.00 30.39  ? 382 GLU D CB  1 
ATOM   15313 C CG  . GLU D  1 382 ? -0.089  -46.596 47.144   1.00 41.29  ? 382 GLU D CG  1 
ATOM   15314 C CD  . GLU D  1 382 ? -0.868  -46.964 45.896   1.00 56.04  ? 382 GLU D CD  1 
ATOM   15315 O OE1 . GLU D  1 382 ? -2.106  -47.126 45.992   1.00 62.08  ? 382 GLU D OE1 1 
ATOM   15316 O OE2 . GLU D  1 382 ? -0.243  -47.089 44.819   1.00 57.05  ? 382 GLU D OE2 1 
ATOM   15317 N N   . THR D  1 383 ? 1.536   -46.133 50.432   1.00 17.99  ? 383 THR D N   1 
ATOM   15318 C CA  . THR D  1 383 ? 1.020   -46.742 51.658   1.00 16.39  ? 383 THR D CA  1 
ATOM   15319 C C   . THR D  1 383 ? -0.401  -47.227 51.427   1.00 17.38  ? 383 THR D C   1 
ATOM   15320 O O   . THR D  1 383 ? -1.178  -46.605 50.699   1.00 22.01  ? 383 THR D O   1 
ATOM   15321 C CB  . THR D  1 383 ? 1.044   -45.758 52.836   1.00 20.22  ? 383 THR D CB  1 
ATOM   15322 O OG1 . THR D  1 383 ? 0.294   -44.582 52.500   1.00 20.77  ? 383 THR D OG1 1 
ATOM   15323 C CG2 . THR D  1 383 ? 2.470   -45.364 53.171   1.00 18.67  ? 383 THR D CG2 1 
ATOM   15324 N N   . LEU D  1 384 ? -0.758  -48.327 52.088   1.00 21.60  ? 384 LEU D N   1 
ATOM   15325 C CA  . LEU D  1 384 ? -2.031  -48.992 51.836   1.00 20.96  ? 384 LEU D CA  1 
ATOM   15326 C C   . LEU D  1 384 ? -2.776  -49.232 53.135   1.00 22.20  ? 384 LEU D C   1 
ATOM   15327 O O   . LEU D  1 384 ? -2.167  -49.497 54.174   1.00 23.79  ? 384 LEU D O   1 
ATOM   15328 C CB  . LEU D  1 384 ? -1.831  -50.349 51.155   1.00 18.86  ? 384 LEU D CB  1 
ATOM   15329 C CG  . LEU D  1 384 ? -1.138  -50.373 49.792   1.00 22.35  ? 384 LEU D CG  1 
ATOM   15330 C CD1 . LEU D  1 384 ? -0.922  -51.844 49.326   1.00 22.66  ? 384 LEU D CD1 1 
ATOM   15331 C CD2 . LEU D  1 384 ? -1.978  -49.589 48.780   1.00 22.89  ? 384 LEU D CD2 1 
ATOM   15332 N N   . THR D  1 385 ? -4.100  -49.185 53.055   1.00 22.35  ? 385 THR D N   1 
ATOM   15333 C CA  . THR D  1 385 ? -4.902  -49.776 54.111   1.00 19.13  ? 385 THR D CA  1 
ATOM   15334 C C   . THR D  1 385 ? -4.758  -51.297 54.062   1.00 25.22  ? 385 THR D C   1 
ATOM   15335 O O   . THR D  1 385 ? -4.165  -51.860 53.132   1.00 25.83  ? 385 THR D O   1 
ATOM   15336 C CB  . THR D  1 385 ? -6.372  -49.371 53.963   1.00 24.30  ? 385 THR D CB  1 
ATOM   15337 O OG1 . THR D  1 385 ? -6.887  -49.888 52.728   1.00 25.70  ? 385 THR D OG1 1 
ATOM   15338 C CG2 . THR D  1 385 ? -6.517  -47.841 53.968   1.00 28.10  ? 385 THR D CG2 1 
ATOM   15339 N N   . LEU D  1 386 ? -5.280  -51.972 55.103   1.00 23.45  ? 386 LEU D N   1 
ATOM   15340 C CA  . LEU D  1 386 ? -5.350  -53.436 55.083   1.00 23.15  ? 386 LEU D CA  1 
ATOM   15341 C C   . LEU D  1 386 ? -6.304  -53.918 53.999   1.00 20.65  ? 386 LEU D C   1 
ATOM   15342 O O   . LEU D  1 386 ? -6.094  -54.973 53.392   1.00 24.04  ? 386 LEU D O   1 
ATOM   15343 C CB  . LEU D  1 386 ? -5.824  -53.969 56.438   1.00 19.84  ? 386 LEU D CB  1 
ATOM   15344 C CG  . LEU D  1 386 ? -4.974  -53.616 57.655   1.00 20.40  ? 386 LEU D CG  1 
ATOM   15345 C CD1 . LEU D  1 386 ? -5.580  -54.195 58.972   1.00 16.13  ? 386 LEU D CD1 1 
ATOM   15346 C CD2 . LEU D  1 386 ? -3.537  -54.067 57.436   1.00 19.41  ? 386 LEU D CD2 1 
ATOM   15347 N N   . GLU D  1 387 ? -7.425  -53.223 53.852   1.00 24.20  ? 387 GLU D N   1 
ATOM   15348 C CA  . GLU D  1 387 ? -8.363  -53.529 52.781   1.00 24.53  ? 387 GLU D CA  1 
ATOM   15349 C C   . GLU D  1 387 ? -7.670  -53.448 51.427   1.00 23.98  ? 387 GLU D C   1 
ATOM   15350 O O   . GLU D  1 387 ? -7.817  -54.346 50.592   1.00 25.84  ? 387 GLU D O   1 
ATOM   15351 C CB  . GLU D  1 387 ? -9.545  -52.564 52.841   1.00 24.73  ? 387 GLU D CB  1 
ATOM   15352 C CG  . GLU D  1 387 ? -10.729 -52.966 51.970   1.00 41.83  ? 387 GLU D CG  1 
ATOM   15353 C CD  . GLU D  1 387 ? -11.587 -51.771 51.565   1.00 58.01  ? 387 GLU D CD  1 
ATOM   15354 O OE1 . GLU D  1 387 ? -11.155 -50.990 50.686   1.00 62.20  ? 387 GLU D OE1 1 
ATOM   15355 O OE2 . GLU D  1 387 ? -12.696 -51.613 52.119   1.00 63.67  ? 387 GLU D OE2 1 
ATOM   15356 N N   . GLU D  1 388 ? -6.871  -52.407 51.212   1.00 21.83  ? 388 GLU D N   1 
ATOM   15357 C CA  . GLU D  1 388 ? -6.184  -52.283 49.925   1.00 29.12  ? 388 GLU D CA  1 
ATOM   15358 C C   . GLU D  1 388 ? -5.137  -53.381 49.744   1.00 28.29  ? 388 GLU D C   1 
ATOM   15359 O O   . GLU D  1 388 ? -5.072  -54.013 48.687   1.00 36.95  ? 388 GLU D O   1 
ATOM   15360 C CB  . GLU D  1 388 ? -5.562  -50.899 49.795   1.00 25.34  ? 388 GLU D CB  1 
ATOM   15361 C CG  . GLU D  1 388 ? -6.607  -49.818 49.578   1.00 28.01  ? 388 GLU D CG  1 
ATOM   15362 C CD  . GLU D  1 388 ? -6.046  -48.426 49.777   1.00 33.15  ? 388 GLU D CD  1 
ATOM   15363 O OE1 . GLU D  1 388 ? -4.968  -48.300 50.395   1.00 29.99  ? 388 GLU D OE1 1 
ATOM   15364 O OE2 . GLU D  1 388 ? -6.676  -47.460 49.297   1.00 38.79  ? 388 GLU D OE2 1 
ATOM   15365 N N   . ALA D  1 389 ? -4.323  -53.633 50.777   1.00 23.89  ? 389 ALA D N   1 
ATOM   15366 C CA  . ALA D  1 389 ? -3.326  -54.699 50.711   1.00 22.23  ? 389 ALA D CA  1 
ATOM   15367 C C   . ALA D  1 389 ? -3.966  -56.064 50.452   1.00 27.47  ? 389 ALA D C   1 
ATOM   15368 O O   . ALA D  1 389 ? -3.396  -56.904 49.742   1.00 25.84  ? 389 ALA D O   1 
ATOM   15369 C CB  . ALA D  1 389 ? -2.504  -54.722 52.008   1.00 24.12  ? 389 ALA D CB  1 
ATOM   15370 N N   . MET D  1 390 ? -5.153  -56.303 51.001   1.00 29.01  ? 390 MET D N   1 
ATOM   15371 C CA  . MET D  1 390 ? -5.812  -57.578 50.749   1.00 33.34  ? 390 MET D CA  1 
ATOM   15372 C C   . MET D  1 390 ? -6.309  -57.691 49.305   1.00 30.02  ? 390 MET D C   1 
ATOM   15373 O O   . MET D  1 390 ? -6.208  -58.761 48.700   1.00 31.71  ? 390 MET D O   1 
ATOM   15374 C CB  . MET D  1 390 ? -6.968  -57.772 51.728   1.00 38.23  ? 390 MET D CB  1 
ATOM   15375 C CG  . MET D  1 390 ? -7.955  -58.798 51.237   1.00 54.19  ? 390 MET D CG  1 
ATOM   15376 S SD  . MET D  1 390 ? -9.180  -59.318 52.436   1.00 65.79  ? 390 MET D SD  1 
ATOM   15377 C CE  . MET D  1 390 ? -9.614  -60.904 51.714   1.00 70.72  ? 390 MET D CE  1 
ATOM   15378 N N   . ARG D  1 391 ? -6.841  -56.607 48.737   1.00 26.41  ? 391 ARG D N   1 
ATOM   15379 C CA  . ARG D  1 391 ? -7.508  -56.633 47.432   1.00 29.39  ? 391 ARG D CA  1 
ATOM   15380 C C   . ARG D  1 391 ? -6.584  -56.351 46.242   1.00 30.69  ? 391 ARG D C   1 
ATOM   15381 O O   . ARG D  1 391 ? -6.977  -56.600 45.097   1.00 34.81  ? 391 ARG D O   1 
ATOM   15382 C CB  . ARG D  1 391 ? -8.641  -55.603 47.411   1.00 35.47  ? 391 ARG D CB  1 
ATOM   15383 C CG  . ARG D  1 391 ? -9.673  -55.766 48.506   1.00 42.31  ? 391 ARG D CG  1 
ATOM   15384 C CD  . ARG D  1 391 ? -10.678 -56.846 48.181   1.00 51.43  ? 391 ARG D CD  1 
ATOM   15385 N NE  . ARG D  1 391 ? -11.818 -56.799 49.093   1.00 60.26  ? 391 ARG D NE  1 
ATOM   15386 C CZ  . ARG D  1 391 ? -13.092 -56.812 48.708   1.00 68.69  ? 391 ARG D CZ  1 
ATOM   15387 N NH1 . ARG D  1 391 ? -13.407 -56.878 47.419   1.00 70.88  ? 391 ARG D NH1 1 
ATOM   15388 N NH2 . ARG D  1 391 ? -14.056 -56.763 49.618   1.00 72.34  ? 391 ARG D NH2 1 
ATOM   15389 N N   . LYS D  1 392 ? -5.379  -55.838 46.475   1.00 32.02  ? 392 LYS D N   1 
ATOM   15390 C CA  . LYS D  1 392 ? -4.523  -55.381 45.380   1.00 35.09  ? 392 LYS D CA  1 
ATOM   15391 C C   . LYS D  1 392 ? -4.250  -56.504 44.380   1.00 38.02  ? 392 LYS D C   1 
ATOM   15392 O O   . LYS D  1 392 ? -3.941  -57.636 44.760   1.00 37.68  ? 392 LYS D O   1 
ATOM   15393 C CB  . LYS D  1 392 ? -3.220  -54.836 45.962   1.00 33.08  ? 392 LYS D CB  1 
ATOM   15394 C CG  . LYS D  1 392 ? -2.393  -54.011 45.029   1.00 40.10  ? 392 LYS D CG  1 
ATOM   15395 C CD  . LYS D  1 392 ? -3.085  -52.722 44.631   1.00 46.80  ? 392 LYS D CD  1 
ATOM   15396 C CE  . LYS D  1 392 ? -2.901  -51.644 45.671   1.00 46.24  ? 392 LYS D CE  1 
ATOM   15397 N NZ  . LYS D  1 392 ? -3.284  -50.326 45.096   1.00 50.51  ? 392 LYS D NZ  1 
ATOM   15398 N N   . GLU D  1 393 ? -4.386  -56.193 43.094   1.00 41.67  ? 393 GLU D N   1 
ATOM   15399 C CA  . GLU D  1 393 ? -4.239  -57.212 42.061   1.00 47.91  ? 393 GLU D CA  1 
ATOM   15400 C C   . GLU D  1 393 ? -2.803  -57.337 41.571   1.00 43.70  ? 393 GLU D C   1 
ATOM   15401 O O   . GLU D  1 393 ? -2.354  -58.444 41.259   1.00 47.51  ? 393 GLU D O   1 
ATOM   15402 C CB  . GLU D  1 393 ? -5.159  -56.905 40.877   1.00 56.83  ? 393 GLU D CB  1 
ATOM   15403 C CG  . GLU D  1 393 ? -6.591  -57.417 41.016   1.00 67.16  ? 393 GLU D CG  1 
ATOM   15404 C CD  . GLU D  1 393 ? -7.447  -57.091 39.789   1.00 77.94  ? 393 GLU D CD  1 
ATOM   15405 O OE1 . GLU D  1 393 ? -7.079  -56.168 39.028   1.00 81.11  ? 393 GLU D OE1 1 
ATOM   15406 O OE2 . GLU D  1 393 ? -8.485  -57.757 39.580   1.00 81.31  ? 393 GLU D OE2 1 
ATOM   15407 N N   . ASP D  1 394 ? -2.069  -56.232 41.501   1.00 39.85  ? 394 ASP D N   1 
ATOM   15408 C CA  . ASP D  1 394 ? -0.719  -56.243 40.934   1.00 43.35  ? 394 ASP D CA  1 
ATOM   15409 C C   . ASP D  1 394 ? 0.337   -56.560 41.990   1.00 40.39  ? 394 ASP D C   1 
ATOM   15410 O O   . ASP D  1 394 ? 1.350   -55.878 42.119   1.00 41.86  ? 394 ASP D O   1 
ATOM   15411 C CB  . ASP D  1 394 ? -0.430  -54.913 40.243   1.00 50.82  ? 394 ASP D CB  1 
ATOM   15412 C CG  . ASP D  1 394 ? -0.994  -53.725 41.002   1.00 53.49  ? 394 ASP D CG  1 
ATOM   15413 O OD1 . ASP D  1 394 ? -1.426  -53.919 42.151   1.00 53.44  ? 394 ASP D OD1 1 
ATOM   15414 O OD2 . ASP D  1 394 ? -0.997  -52.598 40.464   1.00 54.43  ? 394 ASP D OD2 1 
ATOM   15415 N N   . VAL D  1 395 ? 0.096   -57.615 42.765   1.00 38.32  ? 395 VAL D N   1 
ATOM   15416 C CA  . VAL D  1 395 ? 1.050   -58.110 43.747   1.00 39.48  ? 395 VAL D CA  1 
ATOM   15417 C C   . VAL D  1 395 ? 1.292   -59.586 43.461   1.00 35.44  ? 395 VAL D C   1 
ATOM   15418 O O   . VAL D  1 395 ? 0.485   -60.255 42.815   1.00 37.87  ? 395 VAL D O   1 
ATOM   15419 C CB  . VAL D  1 395 ? 0.557   -57.907 45.200   1.00 38.16  ? 395 VAL D CB  1 
ATOM   15420 C CG1 . VAL D  1 395 ? 0.382   -56.438 45.486   1.00 41.01  ? 395 VAL D CG1 1 
ATOM   15421 C CG2 . VAL D  1 395 ? -0.752  -58.638 45.418   1.00 37.59  ? 395 VAL D CG2 1 
ATOM   15422 N N   . LYS D  1 396 ? 2.423   -60.091 43.943   1.00 33.16  ? 396 LYS D N   1 
ATOM   15423 C CA  . LYS D  1 396 ? 2.745   -61.505 43.801   1.00 28.07  ? 396 LYS D CA  1 
ATOM   15424 C C   . LYS D  1 396 ? 2.181   -62.303 44.967   1.00 29.99  ? 396 LYS D C   1 
ATOM   15425 O O   . LYS D  1 396 ? 2.238   -61.870 46.125   1.00 23.89  ? 396 LYS D O   1 
ATOM   15426 C CB  . LYS D  1 396 ? 4.252   -61.733 43.710   1.00 35.73  ? 396 LYS D CB  1 
ATOM   15427 C CG  . LYS D  1 396 ? 4.606   -63.115 43.199   1.00 46.73  ? 396 LYS D CG  1 
ATOM   15428 C CD  . LYS D  1 396 ? 5.950   -63.590 43.713   1.00 47.08  ? 396 LYS D CD  1 
ATOM   15429 C CE  . LYS D  1 396 ? 7.082   -62.864 43.010   1.00 45.57  ? 396 LYS D CE  1 
ATOM   15430 N NZ  . LYS D  1 396 ? 7.011   -62.933 41.532   1.00 47.46  ? 396 LYS D NZ  1 
ATOM   15431 N N   . THR D  1 397 ? 1.715   -63.509 44.644   1.00 35.91  ? 397 THR D N   1 
ATOM   15432 C CA  . THR D  1 397 ? 0.873   -64.337 45.488   1.00 39.16  ? 397 THR D CA  1 
ATOM   15433 C C   . THR D  1 397 ? 1.485   -65.727 45.583   1.00 36.28  ? 397 THR D C   1 
ATOM   15434 O O   . THR D  1 397 ? 2.184   -66.171 44.671   1.00 35.27  ? 397 THR D O   1 
ATOM   15435 C CB  . THR D  1 397 ? -0.549  -64.369 44.886   1.00 44.90  ? 397 THR D CB  1 
ATOM   15436 O OG1 . THR D  1 397 ? -1.259  -63.185 45.282   1.00 47.14  ? 397 THR D OG1 1 
ATOM   15437 C CG2 . THR D  1 397 ? -1.315  -65.594 45.272   1.00 47.57  ? 397 THR D CG2 1 
ATOM   15438 N N   . GLU D  1 398 ? 1.249   -66.405 46.704   1.00 32.78  ? 398 GLU D N   1 
ATOM   15439 C CA  . GLU D  1 398 ? 1.759   -67.756 46.881   1.00 30.18  ? 398 GLU D CA  1 
ATOM   15440 C C   . GLU D  1 398 ? 0.842   -68.492 47.841   1.00 30.95  ? 398 GLU D C   1 
ATOM   15441 O O   . GLU D  1 398 ? 0.391   -67.911 48.830   1.00 27.16  ? 398 GLU D O   1 
ATOM   15442 C CB  . GLU D  1 398 ? 3.193   -67.750 47.432   1.00 38.23  ? 398 GLU D CB  1 
ATOM   15443 C CG  . GLU D  1 398 ? 3.983   -69.046 47.173   1.00 54.37  ? 398 GLU D CG  1 
ATOM   15444 C CD  . GLU D  1 398 ? 5.333   -69.108 47.909   1.00 64.14  ? 398 GLU D CD  1 
ATOM   15445 O OE1 . GLU D  1 398 ? 5.711   -70.206 48.379   1.00 66.62  ? 398 GLU D OE1 1 
ATOM   15446 O OE2 . GLU D  1 398 ? 6.019   -68.068 48.017   1.00 66.52  ? 398 GLU D OE2 1 
ATOM   15447 N N   . VAL D  1 399 ? 0.599   -69.775 47.567   1.00 29.76  ? 399 VAL D N   1 
ATOM   15448 C CA  . VAL D  1 399 ? -0.128  -70.629 48.497   1.00 34.30  ? 399 VAL D CA  1 
ATOM   15449 C C   . VAL D  1 399 ? 0.849   -71.205 49.514   1.00 34.92  ? 399 VAL D C   1 
ATOM   15450 O O   . VAL D  1 399 ? 1.978   -71.573 49.175   1.00 34.87  ? 399 VAL D O   1 
ATOM   15451 C CB  . VAL D  1 399 ? -0.879  -71.740 47.744   1.00 33.32  ? 399 VAL D CB  1 
ATOM   15452 C CG1 . VAL D  1 399 ? -1.494  -72.741 48.723   1.00 33.02  ? 399 VAL D CG1 1 
ATOM   15453 C CG2 . VAL D  1 399 ? -1.946  -71.128 46.905   1.00 31.82  ? 399 VAL D CG2 1 
ATOM   15454 N N   . ILE D  1 400 ? 0.421   -71.257 50.773   1.00 32.47  ? 400 ILE D N   1 
ATOM   15455 C CA  . ILE D  1 400 ? 1.166   -71.888 51.860   1.00 31.32  ? 400 ILE D CA  1 
ATOM   15456 C C   . ILE D  1 400 ? 0.255   -72.952 52.472   1.00 27.21  ? 400 ILE D C   1 
ATOM   15457 O O   . ILE D  1 400 ? -0.933  -72.701 52.694   1.00 28.87  ? 400 ILE D O   1 
ATOM   15458 C CB  . ILE D  1 400 ? 1.630   -70.842 52.898   1.00 34.22  ? 400 ILE D CB  1 
ATOM   15459 C CG1 . ILE D  1 400 ? 2.361   -71.484 54.076   1.00 32.45  ? 400 ILE D CG1 1 
ATOM   15460 C CG2 . ILE D  1 400 ? 0.466   -70.029 53.442   1.00 35.65  ? 400 ILE D CG2 1 
ATOM   15461 C CD1 . ILE D  1 400 ? 3.181   -70.481 54.858   1.00 28.47  ? 400 ILE D CD1 1 
ATOM   15462 N N   . GLU D  1 401 ? 0.781   -74.160 52.680   1.00 27.75  ? 401 GLU D N   1 
ATOM   15463 C CA  . GLU D  1 401 ? -0.075  -75.245 53.145   1.00 28.23  ? 401 GLU D CA  1 
ATOM   15464 C C   . GLU D  1 401 ? -0.007  -75.483 54.652   1.00 26.60  ? 401 GLU D C   1 
ATOM   15465 O O   . GLU D  1 401 ? -0.961  -76.027 55.224   1.00 30.58  ? 401 GLU D O   1 
ATOM   15466 C CB  . GLU D  1 401 ? 0.261   -76.552 52.416   1.00 35.78  ? 401 GLU D CB  1 
ATOM   15467 C CG  . GLU D  1 401 ? 0.313   -76.422 50.894   1.00 47.52  ? 401 GLU D CG  1 
ATOM   15468 C CD  . GLU D  1 401 ? -1.051  -76.149 50.244   1.00 56.75  ? 401 GLU D CD  1 
ATOM   15469 O OE1 . GLU D  1 401 ? -1.075  -75.939 49.011   1.00 62.00  ? 401 GLU D OE1 1 
ATOM   15470 O OE2 . GLU D  1 401 ? -2.091  -76.150 50.945   1.00 59.48  ? 401 GLU D OE2 1 
ATOM   15471 N N   . SER D  1 402 ? 1.064   -75.062 55.310   1.00 23.91  ? 402 SER D N   1 
ATOM   15472 C CA  . SER D  1 402 ? 1.250   -75.388 56.718   1.00 26.23  ? 402 SER D CA  1 
ATOM   15473 C C   . SER D  1 402 ? 2.183   -74.354 57.331   1.00 26.16  ? 402 SER D C   1 
ATOM   15474 O O   . SER D  1 402 ? 3.004   -73.750 56.632   1.00 26.51  ? 402 SER D O   1 
ATOM   15475 C CB  . SER D  1 402 ? 1.816   -76.812 56.871   1.00 28.78  ? 402 SER D CB  1 
ATOM   15476 O OG  . SER D  1 402 ? 2.246   -77.061 58.203   1.00 35.28  ? 402 SER D OG  1 
ATOM   15477 N N   . VAL D  1 403 ? 2.037   -74.188 58.623   1.00 25.72  ? 403 VAL D N   1 
ATOM   15478 C CA  . VAL D  1 403 ? 2.924   -73.344 59.376   1.00 29.57  ? 403 VAL D CA  1 
ATOM   15479 C C   . VAL D  1 403 ? 3.364   -74.039 60.662   1.00 27.92  ? 403 VAL D C   1 
ATOM   15480 O O   . VAL D  1 403 ? 2.655   -74.854 61.154   1.00 28.74  ? 403 VAL D O   1 
ATOM   15481 C CB  . VAL D  1 403 ? 2.333   -71.933 59.723   1.00 23.37  ? 403 VAL D CB  1 
ATOM   15482 C CG1 . VAL D  1 403 ? 1.946   -71.183 58.470   1.00 20.12  ? 403 VAL D CG1 1 
ATOM   15483 C CG2 . VAL D  1 403 ? 1.194   -72.026 60.705   1.00 22.24  ? 403 VAL D CG2 1 
ATOM   15484 N N   . LYS D  1 404 ? 4.557   -73.732 61.123   1.00 30.16  ? 404 LYS D N   1 
ATOM   15485 C CA  . LYS D  1 404 ? 5.007   -74.232 62.420   1.00 32.59  ? 404 LYS D CA  1 
ATOM   15486 C C   . LYS D  1 404 ? 4.580   -73.234 63.484   1.00 30.84  ? 404 LYS D C   1 
ATOM   15487 O O   . LYS D  1 404 ? 4.955   -72.061 63.419   1.00 31.10  ? 404 LYS D O   1 
ATOM   15488 C CB  . LYS D  1 404 ? 6.522   -74.436 62.435   1.00 34.93  ? 404 LYS D CB  1 
ATOM   15489 C CG  . LYS D  1 404 ? 6.958   -75.712 61.731   1.00 44.63  ? 404 LYS D CG  1 
ATOM   15490 C CD  . LYS D  1 404 ? 8.211   -76.305 62.361   1.00 47.67  ? 404 LYS D CD  1 
ATOM   15491 C CE  . LYS D  1 404 ? 8.793   -77.394 61.487   1.00 49.20  ? 404 LYS D CE  1 
ATOM   15492 N NZ  . LYS D  1 404 ? 10.272  -77.411 61.600   1.00 53.57  ? 404 LYS D NZ  1 
ATOM   15493 N N   . ALA D  1 405 ? 3.786   -73.697 64.448   1.00 30.60  ? 405 ALA D N   1 
ATOM   15494 C CA  . ALA D  1 405 ? 3.181   -72.800 65.423   1.00 27.48  ? 405 ALA D CA  1 
ATOM   15495 C C   . ALA D  1 405 ? 4.239   -72.032 66.204   1.00 26.97  ? 405 ALA D C   1 
ATOM   15496 O O   . ALA D  1 405 ? 5.307   -72.554 66.526   1.00 27.22  ? 405 ALA D O   1 
ATOM   15497 C CB  . ALA D  1 405 ? 2.286   -73.583 66.386   1.00 24.33  ? 405 ALA D CB  1 
ATOM   15498 N N   . GLY D  1 406 ? 3.928   -70.779 66.516   1.00 28.57  ? 406 GLY D N   1 
ATOM   15499 C CA  . GLY D  1 406 ? 4.888   -69.944 67.206   1.00 25.33  ? 406 GLY D CA  1 
ATOM   15500 C C   . GLY D  1 406 ? 4.340   -68.551 67.414   1.00 23.70  ? 406 GLY D C   1 
ATOM   15501 O O   . GLY D  1 406 ? 3.145   -68.302 67.247   1.00 23.22  ? 406 GLY D O   1 
ATOM   15502 N N   . THR D  1 407 ? 5.246   -67.645 67.797   1.00 23.85  ? 407 THR D N   1 
ATOM   15503 C CA  . THR D  1 407 ? 4.937   -66.243 68.075   1.00 24.69  ? 407 THR D CA  1 
ATOM   15504 C C   . THR D  1 407 ? 6.001   -65.379 67.416   1.00 17.93  ? 407 THR D C   1 
ATOM   15505 O O   . THR D  1 407 ? 6.957   -65.884 66.841   1.00 24.60  ? 407 THR D O   1 
ATOM   15506 C CB  . THR D  1 407 ? 4.906   -65.946 69.586   1.00 21.69  ? 407 THR D CB  1 
ATOM   15507 O OG1 . THR D  1 407 ? 6.230   -66.056 70.110   1.00 24.10  ? 407 THR D OG1 1 
ATOM   15508 C CG2 . THR D  1 407 ? 3.999   -66.909 70.324   1.00 18.51  ? 407 THR D CG2 1 
ATOM   15509 N N   . TRP D  1 408 ? 5.877   -64.061 67.546   1.00 25.18  ? 408 TRP D N   1 
ATOM   15510 C CA  . TRP D  1 408 ? 6.960   -63.224 67.048   1.00 25.22  ? 408 TRP D CA  1 
ATOM   15511 C C   . TRP D  1 408 ? 8.129   -63.149 68.019   1.00 24.81  ? 408 TRP D C   1 
ATOM   15512 O O   . TRP D  1 408 ? 9.117   -62.461 67.738   1.00 23.54  ? 408 TRP D O   1 
ATOM   15513 C CB  . TRP D  1 408 ? 6.465   -61.813 66.704   1.00 24.51  ? 408 TRP D CB  1 
ATOM   15514 C CG  . TRP D  1 408 ? 5.738   -61.039 67.787   1.00 26.96  ? 408 TRP D CG  1 
ATOM   15515 C CD1 . TRP D  1 408 ? 5.506   -61.419 69.094   1.00 30.01  ? 408 TRP D CD1 1 
ATOM   15516 C CD2 . TRP D  1 408 ? 5.144   -59.741 67.640   1.00 28.72  ? 408 TRP D CD2 1 
ATOM   15517 N NE1 . TRP D  1 408 ? 4.805   -60.435 69.753   1.00 26.22  ? 408 TRP D NE1 1 
ATOM   15518 C CE2 . TRP D  1 408 ? 4.573   -59.394 68.888   1.00 26.01  ? 408 TRP D CE2 1 
ATOM   15519 C CE3 . TRP D  1 408 ? 5.038   -58.835 66.570   1.00 29.84  ? 408 TRP D CE3 1 
ATOM   15520 C CZ2 . TRP D  1 408 ? 3.902   -58.180 69.098   1.00 24.75  ? 408 TRP D CZ2 1 
ATOM   15521 C CZ3 . TRP D  1 408 ? 4.375   -57.629 66.781   1.00 27.93  ? 408 TRP D CZ3 1 
ATOM   15522 C CH2 . TRP D  1 408 ? 3.816   -57.315 68.044   1.00 26.61  ? 408 TRP D CH2 1 
ATOM   15523 N N   . PHE D  1 409 ? 8.041   -63.888 69.119   1.00 20.99  ? 409 PHE D N   1 
ATOM   15524 C CA  . PHE D  1 409 ? 9.181   -63.981 69.996   1.00 29.70  ? 409 PHE D CA  1 
ATOM   15525 C C   . PHE D  1 409 ? 9.956   -65.282 69.705   1.00 31.57  ? 409 PHE D C   1 
ATOM   15526 O O   . PHE D  1 409 ? 9.572   -66.330 70.133   1.00 30.43  ? 409 PHE D O   1 
ATOM   15527 C CB  . PHE D  1 409 ? 8.826   -63.827 71.434   1.00 39.99  ? 409 PHE D CB  1 
ATOM   15528 C CG  . PHE D  1 409 ? 10.000  -63.669 72.331   1.00 57.28  ? 409 PHE D CG  1 
ATOM   15529 C CD1 . PHE D  1 409 ? 10.867  -64.716 72.545   1.00 74.09  ? 409 PHE D CD1 1 
ATOM   15530 C CD2 . PHE D  1 409 ? 10.222  -62.483 72.973   1.00 62.31  ? 409 PHE D CD2 1 
ATOM   15531 C CE1 . PHE D  1 409 ? 11.949  -64.568 73.374   1.00 79.69  ? 409 PHE D CE1 1 
ATOM   15532 C CE2 . PHE D  1 409 ? 11.301  -62.324 73.808   1.00 69.58  ? 409 PHE D CE2 1 
ATOM   15533 C CZ  . PHE D  1 409 ? 12.169  -63.369 74.007   1.00 75.13  ? 409 PHE D CZ  1 
ATOM   15534 N N   . ASP D  1 410 ? 10.975  -65.153 68.873   1.00 32.44  ? 410 ASP D N   1 
ATOM   15535 C CA  . ASP D  1 410 ? 11.820  -66.288 68.500   1.00 36.84  ? 410 ASP D CA  1 
ATOM   15536 C C   . ASP D  1 410 ? 11.064  -67.398 67.764   1.00 36.83  ? 410 ASP D C   1 
ATOM   15537 O O   . ASP D  1 410 ? 11.624  -68.473 67.523   1.00 41.94  ? 410 ASP D O   1 
ATOM   15538 C CB  . ASP D  1 410 ? 12.549  -66.870 69.724   1.00 42.78  ? 410 ASP D CB  1 
ATOM   15539 C CG  . ASP D  1 410 ? 13.567  -65.907 70.311   1.00 53.72  ? 410 ASP D CG  1 
ATOM   15540 O OD1 . ASP D  1 410 ? 13.893  -64.899 69.642   1.00 58.68  ? 410 ASP D OD1 1 
ATOM   15541 O OD2 . ASP D  1 410 ? 14.067  -66.168 71.428   1.00 57.33  ? 410 ASP D OD2 1 
ATOM   15542 N N   . GLY D  1 411 ? 9.808   -67.172 67.391   1.00 33.33  ? 411 GLY D N   1 
ATOM   15543 C CA  . GLY D  1 411 ? 9.055   -68.200 66.703   1.00 34.29  ? 411 GLY D CA  1 
ATOM   15544 C C   . GLY D  1 411 ? 8.571   -69.343 67.573   1.00 37.55  ? 411 GLY D C   1 
ATOM   15545 O O   . GLY D  1 411 ? 8.250   -70.418 67.053   1.00 32.97  ? 411 GLY D O   1 
ATOM   15546 N N   . ASN D  1 412 ? 8.512   -69.155 68.886   1.00 36.64  ? 412 ASN D N   1 
ATOM   15547 C CA  . ASN D  1 412 ? 8.049   -70.223 69.765   1.00 32.01  ? 412 ASN D CA  1 
ATOM   15548 C C   . ASN D  1 412 ? 7.329   -69.587 70.955   1.00 27.14  ? 412 ASN D C   1 
ATOM   15549 O O   . ASN D  1 412 ? 7.091   -68.375 70.977   1.00 24.82  ? 412 ASN D O   1 
ATOM   15550 C CB  . ASN D  1 412 ? 9.230   -71.138 70.138   1.00 30.71  ? 412 ASN D CB  1 
ATOM   15551 C CG  . ASN D  1 412 ? 10.326  -70.418 70.904   1.00 32.98  ? 412 ASN D CG  1 
ATOM   15552 O OD1 . ASN D  1 412 ? 10.058  -69.786 71.918   1.00 36.88  ? 412 ASN D OD1 1 
ATOM   15553 N ND2 . ASN D  1 412 ? 11.573  -70.559 70.458   1.00 35.91  ? 412 ASN D ND2 1 
ATOM   15554 N N   . PHE D  1 413 ? 6.985   -70.406 71.957   1.00 31.06  ? 413 PHE D N   1 
ATOM   15555 C CA  . PHE D  1 413 ? 6.078   -70.009 73.034   1.00 28.41  ? 413 PHE D CA  1 
ATOM   15556 C C   . PHE D  1 413 ? 6.772   -69.860 74.389   1.00 28.90  ? 413 PHE D C   1 
ATOM   15557 O O   . PHE D  1 413 ? 6.093   -69.768 75.420   1.00 25.81  ? 413 PHE D O   1 
ATOM   15558 C CB  . PHE D  1 413 ? 4.922   -71.018 73.143   1.00 27.65  ? 413 PHE D CB  1 
ATOM   15559 C CG  . PHE D  1 413 ? 4.008   -71.036 71.929   1.00 29.83  ? 413 PHE D CG  1 
ATOM   15560 C CD1 . PHE D  1 413 ? 2.953   -70.129 71.819   1.00 28.45  ? 413 PHE D CD1 1 
ATOM   15561 C CD2 . PHE D  1 413 ? 4.205   -71.950 70.905   1.00 31.12  ? 413 PHE D CD2 1 
ATOM   15562 C CE1 . PHE D  1 413 ? 2.111   -70.138 70.705   1.00 29.43  ? 413 PHE D CE1 1 
ATOM   15563 C CE2 . PHE D  1 413 ? 3.367   -71.966 69.783   1.00 32.28  ? 413 PHE D CE2 1 
ATOM   15564 C CZ  . PHE D  1 413 ? 2.323   -71.052 69.682   1.00 31.13  ? 413 PHE D CZ  1 
ATOM   15565 N N   . LEU D  1 414 ? 8.105   -69.808 74.416   1.00 29.32  ? 414 LEU D N   1 
ATOM   15566 C CA  . LEU D  1 414 ? 8.826   -69.928 75.678   1.00 31.31  ? 414 LEU D CA  1 
ATOM   15567 C C   . LEU D  1 414 ? 8.698   -68.710 76.589   1.00 36.62  ? 414 LEU D C   1 
ATOM   15568 O O   . LEU D  1 414 ? 9.070   -68.813 77.762   1.00 36.76  ? 414 LEU D O   1 
ATOM   15569 C CB  . LEU D  1 414 ? 10.306  -70.223 75.419   1.00 32.32  ? 414 LEU D CB  1 
ATOM   15570 C CG  . LEU D  1 414 ? 10.612  -71.586 74.792   1.00 34.09  ? 414 LEU D CG  1 
ATOM   15571 C CD1 . LEU D  1 414 ? 12.101  -71.822 74.711   1.00 37.76  ? 414 LEU D CD1 1 
ATOM   15572 C CD2 . LEU D  1 414 ? 9.927   -72.708 75.562   1.00 31.44  ? 414 LEU D CD2 1 
ATOM   15573 N N   . LYS D  1 415 ? 8.195   -67.571 76.102   1.00 32.28  ? 415 LYS D N   1 
ATOM   15574 C CA  . LYS D  1 415 ? 7.973   -66.425 76.980   1.00 34.10  ? 415 LYS D CA  1 
ATOM   15575 C C   . LYS D  1 415 ? 6.655   -66.474 77.744   1.00 28.62  ? 415 LYS D C   1 
ATOM   15576 O O   . LYS D  1 415 ? 6.410   -65.575 78.554   1.00 34.11  ? 415 LYS D O   1 
ATOM   15577 C CB  . LYS D  1 415 ? 8.006   -65.116 76.201   1.00 38.63  ? 415 LYS D CB  1 
ATOM   15578 C CG  . LYS D  1 415 ? 9.378   -64.695 75.786   1.00 44.51  ? 415 LYS D CG  1 
ATOM   15579 C CD  . LYS D  1 415 ? 10.383  -64.702 76.937   1.00 51.33  ? 415 LYS D CD  1 
ATOM   15580 C CE  . LYS D  1 415 ? 10.321  -63.417 77.740   1.00 55.32  ? 415 LYS D CE  1 
ATOM   15581 N NZ  . LYS D  1 415 ? 11.187  -63.464 78.944   1.00 57.78  ? 415 LYS D NZ  1 
ATOM   15582 N N   . TRP D  1 416 ? 5.797   -67.460 77.481   1.00 23.54  ? 416 TRP D N   1 
ATOM   15583 C CA  . TRP D  1 416 ? 4.533   -67.608 78.189   1.00 27.28  ? 416 TRP D CA  1 
ATOM   15584 C C   . TRP D  1 416 ? 4.335   -68.979 78.811   1.00 30.91  ? 416 TRP D C   1 
ATOM   15585 O O   . TRP D  1 416 ? 3.424   -69.137 79.632   1.00 30.31  ? 416 TRP D O   1 
ATOM   15586 C CB  . TRP D  1 416 ? 3.358   -67.326 77.238   1.00 29.64  ? 416 TRP D CB  1 
ATOM   15587 C CG  . TRP D  1 416 ? 3.489   -65.990 76.601   1.00 27.88  ? 416 TRP D CG  1 
ATOM   15588 C CD1 . TRP D  1 416 ? 3.018   -64.809 77.083   1.00 29.29  ? 416 TRP D CD1 1 
ATOM   15589 C CD2 . TRP D  1 416 ? 4.178   -65.684 75.381   1.00 27.20  ? 416 TRP D CD2 1 
ATOM   15590 N NE1 . TRP D  1 416 ? 3.353   -63.784 76.237   1.00 26.56  ? 416 TRP D NE1 1 
ATOM   15591 C CE2 . TRP D  1 416 ? 4.065   -64.291 75.182   1.00 25.43  ? 416 TRP D CE2 1 
ATOM   15592 C CE3 . TRP D  1 416 ? 4.866   -66.455 74.429   1.00 19.93  ? 416 TRP D CE3 1 
ATOM   15593 C CZ2 . TRP D  1 416 ? 4.614   -63.646 74.077   1.00 22.84  ? 416 TRP D CZ2 1 
ATOM   15594 C CZ3 . TRP D  1 416 ? 5.420   -65.809 73.324   1.00 21.76  ? 416 TRP D CZ3 1 
ATOM   15595 C CH2 . TRP D  1 416 ? 5.281   -64.411 73.162   1.00 24.98  ? 416 TRP D CH2 1 
ATOM   15596 N N   . ILE D  1 417 ? 5.145   -69.973 78.447   1.00 28.28  ? 417 ILE D N   1 
ATOM   15597 C CA  . ILE D  1 417 ? 4.979   -71.327 78.952   1.00 34.89  ? 417 ILE D CA  1 
ATOM   15598 C C   . ILE D  1 417 ? 6.326   -72.020 78.827   1.00 33.35  ? 417 ILE D C   1 
ATOM   15599 O O   . ILE D  1 417 ? 7.159   -71.638 78.001   1.00 33.99  ? 417 ILE D O   1 
ATOM   15600 C CB  . ILE D  1 417 ? 3.855   -72.054 78.169   1.00 35.23  ? 417 ILE D CB  1 
ATOM   15601 C CG1 . ILE D  1 417 ? 3.447   -73.366 78.851   1.00 33.34  ? 417 ILE D CG1 1 
ATOM   15602 C CG2 . ILE D  1 417 ? 4.245   -72.224 76.690   1.00 33.04  ? 417 ILE D CG2 1 
ATOM   15603 C CD1 . ILE D  1 417 ? 2.093   -73.863 78.384   1.00 30.43  ? 417 ILE D CD1 1 
ATOM   15604 N N   . GLY D  1 418 ? 6.558   -73.017 79.672   1.00 31.71  ? 418 GLY D N   1 
ATOM   15605 C CA  . GLY D  1 418 ? 7.743   -73.844 79.574   1.00 36.56  ? 418 GLY D CA  1 
ATOM   15606 C C   . GLY D  1 418 ? 8.692   -73.793 80.754   1.00 43.39  ? 418 GLY D C   1 
ATOM   15607 O O   . GLY D  1 418 ? 9.523   -74.702 80.889   1.00 52.94  ? 418 GLY D O   1 
ATOM   15608 N N   . ASN D  1 419 ? 8.637   -72.775 81.607   1.00 45.75  ? 419 ASN D N   1 
ATOM   15609 C CA  . ASN D  1 419 ? 9.445   -72.804 82.826   1.00 47.34  ? 419 ASN D CA  1 
ATOM   15610 C C   . ASN D  1 419 ? 8.545   -73.004 84.046   1.00 47.19  ? 419 ASN D C   1 
ATOM   15611 O O   . ASN D  1 419 ? 7.317   -73.021 83.949   1.00 47.03  ? 419 ASN D O   1 
ATOM   15612 C CB  . ASN D  1 419 ? 10.331  -71.545 82.951   1.00 48.21  ? 419 ASN D CB  1 
ATOM   15613 C CG  . ASN D  1 419 ? 9.559   -70.266 83.312   1.00 47.10  ? 419 ASN D CG  1 
ATOM   15614 O OD1 . ASN D  1 419 ? 8.403   -70.301 83.736   1.00 44.28  ? 419 ASN D OD1 1 
ATOM   15615 N ND2 . ASN D  1 419 ? 10.236  -69.123 83.177   1.00 46.47  ? 419 ASN D ND2 1 
ATOM   15616 N N   . LYS D  1 420 ? 9.167   -73.154 85.216   1.00 48.69  ? 420 LYS D N   1 
ATOM   15617 C CA  . LYS D  1 420 ? 8.400   -73.552 86.393   1.00 50.87  ? 420 LYS D CA  1 
ATOM   15618 C C   . LYS D  1 420 ? 7.370   -72.497 86.777   1.00 45.43  ? 420 LYS D C   1 
ATOM   15619 O O   . LYS D  1 420 ? 6.212   -72.825 87.059   1.00 42.29  ? 420 LYS D O   1 
ATOM   15620 C CB  . LYS D  1 420 ? 9.332   -73.838 87.570   1.00 59.17  ? 420 LYS D CB  1 
ATOM   15621 C CG  . LYS D  1 420 ? 8.596   -74.308 88.815   1.00 66.38  ? 420 LYS D CG  1 
ATOM   15622 C CD  . LYS D  1 420 ? 7.721   -75.532 88.531   1.00 70.70  ? 420 LYS D CD  1 
ATOM   15623 C CE  . LYS D  1 420 ? 7.267   -76.217 89.829   1.00 74.39  ? 420 LYS D CE  1 
ATOM   15624 N NZ  . LYS D  1 420 ? 6.563   -77.514 89.584   1.00 73.71  ? 420 LYS D NZ  1 
ATOM   15625 N N   . GLU D  1 421 ? 7.778   -71.222 86.809   1.00 48.47  ? 421 GLU D N   1 
ATOM   15626 C CA  . GLU D  1 421 ? 6.861   -70.163 87.229   1.00 54.25  ? 421 GLU D CA  1 
ATOM   15627 C C   . GLU D  1 421 ? 5.752   -69.941 86.203   1.00 50.33  ? 421 GLU D C   1 
ATOM   15628 O O   . GLU D  1 421 ? 4.574   -69.825 86.564   1.00 52.07  ? 421 GLU D O   1 
ATOM   15629 C CB  . GLU D  1 421 ? 7.631   -68.862 87.491   1.00 60.12  ? 421 GLU D CB  1 
ATOM   15630 C CG  . GLU D  1 421 ? 8.930   -69.034 88.277   1.00 68.89  ? 421 GLU D CG  1 
ATOM   15631 C CD  . GLU D  1 421 ? 8.708   -69.254 89.763   1.00 78.58  ? 421 GLU D CD  1 
ATOM   15632 O OE1 . GLU D  1 421 ? 9.469   -68.672 90.569   1.00 83.96  ? 421 GLU D OE1 1 
ATOM   15633 O OE2 . GLU D  1 421 ? 7.784   -70.012 90.132   1.00 81.13  ? 421 GLU D OE2 1 
ATOM   15634 N N   . LYS D  1 422 ? 6.100   -69.873 84.918   1.00 45.82  ? 422 LYS D N   1 
ATOM   15635 C CA  . LYS D  1 422 ? 5.063   -69.686 83.905   1.00 42.22  ? 422 LYS D CA  1 
ATOM   15636 C C   . LYS D  1 422 ? 4.116   -70.880 83.858   1.00 38.51  ? 422 LYS D C   1 
ATOM   15637 O O   . LYS D  1 422 ? 2.894   -70.706 83.738   1.00 35.03  ? 422 LYS D O   1 
ATOM   15638 C CB  . LYS D  1 422 ? 5.697   -69.431 82.540   1.00 37.38  ? 422 LYS D CB  1 
ATOM   15639 C CG  . LYS D  1 422 ? 6.331   -68.050 82.437   1.00 36.90  ? 422 LYS D CG  1 
ATOM   15640 C CD  . LYS D  1 422 ? 7.023   -67.829 81.105   1.00 31.14  ? 422 LYS D CD  1 
ATOM   15641 C CE  . LYS D  1 422 ? 7.969   -66.635 81.166   1.00 32.45  ? 422 LYS D CE  1 
ATOM   15642 N NZ  . LYS D  1 422 ? 7.277   -65.325 81.365   1.00 29.74  ? 422 LYS D NZ  1 
ATOM   15643 N N   . ASN D  1 423 ? 4.657   -72.098 83.981   1.00 32.77  ? 423 ASN D N   1 
ATOM   15644 C CA  . ASN D  1 423 ? 3.804   -73.281 84.026   1.00 35.28  ? 423 ASN D CA  1 
ATOM   15645 C C   . ASN D  1 423 ? 2.873   -73.238 85.226   1.00 34.83  ? 423 ASN D C   1 
ATOM   15646 O O   . ASN D  1 423 ? 1.760   -73.768 85.165   1.00 30.52  ? 423 ASN D O   1 
ATOM   15647 C CB  . ASN D  1 423 ? 4.651   -74.567 84.071   1.00 35.92  ? 423 ASN D CB  1 
ATOM   15648 C CG  . ASN D  1 423 ? 5.145   -75.007 82.684   1.00 34.36  ? 423 ASN D CG  1 
ATOM   15649 O OD1 . ASN D  1 423 ? 4.778   -74.423 81.663   1.00 33.20  ? 423 ASN D OD1 1 
ATOM   15650 N ND2 . ASN D  1 423 ? 5.964   -76.061 82.654   1.00 32.92  ? 423 ASN D ND2 1 
ATOM   15651 N N   . GLU D  1 424 ? 3.320   -72.625 86.328   1.00 40.52  ? 424 GLU D N   1 
ATOM   15652 C CA  . GLU D  1 424 ? 2.454   -72.473 87.495   1.00 45.24  ? 424 GLU D CA  1 
ATOM   15653 C C   . GLU D  1 424 ? 1.180   -71.722 87.135   1.00 37.40  ? 424 GLU D C   1 
ATOM   15654 O O   . GLU D  1 424 ? 0.092   -72.080 87.599   1.00 35.70  ? 424 GLU D O   1 
ATOM   15655 C CB  . GLU D  1 424 ? 3.198   -71.752 88.624   1.00 50.04  ? 424 GLU D CB  1 
ATOM   15656 C CG  . GLU D  1 424 ? 2.379   -71.589 89.892   1.00 59.61  ? 424 GLU D CG  1 
ATOM   15657 C CD  . GLU D  1 424 ? 2.224   -72.899 90.646   1.00 71.72  ? 424 GLU D CD  1 
ATOM   15658 O OE1 . GLU D  1 424 ? 1.074   -73.362 90.821   1.00 74.53  ? 424 GLU D OE1 1 
ATOM   15659 O OE2 . GLU D  1 424 ? 3.256   -73.472 91.063   1.00 78.36  ? 424 GLU D OE2 1 
ATOM   15660 N N   . TYR D  1 425 ? 1.292   -70.685 86.297   1.00 31.46  ? 425 TYR D N   1 
ATOM   15661 C CA  . TYR D  1 425 ? 0.108   -69.926 85.899   1.00 32.44  ? 425 TYR D CA  1 
ATOM   15662 C C   . TYR D  1 425 ? -0.847  -70.772 85.062   1.00 32.90  ? 425 TYR D C   1 
ATOM   15663 O O   . TYR D  1 425 ? -2.069  -70.719 85.259   1.00 32.53  ? 425 TYR D O   1 
ATOM   15664 C CB  . TYR D  1 425 ? 0.520   -68.673 85.130   1.00 32.99  ? 425 TYR D CB  1 
ATOM   15665 C CG  . TYR D  1 425 ? 0.636   -67.436 85.988   1.00 31.77  ? 425 TYR D CG  1 
ATOM   15666 C CD1 . TYR D  1 425 ? 0.985   -67.523 87.330   1.00 28.55  ? 425 TYR D CD1 1 
ATOM   15667 C CD2 . TYR D  1 425 ? 0.392   -66.174 85.449   1.00 30.96  ? 425 TYR D CD2 1 
ATOM   15668 C CE1 . TYR D  1 425 ? 1.094   -66.379 88.112   1.00 35.60  ? 425 TYR D CE1 1 
ATOM   15669 C CE2 . TYR D  1 425 ? 0.497   -65.047 86.206   1.00 32.03  ? 425 TYR D CE2 1 
ATOM   15670 C CZ  . TYR D  1 425 ? 0.839   -65.141 87.539   1.00 33.72  ? 425 TYR D CZ  1 
ATOM   15671 O OH  . TYR D  1 425 ? 0.934   -63.980 88.271   1.00 35.67  ? 425 TYR D OH  1 
ATOM   15672 N N   . TRP D  1 426 ? -0.315  -71.570 84.130   1.00 31.75  ? 426 TRP D N   1 
ATOM   15673 C CA  . TRP D  1 426 ? -1.184  -72.464 83.372   1.00 29.98  ? 426 TRP D CA  1 
ATOM   15674 C C   . TRP D  1 426 ? -1.845  -73.499 84.282   1.00 30.09  ? 426 TRP D C   1 
ATOM   15675 O O   . TRP D  1 426 ? -3.027  -73.818 84.114   1.00 31.73  ? 426 TRP D O   1 
ATOM   15676 C CB  . TRP D  1 426 ? -0.401  -73.129 82.241   1.00 31.12  ? 426 TRP D CB  1 
ATOM   15677 C CG  . TRP D  1 426 ? -0.045  -72.149 81.165   1.00 26.35  ? 426 TRP D CG  1 
ATOM   15678 C CD1 . TRP D  1 426 ? 1.151   -71.505 81.000   1.00 21.28  ? 426 TRP D CD1 1 
ATOM   15679 C CD2 . TRP D  1 426 ? -0.902  -71.677 80.118   1.00 22.65  ? 426 TRP D CD2 1 
ATOM   15680 N NE1 . TRP D  1 426 ? 1.097   -70.680 79.913   1.00 22.72  ? 426 TRP D NE1 1 
ATOM   15681 C CE2 . TRP D  1 426 ? -0.154  -70.764 79.351   1.00 29.30  ? 426 TRP D CE2 1 
ATOM   15682 C CE3 . TRP D  1 426 ? -2.224  -71.948 79.748   1.00 26.22  ? 426 TRP D CE3 1 
ATOM   15683 C CZ2 . TRP D  1 426 ? -0.689  -70.112 78.219   1.00 30.24  ? 426 TRP D CZ2 1 
ATOM   15684 C CZ3 . TRP D  1 426 ? -2.763  -71.294 78.619   1.00 24.32  ? 426 TRP D CZ3 1 
ATOM   15685 C CH2 . TRP D  1 426 ? -1.991  -70.391 77.876   1.00 26.33  ? 426 TRP D CH2 1 
ATOM   15686 N N   . LYS D  1 427 ? -1.101  -74.036 85.251   1.00 32.86  ? 427 LYS D N   1 
ATOM   15687 C CA  . LYS D  1 427 ? -1.704  -74.949 86.217   1.00 36.17  ? 427 LYS D CA  1 
ATOM   15688 C C   . LYS D  1 427 ? -2.835  -74.262 86.979   1.00 33.10  ? 427 LYS D C   1 
ATOM   15689 O O   . LYS D  1 427 ? -3.915  -74.834 87.167   1.00 37.42  ? 427 LYS D O   1 
ATOM   15690 C CB  . LYS D  1 427 ? -0.638  -75.469 87.185   1.00 39.03  ? 427 LYS D CB  1 
ATOM   15691 C CG  . LYS D  1 427 ? 0.388   -76.402 86.551   1.00 45.76  ? 427 LYS D CG  1 
ATOM   15692 C CD  . LYS D  1 427 ? 1.164   -77.170 87.612   1.00 55.37  ? 427 LYS D CD  1 
ATOM   15693 C CE  . LYS D  1 427 ? 2.496   -76.507 87.934   1.00 61.21  ? 427 LYS D CE  1 
ATOM   15694 N NZ  . LYS D  1 427 ? 3.115   -77.075 89.176   1.00 65.73  ? 427 LYS D NZ  1 
ATOM   15695 N N   . ILE D  1 428 ? -2.598  -73.038 87.443   1.00 30.08  ? 428 ILE D N   1 
ATOM   15696 C CA  . ILE D  1 428 ? -3.661  -72.289 88.110   1.00 35.72  ? 428 ILE D CA  1 
ATOM   15697 C C   . ILE D  1 428 ? -4.852  -72.128 87.170   1.00 34.90  ? 428 ILE D C   1 
ATOM   15698 O O   . ILE D  1 428 ? -6.013  -72.347 87.549   1.00 33.85  ? 428 ILE D O   1 
ATOM   15699 C CB  . ILE D  1 428 ? -3.131  -70.928 88.592   1.00 34.10  ? 428 ILE D CB  1 
ATOM   15700 C CG1 . ILE D  1 428 ? -2.124  -71.119 89.735   1.00 32.86  ? 428 ILE D CG1 1 
ATOM   15701 C CG2 . ILE D  1 428 ? -4.291  -70.009 88.960   1.00 35.21  ? 428 ILE D CG2 1 
ATOM   15702 C CD1 . ILE D  1 428 ? -1.363  -69.862 90.099   1.00 37.93  ? 428 ILE D CD1 1 
ATOM   15703 N N   . LEU D  1 429 ? -4.570  -71.769 85.919   1.00 31.60  ? 429 LEU D N   1 
ATOM   15704 C CA  . LEU D  1 429 ? -5.627  -71.548 84.937   1.00 34.74  ? 429 LEU D CA  1 
ATOM   15705 C C   . LEU D  1 429 ? -6.416  -72.819 84.675   1.00 28.27  ? 429 LEU D C   1 
ATOM   15706 O O   . LEU D  1 429 ? -7.650  -72.796 84.642   1.00 30.52  ? 429 LEU D O   1 
ATOM   15707 C CB  . LEU D  1 429 ? -5.022  -71.022 83.638   1.00 35.57  ? 429 LEU D CB  1 
ATOM   15708 C CG  . LEU D  1 429 ? -6.018  -70.947 82.483   1.00 35.00  ? 429 LEU D CG  1 
ATOM   15709 C CD1 . LEU D  1 429 ? -7.114  -69.932 82.782   1.00 36.46  ? 429 LEU D CD1 1 
ATOM   15710 C CD2 . LEU D  1 429 ? -5.313  -70.633 81.169   1.00 30.42  ? 429 LEU D CD2 1 
ATOM   15711 N N   . ILE D  1 430 ? -5.714  -73.945 84.521   1.00 28.80  ? 430 ILE D N   1 
ATOM   15712 C CA  . ILE D  1 430 ? -6.351  -75.214 84.186   1.00 30.30  ? 430 ILE D CA  1 
ATOM   15713 C C   . ILE D  1 430 ? -7.303  -75.656 85.295   1.00 35.34  ? 430 ILE D C   1 
ATOM   15714 O O   . ILE D  1 430 ? -8.452  -76.036 85.037   1.00 36.41  ? 430 ILE D O   1 
ATOM   15715 C CB  . ILE D  1 430 ? -5.272  -76.274 83.903   1.00 30.56  ? 430 ILE D CB  1 
ATOM   15716 C CG1 . ILE D  1 430 ? -4.627  -75.987 82.534   1.00 26.14  ? 430 ILE D CG1 1 
ATOM   15717 C CG2 . ILE D  1 430 ? -5.842  -77.683 84.004   1.00 26.93  ? 430 ILE D CG2 1 
ATOM   15718 C CD1 . ILE D  1 430 ? -3.200  -76.504 82.400   1.00 28.48  ? 430 ILE D CD1 1 
ATOM   15719 N N   . GLU D  1 431 ? -6.836  -75.634 86.546   1.00 41.48  ? 431 GLU D N   1 
ATOM   15720 C CA  . GLU D  1 431 ? -7.706  -76.041 87.646   1.00 43.24  ? 431 GLU D CA  1 
ATOM   15721 C C   . GLU D  1 431 ? -8.903  -75.106 87.771   1.00 36.53  ? 431 GLU D C   1 
ATOM   15722 O O   . GLU D  1 431 ? -10.036 -75.559 87.968   1.00 40.55  ? 431 GLU D O   1 
ATOM   15723 C CB  . GLU D  1 431 ? -6.924  -76.096 88.963   1.00 52.53  ? 431 GLU D CB  1 
ATOM   15724 C CG  . GLU D  1 431 ? -5.605  -76.876 88.913   1.00 61.30  ? 431 GLU D CG  1 
ATOM   15725 C CD  . GLU D  1 431 ? -5.796  -78.375 88.726   1.00 69.49  ? 431 GLU D CD  1 
ATOM   15726 O OE1 . GLU D  1 431 ? -5.143  -78.962 87.827   1.00 74.52  ? 431 GLU D OE1 1 
ATOM   15727 O OE2 . GLU D  1 431 ? -6.601  -78.964 89.476   1.00 69.63  ? 431 GLU D OE2 1 
ATOM   15728 N N   . ALA D  1 432 ? -8.678  -73.798 87.640   1.00 35.20  ? 432 ALA D N   1 
ATOM   15729 C CA  . ALA D  1 432 ? -9.784  -72.846 87.712   1.00 39.21  ? 432 ALA D CA  1 
ATOM   15730 C C   . ALA D  1 432 ? -10.796 -73.066 86.590   1.00 41.26  ? 432 ALA D C   1 
ATOM   15731 O O   . ALA D  1 432 ? -12.005 -72.911 86.800   1.00 46.64  ? 432 ALA D O   1 
ATOM   15732 C CB  . ALA D  1 432 ? -9.253  -71.416 87.662   1.00 37.53  ? 432 ALA D CB  1 
ATOM   15733 N N   . LYS D  1 433 ? -10.316 -73.396 85.386   1.00 37.14  ? 433 LYS D N   1 
ATOM   15734 C CA  . LYS D  1 433 ? -11.218 -73.646 84.265   1.00 34.41  ? 433 LYS D CA  1 
ATOM   15735 C C   . LYS D  1 433 ? -12.147 -74.826 84.532   1.00 41.18  ? 433 LYS D C   1 
ATOM   15736 O O   . LYS D  1 433 ? -13.287 -74.842 84.054   1.00 42.13  ? 433 LYS D O   1 
ATOM   15737 C CB  . LYS D  1 433 ? -10.402 -73.881 82.989   1.00 34.92  ? 433 LYS D CB  1 
ATOM   15738 C CG  . LYS D  1 433 ? -11.212 -74.343 81.780   1.00 33.92  ? 433 LYS D CG  1 
ATOM   15739 C CD  . LYS D  1 433 ? -12.215 -73.309 81.342   1.00 33.96  ? 433 LYS D CD  1 
ATOM   15740 C CE  . LYS D  1 433 ? -12.969 -73.743 80.082   1.00 38.01  ? 433 LYS D CE  1 
ATOM   15741 N NZ  . LYS D  1 433 ? -14.030 -72.743 79.725   1.00 38.61  ? 433 LYS D NZ  1 
ATOM   15742 N N   . LYS D  1 434 ? -11.688 -75.822 85.293   1.00 43.72  ? 434 LYS D N   1 
ATOM   15743 C CA  . LYS D  1 434 ? -12.551 -76.956 85.612   1.00 46.43  ? 434 LYS D CA  1 
ATOM   15744 C C   . LYS D  1 434 ? -13.776 -76.532 86.419   1.00 48.28  ? 434 LYS D C   1 
ATOM   15745 O O   . LYS D  1 434 ? -14.804 -77.216 86.370   1.00 50.66  ? 434 LYS D O   1 
ATOM   15746 C CB  . LYS D  1 434 ? -11.770 -78.029 86.376   1.00 45.95  ? 434 LYS D CB  1 
ATOM   15747 C CG  . LYS D  1 434 ? -10.507 -78.524 85.698   1.00 47.63  ? 434 LYS D CG  1 
ATOM   15748 C CD  . LYS D  1 434 ? -9.989  -79.784 86.388   1.00 52.08  ? 434 LYS D CD  1 
ATOM   15749 C CE  . LYS D  1 434 ? -8.638  -80.215 85.826   1.00 52.07  ? 434 LYS D CE  1 
ATOM   15750 N NZ  . LYS D  1 434 ? -7.949  -81.261 86.646   1.00 51.44  ? 434 LYS D NZ  1 
ATOM   15751 N N   . LYS D  1 435 ? -13.691 -75.419 87.167   1.00 45.07  ? 435 LYS D N   1 
ATOM   15752 C CA  . LYS D  1 435 ? -14.808 -74.909 87.961   1.00 47.23  ? 435 LYS D CA  1 
ATOM   15753 C C   . LYS D  1 435 ? -15.189 -73.476 87.597   1.00 47.24  ? 435 LYS D C   1 
ATOM   15754 O O   . LYS D  1 435 ? -15.787 -72.773 88.425   1.00 48.98  ? 435 LYS D O   1 
ATOM   15755 C CB  . LYS D  1 435 ? -14.498 -74.976 89.462   1.00 48.02  ? 435 LYS D CB  1 
ATOM   15756 C CG  . LYS D  1 435 ? -13.582 -76.104 89.856   1.00 54.54  ? 435 LYS D CG  1 
ATOM   15757 C CD  . LYS D  1 435 ? -13.371 -76.145 91.341   1.00 60.48  ? 435 LYS D CD  1 
ATOM   15758 C CE  . LYS D  1 435 ? -12.576 -77.367 91.740   1.00 63.50  ? 435 LYS D CE  1 
ATOM   15759 N NZ  . LYS D  1 435 ? -12.886 -77.720 93.145   1.00 65.09  ? 435 LYS D NZ  1 
ATOM   15760 N N   . ALA D  1 436 ? -14.853 -73.017 86.393   1.00 37.51  ? 436 ALA D N   1 
ATOM   15761 C CA  . ALA D  1 436 ? -15.207 -71.663 85.991   1.00 36.68  ? 436 ALA D CA  1 
ATOM   15762 C C   . ALA D  1 436 ? -16.700 -71.556 85.712   1.00 37.51  ? 436 ALA D C   1 
ATOM   15763 O O   . ALA D  1 436 ? -17.331 -72.486 85.209   1.00 40.92  ? 436 ALA D O   1 
ATOM   15764 C CB  . ALA D  1 436 ? -14.411 -71.242 84.758   1.00 25.67  ? 436 ALA D CB  1 
ATOM   15765 N N   . LYS D  1 437 ? -17.272 -70.406 86.057   1.00 37.15  ? 437 LYS D N   1 
ATOM   15766 C CA  . LYS D  1 437 ? -18.707 -70.214 85.932   1.00 42.25  ? 437 LYS D CA  1 
ATOM   15767 C C   . LYS D  1 437 ? -19.087 -68.906 85.250   1.00 43.18  ? 437 LYS D C   1 
ATOM   15768 O O   . LYS D  1 437 ? -20.282 -68.609 85.148   1.00 44.99  ? 437 LYS D O   1 
ATOM   15769 C CB  . LYS D  1 437 ? -19.384 -70.289 87.319   1.00 48.79  ? 437 LYS D CB  1 
ATOM   15770 C CG  . LYS D  1 437 ? -19.159 -71.608 88.090   1.00 55.51  ? 437 LYS D CG  1 
ATOM   15771 C CD  . LYS D  1 437 ? -19.678 -72.843 87.324   1.00 62.02  ? 437 LYS D CD  1 
ATOM   15772 C CE  . LYS D  1 437 ? -20.012 -74.016 88.263   1.00 64.88  ? 437 LYS D CE  1 
ATOM   15773 N NZ  . LYS D  1 437 ? -19.163 -75.229 88.015   1.00 64.82  ? 437 LYS D NZ  1 
ATOM   15774 N N   . ASN D  1 438 ? -18.122 -68.123 84.772   1.00 37.44  ? 438 ASN D N   1 
ATOM   15775 C CA  . ASN D  1 438 ? -18.431 -66.886 84.066   1.00 35.59  ? 438 ASN D CA  1 
ATOM   15776 C C   . ASN D  1 438 ? -17.242 -66.535 83.186   1.00 34.78  ? 438 ASN D C   1 
ATOM   15777 O O   . ASN D  1 438 ? -16.226 -67.233 83.186   1.00 35.75  ? 438 ASN D O   1 
ATOM   15778 C CB  . ASN D  1 438 ? -18.753 -65.754 85.042   1.00 40.44  ? 438 ASN D CB  1 
ATOM   15779 C CG  . ASN D  1 438 ? -17.620 -65.483 86.001   1.00 34.78  ? 438 ASN D CG  1 
ATOM   15780 O OD1 . ASN D  1 438 ? -16.520 -65.106 85.595   1.00 35.66  ? 438 ASN D OD1 1 
ATOM   15781 N ND2 . ASN D  1 438 ? -17.878 -65.680 87.278   1.00 34.60  ? 438 ASN D ND2 1 
ATOM   15782 N N   . ASP D  1 439 ? -17.360 -65.412 82.468   1.00 31.23  ? 439 ASP D N   1 
ATOM   15783 C CA  . ASP D  1 439 ? -16.401 -65.022 81.438   1.00 30.85  ? 439 ASP D CA  1 
ATOM   15784 C C   . ASP D  1 439 ? -15.128 -64.397 82.000   1.00 26.90  ? 439 ASP D C   1 
ATOM   15785 O O   . ASP D  1 439 ? -14.231 -64.052 81.228   1.00 29.71  ? 439 ASP D O   1 
ATOM   15786 C CB  . ASP D  1 439 ? -17.066 -64.058 80.442   1.00 34.85  ? 439 ASP D CB  1 
ATOM   15787 C CG  . ASP D  1 439 ? -17.780 -64.783 79.304   1.00 42.59  ? 439 ASP D CG  1 
ATOM   15788 O OD1 . ASP D  1 439 ? -17.760 -66.034 79.278   1.00 44.19  ? 439 ASP D OD1 1 
ATOM   15789 O OD2 . ASP D  1 439 ? -18.370 -64.097 78.435   1.00 46.17  ? 439 ASP D OD2 1 
ATOM   15790 N N   . TYR D  1 440 ? -14.992 -64.272 83.317   1.00 33.04  ? 440 TYR D N   1 
ATOM   15791 C CA  . TYR D  1 440 ? -13.702 -63.866 83.855   1.00 27.09  ? 440 TYR D CA  1 
ATOM   15792 C C   . TYR D  1 440 ? -12.614 -64.907 83.607   1.00 27.37  ? 440 TYR D C   1 
ATOM   15793 O O   . TYR D  1 440 ? -11.430 -64.561 83.659   1.00 31.09  ? 440 TYR D O   1 
ATOM   15794 C CB  . TYR D  1 440 ? -13.832 -63.566 85.351   1.00 30.26  ? 440 TYR D CB  1 
ATOM   15795 C CG  . TYR D  1 440 ? -14.204 -62.129 85.609   1.00 32.78  ? 440 TYR D CG  1 
ATOM   15796 C CD1 . TYR D  1 440 ? -13.272 -61.117 85.439   1.00 34.80  ? 440 TYR D CD1 1 
ATOM   15797 C CD2 . TYR D  1 440 ? -15.496 -61.778 85.997   1.00 34.60  ? 440 TYR D CD2 1 
ATOM   15798 C CE1 . TYR D  1 440 ? -13.608 -59.790 85.662   1.00 35.78  ? 440 TYR D CE1 1 
ATOM   15799 C CE2 . TYR D  1 440 ? -15.844 -60.446 86.226   1.00 37.15  ? 440 TYR D CE2 1 
ATOM   15800 C CZ  . TYR D  1 440 ? -14.894 -59.464 86.056   1.00 38.26  ? 440 TYR D CZ  1 
ATOM   15801 O OH  . TYR D  1 440 ? -15.220 -58.150 86.271   1.00 44.34  ? 440 TYR D OH  1 
ATOM   15802 N N   . ILE D  1 441 ? -12.971 -66.170 83.337   1.00 28.41  ? 441 ILE D N   1 
ATOM   15803 C CA  . ILE D  1 441 ? -11.956 -67.137 82.917   1.00 27.29  ? 441 ILE D CA  1 
ATOM   15804 C C   . ILE D  1 441 ? -11.334 -66.741 81.574   1.00 30.47  ? 441 ILE D C   1 
ATOM   15805 O O   . ILE D  1 441 ? -10.187 -67.105 81.292   1.00 27.82  ? 441 ILE D O   1 
ATOM   15806 C CB  . ILE D  1 441 ? -12.529 -68.570 82.855   1.00 31.51  ? 441 ILE D CB  1 
ATOM   15807 C CG1 . ILE D  1 441 ? -11.392 -69.607 82.870   1.00 29.20  ? 441 ILE D CG1 1 
ATOM   15808 C CG2 . ILE D  1 441 ? -13.486 -68.742 81.662   1.00 31.54  ? 441 ILE D CG2 1 
ATOM   15809 C CD1 . ILE D  1 441 ? -10.673 -69.690 84.220   1.00 34.42  ? 441 ILE D CD1 1 
ATOM   15810 N N   . LEU D  1 442 ? -12.057 -65.979 80.745   1.00 33.36  ? 442 LEU D N   1 
ATOM   15811 C CA  . LEU D  1 442 ? -11.469 -65.473 79.506   1.00 29.58  ? 442 LEU D CA  1 
ATOM   15812 C C   . LEU D  1 442 ? -10.455 -64.378 79.788   1.00 30.78  ? 442 LEU D C   1 
ATOM   15813 O O   . LEU D  1 442 ? -9.412  -64.308 79.125   1.00 27.00  ? 442 LEU D O   1 
ATOM   15814 C CB  . LEU D  1 442 ? -12.559 -64.942 78.573   1.00 26.75  ? 442 LEU D CB  1 
ATOM   15815 C CG  . LEU D  1 442 ? -13.685 -65.886 78.163   1.00 28.97  ? 442 LEU D CG  1 
ATOM   15816 C CD1 . LEU D  1 442 ? -14.528 -65.209 77.106   1.00 30.49  ? 442 LEU D CD1 1 
ATOM   15817 C CD2 . LEU D  1 442 ? -13.131 -67.197 77.626   1.00 29.60  ? 442 LEU D CD2 1 
ATOM   15818 N N   . VAL D  1 443 ? -10.765 -63.488 80.742   1.00 30.34  ? 443 VAL D N   1 
ATOM   15819 C CA  . VAL D  1 443 ? -9.832  -62.425 81.119   1.00 31.33  ? 443 VAL D CA  1 
ATOM   15820 C C   . VAL D  1 443 ? -8.499  -63.024 81.539   1.00 30.50  ? 443 VAL D C   1 
ATOM   15821 O O   . VAL D  1 443 ? -7.425  -62.568 81.117   1.00 28.59  ? 443 VAL D O   1 
ATOM   15822 C CB  . VAL D  1 443 ? -10.432 -61.555 82.243   1.00 29.35  ? 443 VAL D CB  1 
ATOM   15823 C CG1 . VAL D  1 443 ? -9.437  -60.465 82.676   1.00 23.65  ? 443 VAL D CG1 1 
ATOM   15824 C CG2 . VAL D  1 443 ? -11.779 -60.964 81.803   1.00 27.14  ? 443 VAL D CG2 1 
ATOM   15825 N N   . ALA D  1 444 ? -8.554  -64.059 82.380   1.00 27.72  ? 444 ALA D N   1 
ATOM   15826 C CA  . ALA D  1 444 ? -7.345  -64.690 82.895   1.00 29.04  ? 444 ALA D CA  1 
ATOM   15827 C C   . ALA D  1 444 ? -6.583  -65.465 81.829   1.00 31.67  ? 444 ALA D C   1 
ATOM   15828 O O   . ALA D  1 444 ? -5.418  -65.801 82.050   1.00 29.84  ? 444 ALA D O   1 
ATOM   15829 C CB  . ALA D  1 444 ? -7.699  -65.604 84.069   1.00 30.40  ? 444 ALA D CB  1 
ATOM   15830 N N   . GLU D  1 445 ? -7.196  -65.747 80.675   1.00 32.69  ? 445 GLU D N   1 
ATOM   15831 C CA  . GLU D  1 445 ? -6.464  -66.352 79.566   1.00 32.10  ? 445 GLU D CA  1 
ATOM   15832 C C   . GLU D  1 445 ? -5.665  -65.331 78.759   1.00 32.49  ? 445 GLU D C   1 
ATOM   15833 O O   . GLU D  1 445 ? -5.088  -65.695 77.731   1.00 33.44  ? 445 GLU D O   1 
ATOM   15834 C CB  . GLU D  1 445 ? -7.428  -67.103 78.644   1.00 28.79  ? 445 GLU D CB  1 
ATOM   15835 C CG  . GLU D  1 445 ? -7.983  -68.361 79.281   1.00 31.29  ? 445 GLU D CG  1 
ATOM   15836 C CD  . GLU D  1 445 ? -9.347  -68.748 78.756   1.00 39.92  ? 445 GLU D CD  1 
ATOM   15837 O OE1 . GLU D  1 445 ? -9.812  -68.151 77.751   1.00 37.24  ? 445 GLU D OE1 1 
ATOM   15838 O OE2 . GLU D  1 445 ? -9.946  -69.674 79.348   1.00 43.76  ? 445 GLU D OE2 1 
ATOM   15839 N N   . GLY D  1 446 ? -5.635  -64.069 79.180   1.00 23.19  ? 446 GLY D N   1 
ATOM   15840 C CA  . GLY D  1 446 ? -4.863  -63.074 78.454   1.00 22.42  ? 446 GLY D CA  1 
ATOM   15841 C C   . GLY D  1 446 ? -3.374  -63.370 78.529   1.00 23.17  ? 446 GLY D C   1 
ATOM   15842 O O   . GLY D  1 446 ? -2.861  -63.805 79.559   1.00 22.91  ? 446 GLY D O   1 
ATOM   15843 N N   . SER D  1 447 ? -2.668  -63.124 77.416   1.00 21.01  ? 447 SER D N   1 
ATOM   15844 C CA  . SER D  1 447 ? -1.257  -63.500 77.338   1.00 25.62  ? 447 SER D CA  1 
ATOM   15845 C C   . SER D  1 447 ? -0.404  -62.774 78.382   1.00 26.28  ? 447 SER D C   1 
ATOM   15846 O O   . SER D  1 447 ? 0.588   -63.334 78.876   1.00 22.30  ? 447 SER D O   1 
ATOM   15847 C CB  . SER D  1 447 ? -0.718  -63.202 75.933   1.00 24.70  ? 447 SER D CB  1 
ATOM   15848 O OG  . SER D  1 447 ? -0.587  -61.792 75.749   1.00 26.03  ? 447 SER D OG  1 
ATOM   15849 N N   . ASP D  1 448 ? -0.783  -61.539 78.724   1.00 21.19  ? 448 ASP D N   1 
ATOM   15850 C CA  . ASP D  1 448 ? 0.063   -60.649 79.522   1.00 22.35  ? 448 ASP D CA  1 
ATOM   15851 C C   . ASP D  1 448 ? 0.436   -61.256 80.868   1.00 24.62  ? 448 ASP D C   1 
ATOM   15852 O O   . ASP D  1 448 ? 1.566   -61.068 81.348   1.00 23.54  ? 448 ASP D O   1 
ATOM   15853 C CB  . ASP D  1 448 ? -0.651  -59.309 79.740   1.00 19.90  ? 448 ASP D CB  1 
ATOM   15854 C CG  . ASP D  1 448 ? -1.083  -58.654 78.424   1.00 27.82  ? 448 ASP D CG  1 
ATOM   15855 O OD1 . ASP D  1 448 ? -2.095  -59.103 77.835   1.00 20.91  ? 448 ASP D OD1 1 
ATOM   15856 O OD2 . ASP D  1 448 ? -0.403  -57.684 77.989   1.00 31.62  ? 448 ASP D OD2 1 
ATOM   15857 N N   . TRP D  1 449 ? -0.502  -61.958 81.509   1.00 24.57  ? 449 TRP D N   1 
ATOM   15858 C CA  . TRP D  1 449 ? -0.225  -62.485 82.845   1.00 29.37  ? 449 TRP D CA  1 
ATOM   15859 C C   . TRP D  1 449 ? 0.944   -63.451 82.801   1.00 31.67  ? 449 TRP D C   1 
ATOM   15860 O O   . TRP D  1 449 ? 1.847   -63.389 83.646   1.00 28.78  ? 449 TRP D O   1 
ATOM   15861 C CB  . TRP D  1 449 ? -1.467  -63.174 83.413   1.00 26.83  ? 449 TRP D CB  1 
ATOM   15862 C CG  . TRP D  1 449 ? -2.724  -62.460 83.102   1.00 20.57  ? 449 TRP D CG  1 
ATOM   15863 C CD1 . TRP D  1 449 ? -3.795  -62.948 82.410   1.00 23.36  ? 449 TRP D CD1 1 
ATOM   15864 C CD2 . TRP D  1 449 ? -3.055  -61.110 83.454   1.00 22.31  ? 449 TRP D CD2 1 
ATOM   15865 N NE1 . TRP D  1 449 ? -4.764  -61.988 82.308   1.00 22.62  ? 449 TRP D NE1 1 
ATOM   15866 C CE2 . TRP D  1 449 ? -4.337  -60.851 82.942   1.00 22.32  ? 449 TRP D CE2 1 
ATOM   15867 C CE3 . TRP D  1 449 ? -2.393  -60.100 84.165   1.00 26.19  ? 449 TRP D CE3 1 
ATOM   15868 C CZ2 . TRP D  1 449 ? -4.977  -59.618 83.109   1.00 24.37  ? 449 TRP D CZ2 1 
ATOM   15869 C CZ3 . TRP D  1 449 ? -3.029  -58.866 84.315   1.00 25.30  ? 449 TRP D CZ3 1 
ATOM   15870 C CH2 . TRP D  1 449 ? -4.308  -58.646 83.797   1.00 26.56  ? 449 TRP D CH2 1 
ATOM   15871 N N   . PHE D  1 450 ? 0.958   -64.321 81.786   1.00 34.35  ? 450 PHE D N   1 
ATOM   15872 C CA  . PHE D  1 450 ? 2.037   -65.282 81.617   1.00 32.69  ? 450 PHE D CA  1 
ATOM   15873 C C   . PHE D  1 450 ? 3.318   -64.607 81.149   1.00 30.14  ? 450 PHE D C   1 
ATOM   15874 O O   . PHE D  1 450 ? 4.412   -65.100 81.438   1.00 25.24  ? 450 PHE D O   1 
ATOM   15875 C CB  . PHE D  1 450 ? 1.608   -66.373 80.632   1.00 30.91  ? 450 PHE D CB  1 
ATOM   15876 C CG  . PHE D  1 450 ? 0.259   -66.965 80.939   1.00 31.64  ? 450 PHE D CG  1 
ATOM   15877 C CD1 . PHE D  1 450 ? -0.912  -66.346 80.494   1.00 25.68  ? 450 PHE D CD1 1 
ATOM   15878 C CD2 . PHE D  1 450 ? 0.154   -68.130 81.689   1.00 29.37  ? 450 PHE D CD2 1 
ATOM   15879 C CE1 . PHE D  1 450 ? -2.164  -66.887 80.789   1.00 24.18  ? 450 PHE D CE1 1 
ATOM   15880 C CE2 . PHE D  1 450 ? -1.093  -68.676 81.990   1.00 28.43  ? 450 PHE D CE2 1 
ATOM   15881 C CZ  . PHE D  1 450 ? -2.251  -68.053 81.529   1.00 27.79  ? 450 PHE D CZ  1 
ATOM   15882 N N   . TRP D  1 451 ? 3.205   -63.490 80.426   1.00 29.50  ? 451 TRP D N   1 
ATOM   15883 C CA  . TRP D  1 451 ? 4.402   -62.766 80.000   1.00 29.95  ? 451 TRP D CA  1 
ATOM   15884 C C   . TRP D  1 451 ? 5.210   -62.291 81.208   1.00 31.93  ? 451 TRP D C   1 
ATOM   15885 O O   . TRP D  1 451 ? 6.436   -62.466 81.258   1.00 26.32  ? 451 TRP D O   1 
ATOM   15886 C CB  . TRP D  1 451 ? 4.024   -61.581 79.102   1.00 27.13  ? 451 TRP D CB  1 
ATOM   15887 C CG  . TRP D  1 451 ? 5.144   -60.597 78.926   1.00 29.69  ? 451 TRP D CG  1 
ATOM   15888 C CD1 . TRP D  1 451 ? 5.319   -59.412 79.600   1.00 29.97  ? 451 TRP D CD1 1 
ATOM   15889 C CD2 . TRP D  1 451 ? 6.262   -60.723 78.043   1.00 34.49  ? 451 TRP D CD2 1 
ATOM   15890 N NE1 . TRP D  1 451 ? 6.473   -58.798 79.182   1.00 31.90  ? 451 TRP D NE1 1 
ATOM   15891 C CE2 . TRP D  1 451 ? 7.074   -59.580 78.231   1.00 35.03  ? 451 TRP D CE2 1 
ATOM   15892 C CE3 . TRP D  1 451 ? 6.658   -61.689 77.109   1.00 40.67  ? 451 TRP D CE3 1 
ATOM   15893 C CZ2 . TRP D  1 451 ? 8.253   -59.374 77.516   1.00 42.83  ? 451 TRP D CZ2 1 
ATOM   15894 C CZ3 . TRP D  1 451 ? 7.833   -61.490 76.403   1.00 46.95  ? 451 TRP D CZ3 1 
ATOM   15895 C CH2 . TRP D  1 451 ? 8.618   -60.337 76.609   1.00 48.71  ? 451 TRP D CH2 1 
ATOM   15896 N N   . TRP D  1 452 ? 4.551   -61.741 82.212   1.00 31.33  ? 452 TRP D N   1 
ATOM   15897 C CA  . TRP D  1 452 ? 5.256   -61.180 83.361   1.00 34.42  ? 452 TRP D CA  1 
ATOM   15898 C C   . TRP D  1 452 ? 5.698   -62.185 84.394   1.00 39.33  ? 452 TRP D C   1 
ATOM   15899 O O   . TRP D  1 452 ? 6.592   -61.926 85.141   1.00 35.60  ? 452 TRP D O   1 
ATOM   15900 C CB  . TRP D  1 452 ? 4.433   -60.089 84.028   1.00 32.75  ? 452 TRP D CB  1 
ATOM   15901 C CG  . TRP D  1 452 ? 4.207   -58.904 83.163   1.00 32.64  ? 452 TRP D CG  1 
ATOM   15902 C CD1 . TRP D  1 452 ? 3.051   -58.542 82.563   1.00 33.81  ? 452 TRP D CD1 1 
ATOM   15903 C CD2 . TRP D  1 452 ? 5.172   -57.940 82.782   1.00 33.21  ? 452 TRP D CD2 1 
ATOM   15904 N NE1 . TRP D  1 452 ? 3.229   -57.407 81.839   1.00 36.42  ? 452 TRP D NE1 1 
ATOM   15905 C CE2 . TRP D  1 452 ? 4.532   -57.021 81.948   1.00 34.30  ? 452 TRP D CE2 1 
ATOM   15906 C CE3 . TRP D  1 452 ? 6.523   -57.770 83.050   1.00 35.19  ? 452 TRP D CE3 1 
ATOM   15907 C CZ2 . TRP D  1 452 ? 5.190   -55.952 81.393   1.00 33.72  ? 452 TRP D CZ2 1 
ATOM   15908 C CZ3 . TRP D  1 452 ? 7.171   -56.707 82.500   1.00 35.68  ? 452 TRP D CZ3 1 
ATOM   15909 C CH2 . TRP D  1 452 ? 6.507   -55.809 81.683   1.00 35.54  ? 452 TRP D CH2 1 
ATOM   15910 N N   . GLN D  1 453 ? 5.068   -63.335 84.367   1.00 41.08  ? 453 GLN D N   1 
ATOM   15911 C CA  . GLN D  1 453 ? 5.369   -64.341 85.327   1.00 43.92  ? 453 GLN D CA  1 
ATOM   15912 C C   . GLN D  1 453 ? 6.744   -64.810 85.139   1.00 50.16  ? 453 GLN D C   1 
ATOM   15913 O O   . GLN D  1 453 ? 7.244   -64.970 84.079   1.00 47.81  ? 453 GLN D O   1 
ATOM   15914 C CB  . GLN D  1 453 ? 4.419   -65.468 85.271   1.00 40.59  ? 453 GLN D CB  1 
ATOM   15915 C CG  . GLN D  1 453 ? 4.793   -66.680 86.095   1.00 42.22  ? 453 GLN D CG  1 
ATOM   15916 C CD  . GLN D  1 453 ? 4.583   -66.481 87.586   1.00 41.37  ? 453 GLN D CD  1 
ATOM   15917 O OE1 . GLN D  1 453 ? 4.391   -65.375 88.053   1.00 38.11  ? 453 GLN D OE1 1 
ATOM   15918 N NE2 . GLN D  1 453 ? 4.622   -67.566 88.331   1.00 37.76  ? 453 GLN D NE2 1 
ATOM   15919 N N   . GLY D  1 454 ? 7.387   -64.929 86.241   1.00 59.04  ? 454 GLY D N   1 
ATOM   15920 C CA  . GLY D  1 454 ? 8.737   -65.382 86.213   1.00 67.39  ? 454 GLY D CA  1 
ATOM   15921 C C   . GLY D  1 454 ? 9.671   -64.277 85.973   1.00 75.69  ? 454 GLY D C   1 
ATOM   15922 O O   . GLY D  1 454 ? 10.730  -64.504 85.441   1.00 78.47  ? 454 GLY D O   1 
ATOM   15923 N N   . GLU D  1 455 ? 9.280   -63.057 86.316   1.00 80.84  ? 455 GLU D N   1 
ATOM   15924 C CA  . GLU D  1 455 ? 10.231  -61.896 86.168   1.00 84.04  ? 455 GLU D CA  1 
ATOM   15925 C C   . GLU D  1 455 ? 10.677  -61.300 87.518   1.00 86.22  ? 455 GLU D C   1 
ATOM   15926 O O   . GLU D  1 455 ? 11.839  -60.943 87.630   1.00 87.02  ? 455 GLU D O   1 
ATOM   15927 C CB  . GLU D  1 455 ? 9.691   -60.890 85.174   1.00 81.66  ? 455 GLU D CB  1 
ATOM   15928 C CG  . GLU D  1 455 ? 9.749   -61.441 83.751   1.00 81.71  ? 455 GLU D CG  1 
ATOM   15929 C CD  . GLU D  1 455 ? 9.621   -60.379 82.676   1.00 82.84  ? 455 GLU D CD  1 
ATOM   15930 O OE1 . GLU D  1 455 ? 10.179  -59.279 82.863   1.00 84.78  ? 455 GLU D OE1 1 
ATOM   15931 O OE2 . GLU D  1 455 ? 8.979   -60.650 81.639   1.00 80.90  ? 455 GLU D OE2 1 
ATOM   15932 N N   . GLU D  1 456 ? 9.746   -61.066 88.452   1.00 85.74  ? 456 GLU D N   1 
ATOM   15933 C CA  . GLU D  1 456 ? 10.094  -60.673 89.865   1.00 84.74  ? 456 GLU D CA  1 
ATOM   15934 C C   . GLU D  1 456 ? 10.276  -59.226 90.400   1.00 83.25  ? 456 GLU D C   1 
ATOM   15935 O O   . GLU D  1 456 ? 9.423   -58.656 91.077   1.00 83.07  ? 456 GLU D O   1 
ATOM   15936 C CB  . GLU D  1 456 ? 11.356  -61.451 90.305   1.00 84.17  ? 456 GLU D CB  1 
ATOM   15937 N N   . LYS D  1 457 ? 11.394  -58.651 90.114   1.00 80.64  ? 457 LYS D N   1 
ATOM   15938 C CA  . LYS D  1 457 ? 11.575  -57.400 90.773   1.00 76.95  ? 457 LYS D CA  1 
ATOM   15939 C C   . LYS D  1 457 ? 11.350  -56.231 89.946   1.00 78.03  ? 457 LYS D C   1 
ATOM   15940 O O   . LYS D  1 457 ? 11.943  -55.184 90.174   1.00 81.01  ? 457 LYS D O   1 
ATOM   15941 C CB  . LYS D  1 457 ? 13.003  -57.301 91.361   1.00 76.04  ? 457 LYS D CB  1 
ATOM   15942 N N   . ALA D  1 458 ? 10.540  -56.368 88.942   1.00 72.89  ? 458 ALA D N   1 
ATOM   15943 C CA  . ALA D  1 458 ? 10.279  -55.166 88.270   1.00 63.51  ? 458 ALA D CA  1 
ATOM   15944 C C   . ALA D  1 458 ? 9.250   -54.496 89.121   1.00 53.17  ? 458 ALA D C   1 
ATOM   15945 O O   . ALA D  1 458 ? 8.360   -55.108 89.642   1.00 48.07  ? 458 ALA D O   1 
ATOM   15946 C CB  . ALA D  1 458 ? 9.789   -55.416 86.865   1.00 61.30  ? 458 ALA D CB  1 
ATOM   15947 N N   . PRO D  1 459 ? 9.404   -53.220 89.269   1.00 52.12  ? 459 PRO D N   1 
ATOM   15948 C CA  . PRO D  1 459 ? 8.421   -52.482 90.010   1.00 50.86  ? 459 PRO D CA  1 
ATOM   15949 C C   . PRO D  1 459 ? 7.028   -52.696 89.454   1.00 53.01  ? 459 PRO D C   1 
ATOM   15950 O O   . PRO D  1 459 ? 6.857   -52.645 88.279   1.00 46.24  ? 459 PRO D O   1 
ATOM   15951 C CB  . PRO D  1 459 ? 8.843   -51.086 89.773   1.00 51.71  ? 459 PRO D CB  1 
ATOM   15952 C CG  . PRO D  1 459 ? 10.295  -51.109 89.488   1.00 54.19  ? 459 PRO D CG  1 
ATOM   15953 C CD  . PRO D  1 459 ? 10.510  -52.391 88.779   1.00 53.42  ? 459 PRO D CD  1 
ATOM   15954 N N   . PHE D  1 460 ? 6.082   -52.983 90.315   1.00 55.63  ? 460 PHE D N   1 
ATOM   15955 C CA  . PHE D  1 460 ? 4.676   -53.241 89.953   1.00 52.40  ? 460 PHE D CA  1 
ATOM   15956 C C   . PHE D  1 460 ? 4.295   -54.612 89.313   1.00 45.45  ? 460 PHE D C   1 
ATOM   15957 O O   . PHE D  1 460 ? 3.177   -54.787 89.003   1.00 43.25  ? 460 PHE D O   1 
ATOM   15958 C CB  . PHE D  1 460 ? 4.113   -52.077 89.169   1.00 52.03  ? 460 PHE D CB  1 
ATOM   15959 C CG  . PHE D  1 460 ? 4.490   -50.724 89.702   1.00 52.40  ? 460 PHE D CG  1 
ATOM   15960 C CD1 . PHE D  1 460 ? 3.947   -50.248 90.873   1.00 57.50  ? 460 PHE D CD1 1 
ATOM   15961 C CD2 . PHE D  1 460 ? 5.360   -49.920 89.014   1.00 50.83  ? 460 PHE D CD2 1 
ATOM   15962 C CE1 . PHE D  1 460 ? 4.286   -48.995 91.360   1.00 58.58  ? 460 PHE D CE1 1 
ATOM   15963 C CE2 . PHE D  1 460 ? 5.701   -48.670 89.492   1.00 55.37  ? 460 PHE D CE2 1 
ATOM   15964 C CZ  . PHE D  1 460 ? 5.162   -48.208 90.666   1.00 58.07  ? 460 PHE D CZ  1 
ATOM   15965 N N   . VAL D  1 461 ? 5.179   -55.602 89.253   1.00 45.61  ? 461 VAL D N   1 
ATOM   15966 C CA  . VAL D  1 461 ? 4.765   -56.864 88.641   1.00 45.81  ? 461 VAL D CA  1 
ATOM   15967 C C   . VAL D  1 461 ? 3.875   -57.673 89.568   1.00 45.89  ? 461 VAL D C   1 
ATOM   15968 O O   . VAL D  1 461 ? 3.064   -58.479 89.098   1.00 52.08  ? 461 VAL D O   1 
ATOM   15969 C CB  . VAL D  1 461 ? 5.973   -57.707 88.213   1.00 54.26  ? 461 VAL D CB  1 
ATOM   15970 C CG1 . VAL D  1 461 ? 6.825   -56.928 87.210   1.00 55.15  ? 461 VAL D CG1 1 
ATOM   15971 C CG2 . VAL D  1 461 ? 6.735   -58.191 89.455   1.00 59.16  ? 461 VAL D CG2 1 
ATOM   15972 N N   . GLU D  1 462 ? 4.023   -57.517 90.890   1.00 38.09  ? 462 GLU D N   1 
ATOM   15973 C CA  . GLU D  1 462 ? 3.096   -58.183 91.792   1.00 45.45  ? 462 GLU D CA  1 
ATOM   15974 C C   . GLU D  1 462 ? 1.661   -57.775 91.487   1.00 39.82  ? 462 GLU D C   1 
ATOM   15975 O O   . GLU D  1 462 ? 0.731   -58.553 91.731   1.00 44.85  ? 462 GLU D O   1 
ATOM   15976 C CB  . GLU D  1 462 ? 3.459   -57.875 93.253   1.00 58.48  ? 462 GLU D CB  1 
ATOM   15977 C CG  . GLU D  1 462 ? 3.287   -56.401 93.663   1.00 72.02  ? 462 GLU D CG  1 
ATOM   15978 C CD  . GLU D  1 462 ? 4.494   -55.530 93.312   1.00 82.26  ? 462 GLU D CD  1 
ATOM   15979 O OE1 . GLU D  1 462 ? 4.385   -54.282 93.398   1.00 85.62  ? 462 GLU D OE1 1 
ATOM   15980 O OE2 . GLU D  1 462 ? 5.551   -56.095 92.950   1.00 84.41  ? 462 GLU D OE2 1 
ATOM   15981 N N   . VAL D  1 463 ? 1.462   -56.573 90.936   1.00 29.86  ? 463 VAL D N   1 
ATOM   15982 C CA  . VAL D  1 463 ? 0.114   -56.140 90.576   1.00 34.95  ? 463 VAL D CA  1 
ATOM   15983 C C   . VAL D  1 463 ? -0.460  -57.026 89.481   1.00 31.49  ? 463 VAL D C   1 
ATOM   15984 O O   . VAL D  1 463 ? -1.649  -57.367 89.512   1.00 28.61  ? 463 VAL D O   1 
ATOM   15985 C CB  . VAL D  1 463 ? 0.104   -54.656 90.158   1.00 35.93  ? 463 VAL D CB  1 
ATOM   15986 C CG1 . VAL D  1 463 ? -1.286  -54.242 89.675   1.00 33.61  ? 463 VAL D CG1 1 
ATOM   15987 C CG2 . VAL D  1 463 ? 0.570   -53.789 91.309   1.00 32.13  ? 463 VAL D CG2 1 
ATOM   15988 N N   . PHE D  1 464 ? 0.365   -57.394 88.486   1.00 30.85  ? 464 PHE D N   1 
ATOM   15989 C CA  . PHE D  1 464 ? -0.075  -58.326 87.450   1.00 31.36  ? 464 PHE D CA  1 
ATOM   15990 C C   . PHE D  1 464 ? -0.465  -59.665 88.063   1.00 31.35  ? 464 PHE D C   1 
ATOM   15991 O O   . PHE D  1 464 ? -1.440  -60.297 87.633   1.00 27.44  ? 464 PHE D O   1 
ATOM   15992 C CB  . PHE D  1 464 ? 1.025   -58.510 86.385   1.00 28.76  ? 464 PHE D CB  1 
ATOM   15993 C CG  . PHE D  1 464 ? 1.196   -57.316 85.486   1.00 30.58  ? 464 PHE D CG  1 
ATOM   15994 C CD1 . PHE D  1 464 ? 0.312   -57.086 84.443   1.00 29.52  ? 464 PHE D CD1 1 
ATOM   15995 C CD2 . PHE D  1 464 ? 2.207   -56.393 85.711   1.00 35.00  ? 464 PHE D CD2 1 
ATOM   15996 C CE1 . PHE D  1 464 ? 0.439   -55.955 83.619   1.00 25.52  ? 464 PHE D CE1 1 
ATOM   15997 C CE2 . PHE D  1 464 ? 2.343   -55.269 84.898   1.00 35.19  ? 464 PHE D CE2 1 
ATOM   15998 C CZ  . PHE D  1 464 ? 1.452   -55.052 83.848   1.00 30.45  ? 464 PHE D CZ  1 
ATOM   15999 N N   . ASP D  1 465 ? 0.276   -60.108 89.083   1.00 30.61  ? 465 ASP D N   1 
ATOM   16000 C CA  . ASP D  1 465 ? -0.107  -61.337 89.769   1.00 34.06  ? 465 ASP D CA  1 
ATOM   16001 C C   . ASP D  1 465 ? -1.411  -61.152 90.537   1.00 30.89  ? 465 ASP D C   1 
ATOM   16002 O O   . ASP D  1 465 ? -2.277  -62.032 90.507   1.00 31.56  ? 465 ASP D O   1 
ATOM   16003 C CB  . ASP D  1 465 ? 1.011   -61.805 90.707   1.00 29.90  ? 465 ASP D CB  1 
ATOM   16004 C CG  . ASP D  1 465 ? 0.642   -63.066 91.452   1.00 32.99  ? 465 ASP D CG  1 
ATOM   16005 O OD1 . ASP D  1 465 ? 0.729   -64.155 90.838   1.00 28.77  ? 465 ASP D OD1 1 
ATOM   16006 O OD2 . ASP D  1 465 ? 0.262   -62.969 92.651   1.00 36.40  ? 465 ASP D OD2 1 
ATOM   16007 N N   . LYS D  1 466 ? -1.564  -60.018 91.232   1.00 26.67  ? 466 LYS D N   1 
ATOM   16008 C CA  . LYS D  1 466 ? -2.809  -59.733 91.946   1.00 29.75  ? 466 LYS D CA  1 
ATOM   16009 C C   . LYS D  1 466 ? -3.997  -59.744 90.993   1.00 33.14  ? 466 LYS D C   1 
ATOM   16010 O O   . LYS D  1 466 ? -5.022  -60.380 91.263   1.00 31.07  ? 466 LYS D O   1 
ATOM   16011 C CB  . LYS D  1 466 ? -2.707  -58.381 92.668   1.00 36.19  ? 466 LYS D CB  1 
ATOM   16012 C CG  . LYS D  1 466 ? -3.956  -57.971 93.430   1.00 43.24  ? 466 LYS D CG  1 
ATOM   16013 C CD  . LYS D  1 466 ? -3.796  -56.618 94.110   1.00 51.70  ? 466 LYS D CD  1 
ATOM   16014 C CE  . LYS D  1 466 ? -2.909  -56.693 95.346   1.00 61.95  ? 466 LYS D CE  1 
ATOM   16015 N NZ  . LYS D  1 466 ? -1.509  -56.286 95.022   1.00 66.82  ? 466 LYS D NZ  1 
ATOM   16016 N N   . LEU D  1 467 ? -3.865  -59.059 89.853   1.00 30.26  ? 467 LEU D N   1 
ATOM   16017 C CA  . LEU D  1 467 ? -4.939  -59.053 88.865   1.00 27.88  ? 467 LEU D CA  1 
ATOM   16018 C C   . LEU D  1 467 ? -5.255  -60.467 88.362   1.00 30.43  ? 467 LEU D C   1 
ATOM   16019 O O   . LEU D  1 467 ? -6.411  -60.902 88.405   1.00 35.20  ? 467 LEU D O   1 
ATOM   16020 C CB  . LEU D  1 467 ? -4.552  -58.132 87.715   1.00 26.40  ? 467 LEU D CB  1 
ATOM   16021 C CG  . LEU D  1 467 ? -4.596  -56.643 88.060   1.00 26.51  ? 467 LEU D CG  1 
ATOM   16022 C CD1 . LEU D  1 467 ? -3.978  -55.846 86.930   1.00 32.51  ? 467 LEU D CD1 1 
ATOM   16023 C CD2 . LEU D  1 467 ? -6.022  -56.236 88.313   1.00 25.10  ? 467 LEU D CD2 1 
ATOM   16024 N N   . PHE D  1 468 ? -4.242  -61.206 87.891   1.00 27.85  ? 468 PHE D N   1 
ATOM   16025 C CA  . PHE D  1 468 ? -4.477  -62.553 87.351   1.00 32.33  ? 468 PHE D CA  1 
ATOM   16026 C C   . PHE D  1 468 ? -5.241  -63.429 88.342   1.00 33.84  ? 468 PHE D C   1 
ATOM   16027 O O   . PHE D  1 468 ? -6.242  -64.071 87.990   1.00 29.78  ? 468 PHE D O   1 
ATOM   16028 C CB  . PHE D  1 468 ? -3.142  -63.205 86.982   1.00 29.02  ? 468 PHE D CB  1 
ATOM   16029 C CG  . PHE D  1 468 ? -3.234  -64.673 86.608   1.00 31.63  ? 468 PHE D CG  1 
ATOM   16030 C CD1 . PHE D  1 468 ? -3.756  -65.061 85.384   1.00 30.78  ? 468 PHE D CD1 1 
ATOM   16031 C CD2 . PHE D  1 468 ? -2.746  -65.656 87.464   1.00 33.34  ? 468 PHE D CD2 1 
ATOM   16032 C CE1 . PHE D  1 468 ? -3.832  -66.395 85.026   1.00 32.37  ? 468 PHE D CE1 1 
ATOM   16033 C CE2 . PHE D  1 468 ? -2.813  -67.009 87.115   1.00 34.26  ? 468 PHE D CE2 1 
ATOM   16034 C CZ  . PHE D  1 468 ? -3.358  -67.377 85.884   1.00 32.11  ? 468 PHE D CZ  1 
ATOM   16035 N N   . ARG D  1 469 ? -4.785  -63.446 89.595   1.00 30.82  ? 469 ARG D N   1 
ATOM   16036 C CA  . ARG D  1 469 ? -5.394  -64.312 90.601   1.00 32.70  ? 469 ARG D CA  1 
ATOM   16037 C C   . ARG D  1 469 ? -6.795  -63.849 90.957   1.00 31.10  ? 469 ARG D C   1 
ATOM   16038 O O   . ARG D  1 469 ? -7.685  -64.673 91.174   1.00 30.01  ? 469 ARG D O   1 
ATOM   16039 C CB  . ARG D  1 469 ? -4.489  -64.378 91.827   1.00 34.74  ? 469 ARG D CB  1 
ATOM   16040 C CG  . ARG D  1 469 ? -3.163  -65.072 91.515   1.00 37.26  ? 469 ARG D CG  1 
ATOM   16041 C CD  . ARG D  1 469 ? -2.276  -65.106 92.745   1.00 43.68  ? 469 ARG D CD  1 
ATOM   16042 N NE  . ARG D  1 469 ? -1.058  -65.891 92.549   1.00 46.92  ? 469 ARG D NE  1 
ATOM   16043 C CZ  . ARG D  1 469 ? -0.981  -67.215 92.676   1.00 43.21  ? 469 ARG D CZ  1 
ATOM   16044 N NH1 . ARG D  1 469 ? -2.059  -67.934 92.984   1.00 37.97  ? 469 ARG D NH1 1 
ATOM   16045 N NH2 . ARG D  1 469 ? 0.183   -67.820 92.492   1.00 42.72  ? 469 ARG D NH2 1 
ATOM   16046 N N   . SER D  1 470 ? -7.030  -62.534 90.966   1.00 35.31  ? 470 SER D N   1 
ATOM   16047 C CA  . SER D  1 470 ? -8.376  -62.036 91.230   1.00 32.94  ? 470 SER D CA  1 
ATOM   16048 C C   . SER D  1 470 ? -9.345  -62.448 90.124   1.00 32.45  ? 470 SER D C   1 
ATOM   16049 O O   . SER D  1 470 ? -10.480 -62.862 90.401   1.00 32.01  ? 470 SER D O   1 
ATOM   16050 C CB  . SER D  1 470 ? -8.341  -60.520 91.387   1.00 36.15  ? 470 SER D CB  1 
ATOM   16051 O OG  . SER D  1 470 ? -7.501  -60.161 92.470   1.00 44.83  ? 470 SER D OG  1 
ATOM   16052 N N   . PHE D  1 471 ? -8.921  -62.339 88.862   1.00 25.96  ? 471 PHE D N   1 
ATOM   16053 C CA  . PHE D  1 471 ? -9.766  -62.797 87.766   1.00 28.83  ? 471 PHE D CA  1 
ATOM   16054 C C   . PHE D  1 471 ? -9.999  -64.293 87.867   1.00 31.82  ? 471 PHE D C   1 
ATOM   16055 O O   . PHE D  1 471 ? -11.121 -64.771 87.662   1.00 31.45  ? 471 PHE D O   1 
ATOM   16056 C CB  . PHE D  1 471 ? -9.131  -62.458 86.412   1.00 31.49  ? 471 PHE D CB  1 
ATOM   16057 C CG  . PHE D  1 471 ? -8.937  -60.995 86.173   1.00 27.82  ? 471 PHE D CG  1 
ATOM   16058 C CD1 . PHE D  1 471 ? -9.984  -60.110 86.332   1.00 27.00  ? 471 PHE D CD1 1 
ATOM   16059 C CD2 . PHE D  1 471 ? -7.696  -60.504 85.766   1.00 24.59  ? 471 PHE D CD2 1 
ATOM   16060 C CE1 . PHE D  1 471 ? -9.802  -58.772 86.109   1.00 29.38  ? 471 PHE D CE1 1 
ATOM   16061 C CE2 . PHE D  1 471 ? -7.504  -59.161 85.563   1.00 20.69  ? 471 PHE D CE2 1 
ATOM   16062 C CZ  . PHE D  1 471 ? -8.554  -58.295 85.706   1.00 24.24  ? 471 PHE D CZ  1 
ATOM   16063 N N   . VAL D  1 472 ? -8.948  -65.047 88.212   1.00 29.34  ? 472 VAL D N   1 
ATOM   16064 C CA  . VAL D  1 472 ? -9.082  -66.492 88.371   1.00 31.89  ? 472 VAL D CA  1 
ATOM   16065 C C   . VAL D  1 472 ? -10.016 -66.815 89.527   1.00 34.76  ? 472 VAL D C   1 
ATOM   16066 O O   . VAL D  1 472 ? -10.831 -67.737 89.438   1.00 35.81  ? 472 VAL D O   1 
ATOM   16067 C CB  . VAL D  1 472 ? -7.699  -67.148 88.548   1.00 29.90  ? 472 VAL D CB  1 
ATOM   16068 C CG1 . VAL D  1 472 ? -7.838  -68.551 89.084   1.00 36.18  ? 472 VAL D CG1 1 
ATOM   16069 C CG2 . VAL D  1 472 ? -6.951  -67.165 87.203   1.00 29.18  ? 472 VAL D CG2 1 
ATOM   16070 N N   . ARG D  1 473 ? -9.935  -66.053 90.621   1.00 35.80  ? 473 ARG D N   1 
ATOM   16071 C CA  . ARG D  1 473 ? -10.868 -66.283 91.725   1.00 37.09  ? 473 ARG D CA  1 
ATOM   16072 C C   . ARG D  1 473 ? -12.292 -65.924 91.307   1.00 37.81  ? 473 ARG D C   1 
ATOM   16073 O O   . ARG D  1 473 ? -13.218 -66.725 91.474   1.00 35.98  ? 473 ARG D O   1 
ATOM   16074 C CB  . ARG D  1 473 ? -10.441 -65.482 92.955   1.00 36.69  ? 473 ARG D CB  1 
ATOM   16075 C CG  . ARG D  1 473 ? -11.482 -65.442 94.068   1.00 46.09  ? 473 ARG D CG  1 
ATOM   16076 C CD  . ARG D  1 473 ? -10.950 -64.738 95.314   1.00 52.18  ? 473 ARG D CD  1 
ATOM   16077 N NE  . ARG D  1 473 ? -11.980 -64.586 96.347   1.00 63.37  ? 473 ARG D NE  1 
ATOM   16078 C CZ  . ARG D  1 473 ? -12.279 -63.438 96.956   1.00 66.63  ? 473 ARG D CZ  1 
ATOM   16079 N NH1 . ARG D  1 473 ? -11.623 -62.322 96.651   1.00 63.69  ? 473 ARG D NH1 1 
ATOM   16080 N NH2 . ARG D  1 473 ? -13.233 -63.403 97.879   1.00 70.31  ? 473 ARG D NH2 1 
ATOM   16081 N N   . ARG D  1 474 ? -12.468 -64.741 90.703   1.00 36.74  ? 474 ARG D N   1 
ATOM   16082 C CA  . ARG D  1 474 ? -13.795 -64.276 90.306   1.00 38.91  ? 474 ARG D CA  1 
ATOM   16083 C C   . ARG D  1 474 ? -14.462 -65.210 89.299   1.00 41.40  ? 474 ARG D C   1 
ATOM   16084 O O   . ARG D  1 474 ? -15.693 -65.357 89.311   1.00 35.48  ? 474 ARG D O   1 
ATOM   16085 C CB  . ARG D  1 474 ? -13.697 -62.863 89.727   1.00 37.48  ? 474 ARG D CB  1 
ATOM   16086 C CG  . ARG D  1 474 ? -15.031 -62.284 89.270   1.00 42.33  ? 474 ARG D CG  1 
ATOM   16087 C CD  . ARG D  1 474 ? -16.004 -62.119 90.437   1.00 54.86  ? 474 ARG D CD  1 
ATOM   16088 N NE  . ARG D  1 474 ? -16.695 -60.831 90.412   1.00 65.15  ? 474 ARG D NE  1 
ATOM   16089 C CZ  . ARG D  1 474 ? -17.859 -60.612 89.801   1.00 74.81  ? 474 ARG D CZ  1 
ATOM   16090 N NH1 . ARG D  1 474 ? -18.470 -61.598 89.153   1.00 76.32  ? 474 ARG D NH1 1 
ATOM   16091 N NH2 . ARG D  1 474 ? -18.411 -59.405 89.833   1.00 78.99  ? 474 ARG D NH2 1 
ATOM   16092 N N   . ALA D  1 475 ? -13.673 -65.849 88.422   1.00 39.31  ? 475 ALA D N   1 
ATOM   16093 C CA  . ALA D  1 475 ? -14.228 -66.733 87.400   1.00 42.37  ? 475 ALA D CA  1 
ATOM   16094 C C   . ALA D  1 475 ? -14.899 -67.979 87.979   1.00 44.79  ? 475 ALA D C   1 
ATOM   16095 O O   . ALA D  1 475 ? -15.764 -68.562 87.315   1.00 47.71  ? 475 ALA D O   1 
ATOM   16096 C CB  . ALA D  1 475 ? -13.137 -67.146 86.405   1.00 42.94  ? 475 ALA D CB  1 
ATOM   16097 N N   . GLN D  1 476 ? -14.596 -68.363 89.169   1.00 43.81  ? 476 GLN D N   1 
ATOM   16098 C CA  . GLN D  1 476 ? -15.101 -69.613 89.713   1.00 45.62  ? 476 GLN D CA  1 
ATOM   16099 C C   . GLN D  1 476 ? -16.245 -69.342 90.653   1.00 52.02  ? 476 GLN D C   1 
ATOM   16100 O O   . GLN D  1 476 ? -16.832 -70.253 91.205   1.00 48.80  ? 476 GLN D O   1 
ATOM   16101 C CB  . GLN D  1 476 ? -13.966 -70.396 90.361   1.00 44.70  ? 476 GLN D CB  1 
ATOM   16102 C CG  . GLN D  1 476 ? -12.849 -70.921 89.546   1.00 41.74  ? 476 GLN D CG  1 
ATOM   16103 C CD  . GLN D  1 476 ? -11.702 -71.257 90.453   1.00 44.77  ? 476 GLN D CD  1 
ATOM   16104 O OE1 . GLN D  1 476 ? -11.621 -72.344 90.983   1.00 46.93  ? 476 GLN D OE1 1 
ATOM   16105 N NE2 . GLN D  1 476 ? -10.819 -70.312 90.648   1.00 45.97  ? 476 GLN D NE2 1 
ATOM   16106 N N   . GLU D  1 477 ? -16.647 -68.096 90.754   1.00 56.69  ? 477 GLU D N   1 
ATOM   16107 C CA  . GLU D  1 477 ? -17.758 -67.711 91.583   1.00 63.63  ? 477 GLU D CA  1 
ATOM   16108 C C   . GLU D  1 477 ? -18.901 -67.263 90.727   1.00 64.52  ? 477 GLU D C   1 
ATOM   16109 O O   . GLU D  1 477 ? -18.721 -66.916 89.599   1.00 65.59  ? 477 GLU D O   1 
ATOM   16110 C CB  . GLU D  1 477 ? -17.377 -66.554 92.473   1.00 66.09  ? 477 GLU D CB  1 
ATOM   16111 C CG  . GLU D  1 477 ? -16.252 -66.792 93.456   1.00 68.22  ? 477 GLU D CG  1 
ATOM   16112 C CD  . GLU D  1 477 ? -15.898 -65.535 94.229   1.00 69.90  ? 477 GLU D CD  1 
ATOM   16113 O OE1 . GLU D  1 477 ? -14.932 -65.560 95.004   1.00 70.57  ? 477 GLU D OE1 1 
ATOM   16114 O OE2 . GLU D  1 477 ? -16.586 -64.519 94.059   1.00 70.40  ? 477 GLU D OE2 1 
HETATM 16115 C C1  . GLC E  2 .   ? -15.905 -22.052 25.551   1.00 20.00  ? 6   GLC E C1  1 
HETATM 16116 C C2  . GLC E  2 .   ? -17.265 -22.580 26.030   1.00 20.00  ? 6   GLC E C2  1 
HETATM 16117 C C3  . GLC E  2 .   ? -17.454 -23.962 25.422   1.00 20.00  ? 6   GLC E C3  1 
HETATM 16118 C C4  . GLC E  2 .   ? -17.482 -23.830 23.884   1.00 20.00  ? 6   GLC E C4  1 
HETATM 16119 C C5  . GLC E  2 .   ? -16.228 -23.025 23.436   1.00 20.00  ? 6   GLC E C5  1 
HETATM 16120 C C6  . GLC E  2 .   ? -16.190 -22.762 21.934   1.00 20.00  ? 6   GLC E C6  1 
HETATM 16121 O O2  . GLC E  2 .   ? -17.435 -22.634 27.367   1.00 20.00  ? 6   GLC E O2  1 
HETATM 16122 O O3  . GLC E  2 .   ? -18.589 -24.574 25.821   1.00 20.00  ? 6   GLC E O3  1 
HETATM 16123 O O4  . GLC E  2 .   ? -17.378 -25.033 23.328   1.00 20.00  ? 6   GLC E O4  1 
HETATM 16124 O O5  . GLC E  2 .   ? -16.140 -21.881 24.173   1.00 20.00  ? 6   GLC E O5  1 
HETATM 16125 O O6  . GLC E  2 .   ? -17.228 -22.114 21.529   1.00 20.00  ? 6   GLC E O6  1 
HETATM 16126 C C1  . GLC E  2 .   ? -18.281 -25.861 22.929   1.00 20.00  ? 7   GLC E C1  1 
HETATM 16127 C C2  . GLC E  2 .   ? -18.271 -27.260 23.453   1.00 20.00  ? 7   GLC E C2  1 
HETATM 16128 C C3  . GLC E  2 .   ? -17.353 -28.162 22.617   1.00 20.00  ? 7   GLC E C3  1 
HETATM 16129 C C4  . GLC E  2 .   ? -17.536 -27.910 21.096   1.00 20.00  ? 7   GLC E C4  1 
HETATM 16130 C C5  . GLC E  2 .   ? -17.624 -26.444 20.758   1.00 20.00  ? 7   GLC E C5  1 
HETATM 16131 C C6  . GLC E  2 .   ? -18.065 -26.122 19.316   1.00 20.00  ? 7   GLC E C6  1 
HETATM 16132 O O2  . GLC E  2 .   ? -18.222 -27.344 24.848   1.00 20.00  ? 7   GLC E O2  1 
HETATM 16133 O O3  . GLC E  2 .   ? -17.579 -29.435 22.839   1.00 20.00  ? 7   GLC E O3  1 
HETATM 16134 O O4  . GLC E  2 .   ? -16.561 -28.545 20.384   1.00 20.00  ? 7   GLC E O4  1 
HETATM 16135 O O5  . GLC E  2 .   ? -18.486 -25.846 21.592   1.00 20.00  ? 7   GLC E O5  1 
HETATM 16136 O O6  . GLC E  2 .   ? -18.367 -24.828 19.140   1.00 20.00  ? 7   GLC E O6  1 
HETATM 16137 C C1  . GLC E  2 .   ? -16.898 -29.419 19.399   1.00 25.25  ? 8   GLC E C1  1 
HETATM 16138 C C2  . GLC E  2 .   ? -16.206 -30.729 19.756   1.00 25.42  ? 8   GLC E C2  1 
HETATM 16139 C C3  . GLC E  2 .   ? -14.703 -30.511 19.712   1.00 20.62  ? 8   GLC E C3  1 
HETATM 16140 C C4  . GLC E  2 .   ? -14.355 -30.076 18.278   1.00 18.38  ? 8   GLC E C4  1 
HETATM 16141 C C5  . GLC E  2 .   ? -15.121 -28.785 17.914   1.00 17.26  ? 8   GLC E C5  1 
HETATM 16142 C C6  . GLC E  2 .   ? -14.854 -28.317 16.466   1.00 19.23  ? 8   GLC E C6  1 
HETATM 16143 O O2  . GLC E  2 .   ? -16.618 -31.221 21.014   1.00 27.17  ? 8   GLC E O2  1 
HETATM 16144 O O3  . GLC E  2 .   ? -14.029 -31.709 20.011   1.00 24.27  ? 8   GLC E O3  1 
HETATM 16145 O O4  . GLC E  2 .   ? -12.948 -29.877 18.181   1.00 26.83  ? 8   GLC E O4  1 
HETATM 16146 O O5  . GLC E  2 .   ? -16.526 -28.950 18.106   1.00 24.27  ? 8   GLC E O5  1 
HETATM 16147 O O6  . GLC E  2 .   ? -15.195 -29.356 15.571   1.00 21.72  ? 8   GLC E O6  1 
HETATM 16148 C C1  . GLC E  2 .   ? -12.326 -30.406 17.080   1.00 34.33  ? 1   GLC E C1  1 
HETATM 16149 C C2  . GLC E  2 .   ? -11.446 -31.531 17.491   1.00 34.86  ? 1   GLC E C2  1 
HETATM 16150 C C3  . GLC E  2 .   ? -10.209 -31.084 18.179   1.00 40.30  ? 1   GLC E C3  1 
HETATM 16151 C C4  . GLC E  2 .   ? -9.504  -30.020 17.377   1.00 47.94  ? 1   GLC E C4  1 
HETATM 16152 C C5  . GLC E  2 .   ? -10.444 -28.943 16.932   1.00 44.46  ? 1   GLC E C5  1 
HETATM 16153 C C6  . GLC E  2 .   ? -9.739  -27.930 16.063   1.00 54.64  ? 1   GLC E C6  1 
HETATM 16154 O O2  . GLC E  2 .   ? -12.081 -32.524 18.167   1.00 37.74  ? 1   GLC E O2  1 
HETATM 16155 O O3  . GLC E  2 .   ? -9.326  -32.124 18.473   1.00 42.49  ? 1   GLC E O3  1 
HETATM 16156 O O4  . GLC E  2 .   ? -8.490  -29.566 18.159   1.00 55.69  ? 1   GLC E O4  1 
HETATM 16157 O O5  . GLC E  2 .   ? -11.505 -29.641 16.285   1.00 37.41  ? 1   GLC E O5  1 
HETATM 16158 O O6  . GLC E  2 .   ? -8.482  -27.320 16.447   1.00 58.94  ? 1   GLC E O6  1 
HETATM 16159 C C1  . GLC E  2 .   ? -7.323  -30.243 17.834   1.00 64.10  ? 2   GLC E C1  1 
HETATM 16160 C C2  . GLC E  2 .   ? -6.630  -30.831 19.036   1.00 70.37  ? 2   GLC E C2  1 
HETATM 16161 C C3  . GLC E  2 .   ? -5.995  -29.747 19.943   1.00 72.96  ? 2   GLC E C3  1 
HETATM 16162 C C4  . GLC E  2 .   ? -5.441  -28.545 19.185   1.00 73.64  ? 2   GLC E C4  1 
HETATM 16163 C C5  . GLC E  2 .   ? -6.376  -28.224 18.018   1.00 67.93  ? 2   GLC E C5  1 
HETATM 16164 C C6  . GLC E  2 .   ? -6.157  -26.988 17.281   1.00 65.79  ? 2   GLC E C6  1 
HETATM 16165 O O2  . GLC E  2 .   ? -7.618  -31.435 19.732   1.00 71.58  ? 2   GLC E O2  1 
HETATM 16166 O O3  . GLC E  2 .   ? -5.069  -30.293 20.893   1.00 72.53  ? 2   GLC E O3  1 
HETATM 16167 O O4  . GLC E  2 .   ? -5.526  -27.481 20.115   1.00 79.47  ? 2   GLC E O4  1 
HETATM 16168 O O5  . GLC E  2 .   ? -6.421  -29.386 17.226   1.00 66.70  ? 2   GLC E O5  1 
HETATM 16169 O O6  . GLC E  2 .   ? -5.873  -26.058 18.266   1.00 66.54  ? 2   GLC E O6  1 
HETATM 16170 C C1  . GLC E  2 .   ? -4.407  -26.685 20.488   1.00 80.64  ? 3   GLC E C1  1 
HETATM 16171 C C2  . GLC E  2 .   ? -3.951  -27.064 21.935   1.00 79.98  ? 3   GLC E C2  1 
HETATM 16172 C C3  . GLC E  2 .   ? -4.944  -26.630 23.011   1.00 78.24  ? 3   GLC E C3  1 
HETATM 16173 C C4  . GLC E  2 .   ? -5.322  -25.225 22.846   1.00 77.03  ? 3   GLC E C4  1 
HETATM 16174 C C5  . GLC E  2 .   ? -5.534  -24.772 21.384   1.00 79.61  ? 3   GLC E C5  1 
HETATM 16175 C C6  . GLC E  2 .   ? -5.566  -23.244 21.408   1.00 81.24  ? 3   GLC E C6  1 
HETATM 16176 O O2  . GLC E  2 .   ? -3.591  -28.421 22.129   1.00 80.04  ? 3   GLC E O2  1 
HETATM 16177 O O3  . GLC E  2 .   ? -4.422  -26.522 24.327   1.00 78.61  ? 3   GLC E O3  1 
HETATM 16178 O O4  . GLC E  2 .   ? -6.552  -25.111 23.603   1.00 72.63  ? 3   GLC E O4  1 
HETATM 16179 O O5  . GLC E  2 .   ? -4.669  -25.287 20.410   1.00 79.77  ? 3   GLC E O5  1 
HETATM 16180 O O6  . GLC E  2 .   ? -4.456  -22.761 22.214   1.00 80.66  ? 3   GLC E O6  1 
HETATM 16181 C C1  . GLC E  2 .   ? -6.504  -24.518 24.863   1.00 68.51  ? 4   GLC E C1  1 
HETATM 16182 C C2  . GLC E  2 .   ? -7.497  -25.389 25.660   1.00 65.76  ? 4   GLC E C2  1 
HETATM 16183 C C3  . GLC E  2 .   ? -8.954  -24.904 25.635   1.00 60.11  ? 4   GLC E C3  1 
HETATM 16184 C C4  . GLC E  2 .   ? -9.071  -23.382 25.680   1.00 56.34  ? 4   GLC E C4  1 
HETATM 16185 C C5  . GLC E  2 .   ? -8.160  -22.847 24.580   1.00 60.97  ? 4   GLC E C5  1 
HETATM 16186 C C6  . GLC E  2 .   ? -8.240  -21.349 24.342   1.00 59.58  ? 4   GLC E C6  1 
HETATM 16187 O O2  . GLC E  2 .   ? -7.417  -26.722 25.193   1.00 66.16  ? 4   GLC E O2  1 
HETATM 16188 O O3  . GLC E  2 .   ? -9.656  -25.454 26.727   1.00 60.86  ? 4   GLC E O3  1 
HETATM 16189 O O4  . GLC E  2 .   ? -10.430 -22.986 25.539   1.00 45.21  ? 4   GLC E O4  1 
HETATM 16190 O O5  . GLC E  2 .   ? -6.841  -23.142 24.966   1.00 66.29  ? 4   GLC E O5  1 
HETATM 16191 O O6  . GLC E  2 .   ? -7.448  -21.080 23.210   1.00 60.60  ? 4   GLC E O6  1 
HETATM 16192 C C1  . GLC E  2 .   ? -10.799 -22.009 26.548   1.00 38.84  ? 5   GLC E C1  1 
HETATM 16193 C C2  . GLC E  2 .   ? -11.608 -22.672 27.659   1.00 34.62  ? 5   GLC E C2  1 
HETATM 16194 C C3  . GLC E  2 .   ? -12.977 -23.096 27.152   1.00 31.05  ? 5   GLC E C3  1 
HETATM 16195 C C4  . GLC E  2 .   ? -13.731 -22.001 26.401   1.00 25.89  ? 5   GLC E C4  1 
HETATM 16196 C C5  . GLC E  2 .   ? -12.793 -21.384 25.349   1.00 29.61  ? 5   GLC E C5  1 
HETATM 16197 C C6  . GLC E  2 .   ? -13.331 -20.112 24.697   1.00 32.15  ? 5   GLC E C6  1 
HETATM 16198 O O2  . GLC E  2 .   ? -10.909 -23.811 28.084   1.00 37.36  ? 5   GLC E O2  1 
HETATM 16199 O O3  . GLC E  2 .   ? -13.784 -23.582 28.211   1.00 25.95  ? 5   GLC E O3  1 
HETATM 16200 O O4  . GLC E  2 .   ? -14.859 -22.705 25.897   1.00 24.16  ? 5   GLC E O4  1 
HETATM 16201 O O5  . GLC E  2 .   ? -11.597 -20.974 25.992   1.00 35.68  ? 5   GLC E O5  1 
HETATM 16202 O O6  . GLC E  2 .   ? -13.336 -19.069 25.644   1.00 36.42  ? 5   GLC E O6  1 
HETATM 16203 C C1  . GLC F  2 .   ? -20.933 -41.907 -22.948  1.00 16.81  ? 6   GLC F C1  1 
HETATM 16204 C C2  . GLC F  2 .   ? -22.281 -41.231 -23.247  1.00 17.78  ? 6   GLC F C2  1 
HETATM 16205 C C3  . GLC F  2 .   ? -22.185 -39.824 -22.637  1.00 19.84  ? 6   GLC F C3  1 
HETATM 16206 C C4  . GLC F  2 .   ? -21.821 -39.900 -21.131  1.00 18.30  ? 6   GLC F C4  1 
HETATM 16207 C C5  . GLC F  2 .   ? -20.572 -40.766 -20.893  1.00 20.46  ? 6   GLC F C5  1 
HETATM 16208 C C6  . GLC F  2 .   ? -20.257 -41.001 -19.399  1.00 24.86  ? 6   GLC F C6  1 
HETATM 16209 O O2  . GLC F  2 .   ? -22.481 -41.228 -24.677  1.00 21.90  ? 6   GLC F O2  1 
HETATM 16210 O O3  . GLC F  2 .   ? -23.376 -39.050 -22.792  1.00 20.75  ? 6   GLC F O3  1 
HETATM 16211 O O4  . GLC F  2 .   ? -21.566 -38.588 -20.676  1.00 19.78  ? 6   GLC F O4  1 
HETATM 16212 O O5  . GLC F  2 .   ? -20.735 -42.015 -21.543  1.00 17.19  ? 6   GLC F O5  1 
HETATM 16213 O O6  . GLC F  2 .   ? -21.204 -41.908 -18.877  1.00 23.80  ? 6   GLC F O6  1 
HETATM 16214 C C1  . GLC F  2 .   ? -22.702 -37.950 -20.049  1.00 23.58  ? 7   GLC F C1  1 
HETATM 16215 C C2  . GLC F  2 .   ? -22.690 -36.482 -20.471  1.00 22.32  ? 7   GLC F C2  1 
HETATM 16216 C C3  . GLC F  2 .   ? -21.421 -35.823 -19.954  1.00 20.85  ? 7   GLC F C3  1 
HETATM 16217 C C4  . GLC F  2 .   ? -21.332 -36.040 -18.436  1.00 21.99  ? 7   GLC F C4  1 
HETATM 16218 C C5  . GLC F  2 .   ? -21.443 -37.523 -18.084  1.00 20.55  ? 7   GLC F C5  1 
HETATM 16219 C C6  . GLC F  2 .   ? -21.512 -37.762 -16.563  1.00 21.89  ? 7   GLC F C6  1 
HETATM 16220 O O2  . GLC F  2 .   ? -22.808 -36.395 -21.890  1.00 25.02  ? 7   GLC F O2  1 
HETATM 16221 O O3  . GLC F  2 .   ? -21.445 -34.427 -20.191  1.00 23.70  ? 7   GLC F O3  1 
HETATM 16222 O O4  . GLC F  2 .   ? -20.108 -35.496 -17.981  1.00 27.35  ? 7   GLC F O4  1 
HETATM 16223 O O5  . GLC F  2 .   ? -22.643 -38.037 -18.633  1.00 27.79  ? 7   GLC F O5  1 
HETATM 16224 O O6  . GLC F  2 .   ? -21.676 -39.149 -16.407  1.00 24.79  ? 7   GLC F O6  1 
HETATM 16225 C C1  . GLC F  2 .   ? -20.285 -34.505 -16.954  1.00 27.94  ? 8   GLC F C1  1 
HETATM 16226 C C2  . GLC F  2 .   ? -19.650 -33.176 -17.334  1.00 27.99  ? 8   GLC F C2  1 
HETATM 16227 C C3  . GLC F  2 .   ? -18.172 -33.396 -17.525  1.00 26.14  ? 8   GLC F C3  1 
HETATM 16228 C C4  . GLC F  2 .   ? -17.603 -33.886 -16.203  1.00 22.58  ? 8   GLC F C4  1 
HETATM 16229 C C5  . GLC F  2 .   ? -18.341 -35.139 -15.766  1.00 24.17  ? 8   GLC F C5  1 
HETATM 16230 C C6  . GLC F  2 .   ? -17.877 -35.640 -14.397  1.00 27.81  ? 8   GLC F C6  1 
HETATM 16231 O O2  . GLC F  2 .   ? -20.223 -32.659 -18.520  1.00 30.23  ? 8   GLC F O2  1 
HETATM 16232 O O3  . GLC F  2 .   ? -17.576 -32.179 -17.883  1.00 25.13  ? 8   GLC F O3  1 
HETATM 16233 O O4  . GLC F  2 .   ? -16.220 -34.134 -16.362  1.00 28.57  ? 8   GLC F O4  1 
HETATM 16234 O O5  . GLC F  2 .   ? -19.733 -34.882 -15.712  1.00 28.02  ? 8   GLC F O5  1 
HETATM 16235 O O6  . GLC F  2 .   ? -17.916 -34.624 -13.422  1.00 30.25  ? 8   GLC F O6  1 
HETATM 16236 C C1  . GLC F  2 .   ? -15.454 -33.391 -15.416  1.00 40.73  ? 1   GLC F C1  1 
HETATM 16237 C C2  . GLC F  2 .   ? -14.407 -32.494 -16.062  1.00 45.09  ? 1   GLC F C2  1 
HETATM 16238 C C3  . GLC F  2 .   ? -13.343 -33.314 -16.756  1.00 52.24  ? 1   GLC F C3  1 
HETATM 16239 C C4  . GLC F  2 .   ? -12.813 -34.331 -15.757  1.00 60.46  ? 1   GLC F C4  1 
HETATM 16240 C C5  . GLC F  2 .   ? -13.976 -35.145 -15.243  1.00 54.74  ? 1   GLC F C5  1 
HETATM 16241 C C6  . GLC F  2 .   ? -13.542 -36.260 -14.328  1.00 58.33  ? 1   GLC F C6  1 
HETATM 16242 O O2  . GLC F  2 .   ? -15.061 -31.651 -16.990  1.00 45.85  ? 1   GLC F O2  1 
HETATM 16243 O O3  . GLC F  2 .   ? -12.302 -32.457 -17.240  1.00 49.73  ? 1   GLC F O3  1 
HETATM 16244 O O4  . GLC F  2 .   ? -11.873 -35.208 -16.362  1.00 70.80  ? 1   GLC F O4  1 
HETATM 16245 O O5  . GLC F  2 .   ? -14.804 -34.257 -14.524  1.00 49.31  ? 1   GLC F O5  1 
HETATM 16246 O O6  . GLC F  2 .   ? -13.407 -35.746 -13.014  1.00 62.75  ? 1   GLC F O6  1 
HETATM 16247 C C1  . GLC F  2 .   ? -10.627 -35.233 -15.633  1.00 76.90  ? 2   GLC F C1  1 
HETATM 16248 C C2  . GLC F  2 .   ? -9.552  -34.965 -16.638  1.00 82.79  ? 2   GLC F C2  1 
HETATM 16249 C C3  . GLC F  2 .   ? -9.676  -35.989 -17.763  1.00 83.98  ? 2   GLC F C3  1 
HETATM 16250 C C4  . GLC F  2 .   ? -9.573  -37.405 -17.234  1.00 82.14  ? 2   GLC F C4  1 
HETATM 16251 C C5  . GLC F  2 .   ? -10.582 -37.538 -16.105  1.00 80.09  ? 2   GLC F C5  1 
HETATM 16252 C C6  . GLC F  2 .   ? -10.584 -38.907 -15.416  1.00 80.17  ? 2   GLC F C6  1 
HETATM 16253 O O2  . GLC F  2 .   ? -9.766  -33.641 -17.118  1.00 85.06  ? 2   GLC F O2  1 
HETATM 16254 O O3  . GLC F  2 .   ? -8.654  -35.790 -18.742  1.00 84.78  ? 2   GLC F O3  1 
HETATM 16255 O O4  . GLC F  2 .   ? -9.879  -38.273 -18.324  1.00 82.37  ? 2   GLC F O4  1 
HETATM 16256 O O5  . GLC F  2 .   ? -10.319 -36.520 -15.139  1.00 77.73  ? 2   GLC F O5  1 
HETATM 16257 O O6  . GLC F  2 .   ? -9.400  -39.133 -14.639  1.00 80.84  ? 2   GLC F O6  1 
HETATM 16258 C C1  . GLC F  2 .   ? -8.889  -39.281 -18.615  1.00 78.62  ? 3   GLC F C1  1 
HETATM 16259 C C2  . GLC F  2 .   ? -8.212  -38.930 -19.920  1.00 78.82  ? 3   GLC F C2  1 
HETATM 16260 C C3  . GLC F  2 .   ? -9.257  -38.757 -21.002  1.00 77.84  ? 3   GLC F C3  1 
HETATM 16261 C C4  . GLC F  2 .   ? -10.081 -40.011 -21.123  1.00 77.27  ? 3   GLC F C4  1 
HETATM 16262 C C5  . GLC F  2 .   ? -10.574 -40.458 -19.753  1.00 77.67  ? 3   GLC F C5  1 
HETATM 16263 C C6  . GLC F  2 .   ? -11.332 -41.785 -19.816  1.00 77.62  ? 3   GLC F C6  1 
HETATM 16264 O O2  . GLC F  2 .   ? -7.535  -37.697 -19.809  1.00 78.20  ? 3   GLC F O2  1 
HETATM 16265 O O3  . GLC F  2 .   ? -8.614  -38.459 -22.235  1.00 75.81  ? 3   GLC F O3  1 
HETATM 16266 O O4  . GLC F  2 .   ? -11.187 -39.605 -21.895  1.00 76.91  ? 3   GLC F O4  1 
HETATM 16267 O O5  . GLC F  2 .   ? -9.485  -40.550 -18.831  1.00 77.15  ? 3   GLC F O5  1 
HETATM 16268 O O6  . GLC F  2 .   ? -10.472 -42.924 -19.769  1.00 77.23  ? 3   GLC F O6  1 
HETATM 16269 C C1  . GLC F  2 .   ? -11.110 -39.962 -23.292  1.00 75.02  ? 4   GLC F C1  1 
HETATM 16270 C C2  . GLC F  2 .   ? -12.035 -39.004 -24.054  1.00 73.63  ? 4   GLC F C2  1 
HETATM 16271 C C3  . GLC F  2 .   ? -13.504 -39.343 -23.787  1.00 71.27  ? 4   GLC F C3  1 
HETATM 16272 C C4  . GLC F  2 .   ? -13.781 -40.837 -24.013  1.00 65.09  ? 4   GLC F C4  1 
HETATM 16273 C C5  . GLC F  2 .   ? -12.764 -41.604 -23.154  1.00 69.35  ? 4   GLC F C5  1 
HETATM 16274 C C6  . GLC F  2 .   ? -12.885 -43.123 -23.097  1.00 73.48  ? 4   GLC F C6  1 
HETATM 16275 O O2  . GLC F  2 .   ? -11.761 -37.673 -23.675  1.00 74.44  ? 4   GLC F O2  1 
HETATM 16276 O O3  . GLC F  2 .   ? -14.357 -38.528 -24.570  1.00 71.64  ? 4   GLC F O3  1 
HETATM 16277 O O4  . GLC F  2 .   ? -15.141 -41.105 -23.702  1.00 54.48  ? 4   GLC F O4  1 
HETATM 16278 O O5  . GLC F  2 .   ? -11.467 -41.293 -23.619  1.00 71.10  ? 4   GLC F O5  1 
HETATM 16279 O O6  . GLC F  2 .   ? -11.811 -43.616 -22.319  1.00 76.53  ? 4   GLC F O6  1 
HETATM 16280 C C1  . GLC F  2 .   ? -15.784 -42.022 -24.635  1.00 49.24  ? 5   GLC F C1  1 
HETATM 16281 C C2  . GLC F  2 .   ? -16.710 -41.277 -25.609  1.00 48.54  ? 5   GLC F C2  1 
HETATM 16282 C C3  . GLC F  2 .   ? -17.973 -40.763 -24.921  1.00 46.90  ? 5   GLC F C3  1 
HETATM 16283 C C4  . GLC F  2 .   ? -18.748 -41.835 -24.148  1.00 39.78  ? 5   GLC F C4  1 
HETATM 16284 C C5  . GLC F  2 .   ? -17.746 -42.573 -23.241  1.00 41.70  ? 5   GLC F C5  1 
HETATM 16285 C C6  . GLC F  2 .   ? -18.306 -43.851 -22.620  1.00 43.57  ? 5   GLC F C6  1 
HETATM 16286 O O2  . GLC F  2 .   ? -16.026 -40.201 -26.222  1.00 42.51  ? 5   GLC F O2  1 
HETATM 16287 O O3  . GLC F  2 .   ? -18.808 -40.204 -25.910  1.00 48.78  ? 5   GLC F O3  1 
HETATM 16288 O O4  . GLC F  2 .   ? -19.836 -41.144 -23.519  1.00 27.78  ? 5   GLC F O4  1 
HETATM 16289 O O5  . GLC F  2 .   ? -16.591 -42.995 -23.970  1.00 46.15  ? 5   GLC F O5  1 
HETATM 16290 O O6  . GLC F  2 .   ? -18.256 -44.920 -23.540  1.00 41.21  ? 5   GLC F O6  1 
HETATM 16291 C C1  . GLC G  2 .   ? -1.551  -5.758  -69.750  1.00 32.99  ? 6   GLC G C1  1 
HETATM 16292 C C2  . GLC G  2 .   ? -2.873  -6.442  -69.410  1.00 26.79  ? 6   GLC G C2  1 
HETATM 16293 C C3  . GLC G  2 .   ? -2.993  -7.724  -70.224  1.00 26.87  ? 6   GLC G C3  1 
HETATM 16294 C C4  . GLC G  2 .   ? -2.885  -7.410  -71.725  1.00 22.94  ? 6   GLC G C4  1 
HETATM 16295 C C5  . GLC G  2 .   ? -1.639  -6.572  -71.987  1.00 26.57  ? 6   GLC G C5  1 
HETATM 16296 C C6  . GLC G  2 .   ? -1.613  -6.169  -73.469  1.00 24.56  ? 6   GLC G C6  1 
HETATM 16297 O O2  . GLC G  2 .   ? -3.004  -6.717  -68.028  1.00 23.26  ? 6   GLC G O2  1 
HETATM 16298 O O3  . GLC G  2 .   ? -4.227  -8.355  -69.948  1.00 25.67  ? 6   GLC G O3  1 
HETATM 16299 O O4  . GLC G  2 .   ? -2.691  -8.629  -72.399  1.00 24.58  ? 6   GLC G O4  1 
HETATM 16300 O O5  . GLC G  2 .   ? -1.580  -5.430  -71.135  1.00 30.00  ? 6   GLC G O5  1 
HETATM 16301 O O6  . GLC G  2 .   ? -2.507  -5.088  -73.688  1.00 26.56  ? 6   GLC G O6  1 
HETATM 16302 C C1  . GLC G  2 .   ? -3.906  -9.210  -72.888  1.00 22.95  ? 7   GLC G C1  1 
HETATM 16303 C C2  . GLC G  2 .   ? -3.866  -10.725 -72.643  1.00 23.66  ? 7   GLC G C2  1 
HETATM 16304 C C3  . GLC G  2 .   ? -2.745  -11.357 -73.449  1.00 21.69  ? 7   GLC G C3  1 
HETATM 16305 C C4  . GLC G  2 .   ? -2.852  -10.933 -74.924  1.00 23.87  ? 7   GLC G C4  1 
HETATM 16306 C C5  . GLC G  2 .   ? -2.911  -9.402  -75.021  1.00 21.31  ? 7   GLC G C5  1 
HETATM 16307 C C6  . GLC G  2 .   ? -3.085  -8.920  -76.467  1.00 24.71  ? 7   GLC G C6  1 
HETATM 16308 O O2  . GLC G  2 .   ? -3.779  -11.036 -71.249  1.00 23.76  ? 7   GLC G O2  1 
HETATM 16309 O O3  . GLC G  2 .   ? -2.784  -12.772 -73.329  1.00 22.62  ? 7   GLC G O3  1 
HETATM 16310 O O4  . GLC G  2 .   ? -1.694  -11.400 -75.580  1.00 27.05  ? 7   GLC G O4  1 
HETATM 16311 O O5  . GLC G  2 .   ? -4.032  -8.965  -74.272  1.00 27.04  ? 7   GLC G O5  1 
HETATM 16312 O O6  . GLC G  2 .   ? -3.344  -7.539  -76.506  1.00 24.26  ? 7   GLC G O6  1 
HETATM 16313 C C1  . GLC G  2 .   ? -1.993  -12.241 -76.711  1.00 27.32  ? 8   GLC G C1  1 
HETATM 16314 C C2  . GLC G  2 .   ? -1.338  -13.609 -76.506  1.00 30.67  ? 8   GLC G C2  1 
HETATM 16315 C C3  . GLC G  2 .   ? 0.180   -13.487 -76.503  1.00 30.32  ? 8   GLC G C3  1 
HETATM 16316 C C4  . GLC G  2 .   ? 0.625   -12.787 -77.789  1.00 24.67  ? 8   GLC G C4  1 
HETATM 16317 C C5  . GLC G  2 .   ? -0.095  -11.450 -77.963  1.00 23.15  ? 8   GLC G C5  1 
HETATM 16318 C C6  . GLC G  2 .   ? 0.277   -10.759 -79.294  1.00 28.34  ? 8   GLC G C6  1 
HETATM 16319 O O2  . GLC G  2 .   ? -1.765  -14.191 -75.305  1.00 34.94  ? 8   GLC G O2  1 
HETATM 16320 O O3  . GLC G  2 .   ? 0.788   -14.757 -76.397  1.00 34.00  ? 8   GLC G O3  1 
HETATM 16321 O O4  . GLC G  2 .   ? 2.026   -12.621 -77.768  1.00 29.71  ? 8   GLC G O4  1 
HETATM 16322 O O5  . GLC G  2 .   ? -1.500  -11.658 -77.914  1.00 24.41  ? 8   GLC G O5  1 
HETATM 16323 O O6  . GLC G  2 .   ? -0.160  -11.505 -80.426  1.00 31.68  ? 8   GLC G O6  1 
HETATM 16324 C C1  . GLC G  2 .   ? 2.585   -13.410 -78.845  1.00 45.67  ? 1   GLC G C1  1 
HETATM 16325 C C2  . GLC G  2 .   ? 3.812   -14.190 -78.372  1.00 52.99  ? 1   GLC G C2  1 
HETATM 16326 C C3  . GLC G  2 .   ? 4.907   -13.232 -77.909  1.00 58.68  ? 1   GLC G C3  1 
HETATM 16327 C C4  . GLC G  2 .   ? 5.183   -12.147 -78.960  1.00 58.22  ? 1   GLC G C4  1 
HETATM 16328 C C5  . GLC G  2 .   ? 3.876   -11.542 -79.491  1.00 54.08  ? 1   GLC G C5  1 
HETATM 16329 C C6  . GLC G  2 .   ? 4.049   -10.581 -80.674  1.00 54.33  ? 1   GLC G C6  1 
HETATM 16330 O O2  . GLC G  2 .   ? 3.454   -15.101 -77.354  1.00 51.99  ? 1   GLC G O2  1 
HETATM 16331 O O3  . GLC G  2 .   ? 6.081   -13.968 -77.615  1.00 61.66  ? 1   GLC G O3  1 
HETATM 16332 O O4  . GLC G  2 .   ? 6.014   -11.157 -78.376  1.00 62.21  ? 1   GLC G O4  1 
HETATM 16333 O O5  . GLC G  2 .   ? 3.001   -12.571 -79.902  1.00 48.69  ? 1   GLC G O5  1 
HETATM 16334 O O6  . GLC G  2 .   ? 4.624   -11.238 -81.785  1.00 48.46  ? 1   GLC G O6  1 
HETATM 16335 C C1  . GLC G  2 .   ? 7.209   -10.935 -79.176  1.00 65.29  ? 2   GLC G C1  1 
HETATM 16336 C C2  . GLC G  2 .   ? 8.409   -11.729 -78.632  1.00 63.54  ? 2   GLC G C2  1 
HETATM 16337 C C3  . GLC G  2 .   ? 8.909   -11.204 -77.294  1.00 63.72  ? 2   GLC G C3  1 
HETATM 16338 C C4  . GLC G  2 .   ? 8.984   -9.686  -77.238  1.00 65.40  ? 2   GLC G C4  1 
HETATM 16339 C C5  . GLC G  2 .   ? 7.745   -9.057  -77.871  1.00 66.65  ? 2   GLC G C5  1 
HETATM 16340 C C6  . GLC G  2 .   ? 7.778   -7.526  -77.880  1.00 67.28  ? 2   GLC G C6  1 
HETATM 16341 O O2  . GLC G  2 .   ? 8.089   -13.090 -78.460  1.00 63.16  ? 2   GLC G O2  1 
HETATM 16342 O O3  . GLC G  2 .   ? 10.178  -11.752 -77.019  1.00 63.02  ? 2   GLC G O3  1 
HETATM 16343 O O4  . GLC G  2 .   ? 8.963   -9.387  -75.873  1.00 69.76  ? 2   GLC G O4  1 
HETATM 16344 O O5  . GLC G  2 .   ? 7.568   -9.561  -79.179  1.00 66.38  ? 2   GLC G O5  1 
HETATM 16345 O O6  . GLC G  2 .   ? 8.051   -7.042  -79.177  1.00 67.89  ? 2   GLC G O6  1 
HETATM 16346 C C1  . GLC G  2 .   ? 10.063  -8.573  -75.457  1.00 72.28  ? 3   GLC G C1  1 
HETATM 16347 C C2  . GLC G  2 .   ? 10.734  -9.226  -74.253  1.00 74.02  ? 3   GLC G C2  1 
HETATM 16348 C C3  . GLC G  2 .   ? 9.680   -9.480  -73.177  1.00 73.23  ? 3   GLC G C3  1 
HETATM 16349 C C4  . GLC G  2 .   ? 8.875   -8.204  -72.897  1.00 71.95  ? 3   GLC G C4  1 
HETATM 16350 C C5  . GLC G  2 .   ? 8.477   -7.459  -74.188  1.00 72.50  ? 3   GLC G C5  1 
HETATM 16351 C C6  . GLC G  2 .   ? 7.872   -6.092  -73.877  1.00 71.85  ? 3   GLC G C6  1 
HETATM 16352 O O2  . GLC G  2 .   ? 11.366  -10.446 -74.593  1.00 73.35  ? 3   GLC G O2  1 
HETATM 16353 O O3  . GLC G  2 .   ? 10.295  -9.990  -72.005  1.00 72.58  ? 3   GLC G O3  1 
HETATM 16354 O O4  . GLC G  2 .   ? 7.711   -8.522  -72.150  1.00 70.08  ? 3   GLC G O4  1 
HETATM 16355 O O5  . GLC G  2 .   ? 9.566   -7.312  -75.090  1.00 71.35  ? 3   GLC G O5  1 
HETATM 16356 O O6  . GLC G  2 .   ? 8.658   -5.453  -72.898  1.00 72.18  ? 3   GLC G O6  1 
HETATM 16357 C C1  . GLC G  2 .   ? 7.900   -8.160  -70.753  1.00 66.32  ? 4   GLC G C1  1 
HETATM 16358 C C2  . GLC G  2 .   ? 7.080   -9.115  -69.869  1.00 66.39  ? 4   GLC G C2  1 
HETATM 16359 C C3  . GLC G  2 .   ? 5.579   -8.799  -69.884  1.00 60.08  ? 4   GLC G C3  1 
HETATM 16360 C C4  . GLC G  2 .   ? 5.346   -7.330  -69.551  1.00 53.74  ? 4   GLC G C4  1 
HETATM 16361 C C5  . GLC G  2 .   ? 6.116   -6.545  -70.613  1.00 58.30  ? 4   GLC G C5  1 
HETATM 16362 C C6  . GLC G  2 .   ? 5.959   -5.039  -70.511  1.00 60.57  ? 4   GLC G C6  1 
HETATM 16363 O O2  . GLC G  2 .   ? 7.312   -10.438 -70.303  1.00 69.30  ? 4   GLC G O2  1 
HETATM 16364 O O3  . GLC G  2 .   ? 4.857   -9.630  -69.000  1.00 58.87  ? 4   GLC G O3  1 
HETATM 16365 O O4  . GLC G  2 .   ? 3.951   -7.058  -69.526  1.00 45.21  ? 4   GLC G O4  1 
HETATM 16366 O O5  . GLC G  2 .   ? 7.499   -6.819  -70.490  1.00 62.35  ? 4   GLC G O5  1 
HETATM 16367 O O6  . GLC G  2 .   ? 6.824   -4.568  -69.512  1.00 63.51  ? 4   GLC G O6  1 
HETATM 16368 C C1  . GLC G  2 .   ? 3.575   -6.262  -68.368  1.00 41.24  ? 5   GLC G C1  1 
HETATM 16369 C C2  . GLC G  2 .   ? 2.647   -7.041  -67.436  1.00 37.81  ? 5   GLC G C2  1 
HETATM 16370 C C3  . GLC G  2 .   ? 1.312   -7.315  -68.116  1.00 36.17  ? 5   GLC G C3  1 
HETATM 16371 C C4  . GLC G  2 .   ? 0.625   -6.071  -68.677  1.00 38.10  ? 5   GLC G C4  1 
HETATM 16372 C C5  . GLC G  2 .   ? 1.655   -5.237  -69.465  1.00 43.40  ? 5   GLC G C5  1 
HETATM 16373 C C6  . GLC G  2 .   ? 1.203   -3.814  -69.801  1.00 43.74  ? 5   GLC G C6  1 
HETATM 16374 O O2  . GLC G  2 .   ? 3.265   -8.260  -67.098  1.00 40.14  ? 5   GLC G O2  1 
HETATM 16375 O O3  . GLC G  2 .   ? 0.420   -7.977  -67.250  1.00 32.55  ? 5   GLC G O3  1 
HETATM 16376 O O4  . GLC G  2 .   ? -0.443  -6.635  -69.438  1.00 35.33  ? 5   GLC G O4  1 
HETATM 16377 O O5  . GLC G  2 .   ? 2.880   -5.083  -68.753  1.00 45.36  ? 5   GLC G O5  1 
HETATM 16378 O O6  . GLC G  2 .   ? 0.958   -3.076  -68.620  1.00 47.74  ? 5   GLC G O6  1 
HETATM 16379 C C1  . GLC H  2 .   ? 3.379   -57.986 73.526   1.00 24.18  ? 6   GLC H C1  1 
HETATM 16380 C C2  . GLC H  2 .   ? 2.098   -57.307 73.084   1.00 18.90  ? 6   GLC H C2  1 
HETATM 16381 C C3  . GLC H  2 .   ? 1.939   -56.015 73.882   1.00 21.27  ? 6   GLC H C3  1 
HETATM 16382 C C4  . GLC H  2 .   ? 2.020   -56.263 75.403   1.00 22.04  ? 6   GLC H C4  1 
HETATM 16383 C C5  . GLC H  2 .   ? 3.213   -57.155 75.748   1.00 21.93  ? 6   GLC H C5  1 
HETATM 16384 C C6  . GLC H  2 .   ? 3.176   -57.601 77.219   1.00 22.32  ? 6   GLC H C6  1 
HETATM 16385 O O2  . GLC H  2 .   ? 2.237   -57.019 71.704   1.00 22.51  ? 6   GLC H O2  1 
HETATM 16386 O O3  . GLC H  2 .   ? 0.727   -55.356 73.567   1.00 21.76  ? 6   GLC H O3  1 
HETATM 16387 O O4  . GLC H  2 .   ? 2.149   -54.994 75.997   1.00 24.34  ? 6   GLC H O4  1 
HETATM 16388 O O5  . GLC H  2 .   ? 3.229   -58.303 74.903   1.00 27.90  ? 6   GLC H O5  1 
HETATM 16389 O O6  . GLC H  2 .   ? 2.098   -58.506 77.423   1.00 23.14  ? 6   GLC H O6  1 
HETATM 16390 C C1  . GLC H  2 .   ? 0.898   -54.518 76.557   1.00 28.35  ? 7   GLC H C1  1 
HETATM 16391 C C2  . GLC H  2 .   ? 0.870   -52.984 76.399   1.00 21.87  ? 7   GLC H C2  1 
HETATM 16392 C C3  . GLC H  2 .   ? 1.959   -52.356 77.264   1.00 23.15  ? 7   GLC H C3  1 
HETATM 16393 C C4  . GLC H  2 .   ? 1.846   -52.835 78.724   1.00 23.85  ? 7   GLC H C4  1 
HETATM 16394 C C5  . GLC H  2 .   ? 1.761   -54.373 78.780   1.00 24.38  ? 7   GLC H C5  1 
HETATM 16395 C C6  . GLC H  2 .   ? 1.488   -54.911 80.209   1.00 22.59  ? 7   GLC H C6  1 
HETATM 16396 O O2  . GLC H  2 .   ? 1.015   -52.590 75.023   1.00 21.23  ? 7   GLC H O2  1 
HETATM 16397 O O3  . GLC H  2 .   ? 1.876   -50.951 77.162   1.00 25.26  ? 7   GLC H O3  1 
HETATM 16398 O O4  . GLC H  2 .   ? 2.976   -52.376 79.465   1.00 25.66  ? 7   GLC H O4  1 
HETATM 16399 O O5  . GLC H  2 .   ? 0.733   -54.853 77.935   1.00 28.43  ? 7   GLC H O5  1 
HETATM 16400 O O6  . GLC H  2 .   ? 1.244   -56.321 80.210   1.00 22.36  ? 7   GLC H O6  1 
HETATM 16401 C C1  . GLC H  2 .   ? 2.559   -51.614 80.625   1.00 27.45  ? 8   GLC H C1  1 
HETATM 16402 C C2  . GLC H  2 .   ? 3.165   -50.208 80.589   1.00 26.14  ? 8   GLC H C2  1 
HETATM 16403 C C3  . GLC H  2 .   ? 4.679   -50.288 80.601   1.00 26.21  ? 8   GLC H C3  1 
HETATM 16404 C C4  . GLC H  2 .   ? 5.114   -51.023 81.870   1.00 26.99  ? 8   GLC H C4  1 
HETATM 16405 C C5  . GLC H  2 .   ? 4.388   -52.367 81.996   1.00 25.24  ? 8   GLC H C5  1 
HETATM 16406 C C6  . GLC H  2 .   ? 4.625   -53.014 83.374   1.00 26.27  ? 8   GLC H C6  1 
HETATM 16407 O O2  . GLC H  2 .   ? 2.730   -49.473 79.481   1.00 24.65  ? 8   GLC H O2  1 
HETATM 16408 O O3  . GLC H  2 .   ? 5.222   -48.983 80.570   1.00 27.47  ? 8   GLC H O3  1 
HETATM 16409 O O4  . GLC H  2 .   ? 6.523   -51.195 81.851   1.00 31.09  ? 8   GLC H O4  1 
HETATM 16410 O O5  . GLC H  2 .   ? 2.985   -52.234 81.832   1.00 20.97  ? 8   GLC H O5  1 
HETATM 16411 O O6  . GLC H  2 .   ? 4.078   -52.185 84.394   1.00 25.26  ? 8   GLC H O6  1 
HETATM 16412 C C1  . GLC H  2 .   ? 7.061   -50.603 83.072   1.00 38.37  ? 1   GLC H C1  1 
HETATM 16413 C C2  . GLC H  2 .   ? 8.098   -49.514 82.785   1.00 41.52  ? 1   GLC H C2  1 
HETATM 16414 C C3  . GLC H  2 .   ? 9.341   -50.100 82.120   1.00 44.03  ? 1   GLC H C3  1 
HETATM 16415 C C4  . GLC H  2 .   ? 9.914   -51.263 82.929   1.00 47.49  ? 1   GLC H C4  1 
HETATM 16416 C C5  . GLC H  2 .   ? 8.826   -52.263 83.332   1.00 43.51  ? 1   GLC H C5  1 
HETATM 16417 C C6  . GLC H  2 .   ? 9.282   -53.198 84.457   1.00 49.70  ? 1   GLC H C6  1 
HETATM 16418 O O2  . GLC H  2 .   ? 7.499   -48.495 82.010   1.00 44.83  ? 1   GLC H O2  1 
HETATM 16419 O O3  . GLC H  2 .   ? 10.331  -49.099 81.984   1.00 43.87  ? 1   GLC H O3  1 
HETATM 16420 O O4  . GLC H  2 .   ? 10.913  -51.891 82.148   1.00 57.43  ? 1   GLC H O4  1 
HETATM 16421 O O5  . GLC H  2 .   ? 7.693   -51.605 83.857   1.00 40.16  ? 1   GLC H O5  1 
HETATM 16422 O O6  . GLC H  2 .   ? 9.067   -52.633 85.738   1.00 47.09  ? 1   GLC H O6  1 
HETATM 16423 C C1  . GLC H  2 .   ? 12.158  -52.074 82.869   1.00 64.85  ? 2   GLC H C1  1 
HETATM 16424 C C2  . GLC H  2 .   ? 13.374  -51.987 81.919   1.00 70.42  ? 2   GLC H C2  1 
HETATM 16425 C C3  . GLC H  2 .   ? 14.154  -53.304 81.770   1.00 70.33  ? 2   GLC H C3  1 
HETATM 16426 C C4  . GLC H  2 .   ? 13.348  -54.604 81.864   1.00 70.70  ? 2   GLC H C4  1 
HETATM 16427 C C5  . GLC H  2 .   ? 12.017  -54.382 82.565   1.00 69.26  ? 2   GLC H C5  1 
HETATM 16428 C C6  . GLC H  2 .   ? 11.508  -55.656 83.235   1.00 68.35  ? 2   GLC H C6  1 
HETATM 16429 O O2  . GLC H  2 .   ? 13.037  -51.496 80.632   1.00 74.54  ? 2   GLC H O2  1 
HETATM 16430 O O3  . GLC H  2 .   ? 15.199  -53.358 82.716   1.00 71.75  ? 2   GLC H O3  1 
HETATM 16431 O O4  . GLC H  2 .   ? 13.128  -55.142 80.574   1.00 75.31  ? 2   GLC H O4  1 
HETATM 16432 O O5  . GLC H  2 .   ? 12.162  -53.340 83.507   1.00 67.02  ? 2   GLC H O5  1 
HETATM 16433 O O6  . GLC H  2 .   ? 12.575  -56.360 83.825   1.00 68.62  ? 2   GLC H O6  1 
HETATM 16434 C C1  . GLC H  2 .   ? 14.130  -56.128 80.236   1.00 78.93  ? 3   GLC H C1  1 
HETATM 16435 C C2  . GLC H  2 .   ? 15.083  -55.578 79.179   1.00 80.43  ? 3   GLC H C2  1 
HETATM 16436 C C3  . GLC H  2 .   ? 14.256  -55.055 78.012   1.00 78.92  ? 3   GLC H C3  1 
HETATM 16437 C C4  . GLC H  2 .   ? 13.393  -56.190 77.449   1.00 76.33  ? 3   GLC H C4  1 
HETATM 16438 C C5  . GLC H  2 .   ? 12.752  -57.089 78.519   1.00 77.63  ? 3   GLC H C5  1 
HETATM 16439 C C6  . GLC H  2 .   ? 12.442  -58.457 77.910   1.00 77.42  ? 3   GLC H C6  1 
HETATM 16440 O O2  . GLC H  2 .   ? 15.935  -54.575 79.691   1.00 81.12  ? 3   GLC H O2  1 
HETATM 16441 O O3  . GLC H  2 .   ? 15.124  -54.522 77.027   1.00 78.45  ? 3   GLC H O3  1 
HETATM 16442 O O4  . GLC H  2 .   ? 12.386  -55.657 76.605   1.00 73.03  ? 3   GLC H O4  1 
HETATM 16443 O O5  . GLC H  2 .   ? 13.557  -57.294 79.677   1.00 79.78  ? 3   GLC H O5  1 
HETATM 16444 O O6  . GLC H  2 .   ? 12.121  -59.390 78.924   1.00 78.15  ? 3   GLC H O6  1 
HETATM 16445 C C1  . GLC H  2 .   ? 12.856  -55.811 75.240   1.00 66.02  ? 4   GLC H C1  1 
HETATM 16446 C C2  . GLC H  2 .   ? 12.234  -54.748 74.321   1.00 60.24  ? 4   GLC H C2  1 
HETATM 16447 C C3  . GLC H  2 .   ? 10.736  -54.975 74.129   1.00 58.56  ? 4   GLC H C3  1 
HETATM 16448 C C4  . GLC H  2 .   ? 10.450  -56.396 73.626   1.00 56.38  ? 4   GLC H C4  1 
HETATM 16449 C C5  . GLC H  2 .   ? 11.158  -57.423 74.533   1.00 61.64  ? 4   GLC H C5  1 
HETATM 16450 C C6  . GLC H  2 .   ? 11.237  -58.829 73.940   1.00 66.13  ? 4   GLC H C6  1 
HETATM 16451 O O2  . GLC H  2 .   ? 12.498  -53.446 74.809   1.00 57.92  ? 4   GLC H O2  1 
HETATM 16452 O O3  . GLC H  2 .   ? 10.201  -53.993 73.261   1.00 60.48  ? 4   GLC H O3  1 
HETATM 16453 O O4  . GLC H  2 .   ? 9.036   -56.583 73.578   1.00 48.62  ? 4   GLC H O4  1 
HETATM 16454 O O5  . GLC H  2 .   ? 12.519  -57.102 74.744   1.00 64.81  ? 4   GLC H O5  1 
HETATM 16455 O O6  . GLC H  2 .   ? 12.047  -58.800 72.778   1.00 69.55  ? 4   GLC H O6  1 
HETATM 16456 C C1  . GLC H  2 .   ? 8.602   -57.389 72.444   1.00 41.94  ? 5   GLC H C1  1 
HETATM 16457 C C2  . GLC H  2 .   ? 7.716   -56.553 71.523   1.00 38.58  ? 5   GLC H C2  1 
HETATM 16458 C C3  . GLC H  2 .   ? 6.333   -56.311 72.113   1.00 37.89  ? 5   GLC H C3  1 
HETATM 16459 C C4  . GLC H  2 .   ? 5.651   -57.579 72.633   1.00 35.29  ? 5   GLC H C4  1 
HETATM 16460 C C5  . GLC H  2 .   ? 6.635   -58.329 73.545   1.00 38.63  ? 5   GLC H C5  1 
HETATM 16461 C C6  . GLC H  2 .   ? 6.171   -59.730 73.921   1.00 42.10  ? 5   GLC H C6  1 
HETATM 16462 O O2  . GLC H  2 .   ? 8.339   -55.302 71.375   1.00 40.59  ? 5   GLC H O2  1 
HETATM 16463 O O3  . GLC H  2 .   ? 5.515   -55.640 71.169   1.00 36.82  ? 5   GLC H O3  1 
HETATM 16464 O O4  . GLC H  2 .   ? 4.486   -57.085 73.272   1.00 28.03  ? 5   GLC H O4  1 
HETATM 16465 O O5  . GLC H  2 .   ? 7.865   -58.534 72.869   1.00 41.76  ? 5   GLC H O5  1 
HETATM 16466 O O6  . GLC H  2 .   ? 6.043   -60.508 72.749   1.00 46.44  ? 5   GLC H O6  1 
HETATM 16467 C C1  . GOL I  3 .   ? -43.884 -20.859 34.673   1.00 49.33  ? 501 GOL A C1  1 
HETATM 16468 O O1  . GOL I  3 .   ? -44.971 -20.148 35.172   1.00 47.68  ? 501 GOL A O1  1 
HETATM 16469 C C2  . GOL I  3 .   ? -43.374 -20.074 33.441   1.00 51.53  ? 501 GOL A C2  1 
HETATM 16470 O O2  . GOL I  3 .   ? -42.955 -18.795 33.778   1.00 48.93  ? 501 GOL A O2  1 
HETATM 16471 C C3  . GOL I  3 .   ? -42.222 -20.926 32.905   1.00 53.68  ? 501 GOL A C3  1 
HETATM 16472 O O3  . GOL I  3 .   ? -41.699 -20.230 31.838   1.00 57.32  ? 501 GOL A O3  1 
HETATM 16473 C C1  . GOL J  3 .   ? -17.188 -39.773 31.762   1.00 36.43  ? 502 GOL A C1  1 
HETATM 16474 O O1  . GOL J  3 .   ? -16.893 -40.846 30.958   1.00 29.16  ? 502 GOL A O1  1 
HETATM 16475 C C2  . GOL J  3 .   ? -16.098 -38.758 31.569   1.00 33.66  ? 502 GOL A C2  1 
HETATM 16476 O O2  . GOL J  3 .   ? -16.590 -37.419 31.548   1.00 27.27  ? 502 GOL A O2  1 
HETATM 16477 C C3  . GOL J  3 .   ? -15.135 -39.142 32.712   1.00 30.04  ? 502 GOL A C3  1 
HETATM 16478 O O3  . GOL J  3 .   ? -14.472 -38.019 33.067   1.00 32.80  ? 502 GOL A O3  1 
HETATM 16479 C C1  . GOL K  3 .   ? -20.632 -1.324  30.990   1.00 50.99  ? 503 GOL A C1  1 
HETATM 16480 O O1  . GOL K  3 .   ? -21.719 -1.894  31.651   1.00 39.78  ? 503 GOL A O1  1 
HETATM 16481 C C2  . GOL K  3 .   ? -20.660 0.245   31.165   1.00 55.60  ? 503 GOL A C2  1 
HETATM 16482 O O2  . GOL K  3 .   ? -21.832 0.838   30.707   1.00 56.44  ? 503 GOL A O2  1 
HETATM 16483 C C3  . GOL K  3 .   ? -20.423 0.507   32.656   1.00 57.90  ? 503 GOL A C3  1 
HETATM 16484 O O3  . GOL K  3 .   ? -21.670 0.823   33.237   1.00 58.66  ? 503 GOL A O3  1 
HETATM 16485 C C1  . PEG L  4 .   ? -36.587 -20.521 16.808   1.00 49.55  ? 504 PEG A C1  1 
HETATM 16486 O O1  . PEG L  4 .   ? -37.833 -20.737 16.193   1.00 53.78  ? 504 PEG A O1  1 
HETATM 16487 C C2  . PEG L  4 .   ? -35.705 -21.751 16.644   1.00 48.78  ? 504 PEG A C2  1 
HETATM 16488 O O2  . PEG L  4 .   ? -36.293 -22.788 17.377   1.00 53.84  ? 504 PEG A O2  1 
HETATM 16489 C C3  . PEG L  4 .   ? -35.965 -24.064 16.916   1.00 57.00  ? 504 PEG A C3  1 
HETATM 16490 C C4  . PEG L  4 .   ? -34.513 -24.346 17.277   1.00 55.21  ? 504 PEG A C4  1 
HETATM 16491 O O4  . PEG L  4 .   ? -34.358 -25.734 17.341   1.00 55.98  ? 504 PEG A O4  1 
HETATM 16492 C C1  . PEG M  4 .   ? -35.290 -37.020 27.767   1.00 58.96  ? 505 PEG A C1  1 
HETATM 16493 O O1  . PEG M  4 .   ? -35.459 -37.155 29.154   1.00 57.93  ? 505 PEG A O1  1 
HETATM 16494 C C2  . PEG M  4 .   ? -36.666 -36.861 27.130   1.00 64.66  ? 505 PEG A C2  1 
HETATM 16495 O O2  . PEG M  4 .   ? -37.522 -36.285 28.080   1.00 68.62  ? 505 PEG A O2  1 
HETATM 16496 C C3  . PEG M  4 .   ? -37.474 -34.884 28.132   1.00 68.97  ? 505 PEG A C3  1 
HETATM 16497 C C4  . PEG M  4 .   ? -38.621 -34.331 27.292   1.00 69.67  ? 505 PEG A C4  1 
HETATM 16498 O O4  . PEG M  4 .   ? -39.748 -35.150 27.447   1.00 68.04  ? 505 PEG A O4  1 
HETATM 16499 C C1  . EDO N  5 .   ? -11.223 -23.490 31.614   1.00 51.79  ? 506 EDO A C1  1 
HETATM 16500 O O1  . EDO N  5 .   ? -10.120 -23.792 32.478   1.00 51.69  ? 506 EDO A O1  1 
HETATM 16501 C C2  . EDO N  5 .   ? -11.623 -24.745 30.832   1.00 49.88  ? 506 EDO A C2  1 
HETATM 16502 O O2  . EDO N  5 .   ? -12.987 -24.636 30.387   1.00 43.77  ? 506 EDO A O2  1 
HETATM 16503 C C1  . EDO O  5 .   ? -37.060 -12.217 17.616   1.00 65.21  ? 507 EDO A C1  1 
HETATM 16504 O O1  . EDO O  5 .   ? -36.005 -11.613 18.374   1.00 65.17  ? 507 EDO A O1  1 
HETATM 16505 C C2  . EDO O  5 .   ? -37.477 -11.269 16.500   1.00 64.26  ? 507 EDO A C2  1 
HETATM 16506 O O2  . EDO O  5 .   ? -36.300 -10.757 15.863   1.00 60.69  ? 507 EDO A O2  1 
HETATM 16507 C C1  . EDO P  5 .   ? -9.387  -47.296 25.627   1.00 54.08  ? 508 EDO A C1  1 
HETATM 16508 O O1  . EDO P  5 .   ? -8.932  -46.762 26.874   1.00 55.09  ? 508 EDO A O1  1 
HETATM 16509 C C2  . EDO P  5 .   ? -9.527  -46.166 24.614   1.00 53.35  ? 508 EDO A C2  1 
HETATM 16510 O O2  . EDO P  5 .   ? -10.750 -45.445 24.833   1.00 53.66  ? 508 EDO A O2  1 
HETATM 16511 C C1  . GOL Q  3 .   ? -13.325 -18.198 -23.377  1.00 57.33  ? 501 GOL B C1  1 
HETATM 16512 O O1  . GOL Q  3 .   ? -14.679 -18.530 -23.254  1.00 53.71  ? 501 GOL B O1  1 
HETATM 16513 C C2  . GOL Q  3 .   ? -13.234 -16.712 -23.794  1.00 58.21  ? 501 GOL B C2  1 
HETATM 16514 O O2  . GOL Q  3 .   ? -11.917 -16.300 -23.935  1.00 60.34  ? 501 GOL B O2  1 
HETATM 16515 C C3  . GOL Q  3 .   ? -14.043 -16.605 -25.107  1.00 55.32  ? 501 GOL B C3  1 
HETATM 16516 O O3  . GOL Q  3 .   ? -13.791 -17.773 -25.818  1.00 53.89  ? 501 GOL B O3  1 
HETATM 16517 C C1  . GOL R  3 .   ? -22.061 -23.617 -29.427  1.00 49.44  ? 502 GOL B C1  1 
HETATM 16518 O O1  . GOL R  3 .   ? -22.375 -23.117 -28.174  1.00 39.88  ? 502 GOL B O1  1 
HETATM 16519 C C2  . GOL R  3 .   ? -21.226 -24.897 -29.221  1.00 54.63  ? 502 GOL B C2  1 
HETATM 16520 O O2  . GOL R  3 .   ? -21.998 -25.996 -28.780  1.00 52.78  ? 502 GOL B O2  1 
HETATM 16521 C C3  . GOL R  3 .   ? -20.533 -25.119 -30.589  1.00 50.35  ? 502 GOL B C3  1 
HETATM 16522 O O3  . GOL R  3 .   ? -20.807 -26.418 -30.946  1.00 49.58  ? 502 GOL B O3  1 
HETATM 16523 C C1  . PEG S  4 .   ? -27.025 -64.400 -28.980  1.00 67.39  ? 503 PEG B C1  1 
HETATM 16524 O O1  . PEG S  4 .   ? -25.793 -64.035 -29.543  1.00 66.06  ? 503 PEG B O1  1 
HETATM 16525 C C2  . PEG S  4 .   ? -27.195 -63.720 -27.621  1.00 70.19  ? 503 PEG B C2  1 
HETATM 16526 O O2  . PEG S  4 .   ? -27.752 -62.439 -27.776  1.00 69.91  ? 503 PEG B O2  1 
HETATM 16527 C C3  . PEG S  4 .   ? -27.076 -61.414 -27.105  1.00 68.60  ? 503 PEG B C3  1 
HETATM 16528 C C4  . PEG S  4 .   ? -27.749 -61.122 -25.764  1.00 69.12  ? 503 PEG B C4  1 
HETATM 16529 O O4  . PEG S  4 .   ? -27.723 -62.277 -24.971  1.00 67.69  ? 503 PEG B O4  1 
HETATM 16530 C C1  . EDO T  5 .   ? -15.280 -45.956 -31.000  1.00 59.51  ? 504 EDO B C1  1 
HETATM 16531 O O1  . EDO T  5 .   ? -14.659 -47.246 -30.941  1.00 60.09  ? 504 EDO B O1  1 
HETATM 16532 C C2  . EDO T  5 .   ? -14.534 -44.844 -30.254  1.00 58.56  ? 504 EDO B C2  1 
HETATM 16533 O O2  . EDO T  5 .   ? -15.401 -43.722 -30.016  1.00 53.69  ? 504 EDO B O2  1 
HETATM 16534 C C1  . EDO U  5 .   ? -28.848 -49.940 -25.909  1.00 38.31  ? 505 EDO B C1  1 
HETATM 16535 O O1  . EDO U  5 .   ? -28.845 -51.305 -26.296  1.00 39.15  ? 505 EDO B O1  1 
HETATM 16536 C C2  . EDO U  5 .   ? -28.530 -49.733 -24.445  1.00 41.10  ? 505 EDO B C2  1 
HETATM 16537 O O2  . EDO U  5 .   ? -27.134 -49.891 -24.227  1.00 36.25  ? 505 EDO B O2  1 
HETATM 16538 C C1  . EDO V  5 .   ? -25.220 -6.183  -22.340  1.00 71.38  ? 506 EDO B C1  1 
HETATM 16539 O O1  . EDO V  5 .   ? -24.339 -6.760  -23.317  1.00 73.15  ? 506 EDO B O1  1 
HETATM 16540 C C2  . EDO V  5 .   ? -25.410 -4.703  -22.632  1.00 70.72  ? 506 EDO B C2  1 
HETATM 16541 O O2  . EDO V  5 .   ? -24.393 -4.225  -23.524  1.00 69.71  ? 506 EDO B O2  1 
HETATM 16542 C C1  . EDO W  5 .   ? -1.809  -22.901 -65.487  1.00 38.98  ? 501 EDO C C1  1 
HETATM 16543 O O1  . EDO W  5 .   ? -1.255  -23.804 -64.495  1.00 35.69  ? 501 EDO C O1  1 
HETATM 16544 C C2  . EDO W  5 .   ? -3.114  -23.409 -66.113  1.00 33.25  ? 501 EDO C C2  1 
HETATM 16545 O O2  . EDO W  5 .   ? -3.007  -24.796 -66.497  1.00 29.25  ? 501 EDO C O2  1 
HETATM 16546 C C1  . PEG X  4 .   ? -7.886  15.899  -59.084  1.00 57.98  ? 502 PEG C C1  1 
HETATM 16547 O O1  . PEG X  4 .   ? -8.682  16.520  -60.058  1.00 59.67  ? 502 PEG C O1  1 
HETATM 16548 C C2  . PEG X  4 .   ? -6.505  15.617  -59.669  1.00 57.65  ? 502 PEG C C2  1 
HETATM 16549 O O2  . PEG X  4 .   ? -6.644  15.145  -60.982  1.00 58.42  ? 502 PEG C O2  1 
HETATM 16550 C C3  . PEG X  4 .   ? -7.251  13.884  -61.108  1.00 55.07  ? 502 PEG C C3  1 
HETATM 16551 C C4  . PEG X  4 .   ? -6.887  13.282  -62.464  1.00 54.96  ? 502 PEG C C4  1 
HETATM 16552 O O4  . PEG X  4 .   ? -7.682  13.828  -63.485  1.00 53.21  ? 502 PEG C O4  1 
HETATM 16553 C C1  . GOL Y  3 .   ? 1.835   -39.045 69.881   1.00 34.75  ? 501 GOL D C1  1 
HETATM 16554 O O1  . GOL Y  3 .   ? 1.889   -38.241 70.982   1.00 29.47  ? 501 GOL D O1  1 
HETATM 16555 C C2  . GOL Y  3 .   ? 2.896   -40.149 70.067   1.00 35.72  ? 501 GOL D C2  1 
HETATM 16556 O O2  . GOL Y  3 .   ? 2.351   -41.464 70.066   1.00 26.79  ? 501 GOL D O2  1 
HETATM 16557 C C3  . GOL Y  3 .   ? 3.933   -39.837 68.934   1.00 39.38  ? 501 GOL D C3  1 
HETATM 16558 O O3  . GOL Y  3 .   ? 4.313   -41.032 68.389   1.00 39.86  ? 501 GOL D O3  1 
HETATM 16559 O O   . HOH Z  6 .   ? -4.719  -6.632  44.971   1.00 58.29  ? 601 HOH A O   1 
HETATM 16560 O O   . HOH Z  6 .   ? -13.382 -58.464 29.453   1.00 49.02  ? 602 HOH A O   1 
HETATM 16561 O O   . HOH Z  6 .   ? -34.843 -5.444  43.634   1.00 56.06  ? 603 HOH A O   1 
HETATM 16562 O O   . HOH Z  6 .   ? -27.478 -27.902 3.049    1.00 53.07  ? 604 HOH A O   1 
HETATM 16563 O O   . HOH Z  6 .   ? -35.706 -8.910  14.840   1.00 62.49  ? 605 HOH A O   1 
HETATM 16564 O O   . HOH Z  6 .   ? -28.476 -20.906 3.293    1.00 58.97  ? 606 HOH A O   1 
HETATM 16565 O O   . HOH Z  6 .   ? -23.462 -58.165 19.887   1.00 48.84  ? 607 HOH A O   1 
HETATM 16566 O O   . HOH Z  6 .   ? -0.095  -33.885 53.014   1.00 56.48  ? 608 HOH A O   1 
HETATM 16567 O O   . HOH Z  6 .   ? -21.238 1.791   38.743   1.00 59.90  ? 609 HOH A O   1 
HETATM 16568 O O   . HOH Z  6 .   ? -1.541  -38.904 28.276   1.00 43.11  ? 610 HOH A O   1 
HETATM 16569 O O   . HOH Z  6 .   ? -6.206  -18.284 40.825   1.00 34.45  ? 611 HOH A O   1 
HETATM 16570 O O   . HOH Z  6 .   ? -39.843 -16.961 20.945   1.00 61.35  ? 612 HOH A O   1 
HETATM 16571 O O   . HOH Z  6 .   ? -2.614  1.104   42.300   1.00 52.76  ? 613 HOH A O   1 
HETATM 16572 O O   . HOH Z  6 .   ? -32.922 -33.862 12.953   1.00 32.38  ? 614 HOH A O   1 
HETATM 16573 O O   . HOH Z  6 .   ? -22.171 -14.252 27.913   1.00 27.96  ? 615 HOH A O   1 
HETATM 16574 O O   . HOH Z  6 .   ? -31.825 -2.451  36.872   1.00 44.38  ? 616 HOH A O   1 
HETATM 16575 O O   . HOH Z  6 .   ? -9.691  -4.662  15.846   1.00 44.67  ? 617 HOH A O   1 
HETATM 16576 O O   . HOH Z  6 .   ? -12.066 -19.329 60.576   1.00 45.09  ? 618 HOH A O   1 
HETATM 16577 O O   . HOH Z  6 .   ? -15.237 -46.962 36.761   1.00 39.25  ? 619 HOH A O   1 
HETATM 16578 O O   . HOH Z  6 .   ? 1.555   -40.598 16.223   1.00 46.37  ? 620 HOH A O   1 
HETATM 16579 O O   . HOH Z  6 .   ? -10.773 -19.184 18.374   1.00 52.55  ? 621 HOH A O   1 
HETATM 16580 O O   . HOH Z  6 .   ? -22.329 -4.683  28.575   1.00 26.72  ? 622 HOH A O   1 
HETATM 16581 O O   . HOH Z  6 .   ? -12.226 -6.132  24.579   1.00 28.71  ? 623 HOH A O   1 
HETATM 16582 O O   . HOH Z  6 .   ? -23.001 -13.564 21.056   1.00 35.29  ? 624 HOH A O   1 
HETATM 16583 O O   . HOH Z  6 .   ? 0.339   -46.919 22.365   1.00 53.00  ? 625 HOH A O   1 
HETATM 16584 O O   . HOH Z  6 .   ? -23.186 -35.254 12.222   1.00 27.52  ? 626 HOH A O   1 
HETATM 16585 O O   . HOH Z  6 .   ? -27.746 -41.382 47.506   1.00 41.99  ? 627 HOH A O   1 
HETATM 16586 O O   . HOH Z  6 .   ? -21.292 -44.176 26.705   1.00 19.22  ? 628 HOH A O   1 
HETATM 16587 O O   . HOH Z  6 .   ? -21.343 -44.359 29.774   1.00 20.39  ? 629 HOH A O   1 
HETATM 16588 O O   . HOH Z  6 .   ? -13.664 -34.792 26.198   1.00 24.19  ? 630 HOH A O   1 
HETATM 16589 O O   . HOH Z  6 .   ? -23.353 -42.790 51.957   1.00 43.29  ? 631 HOH A O   1 
HETATM 16590 O O   . HOH Z  6 .   ? -34.015 -38.353 30.893   1.00 30.63  ? 632 HOH A O   1 
HETATM 16591 O O   . HOH Z  6 .   ? -14.996 -56.640 11.467   1.00 39.34  ? 633 HOH A O   1 
HETATM 16592 O O   . HOH Z  6 .   ? -13.955 -42.638 26.092   1.00 23.36  ? 634 HOH A O   1 
HETATM 16593 O O   . HOH Z  6 .   ? -22.055 -29.793 51.555   1.00 41.45  ? 635 HOH A O   1 
HETATM 16594 O O   . HOH Z  6 .   ? -32.890 -24.593 20.131   1.00 32.13  ? 636 HOH A O   1 
HETATM 16595 O O   . HOH Z  6 .   ? -23.315 -12.928 30.273   1.00 23.24  ? 637 HOH A O   1 
HETATM 16596 O O   . HOH Z  6 .   ? -32.383 -37.335 28.482   1.00 24.43  ? 638 HOH A O   1 
HETATM 16597 O O   . HOH Z  6 .   ? -33.355 -3.605  21.757   1.00 37.85  ? 639 HOH A O   1 
HETATM 16598 O O   . HOH Z  6 .   ? -14.262 -32.172 22.550   1.00 29.44  ? 640 HOH A O   1 
HETATM 16599 O O   . HOH Z  6 .   ? -6.638  -41.792 48.700   1.00 58.25  ? 641 HOH A O   1 
HETATM 16600 O O   . HOH Z  6 .   ? -23.658 -39.838 6.340    1.00 28.85  ? 642 HOH A O   1 
HETATM 16601 O O   . HOH Z  6 .   ? -5.667  -19.914 44.575   1.00 58.63  ? 643 HOH A O   1 
HETATM 16602 O O   . HOH Z  6 .   ? -13.952 -5.293  27.465   1.00 34.64  ? 644 HOH A O   1 
HETATM 16603 O O   . HOH Z  6 .   ? -7.836  -2.638  35.561   1.00 41.30  ? 645 HOH A O   1 
HETATM 16604 O O   . HOH Z  6 .   ? -18.524 -56.541 29.312   1.00 31.61  ? 646 HOH A O   1 
HETATM 16605 O O   . HOH Z  6 .   ? -15.367 -17.812 57.166   1.00 35.22  ? 647 HOH A O   1 
HETATM 16606 O O   . HOH Z  6 .   ? -21.819 -43.802 38.696   1.00 37.51  ? 648 HOH A O   1 
HETATM 16607 O O   . HOH Z  6 .   ? -17.795 -42.957 48.333   1.00 60.14  ? 649 HOH A O   1 
HETATM 16608 O O   . HOH Z  6 .   ? -21.574 -32.618 7.765    1.00 24.38  ? 650 HOH A O   1 
HETATM 16609 O O   . HOH Z  6 .   ? -7.357  -52.203 18.807   1.00 32.47  ? 651 HOH A O   1 
HETATM 16610 O O   . HOH Z  6 .   ? -35.159 -15.012 41.925   1.00 51.46  ? 652 HOH A O   1 
HETATM 16611 O O   . HOH Z  6 .   ? -27.419 -3.524  21.496   1.00 30.22  ? 653 HOH A O   1 
HETATM 16612 O O   . HOH Z  6 .   ? -15.150 -15.088 44.798   1.00 21.77  ? 654 HOH A O   1 
HETATM 16613 O O   . HOH Z  6 .   ? -28.048 -27.844 48.439   1.00 37.99  ? 655 HOH A O   1 
HETATM 16614 O O   . HOH Z  6 .   ? -29.959 -29.531 44.883   1.00 32.37  ? 656 HOH A O   1 
HETATM 16615 O O   . HOH Z  6 .   ? -18.370 -12.920 4.273    1.00 40.04  ? 657 HOH A O   1 
HETATM 16616 O O   . HOH Z  6 .   ? -40.835 -16.505 10.274   1.00 50.36  ? 658 HOH A O   1 
HETATM 16617 O O   . HOH Z  6 .   ? -11.877 -52.395 28.857   1.00 51.77  ? 659 HOH A O   1 
HETATM 16618 O O   . HOH Z  6 .   ? -29.710 -15.462 57.657   1.00 58.55  ? 660 HOH A O   1 
HETATM 16619 O O   . HOH Z  6 .   ? -18.738 -3.085  32.948   1.00 24.43  ? 661 HOH A O   1 
HETATM 16620 O O   . HOH Z  6 .   ? -8.180  -9.134  10.884   1.00 52.08  ? 662 HOH A O   1 
HETATM 16621 O O   . HOH Z  6 .   ? -14.400 -46.699 -7.013   1.00 41.97  ? 663 HOH A O   1 
HETATM 16622 O O   . HOH Z  6 .   ? -21.731 -60.985 16.438   1.00 25.97  ? 664 HOH A O   1 
HETATM 16623 O O   . HOH Z  6 .   ? -8.802  -52.393 23.357   1.00 50.63  ? 665 HOH A O   1 
HETATM 16624 O O   . HOH Z  6 .   ? -21.824 -33.960 -2.597   1.00 48.02  ? 666 HOH A O   1 
HETATM 16625 O O   . HOH Z  6 .   ? -20.016 -41.742 35.606   1.00 27.13  ? 667 HOH A O   1 
HETATM 16626 O O   . HOH Z  6 .   ? -15.007 -33.592 51.512   1.00 45.97  ? 668 HOH A O   1 
HETATM 16627 O O   . HOH Z  6 .   ? -13.762 -30.104 6.425    1.00 38.80  ? 669 HOH A O   1 
HETATM 16628 O O   . HOH Z  6 .   ? -23.498 -44.670 36.345   1.00 40.93  ? 670 HOH A O   1 
HETATM 16629 O O   . HOH Z  6 .   ? -32.152 -6.078  27.905   1.00 35.47  ? 671 HOH A O   1 
HETATM 16630 O O   . HOH Z  6 .   ? -32.671 -40.821 37.437   1.00 53.11  ? 672 HOH A O   1 
HETATM 16631 O O   . HOH Z  6 .   ? -28.407 -37.163 48.520   1.00 41.71  ? 673 HOH A O   1 
HETATM 16632 O O   . HOH Z  6 .   ? -6.691  -43.817 27.154   1.00 42.78  ? 674 HOH A O   1 
HETATM 16633 O O   . HOH Z  6 .   ? -29.346 -42.924 36.145   1.00 42.51  ? 675 HOH A O   1 
HETATM 16634 O O   . HOH Z  6 .   ? -28.861 -3.886  31.509   1.00 37.97  ? 676 HOH A O   1 
HETATM 16635 O O   . HOH Z  6 .   ? -31.478 -22.363 39.776   1.00 53.35  ? 677 HOH A O   1 
HETATM 16636 O O   . HOH Z  6 .   ? -27.275 -48.170 32.551   1.00 55.95  ? 678 HOH A O   1 
HETATM 16637 O O   . HOH Z  6 .   ? -19.079 -28.705 44.497   1.00 27.06  ? 679 HOH A O   1 
HETATM 16638 O O   . HOH Z  6 .   ? -24.340 -15.772 4.430    1.00 35.02  ? 680 HOH A O   1 
HETATM 16639 O O   . HOH Z  6 .   ? -17.433 -19.501 22.346   1.00 17.88  ? 681 HOH A O   1 
HETATM 16640 O O   . HOH Z  6 .   ? -13.537 -29.654 29.704   1.00 17.47  ? 682 HOH A O   1 
HETATM 16641 O O   . HOH Z  6 .   ? -24.526 -21.493 20.775   1.00 29.02  ? 683 HOH A O   1 
HETATM 16642 O O   . HOH Z  6 .   ? -3.559  -18.520 49.361   1.00 40.90  ? 684 HOH A O   1 
HETATM 16643 O O   . HOH Z  6 .   ? -21.279 0.778   19.036   1.00 36.82  ? 685 HOH A O   1 
HETATM 16644 O O   . HOH Z  6 .   ? -25.952 -0.304  51.495   1.00 56.69  ? 686 HOH A O   1 
HETATM 16645 O O   . HOH Z  6 .   ? -12.377 -48.100 30.220   1.00 43.35  ? 687 HOH A O   1 
HETATM 16646 O O   . HOH Z  6 .   ? -30.180 -26.414 44.152   1.00 36.74  ? 688 HOH A O   1 
HETATM 16647 O O   . HOH Z  6 .   ? -12.128 -7.443  32.351   1.00 32.59  ? 689 HOH A O   1 
HETATM 16648 O O   . HOH Z  6 .   ? -22.057 -39.534 29.448   1.00 20.02  ? 690 HOH A O   1 
HETATM 16649 O O   . HOH Z  6 .   ? -15.115 -16.974 52.573   1.00 23.65  ? 691 HOH A O   1 
HETATM 16650 O O   . HOH Z  6 .   ? -30.603 -40.553 15.955   1.00 47.83  ? 692 HOH A O   1 
HETATM 16651 O O   . HOH Z  6 .   ? -3.823  -38.626 31.515   1.00 34.22  ? 693 HOH A O   1 
HETATM 16652 O O   . HOH Z  6 .   ? -13.215 -50.714 30.117   1.00 52.82  ? 694 HOH A O   1 
HETATM 16653 O O   . HOH Z  6 .   ? -19.050 -23.049 5.057    1.00 28.51  ? 695 HOH A O   1 
HETATM 16654 O O   . HOH Z  6 .   ? -18.943 -20.558 28.696   1.00 20.95  ? 696 HOH A O   1 
HETATM 16655 O O   . HOH Z  6 .   ? -9.872  -10.214 17.242   1.00 39.60  ? 697 HOH A O   1 
HETATM 16656 O O   . HOH Z  6 .   ? -35.802 -25.827 11.134   1.00 43.04  ? 698 HOH A O   1 
HETATM 16657 O O   . HOH Z  6 .   ? -6.628  -44.744 5.068    1.00 50.83  ? 699 HOH A O   1 
HETATM 16658 O O   . HOH Z  6 .   ? -16.434 -32.304 55.281   1.00 53.06  ? 700 HOH A O   1 
HETATM 16659 O O   . HOH Z  6 .   ? -15.502 -47.102 33.837   1.00 33.88  ? 701 HOH A O   1 
HETATM 16660 O O   . HOH Z  6 .   ? 0.613   -29.485 45.440   1.00 40.62  ? 702 HOH A O   1 
HETATM 16661 O O   . HOH Z  6 .   ? -18.134 -35.196 37.325   1.00 19.36  ? 703 HOH A O   1 
HETATM 16662 O O   . HOH Z  6 .   ? -32.479 -26.474 13.272   1.00 33.10  ? 704 HOH A O   1 
HETATM 16663 O O   . HOH Z  6 .   ? -23.958 -27.304 53.741   1.00 49.43  ? 705 HOH A O   1 
HETATM 16664 O O   . HOH Z  6 .   ? -24.397 -33.622 17.458   1.00 21.34  ? 706 HOH A O   1 
HETATM 16665 O O   . HOH Z  6 .   ? -21.457 2.067   36.290   1.00 60.42  ? 707 HOH A O   1 
HETATM 16666 O O   . HOH Z  6 .   ? -5.054  -17.974 30.715   1.00 42.03  ? 708 HOH A O   1 
HETATM 16667 O O   . HOH Z  6 .   ? -25.524 -32.466 52.703   1.00 39.30  ? 709 HOH A O   1 
HETATM 16668 O O   . HOH Z  6 .   ? -37.717 -37.904 35.833   1.00 43.04  ? 710 HOH A O   1 
HETATM 16669 O O   . HOH Z  6 .   ? -39.739 -30.104 25.185   1.00 49.66  ? 711 HOH A O   1 
HETATM 16670 O O   . HOH Z  6 .   ? -3.717  -28.558 27.582   1.00 40.69  ? 712 HOH A O   1 
HETATM 16671 O O   . HOH Z  6 .   ? -32.732 -6.615  20.355   1.00 36.31  ? 713 HOH A O   1 
HETATM 16672 O O   . HOH Z  6 .   ? -4.450  -36.961 35.213   1.00 30.93  ? 714 HOH A O   1 
HETATM 16673 O O   . HOH Z  6 .   ? -5.844  -34.290 55.635   1.00 49.50  ? 715 HOH A O   1 
HETATM 16674 O O   . HOH Z  6 .   ? -5.732  -30.911 31.351   1.00 23.92  ? 716 HOH A O   1 
HETATM 16675 O O   . HOH Z  6 .   ? -7.702  -57.950 12.681   1.00 49.16  ? 717 HOH A O   1 
HETATM 16676 O O   . HOH Z  6 .   ? -34.958 -16.375 37.336   1.00 38.83  ? 718 HOH A O   1 
HETATM 16677 O O   . HOH Z  6 .   ? -28.112 -30.265 49.594   1.00 42.18  ? 719 HOH A O   1 
HETATM 16678 O O   . HOH Z  6 .   ? -5.774  -36.018 17.428   1.00 33.99  ? 720 HOH A O   1 
HETATM 16679 O O   . HOH Z  6 .   ? -25.982 -2.557  19.267   1.00 32.07  ? 721 HOH A O   1 
HETATM 16680 O O   . HOH Z  6 .   ? -20.121 3.166   10.595   1.00 30.12  ? 722 HOH A O   1 
HETATM 16681 O O   . HOH Z  6 .   ? -30.331 -26.125 41.120   1.00 31.08  ? 723 HOH A O   1 
HETATM 16682 O O   . HOH Z  6 .   ? 2.443   -34.666 42.202   1.00 48.45  ? 724 HOH A O   1 
HETATM 16683 O O   . HOH Z  6 .   ? -5.971  -6.451  41.143   1.00 39.68  ? 725 HOH A O   1 
HETATM 16684 O O   . HOH Z  6 .   ? -21.985 3.097   25.115   1.00 55.90  ? 726 HOH A O   1 
HETATM 16685 O O   . HOH Z  6 .   ? -15.872 -21.148 10.396   1.00 35.77  ? 727 HOH A O   1 
HETATM 16686 O O   . HOH Z  6 .   ? -17.190 -33.010 50.620   1.00 33.28  ? 728 HOH A O   1 
HETATM 16687 O O   . HOH Z  6 .   ? -10.793 -12.902 24.123   1.00 36.04  ? 729 HOH A O   1 
HETATM 16688 O O   . HOH Z  6 .   ? -0.983  -17.247 53.676   1.00 51.96  ? 730 HOH A O   1 
HETATM 16689 O O   . HOH Z  6 .   ? -12.771 -19.148 44.412   1.00 25.95  ? 731 HOH A O   1 
HETATM 16690 O O   . HOH Z  6 .   ? -0.210  -32.723 25.753   1.00 45.19  ? 732 HOH A O   1 
HETATM 16691 O O   . HOH Z  6 .   ? -3.943  -42.043 20.467   1.00 35.13  ? 733 HOH A O   1 
HETATM 16692 O O   . HOH Z  6 .   ? -27.114 -10.490 6.588    1.00 36.92  ? 734 HOH A O   1 
HETATM 16693 O O   . HOH Z  6 .   ? -7.317  -40.223 33.967   1.00 27.09  ? 735 HOH A O   1 
HETATM 16694 O O   . HOH Z  6 .   ? -24.075 -40.813 46.722   1.00 45.37  ? 736 HOH A O   1 
HETATM 16695 O O   . HOH Z  6 .   ? -25.560 -0.676  8.435    1.00 47.55  ? 737 HOH A O   1 
HETATM 16696 O O   . HOH Z  6 .   ? -2.386  -43.157 38.970   1.00 33.01  ? 738 HOH A O   1 
HETATM 16697 O O   . HOH Z  6 .   ? -29.769 -3.277  37.756   1.00 54.23  ? 739 HOH A O   1 
HETATM 16698 O O   . HOH Z  6 .   ? -26.212 -22.332 18.874   1.00 22.01  ? 740 HOH A O   1 
HETATM 16699 O O   . HOH Z  6 .   ? -17.677 -10.680 55.743   1.00 31.86  ? 741 HOH A O   1 
HETATM 16700 O O   . HOH Z  6 .   ? -32.694 -11.121 41.314   1.00 43.88  ? 742 HOH A O   1 
HETATM 16701 O O   . HOH Z  6 .   ? -17.815 -46.820 -0.568   1.00 38.06  ? 743 HOH A O   1 
HETATM 16702 O O   . HOH Z  6 .   ? -14.407 -15.482 6.282    1.00 46.11  ? 744 HOH A O   1 
HETATM 16703 O O   . HOH Z  6 .   ? -31.096 -41.402 35.018   1.00 38.93  ? 745 HOH A O   1 
HETATM 16704 O O   . HOH Z  6 .   ? -14.816 -6.857  8.458    1.00 34.86  ? 746 HOH A O   1 
HETATM 16705 O O   . HOH Z  6 .   ? -9.450  -20.541 31.225   1.00 51.31  ? 747 HOH A O   1 
HETATM 16706 O O   . HOH Z  6 .   ? -28.686 -50.201 12.064   1.00 53.89  ? 748 HOH A O   1 
HETATM 16707 O O   . HOH Z  6 .   ? -26.214 -0.186  19.004   1.00 38.96  ? 749 HOH A O   1 
HETATM 16708 O O   . HOH Z  6 .   ? -25.456 3.753   11.766   1.00 54.48  ? 750 HOH A O   1 
HETATM 16709 O O   . HOH Z  6 .   ? -26.528 -27.188 54.085   1.00 50.71  ? 751 HOH A O   1 
HETATM 16710 O O   . HOH Z  6 .   ? -2.902  -35.720 25.755   1.00 43.75  ? 752 HOH A O   1 
HETATM 16711 O O   . HOH Z  6 .   ? -5.477  -10.216 24.518   1.00 48.51  ? 753 HOH A O   1 
HETATM 16712 O O   . HOH Z  6 .   ? -22.771 -43.024 47.616   1.00 50.63  ? 754 HOH A O   1 
HETATM 16713 O O   . HOH Z  6 .   ? -12.130 -17.604 8.758    1.00 43.61  ? 755 HOH A O   1 
HETATM 16714 O O   . HOH Z  6 .   ? -28.187 -41.236 43.054   1.00 36.56  ? 756 HOH A O   1 
HETATM 16715 O O   . HOH Z  6 .   ? -35.565 -6.733  19.046   1.00 39.48  ? 757 HOH A O   1 
HETATM 16716 O O   . HOH Z  6 .   ? -37.759 -26.361 23.026   1.00 48.47  ? 758 HOH A O   1 
HETATM 16717 O O   . HOH Z  6 .   ? -17.106 -10.772 59.655   1.00 46.24  ? 759 HOH A O   1 
HETATM 16718 O O   . HOH Z  6 .   ? -10.122 2.312   27.915   1.00 47.09  ? 760 HOH A O   1 
HETATM 16719 O O   . HOH Z  6 .   ? -15.989 -1.643  43.684   1.00 59.00  ? 761 HOH A O   1 
HETATM 16720 O O   . HOH Z  6 .   ? -6.631  -8.251  31.192   1.00 45.53  ? 762 HOH A O   1 
HETATM 16721 O O   . HOH Z  6 .   ? -17.737 -20.332 12.147   1.00 31.30  ? 763 HOH A O   1 
HETATM 16722 O O   . HOH Z  6 .   ? -14.831 -56.717 1.751    1.00 38.33  ? 764 HOH A O   1 
HETATM 16723 O O   . HOH Z  6 .   ? -39.593 -18.041 16.110   1.00 42.13  ? 765 HOH A O   1 
HETATM 16724 O O   . HOH Z  6 .   ? -6.690  -15.715 30.417   1.00 47.25  ? 766 HOH A O   1 
HETATM 16725 O O   . HOH Z  6 .   ? -19.955 -12.346 56.798   1.00 49.57  ? 767 HOH A O   1 
HETATM 16726 O O   . HOH Z  6 .   ? -13.448 -26.450 27.295   1.00 29.62  ? 768 HOH A O   1 
HETATM 16727 O O   . HOH Z  6 .   ? -21.707 -16.848 60.708   1.00 48.74  ? 769 HOH A O   1 
HETATM 16728 O O   . HOH Z  6 .   ? -27.689 -1.170  22.588   1.00 40.94  ? 770 HOH A O   1 
HETATM 16729 O O   . HOH Z  6 .   ? -3.429  -41.975 34.556   1.00 34.40  ? 771 HOH A O   1 
HETATM 16730 O O   . HOH Z  6 .   ? -35.994 -16.713 39.286   1.00 57.19  ? 772 HOH A O   1 
HETATM 16731 O O   . HOH Z  6 .   ? -7.038  -31.500 28.966   1.00 37.90  ? 773 HOH A O   1 
HETATM 16732 O O   . HOH Z  6 .   ? -6.865  -7.234  28.208   1.00 54.45  ? 774 HOH A O   1 
HETATM 16733 O O   . HOH Z  6 .   ? -19.110 -33.841 51.411   1.00 47.29  ? 775 HOH A O   1 
HETATM 16734 O O   . HOH Z  6 .   ? -4.771  -39.309 34.146   1.00 30.84  ? 776 HOH A O   1 
HETATM 16735 O O   . HOH Z  6 .   ? -36.850 -29.977 7.280    1.00 50.51  ? 777 HOH A O   1 
HETATM 16736 O O   . HOH Z  6 .   ? -11.605 -27.452 29.063   1.00 39.06  ? 778 HOH A O   1 
HETATM 16737 O O   . HOH Z  6 .   ? -39.988 -31.978 23.197   1.00 46.27  ? 779 HOH A O   1 
HETATM 16738 O O   . HOH Z  6 .   ? -25.692 -42.203 47.917   1.00 56.72  ? 780 HOH A O   1 
HETATM 16739 O O   . HOH Z  6 .   ? -38.051 -29.606 9.562    1.00 54.85  ? 781 HOH A O   1 
HETATM 16740 O O   . HOH Z  6 .   ? -8.311  1.015   29.372   1.00 58.65  ? 782 HOH A O   1 
HETATM 16741 O O   . HOH Z  6 .   ? -38.049 -15.619 38.546   1.00 47.39  ? 783 HOH A O   1 
HETATM 16742 O O   . HOH Z  6 .   ? -29.284 -1.306  32.076   1.00 45.24  ? 784 HOH A O   1 
HETATM 16743 O O   . HOH Z  6 .   ? -14.359 -59.334 1.604    1.00 61.14  ? 785 HOH A O   1 
HETATM 16744 O O   . HOH Z  6 .   ? -4.914  -30.021 25.642   1.00 61.36  ? 786 HOH A O   1 
HETATM 16745 O O   . HOH Z  6 .   ? -12.825 -47.435 33.054   1.00 49.67  ? 787 HOH A O   1 
HETATM 16746 O O   . HOH Z  6 .   ? -24.172 -0.133  53.191   1.00 54.76  ? 788 HOH A O   1 
HETATM 16747 O O   . HOH Z  6 .   ? -7.891  -8.864  17.129   1.00 44.49  ? 789 HOH A O   1 
HETATM 16748 O O   . HOH Z  6 .   ? -37.757 -8.016  19.711   1.00 52.55  ? 790 HOH A O   1 
HETATM 16749 O O   . HOH Z  6 .   ? -21.750 -14.515 61.283   1.00 59.62  ? 791 HOH A O   1 
HETATM 16750 O O   . HOH Z  6 .   ? -5.138  -34.277 19.454   1.00 40.31  ? 792 HOH A O   1 
HETATM 16751 O O   . HOH Z  6 .   ? -32.378 -44.842 18.193   1.00 61.16  ? 793 HOH A O   1 
HETATM 16752 O O   . HOH AA 6 .   ? -27.524 -47.138 -1.133   1.00 55.75  ? 601 HOH B O   1 
HETATM 16753 O O   . HOH AA 6 .   ? -42.181 -52.174 -11.744  1.00 43.01  ? 602 HOH B O   1 
HETATM 16754 O O   . HOH AA 6 .   ? -46.693 -44.770 -18.562  1.00 56.42  ? 603 HOH B O   1 
HETATM 16755 O O   . HOH AA 6 .   ? -7.256  -8.844  -7.468   1.00 54.02  ? 604 HOH B O   1 
HETATM 16756 O O   . HOH AA 6 .   ? -35.007 -47.246 2.733    1.00 64.63  ? 605 HOH B O   1 
HETATM 16757 O O   . HOH AA 6 .   ? -22.201 -3.492  -24.469  1.00 48.64  ? 606 HOH B O   1 
HETATM 16758 O O   . HOH AA 6 .   ? -16.658 -17.195 -31.617  1.00 51.43  ? 607 HOH B O   1 
HETATM 16759 O O   . HOH AA 6 .   ? -16.709 -18.312 -37.529  1.00 43.58  ? 608 HOH B O   1 
HETATM 16760 O O   . HOH AA 6 .   ? -34.694 -29.572 -7.854   1.00 30.84  ? 609 HOH B O   1 
HETATM 16761 O O   . HOH AA 6 .   ? -18.360 -21.402 -23.723  1.00 28.26  ? 610 HOH B O   1 
HETATM 16762 O O   . HOH AA 6 .   ? -19.434 -59.075 -25.340  1.00 25.69  ? 611 HOH B O   1 
HETATM 16763 O O   . HOH AA 6 .   ? -40.260 -35.931 -38.169  1.00 49.20  ? 612 HOH B O   1 
HETATM 16764 O O   . HOH AA 6 .   ? -16.788 -16.969 5.850    1.00 42.76  ? 613 HOH B O   1 
HETATM 16765 O O   . HOH AA 6 .   ? -36.505 -21.437 -37.980  1.00 56.58  ? 614 HOH B O   1 
HETATM 16766 O O   . HOH AA 6 .   ? -25.081 -48.426 -1.076   1.00 34.83  ? 615 HOH B O   1 
HETATM 16767 O O   . HOH AA 6 .   ? -25.823 -21.608 -32.011  1.00 25.57  ? 616 HOH B O   1 
HETATM 16768 O O   . HOH AA 6 .   ? -9.270  -25.864 -31.196  1.00 31.59  ? 617 HOH B O   1 
HETATM 16769 O O   . HOH AA 6 .   ? -4.838  -26.016 -21.676  1.00 50.16  ? 618 HOH B O   1 
HETATM 16770 O O   . HOH AA 6 .   ? -22.577 -30.978 -4.346   1.00 44.76  ? 619 HOH B O   1 
HETATM 16771 O O   . HOH AA 6 .   ? -26.871 -13.279 -2.151   1.00 31.77  ? 620 HOH B O   1 
HETATM 16772 O O   . HOH AA 6 .   ? -31.605 -60.168 -16.931  1.00 26.23  ? 621 HOH B O   1 
HETATM 16773 O O   . HOH AA 6 .   ? -38.888 -24.750 -25.199  1.00 36.42  ? 622 HOH B O   1 
HETATM 16774 O O   . HOH AA 6 .   ? -25.062 -64.072 -15.642  1.00 29.04  ? 623 HOH B O   1 
HETATM 16775 O O   . HOH AA 6 .   ? -18.481 -31.704 -20.361  1.00 43.04  ? 624 HOH B O   1 
HETATM 16776 O O   . HOH AA 6 .   ? -35.002 -59.560 -26.732  1.00 39.66  ? 625 HOH B O   1 
HETATM 16777 O O   . HOH AA 6 .   ? -12.974 -48.652 -29.614  1.00 40.22  ? 626 HOH B O   1 
HETATM 16778 O O   . HOH AA 6 .   ? -22.769 -7.183  -26.162  1.00 36.04  ? 627 HOH B O   1 
HETATM 16779 O O   . HOH AA 6 .   ? -18.976 -34.573 -27.608  1.00 24.85  ? 628 HOH B O   1 
HETATM 16780 O O   . HOH AA 6 .   ? -27.007 -50.320 -17.407  1.00 37.69  ? 629 HOH B O   1 
HETATM 16781 O O   . HOH AA 6 .   ? -29.066 -18.889 -32.386  1.00 44.98  ? 630 HOH B O   1 
HETATM 16782 O O   . HOH AA 6 .   ? -26.424 -31.066 -47.324  1.00 33.74  ? 631 HOH B O   1 
HETATM 16783 O O   . HOH AA 6 .   ? -48.002 -35.521 -26.957  1.00 43.48  ? 632 HOH B O   1 
HETATM 16784 O O   . HOH AA 6 .   ? -25.306 -60.713 -29.687  1.00 23.76  ? 633 HOH B O   1 
HETATM 16785 O O   . HOH AA 6 .   ? -17.172 -57.157 -22.790  1.00 35.27  ? 634 HOH B O   1 
HETATM 16786 O O   . HOH AA 6 .   ? -24.705 -47.034 -49.553  1.00 31.96  ? 635 HOH B O   1 
HETATM 16787 O O   . HOH AA 6 .   ? -21.415 -44.555 -41.809  1.00 32.92  ? 636 HOH B O   1 
HETATM 16788 O O   . HOH AA 6 .   ? -24.548 -24.250 -2.776   1.00 31.92  ? 637 HOH B O   1 
HETATM 16789 O O   . HOH AA 6 .   ? -18.178 -29.035 -24.208  1.00 27.01  ? 638 HOH B O   1 
HETATM 16790 O O   . HOH AA 6 .   ? -19.530 -50.654 -1.503   1.00 42.67  ? 639 HOH B O   1 
HETATM 16791 O O   . HOH AA 6 .   ? -37.709 -36.679 -38.995  1.00 33.29  ? 640 HOH B O   1 
HETATM 16792 O O   . HOH AA 6 .   ? -24.595 -61.047 -7.078   1.00 43.34  ? 641 HOH B O   1 
HETATM 16793 O O   . HOH AA 6 .   ? -32.946 -62.614 -42.815  1.00 43.75  ? 642 HOH B O   1 
HETATM 16794 O O   . HOH AA 6 .   ? -36.127 -38.934 -14.329  1.00 42.24  ? 643 HOH B O   1 
HETATM 16795 O O   . HOH AA 6 .   ? -24.690 -28.489 -34.430  1.00 23.09  ? 644 HOH B O   1 
HETATM 16796 O O   . HOH AA 6 .   ? -18.171 -12.402 -28.099  1.00 42.37  ? 645 HOH B O   1 
HETATM 16797 O O   . HOH AA 6 .   ? -27.566 -67.110 -17.015  1.00 44.69  ? 646 HOH B O   1 
HETATM 16798 O O   . HOH AA 6 .   ? -36.470 -32.864 -44.642  1.00 39.11  ? 647 HOH B O   1 
HETATM 16799 O O   . HOH AA 6 .   ? -13.993 -47.468 -42.447  1.00 47.74  ? 648 HOH B O   1 
HETATM 16800 O O   . HOH AA 6 .   ? -21.686 -44.584 -19.646  1.00 27.87  ? 649 HOH B O   1 
HETATM 16801 O O   . HOH AA 6 .   ? -24.999 -28.478 -8.732   1.00 25.40  ? 650 HOH B O   1 
HETATM 16802 O O   . HOH AA 6 .   ? -25.521 -19.408 -23.176  1.00 25.46  ? 651 HOH B O   1 
HETATM 16803 O O   . HOH AA 6 .   ? -28.173 -42.336 -16.654  1.00 28.40  ? 652 HOH B O   1 
HETATM 16804 O O   . HOH AA 6 .   ? -7.906  -20.083 -17.100  1.00 40.89  ? 653 HOH B O   1 
HETATM 16805 O O   . HOH AA 6 .   ? -24.509 -43.334 -25.586  1.00 26.51  ? 654 HOH B O   1 
HETATM 16806 O O   . HOH AA 6 .   ? -19.769 -40.787 -2.344   1.00 32.85  ? 655 HOH B O   1 
HETATM 16807 O O   . HOH AA 6 .   ? -14.625 -44.076 -16.645  1.00 52.42  ? 656 HOH B O   1 
HETATM 16808 O O   . HOH AA 6 .   ? -17.107 -5.649  -3.698   1.00 54.50  ? 657 HOH B O   1 
HETATM 16809 O O   . HOH AA 6 .   ? -42.993 -33.349 -33.936  1.00 45.70  ? 658 HOH B O   1 
HETATM 16810 O O   . HOH AA 6 .   ? -25.874 -19.210 -26.143  1.00 28.90  ? 659 HOH B O   1 
HETATM 16811 O O   . HOH AA 6 .   ? -23.572 -48.682 -41.872  1.00 28.99  ? 660 HOH B O   1 
HETATM 16812 O O   . HOH AA 6 .   ? -27.194 -35.012 -41.279  1.00 29.85  ? 661 HOH B O   1 
HETATM 16813 O O   . HOH AA 6 .   ? -15.894 -7.293  -9.634   1.00 36.09  ? 662 HOH B O   1 
HETATM 16814 O O   . HOH AA 6 .   ? -12.131 -11.493 -22.180  1.00 44.42  ? 663 HOH B O   1 
HETATM 16815 O O   . HOH AA 6 .   ? -10.169 -41.052 -36.219  1.00 32.59  ? 664 HOH B O   1 
HETATM 16816 O O   . HOH AA 6 .   ? -33.928 -51.356 -49.664  1.00 38.20  ? 665 HOH B O   1 
HETATM 16817 O O   . HOH AA 6 .   ? -16.312 -40.322 -31.382  1.00 37.74  ? 666 HOH B O   1 
HETATM 16818 O O   . HOH AA 6 .   ? -34.569 -36.840 -8.019   1.00 27.36  ? 667 HOH B O   1 
HETATM 16819 O O   . HOH AA 6 .   ? -25.876 -58.820 -5.142   1.00 44.14  ? 668 HOH B O   1 
HETATM 16820 O O   . HOH AA 6 .   ? -11.492 -32.792 -30.721  1.00 31.27  ? 669 HOH B O   1 
HETATM 16821 O O   . HOH AA 6 .   ? -31.002 -33.382 -47.800  1.00 43.88  ? 670 HOH B O   1 
HETATM 16822 O O   . HOH AA 6 .   ? -18.451 -47.081 -3.419   1.00 36.08  ? 671 HOH B O   1 
HETATM 16823 O O   . HOH AA 6 .   ? -7.480  -18.679 -3.539   1.00 59.04  ? 672 HOH B O   1 
HETATM 16824 O O   . HOH AA 6 .   ? -23.329 -2.666  -13.047  1.00 26.63  ? 673 HOH B O   1 
HETATM 16825 O O   . HOH AA 6 .   ? -27.034 -29.964 -13.578  1.00 26.91  ? 674 HOH B O   1 
HETATM 16826 O O   . HOH AA 6 .   ? -36.958 -59.127 -11.644  1.00 42.88  ? 675 HOH B O   1 
HETATM 16827 O O   . HOH AA 6 .   ? -14.312 -57.742 -39.950  1.00 37.36  ? 676 HOH B O   1 
HETATM 16828 O O   . HOH AA 6 .   ? -37.127 -25.890 -22.873  1.00 33.26  ? 677 HOH B O   1 
HETATM 16829 O O   . HOH AA 6 .   ? -18.643 -56.542 -30.375  1.00 27.77  ? 678 HOH B O   1 
HETATM 16830 O O   . HOH AA 6 .   ? -12.830 -59.421 -14.798  1.00 46.07  ? 679 HOH B O   1 
HETATM 16831 O O   . HOH AA 6 .   ? -25.903 -46.324 -54.421  1.00 51.91  ? 680 HOH B O   1 
HETATM 16832 O O   . HOH AA 6 .   ? -12.611 -32.167 -28.106  1.00 25.88  ? 681 HOH B O   1 
HETATM 16833 O O   . HOH AA 6 .   ? -6.625  -41.587 -40.125  1.00 34.73  ? 682 HOH B O   1 
HETATM 16834 O O   . HOH AA 6 .   ? -13.438 -23.992 -32.935  1.00 34.24  ? 683 HOH B O   1 
HETATM 16835 O O   . HOH AA 6 .   ? -17.304 -17.395 3.253    1.00 48.75  ? 684 HOH B O   1 
HETATM 16836 O O   . HOH AA 6 .   ? -8.948  -28.387 -16.943  1.00 51.14  ? 685 HOH B O   1 
HETATM 16837 O O   . HOH AA 6 .   ? -12.787 -34.775 -26.359  1.00 36.92  ? 686 HOH B O   1 
HETATM 16838 O O   . HOH AA 6 .   ? -10.694 -43.866 -34.540  1.00 36.66  ? 687 HOH B O   1 
HETATM 16839 O O   . HOH AA 6 .   ? -16.886 -2.862  -12.721  1.00 51.80  ? 688 HOH B O   1 
HETATM 16840 O O   . HOH AA 6 .   ? -13.747 -53.869 -15.942  1.00 48.63  ? 689 HOH B O   1 
HETATM 16841 O O   . HOH AA 6 .   ? -15.335 -65.690 -17.158  1.00 48.30  ? 690 HOH B O   1 
HETATM 16842 O O   . HOH AA 6 .   ? -16.679 -66.769 -23.680  1.00 42.77  ? 691 HOH B O   1 
HETATM 16843 O O   . HOH AA 6 .   ? -2.998  -21.705 -8.690   1.00 50.03  ? 692 HOH B O   1 
HETATM 16844 O O   . HOH AA 6 .   ? -10.117 -12.126 -18.134  1.00 45.58  ? 693 HOH B O   1 
HETATM 16845 O O   . HOH AA 6 .   ? -16.338 -49.266 -47.636  1.00 39.53  ? 694 HOH B O   1 
HETATM 16846 O O   . HOH AA 6 .   ? -38.133 -58.079 -22.537  1.00 42.17  ? 695 HOH B O   1 
HETATM 16847 O O   . HOH AA 6 .   ? -36.815 -56.329 -14.543  1.00 41.96  ? 696 HOH B O   1 
HETATM 16848 O O   . HOH AA 6 .   ? -11.857 -19.827 -26.418  1.00 47.78  ? 697 HOH B O   1 
HETATM 16849 O O   . HOH AA 6 .   ? -13.283 -43.047 -42.923  1.00 40.60  ? 698 HOH B O   1 
HETATM 16850 O O   . HOH AA 6 .   ? -41.852 -57.041 -26.948  1.00 53.67  ? 699 HOH B O   1 
HETATM 16851 O O   . HOH AA 6 .   ? -17.964 -14.648 1.921    1.00 42.83  ? 700 HOH B O   1 
HETATM 16852 O O   . HOH AA 6 .   ? -32.607 -16.078 -13.461  1.00 51.33  ? 701 HOH B O   1 
HETATM 16853 O O   . HOH AA 6 .   ? -34.039 -63.101 -17.114  1.00 44.69  ? 702 HOH B O   1 
HETATM 16854 O O   . HOH AA 6 .   ? -22.465 -61.920 -6.781   1.00 28.99  ? 703 HOH B O   1 
HETATM 16855 O O   . HOH AA 6 .   ? -27.070 -14.745 -31.582  1.00 44.86  ? 704 HOH B O   1 
HETATM 16856 O O   . HOH AA 6 .   ? -2.163  -30.622 -33.794  1.00 41.48  ? 705 HOH B O   1 
HETATM 16857 O O   . HOH AA 6 .   ? -18.972 -39.518 -28.357  1.00 27.90  ? 706 HOH B O   1 
HETATM 16858 O O   . HOH AA 6 .   ? -37.709 -37.293 -35.870  1.00 26.07  ? 707 HOH B O   1 
HETATM 16859 O O   . HOH AA 6 .   ? -26.940 -23.974 -25.739  1.00 23.13  ? 708 HOH B O   1 
HETATM 16860 O O   . HOH AA 6 .   ? -37.589 -40.765 -33.764  1.00 40.04  ? 709 HOH B O   1 
HETATM 16861 O O   . HOH AA 6 .   ? -31.363 -14.220 -12.561  1.00 41.07  ? 710 HOH B O   1 
HETATM 16862 O O   . HOH AA 6 .   ? -30.850 -18.027 -31.679  1.00 39.65  ? 711 HOH B O   1 
HETATM 16863 O O   . HOH AA 6 .   ? -20.057 -43.826 -9.504   1.00 33.46  ? 712 HOH B O   1 
HETATM 16864 O O   . HOH AA 6 .   ? -9.309  -6.525  -12.099  1.00 42.32  ? 713 HOH B O   1 
HETATM 16865 O O   . HOH AA 6 .   ? -28.715 -66.636 -19.032  1.00 47.39  ? 714 HOH B O   1 
HETATM 16866 O O   . HOH AA 6 .   ? -7.068  -29.048 -14.503  1.00 54.01  ? 715 HOH B O   1 
HETATM 16867 O O   . HOH AA 6 .   ? -44.439 -51.409 -28.222  1.00 53.07  ? 716 HOH B O   1 
HETATM 16868 O O   . HOH AA 6 .   ? -30.672 -14.757 -10.220  1.00 47.80  ? 717 HOH B O   1 
HETATM 16869 O O   . HOH AA 6 .   ? -46.691 -49.022 -29.314  1.00 45.04  ? 718 HOH B O   1 
HETATM 16870 O O   . HOH AA 6 .   ? -23.529 -34.033 -57.615  1.00 45.25  ? 719 HOH B O   1 
HETATM 16871 O O   . HOH AA 6 .   ? -11.509 -41.485 -46.071  1.00 42.54  ? 720 HOH B O   1 
HETATM 16872 O O   . HOH AA 6 .   ? -38.109 -59.659 -15.849  1.00 36.90  ? 721 HOH B O   1 
HETATM 16873 O O   . HOH AA 6 .   ? -29.828 -41.307 -14.526  1.00 22.37  ? 722 HOH B O   1 
HETATM 16874 O O   . HOH AA 6 .   ? -29.985 -7.579  -14.251  1.00 39.01  ? 723 HOH B O   1 
HETATM 16875 O O   . HOH AA 6 .   ? -10.541 -7.217  -24.220  1.00 58.03  ? 724 HOH B O   1 
HETATM 16876 O O   . HOH AA 6 .   ? -32.596 -49.489 -51.066  1.00 53.62  ? 725 HOH B O   1 
HETATM 16877 O O   . HOH AA 6 .   ? -13.620 -56.350 -29.714  1.00 43.56  ? 726 HOH B O   1 
HETATM 16878 O O   . HOH AA 6 .   ? -36.143 -62.427 -11.251  1.00 43.72  ? 727 HOH B O   1 
HETATM 16879 O O   . HOH AA 6 .   ? -28.158 -67.533 -8.190   1.00 63.51  ? 728 HOH B O   1 
HETATM 16880 O O   . HOH AA 6 .   ? -32.415 -66.802 -8.282   1.00 52.33  ? 729 HOH B O   1 
HETATM 16881 O O   . HOH AA 6 .   ? -21.786 -5.547  -7.410   1.00 25.33  ? 730 HOH B O   1 
HETATM 16882 O O   . HOH AA 6 .   ? -28.718 -42.403 0.930    1.00 45.45  ? 731 HOH B O   1 
HETATM 16883 O O   . HOH AA 6 .   ? -28.086 -53.080 -2.093   1.00 32.27  ? 732 HOH B O   1 
HETATM 16884 O O   . HOH AA 6 .   ? -11.364 -61.381 -21.501  1.00 38.42  ? 733 HOH B O   1 
HETATM 16885 O O   . HOH AA 6 .   ? -39.629 -39.041 -35.471  1.00 48.53  ? 734 HOH B O   1 
HETATM 16886 O O   . HOH AA 6 .   ? -18.512 -37.703 -25.181  1.00 46.10  ? 735 HOH B O   1 
HETATM 16887 O O   . HOH AA 6 .   ? -32.368 -3.431  -12.153  1.00 47.35  ? 736 HOH B O   1 
HETATM 16888 O O   . HOH AA 6 .   ? -12.383 -57.033 -26.944  1.00 60.98  ? 737 HOH B O   1 
HETATM 16889 O O   . HOH AA 6 .   ? -35.431 -40.384 -48.368  1.00 41.40  ? 738 HOH B O   1 
HETATM 16890 O O   . HOH AA 6 .   ? -12.310 -55.584 -31.840  1.00 52.82  ? 739 HOH B O   1 
HETATM 16891 O O   . HOH AA 6 .   ? -16.789 -15.613 -28.423  1.00 48.64  ? 740 HOH B O   1 
HETATM 16892 O O   . HOH AA 6 .   ? -29.205 -64.641 -18.720  1.00 30.45  ? 741 HOH B O   1 
HETATM 16893 O O   . HOH AA 6 .   ? -11.445 -41.557 -43.536  1.00 34.63  ? 742 HOH B O   1 
HETATM 16894 O O   . HOH AA 6 .   ? -8.613  -12.780 -21.435  1.00 38.29  ? 743 HOH B O   1 
HETATM 16895 O O   . HOH AA 6 .   ? -37.137 -58.997 -24.676  1.00 51.87  ? 744 HOH B O   1 
HETATM 16896 O O   . HOH AA 6 .   ? -14.810 -35.466 -25.860  1.00 42.26  ? 745 HOH B O   1 
HETATM 16897 O O   . HOH AA 6 .   ? -31.422 -51.130 -52.323  1.00 56.66  ? 746 HOH B O   1 
HETATM 16898 O O   . HOH AA 6 .   ? -41.171 -27.160 -19.787  1.00 60.46  ? 747 HOH B O   1 
HETATM 16899 O O   . HOH AA 6 .   ? -41.136 -26.854 -23.855  1.00 42.90  ? 748 HOH B O   1 
HETATM 16900 O O   . HOH AA 6 .   ? -43.618 -23.177 -28.234  1.00 44.55  ? 749 HOH B O   1 
HETATM 16901 O O   . HOH AA 6 .   ? -19.567 -60.680 -44.645  1.00 57.36  ? 750 HOH B O   1 
HETATM 16902 O O   . HOH AA 6 .   ? -17.883 -41.308 -29.201  1.00 53.99  ? 751 HOH B O   1 
HETATM 16903 O O   . HOH AA 6 .   ? -24.871 -10.000 4.588    1.00 50.26  ? 752 HOH B O   1 
HETATM 16904 O O   . HOH AA 6 .   ? -40.990 -51.817 -10.105  1.00 46.16  ? 753 HOH B O   1 
HETATM 16905 O O   . HOH AA 6 .   ? -20.236 -62.476 -42.368  1.00 60.43  ? 754 HOH B O   1 
HETATM 16906 O O   . HOH AA 6 .   ? -46.035 -48.660 -31.443  1.00 45.70  ? 755 HOH B O   1 
HETATM 16907 O O   . HOH AA 6 .   ? -9.285  -39.621 -34.013  1.00 40.35  ? 756 HOH B O   1 
HETATM 16908 O O   . HOH AA 6 .   ? -31.632 -62.793 -17.687  1.00 37.16  ? 757 HOH B O   1 
HETATM 16909 O O   . HOH AA 6 .   ? -43.138 -25.443 -29.576  1.00 44.33  ? 758 HOH B O   1 
HETATM 16910 O O   . HOH AA 6 .   ? -1.044  -12.335 -5.748   1.00 55.21  ? 759 HOH B O   1 
HETATM 16911 O O   . HOH AA 6 .   ? -41.287 -57.931 -24.198  1.00 54.92  ? 760 HOH B O   1 
HETATM 16912 O O   . HOH AA 6 .   ? -2.433  -12.115 -7.982   1.00 58.10  ? 761 HOH B O   1 
HETATM 16913 O O   . HOH AA 6 .   ? -42.867 -32.761 -36.428  1.00 48.25  ? 762 HOH B O   1 
HETATM 16914 O O   . HOH AA 6 .   ? -16.194 -4.096  -9.937   1.00 54.53  ? 763 HOH B O   1 
HETATM 16915 O O   . HOH AA 6 .   ? -17.004 -36.218 -27.171  1.00 37.88  ? 764 HOH B O   1 
HETATM 16916 O O   . HOH AA 6 .   ? -10.259 -11.014 -20.954  1.00 43.20  ? 765 HOH B O   1 
HETATM 16917 O O   . HOH AA 6 .   ? -31.532 -15.459 -26.478  1.00 57.74  ? 766 HOH B O   1 
HETATM 16918 O O   . HOH AA 6 .   ? -16.927 -39.120 -28.984  1.00 40.08  ? 767 HOH B O   1 
HETATM 16919 O O   . HOH AA 6 .   ? -39.970 -26.796 -21.400  1.00 45.69  ? 768 HOH B O   1 
HETATM 16920 O O   . HOH AA 6 .   ? -23.711 -17.372 -40.169  1.00 55.93  ? 769 HOH B O   1 
HETATM 16921 O O   . HOH AA 6 .   ? -37.293 -39.877 -49.271  1.00 59.12  ? 770 HOH B O   1 
HETATM 16922 O O   . HOH BA 6 .   ? 14.847  -27.456 -81.205  1.00 52.66  ? 601 HOH C O   1 
HETATM 16923 O O   . HOH BA 6 .   ? -17.324 -12.089 -55.729  1.00 60.44  ? 602 HOH C O   1 
HETATM 16924 O O   . HOH BA 6 .   ? -11.382 -25.012 -44.903  1.00 53.74  ? 603 HOH C O   1 
HETATM 16925 O O   . HOH BA 6 .   ? -5.444  -32.281 -62.054  1.00 49.52  ? 604 HOH C O   1 
HETATM 16926 O O   . HOH BA 6 .   ? -7.834  1.919   -66.604  1.00 27.75  ? 605 HOH C O   1 
HETATM 16927 O O   . HOH BA 6 .   ? -17.982 13.401  -72.273  1.00 42.82  ? 606 HOH C O   1 
HETATM 16928 O O   . HOH BA 6 .   ? 7.715   14.993  -68.394  1.00 64.06  ? 607 HOH C O   1 
HETATM 16929 O O   . HOH BA 6 .   ? 1.161   4.358   -44.549  1.00 42.64  ? 608 HOH C O   1 
HETATM 16930 O O   . HOH BA 6 .   ? -4.513  -6.505  -37.166  1.00 36.70  ? 609 HOH C O   1 
HETATM 16931 O O   . HOH BA 6 .   ? -16.189 16.355  -89.501  1.00 58.77  ? 610 HOH C O   1 
HETATM 16932 O O   . HOH BA 6 .   ? -17.274 -12.618 -53.642  1.00 54.54  ? 611 HOH C O   1 
HETATM 16933 O O   . HOH BA 6 .   ? -7.820  3.275   -73.297  1.00 39.86  ? 612 HOH C O   1 
HETATM 16934 O O   . HOH BA 6 .   ? 0.704   -18.727 -70.566  1.00 33.11  ? 613 HOH C O   1 
HETATM 16935 O O   . HOH BA 6 .   ? 9.728   -8.939  -57.925  1.00 42.85  ? 614 HOH C O   1 
HETATM 16936 O O   . HOH BA 6 .   ? -13.677 -1.915  -47.427  1.00 55.47  ? 615 HOH C O   1 
HETATM 16937 O O   . HOH BA 6 .   ? 6.876   -35.631 -79.995  1.00 30.36  ? 616 HOH C O   1 
HETATM 16938 O O   . HOH BA 6 .   ? 1.466   -32.061 -66.079  1.00 55.75  ? 617 HOH C O   1 
HETATM 16939 O O   . HOH BA 6 .   ? 6.808   7.787   -50.281  1.00 50.97  ? 618 HOH C O   1 
HETATM 16940 O O   . HOH BA 6 .   ? -12.050 5.072   -41.712  1.00 54.42  ? 619 HOH C O   1 
HETATM 16941 O O   . HOH BA 6 .   ? -2.126  -9.896  -91.007  1.00 55.46  ? 620 HOH C O   1 
HETATM 16942 O O   . HOH BA 6 .   ? -6.767  -26.624 -63.087  1.00 27.74  ? 621 HOH C O   1 
HETATM 16943 O O   . HOH BA 6 .   ? -17.361 -15.461 -85.454  1.00 38.09  ? 622 HOH C O   1 
HETATM 16944 O O   . HOH BA 6 .   ? -13.921 -24.338 -49.034  1.00 52.13  ? 623 HOH C O   1 
HETATM 16945 O O   . HOH BA 6 .   ? 7.397   -4.487  -52.968  1.00 63.93  ? 624 HOH C O   1 
HETATM 16946 O O   . HOH BA 6 .   ? -9.315  -4.404  -74.953  1.00 29.87  ? 625 HOH C O   1 
HETATM 16947 O O   . HOH BA 6 .   ? -6.867  -27.916 -72.110  1.00 36.18  ? 626 HOH C O   1 
HETATM 16948 O O   . HOH BA 6 .   ? -12.608 13.384  -72.176  1.00 41.39  ? 627 HOH C O   1 
HETATM 16949 O O   . HOH BA 6 .   ? 0.232   -26.698 -71.864  1.00 32.07  ? 628 HOH C O   1 
HETATM 16950 O O   . HOH BA 6 .   ? -9.283  2.689   -64.149  1.00 36.82  ? 629 HOH C O   1 
HETATM 16951 O O   . HOH BA 6 .   ? -3.587  -4.317  -42.328  1.00 39.15  ? 630 HOH C O   1 
HETATM 16952 O O   . HOH BA 6 .   ? 0.539   10.869  -64.912  1.00 42.30  ? 631 HOH C O   1 
HETATM 16953 O O   . HOH BA 6 .   ? 0.274   -15.612 -74.079  1.00 32.48  ? 632 HOH C O   1 
HETATM 16954 O O   . HOH BA 6 .   ? 3.496   -8.358  -62.393  1.00 42.64  ? 633 HOH C O   1 
HETATM 16955 O O   . HOH BA 6 .   ? 9.891   -23.630 -64.560  1.00 36.14  ? 634 HOH C O   1 
HETATM 16956 O O   . HOH BA 6 .   ? -6.693  -15.109 -52.271  1.00 28.68  ? 635 HOH C O   1 
HETATM 16957 O O   . HOH BA 6 .   ? -2.539  -1.668  -49.712  1.00 30.17  ? 636 HOH C O   1 
HETATM 16958 O O   . HOH BA 6 .   ? 10.938  -28.623 -57.479  1.00 42.38  ? 637 HOH C O   1 
HETATM 16959 O O   . HOH BA 6 .   ? -7.655  -16.374 -85.440  1.00 41.08  ? 638 HOH C O   1 
HETATM 16960 O O   . HOH BA 6 .   ? 3.511   -29.209 -73.409  1.00 33.93  ? 639 HOH C O   1 
HETATM 16961 O O   . HOH BA 6 .   ? 4.711   -2.150  -61.237  1.00 59.05  ? 640 HOH C O   1 
HETATM 16962 O O   . HOH BA 6 .   ? -9.098  -15.789 -80.037  1.00 27.39  ? 641 HOH C O   1 
HETATM 16963 O O   . HOH BA 6 .   ? -17.206 -16.284 -52.954  1.00 36.81  ? 642 HOH C O   1 
HETATM 16964 O O   . HOH BA 6 .   ? 9.270   -19.022 -78.709  1.00 37.03  ? 643 HOH C O   1 
HETATM 16965 O O   . HOH BA 6 .   ? -19.866 -22.452 -68.846  1.00 43.19  ? 644 HOH C O   1 
HETATM 16966 O O   . HOH BA 6 .   ? -13.860 -31.897 -83.484  1.00 54.14  ? 645 HOH C O   1 
HETATM 16967 O O   . HOH BA 6 .   ? -7.465  -28.551 -69.396  1.00 34.40  ? 646 HOH C O   1 
HETATM 16968 O O   . HOH BA 6 .   ? -4.461  20.585  -72.173  1.00 42.30  ? 647 HOH C O   1 
HETATM 16969 O O   . HOH BA 6 .   ? -4.865  -20.706 -60.040  1.00 24.41  ? 648 HOH C O   1 
HETATM 16970 O O   . HOH BA 6 .   ? -7.058  -19.809 -92.095  1.00 36.99  ? 649 HOH C O   1 
HETATM 16971 O O   . HOH BA 6 .   ? -3.204  -20.601 -45.895  1.00 50.90  ? 650 HOH C O   1 
HETATM 16972 O O   . HOH BA 6 .   ? -4.828  -4.687  -66.433  1.00 29.46  ? 651 HOH C O   1 
HETATM 16973 O O   . HOH BA 6 .   ? 0.784   -10.639 -68.469  1.00 36.97  ? 652 HOH C O   1 
HETATM 16974 O O   . HOH BA 6 .   ? -4.889  11.722  -59.714  1.00 34.46  ? 653 HOH C O   1 
HETATM 16975 O O   . HOH BA 6 .   ? -0.068  -5.851  -50.555  1.00 38.84  ? 654 HOH C O   1 
HETATM 16976 O O   . HOH BA 6 .   ? 1.670   7.602   -60.322  1.00 32.43  ? 655 HOH C O   1 
HETATM 16977 O O   . HOH BA 6 .   ? -12.104 -30.108 -63.479  1.00 43.19  ? 656 HOH C O   1 
HETATM 16978 O O   . HOH BA 6 .   ? 13.794  -16.283 -69.479  1.00 48.91  ? 657 HOH C O   1 
HETATM 16979 O O   . HOH BA 6 .   ? 0.576   -13.956 -66.447  1.00 25.27  ? 658 HOH C O   1 
HETATM 16980 O O   . HOH BA 6 .   ? -8.955  11.560  -64.601  1.00 39.10  ? 659 HOH C O   1 
HETATM 16981 O O   . HOH BA 6 .   ? 11.912  1.933   -66.518  1.00 39.91  ? 660 HOH C O   1 
HETATM 16982 O O   . HOH BA 6 .   ? 4.638   -9.510  -33.343  1.00 47.23  ? 661 HOH C O   1 
HETATM 16983 O O   . HOH BA 6 .   ? -18.181 -20.683 -70.820  1.00 35.14  ? 662 HOH C O   1 
HETATM 16984 O O   . HOH BA 6 .   ? -15.226 -26.575 -56.432  1.00 56.52  ? 663 HOH C O   1 
HETATM 16985 O O   . HOH BA 6 .   ? -6.891  -19.457 -45.938  1.00 49.44  ? 664 HOH C O   1 
HETATM 16986 O O   . HOH BA 6 .   ? -8.226  -23.829 -68.918  1.00 25.11  ? 665 HOH C O   1 
HETATM 16987 O O   . HOH BA 6 .   ? -2.645  -2.753  -72.495  1.00 35.29  ? 666 HOH C O   1 
HETATM 16988 O O   . HOH BA 6 .   ? 5.887   -25.161 -62.951  1.00 33.40  ? 667 HOH C O   1 
HETATM 16989 O O   . HOH BA 6 .   ? 9.103   -22.272 -60.527  1.00 36.73  ? 668 HOH C O   1 
HETATM 16990 O O   . HOH BA 6 .   ? -2.454  -19.476 -100.188 1.00 37.29  ? 669 HOH C O   1 
HETATM 16991 O O   . HOH BA 6 .   ? -1.384  14.945  -58.756  1.00 65.15  ? 670 HOH C O   1 
HETATM 16992 O O   . HOH BA 6 .   ? 9.105   -37.539 -90.548  1.00 53.13  ? 671 HOH C O   1 
HETATM 16993 O O   . HOH BA 6 .   ? -13.671 -23.969 -84.735  1.00 51.65  ? 672 HOH C O   1 
HETATM 16994 O O   . HOH BA 6 .   ? 6.681   -16.273 -66.918  1.00 35.44  ? 673 HOH C O   1 
HETATM 16995 O O   . HOH BA 6 .   ? 9.916   6.700   -81.220  1.00 60.40  ? 674 HOH C O   1 
HETATM 16996 O O   . HOH BA 6 .   ? 7.949   4.986   -47.900  1.00 55.61  ? 675 HOH C O   1 
HETATM 16997 O O   . HOH BA 6 .   ? -4.964  -13.013 -89.049  1.00 41.41  ? 676 HOH C O   1 
HETATM 16998 O O   . HOH BA 6 .   ? 10.575  -25.862 -76.434  1.00 54.39  ? 677 HOH C O   1 
HETATM 16999 O O   . HOH BA 6 .   ? 7.958   -16.046 -64.355  1.00 39.02  ? 678 HOH C O   1 
HETATM 17000 O O   . HOH BA 6 .   ? -2.534  -29.893 -101.211 1.00 45.42  ? 679 HOH C O   1 
HETATM 17001 O O   . HOH BA 6 .   ? -6.174  0.961   -38.303  1.00 31.63  ? 680 HOH C O   1 
HETATM 17002 O O   . HOH BA 6 .   ? 1.323   -30.392 -73.254  1.00 40.96  ? 681 HOH C O   1 
HETATM 17003 O O   . HOH BA 6 .   ? -5.196  -20.561 -46.627  1.00 54.12  ? 682 HOH C O   1 
HETATM 17004 O O   . HOH BA 6 .   ? 7.417   -28.569 -70.119  1.00 45.76  ? 683 HOH C O   1 
HETATM 17005 O O   . HOH BA 6 .   ? -19.369 -26.265 -62.496  1.00 48.38  ? 684 HOH C O   1 
HETATM 17006 O O   . HOH BA 6 .   ? -2.297  7.496   -89.393  1.00 49.62  ? 685 HOH C O   1 
HETATM 17007 O O   . HOH BA 6 .   ? 7.397   -0.000  -62.651  1.00 58.62  ? 686 HOH C O   1 
HETATM 17008 O O   . HOH BA 6 .   ? -2.823  -31.949 -57.589  1.00 47.98  ? 687 HOH C O   1 
HETATM 17009 O O   . HOH BA 6 .   ? -16.522 -21.506 -82.035  1.00 50.45  ? 688 HOH C O   1 
HETATM 17010 O O   . HOH BA 6 .   ? 5.794   -2.803  -35.342  1.00 46.21  ? 689 HOH C O   1 
HETATM 17011 O O   . HOH BA 6 .   ? 7.373   -39.409 -76.846  1.00 56.01  ? 690 HOH C O   1 
HETATM 17012 O O   . HOH BA 6 .   ? -1.905  11.429  -50.293  1.00 54.40  ? 691 HOH C O   1 
HETATM 17013 O O   . HOH BA 6 .   ? 0.966   -9.106  -64.815  1.00 35.14  ? 692 HOH C O   1 
HETATM 17014 O O   . HOH BA 6 .   ? 5.792   -15.392 -98.093  1.00 55.58  ? 693 HOH C O   1 
HETATM 17015 O O   . HOH BA 6 .   ? 8.407   14.013  -73.973  1.00 50.43  ? 694 HOH C O   1 
HETATM 17016 O O   . HOH BA 6 .   ? -8.834  -2.435  -36.066  1.00 60.93  ? 695 HOH C O   1 
HETATM 17017 O O   . HOH BA 6 .   ? -11.458 -4.525  -76.968  1.00 28.51  ? 696 HOH C O   1 
HETATM 17018 O O   . HOH BA 6 .   ? -3.375  15.249  -57.731  1.00 49.08  ? 697 HOH C O   1 
HETATM 17019 O O   . HOH BA 6 .   ? -2.714  11.608  -48.521  1.00 45.48  ? 698 HOH C O   1 
HETATM 17020 O O   . HOH BA 6 .   ? 4.770   -2.128  -37.571  1.00 41.42  ? 699 HOH C O   1 
HETATM 17021 O O   . HOH BA 6 .   ? 1.498   -0.124  -36.166  1.00 53.59  ? 700 HOH C O   1 
HETATM 17022 O O   . HOH BA 6 .   ? -15.407 11.818  -62.419  1.00 52.93  ? 701 HOH C O   1 
HETATM 17023 O O   . HOH BA 6 .   ? 2.444   -12.396 -66.750  1.00 32.41  ? 702 HOH C O   1 
HETATM 17024 O O   . HOH BA 6 .   ? -4.557  -3.499  -35.929  1.00 52.87  ? 703 HOH C O   1 
HETATM 17025 O O   . HOH BA 6 .   ? -0.095  -0.073  -33.970  1.00 57.90  ? 704 HOH C O   1 
HETATM 17026 O O   . HOH BA 6 .   ? 3.186   -10.008 -64.752  1.00 49.20  ? 705 HOH C O   1 
HETATM 17027 O O   . HOH BA 6 .   ? 9.949   -16.939 -76.567  1.00 42.53  ? 706 HOH C O   1 
HETATM 17028 O O   . HOH BA 6 .   ? -3.568  -0.741  -36.026  1.00 47.84  ? 707 HOH C O   1 
HETATM 17029 O O   . HOH CA 6 .   ? -0.250  -36.712 71.193   1.00 72.38  ? 601 HOH D O   1 
HETATM 17030 O O   . HOH CA 6 .   ? -6.973  -68.897 47.147   1.00 63.83  ? 602 HOH D O   1 
HETATM 17031 O O   . HOH CA 6 .   ? -9.929  -33.999 88.622   1.00 40.08  ? 603 HOH D O   1 
HETATM 17032 O O   . HOH CA 6 .   ? -2.553  -65.406 69.954   1.00 22.46  ? 604 HOH D O   1 
HETATM 17033 O O   . HOH CA 6 .   ? -8.480  -59.140 95.174   1.00 51.26  ? 605 HOH D O   1 
HETATM 17034 O O   . HOH CA 6 .   ? -8.989  -40.318 88.689   1.00 59.38  ? 606 HOH D O   1 
HETATM 17035 O O   . HOH CA 6 .   ? -13.150 -48.720 87.958   1.00 31.85  ? 607 HOH D O   1 
HETATM 17036 O O   . HOH CA 6 .   ? 11.042  -34.222 54.860   1.00 52.50  ? 608 HOH D O   1 
HETATM 17037 O O   . HOH CA 6 .   ? 15.038  -57.663 63.798   1.00 38.91  ? 609 HOH D O   1 
HETATM 17038 O O   . HOH CA 6 .   ? 10.989  -28.370 84.837   1.00 41.74  ? 610 HOH D O   1 
HETATM 17039 O O   . HOH CA 6 .   ? -9.279  -26.514 76.215   1.00 55.07  ? 611 HOH D O   1 
HETATM 17040 O O   . HOH CA 6 .   ? 6.010   -74.457 68.818   1.00 23.93  ? 612 HOH D O   1 
HETATM 17041 O O   . HOH CA 6 .   ? -17.597 -58.047 91.573   1.00 61.09  ? 613 HOH D O   1 
HETATM 17042 O O   . HOH CA 6 .   ? 13.576  -55.803 55.003   1.00 40.04  ? 614 HOH D O   1 
HETATM 17043 O O   . HOH CA 6 .   ? -1.843  -26.455 102.510  1.00 45.80  ? 615 HOH D O   1 
HETATM 17044 O O   . HOH CA 6 .   ? -7.091  -33.767 66.843   1.00 31.69  ? 616 HOH D O   1 
HETATM 17045 O O   . HOH CA 6 .   ? -0.089  -47.927 55.819   1.00 20.32  ? 617 HOH D O   1 
HETATM 17046 O O   . HOH CA 6 .   ? 9.677   -27.515 80.831   1.00 48.61  ? 618 HOH D O   1 
HETATM 17047 O O   . HOH CA 6 .   ? 0.737   -36.091 102.323  1.00 49.02  ? 619 HOH D O   1 
HETATM 17048 O O   . HOH CA 6 .   ? 6.408   -52.290 85.929   1.00 42.10  ? 620 HOH D O   1 
HETATM 17049 O O   . HOH CA 6 .   ? -7.464  -76.028 57.408   1.00 42.13  ? 621 HOH D O   1 
HETATM 17050 O O   . HOH CA 6 .   ? -3.360  -46.019 49.260   1.00 39.47  ? 622 HOH D O   1 
HETATM 17051 O O   . HOH CA 6 .   ? 7.700   -55.365 37.114   1.00 47.57  ? 623 HOH D O   1 
HETATM 17052 O O   . HOH CA 6 .   ? -7.771  -44.137 95.304   1.00 46.71  ? 624 HOH D O   1 
HETATM 17053 O O   . HOH CA 6 .   ? -3.790  -66.263 67.470   1.00 26.08  ? 625 HOH D O   1 
HETATM 17054 O O   . HOH CA 6 .   ? -12.647 -73.356 68.632   1.00 37.28  ? 626 HOH D O   1 
HETATM 17055 O O   . HOH CA 6 .   ? 3.606   -42.422 49.699   1.00 44.54  ? 627 HOH D O   1 
HETATM 17056 O O   . HOH CA 6 .   ? -3.101  -34.306 64.001   1.00 36.07  ? 628 HOH D O   1 
HETATM 17057 O O   . HOH CA 6 .   ? -7.848  -76.943 74.814   1.00 35.37  ? 629 HOH D O   1 
HETATM 17058 O O   . HOH CA 6 .   ? 5.390   -21.061 80.303   1.00 53.66  ? 630 HOH D O   1 
HETATM 17059 O O   . HOH CA 6 .   ? -19.823 -50.713 75.432   1.00 42.22  ? 631 HOH D O   1 
HETATM 17060 O O   . HOH CA 6 .   ? -0.030  -52.653 38.131   1.00 42.43  ? 632 HOH D O   1 
HETATM 17061 O O   . HOH CA 6 .   ? 7.164   -71.104 64.209   1.00 33.45  ? 633 HOH D O   1 
HETATM 17062 O O   . HOH CA 6 .   ? 6.284   -78.088 84.934   1.00 52.39  ? 634 HOH D O   1 
HETATM 17063 O O   . HOH CA 6 .   ? -12.533 -49.093 52.578   1.00 68.31  ? 635 HOH D O   1 
HETATM 17064 O O   . HOH CA 6 .   ? 14.898  -41.118 65.892   1.00 35.67  ? 636 HOH D O   1 
HETATM 17065 O O   . HOH CA 6 .   ? 5.549   -33.834 77.462   1.00 40.11  ? 637 HOH D O   1 
HETATM 17066 O O   . HOH CA 6 .   ? -3.324  -45.660 99.094   1.00 57.19  ? 638 HOH D O   1 
HETATM 17067 O O   . HOH CA 6 .   ? -3.088  -74.797 67.681   1.00 25.16  ? 639 HOH D O   1 
HETATM 17068 O O   . HOH CA 6 .   ? 10.272  -61.925 65.483   1.00 41.68  ? 640 HOH D O   1 
HETATM 17069 O O   . HOH CA 6 .   ? -11.439 -51.631 58.832   1.00 28.15  ? 641 HOH D O   1 
HETATM 17070 O O   . HOH CA 6 .   ? 10.114  -58.300 67.183   1.00 37.21  ? 642 HOH D O   1 
HETATM 17071 O O   . HOH CA 6 .   ? -5.558  -36.972 55.210   1.00 46.26  ? 643 HOH D O   1 
HETATM 17072 O O   . HOH CA 6 .   ? -3.720  -47.276 88.870   1.00 25.92  ? 644 HOH D O   1 
HETATM 17073 O O   . HOH CA 6 .   ? -3.221  -66.953 76.429   1.00 41.36  ? 645 HOH D O   1 
HETATM 17074 O O   . HOH CA 6 .   ? 5.149   -37.484 75.902   1.00 29.01  ? 646 HOH D O   1 
HETATM 17075 O O   . HOH CA 6 .   ? 6.813   -67.958 45.541   1.00 39.91  ? 647 HOH D O   1 
HETATM 17076 O O   . HOH CA 6 .   ? -8.491  -75.453 50.483   1.00 29.28  ? 648 HOH D O   1 
HETATM 17077 O O   . HOH CA 6 .   ? 12.195  -70.556 66.057   1.00 39.49  ? 649 HOH D O   1 
HETATM 17078 O O   . HOH CA 6 .   ? 17.777  -53.771 56.046   1.00 53.58  ? 650 HOH D O   1 
HETATM 17079 O O   . HOH CA 6 .   ? -17.854 -41.794 67.194   1.00 46.38  ? 651 HOH D O   1 
HETATM 17080 O O   . HOH CA 6 .   ? 4.018   -61.557 53.508   1.00 22.36  ? 652 HOH D O   1 
HETATM 17081 O O   . HOH CA 6 .   ? -4.772  -59.530 78.214   1.00 26.82  ? 653 HOH D O   1 
HETATM 17082 O O   . HOH CA 6 .   ? 10.021  -70.632 79.417   1.00 46.35  ? 654 HOH D O   1 
HETATM 17083 O O   . HOH CA 6 .   ? 5.739   -49.611 70.459   1.00 23.95  ? 655 HOH D O   1 
HETATM 17084 O O   . HOH CA 6 .   ? 12.465  -72.290 68.657   1.00 35.00  ? 656 HOH D O   1 
HETATM 17085 O O   . HOH CA 6 .   ? -13.270 -76.654 74.654   1.00 38.77  ? 657 HOH D O   1 
HETATM 17086 O O   . HOH CA 6 .   ? 5.743   -45.011 74.685   1.00 29.18  ? 658 HOH D O   1 
HETATM 17087 O O   . HOH CA 6 .   ? 18.697  -53.276 46.559   1.00 50.32  ? 659 HOH D O   1 
HETATM 17088 O O   . HOH CA 6 .   ? 6.024   -57.579 54.456   1.00 25.36  ? 660 HOH D O   1 
HETATM 17089 O O   . HOH CA 6 .   ? 11.311  -61.456 41.733   1.00 45.04  ? 661 HOH D O   1 
HETATM 17090 O O   . HOH CA 6 .   ? -6.366  -77.731 76.693   1.00 56.14  ? 662 HOH D O   1 
HETATM 17091 O O   . HOH CA 6 .   ? 4.884   -48.293 78.049   1.00 48.43  ? 663 HOH D O   1 
HETATM 17092 O O   . HOH CA 6 .   ? 13.302  -44.754 83.246   1.00 59.28  ? 664 HOH D O   1 
HETATM 17093 O O   . HOH CA 6 .   ? 1.941   -60.980 76.188   1.00 29.31  ? 665 HOH D O   1 
HETATM 17094 O O   . HOH CA 6 .   ? -1.210  -36.840 66.871   1.00 24.85  ? 666 HOH D O   1 
HETATM 17095 O O   . HOH CA 6 .   ? -9.219  -48.834 51.877   1.00 27.59  ? 667 HOH D O   1 
HETATM 17096 O O   . HOH CA 6 .   ? 13.365  -47.578 68.954   1.00 30.63  ? 668 HOH D O   1 
HETATM 17097 O O   . HOH CA 6 .   ? -6.989  -44.092 48.936   1.00 66.66  ? 669 HOH D O   1 
HETATM 17098 O O   . HOH CA 6 .   ? 13.661  -58.736 57.700   1.00 42.08  ? 670 HOH D O   1 
HETATM 17099 O O   . HOH CA 6 .   ? -4.971  -47.980 83.446   1.00 25.55  ? 671 HOH D O   1 
HETATM 17100 O O   . HOH CA 6 .   ? -17.692 -57.415 57.510   1.00 50.71  ? 672 HOH D O   1 
HETATM 17101 O O   . HOH CA 6 .   ? 13.358  -56.914 88.588   1.00 69.19  ? 673 HOH D O   1 
HETATM 17102 O O   . HOH CA 6 .   ? 1.244   -43.126 50.379   1.00 26.17  ? 674 HOH D O   1 
HETATM 17103 O O   . HOH CA 6 .   ? 14.396  -60.991 54.864   1.00 61.08  ? 675 HOH D O   1 
HETATM 17104 O O   . HOH CA 6 .   ? 12.308  -63.217 67.441   1.00 44.54  ? 676 HOH D O   1 
HETATM 17105 O O   . HOH CA 6 .   ? -3.113  -39.949 72.579   1.00 22.93  ? 677 HOH D O   1 
HETATM 17106 O O   . HOH CA 6 .   ? -13.650 -56.597 79.542   1.00 32.02  ? 678 HOH D O   1 
HETATM 17107 O O   . HOH CA 6 .   ? 8.730   -83.794 72.082   1.00 52.74  ? 679 HOH D O   1 
HETATM 17108 O O   . HOH CA 6 .   ? -13.311 -66.368 56.378   1.00 34.18  ? 680 HOH D O   1 
HETATM 17109 O O   . HOH CA 6 .   ? 9.051   -62.551 39.711   1.00 39.70  ? 681 HOH D O   1 
HETATM 17110 O O   . HOH CA 6 .   ? -10.928 -35.694 67.072   1.00 37.88  ? 682 HOH D O   1 
HETATM 17111 O O   . HOH CA 6 .   ? -11.221 -80.748 73.303   1.00 48.82  ? 683 HOH D O   1 
HETATM 17112 O O   . HOH CA 6 .   ? -13.014 -55.943 86.568   1.00 36.36  ? 684 HOH D O   1 
HETATM 17113 O O   . HOH CA 6 .   ? -2.159  -79.617 85.342   1.00 42.67  ? 685 HOH D O   1 
HETATM 17114 O O   . HOH CA 6 .   ? 1.883   -70.597 45.254   1.00 37.61  ? 686 HOH D O   1 
HETATM 17115 O O   . HOH CA 6 .   ? 1.590   -32.703 55.791   1.00 54.20  ? 687 HOH D O   1 
HETATM 17116 O O   . HOH CA 6 .   ? -12.636 -79.601 79.454   1.00 48.99  ? 688 HOH D O   1 
HETATM 17117 O O   . HOH CA 6 .   ? 0.814   -42.793 63.882   1.00 19.84  ? 689 HOH D O   1 
HETATM 17118 O O   . HOH CA 6 .   ? -5.235  -85.507 83.290   1.00 52.94  ? 690 HOH D O   1 
HETATM 17119 O O   . HOH CA 6 .   ? 21.294  -47.475 44.077   1.00 54.98  ? 691 HOH D O   1 
HETATM 17120 O O   . HOH CA 6 .   ? -13.223 -42.781 73.316   1.00 27.70  ? 692 HOH D O   1 
HETATM 17121 O O   . HOH CA 6 .   ? -0.332  -24.325 78.913   1.00 56.40  ? 693 HOH D O   1 
HETATM 17122 O O   . HOH CA 6 .   ? -2.790  -35.058 72.739   1.00 30.68  ? 694 HOH D O   1 
HETATM 17123 O O   . HOH CA 6 .   ? 4.002   -58.743 46.093   1.00 26.72  ? 695 HOH D O   1 
HETATM 17124 O O   . HOH CA 6 .   ? -11.213 -48.163 56.137   1.00 31.86  ? 696 HOH D O   1 
HETATM 17125 O O   . HOH CA 6 .   ? -4.519  -33.689 66.370   1.00 35.03  ? 697 HOH D O   1 
HETATM 17126 O O   . HOH CA 6 .   ? 11.400  -38.199 67.756   1.00 24.92  ? 698 HOH D O   1 
HETATM 17127 O O   . HOH CA 6 .   ? -13.085 -74.123 76.407   1.00 31.42  ? 699 HOH D O   1 
HETATM 17128 O O   . HOH CA 6 .   ? 0.276   -38.573 49.452   1.00 32.53  ? 700 HOH D O   1 
HETATM 17129 O O   . HOH CA 6 .   ? 11.571  -61.059 47.616   1.00 36.79  ? 701 HOH D O   1 
HETATM 17130 O O   . HOH CA 6 .   ? -2.296  -35.619 75.836   1.00 31.65  ? 702 HOH D O   1 
HETATM 17131 O O   . HOH CA 6 .   ? -4.154  -21.199 86.565   1.00 37.85  ? 703 HOH D O   1 
HETATM 17132 O O   . HOH CA 6 .   ? -16.347 -50.728 79.813   1.00 37.59  ? 704 HOH D O   1 
HETATM 17133 O O   . HOH CA 6 .   ? 3.113   -31.435 69.184   1.00 42.80  ? 705 HOH D O   1 
HETATM 17134 O O   . HOH CA 6 .   ? 2.090   -62.134 86.421   1.00 38.83  ? 706 HOH D O   1 
HETATM 17135 O O   . HOH CA 6 .   ? -15.206 -41.368 71.055   1.00 27.60  ? 707 HOH D O   1 
HETATM 17136 O O   . HOH CA 6 .   ? -16.933 -55.150 90.242   1.00 57.17  ? 708 HOH D O   1 
HETATM 17137 O O   . HOH CA 6 .   ? -7.759  -33.527 58.450   1.00 44.64  ? 709 HOH D O   1 
HETATM 17138 O O   . HOH CA 6 .   ? -6.732  -51.649 95.534   1.00 50.54  ? 710 HOH D O   1 
HETATM 17139 O O   . HOH CA 6 .   ? 8.588   -34.187 77.859   1.00 31.59  ? 711 HOH D O   1 
HETATM 17140 O O   . HOH CA 6 .   ? -6.786  -58.804 80.251   1.00 23.14  ? 712 HOH D O   1 
HETATM 17141 O O   . HOH CA 6 .   ? 0.691   -75.541 63.153   1.00 24.93  ? 713 HOH D O   1 
HETATM 17142 O O   . HOH CA 6 .   ? 7.090   -73.208 71.245   1.00 32.09  ? 714 HOH D O   1 
HETATM 17143 O O   . HOH CA 6 .   ? -11.198 -50.716 55.954   1.00 35.01  ? 715 HOH D O   1 
HETATM 17144 O O   . HOH CA 6 .   ? 13.005  -77.619 72.660   1.00 46.73  ? 716 HOH D O   1 
HETATM 17145 O O   . HOH CA 6 .   ? 12.783  -73.954 57.962   1.00 44.67  ? 717 HOH D O   1 
HETATM 17146 O O   . HOH CA 6 .   ? -13.985 -77.059 78.786   1.00 41.77  ? 718 HOH D O   1 
HETATM 17147 O O   . HOH CA 6 .   ? -2.959  -79.627 59.576   1.00 42.80  ? 719 HOH D O   1 
HETATM 17148 O O   . HOH CA 6 .   ? 11.942  -26.442 95.428   1.00 41.51  ? 720 HOH D O   1 
HETATM 17149 O O   . HOH CA 6 .   ? 0.559   -58.711 70.096   1.00 29.61  ? 721 HOH D O   1 
HETATM 17150 O O   . HOH CA 6 .   ? 5.969   -53.030 72.714   1.00 34.09  ? 722 HOH D O   1 
HETATM 17151 O O   . HOH CA 6 .   ? -15.521 -74.448 77.845   1.00 46.06  ? 723 HOH D O   1 
HETATM 17152 O O   . HOH CA 6 .   ? 12.357  -35.205 74.899   1.00 46.99  ? 724 HOH D O   1 
HETATM 17153 O O   . HOH CA 6 .   ? -10.308 -41.853 89.288   1.00 48.50  ? 725 HOH D O   1 
HETATM 17154 O O   . HOH CA 6 .   ? 3.556   -30.903 66.364   1.00 43.67  ? 726 HOH D O   1 
HETATM 17155 O O   . HOH CA 6 .   ? 8.852   -81.581 66.936   1.00 43.43  ? 727 HOH D O   1 
HETATM 17156 O O   . HOH CA 6 .   ? 12.082  -47.278 71.326   1.00 34.58  ? 728 HOH D O   1 
HETATM 17157 O O   . HOH CA 6 .   ? -17.306 -45.570 88.935   1.00 51.37  ? 729 HOH D O   1 
HETATM 17158 O O   . HOH CA 6 .   ? -9.518  -46.315 51.296   1.00 34.88  ? 730 HOH D O   1 
HETATM 17159 O O   . HOH CA 6 .   ? 13.130  -28.811 81.678   1.00 43.39  ? 731 HOH D O   1 
HETATM 17160 O O   . HOH CA 6 .   ? 1.453   -64.438 41.781   1.00 47.99  ? 732 HOH D O   1 
HETATM 17161 O O   . HOH CA 6 .   ? -8.840  -26.111 86.334   1.00 43.53  ? 733 HOH D O   1 
HETATM 17162 O O   . HOH CA 6 .   ? -1.754  -30.600 64.061   1.00 45.95  ? 734 HOH D O   1 
HETATM 17163 O O   . HOH CA 6 .   ? -3.224  -44.360 95.548   1.00 44.65  ? 735 HOH D O   1 
HETATM 17164 O O   . HOH CA 6 .   ? 15.152  -38.102 81.315   1.00 44.51  ? 736 HOH D O   1 
HETATM 17165 O O   . HOH CA 6 .   ? 0.690   -80.369 85.439   1.00 36.94  ? 737 HOH D O   1 
HETATM 17166 O O   . HOH CA 6 .   ? 15.667  -36.818 67.036   1.00 43.07  ? 738 HOH D O   1 
HETATM 17167 O O   . HOH CA 6 .   ? 23.842  -36.155 62.266   1.00 53.34  ? 739 HOH D O   1 
HETATM 17168 O O   . HOH CA 6 .   ? -25.083 -59.524 61.646   1.00 54.56  ? 740 HOH D O   1 
HETATM 17169 O O   . HOH CA 6 .   ? -20.175 -64.023 82.012   1.00 42.70  ? 741 HOH D O   1 
HETATM 17170 O O   . HOH CA 6 .   ? 8.449   -33.197 59.765   1.00 61.73  ? 742 HOH D O   1 
HETATM 17171 O O   . HOH CA 6 .   ? 9.970   -33.692 75.343   1.00 55.27  ? 743 HOH D O   1 
HETATM 17172 O O   . HOH CA 6 .   ? -8.226  -33.170 97.042   1.00 50.56  ? 744 HOH D O   1 
HETATM 17173 O O   . HOH CA 6 .   ? -13.073 -36.932 67.491   1.00 44.48  ? 745 HOH D O   1 
HETATM 17174 O O   . HOH CA 6 .   ? 6.495   -54.607 68.711   1.00 32.45  ? 746 HOH D O   1 
HETATM 17175 O O   . HOH CA 6 .   ? 1.359   -49.190 40.337   1.00 56.59  ? 747 HOH D O   1 
HETATM 17176 O O   . HOH CA 6 .   ? -1.462  -76.644 64.446   1.00 33.15  ? 748 HOH D O   1 
HETATM 17177 O O   . HOH CA 6 .   ? -17.571 -44.767 71.944   1.00 49.21  ? 749 HOH D O   1 
HETATM 17178 O O   . HOH CA 6 .   ? -17.204 -42.306 71.399   1.00 43.50  ? 750 HOH D O   1 
HETATM 17179 O O   . HOH CA 6 .   ? -5.264  -23.525 85.303   1.00 43.25  ? 751 HOH D O   1 
HETATM 17180 O O   . HOH CA 6 .   ? 1.675   -39.742 47.105   1.00 58.24  ? 752 HOH D O   1 
HETATM 17181 O O   . HOH CA 6 .   ? -20.451 -56.391 58.094   1.00 54.15  ? 753 HOH D O   1 
HETATM 17182 O O   . HOH CA 6 .   ? -7.964  -23.416 85.107   1.00 43.69  ? 754 HOH D O   1 
HETATM 17183 O O   . HOH CA 6 .   ? 4.197   -61.688 39.880   1.00 49.38  ? 755 HOH D O   1 
HETATM 17184 O O   . HOH CA 6 .   ? -13.544 -80.313 72.871   1.00 57.46  ? 756 HOH D O   1 
HETATM 17185 O O   . HOH CA 6 .   ? 13.970  -39.014 67.258   1.00 35.82  ? 757 HOH D O   1 
HETATM 17186 O O   . HOH CA 6 .   ? 15.170  -59.153 53.530   1.00 64.37  ? 758 HOH D O   1 
HETATM 17187 O O   . HOH CA 6 .   ? 12.944  -48.920 73.151   1.00 49.49  ? 759 HOH D O   1 
HETATM 17188 O O   . HOH CA 6 .   ? 10.410  -32.934 77.343   1.00 49.88  ? 760 HOH D O   1 
HETATM 17189 O O   . HOH CA 6 .   ? -17.192 -70.610 56.425   1.00 53.43  ? 761 HOH D O   1 
HETATM 17190 O O   . HOH CA 6 .   ? -15.944 -60.213 81.990   1.00 44.52  ? 762 HOH D O   1 
HETATM 17191 O O   . HOH CA 6 .   ? -15.428 -58.196 82.345   1.00 46.33  ? 763 HOH D O   1 
HETATM 17192 O O   . HOH CA 6 .   ? -1.773  -79.777 49.518   1.00 53.29  ? 764 HOH D O   1 
HETATM 17193 O O   . HOH CA 6 .   ? -8.331  -31.548 67.856   1.00 47.43  ? 765 HOH D O   1 
HETATM 17194 O O   . HOH CA 6 .   ? 14.286  -46.208 81.400   1.00 57.32  ? 766 HOH D O   1 
HETATM 17195 O O   . HOH CA 6 .   ? -13.706 -46.248 52.392   1.00 55.26  ? 767 HOH D O   1 
HETATM 17196 O O   . HOH CA 6 .   ? 7.537   -51.800 70.922   1.00 44.93  ? 768 HOH D O   1 
HETATM 17197 O O   . HOH CA 6 .   ? 12.379  -72.217 79.008   1.00 49.18  ? 769 HOH D O   1 
HETATM 17198 O O   . HOH CA 6 .   ? 7.743   -53.225 75.146   1.00 41.29  ? 770 HOH D O   1 
HETATM 17199 O O   . HOH CA 6 .   ? 13.611  -75.774 74.913   1.00 53.35  ? 771 HOH D O   1 
HETATM 17200 O O   . HOH CA 6 .   ? -9.132  -32.462 60.530   1.00 56.36  ? 772 HOH D O   1 
HETATM 17201 O O   . HOH CA 6 .   ? -16.088 -43.780 74.229   1.00 40.93  ? 773 HOH D O   1 
HETATM 17202 O O   . HOH CA 6 .   ? 1.765   -51.469 35.836   1.00 35.26  ? 774 HOH D O   1 
HETATM 17203 O O   . HOH CA 6 .   ? 17.525  -54.203 83.543   1.00 54.13  ? 775 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . LYS A 2   ? 0.5367 0.4015 0.3401 -0.0277 -0.0297 -0.0052 2   LYS A N   
2     C CA  . LYS A 2   ? 0.5575 0.4433 0.3872 -0.0324 -0.0300 -0.0075 2   LYS A CA  
3     C C   . LYS A 2   ? 0.5346 0.4382 0.3878 -0.0297 -0.0291 -0.0052 2   LYS A C   
4     O O   . LYS A 2   ? 0.6045 0.5185 0.4631 -0.0248 -0.0379 -0.0044 2   LYS A O   
5     C CB  . LYS A 2   ? 0.5704 0.4661 0.4018 -0.0355 -0.0424 -0.0115 2   LYS A CB  
6     C CG  . LYS A 2   ? 0.6330 0.5513 0.4906 -0.0406 -0.0445 -0.0136 2   LYS A CG  
7     C CD  . LYS A 2   ? 0.7246 0.6506 0.5808 -0.0458 -0.0560 -0.0180 2   LYS A CD  
8     C CE  . LYS A 2   ? 0.7492 0.7037 0.6309 -0.0473 -0.0635 -0.0193 2   LYS A CE  
9     N NZ  . LYS A 2   ? 0.7372 0.7022 0.6241 -0.0379 -0.0695 -0.0169 2   LYS A NZ  
10    N N   . LYS A 3   ? 0.4562 0.3633 0.3228 -0.0322 -0.0185 -0.0044 3   LYS A N   
11    C CA  . LYS A 3   ? 0.4054 0.3258 0.2914 -0.0301 -0.0160 -0.0021 3   LYS A CA  
12    C C   . LYS A 3   ? 0.3882 0.3289 0.2980 -0.0339 -0.0178 -0.0042 3   LYS A C   
13    O O   . LYS A 3   ? 0.3982 0.3396 0.3096 -0.0391 -0.0173 -0.0070 3   LYS A O   
14    C CB  . LYS A 3   ? 0.4105 0.3219 0.2953 -0.0307 -0.0034 0.0002  3   LYS A CB  
15    C CG  . LYS A 3   ? 0.5825 0.4730 0.4434 -0.0285 0.0004  0.0024  3   LYS A CG  
16    C CD  . LYS A 3   ? 0.6401 0.5289 0.5017 -0.0249 0.0013  0.0059  3   LYS A CD  
17    C CE  . LYS A 3   ? 0.7720 0.6371 0.6081 -0.0245 0.0075  0.0084  3   LYS A CE  
18    N NZ  . LYS A 3   ? 0.8344 0.6857 0.6473 -0.0194 -0.0022 0.0090  3   LYS A NZ  
19    N N   . LEU A 4   ? 0.3765 0.3317 0.3027 -0.0312 -0.0198 -0.0028 4   LEU A N   
20    C CA  . LEU A 4   ? 0.3215 0.2938 0.2699 -0.0347 -0.0184 -0.0039 4   LEU A CA  
21    C C   . LEU A 4   ? 0.3163 0.2855 0.2712 -0.0346 -0.0082 -0.0017 4   LEU A C   
22    O O   . LEU A 4   ? 0.3442 0.3090 0.2962 -0.0306 -0.0060 0.0010  4   LEU A O   
23    C CB  . LEU A 4   ? 0.2684 0.2596 0.2311 -0.0318 -0.0262 -0.0041 4   LEU A CB  
24    C CG  . LEU A 4   ? 0.3045 0.3127 0.2889 -0.0356 -0.0239 -0.0049 4   LEU A CG  
25    C CD1 . LEU A 4   ? 0.3592 0.3870 0.3550 -0.0367 -0.0326 -0.0075 4   LEU A CD1 
26    C CD2 . LEU A 4   ? 0.2921 0.3027 0.2861 -0.0320 -0.0182 -0.0022 4   LEU A CD2 
27    N N   . PHE A 5   ? 0.2454 0.2158 0.2076 -0.0388 -0.0024 -0.0029 5   PHE A N   
28    C CA  . PHE A 5   ? 0.2348 0.2047 0.2046 -0.0386 0.0064  -0.0013 5   PHE A CA  
29    C C   . PHE A 5   ? 0.2763 0.2616 0.2653 -0.0389 0.0053  -0.0009 5   PHE A C   
30    O O   . PHE A 5   ? 0.2890 0.2818 0.2860 -0.0421 0.0031  -0.0027 5   PHE A O   
31    C CB  . PHE A 5   ? 0.2962 0.2587 0.2624 -0.0410 0.0132  -0.0030 5   PHE A CB  
32    C CG  . PHE A 5   ? 0.4154 0.3619 0.3622 -0.0404 0.0167  -0.0034 5   PHE A CG  
33    C CD1 . PHE A 5   ? 0.4083 0.3470 0.3460 -0.0384 0.0205  -0.0012 5   PHE A CD1 
34    C CD2 . PHE A 5   ? 0.4127 0.3502 0.3484 -0.0423 0.0166  -0.0060 5   PHE A CD2 
35    C CE1 . PHE A 5   ? 0.4372 0.3601 0.3552 -0.0384 0.0245  -0.0015 5   PHE A CE1 
36    C CE2 . PHE A 5   ? 0.4214 0.3432 0.3376 -0.0416 0.0203  -0.0066 5   PHE A CE2 
37    C CZ  . PHE A 5   ? 0.4345 0.3496 0.3423 -0.0396 0.0245  -0.0042 5   PHE A CZ  
38    N N   . LEU A 6   ? 0.2454 0.2334 0.2396 -0.0360 0.0071  0.0013  6   LEU A N   
39    C CA  . LEU A 6   ? 0.2619 0.2630 0.2718 -0.0355 0.0057  0.0018  6   LEU A CA  
40    C C   . LEU A 6   ? 0.2665 0.2676 0.2839 -0.0365 0.0128  0.0027  6   LEU A C   
41    O O   . LEU A 6   ? 0.2687 0.2619 0.2804 -0.0360 0.0177  0.0040  6   LEU A O   
42    C CB  . LEU A 6   ? 0.2669 0.2707 0.2755 -0.0305 0.0008  0.0032  6   LEU A CB  
43    C CG  . LEU A 6   ? 0.3116 0.3283 0.3343 -0.0285 -0.0008 0.0036  6   LEU A CG  
44    C CD1 . LEU A 6   ? 0.3073 0.3387 0.3421 -0.0318 -0.0040 0.0014  6   LEU A CD1 
45    C CD2 . LEU A 6   ? 0.2952 0.3112 0.3127 -0.0216 -0.0055 0.0048  6   LEU A CD2 
46    N N   . VAL A 7   ? 0.2193 0.2289 0.2488 -0.0384 0.0134  0.0019  7   VAL A N   
47    C CA  . VAL A 7   ? 0.2819 0.2926 0.3188 -0.0390 0.0190  0.0024  7   VAL A CA  
48    C C   . VAL A 7   ? 0.2354 0.2558 0.2840 -0.0386 0.0171  0.0030  7   VAL A C   
49    O O   . VAL A 7   ? 0.2505 0.2770 0.3048 -0.0402 0.0148  0.0021  7   VAL A O   
50    C CB  . VAL A 7   ? 0.2516 0.2595 0.2884 -0.0406 0.0220  0.0007  7   VAL A CB  
51    C CG1 . VAL A 7   ? 0.3368 0.3469 0.3808 -0.0397 0.0274  0.0008  7   VAL A CG1 
52    C CG2 . VAL A 7   ? 0.3019 0.2994 0.3250 -0.0407 0.0233  -0.0004 7   VAL A CG2 
53    N N   . PHE A 8   ? 0.1807 0.2010 0.2311 -0.0370 0.0185  0.0045  8   PHE A N   
54    C CA  . PHE A 8   ? 0.1985 0.2260 0.2585 -0.0365 0.0178  0.0049  8   PHE A CA  
55    C C   . PHE A 8   ? 0.2335 0.2624 0.3000 -0.0382 0.0216  0.0046  8   PHE A C   
56    O O   . PHE A 8   ? 0.2356 0.2610 0.3005 -0.0390 0.0255  0.0046  8   PHE A O   
57    C CB  . PHE A 8   ? 0.2330 0.2578 0.2901 -0.0339 0.0172  0.0064  8   PHE A CB  
58    C CG  . PHE A 8   ? 0.3053 0.3311 0.3578 -0.0299 0.0124  0.0066  8   PHE A CG  
59    C CD1 . PHE A 8   ? 0.3271 0.3444 0.3677 -0.0279 0.0110  0.0072  8   PHE A CD1 
60    C CD2 . PHE A 8   ? 0.3363 0.3722 0.3962 -0.0277 0.0092  0.0060  8   PHE A CD2 
61    C CE1 . PHE A 8   ? 0.2897 0.3087 0.3259 -0.0229 0.0054  0.0071  8   PHE A CE1 
62    C CE2 . PHE A 8   ? 0.2533 0.2933 0.3108 -0.0229 0.0044  0.0057  8   PHE A CE2 
63    C CZ  . PHE A 8   ? 0.3154 0.3474 0.3614 -0.0201 0.0019  0.0062  8   PHE A CZ  
64    N N   . TRP A 9   ? 0.2438 0.2783 0.3174 -0.0387 0.0204  0.0042  9   TRP A N   
65    C CA  . TRP A 9   ? 0.1959 0.2319 0.2752 -0.0391 0.0225  0.0039  9   TRP A CA  
66    C C   . TRP A 9   ? 0.1408 0.1810 0.2252 -0.0389 0.0207  0.0044  9   TRP A C   
67    O O   . TRP A 9   ? 0.1485 0.1911 0.2339 -0.0395 0.0189  0.0042  9   TRP A O   
68    C CB  . TRP A 9   ? 0.1530 0.1870 0.2313 -0.0393 0.0229  0.0027  9   TRP A CB  
69    C CG  . TRP A 9   ? 0.1331 0.1681 0.2158 -0.0377 0.0249  0.0020  9   TRP A CG  
70    C CD1 . TRP A 9   ? 0.2103 0.2502 0.2997 -0.0371 0.0257  0.0020  9   TRP A CD1 
71    C CD2 . TRP A 9   ? 0.2011 0.2321 0.2812 -0.0360 0.0256  0.0007  9   TRP A CD2 
72    N NE1 . TRP A 9   ? 0.1582 0.1998 0.2510 -0.0345 0.0264  0.0008  9   TRP A NE1 
73    C CE2 . TRP A 9   ? 0.1857 0.2208 0.2722 -0.0331 0.0266  0.0001  9   TRP A CE2 
74    C CE3 . TRP A 9   ? 0.1992 0.2226 0.2713 -0.0365 0.0253  -0.0001 9   TRP A CE3 
75    C CZ2 . TRP A 9   ? 0.1714 0.2036 0.2566 -0.0291 0.0272  -0.0012 9   TRP A CZ2 
76    C CZ3 . TRP A 9   ? 0.2545 0.2723 0.3234 -0.0333 0.0264  -0.0014 9   TRP A CZ3 
77    C CH2 . TRP A 9   ? 0.2755 0.2979 0.3510 -0.0289 0.0274  -0.0018 9   TRP A CH2 
78    N N   . TRP A 10  ? 0.1959 0.2362 0.2821 -0.0387 0.0215  0.0049  10  TRP A N   
79    C CA  . TRP A 10  ? 0.2055 0.2479 0.2940 -0.0381 0.0199  0.0053  10  TRP A CA  
80    C C   . TRP A 10  ? 0.1657 0.2099 0.2588 -0.0387 0.0198  0.0048  10  TRP A C   
81    O O   . TRP A 10  ? 0.1653 0.2104 0.2612 -0.0393 0.0210  0.0042  10  TRP A O   
82    C CB  . TRP A 10  ? 0.1767 0.2153 0.2618 -0.0375 0.0203  0.0060  10  TRP A CB  
83    C CG  . TRP A 10  ? 0.1957 0.2304 0.2739 -0.0353 0.0195  0.0067  10  TRP A CG  
84    C CD1 . TRP A 10  ? 0.2395 0.2667 0.3103 -0.0355 0.0210  0.0073  10  TRP A CD1 
85    C CD2 . TRP A 10  ? 0.1940 0.2322 0.2715 -0.0319 0.0169  0.0067  10  TRP A CD2 
86    N NE1 . TRP A 10  ? 0.2212 0.2452 0.2852 -0.0316 0.0186  0.0079  10  TRP A NE1 
87    C CE2 . TRP A 10  ? 0.2101 0.2426 0.2795 -0.0291 0.0159  0.0073  10  TRP A CE2 
88    C CE3 . TRP A 10  ? 0.2639 0.3101 0.3467 -0.0312 0.0156  0.0060  10  TRP A CE3 
89    C CZ2 . TRP A 10  ? 0.1966 0.2329 0.2646 -0.0243 0.0127  0.0071  10  TRP A CZ2 
90    C CZ3 . TRP A 10  ? 0.2569 0.3087 0.3397 -0.0275 0.0134  0.0056  10  TRP A CZ3 
91    C CH2 . TRP A 10  ? 0.2120 0.2596 0.2881 -0.0236 0.0115  0.0061  10  TRP A CH2 
92    N N   . HIS A 11  ? 0.1442 0.1893 0.2378 -0.0385 0.0184  0.0048  11  HIS A N   
93    C CA  . HIS A 11  ? 0.2407 0.2854 0.3360 -0.0380 0.0174  0.0045  11  HIS A CA  
94    C C   . HIS A 11  ? 0.2225 0.2672 0.3181 -0.0380 0.0162  0.0047  11  HIS A C   
95    O O   . HIS A 11  ? 0.2275 0.2717 0.3206 -0.0380 0.0162  0.0052  11  HIS A O   
96    C CB  . HIS A 11  ? 0.2354 0.2771 0.3272 -0.0384 0.0169  0.0046  11  HIS A CB  
97    C CG  . HIS A 11  ? 0.2312 0.2696 0.3211 -0.0373 0.0153  0.0048  11  HIS A CG  
98    N ND1 . HIS A 11  ? 0.2204 0.2593 0.3129 -0.0345 0.0138  0.0042  11  HIS A ND1 
99    C CD2 . HIS A 11  ? 0.2549 0.2895 0.3400 -0.0384 0.0148  0.0054  11  HIS A CD2 
100   C CE1 . HIS A 11  ? 0.2447 0.2791 0.3330 -0.0333 0.0116  0.0045  11  HIS A CE1 
101   N NE2 . HIS A 11  ? 0.2394 0.2699 0.3222 -0.0359 0.0126  0.0054  11  HIS A NE2 
102   N N   . MET A 12  ? 0.2205 0.2667 0.3193 -0.0379 0.0151  0.0040  12  MET A N   
103   C CA  . MET A 12  ? 0.2012 0.2465 0.2992 -0.0385 0.0133  0.0037  12  MET A CA  
104   C C   . MET A 12  ? 0.2585 0.3040 0.3570 -0.0370 0.0102  0.0033  12  MET A C   
105   O O   . MET A 12  ? 0.1847 0.2346 0.2881 -0.0355 0.0091  0.0023  12  MET A O   
106   C CB  . MET A 12  ? 0.1812 0.2282 0.2819 -0.0412 0.0140  0.0029  12  MET A CB  
107   C CG  . MET A 12  ? 0.2309 0.2754 0.3291 -0.0424 0.0170  0.0035  12  MET A CG  
108   S SD  . MET A 12  ? 0.2125 0.2510 0.3032 -0.0401 0.0171  0.0046  12  MET A SD  
109   C CE  . MET A 12  ? 0.3986 0.4315 0.4839 -0.0408 0.0194  0.0052  12  MET A CE  
110   N N   . HIS A 13  ? 0.2293 0.2701 0.3220 -0.0366 0.0087  0.0038  13  HIS A N   
111   C CA  . HIS A 13  ? 0.1777 0.2162 0.2678 -0.0345 0.0051  0.0036  13  HIS A CA  
112   C C   . HIS A 13  ? 0.1890 0.2218 0.2720 -0.0352 0.0036  0.0037  13  HIS A C   
113   O O   . HIS A 13  ? 0.1483 0.1781 0.2271 -0.0363 0.0064  0.0043  13  HIS A O   
114   C CB  . HIS A 13  ? 0.1275 0.1609 0.2128 -0.0327 0.0057  0.0045  13  HIS A CB  
115   C CG  . HIS A 13  ? 0.2445 0.2705 0.3220 -0.0302 0.0023  0.0050  13  HIS A CG  
116   N ND1 . HIS A 13  ? 0.1767 0.2050 0.2564 -0.0265 -0.0025 0.0039  13  HIS A ND1 
117   C CD2 . HIS A 13  ? 0.2139 0.2300 0.2804 -0.0309 0.0029  0.0062  13  HIS A CD2 
118   C CE1 . HIS A 13  ? 0.1884 0.2069 0.2574 -0.0242 -0.0055 0.0048  13  HIS A CE1 
119   N NE2 . HIS A 13  ? 0.2523 0.2622 0.3123 -0.0273 -0.0018 0.0063  13  HIS A NE2 
120   N N   . GLN A 14  ? 0.1703 0.2023 0.2518 -0.0339 -0.0011 0.0029  14  GLN A N   
121   C CA  . GLN A 14  ? 0.1506 0.1745 0.2220 -0.0338 -0.0032 0.0030  14  GLN A CA  
122   C C   . GLN A 14  ? 0.2115 0.2326 0.2791 -0.0302 -0.0085 0.0030  14  GLN A C   
123   O O   . GLN A 14  ? 0.1812 0.2106 0.2572 -0.0283 -0.0123 0.0016  14  GLN A O   
124   C CB  . GLN A 14  ? 0.1462 0.1700 0.2169 -0.0364 -0.0048 0.0016  14  GLN A CB  
125   C CG  . GLN A 14  ? 0.1813 0.2039 0.2517 -0.0385 -0.0002 0.0017  14  GLN A CG  
126   C CD  . GLN A 14  ? 0.2967 0.3136 0.3595 -0.0372 0.0038  0.0028  14  GLN A CD  
127   O OE1 . GLN A 14  ? 0.2527 0.2640 0.3077 -0.0363 0.0035  0.0034  14  GLN A OE1 
128   N NE2 . GLN A 14  ? 0.2634 0.2821 0.3282 -0.0371 0.0078  0.0031  14  GLN A NE2 
129   N N   . PRO A 15  ? 0.2501 0.2601 0.3051 -0.0290 -0.0089 0.0043  15  PRO A N   
130   C CA  . PRO A 15  ? 0.2527 0.2568 0.3003 -0.0247 -0.0152 0.0043  15  PRO A CA  
131   C C   . PRO A 15  ? 0.2011 0.2092 0.2503 -0.0246 -0.0214 0.0023  15  PRO A C   
132   O O   . PRO A 15  ? 0.2561 0.2671 0.3080 -0.0287 -0.0201 0.0012  15  PRO A O   
133   C CB  . PRO A 15  ? 0.2279 0.2165 0.2584 -0.0252 -0.0127 0.0063  15  PRO A CB  
134   C CG  . PRO A 15  ? 0.2266 0.2161 0.2573 -0.0299 -0.0061 0.0065  15  PRO A CG  
135   C CD  . PRO A 15  ? 0.2067 0.2091 0.2529 -0.0313 -0.0033 0.0058  15  PRO A CD  
136   N N   . LEU A 16  ? 0.2177 0.2243 0.2633 -0.0198 -0.0286 0.0017  16  LEU A N   
137   C CA  . LEU A 16  ? 0.2578 0.2700 0.3057 -0.0200 -0.0359 -0.0007 16  LEU A CA  
138   C C   . LEU A 16  ? 0.3044 0.3021 0.3352 -0.0220 -0.0368 -0.0002 16  LEU A C   
139   O O   . LEU A 16  ? 0.2371 0.2209 0.2521 -0.0186 -0.0387 0.0014  16  LEU A O   
140   C CB  . LEU A 16  ? 0.2515 0.2695 0.3025 -0.0129 -0.0443 -0.0019 16  LEU A CB  
141   C CG  . LEU A 16  ? 0.2597 0.2880 0.3163 -0.0133 -0.0530 -0.0052 16  LEU A CG  
142   C CD1 . LEU A 16  ? 0.2689 0.3133 0.3425 -0.0208 -0.0502 -0.0077 16  LEU A CD1 
143   C CD2 . LEU A 16  ? 0.2089 0.2448 0.2695 -0.0040 -0.0618 -0.0065 16  LEU A CD2 
144   N N   . TYR A 17  ? 0.2872 0.2864 0.3194 -0.0274 -0.0350 -0.0016 17  TYR A N   
145   C CA  . TYR A 17  ? 0.2567 0.2421 0.2727 -0.0293 -0.0350 -0.0017 17  TYR A CA  
146   C C   . TYR A 17  ? 0.3132 0.2978 0.3242 -0.0291 -0.0447 -0.0040 17  TYR A C   
147   O O   . TYR A 17  ? 0.3413 0.3131 0.3368 -0.0305 -0.0457 -0.0045 17  TYR A O   
148   C CB  . TYR A 17  ? 0.2118 0.1966 0.2292 -0.0342 -0.0284 -0.0022 17  TYR A CB  
149   C CG  . TYR A 17  ? 0.2425 0.2279 0.2632 -0.0342 -0.0195 -0.0002 17  TYR A CG  
150   C CD1 . TYR A 17  ? 0.2661 0.2417 0.2752 -0.0330 -0.0145 0.0017  17  TYR A CD1 
151   C CD2 . TYR A 17  ? 0.2585 0.2549 0.2936 -0.0359 -0.0160 -0.0003 17  TYR A CD2 
152   C CE1 . TYR A 17  ? 0.2688 0.2477 0.2824 -0.0337 -0.0068 0.0031  17  TYR A CE1 
153   C CE2 . TYR A 17  ? 0.2915 0.2892 0.3294 -0.0357 -0.0090 0.0012  17  TYR A CE2 
154   C CZ  . TYR A 17  ? 0.2829 0.2730 0.3110 -0.0347 -0.0047 0.0028  17  TYR A CZ  
155   O OH  . TYR A 17  ? 0.2170 0.2113 0.2497 -0.0351 0.0018  0.0039  17  TYR A OH  
156   N N   . ARG A 18  ? 0.2886 0.2876 0.3127 -0.0275 -0.0517 -0.0060 18  ARG A N   
157   C CA  . ARG A 18  ? 0.2778 0.2810 0.3010 -0.0279 -0.0620 -0.0090 18  ARG A CA  
158   C C   . ARG A 18  ? 0.3524 0.3449 0.3608 -0.0202 -0.0691 -0.0078 18  ARG A C   
159   O O   . ARG A 18  ? 0.3299 0.3271 0.3428 -0.0134 -0.0717 -0.0069 18  ARG A O   
160   C CB  . ARG A 18  ? 0.2886 0.3152 0.3344 -0.0295 -0.0660 -0.0120 18  ARG A CB  
161   C CG  . ARG A 18  ? 0.2967 0.3318 0.3449 -0.0318 -0.0766 -0.0160 18  ARG A CG  
162   C CD  . ARG A 18  ? 0.2736 0.3355 0.3465 -0.0336 -0.0798 -0.0193 18  ARG A CD  
163   N NE  . ARG A 18  ? 0.3884 0.4602 0.4644 -0.0374 -0.0903 -0.0236 18  ARG A NE  
164   C CZ  . ARG A 18  ? 0.3726 0.4497 0.4470 -0.0302 -0.1016 -0.0251 18  ARG A CZ  
165   N NH1 . ARG A 18  ? 0.4111 0.4822 0.4792 -0.0185 -0.1036 -0.0225 18  ARG A NH1 
166   N NH2 . ARG A 18  ? 0.3878 0.4753 0.4658 -0.0349 -0.1114 -0.0295 18  ARG A NH2 
167   N N   . GLU A 19  ? 0.3414 0.3172 0.3297 -0.0210 -0.0716 -0.0077 19  GLU A N   
168   C CA  . GLU A 19  ? 0.3791 0.3414 0.3492 -0.0142 -0.0790 -0.0066 19  GLU A CA  
169   C C   . GLU A 19  ? 0.3800 0.3578 0.3604 -0.0099 -0.0920 -0.0096 19  GLU A C   
170   O O   . GLU A 19  ? 0.4051 0.3962 0.3962 -0.0153 -0.0970 -0.0134 19  GLU A O   
171   C CB  . GLU A 19  ? 0.3887 0.3307 0.3351 -0.0171 -0.0789 -0.0065 19  GLU A CB  
172   C CG  . GLU A 19  ? 0.4807 0.4002 0.4016 -0.0116 -0.0798 -0.0034 19  GLU A CG  
173   C CD  . GLU A 19  ? 0.5599 0.4761 0.4708 -0.0054 -0.0940 -0.0048 19  GLU A CD  
174   O OE1 . GLU A 19  ? 0.5439 0.4738 0.4650 -0.0072 -0.1031 -0.0086 19  GLU A OE1 
175   O OE2 . GLU A 19  ? 0.6295 0.5293 0.5221 0.0013  -0.0963 -0.0020 19  GLU A OE2 
176   N N   . PRO A 20  ? 0.4075 0.3847 0.3854 -0.0003 -0.0979 -0.0085 20  PRO A N   
177   C CA  . PRO A 20  ? 0.4688 0.4671 0.4626 0.0053  -0.1094 -0.0119 20  PRO A CA  
178   C C   . PRO A 20  ? 0.5333 0.5295 0.5165 0.0069  -0.1228 -0.0146 20  PRO A C   
179   O O   . PRO A 20  ? 0.5648 0.5834 0.5647 0.0092  -0.1328 -0.0186 20  PRO A O   
180   C CB  . PRO A 20  ? 0.4461 0.4404 0.4374 0.0166  -0.1100 -0.0094 20  PRO A CB  
181   C CG  . PRO A 20  ? 0.4183 0.3820 0.3816 0.0172  -0.1041 -0.0048 20  PRO A CG  
182   C CD  . PRO A 20  ? 0.3851 0.3429 0.3461 0.0060  -0.0937 -0.0042 20  PRO A CD  
183   N N   . TYR A 21  ? 0.5456 0.5170 0.5022 0.0055  -0.1233 -0.0130 21  TYR A N   
184   C CA  . TYR A 21  ? 0.5862 0.5531 0.5296 0.0071  -0.1366 -0.0156 21  TYR A CA  
185   C C   . TYR A 21  ? 0.5894 0.5609 0.5356 -0.0044 -0.1375 -0.0193 21  TYR A C   
186   O O   . TYR A 21  ? 0.6621 0.6442 0.6114 -0.0053 -0.1500 -0.0234 21  TYR A O   
187   C CB  . TYR A 21  ? 0.5594 0.4938 0.4681 0.0127  -0.1376 -0.0119 21  TYR A CB  
188   C CG  . TYR A 21  ? 0.5887 0.5160 0.4901 0.0252  -0.1413 -0.0089 21  TYR A CG  
189   C CD1 . TYR A 21  ? 0.6169 0.5492 0.5156 0.0358  -0.1568 -0.0107 21  TYR A CD1 
190   C CD2 . TYR A 21  ? 0.5753 0.4907 0.4721 0.0267  -0.1296 -0.0046 21  TYR A CD2 
191   C CE1 . TYR A 21  ? 0.6698 0.5930 0.5594 0.0486  -0.1604 -0.0081 21  TYR A CE1 
192   C CE2 . TYR A 21  ? 0.6213 0.5267 0.5085 0.0379  -0.1329 -0.0020 21  TYR A CE2 
193   C CZ  . TYR A 21  ? 0.6526 0.5608 0.5355 0.0493  -0.1482 -0.0037 21  TYR A CZ  
194   O OH  . TYR A 21  ? 0.6459 0.5417 0.5169 0.0618  -0.1519 -0.0012 21  TYR A OH  
195   N N   . THR A 22  ? 0.5595 0.5229 0.5039 -0.0129 -0.1250 -0.0181 22  THR A N   
196   C CA  . THR A 22  ? 0.5217 0.4874 0.4684 -0.0240 -0.1241 -0.0216 22  THR A CA  
197   C C   . THR A 22  ? 0.5303 0.5204 0.5057 -0.0310 -0.1197 -0.0239 22  THR A C   
198   O O   . THR A 22  ? 0.5859 0.5838 0.5674 -0.0401 -0.1230 -0.0279 22  THR A O   
199   C CB  . THR A 22  ? 0.4509 0.3918 0.3768 -0.0280 -0.1129 -0.0192 22  THR A CB  
200   O OG1 . THR A 22  ? 0.3619 0.3018 0.2939 -0.0262 -0.1001 -0.0153 22  THR A OG1 
201   C CG2 . THR A 22  ? 0.4275 0.3432 0.3228 -0.0235 -0.1169 -0.0177 22  THR A CG2 
202   N N   . GLY A 23  ? 0.5024 0.5030 0.4935 -0.0277 -0.1122 -0.0215 23  GLY A N   
203   C CA  . GLY A 23  ? 0.5023 0.5213 0.5164 -0.0348 -0.1057 -0.0230 23  GLY A CA  
204   C C   . GLY A 23  ? 0.5133 0.5190 0.5206 -0.0424 -0.0942 -0.0218 23  GLY A C   
205   O O   . GLY A 23  ? 0.5164 0.5333 0.5382 -0.0500 -0.0898 -0.0234 23  GLY A O   
206   N N   . GLU A 24  ? 0.4410 0.4232 0.4263 -0.0403 -0.0890 -0.0189 24  GLU A N   
207   C CA  . GLU A 24  ? 0.3850 0.3549 0.3633 -0.0455 -0.0783 -0.0180 24  GLU A CA  
208   C C   . GLU A 24  ? 0.3446 0.3153 0.3293 -0.0420 -0.0673 -0.0142 24  GLU A C   
209   O O   . GLU A 24  ? 0.3017 0.2683 0.2818 -0.0354 -0.0662 -0.0113 24  GLU A O   
210   C CB  . GLU A 24  ? 0.3943 0.3401 0.3457 -0.0454 -0.0781 -0.0178 24  GLU A CB  
211   C CG  . GLU A 24  ? 0.5179 0.4607 0.4614 -0.0509 -0.0881 -0.0221 24  GLU A CG  
212   C CD  . GLU A 24  ? 0.6787 0.5958 0.5939 -0.0508 -0.0869 -0.0221 24  GLU A CD  
213   O OE1 . GLU A 24  ? 0.6858 0.5902 0.5857 -0.0442 -0.0854 -0.0193 24  GLU A OE1 
214   O OE2 . GLU A 24  ? 0.7927 0.7010 0.6995 -0.0575 -0.0869 -0.0251 24  GLU A OE2 
215   N N   . TYR A 25  ? 0.3636 0.3386 0.3578 -0.0468 -0.0595 -0.0143 25  TYR A N   
216   C CA  . TYR A 25  ? 0.3674 0.3409 0.3647 -0.0444 -0.0490 -0.0111 25  TYR A CA  
217   C C   . TYR A 25  ? 0.3578 0.3120 0.3351 -0.0428 -0.0432 -0.0096 25  TYR A C   
218   O O   . TYR A 25  ? 0.4020 0.3465 0.3699 -0.0462 -0.0411 -0.0112 25  TYR A O   
219   C CB  . TYR A 25  ? 0.2884 0.2711 0.2998 -0.0493 -0.0434 -0.0117 25  TYR A CB  
220   C CG  . TYR A 25  ? 0.3051 0.3080 0.3373 -0.0500 -0.0459 -0.0125 25  TYR A CG  
221   C CD1 . TYR A 25  ? 0.3436 0.3585 0.3841 -0.0531 -0.0546 -0.0157 25  TYR A CD1 
222   C CD2 . TYR A 25  ? 0.3301 0.3409 0.3737 -0.0475 -0.0397 -0.0103 25  TYR A CD2 
223   C CE1 . TYR A 25  ? 0.3130 0.3487 0.3738 -0.0532 -0.0561 -0.0169 25  TYR A CE1 
224   C CE2 . TYR A 25  ? 0.3421 0.3707 0.4035 -0.0476 -0.0412 -0.0112 25  TYR A CE2 
225   C CZ  . TYR A 25  ? 0.3392 0.3807 0.4096 -0.0502 -0.0490 -0.0146 25  TYR A CZ  
226   O OH  . TYR A 25  ? 0.3092 0.3704 0.3984 -0.0497 -0.0497 -0.0159 25  TYR A OH  
227   N N   . LEU A 26  ? 0.3651 0.3134 0.3351 -0.0379 -0.0402 -0.0068 26  LEU A N   
228   C CA  . LEU A 26  ? 0.3941 0.3251 0.3441 -0.0364 -0.0351 -0.0057 26  LEU A CA  
229   C C   . LEU A 26  ? 0.4349 0.3655 0.3871 -0.0367 -0.0239 -0.0047 26  LEU A C   
230   O O   . LEU A 26  ? 0.3903 0.3088 0.3275 -0.0357 -0.0184 -0.0046 26  LEU A O   
231   C CB  . LEU A 26  ? 0.3090 0.2327 0.2486 -0.0321 -0.0363 -0.0032 26  LEU A CB  
232   C CG  . LEU A 26  ? 0.3707 0.2911 0.3028 -0.0300 -0.0483 -0.0044 26  LEU A CG  
233   C CD1 . LEU A 26  ? 0.4056 0.3151 0.3244 -0.0249 -0.0495 -0.0015 26  LEU A CD1 
234   C CD2 . LEU A 26  ? 0.3721 0.2806 0.2884 -0.0325 -0.0526 -0.0070 26  LEU A CD2 
235   N N   . LEU A 27  ? 0.3514 0.2955 0.3215 -0.0375 -0.0206 -0.0041 27  LEU A N   
236   C CA  . LEU A 27  ? 0.3488 0.2958 0.3239 -0.0370 -0.0115 -0.0033 27  LEU A CA  
237   C C   . LEU A 27  ? 0.3639 0.3202 0.3528 -0.0397 -0.0125 -0.0045 27  LEU A C   
238   O O   . LEU A 27  ? 0.3400 0.3062 0.3404 -0.0414 -0.0176 -0.0049 27  LEU A O   
239   C CB  . LEU A 27  ? 0.3172 0.2704 0.2984 -0.0351 -0.0062 -0.0007 27  LEU A CB  
240   C CG  . LEU A 27  ? 0.3545 0.2974 0.3208 -0.0339 -0.0021 0.0006  27  LEU A CG  
241   C CD1 . LEU A 27  ? 0.3363 0.2854 0.3093 -0.0339 0.0019  0.0030  27  LEU A CD1 
242   C CD2 . LEU A 27  ? 0.4163 0.3534 0.3738 -0.0331 0.0052  -0.0004 27  LEU A CD2 
243   N N   . PRO A 28  ? 0.2974 0.2501 0.2845 -0.0397 -0.0074 -0.0052 28  PRO A N   
244   C CA  . PRO A 28  ? 0.2704 0.2269 0.2656 -0.0429 -0.0081 -0.0063 28  PRO A CA  
245   C C   . PRO A 28  ? 0.3078 0.2762 0.3177 -0.0419 -0.0039 -0.0046 28  PRO A C   
246   O O   . PRO A 28  ? 0.2759 0.2445 0.2893 -0.0440 -0.0029 -0.0051 28  PRO A O   
247   C CB  . PRO A 28  ? 0.3135 0.2555 0.2944 -0.0419 -0.0047 -0.0077 28  PRO A CB  
248   C CG  . PRO A 28  ? 0.2733 0.2131 0.2482 -0.0360 0.0018  -0.0065 28  PRO A CG  
249   C CD  . PRO A 28  ? 0.3027 0.2472 0.2791 -0.0360 -0.0003 -0.0050 28  PRO A CD  
250   N N   . TRP A 29  ? 0.2176 0.1938 0.2340 -0.0392 -0.0017 -0.0026 29  TRP A N   
251   C CA  . TRP A 29  ? 0.2449 0.2302 0.2720 -0.0378 0.0028  -0.0011 29  TRP A CA  
252   C C   . TRP A 29  ? 0.2782 0.2720 0.3174 -0.0407 0.0006  -0.0013 29  TRP A C   
253   O O   . TRP A 29  ? 0.2464 0.2440 0.2911 -0.0402 0.0040  -0.0006 29  TRP A O   
254   C CB  . TRP A 29  ? 0.1771 0.1674 0.2068 -0.0359 0.0053  0.0006  29  TRP A CB  
255   C CG  . TRP A 29  ? 0.2791 0.2634 0.2984 -0.0338 0.0098  0.0008  29  TRP A CG  
256   C CD1 . TRP A 29  ? 0.2584 0.2382 0.2701 -0.0339 0.0102  0.0017  29  TRP A CD1 
257   C CD2 . TRP A 29  ? 0.3681 0.3505 0.3832 -0.0310 0.0152  0.0000  29  TRP A CD2 
258   N NE1 . TRP A 29  ? 0.3082 0.2846 0.3120 -0.0325 0.0162  0.0014  29  TRP A NE1 
259   C CE2 . TRP A 29  ? 0.3442 0.3233 0.3508 -0.0301 0.0193  0.0002  29  TRP A CE2 
260   C CE3 . TRP A 29  ? 0.3741 0.3567 0.3909 -0.0285 0.0171  -0.0008 29  TRP A CE3 
261   C CZ2 . TRP A 29  ? 0.3500 0.3290 0.3523 -0.0266 0.0255  -0.0008 29  TRP A CZ2 
262   C CZ3 . TRP A 29  ? 0.3918 0.3728 0.4032 -0.0239 0.0223  -0.0017 29  TRP A CZ3 
263   C CH2 . TRP A 29  ? 0.3868 0.3675 0.3921 -0.0229 0.0267  -0.0019 29  TRP A CH2 
264   N N   . THR A 30  ? 0.2740 0.2721 0.3176 -0.0433 -0.0048 -0.0022 30  THR A N   
265   C CA  . THR A 30  ? 0.2808 0.2884 0.3363 -0.0465 -0.0059 -0.0028 30  THR A CA  
266   C C   . THR A 30  ? 0.2976 0.2993 0.3495 -0.0509 -0.0047 -0.0041 30  THR A C   
267   O O   . THR A 30  ? 0.2704 0.2747 0.3272 -0.0524 -0.0015 -0.0036 30  THR A O   
268   C CB  . THR A 30  ? 0.2291 0.2448 0.2911 -0.0476 -0.0121 -0.0042 30  THR A CB  
269   O OG1 . THR A 30  ? 0.2758 0.2944 0.3394 -0.0428 -0.0127 -0.0026 30  THR A OG1 
270   C CG2 . THR A 30  ? 0.2051 0.2322 0.2797 -0.0518 -0.0124 -0.0055 30  THR A CG2 
271   N N   . PHE A 31  ? 0.2701 0.2614 0.3109 -0.0532 -0.0073 -0.0058 31  PHE A N   
272   C CA  . PHE A 31  ? 0.2803 0.2612 0.3133 -0.0576 -0.0061 -0.0071 31  PHE A CA  
273   C C   . PHE A 31  ? 0.2823 0.2555 0.3098 -0.0534 -0.0001 -0.0055 31  PHE A C   
274   O O   . PHE A 31  ? 0.2752 0.2460 0.3032 -0.0560 0.0022  -0.0053 31  PHE A O   
275   C CB  . PHE A 31  ? 0.3412 0.3091 0.3599 -0.0598 -0.0096 -0.0092 31  PHE A CB  
276   C CG  . PHE A 31  ? 0.3125 0.2650 0.3190 -0.0642 -0.0081 -0.0106 31  PHE A CG  
277   C CD1 . PHE A 31  ? 0.2908 0.2446 0.3003 -0.0737 -0.0105 -0.0126 31  PHE A CD1 
278   C CD2 . PHE A 31  ? 0.3266 0.2631 0.3183 -0.0590 -0.0041 -0.0102 31  PHE A CD2 
279   C CE1 . PHE A 31  ? 0.3459 0.2824 0.3415 -0.0788 -0.0088 -0.0138 31  PHE A CE1 
280   C CE2 . PHE A 31  ? 0.3883 0.3071 0.3659 -0.0623 -0.0028 -0.0114 31  PHE A CE2 
281   C CZ  . PHE A 31  ? 0.3993 0.3167 0.3779 -0.0727 -0.0051 -0.0131 31  PHE A CZ  
282   N N   . PHE A 32  ? 0.2866 0.2564 0.3086 -0.0467 0.0025  -0.0045 32  PHE A N   
283   C CA  . PHE A 32  ? 0.2799 0.2441 0.2968 -0.0413 0.0074  -0.0035 32  PHE A CA  
284   C C   . PHE A 32  ? 0.2540 0.2289 0.2824 -0.0399 0.0097  -0.0017 32  PHE A C   
285   O O   . PHE A 32  ? 0.2341 0.2033 0.2586 -0.0382 0.0119  -0.0012 32  PHE A O   
286   C CB  . PHE A 32  ? 0.2620 0.2237 0.2724 -0.0348 0.0100  -0.0035 32  PHE A CB  
287   C CG  . PHE A 32  ? 0.3442 0.2898 0.3381 -0.0341 0.0096  -0.0054 32  PHE A CG  
288   C CD1 . PHE A 32  ? 0.3158 0.2463 0.2980 -0.0350 0.0097  -0.0065 32  PHE A CD1 
289   C CD2 . PHE A 32  ? 0.3037 0.2468 0.2911 -0.0327 0.0093  -0.0060 32  PHE A CD2 
290   C CE1 . PHE A 32  ? 0.3564 0.2698 0.3213 -0.0343 0.0093  -0.0086 32  PHE A CE1 
291   C CE2 . PHE A 32  ? 0.3483 0.2754 0.3188 -0.0320 0.0091  -0.0080 32  PHE A CE2 
292   C CZ  . PHE A 32  ? 0.3108 0.2229 0.2700 -0.0326 0.0090  -0.0094 32  PHE A CZ  
293   N N   . HIS A 33  ? 0.2160 0.2044 0.2565 -0.0404 0.0090  -0.0008 33  HIS A N   
294   C CA  . HIS A 33  ? 0.1695 0.1664 0.2192 -0.0397 0.0110  0.0006  33  HIS A CA  
295   C C   . HIS A 33  ? 0.1878 0.1851 0.2410 -0.0453 0.0103  0.0002  33  HIS A C   
296   O O   . HIS A 33  ? 0.1607 0.1598 0.2166 -0.0450 0.0125  0.0012  33  HIS A O   
297   C CB  . HIS A 33  ? 0.1502 0.1587 0.2093 -0.0384 0.0109  0.0015  33  HIS A CB  
298   C CG  . HIS A 33  ? 0.1811 0.1911 0.2380 -0.0339 0.0135  0.0021  33  HIS A CG  
299   N ND1 . HIS A 33  ? 0.2301 0.2425 0.2875 -0.0300 0.0163  0.0025  33  HIS A ND1 
300   C CD2 . HIS A 33  ? 0.2187 0.2280 0.2720 -0.0330 0.0138  0.0020  33  HIS A CD2 
301   C CE1 . HIS A 33  ? 0.2357 0.2517 0.2924 -0.0274 0.0186  0.0024  33  HIS A CE1 
302   N NE2 . HIS A 33  ? 0.2343 0.2475 0.2877 -0.0295 0.0177  0.0022  33  HIS A NE2 
303   N N   . ALA A 34  ? 0.2198 0.2157 0.2725 -0.0509 0.0074  -0.0014 34  ALA A N   
304   C CA  . ALA A 34  ? 0.2877 0.2844 0.3434 -0.0577 0.0078  -0.0022 34  ALA A CA  
305   C C   . ALA A 34  ? 0.3644 0.3447 0.4065 -0.0592 0.0104  -0.0021 34  ALA A C   
306   O O   . ALA A 34  ? 0.3549 0.3331 0.3965 -0.0608 0.0133  -0.0011 34  ALA A O   
307   C CB  . ALA A 34  ? 0.2243 0.2270 0.2850 -0.0638 0.0036  -0.0046 34  ALA A CB  
308   N N   . VAL A 35  ? 0.2885 0.2547 0.3172 -0.0580 0.0094  -0.0029 35  VAL A N   
309   C CA  . VAL A 35  ? 0.3037 0.2508 0.3165 -0.0589 0.0116  -0.0029 35  VAL A CA  
310   C C   . VAL A 35  ? 0.2486 0.1923 0.2577 -0.0503 0.0146  -0.0007 35  VAL A C   
311   O O   . VAL A 35  ? 0.2934 0.2231 0.2911 -0.0504 0.0165  0.0000  35  VAL A O   
312   C CB  . VAL A 35  ? 0.3035 0.2340 0.3005 -0.0590 0.0100  -0.0046 35  VAL A CB  
313   C CG1 . VAL A 35  ? 0.2838 0.2176 0.2837 -0.0684 0.0059  -0.0072 35  VAL A CG1 
314   C CG2 . VAL A 35  ? 0.2334 0.1646 0.2280 -0.0490 0.0103  -0.0043 35  VAL A CG2 
315   N N   . LYS A 36  ? 0.3023 0.2578 0.3197 -0.0429 0.0147  0.0002  36  LYS A N   
316   C CA  . LYS A 36  ? 0.3210 0.2768 0.3369 -0.0344 0.0166  0.0016  36  LYS A CA  
317   C C   . LYS A 36  ? 0.2872 0.2541 0.3134 -0.0352 0.0174  0.0031  36  LYS A C   
318   O O   . LYS A 36  ? 0.2659 0.2262 0.2858 -0.0322 0.0185  0.0042  36  LYS A O   
319   C CB  . LYS A 36  ? 0.2837 0.2477 0.3032 -0.0272 0.0169  0.0013  36  LYS A CB  
320   C CG  . LYS A 36  ? 0.2448 0.2108 0.2630 -0.0180 0.0184  0.0020  36  LYS A CG  
321   C CD  . LYS A 36  ? 0.2656 0.2392 0.2861 -0.0113 0.0198  0.0010  36  LYS A CD  
322   C CE  . LYS A 36  ? 0.3167 0.3089 0.3520 -0.0136 0.0202  0.0014  36  LYS A CE  
323   N NZ  . LYS A 36  ? 0.3108 0.3142 0.3554 -0.0124 0.0199  0.0025  36  LYS A NZ  
324   N N   . ASP A 37  ? 0.2826 0.2648 0.3228 -0.0384 0.0167  0.0031  37  ASP A N   
325   C CA  . ASP A 37  ? 0.2745 0.2669 0.3236 -0.0377 0.0176  0.0042  37  ASP A CA  
326   C C   . ASP A 37  ? 0.3032 0.3014 0.3597 -0.0446 0.0181  0.0040  37  ASP A C   
327   O O   . ASP A 37  ? 0.2793 0.2782 0.3363 -0.0451 0.0199  0.0048  37  ASP A O   
328   C CB  . ASP A 37  ? 0.2470 0.2520 0.3050 -0.0338 0.0170  0.0044  37  ASP A CB  
329   C CG  . ASP A 37  ? 0.3042 0.3071 0.3572 -0.0279 0.0173  0.0040  37  ASP A CG  
330   O OD1 . ASP A 37  ? 0.2730 0.2734 0.3214 -0.0220 0.0179  0.0043  37  ASP A OD1 
331   O OD2 . ASP A 37  ? 0.2138 0.2174 0.2667 -0.0285 0.0169  0.0032  37  ASP A OD2 
332   N N   . TYR A 38  ? 0.2009 0.2041 0.2631 -0.0494 0.0166  0.0026  38  TYR A N   
333   C CA  . TYR A 38  ? 0.2346 0.2490 0.3078 -0.0535 0.0171  0.0020  38  TYR A CA  
334   C C   . TYR A 38  ? 0.2707 0.2806 0.3409 -0.0597 0.0202  0.0018  38  TYR A C   
335   O O   . TYR A 38  ? 0.2595 0.2770 0.3364 -0.0612 0.0225  0.0018  38  TYR A O   
336   C CB  . TYR A 38  ? 0.2355 0.2586 0.3166 -0.0555 0.0138  0.0004  38  TYR A CB  
337   C CG  . TYR A 38  ? 0.2077 0.2350 0.2912 -0.0500 0.0116  0.0009  38  TYR A CG  
338   C CD1 . TYR A 38  ? 0.1613 0.1913 0.2464 -0.0457 0.0131  0.0023  38  TYR A CD1 
339   C CD2 . TYR A 38  ? 0.2614 0.2888 0.3440 -0.0500 0.0079  -0.0001 38  TYR A CD2 
340   C CE1 . TYR A 38  ? 0.2576 0.2900 0.3435 -0.0424 0.0119  0.0028  38  TYR A CE1 
341   C CE2 . TYR A 38  ? 0.2216 0.2502 0.3036 -0.0457 0.0066  0.0007  38  TYR A CE2 
342   C CZ  . TYR A 38  ? 0.2879 0.3188 0.3715 -0.0424 0.0089  0.0021  38  TYR A CZ  
343   O OH  . TYR A 38  ? 0.2617 0.2924 0.3433 -0.0398 0.0083  0.0028  38  TYR A OH  
344   N N   . TYR A 39  ? 0.2648 0.2610 0.3235 -0.0635 0.0208  0.0014  39  TYR A N   
345   C CA  . TYR A 39  ? 0.2846 0.2730 0.3368 -0.0700 0.0246  0.0016  39  TYR A CA  
346   C C   . TYR A 39  ? 0.2798 0.2559 0.3201 -0.0647 0.0266  0.0039  39  TYR A C   
347   O O   . TYR A 39  ? 0.2137 0.1882 0.2520 -0.0670 0.0301  0.0048  39  TYR A O   
348   C CB  . TYR A 39  ? 0.2493 0.2256 0.2918 -0.0779 0.0245  0.0001  39  TYR A CB  
349   C CG  . TYR A 39  ? 0.3365 0.2986 0.3668 -0.0852 0.0292  0.0006  39  TYR A CG  
350   C CD1 . TYR A 39  ? 0.3095 0.2808 0.3477 -0.0954 0.0326  -0.0009 39  TYR A CD1 
351   C CD2 . TYR A 39  ? 0.3202 0.2592 0.3301 -0.0817 0.0303  0.0025  39  TYR A CD2 
352   C CE1 . TYR A 39  ? 0.3348 0.2917 0.3600 -0.1035 0.0379  -0.0004 39  TYR A CE1 
353   C CE2 . TYR A 39  ? 0.3683 0.2908 0.3636 -0.0886 0.0347  0.0033  39  TYR A CE2 
354   C CZ  . TYR A 39  ? 0.3577 0.2885 0.3602 -0.1002 0.0388  0.0019  39  TYR A CZ  
355   O OH  . TYR A 39  ? 0.3144 0.2270 0.3003 -0.1081 0.0441  0.0028  39  TYR A OH  
356   N N   . ASP A 40  ? 0.2531 0.2213 0.2856 -0.0569 0.0244  0.0048  40  ASP A N   
357   C CA  . ASP A 40  ? 0.2925 0.2475 0.3116 -0.0509 0.0251  0.0067  40  ASP A CA  
358   C C   . ASP A 40  ? 0.3195 0.2845 0.3452 -0.0461 0.0252  0.0078  40  ASP A C   
359   O O   . ASP A 40  ? 0.3563 0.3113 0.3715 -0.0441 0.0262  0.0093  40  ASP A O   
360   C CB  . ASP A 40  ? 0.3487 0.2948 0.3589 -0.0433 0.0228  0.0066  40  ASP A CB  
361   C CG  . ASP A 40  ? 0.3633 0.2875 0.3556 -0.0467 0.0235  0.0062  40  ASP A CG  
362   O OD1 . ASP A 40  ? 0.4018 0.3100 0.3797 -0.0472 0.0253  0.0075  40  ASP A OD1 
363   O OD2 . ASP A 40  ? 0.2922 0.2136 0.2832 -0.0496 0.0223  0.0045  40  ASP A OD2 
364   N N   . MET A 41  ? 0.3228 0.3053 0.3638 -0.0446 0.0239  0.0072  41  MET A N   
365   C CA  . MET A 41  ? 0.3290 0.3195 0.3749 -0.0412 0.0238  0.0080  41  MET A CA  
366   C C   . MET A 41  ? 0.3140 0.3028 0.3585 -0.0463 0.0272  0.0083  41  MET A C   
367   O O   . MET A 41  ? 0.2958 0.2779 0.3318 -0.0435 0.0276  0.0096  41  MET A O   
368   C CB  . MET A 41  ? 0.2241 0.2302 0.2837 -0.0396 0.0220  0.0072  41  MET A CB  
369   C CG  . MET A 41  ? 0.2497 0.2581 0.3093 -0.0335 0.0196  0.0071  41  MET A CG  
370   S SD  . MET A 41  ? 0.2642 0.2725 0.3190 -0.0263 0.0181  0.0080  41  MET A SD  
371   C CE  . MET A 41  ? 0.3170 0.3395 0.3830 -0.0279 0.0176  0.0076  41  MET A CE  
372   N N   . PRO A 42  ? 0.3018 0.2966 0.3536 -0.0533 0.0298  0.0071  42  PRO A N   
373   C CA  . PRO A 42  ? 0.2403 0.2321 0.2887 -0.0585 0.0345  0.0072  42  PRO A CA  
374   C C   . PRO A 42  ? 0.2803 0.2528 0.3111 -0.0621 0.0371  0.0084  42  PRO A C   
375   O O   . PRO A 42  ? 0.3407 0.3059 0.3630 -0.0643 0.0408  0.0093  42  PRO A O   
376   C CB  . PRO A 42  ? 0.2209 0.2268 0.2834 -0.0646 0.0364  0.0050  42  PRO A CB  
377   C CG  . PRO A 42  ? 0.2144 0.2236 0.2818 -0.0643 0.0322  0.0040  42  PRO A CG  
378   C CD  . PRO A 42  ? 0.2561 0.2622 0.3201 -0.0562 0.0285  0.0053  42  PRO A CD  
379   N N   . ALA A 43  ? 0.2342 0.1956 0.2566 -0.0630 0.0355  0.0084  43  ALA A N   
380   C CA  . ALA A 43  ? 0.3149 0.2541 0.3173 -0.0668 0.0383  0.0096  43  ALA A CA  
381   C C   . ALA A 43  ? 0.3616 0.2863 0.3481 -0.0590 0.0372  0.0120  43  ALA A C   
382   O O   . ALA A 43  ? 0.3241 0.2292 0.2921 -0.0621 0.0402  0.0134  43  ALA A O   
383   C CB  . ALA A 43  ? 0.2630 0.1900 0.2568 -0.0685 0.0365  0.0089  43  ALA A CB  
384   N N   . TYR A 44  ? 0.3566 0.2904 0.3491 -0.0492 0.0329  0.0124  44  TYR A N   
385   C CA  . TYR A 44  ? 0.3601 0.2835 0.3394 -0.0418 0.0310  0.0143  44  TYR A CA  
386   C C   . TYR A 44  ? 0.3558 0.2736 0.3279 -0.0469 0.0353  0.0152  44  TYR A C   
387   O O   . TYR A 44  ? 0.3782 0.2781 0.3312 -0.0438 0.0352  0.0171  44  TYR A O   
388   C CB  . TYR A 44  ? 0.3092 0.2490 0.3005 -0.0330 0.0260  0.0138  44  TYR A CB  
389   C CG  . TYR A 44  ? 0.3263 0.2678 0.3187 -0.0251 0.0219  0.0134  44  TYR A CG  
390   C CD1 . TYR A 44  ? 0.3259 0.2559 0.3045 -0.0155 0.0185  0.0143  44  TYR A CD1 
391   C CD2 . TYR A 44  ? 0.3089 0.2633 0.3152 -0.0264 0.0215  0.0118  44  TYR A CD2 
392   C CE1 . TYR A 44  ? 0.3238 0.2574 0.3043 -0.0073 0.0154  0.0135  44  TYR A CE1 
393   C CE2 . TYR A 44  ? 0.2736 0.2297 0.2803 -0.0193 0.0188  0.0112  44  TYR A CE2 
394   C CZ  . TYR A 44  ? 0.3108 0.2574 0.3054 -0.0096 0.0161  0.0119  44  TYR A CZ  
395   O OH  . TYR A 44  ? 0.2972 0.2470 0.2928 -0.0015 0.0140  0.0108  44  TYR A OH  
396   N N   . LEU A 45  ? 0.3790 0.3114 0.3654 -0.0539 0.0392  0.0138  45  LEU A N   
397   C CA  . LEU A 45  ? 0.4263 0.3552 0.4070 -0.0588 0.0445  0.0142  45  LEU A CA  
398   C C   . LEU A 45  ? 0.4065 0.3144 0.3682 -0.0668 0.0501  0.0153  45  LEU A C   
399   O O   . LEU A 45  ? 0.3317 0.2308 0.2824 -0.0702 0.0549  0.0162  45  LEU A O   
400   C CB  . LEU A 45  ? 0.2992 0.2497 0.3004 -0.0634 0.0476  0.0119  45  LEU A CB  
401   C CG  . LEU A 45  ? 0.2895 0.2566 0.3052 -0.0566 0.0432  0.0110  45  LEU A CG  
402   C CD1 . LEU A 45  ? 0.2536 0.2389 0.2874 -0.0602 0.0459  0.0087  45  LEU A CD1 
403   C CD2 . LEU A 45  ? 0.2559 0.2178 0.2623 -0.0512 0.0414  0.0121  45  LEU A CD2 
404   N N   . LYS A 46  ? 0.4229 0.3209 0.3788 -0.0705 0.0501  0.0152  46  LYS A N   
405   C CA  . LYS A 46  ? 0.5162 0.3895 0.4498 -0.0783 0.0551  0.0164  46  LYS A CA  
406   C C   . LYS A 46  ? 0.5562 0.4032 0.4631 -0.0702 0.0524  0.0194  46  LYS A C   
407   O O   . LYS A 46  ? 0.5369 0.3607 0.4213 -0.0759 0.0573  0.0211  46  LYS A O   
408   C CB  . LYS A 46  ? 0.5727 0.4400 0.5050 -0.0843 0.0549  0.0152  46  LYS A CB  
409   C CG  . LYS A 46  ? 0.5699 0.4613 0.5263 -0.0931 0.0568  0.0120  46  LYS A CG  
410   C CD  . LYS A 46  ? 0.6437 0.5293 0.5984 -0.0962 0.0540  0.0107  46  LYS A CD  
411   C CE  . LYS A 46  ? 0.7190 0.6157 0.6847 -0.1109 0.0583  0.0078  46  LYS A CE  
412   N NZ  . LYS A 46  ? 0.7758 0.6474 0.7204 -0.1211 0.0610  0.0077  46  LYS A NZ  
413   N N   . ASP A 47  ? 0.5828 0.4328 0.4909 -0.0569 0.0449  0.0201  47  ASP A N   
414   C CA  . ASP A 47  ? 0.5577 0.3843 0.4414 -0.0471 0.0408  0.0225  47  ASP A CA  
415   C C   . ASP A 47  ? 0.4775 0.3106 0.3615 -0.0380 0.0365  0.0234  47  ASP A C   
416   O O   . ASP A 47  ? 0.5149 0.3284 0.3771 -0.0298 0.0328  0.0254  47  ASP A O   
417   C CB  . ASP A 47  ? 0.5430 0.3652 0.4245 -0.0377 0.0349  0.0223  47  ASP A CB  
418   C CG  . ASP A 47  ? 0.6109 0.4221 0.4875 -0.0462 0.0383  0.0214  47  ASP A CG  
419   O OD1 . ASP A 47  ? 0.5454 0.3377 0.4061 -0.0571 0.0442  0.0221  47  ASP A OD1 
420   O OD2 . ASP A 47  ? 0.5985 0.4191 0.4862 -0.0427 0.0351  0.0197  47  ASP A OD2 
421   N N   . PHE A 48  ? 0.4531 0.3117 0.3594 -0.0389 0.0362  0.0217  48  PHE A N   
422   C CA  . PHE A 48  ? 0.4640 0.3304 0.3720 -0.0312 0.0315  0.0219  48  PHE A CA  
423   C C   . PHE A 48  ? 0.4675 0.3432 0.3827 -0.0387 0.0369  0.0210  48  PHE A C   
424   O O   . PHE A 48  ? 0.5284 0.4207 0.4623 -0.0457 0.0411  0.0191  48  PHE A O   
425   C CB  . PHE A 48  ? 0.4229 0.3110 0.3502 -0.0228 0.0244  0.0203  48  PHE A CB  
426   C CG  . PHE A 48  ? 0.4748 0.3553 0.3952 -0.0136 0.0194  0.0207  48  PHE A CG  
427   C CD1 . PHE A 48  ? 0.4814 0.3490 0.3846 -0.0027 0.0136  0.0221  48  PHE A CD1 
428   C CD2 . PHE A 48  ? 0.4219 0.3074 0.3517 -0.0152 0.0203  0.0196  48  PHE A CD2 
429   C CE1 . PHE A 48  ? 0.4508 0.3112 0.3470 0.0073  0.0092  0.0223  48  PHE A CE1 
430   C CE2 . PHE A 48  ? 0.4421 0.3191 0.3639 -0.0061 0.0164  0.0197  48  PHE A CE2 
431   C CZ  . PHE A 48  ? 0.4379 0.3030 0.3435 0.0057  0.0110  0.0210  48  PHE A CZ  
432   N N   . GLU A 49  ? 0.4936 0.3578 0.3927 -0.0365 0.0366  0.0223  49  GLU A N   
433   C CA  . GLU A 49  ? 0.4937 0.3619 0.3943 -0.0428 0.0425  0.0216  49  GLU A CA  
434   C C   . GLU A 49  ? 0.4540 0.3426 0.3708 -0.0380 0.0376  0.0197  49  GLU A C   
435   O O   . GLU A 49  ? 0.4350 0.3190 0.3420 -0.0342 0.0347  0.0200  49  GLU A O   
436   C CB  . GLU A 49  ? 0.6058 0.4478 0.4771 -0.0435 0.0452  0.0239  49  GLU A CB  
437   C CG  . GLU A 49  ? 0.7280 0.5503 0.5836 -0.0531 0.0537  0.0253  49  GLU A CG  
438   C CD  . GLU A 49  ? 0.8826 0.6768 0.7118 -0.0478 0.0499  0.0282  49  GLU A CD  
439   O OE1 . GLU A 49  ? 0.8586 0.6558 0.6939 -0.0419 0.0441  0.0280  49  GLU A OE1 
440   O OE2 . GLU A 49  ? 0.9361 0.7038 0.7369 -0.0492 0.0528  0.0306  49  GLU A OE2 
441   N N   . ILE A 50  ? 0.3526 0.2622 0.2930 -0.0385 0.0363  0.0178  50  ILE A N   
442   C CA  . ILE A 50  ? 0.3579 0.2863 0.3147 -0.0363 0.0331  0.0157  50  ILE A CA  
443   C C   . ILE A 50  ? 0.3227 0.2658 0.2977 -0.0428 0.0390  0.0138  50  ILE A C   
444   O O   . ILE A 50  ? 0.3782 0.3199 0.3555 -0.0485 0.0441  0.0138  50  ILE A O   
445   C CB  . ILE A 50  ? 0.3330 0.2728 0.2996 -0.0289 0.0246  0.0152  50  ILE A CB  
446   C CG1 . ILE A 50  ? 0.3635 0.3046 0.3362 -0.0287 0.0246  0.0155  50  ILE A CG1 
447   C CG2 . ILE A 50  ? 0.3889 0.3191 0.3400 -0.0211 0.0176  0.0163  50  ILE A CG2 
448   C CD1 . ILE A 50  ? 0.2656 0.2242 0.2552 -0.0245 0.0195  0.0141  50  ILE A CD1 
449   N N   . LYS A 51  ? 0.3375 0.2941 0.3246 -0.0419 0.0377  0.0120  51  LYS A N   
450   C CA  . LYS A 51  ? 0.3015 0.2728 0.3062 -0.0455 0.0414  0.0100  51  LYS A CA  
451   C C   . LYS A 51  ? 0.2512 0.2352 0.2705 -0.0425 0.0358  0.0093  51  LYS A C   
452   O O   . LYS A 51  ? 0.2551 0.2414 0.2741 -0.0381 0.0299  0.0094  51  LYS A O   
453   C CB  . LYS A 51  ? 0.2932 0.2672 0.2981 -0.0460 0.0445  0.0084  51  LYS A CB  
454   C CG  . LYS A 51  ? 0.2834 0.2428 0.2703 -0.0484 0.0501  0.0090  51  LYS A CG  
455   C CD  . LYS A 51  ? 0.2955 0.2557 0.2847 -0.0551 0.0594  0.0086  51  LYS A CD  
456   C CE  . LYS A 51  ? 0.3836 0.3270 0.3523 -0.0586 0.0660  0.0095  51  LYS A CE  
457   N NZ  . LYS A 51  ? 0.4802 0.4186 0.4393 -0.0551 0.0653  0.0088  51  LYS A NZ  
458   N N   . LEU A 52  ? 0.2044 0.1969 0.2361 -0.0452 0.0378  0.0086  52  LEU A N   
459   C CA  . LEU A 52  ? 0.2623 0.2657 0.3066 -0.0429 0.0335  0.0079  52  LEU A CA  
460   C C   . LEU A 52  ? 0.2610 0.2752 0.3187 -0.0455 0.0363  0.0062  52  LEU A C   
461   O O   . LEU A 52  ? 0.2722 0.2877 0.3323 -0.0495 0.0408  0.0057  52  LEU A O   
462   C CB  . LEU A 52  ? 0.3099 0.3099 0.3526 -0.0417 0.0308  0.0090  52  LEU A CB  
463   C CG  . LEU A 52  ? 0.2882 0.2790 0.3189 -0.0366 0.0268  0.0105  52  LEU A CG  
464   C CD1 . LEU A 52  ? 0.2644 0.2499 0.2923 -0.0351 0.0255  0.0112  52  LEU A CD1 
465   C CD2 . LEU A 52  ? 0.2445 0.2441 0.2798 -0.0320 0.0215  0.0098  52  LEU A CD2 
466   N N   . ASN A 53  ? 0.1625 0.1846 0.2283 -0.0432 0.0334  0.0053  53  ASN A N   
467   C CA  . ASN A 53  ? 0.1378 0.1687 0.2143 -0.0435 0.0349  0.0037  53  ASN A CA  
468   C C   . ASN A 53  ? 0.2614 0.2978 0.3455 -0.0427 0.0312  0.0038  53  ASN A C   
469   O O   . ASN A 53  ? 0.2393 0.2740 0.3212 -0.0413 0.0277  0.0047  53  ASN A O   
470   C CB  . ASN A 53  ? 0.1382 0.1693 0.2139 -0.0413 0.0350  0.0026  53  ASN A CB  
471   C CG  . ASN A 53  ? 0.2136 0.2375 0.2792 -0.0419 0.0384  0.0025  53  ASN A CG  
472   O OD1 . ASN A 53  ? 0.2146 0.2390 0.2802 -0.0437 0.0438  0.0018  53  ASN A OD1 
473   N ND2 . ASN A 53  ? 0.1703 0.1879 0.2271 -0.0408 0.0352  0.0030  53  ASN A ND2 
474   N N   . PHE A 54  ? 0.2379 0.2815 0.3308 -0.0432 0.0321  0.0026  54  PHE A N   
475   C CA  . PHE A 54  ? 0.1822 0.2295 0.2804 -0.0428 0.0287  0.0026  54  PHE A CA  
476   C C   . PHE A 54  ? 0.2405 0.2944 0.3460 -0.0402 0.0276  0.0012  54  PHE A C   
477   O O   . PHE A 54  ? 0.2148 0.2734 0.3243 -0.0393 0.0303  -0.0003 54  PHE A O   
478   C CB  . PHE A 54  ? 0.1435 0.1912 0.2430 -0.0466 0.0295  0.0025  54  PHE A CB  
479   C CG  . PHE A 54  ? 0.2099 0.2477 0.2994 -0.0481 0.0302  0.0040  54  PHE A CG  
480   C CD1 . PHE A 54  ? 0.2426 0.2756 0.3277 -0.0460 0.0270  0.0050  54  PHE A CD1 
481   C CD2 . PHE A 54  ? 0.2079 0.2398 0.2905 -0.0506 0.0343  0.0043  54  PHE A CD2 
482   C CE1 . PHE A 54  ? 0.2519 0.2749 0.3265 -0.0454 0.0272  0.0063  54  PHE A CE1 
483   C CE2 . PHE A 54  ? 0.2171 0.2369 0.2874 -0.0507 0.0343  0.0060  54  PHE A CE2 
484   C CZ  . PHE A 54  ? 0.2589 0.2745 0.3256 -0.0475 0.0304  0.0069  54  PHE A CZ  
485   N N   . ASN A 55  ? 0.1942 0.2476 0.3002 -0.0385 0.0239  0.0016  55  ASN A N   
486   C CA  . ASN A 55  ? 0.2221 0.2793 0.3326 -0.0354 0.0217  0.0006  55  ASN A CA  
487   C C   . ASN A 55  ? 0.2556 0.3160 0.3695 -0.0365 0.0187  0.0005  55  ASN A C   
488   O O   . ASN A 55  ? 0.2319 0.2878 0.3415 -0.0381 0.0175  0.0017  55  ASN A O   
489   C CB  . ASN A 55  ? 0.1623 0.2128 0.2668 -0.0329 0.0199  0.0013  55  ASN A CB  
490   C CG  . ASN A 55  ? 0.2078 0.2583 0.3133 -0.0285 0.0175  0.0005  55  ASN A CG  
491   O OD1 . ASN A 55  ? 0.1839 0.2379 0.2928 -0.0249 0.0186  -0.0010 55  ASN A OD1 
492   N ND2 . ASN A 55  ? 0.1778 0.2240 0.2795 -0.0280 0.0143  0.0014  55  ASN A ND2 
493   N N   . LEU A 56  ? 0.2331 0.3018 0.3548 -0.0352 0.0174  -0.0012 56  LEU A N   
494   C CA  . LEU A 56  ? 0.2459 0.3180 0.3705 -0.0362 0.0135  -0.0018 56  LEU A CA  
495   C C   . LEU A 56  ? 0.2532 0.3278 0.3797 -0.0304 0.0093  -0.0026 56  LEU A C   
496   O O   . LEU A 56  ? 0.1966 0.2795 0.3300 -0.0267 0.0095  -0.0044 56  LEU A O   
497   C CB  . LEU A 56  ? 0.2298 0.3111 0.3621 -0.0411 0.0149  -0.0036 56  LEU A CB  
498   C CG  . LEU A 56  ? 0.2899 0.3661 0.4179 -0.0472 0.0190  -0.0029 56  LEU A CG  
499   C CD1 . LEU A 56  ? 0.2555 0.3406 0.3908 -0.0536 0.0209  -0.0050 56  LEU A CD1 
500   C CD2 . LEU A 56  ? 0.2615 0.3266 0.3800 -0.0482 0.0172  -0.0011 56  LEU A CD2 
501   N N   . THR A 57  ? 0.1936 0.2607 0.3131 -0.0289 0.0054  -0.0015 57  THR A N   
502   C CA  . THR A 57  ? 0.2375 0.3043 0.3559 -0.0229 0.0008  -0.0020 57  THR A CA  
503   C C   . THR A 57  ? 0.2143 0.2940 0.3428 -0.0223 -0.0032 -0.0045 57  THR A C   
504   O O   . THR A 57  ? 0.1870 0.2712 0.3190 -0.0281 -0.0034 -0.0052 57  THR A O   
505   C CB  . THR A 57  ? 0.2153 0.2690 0.3214 -0.0221 -0.0017 -0.0001 57  THR A CB  
506   O OG1 . THR A 57  ? 0.1901 0.2433 0.2947 -0.0261 -0.0031 0.0001  57  THR A OG1 
507   C CG2 . THR A 57  ? 0.2067 0.2508 0.3050 -0.0240 0.0025  0.0018  57  THR A CG2 
508   N N   . PRO A 58  ? 0.1543 0.2406 0.2875 -0.0154 -0.0066 -0.0061 58  PRO A N   
509   C CA  . PRO A 58  ? 0.2227 0.3247 0.3673 -0.0146 -0.0114 -0.0090 58  PRO A CA  
510   C C   . PRO A 58  ? 0.1782 0.2755 0.3168 -0.0166 -0.0175 -0.0086 58  PRO A C   
511   O O   . PRO A 58  ? 0.1820 0.2906 0.3289 -0.0210 -0.0203 -0.0109 58  PRO A O   
512   C CB  . PRO A 58  ? 0.1901 0.2977 0.3382 -0.0040 -0.0145 -0.0105 58  PRO A CB  
513   C CG  . PRO A 58  ? 0.1805 0.2784 0.3224 -0.0016 -0.0086 -0.0091 58  PRO A CG  
514   C CD  . PRO A 58  ? 0.1447 0.2256 0.2736 -0.0078 -0.0060 -0.0058 58  PRO A CD  
515   N N   . VAL A 59  ? 0.1379 0.2180 0.2613 -0.0144 -0.0192 -0.0060 59  VAL A N   
516   C CA  . VAL A 59  ? 0.1686 0.2421 0.2839 -0.0164 -0.0242 -0.0057 59  VAL A CA  
517   C C   . VAL A 59  ? 0.2131 0.2857 0.3286 -0.0254 -0.0207 -0.0056 59  VAL A C   
518   O O   . VAL A 59  ? 0.1881 0.2627 0.3034 -0.0289 -0.0247 -0.0071 59  VAL A O   
519   C CB  . VAL A 59  ? 0.2161 0.2704 0.3137 -0.0125 -0.0254 -0.0029 59  VAL A CB  
520   C CG1 . VAL A 59  ? 0.2698 0.3137 0.3606 -0.0159 -0.0181 -0.0004 59  VAL A CG1 
521   C CG2 . VAL A 59  ? 0.2261 0.2722 0.3130 -0.0137 -0.0307 -0.0027 59  VAL A CG2 
522   N N   . LEU A 60  ? 0.1530 0.2222 0.2681 -0.0290 -0.0138 -0.0042 60  LEU A N   
523   C CA  . LEU A 60  ? 0.1576 0.2243 0.2713 -0.0361 -0.0107 -0.0042 60  LEU A CA  
524   C C   . LEU A 60  ? 0.1884 0.2679 0.3134 -0.0414 -0.0107 -0.0068 60  LEU A C   
525   O O   . LEU A 60  ? 0.2334 0.3108 0.3560 -0.0472 -0.0117 -0.0079 60  LEU A O   
526   C CB  . LEU A 60  ? 0.1855 0.2456 0.2954 -0.0372 -0.0042 -0.0021 60  LEU A CB  
527   C CG  . LEU A 60  ? 0.2391 0.2967 0.3477 -0.0430 -0.0007 -0.0021 60  LEU A CG  
528   C CD1 . LEU A 60  ? 0.2278 0.2757 0.3264 -0.0448 -0.0027 -0.0020 60  LEU A CD1 
529   C CD2 . LEU A 60  ? 0.1531 0.2070 0.2597 -0.0429 0.0046  -0.0005 60  LEU A CD2 
530   N N   . ILE A 61  ? 0.2242 0.3165 0.3609 -0.0399 -0.0090 -0.0082 61  ILE A N   
531   C CA  . ILE A 61  ? 0.2292 0.3359 0.3779 -0.0461 -0.0082 -0.0111 61  ILE A CA  
532   C C   . ILE A 61  ? 0.2538 0.3683 0.4063 -0.0479 -0.0156 -0.0138 61  ILE A C   
533   O O   . ILE A 61  ? 0.2401 0.3575 0.3945 -0.0565 -0.0158 -0.0156 61  ILE A O   
534   C CB  . ILE A 61  ? 0.1182 0.2393 0.2793 -0.0428 -0.0049 -0.0126 61  ILE A CB  
535   C CG1 . ILE A 61  ? 0.1834 0.2953 0.3388 -0.0423 0.0022  -0.0102 61  ILE A CG1 
536   C CG2 . ILE A 61  ? 0.1408 0.2808 0.3165 -0.0495 -0.0043 -0.0163 61  ILE A CG2 
537   C CD1 . ILE A 61  ? 0.1700 0.2932 0.3349 -0.0391 0.0064  -0.0117 61  ILE A CD1 
538   N N   . ASP A 62  ? 0.1973 0.3143 0.3497 -0.0400 -0.0222 -0.0142 62  ASP A N   
539   C CA  . ASP A 62  ? 0.2237 0.3481 0.3788 -0.0405 -0.0308 -0.0168 62  ASP A CA  
540   C C   . ASP A 62  ? 0.2136 0.3248 0.3568 -0.0480 -0.0320 -0.0165 62  ASP A C   
541   O O   . ASP A 62  ? 0.2238 0.3426 0.3715 -0.0551 -0.0356 -0.0194 62  ASP A O   
542   C CB  . ASP A 62  ? 0.2912 0.4118 0.4405 -0.0297 -0.0378 -0.0161 62  ASP A CB  
543   C CG  . ASP A 62  ? 0.3576 0.4946 0.5199 -0.0212 -0.0397 -0.0179 62  ASP A CG  
544   O OD1 . ASP A 62  ? 0.3476 0.5047 0.5270 -0.0245 -0.0372 -0.0209 62  ASP A OD1 
545   O OD2 . ASP A 62  ? 0.3200 0.4488 0.4743 -0.0110 -0.0434 -0.0165 62  ASP A OD2 
546   N N   . GLN A 63  ? 0.2661 0.3577 0.3939 -0.0466 -0.0290 -0.0132 63  GLN A N   
547   C CA  . GLN A 63  ? 0.2782 0.3556 0.3927 -0.0517 -0.0298 -0.0129 63  GLN A CA  
548   C C   . GLN A 63  ? 0.2668 0.3428 0.3824 -0.0610 -0.0248 -0.0138 63  GLN A C   
549   O O   . GLN A 63  ? 0.2228 0.2950 0.3336 -0.0677 -0.0275 -0.0158 63  GLN A O   
550   C CB  . GLN A 63  ? 0.3061 0.3656 0.4056 -0.0471 -0.0269 -0.0095 63  GLN A CB  
551   C CG  . GLN A 63  ? 0.2966 0.3527 0.3907 -0.0389 -0.0311 -0.0082 63  GLN A CG  
552   C CD  . GLN A 63  ? 0.2874 0.3271 0.3673 -0.0365 -0.0267 -0.0051 63  GLN A CD  
553   O OE1 . GLN A 63  ? 0.3203 0.3487 0.3885 -0.0386 -0.0263 -0.0048 63  GLN A OE1 
554   N NE2 . GLN A 63  ? 0.2112 0.2501 0.2921 -0.0326 -0.0231 -0.0031 63  GLN A NE2 
555   N N   . ILE A 64  ? 0.2910 0.3676 0.4103 -0.0617 -0.0175 -0.0123 64  ILE A N   
556   C CA  . ILE A 64  ? 0.2690 0.3429 0.3876 -0.0704 -0.0126 -0.0130 64  ILE A CA  
557   C C   . ILE A 64  ? 0.2232 0.3118 0.3527 -0.0786 -0.0157 -0.0169 64  ILE A C   
558   O O   . ILE A 64  ? 0.1925 0.2740 0.3156 -0.0876 -0.0155 -0.0184 64  ILE A O   
559   C CB  . ILE A 64  ? 0.2000 0.2745 0.3218 -0.0692 -0.0051 -0.0111 64  ILE A CB  
560   C CG1 . ILE A 64  ? 0.1920 0.2522 0.3025 -0.0630 -0.0025 -0.0077 64  ILE A CG1 
561   C CG2 . ILE A 64  ? 0.1916 0.2638 0.3125 -0.0786 -0.0002 -0.0119 64  ILE A CG2 
562   C CD1 . ILE A 64  ? 0.2088 0.2691 0.3212 -0.0607 0.0034  -0.0058 64  ILE A CD1 
563   N N   . GLN A 65  ? 0.1839 0.2931 0.3295 -0.0757 -0.0184 -0.0189 65  GLN A N   
564   C CA  . GLN A 65  ? 0.2583 0.3864 0.4175 -0.0835 -0.0216 -0.0233 65  GLN A CA  
565   C C   . GLN A 65  ? 0.2683 0.3918 0.4205 -0.0878 -0.0297 -0.0255 65  GLN A C   
566   O O   . GLN A 65  ? 0.2444 0.3739 0.4001 -0.0989 -0.0309 -0.0288 65  GLN A O   
567   C CB  . GLN A 65  ? 0.3003 0.4527 0.4782 -0.0767 -0.0243 -0.0254 65  GLN A CB  
568   C CG  . GLN A 65  ? 0.2920 0.4554 0.4811 -0.0767 -0.0160 -0.0254 65  GLN A CG  
569   C CD  . GLN A 65  ? 0.3447 0.5308 0.5508 -0.0678 -0.0187 -0.0277 65  GLN A CD  
570   O OE1 . GLN A 65  ? 0.3206 0.5039 0.5237 -0.0565 -0.0241 -0.0265 65  GLN A OE1 
571   N NE2 . GLN A 65  ? 0.3277 0.5362 0.5512 -0.0729 -0.0148 -0.0312 65  GLN A NE2 
572   N N   . GLU A 66  ? 0.2860 0.3979 0.4269 -0.0798 -0.0351 -0.0238 66  GLU A N   
573   C CA  . GLU A 66  ? 0.3433 0.4511 0.4767 -0.0830 -0.0435 -0.0261 66  GLU A CA  
574   C C   . GLU A 66  ? 0.3034 0.3893 0.4192 -0.0914 -0.0406 -0.0258 66  GLU A C   
575   O O   . GLU A 66  ? 0.2766 0.3620 0.3894 -0.1003 -0.0451 -0.0291 66  GLU A O   
576   C CB  . GLU A 66  ? 0.3790 0.4801 0.5039 -0.0719 -0.0500 -0.0245 66  GLU A CB  
577   C CG  . GLU A 66  ? 0.4708 0.5869 0.6029 -0.0700 -0.0613 -0.0281 66  GLU A CG  
578   C CD  . GLU A 66  ? 0.5167 0.6169 0.6314 -0.0621 -0.0680 -0.0265 66  GLU A CD  
579   O OE1 . GLU A 66  ? 0.5246 0.6122 0.6302 -0.0539 -0.0644 -0.0226 66  GLU A OE1 
580   O OE2 . GLU A 66  ? 0.5456 0.6452 0.6548 -0.0649 -0.0768 -0.0292 66  GLU A OE2 
581   N N   . TYR A 67  ? 0.2825 0.3502 0.3862 -0.0884 -0.0333 -0.0221 67  TYR A N   
582   C CA  . TYR A 67  ? 0.2736 0.3203 0.3604 -0.0950 -0.0300 -0.0219 67  TYR A CA  
583   C C   . TYR A 67  ? 0.2730 0.3235 0.3645 -0.1073 -0.0264 -0.0241 67  TYR A C   
584   O O   . TYR A 67  ? 0.2876 0.3272 0.3686 -0.1166 -0.0281 -0.0264 67  TYR A O   
585   C CB  . TYR A 67  ? 0.2278 0.2576 0.3029 -0.0880 -0.0233 -0.0179 67  TYR A CB  
586   C CG  . TYR A 67  ? 0.1992 0.2183 0.2629 -0.0794 -0.0256 -0.0162 67  TYR A CG  
587   C CD1 . TYR A 67  ? 0.2765 0.2771 0.3221 -0.0804 -0.0272 -0.0169 67  TYR A CD1 
588   C CD2 . TYR A 67  ? 0.2640 0.2900 0.3335 -0.0706 -0.0255 -0.0140 67  TYR A CD2 
589   C CE1 . TYR A 67  ? 0.2688 0.2600 0.3034 -0.0728 -0.0282 -0.0154 67  TYR A CE1 
590   C CE2 . TYR A 67  ? 0.3229 0.3384 0.3808 -0.0639 -0.0267 -0.0123 67  TYR A CE2 
591   C CZ  . TYR A 67  ? 0.2919 0.2910 0.3330 -0.0651 -0.0278 -0.0131 67  TYR A CZ  
592   O OH  . TYR A 67  ? 0.3239 0.3129 0.3532 -0.0590 -0.0276 -0.0116 67  TYR A OH  
593   N N   . ALA A 68  ? 0.3126 0.3769 0.4181 -0.1080 -0.0209 -0.0235 68  ALA A N   
594   C CA  . ALA A 68  ? 0.2517 0.3189 0.3606 -0.1205 -0.0160 -0.0254 68  ALA A CA  
595   C C   . ALA A 68  ? 0.2850 0.3676 0.4034 -0.1316 -0.0218 -0.0305 68  ALA A C   
596   O O   . ALA A 68  ? 0.3377 0.4126 0.4494 -0.1448 -0.0195 -0.0325 68  ALA A O   
597   C CB  . ALA A 68  ? 0.2257 0.3070 0.3484 -0.1186 -0.0091 -0.0242 68  ALA A CB  
598   N N   . GLN A 69  ? 0.3357 0.4390 0.4684 -0.1268 -0.0297 -0.0328 69  GLN A N   
599   C CA  . GLN A 69  ? 0.3589 0.4801 0.5024 -0.1370 -0.0365 -0.0381 69  GLN A CA  
600   C C   . GLN A 69  ? 0.4385 0.5426 0.5647 -0.1412 -0.0441 -0.0398 69  GLN A C   
601   O O   . GLN A 69  ? 0.4940 0.6117 0.6274 -0.1499 -0.0513 -0.0446 69  GLN A O   
602   C CB  . GLN A 69  ? 0.3928 0.5449 0.5592 -0.1290 -0.0429 -0.0403 69  GLN A CB  
603   C CG  . GLN A 69  ? 0.4521 0.6257 0.6383 -0.1271 -0.0358 -0.0403 69  GLN A CG  
604   C CD  . GLN A 69  ? 0.5003 0.6969 0.7037 -0.1136 -0.0409 -0.0411 69  GLN A CD  
605   O OE1 . GLN A 69  ? 0.5491 0.7524 0.7543 -0.1077 -0.0513 -0.0428 69  GLN A OE1 
606   N NE2 . GLN A 69  ? 0.5127 0.7185 0.7262 -0.1077 -0.0336 -0.0396 69  GLN A NE2 
607   N N   . GLY A 70  ? 0.4426 0.5183 0.5465 -0.1351 -0.0428 -0.0364 70  GLY A N   
608   C CA  . GLY A 70  ? 0.4521 0.5097 0.5374 -0.1377 -0.0493 -0.0380 70  GLY A CA  
609   C C   . GLY A 70  ? 0.4581 0.5249 0.5462 -0.1298 -0.0600 -0.0392 70  GLY A C   
610   O O   . GLY A 70  ? 0.5168 0.5735 0.5922 -0.1341 -0.0671 -0.0418 70  GLY A O   
611   N N   . LYS A 71  ? 0.4493 0.5322 0.5509 -0.1180 -0.0614 -0.0375 71  LYS A N   
612   C CA  . LYS A 71  ? 0.4423 0.5336 0.5457 -0.1098 -0.0721 -0.0386 71  LYS A CA  
613   C C   . LYS A 71  ? 0.4583 0.5294 0.5443 -0.0973 -0.0716 -0.0343 71  LYS A C   
614   O O   . LYS A 71  ? 0.4415 0.5129 0.5228 -0.0906 -0.0802 -0.0347 71  LYS A O   
615   C CB  . LYS A 71  ? 0.3406 0.4639 0.4698 -0.1047 -0.0755 -0.0402 71  LYS A CB  
616   N N   . ALA A 72  ? 0.3935 0.4475 0.4697 -0.0941 -0.0620 -0.0303 72  ALA A N   
617   C CA  . ALA A 72  ? 0.3497 0.3872 0.4114 -0.0834 -0.0603 -0.0265 72  ALA A CA  
618   C C   . ALA A 72  ? 0.3771 0.3915 0.4153 -0.0851 -0.0629 -0.0271 72  ALA A C   
619   O O   . ALA A 72  ? 0.3898 0.3902 0.4174 -0.0924 -0.0595 -0.0282 72  ALA A O   
620   C CB  . ALA A 72  ? 0.3319 0.3627 0.3934 -0.0797 -0.0495 -0.0226 72  ALA A CB  
621   N N   . LYS A 73  ? 0.3942 0.4024 0.4222 -0.0780 -0.0687 -0.0265 73  LYS A N   
622   C CA  . LYS A 73  ? 0.3861 0.3713 0.3898 -0.0780 -0.0708 -0.0270 73  LYS A CA  
623   C C   . LYS A 73  ? 0.3627 0.3324 0.3542 -0.0697 -0.0622 -0.0227 73  LYS A C   
624   O O   . LYS A 73  ? 0.4480 0.4178 0.4373 -0.0618 -0.0633 -0.0204 73  LYS A O   
625   C CB  . LYS A 73  ? 0.4235 0.4110 0.4217 -0.0758 -0.0828 -0.0291 73  LYS A CB  
626   C CG  . LYS A 73  ? 0.4910 0.5007 0.5061 -0.0827 -0.0923 -0.0337 73  LYS A CG  
627   C CD  . LYS A 73  ? 0.6571 0.6576 0.6622 -0.0950 -0.0956 -0.0379 73  LYS A CD  
628   C CE  . LYS A 73  ? 0.7516 0.7593 0.7689 -0.1057 -0.0887 -0.0392 73  LYS A CE  
629   N NZ  . LYS A 73  ? 0.7865 0.7755 0.7869 -0.1174 -0.0889 -0.0423 73  LYS A NZ  
630   N N   . ASP A 74  ? 0.3840 0.3401 0.3668 -0.0716 -0.0539 -0.0220 74  ASP A N   
631   C CA  . ASP A 74  ? 0.3452 0.2917 0.3212 -0.0645 -0.0447 -0.0185 74  ASP A CA  
632   C C   . ASP A 74  ? 0.4021 0.3259 0.3539 -0.0630 -0.0432 -0.0192 74  ASP A C   
633   O O   . ASP A 74  ? 0.4122 0.3232 0.3532 -0.0677 -0.0421 -0.0213 74  ASP A O   
634   C CB  . ASP A 74  ? 0.3208 0.2711 0.3065 -0.0659 -0.0366 -0.0172 74  ASP A CB  
635   C CG  . ASP A 74  ? 0.3887 0.3365 0.3736 -0.0584 -0.0281 -0.0138 74  ASP A CG  
636   O OD1 . ASP A 74  ? 0.3986 0.3341 0.3689 -0.0539 -0.0257 -0.0131 74  ASP A OD1 
637   O OD2 . ASP A 74  ? 0.3700 0.3283 0.3685 -0.0574 -0.0236 -0.0120 74  ASP A OD2 
638   N N   . VAL A 75  ? 0.4418 0.3590 0.3831 -0.0567 -0.0426 -0.0174 75  VAL A N   
639   C CA  . VAL A 75  ? 0.4678 0.3640 0.3849 -0.0553 -0.0420 -0.0186 75  VAL A CA  
640   C C   . VAL A 75  ? 0.4678 0.3525 0.3767 -0.0529 -0.0317 -0.0182 75  VAL A C   
641   O O   . VAL A 75  ? 0.4367 0.3039 0.3279 -0.0544 -0.0312 -0.0205 75  VAL A O   
642   C CB  . VAL A 75  ? 0.4571 0.3481 0.3635 -0.0497 -0.0433 -0.0167 75  VAL A CB  
643   C CG1 . VAL A 75  ? 0.4968 0.3947 0.4059 -0.0510 -0.0553 -0.0179 75  VAL A CG1 
644   C CG2 . VAL A 75  ? 0.4512 0.3506 0.3674 -0.0445 -0.0355 -0.0129 75  VAL A CG2 
645   N N   . PHE A 76  ? 0.4040 0.2981 0.3249 -0.0487 -0.0239 -0.0154 76  PHE A N   
646   C CA  . PHE A 76  ? 0.4481 0.3344 0.3634 -0.0450 -0.0148 -0.0152 76  PHE A CA  
647   C C   . PHE A 76  ? 0.4879 0.3682 0.4023 -0.0495 -0.0156 -0.0172 76  PHE A C   
648   O O   . PHE A 76  ? 0.4147 0.2783 0.3135 -0.0475 -0.0119 -0.0187 76  PHE A O   
649   C CB  . PHE A 76  ? 0.4705 0.3709 0.4006 -0.0402 -0.0077 -0.0122 76  PHE A CB  
650   C CG  . PHE A 76  ? 0.6047 0.5044 0.5290 -0.0355 -0.0027 -0.0106 76  PHE A CG  
651   C CD1 . PHE A 76  ? 0.6787 0.5830 0.6047 -0.0361 -0.0064 -0.0090 76  PHE A CD1 
652   C CD2 . PHE A 76  ? 0.6295 0.5238 0.5459 -0.0302 0.0059  -0.0108 76  PHE A CD2 
653   C CE1 . PHE A 76  ? 0.6978 0.5990 0.6160 -0.0331 -0.0011 -0.0074 76  PHE A CE1 
654   C CE2 . PHE A 76  ? 0.6761 0.5711 0.5875 -0.0273 0.0116  -0.0096 76  PHE A CE2 
655   C CZ  . PHE A 76  ? 0.6997 0.5971 0.6111 -0.0296 0.0083  -0.0078 76  PHE A CZ  
656   N N   . LEU A 77  ? 0.4652 0.3578 0.3950 -0.0555 -0.0200 -0.0173 77  LEU A N   
657   C CA  . LEU A 77  ? 0.4271 0.3131 0.3552 -0.0614 -0.0200 -0.0190 77  LEU A CA  
658   C C   . LEU A 77  ? 0.4478 0.3159 0.3574 -0.0677 -0.0253 -0.0226 77  LEU A C   
659   O O   . LEU A 77  ? 0.5010 0.3522 0.3976 -0.0700 -0.0228 -0.0241 77  LEU A O   
660   C CB  . LEU A 77  ? 0.4406 0.3453 0.3897 -0.0672 -0.0225 -0.0185 77  LEU A CB  
661   C CG  . LEU A 77  ? 0.4524 0.3517 0.4015 -0.0732 -0.0201 -0.0192 77  LEU A CG  
662   C CD1 . LEU A 77  ? 0.4017 0.2900 0.3431 -0.0656 -0.0120 -0.0173 77  LEU A CD1 
663   C CD2 . LEU A 77  ? 0.4594 0.3800 0.4306 -0.0782 -0.0215 -0.0186 77  LEU A CD2 
664   N N   . GLU A 78  ? 0.5102 0.3799 0.4163 -0.0703 -0.0329 -0.0242 78  GLU A N   
665   C CA  . GLU A 78  ? 0.5887 0.4412 0.4762 -0.0770 -0.0388 -0.0281 78  GLU A CA  
666   C C   . GLU A 78  ? 0.5380 0.3651 0.3999 -0.0712 -0.0334 -0.0288 78  GLU A C   
667   O O   . GLU A 78  ? 0.5248 0.3316 0.3682 -0.0760 -0.0348 -0.0319 78  GLU A O   
668   C CB  . GLU A 78  ? 0.7361 0.5968 0.6254 -0.0801 -0.0492 -0.0297 78  GLU A CB  
669   C CG  . GLU A 78  ? 0.9420 0.7902 0.8131 -0.0731 -0.0498 -0.0293 78  GLU A CG  
670   C CD  . GLU A 78  ? 1.0777 0.9345 0.9506 -0.0744 -0.0607 -0.0303 78  GLU A CD  
671   O OE1 . GLU A 78  ? 1.1221 0.9624 0.9735 -0.0737 -0.0650 -0.0320 78  GLU A OE1 
672   O OE2 . GLU A 78  ? 1.0778 0.9570 0.9724 -0.0752 -0.0652 -0.0294 78  GLU A OE2 
673   N N   . ALA A 79  ? 0.5298 0.3577 0.3901 -0.0611 -0.0267 -0.0263 79  ALA A N   
674   C CA  . ALA A 79  ? 0.5504 0.3578 0.3893 -0.0541 -0.0198 -0.0271 79  ALA A CA  
675   C C   . ALA A 79  ? 0.5579 0.3564 0.3940 -0.0517 -0.0135 -0.0272 79  ALA A C   
676   O O   . ALA A 79  ? 0.6533 0.4287 0.4674 -0.0492 -0.0107 -0.0294 79  ALA A O   
677   C CB  . ALA A 79  ? 0.5001 0.3146 0.3411 -0.0450 -0.0135 -0.0245 79  ALA A CB  
678   N N   . ILE A 80  ? 0.5473 0.3621 0.4037 -0.0520 -0.0113 -0.0248 80  ILE A N   
679   C CA  . ILE A 80  ? 0.5154 0.3205 0.3682 -0.0505 -0.0068 -0.0247 80  ILE A CA  
680   C C   . ILE A 80  ? 0.4413 0.2279 0.2799 -0.0610 -0.0117 -0.0278 80  ILE A C   
681   O O   . ILE A 80  ? 0.4984 0.2605 0.3159 -0.0590 -0.0089 -0.0294 80  ILE A O   
682   C CB  . ILE A 80  ? 0.5014 0.3279 0.3782 -0.0498 -0.0045 -0.0216 80  ILE A CB  
683   C CG1 . ILE A 80  ? 0.5077 0.3503 0.3964 -0.0401 0.0009  -0.0189 80  ILE A CG1 
684   C CG2 . ILE A 80  ? 0.4653 0.2797 0.3361 -0.0495 -0.0012 -0.0214 80  ILE A CG2 
685   C CD1 . ILE A 80  ? 0.5659 0.3980 0.4427 -0.0293 0.0082  -0.0192 80  ILE A CD1 
686   N N   . ARG A 81  ? 0.4547 0.2525 0.3039 -0.0724 -0.0193 -0.0288 81  ARG A N   
687   C CA  . ARG A 81  ? 0.5015 0.2858 0.3410 -0.0849 -0.0236 -0.0319 81  ARG A CA  
688   C C   . ARG A 81  ? 0.5613 0.3170 0.3714 -0.0868 -0.0260 -0.0356 81  ARG A C   
689   O O   . ARG A 81  ? 0.6248 0.3576 0.4170 -0.0929 -0.0256 -0.0377 81  ARG A O   
690   C CB  . ARG A 81  ? 0.5395 0.3462 0.3989 -0.0963 -0.0315 -0.0329 81  ARG A CB  
691   C CG  . ARG A 81  ? 0.6575 0.4579 0.5145 -0.1108 -0.0339 -0.0355 81  ARG A CG  
692   C CD  . ARG A 81  ? 0.7879 0.6124 0.6643 -0.1220 -0.0424 -0.0377 81  ARG A CD  
693   N NE  . ARG A 81  ? 0.8732 0.7284 0.7783 -0.1176 -0.0416 -0.0348 81  ARG A NE  
694   C CZ  . ARG A 81  ? 0.9253 0.7939 0.8469 -0.1211 -0.0375 -0.0332 81  ARG A CZ  
695   N NH1 . ARG A 81  ? 0.9337 0.7877 0.8460 -0.1296 -0.0336 -0.0340 81  ARG A NH1 
696   N NH2 . ARG A 81  ? 0.9132 0.8079 0.8586 -0.1162 -0.0370 -0.0309 81  ARG A NH2 
697   N N   . LYS A 82  ? 0.4797 0.3944 0.3915 -0.0318 -0.0761 -0.0109 82  LYS A N   
698   C CA  . LYS A 82  ? 0.4586 0.3541 0.3473 -0.0302 -0.0814 -0.0161 82  LYS A CA  
699   C C   . LYS A 82  ? 0.3998 0.2830 0.2813 -0.0306 -0.0725 -0.0167 82  LYS A C   
700   O O   . LYS A 82  ? 0.3922 0.2775 0.2784 -0.0285 -0.0605 -0.0124 82  LYS A O   
701   C CB  . LYS A 82  ? 0.4808 0.3595 0.3417 -0.0228 -0.0827 -0.0149 82  LYS A CB  
702   C CG  . LYS A 82  ? 0.6050 0.4850 0.4612 -0.0200 -0.0989 -0.0188 82  LYS A CG  
703   C CD  . LYS A 82  ? 0.7540 0.6089 0.5733 -0.0125 -0.1019 -0.0183 82  LYS A CD  
704   C CE  . LYS A 82  ? 0.7812 0.6326 0.5933 -0.0071 -0.1018 -0.0121 82  LYS A CE  
705   N NZ  . LYS A 82  ? 0.8127 0.6340 0.5831 -0.0011 -0.1009 -0.0096 82  LYS A NZ  
706   N N   . ASP A 83  ? 0.4726 0.3434 0.3434 -0.0330 -0.0793 -0.0230 83  ASP A N   
707   C CA  . ASP A 83  ? 0.5696 0.4210 0.4234 -0.0300 -0.0726 -0.0254 83  ASP A CA  
708   C C   . ASP A 83  ? 0.5502 0.3906 0.3826 -0.0219 -0.0631 -0.0233 83  ASP A C   
709   O O   . ASP A 83  ? 0.5571 0.3928 0.3743 -0.0193 -0.0674 -0.0228 83  ASP A O   
710   C CB  . ASP A 83  ? 0.6458 0.4817 0.4852 -0.0335 -0.0834 -0.0338 83  ASP A CB  
711   C CG  . ASP A 83  ? 0.7268 0.5406 0.5497 -0.0305 -0.0772 -0.0374 83  ASP A CG  
712   O OD1 . ASP A 83  ? 0.6920 0.4929 0.4941 -0.0224 -0.0698 -0.0381 83  ASP A OD1 
713   O OD2 . ASP A 83  ? 0.7442 0.5521 0.5736 -0.0363 -0.0794 -0.0399 83  ASP A OD2 
714   N N   . PRO A 84  ? 0.5336 0.3702 0.3642 -0.0176 -0.0501 -0.0224 84  PRO A N   
715   C CA  . PRO A 84  ? 0.5561 0.3856 0.3685 -0.0119 -0.0384 -0.0211 84  PRO A CA  
716   C C   . PRO A 84  ? 0.5094 0.3160 0.2873 -0.0088 -0.0418 -0.0261 84  PRO A C   
717   O O   . PRO A 84  ? 0.5666 0.3657 0.3249 -0.0063 -0.0346 -0.0239 84  PRO A O   
718   C CB  . PRO A 84  ? 0.5096 0.3425 0.3309 -0.0075 -0.0256 -0.0222 84  PRO A CB  
719   C CG  . PRO A 84  ? 0.4917 0.3371 0.3393 -0.0109 -0.0305 -0.0202 84  PRO A CG  
720   C CD  . PRO A 84  ? 0.4974 0.3366 0.3428 -0.0174 -0.0453 -0.0226 84  PRO A CD  
721   N N   . ASP A 85  ? 0.5772 0.3705 0.3447 -0.0097 -0.0522 -0.0328 85  ASP A N   
722   C CA  . ASP A 85  ? 0.6371 0.4080 0.3693 -0.0065 -0.0565 -0.0381 85  ASP A CA  
723   C C   . ASP A 85  ? 0.6188 0.3882 0.3391 -0.0069 -0.0681 -0.0359 85  ASP A C   
724   O O   . ASP A 85  ? 0.6586 0.4082 0.3453 -0.0032 -0.0713 -0.0386 85  ASP A O   
725   C CB  . ASP A 85  ? 0.6973 0.4535 0.4211 -0.0080 -0.0658 -0.0470 85  ASP A CB  
726   C CG  . ASP A 85  ? 0.7754 0.5254 0.5027 -0.0047 -0.0553 -0.0500 85  ASP A CG  
727   O OD1 . ASP A 85  ? 0.8131 0.5682 0.5425 0.0009  -0.0399 -0.0474 85  ASP A OD1 
728   O OD2 . ASP A 85  ? 0.8267 0.5667 0.5552 -0.0078 -0.0626 -0.0557 85  ASP A OD2 
729   N N   . ASP A 86  ? 0.5821 0.3709 0.3274 -0.0104 -0.0750 -0.0316 86  ASP A N   
730   C CA  . ASP A 86  ? 0.6623 0.4513 0.3995 -0.0085 -0.0869 -0.0296 86  ASP A CA  
731   C C   . ASP A 86  ? 0.6275 0.4170 0.3604 -0.0060 -0.0771 -0.0209 86  ASP A C   
732   O O   . ASP A 86  ? 0.6828 0.4670 0.4037 -0.0027 -0.0865 -0.0185 86  ASP A O   
733   C CB  . ASP A 86  ? 0.7185 0.5296 0.4864 -0.0133 -0.1010 -0.0320 86  ASP A CB  
734   C CG  . ASP A 86  ? 0.8062 0.6158 0.5773 -0.0184 -0.1117 -0.0413 86  ASP A CG  
735   O OD1 . ASP A 86  ? 0.8421 0.6307 0.5874 -0.0165 -0.1119 -0.0465 86  ASP A OD1 
736   O OD2 . ASP A 86  ? 0.8004 0.6298 0.5992 -0.0250 -0.1196 -0.0440 86  ASP A OD2 
737   N N   . LEU A 87  ? 0.5335 0.3291 0.2761 -0.0074 -0.0593 -0.0166 87  LEU A N   
738   C CA  . LEU A 87  ? 0.5645 0.3619 0.3059 -0.0076 -0.0492 -0.0089 87  LEU A CA  
739   C C   . LEU A 87  ? 0.5893 0.3594 0.2881 -0.0044 -0.0459 -0.0069 87  LEU A C   
740   O O   . LEU A 87  ? 0.6197 0.3729 0.2923 -0.0025 -0.0410 -0.0110 87  LEU A O   
741   C CB  . LEU A 87  ? 0.5267 0.3386 0.2886 -0.0103 -0.0310 -0.0068 87  LEU A CB  
742   C CG  . LEU A 87  ? 0.5276 0.3648 0.3289 -0.0134 -0.0332 -0.0064 87  LEU A CG  
743   C CD1 . LEU A 87  ? 0.5026 0.3534 0.3212 -0.0142 -0.0167 -0.0047 87  LEU A CD1 
744   C CD2 . LEU A 87  ? 0.4825 0.3315 0.2997 -0.0153 -0.0433 -0.0026 87  LEU A CD2 
745   N N   . GLU A 88  ? 0.5918 0.3552 0.2811 -0.0037 -0.0486 -0.0006 88  GLU A N   
746   C CA  . GLU A 88  ? 0.6755 0.4100 0.3219 -0.0023 -0.0420 0.0034  88  GLU A CA  
747   C C   . GLU A 88  ? 0.7273 0.4647 0.3756 -0.0084 -0.0178 0.0072  88  GLU A C   
748   O O   . GLU A 88  ? 0.5656 0.3278 0.2496 -0.0126 -0.0097 0.0084  88  GLU A O   
749   C CB  . GLU A 88  ? 0.7081 0.4287 0.3389 0.0017  -0.0553 0.0087  88  GLU A CB  
750   C CG  . GLU A 88  ? 0.7635 0.4872 0.3978 0.0085  -0.0802 0.0032  88  GLU A CG  
751   C CD  . GLU A 88  ? 0.8816 0.6052 0.5200 0.0136  -0.0939 0.0068  88  GLU A CD  
752   O OE1 . GLU A 88  ? 0.9298 0.6563 0.5692 0.0204  -0.1152 0.0015  88  GLU A OE1 
753   O OE2 . GLU A 88  ? 0.8970 0.6184 0.5384 0.0109  -0.0838 0.0140  88  GLU A OE2 
754   N N   . LYS A 89  ? 0.6405 0.3534 0.2496 -0.0093 -0.0060 0.0084  89  LYS A N   
755   C CA  . LYS A 89  ? 0.6836 0.3989 0.2919 -0.0168 0.0180  0.0115  89  LYS A CA  
756   C C   . LYS A 89  ? 0.6722 0.3967 0.2998 -0.0221 0.0204  0.0186  89  LYS A C   
757   O O   . LYS A 89  ? 0.7027 0.4494 0.3587 -0.0283 0.0352  0.0185  89  LYS A O   
758   C CB  . LYS A 89  ? 0.6978 0.3798 0.2540 -0.0186 0.0289  0.0135  89  LYS A CB  
759   C CG  . LYS A 89  ? 0.9371 0.6028 0.4649 -0.0123 0.0227  0.0069  89  LYS A CG  
760   C CD  . LYS A 89  ? 0.9625 0.6161 0.4616 -0.0159 0.0452  0.0039  89  LYS A CD  
761   C CE  . LYS A 89  ? 1.0387 0.6728 0.5060 -0.0087 0.0362  -0.0033 89  LYS A CE  
762   N NZ  . LYS A 89  ? 1.1086 0.7629 0.5999 -0.0060 0.0434  -0.0137 89  LYS A NZ  
763   N N   . GLU A 90  ? 0.6726 0.3799 0.2850 -0.0188 0.0050  0.0238  90  GLU A N   
764   C CA  . GLU A 90  ? 0.6663 0.3774 0.2929 -0.0229 0.0062  0.0301  90  GLU A CA  
765   C C   . GLU A 90  ? 0.5718 0.3209 0.2515 -0.0238 0.0032  0.0272  90  GLU A C   
766   O O   . GLU A 90  ? 0.5644 0.3264 0.2647 -0.0303 0.0127  0.0300  90  GLU A O   
767   C CB  . GLU A 90  ? 0.6874 0.3728 0.2885 -0.0158 -0.0127 0.0347  90  GLU A CB  
768   C CG  . GLU A 90  ? 0.8757 0.5179 0.4191 -0.0147 -0.0110 0.0396  90  GLU A CG  
769   C CD  . GLU A 90  ? 0.9168 0.5330 0.4369 -0.0065 -0.0299 0.0449  90  GLU A CD  
770   O OE1 . GLU A 90  ? 1.0156 0.5914 0.4835 -0.0033 -0.0329 0.0496  90  GLU A OE1 
771   O OE2 . GLU A 90  ? 0.8107 0.4464 0.3638 -0.0024 -0.0420 0.0439  90  GLU A OE2 
772   N N   . GLU A 91  ? 0.5652 0.3308 0.2651 -0.0182 -0.0100 0.0215  91  GLU A N   
773   C CA  . GLU A 91  ? 0.5217 0.3200 0.2672 -0.0193 -0.0134 0.0191  91  GLU A CA  
774   C C   . GLU A 91  ? 0.5140 0.3324 0.2818 -0.0240 0.0035  0.0165  91  GLU A C   
775   O O   . GLU A 91  ? 0.4921 0.3330 0.2910 -0.0277 0.0081  0.0174  91  GLU A O   
776   C CB  . GLU A 91  ? 0.5401 0.3467 0.2969 -0.0139 -0.0318 0.0137  91  GLU A CB  
777   C CG  . GLU A 91  ? 0.5865 0.3832 0.3328 -0.0080 -0.0509 0.0143  91  GLU A CG  
778   C CD  . GLU A 91  ? 0.6202 0.4290 0.3803 -0.0045 -0.0681 0.0072  91  GLU A CD  
779   O OE1 . GLU A 91  ? 0.5836 0.3853 0.3311 -0.0039 -0.0698 0.0024  91  GLU A OE1 
780   O OE2 . GLU A 91  ? 0.6459 0.4723 0.4304 -0.0033 -0.0793 0.0057  91  GLU A OE2 
781   N N   . VAL A 92  ? 0.5293 0.3406 0.2815 -0.0229 0.0121  0.0124  92  VAL A N   
782   C CA  . VAL A 92  ? 0.5813 0.4116 0.3532 -0.0254 0.0287  0.0089  92  VAL A CA  
783   C C   . VAL A 92  ? 0.5672 0.4029 0.3429 -0.0335 0.0452  0.0125  92  VAL A C   
784   O O   . VAL A 92  ? 0.5121 0.3737 0.3197 -0.0364 0.0531  0.0108  92  VAL A O   
785   C CB  . VAL A 92  ? 0.5690 0.3883 0.3198 -0.0217 0.0356  0.0027  92  VAL A CB  
786   C CG1 . VAL A 92  ? 0.5118 0.3532 0.2855 -0.0219 0.0521  -0.0025 92  VAL A CG1 
787   C CG2 . VAL A 92  ? 0.5118 0.3247 0.2595 -0.0153 0.0188  -0.0017 92  VAL A CG2 
788   N N   . GLU A 93  ? 0.5691 0.3792 0.3112 -0.0376 0.0500  0.0174  93  GLU A N   
789   C CA  . GLU A 93  ? 0.6032 0.4148 0.3459 -0.0478 0.0667  0.0207  93  GLU A CA  
790   C C   . GLU A 93  ? 0.5471 0.3746 0.3194 -0.0508 0.0603  0.0240  93  GLU A C   
791   O O   . GLU A 93  ? 0.4916 0.3395 0.2879 -0.0581 0.0725  0.0229  93  GLU A O   
792   C CB  . GLU A 93  ? 0.6568 0.4306 0.3510 -0.0522 0.0723  0.0264  93  GLU A CB  
793   C CG  . GLU A 93  ? 0.7667 0.5273 0.4309 -0.0539 0.0877  0.0228  93  GLU A CG  
794   C CD  . GLU A 93  ? 0.9005 0.6168 0.5080 -0.0560 0.0888  0.0291  93  GLU A CD  
795   O OE1 . GLU A 93  ? 0.9123 0.6068 0.5035 -0.0565 0.0787  0.0366  93  GLU A OE1 
796   O OE2 . GLU A 93  ? 0.9264 0.6278 0.5032 -0.0563 0.0992  0.0262  93  GLU A OE2 
797   N N   . LYS A 94  ? 0.5477 0.3674 0.3190 -0.0450 0.0413  0.0270  94  LYS A N   
798   C CA  . LYS A 94  ? 0.5723 0.4065 0.3703 -0.0469 0.0351  0.0292  94  LYS A CA  
799   C C   . LYS A 94  ? 0.5336 0.4039 0.3743 -0.0465 0.0356  0.0245  94  LYS A C   
800   O O   . LYS A 94  ? 0.4479 0.3359 0.3129 -0.0517 0.0402  0.0248  94  LYS A O   
801   C CB  . LYS A 94  ? 0.6439 0.4648 0.4331 -0.0393 0.0147  0.0315  94  LYS A CB  
802   C CG  . LYS A 94  ? 0.7510 0.5398 0.5081 -0.0403 0.0129  0.0377  94  LYS A CG  
803   C CD  . LYS A 94  ? 0.8579 0.6274 0.5940 -0.0292 -0.0078 0.0383  94  LYS A CD  
804   C CE  . LYS A 94  ? 0.9792 0.7075 0.6710 -0.0283 -0.0090 0.0449  94  LYS A CE  
805   N NZ  . LYS A 94  ? 1.0340 0.7580 0.7334 -0.0321 -0.0075 0.0486  94  LYS A NZ  
806   N N   . LEU A 95  ? 0.4932 0.3720 0.3408 -0.0403 0.0306  0.0201  95  LEU A N   
807   C CA  . LEU A 95  ? 0.5155 0.4229 0.3979 -0.0388 0.0303  0.0163  95  LEU A CA  
808   C C   . LEU A 95  ? 0.4631 0.3881 0.3604 -0.0431 0.0474  0.0132  95  LEU A C   
809   O O   . LEU A 95  ? 0.4112 0.3601 0.3382 -0.0449 0.0487  0.0120  95  LEU A O   
810   C CB  . LEU A 95  ? 0.5174 0.4226 0.3972 -0.0319 0.0216  0.0125  95  LEU A CB  
811   C CG  . LEU A 95  ? 0.6286 0.5554 0.5378 -0.0292 0.0176  0.0097  95  LEU A CG  
812   C CD1 . LEU A 95  ? 0.5761 0.5132 0.5032 -0.0309 0.0062  0.0124  95  LEU A CD1 
813   C CD2 . LEU A 95  ? 0.6834 0.6011 0.5832 -0.0236 0.0120  0.0054  95  LEU A CD2 
814   N N   . ILE A 96  ? 0.4438 0.3586 0.3211 -0.0448 0.0606  0.0111  96  ILE A N   
815   C CA  . ILE A 96  ? 0.4425 0.3767 0.3348 -0.0498 0.0785  0.0066  96  ILE A CA  
816   C C   . ILE A 96  ? 0.4321 0.3722 0.3334 -0.0606 0.0855  0.0097  96  ILE A C   
817   O O   . ILE A 96  ? 0.4256 0.3934 0.3579 -0.0639 0.0908  0.0062  96  ILE A O   
818   C CB  . ILE A 96  ? 0.4811 0.4019 0.3469 -0.0504 0.0927  0.0031  96  ILE A CB  
819   C CG1 . ILE A 96  ? 0.4665 0.3865 0.3297 -0.0392 0.0872  -0.0023 96  ILE A CG1 
820   C CG2 . ILE A 96  ? 0.4904 0.4326 0.3714 -0.0581 0.1134  -0.0021 96  ILE A CG2 
821   C CD1 . ILE A 96  ? 0.5834 0.4835 0.4129 -0.0385 0.0980  -0.0055 96  ILE A CD1 
822   N N   . GLU A 97  ? 0.4194 0.3317 0.2926 -0.0658 0.0841  0.0161  97  GLU A N   
823   C CA  . GLU A 97  ? 0.4691 0.3804 0.3462 -0.0767 0.0902  0.0193  97  GLU A CA  
824   C C   . GLU A 97  ? 0.4553 0.3891 0.3662 -0.0751 0.0794  0.0189  97  GLU A C   
825   O O   . GLU A 97  ? 0.3744 0.3260 0.3064 -0.0833 0.0869  0.0168  97  GLU A O   
826   C CB  . GLU A 97  ? 0.5581 0.4299 0.3957 -0.0794 0.0864  0.0268  97  GLU A CB  
827   C CG  . GLU A 97  ? 0.7448 0.5904 0.5440 -0.0858 0.1014  0.0285  97  GLU A CG  
828   C CD  . GLU A 97  ? 0.9293 0.7311 0.6834 -0.0827 0.0916  0.0362  97  GLU A CD  
829   O OE1 . GLU A 97  ? 0.9560 0.7523 0.7093 -0.0712 0.0715  0.0376  97  GLU A OE1 
830   O OE2 . GLU A 97  ? 1.0492 0.8221 0.7679 -0.0916 0.1038  0.0404  97  GLU A OE2 
831   N N   . PHE A 98  ? 0.4374 0.3708 0.3530 -0.0657 0.0621  0.0203  98  PHE A N   
832   C CA  . PHE A 98  ? 0.3912 0.3444 0.3355 -0.0646 0.0527  0.0199  98  PHE A CA  
833   C C   . PHE A 98  ? 0.4004 0.3865 0.3772 -0.0643 0.0577  0.0143  98  PHE A C   
834   O O   . PHE A 98  ? 0.3561 0.3606 0.3556 -0.0684 0.0578  0.0130  98  PHE A O   
835   C CB  . PHE A 98  ? 0.3917 0.3394 0.3342 -0.0558 0.0350  0.0216  98  PHE A CB  
836   C CG  . PHE A 98  ? 0.4292 0.3921 0.3945 -0.0555 0.0258  0.0217  98  PHE A CG  
837   C CD1 . PHE A 98  ? 0.4664 0.4183 0.4259 -0.0584 0.0226  0.0244  98  PHE A CD1 
838   C CD2 . PHE A 98  ? 0.4364 0.4219 0.4261 -0.0520 0.0206  0.0191  98  PHE A CD2 
839   C CE1 . PHE A 98  ? 0.4267 0.3929 0.4063 -0.0576 0.0147  0.0234  98  PHE A CE1 
840   C CE2 . PHE A 98  ? 0.3734 0.3721 0.3813 -0.0523 0.0131  0.0191  98  PHE A CE2 
841   C CZ  . PHE A 98  ? 0.3682 0.3585 0.3718 -0.0551 0.0106  0.0208  98  PHE A CZ  
842   N N   . THR A 99  ? 0.3697 0.3625 0.3479 -0.0585 0.0612  0.0104  99  THR A N   
843   C CA  . THR A 99  ? 0.4322 0.4544 0.4392 -0.0553 0.0647  0.0044  99  THR A CA  
844   C C   . THR A 99  ? 0.3826 0.4240 0.4054 -0.0644 0.0793  0.0000  99  THR A C   
845   O O   . THR A 99  ? 0.2952 0.3619 0.3459 -0.0651 0.0775  -0.0032 99  THR A O   
846   C CB  . THR A 99  ? 0.3964 0.4170 0.3975 -0.0461 0.0659  0.0004  99  THR A CB  
847   O OG1 . THR A 99  ? 0.3744 0.3772 0.3614 -0.0397 0.0522  0.0037  99  THR A OG1 
848   C CG2 . THR A 99  ? 0.4017 0.4502 0.4314 -0.0397 0.0664  -0.0058 99  THR A CG2 
849   N N   . LYS A 100 ? 0.3219 0.3520 0.3266 -0.0723 0.0942  -0.0006 100 LYS A N   
850   C CA  . LYS A 100 ? 0.4252 0.4762 0.4467 -0.0831 0.1101  -0.0062 100 LYS A CA  
851   C C   . LYS A 100 ? 0.4208 0.4720 0.4497 -0.0941 0.1087  -0.0034 100 LYS A C   
852   O O   . LYS A 100 ? 0.4149 0.4906 0.4675 -0.1028 0.1173  -0.0092 100 LYS A O   
853   C CB  . LYS A 100 ? 0.5568 0.5942 0.5543 -0.0907 0.1285  -0.0077 100 LYS A CB  
854   C CG  . LYS A 100 ? 0.7621 0.7567 0.7156 -0.0964 0.1297  0.0009  100 LYS A CG  
855   C CD  . LYS A 100 ? 0.8280 0.8067 0.7745 -0.1068 0.1270  0.0071  100 LYS A CD  
856   C CE  . LYS A 100 ? 0.9012 0.8349 0.8019 -0.1113 0.1281  0.0154  100 LYS A CE  
857   N NZ  . LYS A 100 ? 0.8561 0.7766 0.7559 -0.1156 0.1190  0.0206  100 LYS A NZ  
858   N N   . LEU A 101 ? 0.3797 0.4047 0.3897 -0.0937 0.0976  0.0043  101 LEU A N   
859   C CA  . LEU A 101 ? 0.3814 0.4043 0.3976 -0.1020 0.0946  0.0063  101 LEU A CA  
860   C C   . LEU A 101 ? 0.3163 0.3700 0.3670 -0.0977 0.0850  0.0023  101 LEU A C   
861   O O   . LEU A 101 ? 0.3522 0.4200 0.4200 -0.1064 0.0879  -0.0009 101 LEU A O   
862   C CB  . LEU A 101 ? 0.3993 0.3875 0.3871 -0.0992 0.0837  0.0144  101 LEU A CB  
863   C CG  . LEU A 101 ? 0.4886 0.4721 0.4819 -0.1025 0.0755  0.0163  101 LEU A CG  
864   C CD1 . LEU A 101 ? 0.5337 0.5105 0.5235 -0.1185 0.0889  0.0153  101 LEU A CD1 
865   C CD2 . LEU A 101 ? 0.5330 0.4867 0.5014 -0.0946 0.0622  0.0225  101 LEU A CD2 
866   N N   . ASN A 102 ? 0.2994 0.3618 0.3583 -0.0849 0.0735  0.0023  102 ASN A N   
867   C CA  . ASN A 102 ? 0.2856 0.3726 0.3712 -0.0793 0.0634  -0.0004 102 ASN A CA  
868   C C   . ASN A 102 ? 0.3423 0.4585 0.4512 -0.0738 0.0670  -0.0077 102 ASN A C   
869   O O   . ASN A 102 ? 0.2574 0.3925 0.3858 -0.0677 0.0579  -0.0099 102 ASN A O   
870   C CB  . ASN A 102 ? 0.2550 0.3306 0.3327 -0.0696 0.0485  0.0044  102 ASN A CB  
871   C CG  . ASN A 102 ? 0.3410 0.3939 0.4016 -0.0725 0.0426  0.0097  102 ASN A CG  
872   O OD1 . ASN A 102 ? 0.3988 0.4559 0.4677 -0.0772 0.0400  0.0094  102 ASN A OD1 
873   N ND2 . ASN A 102 ? 0.2760 0.3050 0.3126 -0.0687 0.0395  0.0136  102 ASN A ND2 
874   N N   . TYR A 103 ? 0.3538 0.4738 0.4602 -0.0755 0.0802  -0.0120 103 TYR A N   
875   C CA  . TYR A 103 ? 0.3322 0.4764 0.4570 -0.0662 0.0827  -0.0195 103 TYR A CA  
876   C C   . TYR A 103 ? 0.2977 0.4774 0.4569 -0.0653 0.0796  -0.0268 103 TYR A C   
877   O O   . TYR A 103 ? 0.2982 0.4946 0.4725 -0.0525 0.0725  -0.0310 103 TYR A O   
878   C CB  . TYR A 103 ? 0.3988 0.5429 0.5155 -0.0712 0.1006  -0.0242 103 TYR A CB  
879   C CG  . TYR A 103 ? 0.4041 0.5729 0.5390 -0.0605 0.1048  -0.0336 103 TYR A CG  
880   C CD1 . TYR A 103 ? 0.4414 0.5974 0.5637 -0.0467 0.0991  -0.0329 103 TYR A CD1 
881   C CD2 . TYR A 103 ? 0.4649 0.6703 0.6306 -0.0639 0.1140  -0.0442 103 TYR A CD2 
882   C CE1 . TYR A 103 ? 0.5142 0.6905 0.6519 -0.0350 0.1023  -0.0422 103 TYR A CE1 
883   C CE2 . TYR A 103 ? 0.4905 0.7205 0.6747 -0.0519 0.1170  -0.0542 103 TYR A CE2 
884   C CZ  . TYR A 103 ? 0.5450 0.7590 0.7142 -0.0367 0.1110  -0.0530 103 TYR A CZ  
885   O OH  . TYR A 103 ? 0.6015 0.8375 0.7879 -0.0228 0.1134  -0.0636 103 TYR A OH  
886   N N   . GLU A 104 ? 0.2845 0.4749 0.4551 -0.0783 0.0844  -0.0290 104 GLU A N   
887   C CA  . GLU A 104 ? 0.2972 0.5241 0.5012 -0.0788 0.0826  -0.0379 104 GLU A CA  
888   C C   . GLU A 104 ? 0.2447 0.4743 0.4558 -0.0754 0.0663  -0.0349 104 GLU A C   
889   O O   . GLU A 104 ? 0.2345 0.4928 0.4712 -0.0751 0.0621  -0.0420 104 GLU A O   
890   C CB  . GLU A 104 ? 0.3742 0.6150 0.5894 -0.0969 0.0981  -0.0443 104 GLU A CB  
891   C CG  . GLU A 104 ? 0.5143 0.7619 0.7285 -0.1017 0.1169  -0.0501 104 GLU A CG  
892   C CD  . GLU A 104 ? 0.6551 0.9441 0.9021 -0.0919 0.1188  -0.0627 104 GLU A CD  
893   O OE1 . GLU A 104 ? 0.6924 1.0053 0.9636 -0.0825 0.1051  -0.0671 104 GLU A OE1 
894   O OE2 . GLU A 104 ? 0.7279 1.0256 0.9758 -0.0929 0.1338  -0.0689 104 GLU A OE2 
895   N N   . LYS A 105 ? 0.2211 0.4234 0.4109 -0.0728 0.0574  -0.0256 105 LYS A N   
896   C CA  . LYS A 105 ? 0.2049 0.4085 0.3986 -0.0696 0.0433  -0.0228 105 LYS A CA  
897   C C   . LYS A 105 ? 0.2178 0.4321 0.4193 -0.0544 0.0318  -0.0235 105 LYS A C   
898   O O   . LYS A 105 ? 0.2066 0.4103 0.3979 -0.0451 0.0312  -0.0214 105 LYS A O   
899   C CB  . LYS A 105 ? 0.2281 0.4011 0.3975 -0.0717 0.0386  -0.0139 105 LYS A CB  
900   C CG  . LYS A 105 ? 0.2405 0.3986 0.3995 -0.0851 0.0468  -0.0126 105 LYS A CG  
901   C CD  . LYS A 105 ? 0.2090 0.3360 0.3424 -0.0836 0.0425  -0.0047 105 LYS A CD  
902   C CE  . LYS A 105 ? 0.2408 0.3480 0.3597 -0.0950 0.0499  -0.0031 105 LYS A CE  
903   N NZ  . LYS A 105 ? 0.2404 0.3184 0.3353 -0.0912 0.0432  0.0037  105 LYS A NZ  
904   N N   . PRO A 106 ? 0.2398 0.4720 0.4564 -0.0515 0.0220  -0.0264 106 PRO A N   
905   C CA  . PRO A 106 ? 0.2270 0.4640 0.4459 -0.0366 0.0099  -0.0260 106 PRO A CA  
906   C C   . PRO A 106 ? 0.1699 0.3782 0.3648 -0.0303 0.0038  -0.0169 106 PRO A C   
907   O O   . PRO A 106 ? 0.1780 0.3828 0.3694 -0.0182 -0.0021 -0.0164 106 PRO A O   
908   C CB  . PRO A 106 ? 0.2158 0.4682 0.4461 -0.0379 0.0000  -0.0283 106 PRO A CB  
909   C CG  . PRO A 106 ? 0.2293 0.4995 0.4763 -0.0516 0.0092  -0.0355 106 PRO A CG  
910   C CD  . PRO A 106 ? 0.1482 0.3964 0.3794 -0.0617 0.0217  -0.0311 106 PRO A CD  
911   N N   . ILE A 107 ? 0.1538 0.3414 0.3322 -0.0380 0.0047  -0.0105 107 ILE A N   
912   C CA  . ILE A 107 ? 0.1903 0.3545 0.3490 -0.0334 -0.0009 -0.0034 107 ILE A CA  
913   C C   . ILE A 107 ? 0.2465 0.3969 0.3941 -0.0293 0.0046  -0.0029 107 ILE A C   
914   O O   . ILE A 107 ? 0.1950 0.3274 0.3279 -0.0246 -0.0004 0.0014  107 ILE A O   
915   C CB  . ILE A 107 ? 0.1782 0.3285 0.3258 -0.0415 -0.0026 0.0015  107 ILE A CB  
916   C CG1 . ILE A 107 ? 0.1798 0.3227 0.3229 -0.0499 0.0065  0.0011  107 ILE A CG1 
917   C CG2 . ILE A 107 ? 0.1450 0.3065 0.3001 -0.0441 -0.0092 0.0009  107 ILE A CG2 
918   C CD1 . ILE A 107 ? 0.2383 0.3647 0.3684 -0.0543 0.0035  0.0054  107 ILE A CD1 
919   N N   . TYR A 108 ? 0.2540 0.4123 0.4076 -0.0318 0.0154  -0.0077 108 TYR A N   
920   C CA  . TYR A 108 ? 0.3014 0.4486 0.4443 -0.0273 0.0218  -0.0087 108 TYR A CA  
921   C C   . TYR A 108 ? 0.2811 0.4449 0.4375 -0.0160 0.0227  -0.0158 108 TYR A C   
922   O O   . TYR A 108 ? 0.2330 0.3919 0.3833 -0.0119 0.0301  -0.0189 108 TYR A O   
923   C CB  . TYR A 108 ? 0.2770 0.4183 0.4124 -0.0375 0.0345  -0.0094 108 TYR A CB  
924   C CG  . TYR A 108 ? 0.2892 0.4030 0.4010 -0.0418 0.0321  -0.0023 108 TYR A CG  
925   C CD1 . TYR A 108 ? 0.2459 0.3545 0.3558 -0.0468 0.0252  0.0019  108 TYR A CD1 
926   C CD2 . TYR A 108 ? 0.2855 0.3796 0.3770 -0.0400 0.0360  -0.0010 108 TYR A CD2 
927   C CE1 . TYR A 108 ? 0.2848 0.3713 0.3758 -0.0489 0.0218  0.0069  108 TYR A CE1 
928   C CE2 . TYR A 108 ? 0.3155 0.3864 0.3865 -0.0426 0.0318  0.0044  108 TYR A CE2 
929   C CZ  . TYR A 108 ? 0.2936 0.3618 0.3656 -0.0466 0.0244  0.0081  108 TYR A CZ  
930   O OH  . TYR A 108 ? 0.2848 0.3330 0.3389 -0.0475 0.0192  0.0120  108 TYR A OH  
931   N N   . ARG A 109 ? 0.2083 0.3913 0.3820 -0.0095 0.0148  -0.0190 109 ARG A N   
932   C CA  . ARG A 109 ? 0.2143 0.4152 0.4029 0.0035  0.0143  -0.0270 109 ARG A CA  
933   C C   . ARG A 109 ? 0.2722 0.4503 0.4436 0.0168  0.0058  -0.0236 109 ARG A C   
934   O O   . ARG A 109 ? 0.3126 0.4868 0.4823 0.0257  -0.0065 -0.0214 109 ARG A O   
935   C CB  . ARG A 109 ? 0.2649 0.4951 0.4778 0.0068  0.0076  -0.0328 109 ARG A CB  
936   C CG  . ARG A 109 ? 0.3699 0.6331 0.6092 0.0107  0.0156  -0.0453 109 ARG A CG  
937   C CD  . ARG A 109 ? 0.4640 0.7594 0.7294 0.0074  0.0113  -0.0519 109 ARG A CD  
938   N NE  . ARG A 109 ? 0.5100 0.8019 0.7723 0.0178  -0.0065 -0.0484 109 ARG A NE  
939   C CZ  . ARG A 109 ? 0.5076 0.8108 0.7775 0.0120  -0.0139 -0.0483 109 ARG A CZ  
940   N NH1 . ARG A 109 ? 0.4766 0.7949 0.7592 -0.0042 -0.0053 -0.0519 109 ARG A NH1 
941   N NH2 . ARG A 109 ? 0.5067 0.8034 0.7688 0.0222  -0.0298 -0.0446 109 ARG A NH2 
942   N N   . PHE A 110 ? 0.2846 0.4444 0.4402 0.0172  0.0127  -0.0231 110 PHE A N   
943   C CA  . PHE A 110 ? 0.3051 0.4437 0.4453 0.0296  0.0075  -0.0227 110 PHE A CA  
944   C C   . PHE A 110 ? 0.2981 0.4484 0.4459 0.0373  0.0180  -0.0325 110 PHE A C   
945   O O   . PHE A 110 ? 0.3234 0.4790 0.4710 0.0281  0.0314  -0.0351 110 PHE A O   
946   C CB  . PHE A 110 ? 0.2610 0.3669 0.3743 0.0230  0.0060  -0.0148 110 PHE A CB  
947   C CG  . PHE A 110 ? 0.3326 0.4286 0.4390 0.0148  -0.0027 -0.0063 110 PHE A CG  
948   C CD1 . PHE A 110 ? 0.3290 0.4303 0.4378 0.0019  0.0009  -0.0032 110 PHE A CD1 
949   C CD2 . PHE A 110 ? 0.3708 0.4501 0.4665 0.0200  -0.0138 -0.0017 110 PHE A CD2 
950   C CE1 . PHE A 110 ? 0.2884 0.3827 0.3921 -0.0047 -0.0063 0.0030  110 PHE A CE1 
951   C CE2 . PHE A 110 ? 0.3469 0.4189 0.4362 0.0113  -0.0199 0.0052  110 PHE A CE2 
952   C CZ  . PHE A 110 ? 0.3166 0.3980 0.4113 -0.0005 -0.0160 0.0070  110 PHE A CZ  
953   N N   . GLU A 111 ? 0.3376 0.4905 0.4903 0.0544  0.0124  -0.0383 111 GLU A N   
954   C CA  . GLU A 111 ? 0.3956 0.5612 0.5564 0.0631  0.0231  -0.0493 111 GLU A CA  
955   C C   . GLU A 111 ? 0.3468 0.4862 0.4823 0.0579  0.0321  -0.0474 111 GLU A C   
956   O O   . GLU A 111 ? 0.2989 0.4496 0.4376 0.0551  0.0468  -0.0544 111 GLU A O   
957   C CB  . GLU A 111 ? 0.5761 0.7441 0.7433 0.0851  0.0134  -0.0560 111 GLU A CB  
958   C CG  . GLU A 111 ? 0.7155 0.9027 0.8960 0.0965  0.0244  -0.0698 111 GLU A CG  
959   C CD  . GLU A 111 ? 0.8323 1.0666 1.0475 0.0914  0.0354  -0.0801 111 GLU A CD  
960   O OE1 . GLU A 111 ? 0.8799 1.1240 1.0967 0.0792  0.0531  -0.0839 111 GLU A OE1 
961   O OE2 . GLU A 111 ? 0.8604 1.1211 1.0999 0.0989  0.0263  -0.0846 111 GLU A OE2 
962   N N   . ARG A 112 ? 0.3340 0.4392 0.4437 0.0551  0.0238  -0.0383 112 ARG A N   
963   C CA  . ARG A 112 ? 0.4066 0.4860 0.4911 0.0509  0.0297  -0.0371 112 ARG A CA  
964   C C   . ARG A 112 ? 0.4024 0.4877 0.4839 0.0353  0.0421  -0.0355 112 ARG A C   
965   O O   . ARG A 112 ? 0.3950 0.4713 0.4619 0.0336  0.0524  -0.0389 112 ARG A O   
966   C CB  . ARG A 112 ? 0.4138 0.4592 0.4749 0.0488  0.0174  -0.0284 112 ARG A CB  
967   C CG  . ARG A 112 ? 0.4299 0.4483 0.4646 0.0450  0.0208  -0.0281 112 ARG A CG  
968   C CD  . ARG A 112 ? 0.4515 0.4641 0.4795 0.0581  0.0267  -0.0377 112 ARG A CD  
969   N NE  . ARG A 112 ? 0.4732 0.4513 0.4727 0.0578  0.0225  -0.0366 112 ARG A NE  
970   C CZ  . ARG A 112 ? 0.4970 0.4630 0.4812 0.0638  0.0293  -0.0440 112 ARG A CZ  
971   N NH1 . ARG A 112 ? 0.5088 0.4956 0.5039 0.0707  0.0423  -0.0532 112 ARG A NH1 
972   N NH2 . ARG A 112 ? 0.4721 0.4063 0.4304 0.0623  0.0236  -0.0430 112 ARG A NH2 
973   N N   . ILE A 113 ? 0.3909 0.4883 0.4830 0.0240  0.0411  -0.0303 113 ILE A N   
974   C CA  . ILE A 113 ? 0.3625 0.4623 0.4500 0.0095  0.0524  -0.0285 113 ILE A CA  
975   C C   . ILE A 113 ? 0.3615 0.4835 0.4612 0.0092  0.0689  -0.0381 113 ILE A C   
976   O O   . ILE A 113 ? 0.3919 0.5042 0.4752 0.0019  0.0812  -0.0388 113 ILE A O   
977   C CB  . ILE A 113 ? 0.3091 0.4184 0.4077 -0.0011 0.0479  -0.0227 113 ILE A CB  
978   C CG1 . ILE A 113 ? 0.3625 0.4496 0.4465 -0.0034 0.0347  -0.0137 113 ILE A CG1 
979   C CG2 . ILE A 113 ? 0.3129 0.4260 0.4091 -0.0149 0.0607  -0.0224 113 ILE A CG2 
980   C CD1 . ILE A 113 ? 0.3934 0.4557 0.4524 -0.0105 0.0359  -0.0089 113 ILE A CD1 
981   N N   . ARG A 114 ? 0.3673 0.5198 0.4954 0.0170  0.0696  -0.0464 114 ARG A N   
982   C CA  . ARG A 114 ? 0.4461 0.6257 0.5906 0.0165  0.0862  -0.0576 114 ARG A CA  
983   C C   . ARG A 114 ? 0.5188 0.6840 0.6448 0.0242  0.0948  -0.0630 114 ARG A C   
984   O O   . ARG A 114 ? 0.5119 0.6810 0.6314 0.0159  0.1122  -0.0673 114 ARG A O   
985   C CB  . ARG A 114 ? 0.4738 0.6906 0.6542 0.0270  0.0820  -0.0671 114 ARG A CB  
986   C CG  . ARG A 114 ? 0.5638 0.7905 0.7588 0.0227  0.0693  -0.0617 114 ARG A CG  
987   C CD  . ARG A 114 ? 0.6283 0.8926 0.8579 0.0342  0.0635  -0.0720 114 ARG A CD  
988   N NE  . ARG A 114 ? 0.6407 0.9048 0.8754 0.0360  0.0464  -0.0658 114 ARG A NE  
989   C CZ  . ARG A 114 ? 0.6406 0.9196 0.8912 0.0517  0.0329  -0.0702 114 ARG A CZ  
990   N NH1 . ARG A 114 ? 0.6400 0.9369 0.9056 0.0687  0.0334  -0.0816 114 ARG A NH1 
991   N NH2 . ARG A 114 ? 0.6225 0.8978 0.8725 0.0514  0.0184  -0.0637 114 ARG A NH2 
992   N N   . GLU A 115 ? 0.5652 0.7107 0.6795 0.0390  0.0832  -0.0626 115 GLU A N   
993   C CA  . GLU A 115 ? 0.5552 0.6836 0.6494 0.0472  0.0899  -0.0683 115 GLU A CA  
994   C C   . GLU A 115 ? 0.5583 0.6583 0.6194 0.0342  0.0968  -0.0618 115 GLU A C   
995   O O   . GLU A 115 ? 0.6332 0.7336 0.6834 0.0309  0.1128  -0.0675 115 GLU A O   
996   C CB  . GLU A 115 ? 0.5826 0.6892 0.6673 0.0638  0.0742  -0.0679 115 GLU A CB  
997   C CG  . GLU A 115 ? 0.6416 0.7715 0.7540 0.0801  0.0658  -0.0747 115 GLU A CG  
998   C CD  . GLU A 115 ? 0.7152 0.8165 0.8139 0.0934  0.0476  -0.0704 115 GLU A CD  
999   O OE1 . GLU A 115 ? 0.7574 0.8225 0.8268 0.0903  0.0432  -0.0643 115 GLU A OE1 
1000  O OE2 . GLU A 115 ? 0.7106 0.8246 0.8268 0.1066  0.0374  -0.0732 115 GLU A OE2 
1001  N N   . LEU A 116 ? 0.5207 0.5962 0.5650 0.0270  0.0849  -0.0503 116 LEU A N   
1002  C CA  . LEU A 116 ? 0.5127 0.5597 0.5246 0.0172  0.0876  -0.0443 116 LEU A CA  
1003  C C   . LEU A 116 ? 0.5341 0.5891 0.5421 0.0033  0.1041  -0.0441 116 LEU A C   
1004  O O   . LEU A 116 ? 0.5497 0.5853 0.5296 -0.0013 0.1130  -0.0439 116 LEU A O   
1005  C CB  . LEU A 116 ? 0.4802 0.5076 0.4823 0.0120  0.0714  -0.0334 116 LEU A CB  
1006  C CG  . LEU A 116 ? 0.4927 0.5068 0.4937 0.0219  0.0556  -0.0321 116 LEU A CG  
1007  C CD1 . LEU A 116 ? 0.4524 0.4554 0.4501 0.0142  0.0422  -0.0224 116 LEU A CD1 
1008  C CD2 . LEU A 116 ? 0.5192 0.5084 0.4953 0.0292  0.0557  -0.0367 116 LEU A CD2 
1009  N N   . MET A 117 ? 0.5584 0.6392 0.5917 -0.0044 0.1081  -0.0438 117 MET A N   
1010  C CA  . MET A 117 ? 0.5991 0.6839 0.6272 -0.0201 0.1238  -0.0428 117 MET A CA  
1011  C C   . MET A 117 ? 0.6655 0.7646 0.6942 -0.0207 0.1444  -0.0534 117 MET A C   
1012  O O   . MET A 117 ? 0.6642 0.7507 0.6704 -0.0328 0.1590  -0.0519 117 MET A O   
1013  C CB  . MET A 117 ? 0.5622 0.6709 0.6183 -0.0287 0.1224  -0.0412 117 MET A CB  
1014  C CG  . MET A 117 ? 0.5998 0.6900 0.6474 -0.0332 0.1071  -0.0300 117 MET A CG  
1015  S SD  . MET A 117 ? 0.6543 0.7000 0.6559 -0.0383 0.1049  -0.0209 117 MET A SD  
1016  C CE  . MET A 117 ? 0.6701 0.7108 0.6659 -0.0560 0.1129  -0.0151 117 MET A CE  
1017  N N   . ASN A 118 ? 0.7048 0.8288 0.7572 -0.0074 0.1461  -0.0645 118 ASN A N   
1018  C CA  . ASN A 118 ? 0.7605 0.9018 0.8166 -0.0049 0.1653  -0.0770 118 ASN A CA  
1019  C C   . ASN A 118 ? 0.8153 0.9249 0.8337 0.0007  0.1693  -0.0778 118 ASN A C   
1020  O O   . ASN A 118 ? 0.8401 0.9635 0.8610 0.0060  0.1844  -0.0897 118 ASN A O   
1021  C CB  . ASN A 118 ? 0.7722 0.9499 0.8667 0.0114  0.1624  -0.0895 118 ASN A CB  
1022  C CG  . ASN A 118 ? 0.7990 1.0184 0.9335 0.0042  0.1664  -0.0944 118 ASN A CG  
1023  O OD1 . ASN A 118 ? 0.8229 1.0449 0.9567 -0.0148 0.1750  -0.0897 118 ASN A OD1 
1024  N ND2 . ASN A 118 ? 0.7909 1.0420 0.9596 0.0198  0.1594  -0.1044 118 ASN A ND2 
1025  N N   . LYS A 119 ? 0.8125 0.8830 0.7971 -0.0002 0.1573  -0.0675 119 LYS A N   
1026  C CA  . LYS A 119 ? 0.8166 0.8592 0.7704 0.0092  0.1556  -0.0702 119 LYS A CA  
1027  C C   . LYS A 119 ? 0.9126 0.9233 0.8231 -0.0022 0.1634  -0.0644 119 LYS A C   
1028  O O   . LYS A 119 ? 0.9248 0.9212 0.8223 -0.0144 0.1597  -0.0537 119 LYS A O   
1029  C CB  . LYS A 119 ? 0.7497 0.7730 0.7004 0.0202  0.1324  -0.0654 119 LYS A CB  
1030  C CG  . LYS A 119 ? 0.7321 0.7589 0.6911 0.0388  0.1288  -0.0758 119 LYS A CG  
1031  C CD  . LYS A 119 ? 0.7091 0.7397 0.6894 0.0479  0.1095  -0.0724 119 LYS A CD  
1032  C CE  . LYS A 119 ? 0.7271 0.7356 0.6951 0.0638  0.0992  -0.0772 119 LYS A CE  
1033  N NZ  . LYS A 119 ? 0.7099 0.7396 0.7053 0.0809  0.0965  -0.0863 119 LYS A NZ  
1034  N N   . GLU A 120 ? 0.9791 0.9768 0.8652 0.0035  0.1731  -0.0719 120 GLU A N   
1035  C CA  . GLU A 120 ? 1.0324 1.0001 0.8733 -0.0051 0.1831  -0.0691 120 GLU A CA  
1036  C C   . GLU A 120 ? 1.0190 0.9481 0.8276 -0.0062 0.1636  -0.0579 120 GLU A C   
1037  O O   . GLU A 120 ? 1.0327 0.9517 0.8342 -0.0167 0.1580  -0.0472 120 GLU A O   
1038  C CB  . GLU A 120 ? 1.0668 1.0321 0.8922 0.0043  0.1963  -0.0819 120 GLU A CB  
1039  N N   . LYS A 121 ? 0.9658 0.8733 0.7544 0.0047  0.1534  -0.0615 121 LYS A N   
1040  C CA  . LYS A 121 ? 0.9141 0.7933 0.6839 0.0059  0.1312  -0.0536 121 LYS A CA  
1041  C C   . LYS A 121 ? 0.8794 0.7710 0.6818 0.0139  0.1141  -0.0533 121 LYS A C   
1042  O O   . LYS A 121 ? 0.9181 0.8322 0.7486 0.0225  0.1178  -0.0605 121 LYS A O   
1043  C CB  . LYS A 121 ? 0.9254 0.7730 0.6544 0.0113  0.1285  -0.0582 121 LYS A CB  
1044  N N   . LEU A 122 ? 0.7596 0.6364 0.5573 0.0112  0.0953  -0.0450 122 LEU A N   
1045  C CA  . LEU A 122 ? 0.6579 0.5422 0.4812 0.0162  0.0793  -0.0433 122 LEU A CA  
1046  C C   . LEU A 122 ? 0.7054 0.5623 0.5071 0.0201  0.0638  -0.0444 122 LEU A C   
1047  O O   . LEU A 122 ? 0.7723 0.6090 0.5486 0.0148  0.0563  -0.0405 122 LEU A O   
1048  C CB  . LEU A 122 ? 0.6265 0.5226 0.4689 0.0076  0.0716  -0.0335 122 LEU A CB  
1049  C CG  . LEU A 122 ? 0.6345 0.5621 0.5099 0.0046  0.0809  -0.0328 122 LEU A CG  
1050  C CD1 . LEU A 122 ? 0.6745 0.6161 0.5505 0.0038  0.1022  -0.0399 122 LEU A CD1 
1051  C CD2 . LEU A 122 ? 0.5966 0.5252 0.4747 -0.0064 0.0764  -0.0232 122 LEU A CD2 
1052  N N   . ASN A 123 ? 0.6662 0.5211 0.4771 0.0295  0.0582  -0.0503 123 ASN A N   
1053  C CA  . ASN A 123 ? 0.6344 0.4626 0.4261 0.0313  0.0434  -0.0520 123 ASN A CA  
1054  C C   . ASN A 123 ? 0.6286 0.4582 0.4351 0.0247  0.0269  -0.0441 123 ASN A C   
1055  O O   . ASN A 123 ? 0.6265 0.4761 0.4557 0.0198  0.0269  -0.0373 123 ASN A O   
1056  C CB  . ASN A 123 ? 0.6178 0.4370 0.4079 0.0436  0.0445  -0.0618 123 ASN A CB  
1057  C CG  . ASN A 123 ? 0.6292 0.4657 0.4512 0.0506  0.0423  -0.0616 123 ASN A CG  
1058  O OD1 . ASN A 123 ? 0.5931 0.4406 0.4348 0.0451  0.0342  -0.0537 123 ASN A OD1 
1059  N ND2 . ASN A 123 ? 0.6243 0.4623 0.4498 0.0640  0.0490  -0.0711 123 ASN A ND2 
1060  N N   . ARG A 124 ? 0.5117 0.3148 0.3804 -0.0563 0.0551  -0.0733 124 ARG A N   
1061  C CA  . ARG A 124 ? 0.4988 0.3108 0.3726 -0.0589 0.0429  -0.0666 124 ARG A CA  
1062  C C   . ARG A 124 ? 0.5219 0.3452 0.4184 -0.0524 0.0407  -0.0626 124 ARG A C   
1063  O O   . ARG A 124 ? 0.5074 0.3451 0.4144 -0.0518 0.0347  -0.0564 124 ARG A O   
1064  C CB  . ARG A 124 ? 0.5283 0.3268 0.3874 -0.0654 0.0370  -0.0687 124 ARG A CB  
1065  C CG  . ARG A 124 ? 0.5392 0.3466 0.4080 -0.0679 0.0267  -0.0632 124 ARG A CG  
1066  C CD  . ARG A 124 ? 0.6312 0.4289 0.4861 -0.0763 0.0196  -0.0656 124 ARG A CD  
1067  N NE  . ARG A 124 ? 0.6336 0.4429 0.4995 -0.0798 0.0104  -0.0608 124 ARG A NE  
1068  C CZ  . ARG A 124 ? 0.7265 0.5369 0.6043 -0.0792 0.0100  -0.0585 124 ARG A CZ  
1069  N NH1 . ARG A 124 ? 0.7793 0.5793 0.6589 -0.0744 0.0166  -0.0601 124 ARG A NH1 
1070  N NH2 . ARG A 124 ? 0.7081 0.5291 0.5956 -0.0833 0.0032  -0.0547 124 ARG A NH2 
1071  N N   . GLU A 125 ? 0.5743 0.3900 0.4774 -0.0471 0.0452  -0.0662 125 GLU A N   
1072  C CA  . GLU A 125 ? 0.5816 0.4041 0.5025 -0.0403 0.0420  -0.0624 125 GLU A CA  
1073  C C   . GLU A 125 ? 0.4945 0.3345 0.4327 -0.0343 0.0433  -0.0601 125 GLU A C   
1074  O O   . GLU A 125 ? 0.4254 0.2755 0.3752 -0.0312 0.0374  -0.0545 125 GLU A O   
1075  C CB  . GLU A 125 ? 0.6610 0.4696 0.5840 -0.0346 0.0463  -0.0674 125 GLU A CB  
1076  C CG  . GLU A 125 ? 0.7956 0.5847 0.7016 -0.0404 0.0457  -0.0705 125 GLU A CG  
1077  C CD  . GLU A 125 ? 0.9009 0.6804 0.7880 -0.0473 0.0505  -0.0764 125 GLU A CD  
1078  O OE1 . GLU A 125 ? 0.9429 0.7151 0.8154 -0.0557 0.0453  -0.0761 125 GLU A OE1 
1079  O OE2 . GLU A 125 ? 0.9075 0.6861 0.7940 -0.0446 0.0595  -0.0817 125 GLU A OE2 
1080  N N   . GLU A 126 ? 0.4889 0.3316 0.4283 -0.0331 0.0518  -0.0648 126 GLU A N   
1081  C CA  . GLU A 126 ? 0.4549 0.3142 0.4115 -0.0285 0.0541  -0.0637 126 GLU A CA  
1082  C C   . GLU A 126 ? 0.4598 0.3301 0.4131 -0.0334 0.0484  -0.0571 126 GLU A C   
1083  O O   . GLU A 126 ? 0.4344 0.3191 0.4027 -0.0298 0.0454  -0.0533 126 GLU A O   
1084  C CB  . GLU A 126 ? 0.4560 0.3137 0.4147 -0.0272 0.0667  -0.0716 126 GLU A CB  
1085  C CG  . GLU A 126 ? 0.5063 0.3576 0.4761 -0.0200 0.0728  -0.0791 126 GLU A CG  
1086  C CD  . GLU A 126 ? 0.6382 0.4823 0.6038 -0.0213 0.0871  -0.0883 126 GLU A CD  
1087  O OE1 . GLU A 126 ? 0.6661 0.5057 0.6143 -0.0287 0.0925  -0.0887 126 GLU A OE1 
1088  O OE2 . GLU A 126 ? 0.6682 0.5098 0.6471 -0.0146 0.0932  -0.0955 126 GLU A OE2 
1089  N N   . LEU A 127 ? 0.4301 0.2935 0.3641 -0.0411 0.0463  -0.0560 127 LEU A N   
1090  C CA  . LEU A 127 ? 0.4311 0.3043 0.3627 -0.0448 0.0397  -0.0499 127 LEU A CA  
1091  C C   . LEU A 127 ? 0.4011 0.2820 0.3416 -0.0445 0.0299  -0.0439 127 LEU A C   
1092  O O   . LEU A 127 ? 0.4661 0.3599 0.4147 -0.0440 0.0256  -0.0389 127 LEU A O   
1093  C CB  . LEU A 127 ? 0.4308 0.2936 0.3394 -0.0522 0.0378  -0.0506 127 LEU A CB  
1094  C CG  . LEU A 127 ? 0.4510 0.3059 0.3455 -0.0542 0.0470  -0.0546 127 LEU A CG  
1095  C CD1 . LEU A 127 ? 0.5005 0.3406 0.3685 -0.0609 0.0429  -0.0556 127 LEU A CD1 
1096  C CD2 . LEU A 127 ? 0.4490 0.3160 0.3511 -0.0528 0.0486  -0.0510 127 LEU A CD2 
1097  N N   . LEU A 128 ? 0.3974 0.2692 0.3355 -0.0452 0.0273  -0.0446 128 LEU A N   
1098  C CA  . LEU A 128 ? 0.3986 0.2750 0.3439 -0.0454 0.0201  -0.0394 128 LEU A CA  
1099  C C   . LEU A 128 ? 0.4023 0.2884 0.3642 -0.0378 0.0201  -0.0366 128 LEU A C   
1100  O O   . LEU A 128 ? 0.3892 0.2844 0.3576 -0.0379 0.0149  -0.0312 128 LEU A O   
1101  C CB  . LEU A 128 ? 0.3644 0.2259 0.3026 -0.0478 0.0192  -0.0414 128 LEU A CB  
1102  C CG  . LEU A 128 ? 0.4302 0.2884 0.3594 -0.0566 0.0134  -0.0406 128 LEU A CG  
1103  C CD1 . LEU A 128 ? 0.4228 0.2637 0.3442 -0.0593 0.0143  -0.0438 128 LEU A CD1 
1104  C CD2 . LEU A 128 ? 0.4440 0.3153 0.3832 -0.0581 0.0078  -0.0346 128 LEU A CD2 
1105  N N   . ASP A 129 ? 0.4270 0.3113 0.3963 -0.0309 0.0255  -0.0407 129 ASP A N   
1106  C CA  . ASP A 129 ? 0.4221 0.3160 0.4078 -0.0230 0.0240  -0.0389 129 ASP A CA  
1107  C C   . ASP A 129 ? 0.4171 0.3271 0.4112 -0.0230 0.0245  -0.0370 129 ASP A C   
1108  O O   . ASP A 129 ? 0.3775 0.2972 0.3816 -0.0197 0.0200  -0.0330 129 ASP A O   
1109  C CB  . ASP A 129 ? 0.4635 0.3523 0.4581 -0.0151 0.0288  -0.0449 129 ASP A CB  
1110  C CG  . ASP A 129 ? 0.4470 0.3196 0.4356 -0.0127 0.0265  -0.0455 129 ASP A CG  
1111  O OD1 . ASP A 129 ? 0.4502 0.3156 0.4273 -0.0185 0.0225  -0.0414 129 ASP A OD1 
1112  O OD2 . ASP A 129 ? 0.4783 0.3453 0.4742 -0.0052 0.0290  -0.0503 129 ASP A OD2 
1113  N N   . LEU A 130 ? 0.4604 0.3714 0.4486 -0.0269 0.0300  -0.0398 130 LEU A N   
1114  C CA  . LEU A 130 ? 0.4204 0.3445 0.4144 -0.0277 0.0305  -0.0374 130 LEU A CA  
1115  C C   . LEU A 130 ? 0.4067 0.3366 0.3969 -0.0317 0.0225  -0.0306 130 LEU A C   
1116  O O   . LEU A 130 ? 0.3704 0.3121 0.3704 -0.0298 0.0199  -0.0272 130 LEU A O   
1117  C CB  . LEU A 130 ? 0.3487 0.2689 0.3330 -0.0317 0.0386  -0.0414 130 LEU A CB  
1118  C CG  . LEU A 130 ? 0.3594 0.2902 0.3497 -0.0321 0.0418  -0.0403 130 LEU A CG  
1119  C CD1 . LEU A 130 ? 0.4143 0.3568 0.4275 -0.0253 0.0443  -0.0430 130 LEU A CD1 
1120  C CD2 . LEU A 130 ? 0.4453 0.3671 0.4209 -0.0368 0.0511  -0.0442 130 LEU A CD2 
1121  N N   . GLN A 131 ? 0.3388 0.2608 0.3162 -0.0373 0.0186  -0.0294 131 GLN A N   
1122  C CA  . GLN A 131 ? 0.3458 0.2744 0.3227 -0.0411 0.0114  -0.0241 131 GLN A CA  
1123  C C   . GLN A 131 ? 0.2907 0.2246 0.2785 -0.0378 0.0077  -0.0203 131 GLN A C   
1124  O O   . GLN A 131 ? 0.3792 0.3240 0.3740 -0.0373 0.0047  -0.0164 131 GLN A O   
1125  C CB  . GLN A 131 ? 0.3224 0.2421 0.2866 -0.0477 0.0077  -0.0250 131 GLN A CB  
1126  C CG  . GLN A 131 ? 0.3630 0.2770 0.3124 -0.0518 0.0083  -0.0275 131 GLN A CG  
1127  C CD  . GLN A 131 ? 0.4064 0.3110 0.3440 -0.0579 0.0036  -0.0296 131 GLN A CD  
1128  O OE1 . GLN A 131 ? 0.4219 0.3189 0.3593 -0.0589 0.0041  -0.0315 131 GLN A OE1 
1129  N NE2 . GLN A 131 ? 0.4675 0.3716 0.3948 -0.0619 -0.0017 -0.0295 131 GLN A NE2 
1130  N N   . THR A 132 ? 0.2816 0.2061 0.2689 -0.0355 0.0081  -0.0214 132 THR A N   
1131  C CA  . THR A 132 ? 0.2658 0.1899 0.2574 -0.0336 0.0044  -0.0174 132 THR A CA  
1132  C C   . THR A 132 ? 0.3254 0.2569 0.3283 -0.0258 0.0039  -0.0163 132 THR A C   
1133  O O   . THR A 132 ? 0.3165 0.2521 0.3225 -0.0247 0.0004  -0.0120 132 THR A O   
1134  C CB  . THR A 132 ? 0.2818 0.1896 0.2660 -0.0338 0.0049  -0.0188 132 THR A CB  
1135  O OG1 . THR A 132 ? 0.3765 0.2772 0.3506 -0.0410 0.0056  -0.0214 132 THR A OG1 
1136  C CG2 . THR A 132 ? 0.2923 0.1961 0.2757 -0.0340 0.0018  -0.0141 132 THR A CG2 
1137  N N   . LEU A 133 ? 0.2771 0.2099 0.2864 -0.0205 0.0076  -0.0207 133 LEU A N   
1138  C CA  . LEU A 133 ? 0.3167 0.2588 0.3396 -0.0133 0.0064  -0.0209 133 LEU A CA  
1139  C C   . LEU A 133 ? 0.3276 0.2841 0.3560 -0.0154 0.0058  -0.0184 133 LEU A C   
1140  O O   . LEU A 133 ? 0.2691 0.2329 0.3053 -0.0117 0.0021  -0.0160 133 LEU A O   
1141  C CB  . LEU A 133 ? 0.3026 0.2440 0.3343 -0.0076 0.0111  -0.0277 133 LEU A CB  
1142  C CG  . LEU A 133 ? 0.3697 0.2970 0.3992 -0.0023 0.0097  -0.0299 133 LEU A CG  
1143  C CD1 . LEU A 133 ? 0.3452 0.2711 0.3837 0.0026  0.0157  -0.0379 133 LEU A CD1 
1144  C CD2 . LEU A 133 ? 0.3297 0.2550 0.3626 0.0044  0.0021  -0.0263 133 LEU A CD2 
1145  N N   . ASN A 134 ? 0.2801 0.2393 0.3029 -0.0213 0.0087  -0.0186 134 ASN A N   
1146  C CA  . ASN A 134 ? 0.2745 0.2451 0.3008 -0.0233 0.0075  -0.0155 134 ASN A CA  
1147  C C   . ASN A 134 ? 0.3059 0.2794 0.3313 -0.0250 0.0017  -0.0101 134 ASN A C   
1148  O O   . ASN A 134 ? 0.4011 0.3832 0.4337 -0.0227 -0.0004 -0.0077 134 ASN A O   
1149  C CB  . ASN A 134 ? 0.2348 0.2044 0.2519 -0.0288 0.0105  -0.0164 134 ASN A CB  
1150  C CG  . ASN A 134 ? 0.2781 0.2494 0.2990 -0.0274 0.0178  -0.0208 134 ASN A CG  
1151  O OD1 . ASN A 134 ? 0.2569 0.2374 0.2862 -0.0261 0.0191  -0.0203 134 ASN A OD1 
1152  N ND2 . ASN A 134 ? 0.3592 0.3211 0.3742 -0.0280 0.0236  -0.0257 134 ASN A ND2 
1153  N N   . LEU A 135 ? 0.3065 0.2724 0.3233 -0.0293 -0.0003 -0.0087 135 LEU A N   
1154  C CA  . LEU A 135 ? 0.3265 0.2935 0.3430 -0.0314 -0.0039 -0.0044 135 LEU A CA  
1155  C C   . LEU A 135 ? 0.2972 0.2624 0.3174 -0.0257 -0.0055 -0.0026 135 LEU A C   
1156  O O   . LEU A 135 ? 0.2863 0.2583 0.3102 -0.0248 -0.0075 0.0004  135 LEU A O   
1157  C CB  . LEU A 135 ? 0.4108 0.3677 0.4188 -0.0370 -0.0042 -0.0048 135 LEU A CB  
1158  C CG  . LEU A 135 ? 0.4476 0.4087 0.4538 -0.0442 -0.0063 -0.0044 135 LEU A CG  
1159  C CD1 . LEU A 135 ? 0.4416 0.3920 0.4417 -0.0494 -0.0063 -0.0055 135 LEU A CD1 
1160  C CD2 . LEU A 135 ? 0.3889 0.3622 0.4027 -0.0450 -0.0084 -0.0011 135 LEU A CD2 
1161  N N   . LEU A 136 ? 0.2812 0.2356 0.2989 -0.0214 -0.0053 -0.0045 136 LEU A N   
1162  C CA  . LEU A 136 ? 0.3168 0.2649 0.3338 -0.0156 -0.0086 -0.0025 136 LEU A CA  
1163  C C   . LEU A 136 ? 0.3462 0.3049 0.3742 -0.0092 -0.0109 -0.0033 136 LEU A C   
1164  O O   . LEU A 136 ? 0.3419 0.2982 0.3686 -0.0052 -0.0150 -0.0008 136 LEU A O   
1165  C CB  . LEU A 136 ? 0.2863 0.2189 0.2979 -0.0115 -0.0087 -0.0048 136 LEU A CB  
1166  C CG  . LEU A 136 ? 0.3671 0.2849 0.3659 -0.0173 -0.0073 -0.0035 136 LEU A CG  
1167  C CD1 . LEU A 136 ? 0.4086 0.3119 0.4032 -0.0133 -0.0064 -0.0070 136 LEU A CD1 
1168  C CD2 . LEU A 136 ? 0.3588 0.2688 0.3491 -0.0189 -0.0092 0.0018  136 LEU A CD2 
1169  N N   . ALA A 137 ? 0.3456 0.3146 0.3833 -0.0083 -0.0081 -0.0071 137 ALA A N   
1170  C CA  . ALA A 137 ? 0.3566 0.3373 0.4067 -0.0036 -0.0096 -0.0086 137 ALA A CA  
1171  C C   . ALA A 137 ? 0.3292 0.3167 0.3785 -0.0057 -0.0123 -0.0041 137 ALA A C   
1172  O O   . ALA A 137 ? 0.2836 0.2761 0.3393 -0.0011 -0.0159 -0.0042 137 ALA A O   
1173  C CB  . ALA A 137 ? 0.2897 0.2794 0.3485 -0.0050 -0.0039 -0.0131 137 ALA A CB  
1174  N N   . TRP A 138 ? 0.3052 0.2929 0.3475 -0.0125 -0.0108 -0.0007 138 TRP A N   
1175  C CA  . TRP A 138 ? 0.2847 0.2798 0.3277 -0.0149 -0.0121 0.0028  138 TRP A CA  
1176  C C   . TRP A 138 ? 0.3216 0.3084 0.3557 -0.0160 -0.0140 0.0066  138 TRP A C   
1177  O O   . TRP A 138 ? 0.2881 0.2795 0.3217 -0.0193 -0.0137 0.0092  138 TRP A O   
1178  C CB  . TRP A 138 ? 0.2093 0.2110 0.2524 -0.0209 -0.0096 0.0032  138 TRP A CB  
1179  C CG  . TRP A 138 ? 0.2855 0.2934 0.3346 -0.0198 -0.0069 0.0001  138 TRP A CG  
1180  C CD1 . TRP A 138 ? 0.2560 0.2600 0.3036 -0.0202 -0.0034 -0.0035 138 TRP A CD1 
1181  C CD2 . TRP A 138 ? 0.2931 0.3107 0.3500 -0.0185 -0.0064 -0.0001 138 TRP A CD2 
1182  N NE1 . TRP A 138 ? 0.2302 0.2406 0.2839 -0.0197 0.0001  -0.0059 138 TRP A NE1 
1183  C CE2 . TRP A 138 ? 0.2730 0.2918 0.3327 -0.0187 -0.0019 -0.0039 138 TRP A CE2 
1184  C CE3 . TRP A 138 ? 0.2812 0.3055 0.3422 -0.0175 -0.0086 0.0021  138 TRP A CE3 
1185  C CZ2 . TRP A 138 ? 0.2190 0.2452 0.2858 -0.0185 0.0007  -0.0053 138 TRP A CZ2 
1186  C CZ3 . TRP A 138 ? 0.2488 0.2810 0.3172 -0.0168 -0.0070 0.0006  138 TRP A CZ3 
1187  C CH2 . TRP A 138 ? 0.3197 0.3525 0.3910 -0.0175 -0.0022 -0.0030 138 TRP A CH2 
1188  N N   . CYS A 139 ? 0.2482 0.2215 0.2748 -0.0133 -0.0154 0.0067  139 CYS A N   
1189  C CA  . CYS A 139 ? 0.2995 0.2605 0.3140 -0.0153 -0.0158 0.0104  139 CYS A CA  
1190  C C   . CYS A 139 ? 0.2825 0.2435 0.2943 -0.0118 -0.0189 0.0127  139 CYS A C   
1191  O O   . CYS A 139 ? 0.2750 0.2379 0.2913 -0.0047 -0.0235 0.0111  139 CYS A O   
1192  C CB  . CYS A 139 ? 0.3556 0.2994 0.3608 -0.0124 -0.0168 0.0099  139 CYS A CB  
1193  S SG  . CYS A 139 ? 0.3664 0.2907 0.3533 -0.0169 -0.0150 0.0143  139 CYS A SG  
1194  N N   . GLY A 140 ? 0.2820 0.2405 0.2869 -0.0170 -0.0163 0.0160  140 GLY A N   
1195  C CA  . GLY A 140 ? 0.3091 0.2663 0.3091 -0.0146 -0.0183 0.0181  140 GLY A CA  
1196  C C   . GLY A 140 ? 0.3239 0.2606 0.3066 -0.0104 -0.0215 0.0204  140 GLY A C   
1197  O O   . GLY A 140 ? 0.3856 0.3080 0.3598 -0.0096 -0.0217 0.0207  140 GLY A O   
1198  N N   . ARG A 141 ? 0.2602 0.1938 0.2360 -0.0074 -0.0245 0.0219  141 ARG A N   
1199  C CA  . ARG A 141 ? 0.3118 0.2234 0.2672 -0.0029 -0.0288 0.0245  141 ARG A CA  
1200  C C   . ARG A 141 ? 0.3602 0.2522 0.2982 -0.0090 -0.0226 0.0277  141 ARG A C   
1201  O O   . ARG A 141 ? 0.3993 0.2724 0.3245 -0.0052 -0.0257 0.0288  141 ARG A O   
1202  C CB  . ARG A 141 ? 0.2790 0.1899 0.2271 -0.0012 -0.0311 0.0258  141 ARG A CB  
1203  C CG  . ARG A 141 ? 0.3085 0.1939 0.2314 0.0037  -0.0364 0.0288  141 ARG A CG  
1204  C CD  . ARG A 141 ? 0.3402 0.2249 0.2561 0.0070  -0.0410 0.0290  141 ARG A CD  
1205  N NE  . ARG A 141 ? 0.4610 0.3175 0.3463 0.0087  -0.0432 0.0329  141 ARG A NE  
1206  C CZ  . ARG A 141 ? 0.5226 0.3656 0.3891 0.0012  -0.0341 0.0363  141 ARG A CZ  
1207  N NH1 . ARG A 141 ? 0.4248 0.2820 0.3028 -0.0082 -0.0228 0.0357  141 ARG A NH1 
1208  N NH2 . ARG A 141 ? 0.6013 0.4152 0.4366 0.0033  -0.0365 0.0399  141 ARG A NH2 
1209  N N   . THR A 142 ? 0.3785 0.2745 0.3168 -0.0184 -0.0138 0.0288  142 THR A N   
1210  C CA  . THR A 142 ? 0.4007 0.2784 0.3234 -0.0259 -0.0063 0.0311  142 THR A CA  
1211  C C   . THR A 142 ? 0.3955 0.2659 0.3187 -0.0267 -0.0061 0.0301  142 THR A C   
1212  O O   . THR A 142 ? 0.4471 0.2934 0.3513 -0.0265 -0.0055 0.0323  142 THR A O   
1213  C CB  . THR A 142 ? 0.3890 0.2788 0.3204 -0.0360 0.0033  0.0304  142 THR A CB  
1214  O OG1 . THR A 142 ? 0.3734 0.2675 0.3025 -0.0353 0.0041  0.0312  142 THR A OG1 
1215  C CG2 . THR A 142 ? 0.3439 0.2173 0.2631 -0.0452 0.0125  0.0315  142 THR A CG2 
1216  N N   . LEU A 143 ? 0.3754 0.2641 0.3181 -0.0275 -0.0066 0.0266  143 LEU A N   
1217  C CA  . LEU A 143 ? 0.3661 0.2474 0.3084 -0.0294 -0.0055 0.0251  143 LEU A CA  
1218  C C   . LEU A 143 ? 0.4451 0.3181 0.3849 -0.0194 -0.0129 0.0241  143 LEU A C   
1219  O O   . LEU A 143 ? 0.4309 0.2911 0.3651 -0.0197 -0.0121 0.0233  143 LEU A O   
1220  C CB  . LEU A 143 ? 0.3121 0.2133 0.2729 -0.0349 -0.0030 0.0215  143 LEU A CB  
1221  C CG  . LEU A 143 ? 0.3813 0.2900 0.3471 -0.0453 0.0039  0.0212  143 LEU A CG  
1222  C CD1 . LEU A 143 ? 0.3542 0.2802 0.3364 -0.0494 0.0039  0.0175  143 LEU A CD1 
1223  C CD2 . LEU A 143 ? 0.3703 0.2588 0.3212 -0.0522 0.0103  0.0227  143 LEU A CD2 
1224  N N   . ARG A 144 ? 0.4374 0.3176 0.3828 -0.0106 -0.0199 0.0233  144 ARG A N   
1225  C CA  . ARG A 144 ? 0.4748 0.3466 0.4193 -0.0004 -0.0273 0.0216  144 ARG A CA  
1226  C C   . ARG A 144 ? 0.5320 0.3741 0.4526 0.0027  -0.0297 0.0251  144 ARG A C   
1227  O O   . ARG A 144 ? 0.6039 0.4356 0.5229 0.0105  -0.0350 0.0235  144 ARG A O   
1228  C CB  . ARG A 144 ? 0.4454 0.3302 0.4010 0.0080  -0.0348 0.0196  144 ARG A CB  
1229  C CG  . ARG A 144 ? 0.4523 0.3602 0.4316 0.0089  -0.0341 0.0145  144 ARG A CG  
1230  C CD  . ARG A 144 ? 0.4450 0.3676 0.4364 0.0144  -0.0394 0.0123  144 ARG A CD  
1231  N NE  . ARG A 144 ? 0.4365 0.3799 0.4491 0.0139  -0.0370 0.0076  144 ARG A NE  
1232  C CZ  . ARG A 144 ? 0.4672 0.4165 0.4937 0.0205  -0.0399 0.0023  144 ARG A CZ  
1233  N NH1 . ARG A 144 ? 0.5590 0.4963 0.5824 0.0290  -0.0466 0.0008  144 ARG A NH1 
1234  N NH2 . ARG A 144 ? 0.3732 0.3398 0.4167 0.0185  -0.0357 -0.0018 144 ARG A NH2 
1235  N N   . LYS A 145 ? 0.5629 0.3900 0.4647 -0.0031 -0.0253 0.0295  145 LYS A N   
1236  C CA  . LYS A 145 ? 0.6077 0.4026 0.4829 -0.0021 -0.0254 0.0333  145 LYS A CA  
1237  C C   . LYS A 145 ? 0.5864 0.3708 0.4565 -0.0114 -0.0166 0.0334  145 LYS A C   
1238  O O   . LYS A 145 ? 0.6562 0.4212 0.5160 -0.0078 -0.0187 0.0336  145 LYS A O   
1239  C CB  . LYS A 145 ? 0.7160 0.4962 0.5697 -0.0044 -0.0238 0.0379  145 LYS A CB  
1240  C CG  . LYS A 145 ? 0.7833 0.5749 0.6418 0.0029  -0.0317 0.0374  145 LYS A CG  
1241  C CD  . LYS A 145 ? 0.8627 0.6564 0.7138 -0.0051 -0.0244 0.0397  145 LYS A CD  
1242  C CE  . LYS A 145 ? 0.8862 0.6843 0.7351 0.0022  -0.0327 0.0397  145 LYS A CE  
1243  N NZ  . LYS A 145 ? 0.8691 0.6829 0.7248 -0.0052 -0.0253 0.0394  145 LYS A NZ  
1244  N N   . ASP A 146 ? 0.5633 0.3603 0.4417 -0.0232 -0.0072 0.0327  146 ASP A N   
1245  C CA  . ASP A 146 ? 0.6195 0.4093 0.4963 -0.0329 0.0008  0.0315  146 ASP A CA  
1246  C C   . ASP A 146 ? 0.6548 0.4497 0.5432 -0.0294 -0.0025 0.0275  146 ASP A C   
1247  O O   . ASP A 146 ? 0.6879 0.4642 0.5661 -0.0317 -0.0001 0.0272  146 ASP A O   
1248  C CB  . ASP A 146 ? 0.7133 0.5221 0.6038 -0.0447 0.0092  0.0298  146 ASP A CB  
1249  C CG  . ASP A 146 ? 0.7890 0.5922 0.6686 -0.0495 0.0149  0.0329  146 ASP A CG  
1250  O OD1 . ASP A 146 ? 0.7981 0.5884 0.6618 -0.0426 0.0106  0.0364  146 ASP A OD1 
1251  O OD2 . ASP A 146 ? 0.7953 0.6075 0.6830 -0.0603 0.0237  0.0313  146 ASP A OD2 
1252  N N   . LEU A 147 ? 0.5399 0.3588 0.4489 -0.0245 -0.0070 0.0240  147 LEU A N   
1253  C CA  . LEU A 147 ? 0.5060 0.3307 0.4260 -0.0220 -0.0086 0.0195  147 LEU A CA  
1254  C C   . LEU A 147 ? 0.4925 0.3099 0.4121 -0.0091 -0.0164 0.0183  147 LEU A C   
1255  O O   . LEU A 147 ? 0.4425 0.2703 0.3757 -0.0053 -0.0178 0.0137  147 LEU A O   
1256  C CB  . LEU A 147 ? 0.4221 0.2752 0.3634 -0.0253 -0.0075 0.0160  147 LEU A CB  
1257  C CG  . LEU A 147 ? 0.4694 0.3354 0.4164 -0.0358 -0.0021 0.0165  147 LEU A CG  
1258  C CD1 . LEU A 147 ? 0.4383 0.3294 0.4037 -0.0366 -0.0032 0.0135  147 LEU A CD1 
1259  C CD2 . LEU A 147 ? 0.5461 0.4007 0.4864 -0.0460 0.0040  0.0158  147 LEU A CD2 
1260  N N   . LYS A 148 ? 0.5324 0.3311 0.4362 -0.0021 -0.0216 0.0219  148 LYS A N   
1261  C CA  . LYS A 148 ? 0.5460 0.3407 0.4526 0.0116  -0.0311 0.0200  148 LYS A CA  
1262  C C   . LYS A 148 ? 0.5614 0.3482 0.4716 0.0156  -0.0313 0.0160  148 LYS A C   
1263  O O   . LYS A 148 ? 0.5529 0.3507 0.4793 0.0244  -0.0361 0.0111  148 LYS A O   
1264  C CB  . LYS A 148 ? 0.6001 0.3703 0.4839 0.0180  -0.0375 0.0250  148 LYS A CB  
1265  C CG  . LYS A 148 ? 0.6793 0.4331 0.5585 0.0317  -0.0475 0.0236  148 LYS A CG  
1266  C CD  . LYS A 148 ? 0.7742 0.5108 0.6352 0.0407  -0.0577 0.0275  148 LYS A CD  
1267  C CE  . LYS A 148 ? 0.8391 0.5493 0.6872 0.0533  -0.0675 0.0275  148 LYS A CE  
1268  N NZ  . LYS A 148 ? 0.8301 0.5561 0.7047 0.0633  -0.0731 0.0200  148 LYS A NZ  
1269  N N   . ASP A 149 ? 0.5287 0.2970 0.4252 0.0087  -0.0255 0.0172  149 ASP A N   
1270  C CA  . ASP A 149 ? 0.6152 0.3737 0.5133 0.0122  -0.0252 0.0131  149 ASP A CA  
1271  C C   . ASP A 149 ? 0.5521 0.3346 0.4718 0.0089  -0.0211 0.0070  149 ASP A C   
1272  O O   . ASP A 149 ? 0.5268 0.3106 0.4559 0.0159  -0.0227 0.0019  149 ASP A O   
1273  C CB  . ASP A 149 ? 0.6732 0.4046 0.5502 0.0046  -0.0194 0.0157  149 ASP A CB  
1274  C CG  . ASP A 149 ? 0.8392 0.5413 0.6899 0.0073  -0.0222 0.0222  149 ASP A CG  
1275  O OD1 . ASP A 149 ? 0.9849 0.6801 0.8314 0.0197  -0.0319 0.0236  149 ASP A OD1 
1276  O OD2 . ASP A 149 ? 0.8470 0.5320 0.6807 -0.0032 -0.0147 0.0255  149 ASP A OD2 
1277  N N   . LEU A 150 ? 0.4532 0.2537 0.3800 -0.0015 -0.0157 0.0071  150 LEU A N   
1278  C CA  . LEU A 150 ? 0.4687 0.2890 0.4119 -0.0047 -0.0123 0.0018  150 LEU A CA  
1279  C C   . LEU A 150 ? 0.4970 0.3369 0.4580 0.0036  -0.0161 -0.0014 150 LEU A C   
1280  O O   . LEU A 150 ? 0.4645 0.3126 0.4367 0.0059  -0.0141 -0.0069 150 LEU A O   
1281  C CB  . LEU A 150 ? 0.4629 0.2960 0.4084 -0.0171 -0.0073 0.0027  150 LEU A CB  
1282  C CG  . LEU A 150 ? 0.5036 0.3223 0.4371 -0.0275 -0.0023 0.0035  150 LEU A CG  
1283  C CD1 . LEU A 150 ? 0.5028 0.3391 0.4446 -0.0384 0.0010  0.0027  150 LEU A CD1 
1284  C CD2 . LEU A 150 ? 0.5071 0.3107 0.4354 -0.0267 -0.0007 -0.0005 150 LEU A CD2 
1285  N N   . LEU A 151 ? 0.5180 0.3651 0.4815 0.0076  -0.0207 0.0016  151 LEU A N   
1286  C CA  . LEU A 151 ? 0.5168 0.3821 0.4981 0.0152  -0.0245 -0.0018 151 LEU A CA  
1287  C C   . LEU A 151 ? 0.5774 0.4361 0.5654 0.0267  -0.0289 -0.0065 151 LEU A C   
1288  O O   . LEU A 151 ? 0.5659 0.4390 0.5716 0.0301  -0.0273 -0.0126 151 LEU A O   
1289  C CB  . LEU A 151 ? 0.4851 0.3557 0.4651 0.0173  -0.0294 0.0023  151 LEU A CB  
1290  C CG  . LEU A 151 ? 0.5144 0.4009 0.4977 0.0085  -0.0255 0.0047  151 LEU A CG  
1291  C CD1 . LEU A 151 ? 0.5877 0.4711 0.5632 0.0106  -0.0300 0.0092  151 LEU A CD1 
1292  C CD2 . LEU A 151 ? 0.4079 0.3173 0.4104 0.0082  -0.0234 0.0004  151 LEU A CD2 
1293  N N   . ASN A 152 ? 0.6382 0.4745 0.6122 0.0332  -0.0345 -0.0040 152 ASN A N   
1294  C CA  . ASN A 152 ? 0.6458 0.4746 0.6268 0.0456  -0.0402 -0.0088 152 ASN A CA  
1295  C C   . ASN A 152 ? 0.5586 0.3848 0.5449 0.0444  -0.0336 -0.0144 152 ASN A C   
1296  O O   . ASN A 152 ? 0.5474 0.3766 0.5483 0.0536  -0.0356 -0.0209 152 ASN A O   
1297  C CB  . ASN A 152 ? 0.6962 0.4972 0.6567 0.0526  -0.0481 -0.0042 152 ASN A CB  
1298  C CG  . ASN A 152 ? 0.8103 0.6115 0.7650 0.0569  -0.0565 0.0001  152 ASN A CG  
1299  O OD1 . ASN A 152 ? 0.8554 0.6324 0.7867 0.0589  -0.0611 0.0058  152 ASN A OD1 
1300  N ND2 . ASN A 152 ? 0.8115 0.6380 0.7855 0.0578  -0.0580 -0.0027 152 ASN A ND2 
1301  N N   . LYS A 153 ? 0.4999 0.3196 0.4747 0.0333  -0.0260 -0.0127 153 LYS A N   
1302  C CA  . LYS A 153 ? 0.4987 0.3165 0.4768 0.0306  -0.0192 -0.0183 153 LYS A CA  
1303  C C   . LYS A 153 ? 0.5272 0.3674 0.5274 0.0329  -0.0157 -0.0254 153 LYS A C   
1304  O O   . LYS A 153 ? 0.5677 0.4062 0.5776 0.0395  -0.0140 -0.0321 153 LYS A O   
1305  C CB  . LYS A 153 ? 0.5467 0.3604 0.5119 0.0167  -0.0126 -0.0156 153 LYS A CB  
1306  C CG  . LYS A 153 ? 0.6083 0.4177 0.5728 0.0125  -0.0062 -0.0210 153 LYS A CG  
1307  C CD  . LYS A 153 ? 0.6000 0.4057 0.5525 -0.0010 -0.0017 -0.0187 153 LYS A CD  
1308  C CE  . LYS A 153 ? 0.5735 0.3673 0.5203 -0.0043 0.0033  -0.0240 153 LYS A CE  
1309  N NZ  . LYS A 153 ? 0.6833 0.4689 0.6175 -0.0168 0.0061  -0.0223 153 LYS A NZ  
1310  N N   . GLY A 154 ? 0.5197 0.3801 0.5278 0.0273  -0.0138 -0.0242 154 GLY A N   
1311  C CA  . GLY A 154 ? 0.4839 0.3649 0.5113 0.0286  -0.0099 -0.0301 154 GLY A CA  
1312  C C   . GLY A 154 ? 0.4994 0.3819 0.5278 0.0232  -0.0005 -0.0357 154 GLY A C   
1313  O O   . GLY A 154 ? 0.4169 0.3148 0.4584 0.0225  0.0045  -0.0402 154 GLY A O   
1314  N N   . ARG A 155 ? 0.5034 0.3692 0.5173 0.0188  0.0024  -0.0358 155 ARG A N   
1315  C CA  . ARG A 155 ? 0.4792 0.3430 0.4913 0.0143  0.0109  -0.0418 155 ARG A CA  
1316  C C   . ARG A 155 ? 0.4543 0.2995 0.4470 0.0072  0.0120  -0.0398 155 ARG A C   
1317  O O   . ARG A 155 ? 0.4863 0.3190 0.4689 0.0070  0.0072  -0.0347 155 ARG A O   
1318  C CB  . ARG A 155 ? 0.5063 0.3693 0.5322 0.0236  0.0142  -0.0501 155 ARG A CB  
1319  C CG  . ARG A 155 ? 0.5550 0.4024 0.5805 0.0339  0.0072  -0.0498 155 ARG A CG  
1320  C CD  . ARG A 155 ? 0.6249 0.4718 0.6665 0.0440  0.0100  -0.0590 155 ARG A CD  
1321  N NE  . ARG A 155 ? 0.6443 0.5129 0.7104 0.0497  0.0102  -0.0637 155 ARG A NE  
1322  C CZ  . ARG A 155 ? 0.6851 0.5663 0.7645 0.0475  0.0202  -0.0714 155 ARG A CZ  
1323  N NH1 . ARG A 155 ? 0.7001 0.6008 0.8030 0.0520  0.0207  -0.0760 155 ARG A NH1 
1324  N NH2 . ARG A 155 ? 0.6690 0.5423 0.7372 0.0402  0.0302  -0.0746 155 ARG A NH2 
1325  N N   . ASN A 156 ? 0.4521 0.2945 0.4386 0.0008  0.0187  -0.0443 156 ASN A N   
1326  C CA  . ASN A 156 ? 0.5357 0.3599 0.5054 -0.0057 0.0203  -0.0449 156 ASN A CA  
1327  C C   . ASN A 156 ? 0.5455 0.3678 0.5047 -0.0144 0.0161  -0.0381 156 ASN A C   
1328  O O   . ASN A 156 ? 0.5372 0.3430 0.4857 -0.0167 0.0146  -0.0359 156 ASN A O   
1329  C CB  . ASN A 156 ? 0.6017 0.4065 0.5689 0.0020  0.0199  -0.0476 156 ASN A CB  
1330  C CG  . ASN A 156 ? 0.6626 0.4705 0.6437 0.0113  0.0243  -0.0555 156 ASN A CG  
1331  O OD1 . ASN A 156 ? 0.7014 0.5091 0.6942 0.0224  0.0204  -0.0564 156 ASN A OD1 
1332  N ND2 . ASN A 156 ? 0.6643 0.4742 0.6441 0.0069  0.0325  -0.0617 156 ASN A ND2 
1333  N N   . TYR A 157 ? 0.3989 0.2380 0.3619 -0.0194 0.0149  -0.0351 157 TYR A N   
1334  C CA  . TYR A 157 ? 0.4058 0.2465 0.3625 -0.0279 0.0117  -0.0298 157 TYR A CA  
1335  C C   . TYR A 157 ? 0.4192 0.2533 0.3650 -0.0379 0.0134  -0.0326 157 TYR A C   
1336  O O   . TYR A 157 ? 0.3816 0.2148 0.3239 -0.0393 0.0167  -0.0378 157 TYR A O   
1337  C CB  . TYR A 157 ? 0.3996 0.2605 0.3652 -0.0289 0.0094  -0.0261 157 TYR A CB  
1338  C CG  . TYR A 157 ? 0.3779 0.2441 0.3528 -0.0202 0.0063  -0.0231 157 TYR A CG  
1339  C CD1 . TYR A 157 ? 0.3576 0.2165 0.3279 -0.0196 0.0027  -0.0178 157 TYR A CD1 
1340  C CD2 . TYR A 157 ? 0.3269 0.2040 0.3142 -0.0129 0.0073  -0.0259 157 TYR A CD2 
1341  C CE1 . TYR A 157 ? 0.3819 0.2432 0.3578 -0.0113 -0.0013 -0.0151 157 TYR A CE1 
1342  C CE2 . TYR A 157 ? 0.3073 0.1894 0.3037 -0.0048 0.0031  -0.0238 157 TYR A CE2 
1343  C CZ  . TYR A 157 ? 0.3548 0.2285 0.3445 -0.0038 -0.0019 -0.0183 157 TYR A CZ  
1344  O OH  . TYR A 157 ? 0.4009 0.2775 0.3969 0.0045  -0.0072 -0.0163 157 TYR A OH  
1345  N N   . THR A 158 ? 0.4104 0.2394 0.3505 -0.0453 0.0112  -0.0297 158 THR A N   
1346  C CA  . THR A 158 ? 0.4037 0.2290 0.3360 -0.0555 0.0112  -0.0327 158 THR A CA  
1347  C C   . THR A 158 ? 0.3929 0.2355 0.3309 -0.0619 0.0074  -0.0301 158 THR A C   
1348  O O   . THR A 158 ? 0.4094 0.2635 0.3557 -0.0596 0.0057  -0.0253 158 THR A O   
1349  C CB  . THR A 158 ? 0.3965 0.2025 0.3196 -0.0603 0.0122  -0.0332 158 THR A CB  
1350  O OG1 . THR A 158 ? 0.4353 0.2412 0.3604 -0.0622 0.0111  -0.0275 158 THR A OG1 
1351  C CG2 . THR A 158 ? 0.4395 0.2278 0.3573 -0.0525 0.0153  -0.0357 158 THR A CG2 
1352  N N   . GLN A 159 ? 0.3904 0.2341 0.3237 -0.0696 0.0056  -0.0338 159 GLN A N   
1353  C CA  . GLN A 159 ? 0.3805 0.2398 0.3199 -0.0755 0.0007  -0.0323 159 GLN A CA  
1354  C C   . GLN A 159 ? 0.3902 0.2527 0.3369 -0.0797 0.0001  -0.0286 159 GLN A C   
1355  O O   . GLN A 159 ? 0.4228 0.3007 0.3792 -0.0802 -0.0023 -0.0254 159 GLN A O   
1356  C CB  . GLN A 159 ? 0.3915 0.2480 0.3231 -0.0829 -0.0027 -0.0377 159 GLN A CB  
1357  C CG  . GLN A 159 ? 0.4591 0.3308 0.3978 -0.0887 -0.0095 -0.0375 159 GLN A CG  
1358  C CD  . GLN A 159 ? 0.4535 0.3386 0.3948 -0.0840 -0.0121 -0.0351 159 GLN A CD  
1359  O OE1 . GLN A 159 ? 0.5029 0.3846 0.4379 -0.0783 -0.0086 -0.0353 159 GLN A OE1 
1360  N NE2 . GLN A 159 ? 0.4881 0.3881 0.4392 -0.0865 -0.0178 -0.0333 159 GLN A NE2 
1361  N N   . GLU A 160 ? 0.3604 0.2070 0.3016 -0.0832 0.0031  -0.0292 160 GLU A N   
1362  C CA  . GLU A 160 ? 0.5031 0.3498 0.4489 -0.0885 0.0044  -0.0262 160 GLU A CA  
1363  C C   . GLU A 160 ? 0.4846 0.3342 0.4334 -0.0811 0.0059  -0.0199 160 GLU A C   
1364  O O   . GLU A 160 ? 0.5034 0.3600 0.4583 -0.0846 0.0066  -0.0168 160 GLU A O   
1365  C CB  . GLU A 160 ? 0.5799 0.4055 0.5164 -0.0945 0.0083  -0.0283 160 GLU A CB  
1366  C CG  . GLU A 160 ? 0.6925 0.5172 0.6333 -0.1032 0.0113  -0.0266 160 GLU A CG  
1367  C CD  . GLU A 160 ? 0.8567 0.6698 0.7911 -0.0980 0.0154  -0.0204 160 GLU A CD  
1368  O OE1 . GLU A 160 ? 0.9149 0.7326 0.8539 -0.1022 0.0181  -0.0173 160 GLU A OE1 
1369  O OE2 . GLU A 160 ? 0.9261 0.7249 0.8507 -0.0893 0.0158  -0.0189 160 GLU A OE2 
1370  N N   . GLU A 161 ? 0.4122 0.2565 0.3575 -0.0710 0.0063  -0.0186 161 GLU A N   
1371  C CA  . GLU A 161 ? 0.3865 0.2347 0.3351 -0.0634 0.0060  -0.0134 161 GLU A CA  
1372  C C   . GLU A 161 ? 0.3892 0.2599 0.3493 -0.0617 0.0032  -0.0119 161 GLU A C   
1373  O O   . GLU A 161 ? 0.3373 0.2156 0.3021 -0.0609 0.0028  -0.0078 161 GLU A O   
1374  C CB  . GLU A 161 ? 0.3934 0.2305 0.3377 -0.0527 0.0061  -0.0136 161 GLU A CB  
1375  C CG  . GLU A 161 ? 0.3993 0.2117 0.3312 -0.0525 0.0082  -0.0136 161 GLU A CG  
1376  C CD  . GLU A 161 ? 0.5552 0.3570 0.4848 -0.0419 0.0078  -0.0159 161 GLU A CD  
1377  O OE1 . GLU A 161 ? 0.5270 0.3419 0.4660 -0.0359 0.0070  -0.0185 161 GLU A OE1 
1378  O OE2 . GLU A 161 ? 0.5884 0.3682 0.5072 -0.0396 0.0087  -0.0155 161 GLU A OE2 
1379  N N   . LYS A 162 ? 0.3649 0.2445 0.3277 -0.0612 0.0017  -0.0153 162 LYS A N   
1380  C CA  . LYS A 162 ? 0.3511 0.2496 0.3228 -0.0602 -0.0008 -0.0140 162 LYS A CA  
1381  C C   . LYS A 162 ? 0.3542 0.2629 0.3323 -0.0675 -0.0028 -0.0126 162 LYS A C   
1382  O O   . LYS A 162 ? 0.3530 0.2745 0.3392 -0.0658 -0.0039 -0.0095 162 LYS A O   
1383  C CB  . LYS A 162 ? 0.2957 0.1972 0.2647 -0.0600 -0.0015 -0.0181 162 LYS A CB  
1384  C CG  . LYS A 162 ? 0.3536 0.2714 0.3286 -0.0597 -0.0043 -0.0168 162 LYS A CG  
1385  C CD  . LYS A 162 ? 0.3290 0.2448 0.2965 -0.0594 -0.0038 -0.0206 162 LYS A CD  
1386  C CE  . LYS A 162 ? 0.3633 0.2716 0.3215 -0.0666 -0.0066 -0.0246 162 LYS A CE  
1387  N NZ  . LYS A 162 ? 0.3776 0.2822 0.3245 -0.0668 -0.0067 -0.0280 162 LYS A NZ  
1388  N N   . GLU A 163 ? 0.3546 0.2581 0.3306 -0.0758 -0.0030 -0.0157 163 GLU A N   
1389  C CA  . GLU A 163 ? 0.3984 0.3133 0.3841 -0.0831 -0.0047 -0.0159 163 GLU A CA  
1390  C C   . GLU A 163 ? 0.3773 0.2897 0.3655 -0.0844 -0.0003 -0.0120 163 GLU A C   
1391  O O   . GLU A 163 ? 0.3561 0.2817 0.3546 -0.0866 -0.0006 -0.0107 163 GLU A O   
1392  C CB  . GLU A 163 ? 0.4085 0.3192 0.3930 -0.0921 -0.0065 -0.0214 163 GLU A CB  
1393  C CG  . GLU A 163 ? 0.3851 0.2990 0.3655 -0.0914 -0.0121 -0.0252 163 GLU A CG  
1394  C CD  . GLU A 163 ? 0.5598 0.4670 0.5366 -0.0996 -0.0149 -0.0313 163 GLU A CD  
1395  O OE1 . GLU A 163 ? 0.5754 0.4868 0.5494 -0.1006 -0.0212 -0.0347 163 GLU A OE1 
1396  O OE2 . GLU A 163 ? 0.5531 0.4493 0.5285 -0.1053 -0.0110 -0.0329 163 GLU A OE2 
1397  N N   . TYR A 164 ? 0.3914 0.2854 0.3689 -0.0827 0.0038  -0.0103 164 TYR A N   
1398  C CA  . TYR A 164 ? 0.4374 0.3247 0.4119 -0.0829 0.0081  -0.0060 164 TYR A CA  
1399  C C   . TYR A 164 ? 0.4165 0.3159 0.3962 -0.0756 0.0063  -0.0019 164 TYR A C   
1400  O O   . TYR A 164 ? 0.4096 0.3165 0.3948 -0.0784 0.0083  0.0001  164 TYR A O   
1401  C CB  . TYR A 164 ? 0.3946 0.2572 0.3535 -0.0801 0.0110  -0.0044 164 TYR A CB  
1402  C CG  . TYR A 164 ? 0.3890 0.2405 0.3401 -0.0803 0.0152  0.0004  164 TYR A CG  
1403  C CD1 . TYR A 164 ? 0.4554 0.3023 0.4061 -0.0908 0.0212  0.0000  164 TYR A CD1 
1404  C CD2 . TYR A 164 ? 0.4095 0.2555 0.3538 -0.0704 0.0132  0.0049  164 TYR A CD2 
1405  C CE1 . TYR A 164 ? 0.5277 0.3623 0.4684 -0.0918 0.0263  0.0045  164 TYR A CE1 
1406  C CE2 . TYR A 164 ? 0.3849 0.2186 0.3187 -0.0706 0.0165  0.0094  164 TYR A CE2 
1407  C CZ  . TYR A 164 ? 0.4854 0.3124 0.4159 -0.0815 0.0236  0.0094  164 TYR A CZ  
1408  O OH  . TYR A 164 ? 0.5451 0.3572 0.4620 -0.0824 0.0282  0.0140  164 TYR A OH  
1409  N N   . VAL A 165 ? 0.4237 0.3256 0.4027 -0.0667 0.0031  -0.0014 165 VAL A N   
1410  C CA  . VAL A 165 ? 0.3708 0.2846 0.3556 -0.0599 0.0010  0.0015  165 VAL A CA  
1411  C C   . VAL A 165 ? 0.4105 0.3440 0.4076 -0.0637 -0.0005 0.0011  165 VAL A C   
1412  O O   . VAL A 165 ? 0.3182 0.2593 0.3199 -0.0627 0.0002  0.0039  165 VAL A O   
1413  C CB  . VAL A 165 ? 0.2767 0.1914 0.2617 -0.0512 -0.0014 0.0003  165 VAL A CB  
1414  C CG1 . VAL A 165 ? 0.2549 0.1837 0.2479 -0.0453 -0.0035 0.0024  165 VAL A CG1 
1415  C CG2 . VAL A 165 ? 0.3120 0.2076 0.2869 -0.0457 -0.0008 0.0006  165 VAL A CG2 
1416  N N   . LEU A 166 ? 0.3606 0.3016 0.3623 -0.0676 -0.0030 -0.0025 166 LEU A N   
1417  C CA  . LEU A 166 ? 0.2706 0.2292 0.2837 -0.0699 -0.0060 -0.0032 166 LEU A CA  
1418  C C   . LEU A 166 ? 0.2800 0.2438 0.3011 -0.0763 -0.0034 -0.0029 166 LEU A C   
1419  O O   . LEU A 166 ? 0.2857 0.2626 0.3163 -0.0755 -0.0040 -0.0016 166 LEU A O   
1420  C CB  . LEU A 166 ? 0.2756 0.2375 0.2890 -0.0731 -0.0105 -0.0074 166 LEU A CB  
1421  C CG  . LEU A 166 ? 0.3507 0.3141 0.3594 -0.0672 -0.0129 -0.0076 166 LEU A CG  
1422  C CD1 . LEU A 166 ? 0.4346 0.3945 0.4373 -0.0709 -0.0166 -0.0120 166 LEU A CD1 
1423  C CD2 . LEU A 166 ? 0.3367 0.3143 0.3533 -0.0634 -0.0150 -0.0050 166 LEU A CD2 
1424  N N   . ASN A 167 ? 0.2690 0.2222 0.2868 -0.0832 0.0003  -0.0047 167 ASN A N   
1425  C CA  . ASN A 167 ? 0.3836 0.3405 0.4094 -0.0907 0.0049  -0.0054 167 ASN A CA  
1426  C C   . ASN A 167 ? 0.3754 0.3299 0.3979 -0.0874 0.0096  -0.0007 167 ASN A C   
1427  O O   . ASN A 167 ? 0.3487 0.3151 0.3819 -0.0898 0.0117  -0.0008 167 ASN A O   
1428  C CB  . ASN A 167 ? 0.4500 0.3922 0.4703 -0.0990 0.0094  -0.0082 167 ASN A CB  
1429  C CG  . ASN A 167 ? 0.6917 0.6350 0.7192 -0.1077 0.0168  -0.0093 167 ASN A CG  
1430  O OD1 . ASN A 167 ? 0.7801 0.7412 0.8253 -0.1118 0.0160  -0.0126 167 ASN A OD1 
1431  N ND2 . ASN A 167 ? 0.7580 0.6811 0.7716 -0.1105 0.0244  -0.0068 167 ASN A ND2 
1432  N N   . LYS A 168 ? 0.3443 0.2828 0.3516 -0.0816 0.0108  0.0030  168 LYS A N   
1433  C CA  . LYS A 168 ? 0.3471 0.2804 0.3476 -0.0778 0.0138  0.0075  168 LYS A CA  
1434  C C   . LYS A 168 ? 0.3450 0.2958 0.3552 -0.0721 0.0101  0.0087  168 LYS A C   
1435  O O   . LYS A 168 ? 0.3047 0.2598 0.3173 -0.0728 0.0133  0.0103  168 LYS A O   
1436  C CB  . LYS A 168 ? 0.3298 0.2428 0.3127 -0.0711 0.0130  0.0106  168 LYS A CB  
1437  C CG  . LYS A 168 ? 0.3625 0.2545 0.3333 -0.0762 0.0169  0.0099  168 LYS A CG  
1438  C CD  . LYS A 168 ? 0.4692 0.3521 0.4350 -0.0851 0.0253  0.0108  168 LYS A CD  
1439  C CE  . LYS A 168 ? 0.5869 0.4539 0.5357 -0.0803 0.0273  0.0161  168 LYS A CE  
1440  N NZ  . LYS A 168 ? 0.6832 0.5383 0.6239 -0.0898 0.0375  0.0169  168 LYS A NZ  
1441  N N   . TYR A 169 ? 0.3006 0.2604 0.3156 -0.0669 0.0043  0.0076  169 TYR A N   
1442  C CA  . TYR A 169 ? 0.2359 0.2113 0.2598 -0.0621 0.0010  0.0084  169 TYR A CA  
1443  C C   . TYR A 169 ? 0.3165 0.3068 0.3541 -0.0671 0.0018  0.0068  169 TYR A C   
1444  O O   . TYR A 169 ? 0.2759 0.2744 0.3184 -0.0646 0.0025  0.0084  169 TYR A O   
1445  C CB  . TYR A 169 ? 0.2245 0.2049 0.2502 -0.0577 -0.0039 0.0068  169 TYR A CB  
1446  C CG  . TYR A 169 ? 0.2902 0.2626 0.3085 -0.0501 -0.0049 0.0080  169 TYR A CG  
1447  C CD1 . TYR A 169 ? 0.3095 0.2673 0.3179 -0.0475 -0.0033 0.0100  169 TYR A CD1 
1448  C CD2 . TYR A 169 ? 0.3064 0.2849 0.3277 -0.0455 -0.0073 0.0067  169 TYR A CD2 
1449  C CE1 . TYR A 169 ? 0.2572 0.2090 0.2618 -0.0396 -0.0055 0.0102  169 TYR A CE1 
1450  C CE2 . TYR A 169 ? 0.3127 0.2860 0.3312 -0.0388 -0.0077 0.0065  169 TYR A CE2 
1451  C CZ  . TYR A 169 ? 0.3046 0.2658 0.3163 -0.0355 -0.0075 0.0080  169 TYR A CZ  
1452  O OH  . TYR A 169 ? 0.3178 0.2754 0.3297 -0.0280 -0.0092 0.0068  169 TYR A OH  
1453  N N   . PHE A 170 ? 0.3476 0.3425 0.3927 -0.0737 0.0012  0.0030  170 PHE A N   
1454  C CA  . PHE A 170 ? 0.3018 0.3125 0.3632 -0.0776 0.0010  0.0005  170 PHE A CA  
1455  C C   . PHE A 170 ? 0.2764 0.2854 0.3406 -0.0826 0.0092  0.0007  170 PHE A C   
1456  O O   . PHE A 170 ? 0.3388 0.3608 0.4158 -0.0833 0.0105  -0.0005 170 PHE A O   
1457  C CB  . PHE A 170 ? 0.3041 0.3210 0.3744 -0.0829 -0.0036 -0.0046 170 PHE A CB  
1458  C CG  . PHE A 170 ? 0.3254 0.3490 0.3960 -0.0779 -0.0122 -0.0051 170 PHE A CG  
1459  C CD1 . PHE A 170 ? 0.3370 0.3739 0.4168 -0.0738 -0.0162 -0.0045 170 PHE A CD1 
1460  C CD2 . PHE A 170 ? 0.3950 0.4094 0.4549 -0.0773 -0.0156 -0.0062 170 PHE A CD2 
1461  C CE1 . PHE A 170 ? 0.3844 0.4238 0.4609 -0.0694 -0.0235 -0.0045 170 PHE A CE1 
1462  C CE2 . PHE A 170 ? 0.4194 0.4370 0.4761 -0.0732 -0.0223 -0.0066 170 PHE A CE2 
1463  C CZ  . PHE A 170 ? 0.4350 0.4643 0.4991 -0.0694 -0.0263 -0.0055 170 PHE A CZ  
1464  N N   . GLU A 171 ? 0.3306 0.3222 0.3817 -0.0860 0.0153  0.0021  171 GLU A N   
1465  C CA  . GLU A 171 ? 0.3860 0.3714 0.4343 -0.0906 0.0246  0.0030  171 GLU A CA  
1466  C C   . GLU A 171 ? 0.3549 0.3410 0.3977 -0.0839 0.0250  0.0070  171 GLU A C   
1467  O O   . GLU A 171 ? 0.3801 0.3706 0.4279 -0.0867 0.0311  0.0065  171 GLU A O   
1468  C CB  . GLU A 171 ? 0.3745 0.3365 0.4050 -0.0949 0.0305  0.0045  171 GLU A CB  
1469  C CG  . GLU A 171 ? 0.5033 0.4633 0.5402 -0.1047 0.0336  -0.0003 171 GLU A CG  
1470  C CD  . GLU A 171 ? 0.6804 0.6138 0.6967 -0.1082 0.0393  0.0017  171 GLU A CD  
1471  O OE1 . GLU A 171 ? 0.7265 0.6430 0.7237 -0.1033 0.0413  0.0069  171 GLU A OE1 
1472  O OE2 . GLU A 171 ? 0.7345 0.6630 0.7531 -0.1156 0.0411  -0.0021 171 GLU A OE2 
1473  N N   . ILE A 172 ? 0.3360 0.3183 0.3697 -0.0752 0.0189  0.0102  172 ILE A N   
1474  C CA  . ILE A 172 ? 0.3195 0.3035 0.3491 -0.0685 0.0178  0.0132  172 ILE A CA  
1475  C C   . ILE A 172 ? 0.3307 0.3351 0.3778 -0.0677 0.0162  0.0114  172 ILE A C   
1476  O O   . ILE A 172 ? 0.2440 0.2512 0.2918 -0.0668 0.0195  0.0122  172 ILE A O   
1477  C CB  . ILE A 172 ? 0.3362 0.3144 0.3569 -0.0599 0.0111  0.0155  172 ILE A CB  
1478  C CG1 . ILE A 172 ? 0.3530 0.3092 0.3555 -0.0590 0.0122  0.0176  172 ILE A CG1 
1479  C CG2 . ILE A 172 ? 0.3117 0.2957 0.3327 -0.0533 0.0085  0.0174  172 ILE A CG2 
1480  C CD1 . ILE A 172 ? 0.3222 0.2633 0.3088 -0.0582 0.0159  0.0209  172 ILE A CD1 
1481  N N   . ILE A 173 ? 0.2557 0.2729 0.3152 -0.0673 0.0104  0.0089  173 ILE A N   
1482  C CA  . ILE A 173 ? 0.2642 0.2988 0.3392 -0.0657 0.0077  0.0072  173 ILE A CA  
1483  C C   . ILE A 173 ? 0.2409 0.2834 0.3291 -0.0721 0.0137  0.0039  173 ILE A C   
1484  O O   . ILE A 173 ? 0.3021 0.3536 0.3986 -0.0705 0.0156  0.0035  173 ILE A O   
1485  C CB  . ILE A 173 ? 0.3022 0.3446 0.3836 -0.0641 -0.0004 0.0054  173 ILE A CB  
1486  C CG1 . ILE A 173 ? 0.2759 0.3102 0.3449 -0.0583 -0.0041 0.0079  173 ILE A CG1 
1487  C CG2 . ILE A 173 ? 0.2744 0.3327 0.3705 -0.0619 -0.0041 0.0038  173 ILE A CG2 
1488  C CD1 . ILE A 173 ? 0.3350 0.3713 0.4042 -0.0577 -0.0102 0.0061  173 ILE A CD1 
1489  N N   . LYS A 174 ? 0.2318 0.2712 0.3233 -0.0797 0.0173  0.0009  174 LYS A N   
1490  C CA  . LYS A 174 ? 0.2966 0.3438 0.4028 -0.0869 0.0247  -0.0034 174 LYS A CA  
1491  C C   . LYS A 174 ? 0.3339 0.3728 0.4314 -0.0881 0.0348  -0.0014 174 LYS A C   
1492  O O   . LYS A 174 ? 0.3438 0.3920 0.4553 -0.0922 0.0415  -0.0050 174 LYS A O   
1493  C CB  . LYS A 174 ? 0.3464 0.3888 0.4556 -0.0959 0.0282  -0.0072 174 LYS A CB  
1494  C CG  . LYS A 174 ? 0.3855 0.4389 0.5077 -0.0966 0.0187  -0.0113 174 LYS A CG  
1495  C CD  . LYS A 174 ? 0.4587 0.5084 0.5863 -0.1068 0.0231  -0.0163 174 LYS A CD  
1496  C CE  . LYS A 174 ? 0.5425 0.6012 0.6805 -0.1075 0.0124  -0.0207 174 LYS A CE  
1497  N NZ  . LYS A 174 ? 0.5825 0.6354 0.7234 -0.1175 0.0159  -0.0257 174 LYS A NZ  
1498  N N   . LYS A 175 ? 0.3373 0.3589 0.4122 -0.0843 0.0358  0.0039  175 LYS A N   
1499  C CA  . LYS A 175 ? 0.3706 0.3799 0.4313 -0.0849 0.0441  0.0063  175 LYS A CA  
1500  C C   . LYS A 175 ? 0.3366 0.3528 0.3977 -0.0775 0.0410  0.0081  175 LYS A C   
1501  O O   . LYS A 175 ? 0.3398 0.3468 0.3891 -0.0775 0.0471  0.0096  175 LYS A O   
1502  C CB  . LYS A 175 ? 0.3892 0.3736 0.4231 -0.0837 0.0448  0.0109  175 LYS A CB  
1503  C CG  . LYS A 175 ? 0.4807 0.4500 0.5065 -0.0918 0.0512  0.0101  175 LYS A CG  
1504  C CD  . LYS A 175 ? 0.6427 0.5838 0.6382 -0.0897 0.0531  0.0153  175 LYS A CD  
1505  C CE  . LYS A 175 ? 0.7183 0.6503 0.7044 -0.0836 0.0439  0.0177  175 LYS A CE  
1506  N NZ  . LYS A 175 ? 0.7670 0.6808 0.7303 -0.0752 0.0392  0.0227  175 LYS A NZ  
1507  N N   . THR A 176 ? 0.2312 0.2611 0.3030 -0.0713 0.0316  0.0080  176 THR A N   
1508  C CA  . THR A 176 ? 0.2108 0.2422 0.2776 -0.0636 0.0273  0.0106  176 THR A CA  
1509  C C   . THR A 176 ? 0.3115 0.3526 0.3882 -0.0635 0.0319  0.0087  176 THR A C   
1510  O O   . THR A 176 ? 0.3674 0.4014 0.4326 -0.0607 0.0341  0.0105  176 THR A O   
1511  C CB  . THR A 176 ? 0.2146 0.2544 0.2871 -0.0579 0.0173  0.0112  176 THR A CB  
1512  O OG1 . THR A 176 ? 0.2787 0.3068 0.3393 -0.0573 0.0144  0.0129  176 THR A OG1 
1513  C CG2 . THR A 176 ? 0.2300 0.2733 0.3010 -0.0511 0.0136  0.0129  176 THR A CG2 
1514  N N   . LEU A 177 ? 0.2433 0.3004 0.3414 -0.0662 0.0328  0.0044  177 LEU A N   
1515  C CA  . LEU A 177 ? 0.2321 0.2982 0.3407 -0.0657 0.0377  0.0019  177 LEU A CA  
1516  C C   . LEU A 177 ? 0.2474 0.3031 0.3477 -0.0720 0.0506  0.0008  177 LEU A C   
1517  O O   . LEU A 177 ? 0.2603 0.3149 0.3578 -0.0708 0.0560  0.0003  177 LEU A O   
1518  C CB  . LEU A 177 ? 0.2760 0.3618 0.4112 -0.0661 0.0347  -0.0030 177 LEU A CB  
1519  C CG  . LEU A 177 ? 0.2561 0.3503 0.3972 -0.0595 0.0222  -0.0018 177 LEU A CG  
1520  C CD1 . LEU A 177 ? 0.2951 0.4065 0.4608 -0.0599 0.0181  -0.0070 177 LEU A CD1 
1521  C CD2 . LEU A 177 ? 0.2292 0.3222 0.3634 -0.0525 0.0194  0.0011  177 LEU A CD2 
1522  N N   . SER A 178 ? 0.2523 0.2979 0.3463 -0.0791 0.0563  0.0003  178 SER A N   
1523  C CA  . SER A 178 ? 0.2537 0.2863 0.3372 -0.0864 0.0702  -0.0008 178 SER A CA  
1524  C C   . SER A 178 ? 0.2428 0.2538 0.2961 -0.0831 0.0716  0.0045  178 SER A C   
1525  O O   . SER A 178 ? 0.2727 0.2728 0.3146 -0.0869 0.0823  0.0038  178 SER A O   
1526  C CB  . SER A 178 ? 0.3875 0.4124 0.4701 -0.0953 0.0760  -0.0025 178 SER A CB  
1527  O OG  . SER A 178 ? 0.4543 0.4984 0.5662 -0.1009 0.0791  -0.0094 178 SER A OG  
1528  N N   . ILE A 179 ? 0.3075 0.3113 0.3472 -0.0761 0.0609  0.0091  179 ILE A N   
1529  C CA  . ILE A 179 ? 0.3862 0.3695 0.3981 -0.0725 0.0606  0.0134  179 ILE A CA  
1530  C C   . ILE A 179 ? 0.3266 0.3167 0.3401 -0.0667 0.0582  0.0131  179 ILE A C   
1531  O O   . ILE A 179 ? 0.3622 0.3372 0.3556 -0.0662 0.0621  0.0145  179 ILE A O   
1532  C CB  . ILE A 179 ? 0.3553 0.3270 0.3526 -0.0672 0.0505  0.0176  179 ILE A CB  
1533  C CG1 . ILE A 179 ? 0.4408 0.3883 0.4080 -0.0641 0.0502  0.0215  179 ILE A CG1 
1534  C CG2 . ILE A 179 ? 0.3022 0.2899 0.3132 -0.0596 0.0389  0.0177  179 ILE A CG2 
1535  C CD1 . ILE A 179 ? 0.4884 0.4213 0.4402 -0.0591 0.0415  0.0250  179 ILE A CD1 
1536  N N   . TYR A 180 ? 0.2527 0.2636 0.2879 -0.0625 0.0518  0.0112  180 TYR A N   
1537  C CA  . TYR A 180 ? 0.2447 0.2622 0.2834 -0.0582 0.0513  0.0102  180 TYR A CA  
1538  C C   . TYR A 180 ? 0.2932 0.3104 0.3345 -0.0636 0.0641  0.0065  180 TYR A C   
1539  O O   . TYR A 180 ? 0.2796 0.2883 0.3078 -0.0622 0.0677  0.0066  180 TYR A O   
1540  C CB  . TYR A 180 ? 0.2953 0.3328 0.3560 -0.0535 0.0432  0.0088  180 TYR A CB  
1541  C CG  . TYR A 180 ? 0.2701 0.3061 0.3251 -0.0474 0.0321  0.0120  180 TYR A CG  
1542  C CD1 . TYR A 180 ? 0.2830 0.3120 0.3254 -0.0423 0.0279  0.0137  180 TYR A CD1 
1543  C CD2 . TYR A 180 ? 0.2999 0.3414 0.3625 -0.0472 0.0263  0.0125  180 TYR A CD2 
1544  C CE1 . TYR A 180 ? 0.2766 0.3058 0.3170 -0.0372 0.0187  0.0154  180 TYR A CE1 
1545  C CE2 . TYR A 180 ? 0.2766 0.3166 0.3349 -0.0421 0.0178  0.0146  180 TYR A CE2 
1546  C CZ  . TYR A 180 ? 0.2750 0.3097 0.3235 -0.0372 0.0144  0.0159  180 TYR A CZ  
1547  O OH  . TYR A 180 ? 0.2505 0.2852 0.2976 -0.0325 0.0070  0.0169  180 TYR A OH  
1548  N N   . ARG A 181 ? 0.2762 0.3025 0.3349 -0.0701 0.0715  0.0027  181 ARG A N   
1549  C CA  . ARG A 181 ? 0.2747 0.3013 0.3384 -0.0762 0.0857  -0.0019 181 ARG A CA  
1550  C C   . ARG A 181 ? 0.3215 0.3220 0.3551 -0.0816 0.0961  0.0002  181 ARG A C   
1551  O O   . ARG A 181 ? 0.3497 0.3435 0.3758 -0.0843 0.1069  -0.0021 181 ARG A O   
1552  C CB  . ARG A 181 ? 0.2366 0.2805 0.3289 -0.0821 0.0901  -0.0075 181 ARG A CB  
1553  C CG  . ARG A 181 ? 0.2795 0.3270 0.3833 -0.0893 0.1059  -0.0138 181 ARG A CG  
1554  C CD  . ARG A 181 ? 0.2995 0.3666 0.4355 -0.0945 0.1076  -0.0201 181 ARG A CD  
1555  N NE  . ARG A 181 ? 0.2833 0.3699 0.4402 -0.0871 0.0923  -0.0204 181 ARG A NE  
1556  C CZ  . ARG A 181 ? 0.3221 0.4149 0.4873 -0.0874 0.0829  -0.0199 181 ARG A CZ  
1557  N NH1 . ARG A 181 ? 0.3404 0.4227 0.4969 -0.0947 0.0870  -0.0194 181 ARG A NH1 
1558  N NH2 . ARG A 181 ? 0.2668 0.3748 0.4476 -0.0804 0.0696  -0.0201 181 ARG A NH2 
1559  N N   . GLU A 182 ? 0.2711 0.2548 0.2855 -0.0831 0.0934  0.0044  182 GLU A N   
1560  C CA  . GLU A 182 ? 0.3887 0.3437 0.3704 -0.0877 0.1024  0.0070  182 GLU A CA  
1561  C C   . GLU A 182 ? 0.3588 0.2983 0.3143 -0.0808 0.0969  0.0107  182 GLU A C   
1562  O O   . GLU A 182 ? 0.3938 0.3158 0.3281 -0.0840 0.1068  0.0104  182 GLU A O   
1563  C CB  . GLU A 182 ? 0.3590 0.2987 0.3271 -0.0905 0.1002  0.0106  182 GLU A CB  
1564  C CG  . GLU A 182 ? 0.4399 0.3451 0.3683 -0.0929 0.1059  0.0149  182 GLU A CG  
1565  C CD  . GLU A 182 ? 0.5372 0.4243 0.4503 -0.0955 0.1043  0.0184  182 GLU A CD  
1566  O OE1 . GLU A 182 ? 0.6099 0.4663 0.4891 -0.0979 0.1096  0.0220  182 GLU A OE1 
1567  O OE2 . GLU A 182 ? 0.4836 0.3845 0.4158 -0.0951 0.0977  0.0177  182 GLU A OE2 
1568  N N   . ILE A 183 ? 0.3054 0.2497 0.2607 -0.0717 0.0815  0.0137  183 ILE A N   
1569  C CA  . ILE A 183 ? 0.3659 0.2970 0.2988 -0.0653 0.0753  0.0161  183 ILE A CA  
1570  C C   . ILE A 183 ? 0.4050 0.3451 0.3457 -0.0651 0.0812  0.0122  183 ILE A C   
1571  O O   . ILE A 183 ? 0.4187 0.3420 0.3358 -0.0643 0.0838  0.0127  183 ILE A O   
1572  C CB  . ILE A 183 ? 0.3690 0.3062 0.3049 -0.0560 0.0583  0.0188  183 ILE A CB  
1573  C CG1 . ILE A 183 ? 0.3719 0.3371 0.3393 -0.0527 0.0530  0.0161  183 ILE A CG1 
1574  C CG2 . ILE A 183 ? 0.3392 0.2669 0.2679 -0.0558 0.0532  0.0220  183 ILE A CG2 
1575  C CD1 . ILE A 183 ? 0.2978 0.2687 0.2665 -0.0474 0.0488  0.0147  183 ILE A CD1 
1576  N N   . LYS A 184 ? 0.2825 0.2478 0.2552 -0.0656 0.0829  0.0082  184 LYS A N   
1577  C CA  . LYS A 184 ? 0.3121 0.2858 0.2940 -0.0656 0.0898  0.0039  184 LYS A CA  
1578  C C   . LYS A 184 ? 0.3055 0.2651 0.2746 -0.0739 0.1074  0.0011  184 LYS A C   
1579  O O   . LYS A 184 ? 0.3469 0.2964 0.3013 -0.0738 0.1133  -0.0004 184 LYS A O   
1580  C CB  . LYS A 184 ? 0.2839 0.2859 0.3027 -0.0642 0.0877  0.0001  184 LYS A CB  
1581  C CG  . LYS A 184 ? 0.2888 0.3006 0.3198 -0.0626 0.0933  -0.0046 184 LYS A CG  
1582  C CD  . LYS A 184 ? 0.2918 0.3298 0.3583 -0.0600 0.0892  -0.0080 184 LYS A CD  
1583  C CE  . LYS A 184 ? 0.3565 0.4032 0.4356 -0.0577 0.0944  -0.0128 184 LYS A CE  
1584  N NZ  . LYS A 184 ? 0.4318 0.4713 0.5069 -0.0646 0.1117  -0.0175 184 LYS A NZ  
1585  N N   . GLU A 185 ? 0.3853 0.3428 0.3590 -0.0818 0.1167  -0.0001 185 GLU A N   
1586  C CA  . GLU A 185 ? 0.3904 0.3357 0.3549 -0.0910 0.1357  -0.0038 185 GLU A CA  
1587  C C   . GLU A 185 ? 0.4666 0.3768 0.3859 -0.0926 0.1396  0.0007  185 GLU A C   
1588  O O   . GLU A 185 ? 0.5073 0.4030 0.4098 -0.0971 0.1530  -0.0018 185 GLU A O   
1589  C CB  . GLU A 185 ? 0.4491 0.4024 0.4330 -0.0998 0.1452  -0.0071 185 GLU A CB  
1590  C CG  . GLU A 185 ? 0.6235 0.5770 0.6156 -0.1095 0.1663  -0.0141 185 GLU A CG  
1591  C CD  . GLU A 185 ? 0.8080 0.7269 0.7605 -0.1173 0.1811  -0.0122 185 GLU A CD  
1592  O OE1 . GLU A 185 ? 0.8445 0.7587 0.7952 -0.1223 0.1963  -0.0176 185 GLU A OE1 
1593  O OE2 . GLU A 185 ? 0.8559 0.7514 0.7784 -0.1170 0.1755  -0.0056 185 GLU A OE2 
1594  N N   . GLU A 186 ? 0.4944 0.3894 0.3927 -0.0887 0.1278  0.0069  186 GLU A N   
1595  C CA  . GLU A 186 ? 0.4809 0.3406 0.3347 -0.0890 0.1289  0.0115  186 GLU A CA  
1596  C C   . GLU A 186 ? 0.5113 0.3619 0.3452 -0.0811 0.1198  0.0128  186 GLU A C   
1597  O O   . GLU A 186 ? 0.5636 0.3838 0.3584 -0.0800 0.1179  0.0165  186 GLU A O   
1598  C CB  . GLU A 186 ? 0.5154 0.3622 0.3561 -0.0872 0.1191  0.0171  186 GLU A CB  
1599  C CG  . GLU A 186 ? 0.4952 0.3449 0.3493 -0.0965 0.1297  0.0156  186 GLU A CG  
1600  C CD  . GLU A 186 ? 0.5737 0.4116 0.4169 -0.0943 0.1200  0.0207  186 GLU A CD  
1601  O OE1 . GLU A 186 ? 0.5872 0.4251 0.4249 -0.0843 0.1030  0.0244  186 GLU A OE1 
1602  O OE2 . GLU A 186 ? 0.6078 0.4369 0.4493 -0.1028 0.1297  0.0205  186 GLU A OE2 
1603  N N   . GLY A 187 ? 0.4302 0.3048 0.2887 -0.0758 0.1140  0.0096  187 GLY A N   
1604  C CA  . GLY A 187 ? 0.4396 0.3080 0.2829 -0.0687 0.1047  0.0100  187 GLY A CA  
1605  C C   . GLY A 187 ? 0.4700 0.3331 0.3024 -0.0599 0.0852  0.0146  187 GLY A C   
1606  O O   . GLY A 187 ? 0.4817 0.3336 0.2949 -0.0544 0.0766  0.0151  187 GLY A O   
1607  N N   . LYS A 188 ? 0.5116 0.3829 0.3570 -0.0584 0.0777  0.0173  188 LYS A N   
1608  C CA  . LYS A 188 ? 0.4826 0.3505 0.3211 -0.0499 0.0598  0.0207  188 LYS A CA  
1609  C C   . LYS A 188 ? 0.4668 0.3613 0.3338 -0.0433 0.0485  0.0186  188 LYS A C   
1610  O O   . LYS A 188 ? 0.4260 0.3192 0.2891 -0.0361 0.0342  0.0200  188 LYS A O   
1611  C CB  . LYS A 188 ? 0.4480 0.3100 0.2852 -0.0511 0.0577  0.0242  188 LYS A CB  
1612  C CG  . LYS A 188 ? 0.5458 0.3792 0.3537 -0.0583 0.0694  0.0265  188 LYS A CG  
1613  C CD  . LYS A 188 ? 0.5383 0.3632 0.3427 -0.0589 0.0660  0.0301  188 LYS A CD  
1614  C CE  . LYS A 188 ? 0.6563 0.4463 0.4241 -0.0652 0.0765  0.0331  188 LYS A CE  
1615  N NZ  . LYS A 188 ? 0.7583 0.5377 0.5216 -0.0672 0.0758  0.0362  188 LYS A NZ  
1616  N N   . GLY A 189 ? 0.3702 0.2877 0.2656 -0.0456 0.0546  0.0151  189 GLY A N   
1617  C CA  . GLY A 189 ? 0.4014 0.3411 0.3210 -0.0400 0.0454  0.0133  189 GLY A CA  
1618  C C   . GLY A 189 ? 0.4152 0.3740 0.3597 -0.0429 0.0542  0.0094  189 GLY A C   
1619  O O   . GLY A 189 ? 0.3918 0.3520 0.3422 -0.0492 0.0664  0.0077  189 GLY A O   
1620  N N   . SER A 190 ? 0.3589 0.3317 0.3182 -0.0383 0.0481  0.0075  190 SER A N   
1621  C CA  . SER A 190 ? 0.2663 0.2586 0.2519 -0.0392 0.0536  0.0041  190 SER A CA  
1622  C C   . SER A 190 ? 0.2981 0.3081 0.3067 -0.0366 0.0454  0.0053  190 SER A C   
1623  O O   . SER A 190 ? 0.2780 0.2868 0.2831 -0.0330 0.0353  0.0078  190 SER A O   
1624  C CB  . SER A 190 ? 0.2795 0.2732 0.2649 -0.0362 0.0536  0.0010  190 SER A CB  
1625  O OG  . SER A 190 ? 0.3333 0.3093 0.2959 -0.0392 0.0624  -0.0007 190 SER A OG  
1626  N N   . VAL A 191 ? 0.2595 0.2850 0.2911 -0.0384 0.0499  0.0032  191 VAL A N   
1627  C CA  . VAL A 191 ? 0.2498 0.2904 0.3011 -0.0360 0.0423  0.0040  191 VAL A CA  
1628  C C   . VAL A 191 ? 0.2947 0.3484 0.3639 -0.0327 0.0416  0.0013  191 VAL A C   
1629  O O   . VAL A 191 ? 0.2649 0.3231 0.3431 -0.0342 0.0496  -0.0022 191 VAL A O   
1630  C CB  . VAL A 191 ? 0.2194 0.2659 0.2818 -0.0404 0.0454  0.0040  191 VAL A CB  
1631  C CG1 . VAL A 191 ? 0.1806 0.2411 0.2606 -0.0373 0.0363  0.0048  191 VAL A CG1 
1632  C CG2 . VAL A 191 ? 0.1956 0.2263 0.2384 -0.0439 0.0469  0.0068  191 VAL A CG2 
1633  N N   . SER A 192 ? 0.2803 0.3391 0.3544 -0.0281 0.0326  0.0027  192 SER A N   
1634  C CA  . SER A 192 ? 0.2013 0.2700 0.2903 -0.0247 0.0310  0.0009  192 SER A CA  
1635  C C   . SER A 192 ? 0.2914 0.3706 0.3955 -0.0233 0.0251  0.0022  192 SER A C   
1636  O O   . SER A 192 ? 0.1342 0.2134 0.2370 -0.0251 0.0222  0.0042  192 SER A O   
1637  C CB  . SER A 192 ? 0.1934 0.2571 0.2742 -0.0213 0.0265  0.0010  192 SER A CB  
1638  O OG  . SER A 192 ? 0.2047 0.2679 0.2826 -0.0198 0.0185  0.0036  192 SER A OG  
1639  N N   . THR A 193 ? 0.2151 0.3016 0.3318 -0.0198 0.0228  0.0009  193 THR A N   
1640  C CA  . THR A 193 ? 0.2018 0.2945 0.3278 -0.0177 0.0157  0.0026  193 THR A CA  
1641  C C   . THR A 193 ? 0.2313 0.3224 0.3572 -0.0134 0.0114  0.0033  193 THR A C   
1642  O O   . THR A 193 ? 0.2261 0.3128 0.3470 -0.0123 0.0140  0.0020  193 THR A O   
1643  C CB  . THR A 193 ? 0.1303 0.2334 0.2737 -0.0180 0.0164  0.0002  193 THR A CB  
1644  O OG1 . THR A 193 ? 0.1865 0.2925 0.3337 -0.0164 0.0081  0.0023  193 THR A OG1 
1645  C CG2 . THR A 193 ? 0.1836 0.2922 0.3400 -0.0147 0.0191  -0.0033 193 THR A CG2 
1646  N N   . SER A 194 ? 0.1645 0.2575 0.2942 -0.0113 0.0050  0.0052  194 SER A N   
1647  C CA  . SER A 194 ? 0.2237 0.3129 0.3521 -0.0078 0.0017  0.0062  194 SER A CA  
1648  C C   . SER A 194 ? 0.2153 0.3085 0.3549 -0.0039 -0.0022 0.0058  194 SER A C   
1649  O O   . SER A 194 ? 0.1484 0.2490 0.2979 -0.0042 -0.0035 0.0046  194 SER A O   
1650  C CB  . SER A 194 ? 0.2126 0.2963 0.3315 -0.0088 -0.0021 0.0089  194 SER A CB  
1651  O OG  . SER A 194 ? 0.2206 0.3007 0.3311 -0.0110 -0.0001 0.0086  194 SER A OG  
1652  N N   . PRO A 195 ? 0.2480 0.3361 0.3866 0.0000  -0.0046 0.0064  195 PRO A N   
1653  C CA  . PRO A 195 ? 0.2383 0.3271 0.3838 0.0046  -0.0110 0.0069  195 PRO A CA  
1654  C C   . PRO A 195 ? 0.2294 0.3184 0.3715 0.0032  -0.0169 0.0093  195 PRO A C   
1655  O O   . PRO A 195 ? 0.1261 0.2103 0.2570 -0.0003 -0.0163 0.0115  195 PRO A O   
1656  C CB  . PRO A 195 ? 0.2579 0.3357 0.3954 0.0076  -0.0122 0.0085  195 PRO A CB  
1657  C CG  . PRO A 195 ? 0.3539 0.4302 0.4887 0.0056  -0.0051 0.0064  195 PRO A CG  
1658  C CD  . PRO A 195 ? 0.2860 0.3665 0.4172 0.0005  -0.0018 0.0061  195 PRO A CD  
1659  N N   . TYR A 196 ? 0.2343 0.3288 0.3868 0.0063  -0.0229 0.0082  196 TYR A N   
1660  C CA  . TYR A 196 ? 0.2134 0.3130 0.3685 0.0039  -0.0272 0.0081  196 TYR A CA  
1661  C C   . TYR A 196 ? 0.2611 0.3513 0.3991 0.0011  -0.0294 0.0119  196 TYR A C   
1662  O O   . TYR A 196 ? 0.2037 0.2960 0.3389 -0.0035 -0.0271 0.0120  196 TYR A O   
1663  C CB  . TYR A 196 ? 0.1287 0.2337 0.2966 0.0089  -0.0360 0.0061  196 TYR A CB  
1664  C CG  . TYR A 196 ? 0.2130 0.3282 0.3914 0.0057  -0.0386 0.0035  196 TYR A CG  
1665  C CD1 . TYR A 196 ? 0.2559 0.3662 0.4229 0.0029  -0.0433 0.0058  196 TYR A CD1 
1666  C CD2 . TYR A 196 ? 0.1632 0.2928 0.3631 0.0048  -0.0353 -0.0019 196 TYR A CD2 
1667  C CE1 . TYR A 196 ? 0.2427 0.3614 0.4188 -0.0006 -0.0455 0.0031  196 TYR A CE1 
1668  C CE2 . TYR A 196 ? 0.1186 0.2573 0.3289 0.0009  -0.0368 -0.0049 196 TYR A CE2 
1669  C CZ  . TYR A 196 ? 0.2429 0.3761 0.4411 -0.0018 -0.0424 -0.0023 196 TYR A CZ  
1670  O OH  . TYR A 196 ? 0.2586 0.4001 0.4668 -0.0062 -0.0440 -0.0056 196 TYR A OH  
1671  N N   . TYR A 197 ? 0.2254 0.3037 0.3511 0.0037  -0.0331 0.0149  197 TYR A N   
1672  C CA  . TYR A 197 ? 0.2025 0.2711 0.3123 0.0010  -0.0345 0.0178  197 TYR A CA  
1673  C C   . TYR A 197 ? 0.1994 0.2603 0.2984 -0.0018 -0.0277 0.0191  197 TYR A C   
1674  O O   . TYR A 197 ? 0.1930 0.2431 0.2785 -0.0031 -0.0278 0.0213  197 TYR A O   
1675  C CB  . TYR A 197 ? 0.1967 0.2551 0.2974 0.0049  -0.0433 0.0199  197 TYR A CB  
1676  C CG  . TYR A 197 ? 0.2003 0.2672 0.3119 0.0070  -0.0517 0.0177  197 TYR A CG  
1677  C CD1 . TYR A 197 ? 0.1533 0.2248 0.2649 0.0028  -0.0528 0.0168  197 TYR A CD1 
1678  C CD2 . TYR A 197 ? 0.1928 0.2642 0.3169 0.0131  -0.0583 0.0158  197 TYR A CD2 
1679  C CE1 . TYR A 197 ? 0.2186 0.2988 0.3420 0.0039  -0.0604 0.0139  197 TYR A CE1 
1680  C CE2 . TYR A 197 ? 0.1737 0.2552 0.3115 0.0148  -0.0664 0.0126  197 TYR A CE2 
1681  C CZ  . TYR A 197 ? 0.2259 0.3119 0.3633 0.0098  -0.0673 0.0115  197 TYR A CZ  
1682  O OH  . TYR A 197 ? 0.2806 0.3772 0.4330 0.0108  -0.0755 0.0075  197 TYR A OH  
1683  N N   . HIS A 198 ? 0.2381 0.3039 0.3428 -0.0030 -0.0217 0.0174  198 HIS A N   
1684  C CA  . HIS A 198 ? 0.2455 0.3061 0.3431 -0.0056 -0.0163 0.0174  198 HIS A CA  
1685  C C   . HIS A 198 ? 0.1928 0.2409 0.2811 -0.0044 -0.0160 0.0191  198 HIS A C   
1686  O O   . HIS A 198 ? 0.2803 0.3211 0.3595 -0.0074 -0.0131 0.0197  198 HIS A O   
1687  C CB  . HIS A 198 ? 0.2385 0.2995 0.3313 -0.0095 -0.0147 0.0176  198 HIS A CB  
1688  C CG  . HIS A 198 ? 0.2104 0.2720 0.3026 -0.0120 -0.0099 0.0159  198 HIS A CG  
1689  N ND1 . HIS A 198 ? 0.2350 0.2902 0.3214 -0.0139 -0.0071 0.0156  198 HIS A ND1 
1690  C CD2 . HIS A 198 ? 0.2274 0.2948 0.3239 -0.0128 -0.0079 0.0140  198 HIS A CD2 
1691  C CE1 . HIS A 198 ? 0.2563 0.3152 0.3462 -0.0153 -0.0046 0.0130  198 HIS A CE1 
1692  N NE2 . HIS A 198 ? 0.2134 0.2787 0.3078 -0.0144 -0.0055 0.0124  198 HIS A NE2 
1693  N N   . PRO A 199 ? 0.1803 0.2247 0.2704 -0.0001 -0.0184 0.0194  199 PRO A N   
1694  C CA  . PRO A 199 ? 0.2306 0.2602 0.3098 0.0008  -0.0174 0.0212  199 PRO A CA  
1695  C C   . PRO A 199 ? 0.3483 0.3769 0.4293 -0.0013 -0.0108 0.0190  199 PRO A C   
1696  O O   . PRO A 199 ? 0.2828 0.3215 0.3732 -0.0020 -0.0084 0.0162  199 PRO A O   
1697  C CB  . PRO A 199 ? 0.2226 0.2494 0.3050 0.0073  -0.0236 0.0220  199 PRO A CB  
1698  C CG  . PRO A 199 ? 0.1825 0.2251 0.2823 0.0087  -0.0228 0.0186  199 PRO A CG  
1699  C CD  . PRO A 199 ? 0.2079 0.2607 0.3109 0.0042  -0.0214 0.0178  199 PRO A CD  
1700  N N   . LEU A 200 ? 0.3037 0.3184 0.3743 -0.0025 -0.0081 0.0201  200 LEU A N   
1701  C CA  . LEU A 200 ? 0.3328 0.3444 0.4050 -0.0042 -0.0027 0.0176  200 LEU A CA  
1702  C C   . LEU A 200 ? 0.3277 0.3356 0.4030 0.0013  -0.0049 0.0176  200 LEU A C   
1703  O O   . LEU A 200 ? 0.3016 0.2948 0.3676 0.0038  -0.0063 0.0200  200 LEU A O   
1704  C CB  . LEU A 200 ? 0.3357 0.3339 0.3968 -0.0090 0.0026  0.0180  200 LEU A CB  
1705  C CG  . LEU A 200 ? 0.3670 0.3707 0.4286 -0.0143 0.0060  0.0165  200 LEU A CG  
1706  C CD1 . LEU A 200 ? 0.4074 0.3956 0.4556 -0.0187 0.0112  0.0177  200 LEU A CD1 
1707  C CD2 . LEU A 200 ? 0.3639 0.3796 0.4374 -0.0172 0.0090  0.0116  200 LEU A CD2 
1708  N N   . ILE A 201 ? 0.2835 0.3315 0.3297 -0.0094 -0.0094 0.0044  201 ILE A N   
1709  C CA  . ILE A 201 ? 0.1982 0.2433 0.2517 -0.0098 -0.0124 0.0021  201 ILE A CA  
1710  C C   . ILE A 201 ? 0.2315 0.2735 0.2856 -0.0128 -0.0111 0.0031  201 ILE A C   
1711  O O   . ILE A 201 ? 0.2436 0.2782 0.2993 -0.0119 -0.0130 0.0038  201 ILE A O   
1712  C CB  . ILE A 201 ? 0.2429 0.2929 0.3039 -0.0094 -0.0112 -0.0020 201 ILE A CB  
1713  C CG1 . ILE A 201 ? 0.2786 0.3292 0.3393 -0.0069 -0.0123 -0.0033 201 ILE A CG1 
1714  C CG2 . ILE A 201 ? 0.2232 0.2689 0.2919 -0.0098 -0.0118 -0.0041 201 ILE A CG2 
1715  C CD1 . ILE A 201 ? 0.2788 0.3253 0.3436 -0.0057 -0.0175 -0.0033 201 ILE A CD1 
1716  N N   . PRO A 202 ? 0.2479 0.2956 0.3015 -0.0166 -0.0078 0.0033  202 PRO A N   
1717  C CA  . PRO A 202 ? 0.2200 0.2629 0.2732 -0.0210 -0.0061 0.0035  202 PRO A CA  
1718  C C   . PRO A 202 ? 0.2209 0.2541 0.2684 -0.0196 -0.0067 0.0074  202 PRO A C   
1719  O O   . PRO A 202 ? 0.2748 0.2988 0.3223 -0.0204 -0.0060 0.0075  202 PRO A O   
1720  C CB  . PRO A 202 ? 0.2183 0.2722 0.2720 -0.0259 -0.0035 0.0041  202 PRO A CB  
1721  C CG  . PRO A 202 ? 0.2482 0.3123 0.3049 -0.0238 -0.0038 0.0028  202 PRO A CG  
1722  C CD  . PRO A 202 ? 0.2430 0.3021 0.2972 -0.0175 -0.0053 0.0037  202 PRO A CD  
1723  N N   . ILE A 203 ? 0.2301 0.2633 0.2713 -0.0173 -0.0071 0.0107  203 ILE A N   
1724  C CA  . ILE A 203 ? 0.2848 0.3073 0.3180 -0.0161 -0.0075 0.0146  203 ILE A CA  
1725  C C   . ILE A 203 ? 0.2957 0.3105 0.3286 -0.0122 -0.0127 0.0152  203 ILE A C   
1726  O O   . ILE A 203 ? 0.3525 0.3583 0.3833 -0.0114 -0.0130 0.0178  203 ILE A O   
1727  C CB  . ILE A 203 ? 0.2999 0.3220 0.3241 -0.0149 -0.0054 0.0180  203 ILE A CB  
1728  C CG1 . ILE A 203 ? 0.2474 0.2782 0.2746 -0.0184 0.0004  0.0194  203 ILE A CG1 
1729  C CG2 . ILE A 203 ? 0.3110 0.3194 0.3236 -0.0132 -0.0067 0.0219  203 ILE A CG2 
1730  C CD1 . ILE A 203 ? 0.2895 0.3181 0.3086 -0.0167 0.0048  0.0237  203 ILE A CD1 
1731  N N   . LEU A 204 ? 0.2933 0.3123 0.3292 -0.0097 -0.0165 0.0134  204 LEU A N   
1732  C CA  . LEU A 204 ? 0.2843 0.2994 0.3225 -0.0063 -0.0224 0.0150  204 LEU A CA  
1733  C C   . LEU A 204 ? 0.3180 0.3304 0.3660 -0.0052 -0.0211 0.0147  204 LEU A C   
1734  O O   . LEU A 204 ? 0.3208 0.3274 0.3699 -0.0019 -0.0239 0.0187  204 LEU A O   
1735  C CB  . LEU A 204 ? 0.3076 0.3291 0.3492 -0.0052 -0.0262 0.0126  204 LEU A CB  
1736  C CG  . LEU A 204 ? 0.2825 0.3036 0.3129 -0.0062 -0.0266 0.0124  204 LEU A CG  
1737  C CD1 . LEU A 204 ? 0.2163 0.2423 0.2516 -0.0060 -0.0305 0.0096  204 LEU A CD1 
1738  C CD2 . LEU A 204 ? 0.2285 0.2400 0.2440 -0.0064 -0.0290 0.0168  204 LEU A CD2 
1739  N N   . LEU A 205 ? 0.3148 0.3303 0.3690 -0.0080 -0.0164 0.0105  205 LEU A N   
1740  C CA  . LEU A 205 ? 0.2686 0.2782 0.3297 -0.0076 -0.0131 0.0097  205 LEU A CA  
1741  C C   . LEU A 205 ? 0.3142 0.3132 0.3692 -0.0097 -0.0088 0.0120  205 LEU A C   
1742  O O   . LEU A 205 ? 0.3118 0.3013 0.3696 -0.0069 -0.0067 0.0143  205 LEU A O   
1743  C CB  . LEU A 205 ? 0.2504 0.2644 0.3166 -0.0110 -0.0090 0.0039  205 LEU A CB  
1744  C CG  . LEU A 205 ? 0.2760 0.2968 0.3505 -0.0080 -0.0111 0.0015  205 LEU A CG  
1745  C CD1 . LEU A 205 ? 0.2239 0.2479 0.3000 -0.0118 -0.0067 -0.0040 205 LEU A CD1 
1746  C CD2 . LEU A 205 ? 0.2567 0.2736 0.3408 -0.0028 -0.0123 0.0039  205 LEU A CD2 
1747  N N   . ASN A 206 ? 0.3081 0.3082 0.3556 -0.0143 -0.0067 0.0120  206 ASN A N   
1748  C CA  . ASN A 206 ? 0.3233 0.3136 0.3657 -0.0180 -0.0014 0.0131  206 ASN A CA  
1749  C C   . ASN A 206 ? 0.2781 0.2721 0.3135 -0.0217 -0.0002 0.0148  206 ASN A C   
1750  O O   . ASN A 206 ? 0.2475 0.2506 0.2847 -0.0274 0.0021  0.0121  206 ASN A O   
1751  C CB  . ASN A 206 ? 0.3834 0.3710 0.4288 -0.0240 0.0044  0.0080  206 ASN A CB  
1752  C CG  . ASN A 206 ? 0.4294 0.4058 0.4686 -0.0298 0.0108  0.0084  206 ASN A CG  
1753  O OD1 . ASN A 206 ? 0.4166 0.3865 0.4501 -0.0281 0.0114  0.0129  206 ASN A OD1 
1754  N ND2 . ASN A 206 ? 0.3988 0.3722 0.4378 -0.0373 0.0159  0.0033  206 ASN A ND2 
1755  N N   . PRO A 207 ? 0.2453 0.2328 0.2728 -0.0184 -0.0015 0.0197  207 PRO A N   
1756  C CA  . PRO A 207 ? 0.3251 0.3146 0.3458 -0.0211 0.0010  0.0219  207 PRO A CA  
1757  C C   . PRO A 207 ? 0.3396 0.3290 0.3613 -0.0284 0.0076  0.0208  207 PRO A C   
1758  O O   . PRO A 207 ? 0.4157 0.4132 0.4373 -0.0317 0.0101  0.0218  207 PRO A O   
1759  C CB  . PRO A 207 ? 0.2639 0.2414 0.2736 -0.0162 -0.0010 0.0274  207 PRO A CB  
1760  C CG  . PRO A 207 ? 0.2804 0.2577 0.2931 -0.0106 -0.0079 0.0279  207 PRO A CG  
1761  C CD  . PRO A 207 ? 0.2593 0.2390 0.2837 -0.0116 -0.0062 0.0241  207 PRO A CD  
1762  N N   . ASN A 208 ? 0.2876 0.2679 0.3104 -0.0315 0.0110  0.0190  208 ASN A N   
1763  C CA  . ASN A 208 ? 0.3586 0.3384 0.3816 -0.0406 0.0172  0.0170  208 ASN A CA  
1764  C C   . ASN A 208 ? 0.3537 0.3504 0.3842 -0.0475 0.0164  0.0126  208 ASN A C   
1765  O O   . ASN A 208 ? 0.3630 0.3648 0.3949 -0.0563 0.0200  0.0116  208 ASN A O   
1766  C CB  . ASN A 208 ? 0.3037 0.2663 0.3239 -0.0426 0.0224  0.0157  208 ASN A CB  
1767  C CG  . ASN A 208 ? 0.3688 0.3152 0.3820 -0.0346 0.0230  0.0215  208 ASN A CG  
1768  O OD1 . ASN A 208 ? 0.3320 0.2760 0.3385 -0.0320 0.0225  0.0261  208 ASN A OD1 
1769  N ND2 . ASN A 208 ? 0.4690 0.4038 0.4831 -0.0303 0.0245  0.0219  208 ASN A ND2 
1770  N N   . CYS A 209 ? 0.3075 0.3139 0.3429 -0.0442 0.0117  0.0105  209 CYS A N   
1771  C CA  . CYS A 209 ? 0.3615 0.3842 0.4027 -0.0503 0.0108  0.0074  209 CYS A CA  
1772  C C   . CYS A 209 ? 0.3610 0.3985 0.4051 -0.0524 0.0114  0.0113  209 CYS A C   
1773  O O   . CYS A 209 ? 0.3026 0.3550 0.3522 -0.0592 0.0111  0.0102  209 CYS A O   
1774  C CB  . CYS A 209 ? 0.3415 0.3705 0.3864 -0.0454 0.0065  0.0050  209 CYS A CB  
1775  S SG  . CYS A 209 ? 0.3502 0.3884 0.3960 -0.0368 0.0029  0.0089  209 CYS A SG  
1776  N N   . VAL A 210 ? 0.3398 0.3736 0.3801 -0.0472 0.0128  0.0164  210 VAL A N   
1777  C CA  . VAL A 210 ? 0.2974 0.3443 0.3416 -0.0489 0.0155  0.0208  210 VAL A CA  
1778  C C   . VAL A 210 ? 0.2699 0.3213 0.3180 -0.0592 0.0194  0.0207  210 VAL A C   
1779  O O   . VAL A 210 ? 0.3185 0.3878 0.3750 -0.0631 0.0205  0.0237  210 VAL A O   
1780  C CB  . VAL A 210 ? 0.3580 0.3964 0.3947 -0.0416 0.0178  0.0259  210 VAL A CB  
1781  C CG1 . VAL A 210 ? 0.3771 0.4109 0.4088 -0.0334 0.0135  0.0254  210 VAL A CG1 
1782  C CG2 . VAL A 210 ? 0.3041 0.3246 0.3323 -0.0425 0.0212  0.0274  210 VAL A CG2 
1783  N N   . TYR A 211 ? 0.2484 0.2845 0.2913 -0.0640 0.0218  0.0178  211 TYR A N   
1784  C CA  . TYR A 211 ? 0.2554 0.2929 0.3003 -0.0753 0.0263  0.0168  211 TYR A CA  
1785  C C   . TYR A 211 ? 0.2947 0.3467 0.3456 -0.0860 0.0237  0.0122  211 TYR A C   
1786  O O   . TYR A 211 ? 0.2900 0.3457 0.3429 -0.0977 0.0265  0.0108  211 TYR A O   
1787  C CB  . TYR A 211 ? 0.3440 0.3570 0.3793 -0.0765 0.0312  0.0152  211 TYR A CB  
1788  C CG  . TYR A 211 ? 0.3777 0.3776 0.4056 -0.0668 0.0330  0.0206  211 TYR A CG  
1789  C CD1 . TYR A 211 ? 0.4073 0.4119 0.4359 -0.0664 0.0368  0.0258  211 TYR A CD1 
1790  C CD2 . TYR A 211 ? 0.4107 0.3948 0.4311 -0.0578 0.0308  0.0211  211 TYR A CD2 
1791  C CE1 . TYR A 211 ? 0.4174 0.4084 0.4363 -0.0583 0.0387  0.0306  211 TYR A CE1 
1792  C CE2 . TYR A 211 ? 0.4339 0.4068 0.4455 -0.0497 0.0312  0.0264  211 TYR A CE2 
1793  C CZ  . TYR A 211 ? 0.5018 0.4772 0.5113 -0.0503 0.0353  0.0307  211 TYR A CZ  
1794  O OH  . TYR A 211 ? 0.6133 0.5758 0.6112 -0.0433 0.0363  0.0357  211 TYR A OH  
1795  N N   . GLU A 212 ? 0.3012 0.3610 0.3540 -0.0834 0.0184  0.0095  212 GLU A N   
1796  C CA  . GLU A 212 ? 0.3073 0.3815 0.3638 -0.0942 0.0155  0.0058  212 GLU A CA  
1797  C C   . GLU A 212 ? 0.3621 0.4635 0.4301 -0.0978 0.0134  0.0113  212 GLU A C   
1798  O O   . GLU A 212 ? 0.3790 0.4945 0.4508 -0.1099 0.0113  0.0096  212 GLU A O   
1799  C CB  . GLU A 212 ? 0.3150 0.3886 0.3692 -0.0902 0.0113  0.0017  212 GLU A CB  
1800  C CG  . GLU A 212 ? 0.3779 0.4267 0.4234 -0.0868 0.0139  -0.0031 212 GLU A CG  
1801  C CD  . GLU A 212 ? 0.5077 0.5563 0.5527 -0.0815 0.0107  -0.0063 212 GLU A CD  
1802  O OE1 . GLU A 212 ? 0.5573 0.5919 0.6004 -0.0727 0.0115  -0.0067 212 GLU A OE1 
1803  O OE2 . GLU A 212 ? 0.5174 0.5806 0.5644 -0.0860 0.0072  -0.0079 212 GLU A OE2 
1804  N N   . THR A 213 ? 0.3401 0.4490 0.4134 -0.0878 0.0143  0.0181  213 THR A N   
1805  C CA  . THR A 213 ? 0.3326 0.4675 0.4187 -0.0885 0.0138  0.0251  213 THR A CA  
1806  C C   . THR A 213 ? 0.3123 0.4476 0.4029 -0.0876 0.0203  0.0313  213 THR A C   
1807  O O   . THR A 213 ? 0.3338 0.4900 0.4367 -0.0938 0.0212  0.0362  213 THR A O   
1808  C CB  . THR A 213 ? 0.3579 0.5024 0.4471 -0.0768 0.0115  0.0288  213 THR A CB  
1809  O OG1 . THR A 213 ? 0.3316 0.4571 0.4125 -0.0657 0.0145  0.0294  213 THR A OG1 
1810  C CG2 . THR A 213 ? 0.3876 0.5355 0.4740 -0.0785 0.0055  0.0236  213 THR A CG2 
1811  N N   . THR A 214 ? 0.2951 0.4087 0.3763 -0.0801 0.0248  0.0318  214 THR A N   
1812  C CA  . THR A 214 ? 0.3054 0.4157 0.3879 -0.0777 0.0321  0.0379  214 THR A CA  
1813  C C   . THR A 214 ? 0.3498 0.4347 0.4205 -0.0805 0.0361  0.0345  214 THR A C   
1814  O O   . THR A 214 ? 0.4247 0.4895 0.4836 -0.0720 0.0376  0.0348  214 THR A O   
1815  C CB  . THR A 214 ? 0.3200 0.4272 0.3994 -0.0644 0.0346  0.0431  214 THR A CB  
1816  O OG1 . THR A 214 ? 0.4063 0.4943 0.4725 -0.0575 0.0312  0.0388  214 THR A OG1 
1817  C CG2 . THR A 214 ? 0.2714 0.4033 0.3631 -0.0609 0.0328  0.0478  214 THR A CG2 
1818  N N   . PRO A 215 ? 0.3988 0.4839 0.4717 -0.0929 0.0380  0.0314  215 PRO A N   
1819  C CA  . PRO A 215 ? 0.4593 0.5181 0.5201 -0.0954 0.0428  0.0282  215 PRO A CA  
1820  C C   . PRO A 215 ? 0.4603 0.5051 0.5152 -0.0895 0.0503  0.0337  215 PRO A C   
1821  O O   . PRO A 215 ? 0.4980 0.5183 0.5399 -0.0864 0.0533  0.0325  215 PRO A O   
1822  C CB  . PRO A 215 ? 0.5061 0.5707 0.5714 -0.1118 0.0444  0.0240  215 PRO A CB  
1823  C CG  . PRO A 215 ? 0.4570 0.5543 0.5392 -0.1176 0.0410  0.0277  215 PRO A CG  
1824  C CD  . PRO A 215 ? 0.4035 0.5116 0.4884 -0.1059 0.0351  0.0302  215 PRO A CD  
1825  N N   . ASN A 216 ? 0.4042 0.4631 0.4678 -0.0873 0.0540  0.0403  216 ASN A N   
1826  C CA  . ASN A 216 ? 0.4478 0.4922 0.5046 -0.0830 0.0626  0.0455  216 ASN A CA  
1827  C C   . ASN A 216 ? 0.4945 0.5253 0.5388 -0.0694 0.0623  0.0485  216 ASN A C   
1828  O O   . ASN A 216 ? 0.5556 0.5716 0.5906 -0.0651 0.0693  0.0528  216 ASN A O   
1829  C CB  . ASN A 216 ? 0.4830 0.5475 0.5554 -0.0879 0.0689  0.0516  216 ASN A CB  
1830  C CG  . ASN A 216 ? 0.5877 0.6666 0.6724 -0.1035 0.0690  0.0488  216 ASN A CG  
1831  O OD1 . ASN A 216 ? 0.6087 0.7163 0.7114 -0.1092 0.0670  0.0519  216 ASN A OD1 
1832  N ND2 . ASN A 216 ? 0.6363 0.6953 0.7109 -0.1109 0.0716  0.0434  216 ASN A ND2 
1833  N N   . VAL A 217 ? 0.4952 0.5297 0.5379 -0.0633 0.0547  0.0461  217 VAL A N   
1834  C CA  . VAL A 217 ? 0.4609 0.4842 0.4918 -0.0521 0.0540  0.0486  217 VAL A CA  
1835  C C   . VAL A 217 ? 0.4110 0.4072 0.4237 -0.0484 0.0539  0.0476  217 VAL A C   
1836  O O   . VAL A 217 ? 0.3965 0.3836 0.4067 -0.0520 0.0518  0.0439  217 VAL A O   
1837  C CB  . VAL A 217 ? 0.4288 0.4632 0.4634 -0.0477 0.0461  0.0459  217 VAL A CB  
1838  C CG1 . VAL A 217 ? 0.4465 0.4735 0.4776 -0.0492 0.0388  0.0394  217 VAL A CG1 
1839  C CG2 . VAL A 217 ? 0.4722 0.4984 0.4962 -0.0380 0.0469  0.0486  217 VAL A CG2 
1840  N N   . LYS A 218 ? 0.4230 0.4057 0.4220 -0.0411 0.0566  0.0514  218 LYS A N   
1841  C CA  . LYS A 218 ? 0.3930 0.3516 0.3732 -0.0366 0.0551  0.0520  218 LYS A CA  
1842  C C   . LYS A 218 ? 0.3548 0.3113 0.3278 -0.0300 0.0463  0.0502  218 LYS A C   
1843  O O   . LYS A 218 ? 0.4769 0.4402 0.4496 -0.0267 0.0463  0.0510  218 LYS A O   
1844  C CB  . LYS A 218 ? 0.5195 0.4624 0.4862 -0.0345 0.0642  0.0575  218 LYS A CB  
1845  C CG  . LYS A 218 ? 0.6736 0.6206 0.6497 -0.0413 0.0747  0.0600  218 LYS A CG  
1846  C CD  . LYS A 218 ? 0.7665 0.7385 0.7617 -0.0439 0.0788  0.0622  218 LYS A CD  
1847  C CE  . LYS A 218 ? 0.8169 0.7942 0.8217 -0.0496 0.0901  0.0666  218 LYS A CE  
1848  N NZ  . LYS A 218 ? 0.7837 0.7915 0.8122 -0.0530 0.0909  0.0687  218 LYS A NZ  
1849  N N   . ILE A 219 ? 0.3155 0.2630 0.2835 -0.0282 0.0395  0.0480  219 ILE A N   
1850  C CA  . ILE A 219 ? 0.3905 0.3371 0.3532 -0.0227 0.0307  0.0466  219 ILE A CA  
1851  C C   . ILE A 219 ? 0.3823 0.3097 0.3288 -0.0185 0.0271  0.0495  219 ILE A C   
1852  O O   . ILE A 219 ? 0.4123 0.3280 0.3546 -0.0194 0.0308  0.0517  219 ILE A O   
1853  C CB  . ILE A 219 ? 0.3896 0.3502 0.3670 -0.0240 0.0243  0.0414  219 ILE A CB  
1854  C CG1 . ILE A 219 ? 0.3865 0.3393 0.3662 -0.0254 0.0231  0.0400  219 ILE A CG1 
1855  C CG2 . ILE A 219 ? 0.3701 0.3501 0.3627 -0.0289 0.0275  0.0393  219 ILE A CG2 
1856  C CD1 . ILE A 219 ? 0.3679 0.3292 0.3579 -0.0247 0.0168  0.0355  219 ILE A CD1 
1857  N N   . PRO A 220 ? 0.4072 0.3310 0.3438 -0.0141 0.0198  0.0500  220 PRO A N   
1858  C CA  . PRO A 220 ? 0.4642 0.3721 0.3851 -0.0102 0.0147  0.0539  220 PRO A CA  
1859  C C   . PRO A 220 ? 0.4556 0.3646 0.3857 -0.0081 0.0091  0.0538  220 PRO A C   
1860  O O   . PRO A 220 ? 0.4445 0.3647 0.3913 -0.0100 0.0090  0.0497  220 PRO A O   
1861  C CB  . PRO A 220 ? 0.4541 0.3612 0.3631 -0.0081 0.0081  0.0538  220 PRO A CB  
1862  C CG  . PRO A 220 ? 0.4304 0.3545 0.3538 -0.0098 0.0080  0.0486  220 PRO A CG  
1863  C CD  . PRO A 220 ? 0.3887 0.3210 0.3250 -0.0131 0.0173  0.0478  220 PRO A CD  
1864  N N   . ASP A 221 ? 0.4192 0.3151 0.3370 -0.0038 0.0050  0.0591  221 ASP A N   
1865  C CA  . ASP A 221 ? 0.4299 0.3243 0.3550 0.0002  0.0007  0.0613  221 ASP A CA  
1866  C C   . ASP A 221 ? 0.4290 0.3370 0.3637 0.0026  -0.0098 0.0593  221 ASP A C   
1867  O O   . ASP A 221 ? 0.4120 0.3196 0.3371 0.0050  -0.0184 0.0622  221 ASP A O   
1868  C CB  . ASP A 221 ? 0.4468 0.3238 0.3551 0.0049  -0.0001 0.0693  221 ASP A CB  
1869  C CG  . ASP A 221 ? 0.4919 0.3643 0.4084 0.0098  -0.0002 0.0731  221 ASP A CG  
1870  O OD1 . ASP A 221 ? 0.5132 0.3933 0.4469 0.0085  0.0023  0.0689  221 ASP A OD1 
1871  O OD2 . ASP A 221 ? 0.5983 0.4586 0.5032 0.0152  -0.0022 0.0808  221 ASP A OD2 
1872  N N   . PHE A 222 ? 0.3825 0.3023 0.3356 0.0011  -0.0090 0.0542  222 PHE A N   
1873  C CA  . PHE A 222 ? 0.3268 0.2593 0.2910 0.0033  -0.0175 0.0521  222 PHE A CA  
1874  C C   . PHE A 222 ? 0.4456 0.3747 0.4144 0.0096  -0.0223 0.0579  222 PHE A C   
1875  O O   . PHE A 222 ? 0.4393 0.3703 0.4220 0.0114  -0.0195 0.0570  222 PHE A O   
1876  C CB  . PHE A 222 ? 0.3049 0.2496 0.2851 -0.0005 -0.0141 0.0450  222 PHE A CB  
1877  C CG  . PHE A 222 ? 0.3418 0.2952 0.3201 -0.0042 -0.0134 0.0408  222 PHE A CG  
1878  C CD1 . PHE A 222 ? 0.3021 0.2533 0.2749 -0.0081 -0.0058 0.0404  222 PHE A CD1 
1879  C CD2 . PHE A 222 ? 0.2832 0.2465 0.2653 -0.0036 -0.0195 0.0381  222 PHE A CD2 
1880  C CE1 . PHE A 222 ? 0.2868 0.2455 0.2584 -0.0101 -0.0040 0.0380  222 PHE A CE1 
1881  C CE2 . PHE A 222 ? 0.3569 0.3260 0.3362 -0.0062 -0.0173 0.0350  222 PHE A CE2 
1882  C CZ  . PHE A 222 ? 0.3772 0.3439 0.3513 -0.0089 -0.0094 0.0354  222 PHE A CZ  
1883  N N   . ALA A 223 ? 0.5034 0.4272 0.4595 0.0132  -0.0295 0.0646  223 ALA A N   
1884  C CA  . ALA A 223 ? 0.4536 0.3748 0.4132 0.0204  -0.0344 0.0726  223 ALA A CA  
1885  C C   . ALA A 223 ? 0.4426 0.3797 0.4176 0.0234  -0.0441 0.0732  223 ALA A C   
1886  O O   . ALA A 223 ? 0.5040 0.4423 0.4851 0.0301  -0.0489 0.0811  223 ALA A O   
1887  C CB  . ALA A 223 ? 0.4385 0.3480 0.3770 0.0230  -0.0388 0.0807  223 ALA A CB  
1888  N N   . VAL A 224 ? 0.3647 0.3142 0.3469 0.0190  -0.0468 0.0660  224 VAL A N   
1889  C CA  . VAL A 224 ? 0.3710 0.3358 0.3708 0.0211  -0.0539 0.0656  224 VAL A CA  
1890  C C   . VAL A 224 ? 0.3102 0.2816 0.3249 0.0183  -0.0469 0.0571  224 VAL A C   
1891  O O   . VAL A 224 ? 0.3264 0.2937 0.3365 0.0136  -0.0392 0.0514  224 VAL A O   
1892  C CB  . VAL A 224 ? 0.4376 0.4114 0.4303 0.0181  -0.0655 0.0655  224 VAL A CB  
1893  C CG1 . VAL A 224 ? 0.5304 0.5003 0.5107 0.0211  -0.0745 0.0750  224 VAL A CG1 
1894  C CG2 . VAL A 224 ? 0.5065 0.4762 0.4842 0.0110  -0.0619 0.0583  224 VAL A CG2 
1895  N N   . SER A 225 ? 0.3264 0.3088 0.3593 0.0211  -0.0499 0.0569  225 SER A N   
1896  C CA  . SER A 225 ? 0.2935 0.2820 0.3396 0.0186  -0.0440 0.0491  225 SER A CA  
1897  C C   . SER A 225 ? 0.2975 0.2973 0.3438 0.0142  -0.0492 0.0434  225 SER A C   
1898  O O   . SER A 225 ? 0.3057 0.3136 0.3535 0.0146  -0.0585 0.0460  225 SER A O   
1899  C CB  . SER A 225 ? 0.3417 0.3334 0.4071 0.0244  -0.0418 0.0518  225 SER A CB  
1900  O OG  . SER A 225 ? 0.2886 0.2836 0.3640 0.0217  -0.0353 0.0441  225 SER A OG  
1901  N N   . PHE A 226 ? 0.3039 0.3045 0.3487 0.0095  -0.0431 0.0361  226 PHE A N   
1902  C CA  . PHE A 226 ? 0.3302 0.3400 0.3766 0.0061  -0.0455 0.0306  226 PHE A CA  
1903  C C   . PHE A 226 ? 0.3441 0.3610 0.4068 0.0064  -0.0414 0.0257  226 PHE A C   
1904  O O   . PHE A 226 ? 0.2612 0.2847 0.3255 0.0037  -0.0414 0.0207  226 PHE A O   
1905  C CB  . PHE A 226 ? 0.3777 0.3840 0.4099 0.0016  -0.0413 0.0270  226 PHE A CB  
1906  C CG  . PHE A 226 ? 0.3535 0.3520 0.3673 0.0005  -0.0447 0.0308  226 PHE A CG  
1907  C CD1 . PHE A 226 ? 0.3205 0.3208 0.3260 -0.0015 -0.0514 0.0306  226 PHE A CD1 
1908  C CD2 . PHE A 226 ? 0.3628 0.3507 0.3661 0.0007  -0.0404 0.0341  226 PHE A CD2 
1909  C CE1 . PHE A 226 ? 0.3940 0.3844 0.3790 -0.0034 -0.0539 0.0336  226 PHE A CE1 
1910  C CE2 . PHE A 226 ? 0.3743 0.3528 0.3584 -0.0003 -0.0424 0.0375  226 PHE A CE2 
1911  C CZ  . PHE A 226 ? 0.3623 0.3416 0.3365 -0.0023 -0.0492 0.0372  226 PHE A CZ  
1912  N N   . ARG A 227 ? 0.2688 0.2824 0.3421 0.0097  -0.0369 0.0271  227 ARG A N   
1913  C CA  . ARG A 227 ? 0.3623 0.3789 0.4478 0.0094  -0.0311 0.0221  227 ARG A CA  
1914  C C   . ARG A 227 ? 0.3495 0.3771 0.4480 0.0112  -0.0357 0.0213  227 ARG A C   
1915  O O   . ARG A 227 ? 0.3628 0.3946 0.4663 0.0091  -0.0323 0.0156  227 ARG A O   
1916  C CB  . ARG A 227 ? 0.4029 0.4102 0.4946 0.0124  -0.0241 0.0241  227 ARG A CB  
1917  C CG  . ARG A 227 ? 0.4016 0.3972 0.4813 0.0091  -0.0179 0.0236  227 ARG A CG  
1918  C CD  . ARG A 227 ? 0.2698 0.2533 0.3542 0.0115  -0.0095 0.0251  227 ARG A CD  
1919  N NE  . ARG A 227 ? 0.3126 0.2968 0.4068 0.0110  -0.0039 0.0202  227 ARG A NE  
1920  C CZ  . ARG A 227 ? 0.3968 0.3778 0.4862 0.0043  0.0022  0.0130  227 ARG A CZ  
1921  N NH1 . ARG A 227 ? 0.4455 0.4251 0.5231 -0.0024 0.0031  0.0103  227 ARG A NH1 
1922  N NH2 . ARG A 227 ? 0.4042 0.3839 0.5005 0.0041  0.0075  0.0089  227 ARG A NH2 
1923  N N   . GLU A 228 ? 0.3074 0.3404 0.4122 0.0147  -0.0434 0.0274  228 GLU A N   
1924  C CA  . GLU A 228 ? 0.3711 0.4163 0.4897 0.0151  -0.0478 0.0265  228 GLU A CA  
1925  C C   . GLU A 228 ? 0.3481 0.3981 0.4567 0.0093  -0.0523 0.0218  228 GLU A C   
1926  O O   . GLU A 228 ? 0.3198 0.3769 0.4367 0.0075  -0.0518 0.0176  228 GLU A O   
1927  C CB  . GLU A 228 ? 0.5226 0.5752 0.6540 0.0203  -0.0551 0.0352  228 GLU A CB  
1928  C CG  . GLU A 228 ? 0.6845 0.7343 0.8327 0.0273  -0.0478 0.0393  228 GLU A CG  
1929  C CD  . GLU A 228 ? 0.8159 0.8632 0.9723 0.0264  -0.0376 0.0320  228 GLU A CD  
1930  O OE1 . GLU A 228 ? 0.8543 0.8896 1.0011 0.0242  -0.0289 0.0272  228 GLU A OE1 
1931  O OE2 . GLU A 228 ? 0.8387 0.8962 1.0107 0.0272  -0.0384 0.0311  228 GLU A OE2 
1932  N N   . ASP A 229 ? 0.2881 0.3326 0.3782 0.0062  -0.0552 0.0224  229 ASP A N   
1933  C CA  . ASP A 229 ? 0.3031 0.3482 0.3814 0.0008  -0.0562 0.0175  229 ASP A CA  
1934  C C   . ASP A 229 ? 0.3135 0.3577 0.3923 -0.0005 -0.0471 0.0110  229 ASP A C   
1935  O O   . ASP A 229 ? 0.3155 0.3632 0.3938 -0.0032 -0.0462 0.0065  229 ASP A O   
1936  C CB  . ASP A 229 ? 0.2243 0.2607 0.2813 -0.0016 -0.0585 0.0197  229 ASP A CB  
1937  C CG  . ASP A 229 ? 0.2376 0.2761 0.2889 -0.0030 -0.0693 0.0246  229 ASP A CG  
1938  O OD1 . ASP A 229 ? 0.2753 0.3244 0.3415 -0.0019 -0.0758 0.0269  229 ASP A OD1 
1939  O OD2 . ASP A 229 ? 0.3491 0.3787 0.3808 -0.0053 -0.0713 0.0265  229 ASP A OD2 
1940  N N   . ALA A 230 ? 0.2473 0.2868 0.3262 0.0008  -0.0405 0.0104  230 ALA A N   
1941  C CA  . ALA A 230 ? 0.2832 0.3236 0.3624 -0.0009 -0.0331 0.0051  230 ALA A CA  
1942  C C   . ALA A 230 ? 0.2546 0.3009 0.3476 0.0000  -0.0314 0.0016  230 ALA A C   
1943  O O   . ALA A 230 ? 0.2696 0.3187 0.3610 -0.0016 -0.0286 -0.0026 230 ALA A O   
1944  C CB  . ALA A 230 ? 0.3137 0.3489 0.3913 -0.0012 -0.0274 0.0052  230 ALA A CB  
1945  N N   . SER A 231 ? 0.2721 0.3197 0.3787 0.0032  -0.0325 0.0039  231 SER A N   
1946  C CA  . SER A 231 ? 0.3183 0.3713 0.4393 0.0045  -0.0303 0.0012  231 SER A CA  
1947  C C   . SER A 231 ? 0.2830 0.3433 0.4055 0.0022  -0.0353 -0.0002 231 SER A C   
1948  O O   . SER A 231 ? 0.2558 0.3191 0.3837 0.0012  -0.0315 -0.0046 231 SER A O   
1949  C CB  . SER A 231 ? 0.2832 0.3365 0.4198 0.0092  -0.0301 0.0056  231 SER A CB  
1950  O OG  . SER A 231 ? 0.3564 0.4009 0.4929 0.0102  -0.0217 0.0040  231 SER A OG  
1951  N N   . LYS A 232 ? 0.2775 0.3400 0.3944 0.0007  -0.0436 0.0034  232 LYS A N   
1952  C CA  . LYS A 232 ? 0.2956 0.3643 0.4131 -0.0032 -0.0486 0.0017  232 LYS A CA  
1953  C C   . LYS A 232 ? 0.2428 0.3065 0.3457 -0.0070 -0.0436 -0.0040 232 LYS A C   
1954  O O   . LYS A 232 ? 0.2744 0.3410 0.3805 -0.0097 -0.0421 -0.0079 232 LYS A O   
1955  C CB  . LYS A 232 ? 0.4245 0.4961 0.5371 -0.0051 -0.0594 0.0070  232 LYS A CB  
1956  C CG  . LYS A 232 ? 0.5086 0.5905 0.6293 -0.0095 -0.0663 0.0063  232 LYS A CG  
1957  C CD  . LYS A 232 ? 0.5703 0.6592 0.6917 -0.0109 -0.0788 0.0132  232 LYS A CD  
1958  C CE  . LYS A 232 ? 0.5991 0.7002 0.7295 -0.0172 -0.0860 0.0120  232 LYS A CE  
1959  N NZ  . LYS A 232 ? 0.5876 0.6976 0.7172 -0.0200 -0.1000 0.0190  232 LYS A NZ  
1960  N N   . HIS A 233 ? 0.2213 0.2775 0.3092 -0.0070 -0.0401 -0.0039 233 HIS A N   
1961  C CA  . HIS A 233 ? 0.2536 0.3057 0.3297 -0.0089 -0.0336 -0.0078 233 HIS A CA  
1962  C C   . HIS A 233 ? 0.2868 0.3421 0.3727 -0.0074 -0.0268 -0.0119 233 HIS A C   
1963  O O   . HIS A 233 ? 0.2482 0.3028 0.3310 -0.0090 -0.0231 -0.0153 233 HIS A O   
1964  C CB  . HIS A 233 ? 0.2813 0.3276 0.3445 -0.0080 -0.0299 -0.0059 233 HIS A CB  
1965  C CG  . HIS A 233 ? 0.2673 0.3069 0.3150 -0.0101 -0.0337 -0.0029 233 HIS A CG  
1966  N ND1 . HIS A 233 ? 0.2859 0.3190 0.3185 -0.0130 -0.0314 -0.0043 233 HIS A ND1 
1967  C CD2 . HIS A 233 ? 0.2521 0.2883 0.2954 -0.0095 -0.0381 0.0016  233 HIS A CD2 
1968  C CE1 . HIS A 233 ? 0.3023 0.3282 0.3211 -0.0146 -0.0347 -0.0011 233 HIS A CE1 
1969  N NE2 . HIS A 233 ? 0.2820 0.3101 0.3072 -0.0123 -0.0391 0.0027  233 HIS A NE2 
1970  N N   . VAL A 234 ? 0.2376 0.2946 0.3340 -0.0045 -0.0245 -0.0116 234 VAL A N   
1971  C CA  . VAL A 234 ? 0.2467 0.3048 0.3497 -0.0034 -0.0176 -0.0154 234 VAL A CA  
1972  C C   . VAL A 234 ? 0.2538 0.3163 0.3701 -0.0037 -0.0184 -0.0174 234 VAL A C   
1973  O O   . VAL A 234 ? 0.2850 0.3473 0.4009 -0.0047 -0.0138 -0.0210 234 VAL A O   
1974  C CB  . VAL A 234 ? 0.1797 0.2358 0.2867 -0.0016 -0.0141 -0.0151 234 VAL A CB  
1975  C CG1 . VAL A 234 ? 0.1707 0.2262 0.2803 -0.0012 -0.0069 -0.0192 234 VAL A CG1 
1976  C CG2 . VAL A 234 ? 0.2121 0.2656 0.3073 -0.0026 -0.0140 -0.0131 234 VAL A CG2 
1977  N N   . GLU A 235 ? 0.2980 0.3647 0.4266 -0.0028 -0.0240 -0.0142 235 GLU A N   
1978  C CA  . GLU A 235 ? 0.3257 0.3993 0.4705 -0.0032 -0.0250 -0.0151 235 GLU A CA  
1979  C C   . GLU A 235 ? 0.2889 0.3644 0.4280 -0.0084 -0.0272 -0.0180 235 GLU A C   
1980  O O   . GLU A 235 ? 0.2817 0.3584 0.4270 -0.0097 -0.0224 -0.0218 235 GLU A O   
1981  C CB  . GLU A 235 ? 0.4061 0.4863 0.5657 -0.0009 -0.0316 -0.0092 235 GLU A CB  
1982  C CG  . GLU A 235 ? 0.5572 0.6453 0.7391 0.0008  -0.0297 -0.0089 235 GLU A CG  
1983  C CD  . GLU A 235 ? 0.6610 0.7424 0.8478 0.0043  -0.0184 -0.0121 235 GLU A CD  
1984  O OE1 . GLU A 235 ? 0.6970 0.7720 0.8834 0.0080  -0.0149 -0.0100 235 GLU A OE1 
1985  O OE2 . GLU A 235 ? 0.6904 0.7715 0.8798 0.0028  -0.0127 -0.0168 235 GLU A OE2 
1986  N N   . LEU A 236 ? 0.2613 0.3351 0.3871 -0.0119 -0.0335 -0.0164 236 LEU A N   
1987  C CA  . LEU A 236 ? 0.2775 0.3503 0.3949 -0.0181 -0.0349 -0.0197 236 LEU A CA  
1988  C C   . LEU A 236 ? 0.2426 0.3069 0.3483 -0.0183 -0.0246 -0.0245 236 LEU A C   
1989  O O   . LEU A 236 ? 0.2699 0.3327 0.3742 -0.0225 -0.0216 -0.0286 236 LEU A O   
1990  C CB  . LEU A 236 ? 0.3496 0.4192 0.4513 -0.0222 -0.0429 -0.0171 236 LEU A CB  
1991  C CG  . LEU A 236 ? 0.3371 0.4158 0.4479 -0.0230 -0.0547 -0.0115 236 LEU A CG  
1992  C CD1 . LEU A 236 ? 0.2999 0.3717 0.3903 -0.0258 -0.0608 -0.0087 236 LEU A CD1 
1993  C CD2 . LEU A 236 ? 0.3408 0.4304 0.4650 -0.0284 -0.0604 -0.0124 236 LEU A CD2 
1994  N N   . ALA A 237 ? 0.2173 0.2765 0.3149 -0.0140 -0.0190 -0.0238 237 ALA A N   
1995  C CA  . ALA A 237 ? 0.2365 0.2898 0.3249 -0.0127 -0.0092 -0.0266 237 ALA A CA  
1996  C C   . ALA A 237 ? 0.3191 0.3746 0.4195 -0.0114 -0.0033 -0.0300 237 ALA A C   
1997  O O   . ALA A 237 ? 0.3078 0.3587 0.4030 -0.0125 0.0035  -0.0332 237 ALA A O   
1998  C CB  . ALA A 237 ? 0.1653 0.2169 0.2462 -0.0086 -0.0060 -0.0239 237 ALA A CB  
1999  N N   . LYS A 238 ? 0.2147 0.2754 0.3302 -0.0088 -0.0045 -0.0292 238 LYS A N   
2000  C CA  . LYS A 238 ? 0.2070 0.2687 0.3346 -0.0075 0.0015  -0.0321 238 LYS A CA  
2001  C C   . LYS A 238 ? 0.1866 0.2512 0.3221 -0.0120 0.0009  -0.0348 238 LYS A C   
2002  O O   . LYS A 238 ? 0.2713 0.3330 0.4091 -0.0122 0.0086  -0.0384 238 LYS A O   
2003  C CB  . LYS A 238 ? 0.3205 0.3855 0.4626 -0.0043 0.0005  -0.0301 238 LYS A CB  
2004  C CG  . LYS A 238 ? 0.3044 0.3648 0.4385 -0.0014 0.0036  -0.0292 238 LYS A CG  
2005  C CD  . LYS A 238 ? 0.3140 0.3744 0.4601 0.0011  0.0034  -0.0273 238 LYS A CD  
2006  C CE  . LYS A 238 ? 0.3438 0.4045 0.5056 0.0026  0.0093  -0.0292 238 LYS A CE  
2007  N NZ  . LYS A 238 ? 0.3578 0.4153 0.5295 0.0058  0.0118  -0.0270 238 LYS A NZ  
2008  N N   . GLU A 239 ? 0.1875 0.2581 0.3273 -0.0161 -0.0084 -0.0329 239 GLU A N   
2009  C CA  . GLU A 239 ? 0.1699 0.2451 0.3173 -0.0224 -0.0105 -0.0355 239 GLU A CA  
2010  C C   . GLU A 239 ? 0.2445 0.3096 0.3734 -0.0272 -0.0050 -0.0399 239 GLU A C   
2011  O O   . GLU A 239 ? 0.2773 0.3409 0.4100 -0.0307 0.0005  -0.0440 239 GLU A O   
2012  C CB  . GLU A 239 ? 0.2969 0.3821 0.4512 -0.0266 -0.0234 -0.0316 239 GLU A CB  
2013  C CG  . GLU A 239 ? 0.4526 0.5478 0.6258 -0.0214 -0.0287 -0.0257 239 GLU A CG  
2014  C CD  . GLU A 239 ? 0.5646 0.6699 0.7421 -0.0248 -0.0422 -0.0205 239 GLU A CD  
2015  O OE1 . GLU A 239 ? 0.5417 0.6518 0.7277 -0.0195 -0.0467 -0.0144 239 GLU A OE1 
2016  O OE2 . GLU A 239 ? 0.5988 0.7065 0.7699 -0.0331 -0.0478 -0.0224 239 GLU A OE2 
2017  N N   . LYS A 240 ? 0.1949 0.2520 0.3036 -0.0274 -0.0056 -0.0388 240 LYS A N   
2018  C CA  . LYS A 240 ? 0.2758 0.3208 0.3658 -0.0311 0.0016  -0.0424 240 LYS A CA  
2019  C C   . LYS A 240 ? 0.2839 0.3225 0.3717 -0.0259 0.0144  -0.0444 240 LYS A C   
2020  O O   . LYS A 240 ? 0.2935 0.3243 0.3754 -0.0290 0.0222  -0.0483 240 LYS A O   
2021  C CB  . LYS A 240 ? 0.2683 0.3051 0.3377 -0.0311 0.0003  -0.0399 240 LYS A CB  
2022  C CG  . LYS A 240 ? 0.3361 0.3584 0.3853 -0.0359 0.0081  -0.0434 240 LYS A CG  
2023  C CD  . LYS A 240 ? 0.3685 0.3902 0.4149 -0.0472 0.0016  -0.0471 240 LYS A CD  
2024  C CE  . LYS A 240 ? 0.3880 0.3923 0.4144 -0.0527 0.0124  -0.0519 240 LYS A CE  
2025  N NZ  . LYS A 240 ? 0.3613 0.3640 0.3834 -0.0659 0.0068  -0.0566 240 LYS A NZ  
2026  N N   . TYR A 241 ? 0.2707 0.3116 0.3617 -0.0185 0.0167  -0.0416 241 TYR A N   
2027  C CA  . TYR A 241 ? 0.2537 0.2898 0.3423 -0.0135 0.0276  -0.0427 241 TYR A CA  
2028  C C   . TYR A 241 ? 0.2835 0.3210 0.3861 -0.0151 0.0318  -0.0466 241 TYR A C   
2029  O O   . TYR A 241 ? 0.2767 0.3066 0.3740 -0.0144 0.0418  -0.0491 241 TYR A O   
2030  C CB  . TYR A 241 ? 0.2374 0.2773 0.3268 -0.0073 0.0272  -0.0391 241 TYR A CB  
2031  C CG  . TYR A 241 ? 0.2813 0.3174 0.3654 -0.0022 0.0367  -0.0390 241 TYR A CG  
2032  C CD1 . TYR A 241 ? 0.2119 0.2478 0.3053 -0.0009 0.0414  -0.0415 241 TYR A CD1 
2033  C CD2 . TYR A 241 ? 0.2193 0.2522 0.2892 0.0016  0.0415  -0.0356 241 TYR A CD2 
2034  C CE1 . TYR A 241 ? 0.2267 0.2585 0.3132 0.0036  0.0497  -0.0411 241 TYR A CE1 
2035  C CE2 . TYR A 241 ? 0.2394 0.2706 0.3046 0.0066  0.0493  -0.0343 241 TYR A CE2 
2036  C CZ  . TYR A 241 ? 0.2398 0.2701 0.3122 0.0073  0.0530  -0.0372 241 TYR A CZ  
2037  O OH  . TYR A 241 ? 0.2936 0.3215 0.3593 0.0120  0.0604  -0.0356 241 TYR A OH  
2038  N N   . PHE A 242 ? 0.2584 0.3055 0.3795 -0.0168 0.0251  -0.0464 242 PHE A N   
2039  C CA  . PHE A 242 ? 0.2752 0.3246 0.4121 -0.0183 0.0297  -0.0495 242 PHE A CA  
2040  C C   . PHE A 242 ? 0.2332 0.2790 0.3673 -0.0258 0.0324  -0.0537 242 PHE A C   
2041  O O   . PHE A 242 ? 0.2921 0.3330 0.4293 -0.0265 0.0418  -0.0572 242 PHE A O   
2042  C CB  . PHE A 242 ? 0.1631 0.2246 0.3222 -0.0182 0.0223  -0.0472 242 PHE A CB  
2043  C CG  . PHE A 242 ? 0.1836 0.2487 0.3617 -0.0194 0.0277  -0.0495 242 PHE A CG  
2044  C CD1 . PHE A 242 ? 0.1675 0.2396 0.3564 -0.0269 0.0245  -0.0514 242 PHE A CD1 
2045  C CD2 . PHE A 242 ? 0.2277 0.2886 0.4116 -0.0137 0.0366  -0.0501 242 PHE A CD2 
2046  C CE1 . PHE A 242 ? 0.1674 0.2438 0.3757 -0.0283 0.0303  -0.0533 242 PHE A CE1 
2047  C CE2 . PHE A 242 ? 0.2187 0.2815 0.4198 -0.0145 0.0433  -0.0521 242 PHE A CE2 
2048  C CZ  . PHE A 242 ? 0.2237 0.2950 0.4384 -0.0215 0.0404  -0.0536 242 PHE A CZ  
2049  N N   . GLU A 243 ? 0.2481 0.2950 0.3750 -0.0324 0.0245  -0.0537 243 GLU A N   
2050  C CA  . GLU A 243 ? 0.3118 0.3530 0.4322 -0.0414 0.0272  -0.0584 243 GLU A CA  
2051  C C   . GLU A 243 ? 0.3060 0.3302 0.4071 -0.0393 0.0413  -0.0611 243 GLU A C   
2052  O O   . GLU A 243 ? 0.2669 0.2844 0.3678 -0.0437 0.0497  -0.0656 243 GLU A O   
2053  C CB  . GLU A 243 ? 0.3402 0.3829 0.4508 -0.0492 0.0164  -0.0577 243 GLU A CB  
2054  C CG  . GLU A 243 ? 0.3601 0.3964 0.4624 -0.0611 0.0181  -0.0633 243 GLU A CG  
2055  C CD  . GLU A 243 ? 0.4325 0.4592 0.5110 -0.0676 0.0136  -0.0637 243 GLU A CD  
2056  O OE1 . GLU A 243 ? 0.4983 0.5136 0.5629 -0.0772 0.0185  -0.0690 243 GLU A OE1 
2057  O OE2 . GLU A 243 ? 0.4276 0.4563 0.4999 -0.0637 0.0065  -0.0591 243 GLU A OE2 
2058  N N   . ILE A 244 ? 0.2819 0.2993 0.3675 -0.0324 0.0445  -0.0577 244 ILE A N   
2059  C CA  . ILE A 244 ? 0.3424 0.3441 0.4091 -0.0298 0.0577  -0.0586 244 ILE A CA  
2060  C C   . ILE A 244 ? 0.3274 0.3265 0.3982 -0.0224 0.0681  -0.0584 244 ILE A C   
2061  O O   . ILE A 244 ? 0.3515 0.3385 0.4135 -0.0222 0.0803  -0.0607 244 ILE A O   
2062  C CB  . ILE A 244 ? 0.3380 0.3345 0.3873 -0.0254 0.0575  -0.0541 244 ILE A CB  
2063  C CG1 . ILE A 244 ? 0.2958 0.2922 0.3383 -0.0335 0.0479  -0.0547 244 ILE A CG1 
2064  C CG2 . ILE A 244 ? 0.3428 0.3231 0.3736 -0.0219 0.0723  -0.0537 244 ILE A CG2 
2065  C CD1 . ILE A 244 ? 0.3338 0.3190 0.3661 -0.0441 0.0517  -0.0605 244 ILE A CD1 
2066  N N   . PHE A 245 ? 0.2915 0.3001 0.3734 -0.0163 0.0643  -0.0555 245 PHE A N   
2067  C CA  . PHE A 245 ? 0.3109 0.3161 0.3923 -0.0090 0.0736  -0.0545 245 PHE A CA  
2068  C C   . PHE A 245 ? 0.3384 0.3491 0.4382 -0.0093 0.0737  -0.0569 245 PHE A C   
2069  O O   . PHE A 245 ? 0.3393 0.3454 0.4374 -0.0041 0.0819  -0.0567 245 PHE A O   
2070  C CB  . PHE A 245 ? 0.2264 0.2347 0.2996 -0.0015 0.0717  -0.0488 245 PHE A CB  
2071  C CG  . PHE A 245 ? 0.3003 0.3034 0.3570 0.0002  0.0738  -0.0453 245 PHE A CG  
2072  C CD1 . PHE A 245 ? 0.3345 0.3257 0.3776 0.0036  0.0862  -0.0444 245 PHE A CD1 
2073  C CD2 . PHE A 245 ? 0.3383 0.3466 0.3926 -0.0012 0.0647  -0.0427 245 PHE A CD2 
2074  C CE1 . PHE A 245 ? 0.3566 0.3417 0.3851 0.0059  0.0901  -0.0406 245 PHE A CE1 
2075  C CE2 . PHE A 245 ? 0.3159 0.3180 0.3551 0.0007  0.0683  -0.0392 245 PHE A CE2 
2076  C CZ  . PHE A 245 ? 0.3780 0.3686 0.4047 0.0044  0.0812  -0.0381 245 PHE A CZ  
2077  N N   . GLY A 246 ? 0.2607 0.4848 0.3940 -0.0714 0.0866  0.0180  246 GLY A N   
2078  C CA  . GLY A 246 ? 0.2635 0.5049 0.3920 -0.0709 0.0894  0.0151  246 GLY A CA  
2079  C C   . GLY A 246 ? 0.2380 0.4900 0.3603 -0.0648 0.0889  0.0124  246 GLY A C   
2080  O O   . GLY A 246 ? 0.1778 0.4431 0.2947 -0.0655 0.0925  0.0107  246 GLY A O   
2081  N N   . GLU A 247 ? 0.2691 0.5159 0.3918 -0.0591 0.0849  0.0118  247 GLU A N   
2082  C CA  . GLU A 247 ? 0.2934 0.5503 0.4115 -0.0521 0.0840  0.0082  247 GLU A CA  
2083  C C   . GLU A 247 ? 0.2383 0.4909 0.3620 -0.0449 0.0786  0.0054  247 GLU A C   
2084  O O   . GLU A 247 ? 0.2522 0.4917 0.3806 -0.0471 0.0758  0.0079  247 GLU A O   
2085  C CB  . GLU A 247 ? 0.3204 0.5749 0.4285 -0.0555 0.0852  0.0133  247 GLU A CB  
2086  C CG  . GLU A 247 ? 0.4083 0.6566 0.5113 -0.0661 0.0883  0.0214  247 GLU A CG  
2087  C CD  . GLU A 247 ? 0.4436 0.6872 0.5375 -0.0701 0.0870  0.0291  247 GLU A CD  
2088  O OE1 . GLU A 247 ? 0.3979 0.6317 0.4961 -0.0684 0.0825  0.0324  247 GLU A OE1 
2089  O OE2 . GLU A 247 ? 0.5188 0.7694 0.6010 -0.0756 0.0900  0.0323  247 GLU A OE2 
2090  N N   . HIS A 248 ? 0.2170 0.4806 0.3405 -0.0364 0.0774  -0.0002 248 HIS A N   
2091  C CA  . HIS A 248 ? 0.2328 0.4914 0.3603 -0.0304 0.0720  -0.0014 248 HIS A CA  
2092  C C   . HIS A 248 ? 0.1884 0.4376 0.3107 -0.0328 0.0708  0.0034  248 HIS A C   
2093  O O   . HIS A 248 ? 0.2264 0.4793 0.3405 -0.0356 0.0739  0.0057  248 HIS A O   
2094  C CB  . HIS A 248 ? 0.2562 0.5286 0.3870 -0.0194 0.0706  -0.0090 248 HIS A CB  
2095  C CG  . HIS A 248 ? 0.3697 0.6517 0.5091 -0.0165 0.0697  -0.0125 248 HIS A CG  
2096  N ND1 . HIS A 248 ? 0.4307 0.7283 0.5726 -0.0122 0.0731  -0.0179 248 HIS A ND1 
2097  C CD2 . HIS A 248 ? 0.3987 0.6782 0.5449 -0.0182 0.0658  -0.0111 248 HIS A CD2 
2098  C CE1 . HIS A 248 ? 0.4012 0.7062 0.5525 -0.0109 0.0708  -0.0191 248 HIS A CE1 
2099  N NE2 . HIS A 248 ? 0.4227 0.7173 0.5758 -0.0148 0.0663  -0.0149 248 HIS A NE2 
2100  N N   . PRO A 249 ? 0.1766 0.4145 0.3033 -0.0329 0.0663  0.0057  249 PRO A N   
2101  C CA  . PRO A 249 ? 0.2045 0.4259 0.3257 -0.0347 0.0630  0.0111  249 PRO A CA  
2102  C C   . PRO A 249 ? 0.2189 0.4336 0.3294 -0.0265 0.0583  0.0082  249 PRO A C   
2103  O O   . PRO A 249 ? 0.2764 0.4912 0.3876 -0.0184 0.0549  0.0025  249 PRO A O   
2104  C CB  . PRO A 249 ? 0.1728 0.3826 0.3024 -0.0367 0.0596  0.0124  249 PRO A CB  
2105  C CG  . PRO A 249 ? 0.1323 0.3528 0.2676 -0.0326 0.0587  0.0066  249 PRO A CG  
2106  C CD  . PRO A 249 ? 0.1497 0.3823 0.2837 -0.0318 0.0627  0.0038  249 PRO A CD  
2107  N N   . VAL A 250 ? 0.2470 0.4552 0.3472 -0.0291 0.0578  0.0123  250 VAL A N   
2108  C CA  . VAL A 250 ? 0.2752 0.4758 0.3642 -0.0228 0.0531  0.0091  250 VAL A CA  
2109  C C   . VAL A 250 ? 0.2338 0.4151 0.3216 -0.0233 0.0459  0.0139  250 VAL A C   
2110  O O   . VAL A 250 ? 0.2108 0.3837 0.2904 -0.0184 0.0409  0.0108  250 VAL A O   
2111  C CB  . VAL A 250 ? 0.3065 0.5150 0.3821 -0.0252 0.0568  0.0087  250 VAL A CB  
2112  C CG1 . VAL A 250 ? 0.2885 0.5182 0.3667 -0.0230 0.0644  0.0013  250 VAL A CG1 
2113  C CG2 . VAL A 250 ? 0.3035 0.5084 0.3754 -0.0352 0.0575  0.0192  250 VAL A CG2 
2114  N N   . TYR A 251 ? 0.1559 0.3305 0.2530 -0.0291 0.0453  0.0203  251 TYR A N   
2115  C CA  . TYR A 251 ? 0.1446 0.3034 0.2451 -0.0295 0.0392  0.0240  251 TYR A CA  
2116  C C   . TYR A 251 ? 0.1852 0.3415 0.2981 -0.0297 0.0394  0.0215  251 TYR A C   
2117  O O   . TYR A 251 ? 0.2010 0.3651 0.3223 -0.0336 0.0446  0.0212  251 TYR A O   
2118  C CB  . TYR A 251 ? 0.2244 0.3768 0.3273 -0.0362 0.0382  0.0335  251 TYR A CB  
2119  C CG  . TYR A 251 ? 0.3128 0.4705 0.4024 -0.0389 0.0390  0.0375  251 TYR A CG  
2120  C CD1 . TYR A 251 ? 0.3914 0.5443 0.4677 -0.0370 0.0335  0.0378  251 TYR A CD1 
2121  C CD2 . TYR A 251 ? 0.4078 0.5759 0.4968 -0.0445 0.0454  0.0403  251 TYR A CD2 
2122  C CE1 . TYR A 251 ? 0.4681 0.6269 0.5300 -0.0409 0.0344  0.0409  251 TYR A CE1 
2123  C CE2 . TYR A 251 ? 0.4474 0.6214 0.5223 -0.0484 0.0465  0.0440  251 TYR A CE2 
2124  C CZ  . TYR A 251 ? 0.4774 0.6469 0.5381 -0.0466 0.0410  0.0441  251 TYR A CZ  
2125  O OH  . TYR A 251 ? 0.4712 0.6475 0.5156 -0.0519 0.0424  0.0472  251 TYR A OH  
2126  N N   . MET A 252 ? 0.1322 0.2779 0.2455 -0.0269 0.0340  0.0198  252 MET A N   
2127  C CA  . MET A 252 ? 0.1158 0.2583 0.2395 -0.0292 0.0343  0.0183  252 MET A CA  
2128  C C   . MET A 252 ? 0.1843 0.3139 0.3117 -0.0308 0.0297  0.0208  252 MET A C   
2129  O O   . MET A 252 ? 0.2216 0.3442 0.3416 -0.0282 0.0245  0.0222  252 MET A O   
2130  C CB  . MET A 252 ? 0.1899 0.3359 0.3113 -0.0246 0.0326  0.0125  252 MET A CB  
2131  C CG  . MET A 252 ? 0.2467 0.4081 0.3717 -0.0248 0.0375  0.0100  252 MET A CG  
2132  S SD  . MET A 252 ? 0.2672 0.4329 0.3937 -0.0211 0.0342  0.0057  252 MET A SD  
2133  C CE  . MET A 252 ? 0.2578 0.4452 0.3903 -0.0223 0.0403  0.0038  252 MET A CE  
2134  N N   . TRP A 253 ? 0.2056 0.3331 0.3451 -0.0358 0.0322  0.0207  253 TRP A N   
2135  C CA  . TRP A 253 ? 0.1463 0.2641 0.2919 -0.0374 0.0289  0.0211  253 TRP A CA  
2136  C C   . TRP A 253 ? 0.1926 0.3093 0.3364 -0.0377 0.0278  0.0160  253 TRP A C   
2137  O O   . TRP A 253 ? 0.1647 0.2877 0.3131 -0.0414 0.0323  0.0131  253 TRP A O   
2138  C CB  . TRP A 253 ? 0.1173 0.2333 0.2792 -0.0429 0.0329  0.0233  253 TRP A CB  
2139  C CG  . TRP A 253 ? 0.1166 0.2260 0.2877 -0.0451 0.0313  0.0212  253 TRP A CG  
2140  C CD1 . TRP A 253 ? 0.1436 0.2523 0.3192 -0.0493 0.0351  0.0155  253 TRP A CD1 
2141  C CD2 . TRP A 253 ? 0.1265 0.2291 0.2979 -0.0431 0.0250  0.0236  253 TRP A CD2 
2142  N NE1 . TRP A 253 ? 0.1626 0.2647 0.3418 -0.0499 0.0322  0.0141  253 TRP A NE1 
2143  C CE2 . TRP A 253 ? 0.1152 0.2155 0.2975 -0.0469 0.0264  0.0197  253 TRP A CE2 
2144  C CE3 . TRP A 253 ? 0.1825 0.2816 0.3455 -0.0394 0.0182  0.0285  253 TRP A CE3 
2145  C CZ2 . TRP A 253 ? 0.1637 0.2590 0.3504 -0.0467 0.0213  0.0206  253 TRP A CZ2 
2146  C CZ3 . TRP A 253 ? 0.2053 0.2990 0.3718 -0.0393 0.0125  0.0297  253 TRP A CZ3 
2147  C CH2 . TRP A 253 ? 0.1671 0.2592 0.3461 -0.0427 0.0140  0.0259  253 TRP A CH2 
2148  N N   . PRO A 254 ? 0.1783 0.2875 0.3145 -0.0347 0.0217  0.0150  254 PRO A N   
2149  C CA  . PRO A 254 ? 0.1632 0.2698 0.2970 -0.0362 0.0200  0.0116  254 PRO A CA  
2150  C C   . PRO A 254 ? 0.2103 0.3157 0.3555 -0.0438 0.0232  0.0103  254 PRO A C   
2151  O O   . PRO A 254 ? 0.2110 0.3116 0.3636 -0.0454 0.0224  0.0116  254 PRO A O   
2152  C CB  . PRO A 254 ? 0.1394 0.2360 0.2625 -0.0318 0.0126  0.0115  254 PRO A CB  
2153  C CG  . PRO A 254 ? 0.1726 0.2662 0.2966 -0.0308 0.0107  0.0147  254 PRO A CG  
2154  C CD  . PRO A 254 ? 0.1721 0.2745 0.3006 -0.0309 0.0159  0.0172  254 PRO A CD  
2155  N N   . PRO A 255 ? 0.1851 0.2958 0.3323 -0.0489 0.0269  0.0073  255 PRO A N   
2156  C CA  . PRO A 255 ? 0.1330 0.2435 0.2901 -0.0572 0.0312  0.0042  255 PRO A CA  
2157  C C   . PRO A 255 ? 0.1282 0.2304 0.2852 -0.0584 0.0271  0.0042  255 PRO A C   
2158  O O   . PRO A 255 ? 0.1492 0.2452 0.2944 -0.0559 0.0207  0.0052  255 PRO A O   
2159  C CB  . PRO A 255 ? 0.1580 0.2734 0.3072 -0.0615 0.0322  0.0019  255 PRO A CB  
2160  C CG  . PRO A 255 ? 0.1657 0.2898 0.3129 -0.0572 0.0327  0.0029  255 PRO A CG  
2161  C CD  . PRO A 255 ? 0.1836 0.3023 0.3249 -0.0479 0.0275  0.0062  255 PRO A CD  
2162  N N   . GLU A 256 ? 0.1053 0.2034 0.2668 -0.0595 0.0286  0.0033  256 GLU A N   
2163  C CA  . GLU A 256 ? 0.1405 0.2332 0.3046 -0.0613 0.0257  0.0028  256 GLU A CA  
2164  C C   . GLU A 256 ? 0.1401 0.2299 0.3079 -0.0575 0.0193  0.0069  256 GLU A C   
2165  O O   . GLU A 256 ? 0.1595 0.2441 0.3246 -0.0593 0.0149  0.0066  256 GLU A O   
2166  C CB  . GLU A 256 ? 0.2204 0.3115 0.3754 -0.0675 0.0250  0.0001  256 GLU A CB  
2167  C CG  . GLU A 256 ? 0.2164 0.3099 0.3645 -0.0707 0.0291  -0.0018 256 GLU A CG  
2168  C CD  . GLU A 256 ? 0.2366 0.3289 0.3898 -0.0693 0.0332  -0.0044 256 GLU A CD  
2169  O OE1 . GLU A 256 ? 0.3215 0.4152 0.4721 -0.0703 0.0368  -0.0063 256 GLU A OE1 
2170  O OE2 . GLU A 256 ? 0.2988 0.3887 0.4605 -0.0674 0.0329  -0.0049 256 GLU A OE2 
2171  N N   . ALA A 257 ? 0.1322 0.2223 0.2958 -0.0510 0.0173  0.0107  257 ALA A N   
2172  C CA  . ALA A 257 ? 0.1086 0.1930 0.2616 -0.0454 0.0098  0.0141  257 ALA A CA  
2173  C C   . ALA A 257 ? 0.1782 0.2559 0.3153 -0.0439 0.0048  0.0122  257 ALA A C   
2174  O O   . ALA A 257 ? 0.1464 0.2173 0.2751 -0.0412 -0.0014 0.0131  257 ALA A O   
2175  C CB  . ALA A 257 ? 0.1100 0.1919 0.2723 -0.0464 0.0059  0.0167  257 ALA A CB  
2176  N N   A SER A 258 ? 0.1998 0.2787 0.3326 -0.0459 0.0069  0.0098  258 SER A N   
2177  N N   B SER A 258 ? 0.1920 0.2710 0.3247 -0.0458 0.0069  0.0098  258 SER A N   
2178  C CA  A SER A 258 ? 0.2254 0.2960 0.3460 -0.0461 0.0016  0.0089  258 SER A CA  
2179  C CA  B SER A 258 ? 0.2385 0.3090 0.3590 -0.0459 0.0016  0.0089  258 SER A CA  
2180  C C   A SER A 258 ? 0.2328 0.2993 0.3409 -0.0374 -0.0027 0.0091  258 SER A C   
2181  C C   B SER A 258 ? 0.2328 0.2993 0.3409 -0.0374 -0.0028 0.0091  258 SER A C   
2182  O O   A SER A 258 ? 0.2486 0.3224 0.3561 -0.0333 0.0000  0.0088  258 SER A O   
2183  O O   B SER A 258 ? 0.2599 0.3336 0.3672 -0.0333 -0.0001 0.0088  258 SER A O   
2184  C CB  A SER A 258 ? 0.2120 0.2858 0.3324 -0.0522 0.0045  0.0074  258 SER A CB  
2185  C CB  B SER A 258 ? 0.2111 0.2845 0.3314 -0.0523 0.0043  0.0074  258 SER A CB  
2186  O OG  A SER A 258 ? 0.1975 0.2788 0.3162 -0.0490 0.0069  0.0074  258 SER A OG  
2187  O OG  B SER A 258 ? 0.2011 0.2644 0.3093 -0.0525 -0.0021 0.0082  258 SER A OG  
2188  N N   . VAL A 259 ? 0.1934 0.2488 0.2923 -0.0351 -0.0091 0.0087  259 VAL A N   
2189  C CA  . VAL A 259 ? 0.2281 0.2782 0.3158 -0.0268 -0.0128 0.0071  259 VAL A CA  
2190  C C   . VAL A 259 ? 0.2863 0.3214 0.3646 -0.0273 -0.0195 0.0061  259 VAL A C   
2191  O O   . VAL A 259 ? 0.2812 0.3105 0.3603 -0.0345 -0.0215 0.0072  259 VAL A O   
2192  C CB  . VAL A 259 ? 0.2082 0.2596 0.2928 -0.0229 -0.0134 0.0067  259 VAL A CB  
2193  C CG1 . VAL A 259 ? 0.1960 0.2606 0.2890 -0.0231 -0.0074 0.0089  259 VAL A CG1 
2194  C CG2 . VAL A 259 ? 0.1863 0.2313 0.2711 -0.0276 -0.0175 0.0078  259 VAL A CG2 
2195  N N   . SER A 260 ? 0.1738 0.2031 0.2440 -0.0195 -0.0225 0.0039  260 SER A N   
2196  C CA  . SER A 260 ? 0.2277 0.2400 0.2885 -0.0177 -0.0293 0.0025  260 SER A CA  
2197  C C   . SER A 260 ? 0.2392 0.2491 0.2945 -0.0070 -0.0302 -0.0022 260 SER A C   
2198  O O   . SER A 260 ? 0.2920 0.3150 0.3509 -0.0021 -0.0252 -0.0037 260 SER A O   
2199  C CB  . SER A 260 ? 0.2753 0.2827 0.3354 -0.0208 -0.0321 0.0059  260 SER A CB  
2200  O OG  . SER A 260 ? 0.2421 0.2571 0.3049 -0.0140 -0.0311 0.0061  260 SER A OG  
2201  N N   . ASN A 261 ? 0.2462 0.2391 0.2929 -0.0037 -0.0359 -0.0053 261 ASN A N   
2202  C CA  . ASN A 261 ? 0.2815 0.2719 0.3244 0.0070  -0.0358 -0.0116 261 ASN A CA  
2203  C C   . ASN A 261 ? 0.2751 0.2764 0.3256 0.0144  -0.0334 -0.0112 261 ASN A C   
2204  O O   . ASN A 261 ? 0.2537 0.2665 0.3065 0.0212  -0.0287 -0.0156 261 ASN A O   
2205  C CB  . ASN A 261 ? 0.2496 0.2176 0.2839 0.0093  -0.0425 -0.0153 261 ASN A CB  
2206  C CG  . ASN A 261 ? 0.2973 0.2564 0.3234 0.0024  -0.0448 -0.0173 261 ASN A CG  
2207  O OD1 . ASN A 261 ? 0.2965 0.2668 0.3229 -0.0013 -0.0416 -0.0172 261 ASN A OD1 
2208  N ND2 . ASN A 261 ? 0.3464 0.2853 0.3657 -0.0001 -0.0510 -0.0183 261 ASN A ND2 
2209  N N   . GLU A 262 ? 0.2533 0.2529 0.3077 0.0122  -0.0365 -0.0057 262 GLU A N   
2210  C CA  . GLU A 262 ? 0.2304 0.2409 0.2925 0.0189  -0.0358 -0.0047 262 GLU A CA  
2211  C C   . GLU A 262 ? 0.2353 0.2685 0.3051 0.0164  -0.0281 -0.0036 262 GLU A C   
2212  O O   . GLU A 262 ? 0.2600 0.3065 0.3360 0.0234  -0.0251 -0.0058 262 GLU A O   
2213  C CB  . GLU A 262 ? 0.2860 0.2883 0.3482 0.0156  -0.0425 0.0021  262 GLU A CB  
2214  C CG  . GLU A 262 ? 0.3088 0.2869 0.3645 0.0194  -0.0511 0.0019  262 GLU A CG  
2215  C CD  . GLU A 262 ? 0.4112 0.3818 0.4668 0.0168  -0.0587 0.0101  262 GLU A CD  
2216  O OE1 . GLU A 262 ? 0.3590 0.3424 0.4223 0.0213  -0.0593 0.0130  262 GLU A OE1 
2217  O OE2 . GLU A 262 ? 0.4677 0.4205 0.5151 0.0093  -0.0643 0.0141  262 GLU A OE2 
2218  N N   . ALA A 263 ? 0.2658 0.3039 0.3363 0.0064  -0.0247 -0.0005 263 ALA A N   
2219  C CA  . ALA A 263 ? 0.2467 0.3040 0.3250 0.0037  -0.0174 0.0005  263 ALA A CA  
2220  C C   . ALA A 263 ? 0.2418 0.3068 0.3193 0.0084  -0.0125 -0.0037 263 ALA A C   
2221  O O   . ALA A 263 ? 0.2858 0.3665 0.3689 0.0107  -0.0072 -0.0045 263 ALA A O   
2222  C CB  . ALA A 263 ? 0.2473 0.3067 0.3288 -0.0076 -0.0148 0.0042  263 ALA A CB  
2223  N N   . LEU A 264 ? 0.1935 0.2481 0.2632 0.0089  -0.0144 -0.0063 264 LEU A N   
2224  C CA  . LEU A 264 ? 0.2345 0.2963 0.3006 0.0122  -0.0103 -0.0102 264 LEU A CA  
2225  C C   . LEU A 264 ? 0.2812 0.3494 0.3479 0.0221  -0.0082 -0.0162 264 LEU A C   
2226  O O   . LEU A 264 ? 0.2765 0.3594 0.3446 0.0237  -0.0021 -0.0184 264 LEU A O   
2227  C CB  . LEU A 264 ? 0.2233 0.2722 0.2792 0.0102  -0.0140 -0.0123 264 LEU A CB  
2228  C CG  . LEU A 264 ? 0.3024 0.3509 0.3609 0.0007  -0.0147 -0.0065 264 LEU A CG  
2229  C CD1 . LEU A 264 ? 0.3845 0.4219 0.4338 -0.0019 -0.0194 -0.0080 264 LEU A CD1 
2230  C CD2 . LEU A 264 ? 0.3060 0.3701 0.3706 -0.0018 -0.0086 -0.0031 264 LEU A CD2 
2231  N N   . GLU A 265 ? 0.2466 0.3039 0.3131 0.0287  -0.0133 -0.0190 265 GLU A N   
2232  C CA  . GLU A 265 ? 0.3040 0.3676 0.3751 0.0396  -0.0118 -0.0251 265 GLU A CA  
2233  C C   . GLU A 265 ? 0.3010 0.3847 0.3838 0.0405  -0.0080 -0.0223 265 GLU A C   
2234  O O   . GLU A 265 ? 0.3115 0.4107 0.3988 0.0459  -0.0023 -0.0273 265 GLU A O   
2235  C CB  . GLU A 265 ? 0.3776 0.4227 0.4482 0.0464  -0.0195 -0.0271 265 GLU A CB  
2236  C CG  . GLU A 265 ? 0.5946 0.6184 0.6532 0.0442  -0.0236 -0.0304 265 GLU A CG  
2237  C CD  . GLU A 265 ? 0.7470 0.7583 0.8035 0.0547  -0.0255 -0.0400 265 GLU A CD  
2238  O OE1 . GLU A 265 ? 0.7120 0.7176 0.7588 0.0543  -0.0234 -0.0474 265 GLU A OE1 
2239  O OE2 . GLU A 265 ? 0.8339 0.8409 0.8989 0.0632  -0.0293 -0.0402 265 GLU A OE2 
2240  N N   . LEU A 266 ? 0.2715 0.3565 0.3588 0.0344  -0.0105 -0.0150 266 LEU A N   
2241  C CA  . LEU A 266 ? 0.3047 0.4090 0.4024 0.0336  -0.0072 -0.0124 266 LEU A CA  
2242  C C   . LEU A 266 ? 0.2569 0.3778 0.3562 0.0292  0.0016  -0.0132 266 LEU A C   
2243  O O   . LEU A 266 ? 0.2706 0.4094 0.3772 0.0326  0.0062  -0.0156 266 LEU A O   
2244  C CB  . LEU A 266 ? 0.2776 0.3794 0.3770 0.0253  -0.0110 -0.0051 266 LEU A CB  
2245  C CG  . LEU A 266 ? 0.2678 0.3893 0.3761 0.0210  -0.0075 -0.0022 266 LEU A CG  
2246  C CD1 . LEU A 266 ? 0.3320 0.4657 0.4492 0.0306  -0.0096 -0.0040 266 LEU A CD1 
2247  C CD2 . LEU A 266 ? 0.2638 0.3820 0.3712 0.0107  -0.0104 0.0037  266 LEU A CD2 
2248  N N   . TYR A 267 ? 0.2119 0.3276 0.3055 0.0212  0.0037  -0.0107 267 TYR A N   
2249  C CA  . TYR A 267 ? 0.2434 0.3723 0.3382 0.0166  0.0111  -0.0099 267 TYR A CA  
2250  C C   . TYR A 267 ? 0.2788 0.4158 0.3698 0.0228  0.0152  -0.0161 267 TYR A C   
2251  O O   . TYR A 267 ? 0.2884 0.4427 0.3838 0.0219  0.0216  -0.0169 267 TYR A O   
2252  C CB  . TYR A 267 ? 0.2415 0.3613 0.3319 0.0084  0.0109  -0.0056 267 TYR A CB  
2253  C CG  . TYR A 267 ? 0.2250 0.3429 0.3219 0.0003  0.0106  -0.0006 267 TYR A CG  
2254  C CD1 . TYR A 267 ? 0.2562 0.3872 0.3618 -0.0044 0.0157  0.0013  267 TYR A CD1 
2255  C CD2 . TYR A 267 ? 0.2046 0.3082 0.2991 -0.0035 0.0059  0.0014  267 TYR A CD2 
2256  C CE1 . TYR A 267 ? 0.2342 0.3635 0.3456 -0.0124 0.0164  0.0042  267 TYR A CE1 
2257  C CE2 . TYR A 267 ? 0.2604 0.3634 0.3611 -0.0113 0.0067  0.0045  267 TYR A CE2 
2258  C CZ  . TYR A 267 ? 0.2930 0.4086 0.4020 -0.0156 0.0122  0.0055  267 TYR A CZ  
2259  O OH  . TYR A 267 ? 0.3010 0.4159 0.4161 -0.0239 0.0140  0.0069  267 TYR A OH  
2260  N N   . TYR A 268 ? 0.2179 0.3430 0.3005 0.0283  0.0121  -0.0213 268 TYR A N   
2261  C CA  . TYR A 268 ? 0.2515 0.3846 0.3300 0.0341  0.0168  -0.0293 268 TYR A CA  
2262  C C   . TYR A 268 ? 0.2658 0.4146 0.3561 0.0421  0.0197  -0.0339 268 TYR A C   
2263  O O   . TYR A 268 ? 0.2404 0.4073 0.3329 0.0426  0.0271  -0.0375 268 TYR A O   
2264  C CB  . TYR A 268 ? 0.2560 0.3721 0.3242 0.0386  0.0127  -0.0356 268 TYR A CB  
2265  C CG  . TYR A 268 ? 0.2861 0.4078 0.3551 0.0486  0.0162  -0.0467 268 TYR A CG  
2266  C CD1 . TYR A 268 ? 0.2926 0.4279 0.3554 0.0476  0.0241  -0.0526 268 TYR A CD1 
2267  C CD2 . TYR A 268 ? 0.3358 0.4495 0.4122 0.0588  0.0118  -0.0513 268 TYR A CD2 
2268  C CE1 . TYR A 268 ? 0.3345 0.4766 0.3992 0.0565  0.0286  -0.0646 268 TYR A CE1 
2269  C CE2 . TYR A 268 ? 0.3992 0.5180 0.4794 0.0690  0.0154  -0.0626 268 TYR A CE2 
2270  C CZ  . TYR A 268 ? 0.4263 0.5601 0.5010 0.0679  0.0245  -0.0700 268 TYR A CZ  
2271  O OH  . TYR A 268 ? 0.4351 0.5754 0.5149 0.0779  0.0292  -0.0828 268 TYR A OH  
2272  N N   . GLU A 269 ? 0.2379 0.3808 0.3361 0.0481  0.0136  -0.0332 269 GLU A N   
2273  C CA  . GLU A 269 ? 0.2146 0.3729 0.3262 0.0567  0.0148  -0.0370 269 GLU A CA  
2274  C C   . GLU A 269 ? 0.2141 0.3952 0.3341 0.0510  0.0206  -0.0334 269 GLU A C   
2275  O O   . GLU A 269 ? 0.2229 0.4233 0.3531 0.0564  0.0249  -0.0382 269 GLU A O   
2276  C CB  . GLU A 269 ? 0.3061 0.4532 0.4245 0.0627  0.0054  -0.0341 269 GLU A CB  
2277  C CG  . GLU A 269 ? 0.4260 0.5525 0.5399 0.0713  0.0001  -0.0398 269 GLU A CG  
2278  C CD  . GLU A 269 ? 0.5798 0.6895 0.6961 0.0732  -0.0106 -0.0335 269 GLU A CD  
2279  O OE1 . GLU A 269 ? 0.6029 0.6925 0.7154 0.0792  -0.0159 -0.0369 269 GLU A OE1 
2280  O OE2 . GLU A 269 ? 0.6279 0.7441 0.7490 0.0678  -0.0136 -0.0253 269 GLU A OE2 
2281  N N   . LYS A 270 ? 0.2238 0.4033 0.3408 0.0399  0.0211  -0.0257 270 LYS A N   
2282  C CA  . LYS A 270 ? 0.2802 0.4784 0.4047 0.0329  0.0263  -0.0222 270 LYS A CA  
2283  C C   . LYS A 270 ? 0.2881 0.4960 0.4077 0.0265  0.0349  -0.0226 270 LYS A C   
2284  O O   . LYS A 270 ? 0.2726 0.4920 0.3968 0.0185  0.0393  -0.0187 270 LYS A O   
2285  C CB  . LYS A 270 ? 0.2523 0.4434 0.3777 0.0240  0.0228  -0.0146 270 LYS A CB  
2286  C CG  . LYS A 270 ? 0.3137 0.5014 0.4447 0.0278  0.0149  -0.0126 270 LYS A CG  
2287  C CD  . LYS A 270 ? 0.3315 0.5388 0.4747 0.0351  0.0150  -0.0155 270 LYS A CD  
2288  C CE  . LYS A 270 ? 0.4172 0.6240 0.5662 0.0355  0.0065  -0.0106 270 LYS A CE  
2289  N NZ  . LYS A 270 ? 0.4438 0.6558 0.6029 0.0486  0.0007  -0.0132 270 LYS A NZ  
2290  N N   . GLY A 271 ? 0.2909 0.4939 0.4006 0.0288  0.0370  -0.0270 271 GLY A N   
2291  C CA  . GLY A 271 ? 0.2767 0.4899 0.3799 0.0227  0.0446  -0.0271 271 GLY A CA  
2292  C C   . GLY A 271 ? 0.2947 0.4965 0.3893 0.0127  0.0439  -0.0192 271 GLY A C   
2293  O O   . GLY A 271 ? 0.2705 0.4807 0.3610 0.0057  0.0495  -0.0164 271 GLY A O   
2294  N N   . ILE A 272 ? 0.2197 0.4034 0.3125 0.0114  0.0371  -0.0151 272 ILE A N   
2295  C CA  . ILE A 272 ? 0.2426 0.4159 0.3299 0.0032  0.0358  -0.0080 272 ILE A CA  
2296  C C   . ILE A 272 ? 0.2684 0.4338 0.3416 0.0041  0.0341  -0.0101 272 ILE A C   
2297  O O   . ILE A 272 ? 0.2352 0.3909 0.3033 0.0104  0.0299  -0.0157 272 ILE A O   
2298  C CB  . ILE A 272 ? 0.2638 0.4232 0.3560 0.0009  0.0301  -0.0038 272 ILE A CB  
2299  C CG1 . ILE A 272 ? 0.2897 0.4574 0.3937 -0.0005 0.0315  -0.0030 272 ILE A CG1 
2300  C CG2 . ILE A 272 ? 0.2499 0.4010 0.3405 -0.0070 0.0292  0.0032  272 ILE A CG2 
2301  C CD1 . ILE A 272 ? 0.3289 0.5114 0.4390 -0.0068 0.0385  -0.0006 272 ILE A CD1 
2302  N N   . ASN A 273 ? 0.2175 0.3865 0.2839 -0.0028 0.0368  -0.0055 273 ASN A N   
2303  C CA  . ASN A 273 ? 0.2956 0.4592 0.3468 -0.0034 0.0350  -0.0074 273 ASN A CA  
2304  C C   . ASN A 273 ? 0.2891 0.4378 0.3362 -0.0085 0.0280  0.0000  273 ASN A C   
2305  O O   . ASN A 273 ? 0.3037 0.4452 0.3385 -0.0085 0.0242  -0.0021 273 ASN A O   
2306  C CB  . ASN A 273 ? 0.3539 0.5321 0.3966 -0.0084 0.0418  -0.0072 273 ASN A CB  
2307  C CG  . ASN A 273 ? 0.4905 0.6857 0.5371 -0.0032 0.0492  -0.0163 273 ASN A CG  
2308  O OD1 . ASN A 273 ? 0.5333 0.7276 0.5824 0.0061  0.0486  -0.0256 273 ASN A OD1 
2309  N ND2 . ASN A 273 ? 0.5186 0.7297 0.5674 -0.0090 0.0562  -0.0134 273 ASN A ND2 
2310  N N   A MET A 274 ? 0.3003 0.4450 0.3584 -0.0128 0.0264  0.0078  274 MET A N   
2311  N N   B MET A 274 ? 0.3003 0.4450 0.3584 -0.0128 0.0264  0.0078  274 MET A N   
2312  C CA  A MET A 274 ? 0.3351 0.4673 0.3934 -0.0167 0.0197  0.0144  274 MET A CA  
2313  C CA  B MET A 274 ? 0.3351 0.4673 0.3934 -0.0167 0.0197  0.0144  274 MET A CA  
2314  C C   A MET A 274 ? 0.2640 0.3907 0.3378 -0.0179 0.0185  0.0176  274 MET A C   
2315  C C   B MET A 274 ? 0.2640 0.3907 0.3378 -0.0179 0.0185  0.0176  274 MET A C   
2316  O O   A MET A 274 ? 0.2591 0.3929 0.3430 -0.0195 0.0235  0.0185  274 MET A O   
2317  O O   B MET A 274 ? 0.2591 0.3929 0.3430 -0.0195 0.0235  0.0185  274 MET A O   
2318  C CB  A MET A 274 ? 0.4449 0.5795 0.4981 -0.0239 0.0193  0.0231  274 MET A CB  
2319  C CB  B MET A 274 ? 0.4449 0.5795 0.4981 -0.0239 0.0193  0.0231  274 MET A CB  
2320  C CG  A MET A 274 ? 0.6620 0.7854 0.7162 -0.0271 0.0113  0.0301  274 MET A CG  
2321  C CG  B MET A 274 ? 0.6620 0.7854 0.7162 -0.0271 0.0113  0.0301  274 MET A CG  
2322  S SD  A MET A 274 ? 0.8096 0.9299 0.8847 -0.0314 0.0113  0.0395  274 MET A SD  
2323  S SD  B MET A 274 ? 0.8096 0.9299 0.8847 -0.0314 0.0113  0.0395  274 MET A SD  
2324  C CE  A MET A 274 ? 0.8217 0.9477 0.8906 -0.0384 0.0121  0.0502  274 MET A CE  
2325  C CE  B MET A 274 ? 0.8217 0.9477 0.8906 -0.0384 0.0121  0.0502  274 MET A CE  
2326  N N   . LEU A 275 ? 0.2314 0.3464 0.3069 -0.0183 0.0123  0.0188  275 LEU A N   
2327  C CA  . LEU A 275 ? 0.2401 0.3504 0.3300 -0.0212 0.0116  0.0219  275 LEU A CA  
2328  C C   . LEU A 275 ? 0.2217 0.3235 0.3133 -0.0242 0.0052  0.0269  275 LEU A C   
2329  O O   . LEU A 275 ? 0.2746 0.3742 0.3550 -0.0244 0.0008  0.0283  275 LEU A O   
2330  C CB  . LEU A 275 ? 0.3141 0.4214 0.4072 -0.0180 0.0114  0.0161  275 LEU A CB  
2331  C CG  . LEU A 275 ? 0.3249 0.4235 0.4078 -0.0131 0.0063  0.0106  275 LEU A CG  
2332  C CD1 . LEU A 275 ? 0.2523 0.3396 0.3359 -0.0162 0.0002  0.0126  275 LEU A CD1 
2333  C CD2 . LEU A 275 ? 0.3876 0.4869 0.4732 -0.0094 0.0072  0.0062  275 LEU A CD2 
2334  N N   . ALA A 276 ? 0.2142 0.3125 0.3204 -0.0271 0.0049  0.0292  276 ALA A N   
2335  C CA  . ALA A 276 ? 0.1717 0.2632 0.2835 -0.0294 -0.0013 0.0327  276 ALA A CA  
2336  C C   . ALA A 276 ? 0.1889 0.2756 0.3081 -0.0301 -0.0015 0.0281  276 ALA A C   
2337  O O   . ALA A 276 ? 0.1818 0.2709 0.3049 -0.0301 0.0034  0.0244  276 ALA A O   
2338  C CB  . ALA A 276 ? 0.1462 0.2394 0.2727 -0.0329 -0.0012 0.0408  276 ALA A CB  
2339  N N   . THR A 277 ? 0.2123 0.2930 0.3324 -0.0315 -0.0076 0.0286  277 THR A N   
2340  C CA  . THR A 277 ? 0.1863 0.2629 0.3142 -0.0341 -0.0079 0.0251  277 THR A CA  
2341  C C   . THR A 277 ? 0.2384 0.3139 0.3772 -0.0371 -0.0128 0.0289  277 THR A C   
2342  O O   . THR A 277 ? 0.2294 0.3079 0.3729 -0.0370 -0.0154 0.0351  277 THR A O   
2343  C CB  . THR A 277 ? 0.2195 0.2888 0.3331 -0.0323 -0.0107 0.0196  277 THR A CB  
2344  O OG1 . THR A 277 ? 0.2129 0.2786 0.3333 -0.0367 -0.0109 0.0174  277 THR A OG1 
2345  C CG2 . THR A 277 ? 0.2110 0.2743 0.3105 -0.0306 -0.0177 0.0193  277 THR A CG2 
2346  N N   . ASP A 278 ? 0.2132 0.2852 0.3562 -0.0403 -0.0149 0.0258  278 ASP A N   
2347  C CA  . ASP A 278 ? 0.2114 0.2856 0.3707 -0.0435 -0.0180 0.0285  278 ASP A CA  
2348  C C   . ASP A 278 ? 0.1528 0.2233 0.3037 -0.0445 -0.0271 0.0298  278 ASP A C   
2349  O O   . ASP A 278 ? 0.1857 0.2490 0.3192 -0.0443 -0.0301 0.0261  278 ASP A O   
2350  C CB  . ASP A 278 ? 0.2118 0.2874 0.3844 -0.0482 -0.0131 0.0236  278 ASP A CB  
2351  C CG  . ASP A 278 ? 0.2894 0.3701 0.4836 -0.0510 -0.0145 0.0251  278 ASP A CG  
2352  O OD1 . ASP A 278 ? 0.3049 0.3901 0.5139 -0.0488 -0.0145 0.0300  278 ASP A OD1 
2353  O OD2 . ASP A 278 ? 0.3643 0.4445 0.5613 -0.0556 -0.0160 0.0217  278 ASP A OD2 
2354  N N   . GLU A 279 ? 0.2351 0.3410 0.3225 -0.0550 0.0162  0.0243  279 GLU A N   
2355  C CA  . GLU A 279 ? 0.3240 0.4176 0.4083 -0.0627 0.0094  0.0270  279 GLU A CA  
2356  C C   . GLU A 279 ? 0.2979 0.3898 0.3826 -0.0699 0.0088  0.0333  279 GLU A C   
2357  O O   . GLU A 279 ? 0.2937 0.3678 0.3701 -0.0755 0.0025  0.0357  279 GLU A O   
2358  C CB  . GLU A 279 ? 0.3403 0.4450 0.4387 -0.0659 0.0055  0.0257  279 GLU A CB  
2359  C CG  . GLU A 279 ? 0.4096 0.5017 0.5065 -0.0737 -0.0041 0.0277  279 GLU A CG  
2360  C CD  . GLU A 279 ? 0.4368 0.5365 0.5451 -0.0748 -0.0097 0.0254  279 GLU A CD  
2361  O OE1 . GLU A 279 ? 0.3326 0.4476 0.4503 -0.0697 -0.0053 0.0225  279 GLU A OE1 
2362  O OE2 . GLU A 279 ? 0.4988 0.5879 0.6064 -0.0809 -0.0195 0.0265  279 GLU A OE2 
2363  N N   . VAL A 280 ? 0.2783 0.3867 0.3712 -0.0701 0.0151  0.0362  280 VAL A N   
2364  C CA  . VAL A 280 ? 0.2644 0.3704 0.3571 -0.0774 0.0158  0.0435  280 VAL A CA  
2365  C C   . VAL A 280 ? 0.2931 0.3761 0.3660 -0.0757 0.0141  0.0452  280 VAL A C   
2366  O O   . VAL A 280 ? 0.2989 0.3685 0.3671 -0.0831 0.0104  0.0505  280 VAL A O   
2367  C CB  . VAL A 280 ? 0.2342 0.3610 0.3357 -0.0764 0.0245  0.0466  280 VAL A CB  
2368  C CG1 . VAL A 280 ? 0.2921 0.4137 0.3903 -0.0835 0.0269  0.0554  280 VAL A CG1 
2369  C CG2 . VAL A 280 ? 0.2561 0.4050 0.3782 -0.0781 0.0263  0.0455  280 VAL A CG2 
2370  N N   . ILE A 281 ? 0.2832 0.3614 0.3457 -0.0660 0.0165  0.0408  281 ILE A N   
2371  C CA  . ILE A 281 ? 0.3355 0.3920 0.3801 -0.0624 0.0148  0.0415  281 ILE A CA  
2372  C C   . ILE A 281 ? 0.3473 0.3812 0.3818 -0.0656 0.0076  0.0406  281 ILE A C   
2373  O O   . ILE A 281 ? 0.3412 0.3557 0.3639 -0.0691 0.0037  0.0442  281 ILE A O   
2374  C CB  . ILE A 281 ? 0.3656 0.4240 0.4059 -0.0509 0.0183  0.0364  281 ILE A CB  
2375  C CG1 . ILE A 281 ? 0.3808 0.4596 0.4295 -0.0470 0.0234  0.0360  281 ILE A CG1 
2376  C CG2 . ILE A 281 ? 0.3756 0.4126 0.3993 -0.0462 0.0167  0.0373  281 ILE A CG2 
2377  C CD1 . ILE A 281 ? 0.3516 0.4289 0.3935 -0.0490 0.0253  0.0421  281 ILE A CD1 
2378  N N   . LEU A 282 ? 0.3888 0.4226 0.4252 -0.0638 0.0053  0.0356  282 LEU A N   
2379  C CA  . LEU A 282 ? 0.4265 0.4371 0.4500 -0.0657 -0.0022 0.0339  282 LEU A CA  
2380  C C   . LEU A 282 ? 0.3862 0.3894 0.4127 -0.0776 -0.0100 0.0388  282 LEU A C   
2381  O O   . LEU A 282 ? 0.3234 0.3017 0.3347 -0.0800 -0.0166 0.0397  282 LEU A O   
2382  C CB  . LEU A 282 ? 0.4148 0.4291 0.4409 -0.0626 -0.0031 0.0288  282 LEU A CB  
2383  C CG  . LEU A 282 ? 0.4243 0.4133 0.4336 -0.0633 -0.0112 0.0264  282 LEU A CG  
2384  C CD1 . LEU A 282 ? 0.3342 0.2980 0.3199 -0.0552 -0.0096 0.0242  282 LEU A CD1 
2385  C CD2 . LEU A 282 ? 0.3306 0.3255 0.3437 -0.0612 -0.0122 0.0226  282 LEU A CD2 
2386  N N   . LYS A 283 ? 0.3921 0.4167 0.4393 -0.0848 -0.0098 0.0418  283 LYS A N   
2387  C CA  . LYS A 283 ? 0.3962 0.4179 0.4526 -0.0971 -0.0171 0.0471  283 LYS A CA  
2388  C C   . LYS A 283 ? 0.3908 0.4012 0.4405 -0.1020 -0.0162 0.0537  283 LYS A C   
2389  O O   . LYS A 283 ? 0.4735 0.4653 0.5189 -0.1103 -0.0250 0.0568  283 LYS A O   
2390  C CB  . LYS A 283 ? 0.4376 0.4886 0.5207 -0.1025 -0.0143 0.0496  283 LYS A CB  
2391  C CG  . LYS A 283 ? 0.5483 0.6076 0.6400 -0.1004 -0.0186 0.0442  283 LYS A CG  
2392  C CD  . LYS A 283 ? 0.6290 0.6612 0.7025 -0.0996 -0.0295 0.0399  283 LYS A CD  
2393  C CE  . LYS A 283 ? 0.6962 0.7345 0.7796 -0.1007 -0.0369 0.0366  283 LYS A CE  
2394  N NZ  . LYS A 283 ? 0.7447 0.7538 0.8091 -0.1019 -0.0498 0.0335  283 LYS A NZ  
2395  N N   . ASN A 284 ? 0.3298 0.3495 0.3776 -0.0969 -0.0067 0.0560  284 ASN A N   
2396  C CA  . ASN A 284 ? 0.3634 0.3705 0.4016 -0.0999 -0.0054 0.0626  284 ASN A CA  
2397  C C   . ASN A 284 ? 0.3851 0.3601 0.3994 -0.0957 -0.0115 0.0603  284 ASN A C   
2398  O O   . ASN A 284 ? 0.4044 0.3622 0.4100 -0.1007 -0.0143 0.0660  284 ASN A O   
2399  C CB  . ASN A 284 ? 0.3416 0.3638 0.3793 -0.0931 0.0051  0.0645  284 ASN A CB  
2400  C CG  . ASN A 284 ? 0.3650 0.4133 0.4216 -0.0984 0.0121  0.0695  284 ASN A CG  
2401  O OD1 . ASN A 284 ? 0.4418 0.4991 0.5153 -0.1078 0.0097  0.0723  284 ASN A OD1 
2402  N ND2 . ASN A 284 ? 0.3642 0.4248 0.4182 -0.0920 0.0206  0.0704  284 ASN A ND2 
2403  N N   . SER A 285 ? 0.3715 0.3382 0.3749 -0.0859 -0.0126 0.0525  285 SER A N   
2404  C CA  . SER A 285 ? 0.4381 0.3781 0.4186 -0.0777 -0.0148 0.0493  285 SER A CA  
2405  C C   . SER A 285 ? 0.4964 0.4094 0.4626 -0.0799 -0.0250 0.0459  285 SER A C   
2406  O O   . SER A 285 ? 0.5418 0.4273 0.4887 -0.0775 -0.0294 0.0458  285 SER A O   
2407  C CB  . SER A 285 ? 0.3654 0.3142 0.3433 -0.0641 -0.0075 0.0432  285 SER A CB  
2408  O OG  . SER A 285 ? 0.3779 0.3481 0.3660 -0.0609 0.0000  0.0453  285 SER A OG  
2409  N N   . VAL A 286 ? 0.4336 0.3522 0.4072 -0.0836 -0.0296 0.0428  286 VAL A N   
2410  C CA  . VAL A 286 ? 0.4714 0.3636 0.4289 -0.0845 -0.0402 0.0386  286 VAL A CA  
2411  C C   . VAL A 286 ? 0.4972 0.3957 0.4707 -0.0974 -0.0500 0.0409  286 VAL A C   
2412  O O   . VAL A 286 ? 0.4010 0.3269 0.3959 -0.1000 -0.0466 0.0416  286 VAL A O   
2413  C CB  . VAL A 286 ? 0.4447 0.3332 0.3901 -0.0727 -0.0366 0.0312  286 VAL A CB  
2414  C CG1 . VAL A 286 ? 0.5083 0.3632 0.4293 -0.0717 -0.0473 0.0268  286 VAL A CG1 
2415  C CG2 . VAL A 286 ? 0.4249 0.3166 0.3638 -0.0601 -0.0253 0.0294  286 VAL A CG2 
2416  N N   . GLU A 287 ? 0.5918 0.4643 0.5555 -0.1050 -0.0629 0.0418  287 GLU A N   
2417  C CA  . GLU A 287 ? 0.7361 0.6101 0.7135 -0.1165 -0.0753 0.0427  287 GLU A CA  
2418  C C   . GLU A 287 ? 0.8112 0.6908 0.7874 -0.1110 -0.0776 0.0363  287 GLU A C   
2419  O O   . GLU A 287 ? 0.8281 0.7346 0.8285 -0.1152 -0.0767 0.0376  287 GLU A O   
2420  C CB  . GLU A 287 ? 0.8232 0.6610 0.7836 -0.1231 -0.0908 0.0426  287 GLU A CB  
2421  C CG  . GLU A 287 ? 0.8536 0.6891 0.8255 -0.1352 -0.0932 0.0512  287 GLU A CG  
2422  C CD  . GLU A 287 ? 0.8701 0.7232 0.8734 -0.1511 -0.1011 0.0570  287 GLU A CD  
2423  O OE1 . GLU A 287 ? 0.9237 0.7693 0.9359 -0.1632 -0.1062 0.0643  287 GLU A OE1 
2424  O OE2 . GLU A 287 ? 0.8310 0.7056 0.8513 -0.1515 -0.1020 0.0548  287 GLU A OE2 
2425  N N   . ARG A 288 ? 0.8475 0.7007 0.7943 -0.1010 -0.0804 0.0295  288 ARG A N   
2426  C CA  . ARG A 288 ? 0.8722 0.7241 0.8113 -0.0950 -0.0828 0.0238  288 ARG A CA  
2427  C C   . ARG A 288 ? 0.8903 0.7656 0.8354 -0.0847 -0.0667 0.0223  288 ARG A C   
2428  O O   . ARG A 288 ? 0.9960 0.8608 0.9224 -0.0734 -0.0580 0.0192  288 ARG A O   
2429  C CB  . ARG A 288 ? 0.9273 0.7391 0.8296 -0.0880 -0.0911 0.0177  288 ARG A CB  
2430  C CG  . ARG A 288 ? 0.9335 0.7418 0.8242 -0.0810 -0.0925 0.0125  288 ARG A CG  
2431  C CD  . ARG A 288 ? 0.9182 0.7070 0.8020 -0.0884 -0.1124 0.0104  288 ARG A CD  
2432  N NE  . ARG A 288 ? 0.9069 0.6600 0.7688 -0.0916 -0.1251 0.0090  288 ARG A NE  
2433  C CZ  . ARG A 288 ? 0.8723 0.5913 0.6969 -0.0809 -0.1241 0.0041  288 ARG A CZ  
2434  N NH1 . ARG A 288 ? 0.8357 0.5216 0.6417 -0.0846 -0.1373 0.0026  288 ARG A NH1 
2435  N NH2 . ARG A 288 ? 0.8861 0.6036 0.6928 -0.0666 -0.1098 0.0008  288 ARG A NH2 
2436  N N   . ALA A 289 ? 0.7734 0.6804 0.7456 -0.0884 -0.0630 0.0244  289 ALA A N   
2437  C CA  . ALA A 289 ? 0.7074 0.6393 0.6901 -0.0806 -0.0483 0.0239  289 ALA A CA  
2438  C C   . ALA A 289 ? 0.5360 0.4819 0.5278 -0.0786 -0.0487 0.0212  289 ALA A C   
2439  O O   . ALA A 289 ? 0.4827 0.4539 0.5000 -0.0841 -0.0488 0.0235  289 ALA A O   
2440  C CB  . ALA A 289 ? 0.7633 0.7204 0.7689 -0.0857 -0.0410 0.0294  289 ALA A CB  
2441  N N   . SER A 290 ? 0.4981 0.4266 0.4682 -0.0700 -0.0483 0.0166  290 SER A N   
2442  C CA  . SER A 290 ? 0.4476 0.3911 0.4262 -0.0662 -0.0451 0.0147  290 SER A CA  
2443  C C   . SER A 290 ? 0.4377 0.3991 0.4235 -0.0584 -0.0296 0.0144  290 SER A C   
2444  O O   . SER A 290 ? 0.4478 0.3969 0.4176 -0.0508 -0.0221 0.0132  290 SER A O   
2445  C CB  . SER A 290 ? 0.4687 0.3865 0.4214 -0.0611 -0.0513 0.0109  290 SER A CB  
2446  O OG  . SER A 290 ? 0.4373 0.3681 0.3952 -0.0554 -0.0442 0.0098  290 SER A OG  
2447  N N   . PRO A 291 ? 0.4084 0.3979 0.4181 -0.0595 -0.0250 0.0152  291 PRO A N   
2448  C CA  . PRO A 291 ? 0.3386 0.3436 0.3556 -0.0523 -0.0123 0.0143  291 PRO A CA  
2449  C C   . PRO A 291 ? 0.3127 0.3115 0.3202 -0.0450 -0.0079 0.0117  291 PRO A C   
2450  O O   . PRO A 291 ? 0.2599 0.2732 0.2774 -0.0402 0.0013  0.0111  291 PRO A O   
2451  C CB  . PRO A 291 ? 0.3632 0.3977 0.4075 -0.0567 -0.0110 0.0158  291 PRO A CB  
2452  C CG  . PRO A 291 ? 0.3764 0.4110 0.4270 -0.0627 -0.0217 0.0160  291 PRO A CG  
2453  C CD  . PRO A 291 ? 0.3736 0.3812 0.4051 -0.0665 -0.0318 0.0165  291 PRO A CD  
2454  N N   . TYR A 292 ? 0.2776 0.2544 0.2657 -0.0441 -0.0147 0.0104  292 TYR A N   
2455  C CA  . TYR A 292 ? 0.3325 0.3018 0.3097 -0.0376 -0.0103 0.0090  292 TYR A CA  
2456  C C   . TYR A 292 ? 0.3614 0.3098 0.3146 -0.0292 -0.0018 0.0082  292 TYR A C   
2457  O O   . TYR A 292 ? 0.3487 0.2882 0.2899 -0.0233 0.0037  0.0080  292 TYR A O   
2458  C CB  . TYR A 292 ? 0.3314 0.2880 0.2993 -0.0404 -0.0226 0.0082  292 TYR A CB  
2459  C CG  . TYR A 292 ? 0.3797 0.3592 0.3745 -0.0477 -0.0304 0.0090  292 TYR A CG  
2460  C CD1 . TYR A 292 ? 0.4025 0.4101 0.4226 -0.0475 -0.0229 0.0095  292 TYR A CD1 
2461  C CD2 . TYR A 292 ? 0.4883 0.4611 0.4838 -0.0542 -0.0453 0.0091  292 TYR A CD2 
2462  C CE1 . TYR A 292 ? 0.3952 0.4237 0.4393 -0.0527 -0.0285 0.0101  292 TYR A CE1 
2463  C CE2 . TYR A 292 ? 0.4875 0.4835 0.5107 -0.0601 -0.0511 0.0102  292 TYR A CE2 
2464  C CZ  . TYR A 292 ? 0.4502 0.4741 0.4970 -0.0588 -0.0418 0.0107  292 TYR A CZ  
2465  O OH  . TYR A 292 ? 0.4946 0.5416 0.5681 -0.0631 -0.0460 0.0115  292 TYR A OH  
2466  N N   . LEU A 293 ? 0.3287 0.2694 0.2752 -0.0282 -0.0001 0.0083  293 LEU A N   
2467  C CA  . LEU A 293 ? 0.3775 0.2977 0.3015 -0.0195 0.0076  0.0074  293 LEU A CA  
2468  C C   . LEU A 293 ? 0.3641 0.3026 0.3042 -0.0143 0.0206  0.0083  293 LEU A C   
2469  O O   . LEU A 293 ? 0.3036 0.2656 0.2675 -0.0183 0.0210  0.0093  293 LEU A O   
2470  C CB  . LEU A 293 ? 0.4276 0.3248 0.3331 -0.0212 -0.0007 0.0066  293 LEU A CB  
2471  C CG  . LEU A 293 ? 0.5070 0.3738 0.3854 -0.0230 -0.0137 0.0045  293 LEU A CG  
2472  C CD1 . LEU A 293 ? 0.5014 0.3738 0.3865 -0.0288 -0.0232 0.0046  293 LEU A CD1 
2473  C CD2 . LEU A 293 ? 0.4718 0.3252 0.3453 -0.0293 -0.0247 0.0046  293 LEU A CD2 
2474  N N   . ARG A 294 ? 0.3558 0.2830 0.2826 -0.0049 0.0312  0.0079  294 ARG A N   
2475  C CA  . ARG A 294 ? 0.3431 0.2838 0.2837 0.0008  0.0420  0.0086  294 ARG A CA  
2476  C C   . ARG A 294 ? 0.3483 0.2739 0.2761 0.0032  0.0393  0.0079  294 ARG A C   
2477  O O   . ARG A 294 ? 0.3735 0.2715 0.2739 0.0075  0.0379  0.0065  294 ARG A O   
2478  C CB  . ARG A 294 ? 0.3426 0.2807 0.2792 0.0099  0.0559  0.0093  294 ARG A CB  
2479  C CG  . ARG A 294 ? 0.3862 0.3395 0.3406 0.0163  0.0663  0.0100  294 ARG A CG  
2480  C CD  . ARG A 294 ? 0.3651 0.3242 0.3262 0.0230  0.0806  0.0119  294 ARG A CD  
2481  N NE  . ARG A 294 ? 0.4334 0.3663 0.3651 0.0310  0.0881  0.0121  294 ARG A NE  
2482  C CZ  . ARG A 294 ? 0.4342 0.3576 0.3533 0.0328  0.0940  0.0138  294 ARG A CZ  
2483  N NH1 . ARG A 294 ? 0.4097 0.3475 0.3444 0.0268  0.0928  0.0156  294 ARG A NH1 
2484  N NH2 . ARG A 294 ? 0.4997 0.3970 0.3883 0.0413  0.1012  0.0139  294 ARG A NH2 
2485  N N   . TYR A 295 ? 0.2702 0.2113 0.2153 0.0004  0.0378  0.0089  295 TYR A N   
2486  C CA  . TYR A 295 ? 0.3072 0.2334 0.2407 0.0022  0.0344  0.0089  295 TYR A CA  
2487  C C   . TYR A 295 ? 0.3378 0.2669 0.2750 0.0129  0.0448  0.0088  295 TYR A C   
2488  O O   . TYR A 295 ? 0.3483 0.2984 0.3057 0.0163  0.0530  0.0093  295 TYR A O   
2489  C CB  . TYR A 295 ? 0.3412 0.2790 0.2879 -0.0071 0.0260  0.0111  295 TYR A CB  
2490  C CG  . TYR A 295 ? 0.3791 0.3092 0.3205 -0.0174 0.0145  0.0116  295 TYR A CG  
2491  C CD1 . TYR A 295 ? 0.3043 0.2502 0.2592 -0.0231 0.0122  0.0117  295 TYR A CD1 
2492  C CD2 . TYR A 295 ? 0.3570 0.2635 0.2811 -0.0212 0.0053  0.0120  295 TYR A CD2 
2493  C CE1 . TYR A 295 ? 0.3762 0.3170 0.3297 -0.0321 0.0011  0.0123  295 TYR A CE1 
2494  C CE2 . TYR A 295 ? 0.4292 0.3300 0.3523 -0.0314 -0.0064 0.0127  295 TYR A CE2 
2495  C CZ  . TYR A 295 ? 0.4284 0.3474 0.3671 -0.0366 -0.0083 0.0129  295 TYR A CZ  
2496  O OH  . TYR A 295 ? 0.4378 0.3526 0.3784 -0.0462 -0.0205 0.0137  295 TYR A OH  
2497  N N   . TYR A 296 ? 0.3673 0.2743 0.2857 0.0183  0.0438  0.0079  296 TYR A N   
2498  C CA  . TYR A 296 ? 0.4626 0.3717 0.3853 0.0291  0.0523  0.0078  296 TYR A CA  
2499  C C   . TYR A 296 ? 0.4696 0.3714 0.3893 0.0275  0.0446  0.0088  296 TYR A C   
2500  O O   . TYR A 296 ? 0.4668 0.3421 0.3635 0.0264  0.0376  0.0080  296 TYR A O   
2501  C CB  . TYR A 296 ? 0.5257 0.4133 0.4269 0.0408  0.0613  0.0058  296 TYR A CB  
2502  C CG  . TYR A 296 ? 0.6267 0.5205 0.5298 0.0432  0.0708  0.0060  296 TYR A CG  
2503  C CD1 . TYR A 296 ? 0.6140 0.5308 0.5410 0.0484  0.0830  0.0075  296 TYR A CD1 
2504  C CD2 . TYR A 296 ? 0.7181 0.5936 0.5990 0.0399  0.0669  0.0049  296 TYR A CD2 
2505  C CE1 . TYR A 296 ? 0.6418 0.5629 0.5704 0.0499  0.0923  0.0087  296 TYR A CE1 
2506  C CE2 . TYR A 296 ? 0.7166 0.5955 0.5967 0.0422  0.0757  0.0058  296 TYR A CE2 
2507  C CZ  . TYR A 296 ? 0.6870 0.5884 0.5907 0.0469  0.0889  0.0081  296 TYR A CZ  
2508  O OH  . TYR A 296 ? 0.7368 0.6394 0.6387 0.0485  0.0979  0.0099  296 TYR A OH  
2509  N N   . PHE A 297 ? 0.4119 0.3354 0.3535 0.0272  0.0452  0.0106  297 PHE A N   
2510  C CA  . PHE A 297 ? 0.3422 0.2588 0.2803 0.0262  0.0385  0.0125  297 PHE A CA  
2511  C C   . PHE A 297 ? 0.3507 0.2502 0.2770 0.0391  0.0428  0.0111  297 PHE A C   
2512  O O   . PHE A 297 ? 0.3916 0.3052 0.3330 0.0484  0.0507  0.0105  297 PHE A O   
2513  C CB  . PHE A 297 ? 0.3100 0.2533 0.2718 0.0226  0.0372  0.0148  297 PHE A CB  
2514  C CG  . PHE A 297 ? 0.3475 0.2832 0.3043 0.0223  0.0310  0.0175  297 PHE A CG  
2515  C CD1 . PHE A 297 ? 0.3392 0.2635 0.2855 0.0120  0.0228  0.0206  297 PHE A CD1 
2516  C CD2 . PHE A 297 ? 0.3503 0.2895 0.3133 0.0323  0.0332  0.0175  297 PHE A CD2 
2517  C CE1 . PHE A 297 ? 0.3648 0.2808 0.3055 0.0112  0.0178  0.0243  297 PHE A CE1 
2518  C CE2 . PHE A 297 ? 0.3319 0.2620 0.2881 0.0324  0.0270  0.0206  297 PHE A CE2 
2519  C CZ  . PHE A 297 ? 0.3210 0.2388 0.2649 0.0216  0.0197  0.0242  297 PHE A CZ  
2520  N N   . ARG A 298 ? 0.3873 0.2563 0.2878 0.0398  0.0370  0.0104  298 ARG A N   
2521  C CA  . ARG A 298 ? 0.3814 0.2291 0.2664 0.0527  0.0399  0.0086  298 ARG A CA  
2522  C C   . ARG A 298 ? 0.4671 0.3183 0.3540 0.0658  0.0534  0.0058  298 ARG A C   
2523  O O   . ARG A 298 ? 0.5303 0.3792 0.4192 0.0784  0.0595  0.0049  298 ARG A O   
2524  C CB  . ARG A 298 ? 0.4383 0.2930 0.3344 0.0560  0.0370  0.0111  298 ARG A CB  
2525  C CG  . ARG A 298 ? 0.4646 0.3151 0.3578 0.0436  0.0255  0.0152  298 ARG A CG  
2526  C CD  . ARG A 298 ? 0.4152 0.2691 0.3148 0.0474  0.0223  0.0182  298 ARG A CD  
2527  N NE  . ARG A 298 ? 0.4674 0.3139 0.3608 0.0352  0.0129  0.0231  298 ARG A NE  
2528  C CZ  . ARG A 298 ? 0.4711 0.3221 0.3690 0.0344  0.0090  0.0274  298 ARG A CZ  
2529  N NH1 . ARG A 298 ? 0.4451 0.3081 0.3543 0.0455  0.0119  0.0268  298 ARG A NH1 
2530  N NH2 . ARG A 298 ? 0.4690 0.3128 0.3608 0.0226  0.0022  0.0327  298 ARG A NH2 
2531  N N   . GLU A 299 ? 0.4973 0.3547 0.3849 0.0630  0.0586  0.0049  299 GLU A N   
2532  C CA  . GLU A 299 ? 0.5506 0.4131 0.4412 0.0740  0.0733  0.0036  299 GLU A CA  
2533  C C   . GLU A 299 ? 0.5404 0.4328 0.4640 0.0802  0.0814  0.0053  299 GLU A C   
2534  O O   . GLU A 299 ? 0.5651 0.4613 0.4947 0.0919  0.0940  0.0049  299 GLU A O   
2535  C CB  . GLU A 299 ? 0.6220 0.4515 0.4810 0.0864  0.0779  0.0005  299 GLU A CB  
2536  C CG  . GLU A 299 ? 0.7698 0.5774 0.6008 0.0849  0.0786  -0.0016 299 GLU A CG  
2537  C CD  . GLU A 299 ? 0.8942 0.6600 0.6850 0.0922  0.0744  -0.0056 299 GLU A CD  
2538  O OE1 . GLU A 299 ? 0.9513 0.7044 0.7355 0.1014  0.0746  -0.0070 299 GLU A OE1 
2539  O OE2 . GLU A 299 ? 0.9150 0.6590 0.6798 0.0891  0.0698  -0.0077 299 GLU A OE2 
2540  N N   . LEU A 300 ? 0.4941 0.4079 0.4399 0.0727  0.0741  0.0073  300 LEU A N   
2541  C CA  . LEU A 300 ? 0.4637 0.4048 0.4408 0.0776  0.0782  0.0084  300 LEU A CA  
2542  C C   . LEU A 300 ? 0.4080 0.3777 0.4113 0.0705  0.0806  0.0094  300 LEU A C   
2543  O O   . LEU A 300 ? 0.3861 0.3764 0.4149 0.0760  0.0878  0.0099  300 LEU A O   
2544  C CB  . LEU A 300 ? 0.5055 0.4478 0.4866 0.0766  0.0675  0.0096  300 LEU A CB  
2545  C CG  . LEU A 300 ? 0.5873 0.5040 0.5486 0.0863  0.0653  0.0088  300 LEU A CG  
2546  C CD1 . LEU A 300 ? 0.6045 0.5213 0.5680 0.0840  0.0543  0.0111  300 LEU A CD1 
2547  C CD2 . LEU A 300 ? 0.6039 0.5223 0.5731 0.1023  0.0768  0.0073  300 LEU A CD2 
2548  N N   . ILE A 301 ? 0.3300 0.3010 0.3285 0.0585  0.0746  0.0097  301 ILE A N   
2549  C CA  . ILE A 301 ? 0.3684 0.3649 0.3904 0.0514  0.0747  0.0103  301 ILE A CA  
2550  C C   . ILE A 301 ? 0.3560 0.3450 0.3645 0.0414  0.0709  0.0103  301 ILE A C   
2551  O O   . ILE A 301 ? 0.4187 0.3891 0.4061 0.0367  0.0635  0.0102  301 ILE A O   
2552  C CB  . ILE A 301 ? 0.3335 0.3481 0.3739 0.0480  0.0662  0.0109  301 ILE A CB  
2553  C CG1 . ILE A 301 ? 0.3210 0.3611 0.3859 0.0423  0.0662  0.0106  301 ILE A CG1 
2554  C CG2 . ILE A 301 ? 0.3070 0.3089 0.3300 0.0408  0.0555  0.0120  301 ILE A CG2 
2555  C CD1 . ILE A 301 ? 0.2850 0.3415 0.3656 0.0406  0.0577  0.0105  301 ILE A CD1 
2556  N N   . SER A 302 ? 0.3522 0.3552 0.3736 0.0381  0.0754  0.0105  302 SER A N   
2557  C CA  . SER A 302 ? 0.3487 0.3465 0.3597 0.0292  0.0709  0.0104  302 SER A CA  
2558  C C   . SER A 302 ? 0.3227 0.3365 0.3468 0.0197  0.0615  0.0105  302 SER A C   
2559  O O   . SER A 302 ? 0.3330 0.3667 0.3782 0.0199  0.0609  0.0105  302 SER A O   
2560  C CB  . SER A 302 ? 0.3466 0.3497 0.3634 0.0301  0.0795  0.0109  302 SER A CB  
2561  O OG  . SER A 302 ? 0.3717 0.3588 0.3736 0.0394  0.0898  0.0112  302 SER A OG  
2562  N N   . VAL A 303 ? 0.3347 0.3392 0.3459 0.0117  0.0541  0.0107  303 VAL A N   
2563  C CA  . VAL A 303 ? 0.2843 0.3023 0.3055 0.0030  0.0463  0.0114  303 VAL A CA  
2564  C C   . VAL A 303 ? 0.2883 0.3045 0.3057 -0.0041 0.0425  0.0111  303 VAL A C   
2565  O O   . VAL A 303 ? 0.3309 0.3271 0.3291 -0.0060 0.0388  0.0111  303 VAL A O   
2566  C CB  . VAL A 303 ? 0.3160 0.3243 0.3273 0.0000  0.0395  0.0130  303 VAL A CB  
2567  C CG1 . VAL A 303 ? 0.2864 0.3085 0.3072 -0.0093 0.0334  0.0146  303 VAL A CG1 
2568  C CG2 . VAL A 303 ? 0.2986 0.3083 0.3135 0.0077  0.0419  0.0134  303 VAL A CG2 
2569  N N   . PHE A 304 ? 0.2554 0.2913 0.2906 -0.0076 0.0424  0.0106  304 PHE A N   
2570  C CA  . PHE A 304 ? 0.2665 0.3038 0.3015 -0.0146 0.0370  0.0105  304 PHE A CA  
2571  C C   . PHE A 304 ? 0.2859 0.3356 0.3301 -0.0214 0.0308  0.0116  304 PHE A C   
2572  O O   . PHE A 304 ? 0.2403 0.3034 0.2952 -0.0203 0.0321  0.0118  304 PHE A O   
2573  C CB  . PHE A 304 ? 0.1631 0.2119 0.2102 -0.0138 0.0408  0.0094  304 PHE A CB  
2574  C CG  . PHE A 304 ? 0.2484 0.2816 0.2823 -0.0089 0.0468  0.0096  304 PHE A CG  
2575  C CD1 . PHE A 304 ? 0.2606 0.2756 0.2756 -0.0108 0.0427  0.0098  304 PHE A CD1 
2576  C CD2 . PHE A 304 ? 0.2706 0.3071 0.3110 -0.0022 0.0565  0.0100  304 PHE A CD2 
2577  C CE1 . PHE A 304 ? 0.3001 0.2984 0.2987 -0.0054 0.0490  0.0103  304 PHE A CE1 
2578  C CE2 . PHE A 304 ? 0.3019 0.3240 0.3293 0.0028  0.0643  0.0111  304 PHE A CE2 
2579  C CZ  . PHE A 304 ? 0.3066 0.3087 0.3111 0.0015  0.0609  0.0113  304 PHE A CZ  
2580  N N   . PHE A 305 ? 0.2735 0.3184 0.3134 -0.0283 0.0242  0.0125  305 PHE A N   
2581  C CA  . PHE A 305 ? 0.1604 0.2189 0.2113 -0.0351 0.0200  0.0143  305 PHE A CA  
2582  C C   . PHE A 305 ? 0.2610 0.3344 0.3257 -0.0376 0.0186  0.0129  305 PHE A C   
2583  O O   . PHE A 305 ? 0.2613 0.3263 0.3210 -0.0394 0.0146  0.0123  305 PHE A O   
2584  C CB  . PHE A 305 ? 0.1976 0.2415 0.2380 -0.0416 0.0132  0.0171  305 PHE A CB  
2585  C CG  . PHE A 305 ? 0.3110 0.3391 0.3376 -0.0389 0.0139  0.0186  305 PHE A CG  
2586  C CD1 . PHE A 305 ? 0.3522 0.3574 0.3598 -0.0338 0.0141  0.0170  305 PHE A CD1 
2587  C CD2 . PHE A 305 ? 0.2711 0.3058 0.3017 -0.0405 0.0148  0.0215  305 PHE A CD2 
2588  C CE1 . PHE A 305 ? 0.3224 0.3122 0.3172 -0.0301 0.0147  0.0179  305 PHE A CE1 
2589  C CE2 . PHE A 305 ? 0.2403 0.2588 0.2575 -0.0374 0.0148  0.0230  305 PHE A CE2 
2590  C CZ  . PHE A 305 ? 0.3443 0.3406 0.3444 -0.0320 0.0145  0.0209  305 PHE A CZ  
2591  N N   . ARG A 306 ? 0.1911 0.2849 0.2714 -0.0367 0.0213  0.0120  306 ARG A N   
2592  C CA  . ARG A 306 ? 0.2413 0.3485 0.3346 -0.0374 0.0205  0.0100  306 ARG A CA  
2593  C C   . ARG A 306 ? 0.2545 0.3639 0.3517 -0.0441 0.0143  0.0117  306 ARG A C   
2594  O O   . ARG A 306 ? 0.3256 0.4318 0.4204 -0.0493 0.0115  0.0149  306 ARG A O   
2595  C CB  . ARG A 306 ? 0.2979 0.4243 0.4048 -0.0346 0.0238  0.0081  306 ARG A CB  
2596  C CG  . ARG A 306 ? 0.3056 0.4423 0.4166 -0.0380 0.0235  0.0104  306 ARG A CG  
2597  C CD  . ARG A 306 ? 0.3172 0.4719 0.4398 -0.0349 0.0259  0.0077  306 ARG A CD  
2598  N NE  . ARG A 306 ? 0.3445 0.5084 0.4697 -0.0383 0.0270  0.0108  306 ARG A NE  
2599  C CZ  . ARG A 306 ? 0.2576 0.4371 0.3910 -0.0363 0.0295  0.0093  306 ARG A CZ  
2600  N NH1 . ARG A 306 ? 0.2082 0.3949 0.3481 -0.0309 0.0296  0.0040  306 ARG A NH1 
2601  N NH2 . ARG A 306 ? 0.2417 0.4284 0.3764 -0.0395 0.0323  0.0134  306 ARG A NH2 
2602  N N   . ASP A 307 ? 0.2471 0.3617 0.3517 -0.0440 0.0118  0.0099  307 ASP A N   
2603  C CA  . ASP A 307 ? 0.2361 0.3564 0.3494 -0.0494 0.0053  0.0110  307 ASP A CA  
2604  C C   . ASP A 307 ? 0.2151 0.3585 0.3462 -0.0499 0.0086  0.0112  307 ASP A C   
2605  O O   . ASP A 307 ? 0.2343 0.3897 0.3750 -0.0458 0.0108  0.0081  307 ASP A O   
2606  C CB  . ASP A 307 ? 0.1854 0.3004 0.2981 -0.0479 0.0007  0.0090  307 ASP A CB  
2607  C CG  . ASP A 307 ? 0.2646 0.3829 0.3859 -0.0533 -0.0082 0.0103  307 ASP A CG  
2608  O OD1 . ASP A 307 ? 0.3069 0.4440 0.4460 -0.0562 -0.0080 0.0115  307 ASP A OD1 
2609  O OD2 . ASP A 307 ? 0.3008 0.4024 0.4109 -0.0543 -0.0157 0.0102  307 ASP A OD2 
2610  N N   . LYS A 308 ? 0.1955 0.3438 0.3300 -0.0550 0.0088  0.0149  308 LYS A N   
2611  C CA  . LYS A 308 ? 0.1218 0.2906 0.2697 -0.0547 0.0141  0.0159  308 LYS A CA  
2612  C C   . LYS A 308 ? 0.1577 0.3427 0.3231 -0.0541 0.0125  0.0141  308 LYS A C   
2613  O O   . LYS A 308 ? 0.1212 0.3123 0.2899 -0.0470 0.0171  0.0104  308 LYS A O   
2614  C CB  . LYS A 308 ? 0.1165 0.2855 0.2644 -0.0614 0.0150  0.0218  308 LYS A CB  
2615  C CG  . LYS A 308 ? 0.2117 0.3997 0.3687 -0.0602 0.0229  0.0238  308 LYS A CG  
2616  C CD  . LYS A 308 ? 0.2364 0.4240 0.3939 -0.0678 0.0248  0.0312  308 LYS A CD  
2617  C CE  . LYS A 308 ? 0.3176 0.5157 0.4743 -0.0642 0.0342  0.0330  308 LYS A CE  
2618  N NZ  . LYS A 308 ? 0.3334 0.5406 0.4949 -0.0550 0.0379  0.0267  308 LYS A NZ  
2619  N N   . THR A 309 ? 0.1690 0.3514 0.3407 -0.0589 0.0050  0.0155  309 THR A N   
2620  C CA  . THR A 309 ? 0.2205 0.4127 0.4069 -0.0561 0.0032  0.0127  309 THR A CA  
2621  C C   . THR A 309 ? 0.1858 0.3786 0.3720 -0.0483 0.0037  0.0074  309 THR A C   
2622  O O   . THR A 309 ? 0.1945 0.3938 0.3886 -0.0422 0.0069  0.0044  309 THR A O   
2623  C CB  . THR A 309 ? 0.2730 0.4628 0.4671 -0.0629 -0.0072 0.0152  309 THR A CB  
2624  O OG1 . THR A 309 ? 0.4558 0.6284 0.6368 -0.0628 -0.0146 0.0141  309 THR A OG1 
2625  C CG2 . THR A 309 ? 0.1942 0.3806 0.3892 -0.0713 -0.0090 0.0206  309 THR A CG2 
2626  N N   . LEU A 310 ? 0.2021 0.3845 0.3781 -0.0482 0.0004  0.0067  310 LEU A N   
2627  C CA  . LEU A 310 ? 0.1250 0.3067 0.3010 -0.0419 0.0010  0.0024  310 LEU A CA  
2628  C C   . LEU A 310 ? 0.1498 0.3355 0.3247 -0.0358 0.0085  -0.0002 310 LEU A C   
2629  O O   . LEU A 310 ? 0.1307 0.3183 0.3098 -0.0299 0.0089  -0.0027 310 LEU A O   
2630  C CB  . LEU A 310 ? 0.1238 0.2835 0.2828 -0.0412 -0.0019 0.0022  310 LEU A CB  
2631  C CG  . LEU A 310 ? 0.2431 0.3903 0.3971 -0.0441 -0.0116 0.0036  310 LEU A CG  
2632  C CD1 . LEU A 310 ? 0.2490 0.3729 0.3819 -0.0419 -0.0121 0.0037  310 LEU A CD1 
2633  C CD2 . LEU A 310 ? 0.2356 0.3938 0.4050 -0.0423 -0.0171 0.0021  310 LEU A CD2 
2634  N N   . SER A 311 ? 0.1589 0.3421 0.3255 -0.0368 0.0130  0.0011  311 SER A N   
2635  C CA  . SER A 311 ? 0.1671 0.3507 0.3304 -0.0308 0.0179  -0.0010 311 SER A CA  
2636  C C   . SER A 311 ? 0.1797 0.3713 0.3486 -0.0275 0.0203  -0.0011 311 SER A C   
2637  O O   . SER A 311 ? 0.2132 0.4070 0.3823 -0.0217 0.0216  -0.0042 311 SER A O   
2638  C CB  . SER A 311 ? 0.1213 0.3024 0.2757 -0.0327 0.0212  0.0007  311 SER A CB  
2639  O OG  . SER A 311 ? 0.1544 0.3239 0.3015 -0.0342 0.0199  0.0012  311 SER A OG  
2640  N N   . ASP A 312 ? 0.1964 0.3934 0.3708 -0.0316 0.0209  0.0020  312 ASP A N   
2641  C CA  . ASP A 312 ? 0.2311 0.4378 0.4117 -0.0287 0.0254  0.0022  312 ASP A CA  
2642  C C   . ASP A 312 ? 0.2300 0.4415 0.4220 -0.0247 0.0231  0.0003  312 ASP A C   
2643  O O   . ASP A 312 ? 0.1404 0.3598 0.3358 -0.0195 0.0274  -0.0010 312 ASP A O   
2644  C CB  . ASP A 312 ? 0.1328 0.3446 0.3175 -0.0351 0.0282  0.0070  312 ASP A CB  
2645  C CG  . ASP A 312 ? 0.1524 0.3624 0.3252 -0.0377 0.0324  0.0103  312 ASP A CG  
2646  O OD1 . ASP A 312 ? 0.1616 0.3690 0.3245 -0.0336 0.0338  0.0080  312 ASP A OD1 
2647  O OD2 . ASP A 312 ? 0.1575 0.3693 0.3320 -0.0443 0.0339  0.0156  312 ASP A OD2 
2648  N N   . LEU A 313 ? 0.1817 0.3895 0.3789 -0.0266 0.0163  0.0002  313 LEU A N   
2649  C CA  . LEU A 313 ? 0.1285 0.3411 0.3353 -0.0223 0.0131  -0.0008 313 LEU A CA  
2650  C C   . LEU A 313 ? 0.1088 0.3207 0.3091 -0.0151 0.0151  -0.0048 313 LEU A C   
2651  O O   . LEU A 313 ? 0.1377 0.3572 0.3434 -0.0096 0.0171  -0.0066 313 LEU A O   
2652  C CB  . LEU A 313 ? 0.1075 0.3162 0.3174 -0.0257 0.0045  -0.0002 313 LEU A CB  
2653  C CG  . LEU A 313 ? 0.1234 0.3333 0.3425 -0.0319 -0.0009 0.0000  313 LEU A CG  
2654  C CD1 . LEU A 313 ? 0.0802 0.2875 0.2924 -0.0355 -0.0097 -0.0037 313 LEU A CD1 
2655  C CD2 . LEU A 313 ? 0.1606 0.3801 0.3949 -0.0292 -0.0007 -0.0002 313 LEU A CD2 
2656  N N   . ILE A 314 ? 0.0721 0.2752 0.2619 -0.0150 0.0145  -0.0069 314 ILE A N   
2657  C CA  . ILE A 314 ? 0.0716 0.2730 0.2574 -0.0092 0.0148  -0.0118 314 ILE A CA  
2658  C C   . ILE A 314 ? 0.1485 0.3557 0.3306 -0.0053 0.0201  -0.0143 314 ILE A C   
2659  O O   . ILE A 314 ? 0.1521 0.3643 0.3357 0.0007  0.0208  -0.0190 314 ILE A O   
2660  C CB  . ILE A 314 ? 0.1017 0.2931 0.2809 -0.0110 0.0130  -0.0127 314 ILE A CB  
2661  C CG1 . ILE A 314 ? 0.0999 0.2873 0.2823 -0.0136 0.0085  -0.0122 314 ILE A CG1 
2662  C CG2 . ILE A 314 ? 0.0869 0.2767 0.2636 -0.0064 0.0133  -0.0176 314 ILE A CG2 
2663  C CD1 . ILE A 314 ? 0.1021 0.2806 0.2798 -0.0155 0.0090  -0.0129 314 ILE A CD1 
2664  N N   . GLY A 315 ? 0.1303 0.3375 0.3068 -0.0083 0.0236  -0.0119 315 GLY A N   
2665  C CA  . GLY A 315 ? 0.1653 0.3790 0.3358 -0.0047 0.0284  -0.0144 315 GLY A CA  
2666  C C   . GLY A 315 ? 0.1868 0.4121 0.3612 -0.0025 0.0344  -0.0133 315 GLY A C   
2667  O O   . GLY A 315 ? 0.2140 0.4468 0.3832 0.0032  0.0385  -0.0170 315 GLY A O   
2668  N N   . PHE A 316 ? 0.1364 0.3645 0.3207 -0.0063 0.0351  -0.0087 316 PHE A N   
2669  C CA  . PHE A 316 ? 0.1535 0.3933 0.3444 -0.0050 0.0423  -0.0066 316 PHE A CA  
2670  C C   . PHE A 316 ? 0.1649 0.4109 0.3705 -0.0020 0.0413  -0.0070 316 PHE A C   
2671  O O   . PHE A 316 ? 0.1754 0.4318 0.3856 0.0031  0.0479  -0.0080 316 PHE A O   
2672  C CB  . PHE A 316 ? 0.2631 0.5042 0.4572 -0.0130 0.0453  -0.0003 316 PHE A CB  
2673  C CG  . PHE A 316 ? 0.4492 0.6873 0.6292 -0.0155 0.0481  0.0016  316 PHE A CG  
2674  C CD1 . PHE A 316 ? 0.5349 0.7754 0.7024 -0.0095 0.0510  -0.0019 316 PHE A CD1 
2675  C CD2 . PHE A 316 ? 0.5281 0.7618 0.7076 -0.0237 0.0470  0.0068  316 PHE A CD2 
2676  C CE1 . PHE A 316 ? 0.5554 0.7945 0.7108 -0.0114 0.0530  0.0003  316 PHE A CE1 
2677  C CE2 . PHE A 316 ? 0.5672 0.7984 0.7339 -0.0259 0.0494  0.0094  316 PHE A CE2 
2678  C CZ  . PHE A 316 ? 0.5596 0.7939 0.7146 -0.0196 0.0525  0.0064  316 PHE A CZ  
2679  N N   . SER A 317 ? 0.1617 0.4025 0.3750 -0.0048 0.0336  -0.0057 317 SER A N   
2680  C CA  . SER A 317 ? 0.1861 0.4350 0.4161 -0.0031 0.0322  -0.0042 317 SER A CA  
2681  C C   . SER A 317 ? 0.1508 0.4005 0.3811 0.0044  0.0285  -0.0088 317 SER A C   
2682  O O   . SER A 317 ? 0.1177 0.3773 0.3573 0.0103  0.0319  -0.0100 317 SER A O   
2683  C CB  . SER A 317 ? 0.2289 0.4742 0.4685 -0.0108 0.0250  0.0001  317 SER A CB  
2684  O OG  . SER A 317 ? 0.3658 0.6198 0.6221 -0.0096 0.0226  0.0021  317 SER A OG  
2685  N N   . TYR A 318 ? 0.1425 0.3816 0.3631 0.0044  0.0223  -0.0121 318 TYR A N   
2686  C CA  . TYR A 318 ? 0.1292 0.3664 0.3524 0.0088  0.0163  -0.0160 318 TYR A CA  
2687  C C   . TYR A 318 ? 0.1831 0.4231 0.4039 0.0178  0.0189  -0.0237 318 TYR A C   
2688  O O   . TYR A 318 ? 0.1512 0.3917 0.3774 0.0230  0.0150  -0.0276 318 TYR A O   
2689  C CB  . TYR A 318 ? 0.1103 0.3347 0.3254 0.0049  0.0099  -0.0169 318 TYR A CB  
2690  C CG  . TYR A 318 ? 0.1393 0.3610 0.3573 -0.0020 0.0045  -0.0120 318 TYR A CG  
2691  C CD1 . TYR A 318 ? 0.1310 0.3619 0.3606 -0.0040 0.0021  -0.0076 318 TYR A CD1 
2692  C CD2 . TYR A 318 ? 0.1470 0.3577 0.3567 -0.0063 0.0012  -0.0123 318 TYR A CD2 
2693  C CE1 . TYR A 318 ? 0.1445 0.3735 0.3752 -0.0105 -0.0050 -0.0048 318 TYR A CE1 
2694  C CE2 . TYR A 318 ? 0.1311 0.3392 0.3422 -0.0120 -0.0043 -0.0097 318 TYR A CE2 
2695  C CZ  . TYR A 318 ? 0.1410 0.3578 0.3618 -0.0142 -0.0081 -0.0066 318 TYR A CZ  
2696  O OH  . TYR A 318 ? 0.2470 0.4603 0.4684 -0.0200 -0.0154 -0.0061 318 TYR A OH  
2697  N N   . HIS A 319 ? 0.1953 0.4371 0.4077 0.0204  0.0248  -0.0267 319 HIS A N   
2698  C CA  . HIS A 319 ? 0.2121 0.4580 0.4215 0.0299  0.0271  -0.0349 319 HIS A CA  
2699  C C   . HIS A 319 ? 0.2202 0.4768 0.4410 0.0364  0.0306  -0.0352 319 HIS A C   
2700  O O   . HIS A 319 ? 0.2574 0.5149 0.4782 0.0453  0.0297  -0.0427 319 HIS A O   
2701  C CB  . HIS A 319 ? 0.2078 0.4571 0.4059 0.0320  0.0336  -0.0372 319 HIS A CB  
2702  C CG  . HIS A 319 ? 0.2158 0.4760 0.4169 0.0318  0.0432  -0.0318 319 HIS A CG  
2703  N ND1 . HIS A 319 ? 0.2409 0.5012 0.4452 0.0230  0.0455  -0.0235 319 HIS A ND1 
2704  C CD2 . HIS A 319 ? 0.2518 0.5225 0.4539 0.0393  0.0517  -0.0337 319 HIS A CD2 
2705  C CE1 . HIS A 319 ? 0.2771 0.5478 0.4858 0.0242  0.0550  -0.0203 319 HIS A CE1 
2706  N NE2 . HIS A 319 ? 0.2736 0.5510 0.4807 0.0342  0.0596  -0.0259 319 HIS A NE2 
2707  N N   . ALA A 320 ? 0.1750 0.4397 0.4069 0.0324  0.0345  -0.0274 320 ALA A N   
2708  C CA  . ALA A 320 ? 0.2017 0.4788 0.4483 0.0379  0.0391  -0.0259 320 ALA A CA  
2709  C C   . ALA A 320 ? 0.2114 0.4890 0.4708 0.0378  0.0306  -0.0241 320 ALA A C   
2710  O O   . ALA A 320 ? 0.2282 0.5171 0.5025 0.0424  0.0330  -0.0223 320 ALA A O   
2711  C CB  . ALA A 320 ? 0.2159 0.5025 0.4716 0.0330  0.0479  -0.0184 320 ALA A CB  
2712  N N   . TRP A 321 ? 0.2142 0.4804 0.4680 0.0331  0.0210  -0.0247 321 TRP A N   
2713  C CA  . TRP A 321 ? 0.2322 0.4975 0.4947 0.0328  0.0120  -0.0238 321 TRP A CA  
2714  C C   . TRP A 321 ? 0.2362 0.4914 0.4934 0.0390  0.0061  -0.0325 321 TRP A C   
2715  O O   . TRP A 321 ? 0.2578 0.5041 0.5037 0.0401  0.0064  -0.0380 321 TRP A O   
2716  C CB  . TRP A 321 ? 0.2001 0.4588 0.4599 0.0227  0.0052  -0.0183 321 TRP A CB  
2717  C CG  . TRP A 321 ? 0.2440 0.5096 0.5089 0.0150  0.0080  -0.0099 321 TRP A CG  
2718  C CD1 . TRP A 321 ? 0.2438 0.5150 0.5110 0.0140  0.0174  -0.0067 321 TRP A CD1 
2719  C CD2 . TRP A 321 ? 0.2387 0.5052 0.5068 0.0072  0.0006  -0.0048 321 TRP A CD2 
2720  N NE1 . TRP A 321 ? 0.2697 0.5436 0.5434 0.0056  0.0162  0.0007  321 TRP A NE1 
2721  C CE2 . TRP A 321 ? 0.2881 0.5602 0.5600 0.0012  0.0054  0.0019  321 TRP A CE2 
2722  C CE3 . TRP A 321 ? 0.2271 0.4876 0.4938 0.0047  -0.0100 -0.0068 321 TRP A CE3 
2723  C CZ2 . TRP A 321 ? 0.2696 0.5439 0.5394 -0.0076 -0.0009 0.0051  321 TRP A CZ2 
2724  C CZ3 . TRP A 321 ? 0.2530 0.5158 0.5213 -0.0033 -0.0159 -0.0038 321 TRP A CZ3 
2725  C CH2 . TRP A 321 ? 0.2935 0.5652 0.5626 -0.0097 -0.0115 0.0007  321 TRP A CH2 
2726  N N   . ASN A 322 ? 0.1967 0.4529 0.4636 0.0427  -0.0004 -0.0336 322 ASN A N   
2727  C CA  . ASN A 322 ? 0.2679 0.5111 0.5317 0.0462  -0.0086 -0.0402 322 ASN A CA  
2728  C C   . ASN A 322 ? 0.2533 0.4836 0.5088 0.0376  -0.0138 -0.0382 322 ASN A C   
2729  O O   . ASN A 322 ? 0.2896 0.5213 0.5450 0.0300  -0.0149 -0.0319 322 ASN A O   
2730  C CB  . ASN A 322 ? 0.3700 0.6168 0.6469 0.0519  -0.0151 -0.0407 322 ASN A CB  
2731  C CG  . ASN A 322 ? 0.5078 0.7387 0.7830 0.0532  -0.0257 -0.0448 322 ASN A CG  
2732  O OD1 . ASN A 322 ? 0.5490 0.7734 0.8240 0.0472  -0.0326 -0.0412 322 ASN A OD1 
2733  N ND2 . ASN A 322 ? 0.5709 0.7947 0.8451 0.0616  -0.0276 -0.0525 322 ASN A ND2 
2734  N N   . ALA A 323 ? 0.3313 0.4046 0.5241 0.0596  -0.0809 -0.0708 323 ALA A N   
2735  C CA  . ALA A 323 ? 0.3599 0.4109 0.5204 0.0507  -0.0807 -0.0522 323 ALA A CA  
2736  C C   . ALA A 323 ? 0.3875 0.4272 0.5394 0.0595  -0.0980 -0.0508 323 ALA A C   
2737  O O   . ALA A 323 ? 0.3798 0.4224 0.5239 0.0513  -0.0942 -0.0434 323 ALA A O   
2738  C CB  . ALA A 323 ? 0.3129 0.3309 0.4412 0.0469  -0.0802 -0.0403 323 ALA A CB  
2739  N N   . GLU A 324 ? 0.4194 0.4435 0.5700 0.0770  -0.1182 -0.0582 324 GLU A N   
2740  C CA  . GLU A 324 ? 0.4919 0.5014 0.6299 0.0866  -0.1376 -0.0571 324 GLU A CA  
2741  C C   . GLU A 324 ? 0.4134 0.4596 0.5806 0.0838  -0.1353 -0.0662 324 GLU A C   
2742  O O   . GLU A 324 ? 0.4645 0.5029 0.6150 0.0783  -0.1379 -0.0580 324 GLU A O   
2743  C CB  . GLU A 324 ? 0.6400 0.6296 0.7762 0.1094  -0.1620 -0.0669 324 GLU A CB  
2744  C CG  . GLU A 324 ? 0.8160 0.7569 0.9066 0.1167  -0.1825 -0.0556 324 GLU A CG  
2745  C CD  . GLU A 324 ? 0.9643 0.9149 1.0626 0.1262  -0.1994 -0.0630 324 GLU A CD  
2746  O OE1 . GLU A 324 ? 1.0297 0.9487 1.0904 0.1231  -0.2084 -0.0510 324 GLU A OE1 
2747  O OE2 . GLU A 324 ? 0.9989 0.9870 1.1355 0.1316  -0.1982 -0.0812 324 GLU A OE2 
2748  N N   . ASP A 325 ? 0.2665 0.3525 0.4761 0.0857  -0.1291 -0.0841 325 ASP A N   
2749  C CA  . ASP A 325 ? 0.2767 0.3977 0.5142 0.0809  -0.1259 -0.0952 325 ASP A CA  
2750  C C   . ASP A 325 ? 0.2733 0.3973 0.4985 0.0602  -0.1057 -0.0828 325 ASP A C   
2751  O O   . ASP A 325 ? 0.3253 0.4558 0.5500 0.0554  -0.1073 -0.0824 325 ASP A O   
2752  C CB  . ASP A 325 ? 0.3493 0.5019 0.6191 0.0800  -0.1147 -0.1153 325 ASP A CB  
2753  C CG  . ASP A 325 ? 0.4792 0.6248 0.7541 0.0987  -0.1313 -0.1280 325 ASP A CG  
2754  O OD1 . ASP A 325 ? 0.5212 0.6327 0.7707 0.1123  -0.1509 -0.1200 325 ASP A OD1 
2755  O OD2 . ASP A 325 ? 0.5333 0.7051 0.8350 0.0992  -0.1246 -0.1466 325 ASP A OD2 
2756  N N   . ALA A 326 ? 0.2300 0.3483 0.4445 0.0489  -0.0878 -0.0732 326 ALA A N   
2757  C CA  . ALA A 326 ? 0.1948 0.3115 0.3944 0.0325  -0.0709 -0.0608 326 ALA A CA  
2758  C C   . ALA A 326 ? 0.2441 0.3353 0.4126 0.0314  -0.0778 -0.0461 326 ALA A C   
2759  O O   . ALA A 326 ? 0.2397 0.3358 0.4049 0.0238  -0.0725 -0.0433 326 ALA A O   
2760  C CB  . ALA A 326 ? 0.1459 0.2569 0.3360 0.0244  -0.0559 -0.0531 326 ALA A CB  
2761  N N   . VAL A 327 ? 0.2211 0.2827 0.3639 0.0375  -0.0882 -0.0371 327 VAL A N   
2762  C CA  . VAL A 327 ? 0.2818 0.3162 0.3905 0.0337  -0.0921 -0.0234 327 VAL A CA  
2763  C C   . VAL A 327 ? 0.2827 0.3147 0.3892 0.0397  -0.1069 -0.0276 327 VAL A C   
2764  O O   . VAL A 327 ? 0.3380 0.3656 0.4305 0.0321  -0.1028 -0.0213 327 VAL A O   
2765  C CB  . VAL A 327 ? 0.3084 0.3084 0.3871 0.0364  -0.0987 -0.0148 327 VAL A CB  
2766  C CG1 . VAL A 327 ? 0.3392 0.3071 0.3798 0.0331  -0.1056 -0.0040 327 VAL A CG1 
2767  C CG2 . VAL A 327 ? 0.3314 0.3341 0.4076 0.0262  -0.0820 -0.0087 327 VAL A CG2 
2768  N N   . ARG A 328 ? 0.2630 0.2987 0.3838 0.0542  -0.1251 -0.0395 328 ARG A N   
2769  C CA  . ARG A 328 ? 0.3521 0.3903 0.4745 0.0606  -0.1411 -0.0459 328 ARG A CA  
2770  C C   . ARG A 328 ? 0.3301 0.4010 0.4769 0.0500  -0.1288 -0.0530 328 ARG A C   
2771  O O   . ARG A 328 ? 0.3106 0.3775 0.4468 0.0471  -0.1341 -0.0518 328 ARG A O   
2772  C CB  . ARG A 328 ? 0.4409 0.4842 0.5817 0.0804  -0.1641 -0.0609 328 ARG A CB  
2773  C CG  . ARG A 328 ? 0.6487 0.6481 0.7558 0.0935  -0.1821 -0.0538 328 ARG A CG  
2774  C CD  . ARG A 328 ? 0.7938 0.7457 0.8454 0.0856  -0.1843 -0.0346 328 ARG A CD  
2775  N NE  . ARG A 328 ? 0.9175 0.8225 0.9325 0.0954  -0.1992 -0.0283 328 ARG A NE  
2776  C CZ  . ARG A 328 ? 1.0059 0.8727 0.9783 0.0836  -0.1904 -0.0128 328 ARG A CZ  
2777  N NH1 . ARG A 328 ? 1.0503 0.8706 0.9865 0.0915  -0.2042 -0.0082 328 ARG A NH1 
2778  N NH2 . ARG A 328 ? 0.9898 0.8649 0.9561 0.0637  -0.1674 -0.0033 328 ARG A NH2 
2779  N N   . ASP A 329 ? 0.2953 0.3947 0.4703 0.0427  -0.1117 -0.0603 329 ASP A N   
2780  C CA  . ASP A 329 ? 0.2456 0.3697 0.4378 0.0303  -0.0982 -0.0668 329 ASP A CA  
2781  C C   . ASP A 329 ? 0.2482 0.3544 0.4122 0.0182  -0.0853 -0.0510 329 ASP A C   
2782  O O   . ASP A 329 ? 0.2441 0.3520 0.4039 0.0122  -0.0843 -0.0519 329 ASP A O   
2783  C CB  . ASP A 329 ? 0.2604 0.4120 0.4815 0.0235  -0.0818 -0.0775 329 ASP A CB  
2784  C CG  . ASP A 329 ? 0.2593 0.4285 0.4901 0.0075  -0.0653 -0.0830 329 ASP A CG  
2785  O OD1 . ASP A 329 ? 0.1874 0.3433 0.3981 -0.0034 -0.0499 -0.0707 329 ASP A OD1 
2786  O OD2 . ASP A 329 ? 0.2697 0.4658 0.5279 0.0060  -0.0681 -0.1009 329 ASP A OD2 
2787  N N   . PHE A 330 ? 0.1671 0.2574 0.3130 0.0149  -0.0756 -0.0380 330 PHE A N   
2788  C CA  . PHE A 330 ? 0.1989 0.2750 0.3210 0.0058  -0.0638 -0.0248 330 PHE A CA  
2789  C C   . PHE A 330 ? 0.1877 0.2423 0.2837 0.0071  -0.0735 -0.0182 330 PHE A C   
2790  O O   . PHE A 330 ? 0.1986 0.2504 0.2847 0.0003  -0.0665 -0.0150 330 PHE A O   
2791  C CB  . PHE A 330 ? 0.1777 0.2444 0.2887 0.0040  -0.0553 -0.0150 330 PHE A CB  
2792  C CG  . PHE A 330 ? 0.2150 0.2779 0.3125 -0.0043 -0.0408 -0.0055 330 PHE A CG  
2793  C CD1 . PHE A 330 ? 0.1886 0.2639 0.2961 -0.0101 -0.0279 -0.0075 330 PHE A CD1 
2794  C CD2 . PHE A 330 ? 0.2550 0.3005 0.3284 -0.0062 -0.0402 0.0043  330 PHE A CD2 
2795  C CE1 . PHE A 330 ? 0.2023 0.2721 0.2966 -0.0143 -0.0175 0.0004  330 PHE A CE1 
2796  C CE2 . PHE A 330 ? 0.2661 0.3124 0.3316 -0.0114 -0.0281 0.0103  330 PHE A CE2 
2797  C CZ  . PHE A 330 ? 0.2354 0.2935 0.3118 -0.0137 -0.0181 0.0086  330 PHE A CZ  
2798  N N   . ILE A 331 ? 0.2341 0.2688 0.3141 0.0151  -0.0887 -0.0155 331 ILE A N   
2799  C CA  . ILE A 331 ? 0.3190 0.3280 0.3680 0.0151  -0.0985 -0.0095 331 ILE A CA  
2800  C C   . ILE A 331 ? 0.3566 0.3761 0.4149 0.0167  -0.1080 -0.0187 331 ILE A C   
2801  O O   . ILE A 331 ? 0.4033 0.4108 0.4412 0.0110  -0.1070 -0.0146 331 ILE A O   
2802  C CB  . ILE A 331 ? 0.3810 0.3605 0.4060 0.0234  -0.1148 -0.0055 331 ILE A CB  
2803  C CG1 . ILE A 331 ? 0.4245 0.3928 0.4384 0.0188  -0.1040 0.0029  331 ILE A CG1 
2804  C CG2 . ILE A 331 ? 0.4082 0.3554 0.3942 0.0224  -0.1261 0.0005  331 ILE A CG2 
2805  C CD1 . ILE A 331 ? 0.4129 0.3818 0.4153 0.0057  -0.0848 0.0115  331 ILE A CD1 
2806  N N   . GLY A 332 ? 0.3156 0.3589 0.4053 0.0241  -0.1174 -0.0329 332 GLY A N   
2807  C CA  . GLY A 332 ? 0.3135 0.3741 0.4181 0.0235  -0.1248 -0.0447 332 GLY A CA  
2808  C C   . GLY A 332 ? 0.3613 0.4314 0.4675 0.0089  -0.1058 -0.0437 332 GLY A C   
2809  O O   . GLY A 332 ? 0.3147 0.3810 0.4113 0.0048  -0.1097 -0.0458 332 GLY A O   
2810  N N   . ARG A 333 ? 0.3519 0.4312 0.4674 0.0014  -0.0861 -0.0406 333 ARG A N   
2811  C CA  . ARG A 333 ? 0.2683 0.3512 0.3819 -0.0109 -0.0692 -0.0399 333 ARG A CA  
2812  C C   . ARG A 333 ? 0.2535 0.3112 0.3345 -0.0142 -0.0647 -0.0273 333 ARG A C   
2813  O O   . ARG A 333 ? 0.3310 0.3849 0.4038 -0.0208 -0.0604 -0.0289 333 ARG A O   
2814  C CB  . ARG A 333 ? 0.2359 0.3290 0.3613 -0.0168 -0.0514 -0.0391 333 ARG A CB  
2815  C CG  . ARG A 333 ? 0.3422 0.4607 0.4990 -0.0158 -0.0525 -0.0530 333 ARG A CG  
2816  C CD  . ARG A 333 ? 0.4148 0.5441 0.5813 -0.0281 -0.0335 -0.0578 333 ARG A CD  
2817  N NE  . ARG A 333 ? 0.4075 0.5614 0.6034 -0.0273 -0.0329 -0.0716 333 ARG A NE  
2818  C CZ  . ARG A 333 ? 0.4864 0.6666 0.7108 -0.0274 -0.0396 -0.0902 333 ARG A CZ  
2819  N NH1 . ARG A 333 ? 0.5095 0.6938 0.7353 -0.0289 -0.0485 -0.0964 333 ARG A NH1 
2820  N NH2 . ARG A 333 ? 0.5159 0.7203 0.7686 -0.0262 -0.0375 -0.1042 333 ARG A NH2 
2821  N N   . LEU A 334 ? 0.2844 0.3257 0.3471 -0.0109 -0.0637 -0.0159 334 LEU A N   
2822  C CA  . LEU A 334 ? 0.3144 0.3343 0.3474 -0.0143 -0.0594 -0.0064 334 LEU A CA  
2823  C C   . LEU A 334 ? 0.2943 0.3002 0.3093 -0.0139 -0.0727 -0.0088 334 LEU A C   
2824  O O   . LEU A 334 ? 0.3417 0.3366 0.3387 -0.0196 -0.0667 -0.0065 334 LEU A O   
2825  C CB  . LEU A 334 ? 0.3424 0.3492 0.3604 -0.0126 -0.0577 0.0030  334 LEU A CB  
2826  C CG  . LEU A 334 ? 0.3013 0.3210 0.3338 -0.0134 -0.0450 0.0058  334 LEU A CG  
2827  C CD1 . LEU A 334 ? 0.2934 0.3017 0.3128 -0.0128 -0.0457 0.0126  334 LEU A CD1 
2828  C CD2 . LEU A 334 ? 0.3138 0.3370 0.3444 -0.0180 -0.0297 0.0082  334 LEU A CD2 
2829  N N   . LYS A 335 ? 0.3409 0.3462 0.3598 -0.0063 -0.0919 -0.0143 335 LYS A N   
2830  C CA  . LYS A 335 ? 0.3354 0.3256 0.3346 -0.0046 -0.1082 -0.0169 335 LYS A CA  
2831  C C   . LYS A 335 ? 0.3773 0.3820 0.3880 -0.0109 -0.1057 -0.0263 335 LYS A C   
2832  O O   . LYS A 335 ? 0.4019 0.3903 0.3883 -0.0154 -0.1083 -0.0250 335 LYS A O   
2833  C CB  . LYS A 335 ? 0.3714 0.3591 0.3749 0.0082  -0.1322 -0.0226 335 LYS A CB  
2834  C CG  . LYS A 335 ? 0.5221 0.4959 0.5068 0.0116  -0.1526 -0.0272 335 LYS A CG  
2835  C CD  . LYS A 335 ? 0.6826 0.6308 0.6458 0.0249  -0.1773 -0.0254 335 LYS A CD  
2836  C CE  . LYS A 335 ? 0.7538 0.7278 0.7552 0.0394  -0.1920 -0.0382 335 LYS A CE  
2837  N NZ  . LYS A 335 ? 0.8586 0.8051 0.8373 0.0557  -0.2217 -0.0390 335 LYS A NZ  
2838  N N   . LYS A 336 ? 0.3310 0.3647 0.3762 -0.0131 -0.0999 -0.0367 336 LYS A N   
2839  C CA  . LYS A 336 ? 0.3711 0.4169 0.4254 -0.0224 -0.0950 -0.0464 336 LYS A CA  
2840  C C   . LYS A 336 ? 0.3258 0.3559 0.3597 -0.0319 -0.0756 -0.0383 336 LYS A C   
2841  O O   . LYS A 336 ? 0.3748 0.3971 0.3960 -0.0386 -0.0746 -0.0416 336 LYS A O   
2842  C CB  . LYS A 336 ? 0.4746 0.5531 0.5675 -0.0258 -0.0901 -0.0603 336 LYS A CB  
2843  C CG  . LYS A 336 ? 0.5798 0.6767 0.6981 -0.0143 -0.1034 -0.0676 336 LYS A CG  
2844  C CD  . LYS A 336 ? 0.6827 0.7796 0.8006 -0.0028 -0.1306 -0.0751 336 LYS A CD  
2845  C CE  . LYS A 336 ? 0.7072 0.8154 0.8456 0.0126  -0.1452 -0.0809 336 LYS A CE  
2846  N NZ  . LYS A 336 ? 0.6940 0.7668 0.7990 0.0232  -0.1559 -0.0659 336 LYS A NZ  
2847  N N   . ILE A 337 ? 0.2965 0.3220 0.3276 -0.0318 -0.0608 -0.0289 337 ILE A N   
2848  C CA  . ILE A 337 ? 0.3045 0.3139 0.3154 -0.0367 -0.0452 -0.0216 337 ILE A CA  
2849  C C   . ILE A 337 ? 0.3156 0.3031 0.2962 -0.0365 -0.0501 -0.0165 337 ILE A C   
2850  O O   . ILE A 337 ? 0.3847 0.3606 0.3493 -0.0419 -0.0441 -0.0177 337 ILE A O   
2851  C CB  . ILE A 337 ? 0.2580 0.2685 0.2721 -0.0338 -0.0326 -0.0133 337 ILE A CB  
2852  C CG1 . ILE A 337 ? 0.2538 0.2804 0.2909 -0.0365 -0.0253 -0.0184 337 ILE A CG1 
2853  C CG2 . ILE A 337 ? 0.2337 0.2292 0.2283 -0.0351 -0.0197 -0.0073 337 ILE A CG2 
2854  C CD1 . ILE A 337 ? 0.2805 0.3099 0.3219 -0.0324 -0.0172 -0.0109 337 ILE A CD1 
2855  N N   . HIS A 338 ? 0.3403 0.3186 0.3091 -0.0314 -0.0601 -0.0111 338 HIS A N   
2856  C CA  . HIS A 338 ? 0.3721 0.3254 0.3062 -0.0338 -0.0632 -0.0061 338 HIS A CA  
2857  C C   . HIS A 338 ? 0.4763 0.4221 0.3986 -0.0370 -0.0745 -0.0132 338 HIS A C   
2858  O O   . HIS A 338 ? 0.5241 0.4526 0.4208 -0.0429 -0.0689 -0.0120 338 HIS A O   
2859  C CB  . HIS A 338 ? 0.3643 0.3039 0.2837 -0.0293 -0.0738 0.0001  338 HIS A CB  
2860  C CG  . HIS A 338 ? 0.4155 0.3243 0.2932 -0.0339 -0.0781 0.0047  338 HIS A CG  
2861  N ND1 . HIS A 338 ? 0.5071 0.3961 0.3631 -0.0305 -0.0996 0.0039  338 HIS A ND1 
2862  C CD2 . HIS A 338 ? 0.4389 0.3322 0.2908 -0.0419 -0.0637 0.0092  338 HIS A CD2 
2863  C CE1 . HIS A 338 ? 0.5196 0.3782 0.3336 -0.0379 -0.0976 0.0089  338 HIS A CE1 
2864  N NE2 . HIS A 338 ? 0.5328 0.3956 0.3453 -0.0457 -0.0747 0.0115  338 HIS A NE2 
2865  N N   . GLU A 339 ? 0.4766 0.4378 0.4191 -0.0334 -0.0899 -0.0222 339 GLU A N   
2866  C CA  . GLU A 339 ? 0.5092 0.4681 0.4445 -0.0361 -0.1034 -0.0311 339 GLU A CA  
2867  C C   . GLU A 339 ? 0.4638 0.4358 0.4133 -0.0455 -0.0917 -0.0397 339 GLU A C   
2868  O O   . GLU A 339 ? 0.5328 0.5030 0.4753 -0.0502 -0.1006 -0.0479 339 GLU A O   
2869  C CB  . GLU A 339 ? 0.5173 0.4898 0.4703 -0.0267 -0.1279 -0.0397 339 GLU A CB  
2870  C CG  . GLU A 339 ? 0.6357 0.5855 0.5655 -0.0167 -0.1440 -0.0318 339 GLU A CG  
2871  C CD  . GLU A 339 ? 0.7191 0.6868 0.6758 -0.0034 -0.1652 -0.0407 339 GLU A CD  
2872  O OE1 . GLU A 339 ? 0.7557 0.7591 0.7545 -0.0032 -0.1618 -0.0524 339 GLU A OE1 
2873  O OE2 . GLU A 339 ? 0.7471 0.6919 0.6815 0.0068  -0.1846 -0.0367 339 GLU A OE2 
2874  N N   . SER A 340 ? 0.4167 0.3985 0.3822 -0.0488 -0.0729 -0.0382 340 SER A N   
2875  C CA  . SER A 340 ? 0.3961 0.3838 0.3696 -0.0588 -0.0615 -0.0463 340 SER A CA  
2876  C C   . SER A 340 ? 0.3921 0.3553 0.3370 -0.0643 -0.0480 -0.0419 340 SER A C   
2877  O O   . SER A 340 ? 0.4487 0.4087 0.3914 -0.0734 -0.0413 -0.0492 340 SER A O   
2878  C CB  . SER A 340 ? 0.4030 0.4068 0.4014 -0.0607 -0.0482 -0.0475 340 SER A CB  
2879  O OG  . SER A 340 ? 0.4346 0.4248 0.4214 -0.0578 -0.0329 -0.0363 340 SER A OG  
2880  N N   . VAL A 341 ? 0.3877 0.3335 0.3106 -0.0598 -0.0430 -0.0318 341 VAL A N   
2881  C CA  . VAL A 341 ? 0.4773 0.4028 0.3766 -0.0633 -0.0289 -0.0298 341 VAL A CA  
2882  C C   . VAL A 341 ? 0.4819 0.3886 0.3508 -0.0635 -0.0336 -0.0260 341 VAL A C   
2883  O O   . VAL A 341 ? 0.4385 0.3440 0.3021 -0.0597 -0.0435 -0.0210 341 VAL A O   
2884  C CB  . VAL A 341 ? 0.4389 0.3642 0.3437 -0.0584 -0.0117 -0.0237 341 VAL A CB  
2885  C CG1 . VAL A 341 ? 0.4596 0.3942 0.3839 -0.0607 -0.0058 -0.0273 341 VAL A CG1 
2886  C CG2 . VAL A 341 ? 0.4587 0.3915 0.3690 -0.0511 -0.0126 -0.0154 341 VAL A CG2 
2887  N N   . ASP A 342 ? 0.5410 0.4296 0.3865 -0.0689 -0.0255 -0.0288 342 ASP A N   
2888  C CA  . ASP A 342 ? 0.5666 0.4345 0.3787 -0.0717 -0.0262 -0.0264 342 ASP A CA  
2889  C C   . ASP A 342 ? 0.5605 0.4243 0.3651 -0.0689 -0.0095 -0.0209 342 ASP A C   
2890  O O   . ASP A 342 ? 0.6499 0.4986 0.4276 -0.0729 -0.0080 -0.0189 342 ASP A O   
2891  C CB  . ASP A 342 ? 0.7303 0.5809 0.5195 -0.0799 -0.0249 -0.0339 342 ASP A CB  
2892  C CG  . ASP A 342 ? 0.8234 0.6712 0.6036 -0.0843 -0.0466 -0.0390 342 ASP A CG  
2893  O OD1 . ASP A 342 ? 0.8439 0.7113 0.6493 -0.0808 -0.0608 -0.0414 342 ASP A OD1 
2894  O OD2 . ASP A 342 ? 0.8946 0.7214 0.6427 -0.0908 -0.0500 -0.0419 342 ASP A OD2 
2895  N N   . PHE A 343 ? 0.5228 0.3997 0.3494 -0.0626 0.0030  -0.0194 343 PHE A N   
2896  C CA  . PHE A 343 ? 0.5042 0.3838 0.3296 -0.0587 0.0175  -0.0167 343 PHE A CA  
2897  C C   . PHE A 343 ? 0.4662 0.3622 0.3096 -0.0544 0.0138  -0.0101 343 PHE A C   
2898  O O   . PHE A 343 ? 0.4696 0.3722 0.3243 -0.0535 0.0003  -0.0076 343 PHE A O   
2899  C CB  . PHE A 343 ? 0.4507 0.3312 0.2848 -0.0525 0.0320  -0.0206 343 PHE A CB  
2900  C CG  . PHE A 343 ? 0.4109 0.3012 0.2686 -0.0470 0.0303  -0.0192 343 PHE A CG  
2901  C CD1 . PHE A 343 ? 0.4106 0.2944 0.2689 -0.0522 0.0250  -0.0230 343 PHE A CD1 
2902  C CD2 . PHE A 343 ? 0.3973 0.3027 0.2746 -0.0383 0.0348  -0.0150 343 PHE A CD2 
2903  C CE1 . PHE A 343 ? 0.4326 0.3224 0.3083 -0.0502 0.0259  -0.0224 343 PHE A CE1 
2904  C CE2 . PHE A 343 ? 0.4202 0.3303 0.3136 -0.0345 0.0338  -0.0135 343 PHE A CE2 
2905  C CZ  . PHE A 343 ? 0.4450 0.3459 0.3362 -0.0412 0.0303  -0.0171 343 PHE A CZ  
2906  N N   . GLN A 344 ? 0.4505 0.3540 0.2969 -0.0519 0.0258  -0.0087 344 GLN A N   
2907  C CA  . GLN A 344 ? 0.3406 0.2592 0.2032 -0.0490 0.0233  -0.0031 344 GLN A CA  
2908  C C   . GLN A 344 ? 0.3470 0.2834 0.2386 -0.0395 0.0274  -0.0026 344 GLN A C   
2909  O O   . GLN A 344 ? 0.3933 0.3370 0.2918 -0.0337 0.0390  -0.0053 344 GLN A O   
2910  C CB  . GLN A 344 ? 0.3858 0.3050 0.2364 -0.0541 0.0339  -0.0031 344 GLN A CB  
2911  C CG  . GLN A 344 ? 0.4142 0.3087 0.2275 -0.0657 0.0315  -0.0035 344 GLN A CG  
2912  C CD  . GLN A 344 ? 0.4738 0.3670 0.2717 -0.0749 0.0442  -0.0045 344 GLN A CD  
2913  O OE1 . GLN A 344 ? 0.4749 0.3538 0.2529 -0.0827 0.0382  0.0005  344 GLN A OE1 
2914  N NE2 . GLN A 344 ? 0.4596 0.3662 0.2652 -0.0744 0.0621  -0.0123 344 GLN A NE2 
2915  N N   . PRO A 345 ? 0.3427 0.2858 0.2504 -0.0373 0.0178  -0.0002 345 PRO A N   
2916  C CA  . PRO A 345 ? 0.2917 0.2463 0.2205 -0.0301 0.0219  0.0005  345 PRO A CA  
2917  C C   . PRO A 345 ? 0.2989 0.2696 0.2415 -0.0252 0.0257  0.0042  345 PRO A C   
2918  O O   . PRO A 345 ? 0.3780 0.3528 0.3184 -0.0288 0.0227  0.0069  345 PRO A O   
2919  C CB  . PRO A 345 ? 0.2686 0.2267 0.2088 -0.0327 0.0113  0.0001  345 PRO A CB  
2920  C CG  . PRO A 345 ? 0.2970 0.2547 0.2320 -0.0360 -0.0002 0.0017  345 PRO A CG  
2921  C CD  . PRO A 345 ? 0.3649 0.3064 0.2728 -0.0406 0.0023  0.0012  345 PRO A CD  
2922  N N   . VAL A 346 ? 0.2695 0.2469 0.2239 -0.0171 0.0314  0.0040  346 VAL A N   
2923  C CA  . VAL A 346 ? 0.3098 0.3046 0.2794 -0.0117 0.0335  0.0064  346 VAL A CA  
2924  C C   . VAL A 346 ? 0.3104 0.3085 0.2923 -0.0097 0.0282  0.0098  346 VAL A C   
2925  O O   . VAL A 346 ? 0.2896 0.2778 0.2694 -0.0072 0.0294  0.0089  346 VAL A O   
2926  C CB  . VAL A 346 ? 0.3261 0.3276 0.2991 -0.0021 0.0423  0.0023  346 VAL A CB  
2927  C CG1 . VAL A 346 ? 0.3465 0.3693 0.3371 0.0029  0.0423  0.0036  346 VAL A CG1 
2928  C CG2 . VAL A 346 ? 0.3627 0.3635 0.3248 -0.0059 0.0500  -0.0034 346 VAL A CG2 
2929  N N   . VAL A 347 ? 0.3142 0.3233 0.3060 -0.0122 0.0231  0.0129  347 VAL A N   
2930  C CA  . VAL A 347 ? 0.2832 0.2960 0.2864 -0.0126 0.0185  0.0145  347 VAL A CA  
2931  C C   . VAL A 347 ? 0.2309 0.2572 0.2452 -0.0080 0.0200  0.0173  347 VAL A C   
2932  O O   . VAL A 347 ? 0.2717 0.3073 0.2902 -0.0102 0.0181  0.0189  347 VAL A O   
2933  C CB  . VAL A 347 ? 0.3127 0.3262 0.3189 -0.0184 0.0093  0.0139  347 VAL A CB  
2934  C CG1 . VAL A 347 ? 0.2606 0.2804 0.2810 -0.0193 0.0068  0.0121  347 VAL A CG1 
2935  C CG2 . VAL A 347 ? 0.3691 0.3705 0.3625 -0.0228 0.0056  0.0104  347 VAL A CG2 
2936  N N   . PHE A 348 ? 0.2640 0.2880 0.2796 -0.0022 0.0227  0.0178  348 PHE A N   
2937  C CA  . PHE A 348 ? 0.2317 0.2671 0.2556 0.0033  0.0226  0.0199  348 PHE A CA  
2938  C C   . PHE A 348 ? 0.2435 0.2801 0.2734 -0.0010 0.0197  0.0215  348 PHE A C   
2939  O O   . PHE A 348 ? 0.2774 0.3022 0.3021 -0.0038 0.0209  0.0206  348 PHE A O   
2940  C CB  . PHE A 348 ? 0.2118 0.2401 0.2291 0.0140  0.0250  0.0192  348 PHE A CB  
2941  C CG  . PHE A 348 ? 0.2666 0.3091 0.2896 0.0217  0.0272  0.0157  348 PHE A CG  
2942  C CD1 . PHE A 348 ? 0.2968 0.3391 0.3159 0.0199  0.0318  0.0117  348 PHE A CD1 
2943  C CD2 . PHE A 348 ? 0.2686 0.3259 0.3009 0.0304  0.0249  0.0149  348 PHE A CD2 
2944  C CE1 . PHE A 348 ? 0.2537 0.3125 0.2802 0.0258  0.0360  0.0057  348 PHE A CE1 
2945  C CE2 . PHE A 348 ? 0.2268 0.3032 0.2692 0.0373  0.0274  0.0085  348 PHE A CE2 
2946  C CZ  . PHE A 348 ? 0.2833 0.3614 0.3237 0.0345  0.0340  0.0033  348 PHE A CZ  
2947  N N   . VAL A 349 ? 0.2148 0.2648 0.2546 -0.0031 0.0170  0.0228  349 VAL A N   
2948  C CA  . VAL A 349 ? 0.1537 0.2072 0.2007 -0.0062 0.0150  0.0232  349 VAL A CA  
2949  C C   . VAL A 349 ? 0.2072 0.2674 0.2552 -0.0010 0.0156  0.0253  349 VAL A C   
2950  O O   . VAL A 349 ? 0.2348 0.3082 0.2885 0.0004  0.0147  0.0256  349 VAL A O   
2951  C CB  . VAL A 349 ? 0.1770 0.2368 0.2317 -0.0110 0.0103  0.0224  349 VAL A CB  
2952  C CG1 . VAL A 349 ? 0.2191 0.2846 0.2827 -0.0128 0.0091  0.0214  349 VAL A CG1 
2953  C CG2 . VAL A 349 ? 0.1878 0.2404 0.2407 -0.0141 0.0063  0.0193  349 VAL A CG2 
2954  N N   . VAL A 350 ? 0.2357 0.2853 0.2756 0.0011  0.0169  0.0262  350 VAL A N   
2955  C CA  . VAL A 350 ? 0.2379 0.2895 0.2738 0.0083  0.0149  0.0282  350 VAL A CA  
2956  C C   . VAL A 350 ? 0.2346 0.2790 0.2650 0.0033  0.0156  0.0291  350 VAL A C   
2957  O O   . VAL A 350 ? 0.2039 0.2305 0.2223 -0.0017 0.0195  0.0285  350 VAL A O   
2958  C CB  . VAL A 350 ? 0.2346 0.2722 0.2568 0.0188  0.0144  0.0287  350 VAL A CB  
2959  C CG1 . VAL A 350 ? 0.2656 0.3077 0.2851 0.0291  0.0086  0.0297  350 VAL A CG1 
2960  C CG2 . VAL A 350 ? 0.2814 0.3262 0.3090 0.0227  0.0159  0.0258  350 VAL A CG2 
2961  N N   . LEU A 351 ? 0.2205 0.2780 0.2581 0.0030  0.0129  0.0295  351 LEU A N   
2962  C CA  . LEU A 351 ? 0.2636 0.3136 0.2932 -0.0017 0.0140  0.0298  351 LEU A CA  
2963  C C   . LEU A 351 ? 0.2209 0.2848 0.2549 0.0017  0.0090  0.0306  351 LEU A C   
2964  O O   . LEU A 351 ? 0.1753 0.2568 0.2208 0.0060  0.0057  0.0298  351 LEU A O   
2965  C CB  . LEU A 351 ? 0.2667 0.3187 0.3053 -0.0124 0.0187  0.0257  351 LEU A CB  
2966  C CG  . LEU A 351 ? 0.2516 0.3205 0.3090 -0.0146 0.0162  0.0234  351 LEU A CG  
2967  C CD1 . LEU A 351 ? 0.2638 0.3351 0.3286 -0.0217 0.0191  0.0181  351 LEU A CD1 
2968  C CD2 . LEU A 351 ? 0.3078 0.3775 0.3707 -0.0138 0.0150  0.0225  351 LEU A CD2 
2969  N N   . ASN A 352 ? 0.2214 0.2769 0.2443 -0.0017 0.0092  0.0311  352 ASN A N   
2970  C CA  . ASN A 352 ? 0.2363 0.3050 0.2628 -0.0006 0.0043  0.0309  352 ASN A CA  
2971  C C   . ASN A 352 ? 0.1972 0.2845 0.2437 -0.0070 0.0058  0.0280  352 ASN A C   
2972  O O   . ASN A 352 ? 0.1953 0.2801 0.2483 -0.0133 0.0102  0.0259  352 ASN A O   
2973  C CB  . ASN A 352 ? 0.2797 0.3324 0.2872 -0.0056 0.0055  0.0315  352 ASN A CB  
2974  C CG  . ASN A 352 ? 0.3409 0.3771 0.3247 0.0037  -0.0018 0.0352  352 ASN A CG  
2975  O OD1 . ASN A 352 ? 0.3483 0.3586 0.3105 0.0058  -0.0003 0.0378  352 ASN A OD1 
2976  N ND2 . ASN A 352 ? 0.2918 0.3409 0.2771 0.0094  -0.0107 0.0349  352 ASN A ND2 
2977  N N   . GLY A 353 ? 0.1359 0.2414 0.1918 -0.0052 0.0017  0.0270  353 GLY A N   
2978  C CA  . GLY A 353 ? 0.1543 0.2715 0.2225 -0.0124 0.0031  0.0246  353 GLY A CA  
2979  C C   . GLY A 353 ? 0.2153 0.3332 0.2830 -0.0194 0.0033  0.0227  353 GLY A C   
2980  O O   . GLY A 353 ? 0.1696 0.2916 0.2436 -0.0255 0.0042  0.0208  353 GLY A O   
2981  N N   . GLU A 354 ? 0.2039 0.3134 0.2604 -0.0196 0.0029  0.0229  354 GLU A N   
2982  C CA  . GLU A 354 ? 0.1895 0.3011 0.2446 -0.0262 0.0031  0.0202  354 GLU A CA  
2983  C C   . GLU A 354 ? 0.2042 0.3009 0.2493 -0.0310 0.0083  0.0183  354 GLU A C   
2984  O O   . GLU A 354 ? 0.2613 0.3582 0.3052 -0.0369 0.0097  0.0149  354 GLU A O   
2985  C CB  . GLU A 354 ? 0.2195 0.3431 0.2709 -0.0237 -0.0039 0.0198  354 GLU A CB  
2986  C CG  . GLU A 354 ? 0.2253 0.3366 0.2568 -0.0184 -0.0085 0.0222  354 GLU A CG  
2987  C CD  . GLU A 354 ? 0.2374 0.3429 0.2624 -0.0066 -0.0130 0.0256  354 GLU A CD  
2988  O OE1 . GLU A 354 ? 0.2197 0.3308 0.2395 0.0028  -0.0229 0.0255  354 GLU A OE1 
2989  O OE2 . GLU A 354 ? 0.2465 0.3412 0.2714 -0.0059 -0.0076 0.0275  354 GLU A OE2 
2990  N N   . ASN A 355 ? 0.2127 0.2964 0.2504 -0.0305 0.0127  0.0190  355 ASN A N   
2991  C CA  . ASN A 355 ? 0.2113 0.2817 0.2369 -0.0377 0.0199  0.0154  355 ASN A CA  
2992  C C   . ASN A 355 ? 0.2226 0.2952 0.2633 -0.0429 0.0276  0.0082  355 ASN A C   
2993  O O   . ASN A 355 ? 0.1883 0.2567 0.2256 -0.0504 0.0351  0.0017  355 ASN A O   
2994  C CB  . ASN A 355 ? 0.2441 0.2945 0.2452 -0.0367 0.0209  0.0193  355 ASN A CB  
2995  C CG  . ASN A 355 ? 0.2716 0.3176 0.2552 -0.0293 0.0107  0.0247  355 ASN A CG  
2996  O OD1 . ASN A 355 ? 0.3189 0.3748 0.3042 -0.0298 0.0060  0.0237  355 ASN A OD1 
2997  N ND2 . ASN A 355 ? 0.2596 0.2907 0.2267 -0.0216 0.0064  0.0296  355 ASN A ND2 
2998  N N   . CYS A 356 ? 0.2156 0.2953 0.2727 -0.0390 0.0257  0.0077  356 CYS A N   
2999  C CA  . CYS A 356 ? 0.1647 0.2484 0.2375 -0.0416 0.0305  -0.0007 356 CYS A CA  
3000  C C   . CYS A 356 ? 0.1792 0.2703 0.2668 -0.0402 0.0276  -0.0061 356 CYS A C   
3001  O O   . CYS A 356 ? 0.2781 0.3736 0.3787 -0.0417 0.0315  -0.0161 356 CYS A O   
3002  C CB  . CYS A 356 ? 0.2188 0.3038 0.2993 -0.0378 0.0283  0.0004  356 CYS A CB  
3003  S SG  . CYS A 356 ? 0.2075 0.2970 0.2930 -0.0300 0.0184  0.0074  356 CYS A SG  
3004  N N   . TRP A 357 ? 0.2359 0.3278 0.3210 -0.0378 0.0212  -0.0011 357 TRP A N   
3005  C CA  . TRP A 357 ? 0.2199 0.3113 0.3136 -0.0361 0.0174  -0.0051 357 TRP A CA  
3006  C C   . TRP A 357 ? 0.2188 0.3091 0.3133 -0.0400 0.0220  -0.0130 357 TRP A C   
3007  O O   . TRP A 357 ? 0.2224 0.3108 0.3271 -0.0367 0.0201  -0.0202 357 TRP A O   
3008  C CB  . TRP A 357 ? 0.2066 0.2966 0.2935 -0.0362 0.0116  0.0017  357 TRP A CB  
3009  C CG  . TRP A 357 ? 0.2630 0.3560 0.3479 -0.0336 0.0093  0.0083  357 TRP A CG  
3010  C CD1 . TRP A 357 ? 0.2446 0.3445 0.3233 -0.0340 0.0087  0.0132  357 TRP A CD1 
3011  C CD2 . TRP A 357 ? 0.2580 0.3485 0.3479 -0.0293 0.0069  0.0090  357 TRP A CD2 
3012  N NE1 . TRP A 357 ? 0.2658 0.3671 0.3456 -0.0303 0.0075  0.0167  357 TRP A NE1 
3013  C CE2 . TRP A 357 ? 0.2362 0.3306 0.3211 -0.0282 0.0067  0.0148  357 TRP A CE2 
3014  C CE3 . TRP A 357 ? 0.2659 0.3522 0.3646 -0.0255 0.0041  0.0041  357 TRP A CE3 
3015  C CZ2 . TRP A 357 ? 0.2030 0.2947 0.2886 -0.0251 0.0050  0.0167  357 TRP A CZ2 
3016  C CZ3 . TRP A 357 ? 0.2840 0.3683 0.3832 -0.0222 0.0007  0.0063  357 TRP A CZ3 
3017  C CH2 . TRP A 357 ? 0.2211 0.3070 0.3125 -0.0229 0.0020  0.0129  357 TRP A CH2 
3018  N N   . GLU A 358 ? 0.1942 0.2834 0.2761 -0.0461 0.0272  -0.0124 358 GLU A N   
3019  C CA  . GLU A 358 ? 0.1564 0.2433 0.2369 -0.0510 0.0329  -0.0209 358 GLU A CA  
3020  C C   . GLU A 358 ? 0.1959 0.2877 0.2919 -0.0512 0.0403  -0.0334 358 GLU A C   
3021  O O   . GLU A 358 ? 0.1763 0.2685 0.2775 -0.0529 0.0448  -0.0436 358 GLU A O   
3022  C CB  . GLU A 358 ? 0.1672 0.2489 0.2263 -0.0583 0.0367  -0.0180 358 GLU A CB  
3023  C CG  . GLU A 358 ? 0.2987 0.3753 0.3463 -0.0608 0.0415  -0.0152 358 GLU A CG  
3024  C CD  . GLU A 358 ? 0.3478 0.4147 0.3691 -0.0634 0.0385  -0.0080 358 GLU A CD  
3025  O OE1 . GLU A 358 ? 0.4415 0.4960 0.4432 -0.0713 0.0457  -0.0109 358 GLU A OE1 
3026  O OE2 . GLU A 358 ? 0.2904 0.3619 0.3100 -0.0576 0.0287  -0.0004 358 GLU A OE2 
3027  N N   . TYR A 359 ? 0.1516 0.2487 0.2563 -0.0498 0.0420  -0.0347 359 TYR A N   
3028  C CA  . TYR A 359 ? 0.2410 0.3489 0.3655 -0.0507 0.0489  -0.0492 359 TYR A CA  
3029  C C   . TYR A 359 ? 0.2396 0.3552 0.3873 -0.0390 0.0392  -0.0548 359 TYR A C   
3030  O O   . TYR A 359 ? 0.1895 0.3186 0.3593 -0.0370 0.0423  -0.0696 359 TYR A O   
3031  C CB  . TYR A 359 ? 0.2875 0.3963 0.4068 -0.0585 0.0574  -0.0498 359 TYR A CB  
3032  C CG  . TYR A 359 ? 0.3462 0.4404 0.4361 -0.0694 0.0659  -0.0446 359 TYR A CG  
3033  C CD1 . TYR A 359 ? 0.3441 0.4365 0.4272 -0.0802 0.0785  -0.0550 359 TYR A CD1 
3034  C CD2 . TYR A 359 ? 0.3731 0.4538 0.4402 -0.0681 0.0605  -0.0301 359 TYR A CD2 
3035  C CE1 . TYR A 359 ? 0.3750 0.4484 0.4247 -0.0903 0.0848  -0.0496 359 TYR A CE1 
3036  C CE2 . TYR A 359 ? 0.4168 0.4800 0.4532 -0.0756 0.0649  -0.0252 359 TYR A CE2 
3037  C CZ  . TYR A 359 ? 0.4597 0.5172 0.4852 -0.0871 0.0766  -0.0341 359 TYR A CZ  
3038  O OH  . TYR A 359 ? 0.4922 0.5268 0.4806 -0.0947 0.0796  -0.0284 359 TYR A OH  
3039  N N   . TYR A 360 ? 0.2453 0.3523 0.3877 -0.0317 0.0273  -0.0445 360 TYR A N   
3040  C CA  . TYR A 360 ? 0.2494 0.3554 0.4052 -0.0202 0.0159  -0.0483 360 TYR A CA  
3041  C C   . TYR A 360 ? 0.2445 0.3410 0.4003 -0.0151 0.0118  -0.0537 360 TYR A C   
3042  O O   . TYR A 360 ? 0.2503 0.3378 0.3905 -0.0210 0.0151  -0.0489 360 TYR A O   
3043  C CB  . TYR A 360 ? 0.1999 0.2951 0.3432 -0.0170 0.0064  -0.0348 360 TYR A CB  
3044  C CG  . TYR A 360 ? 0.1736 0.2742 0.3177 -0.0179 0.0065  -0.0302 360 TYR A CG  
3045  C CD1 . TYR A 360 ? 0.1310 0.2348 0.2664 -0.0259 0.0153  -0.0254 360 TYR A CD1 
3046  C CD2 . TYR A 360 ? 0.1713 0.2693 0.3204 -0.0103 -0.0038 -0.0301 360 TYR A CD2 
3047  C CE1 . TYR A 360 ? 0.1705 0.2753 0.3040 -0.0263 0.0152  -0.0212 360 TYR A CE1 
3048  C CE2 . TYR A 360 ? 0.1888 0.2901 0.3368 -0.0117 -0.0037 -0.0261 360 TYR A CE2 
3049  C CZ  . TYR A 360 ? 0.1724 0.2771 0.3133 -0.0197 0.0062  -0.0219 360 TYR A CZ  
3050  O OH  . TYR A 360 ? 0.1727 0.2777 0.3111 -0.0206 0.0062  -0.0188 360 TYR A OH  
3051  N N   . GLU A 361 ? 0.2093 0.3058 0.3808 -0.0030 0.0028  -0.0637 361 GLU A N   
3052  C CA  . GLU A 361 ? 0.2931 0.3722 0.4591 0.0044  -0.0042 -0.0671 361 GLU A CA  
3053  C C   . GLU A 361 ? 0.2886 0.3434 0.4261 0.0004  -0.0097 -0.0514 361 GLU A C   
3054  O O   . GLU A 361 ? 0.3117 0.3607 0.4392 -0.0002 -0.0150 -0.0408 361 GLU A O   
3055  C CB  . GLU A 361 ? 0.4298 0.5080 0.6134 0.0216  -0.0176 -0.0788 361 GLU A CB  
3056  C CG  . GLU A 361 ? 0.5568 0.6659 0.7752 0.0254  -0.0120 -0.0987 361 GLU A CG  
3057  C CD  . GLU A 361 ? 0.6773 0.7988 0.9046 0.0177  0.0039  -0.1112 361 GLU A CD  
3058  O OE1 . GLU A 361 ? 0.7369 0.8411 0.9450 0.0130  0.0076  -0.1062 361 GLU A OE1 
3059  O OE2 . GLU A 361 ? 0.7045 0.8535 0.9572 0.0145  0.0139  -0.1272 361 GLU A OE2 
3060  N N   . GLU A 362 ? 0.3188 0.3602 0.4429 -0.0039 -0.0070 -0.0513 362 GLU A N   
3061  C CA  . GLU A 362 ? 0.3305 0.3507 0.4282 -0.0112 -0.0097 -0.0395 362 GLU A CA  
3062  C C   . GLU A 362 ? 0.3556 0.3855 0.4451 -0.0211 -0.0060 -0.0272 362 GLU A C   
3063  O O   . GLU A 362 ? 0.3732 0.3904 0.4472 -0.0241 -0.0106 -0.0183 362 GLU A O   
3064  C CB  . GLU A 362 ? 0.4483 0.4389 0.5319 -0.0023 -0.0230 -0.0377 362 GLU A CB  
3065  C CG  . GLU A 362 ? 0.5811 0.5492 0.6573 0.0034  -0.0266 -0.0461 362 GLU A CG  
3066  C CD  . GLU A 362 ? 0.7222 0.6575 0.7842 0.0168  -0.0424 -0.0462 362 GLU A CD  
3067  O OE1 . GLU A 362 ? 0.8081 0.7436 0.8869 0.0338  -0.0507 -0.0586 362 GLU A OE1 
3068  O OE2 . GLU A 362 ? 0.7158 0.6248 0.7489 0.0103  -0.0469 -0.0348 362 GLU A OE2 
3069  N N   . ASN A 363 ? 0.3299 0.3805 0.4277 -0.0264 0.0027  -0.0273 363 ASN A N   
3070  C CA  . ASN A 363 ? 0.2726 0.3321 0.3624 -0.0337 0.0055  -0.0171 363 ASN A CA  
3071  C C   . ASN A 363 ? 0.2511 0.3104 0.3417 -0.0296 0.0003  -0.0108 363 ASN A C   
3072  O O   . ASN A 363 ? 0.1898 0.2506 0.2711 -0.0343 0.0002  -0.0027 363 ASN A O   
3073  C CB  . ASN A 363 ? 0.3071 0.3610 0.3809 -0.0428 0.0060  -0.0122 363 ASN A CB  
3074  C CG  . ASN A 363 ? 0.2946 0.3639 0.3651 -0.0484 0.0088  -0.0058 363 ASN A CG  
3075  O OD1 . ASN A 363 ? 0.2551 0.3343 0.3299 -0.0471 0.0123  -0.0059 363 ASN A OD1 
3076  N ND2 . ASN A 363 ? 0.3168 0.3872 0.3788 -0.0547 0.0071  -0.0012 363 ASN A ND2 
3077  N N   . GLY A 364 ? 0.2203 0.2793 0.3227 -0.0209 -0.0042 -0.0159 364 GLY A N   
3078  C CA  . GLY A 364 ? 0.2389 0.2966 0.3406 -0.0173 -0.0096 -0.0107 364 GLY A CA  
3079  C C   . GLY A 364 ? 0.2901 0.3270 0.3731 -0.0177 -0.0169 -0.0040 364 GLY A C   
3080  O O   . GLY A 364 ? 0.2795 0.3140 0.3573 -0.0170 -0.0199 0.0012  364 GLY A O   
3081  N N   . ILE A 365 ? 0.3263 0.3453 0.3960 -0.0200 -0.0191 -0.0043 365 ILE A N   
3082  C CA  . ILE A 365 ? 0.3000 0.2947 0.3452 -0.0248 -0.0235 0.0023  365 ILE A CA  
3083  C C   . ILE A 365 ? 0.3245 0.2977 0.3626 -0.0138 -0.0361 0.0015  365 ILE A C   
3084  O O   . ILE A 365 ? 0.3220 0.2839 0.3446 -0.0165 -0.0390 0.0079  365 ILE A O   
3085  C CB  . ILE A 365 ? 0.3280 0.3067 0.3568 -0.0334 -0.0210 0.0020  365 ILE A CB  
3086  C CG1 . ILE A 365 ? 0.3393 0.3427 0.3754 -0.0440 -0.0107 0.0028  365 ILE A CG1 
3087  C CG2 . ILE A 365 ? 0.3760 0.3249 0.3747 -0.0414 -0.0239 0.0080  365 ILE A CG2 
3088  C CD1 . ILE A 365 ? 0.3410 0.3360 0.3674 -0.0523 -0.0075 -0.0004 365 ILE A CD1 
3089  N N   . PRO A 366 ? 0.2854 0.2534 0.3344 -0.0008 -0.0444 -0.0074 366 PRO A N   
3090  C CA  . PRO A 366 ? 0.3536 0.3047 0.3981 0.0122  -0.0594 -0.0092 366 PRO A CA  
3091  C C   . PRO A 366 ? 0.3788 0.3483 0.4342 0.0130  -0.0597 -0.0071 366 PRO A C   
3092  O O   . PRO A 366 ? 0.4375 0.3878 0.4753 0.0162  -0.0694 -0.0026 366 PRO A O   
3093  C CB  . PRO A 366 ? 0.3092 0.2657 0.3755 0.0271  -0.0662 -0.0230 366 PRO A CB  
3094  C CG  . PRO A 366 ? 0.2997 0.2542 0.3637 0.0203  -0.0569 -0.0253 366 PRO A CG  
3095  C CD  . PRO A 366 ? 0.3070 0.2813 0.3704 0.0034  -0.0418 -0.0173 366 PRO A CD  
3096  N N   . PHE A 367 ? 0.3106 0.3128 0.3900 0.0093  -0.0491 -0.0099 367 PHE A N   
3097  C CA  . PHE A 367 ? 0.2871 0.3040 0.3745 0.0089  -0.0483 -0.0082 367 PHE A CA  
3098  C C   . PHE A 367 ? 0.3271 0.3336 0.3918 -0.0004 -0.0448 0.0035  367 PHE A C   
3099  O O   . PHE A 367 ? 0.3046 0.3010 0.3588 0.0017  -0.0514 0.0064  367 PHE A O   
3100  C CB  . PHE A 367 ? 0.2490 0.2958 0.3598 0.0049  -0.0366 -0.0130 367 PHE A CB  
3101  C CG  . PHE A 367 ? 0.2502 0.3072 0.3636 0.0023  -0.0340 -0.0101 367 PHE A CG  
3102  C CD1 . PHE A 367 ? 0.2268 0.2868 0.3495 0.0094  -0.0431 -0.0159 367 PHE A CD1 
3103  C CD2 . PHE A 367 ? 0.2498 0.3123 0.3555 -0.0063 -0.0240 -0.0021 367 PHE A CD2 
3104  C CE1 . PHE A 367 ? 0.2513 0.3182 0.3742 0.0060  -0.0405 -0.0136 367 PHE A CE1 
3105  C CE2 . PHE A 367 ? 0.1917 0.2598 0.2977 -0.0077 -0.0218 0.0001  367 PHE A CE2 
3106  C CZ  . PHE A 367 ? 0.1795 0.2487 0.2930 -0.0025 -0.0295 -0.0054 367 PHE A CZ  
3107  N N   . LEU A 368 ? 0.2453 0.2559 0.3030 -0.0110 -0.0342 0.0087  368 LEU A N   
3108  C CA  . LEU A 368 ? 0.2840 0.2926 0.3266 -0.0198 -0.0290 0.0164  368 LEU A CA  
3109  C C   . LEU A 368 ? 0.3480 0.3249 0.3606 -0.0238 -0.0348 0.0209  368 LEU A C   
3110  O O   . LEU A 368 ? 0.3755 0.3454 0.3738 -0.0282 -0.0340 0.0252  368 LEU A O   
3111  C CB  . LEU A 368 ? 0.2291 0.2550 0.2757 -0.0288 -0.0177 0.0183  368 LEU A CB  
3112  C CG  . LEU A 368 ? 0.2558 0.3067 0.3214 -0.0266 -0.0115 0.0167  368 LEU A CG  
3113  C CD1 . LEU A 368 ? 0.2285 0.2928 0.2943 -0.0333 -0.0044 0.0183  368 LEU A CD1 
3114  C CD2 . LEU A 368 ? 0.2231 0.2789 0.2903 -0.0241 -0.0110 0.0188  368 LEU A CD2 
3115  N N   . GLU A 369 ? 0.3487 0.3025 0.3475 -0.0234 -0.0400 0.0198  369 GLU A N   
3116  C CA  . GLU A 369 ? 0.4261 0.3410 0.3884 -0.0283 -0.0459 0.0245  369 GLU A CA  
3117  C C   . GLU A 369 ? 0.4320 0.3276 0.3834 -0.0175 -0.0601 0.0250  369 GLU A C   
3118  O O   . GLU A 369 ? 0.4148 0.2840 0.3349 -0.0239 -0.0623 0.0306  369 GLU A O   
3119  C CB  . GLU A 369 ? 0.3870 0.2751 0.3330 -0.0291 -0.0495 0.0229  369 GLU A CB  
3120  C CG  . GLU A 369 ? 0.3435 0.2416 0.2879 -0.0450 -0.0358 0.0233  369 GLU A CG  
3121  C CD  . GLU A 369 ? 0.4332 0.2994 0.3568 -0.0473 -0.0392 0.0216  369 GLU A CD  
3122  O OE1 . GLU A 369 ? 0.4827 0.3241 0.3999 -0.0329 -0.0525 0.0188  369 GLU A OE1 
3123  O OE2 . GLU A 369 ? 0.4774 0.3434 0.3911 -0.0632 -0.0292 0.0219  369 GLU A OE2 
3124  N N   . LYS A 370 ? 0.3596 0.2684 0.3356 -0.0019 -0.0698 0.0180  370 LYS A N   
3125  C CA  . LYS A 370 ? 0.3775 0.2725 0.3461 0.0089  -0.0851 0.0169  370 LYS A CA  
3126  C C   . LYS A 370 ? 0.3864 0.3024 0.3634 0.0042  -0.0789 0.0192  370 LYS A C   
3127  O O   . LYS A 370 ? 0.3833 0.2795 0.3382 0.0045  -0.0868 0.0226  370 LYS A O   
3128  C CB  . LYS A 370 ? 0.4238 0.3293 0.4189 0.0272  -0.0982 0.0056  370 LYS A CB  
3129  C CG  . LYS A 370 ? 0.5976 0.4972 0.5921 0.0398  -0.1158 0.0018  370 LYS A CG  
3130  C CD  . LYS A 370 ? 0.7346 0.6189 0.7326 0.0596  -0.1362 -0.0077 370 LYS A CD  
3131  C CE  . LYS A 370 ? 0.8237 0.6930 0.8105 0.0722  -0.1576 -0.0100 370 LYS A CE  
3132  N NZ  . LYS A 370 ? 0.8902 0.7190 0.8269 0.0611  -0.1588 0.0041  370 LYS A NZ  
3133  N N   . LEU A 371 ? 0.3117 0.2630 0.3158 -0.0006 -0.0651 0.0175  371 LEU A N   
3134  C CA  . LEU A 371 ? 0.2709 0.2377 0.2796 -0.0051 -0.0585 0.0197  371 LEU A CA  
3135  C C   . LEU A 371 ? 0.3247 0.2733 0.3030 -0.0168 -0.0526 0.0275  371 LEU A C   
3136  O O   . LEU A 371 ? 0.3432 0.2780 0.3044 -0.0174 -0.0572 0.0296  371 LEU A O   
3137  C CB  . LEU A 371 ? 0.2155 0.2155 0.2514 -0.0080 -0.0453 0.0174  371 LEU A CB  
3138  C CG  . LEU A 371 ? 0.2529 0.2649 0.2904 -0.0122 -0.0376 0.0199  371 LEU A CG  
3139  C CD1 . LEU A 371 ? 0.3081 0.3170 0.3473 -0.0061 -0.0473 0.0162  371 LEU A CD1 
3140  C CD2 . LEU A 371 ? 0.2905 0.3271 0.3473 -0.0140 -0.0262 0.0185  371 LEU A CD2 
3141  N N   . TYR A 372 ? 0.3696 0.3176 0.3401 -0.0272 -0.0422 0.0304  372 TYR A N   
3142  C CA  . TYR A 372 ? 0.3173 0.2557 0.2642 -0.0411 -0.0326 0.0347  372 TYR A CA  
3143  C C   . TYR A 372 ? 0.4562 0.3512 0.3620 -0.0452 -0.0411 0.0386  372 TYR A C   
3144  O O   . TYR A 372 ? 0.4746 0.3583 0.3584 -0.0542 -0.0363 0.0411  372 TYR A O   
3145  C CB  . TYR A 372 ? 0.2794 0.2303 0.2308 -0.0515 -0.0208 0.0343  372 TYR A CB  
3146  C CG  . TYR A 372 ? 0.2913 0.2812 0.2756 -0.0487 -0.0125 0.0314  372 TYR A CG  
3147  C CD1 . TYR A 372 ? 0.2506 0.2583 0.2523 -0.0408 -0.0123 0.0304  372 TYR A CD1 
3148  C CD2 . TYR A 372 ? 0.3140 0.3195 0.3079 -0.0544 -0.0055 0.0296  372 TYR A CD2 
3149  C CE1 . TYR A 372 ? 0.2761 0.3112 0.3000 -0.0380 -0.0058 0.0286  372 TYR A CE1 
3150  C CE2 . TYR A 372 ? 0.2920 0.3283 0.3105 -0.0507 -0.0003 0.0274  372 TYR A CE2 
3151  C CZ  . TYR A 372 ? 0.2710 0.3195 0.3025 -0.0422 -0.0006 0.0274  372 TYR A CZ  
3152  O OH  . TYR A 372 ? 0.2025 0.2738 0.2513 -0.0381 0.0034  0.0260  372 TYR A OH  
3153  N N   . SER A 373 ? 0.4586 0.3260 0.3505 -0.0387 -0.0537 0.0387  373 SER A N   
3154  C CA  . SER A 373 ? 0.4607 0.2785 0.3073 -0.0402 -0.0652 0.0429  373 SER A CA  
3155  C C   . SER A 373 ? 0.4652 0.2747 0.3051 -0.0305 -0.0782 0.0430  373 SER A C   
3156  O O   . SER A 373 ? 0.4957 0.2703 0.2948 -0.0375 -0.0817 0.0477  373 SER A O   
3157  C CB  . SER A 373 ? 0.4879 0.2775 0.3235 -0.0309 -0.0785 0.0418  373 SER A CB  
3158  O OG  . SER A 373 ? 0.6058 0.3453 0.3990 -0.0255 -0.0958 0.0453  373 SER A OG  
3159  N N   . THR A 374 ? 0.3873 0.2261 0.2641 -0.0155 -0.0859 0.0371  374 THR A N   
3160  C CA  . THR A 374 ? 0.5011 0.3373 0.3759 -0.0070 -0.0984 0.0353  374 THR A CA  
3161  C C   . THR A 374 ? 0.5145 0.3652 0.3878 -0.0183 -0.0846 0.0376  374 THR A C   
3162  O O   . THR A 374 ? 0.5422 0.3720 0.3893 -0.0200 -0.0911 0.0397  374 THR A O   
3163  C CB  . THR A 374 ? 0.4885 0.3562 0.4063 0.0092  -0.1078 0.0258  374 THR A CB  
3164  O OG1 . THR A 374 ? 0.4573 0.3136 0.3787 0.0204  -0.1191 0.0218  374 THR A OG1 
3165  C CG2 . THR A 374 ? 0.4801 0.3471 0.3976 0.0179  -0.1227 0.0218  374 THR A CG2 
3166  N N   . LEU A 375 ? 0.4036 0.2884 0.3033 -0.0252 -0.0665 0.0367  375 LEU A N   
3167  C CA  . LEU A 375 ? 0.4155 0.3141 0.3149 -0.0339 -0.0532 0.0375  375 LEU A CA  
3168  C C   . LEU A 375 ? 0.4943 0.3633 0.3520 -0.0486 -0.0467 0.0420  375 LEU A C   
3169  O O   . LEU A 375 ? 0.5173 0.3763 0.3570 -0.0525 -0.0459 0.0425  375 LEU A O   
3170  C CB  . LEU A 375 ? 0.3937 0.3294 0.3250 -0.0367 -0.0371 0.0354  375 LEU A CB  
3171  C CG  . LEU A 375 ? 0.3883 0.3521 0.3562 -0.0260 -0.0393 0.0308  375 LEU A CG  
3172  C CD1 . LEU A 375 ? 0.3681 0.3603 0.3574 -0.0291 -0.0246 0.0301  375 LEU A CD1 
3173  C CD2 . LEU A 375 ? 0.3253 0.2913 0.2973 -0.0206 -0.0458 0.0278  375 LEU A CD2 
3174  N N   . GLU A 376 ? 0.5817 0.4351 0.4216 -0.0585 -0.0410 0.0444  376 GLU A N   
3175  C CA  . GLU A 376 ? 0.6170 0.4424 0.4156 -0.0766 -0.0314 0.0471  376 GLU A CA  
3176  C C   . GLU A 376 ? 0.6983 0.4738 0.4493 -0.0764 -0.0464 0.0515  376 GLU A C   
3177  O O   . GLU A 376 ? 0.7875 0.5356 0.4982 -0.0930 -0.0378 0.0536  376 GLU A O   
3178  C CB  . GLU A 376 ? 0.5461 0.3645 0.3353 -0.0892 -0.0221 0.0475  376 GLU A CB  
3179  C CG  . GLU A 376 ? 0.6411 0.4173 0.4027 -0.0847 -0.0376 0.0514  376 GLU A CG  
3180  C CD  . GLU A 376 ? 0.7415 0.5118 0.4955 -0.0981 -0.0274 0.0509  376 GLU A CD  
3181  O OE1 . GLU A 376 ? 0.8184 0.5525 0.5493 -0.0946 -0.0388 0.0535  376 GLU A OE1 
3182  O OE2 . GLU A 376 ? 0.7599 0.5615 0.5310 -0.1116 -0.0087 0.0469  376 GLU A OE2 
3183  N N   . LYS A 377 ? 0.7263 0.4898 0.4804 -0.0584 -0.0685 0.0518  377 LYS A N   
3184  C CA  . LYS A 377 ? 0.7664 0.4823 0.4760 -0.0542 -0.0876 0.0553  377 LYS A CA  
3185  C C   . LYS A 377 ? 0.7791 0.5027 0.4899 -0.0504 -0.0925 0.0534  377 LYS A C   
3186  O O   . LYS A 377 ? 0.8921 0.5743 0.5584 -0.0512 -0.1055 0.0567  377 LYS A O   
3187  C CB  . LYS A 377 ? 0.7667 0.4668 0.4805 -0.0338 -0.1124 0.0541  377 LYS A CB  
3188  C CG  . LYS A 377 ? 0.8173 0.4952 0.5183 -0.0354 -0.1127 0.0563  377 LYS A CG  
3189  C CD  . LYS A 377 ? 0.8624 0.5164 0.5599 -0.0127 -0.1403 0.0539  377 LYS A CD  
3190  C CE  . LYS A 377 ? 0.8519 0.4964 0.5524 -0.0106 -0.1394 0.0534  377 LYS A CE  
3191  N NZ  . LYS A 377 ? 0.8668 0.5628 0.6292 0.0046  -0.1400 0.0443  377 LYS A NZ  
3192  N N   . GLU A 378 ? 0.7081 0.4793 0.4644 -0.0464 -0.0835 0.0483  378 GLU A N   
3193  C CA  . GLU A 378 ? 0.6615 0.4412 0.4229 -0.0412 -0.0900 0.0451  378 GLU A CA  
3194  C C   . GLU A 378 ? 0.6115 0.3846 0.3485 -0.0576 -0.0729 0.0463  378 GLU A C   
3195  O O   . GLU A 378 ? 0.5391 0.3409 0.2969 -0.0658 -0.0518 0.0442  378 GLU A O   
3196  C CB  . GLU A 378 ? 0.5680 0.3959 0.3848 -0.0303 -0.0883 0.0384  378 GLU A CB  
3197  C CG  . GLU A 378 ? 0.5694 0.4096 0.4149 -0.0155 -0.1018 0.0345  378 GLU A CG  
3198  C CD  . GLU A 378 ? 0.6648 0.4897 0.5043 -0.0008 -0.1283 0.0302  378 GLU A CD  
3199  O OE1 . GLU A 378 ? 0.7254 0.5172 0.5261 -0.0022 -0.1399 0.0330  378 GLU A OE1 
3200  O OE2 . GLU A 378 ? 0.6562 0.5029 0.5299 0.0123  -0.1381 0.0229  378 GLU A OE2 
3201  N N   . GLU A 379 ? 0.6170 0.3522 0.3093 -0.0615 -0.0828 0.0487  379 GLU A N   
3202  C CA  . GLU A 379 ? 0.5525 0.2778 0.2170 -0.0781 -0.0663 0.0486  379 GLU A CA  
3203  C C   . GLU A 379 ? 0.5626 0.3281 0.2636 -0.0754 -0.0555 0.0423  379 GLU A C   
3204  O O   . GLU A 379 ? 0.5714 0.3470 0.2698 -0.0874 -0.0347 0.0396  379 GLU A O   
3205  C CB  . GLU A 379 ? 0.6680 0.3397 0.2724 -0.0822 -0.0816 0.0525  379 GLU A CB  
3206  N N   . TRP A 380 ? 0.5272 0.3155 0.2622 -0.0601 -0.0686 0.0387  380 TRP A N   
3207  C CA  . TRP A 380 ? 0.5385 0.3579 0.3032 -0.0576 -0.0603 0.0329  380 TRP A CA  
3208  C C   . TRP A 380 ? 0.4982 0.3584 0.3087 -0.0545 -0.0448 0.0304  380 TRP A C   
3209  O O   . TRP A 380 ? 0.4641 0.3462 0.2968 -0.0520 -0.0375 0.0259  380 TRP A O   
3210  C CB  . TRP A 380 ? 0.5519 0.3747 0.3282 -0.0458 -0.0811 0.0287  380 TRP A CB  
3211  C CG  . TRP A 380 ? 0.5421 0.3747 0.3433 -0.0323 -0.0979 0.0273  380 TRP A CG  
3212  C CD1 . TRP A 380 ? 0.5996 0.4043 0.3788 -0.0254 -0.1179 0.0299  380 TRP A CD1 
3213  C CD2 . TRP A 380 ? 0.4815 0.3526 0.3321 -0.0241 -0.0957 0.0219  380 TRP A CD2 
3214  N NE1 . TRP A 380 ? 0.5589 0.3863 0.3752 -0.0122 -0.1280 0.0252  380 TRP A NE1 
3215  C CE2 . TRP A 380 ? 0.5349 0.4035 0.3948 -0.0126 -0.1136 0.0201  380 TRP A CE2 
3216  C CE3 . TRP A 380 ? 0.4054 0.3088 0.2895 -0.0254 -0.0803 0.0180  380 TRP A CE3 
3217  C CZ2 . TRP A 380 ? 0.4888 0.3903 0.3929 -0.0042 -0.1145 0.0136  380 TRP A CZ2 
3218  C CZ3 . TRP A 380 ? 0.4172 0.3488 0.3405 -0.0181 -0.0817 0.0130  380 TRP A CZ3 
3219  C CH2 . TRP A 380 ? 0.4074 0.3396 0.3414 -0.0084 -0.0977 0.0103  380 TRP A CH2 
3220  N N   . ILE A 381 ? 0.4859 0.3535 0.3075 -0.0547 -0.0403 0.0329  381 ILE A N   
3221  C CA  . ILE A 381 ? 0.4052 0.3074 0.2632 -0.0529 -0.0259 0.0309  381 ILE A CA  
3222  C C   . ILE A 381 ? 0.4389 0.3419 0.2850 -0.0653 -0.0081 0.0312  381 ILE A C   
3223  O O   . ILE A 381 ? 0.4594 0.3405 0.2800 -0.0740 -0.0086 0.0344  381 ILE A O   
3224  C CB  . ILE A 381 ? 0.3670 0.2826 0.2514 -0.0439 -0.0340 0.0315  381 ILE A CB  
3225  C CG1 . ILE A 381 ? 0.3690 0.2881 0.2683 -0.0328 -0.0508 0.0281  381 ILE A CG1 
3226  C CG2 . ILE A 381 ? 0.3332 0.2815 0.2504 -0.0424 -0.0199 0.0297  381 ILE A CG2 
3227  C CD1 . ILE A 381 ? 0.3300 0.2657 0.2581 -0.0244 -0.0562 0.0263  381 ILE A CD1 
3228  N N   . GLU A 382 ? 0.3951 0.3227 0.2594 -0.0663 0.0074  0.0265  382 GLU A N   
3229  C CA  . GLU A 382 ? 0.3928 0.3355 0.2607 -0.0754 0.0246  0.0232  382 GLU A CA  
3230  C C   . GLU A 382 ? 0.3232 0.3010 0.2316 -0.0654 0.0286  0.0208  382 GLU A C   
3231  O O   . GLU A 382 ? 0.3293 0.3227 0.2561 -0.0565 0.0313  0.0177  382 GLU A O   
3232  C CB  . GLU A 382 ? 0.4419 0.3841 0.2953 -0.0840 0.0391  0.0171  382 GLU A CB  
3233  C CG  . GLU A 382 ? 0.4633 0.4269 0.3246 -0.0940 0.0575  0.0101  382 GLU A CG  
3234  C CD  . GLU A 382 ? 0.6196 0.5871 0.4708 -0.1016 0.0735  0.0012  382 GLU A CD  
3235  O OE1 . GLU A 382 ? 0.6790 0.6726 0.5448 -0.1079 0.0895  -0.0081 382 GLU A OE1 
3236  O OE2 . GLU A 382 ? 0.5517 0.4985 0.3821 -0.1013 0.0701  0.0019  382 GLU A OE2 
3237  N N   . THR A 383 ? 0.2734 0.2599 0.1916 -0.0672 0.0288  0.0222  383 THR A N   
3238  C CA  . THR A 383 ? 0.2575 0.2759 0.2096 -0.0589 0.0327  0.0196  383 THR A CA  
3239  C C   . THR A 383 ? 0.2911 0.3328 0.2528 -0.0627 0.0479  0.0115  383 THR A C   
3240  O O   . THR A 383 ? 0.3315 0.3688 0.2761 -0.0766 0.0579  0.0075  383 THR A O   
3241  C CB  . THR A 383 ? 0.3162 0.3371 0.2755 -0.0600 0.0278  0.0227  383 THR A CB  
3242  O OG1 . THR A 383 ? 0.3307 0.3401 0.2692 -0.0750 0.0339  0.0221  383 THR A OG1 
3243  C CG2 . THR A 383 ? 0.3362 0.3396 0.2929 -0.0529 0.0126  0.0278  383 THR A CG2 
3244  N N   . LEU A 384 ? 0.2476 0.3124 0.2346 -0.0503 0.0496  0.0079  384 LEU A N   
3245  C CA  . LEU A 384 ? 0.2300 0.3200 0.2309 -0.0487 0.0615  -0.0019 384 LEU A CA  
3246  C C   . LEU A 384 ? 0.2212 0.3410 0.2498 -0.0416 0.0611  -0.0054 384 LEU A C   
3247  O O   . LEU A 384 ? 0.1901 0.3098 0.2285 -0.0324 0.0517  0.0001  384 LEU A O   
3248  C CB  . LEU A 384 ? 0.2795 0.3676 0.2831 -0.0372 0.0623  -0.0047 384 LEU A CB  
3249  C CG  . LEU A 384 ? 0.2846 0.3456 0.2619 -0.0432 0.0624  -0.0029 384 LEU A CG  
3250  C CD1 . LEU A 384 ? 0.2955 0.3564 0.2771 -0.0318 0.0647  -0.0072 384 LEU A CD1 
3251  C CD2 . LEU A 384 ? 0.3517 0.4073 0.3082 -0.0605 0.0736  -0.0077 384 LEU A CD2 
3252  N N   . THR A 385 ? 0.2940 0.4406 0.3353 -0.0461 0.0716  -0.0162 385 THR A N   
3253  C CA  . THR A 385 ? 0.2605 0.4391 0.3309 -0.0343 0.0694  -0.0223 385 THR A CA  
3254  C C   . THR A 385 ? 0.2967 0.4774 0.3767 -0.0142 0.0653  -0.0242 385 THR A C   
3255  O O   . THR A 385 ? 0.2350 0.3974 0.3014 -0.0122 0.0676  -0.0234 385 THR A O   
3256  C CB  . THR A 385 ? 0.2129 0.4252 0.2985 -0.0440 0.0815  -0.0366 385 THR A CB  
3257  O OG1 . THR A 385 ? 0.1969 0.4171 0.2833 -0.0433 0.0923  -0.0470 385 THR A OG1 
3258  C CG2 . THR A 385 ? 0.2219 0.4245 0.2898 -0.0678 0.0882  -0.0351 385 THR A CG2 
3259  N N   . LEU A 386 ? 0.2466 0.4463 0.3467 0.0007  0.0584  -0.0269 386 LEU A N   
3260  C CA  . LEU A 386 ? 0.2240 0.4216 0.3291 0.0208  0.0541  -0.0297 386 LEU A CA  
3261  C C   . LEU A 386 ? 0.2248 0.4385 0.3375 0.0235  0.0646  -0.0434 386 LEU A C   
3262  O O   . LEU A 386 ? 0.2254 0.4233 0.3301 0.0342  0.0648  -0.0444 386 LEU A O   
3263  C CB  . LEU A 386 ? 0.2483 0.4620 0.3699 0.0368  0.0434  -0.0312 386 LEU A CB  
3264  C CG  . LEU A 386 ? 0.2244 0.4214 0.3374 0.0353  0.0337  -0.0189 386 LEU A CG  
3265  C CD1 . LEU A 386 ? 0.1565 0.3659 0.2806 0.0520  0.0225  -0.0211 386 LEU A CD1 
3266  C CD2 . LEU A 386 ? 0.1605 0.3203 0.2514 0.0343  0.0315  -0.0080 386 LEU A CD2 
3267  N N   . GLU A 387 ? 0.1930 0.4394 0.3219 0.0137  0.0743  -0.0558 387 GLU A N   
3268  C CA  . GLU A 387 ? 0.2148 0.4815 0.3536 0.0142  0.0870  -0.0720 387 GLU A CA  
3269  C C   . GLU A 387 ? 0.2239 0.4595 0.3347 0.0035  0.0956  -0.0680 387 GLU A C   
3270  O O   . GLU A 387 ? 0.2249 0.4565 0.3344 0.0135  0.0997  -0.0748 387 GLU A O   
3271  C CB  . GLU A 387 ? 0.3071 0.6136 0.4656 -0.0011 0.0987  -0.0867 387 GLU A CB  
3272  C CG  . GLU A 387 ? 0.4611 0.7845 0.6272 -0.0045 0.1125  -0.1037 387 GLU A CG  
3273  C CD  . GLU A 387 ? 0.6558 1.0017 0.8489 0.0215  0.1049  -0.1158 387 GLU A CD  
3274  O OE1 . GLU A 387 ? 0.7118 1.0649 0.9187 0.0398  0.0892  -0.1125 387 GLU A OE1 
3275  O OE2 . GLU A 387 ? 0.7292 1.0830 0.9272 0.0237  0.1137  -0.1284 387 GLU A OE2 
3276  N N   . GLU A 388 ? 0.2138 0.4244 0.2998 -0.0157 0.0968  -0.0569 388 GLU A N   
3277  C CA  . GLU A 388 ? 0.2537 0.4324 0.3094 -0.0263 0.1022  -0.0525 388 GLU A CA  
3278  C C   . GLU A 388 ? 0.2700 0.4216 0.3154 -0.0116 0.0926  -0.0443 388 GLU A C   
3279  O O   . GLU A 388 ? 0.3629 0.5019 0.3963 -0.0103 0.0984  -0.0487 388 GLU A O   
3280  C CB  . GLU A 388 ? 0.3647 0.5201 0.3949 -0.0469 0.1015  -0.0423 388 GLU A CB  
3281  C CG  . GLU A 388 ? 0.4568 0.6312 0.4879 -0.0667 0.1147  -0.0514 388 GLU A CG  
3282  C CD  . GLU A 388 ? 0.5513 0.6969 0.5534 -0.0855 0.1121  -0.0406 388 GLU A CD  
3283  O OE1 . GLU A 388 ? 0.4775 0.6054 0.4756 -0.0793 0.0975  -0.0278 388 GLU A OE1 
3284  O OE2 . GLU A 388 ? 0.6092 0.7483 0.5907 -0.1069 0.1251  -0.0459 388 GLU A OE2 
3285  N N   . ALA A 389 ? 0.2299 0.3718 0.2788 -0.0017 0.0790  -0.0337 389 ALA A N   
3286  C CA  . ALA A 389 ? 0.2301 0.3457 0.2680 0.0091  0.0714  -0.0271 389 ALA A CA  
3287  C C   . ALA A 389 ? 0.2880 0.4085 0.3336 0.0262  0.0743  -0.0367 389 ALA A C   
3288  O O   . ALA A 389 ? 0.3255 0.4215 0.3554 0.0304  0.0741  -0.0354 389 ALA A O   
3289  C CB  . ALA A 389 ? 0.2524 0.3604 0.2940 0.0152  0.0590  -0.0167 389 ALA A CB  
3290  N N   . MET A 390 ? 0.2564 0.4084 0.3262 0.0369  0.0763  -0.0475 390 MET A N   
3291  C CA  . MET A 390 ? 0.3415 0.4983 0.4204 0.0573  0.0764  -0.0579 390 MET A CA  
3292  C C   . MET A 390 ? 0.3706 0.5319 0.4458 0.0523  0.0909  -0.0705 390 MET A C   
3293  O O   . MET A 390 ? 0.3273 0.4712 0.3938 0.0642  0.0918  -0.0746 390 MET A O   
3294  C CB  . MET A 390 ? 0.3283 0.5199 0.4367 0.0730  0.0707  -0.0670 390 MET A CB  
3295  C CG  . MET A 390 ? 0.4727 0.6704 0.5919 0.0981  0.0683  -0.0797 390 MET A CG  
3296  S SD  . MET A 390 ? 0.5763 0.8315 0.7384 0.1122  0.0662  -0.0990 390 MET A SD  
3297  C CE  . MET A 390 ? 0.6477 0.8887 0.8072 0.1327  0.0437  -0.0881 390 MET A CE  
3298  N N   . ARG A 391 ? 0.3220 0.5023 0.3997 0.0330  0.1033  -0.0769 391 ARG A N   
3299  C CA  . ARG A 391 ? 0.3213 0.5092 0.3954 0.0256  0.1198  -0.0912 391 ARG A CA  
3300  C C   . ARG A 391 ? 0.3556 0.5082 0.3932 0.0065  0.1254  -0.0834 391 ARG A C   
3301  O O   . ARG A 391 ? 0.4072 0.5578 0.4351 0.0010  0.1385  -0.0942 391 ARG A O   
3302  C CB  . ARG A 391 ? 0.2939 0.5247 0.3903 0.0136  0.1329  -0.1065 391 ARG A CB  
3303  C CG  . ARG A 391 ? 0.3480 0.6205 0.4838 0.0315  0.1262  -0.1168 391 ARG A CG  
3304  C CD  . ARG A 391 ? 0.5089 0.8167 0.6688 0.0319  0.1367  -0.1373 391 ARG A CD  
3305  N NE  . ARG A 391 ? 0.5821 0.9210 0.7740 0.0457  0.1247  -0.1431 391 ARG A NE  
3306  C CZ  . ARG A 391 ? 0.6820 1.0271 0.8911 0.0746  0.1113  -0.1475 391 ARG A CZ  
3307  N NH1 . ARG A 391 ? 0.7247 1.0452 0.9220 0.0932  0.1088  -0.1468 391 ARG A NH1 
3308  N NH2 . ARG A 391 ? 0.7190 1.0904 0.9531 0.0845  0.0995  -0.1528 391 ARG A NH2 
3309  N N   . LYS A 392 ? 0.2916 0.4178 0.3094 -0.0033 0.1155  -0.0664 392 LYS A N   
3310  C CA  . LYS A 392 ? 0.4148 0.5079 0.3979 -0.0202 0.1169  -0.0590 392 LYS A CA  
3311  C C   . LYS A 392 ? 0.4780 0.5494 0.4451 -0.0143 0.1199  -0.0630 392 LYS A C   
3312  O O   . LYS A 392 ? 0.4439 0.5052 0.4158 0.0022  0.1122  -0.0607 392 LYS A O   
3313  C CB  . LYS A 392 ? 0.5198 0.5912 0.4919 -0.0235 0.1015  -0.0421 392 LYS A CB  
3314  C CG  . LYS A 392 ? 0.6007 0.6425 0.5395 -0.0408 0.0993  -0.0347 392 LYS A CG  
3315  C CD  . LYS A 392 ? 0.6460 0.6925 0.5724 -0.0598 0.1098  -0.0384 392 LYS A CD  
3316  C CE  . LYS A 392 ? 0.6503 0.6870 0.5691 -0.0680 0.0996  -0.0271 392 LYS A CE  
3317  N NZ  . LYS A 392 ? 0.6777 0.7091 0.5748 -0.0890 0.1105  -0.0303 392 LYS A NZ  
3318  N N   . GLU A 393 ? 0.4674 0.5277 0.4112 -0.0294 0.1316  -0.0688 393 GLU A N   
3319  C CA  . GLU A 393 ? 0.5293 0.5720 0.4581 -0.0252 0.1375  -0.0758 393 GLU A CA  
3320  C C   . GLU A 393 ? 0.5554 0.5586 0.4519 -0.0324 0.1276  -0.0643 393 GLU A C   
3321  O O   . GLU A 393 ? 0.5538 0.5396 0.4413 -0.0247 0.1272  -0.0671 393 GLU A O   
3322  C CB  . GLU A 393 ? 0.6348 0.6887 0.5558 -0.0378 0.1579  -0.0917 393 GLU A CB  
3323  C CG  . GLU A 393 ? 0.7250 0.8113 0.6771 -0.0212 0.1689  -0.1107 393 GLU A CG  
3324  C CD  . GLU A 393 ? 0.8320 0.9341 0.7792 -0.0359 0.1918  -0.1293 393 GLU A CD  
3325  O OE1 . GLU A 393 ? 0.8503 0.9920 0.8311 -0.0264 0.2017  -0.1471 393 GLU A OE1 
3326  O OE2 . GLU A 393 ? 0.8671 0.9419 0.7764 -0.0569 0.1991  -0.1268 393 GLU A OE2 
3327  N N   . ASP A 394 ? 0.4686 0.4572 0.3472 -0.0464 0.1190  -0.0529 394 ASP A N   
3328  C CA  . ASP A 394 ? 0.5472 0.5026 0.3975 -0.0528 0.1076  -0.0442 394 ASP A CA  
3329  C C   . ASP A 394 ? 0.5171 0.4691 0.3818 -0.0422 0.0912  -0.0343 394 ASP A C   
3330  O O   . ASP A 394 ? 0.5045 0.4441 0.3600 -0.0479 0.0781  -0.0251 394 ASP A O   
3331  C CB  . ASP A 394 ? 0.6361 0.5740 0.4561 -0.0718 0.1051  -0.0386 394 ASP A CB  
3332  C CG  . ASP A 394 ? 0.7546 0.7080 0.5866 -0.0763 0.1036  -0.0337 394 ASP A CG  
3333  O OD1 . ASP A 394 ? 0.7769 0.7578 0.6427 -0.0650 0.1044  -0.0351 394 ASP A OD1 
3334  O OD2 . ASP A 394 ? 0.8031 0.7379 0.6079 -0.0909 0.1006  -0.0284 394 ASP A OD2 
3335  N N   . VAL A 395 ? 0.5135 0.4762 0.4002 -0.0263 0.0921  -0.0372 395 VAL A N   
3336  C CA  . VAL A 395 ? 0.5130 0.4731 0.4129 -0.0170 0.0803  -0.0295 395 VAL A CA  
3337  C C   . VAL A 395 ? 0.5368 0.4798 0.4308 -0.0075 0.0820  -0.0339 395 VAL A C   
3338  O O   . VAL A 395 ? 0.5675 0.5097 0.4579 -0.0021 0.0924  -0.0437 395 VAL A O   
3339  C CB  . VAL A 395 ? 0.5375 0.5233 0.4651 -0.0076 0.0789  -0.0277 395 VAL A CB  
3340  C CG1 . VAL A 395 ? 0.6327 0.6137 0.5711 0.0057  0.0718  -0.0239 395 VAL A CG1 
3341  C CG2 . VAL A 395 ? 0.4611 0.4553 0.3911 -0.0181 0.0731  -0.0203 395 VAL A CG2 
3342  N N   . LYS A 396 ? 0.4215 0.3494 0.3129 -0.0068 0.0727  -0.0280 396 LYS A N   
3343  C CA  . LYS A 396 ? 0.4402 0.3459 0.3208 -0.0002 0.0748  -0.0319 396 LYS A CA  
3344  C C   . LYS A 396 ? 0.4599 0.3670 0.3536 0.0161  0.0740  -0.0311 396 LYS A C   
3345  O O   . LYS A 396 ? 0.4061 0.3292 0.3167 0.0198  0.0687  -0.0254 396 LYS A O   
3346  C CB  . LYS A 396 ? 0.5565 0.4421 0.4224 -0.0117 0.0673  -0.0287 396 LYS A CB  
3347  C CG  . LYS A 396 ? 0.6011 0.4802 0.4484 -0.0257 0.0660  -0.0308 396 LYS A CG  
3348  C CD  . LYS A 396 ? 0.6199 0.4867 0.4489 -0.0253 0.0775  -0.0399 396 LYS A CD  
3349  C CE  . LYS A 396 ? 0.6690 0.5258 0.4739 -0.0402 0.0759  -0.0415 396 LYS A CE  
3350  N NZ  . LYS A 396 ? 0.7127 0.5711 0.5060 -0.0420 0.0898  -0.0493 396 LYS A NZ  
3351  N N   . THR A 397 ? 0.4272 0.5255 0.3323 -0.0607 -0.0834 0.0265  397 THR A N   
3352  C CA  . THR A 397 ? 0.4390 0.5315 0.3536 -0.0597 -0.0731 0.0196  397 THR A CA  
3353  C C   . THR A 397 ? 0.4094 0.4997 0.3288 -0.0630 -0.0763 0.0091  397 THR A C   
3354  O O   . THR A 397 ? 0.4387 0.5305 0.3474 -0.0678 -0.0843 0.0047  397 THR A O   
3355  C CB  . THR A 397 ? 0.4649 0.5530 0.3621 -0.0594 -0.0630 0.0168  397 THR A CB  
3356  O OG1 . THR A 397 ? 0.5133 0.6014 0.4208 -0.0566 -0.0543 0.0223  397 THR A OG1 
3357  C CG2 . THR A 397 ? 0.4626 0.5448 0.3517 -0.0600 -0.0584 0.0036  397 THR A CG2 
3358  N N   . GLU A 398 ? 0.3856 0.4712 0.3198 -0.0612 -0.0704 0.0053  398 GLU A N   
3359  C CA  . GLU A 398 ? 0.4014 0.4807 0.3381 -0.0649 -0.0722 -0.0041 398 GLU A CA  
3360  C C   . GLU A 398 ? 0.3946 0.4646 0.3385 -0.0607 -0.0628 -0.0085 398 GLU A C   
3361  O O   . GLU A 398 ? 0.4271 0.4998 0.3836 -0.0561 -0.0578 -0.0030 398 GLU A O   
3362  C CB  . GLU A 398 ? 0.4633 0.5506 0.4164 -0.0687 -0.0808 -0.0015 398 GLU A CB  
3363  C CG  . GLU A 398 ? 0.6184 0.6985 0.5738 -0.0750 -0.0824 -0.0107 398 GLU A CG  
3364  C CD  . GLU A 398 ? 0.7920 0.8660 0.7263 -0.0816 -0.0870 -0.0198 398 GLU A CD  
3365  O OE1 . GLU A 398 ? 0.8487 0.9095 0.7659 -0.0795 -0.0807 -0.0266 398 GLU A OE1 
3366  O OE2 . GLU A 398 ? 0.8571 0.9403 0.7920 -0.0888 -0.0971 -0.0205 398 GLU A OE2 
3367  N N   . VAL A 399 ? 0.3847 0.4428 0.3194 -0.0620 -0.0608 -0.0186 399 VAL A N   
3368  C CA  . VAL A 399 ? 0.4006 0.4481 0.3408 -0.0571 -0.0533 -0.0230 399 VAL A CA  
3369  C C   . VAL A 399 ? 0.4272 0.4694 0.3801 -0.0609 -0.0566 -0.0236 399 VAL A C   
3370  O O   . VAL A 399 ? 0.4232 0.4644 0.3736 -0.0688 -0.0633 -0.0264 399 VAL A O   
3371  C CB  . VAL A 399 ? 0.4402 0.4747 0.3611 -0.0545 -0.0484 -0.0335 399 VAL A CB  
3372  C CG1 . VAL A 399 ? 0.4318 0.4544 0.3577 -0.0478 -0.0419 -0.0378 399 VAL A CG1 
3373  C CG2 . VAL A 399 ? 0.4066 0.4491 0.3163 -0.0508 -0.0435 -0.0324 399 VAL A CG2 
3374  N N   . ILE A 400 ? 0.3717 0.4112 0.3377 -0.0561 -0.0517 -0.0210 400 ILE A N   
3375  C CA  . ILE A 400 ? 0.4025 0.4347 0.3784 -0.0591 -0.0526 -0.0216 400 ILE A CA  
3376  C C   . ILE A 400 ? 0.3706 0.3868 0.3423 -0.0526 -0.0459 -0.0262 400 ILE A C   
3377  O O   . ILE A 400 ? 0.3484 0.3673 0.3207 -0.0443 -0.0407 -0.0253 400 ILE A O   
3378  C CB  . ILE A 400 ? 0.3981 0.4433 0.3938 -0.0592 -0.0542 -0.0126 400 ILE A CB  
3379  C CG1 . ILE A 400 ? 0.4792 0.5189 0.4846 -0.0636 -0.0544 -0.0130 400 ILE A CG1 
3380  C CG2 . ILE A 400 ? 0.3432 0.3928 0.3462 -0.0513 -0.0488 -0.0074 400 ILE A CG2 
3381  C CD1 . ILE A 400 ? 0.4506 0.5027 0.4747 -0.0621 -0.0546 -0.0050 400 ILE A CD1 
3382  N N   . GLU A 401 ? 0.3801 0.3793 0.3466 -0.0564 -0.0461 -0.0313 401 GLU A N   
3383  C CA  . GLU A 401 ? 0.3862 0.3667 0.3449 -0.0489 -0.0405 -0.0358 401 GLU A CA  
3384  C C   . GLU A 401 ? 0.3313 0.3059 0.3007 -0.0474 -0.0385 -0.0315 401 GLU A C   
3385  O O   . GLU A 401 ? 0.3582 0.3218 0.3241 -0.0384 -0.0343 -0.0327 401 GLU A O   
3386  C CB  . GLU A 401 ? 0.4474 0.4054 0.3864 -0.0525 -0.0410 -0.0453 401 GLU A CB  
3387  C CG  . GLU A 401 ? 0.5085 0.4696 0.4329 -0.0543 -0.0429 -0.0510 401 GLU A CG  
3388  C CD  . GLU A 401 ? 0.5830 0.5474 0.5010 -0.0421 -0.0367 -0.0533 401 GLU A CD  
3389  O OE1 . GLU A 401 ? 0.6512 0.6228 0.5589 -0.0426 -0.0369 -0.0561 401 GLU A OE1 
3390  O OE2 . GLU A 401 ? 0.6002 0.5610 0.5233 -0.0320 -0.0317 -0.0524 401 GLU A OE2 
3391  N N   . SER A 402 ? 0.3246 0.3074 0.3066 -0.0552 -0.0414 -0.0264 402 SER A N   
3392  C CA  . SER A 402 ? 0.3828 0.3591 0.3727 -0.0553 -0.0389 -0.0227 402 SER A CA  
3393  C C   . SER A 402 ? 0.3671 0.3633 0.3755 -0.0592 -0.0408 -0.0155 402 SER A C   
3394  O O   . SER A 402 ? 0.2917 0.3024 0.3059 -0.0653 -0.0455 -0.0143 402 SER A O   
3395  C CB  . SER A 402 ? 0.3828 0.3374 0.3625 -0.0631 -0.0387 -0.0270 402 SER A CB  
3396  O OG  . SER A 402 ? 0.4159 0.3630 0.4009 -0.0634 -0.0354 -0.0228 402 SER A OG  
3397  N N   . VAL A 403 ? 0.3284 0.3250 0.3453 -0.0546 -0.0374 -0.0108 403 VAL A N   
3398  C CA  . VAL A 403 ? 0.3466 0.3582 0.3797 -0.0572 -0.0378 -0.0047 403 VAL A CA  
3399  C C   . VAL A 403 ? 0.3565 0.3572 0.3910 -0.0595 -0.0338 -0.0034 403 VAL A C   
3400  O O   . VAL A 403 ? 0.3680 0.3504 0.3916 -0.0555 -0.0307 -0.0052 403 VAL A O   
3401  C CB  . VAL A 403 ? 0.3004 0.3248 0.3418 -0.0495 -0.0370 0.0001  403 VAL A CB  
3402  C CG1 . VAL A 403 ? 0.3013 0.3332 0.3378 -0.0471 -0.0394 -0.0009 403 VAL A CG1 
3403  C CG2 . VAL A 403 ? 0.3534 0.3687 0.3927 -0.0421 -0.0327 0.0008  403 VAL A CG2 
3404  N N   . LYS A 404 ? 0.3236 0.3359 0.3710 -0.0656 -0.0338 -0.0001 404 LYS A N   
3405  C CA  . LYS A 404 ? 0.3460 0.3519 0.3965 -0.0683 -0.0289 0.0022  404 LYS A CA  
3406  C C   . LYS A 404 ? 0.2882 0.3004 0.3459 -0.0597 -0.0261 0.0068  404 LYS A C   
3407  O O   . LYS A 404 ? 0.2589 0.2886 0.3294 -0.0579 -0.0274 0.0100  404 LYS A O   
3408  C CB  . LYS A 404 ? 0.3885 0.4069 0.4506 -0.0795 -0.0295 0.0027  404 LYS A CB  
3409  C CG  . LYS A 404 ? 0.4419 0.4542 0.5063 -0.0845 -0.0231 0.0047  404 LYS A CG  
3410  C CD  . LYS A 404 ? 0.4966 0.5138 0.5660 -0.0991 -0.0234 0.0026  404 LYS A CD  
3411  C CE  . LYS A 404 ? 0.5944 0.5906 0.6461 -0.1056 -0.0260 -0.0033 404 LYS A CE  
3412  N NZ  . LYS A 404 ? 0.6582 0.6250 0.6897 -0.0979 -0.0227 -0.0041 404 LYS A NZ  
3413  N N   . ALA A 405 ? 0.2671 0.2641 0.3153 -0.0540 -0.0227 0.0071  405 ALA A N   
3414  C CA  . ALA A 405 ? 0.3033 0.3040 0.3554 -0.0464 -0.0206 0.0104  405 ALA A CA  
3415  C C   . ALA A 405 ? 0.2381 0.2519 0.3038 -0.0489 -0.0180 0.0140  405 ALA A C   
3416  O O   . ALA A 405 ? 0.2525 0.2680 0.3224 -0.0562 -0.0155 0.0144  405 ALA A O   
3417  C CB  . ALA A 405 ? 0.2278 0.2098 0.2668 -0.0418 -0.0177 0.0102  405 ALA A CB  
3418  N N   . GLY A 406 ? 0.2433 0.2661 0.3157 -0.0429 -0.0183 0.0163  406 GLY A N   
3419  C CA  . GLY A 406 ? 0.2430 0.2774 0.3278 -0.0431 -0.0156 0.0192  406 GLY A CA  
3420  C C   . GLY A 406 ? 0.2003 0.2400 0.2892 -0.0362 -0.0165 0.0213  406 GLY A C   
3421  O O   . GLY A 406 ? 0.2504 0.2857 0.3330 -0.0325 -0.0186 0.0205  406 GLY A O   
3422  N N   . THR A 407 ? 0.2405 0.2899 0.3402 -0.0347 -0.0144 0.0237  407 THR A N   
3423  C CA  . THR A 407 ? 0.1737 0.2256 0.2769 -0.0284 -0.0147 0.0258  407 THR A CA  
3424  C C   . THR A 407 ? 0.1826 0.2495 0.2991 -0.0272 -0.0167 0.0285  407 THR A C   
3425  O O   . THR A 407 ? 0.2517 0.3296 0.3762 -0.0315 -0.0174 0.0284  407 THR A O   
3426  C CB  . THR A 407 ? 0.2377 0.2818 0.3378 -0.0248 -0.0092 0.0256  407 THR A CB  
3427  O OG1 . THR A 407 ? 0.2130 0.2650 0.3223 -0.0255 -0.0043 0.0264  407 THR A OG1 
3428  C CG2 . THR A 407 ? 0.2220 0.2523 0.3085 -0.0257 -0.0077 0.0232  407 THR A CG2 
3429  N N   . TRP A 408 ? 0.1690 0.2362 0.2877 -0.0211 -0.0175 0.0311  408 TRP A N   
3430  C CA  . TRP A 408 ? 0.1691 0.2499 0.3002 -0.0173 -0.0196 0.0344  408 TRP A CA  
3431  C C   . TRP A 408 ? 0.2439 0.3317 0.3855 -0.0139 -0.0136 0.0345  408 TRP A C   
3432  O O   . TRP A 408 ? 0.2008 0.3020 0.3546 -0.0088 -0.0149 0.0371  408 TRP A O   
3433  C CB  . TRP A 408 ? 0.1875 0.2631 0.3152 -0.0114 -0.0227 0.0380  408 TRP A CB  
3434  C CG  . TRP A 408 ? 0.2319 0.2917 0.3521 -0.0072 -0.0185 0.0377  408 TRP A CG  
3435  C CD1 . TRP A 408 ? 0.2490 0.3001 0.3651 -0.0071 -0.0127 0.0344  408 TRP A CD1 
3436  C CD2 . TRP A 408 ? 0.2092 0.2588 0.3232 -0.0038 -0.0202 0.0405  408 TRP A CD2 
3437  N NE1 . TRP A 408 ? 0.2069 0.2440 0.3153 -0.0039 -0.0112 0.0343  408 TRP A NE1 
3438  C CE2 . TRP A 408 ? 0.2306 0.2659 0.3377 -0.0024 -0.0155 0.0381  408 TRP A CE2 
3439  C CE3 . TRP A 408 ? 0.2557 0.3054 0.3675 -0.0024 -0.0251 0.0451  408 TRP A CE3 
3440  C CZ2 . TRP A 408 ? 0.2544 0.2753 0.3536 -0.0006 -0.0155 0.0396  408 TRP A CZ2 
3441  C CZ3 . TRP A 408 ? 0.2317 0.2663 0.3349 -0.0003 -0.0246 0.0475  408 TRP A CZ3 
3442  C CH2 . TRP A 408 ? 0.2782 0.2984 0.3757 0.0000  -0.0198 0.0445  408 TRP A CH2 
3443  N N   . PHE A 409 ? 0.2291 0.3089 0.3659 -0.0157 -0.0070 0.0318  409 PHE A N   
3444  C CA  . PHE A 409 ? 0.2679 0.3568 0.4144 -0.0146 0.0000  0.0313  409 PHE A CA  
3445  C C   . PHE A 409 ? 0.2663 0.3650 0.4179 -0.0242 0.0009  0.0301  409 PHE A C   
3446  O O   . PHE A 409 ? 0.2823 0.3693 0.4231 -0.0301 0.0042  0.0282  409 PHE A O   
3447  C CB  . PHE A 409 ? 0.2681 0.3421 0.4043 -0.0117 0.0073  0.0294  409 PHE A CB  
3448  C CG  . PHE A 409 ? 0.4056 0.4889 0.5515 -0.0074 0.0154  0.0291  409 PHE A CG  
3449  C CD1 . PHE A 409 ? 0.4322 0.5295 0.5873 -0.0134 0.0204  0.0286  409 PHE A CD1 
3450  C CD2 . PHE A 409 ? 0.4584 0.5365 0.6040 0.0024  0.0187  0.0290  409 PHE A CD2 
3451  C CE1 . PHE A 409 ? 0.4844 0.5935 0.6500 -0.0094 0.0290  0.0282  409 PHE A CE1 
3452  C CE2 . PHE A 409 ? 0.4411 0.5287 0.5958 0.0078  0.0271  0.0281  409 PHE A CE2 
3453  C CZ  . PHE A 409 ? 0.4463 0.5512 0.6119 0.0021  0.0325  0.0277  409 PHE A CZ  
3454  N N   . ASP A 410 ? 0.2203 0.3400 0.3876 -0.0260 -0.0025 0.0312  410 ASP A N   
3455  C CA  . ASP A 410 ? 0.2937 0.4264 0.4690 -0.0366 -0.0020 0.0298  410 ASP A CA  
3456  C C   . ASP A 410 ? 0.2862 0.4062 0.4483 -0.0458 -0.0064 0.0276  410 ASP A C   
3457  O O   . ASP A 410 ? 0.3166 0.4394 0.4799 -0.0563 -0.0048 0.0258  410 ASP A O   
3458  C CB  . ASP A 410 ? 0.3773 0.5119 0.5557 -0.0402 0.0086  0.0287  410 ASP A CB  
3459  C CG  . ASP A 410 ? 0.4964 0.6487 0.6911 -0.0316 0.0140  0.0299  410 ASP A CG  
3460  O OD1 . ASP A 410 ? 0.4668 0.6339 0.6739 -0.0240 0.0083  0.0318  410 ASP A OD1 
3461  O OD2 . ASP A 410 ? 0.6031 0.7539 0.7972 -0.0316 0.0240  0.0290  410 ASP A OD2 
3462  N N   . GLY A 411 ? 0.2349 0.3407 0.3841 -0.0424 -0.0113 0.0276  411 GLY A N   
3463  C CA  . GLY A 411 ? 0.2636 0.3561 0.3993 -0.0489 -0.0143 0.0250  411 GLY A CA  
3464  C C   . GLY A 411 ? 0.2575 0.3311 0.3798 -0.0521 -0.0084 0.0233  411 GLY A C   
3465  O O   . GLY A 411 ? 0.2823 0.3450 0.3946 -0.0583 -0.0098 0.0209  411 GLY A O   
3466  N N   . ASN A 412 ? 0.2118 0.2795 0.3318 -0.0476 -0.0020 0.0243  412 ASN A N   
3467  C CA  . ASN A 412 ? 0.2536 0.3027 0.3588 -0.0503 0.0031  0.0235  412 ASN A CA  
3468  C C   . ASN A 412 ? 0.2698 0.3091 0.3670 -0.0421 0.0060  0.0241  412 ASN A C   
3469  O O   . ASN A 412 ? 0.2776 0.3227 0.3804 -0.0354 0.0044  0.0247  412 ASN A O   
3470  C CB  . ASN A 412 ? 0.2903 0.3437 0.4000 -0.0592 0.0099  0.0237  412 ASN A CB  
3471  C CG  . ASN A 412 ? 0.3249 0.3939 0.4482 -0.0561 0.0164  0.0252  412 ASN A CG  
3472  O OD1 . ASN A 412 ? 0.3829 0.4467 0.5021 -0.0478 0.0194  0.0257  412 ASN A OD1 
3473  N ND2 . ASN A 412 ? 0.3201 0.4091 0.4597 -0.0628 0.0189  0.0253  412 ASN A ND2 
3474  N N   . PHE A 413 ? 0.3169 0.3397 0.3994 -0.0430 0.0101  0.0238  413 PHE A N   
3475  C CA  . PHE A 413 ? 0.2911 0.3023 0.3620 -0.0362 0.0112  0.0236  413 PHE A CA  
3476  C C   . PHE A 413 ? 0.3081 0.3173 0.3763 -0.0356 0.0197  0.0244  413 PHE A C   
3477  O O   . PHE A 413 ? 0.2617 0.2584 0.3161 -0.0315 0.0210  0.0239  413 PHE A O   
3478  C CB  . PHE A 413 ? 0.2862 0.2796 0.3397 -0.0354 0.0080  0.0229  413 PHE A CB  
3479  C CG  . PHE A 413 ? 0.3147 0.3096 0.3692 -0.0339 0.0006  0.0214  413 PHE A CG  
3480  C CD1 . PHE A 413 ? 0.3732 0.3673 0.4281 -0.0393 -0.0015 0.0206  413 PHE A CD1 
3481  C CD2 . PHE A 413 ? 0.2845 0.2811 0.3382 -0.0280 -0.0038 0.0204  413 PHE A CD2 
3482  C CE1 . PHE A 413 ? 0.3294 0.3246 0.3836 -0.0374 -0.0074 0.0186  413 PHE A CE1 
3483  C CE2 . PHE A 413 ? 0.2808 0.2804 0.3353 -0.0268 -0.0094 0.0190  413 PHE A CE2 
3484  C CZ  . PHE A 413 ? 0.2967 0.2955 0.3511 -0.0309 -0.0109 0.0181  413 PHE A CZ  
3485  N N   . LEU A 414 ? 0.3169 0.3397 0.3979 -0.0396 0.0256  0.0252  414 LEU A N   
3486  C CA  . LEU A 414 ? 0.3828 0.4040 0.4600 -0.0405 0.0355  0.0257  414 LEU A CA  
3487  C C   . LEU A 414 ? 0.4022 0.4209 0.4760 -0.0314 0.0380  0.0244  414 LEU A C   
3488  O O   . LEU A 414 ? 0.4938 0.5032 0.5553 -0.0306 0.0449  0.0242  414 LEU A O   
3489  C CB  . LEU A 414 ? 0.3553 0.3969 0.4509 -0.0465 0.0414  0.0265  414 LEU A CB  
3490  C CG  . LEU A 414 ? 0.3143 0.3579 0.4123 -0.0585 0.0412  0.0271  414 LEU A CG  
3491  C CD1 . LEU A 414 ? 0.2887 0.3536 0.4038 -0.0652 0.0497  0.0276  414 LEU A CD1 
3492  C CD2 . LEU A 414 ? 0.3468 0.3637 0.4208 -0.0630 0.0423  0.0281  414 LEU A CD2 
3493  N N   . LYS A 415 ? 0.3398 0.3644 0.4219 -0.0251 0.0325  0.0236  415 LYS A N   
3494  C CA  . LYS A 415 ? 0.3782 0.3982 0.4566 -0.0172 0.0350  0.0218  415 LYS A CA  
3495  C C   . LYS A 415 ? 0.2766 0.2777 0.3349 -0.0153 0.0317  0.0200  415 LYS A C   
3496  O O   . LYS A 415 ? 0.2695 0.2640 0.3217 -0.0102 0.0335  0.0176  415 LYS A O   
3497  C CB  . LYS A 415 ? 0.4372 0.4672 0.5298 -0.0115 0.0306  0.0220  415 LYS A CB  
3498  C CG  . LYS A 415 ? 0.5121 0.5637 0.6255 -0.0110 0.0336  0.0237  415 LYS A CG  
3499  C CD  . LYS A 415 ? 0.5738 0.6311 0.6909 -0.0073 0.0446  0.0225  415 LYS A CD  
3500  C CE  . LYS A 415 ? 0.6334 0.6839 0.7483 0.0035  0.0464  0.0206  415 LYS A CE  
3501  N NZ  . LYS A 415 ? 0.6724 0.7294 0.7914 0.0087  0.0579  0.0188  415 LYS A NZ  
3502  N N   . TRP A 416 ? 0.2810 0.2733 0.3287 -0.0190 0.0271  0.0207  416 TRP A N   
3503  C CA  . TRP A 416 ? 0.2892 0.2671 0.3195 -0.0167 0.0226  0.0191  416 TRP A CA  
3504  C C   . TRP A 416 ? 0.3714 0.3367 0.3851 -0.0193 0.0235  0.0206  416 TRP A C   
3505  O O   . TRP A 416 ? 0.3423 0.2967 0.3405 -0.0164 0.0197  0.0196  416 TRP A O   
3506  C CB  . TRP A 416 ? 0.2939 0.2745 0.3283 -0.0156 0.0132  0.0184  416 TRP A CB  
3507  C CG  . TRP A 416 ? 0.3073 0.2967 0.3548 -0.0134 0.0116  0.0179  416 TRP A CG  
3508  C CD1 . TRP A 416 ? 0.2601 0.2450 0.3048 -0.0103 0.0108  0.0157  416 TRP A CD1 
3509  C CD2 . TRP A 416 ? 0.2680 0.2702 0.3315 -0.0144 0.0103  0.0199  416 TRP A CD2 
3510  N NE1 . TRP A 416 ? 0.2143 0.2065 0.2716 -0.0088 0.0095  0.0169  416 TRP A NE1 
3511  C CE2 . TRP A 416 ? 0.2487 0.2525 0.3177 -0.0107 0.0089  0.0197  416 TRP A CE2 
3512  C CE3 . TRP A 416 ? 0.2175 0.2290 0.2899 -0.0184 0.0098  0.0218  416 TRP A CE3 
3513  C CZ2 . TRP A 416 ? 0.2248 0.2394 0.3073 -0.0097 0.0067  0.0221  416 TRP A CZ2 
3514  C CZ3 . TRP A 416 ? 0.2494 0.2738 0.3362 -0.0181 0.0073  0.0234  416 TRP A CZ3 
3515  C CH2 . TRP A 416 ? 0.2490 0.2750 0.3405 -0.0131 0.0055  0.0239  416 TRP A CH2 
3516  N N   . ILE A 417 ? 0.2573 0.2233 0.2730 -0.0248 0.0279  0.0231  417 ILE A N   
3517  C CA  . ILE A 417 ? 0.3580 0.3081 0.3554 -0.0276 0.0300  0.0254  417 ILE A CA  
3518  C C   . ILE A 417 ? 0.3871 0.3408 0.3893 -0.0354 0.0394  0.0277  417 ILE A C   
3519  O O   . ILE A 417 ? 0.3335 0.3041 0.3555 -0.0390 0.0410  0.0274  417 ILE A O   
3520  C CB  . ILE A 417 ? 0.3682 0.3103 0.3599 -0.0267 0.0215  0.0259  417 ILE A CB  
3521  C CG1 . ILE A 417 ? 0.3820 0.3030 0.3507 -0.0267 0.0222  0.0286  417 ILE A CG1 
3522  C CG2 . ILE A 417 ? 0.3725 0.3242 0.3796 -0.0320 0.0200  0.0260  417 ILE A CG2 
3523  C CD1 . ILE A 417 ? 0.3753 0.2883 0.3351 -0.0202 0.0127  0.0281  417 ILE A CD1 
3524  N N   . GLY A 418 ? 0.3687 0.3077 0.3527 -0.0384 0.0457  0.0301  418 GLY A N   
3525  C CA  . GLY A 418 ? 0.4397 0.3808 0.4271 -0.0482 0.0545  0.0326  418 GLY A CA  
3526  C C   . GLY A 418 ? 0.5288 0.4694 0.5091 -0.0510 0.0669  0.0339  418 GLY A C   
3527  O O   . GLY A 418 ? 0.7522 0.6861 0.7254 -0.0601 0.0746  0.0370  418 GLY A O   
3528  N N   . ASN A 419 ? 0.4417 0.3884 0.4228 -0.0441 0.0699  0.0313  419 ASN A N   
3529  C CA  . ASN A 419 ? 0.4728 0.4177 0.4442 -0.0457 0.0825  0.0319  419 ASN A CA  
3530  C C   . ASN A 419 ? 0.4922 0.4140 0.4332 -0.0406 0.0808  0.0323  419 ASN A C   
3531  O O   . ASN A 419 ? 0.5062 0.4178 0.4381 -0.0350 0.0695  0.0316  419 ASN A O   
3532  C CB  . ASN A 419 ? 0.4558 0.4225 0.4471 -0.0412 0.0890  0.0282  419 ASN A CB  
3533  C CG  . ASN A 419 ? 0.4679 0.4321 0.4570 -0.0303 0.0827  0.0239  419 ASN A CG  
3534  O OD1 . ASN A 419 ? 0.4855 0.4323 0.4549 -0.0266 0.0761  0.0232  419 ASN A OD1 
3535  N ND2 . ASN A 419 ? 0.4725 0.4541 0.4818 -0.0251 0.0849  0.0210  419 ASN A ND2 
3536  N N   . LYS A 420 ? 0.4569 0.3722 0.3824 -0.0425 0.0923  0.0334  420 LYS A N   
3537  C CA  . LYS A 420 ? 0.5066 0.3989 0.3998 -0.0387 0.0910  0.0345  420 LYS A CA  
3538  C C   . LYS A 420 ? 0.4816 0.3729 0.3715 -0.0287 0.0813  0.0293  420 LYS A C   
3539  O O   . LYS A 420 ? 0.4735 0.3505 0.3461 -0.0247 0.0711  0.0299  420 LYS A O   
3540  C CB  . LYS A 420 ? 0.6018 0.4899 0.4797 -0.0424 0.1063  0.0358  420 LYS A CB  
3541  C CG  . LYS A 420 ? 0.7784 0.6634 0.6543 -0.0546 0.1161  0.0417  420 LYS A CG  
3542  C CD  . LYS A 420 ? 0.8903 0.7862 0.7674 -0.0597 0.1342  0.0415  420 LYS A CD  
3543  C CE  . LYS A 420 ? 0.9599 0.8562 0.8391 -0.0744 0.1444  0.0471  420 LYS A CE  
3544  N NZ  . LYS A 420 ? 0.9782 0.9078 0.8926 -0.0800 0.1533  0.0446  420 LYS A NZ  
3545  N N   . GLU A 421 ? 0.4174 0.3243 0.3249 -0.0247 0.0838  0.0242  421 GLU A N   
3546  C CA  . GLU A 421 ? 0.4385 0.3417 0.3402 -0.0171 0.0765  0.0188  421 GLU A CA  
3547  C C   . GLU A 421 ? 0.4107 0.3169 0.3232 -0.0149 0.0619  0.0181  421 GLU A C   
3548  O O   . GLU A 421 ? 0.4226 0.3196 0.3213 -0.0113 0.0525  0.0161  421 GLU A O   
3549  C CB  . GLU A 421 ? 0.5470 0.4619 0.4618 -0.0130 0.0846  0.0136  421 GLU A CB  
3550  C CG  . GLU A 421 ? 0.6543 0.5689 0.5596 -0.0142 0.1006  0.0134  421 GLU A CG  
3551  C CD  . GLU A 421 ? 0.7786 0.7133 0.7078 -0.0192 0.1109  0.0163  421 GLU A CD  
3552  O OE1 . GLU A 421 ? 0.8562 0.8017 0.7920 -0.0169 0.1234  0.0137  421 GLU A OE1 
3553  O OE2 . GLU A 421 ? 0.8210 0.7618 0.7626 -0.0254 0.1064  0.0206  421 GLU A OE2 
3554  N N   . LYS A 422 ? 0.4063 0.3268 0.3431 -0.0172 0.0598  0.0194  422 LYS A N   
3555  C CA  . LYS A 422 ? 0.3420 0.2653 0.2875 -0.0156 0.0471  0.0191  422 LYS A CA  
3556  C C   . LYS A 422 ? 0.4212 0.3311 0.3502 -0.0162 0.0403  0.0224  422 LYS A C   
3557  O O   . LYS A 422 ? 0.3309 0.2389 0.2567 -0.0124 0.0297  0.0210  422 LYS A O   
3558  C CB  . LYS A 422 ? 0.3043 0.2447 0.2764 -0.0181 0.0467  0.0200  422 LYS A CB  
3559  C CG  . LYS A 422 ? 0.3662 0.3198 0.3554 -0.0147 0.0507  0.0170  422 LYS A CG  
3560  C CD  . LYS A 422 ? 0.3010 0.2725 0.3154 -0.0167 0.0497  0.0186  422 LYS A CD  
3561  C CE  . LYS A 422 ? 0.3223 0.3064 0.3520 -0.0118 0.0555  0.0165  422 LYS A CE  
3562  N NZ  . LYS A 422 ? 0.3383 0.3147 0.3632 -0.0052 0.0516  0.0128  422 LYS A NZ  
3563  N N   . ASN A 423 ? 0.3508 0.2512 0.2689 -0.0208 0.0464  0.0270  423 ASN A N   
3564  C CA  . ASN A 423 ? 0.3931 0.2775 0.2938 -0.0197 0.0397  0.0306  423 ASN A CA  
3565  C C   . ASN A 423 ? 0.4463 0.3178 0.3226 -0.0135 0.0345  0.0298  423 ASN A C   
3566  O O   . ASN A 423 ? 0.4283 0.2927 0.2953 -0.0086 0.0243  0.0309  423 ASN A O   
3567  C CB  . ASN A 423 ? 0.3900 0.2627 0.2813 -0.0268 0.0477  0.0360  423 ASN A CB  
3568  C CG  . ASN A 423 ? 0.4353 0.3176 0.3474 -0.0331 0.0482  0.0368  423 ASN A CG  
3569  O OD1 . ASN A 423 ? 0.3938 0.2898 0.3248 -0.0309 0.0412  0.0338  423 ASN A OD1 
3570  N ND2 . ASN A 423 ? 0.4654 0.3403 0.3730 -0.0421 0.0565  0.0406  423 ASN A ND2 
3571  N N   . GLU A 424 ? 0.5116 0.3812 0.3776 -0.0131 0.0409  0.0275  424 GLU A N   
3572  C CA  . GLU A 424 ? 0.5929 0.4508 0.4343 -0.0080 0.0353  0.0261  424 GLU A CA  
3573  C C   . GLU A 424 ? 0.5489 0.4159 0.3988 -0.0032 0.0223  0.0212  424 GLU A C   
3574  O O   . GLU A 424 ? 0.5009 0.3616 0.3356 0.0014  0.0124  0.0213  424 GLU A O   
3575  C CB  . GLU A 424 ? 0.6306 0.4844 0.4589 -0.0089 0.0457  0.0234  424 GLU A CB  
3576  C CG  . GLU A 424 ? 0.6934 0.5373 0.4974 -0.0042 0.0390  0.0199  424 GLU A CG  
3577  C CD  . GLU A 424 ? 0.8214 0.6467 0.5951 -0.0019 0.0347  0.0256  424 GLU A CD  
3578  O OE1 . GLU A 424 ? 0.8419 0.6598 0.5941 0.0021  0.0277  0.0231  424 GLU A OE1 
3579  O OE2 . GLU A 424 ? 0.8528 0.6698 0.6231 -0.0042 0.0378  0.0325  424 GLU A OE2 
3580  N N   . TYR A 425 ? 0.5028 0.3852 0.3768 -0.0044 0.0222  0.0170  425 TYR A N   
3581  C CA  . TYR A 425 ? 0.4349 0.3269 0.3192 -0.0020 0.0109  0.0128  425 TYR A CA  
3582  C C   . TYR A 425 ? 0.4507 0.3458 0.3396 0.0005  0.0014  0.0157  425 TYR A C   
3583  O O   . TYR A 425 ? 0.3925 0.2913 0.2782 0.0040  -0.0091 0.0135  425 TYR A O   
3584  C CB  . TYR A 425 ? 0.4062 0.3111 0.3142 -0.0041 0.0138  0.0096  425 TYR A CB  
3585  C CG  . TYR A 425 ? 0.4514 0.3541 0.3556 -0.0038 0.0168  0.0039  425 TYR A CG  
3586  C CD1 . TYR A 425 ? 0.4181 0.3085 0.3001 -0.0029 0.0224  0.0020  425 TYR A CD1 
3587  C CD2 . TYR A 425 ? 0.3665 0.2772 0.2872 -0.0044 0.0147  0.0003  425 TYR A CD2 
3588  C CE1 . TYR A 425 ? 0.4200 0.3059 0.2968 -0.0022 0.0256  -0.0042 425 TYR A CE1 
3589  C CE2 . TYR A 425 ? 0.3968 0.3015 0.3123 -0.0039 0.0176  -0.0052 425 TYR A CE2 
3590  C CZ  . TYR A 425 ? 0.4704 0.3625 0.3638 -0.0026 0.0231  -0.0079 425 TYR A CZ  
3591  O OH  . TYR A 425 ? 0.3785 0.2619 0.2641 -0.0018 0.0266  -0.0144 425 TYR A OH  
3592  N N   . TRP A 426 ? 0.3454 0.2403 0.2427 -0.0014 0.0050  0.0199  426 TRP A N   
3593  C CA  . TRP A 426 ? 0.4286 0.3237 0.3282 0.0020  -0.0030 0.0221  426 TRP A CA  
3594  C C   . TRP A 426 ? 0.3956 0.2758 0.2704 0.0080  -0.0086 0.0250  426 TRP A C   
3595  O O   . TRP A 426 ? 0.4291 0.3139 0.3038 0.0142  -0.0189 0.0242  426 TRP A O   
3596  C CB  . TRP A 426 ? 0.4301 0.3247 0.3406 -0.0021 0.0023  0.0253  426 TRP A CB  
3597  C CG  . TRP A 426 ? 0.3304 0.2427 0.2667 -0.0056 0.0031  0.0226  426 TRP A CG  
3598  C CD1 . TRP A 426 ? 0.3037 0.2235 0.2530 -0.0107 0.0112  0.0224  426 TRP A CD1 
3599  C CD2 . TRP A 426 ? 0.3078 0.2330 0.2588 -0.0034 -0.0046 0.0201  426 TRP A CD2 
3600  N NE1 . TRP A 426 ? 0.3102 0.2449 0.2800 -0.0114 0.0081  0.0203  426 TRP A NE1 
3601  C CE2 . TRP A 426 ? 0.3550 0.2926 0.3254 -0.0077 -0.0010 0.0190  426 TRP A CE2 
3602  C CE3 . TRP A 426 ? 0.3844 0.3132 0.3344 0.0020  -0.0139 0.0188  426 TRP A CE3 
3603  C CZ2 . TRP A 426 ? 0.3698 0.3204 0.3558 -0.0075 -0.0061 0.0171  426 TRP A CZ2 
3604  C CZ3 . TRP A 426 ? 0.3830 0.3273 0.3509 0.0017  -0.0181 0.0163  426 TRP A CZ3 
3605  C CH2 . TRP A 426 ? 0.3649 0.3185 0.3491 -0.0034 -0.0140 0.0157  426 TRP A CH2 
3606  N N   . LYS A 427 ? 0.4004 0.2637 0.2537 0.0067  -0.0020 0.0287  427 LYS A N   
3607  C CA  . LYS A 427 ? 0.4710 0.3186 0.2985 0.0135  -0.0084 0.0323  427 LYS A CA  
3608  C C   . LYS A 427 ? 0.4363 0.2905 0.2557 0.0183  -0.0179 0.0280  427 LYS A C   
3609  O O   . LYS A 427 ? 0.4719 0.3243 0.2810 0.0262  -0.0286 0.0292  427 LYS A O   
3610  C CB  . LYS A 427 ? 0.5843 0.4096 0.3874 0.0104  0.0011  0.0383  427 LYS A CB  
3611  C CG  . LYS A 427 ? 0.7843 0.5887 0.5571 0.0183  -0.0057 0.0439  427 LYS A CG  
3612  C CD  . LYS A 427 ? 0.7261 0.5313 0.5038 0.0274  -0.0173 0.0452  427 LYS A CD  
3613  C CE  . LYS A 427 ? 0.7116 0.5119 0.5022 0.0237  -0.0124 0.0474  427 LYS A CE  
3614  N NZ  . LYS A 427 ? 0.6895 0.4685 0.4631 0.0317  -0.0174 0.0529  427 LYS A NZ  
3615  N N   . ILE A 428 ? 0.4251 0.2877 0.2499 0.0140  -0.0147 0.0225  428 ILE A N   
3616  C CA  . ILE A 428 ? 0.4749 0.3453 0.2948 0.0164  -0.0244 0.0170  428 ILE A CA  
3617  C C   . ILE A 428 ? 0.4689 0.3576 0.3086 0.0194  -0.0356 0.0144  428 ILE A C   
3618  O O   . ILE A 428 ? 0.4715 0.3659 0.3045 0.0248  -0.0472 0.0131  428 ILE A O   
3619  C CB  . ILE A 428 ? 0.4908 0.3640 0.3140 0.0105  -0.0178 0.0109  428 ILE A CB  
3620  C CG1 . ILE A 428 ? 0.5028 0.3588 0.3012 0.0092  -0.0079 0.0124  428 ILE A CG1 
3621  C CG2 . ILE A 428 ? 0.4458 0.3295 0.2704 0.0101  -0.0282 0.0036  428 ILE A CG2 
3622  C CD1 . ILE A 428 ? 0.5174 0.3742 0.3178 0.0051  0.0003  0.0061  428 ILE A CD1 
3623  N N   . LEU A 429 ? 0.3723 0.2720 0.2368 0.0162  -0.0322 0.0138  429 LEU A N   
3624  C CA  . LEU A 429 ? 0.4171 0.3351 0.3014 0.0183  -0.0407 0.0115  429 LEU A CA  
3625  C C   . LEU A 429 ? 0.3618 0.2777 0.2404 0.0272  -0.0478 0.0154  429 LEU A C   
3626  O O   . LEU A 429 ? 0.4514 0.3813 0.3349 0.0324  -0.0582 0.0131  429 LEU A O   
3627  C CB  . LEU A 429 ? 0.3976 0.3246 0.3056 0.0130  -0.0345 0.0109  429 LEU A CB  
3628  C CG  . LEU A 429 ? 0.4054 0.3521 0.3339 0.0134  -0.0413 0.0081  429 LEU A CG  
3629  C CD1 . LEU A 429 ? 0.3570 0.3152 0.2900 0.0092  -0.0463 0.0022  429 LEU A CD1 
3630  C CD2 . LEU A 429 ? 0.4028 0.3545 0.3500 0.0094  -0.0350 0.0092  429 LEU A CD2 
3631  N N   . ILE A 430 ? 0.3733 0.2714 0.2411 0.0291  -0.0421 0.0212  430 ILE A N   
3632  C CA  . ILE A 430 ? 0.4536 0.3441 0.3126 0.0387  -0.0481 0.0253  430 ILE A CA  
3633  C C   . ILE A 430 ? 0.4992 0.3857 0.3374 0.0473  -0.0580 0.0263  430 ILE A C   
3634  O O   . ILE A 430 ? 0.4414 0.3380 0.2826 0.0569  -0.0684 0.0258  430 ILE A O   
3635  C CB  . ILE A 430 ? 0.4841 0.3515 0.3320 0.0370  -0.0393 0.0313  430 ILE A CB  
3636  C CG1 . ILE A 430 ? 0.4811 0.3563 0.3517 0.0299  -0.0325 0.0297  430 ILE A CG1 
3637  C CG2 . ILE A 430 ? 0.5017 0.3530 0.3325 0.0482  -0.0454 0.0362  430 ILE A CG2 
3638  C CD1 . ILE A 430 ? 0.5156 0.3739 0.3798 0.0219  -0.0210 0.0337  430 ILE A CD1 
3639  N N   . GLU A 431 ? 0.4981 0.3708 0.3146 0.0446  -0.0549 0.0278  431 GLU A N   
3640  C CA  . GLU A 431 ? 0.5671 0.4361 0.3615 0.0524  -0.0651 0.0287  431 GLU A CA  
3641  C C   . GLU A 431 ? 0.5416 0.4378 0.3513 0.0538  -0.0769 0.0217  431 GLU A C   
3642  O O   . GLU A 431 ? 0.5638 0.4690 0.3705 0.0638  -0.0891 0.0221  431 GLU A O   
3643  C CB  . GLU A 431 ? 0.6445 0.4957 0.4131 0.0475  -0.0587 0.0301  431 GLU A CB  
3644  C CG  . GLU A 431 ? 0.7787 0.6007 0.5225 0.0484  -0.0502 0.0387  431 GLU A CG  
3645  C CD  . GLU A 431 ? 0.9101 0.7199 0.6430 0.0600  -0.0576 0.0451  431 GLU A CD  
3646  O OE1 . GLU A 431 ? 0.9419 0.7430 0.6827 0.0592  -0.0519 0.0484  431 GLU A OE1 
3647  O OE2 . GLU A 431 ? 0.9193 0.7280 0.6355 0.0702  -0.0695 0.0467  431 GLU A OE2 
3648  N N   . ALA A 432 ? 0.4402 0.3504 0.2673 0.0438  -0.0733 0.0153  432 ALA A N   
3649  C CA  . ALA A 432 ? 0.4920 0.4268 0.3333 0.0416  -0.0831 0.0082  432 ALA A CA  
3650  C C   . ALA A 432 ? 0.4857 0.4428 0.3510 0.0467  -0.0897 0.0072  432 ALA A C   
3651  O O   . ALA A 432 ? 0.4372 0.4153 0.3094 0.0500  -0.1012 0.0034  432 ALA A O   
3652  C CB  . ALA A 432 ? 0.4667 0.4053 0.3188 0.0293  -0.0759 0.0023  432 ALA A CB  
3653  N N   . LYS A 433 ? 0.4341 0.3887 0.3129 0.0470  -0.0824 0.0098  433 LYS A N   
3654  C CA  . LYS A 433 ? 0.4813 0.4553 0.3806 0.0527  -0.0872 0.0088  433 LYS A CA  
3655  C C   . LYS A 433 ? 0.5023 0.4777 0.3912 0.0676  -0.0977 0.0117  433 LYS A C   
3656  O O   . LYS A 433 ? 0.4101 0.4104 0.3151 0.0734  -0.1060 0.0086  433 LYS A O   
3657  C CB  . LYS A 433 ? 0.4710 0.4372 0.3811 0.0504  -0.0772 0.0113  433 LYS A CB  
3658  C CG  . LYS A 433 ? 0.5182 0.4998 0.4454 0.0573  -0.0804 0.0104  433 LYS A CG  
3659  C CD  . LYS A 433 ? 0.4853 0.4983 0.4350 0.0537  -0.0857 0.0043  433 LYS A CD  
3660  C CE  . LYS A 433 ? 0.4478 0.4764 0.4147 0.0603  -0.0864 0.0033  433 LYS A CE  
3661  N NZ  . LYS A 433 ? 0.4158 0.4774 0.4046 0.0569  -0.0913 -0.0022 433 LYS A NZ  
3662  N N   . LYS A 434 ? 0.5281 0.4778 0.3896 0.0742  -0.0977 0.0177  434 LYS A N   
3663  C CA  . LYS A 434 ? 0.5717 0.5197 0.4198 0.0899  -0.1085 0.0212  434 LYS A CA  
3664  C C   . LYS A 434 ? 0.5662 0.5397 0.4174 0.0926  -0.1222 0.0166  434 LYS A C   
3665  O O   . LYS A 434 ? 0.5474 0.5344 0.4004 0.1062  -0.1333 0.0172  434 LYS A O   
3666  C CB  . LYS A 434 ? 0.7001 0.6126 0.5141 0.0945  -0.1056 0.0291  434 LYS A CB  
3667  C CG  . LYS A 434 ? 0.7335 0.6184 0.5409 0.0903  -0.0923 0.0342  434 LYS A CG  
3668  C CD  . LYS A 434 ? 0.7904 0.6402 0.5622 0.0952  -0.0902 0.0427  434 LYS A CD  
3669  C CE  . LYS A 434 ? 0.7892 0.6131 0.5559 0.0882  -0.0765 0.0472  434 LYS A CE  
3670  N NZ  . LYS A 434 ? 0.8065 0.5952 0.5379 0.0896  -0.0723 0.0557  434 LYS A NZ  
3671  N N   . LYS A 435 ? 0.5742 0.5540 0.4251 0.0803  -0.1218 0.0116  435 LYS A N   
3672  C CA  . LYS A 435 ? 0.5679 0.5687 0.4175 0.0803  -0.1349 0.0066  435 LYS A CA  
3673  C C   . LYS A 435 ? 0.5271 0.5581 0.4052 0.0684  -0.1363 -0.0020 435 LYS A C   
3674  O O   . LYS A 435 ? 0.5381 0.5857 0.4160 0.0635  -0.1456 -0.0076 435 LYS A O   
3675  C CB  . LYS A 435 ? 0.6124 0.5922 0.4314 0.0758  -0.1349 0.0073  435 LYS A CB  
3676  C CG  . LYS A 435 ? 0.6643 0.6158 0.4509 0.0880  -0.1362 0.0162  435 LYS A CG  
3677  C CD  . LYS A 435 ? 0.7498 0.6761 0.5059 0.0811  -0.1306 0.0174  435 LYS A CD  
3678  C CE  . LYS A 435 ? 0.8338 0.7719 0.5763 0.0800  -0.1435 0.0122  435 LYS A CE  
3679  N NZ  . LYS A 435 ? 0.9020 0.8343 0.6388 0.0649  -0.1360 0.0055  435 LYS A NZ  
3680  N N   . ALA A 436 ? 0.4947 0.4776 0.4832 0.1026  -0.1333 -0.0067 436 ALA A N   
3681  C CA  . ALA A 436 ? 0.4744 0.4989 0.5013 0.0925  -0.1251 -0.0084 436 ALA A CA  
3682  C C   . ALA A 436 ? 0.4264 0.4881 0.4990 0.1043  -0.1335 -0.0135 436 ALA A C   
3683  O O   . ALA A 436 ? 0.4014 0.4649 0.4834 0.1217  -0.1366 -0.0169 436 ALA A O   
3684  C CB  . ALA A 436 ? 0.4561 0.4887 0.4845 0.0836  -0.1032 -0.0082 436 ALA A CB  
3685  N N   . LYS A 437 ? 0.4150 0.5065 0.5178 0.0947  -0.1368 -0.0142 437 LYS A N   
3686  C CA  . LYS A 437 ? 0.3931 0.5265 0.5467 0.1020  -0.1436 -0.0193 437 LYS A CA  
3687  C C   . LYS A 437 ? 0.3609 0.5324 0.5514 0.0882  -0.1264 -0.0201 437 LYS A C   
3688  O O   . LYS A 437 ? 0.4192 0.6297 0.6564 0.0923  -0.1273 -0.0245 437 LYS A O   
3689  C CB  . LYS A 437 ? 0.4226 0.5573 0.5825 0.1039  -0.1703 -0.0205 437 LYS A CB  
3690  C CG  . LYS A 437 ? 0.5524 0.6597 0.6891 0.1236  -0.1909 -0.0205 437 LYS A CG  
3691  C CD  . LYS A 437 ? 0.6512 0.7175 0.7399 0.1169  -0.2056 -0.0164 437 LYS A CD  
3692  C CE  . LYS A 437 ? 0.6955 0.7164 0.7390 0.1304  -0.2127 -0.0129 437 LYS A CE  
3693  N NZ  . LYS A 437 ? 0.6740 0.6479 0.6600 0.1206  -0.2104 -0.0074 437 LYS A NZ  
3694  N N   . ASN A 438 ? 0.2973 0.4590 0.4693 0.0721  -0.1111 -0.0156 438 ASN A N   
3695  C CA  . ASN A 438 ? 0.3165 0.5077 0.5169 0.0584  -0.0951 -0.0147 438 ASN A CA  
3696  C C   . ASN A 438 ? 0.3263 0.4994 0.4973 0.0486  -0.0770 -0.0095 438 ASN A C   
3697  O O   . ASN A 438 ? 0.2907 0.4321 0.4242 0.0509  -0.0775 -0.0074 438 ASN A O   
3698  C CB  . ASN A 438 ? 0.2833 0.4859 0.5012 0.0448  -0.1055 -0.0143 438 ASN A CB  
3699  C CG  . ASN A 438 ? 0.2929 0.4592 0.4707 0.0375  -0.1142 -0.0110 438 ASN A CG  
3700  O OD1 . ASN A 438 ? 0.3299 0.4790 0.4837 0.0287  -0.1014 -0.0063 438 ASN A OD1 
3701  N ND2 . ASN A 438 ? 0.3091 0.4630 0.4782 0.0420  -0.1361 -0.0136 438 ASN A ND2 
3702  N N   . ASP A 439 ? 0.2943 0.4871 0.4824 0.0364  -0.0619 -0.0069 439 ASP A N   
3703  C CA  . ASP A 439 ? 0.3134 0.4944 0.4782 0.0292  -0.0453 -0.0020 439 ASP A CA  
3704  C C   . ASP A 439 ? 0.2674 0.4237 0.4048 0.0185  -0.0481 0.0035  439 ASP A C   
3705  O O   . ASP A 439 ? 0.2606 0.4093 0.3818 0.0122  -0.0369 0.0082  439 ASP A O   
3706  C CB  . ASP A 439 ? 0.4056 0.6134 0.5945 0.0212  -0.0276 -0.0002 439 ASP A CB  
3707  C CG  . ASP A 439 ? 0.4575 0.6847 0.6629 0.0327  -0.0164 -0.0056 439 ASP A CG  
3708  O OD1 . ASP A 439 ? 0.4900 0.7021 0.6778 0.0463  -0.0192 -0.0097 439 ASP A OD1 
3709  O OD2 . ASP A 439 ? 0.5085 0.7648 0.7444 0.0280  -0.0037 -0.0061 439 ASP A OD2 
3710  N N   . TYR A 440 ? 0.2702 0.4136 0.4013 0.0170  -0.0630 0.0029  440 TYR A N   
3711  C CA  . TYR A 440 ? 0.2476 0.3662 0.3514 0.0092  -0.0634 0.0070  440 TYR A CA  
3712  C C   . TYR A 440 ? 0.2390 0.3339 0.3109 0.0140  -0.0606 0.0081  440 TYR A C   
3713  O O   . TYR A 440 ? 0.2926 0.3730 0.3466 0.0074  -0.0562 0.0118  440 TYR A O   
3714  C CB  . TYR A 440 ? 0.3349 0.4427 0.4356 0.0066  -0.0786 0.0049  440 TYR A CB  
3715  C CG  . TYR A 440 ? 0.2809 0.4005 0.4017 -0.0056 -0.0776 0.0059  440 TYR A CG  
3716  C CD1 . TYR A 440 ? 0.3143 0.4239 0.4251 -0.0148 -0.0678 0.0110  440 TYR A CD1 
3717  C CD2 . TYR A 440 ? 0.3641 0.5048 0.5155 -0.0079 -0.0870 0.0017  440 TYR A CD2 
3718  C CE1 . TYR A 440 ? 0.4005 0.5152 0.5265 -0.0260 -0.0667 0.0122  440 TYR A CE1 
3719  C CE2 . TYR A 440 ? 0.4100 0.5588 0.5793 -0.0214 -0.0859 0.0023  440 TYR A CE2 
3720  C CZ  . TYR A 440 ? 0.4368 0.5700 0.5911 -0.0304 -0.0752 0.0078  440 TYR A CZ  
3721  O OH  . TYR A 440 ? 0.4954 0.6310 0.6644 -0.0438 -0.0739 0.0088  440 TYR A OH  
3722  N N   . ILE A 441 ? 0.2648 0.3556 0.3313 0.0251  -0.0629 0.0046  441 ILE A N   
3723  C CA  . ILE A 441 ? 0.2795 0.3478 0.3173 0.0280  -0.0590 0.0051  441 ILE A CA  
3724  C C   . ILE A 441 ? 0.2349 0.3101 0.2704 0.0221  -0.0450 0.0074  441 ILE A C   
3725  O O   . ILE A 441 ? 0.2865 0.3456 0.3004 0.0178  -0.0417 0.0093  441 ILE A O   
3726  C CB  . ILE A 441 ? 0.3043 0.3639 0.3373 0.0423  -0.0654 0.0004  441 ILE A CB  
3727  C CG1 . ILE A 441 ? 0.2947 0.3229 0.2935 0.0433  -0.0636 0.0007  441 ILE A CG1 
3728  C CG2 . ILE A 441 ? 0.3016 0.3854 0.3585 0.0498  -0.0575 -0.0035 441 ILE A CG2 
3729  C CD1 . ILE A 441 ? 0.3225 0.3224 0.2958 0.0417  -0.0728 0.0029  441 ILE A CD1 
3730  N N   . LEU A 442 ? 0.2242 0.3234 0.2811 0.0210  -0.0367 0.0075  442 LEU A N   
3731  C CA  . LEU A 442 ? 0.2011 0.3051 0.2519 0.0146  -0.0247 0.0110  442 LEU A CA  
3732  C C   . LEU A 442 ? 0.2155 0.3150 0.2610 0.0039  -0.0244 0.0176  442 LEU A C   
3733  O O   . LEU A 442 ? 0.2555 0.3487 0.2859 -0.0002 -0.0201 0.0207  442 LEU A O   
3734  C CB  . LEU A 442 ? 0.1897 0.3184 0.2626 0.0152  -0.0142 0.0102  442 LEU A CB  
3735  C CG  . LEU A 442 ? 0.3003 0.4385 0.3845 0.0279  -0.0118 0.0029  442 LEU A CG  
3736  C CD1 . LEU A 442 ? 0.3662 0.5332 0.4775 0.0266  0.0013  0.0024  442 LEU A CD1 
3737  C CD2 . LEU A 442 ? 0.2768 0.3949 0.3329 0.0346  -0.0086 -0.0011 442 LEU A CD2 
3738  N N   . VAL A 443 ? 0.1987 0.3013 0.2570 -0.0001 -0.0295 0.0192  443 VAL A N   
3739  C CA  . VAL A 443 ? 0.2419 0.3370 0.2951 -0.0081 -0.0291 0.0247  443 VAL A CA  
3740  C C   . VAL A 443 ? 0.3057 0.3819 0.3376 -0.0075 -0.0320 0.0246  443 VAL A C   
3741  O O   . VAL A 443 ? 0.3113 0.3846 0.3364 -0.0115 -0.0283 0.0287  443 VAL A O   
3742  C CB  . VAL A 443 ? 0.3490 0.4459 0.4166 -0.0121 -0.0349 0.0244  443 VAL A CB  
3743  C CG1 . VAL A 443 ? 0.3750 0.4619 0.4374 -0.0188 -0.0329 0.0295  443 VAL A CG1 
3744  C CG2 . VAL A 443 ? 0.3332 0.4520 0.4269 -0.0143 -0.0321 0.0235  443 VAL A CG2 
3745  N N   . ALA A 444 ? 0.3095 0.3728 0.3314 -0.0027 -0.0386 0.0202  444 ALA A N   
3746  C CA  . ALA A 444 ? 0.2980 0.3422 0.2993 -0.0038 -0.0392 0.0200  444 ALA A CA  
3747  C C   . ALA A 444 ? 0.3095 0.3517 0.3004 -0.0047 -0.0344 0.0201  444 ALA A C   
3748  O O   . ALA A 444 ? 0.3328 0.3638 0.3115 -0.0087 -0.0330 0.0206  444 ALA A O   
3749  C CB  . ALA A 444 ? 0.2853 0.3116 0.2730 0.0014  -0.0473 0.0163  444 ALA A CB  
3750  N N   . GLU A 445 ? 0.2996 0.3525 0.2948 -0.0021 -0.0312 0.0190  445 GLU A N   
3751  C CA  . GLU A 445 ? 0.3156 0.3645 0.2978 -0.0042 -0.0278 0.0181  445 GLU A CA  
3752  C C   . GLU A 445 ? 0.3140 0.3734 0.2991 -0.0108 -0.0247 0.0233  445 GLU A C   
3753  O O   . GLU A 445 ? 0.3087 0.3664 0.2829 -0.0135 -0.0241 0.0226  445 GLU A O   
3754  C CB  . GLU A 445 ? 0.3328 0.3834 0.3122 0.0027  -0.0251 0.0132  445 GLU A CB  
3755  C CG  . GLU A 445 ? 0.3842 0.4178 0.3543 0.0108  -0.0297 0.0078  445 GLU A CG  
3756  C CD  . GLU A 445 ? 0.4361 0.4782 0.4158 0.0218  -0.0276 0.0029  445 GLU A CD  
3757  O OE1 . GLU A 445 ? 0.4443 0.5028 0.4322 0.0217  -0.0194 0.0026  445 GLU A OE1 
3758  O OE2 . GLU A 445 ? 0.4000 0.4320 0.3788 0.0311  -0.0338 -0.0005 445 GLU A OE2 
3759  N N   . GLY A 446 ? 0.2873 0.3553 0.2854 -0.0130 -0.0242 0.0285  446 GLY A N   
3760  C CA  . GLY A 446 ? 0.2717 0.3469 0.2713 -0.0171 -0.0229 0.0345  446 GLY A CA  
3761  C C   . GLY A 446 ? 0.2690 0.3404 0.2639 -0.0206 -0.0258 0.0348  446 GLY A C   
3762  O O   . GLY A 446 ? 0.1893 0.2527 0.1839 -0.0214 -0.0264 0.0324  446 GLY A O   
3763  N N   . SER A 447 ? 0.2371 0.3146 0.2278 -0.0231 -0.0277 0.0378  447 SER A N   
3764  C CA  . SER A 447 ? 0.3121 0.3910 0.3033 -0.0274 -0.0317 0.0371  447 SER A CA  
3765  C C   . SER A 447 ? 0.2456 0.3288 0.2530 -0.0271 -0.0310 0.0405  447 SER A C   
3766  O O   . SER A 447 ? 0.2484 0.3318 0.2604 -0.0306 -0.0306 0.0379  447 SER A O   
3767  C CB  . SER A 447 ? 0.2786 0.3641 0.2620 -0.0298 -0.0370 0.0394  447 SER A CB  
3768  O OG  . SER A 447 ? 0.2744 0.3674 0.2635 -0.0273 -0.0386 0.0476  447 SER A OG  
3769  N N   . ASP A 448 ? 0.2127 0.2981 0.2285 -0.0234 -0.0297 0.0457  448 ASP A N   
3770  C CA  . ASP A 448 ? 0.2001 0.2881 0.2301 -0.0212 -0.0287 0.0487  448 ASP A CA  
3771  C C   . ASP A 448 ? 0.2461 0.3262 0.2774 -0.0222 -0.0238 0.0433  448 ASP A C   
3772  O O   . ASP A 448 ? 0.2485 0.3334 0.2910 -0.0220 -0.0211 0.0433  448 ASP A O   
3773  C CB  . ASP A 448 ? 0.2194 0.3033 0.2535 -0.0177 -0.0272 0.0539  448 ASP A CB  
3774  C CG  . ASP A 448 ? 0.2462 0.3333 0.2741 -0.0176 -0.0296 0.0604  448 ASP A CG  
3775  O OD1 . ASP A 448 ? 0.2781 0.3636 0.2979 -0.0196 -0.0269 0.0592  448 ASP A OD1 
3776  O OD2 . ASP A 448 ? 0.2740 0.3649 0.3046 -0.0151 -0.0338 0.0669  448 ASP A OD2 
3777  N N   . TRP A 449 ? 0.2859 0.3539 0.3057 -0.0227 -0.0222 0.0389  449 TRP A N   
3778  C CA  . TRP A 449 ? 0.3197 0.3749 0.3330 -0.0237 -0.0180 0.0345  449 TRP A CA  
3779  C C   . TRP A 449 ? 0.2601 0.3163 0.2719 -0.0293 -0.0151 0.0322  449 TRP A C   
3780  O O   . TRP A 449 ? 0.2565 0.3099 0.2711 -0.0311 -0.0084 0.0309  449 TRP A O   
3781  C CB  . TRP A 449 ? 0.3149 0.3561 0.3141 -0.0221 -0.0204 0.0309  449 TRP A CB  
3782  C CG  . TRP A 449 ? 0.2789 0.3247 0.2842 -0.0190 -0.0240 0.0324  449 TRP A CG  
3783  C CD1 . TRP A 449 ? 0.2954 0.3452 0.2999 -0.0172 -0.0268 0.0313  449 TRP A CD1 
3784  C CD2 . TRP A 449 ? 0.2099 0.2562 0.2244 -0.0181 -0.0236 0.0349  449 TRP A CD2 
3785  N NE1 . TRP A 449 ? 0.2613 0.3177 0.2769 -0.0167 -0.0275 0.0333  449 TRP A NE1 
3786  C CE2 . TRP A 449 ? 0.2082 0.2603 0.2284 -0.0180 -0.0263 0.0356  449 TRP A CE2 
3787  C CE3 . TRP A 449 ? 0.2744 0.3155 0.2930 -0.0175 -0.0204 0.0360  449 TRP A CE3 
3788  C CZ2 . TRP A 449 ? 0.2205 0.2726 0.2500 -0.0194 -0.0265 0.0379  449 TRP A CZ2 
3789  C CZ3 . TRP A 449 ? 0.2782 0.3160 0.3032 -0.0171 -0.0212 0.0379  449 TRP A CZ3 
3790  C CH2 . TRP A 449 ? 0.2160 0.2587 0.2461 -0.0192 -0.0246 0.0391  449 TRP A CH2 
3791  N N   . PHE A 450 ? 0.2740 0.3336 0.2809 -0.0328 -0.0191 0.0312  450 PHE A N   
3792  C CA  . PHE A 450 ? 0.3297 0.3897 0.3362 -0.0408 -0.0171 0.0286  450 PHE A CA  
3793  C C   . PHE A 450 ? 0.2770 0.3588 0.3066 -0.0432 -0.0175 0.0310  450 PHE A C   
3794  O O   . PHE A 450 ? 0.2559 0.3420 0.2944 -0.0495 -0.0119 0.0290  450 PHE A O   
3795  C CB  . PHE A 450 ? 0.3471 0.3999 0.3387 -0.0441 -0.0220 0.0255  450 PHE A CB  
3796  C CG  . PHE A 450 ? 0.2972 0.3308 0.2703 -0.0391 -0.0223 0.0230  450 PHE A CG  
3797  C CD1 . PHE A 450 ? 0.2972 0.3349 0.2705 -0.0317 -0.0254 0.0239  450 PHE A CD1 
3798  C CD2 . PHE A 450 ? 0.2874 0.2989 0.2438 -0.0414 -0.0194 0.0201  450 PHE A CD2 
3799  C CE1 . PHE A 450 ? 0.3195 0.3442 0.2819 -0.0257 -0.0266 0.0211  450 PHE A CE1 
3800  C CE2 . PHE A 450 ? 0.3390 0.3331 0.2798 -0.0344 -0.0222 0.0182  450 PHE A CE2 
3801  C CZ  . PHE A 450 ? 0.3482 0.3513 0.2948 -0.0260 -0.0263 0.0183  450 PHE A CZ  
3802  N N   . TRP A 451 ? 0.2810 0.3767 0.3210 -0.0380 -0.0237 0.0356  451 TRP A N   
3803  C CA  . TRP A 451 ? 0.2902 0.4073 0.3539 -0.0371 -0.0269 0.0387  451 TRP A CA  
3804  C C   . TRP A 451 ? 0.2889 0.4099 0.3696 -0.0343 -0.0171 0.0383  451 TRP A C   
3805  O O   . TRP A 451 ? 0.3033 0.4411 0.4050 -0.0377 -0.0146 0.0370  451 TRP A O   
3806  C CB  . TRP A 451 ? 0.2414 0.3648 0.3067 -0.0299 -0.0350 0.0453  451 TRP A CB  
3807  C CG  . TRP A 451 ? 0.3054 0.4474 0.3948 -0.0246 -0.0395 0.0501  451 TRP A CG  
3808  C CD1 . TRP A 451 ? 0.3296 0.4720 0.4321 -0.0155 -0.0359 0.0539  451 TRP A CD1 
3809  C CD2 . TRP A 451 ? 0.3596 0.5219 0.4635 -0.0271 -0.0500 0.0510  451 TRP A CD2 
3810  N NE1 . TRP A 451 ? 0.2996 0.4617 0.4252 -0.0104 -0.0430 0.0577  451 TRP A NE1 
3811  C CE2 . TRP A 451 ? 0.3617 0.5383 0.4898 -0.0177 -0.0527 0.0561  451 TRP A CE2 
3812  C CE3 . TRP A 451 ? 0.4346 0.6034 0.5329 -0.0364 -0.0586 0.0475  451 TRP A CE3 
3813  C CZ2 . TRP A 451 ? 0.3705 0.5710 0.5204 -0.0164 -0.0650 0.0582  451 TRP A CZ2 
3814  C CZ3 . TRP A 451 ? 0.4247 0.6163 0.5426 -0.0373 -0.0710 0.0490  451 TRP A CZ3 
3815  C CH2 . TRP A 451 ? 0.4131 0.6220 0.5581 -0.0269 -0.0747 0.0546  451 TRP A CH2 
3816  N N   . TRP A 452 ? 0.2060 0.3126 0.2793 -0.0281 -0.0113 0.0387  452 TRP A N   
3817  C CA  . TRP A 452 ? 0.2436 0.3504 0.3290 -0.0239 -0.0011 0.0375  452 TRP A CA  
3818  C C   . TRP A 452 ? 0.2685 0.3652 0.3452 -0.0309 0.0108  0.0320  452 TRP A C   
3819  O O   . TRP A 452 ? 0.2368 0.3395 0.3274 -0.0297 0.0219  0.0301  452 TRP A O   
3820  C CB  . TRP A 452 ? 0.2290 0.3200 0.3058 -0.0160 0.0000  0.0390  452 TRP A CB  
3821  C CG  . TRP A 452 ? 0.2698 0.3675 0.3553 -0.0094 -0.0087 0.0457  452 TRP A CG  
3822  C CD1 . TRP A 452 ? 0.3074 0.3970 0.3803 -0.0092 -0.0151 0.0492  452 TRP A CD1 
3823  C CD2 . TRP A 452 ? 0.2543 0.3672 0.3622 -0.0019 -0.0115 0.0503  452 TRP A CD2 
3824  N NE1 . TRP A 452 ? 0.2624 0.3575 0.3441 -0.0034 -0.0207 0.0564  452 TRP A NE1 
3825  C CE2 . TRP A 452 ? 0.2482 0.3567 0.3506 0.0022  -0.0201 0.0574  452 TRP A CE2 
3826  C CE3 . TRP A 452 ? 0.2230 0.3535 0.3564 0.0022  -0.0074 0.0492  452 TRP A CE3 
3827  C CZ2 . TRP A 452 ? 0.2651 0.3818 0.3821 0.0110  -0.0265 0.0643  452 TRP A CZ2 
3828  C CZ3 . TRP A 452 ? 0.2717 0.4147 0.4250 0.0123  -0.0143 0.0551  452 TRP A CZ3 
3829  C CH2 . TRP A 452 ? 0.2918 0.4257 0.4346 0.0170  -0.0247 0.0631  452 TRP A CH2 
3830  N N   . GLN A 453 ? 0.2445 0.3252 0.2982 -0.0379 0.0096  0.0297  453 GLN A N   
3831  C CA  . GLN A 453 ? 0.3489 0.4131 0.3873 -0.0447 0.0208  0.0259  453 GLN A CA  
3832  C C   . GLN A 453 ? 0.4173 0.5001 0.4770 -0.0535 0.0285  0.0245  453 GLN A C   
3833  O O   . GLN A 453 ? 0.3823 0.4823 0.4560 -0.0590 0.0204  0.0250  453 GLN A O   
3834  C CB  . GLN A 453 ? 0.3109 0.3518 0.3197 -0.0485 0.0159  0.0246  453 GLN A CB  
3835  C CG  . GLN A 453 ? 0.3045 0.3233 0.2921 -0.0566 0.0264  0.0222  453 GLN A CG  
3836  C CD  . GLN A 453 ? 0.3847 0.3836 0.3543 -0.0523 0.0354  0.0211  453 GLN A CD  
3837  O OE1 . GLN A 453 ? 0.4441 0.4502 0.4245 -0.0449 0.0369  0.0210  453 GLN A OE1 
3838  N NE2 . GLN A 453 ? 0.4538 0.4239 0.3924 -0.0572 0.0410  0.0202  453 GLN A NE2 
3839  N N   . GLY A 454 ? 0.4843 0.5630 0.5454 -0.0557 0.0445  0.0222  454 GLY A N   
3840  C CA  . GLY A 454 ? 0.5611 0.6662 0.6553 -0.0598 0.0554  0.0208  454 GLY A CA  
3841  C C   . GLY A 454 ? 0.6196 0.7520 0.7406 -0.0699 0.0487  0.0207  454 GLY A C   
3842  O O   . GLY A 454 ? 0.6268 0.7468 0.7311 -0.0816 0.0459  0.0196  454 GLY A O   
3843  N N   . GLU A 455 ? 0.6946 0.8623 0.8561 -0.0656 0.0446  0.0216  455 GLU A N   
3844  C CA  . GLU A 455 ? 0.7260 0.9099 0.9113 -0.0495 0.0444  0.0236  455 GLU A CA  
3845  C C   . GLU A 455 ? 0.7730 0.9537 0.9648 -0.0431 0.0652  0.0206  455 GLU A C   
3846  O O   . GLU A 455 ? 0.7686 0.9185 0.9276 -0.0438 0.0766  0.0185  455 GLU A O   
3847  C CB  . GLU A 455 ? 0.7338 0.9014 0.8987 -0.0380 0.0307  0.0279  455 GLU A CB  
3848  C CG  . GLU A 455 ? 0.7368 0.8973 0.8827 -0.0437 0.0145  0.0300  455 GLU A CG  
3849  C CD  . GLU A 455 ? 0.7595 0.9481 0.9295 -0.0489 0.0017  0.0309  455 GLU A CD  
3850  O OE1 . GLU A 455 ? 0.7784 0.9891 0.9741 -0.0397 -0.0063 0.0345  455 GLU A OE1 
3851  O OE2 . GLU A 455 ? 0.7854 0.9717 0.9468 -0.0619 -0.0017 0.0280  455 GLU A OE2 
3852  N N   . GLU A 456 ? 0.8017 1.0148 1.0363 -0.0356 0.0691  0.0201  456 GLU A N   
3853  C CA  . GLU A 456 ? 0.8183 1.0321 1.0645 -0.0266 0.0896  0.0164  456 GLU A CA  
3854  C C   . GLU A 456 ? 0.8017 0.9839 1.0187 -0.0127 0.0888  0.0171  456 GLU A C   
3855  O O   . GLU A 456 ? 0.7619 0.9316 0.9626 -0.0082 0.0711  0.0216  456 GLU A O   
3856  C CB  . GLU A 456 ? 0.8042 1.0620 1.1070 -0.0177 0.0903  0.0160  456 GLU A CB  
3857  N N   . LYS A 457 ? 0.8155 0.9843 1.0257 -0.0068 0.1092  0.0120  457 LYS A N   
3858  C CA  . LYS A 457 ? 0.8435 0.9767 1.0208 0.0032  0.1117  0.0102  457 LYS A CA  
3859  C C   . LYS A 457 ? 0.8664 0.9963 1.0463 0.0148  0.0917  0.0156  457 LYS A C   
3860  O O   . LYS A 457 ? 0.9302 1.0430 1.0843 0.0101  0.0770  0.0191  457 LYS A O   
3861  C CB  . LYS A 457 ? 0.8609 0.9910 1.0457 0.0124  0.1356  0.0034  457 LYS A CB  
3862  N N   . ALA A 458 ? 0.7997 0.9450 1.0104 0.0301  0.0918  0.0165  458 ALA A N   
3863  C CA  . ALA A 458 ? 0.7071 0.8466 0.9205 0.0420  0.0748  0.0227  458 ALA A CA  
3864  C C   . ALA A 458 ? 0.5712 0.6686 0.7456 0.0446  0.0744  0.0211  458 ALA A C   
3865  O O   . ALA A 458 ? 0.5266 0.6016 0.6668 0.0338  0.0753  0.0184  458 ALA A O   
3866  C CB  . ALA A 458 ? 0.7108 0.8655 0.9284 0.0355  0.0529  0.0307  458 ALA A CB  
3867  N N   . PRO A 459 ? 0.4942 0.5791 0.6729 0.0587  0.0718  0.0227  459 PRO A N   
3868  C CA  . PRO A 459 ? 0.5135 0.5575 0.6570 0.0596  0.0724  0.0196  459 PRO A CA  
3869  C C   . PRO A 459 ? 0.5818 0.6127 0.7023 0.0495  0.0552  0.0252  459 PRO A C   
3870  O O   . PRO A 459 ? 0.5793 0.6265 0.7119 0.0483  0.0412  0.0336  459 PRO A O   
3871  C CB  . PRO A 459 ? 0.5031 0.5389 0.6623 0.0775  0.0735  0.0206  459 PRO A CB  
3872  C CG  . PRO A 459 ? 0.4758 0.5498 0.6796 0.0879  0.0790  0.0216  459 PRO A CG  
3873  C CD  . PRO A 459 ? 0.4992 0.6044 0.7151 0.0750  0.0687  0.0267  459 PRO A CD  
3874  N N   . PHE A 460 ? 0.5501 0.5518 0.6370 0.0422  0.0567  0.0199  460 PHE A N   
3875  C CA  . PHE A 460 ? 0.4689 0.4566 0.5343 0.0326  0.0431  0.0226  460 PHE A CA  
3876  C C   . PHE A 460 ? 0.3372 0.3410 0.3987 0.0214  0.0365  0.0250  460 PHE A C   
3877  O O   . PHE A 460 ? 0.3433 0.3385 0.3897 0.0144  0.0266  0.0264  460 PHE A O   
3878  C CB  . PHE A 460 ? 0.4893 0.4735 0.5626 0.0365  0.0313  0.0307  460 PHE A CB  
3879  C CG  . PHE A 460 ? 0.5665 0.5265 0.6384 0.0469  0.0360  0.0286  460 PHE A CG  
3880  C CD1 . PHE A 460 ? 0.5688 0.4967 0.6153 0.0448  0.0415  0.0195  460 PHE A CD1 
3881  C CD2 . PHE A 460 ? 0.5829 0.5494 0.6766 0.0595  0.0340  0.0353  460 PHE A CD2 
3882  C CE1 . PHE A 460 ? 0.5749 0.4760 0.6175 0.0544  0.0462  0.0163  460 PHE A CE1 
3883  C CE2 . PHE A 460 ? 0.5798 0.5200 0.6710 0.0705  0.0386  0.0332  460 PHE A CE2 
3884  C CZ  . PHE A 460 ? 0.5882 0.4947 0.6535 0.0676  0.0455  0.0232  460 PHE A CZ  
3885  N N   . VAL A 461 ? 0.3166 0.3422 0.3913 0.0190  0.0424  0.0246  461 VAL A N   
3886  C CA  . VAL A 461 ? 0.4211 0.4560 0.4884 0.0084  0.0358  0.0264  461 VAL A CA  
3887  C C   . VAL A 461 ? 0.4581 0.4689 0.4925 0.0013  0.0365  0.0213  461 VAL A C   
3888  O O   . VAL A 461 ? 0.5289 0.5405 0.5534 -0.0053 0.0277  0.0231  461 VAL A O   
3889  C CB  . VAL A 461 ? 0.5555 0.6157 0.6426 0.0049  0.0420  0.0263  461 VAL A CB  
3890  C CG1 . VAL A 461 ? 0.5800 0.6662 0.7023 0.0135  0.0394  0.0307  461 VAL A CG1 
3891  C CG2 . VAL A 461 ? 0.6111 0.6613 0.6872 0.0018  0.0598  0.0194  461 VAL A CG2 
3892  N N   . GLU A 462 ? 0.3430 0.3306 0.3583 0.0033  0.0462  0.0149  462 GLU A N   
3893  C CA  . GLU A 462 ? 0.4077 0.3697 0.3882 -0.0024 0.0434  0.0105  462 GLU A CA  
3894  C C   . GLU A 462 ? 0.3684 0.3222 0.3421 -0.0038 0.0273  0.0120  462 GLU A C   
3895  O O   . GLU A 462 ? 0.4249 0.3683 0.3791 -0.0086 0.0190  0.0105  462 GLU A O   
3896  C CB  . GLU A 462 ? 0.5396 0.4755 0.4964 0.0001  0.0567  0.0028  462 GLU A CB  
3897  C CG  . GLU A 462 ? 0.7162 0.6631 0.6885 0.0043  0.0766  0.0006  462 GLU A CG  
3898  C CD  . GLU A 462 ? 0.8695 0.8230 0.8666 0.0158  0.0807  0.0001  462 GLU A CD  
3899  O OE1 . GLU A 462 ? 0.8952 0.8337 0.8866 0.0193  0.0705  0.0002  462 GLU A OE1 
3900  O OE2 . GLU A 462 ? 0.9262 0.8998 0.9499 0.0215  0.0939  -0.0002 462 GLU A OE2 
3901  N N   . VAL A 463 ? 0.3749 0.3332 0.3654 0.0003  0.0228  0.0150  463 VAL A N   
3902  C CA  . VAL A 463 ? 0.3575 0.3119 0.3466 -0.0032 0.0095  0.0171  463 VAL A CA  
3903  C C   . VAL A 463 ? 0.3514 0.3251 0.3476 -0.0078 0.0011  0.0219  463 VAL A C   
3904  O O   . VAL A 463 ? 0.2920 0.2619 0.2803 -0.0119 -0.0081 0.0207  463 VAL A O   
3905  C CB  . VAL A 463 ? 0.3949 0.3479 0.3993 0.0011  0.0085  0.0210  463 VAL A CB  
3906  C CG1 . VAL A 463 ? 0.3928 0.3438 0.3982 -0.0052 -0.0030 0.0237  463 VAL A CG1 
3907  C CG2 . VAL A 463 ? 0.3940 0.3231 0.3883 0.0068  0.0171  0.0146  463 VAL A CG2 
3908  N N   . PHE A 464 ? 0.3641 0.3591 0.3764 -0.0068 0.0036  0.0268  464 PHE A N   
3909  C CA  . PHE A 464 ? 0.2904 0.2998 0.3051 -0.0108 -0.0031 0.0298  464 PHE A CA  
3910  C C   . PHE A 464 ? 0.3726 0.3716 0.3674 -0.0144 -0.0040 0.0253  464 PHE A C   
3911  O O   . PHE A 464 ? 0.2966 0.2975 0.2871 -0.0163 -0.0118 0.0254  464 PHE A O   
3912  C CB  . PHE A 464 ? 0.2088 0.2395 0.2404 -0.0101 -0.0013 0.0343  464 PHE A CB  
3913  C CG  . PHE A 464 ? 0.2452 0.2857 0.2933 -0.0056 -0.0044 0.0409  464 PHE A CG  
3914  C CD1 . PHE A 464 ? 0.2943 0.3398 0.3428 -0.0075 -0.0116 0.0460  464 PHE A CD1 
3915  C CD2 . PHE A 464 ? 0.2540 0.2962 0.3153 0.0012  0.0005  0.0422  464 PHE A CD2 
3916  C CE1 . PHE A 464 ? 0.3420 0.3914 0.3997 -0.0038 -0.0143 0.0535  464 PHE A CE1 
3917  C CE2 . PHE A 464 ? 0.3155 0.3621 0.3887 0.0069  -0.0039 0.0494  464 PHE A CE2 
3918  C CZ  . PHE A 464 ? 0.2797 0.3281 0.3488 0.0037  -0.0116 0.0556  464 PHE A CZ  
3919  N N   . ASP A 465 ? 0.3854 0.3724 0.3674 -0.0148 0.0047  0.0214  465 ASP A N   
3920  C CA  . ASP A 465 ? 0.3303 0.3009 0.2873 -0.0180 0.0039  0.0183  465 ASP A CA  
3921  C C   . ASP A 465 ? 0.3776 0.3297 0.3162 -0.0170 -0.0062 0.0149  465 ASP A C   
3922  O O   . ASP A 465 ? 0.3706 0.3173 0.2976 -0.0175 -0.0150 0.0144  465 ASP A O   
3923  C CB  . ASP A 465 ? 0.3566 0.3166 0.3016 -0.0198 0.0182  0.0156  465 ASP A CB  
3924  C CG  . ASP A 465 ? 0.4035 0.3385 0.3148 -0.0232 0.0180  0.0134  465 ASP A CG  
3925  O OD1 . ASP A 465 ? 0.4057 0.3426 0.3136 -0.0271 0.0164  0.0155  465 ASP A OD1 
3926  O OD2 . ASP A 465 ? 0.4647 0.3752 0.3499 -0.0219 0.0185  0.0094  465 ASP A OD2 
3927  N N   . LYS A 466 ? 0.3839 0.3263 0.3212 -0.0153 -0.0063 0.0121  466 LYS A N   
3928  C CA  . LYS A 466 ? 0.3936 0.3205 0.3166 -0.0160 -0.0183 0.0080  466 LYS A CA  
3929  C C   . LYS A 466 ? 0.3777 0.3229 0.3200 -0.0171 -0.0303 0.0108  466 LYS A C   
3930  O O   . LYS A 466 ? 0.3643 0.3054 0.2988 -0.0172 -0.0421 0.0084  466 LYS A O   
3931  C CB  . LYS A 466 ? 0.3910 0.3029 0.3101 -0.0154 -0.0156 0.0038  466 LYS A CB  
3932  C CG  . LYS A 466 ? 0.4973 0.3979 0.4099 -0.0184 -0.0301 -0.0005 466 LYS A CG  
3933  C CD  . LYS A 466 ? 0.5084 0.3818 0.4022 -0.0184 -0.0268 -0.0075 466 LYS A CD  
3934  C CE  . LYS A 466 ? 0.5845 0.4540 0.4874 -0.0235 -0.0390 -0.0102 466 LYS A CE  
3935  N NZ  . LYS A 466 ? 0.6674 0.5214 0.5496 -0.0278 -0.0558 -0.0171 466 LYS A NZ  
3936  N N   . LEU A 467 ? 0.3000 0.2657 0.2675 -0.0173 -0.0273 0.0159  467 LEU A N   
3937  C CA  . LEU A 467 ? 0.3282 0.3120 0.3134 -0.0189 -0.0348 0.0187  467 LEU A CA  
3938  C C   . LEU A 467 ? 0.3463 0.3374 0.3278 -0.0171 -0.0383 0.0189  467 LEU A C   
3939  O O   . LEU A 467 ? 0.3338 0.3288 0.3182 -0.0162 -0.0476 0.0168  467 LEU A O   
3940  C CB  . LEU A 467 ? 0.2820 0.2813 0.2872 -0.0194 -0.0293 0.0252  467 LEU A CB  
3941  C CG  . LEU A 467 ? 0.2713 0.2603 0.2811 -0.0211 -0.0286 0.0254  467 LEU A CG  
3942  C CD1 . LEU A 467 ? 0.3030 0.3000 0.3265 -0.0195 -0.0228 0.0330  467 LEU A CD1 
3943  C CD2 . LEU A 467 ? 0.2411 0.2300 0.2568 -0.0268 -0.0376 0.0227  467 LEU A CD2 
3944  N N   . PHE A 468 ? 0.3284 0.3219 0.3057 -0.0163 -0.0314 0.0209  468 PHE A N   
3945  C CA  . PHE A 468 ? 0.3494 0.3449 0.3205 -0.0149 -0.0342 0.0207  468 PHE A CA  
3946  C C   . PHE A 468 ? 0.3870 0.3639 0.3378 -0.0122 -0.0425 0.0167  468 PHE A C   
3947  O O   . PHE A 468 ? 0.3625 0.3439 0.3166 -0.0084 -0.0511 0.0155  468 PHE A O   
3948  C CB  . PHE A 468 ? 0.3820 0.3780 0.3489 -0.0171 -0.0256 0.0224  468 PHE A CB  
3949  C CG  . PHE A 468 ? 0.3948 0.3842 0.3492 -0.0169 -0.0276 0.0214  468 PHE A CG  
3950  C CD1 . PHE A 468 ? 0.3698 0.3717 0.3327 -0.0152 -0.0306 0.0219  468 PHE A CD1 
3951  C CD2 . PHE A 468 ? 0.3914 0.3588 0.3223 -0.0185 -0.0250 0.0198  468 PHE A CD2 
3952  C CE1 . PHE A 468 ? 0.3472 0.3389 0.2966 -0.0142 -0.0321 0.0201  468 PHE A CE1 
3953  C CE2 . PHE A 468 ? 0.3358 0.2918 0.2525 -0.0185 -0.0268 0.0193  468 PHE A CE2 
3954  C CZ  . PHE A 468 ? 0.4159 0.3837 0.3426 -0.0159 -0.0308 0.0190  468 PHE A CZ  
3955  N N   . ARG A 469 ? 0.3732 0.3282 0.3019 -0.0132 -0.0403 0.0145  469 ARG A N   
3956  C CA  . ARG A 469 ? 0.4140 0.3466 0.3166 -0.0102 -0.0497 0.0117  469 ARG A CA  
3957  C C   . ARG A 469 ? 0.4335 0.3703 0.3442 -0.0078 -0.0646 0.0086  469 ARG A C   
3958  O O   . ARG A 469 ? 0.4639 0.3951 0.3668 -0.0027 -0.0771 0.0072  469 ARG A O   
3959  C CB  . ARG A 469 ? 0.4285 0.3341 0.3006 -0.0127 -0.0420 0.0102  469 ARG A CB  
3960  C CG  . ARG A 469 ? 0.4742 0.3776 0.3409 -0.0166 -0.0272 0.0129  469 ARG A CG  
3961  C CD  . ARG A 469 ? 0.4384 0.3208 0.2815 -0.0200 -0.0142 0.0113  469 ARG A CD  
3962  N NE  . ARG A 469 ? 0.3725 0.2543 0.2130 -0.0256 0.0005  0.0136  469 ARG A NE  
3963  C CZ  . ARG A 469 ? 0.4820 0.3423 0.2960 -0.0286 0.0022  0.0153  469 ARG A CZ  
3964  N NH1 . ARG A 469 ? 0.5010 0.3373 0.2870 -0.0241 -0.0112 0.0154  469 ARG A NH1 
3965  N NH2 . ARG A 469 ? 0.4864 0.3481 0.3020 -0.0363 0.0167  0.0171  469 ARG A NH2 
3966  N N   . SER A 470 ? 0.4305 0.3775 0.3588 -0.0114 -0.0642 0.0076  470 SER A N   
3967  C CA  . SER A 470 ? 0.4705 0.4250 0.4120 -0.0119 -0.0781 0.0042  470 SER A CA  
3968  C C   . SER A 470 ? 0.3991 0.3803 0.3683 -0.0089 -0.0830 0.0057  470 SER A C   
3969  O O   . SER A 470 ? 0.3577 0.3445 0.3340 -0.0056 -0.0971 0.0025  470 SER A O   
3970  C CB  . SER A 470 ? 0.5011 0.4580 0.4553 -0.0182 -0.0745 0.0033  470 SER A CB  
3971  O OG  . SER A 470 ? 0.6026 0.5325 0.5299 -0.0194 -0.0706 -0.0001 470 SER A OG  
3972  N N   . PHE A 471 ? 0.3746 0.3731 0.3599 -0.0096 -0.0718 0.0101  471 PHE A N   
3973  C CA  . PHE A 471 ? 0.2816 0.3031 0.2889 -0.0061 -0.0729 0.0108  471 PHE A CA  
3974  C C   . PHE A 471 ? 0.3020 0.3150 0.2957 0.0027  -0.0794 0.0090  471 PHE A C   
3975  O O   . PHE A 471 ? 0.3486 0.3746 0.3575 0.0088  -0.0877 0.0066  471 PHE A O   
3976  C CB  . PHE A 471 ? 0.2870 0.3226 0.3053 -0.0088 -0.0595 0.0157  471 PHE A CB  
3977  C CG  . PHE A 471 ? 0.3071 0.3503 0.3397 -0.0160 -0.0539 0.0190  471 PHE A CG  
3978  C CD1 . PHE A 471 ? 0.3292 0.3820 0.3804 -0.0205 -0.0587 0.0176  471 PHE A CD1 
3979  C CD2 . PHE A 471 ? 0.3546 0.3947 0.3828 -0.0182 -0.0446 0.0237  471 PHE A CD2 
3980  C CE1 . PHE A 471 ? 0.3075 0.3620 0.3687 -0.0278 -0.0532 0.0212  471 PHE A CE1 
3981  C CE2 . PHE A 471 ? 0.2846 0.3271 0.3232 -0.0231 -0.0403 0.0276  471 PHE A CE2 
3982  C CZ  . PHE A 471 ? 0.2746 0.3220 0.3277 -0.0282 -0.0440 0.0266  471 PHE A CZ  
3983  N N   . VAL A 472 ? 0.3283 0.3189 0.2943 0.0035  -0.0750 0.0103  472 VAL A N   
3984  C CA  . VAL A 472 ? 0.4216 0.3952 0.3677 0.0111  -0.0810 0.0095  472 VAL A CA  
3985  C C   . VAL A 472 ? 0.4309 0.3939 0.3685 0.0172  -0.0984 0.0064  472 VAL A C   
3986  O O   . VAL A 472 ? 0.3973 0.3595 0.3357 0.0271  -0.1083 0.0052  472 VAL A O   
3987  C CB  . VAL A 472 ? 0.4676 0.4159 0.3838 0.0072  -0.0719 0.0117  472 VAL A CB  
3988  C CG1 . VAL A 472 ? 0.5201 0.4406 0.4072 0.0137  -0.0798 0.0116  472 VAL A CG1 
3989  C CG2 . VAL A 472 ? 0.4825 0.4430 0.4086 0.0029  -0.0591 0.0140  472 VAL A CG2 
3990  N N   . ARG A 473 ? 0.4172 0.3702 0.3452 0.0123  -0.1034 0.0047  473 ARG A N   
3991  C CA  . ARG A 473 ? 0.4435 0.3842 0.3594 0.0174  -0.1228 0.0014  473 ARG A CA  
3992  C C   . ARG A 473 ? 0.4270 0.3996 0.3824 0.0201  -0.1347 -0.0019 473 ARG A C   
3993  O O   . ARG A 473 ? 0.3793 0.3544 0.3388 0.0298  -0.1511 -0.0039 473 ARG A O   
3994  C CB  . ARG A 473 ? 0.5157 0.4334 0.4057 0.0105  -0.1245 -0.0008 473 ARG A CB  
3995  C CG  . ARG A 473 ? 0.5926 0.5003 0.4721 0.0138  -0.1478 -0.0054 473 ARG A CG  
3996  C CD  . ARG A 473 ? 0.7329 0.6041 0.5683 0.0092  -0.1489 -0.0077 473 ARG A CD  
3997  N NE  . ARG A 473 ? 0.8257 0.7009 0.6703 -0.0007 -0.1405 -0.0111 473 ARG A NE  
3998  C CZ  . ARG A 473 ? 0.9012 0.7763 0.7502 -0.0055 -0.1543 -0.0172 473 ARG A CZ  
3999  N NH1 . ARG A 473 ? 0.9208 0.7965 0.7693 -0.0016 -0.1789 -0.0208 473 ARG A NH1 
4000  N NH2 . ARG A 473 ? 0.8929 0.7665 0.7476 -0.0141 -0.1445 -0.0199 473 ARG A NH2 
4001  N N   . ARG A 474 ? 0.4232 0.4209 0.4093 0.0118  -0.1262 -0.0021 474 ARG A N   
4002  C CA  . ARG A 474 ? 0.4198 0.4509 0.4475 0.0115  -0.1333 -0.0049 474 ARG A CA  
4003  C C   . ARG A 474 ? 0.4060 0.4576 0.4547 0.0224  -0.1324 -0.0047 474 ARG A C   
4004  O O   . ARG A 474 ? 0.4141 0.4879 0.4910 0.0282  -0.1446 -0.0084 474 ARG A O   
4005  C CB  . ARG A 474 ? 0.4076 0.4554 0.4577 -0.0006 -0.1202 -0.0032 474 ARG A CB  
4006  C CG  . ARG A 474 ? 0.4468 0.5247 0.5372 -0.0061 -0.1263 -0.0062 474 ARG A CG  
4007  C CD  . ARG A 474 ? 0.5790 0.6518 0.6687 -0.0066 -0.1488 -0.0124 474 ARG A CD  
4008  N NE  . ARG A 474 ? 0.6954 0.7817 0.8103 -0.0204 -0.1517 -0.0152 474 ARG A NE  
4009  C CZ  . ARG A 474 ? 0.8003 0.9224 0.9603 -0.0260 -0.1492 -0.0160 474 ARG A CZ  
4010  N NH1 . ARG A 474 ? 0.8211 0.9705 1.0062 -0.0170 -0.1432 -0.0147 474 ARG A NH1 
4011  N NH2 . ARG A 474 ? 0.8330 0.9621 1.0123 -0.0410 -0.1515 -0.0184 474 ARG A NH2 
4012  N N   . ALA A 475 ? 0.3968 0.4411 0.4327 0.0258  -0.1185 -0.0014 475 ALA A N   
4013  C CA  . ALA A 475 ? 0.3612 0.4203 0.4125 0.0365  -0.1154 -0.0023 475 ALA A CA  
4014  C C   . ALA A 475 ? 0.4093 0.4585 0.4539 0.0515  -0.1329 -0.0050 475 ALA A C   
4015  O O   . ALA A 475 ? 0.4269 0.4943 0.4941 0.0627  -0.1337 -0.0076 475 ALA A O   
4016  C CB  . ALA A 475 ? 0.3763 0.4223 0.4076 0.0355  -0.0992 0.0010  475 ALA A CB  
4017  N N   . GLN A 476 ? 0.4338 0.4531 0.4463 0.0530  -0.1469 -0.0045 476 GLN A N   
4018  C CA  . GLN A 476 ? 0.4870 0.4899 0.4854 0.0682  -0.1654 -0.0055 476 GLN A CA  
4019  C C   . GLN A 476 ? 0.5135 0.5308 0.5308 0.0716  -0.1888 -0.0095 476 GLN A C   
4020  O O   . GLN A 476 ? 0.5298 0.5311 0.5324 0.0846  -0.2087 -0.0099 476 GLN A O   
4021  C CB  . GLN A 476 ? 0.4997 0.4543 0.4428 0.0682  -0.1657 -0.0013 476 GLN A CB  
4022  C CG  . GLN A 476 ? 0.4957 0.4380 0.4224 0.0607  -0.1429 0.0021  476 GLN A CG  
4023  C CD  . GLN A 476 ? 0.5323 0.4300 0.4084 0.0568  -0.1398 0.0063  476 GLN A CD  
4024  O OE1 . GLN A 476 ? 0.6258 0.4939 0.4736 0.0662  -0.1481 0.0083  476 GLN A OE1 
4025  N NE2 . GLN A 476 ? 0.5205 0.4127 0.3852 0.0431  -0.1264 0.0078  476 GLN A NE2 
4026  N N   . GLU A 477 ? 0.5258 0.5717 0.5752 0.0600  -0.1882 -0.0125 477 GLU A N   
4027  C CA  . GLU A 477 ? 0.6124 0.6710 0.6793 0.0598  -0.2119 -0.0172 477 GLU A CA  
4028  C C   . GLU A 477 ? 0.6074 0.7168 0.7358 0.0601  -0.2119 -0.0214 477 GLU A C   
4029  O O   . GLU A 477 ? 0.5641 0.7000 0.7225 0.0584  -0.1940 -0.0210 477 GLU A O   
4030  C CB  . GLU A 477 ? 0.6868 0.7287 0.7333 0.0433  -0.2129 -0.0182 477 GLU A CB  
4031  C CG  . GLU A 477 ? 0.7752 0.7678 0.7608 0.0421  -0.2090 -0.0146 477 GLU A CG  
4032  C CD  . GLU A 477 ? 0.8501 0.8243 0.8142 0.0284  -0.2107 -0.0172 477 GLU A CD  
4033  O OE1 . GLU A 477 ? 0.8570 0.7908 0.7706 0.0287  -0.2140 -0.0163 477 GLU A OE1 
4034  O OE2 . GLU A 477 ? 0.8610 0.8586 0.8565 0.0170  -0.2076 -0.0203 477 GLU A OE2 
4035  N N   . LYS B 2   ? 0.9034 0.6393 0.2839 0.1655  0.0063  -0.0330 2   LYS B N   
4036  C CA  . LYS B 2   ? 0.8997 0.6604 0.3123 0.1628  0.0080  -0.0388 2   LYS B CA  
4037  C C   . LYS B 2   ? 0.8862 0.6644 0.3240 0.1569  0.0156  -0.0336 2   LYS B C   
4038  O O   . LYS B 2   ? 0.9398 0.7176 0.3753 0.1523  0.0341  -0.0282 2   LYS B O   
4039  C CB  . LYS B 2   ? 0.9459 0.7090 0.3550 0.1619  0.0241  -0.0444 2   LYS B CB  
4040  C CG  . LYS B 2   ? 0.9067 0.6921 0.3458 0.1607  0.0227  -0.0523 2   LYS B CG  
4041  C CD  . LYS B 2   ? 0.8952 0.6928 0.3472 0.1556  0.0458  -0.0531 2   LYS B CD  
4042  C CE  . LYS B 2   ? 0.9818 0.7719 0.4190 0.1577  0.0563  -0.0593 2   LYS B CE  
4043  N NZ  . LYS B 2   ? 0.9466 0.7508 0.4016 0.1529  0.0785  -0.0611 2   LYS B NZ  
4044  N N   . LYS B 3   ? 0.8112 0.6045 0.2737 0.1569  0.0015  -0.0351 3   LYS B N   
4045  C CA  . LYS B 3   ? 0.8266 0.6349 0.3114 0.1520  0.0066  -0.0301 3   LYS B CA  
4046  C C   . LYS B 3   ? 0.8164 0.6479 0.3310 0.1492  0.0101  -0.0358 3   LYS B C   
4047  O O   . LYS B 3   ? 0.8348 0.6722 0.3565 0.1516  0.0027  -0.0438 3   LYS B O   
4048  C CB  . LYS B 3   ? 0.8484 0.6560 0.3392 0.1540  -0.0112 -0.0267 3   LYS B CB  
4049  C CG  . LYS B 3   ? 0.9461 0.7368 0.4173 0.1539  -0.0088 -0.0180 3   LYS B CG  
4050  C CD  . LYS B 3   ? 1.0287 0.8000 0.4784 0.1601  -0.0252 -0.0186 3   LYS B CD  
4051  C CE  . LYS B 3   ? 1.0722 0.8315 0.5125 0.1606  -0.0294 -0.0108 3   LYS B CE  
4052  N NZ  . LYS B 3   ? 1.0881 0.8362 0.5106 0.1568  -0.0102 -0.0034 3   LYS B NZ  
4053  N N   . LEU B 4   ? 0.7310 0.5746 0.2624 0.1441  0.0218  -0.0317 4   LEU B N   
4054  C CA  . LEU B 4   ? 0.6879 0.5539 0.2498 0.1415  0.0221  -0.0358 4   LEU B CA  
4055  C C   . LEU B 4   ? 0.6672 0.5411 0.2438 0.1416  0.0071  -0.0331 4   LEU B C   
4056  O O   . LEU B 4   ? 0.7121 0.5788 0.2818 0.1408  0.0072  -0.0256 4   LEU B O   
4057  C CB  . LEU B 4   ? 0.6477 0.5226 0.2214 0.1360  0.0435  -0.0333 4   LEU B CB  
4058  C CG  . LEU B 4   ? 0.6093 0.5071 0.2165 0.1328  0.0451  -0.0368 4   LEU B CG  
4059  C CD1 . LEU B 4   ? 0.6431 0.5474 0.2609 0.1291  0.0653  -0.0390 4   LEU B CD1 
4060  C CD2 . LEU B 4   ? 0.5908 0.4978 0.2196 0.1273  0.0419  -0.0298 4   LEU B CD2 
4061  N N   . PHE B 5   ? 0.6477 0.5357 0.2445 0.1427  -0.0059 -0.0392 5   PHE B N   
4062  C CA  . PHE B 5   ? 0.6227 0.5205 0.2378 0.1421  -0.0198 -0.0374 5   PHE B CA  
4063  C C   . PHE B 5   ? 0.5770 0.4960 0.2293 0.1337  -0.0117 -0.0357 5   PHE B C   
4064  O O   . PHE B 5   ? 0.5944 0.5264 0.2670 0.1310  -0.0100 -0.0412 5   PHE B O   
4065  C CB  . PHE B 5   ? 0.6438 0.5448 0.2665 0.1458  -0.0398 -0.0440 5   PHE B CB  
4066  C CG  . PHE B 5   ? 0.6876 0.5696 0.2878 0.1508  -0.0498 -0.0443 5   PHE B CG  
4067  C CD1 . PHE B 5   ? 0.6846 0.5529 0.2697 0.1524  -0.0529 -0.0378 5   PHE B CD1 
4068  C CD2 . PHE B 5   ? 0.7124 0.5896 0.3068 0.1539  -0.0565 -0.0515 5   PHE B CD2 
4069  C CE1 . PHE B 5   ? 0.7263 0.5764 0.2908 0.1573  -0.0628 -0.0384 5   PHE B CE1 
4070  C CE2 . PHE B 5   ? 0.7059 0.5649 0.2794 0.1587  -0.0661 -0.0520 5   PHE B CE2 
4071  C CZ  . PHE B 5   ? 0.7713 0.6166 0.3295 0.1604  -0.0694 -0.0456 5   PHE B CZ  
4072  N N   . LEU B 6   ? 0.5251 0.4461 0.1849 0.1300  -0.0075 -0.0284 6   LEU B N   
4073  C CA  . LEU B 6   ? 0.5456 0.4834 0.2367 0.1222  0.0004  -0.0261 6   LEU B CA  
4074  C C   . LEU B 6   ? 0.5494 0.4977 0.2627 0.1204  -0.0124 -0.0248 6   LEU B C   
4075  O O   . LEU B 6   ? 0.5610 0.5014 0.2642 0.1237  -0.0205 -0.0212 6   LEU B O   
4076  C CB  . LEU B 6   ? 0.5906 0.5218 0.2738 0.1188  0.0164  -0.0188 6   LEU B CB  
4077  C CG  . LEU B 6   ? 0.5636 0.5091 0.2761 0.1108  0.0254  -0.0161 6   LEU B CG  
4078  C CD1 . LEU B 6   ? 0.5525 0.5108 0.2848 0.1074  0.0317  -0.0220 6   LEU B CD1 
4079  C CD2 . LEU B 6   ? 0.5551 0.4908 0.2560 0.1083  0.0393  -0.0086 6   LEU B CD2 
4080  N N   . VAL B 7   ? 0.5341 0.4994 0.2772 0.1154  -0.0139 -0.0277 7   VAL B N   
4081  C CA  . VAL B 7   ? 0.5144 0.4903 0.2794 0.1135  -0.0249 -0.0273 7   VAL B CA  
4082  C C   . VAL B 7   ? 0.4899 0.4780 0.2793 0.1060  -0.0169 -0.0249 7   VAL B C   
4083  O O   . VAL B 7   ? 0.4948 0.4922 0.2997 0.1023  -0.0136 -0.0286 7   VAL B O   
4084  C CB  . VAL B 7   ? 0.4837 0.4665 0.2592 0.1153  -0.0381 -0.0340 7   VAL B CB  
4085  C CG1 . VAL B 7   ? 0.4829 0.4756 0.2802 0.1132  -0.0479 -0.0330 7   VAL B CG1 
4086  C CG2 . VAL B 7   ? 0.5296 0.4986 0.2792 0.1230  -0.0468 -0.0374 7   VAL B CG2 
4087  N N   . PHE B 8   ? 0.4161 0.4029 0.2080 0.1041  -0.0143 -0.0190 8   PHE B N   
4088  C CA  . PHE B 8   ? 0.3612 0.3582 0.1757 0.0975  -0.0099 -0.0168 8   PHE B CA  
4089  C C   . PHE B 8   ? 0.3532 0.3596 0.1860 0.0965  -0.0206 -0.0183 8   PHE B C   
4090  O O   . PHE B 8   ? 0.3864 0.3899 0.2153 0.1002  -0.0287 -0.0171 8   PHE B O   
4091  C CB  . PHE B 8   ? 0.4755 0.4656 0.2839 0.0959  -0.0021 -0.0100 8   PHE B CB  
4092  C CG  . PHE B 8   ? 0.4958 0.4782 0.2914 0.0949  0.0111  -0.0077 8   PHE B CG  
4093  C CD1 . PHE B 8   ? 0.4150 0.4042 0.2259 0.0890  0.0208  -0.0081 8   PHE B CD1 
4094  C CD2 . PHE B 8   ? 0.5348 0.5023 0.3030 0.0997  0.0138  -0.0052 8   PHE B CD2 
4095  C CE1 . PHE B 8   ? 0.4762 0.4592 0.2781 0.0877  0.0341  -0.0060 8   PHE B CE1 
4096  C CE2 . PHE B 8   ? 0.5527 0.5123 0.3085 0.0984  0.0277  -0.0027 8   PHE B CE2 
4097  C CZ  . PHE B 8   ? 0.5207 0.4891 0.2949 0.0922  0.0384  -0.0032 8   PHE B CZ  
4098  N N   . TRP B 9   ? 0.3563 0.3737 0.2095 0.0913  -0.0202 -0.0208 9   TRP B N   
4099  C CA  . TRP B 9   ? 0.3737 0.3998 0.2450 0.0890  -0.0279 -0.0217 9   TRP B CA  
4100  C C   . TRP B 9   ? 0.3054 0.3366 0.1912 0.0825  -0.0214 -0.0196 9   TRP B C   
4101  O O   . TRP B 9   ? 0.3181 0.3539 0.2131 0.0788  -0.0188 -0.0221 9   TRP B O   
4102  C CB  . TRP B 9   ? 0.3288 0.3609 0.2078 0.0896  -0.0362 -0.0275 9   TRP B CB  
4103  C CG  . TRP B 9   ? 0.3171 0.3564 0.2117 0.0886  -0.0452 -0.0286 9   TRP B CG  
4104  C CD1 . TRP B 9   ? 0.3414 0.3837 0.2455 0.0867  -0.0453 -0.0253 9   TRP B CD1 
4105  C CD2 . TRP B 9   ? 0.3545 0.3987 0.2575 0.0892  -0.0544 -0.0334 9   TRP B CD2 
4106  N NE1 . TRP B 9   ? 0.3294 0.3787 0.2480 0.0860  -0.0531 -0.0277 9   TRP B NE1 
4107  C CE2 . TRP B 9   ? 0.3378 0.3883 0.2563 0.0872  -0.0592 -0.0325 9   TRP B CE2 
4108  C CE3 . TRP B 9   ? 0.3912 0.4345 0.2902 0.0912  -0.0590 -0.0387 9   TRP B CE3 
4109  C CZ2 . TRP B 9   ? 0.3733 0.4297 0.3047 0.0866  -0.0681 -0.0362 9   TRP B CZ2 
4110  C CZ3 . TRP B 9   ? 0.4209 0.4694 0.3318 0.0910  -0.0690 -0.0426 9   TRP B CZ3 
4111  C CH2 . TRP B 9   ? 0.4374 0.4925 0.3650 0.0883  -0.0734 -0.0411 9   TRP B CH2 
4112  N N   . TRP B 10  ? 0.3592 0.3884 0.2462 0.0816  -0.0194 -0.0152 10  TRP B N   
4113  C CA  . TRP B 10  ? 0.3042 0.3354 0.2017 0.0760  -0.0140 -0.0130 10  TRP B CA  
4114  C C   . TRP B 10  ? 0.2977 0.3359 0.2101 0.0732  -0.0193 -0.0143 10  TRP B C   
4115  O O   . TRP B 10  ? 0.3357 0.3749 0.2498 0.0755  -0.0239 -0.0137 10  TRP B O   
4116  C CB  . TRP B 10  ? 0.3151 0.3388 0.2045 0.0767  -0.0089 -0.0077 10  TRP B CB  
4117  C CG  . TRP B 10  ? 0.3909 0.4058 0.2644 0.0788  -0.0024 -0.0051 10  TRP B CG  
4118  C CD1 . TRP B 10  ? 0.3559 0.3620 0.2122 0.0842  -0.0037 -0.0027 10  TRP B CD1 
4119  C CD2 . TRP B 10  ? 0.3868 0.3999 0.2599 0.0755  0.0068  -0.0044 10  TRP B CD2 
4120  N NE1 . TRP B 10  ? 0.4108 0.4087 0.2538 0.0842  0.0050  -0.0001 10  TRP B NE1 
4121  C CE2 . TRP B 10  ? 0.4206 0.4236 0.2752 0.0788  0.0121  -0.0012 10  TRP B CE2 
4122  C CE3 . TRP B 10  ? 0.3284 0.3472 0.2159 0.0701  0.0107  -0.0063 10  TRP B CE3 
4123  C CZ2 . TRP B 10  ? 0.4368 0.4359 0.2875 0.0764  0.0228  0.0003  10  TRP B CZ2 
4124  C CZ3 . TRP B 10  ? 0.3066 0.3225 0.1926 0.0681  0.0202  -0.0053 10  TRP B CZ3 
4125  C CH2 . TRP B 10  ? 0.3731 0.3797 0.2413 0.0711  0.0269  -0.0020 10  TRP B CH2 
4126  N N   . HIS B 11  ? 0.2913 0.3336 0.2144 0.0682  -0.0186 -0.0162 11  HIS B N   
4127  C CA  . HIS B 11  ? 0.3374 0.3849 0.2724 0.0651  -0.0232 -0.0175 11  HIS B CA  
4128  C C   . HIS B 11  ? 0.3713 0.4161 0.3097 0.0613  -0.0192 -0.0145 11  HIS B C   
4129  O O   . HIS B 11  ? 0.3853 0.4268 0.3235 0.0583  -0.0148 -0.0134 11  HIS B O   
4130  C CB  . HIS B 11  ? 0.3007 0.3521 0.2434 0.0623  -0.0261 -0.0214 11  HIS B CB  
4131  C CG  . HIS B 11  ? 0.2942 0.3479 0.2474 0.0574  -0.0288 -0.0218 11  HIS B CG  
4132  N ND1 . HIS B 11  ? 0.2631 0.3197 0.2214 0.0573  -0.0324 -0.0217 11  HIS B ND1 
4133  C CD2 . HIS B 11  ? 0.2950 0.3474 0.2538 0.0525  -0.0283 -0.0222 11  HIS B CD2 
4134  C CE1 . HIS B 11  ? 0.2512 0.3076 0.2161 0.0523  -0.0330 -0.0216 11  HIS B CE1 
4135  N NE2 . HIS B 11  ? 0.2900 0.3432 0.2544 0.0495  -0.0313 -0.0219 11  HIS B NE2 
4136  N N   . MET B 12  ? 0.3089 0.3548 0.2509 0.0615  -0.0207 -0.0134 12  MET B N   
4137  C CA  . MET B 12  ? 0.2846 0.3264 0.2272 0.0590  -0.0167 -0.0108 12  MET B CA  
4138  C C   . MET B 12  ? 0.3239 0.3682 0.2746 0.0551  -0.0185 -0.0120 12  MET B C   
4139  O O   . MET B 12  ? 0.3560 0.4055 0.3128 0.0563  -0.0216 -0.0132 12  MET B O   
4140  C CB  . MET B 12  ? 0.3319 0.3713 0.2701 0.0633  -0.0153 -0.0084 12  MET B CB  
4141  C CG  . MET B 12  ? 0.3469 0.3825 0.2744 0.0680  -0.0148 -0.0069 12  MET B CG  
4142  S SD  . MET B 12  ? 0.4272 0.4554 0.3482 0.0648  -0.0076 -0.0043 12  MET B SD  
4143  C CE  . MET B 12  ? 0.5412 0.5660 0.4502 0.0684  -0.0054 -0.0036 12  MET B CE  
4144  N N   . HIS B 13  ? 0.2707 0.3104 0.2216 0.0504  -0.0166 -0.0115 13  HIS B N   
4145  C CA  . HIS B 13  ? 0.2570 0.2967 0.2125 0.0464  -0.0181 -0.0123 13  HIS B CA  
4146  C C   . HIS B 13  ? 0.2825 0.3133 0.2332 0.0425  -0.0153 -0.0109 13  HIS B C   
4147  O O   . HIS B 13  ? 0.2835 0.3100 0.2316 0.0413  -0.0149 -0.0106 13  HIS B O   
4148  C CB  . HIS B 13  ? 0.2860 0.3295 0.2470 0.0442  -0.0233 -0.0151 13  HIS B CB  
4149  C CG  . HIS B 13  ? 0.3037 0.3438 0.2668 0.0391  -0.0249 -0.0153 13  HIS B CG  
4150  N ND1 . HIS B 13  ? 0.2836 0.3239 0.2486 0.0378  -0.0231 -0.0143 13  HIS B ND1 
4151  C CD2 . HIS B 13  ? 0.2768 0.3123 0.2398 0.0351  -0.0280 -0.0162 13  HIS B CD2 
4152  C CE1 . HIS B 13  ? 0.2779 0.3126 0.2416 0.0329  -0.0244 -0.0143 13  HIS B CE1 
4153  N NE2 . HIS B 13  ? 0.2774 0.3087 0.2396 0.0313  -0.0282 -0.0154 13  HIS B NE2 
4154  N N   . GLN B 14  ? 0.2555 0.2831 0.2051 0.0405  -0.0133 -0.0102 14  GLN B N   
4155  C CA  . GLN B 14  ? 0.2970 0.3143 0.2402 0.0362  -0.0125 -0.0096 14  GLN B CA  
4156  C C   . GLN B 14  ? 0.3087 0.3249 0.2527 0.0328  -0.0129 -0.0099 14  GLN B C   
4157  O O   . GLN B 14  ? 0.3277 0.3499 0.2769 0.0342  -0.0104 -0.0098 14  GLN B O   
4158  C CB  . GLN B 14  ? 0.2583 0.2682 0.1941 0.0374  -0.0074 -0.0078 14  GLN B CB  
4159  C CG  . GLN B 14  ? 0.2984 0.3063 0.2319 0.0398  -0.0062 -0.0067 14  GLN B CG  
4160  C CD  . GLN B 14  ? 0.3351 0.3384 0.2684 0.0367  -0.0094 -0.0072 14  GLN B CD  
4161  O OE1 . GLN B 14  ? 0.3451 0.3431 0.2772 0.0327  -0.0128 -0.0082 14  GLN B OE1 
4162  N NE2 . GLN B 14  ? 0.4163 0.4213 0.3513 0.0385  -0.0083 -0.0064 14  GLN B NE2 
4163  N N   . PRO B 15  ? 0.3282 0.3363 0.2675 0.0282  -0.0161 -0.0102 15  PRO B N   
4164  C CA  . PRO B 15  ? 0.3982 0.4015 0.3343 0.0246  -0.0150 -0.0096 15  PRO B CA  
4165  C C   . PRO B 15  ? 0.3667 0.3625 0.2939 0.0246  -0.0077 -0.0081 15  PRO B C   
4166  O O   . PRO B 15  ? 0.3671 0.3598 0.2900 0.0271  -0.0049 -0.0077 15  PRO B O   
4167  C CB  . PRO B 15  ? 0.3717 0.3655 0.3026 0.0202  -0.0215 -0.0101 15  PRO B CB  
4168  C CG  . PRO B 15  ? 0.2884 0.2789 0.2178 0.0213  -0.0240 -0.0107 15  PRO B CG  
4169  C CD  . PRO B 15  ? 0.2572 0.2596 0.1947 0.0262  -0.0211 -0.0110 15  PRO B CD  
4170  N N   . LEU B 16  ? 0.3609 0.3535 0.2856 0.0218  -0.0040 -0.0073 16  LEU B N   
4171  C CA  . LEU B 16  ? 0.3426 0.3283 0.2591 0.0219  0.0045  -0.0063 16  LEU B CA  
4172  C C   . LEU B 16  ? 0.4111 0.3788 0.3091 0.0194  0.0039  -0.0058 16  LEU B C   
4173  O O   . LEU B 16  ? 0.4242 0.3808 0.3121 0.0149  0.0012  -0.0052 16  LEU B O   
4174  C CB  . LEU B 16  ? 0.3363 0.3246 0.2571 0.0194  0.0100  -0.0056 16  LEU B CB  
4175  C CG  . LEU B 16  ? 0.3841 0.3679 0.2998 0.0203  0.0210  -0.0051 16  LEU B CG  
4176  C CD1 . LEU B 16  ? 0.3622 0.3560 0.2877 0.0266  0.0241  -0.0061 16  LEU B CD1 
4177  C CD2 . LEU B 16  ? 0.4430 0.4295 0.3646 0.0168  0.0272  -0.0041 16  LEU B CD2 
4178  N N   . TYR B 17  ? 0.4278 0.3911 0.3204 0.0223  0.0057  -0.0061 17  TYR B N   
4179  C CA  . TYR B 17  ? 0.3813 0.3267 0.2565 0.0204  0.0042  -0.0061 17  TYR B CA  
4180  C C   . TYR B 17  ? 0.4120 0.3460 0.2731 0.0199  0.0130  -0.0057 17  TYR B C   
4181  O O   . TYR B 17  ? 0.4107 0.3272 0.2539 0.0183  0.0118  -0.0059 17  TYR B O   
4182  C CB  . TYR B 17  ? 0.3540 0.2984 0.2299 0.0233  0.0018  -0.0067 17  TYR B CB  
4183  C CG  . TYR B 17  ? 0.3668 0.3203 0.2547 0.0236  -0.0054 -0.0071 17  TYR B CG  
4184  C CD1 . TYR B 17  ? 0.3792 0.3281 0.2667 0.0200  -0.0136 -0.0077 17  TYR B CD1 
4185  C CD2 . TYR B 17  ? 0.3979 0.3636 0.2970 0.0276  -0.0038 -0.0069 17  TYR B CD2 
4186  C CE1 . TYR B 17  ? 0.3816 0.3394 0.2815 0.0206  -0.0188 -0.0086 17  TYR B CE1 
4187  C CE2 . TYR B 17  ? 0.3896 0.3627 0.2981 0.0280  -0.0087 -0.0073 17  TYR B CE2 
4188  C CZ  . TYR B 17  ? 0.3654 0.3353 0.2752 0.0244  -0.0156 -0.0084 17  TYR B CZ  
4189  O OH  . TYR B 17  ? 0.3185 0.2962 0.2388 0.0250  -0.0192 -0.0092 17  TYR B OH  
4190  N N   . ARG B 18  ? 0.4095 0.3525 0.2784 0.0213  0.0216  -0.0054 18  ARG B N   
4191  C CA  . ARG B 18  ? 0.4784 0.4129 0.3368 0.0214  0.0323  -0.0054 18  ARG B CA  
4192  C C   . ARG B 18  ? 0.4778 0.3999 0.3225 0.0158  0.0340  -0.0041 18  ARG B C   
4193  O O   . ARG B 18  ? 0.4423 0.3728 0.2972 0.0132  0.0351  -0.0030 18  ARG B O   
4194  C CB  . ARG B 18  ? 0.4615 0.4121 0.3377 0.0252  0.0406  -0.0060 18  ARG B CB  
4195  C CG  . ARG B 18  ? 0.4908 0.4347 0.3598 0.0265  0.0530  -0.0067 18  ARG B CG  
4196  C CD  . ARG B 18  ? 0.5497 0.5114 0.4410 0.0295  0.0602  -0.0073 18  ARG B CD  
4197  N NE  . ARG B 18  ? 0.5710 0.5283 0.4590 0.0315  0.0732  -0.0086 18  ARG B NE  
4198  C CZ  . ARG B 18  ? 0.6462 0.5971 0.5276 0.0278  0.0835  -0.0080 18  ARG B CZ  
4199  N NH1 . ARG B 18  ? 0.6501 0.5974 0.5271 0.0217  0.0815  -0.0058 18  ARG B NH1 
4200  N NH2 . ARG B 18  ? 0.6059 0.5534 0.4852 0.0304  0.0963  -0.0097 18  ARG B NH2 
4201  N N   . GLU B 19  ? 0.5154 0.4164 0.3364 0.0139  0.0335  -0.0040 19  GLU B N   
4202  C CA  . GLU B 19  ? 0.5202 0.4050 0.3228 0.0087  0.0350  -0.0024 19  GLU B CA  
4203  C C   . GLU B 19  ? 0.5608 0.4480 0.3642 0.0080  0.0499  -0.0016 19  GLU B C   
4204  O O   . GLU B 19  ? 0.6075 0.4937 0.4084 0.0115  0.0598  -0.0030 19  GLU B O   
4205  C CB  . GLU B 19  ? 0.5767 0.4363 0.3513 0.0076  0.0310  -0.0029 19  GLU B CB  
4206  C CG  . GLU B 19  ? 0.6687 0.5104 0.4247 0.0021  0.0246  -0.0011 19  GLU B CG  
4207  C CD  . GLU B 19  ? 0.7281 0.5546 0.4636 -0.0008 0.0365  0.0007  19  GLU B CD  
4208  O OE1 . GLU B 19  ? 0.7133 0.5410 0.4468 0.0017  0.0499  -0.0002 19  GLU B OE1 
4209  O OE2 . GLU B 19  ? 0.7874 0.6006 0.5090 -0.0057 0.0329  0.0030  19  GLU B OE2 
4210  N N   . PRO B 20  ? 0.5379 0.4280 0.3459 0.0036  0.0523  0.0006  20  PRO B N   
4211  C CA  . PRO B 20  ? 0.5833 0.4812 0.4006 0.0031  0.0671  0.0012  20  PRO B CA  
4212  C C   . PRO B 20  ? 0.6348 0.5128 0.4273 0.0016  0.0799  0.0017  20  PRO B C   
4213  O O   . PRO B 20  ? 0.6880 0.5732 0.4895 0.0027  0.0942  0.0012  20  PRO B O   
4214  C CB  . PRO B 20  ? 0.5853 0.4909 0.4149 -0.0019 0.0641  0.0035  20  PRO B CB  
4215  C CG  . PRO B 20  ? 0.5776 0.4691 0.3915 -0.0051 0.0506  0.0046  20  PRO B CG  
4216  C CD  . PRO B 20  ? 0.5421 0.4304 0.3506 -0.0009 0.0416  0.0023  20  PRO B CD  
4217  N N   . TYR B 21  ? 0.5983 0.4513 0.3600 -0.0005 0.0755  0.0023  21  TYR B N   
4218  C CA  . TYR B 21  ? 0.6768 0.5087 0.4114 -0.0017 0.0882  0.0026  21  TYR B CA  
4219  C C   . TYR B 21  ? 0.7238 0.5487 0.4481 0.0040  0.0921  -0.0008 21  TYR B C   
4220  O O   . TYR B 21  ? 0.7634 0.5795 0.4756 0.0051  0.1069  -0.0017 21  TYR B O   
4221  C CB  . TYR B 21  ? 0.6984 0.5028 0.4007 -0.0070 0.0817  0.0051  21  TYR B CB  
4222  C CG  . TYR B 21  ? 0.7082 0.5143 0.4153 -0.0132 0.0808  0.0089  21  TYR B CG  
4223  C CD1 . TYR B 21  ? 0.6851 0.5002 0.4063 -0.0148 0.0653  0.0097  21  TYR B CD1 
4224  C CD2 . TYR B 21  ? 0.7631 0.5616 0.4611 -0.0175 0.0960  0.0117  21  TYR B CD2 
4225  C CE1 . TYR B 21  ? 0.6936 0.5094 0.4193 -0.0202 0.0637  0.0129  21  TYR B CE1 
4226  C CE2 . TYR B 21  ? 0.7927 0.5919 0.4953 -0.0236 0.0949  0.0155  21  TYR B CE2 
4227  C CZ  . TYR B 21  ? 0.7577 0.5655 0.4743 -0.0248 0.0781  0.0160  21  TYR B CZ  
4228  O OH  . TYR B 21  ? 0.7661 0.5738 0.4876 -0.0306 0.0758  0.0196  21  TYR B OH  
4229  N N   . THR B 22  ? 0.6915 0.5198 0.4207 0.0077  0.0799  -0.0028 22  THR B N   
4230  C CA  . THR B 22  ? 0.6739 0.4968 0.3963 0.0131  0.0825  -0.0061 22  THR B CA  
4231  C C   . THR B 22  ? 0.6504 0.4982 0.4032 0.0187  0.0846  -0.0079 22  THR B C   
4232  O O   . THR B 22  ? 0.6575 0.5030 0.4080 0.0237  0.0907  -0.0106 22  THR B O   
4233  C CB  . THR B 22  ? 0.6759 0.4822 0.3809 0.0133  0.0674  -0.0071 22  THR B CB  
4234  O OG1 . THR B 22  ? 0.6404 0.4625 0.3669 0.0130  0.0541  -0.0065 22  THR B OG1 
4235  C CG2 . THR B 22  ? 0.6297 0.4075 0.3011 0.0086  0.0633  -0.0057 22  THR B CG2 
4236  N N   . GLY B 23  ? 0.6425 0.5121 0.4221 0.0184  0.0790  -0.0067 23  GLY B N   
4237  C CA  . GLY B 23  ? 0.6168 0.5077 0.4227 0.0238  0.0784  -0.0082 23  GLY B CA  
4238  C C   . GLY B 23  ? 0.6244 0.5138 0.4296 0.0269  0.0672  -0.0093 23  GLY B C   
4239  O O   . GLY B 23  ? 0.6531 0.5571 0.4764 0.0317  0.0665  -0.0102 23  GLY B O   
4240  N N   . GLU B 24  ? 0.5739 0.4457 0.3593 0.0243  0.0582  -0.0091 24  GLU B N   
4241  C CA  . GLU B 24  ? 0.5358 0.4053 0.3214 0.0266  0.0480  -0.0101 24  GLU B CA  
4242  C C   . GLU B 24  ? 0.4813 0.3651 0.2847 0.0252  0.0370  -0.0088 24  GLU B C   
4243  O O   . GLU B 24  ? 0.4428 0.3277 0.2472 0.0210  0.0324  -0.0074 24  GLU B O   
4244  C CB  . GLU B 24  ? 0.5567 0.4002 0.3146 0.0246  0.0426  -0.0111 24  GLU B CB  
4245  C CG  . GLU B 24  ? 0.7162 0.5423 0.4518 0.0258  0.0539  -0.0126 24  GLU B CG  
4246  C CD  . GLU B 24  ? 0.9031 0.7011 0.6078 0.0230  0.0473  -0.0134 24  GLU B CD  
4247  O OE1 . GLU B 24  ? 0.9592 0.7530 0.6638 0.0209  0.0331  -0.0130 24  GLU B OE1 
4248  O OE2 . GLU B 24  ? 1.0458 0.8254 0.7265 0.0231  0.0559  -0.0144 24  GLU B OE2 
4249  N N   . TYR B 25  ? 0.4633 0.3573 0.2802 0.0288  0.0333  -0.0092 25  TYR B N   
4250  C CA  . TYR B 25  ? 0.4357 0.3408 0.2668 0.0278  0.0235  -0.0083 25  TYR B CA  
4251  C C   . TYR B 25  ? 0.4154 0.3054 0.2345 0.0248  0.0135  -0.0087 25  TYR B C   
4252  O O   . TYR B 25  ? 0.4265 0.3071 0.2389 0.0265  0.0115  -0.0097 25  TYR B O   
4253  C CB  . TYR B 25  ? 0.4065 0.3262 0.2543 0.0326  0.0239  -0.0083 25  TYR B CB  
4254  C CG  . TYR B 25  ? 0.4102 0.3478 0.2749 0.0351  0.0293  -0.0079 25  TYR B CG  
4255  C CD1 . TYR B 25  ? 0.3749 0.3138 0.2401 0.0370  0.0394  -0.0086 25  TYR B CD1 
4256  C CD2 . TYR B 25  ? 0.4118 0.3648 0.2925 0.0357  0.0243  -0.0071 25  TYR B CD2 
4257  C CE1 . TYR B 25  ? 0.4341 0.3899 0.3177 0.0393  0.0432  -0.0086 25  TYR B CE1 
4258  C CE2 . TYR B 25  ? 0.4314 0.3997 0.3276 0.0382  0.0275  -0.0071 25  TYR B CE2 
4259  C CZ  . TYR B 25  ? 0.4450 0.4151 0.3438 0.0399  0.0364  -0.0079 25  TYR B CZ  
4260  O OH  . TYR B 25  ? 0.4138 0.3996 0.3308 0.0423  0.0383  -0.0082 25  TYR B OH  
4261  N N   . LEU B 26  ? 0.3845 0.2717 0.2017 0.0205  0.0065  -0.0081 26  LEU B N   
4262  C CA  . LEU B 26  ? 0.4264 0.2973 0.2317 0.0175  -0.0038 -0.0089 26  LEU B CA  
4263  C C   . LEU B 26  ? 0.4529 0.3305 0.2724 0.0181  -0.0120 -0.0094 26  LEU B C   
4264  O O   . LEU B 26  ? 0.4896 0.3537 0.3017 0.0167  -0.0198 -0.0106 26  LEU B O   
4265  C CB  . LEU B 26  ? 0.4587 0.3237 0.2579 0.0130  -0.0091 -0.0081 26  LEU B CB  
4266  C CG  . LEU B 26  ? 0.5244 0.3790 0.3064 0.0112  -0.0008 -0.0070 26  LEU B CG  
4267  C CD1 . LEU B 26  ? 0.5221 0.3639 0.2923 0.0064  -0.0082 -0.0059 26  LEU B CD1 
4268  C CD2 . LEU B 26  ? 0.5583 0.3957 0.3197 0.0130  0.0054  -0.0081 26  LEU B CD2 
4269  N N   . LEU B 27  ? 0.4728 0.3701 0.3121 0.0201  -0.0103 -0.0087 27  LEU B N   
4270  C CA  . LEU B 27  ? 0.4575 0.3625 0.3107 0.0211  -0.0148 -0.0089 27  LEU B CA  
4271  C C   . LEU B 27  ? 0.4561 0.3727 0.3181 0.0256  -0.0075 -0.0079 27  LEU B C   
4272  O O   . LEU B 27  ? 0.4240 0.3486 0.2880 0.0281  -0.0006 -0.0074 27  LEU B O   
4273  C CB  . LEU B 27  ? 0.4848 0.4007 0.3521 0.0191  -0.0210 -0.0090 27  LEU B CB  
4274  C CG  . LEU B 27  ? 0.5118 0.4153 0.3728 0.0149  -0.0308 -0.0102 27  LEU B CG  
4275  C CD1 . LEU B 27  ? 0.4626 0.3771 0.3378 0.0134  -0.0363 -0.0108 27  LEU B CD1 
4276  C CD2 . LEU B 27  ? 0.4955 0.3866 0.3536 0.0138  -0.0377 -0.0115 27  LEU B CD2 
4277  N N   . PRO B 28  ? 0.4329 0.3498 0.3004 0.0269  -0.0091 -0.0076 28  PRO B N   
4278  C CA  . PRO B 28  ? 0.4300 0.3547 0.3030 0.0314  -0.0028 -0.0064 28  PRO B CA  
4279  C C   . PRO B 28  ? 0.4070 0.3478 0.2948 0.0330  -0.0026 -0.0051 28  PRO B C   
4280  O O   . PRO B 28  ? 0.4186 0.3637 0.3103 0.0364  0.0006  -0.0037 28  PRO B O   
4281  C CB  . PRO B 28  ? 0.4118 0.3242 0.2796 0.0314  -0.0047 -0.0065 28  PRO B CB  
4282  C CG  . PRO B 28  ? 0.4478 0.3551 0.3187 0.0268  -0.0134 -0.0074 28  PRO B CG  
4283  C CD  . PRO B 28  ? 0.4658 0.3724 0.3326 0.0241  -0.0166 -0.0085 28  PRO B CD  
4284  N N   . TRP B 29  ? 0.3196 0.2680 0.2145 0.0308  -0.0063 -0.0056 29  TRP B N   
4285  C CA  . TRP B 29  ? 0.3564 0.3177 0.2636 0.0320  -0.0067 -0.0049 29  TRP B CA  
4286  C C   . TRP B 29  ? 0.3606 0.3328 0.2714 0.0366  -0.0020 -0.0039 29  TRP B C   
4287  O O   . TRP B 29  ? 0.3321 0.3108 0.2481 0.0390  -0.0010 -0.0028 29  TRP B O   
4288  C CB  . TRP B 29  ? 0.3072 0.2734 0.2211 0.0290  -0.0120 -0.0064 29  TRP B CB  
4289  C CG  . TRP B 29  ? 0.2849 0.2417 0.1985 0.0249  -0.0185 -0.0077 29  TRP B CG  
4290  C CD1 . TRP B 29  ? 0.3195 0.2706 0.2302 0.0217  -0.0244 -0.0092 29  TRP B CD1 
4291  C CD2 . TRP B 29  ? 0.3588 0.3110 0.2771 0.0236  -0.0206 -0.0077 29  TRP B CD2 
4292  N NE1 . TRP B 29  ? 0.3659 0.3090 0.2792 0.0188  -0.0310 -0.0105 29  TRP B NE1 
4293  C CE2 . TRP B 29  ? 0.3794 0.3237 0.2987 0.0197  -0.0286 -0.0097 29  TRP B CE2 
4294  C CE3 . TRP B 29  ? 0.4016 0.3552 0.3240 0.0250  -0.0168 -0.0061 29  TRP B CE3 
4295  C CZ2 . TRP B 29  ? 0.4337 0.3724 0.3600 0.0174  -0.0332 -0.0105 29  TRP B CZ2 
4296  C CZ3 . TRP B 29  ? 0.4248 0.3726 0.3536 0.0223  -0.0201 -0.0065 29  TRP B CZ3 
4297  C CH2 . TRP B 29  ? 0.4292 0.3704 0.3611 0.0185  -0.0284 -0.0089 29  TRP B CH2 
4298  N N   . THR B 30  ? 0.3505 0.3245 0.2590 0.0378  0.0007  -0.0044 30  THR B N   
4299  C CA  . THR B 30  ? 0.3485 0.3322 0.2622 0.0426  0.0042  -0.0038 30  THR B CA  
4300  C C   . THR B 30  ? 0.3748 0.3543 0.2854 0.0464  0.0074  -0.0024 30  THR B C   
4301  O O   . THR B 30  ? 0.4305 0.4161 0.3451 0.0502  0.0077  -0.0012 30  THR B O   
4302  C CB  . THR B 30  ? 0.3309 0.3171 0.2454 0.0427  0.0072  -0.0048 30  THR B CB  
4303  O OG1 . THR B 30  ? 0.3309 0.3208 0.2486 0.0390  0.0037  -0.0057 30  THR B OG1 
4304  C CG2 . THR B 30  ? 0.3616 0.3581 0.2844 0.0479  0.0098  -0.0046 30  THR B CG2 
4305  N N   . PHE B 31  ? 0.3109 0.2785 0.2131 0.0456  0.0092  -0.0025 31  PHE B N   
4306  C CA  . PHE B 31  ? 0.3670 0.3290 0.2659 0.0492  0.0118  -0.0013 31  PHE B CA  
4307  C C   . PHE B 31  ? 0.3946 0.3560 0.2955 0.0488  0.0096  0.0008  31  PHE B C   
4308  O O   . PHE B 31  ? 0.4086 0.3715 0.3104 0.0528  0.0112  0.0027  31  PHE B O   
4309  C CB  . PHE B 31  ? 0.3849 0.3326 0.2732 0.0481  0.0135  -0.0025 31  PHE B CB  
4310  C CG  . PHE B 31  ? 0.3347 0.2749 0.2195 0.0516  0.0153  -0.0015 31  PHE B CG  
4311  C CD1 . PHE B 31  ? 0.3037 0.2459 0.1896 0.0570  0.0197  -0.0017 31  PHE B CD1 
4312  C CD2 . PHE B 31  ? 0.3431 0.2743 0.2250 0.0494  0.0125  -0.0004 31  PHE B CD2 
4313  C CE1 . PHE B 31  ? 0.3269 0.2613 0.2095 0.0604  0.0208  -0.0009 31  PHE B CE1 
4314  C CE2 . PHE B 31  ? 0.3187 0.2420 0.1973 0.0523  0.0140  0.0008  31  PHE B CE2 
4315  C CZ  . PHE B 31  ? 0.3456 0.2700 0.2237 0.0580  0.0179  0.0005  31  PHE B CZ  
4316  N N   . PHE B 32  ? 0.3245 0.2824 0.2261 0.0441  0.0062  0.0005  32  PHE B N   
4317  C CA  . PHE B 32  ? 0.3584 0.3149 0.2632 0.0433  0.0058  0.0025  32  PHE B CA  
4318  C C   . PHE B 32  ? 0.3766 0.3445 0.2871 0.0454  0.0067  0.0038  32  PHE B C   
4319  O O   . PHE B 32  ? 0.3435 0.3105 0.2534 0.0473  0.0090  0.0064  32  PHE B O   
4320  C CB  . PHE B 32  ? 0.2766 0.2273 0.1840 0.0378  0.0017  0.0014  32  PHE B CB  
4321  C CG  . PHE B 32  ? 0.3998 0.3358 0.2999 0.0362  0.0001  0.0007  32  PHE B CG  
4322  C CD1 . PHE B 32  ? 0.3552 0.2836 0.2513 0.0383  0.0026  0.0024  32  PHE B CD1 
4323  C CD2 . PHE B 32  ? 0.4701 0.3983 0.3658 0.0327  -0.0046 -0.0018 32  PHE B CD2 
4324  C CE1 . PHE B 32  ? 0.4251 0.3390 0.3137 0.0371  0.0006  0.0012  32  PHE B CE1 
4325  C CE2 . PHE B 32  ? 0.4556 0.3684 0.3424 0.0315  -0.0070 -0.0029 32  PHE B CE2 
4326  C CZ  . PHE B 32  ? 0.4035 0.3094 0.2870 0.0337  -0.0043 -0.0016 32  PHE B CZ  
4327  N N   . HIS B 33  ? 0.3775 0.3548 0.2923 0.0452  0.0049  0.0021  33  HIS B N   
4328  C CA  . HIS B 33  ? 0.3792 0.3658 0.2974 0.0478  0.0053  0.0028  33  HIS B CA  
4329  C C   . HIS B 33  ? 0.3886 0.3782 0.3040 0.0536  0.0066  0.0039  33  HIS B C   
4330  O O   . HIS B 33  ? 0.3823 0.3748 0.2963 0.0566  0.0070  0.0055  33  HIS B O   
4331  C CB  . HIS B 33  ? 0.3418 0.3366 0.2659 0.0458  0.0021  0.0002  33  HIS B CB  
4332  C CG  . HIS B 33  ? 0.4157 0.4097 0.3449 0.0414  0.0003  -0.0008 33  HIS B CG  
4333  N ND1 . HIS B 33  ? 0.4203 0.4141 0.3521 0.0410  0.0029  0.0006  33  HIS B ND1 
4334  C CD2 . HIS B 33  ? 0.4041 0.3970 0.3374 0.0373  -0.0037 -0.0031 33  HIS B CD2 
4335  C CE1 . HIS B 33  ? 0.4351 0.4290 0.3745 0.0369  0.0006  -0.0012 33  HIS B CE1 
4336  N NE2 . HIS B 33  ? 0.4175 0.4105 0.3576 0.0348  -0.0042 -0.0035 33  HIS B NE2 
4337  N N   . ALA B 34  ? 0.3339 0.3218 0.2483 0.0554  0.0074  0.0031  34  ALA B N   
4338  C CA  . ALA B 34  ? 0.3351 0.3253 0.2494 0.0613  0.0080  0.0039  34  ALA B CA  
4339  C C   . ALA B 34  ? 0.4167 0.3983 0.3246 0.0639  0.0097  0.0069  34  ALA B C   
4340  O O   . ALA B 34  ? 0.4153 0.3981 0.3212 0.0684  0.0088  0.0087  34  ALA B O   
4341  C CB  . ALA B 34  ? 0.3161 0.3073 0.2332 0.0623  0.0096  0.0019  34  ALA B CB  
4342  N N   . VAL B 35  ? 0.4307 0.4024 0.3347 0.0611  0.0115  0.0077  35  VAL B N   
4343  C CA  . VAL B 35  ? 0.3843 0.3469 0.2828 0.0631  0.0130  0.0108  35  VAL B CA  
4344  C C   . VAL B 35  ? 0.3991 0.3608 0.2961 0.0609  0.0138  0.0136  35  VAL B C   
4345  O O   . VAL B 35  ? 0.4525 0.4075 0.3441 0.0630  0.0154  0.0170  35  VAL B O   
4346  C CB  . VAL B 35  ? 0.4155 0.3666 0.3104 0.0610  0.0142  0.0104  35  VAL B CB  
4347  C CG1 . VAL B 35  ? 0.4201 0.3711 0.3149 0.0632  0.0152  0.0074  35  VAL B CG1 
4348  C CG2 . VAL B 35  ? 0.4333 0.3812 0.3298 0.0545  0.0131  0.0096  35  VAL B CG2 
4349  N N   . LYS B 36  ? 0.3957 0.3633 0.2976 0.0568  0.0133  0.0123  36  LYS B N   
4350  C CA  . LYS B 36  ? 0.4399 0.4071 0.3416 0.0548  0.0156  0.0146  36  LYS B CA  
4351  C C   . LYS B 36  ? 0.4393 0.4141 0.3389 0.0580  0.0154  0.0147  36  LYS B C   
4352  O O   . LYS B 36  ? 0.4607 0.4320 0.3541 0.0593  0.0184  0.0178  36  LYS B O   
4353  C CB  . LYS B 36  ? 0.3453 0.3136 0.2551 0.0486  0.0153  0.0127  36  LYS B CB  
4354  C CG  . LYS B 36  ? 0.3642 0.3301 0.2765 0.0457  0.0195  0.0152  36  LYS B CG  
4355  C CD  . LYS B 36  ? 0.4102 0.3769 0.3339 0.0397  0.0181  0.0130  36  LYS B CD  
4356  C CE  . LYS B 36  ? 0.3993 0.3764 0.3295 0.0388  0.0155  0.0093  36  LYS B CE  
4357  N NZ  . LYS B 36  ? 0.3811 0.3647 0.3112 0.0406  0.0197  0.0100  36  LYS B NZ  
4358  N N   . ASP B 37  ? 0.4168 0.4007 0.3203 0.0592  0.0120  0.0115  37  ASP B N   
4359  C CA  . ASP B 37  ? 0.3614 0.3520 0.2635 0.0613  0.0110  0.0108  37  ASP B CA  
4360  C C   . ASP B 37  ? 0.3689 0.3646 0.2699 0.0667  0.0066  0.0095  37  ASP B C   
4361  O O   . ASP B 37  ? 0.3675 0.3630 0.2616 0.0707  0.0054  0.0105  37  ASP B O   
4362  C CB  . ASP B 37  ? 0.3454 0.3430 0.2559 0.0569  0.0102  0.0076  37  ASP B CB  
4363  C CG  . ASP B 37  ? 0.4070 0.4004 0.3223 0.0516  0.0133  0.0081  37  ASP B CG  
4364  O OD1 . ASP B 37  ? 0.3731 0.3627 0.2859 0.0509  0.0180  0.0107  37  ASP B OD1 
4365  O OD2 . ASP B 37  ? 0.3945 0.3875 0.3161 0.0478  0.0108  0.0062  37  ASP B OD2 
4366  N N   . TYR B 38  ? 0.3116 0.3110 0.2191 0.0669  0.0043  0.0073  38  TYR B N   
4367  C CA  . TYR B 38  ? 0.3094 0.3163 0.2208 0.0709  -0.0002 0.0052  38  TYR B CA  
4368  C C   . TYR B 38  ? 0.3674 0.3708 0.2734 0.0774  -0.0023 0.0071  38  TYR B C   
4369  O O   . TYR B 38  ? 0.3746 0.3827 0.2814 0.0814  -0.0073 0.0058  38  TYR B O   
4370  C CB  . TYR B 38  ? 0.3726 0.3840 0.2931 0.0689  -0.0006 0.0027  38  TYR B CB  
4371  C CG  . TYR B 38  ? 0.4217 0.4364 0.3466 0.0632  -0.0008 0.0006  38  TYR B CG  
4372  C CD1 . TYR B 38  ? 0.3948 0.4138 0.3203 0.0621  -0.0029 -0.0005 38  TYR B CD1 
4373  C CD2 . TYR B 38  ? 0.3797 0.3918 0.3068 0.0592  0.0009  -0.0004 38  TYR B CD2 
4374  C CE1 . TYR B 38  ? 0.3977 0.4192 0.3280 0.0573  -0.0039 -0.0026 38  TYR B CE1 
4375  C CE2 . TYR B 38  ? 0.3870 0.4002 0.3169 0.0542  -0.0005 -0.0021 38  TYR B CE2 
4376  C CZ  . TYR B 38  ? 0.3880 0.4064 0.3206 0.0533  -0.0032 -0.0032 38  TYR B CZ  
4377  O OH  . TYR B 38  ? 0.4131 0.4322 0.3493 0.0487  -0.0054 -0.0051 38  TYR B OH  
4378  N N   . TYR B 39  ? 0.3772 0.3718 0.2781 0.0787  0.0003  0.0099  39  TYR B N   
4379  C CA  . TYR B 39  ? 0.3638 0.3527 0.2577 0.0850  -0.0024 0.0122  39  TYR B CA  
4380  C C   . TYR B 39  ? 0.3532 0.3342 0.2334 0.0853  -0.0008 0.0158  39  TYR B C   
4381  O O   . TYR B 39  ? 0.3615 0.3395 0.2332 0.0903  -0.0047 0.0169  39  TYR B O   
4382  C CB  . TYR B 39  ? 0.3835 0.3655 0.2780 0.0868  -0.0006 0.0135  39  TYR B CB  
4383  C CG  . TYR B 39  ? 0.4050 0.3784 0.2909 0.0931  -0.0035 0.0166  39  TYR B CG  
4384  C CD1 . TYR B 39  ? 0.3934 0.3703 0.2845 0.0996  -0.0096 0.0150  39  TYR B CD1 
4385  C CD2 . TYR B 39  ? 0.3938 0.3548 0.2671 0.0926  -0.0007 0.0211  39  TYR B CD2 
4386  C CE1 . TYR B 39  ? 0.4422 0.4100 0.3251 0.1057  -0.0138 0.0177  39  TYR B CE1 
4387  C CE2 . TYR B 39  ? 0.4319 0.3830 0.2955 0.0984  -0.0039 0.0244  39  TYR B CE2 
4388  C CZ  . TYR B 39  ? 0.4547 0.4089 0.3226 0.1052  -0.0110 0.0225  39  TYR B CZ  
4389  O OH  . TYR B 39  ? 0.4795 0.4227 0.3376 0.1113  -0.0156 0.0256  39  TYR B OH  
4390  N N   . ASP B 40  ? 0.3316 0.3084 0.2094 0.0800  0.0050  0.0175  40  ASP B N   
4391  C CA  . ASP B 40  ? 0.3811 0.3488 0.2463 0.0800  0.0087  0.0216  40  ASP B CA  
4392  C C   . ASP B 40  ? 0.4261 0.3973 0.2854 0.0807  0.0083  0.0206  40  ASP B C   
4393  O O   . ASP B 40  ? 0.4437 0.4063 0.2886 0.0831  0.0101  0.0239  40  ASP B O   
4394  C CB  . ASP B 40  ? 0.3996 0.3623 0.2672 0.0738  0.0151  0.0235  40  ASP B CB  
4395  C CG  . ASP B 40  ? 0.4868 0.4387 0.3509 0.0748  0.0162  0.0267  40  ASP B CG  
4396  O OD1 . ASP B 40  ? 0.4577 0.3996 0.3099 0.0777  0.0171  0.0310  40  ASP B OD1 
4397  O OD2 . ASP B 40  ? 0.4495 0.4017 0.3214 0.0729  0.0158  0.0249  40  ASP B OD2 
4398  N N   . MET B 41  ? 0.4032 0.3855 0.2719 0.0788  0.0063  0.0162  41  MET B N   
4399  C CA  . MET B 41  ? 0.3841 0.3688 0.2465 0.0799  0.0058  0.0147  41  MET B CA  
4400  C C   . MET B 41  ? 0.4240 0.4054 0.2755 0.0870  -0.0009 0.0149  41  MET B C   
4401  O O   . MET B 41  ? 0.4366 0.4092 0.2717 0.0896  0.0009  0.0172  41  MET B O   
4402  C CB  . MET B 41  ? 0.3201 0.3163 0.1955 0.0763  0.0044  0.0099  41  MET B CB  
4403  C CG  . MET B 41  ? 0.3167 0.3139 0.1995 0.0698  0.0107  0.0098  41  MET B CG  
4404  S SD  . MET B 41  ? 0.3841 0.3759 0.2570 0.0689  0.0190  0.0119  41  MET B SD  
4405  C CE  . MET B 41  ? 0.3291 0.3298 0.2040 0.0702  0.0158  0.0064  41  MET B CE  
4406  N N   . PRO B 42  ? 0.3845 0.3712 0.2438 0.0905  -0.0084 0.0125  42  PRO B N   
4407  C CA  . PRO B 42  ? 0.4117 0.3935 0.2612 0.0977  -0.0162 0.0128  42  PRO B CA  
4408  C C   . PRO B 42  ? 0.4179 0.3861 0.2541 0.1015  -0.0158 0.0178  42  PRO B C   
4409  O O   . PRO B 42  ? 0.4584 0.4184 0.2804 0.1072  -0.0215 0.0190  42  PRO B O   
4410  C CB  . PRO B 42  ? 0.3671 0.3596 0.2338 0.0995  -0.0234 0.0089  42  PRO B CB  
4411  C CG  . PRO B 42  ? 0.3273 0.3253 0.2078 0.0941  -0.0177 0.0085  42  PRO B CG  
4412  C CD  . PRO B 42  ? 0.3346 0.3315 0.2118 0.0882  -0.0104 0.0093  42  PRO B CD  
4413  N N   . ALA B 43  ? 0.4044 0.3688 0.2439 0.0986  -0.0102 0.0207  43  ALA B N   
4414  C CA  . ALA B 43  ? 0.3920 0.3421 0.2183 0.1020  -0.0099 0.0257  43  ALA B CA  
4415  C C   . ALA B 43  ? 0.4687 0.4064 0.2737 0.1019  -0.0053 0.0299  43  ALA B C   
4416  O O   . ALA B 43  ? 0.4579 0.3817 0.2471 0.1060  -0.0071 0.0342  43  ALA B O   
4417  C CB  . ALA B 43  ? 0.3924 0.3398 0.2261 0.0985  -0.0047 0.0276  43  ALA B CB  
4418  N N   . TYR B 44  ? 0.4745 0.4162 0.2784 0.0975  0.0009  0.0288  44  TYR B N   
4419  C CA  . TYR B 44  ? 0.5054 0.4352 0.2884 0.0977  0.0066  0.0325  44  TYR B CA  
4420  C C   . TYR B 44  ? 0.5126 0.4332 0.2765 0.1054  -0.0017 0.0329  44  TYR B C   
4421  O O   . TYR B 44  ? 0.5181 0.4227 0.2596 0.1075  0.0010  0.0377  44  TYR B O   
4422  C CB  . TYR B 44  ? 0.4567 0.3940 0.2435 0.0929  0.0138  0.0298  44  TYR B CB  
4423  C CG  . TYR B 44  ? 0.4662 0.4063 0.2645 0.0854  0.0239  0.0312  44  TYR B CG  
4424  C CD1 . TYR B 44  ? 0.4598 0.3895 0.2473 0.0825  0.0341  0.0361  44  TYR B CD1 
4425  C CD2 . TYR B 44  ? 0.4015 0.3538 0.2215 0.0809  0.0231  0.0277  44  TYR B CD2 
4426  C CE1 . TYR B 44  ? 0.4805 0.4133 0.2816 0.0755  0.0426  0.0369  44  TYR B CE1 
4427  C CE2 . TYR B 44  ? 0.3855 0.3396 0.2165 0.0743  0.0306  0.0285  44  TYR B CE2 
4428  C CZ  . TYR B 44  ? 0.4695 0.4146 0.2925 0.0716  0.0400  0.0329  44  TYR B CZ  
4429  O OH  . TYR B 44  ? 0.4696 0.4167 0.3063 0.0648  0.0466  0.0334  44  TYR B OH  
4430  N N   . LEU B 45  ? 0.5078 0.4374 0.2799 0.1093  -0.0121 0.0279  45  LEU B N   
4431  C CA  . LEU B 45  ? 0.5622 0.4832 0.3183 0.1169  -0.0225 0.0274  45  LEU B CA  
4432  C C   . LEU B 45  ? 0.5717 0.4779 0.3158 0.1221  -0.0276 0.0322  45  LEU B C   
4433  O O   . LEU B 45  ? 0.5702 0.4634 0.2939 0.1284  -0.0351 0.0335  45  LEU B O   
4434  C CB  . LEU B 45  ? 0.5004 0.4354 0.2738 0.1195  -0.0332 0.0210  45  LEU B CB  
4435  C CG  . LEU B 45  ? 0.4745 0.4212 0.2557 0.1155  -0.0303 0.0162  45  LEU B CG  
4436  C CD1 . LEU B 45  ? 0.4267 0.3870 0.2269 0.1172  -0.0405 0.0103  45  LEU B CD1 
4437  C CD2 . LEU B 45  ? 0.4620 0.3983 0.2191 0.1171  -0.0274 0.0165  45  LEU B CD2 
4438  N N   . LYS B 46  ? 0.5309 0.4376 0.2860 0.1200  -0.0243 0.0347  46  LYS B N   
4439  C CA  . LYS B 46  ? 0.5639 0.4556 0.3078 0.1250  -0.0290 0.0392  46  LYS B CA  
4440  C C   . LYS B 46  ? 0.6338 0.5053 0.3491 0.1248  -0.0227 0.0459  46  LYS B C   
4441  O O   . LYS B 46  ? 0.6456 0.5005 0.3422 0.1307  -0.0294 0.0497  46  LYS B O   
4442  C CB  . LYS B 46  ? 0.5511 0.4472 0.3130 0.1225  -0.0261 0.0399  46  LYS B CB  
4443  C CG  . LYS B 46  ? 0.6199 0.5322 0.4075 0.1244  -0.0328 0.0341  46  LYS B CG  
4444  C CD  . LYS B 46  ? 0.6826 0.5972 0.4845 0.1217  -0.0280 0.0347  46  LYS B CD  
4445  C CE  . LYS B 46  ? 0.7647 0.6878 0.5856 0.1266  -0.0358 0.0306  46  LYS B CE  
4446  N NZ  . LYS B 46  ? 0.8552 0.7661 0.6682 0.1349  -0.0452 0.0327  46  LYS B NZ  
4447  N N   . ASP B 47  ? 0.6042 0.4764 0.3157 0.1181  -0.0099 0.0475  47  ASP B N   
4448  C CA  . ASP B 47  ? 0.6643 0.5183 0.3517 0.1163  -0.0007 0.0543  47  ASP B CA  
4449  C C   . ASP B 47  ? 0.6572 0.5055 0.3240 0.1167  0.0038  0.0540  47  ASP B C   
4450  O O   . ASP B 47  ? 0.6556 0.4864 0.2981 0.1162  0.0113  0.0598  47  ASP B O   
4451  C CB  . ASP B 47  ? 0.6748 0.5319 0.3745 0.1078  0.0124  0.0571  47  ASP B CB  
4452  C CG  . ASP B 47  ? 0.7351 0.5974 0.4546 0.1071  0.0089  0.0567  47  ASP B CG  
4453  O OD1 . ASP B 47  ? 0.7439 0.5979 0.4587 0.1130  0.0000  0.0583  47  ASP B OD1 
4454  O OD2 . ASP B 47  ? 0.7362 0.6105 0.4759 0.1008  0.0148  0.0545  47  ASP B OD2 
4455  N N   . PHE B 48  ? 0.6347 0.4963 0.3097 0.1175  0.0000  0.0474  48  PHE B N   
4456  C CA  . PHE B 48  ? 0.6855 0.5427 0.3426 0.1176  0.0054  0.0462  48  PHE B CA  
4457  C C   . PHE B 48  ? 0.7075 0.5660 0.3583 0.1246  -0.0086 0.0408  48  PHE B C   
4458  O O   . PHE B 48  ? 0.6684 0.5429 0.3420 0.1255  -0.0176 0.0353  48  PHE B O   
4459  C CB  . PHE B 48  ? 0.6151 0.4879 0.2905 0.1101  0.0173  0.0430  48  PHE B CB  
4460  C CG  . PHE B 48  ? 0.5974 0.4688 0.2804 0.1028  0.0308  0.0479  48  PHE B CG  
4461  C CD1 . PHE B 48  ? 0.6417 0.4979 0.3040 0.1007  0.0431  0.0536  48  PHE B CD1 
4462  C CD2 . PHE B 48  ? 0.5824 0.4669 0.2928 0.0980  0.0312  0.0467  48  PHE B CD2 
4463  C CE1 . PHE B 48  ? 0.6316 0.4867 0.3033 0.0936  0.0552  0.0581  48  PHE B CE1 
4464  C CE2 . PHE B 48  ? 0.5408 0.4231 0.2587 0.0914  0.0421  0.0508  48  PHE B CE2 
4465  C CZ  . PHE B 48  ? 0.5241 0.3924 0.2241 0.0890  0.0540  0.0565  48  PHE B CZ  
4466  N N   . GLU B 49  ? 0.7103 0.5506 0.3292 0.1296  -0.0106 0.0425  49  GLU B N   
4467  C CA  . GLU B 49  ? 0.7676 0.6054 0.3767 0.1369  -0.0254 0.0375  49  GLU B CA  
4468  C C   . GLU B 49  ? 0.6994 0.5471 0.3110 0.1351  -0.0212 0.0313  49  GLU B C   
4469  O O   . GLU B 49  ? 0.6665 0.5012 0.2512 0.1378  -0.0186 0.0309  49  GLU B O   
4470  C CB  . GLU B 49  ? 0.8843 0.6960 0.4580 0.1432  -0.0314 0.0417  49  GLU B CB  
4471  C CG  . GLU B 49  ? 1.0179 0.8198 0.5915 0.1460  -0.0387 0.0468  49  GLU B CG  
4472  C CD  . GLU B 49  ? 1.1288 0.9374 0.7180 0.1525  -0.0584 0.0422  49  GLU B CD  
4473  O OE1 . GLU B 49  ? 1.2019 0.9968 0.7788 0.1572  -0.0697 0.0415  49  GLU B OE1 
4474  O OE2 . GLU B 49  ? 1.0963 0.9255 0.7163 0.1511  -0.0612 0.0384  49  GLU B OE2 
4475  N N   . ILE B 50  ? 0.6153 0.4856 0.2593 0.1302  -0.0198 0.0266  50  ILE B N   
4476  C CA  . ILE B 50  ? 0.6737 0.5564 0.3268 0.1287  -0.0187 0.0198  50  ILE B CA  
4477  C C   . ILE B 50  ? 0.6016 0.5025 0.2837 0.1290  -0.0310 0.0141  50  ILE B C   
4478  O O   . ILE B 50  ? 0.5687 0.4738 0.2652 0.1298  -0.0377 0.0155  50  ILE B O   
4479  C CB  . ILE B 50  ? 0.6303 0.5220 0.2945 0.1209  -0.0017 0.0200  50  ILE B CB  
4480  C CG1 . ILE B 50  ? 0.6078 0.5127 0.3005 0.1147  0.0021  0.0218  50  ILE B CG1 
4481  C CG2 . ILE B 50  ? 0.6752 0.5494 0.3123 0.1201  0.0120  0.0255  50  ILE B CG2 
4482  C CD1 . ILE B 50  ? 0.5719 0.4895 0.2828 0.1075  0.0141  0.0199  50  ILE B CD1 
4483  N N   . LYS B 51  ? 0.5587 0.4700 0.2495 0.1284  -0.0333 0.0077  51  LYS B N   
4484  C CA  . LYS B 51  ? 0.4872 0.4162 0.2063 0.1276  -0.0431 0.0023  51  LYS B CA  
4485  C C   . LYS B 51  ? 0.4429 0.3883 0.1864 0.1196  -0.0330 0.0009  51  LYS B C   
4486  O O   . LYS B 51  ? 0.4600 0.4057 0.1991 0.1165  -0.0228 0.0000  51  LYS B O   
4487  C CB  . LYS B 51  ? 0.5121 0.4409 0.2258 0.1322  -0.0547 -0.0041 51  LYS B CB  
4488  C CG  . LYS B 51  ? 0.6042 0.5141 0.2898 0.1407  -0.0662 -0.0036 51  LYS B CG  
4489  C CD  . LYS B 51  ? 0.6151 0.5221 0.3066 0.1442  -0.0763 -0.0005 51  LYS B CD  
4490  C CE  . LYS B 51  ? 0.7149 0.6026 0.3797 0.1530  -0.0903 -0.0004 51  LYS B CE  
4491  N NZ  . LYS B 51  ? 0.7736 0.6436 0.4173 0.1554  -0.0872 0.0071  51  LYS B NZ  
4492  N N   . LEU B 52  ? 0.4045 0.3627 0.1735 0.1166  -0.0359 0.0005  52  LEU B N   
4493  C CA  . LEU B 52  ? 0.4496 0.4223 0.2413 0.1094  -0.0289 -0.0012 52  LEU B CA  
4494  C C   . LEU B 52  ? 0.4640 0.4503 0.2791 0.1088  -0.0382 -0.0052 52  LEU B C   
4495  O O   . LEU B 52  ? 0.4386 0.4250 0.2591 0.1119  -0.0458 -0.0045 52  LEU B O   
4496  C CB  . LEU B 52  ? 0.4417 0.4136 0.2389 0.1046  -0.0187 0.0040  52  LEU B CB  
4497  C CG  . LEU B 52  ? 0.4807 0.4408 0.2602 0.1031  -0.0068 0.0087  52  LEU B CG  
4498  C CD1 . LEU B 52  ? 0.4824 0.4432 0.2722 0.0981  0.0005  0.0131  52  LEU B CD1 
4499  C CD2 . LEU B 52  ? 0.4621 0.4240 0.2379 0.1007  0.0012  0.0059  52  LEU B CD2 
4500  N N   . ASN B 53  ? 0.4534 0.4508 0.2831 0.1046  -0.0372 -0.0094 53  ASN B N   
4501  C CA  . ASN B 53  ? 0.3554 0.3647 0.2061 0.1034  -0.0452 -0.0132 53  ASN B CA  
4502  C C   . ASN B 53  ? 0.3315 0.3506 0.2011 0.0963  -0.0386 -0.0128 53  ASN B C   
4503  O O   . ASN B 53  ? 0.3515 0.3698 0.2196 0.0923  -0.0296 -0.0113 53  ASN B O   
4504  C CB  . ASN B 53  ? 0.3319 0.3441 0.1824 0.1052  -0.0525 -0.0188 53  ASN B CB  
4505  C CG  . ASN B 53  ? 0.4046 0.4044 0.2321 0.1124  -0.0588 -0.0197 53  ASN B CG  
4506  O OD1 . ASN B 53  ? 0.4607 0.4570 0.2862 0.1173  -0.0690 -0.0198 53  ASN B OD1 
4507  N ND2 . ASN B 53  ? 0.3882 0.3805 0.1978 0.1131  -0.0526 -0.0203 53  ASN B ND2 
4508  N N   . PHE B 54  ? 0.3648 0.3927 0.2525 0.0949  -0.0435 -0.0142 54  PHE B N   
4509  C CA  . PHE B 54  ? 0.3622 0.3965 0.2647 0.0889  -0.0380 -0.0131 54  PHE B CA  
4510  C C   . PHE B 54  ? 0.3252 0.3696 0.2454 0.0862  -0.0431 -0.0167 54  PHE B C   
4511  O O   . PHE B 54  ? 0.3191 0.3669 0.2455 0.0893  -0.0512 -0.0190 54  PHE B O   
4512  C CB  . PHE B 54  ? 0.3651 0.3963 0.2688 0.0898  -0.0352 -0.0092 54  PHE B CB  
4513  C CG  . PHE B 54  ? 0.4085 0.4290 0.2958 0.0912  -0.0294 -0.0050 54  PHE B CG  
4514  C CD1 . PHE B 54  ? 0.3875 0.4059 0.2743 0.0863  -0.0205 -0.0027 54  PHE B CD1 
4515  C CD2 . PHE B 54  ? 0.4337 0.4452 0.3053 0.0973  -0.0333 -0.0035 54  PHE B CD2 
4516  C CE1 . PHE B 54  ? 0.4160 0.4243 0.2887 0.0870  -0.0146 0.0013  54  PHE B CE1 
4517  C CE2 . PHE B 54  ? 0.4309 0.4311 0.2858 0.0983  -0.0273 0.0008  54  PHE B CE2 
4518  C CZ  . PHE B 54  ? 0.4421 0.4412 0.2984 0.0928  -0.0174 0.0033  54  PHE B CZ  
4519  N N   . ASN B 55  ? 0.3284 0.3769 0.2571 0.0802  -0.0386 -0.0172 55  ASN B N   
4520  C CA  . ASN B 55  ? 0.3813 0.4375 0.3261 0.0764  -0.0413 -0.0192 55  ASN B CA  
4521  C C   . ASN B 55  ? 0.3716 0.4278 0.3223 0.0727  -0.0352 -0.0164 55  ASN B C   
4522  O O   . ASN B 55  ? 0.3527 0.4042 0.2976 0.0701  -0.0291 -0.0143 55  ASN B O   
4523  C CB  . ASN B 55  ? 0.2334 0.2922 0.1815 0.0726  -0.0422 -0.0222 55  ASN B CB  
4524  C CG  . ASN B 55  ? 0.3106 0.3756 0.2735 0.0684  -0.0453 -0.0238 55  ASN B CG  
4525  O OD1 . ASN B 55  ? 0.3462 0.4156 0.3166 0.0700  -0.0519 -0.0262 55  ASN B OD1 
4526  N ND2 . ASN B 55  ? 0.2986 0.3630 0.2656 0.0629  -0.0407 -0.0226 55  ASN B ND2 
4527  N N   . LEU B 56  ? 0.3461 0.4072 0.3085 0.0724  -0.0368 -0.0167 56  LEU B N   
4528  C CA  . LEU B 56  ? 0.3959 0.4567 0.3638 0.0687  -0.0308 -0.0148 56  LEU B CA  
4529  C C   . LEU B 56  ? 0.3878 0.4543 0.3682 0.0640  -0.0319 -0.0166 56  LEU B C   
4530  O O   . LEU B 56  ? 0.3742 0.4470 0.3656 0.0654  -0.0366 -0.0185 56  LEU B O   
4531  C CB  . LEU B 56  ? 0.3418 0.4021 0.3121 0.0728  -0.0295 -0.0132 56  LEU B CB  
4532  C CG  . LEU B 56  ? 0.3389 0.3925 0.2968 0.0780  -0.0296 -0.0110 56  LEU B CG  
4533  C CD1 . LEU B 56  ? 0.3831 0.4365 0.3459 0.0824  -0.0298 -0.0100 56  LEU B CD1 
4534  C CD2 . LEU B 56  ? 0.4123 0.4582 0.3588 0.0750  -0.0232 -0.0085 56  LEU B CD2 
4535  N N   . THR B 57  ? 0.3448 0.4082 0.3235 0.0584  -0.0281 -0.0160 57  THR B N   
4536  C CA  . THR B 57  ? 0.3346 0.4010 0.3228 0.0537  -0.0283 -0.0169 57  THR B CA  
4537  C C   . THR B 57  ? 0.3166 0.3845 0.3118 0.0534  -0.0231 -0.0156 57  THR B C   
4538  O O   . THR B 57  ? 0.2861 0.3497 0.2758 0.0551  -0.0181 -0.0138 57  THR B O   
4539  C CB  . THR B 57  ? 0.3224 0.3829 0.3052 0.0480  -0.0265 -0.0164 57  THR B CB  
4540  O OG1 . THR B 57  ? 0.2796 0.3326 0.2539 0.0469  -0.0207 -0.0140 57  THR B OG1 
4541  C CG2 . THR B 57  ? 0.2985 0.3585 0.2774 0.0483  -0.0311 -0.0183 57  THR B CG2 
4542  N N   . PRO B 58  ? 0.3304 0.4041 0.3386 0.0512  -0.0238 -0.0167 58  PRO B N   
4543  C CA  . PRO B 58  ? 0.3322 0.4081 0.3491 0.0508  -0.0174 -0.0158 58  PRO B CA  
4544  C C   . PRO B 58  ? 0.3127 0.3797 0.3194 0.0472  -0.0088 -0.0137 58  PRO B C   
4545  O O   . PRO B 58  ? 0.2919 0.3578 0.2993 0.0494  -0.0027 -0.0129 58  PRO B O   
4546  C CB  . PRO B 58  ? 0.3225 0.4055 0.3552 0.0475  -0.0194 -0.0173 58  PRO B CB  
4547  C CG  . PRO B 58  ? 0.2803 0.3668 0.3146 0.0493  -0.0297 -0.0196 58  PRO B CG  
4548  C CD  . PRO B 58  ? 0.2757 0.3545 0.2927 0.0492  -0.0304 -0.0189 58  PRO B CD  
4549  N N   . VAL B 59  ? 0.2791 0.3388 0.2759 0.0423  -0.0088 -0.0129 59  VAL B N   
4550  C CA  . VAL B 59  ? 0.2867 0.3356 0.2715 0.0389  -0.0022 -0.0111 59  VAL B CA  
4551  C C   . VAL B 59  ? 0.3392 0.3827 0.3140 0.0425  -0.0004 -0.0102 59  VAL B C   
4552  O O   . VAL B 59  ? 0.2950 0.3313 0.2628 0.0422  0.0059  -0.0092 59  VAL B O   
4553  C CB  . VAL B 59  ? 0.2852 0.3265 0.2619 0.0331  -0.0048 -0.0107 59  VAL B CB  
4554  C CG1 . VAL B 59  ? 0.3102 0.3518 0.2838 0.0342  -0.0122 -0.0118 59  VAL B CG1 
4555  C CG2 . VAL B 59  ? 0.2455 0.2733 0.2076 0.0298  0.0008  -0.0090 59  VAL B CG2 
4556  N N   . LEU B 60  ? 0.2935 0.3393 0.2668 0.0460  -0.0054 -0.0106 60  LEU B N   
4557  C CA  . LEU B 60  ? 0.3170 0.3577 0.2821 0.0495  -0.0034 -0.0093 60  LEU B CA  
4558  C C   . LEU B 60  ? 0.3641 0.4080 0.3348 0.0544  -0.0001 -0.0092 60  LEU B C   
4559  O O   . LEU B 60  ? 0.3809 0.4184 0.3457 0.0555  0.0048  -0.0082 60  LEU B O   
4560  C CB  . LEU B 60  ? 0.2536 0.2956 0.2154 0.0519  -0.0084 -0.0094 60  LEU B CB  
4561  C CG  . LEU B 60  ? 0.2840 0.3206 0.2380 0.0553  -0.0061 -0.0076 60  LEU B CG  
4562  C CD1 . LEU B 60  ? 0.3662 0.3926 0.3117 0.0518  -0.0023 -0.0064 60  LEU B CD1 
4563  C CD2 . LEU B 60  ? 0.2772 0.3149 0.2276 0.0575  -0.0097 -0.0075 60  LEU B CD2 
4564  N N   . ILE B 61  ? 0.3080 0.3617 0.2910 0.0576  -0.0036 -0.0105 61  ILE B N   
4565  C CA  . ILE B 61  ? 0.2925 0.3501 0.2839 0.0627  -0.0018 -0.0109 61  ILE B CA  
4566  C C   . ILE B 61  ? 0.2825 0.3376 0.2764 0.0608  0.0070  -0.0108 61  ILE B C   
4567  O O   . ILE B 61  ? 0.3406 0.3919 0.3323 0.0642  0.0112  -0.0105 61  ILE B O   
4568  C CB  . ILE B 61  ? 0.3054 0.3739 0.3120 0.0657  -0.0083 -0.0129 61  ILE B CB  
4569  C CG1 . ILE B 61  ? 0.3054 0.3736 0.3051 0.0686  -0.0165 -0.0131 61  ILE B CG1 
4570  C CG2 . ILE B 61  ? 0.2701 0.3432 0.2887 0.0711  -0.0070 -0.0137 61  ILE B CG2 
4571  C CD1 . ILE B 61  ? 0.3559 0.4328 0.3679 0.0714  -0.0248 -0.0155 61  ILE B CD1 
4572  N N   . ASP B 62  ? 0.2863 0.3418 0.2830 0.0552  0.0102  -0.0112 62  ASP B N   
4573  C CA  . ASP B 62  ? 0.3584 0.4098 0.3548 0.0530  0.0200  -0.0111 62  ASP B CA  
4574  C C   . ASP B 62  ? 0.3785 0.4171 0.3578 0.0533  0.0243  -0.0100 62  ASP B C   
4575  O O   . ASP B 62  ? 0.3427 0.3786 0.3223 0.0560  0.0311  -0.0106 62  ASP B O   
4576  C CB  . ASP B 62  ? 0.3905 0.4405 0.3867 0.0461  0.0223  -0.0108 62  ASP B CB  
4577  C CG  . ASP B 62  ? 0.4528 0.5151 0.4694 0.0455  0.0215  -0.0120 62  ASP B CG  
4578  O OD1 . ASP B 62  ? 0.4314 0.5026 0.4635 0.0501  0.0226  -0.0134 62  ASP B OD1 
4579  O OD2 . ASP B 62  ? 0.4861 0.5490 0.5042 0.0404  0.0190  -0.0117 62  ASP B OD2 
4580  N N   . GLN B 63  ? 0.4121 0.4426 0.3776 0.0509  0.0202  -0.0089 63  GLN B N   
4581  C CA  . GLN B 63  ? 0.3935 0.4113 0.3437 0.0508  0.0228  -0.0080 63  GLN B CA  
4582  C C   . GLN B 63  ? 0.3878 0.4057 0.3386 0.0569  0.0223  -0.0077 63  GLN B C   
4583  O O   . GLN B 63  ? 0.3927 0.4028 0.3371 0.0587  0.0272  -0.0078 63  GLN B O   
4584  C CB  . GLN B 63  ? 0.3169 0.3273 0.2561 0.0466  0.0176  -0.0071 63  GLN B CB  
4585  C CG  . GLN B 63  ? 0.3470 0.3534 0.2823 0.0406  0.0175  -0.0072 63  GLN B CG  
4586  C CD  . GLN B 63  ? 0.3895 0.3902 0.3177 0.0371  0.0107  -0.0069 63  GLN B CD  
4587  O OE1 . GLN B 63  ? 0.4118 0.4007 0.3282 0.0355  0.0102  -0.0065 63  GLN B OE1 
4588  N NE2 . GLN B 63  ? 0.3330 0.3419 0.2693 0.0361  0.0051  -0.0074 63  GLN B NE2 
4589  N N   . ILE B 64  ? 0.3866 0.4117 0.3432 0.0602  0.0161  -0.0073 64  ILE B N   
4590  C CA  . ILE B 64  ? 0.3509 0.3744 0.3067 0.0660  0.0153  -0.0065 64  ILE B CA  
4591  C C   . ILE B 64  ? 0.3612 0.3874 0.3260 0.0702  0.0203  -0.0079 64  ILE B C   
4592  O O   . ILE B 64  ? 0.3795 0.3984 0.3391 0.0732  0.0236  -0.0077 64  ILE B O   
4593  C CB  . ILE B 64  ? 0.3975 0.4274 0.3569 0.0693  0.0081  -0.0059 64  ILE B CB  
4594  C CG1 . ILE B 64  ? 0.3804 0.4062 0.3301 0.0658  0.0050  -0.0046 64  ILE B CG1 
4595  C CG2 . ILE B 64  ? 0.4479 0.4757 0.4069 0.0760  0.0068  -0.0049 64  ILE B CG2 
4596  C CD1 . ILE B 64  ? 0.3561 0.3861 0.3059 0.0687  -0.0008 -0.0042 64  ILE B CD1 
4597  N N   . GLN B 65  ? 0.3289 0.3653 0.3084 0.0702  0.0214  -0.0097 65  GLN B N   
4598  C CA  . GLN B 65  ? 0.3205 0.3613 0.3125 0.0741  0.0269  -0.0115 65  GLN B CA  
4599  C C   . GLN B 65  ? 0.3739 0.4047 0.3565 0.0723  0.0366  -0.0121 65  GLN B C   
4600  O O   . GLN B 65  ? 0.3860 0.4141 0.3707 0.0771  0.0408  -0.0132 65  GLN B O   
4601  C CB  . GLN B 65  ? 0.3316 0.3854 0.3429 0.0729  0.0270  -0.0133 65  GLN B CB  
4602  C CG  . GLN B 65  ? 0.3563 0.4201 0.3805 0.0775  0.0171  -0.0139 65  GLN B CG  
4603  C CD  . GLN B 65  ? 0.4445 0.5209 0.4891 0.0758  0.0159  -0.0159 65  GLN B CD  
4604  O OE1 . GLN B 65  ? 0.4554 0.5329 0.4994 0.0696  0.0175  -0.0156 65  GLN B OE1 
4605  N NE2 . GLN B 65  ? 0.5282 0.6138 0.5919 0.0813  0.0123  -0.0179 65  GLN B NE2 
4606  N N   . GLU B 66  ? 0.3845 0.4083 0.3557 0.0659  0.0399  -0.0115 66  GLU B N   
4607  C CA  . GLU B 66  ? 0.4181 0.4301 0.3770 0.0641  0.0487  -0.0122 66  GLU B CA  
4608  C C   . GLU B 66  ? 0.4122 0.4119 0.3571 0.0669  0.0476  -0.0117 66  GLU B C   
4609  O O   . GLU B 66  ? 0.4275 0.4208 0.3691 0.0700  0.0542  -0.0132 66  GLU B O   
4610  C CB  . GLU B 66  ? 0.4238 0.4285 0.3708 0.0567  0.0503  -0.0113 66  GLU B CB  
4611  C CG  . GLU B 66  ? 0.5190 0.5142 0.4572 0.0548  0.0614  -0.0125 66  GLU B CG  
4612  C CD  . GLU B 66  ? 0.5929 0.5777 0.5157 0.0476  0.0623  -0.0113 66  GLU B CD  
4613  O OE1 . GLU B 66  ? 0.6303 0.6004 0.5360 0.0460  0.0692  -0.0118 66  GLU B OE1 
4614  O OE2 . GLU B 66  ? 0.5949 0.5851 0.5219 0.0439  0.0559  -0.0100 66  GLU B OE2 
4615  N N   . TYR B 67  ? 0.3897 0.3859 0.3269 0.0659  0.0398  -0.0097 67  TYR B N   
4616  C CA  . TYR B 67  ? 0.4346 0.4195 0.3607 0.0682  0.0385  -0.0089 67  TYR B CA  
4617  C C   . TYR B 67  ? 0.4327 0.4211 0.3675 0.0755  0.0387  -0.0093 67  TYR B C   
4618  O O   . TYR B 67  ? 0.4415 0.4203 0.3697 0.0784  0.0416  -0.0099 67  TYR B O   
4619  C CB  . TYR B 67  ? 0.3802 0.3624 0.2999 0.0654  0.0310  -0.0066 67  TYR B CB  
4620  C CG  . TYR B 67  ? 0.3810 0.3539 0.2887 0.0589  0.0299  -0.0064 67  TYR B CG  
4621  C CD1 . TYR B 67  ? 0.4113 0.3689 0.3052 0.0575  0.0306  -0.0067 67  TYR B CD1 
4622  C CD2 . TYR B 67  ? 0.3838 0.3623 0.2943 0.0544  0.0269  -0.0063 67  TYR B CD2 
4623  C CE1 . TYR B 67  ? 0.3997 0.3478 0.2830 0.0518  0.0278  -0.0068 67  TYR B CE1 
4624  C CE2 . TYR B 67  ? 0.3816 0.3508 0.2818 0.0489  0.0245  -0.0062 67  TYR B CE2 
4625  C CZ  . TYR B 67  ? 0.4286 0.3826 0.3153 0.0477  0.0247  -0.0065 67  TYR B CZ  
4626  O OH  . TYR B 67  ? 0.4203 0.3643 0.2972 0.0425  0.0206  -0.0067 67  TYR B OH  
4627  N N   . ALA B 68  ? 0.4379 0.4392 0.3873 0.0789  0.0347  -0.0092 68  ALA B N   
4628  C CA  . ALA B 68  ? 0.4423 0.4464 0.4004 0.0863  0.0331  -0.0096 68  ALA B CA  
4629  C C   . ALA B 68  ? 0.4894 0.4937 0.4554 0.0898  0.0412  -0.0127 68  ALA B C   
4630  O O   . ALA B 68  ? 0.5603 0.5589 0.5256 0.0952  0.0420  -0.0133 68  ALA B O   
4631  C CB  . ALA B 68  ? 0.4291 0.4459 0.4008 0.0891  0.0260  -0.0092 68  ALA B CB  
4632  N N   . GLN B 69  ? 0.4726 0.4831 0.4464 0.0869  0.0477  -0.0147 69  GLN B N   
4633  C CA  . GLN B 69  ? 0.5127 0.5238 0.4946 0.0898  0.0576  -0.0180 69  GLN B CA  
4634  C C   . GLN B 69  ? 0.5298 0.5246 0.4925 0.0883  0.0650  -0.0189 69  GLN B C   
4635  O O   . GLN B 69  ? 0.6261 0.6194 0.5925 0.0906  0.0748  -0.0219 69  GLN B O   
4636  C CB  . GLN B 69  ? 0.5371 0.5600 0.5340 0.0866  0.0632  -0.0195 69  GLN B CB  
4637  C CG  . GLN B 69  ? 0.6038 0.6433 0.6240 0.0894  0.0562  -0.0198 69  GLN B CG  
4638  C CD  . GLN B 69  ? 0.7017 0.7510 0.7320 0.0835  0.0578  -0.0198 69  GLN B CD  
4639  O OE1 . GLN B 69  ? 0.7257 0.7700 0.7479 0.0778  0.0662  -0.0197 69  GLN B OE1 
4640  N NE2 . GLN B 69  ? 0.7258 0.7876 0.7729 0.0849  0.0492  -0.0199 69  GLN B NE2 
4641  N N   . GLY B 70  ? 0.5109 0.4932 0.4539 0.0847  0.0609  -0.0168 70  GLY B N   
4642  C CA  . GLY B 70  ? 0.5577 0.5231 0.4818 0.0832  0.0664  -0.0180 70  GLY B CA  
4643  C C   . GLY B 70  ? 0.5627 0.5233 0.4780 0.0779  0.0745  -0.0193 70  GLY B C   
4644  O O   . GLY B 70  ? 0.6056 0.5522 0.5061 0.0780  0.0813  -0.0213 70  GLY B O   
4645  N N   . LYS B 71  ? 0.5774 0.5476 0.4998 0.0733  0.0739  -0.0180 71  LYS B N   
4646  C CA  . LYS B 71  ? 0.5193 0.4848 0.4337 0.0681  0.0819  -0.0187 71  LYS B CA  
4647  C C   . LYS B 71  ? 0.5310 0.4861 0.4273 0.0612  0.0760  -0.0164 71  LYS B C   
4648  O O   . LYS B 71  ? 0.5238 0.4709 0.4085 0.0565  0.0814  -0.0165 71  LYS B O   
4649  C CB  . LYS B 71  ? 0.5213 0.5041 0.4580 0.0675  0.0861  -0.0190 71  LYS B CB  
4650  N N   . ALA B 72  ? 0.4962 0.4501 0.3894 0.0605  0.0653  -0.0145 72  ALA B N   
4651  C CA  . ALA B 72  ? 0.4516 0.3975 0.3319 0.0544  0.0585  -0.0128 72  ALA B CA  
4652  C C   . ALA B 72  ? 0.4967 0.4214 0.3537 0.0529  0.0589  -0.0137 72  ALA B C   
4653  O O   . ALA B 72  ? 0.5080 0.4256 0.3604 0.0563  0.0573  -0.0145 72  ALA B O   
4654  C CB  . ALA B 72  ? 0.4111 0.3649 0.2992 0.0545  0.0480  -0.0108 72  ALA B CB  
4655  N N   . LYS B 73  ? 0.5069 0.4203 0.3487 0.0479  0.0606  -0.0138 73  LYS B N   
4656  C CA  . LYS B 73  ? 0.5168 0.4080 0.3344 0.0460  0.0587  -0.0148 73  LYS B CA  
4657  C C   . LYS B 73  ? 0.5188 0.4065 0.3332 0.0417  0.0462  -0.0131 73  LYS B C   
4658  O O   . LYS B 73  ? 0.6234 0.5104 0.4349 0.0369  0.0428  -0.0119 73  LYS B O   
4659  C CB  . LYS B 73  ? 0.5280 0.4062 0.3280 0.0434  0.0674  -0.0158 73  LYS B CB  
4660  C CG  . LYS B 73  ? 0.6489 0.5294 0.4523 0.0479  0.0814  -0.0181 73  LYS B CG  
4661  C CD  . LYS B 73  ? 0.7636 0.6379 0.5567 0.0445  0.0926  -0.0181 73  LYS B CD  
4662  C CE  . LYS B 73  ? 0.8213 0.7142 0.6346 0.0413  0.0937  -0.0158 73  LYS B CE  
4663  N NZ  . LYS B 73  ? 0.8017 0.7166 0.6440 0.0461  0.0989  -0.0167 73  LYS B NZ  
4664  N N   . ASP B 74  ? 0.4465 0.3325 0.2632 0.0433  0.0394  -0.0130 74  ASP B N   
4665  C CA  . ASP B 74  ? 0.4244 0.3103 0.2437 0.0398  0.0283  -0.0116 74  ASP B CA  
4666  C C   . ASP B 74  ? 0.4581 0.3224 0.2586 0.0378  0.0229  -0.0131 74  ASP B C   
4667  O O   . ASP B 74  ? 0.4642 0.3206 0.2605 0.0407  0.0231  -0.0142 74  ASP B O   
4668  C CB  . ASP B 74  ? 0.4552 0.3549 0.2919 0.0427  0.0254  -0.0102 74  ASP B CB  
4669  C CG  . ASP B 74  ? 0.5170 0.4184 0.3591 0.0392  0.0159  -0.0089 74  ASP B CG  
4670  O OD1 . ASP B 74  ? 0.5231 0.4106 0.3551 0.0359  0.0098  -0.0097 74  ASP B OD1 
4671  O OD2 . ASP B 74  ? 0.4919 0.4084 0.3488 0.0401  0.0144  -0.0074 74  ASP B OD2 
4672  N N   . VAL B 75  ? 0.4953 0.3489 0.2843 0.0331  0.0170  -0.0132 75  VAL B N   
4673  C CA  . VAL B 75  ? 0.5700 0.4002 0.3382 0.0316  0.0116  -0.0151 75  VAL B CA  
4674  C C   . VAL B 75  ? 0.5426 0.3710 0.3184 0.0313  0.0022  -0.0152 75  VAL B C   
4675  O O   . VAL B 75  ? 0.5592 0.3728 0.3244 0.0326  0.0003  -0.0170 75  VAL B O   
4676  C CB  . VAL B 75  ? 0.6659 0.4824 0.4176 0.0268  0.0066  -0.0152 75  VAL B CB  
4677  C CG1 . VAL B 75  ? 0.7387 0.5532 0.4796 0.0269  0.0178  -0.0149 75  VAL B CG1 
4678  C CG2 . VAL B 75  ? 0.6697 0.4969 0.4360 0.0232  -0.0026 -0.0136 75  VAL B CG2 
4679  N N   . PHE B 76  ? 0.5510 0.3942 0.3456 0.0295  -0.0031 -0.0135 76  PHE B N   
4680  C CA  . PHE B 76  ? 0.5604 0.4033 0.3649 0.0288  -0.0103 -0.0133 76  PHE B CA  
4681  C C   . PHE B 76  ? 0.5660 0.4128 0.3763 0.0331  -0.0048 -0.0127 76  PHE B C   
4682  O O   . PHE B 76  ? 0.5389 0.3760 0.3480 0.0330  -0.0092 -0.0133 76  PHE B O   
4683  C CB  . PHE B 76  ? 0.6250 0.4833 0.4484 0.0262  -0.0153 -0.0117 76  PHE B CB  
4684  C CG  . PHE B 76  ? 0.7703 0.6267 0.6038 0.0244  -0.0225 -0.0117 76  PHE B CG  
4685  C CD1 . PHE B 76  ? 0.8093 0.6532 0.6395 0.0205  -0.0330 -0.0135 76  PHE B CD1 
4686  C CD2 . PHE B 76  ? 0.8213 0.6869 0.6673 0.0266  -0.0188 -0.0100 76  PHE B CD2 
4687  C CE1 . PHE B 76  ? 0.8738 0.7165 0.7163 0.0186  -0.0393 -0.0137 76  PHE B CE1 
4688  C CE2 . PHE B 76  ? 0.8458 0.7092 0.7018 0.0244  -0.0241 -0.0097 76  PHE B CE2 
4689  C CZ  . PHE B 76  ? 0.8686 0.7214 0.7244 0.0203  -0.0342 -0.0117 76  PHE B CZ  
4690  N N   . LEU B 77  ? 0.5583 0.4188 0.3757 0.0370  0.0040  -0.0115 77  LEU B N   
4691  C CA  . LEU B 77  ? 0.5815 0.4439 0.4031 0.0417  0.0086  -0.0110 77  LEU B CA  
4692  C C   . LEU B 77  ? 0.5931 0.4378 0.3979 0.0442  0.0116  -0.0137 77  LEU B C   
4693  O O   . LEU B 77  ? 0.5704 0.4097 0.3756 0.0469  0.0116  -0.0138 77  LEU B O   
4694  C CB  . LEU B 77  ? 0.5404 0.4208 0.3741 0.0457  0.0157  -0.0096 77  LEU B CB  
4695  C CG  . LEU B 77  ? 0.5580 0.4430 0.3993 0.0507  0.0186  -0.0083 77  LEU B CG  
4696  C CD1 . LEU B 77  ? 0.4642 0.3491 0.3125 0.0489  0.0129  -0.0059 77  LEU B CD1 
4697  C CD2 . LEU B 77  ? 0.5927 0.4948 0.4458 0.0543  0.0235  -0.0073 77  LEU B CD2 
4698  N N   . GLU B 78  ? 0.6127 0.4472 0.4015 0.0435  0.0146  -0.0159 78  GLU B N   
4699  C CA  . GLU B 78  ? 0.6210 0.4359 0.3905 0.0459  0.0175  -0.0190 78  GLU B CA  
4700  C C   . GLU B 78  ? 0.5771 0.3742 0.3377 0.0435  0.0073  -0.0203 78  GLU B C   
4701  O O   . GLU B 78  ? 0.5806 0.3654 0.3336 0.0465  0.0077  -0.0222 78  GLU B O   
4702  C CB  . GLU B 78  ? 0.7193 0.5253 0.4712 0.0449  0.0232  -0.0207 78  GLU B CB  
4703  C CG  . GLU B 78  ? 0.8593 0.6805 0.6197 0.0478  0.0353  -0.0203 78  GLU B CG  
4704  C CD  . GLU B 78  ? 1.0239 0.8369 0.7682 0.0454  0.0414  -0.0211 78  GLU B CD  
4705  O OE1 . GLU B 78  ? 1.0928 0.8855 0.8142 0.0461  0.0447  -0.0238 78  GLU B OE1 
4706  O OE2 . GLU B 78  ? 1.0497 0.8753 0.8031 0.0427  0.0430  -0.0191 78  GLU B OE2 
4707  N N   . ALA B 79  ? 0.5860 0.3812 0.3487 0.0384  -0.0025 -0.0196 79  ALA B N   
4708  C CA  . ALA B 79  ? 0.5742 0.3545 0.3337 0.0357  -0.0135 -0.0209 79  ALA B CA  
4709  C C   . ALA B 79  ? 0.5236 0.3109 0.2999 0.0369  -0.0146 -0.0191 79  ALA B C   
4710  O O   . ALA B 79  ? 0.5253 0.2979 0.2971 0.0366  -0.0202 -0.0207 79  ALA B O   
4711  C CB  . ALA B 79  ? 0.5205 0.3008 0.2840 0.0302  -0.0238 -0.0204 79  ALA B CB  
4712  N N   . ILE B 80  ? 0.5044 0.3125 0.2994 0.0380  -0.0097 -0.0158 80  ILE B N   
4713  C CA  . ILE B 80  ? 0.4612 0.2743 0.2695 0.0393  -0.0095 -0.0136 80  ILE B CA  
4714  C C   . ILE B 80  ? 0.4474 0.2518 0.2469 0.0447  -0.0039 -0.0148 80  ILE B C   
4715  O O   . ILE B 80  ? 0.4530 0.2470 0.2523 0.0451  -0.0071 -0.0150 80  ILE B O   
4716  C CB  . ILE B 80  ? 0.4559 0.2914 0.2825 0.0397  -0.0055 -0.0098 80  ILE B CB  
4717  C CG1 . ILE B 80  ? 0.5476 0.3914 0.3848 0.0346  -0.0112 -0.0090 80  ILE B CG1 
4718  C CG2 . ILE B 80  ? 0.4722 0.3109 0.3084 0.0418  -0.0035 -0.0070 80  ILE B CG2 
4719  C CD1 . ILE B 80  ? 0.5824 0.4237 0.4310 0.0308  -0.0175 -0.0079 80  ILE B CD1 
4720  N N   . ARG B 81  ? 0.5399 0.3486 0.3335 0.0490  0.0046  -0.0159 81  ARG B N   
4721  C CA  . ARG B 81  ? 0.5799 0.3853 0.3707 0.0551  0.0111  -0.0169 81  ARG B CA  
4722  C C   . ARG B 81  ? 0.5975 0.3795 0.3696 0.0564  0.0091  -0.0210 81  ARG B C   
4723  O O   . ARG B 81  ? 0.5218 0.2967 0.2934 0.0601  0.0100  -0.0216 81  ARG B O   
4724  C CB  . ARG B 81  ? 0.6186 0.4364 0.4114 0.0592  0.0208  -0.0174 81  ARG B CB  
4725  C CG  . ARG B 81  ? 0.7026 0.5129 0.4876 0.0655  0.0284  -0.0206 81  ARG B CG  
4726  C CD  . ARG B 81  ? 0.7761 0.6046 0.5747 0.0703  0.0366  -0.0198 81  ARG B CD  
4727  N NE  . ARG B 81  ? 0.8618 0.7043 0.6665 0.0672  0.0387  -0.0186 81  ARG B NE  
4728  C CZ  . ARG B 81  ? 0.8745 0.7364 0.6961 0.0691  0.0413  -0.0166 81  ARG B CZ  
4729  N NH1 . ARG B 81  ? 0.8927 0.7617 0.7258 0.0742  0.0419  -0.0153 81  ARG B NH1 
4730  N NH2 . ARG B 81  ? 0.8515 0.7244 0.6778 0.0659  0.0425  -0.0158 81  ARG B NH2 
4731  N N   . LYS B 82  ? 0.6546 0.4231 0.4103 0.0533  0.0057  -0.0238 82  LYS B N   
4732  C CA  . LYS B 82  ? 0.6548 0.3987 0.3884 0.0547  0.0037  -0.0283 82  LYS B CA  
4733  C C   . LYS B 82  ? 0.5965 0.3283 0.3325 0.0540  -0.0048 -0.0286 82  LYS B C   
4734  O O   . LYS B 82  ? 0.5893 0.3263 0.3396 0.0495  -0.0125 -0.0258 82  LYS B O   
4735  C CB  . LYS B 82  ? 0.6944 0.4249 0.4104 0.0503  -0.0020 -0.0303 82  LYS B CB  
4736  C CG  . LYS B 82  ? 0.7752 0.5039 0.4757 0.0517  0.0072  -0.0319 82  LYS B CG  
4737  C CD  . LYS B 82  ? 0.8058 0.5131 0.4827 0.0478  -0.0005 -0.0342 82  LYS B CD  
4738  C CE  . LYS B 82  ? 0.8607 0.5663 0.5222 0.0477  0.0086  -0.0346 82  LYS B CE  
4739  N NZ  . LYS B 82  ? 0.9129 0.5948 0.5484 0.0440  0.0001  -0.0365 82  LYS B NZ  
4740  N N   . ASP B 83  ? 0.5643 0.2792 0.2866 0.0583  -0.0030 -0.0322 83  ASP B N   
4741  C CA  . ASP B 83  ? 0.6430 0.3394 0.3610 0.0567  -0.0131 -0.0339 83  ASP B CA  
4742  C C   . ASP B 83  ? 0.6777 0.3612 0.3863 0.0508  -0.0247 -0.0355 83  ASP B C   
4743  O O   . ASP B 83  ? 0.7118 0.3862 0.4011 0.0506  -0.0238 -0.0381 83  ASP B O   
4744  C CB  . ASP B 83  ? 0.7107 0.3879 0.4108 0.0627  -0.0096 -0.0387 83  ASP B CB  
4745  C CG  . ASP B 83  ? 0.7665 0.4245 0.4637 0.0614  -0.0203 -0.0405 83  ASP B CG  
4746  O OD1 . ASP B 83  ? 0.7577 0.3994 0.4440 0.0572  -0.0310 -0.0429 83  ASP B OD1 
4747  O OD2 . ASP B 83  ? 0.8372 0.4955 0.5433 0.0645  -0.0187 -0.0395 83  ASP B OD2 
4748  N N   . PRO B 84  ? 0.6857 0.3677 0.4076 0.0458  -0.0357 -0.0340 84  PRO B N   
4749  C CA  . PRO B 84  ? 0.6989 0.3716 0.4167 0.0401  -0.0479 -0.0354 84  PRO B CA  
4750  C C   . PRO B 84  ? 0.6567 0.3013 0.3444 0.0411  -0.0540 -0.0411 84  PRO B C   
4751  O O   . PRO B 84  ? 0.6797 0.3164 0.3580 0.0376  -0.0620 -0.0423 84  PRO B O   
4752  C CB  . PRO B 84  ? 0.7216 0.3957 0.4610 0.0356  -0.0575 -0.0334 84  PRO B CB  
4753  C CG  . PRO B 84  ? 0.6840 0.3764 0.4421 0.0379  -0.0479 -0.0288 84  PRO B CG  
4754  C CD  . PRO B 84  ? 0.7019 0.3910 0.4445 0.0450  -0.0372 -0.0306 84  PRO B CD  
4755  N N   . ASP B 85  ? 0.6689 0.2967 0.3400 0.0460  -0.0509 -0.0447 85  ASP B N   
4756  C CA  . ASP B 85  ? 0.7292 0.3280 0.3680 0.0474  -0.0561 -0.0505 85  ASP B CA  
4757  C C   . ASP B 85  ? 0.7202 0.3177 0.3378 0.0494  -0.0466 -0.0514 85  ASP B C   
4758  O O   . ASP B 85  ? 0.7149 0.2887 0.3039 0.0492  -0.0517 -0.0554 85  ASP B O   
4759  C CB  . ASP B 85  ? 0.8351 0.4160 0.4615 0.0526  -0.0546 -0.0545 85  ASP B CB  
4760  C CG  . ASP B 85  ? 0.8420 0.4161 0.4837 0.0498  -0.0670 -0.0544 85  ASP B CG  
4761  O OD1 . ASP B 85  ? 0.8695 0.4457 0.5252 0.0435  -0.0791 -0.0529 85  ASP B OD1 
4762  O OD2 . ASP B 85  ? 0.7952 0.3621 0.4362 0.0537  -0.0644 -0.0560 85  ASP B OD2 
4763  N N   . ASP B 86  ? 0.7293 0.3504 0.3594 0.0510  -0.0332 -0.0479 86  ASP B N   
4764  C CA  . ASP B 86  ? 0.7542 0.3770 0.3688 0.0518  -0.0236 -0.0481 86  ASP B CA  
4765  C C   . ASP B 86  ? 0.7008 0.3347 0.3239 0.0460  -0.0292 -0.0446 86  ASP B C   
4766  O O   . ASP B 86  ? 0.6818 0.3167 0.2928 0.0456  -0.0223 -0.0441 86  ASP B O   
4767  C CB  . ASP B 86  ? 0.7602 0.4023 0.3853 0.0568  -0.0064 -0.0466 86  ASP B CB  
4768  C CG  . ASP B 86  ? 0.7868 0.4190 0.4054 0.0634  -0.0003 -0.0503 86  ASP B CG  
4769  O OD1 . ASP B 86  ? 0.8061 0.4121 0.4024 0.0647  -0.0062 -0.0550 86  ASP B OD1 
4770  O OD2 . ASP B 86  ? 0.8123 0.4627 0.4482 0.0674  0.0099  -0.0487 86  ASP B OD2 
4771  N N   . LEU B 87  ? 0.6225 0.2648 0.2669 0.0415  -0.0409 -0.0423 87  LEU B N   
4772  C CA  . LEU B 87  ? 0.6102 0.2642 0.2657 0.0364  -0.0466 -0.0394 87  LEU B CA  
4773  C C   . LEU B 87  ? 0.6614 0.2921 0.2901 0.0339  -0.0558 -0.0420 87  LEU B C   
4774  O O   . LEU B 87  ? 0.6873 0.2928 0.2983 0.0337  -0.0667 -0.0459 87  LEU B O   
4775  C CB  . LEU B 87  ? 0.5698 0.2355 0.2538 0.0323  -0.0570 -0.0372 87  LEU B CB  
4776  C CG  . LEU B 87  ? 0.5593 0.2525 0.2714 0.0334  -0.0479 -0.0329 87  LEU B CG  
4777  C CD1 . LEU B 87  ? 0.5358 0.2354 0.2726 0.0295  -0.0571 -0.0312 87  LEU B CD1 
4778  C CD2 . LEU B 87  ? 0.5383 0.2527 0.2590 0.0329  -0.0400 -0.0297 87  LEU B CD2 
4779  N N   . GLU B 88  ? 0.6584 0.2966 0.2840 0.0319  -0.0524 -0.0399 88  GLU B N   
4780  C CA  . GLU B 88  ? 0.6743 0.2917 0.2777 0.0288  -0.0634 -0.0414 88  GLU B CA  
4781  C C   . GLU B 88  ? 0.6286 0.2513 0.2533 0.0240  -0.0799 -0.0405 88  GLU B C   
4782  O O   . GLU B 88  ? 0.6157 0.2625 0.2725 0.0226  -0.0792 -0.0378 88  GLU B O   
4783  C CB  . GLU B 88  ? 0.6767 0.2985 0.2683 0.0282  -0.0536 -0.0391 88  GLU B CB  
4784  C CG  . GLU B 88  ? 0.7486 0.3712 0.3270 0.0327  -0.0350 -0.0396 88  GLU B CG  
4785  C CD  . GLU B 88  ? 0.8573 0.4929 0.4358 0.0316  -0.0232 -0.0364 88  GLU B CD  
4786  O OE1 . GLU B 88  ? 0.9173 0.5546 0.4871 0.0350  -0.0072 -0.0368 88  GLU B OE1 
4787  O OE2 . GLU B 88  ? 0.8694 0.5135 0.4577 0.0274  -0.0299 -0.0336 88  GLU B OE2 
4788  N N   . LYS B 89  ? 0.4824 0.2803 0.2193 -0.0022 -0.0381 -0.0011 89  LYS B N   
4789  C CA  . LYS B 89  ? 0.5996 0.4009 0.3420 0.0130  -0.0487 -0.0017 89  LYS B CA  
4790  C C   . LYS B 89  ? 0.5838 0.3715 0.3152 0.0133  -0.0405 0.0003  89  LYS B C   
4791  O O   . LYS B 89  ? 0.5726 0.3802 0.3260 0.0194  -0.0444 -0.0010 89  LYS B O   
4792  C CB  . LYS B 89  ? 0.5524 0.3299 0.2666 0.0300  -0.0615 -0.0028 89  LYS B CB  
4793  C CG  . LYS B 89  ? 0.6103 0.4024 0.3367 0.0323  -0.0725 -0.0058 89  LYS B CG  
4794  C CD  . LYS B 89  ? 0.6662 0.4344 0.3638 0.0519  -0.0870 -0.0080 89  LYS B CD  
4795  C CE  . LYS B 89  ? 0.7692 0.5495 0.4764 0.0549  -0.0990 -0.0117 89  LYS B CE  
4796  N NZ  . LYS B 89  ? 0.7905 0.5782 0.5053 0.0380  -0.0897 -0.0101 89  LYS B NZ  
4797  N N   . GLU B 90  ? 0.5931 0.3463 0.2895 0.0061  -0.0287 0.0030  90  GLU B N   
4798  C CA  . GLU B 90  ? 0.6706 0.4066 0.3533 0.0049  -0.0207 0.0047  90  GLU B CA  
4799  C C   . GLU B 90  ? 0.6484 0.4175 0.3681 -0.0058 -0.0138 0.0037  90  GLU B C   
4800  O O   . GLU B 90  ? 0.6100 0.3804 0.3338 -0.0009 -0.0132 0.0038  90  GLU B O   
4801  C CB  . GLU B 90  ? 0.7974 0.4903 0.4360 -0.0056 -0.0074 0.0071  90  GLU B CB  
4802  C CG  . GLU B 90  ? 0.9764 0.6822 0.6253 -0.0269 0.0061  0.0055  90  GLU B CG  
4803  C CD  . GLU B 90  ? 1.1834 0.8638 0.8078 -0.0431 0.0231  0.0056  90  GLU B CD  
4804  O OE1 . GLU B 90  ? 1.1690 0.8739 0.8189 -0.0567 0.0319  0.0024  90  GLU B OE1 
4805  O OE2 . GLU B 90  ? 1.2983 0.9329 0.8762 -0.0426 0.0275  0.0083  90  GLU B OE2 
4806  N N   . GLU B 91  ? 0.5994 0.3944 0.3442 -0.0186 -0.0097 0.0021  91  GLU B N   
4807  C CA  . GLU B 91  ? 0.5075 0.3303 0.2831 -0.0277 -0.0041 0.0008  91  GLU B CA  
4808  C C   . GLU B 91  ? 0.5090 0.3621 0.3168 -0.0193 -0.0136 0.0003  91  GLU B C   
4809  O O   . GLU B 91  ? 0.5587 0.4250 0.3820 -0.0203 -0.0102 0.0003  91  GLU B O   
4810  C CB  . GLU B 91  ? 0.5624 0.3999 0.3501 -0.0419 0.0022  -0.0020 91  GLU B CB  
4811  C CG  . GLU B 91  ? 0.5939 0.4085 0.3545 -0.0535 0.0146  -0.0035 91  GLU B CG  
4812  C CD  . GLU B 91  ? 0.5969 0.4323 0.3728 -0.0656 0.0201  -0.0089 91  GLU B CD  
4813  O OE1 . GLU B 91  ? 0.5854 0.4340 0.3714 -0.0627 0.0129  -0.0101 91  GLU B OE1 
4814  O OE2 . GLU B 91  ? 0.6172 0.4566 0.3955 -0.0772 0.0308  -0.0129 91  GLU B OE2 
4815  N N   . VAL B 92  ? 0.4753 0.3402 0.2931 -0.0118 -0.0251 -0.0007 92  VAL B N   
4816  C CA  . VAL B 92  ? 0.4808 0.3747 0.3282 -0.0052 -0.0334 -0.0023 92  VAL B CA  
4817  C C   . VAL B 92  ? 0.4570 0.3452 0.2974 0.0083  -0.0358 -0.0030 92  VAL B C   
4818  O O   . VAL B 92  ? 0.4376 0.3469 0.2992 0.0090  -0.0338 -0.0039 92  VAL B O   
4819  C CB  . VAL B 92  ? 0.4772 0.3835 0.3353 -0.0005 -0.0459 -0.0048 92  VAL B CB  
4820  C CG1 . VAL B 92  ? 0.4574 0.3968 0.3482 0.0032  -0.0528 -0.0079 92  VAL B CG1 
4821  C CG2 . VAL B 92  ? 0.5053 0.4160 0.3689 -0.0125 -0.0441 -0.0046 92  VAL B CG2 
4822  N N   . GLU B 93  ? 0.4959 0.3537 0.3036 0.0203  -0.0402 -0.0029 93  GLU B N   
4823  C CA  . GLU B 93  ? 0.5279 0.3765 0.3243 0.0359  -0.0440 -0.0045 93  GLU B CA  
4824  C C   . GLU B 93  ? 0.5673 0.4116 0.3627 0.0294  -0.0323 -0.0024 93  GLU B C   
4825  O O   . GLU B 93  ? 0.5043 0.3677 0.3169 0.0366  -0.0335 -0.0046 93  GLU B O   
4826  C CB  . GLU B 93  ? 0.6203 0.4264 0.3719 0.0494  -0.0500 -0.0041 93  GLU B CB  
4827  C CG  . GLU B 93  ? 0.7603 0.5737 0.5136 0.0655  -0.0665 -0.0087 93  GLU B CG  
4828  C CD  . GLU B 93  ? 0.9172 0.6828 0.6207 0.0754  -0.0713 -0.0073 93  GLU B CD  
4829  O OE1 . GLU B 93  ? 0.9543 0.7206 0.6553 0.0799  -0.0806 -0.0092 93  GLU B OE1 
4830  O OE2 . GLU B 93  ? 0.9861 0.7106 0.6500 0.0783  -0.0657 -0.0042 93  GLU B OE2 
4831  N N   . LYS B 94  ? 0.5724 0.3950 0.3501 0.0150  -0.0207 0.0007  94  LYS B N   
4832  C CA  . LYS B 94  ? 0.5538 0.3708 0.3293 0.0081  -0.0103 0.0017  94  LYS B CA  
4833  C C   . LYS B 94  ? 0.5343 0.3902 0.3490 0.0026  -0.0078 0.0006  94  LYS B C   
4834  O O   . LYS B 94  ? 0.4946 0.3541 0.3133 0.0058  -0.0044 0.0001  94  LYS B O   
4835  C CB  . LYS B 94  ? 0.6521 0.4452 0.4066 -0.0085 0.0015  0.0031  94  LYS B CB  
4836  C CG  . LYS B 94  ? 0.7999 0.5443 0.5066 -0.0052 0.0038  0.0048  94  LYS B CG  
4837  C CD  . LYS B 94  ? 0.8685 0.5926 0.5571 -0.0249 0.0184  0.0048  94  LYS B CD  
4838  C CE  . LYS B 94  ? 0.9983 0.6683 0.6343 -0.0243 0.0223  0.0070  94  LYS B CE  
4839  N NZ  . LYS B 94  ? 1.0719 0.7199 0.6910 -0.0346 0.0330  0.0064  94  LYS B NZ  
4840  N N   . LEU B 95  ? 0.4518 0.3337 0.2921 -0.0054 -0.0095 0.0001  95  LEU B N   
4841  C CA  . LEU B 95  ? 0.4679 0.3815 0.3402 -0.0113 -0.0071 -0.0005 95  LEU B CA  
4842  C C   . LEU B 95  ? 0.4397 0.3758 0.3304 0.0002  -0.0129 -0.0025 95  LEU B C   
4843  O O   . LEU B 95  ? 0.3982 0.3494 0.3030 -0.0005 -0.0080 -0.0028 95  LEU B O   
4844  C CB  . LEU B 95  ? 0.5450 0.4742 0.4337 -0.0217 -0.0088 -0.0006 95  LEU B CB  
4845  C CG  . LEU B 95  ? 0.6901 0.6441 0.6045 -0.0293 -0.0060 -0.0007 95  LEU B CG  
4846  C CD1 . LEU B 95  ? 0.7087 0.6559 0.6179 -0.0353 0.0036  -0.0006 95  LEU B CD1 
4847  C CD2 . LEU B 95  ? 0.7372 0.7008 0.6623 -0.0374 -0.0100 -0.0012 95  LEU B CD2 
4848  N N   . ILE B 96  ? 0.4126 0.3528 0.3037 0.0112  -0.0235 -0.0049 96  ILE B N   
4849  C CA  . ILE B 96  ? 0.4836 0.4482 0.3927 0.0240  -0.0299 -0.0095 96  ILE B CA  
4850  C C   . ILE B 96  ? 0.5137 0.4650 0.4066 0.0368  -0.0278 -0.0106 96  ILE B C   
4851  O O   . ILE B 96  ? 0.4917 0.4664 0.4032 0.0406  -0.0253 -0.0132 96  ILE B O   
4852  C CB  . ILE B 96  ? 0.4640 0.4330 0.3733 0.0350  -0.0434 -0.0137 96  ILE B CB  
4853  C CG1 . ILE B 96  ? 0.4415 0.4321 0.3744 0.0227  -0.0464 -0.0141 96  ILE B CG1 
4854  C CG2 . ILE B 96  ? 0.5070 0.4966 0.4277 0.0530  -0.0514 -0.0210 96  ILE B CG2 
4855  C CD1 . ILE B 96  ? 0.4571 0.4431 0.3833 0.0308  -0.0593 -0.0174 96  ILE B CD1 
4856  N N   . GLU B 97  ? 0.5379 0.4493 0.3934 0.0435  -0.0287 -0.0088 97  GLU B N   
4857  C CA  . GLU B 97  ? 0.5623 0.4542 0.3967 0.0563  -0.0277 -0.0099 97  GLU B CA  
4858  C C   . GLU B 97  ? 0.4972 0.3949 0.3404 0.0462  -0.0160 -0.0079 97  GLU B C   
4859  O O   . GLU B 97  ? 0.4921 0.3996 0.3404 0.0564  -0.0155 -0.0106 97  GLU B O   
4860  C CB  . GLU B 97  ? 0.7600 0.6001 0.5465 0.0614  -0.0291 -0.0074 97  GLU B CB  
4861  C CG  . GLU B 97  ? 0.9265 0.7523 0.6960 0.0715  -0.0405 -0.0088 97  GLU B CG  
4862  C CD  . GLU B 97  ? 1.0904 0.8631 0.8119 0.0672  -0.0369 -0.0043 97  GLU B CD  
4863  O OE1 . GLU B 97  ? 1.0706 0.8257 0.7723 0.0743  -0.0450 -0.0046 97  GLU B OE1 
4864  O OE2 . GLU B 97  ? 1.1535 0.9017 0.8563 0.0559  -0.0256 -0.0010 97  GLU B OE2 
4865  N N   . PHE B 98  ? 0.4611 0.3539 0.3058 0.0276  -0.0071 -0.0041 98  PHE B N   
4866  C CA  . PHE B 98  ? 0.4790 0.3775 0.3318 0.0186  0.0027  -0.0031 98  PHE B CA  
4867  C C   . PHE B 98  ? 0.4558 0.3933 0.3420 0.0199  0.0036  -0.0049 98  PHE B C   
4868  O O   . PHE B 98  ? 0.4823 0.4248 0.3708 0.0246  0.0079  -0.0060 98  PHE B O   
4869  C CB  . PHE B 98  ? 0.4752 0.3674 0.3274 0.0001  0.0097  -0.0010 98  PHE B CB  
4870  C CG  . PHE B 98  ? 0.4454 0.3354 0.2982 -0.0083 0.0186  -0.0013 98  PHE B CG  
4871  C CD1 . PHE B 98  ? 0.5426 0.4021 0.3687 -0.0095 0.0233  -0.0018 98  PHE B CD1 
4872  C CD2 . PHE B 98  ? 0.4910 0.4066 0.3684 -0.0153 0.0218  -0.0015 98  PHE B CD2 
4873  C CE1 . PHE B 98  ? 0.5860 0.4447 0.4137 -0.0170 0.0305  -0.0033 98  PHE B CE1 
4874  C CE2 . PHE B 98  ? 0.5178 0.4306 0.3941 -0.0212 0.0286  -0.0026 98  PHE B CE2 
4875  C CZ  . PHE B 98  ? 0.5312 0.4175 0.3844 -0.0218 0.0326  -0.0040 98  PHE B CZ  
4876  N N   . THR B 99  ? 0.3848 0.3488 0.2953 0.0150  0.0000  -0.0055 99  THR B N   
4877  C CA  . THR B 99  ? 0.4348 0.4348 0.3755 0.0132  0.0022  -0.0073 99  THR B CA  
4878  C C   . THR B 99  ? 0.4571 0.4724 0.4035 0.0301  -0.0009 -0.0125 99  THR B C   
4879  O O   . THR B 99  ? 0.4742 0.5060 0.4318 0.0310  0.0057  -0.0137 99  THR B O   
4880  C CB  . THR B 99  ? 0.4382 0.4591 0.3998 0.0050  -0.0025 -0.0079 99  THR B CB  
4881  O OG1 . THR B 99  ? 0.4218 0.4286 0.3769 -0.0087 -0.0002 -0.0041 99  THR B OG1 
4882  C CG2 . THR B 99  ? 0.4159 0.4721 0.4067 -0.0002 0.0015  -0.0100 99  THR B CG2 
4883  N N   . LYS B 100 ? 0.4281 0.4381 0.3654 0.0450  -0.0113 -0.0164 100 LYS B N   
4884  C CA  . LYS B 100 ? 0.4692 0.4943 0.4104 0.0647  -0.0164 -0.0234 100 LYS B CA  
4885  C C   . LYS B 100 ? 0.4705 0.4736 0.3897 0.0732  -0.0113 -0.0226 100 LYS B C   
4886  O O   . LYS B 100 ? 0.4044 0.4282 0.3340 0.0851  -0.0106 -0.0280 100 LYS B O   
4887  C CB  . LYS B 100 ? 0.5091 0.5239 0.4365 0.0817  -0.0305 -0.0281 100 LYS B CB  
4888  C CG  . LYS B 100 ? 0.5768 0.6305 0.5356 0.0826  -0.0385 -0.0346 100 LYS B CG  
4889  C CD  . LYS B 100 ? 0.6292 0.6669 0.5694 0.0999  -0.0538 -0.0392 100 LYS B CD  
4890  C CE  . LYS B 100 ? 0.6440 0.7230 0.6179 0.1007  -0.0628 -0.0474 100 LYS B CE  
4891  N NZ  . LYS B 100 ? 0.6326 0.6900 0.5863 0.1109  -0.0769 -0.0491 100 LYS B NZ  
4892  N N   . LEU B 101 ? 0.4616 0.4235 0.3501 0.0675  -0.0079 -0.0171 101 LEU B N   
4893  C CA  . LEU B 101 ? 0.4902 0.4282 0.3562 0.0736  -0.0033 -0.0166 101 LEU B CA  
4894  C C   . LEU B 101 ? 0.4121 0.3738 0.2991 0.0657  0.0069  -0.0162 101 LEU B C   
4895  O O   . LEU B 101 ? 0.4116 0.3728 0.2927 0.0769  0.0089  -0.0190 101 LEU B O   
4896  C CB  . LEU B 101 ? 0.5256 0.4174 0.3575 0.0642  -0.0001 -0.0116 101 LEU B CB  
4897  C CG  . LEU B 101 ? 0.5587 0.4208 0.3657 0.0646  0.0058  -0.0108 101 LEU B CG  
4898  C CD1 . LEU B 101 ? 0.6121 0.4538 0.3935 0.0879  -0.0018 -0.0148 101 LEU B CD1 
4899  C CD2 . LEU B 101 ? 0.5507 0.3767 0.3327 0.0483  0.0109  -0.0069 101 LEU B CD2 
4900  N N   . ASN B 102 ? 0.3995 0.3797 0.3080 0.0477  0.0130  -0.0129 102 ASN B N   
4901  C CA  . ASN B 102 ? 0.3999 0.3947 0.3217 0.0386  0.0229  -0.0115 102 ASN B CA  
4902  C C   . ASN B 102 ? 0.4097 0.4468 0.3634 0.0369  0.0259  -0.0141 102 ASN B C   
4903  O O   . ASN B 102 ? 0.3302 0.3789 0.2925 0.0302  0.0348  -0.0130 102 ASN B O   
4904  C CB  . ASN B 102 ? 0.4149 0.3968 0.3337 0.0202  0.0276  -0.0069 102 ASN B CB  
4905  C CG  . ASN B 102 ? 0.4815 0.4261 0.3716 0.0182  0.0282  -0.0057 102 ASN B CG  
4906  O OD1 . ASN B 102 ? 0.5050 0.4343 0.3804 0.0233  0.0314  -0.0068 102 ASN B OD1 
4907  N ND2 . ASN B 102 ? 0.3789 0.3085 0.2604 0.0100  0.0257  -0.0042 102 ASN B ND2 
4908  N N   . TYR B 103 ? 0.3675 0.4267 0.3367 0.0433  0.0187  -0.0185 103 TYR B N   
4909  C CA  . TYR B 103 ? 0.4250 0.5243 0.4266 0.0354  0.0211  -0.0213 103 TYR B CA  
4910  C C   . TYR B 103 ? 0.3940 0.5204 0.4106 0.0367  0.0310  -0.0244 103 TYR B C   
4911  O O   . TYR B 103 ? 0.3916 0.5415 0.4282 0.0223  0.0387  -0.0238 103 TYR B O   
4912  C CB  . TYR B 103 ? 0.4331 0.5505 0.4464 0.0462  0.0097  -0.0280 103 TYR B CB  
4913  C CG  . TYR B 103 ? 0.4422 0.6050 0.4909 0.0394  0.0111  -0.0338 103 TYR B CG  
4914  C CD1 . TYR B 103 ? 0.5107 0.6809 0.5731 0.0209  0.0116  -0.0309 103 TYR B CD1 
4915  C CD2 . TYR B 103 ? 0.5000 0.6988 0.5681 0.0511  0.0121  -0.0433 103 TYR B CD2 
4916  C CE1 . TYR B 103 ? 0.5372 0.7475 0.6311 0.0120  0.0135  -0.0368 103 TYR B CE1 
4917  C CE2 . TYR B 103 ? 0.5508 0.7945 0.6534 0.0424  0.0147  -0.0502 103 TYR B CE2 
4918  C CZ  . TYR B 103 ? 0.5769 0.8251 0.6918 0.0218  0.0157  -0.0466 103 TYR B CZ  
4919  O OH  . TYR B 103 ? 0.6694 0.9609 0.8177 0.0109  0.0190  -0.0540 103 TYR B OH  
4920  N N   . GLU B 104 ? 0.3708 0.4934 0.3764 0.0539  0.0309  -0.0283 104 GLU B N   
4921  C CA  . GLU B 104 ? 0.4105 0.5622 0.4306 0.0580  0.0399  -0.0330 104 GLU B CA  
4922  C C   . GLU B 104 ? 0.3934 0.5268 0.3990 0.0510  0.0507  -0.0272 104 GLU B C   
4923  O O   . GLU B 104 ? 0.3924 0.5469 0.4069 0.0527  0.0600  -0.0300 104 GLU B O   
4924  C CB  . GLU B 104 ? 0.4681 0.6292 0.4847 0.0835  0.0330  -0.0422 104 GLU B CB  
4925  C CG  . GLU B 104 ? 0.5941 0.7726 0.6225 0.0948  0.0201  -0.0498 104 GLU B CG  
4926  C CD  . GLU B 104 ? 0.6957 0.9285 0.7646 0.0871  0.0236  -0.0574 104 GLU B CD  
4927  O OE1 . GLU B 104 ? 0.7274 0.9868 0.8132 0.0780  0.0369  -0.0586 104 GLU B OE1 
4928  O OE2 . GLU B 104 ? 0.7482 0.9966 0.8308 0.0897  0.0134  -0.0628 104 GLU B OE2 
4929  N N   . LYS B 105 ? 0.3650 0.4613 0.3487 0.0433  0.0497  -0.0203 105 LYS B N   
4930  C CA  . LYS B 105 ? 0.3747 0.4534 0.3446 0.0370  0.0581  -0.0161 105 LYS B CA  
4931  C C   . LYS B 105 ? 0.3527 0.4482 0.3372 0.0198  0.0674  -0.0128 105 LYS B C   
4932  O O   . LYS B 105 ? 0.4006 0.5047 0.3977 0.0077  0.0655  -0.0110 105 LYS B O   
4933  C CB  . LYS B 105 ? 0.3478 0.3870 0.2937 0.0327  0.0537  -0.0119 105 LYS B CB  
4934  C CG  . LYS B 105 ? 0.3593 0.3740 0.2838 0.0475  0.0461  -0.0144 105 LYS B CG  
4935  C CD  . LYS B 105 ? 0.3663 0.3438 0.2679 0.0400  0.0436  -0.0112 105 LYS B CD  
4936  C CE  . LYS B 105 ? 0.4367 0.3855 0.3125 0.0534  0.0368  -0.0134 105 LYS B CE  
4937  N NZ  . LYS B 105 ? 0.4708 0.3830 0.3230 0.0433  0.0368  -0.0111 105 LYS B NZ  
4938  N N   . PRO B 106 ? 0.3798 0.4774 0.3599 0.0188  0.0773  -0.0121 106 PRO B N   
4939  C CA  . PRO B 106 ? 0.3251 0.4318 0.3122 0.0023  0.0866  -0.0085 106 PRO B CA  
4940  C C   . PRO B 106 ? 0.3146 0.3984 0.2929 -0.0115 0.0829  -0.0030 106 PRO B C   
4941  O O   . PRO B 106 ? 0.3111 0.4028 0.2975 -0.0255 0.0863  -0.0006 106 PRO B O   
4942  C CB  . PRO B 106 ? 0.3959 0.4967 0.3694 0.0071  0.0961  -0.0084 106 PRO B CB  
4943  C CG  . PRO B 106 ? 0.4029 0.5125 0.3763 0.0262  0.0939  -0.0144 106 PRO B CG  
4944  C CD  . PRO B 106 ? 0.3776 0.4707 0.3454 0.0337  0.0806  -0.0153 106 PRO B CD  
4945  N N   . ILE B 107 ? 0.3393 0.3949 0.3004 -0.0083 0.0761  -0.0019 107 ILE B N   
4946  C CA  . ILE B 107 ? 0.3877 0.4257 0.3422 -0.0196 0.0720  0.0013  107 ILE B CA  
4947  C C   . ILE B 107 ? 0.4257 0.4731 0.3939 -0.0261 0.0654  0.0018  107 ILE B C   
4948  O O   . ILE B 107 ? 0.3819 0.4192 0.3471 -0.0361 0.0624  0.0040  107 ILE B O   
4949  C CB  . ILE B 107 ? 0.4102 0.4211 0.3462 -0.0156 0.0672  0.0002  107 ILE B CB  
4950  C CG1 . ILE B 107 ? 0.3159 0.3209 0.2490 -0.0068 0.0610  -0.0021 107 ILE B CG1 
4951  C CG2 . ILE B 107 ? 0.3331 0.3334 0.2546 -0.0101 0.0728  -0.0008 107 ILE B CG2 
4952  C CD1 . ILE B 107 ? 0.3782 0.3571 0.2951 -0.0091 0.0567  -0.0033 107 ILE B CD1 
4953  N N   . TYR B 108 ? 0.4149 0.4807 0.3968 -0.0194 0.0622  -0.0012 108 TYR B N   
4954  C CA  . TYR B 108 ? 0.4034 0.4808 0.3995 -0.0246 0.0556  -0.0016 108 TYR B CA  
4955  C C   . TYR B 108 ? 0.4349 0.5431 0.4532 -0.0324 0.0606  -0.0033 108 TYR B C   
4956  O O   . TYR B 108 ? 0.4455 0.5684 0.4788 -0.0358 0.0548  -0.0054 108 TYR B O   
4957  C CB  . TYR B 108 ? 0.2934 0.3686 0.2877 -0.0116 0.0468  -0.0049 108 TYR B CB  
4958  C CG  . TYR B 108 ? 0.3363 0.3822 0.3125 -0.0125 0.0407  -0.0028 108 TYR B CG  
4959  C CD1 . TYR B 108 ? 0.3764 0.3979 0.3329 -0.0109 0.0432  -0.0019 108 TYR B CD1 
4960  C CD2 . TYR B 108 ? 0.3475 0.3912 0.3262 -0.0153 0.0329  -0.0026 108 TYR B CD2 
4961  C CE1 . TYR B 108 ? 0.3814 0.3795 0.3229 -0.0140 0.0393  -0.0013 108 TYR B CE1 
4962  C CE2 . TYR B 108 ? 0.3528 0.3712 0.3144 -0.0171 0.0290  -0.0013 108 TYR B CE2 
4963  C CZ  . TYR B 108 ? 0.4113 0.4083 0.3552 -0.0173 0.0329  -0.0009 108 TYR B CZ  
4964  O OH  . TYR B 108 ? 0.4382 0.4133 0.3667 -0.0212 0.0309  -0.0009 108 TYR B OH  
4965  N N   . ARG B 109 ? 0.4750 0.5932 0.4950 -0.0365 0.0717  -0.0030 109 ARG B N   
4966  C CA  . ARG B 109 ? 0.5053 0.6538 0.5458 -0.0471 0.0793  -0.0053 109 ARG B CA  
4967  C C   . ARG B 109 ? 0.4853 0.6236 0.5242 -0.0657 0.0790  -0.0009 109 ARG B C   
4968  O O   . ARG B 109 ? 0.4629 0.5871 0.4888 -0.0768 0.0868  0.0035  109 ARG B O   
4969  C CB  . ARG B 109 ? 0.5649 0.7242 0.6038 -0.0471 0.0931  -0.0060 109 ARG B CB  
4970  C CG  . ARG B 109 ? 0.6656 0.8592 0.7266 -0.0603 0.1034  -0.0095 109 ARG B CG  
4971  C CD  . ARG B 109 ? 0.7417 0.9682 0.8167 -0.0499 0.1118  -0.0169 109 ARG B CD  
4972  N NE  . ARG B 109 ? 0.7824 0.9915 0.8359 -0.0436 0.1204  -0.0138 109 ARG B NE  
4973  C CZ  . ARG B 109 ? 0.7780 0.9845 0.8241 -0.0235 0.1176  -0.0169 109 ARG B CZ  
4974  N NH1 . ARG B 109 ? 0.8127 1.0303 0.8687 -0.0074 0.1064  -0.0229 109 ARG B NH1 
4975  N NH2 . ARG B 109 ? 0.7732 0.9631 0.7992 -0.0190 0.1253  -0.0143 109 ARG B NH2 
4976  N N   . PHE B 110 ? 0.4206 0.5629 0.4697 -0.0678 0.0688  -0.0023 110 PHE B N   
4977  C CA  . PHE B 110 ? 0.3816 0.5157 0.4305 -0.0840 0.0663  0.0005  110 PHE B CA  
4978  C C   . PHE B 110 ? 0.4139 0.5797 0.4899 -0.0891 0.0627  -0.0054 110 PHE B C   
4979  O O   . PHE B 110 ? 0.3707 0.5474 0.4568 -0.0770 0.0528  -0.0100 110 PHE B O   
4980  C CB  . PHE B 110 ? 0.3246 0.4292 0.3569 -0.0815 0.0554  0.0038  110 PHE B CB  
4981  C CG  . PHE B 110 ? 0.3674 0.4421 0.3747 -0.0794 0.0575  0.0079  110 PHE B CG  
4982  C CD1 . PHE B 110 ? 0.3742 0.4299 0.3662 -0.0904 0.0606  0.0116  110 PHE B CD1 
4983  C CD2 . PHE B 110 ? 0.4117 0.4753 0.4090 -0.0663 0.0549  0.0071  110 PHE B CD2 
4984  C CE1 . PHE B 110 ? 0.4635 0.4932 0.4329 -0.0862 0.0602  0.0134  110 PHE B CE1 
4985  C CE2 . PHE B 110 ? 0.4074 0.4469 0.3845 -0.0647 0.0557  0.0088  110 PHE B CE2 
4986  C CZ  . PHE B 110 ? 0.4435 0.4678 0.4078 -0.0735 0.0577  0.0114  110 PHE B CZ  
4987  N N   . GLU B 111 ? 0.4144 0.5927 0.4998 -0.1073 0.0706  -0.0059 111 GLU B N   
4988  C CA  . GLU B 111 ? 0.4487 0.6587 0.5617 -0.1154 0.0673  -0.0129 111 GLU B CA  
4989  C C   . GLU B 111 ? 0.4452 0.6450 0.5585 -0.1112 0.0511  -0.0134 111 GLU B C   
4990  O O   . GLU B 111 ? 0.4959 0.7223 0.6311 -0.1058 0.0431  -0.0211 111 GLU B O   
4991  C CB  . GLU B 111 ? 0.5081 0.7219 0.6237 -0.1402 0.0786  -0.0117 111 GLU B CB  
4992  C CG  . GLU B 111 ? 0.6374 0.8795 0.7797 -0.1532 0.0747  -0.0191 111 GLU B CG  
4993  C CD  . GLU B 111 ? 0.7456 1.0395 0.9229 -0.1445 0.0753  -0.0313 111 GLU B CD  
4994  O OE1 . GLU B 111 ? 0.7926 1.1030 0.9736 -0.1356 0.0848  -0.0336 111 GLU B OE1 
4995  O OE2 . GLU B 111 ? 0.7640 1.0824 0.9646 -0.1452 0.0653  -0.0395 111 GLU B OE2 
4996  N N   . ARG B 112 ? 0.4076 0.5702 0.4966 -0.1121 0.0456  -0.0065 112 ARG B N   
4997  C CA  . ARG B 112 ? 0.3988 0.5512 0.4862 -0.1083 0.0313  -0.0071 112 ARG B CA  
4998  C C   . ARG B 112 ? 0.3478 0.5054 0.4375 -0.0878 0.0228  -0.0105 112 ARG B C   
4999  O O   . ARG B 112 ? 0.3847 0.5507 0.4835 -0.0827 0.0119  -0.0148 112 ARG B O   
5000  C CB  . ARG B 112 ? 0.4225 0.5365 0.4833 -0.1125 0.0280  -0.0003 112 ARG B CB  
5001  C CG  . ARG B 112 ? 0.4854 0.5874 0.5421 -0.1091 0.0143  -0.0010 112 ARG B CG  
5002  C CD  . ARG B 112 ? 0.4949 0.6107 0.5672 -0.1208 0.0088  -0.0047 112 ARG B CD  
5003  N NE  . ARG B 112 ? 0.5089 0.6022 0.5680 -0.1214 -0.0024 -0.0034 112 ARG B NE  
5004  C CZ  . ARG B 112 ? 0.5131 0.6148 0.5829 -0.1239 -0.0125 -0.0075 112 ARG B CZ  
5005  N NH1 . ARG B 112 ? 0.5221 0.6562 0.6180 -0.1264 -0.0133 -0.0142 112 ARG B NH1 
5006  N NH2 . ARG B 112 ? 0.5373 0.6167 0.5924 -0.1231 -0.0222 -0.0062 112 ARG B NH2 
5007  N N   . ILE B 113 ? 0.3804 0.5297 0.4587 -0.0757 0.0272  -0.0088 113 ILE B N   
5008  C CA  . ILE B 113 ? 0.3913 0.5392 0.4659 -0.0568 0.0197  -0.0117 113 ILE B CA  
5009  C C   . ILE B 113 ? 0.4021 0.5854 0.5006 -0.0484 0.0158  -0.0207 113 ILE B C   
5010  O O   . ILE B 113 ? 0.3717 0.5554 0.4697 -0.0351 0.0045  -0.0248 113 ILE B O   
5011  C CB  . ILE B 113 ? 0.4374 0.5681 0.4939 -0.0473 0.0258  -0.0087 113 ILE B CB  
5012  C CG1 . ILE B 113 ? 0.4559 0.5535 0.4899 -0.0528 0.0262  -0.0025 113 ILE B CG1 
5013  C CG2 . ILE B 113 ? 0.4639 0.5918 0.5140 -0.0281 0.0192  -0.0123 113 ILE B CG2 
5014  C CD1 . ILE B 113 ? 0.4834 0.5671 0.5026 -0.0487 0.0339  -0.0002 113 ILE B CD1 
5015  N N   . ARG B 114 ? 0.4293 0.6434 0.5485 -0.0558 0.0248  -0.0249 114 ARG B N   
5016  C CA  . ARG B 114 ? 0.4690 0.7240 0.6157 -0.0483 0.0210  -0.0362 114 ARG B CA  
5017  C C   . ARG B 114 ? 0.4952 0.7608 0.6559 -0.0533 0.0092  -0.0410 114 ARG B C   
5018  O O   . ARG B 114 ? 0.5305 0.8112 0.7003 -0.0378 -0.0027 -0.0491 114 ARG B O   
5019  C CB  . ARG B 114 ? 0.5201 0.8088 0.6876 -0.0591 0.0354  -0.0405 114 ARG B CB  
5020  C CG  . ARG B 114 ? 0.6020 0.9418 0.8055 -0.0584 0.0329  -0.0544 114 ARG B CG  
5021  C CD  . ARG B 114 ? 0.6578 1.0150 0.8665 -0.0305 0.0235  -0.0639 114 ARG B CD  
5022  N NE  . ARG B 114 ? 0.6818 1.0888 0.9252 -0.0261 0.0169  -0.0795 114 ARG B NE  
5023  C CZ  . ARG B 114 ? 0.6660 1.1134 0.9297 -0.0117 0.0186  -0.0921 114 ARG B CZ  
5024  N NH1 . ARG B 114 ? 0.6404 1.0814 0.8910 -0.0004 0.0271  -0.0897 114 ARG B NH1 
5025  N NH2 . ARG B 114 ? 0.6546 1.1501 0.9520 -0.0076 0.0111  -0.1082 114 ARG B NH2 
5026  N N   . GLU B 115 ? 0.4612 0.7155 0.6204 -0.0735 0.0111  -0.0362 115 GLU B N   
5027  C CA  . GLU B 115 ? 0.4529 0.7140 0.6233 -0.0793 -0.0005 -0.0405 115 GLU B CA  
5028  C C   . GLU B 115 ? 0.4446 0.6783 0.5953 -0.0640 -0.0147 -0.0382 115 GLU B C   
5029  O O   . GLU B 115 ? 0.4801 0.7269 0.6410 -0.0554 -0.0275 -0.0456 115 GLU B O   
5030  C CB  . GLU B 115 ? 0.4587 0.7064 0.6256 -0.1038 0.0046  -0.0352 115 GLU B CB  
5031  C CG  . GLU B 115 ? 0.5003 0.7657 0.6785 -0.1216 0.0205  -0.0357 115 GLU B CG  
5032  C CD  . GLU B 115 ? 0.5460 0.7833 0.7078 -0.1434 0.0254  -0.0282 115 GLU B CD  
5033  O OE1 . GLU B 115 ? 0.5688 0.7809 0.7171 -0.1442 0.0144  -0.0249 115 GLU B OE1 
5034  O OE2 . GLU B 115 ? 0.5588 0.7970 0.7184 -0.1591 0.0399  -0.0257 115 GLU B OE2 
5035  N N   . LEU B 116 ? 0.4371 0.6331 0.5591 -0.0611 -0.0125 -0.0287 116 LEU B N   
5036  C CA  . LEU B 116 ? 0.4100 0.5786 0.5111 -0.0499 -0.0234 -0.0263 116 LEU B CA  
5037  C C   . LEU B 116 ? 0.4885 0.6630 0.5876 -0.0280 -0.0316 -0.0322 116 LEU B C   
5038  O O   . LEU B 116 ? 0.4615 0.6285 0.5542 -0.0187 -0.0440 -0.0350 116 LEU B O   
5039  C CB  . LEU B 116 ? 0.3775 0.5104 0.4513 -0.0518 -0.0176 -0.0172 116 LEU B CB  
5040  C CG  . LEU B 116 ? 0.4124 0.5307 0.4801 -0.0691 -0.0137 -0.0119 116 LEU B CG  
5041  C CD1 . LEU B 116 ? 0.4399 0.5310 0.4850 -0.0689 -0.0072 -0.0057 116 LEU B CD1 
5042  C CD2 . LEU B 116 ? 0.4131 0.5224 0.4778 -0.0723 -0.0246 -0.0127 116 LEU B CD2 
5043  N N   . MET B 117 ? 0.5409 0.7264 0.6426 -0.0181 -0.0256 -0.0344 117 MET B N   
5044  C CA  . MET B 117 ? 0.5717 0.7599 0.6678 0.0050  -0.0344 -0.0408 117 MET B CA  
5045  C C   . MET B 117 ? 0.5979 0.8255 0.7220 0.0121  -0.0445 -0.0535 117 MET B C   
5046  O O   . MET B 117 ? 0.6392 0.8677 0.7568 0.0338  -0.0556 -0.0604 117 MET B O   
5047  C CB  . MET B 117 ? 0.5966 0.7832 0.6850 0.0145  -0.0258 -0.0402 117 MET B CB  
5048  C CG  . MET B 117 ? 0.6175 0.7626 0.6747 0.0125  -0.0192 -0.0300 117 MET B CG  
5049  S SD  . MET B 117 ? 0.6702 0.7744 0.6981 0.0138  -0.0282 -0.0247 117 MET B SD  
5050  C CE  . MET B 117 ? 0.6980 0.7674 0.6909 0.0317  -0.0286 -0.0231 117 MET B CE  
5051  N N   . ASN B 118 ? 0.5744 0.8326 0.7275 -0.0056 -0.0415 -0.0575 118 ASN B N   
5052  C CA  . ASN B 118 ? 0.5875 0.8892 0.7725 -0.0023 -0.0502 -0.0716 118 ASN B CA  
5053  C C   . ASN B 118 ? 0.5539 0.8495 0.7390 -0.0038 -0.0648 -0.0743 118 ASN B C   
5054  O O   . ASN B 118 ? 0.5529 0.8843 0.7648 -0.0013 -0.0741 -0.0871 118 ASN B O   
5055  C CB  . ASN B 118 ? 0.6666 1.0077 0.8842 -0.0235 -0.0372 -0.0760 118 ASN B CB  
5056  C CG  . ASN B 118 ? 0.7432 1.1159 0.9758 -0.0139 -0.0285 -0.0831 118 ASN B CG  
5057  O OD1 . ASN B 118 ? 0.7829 1.1583 1.0169 -0.0269 -0.0121 -0.0780 118 ASN B OD1 
5058  N ND2 . ASN B 118 ? 0.7324 1.1281 0.9742 0.0102  -0.0400 -0.0956 118 ASN B ND2 
5059  N N   . LYS B 119 ? 0.5357 0.7891 0.6925 -0.0073 -0.0673 -0.0638 119 LYS B N   
5060  C CA  . LYS B 119 ? 0.5606 0.8054 0.7150 -0.0098 -0.0801 -0.0655 119 LYS B CA  
5061  C C   . LYS B 119 ? 0.5991 0.8149 0.7245 0.0131  -0.0932 -0.0654 119 LYS B C   
5062  O O   . LYS B 119 ? 0.6219 0.8062 0.7182 0.0226  -0.0890 -0.0580 119 LYS B O   
5063  C CB  . LYS B 119 ? 0.5515 0.7710 0.6947 -0.0309 -0.0737 -0.0550 119 LYS B CB  
5064  C CG  . LYS B 119 ? 0.5857 0.8284 0.7528 -0.0545 -0.0627 -0.0556 119 LYS B CG  
5065  C CD  . LYS B 119 ? 0.5973 0.8089 0.7470 -0.0715 -0.0587 -0.0458 119 LYS B CD  
5066  C CE  . LYS B 119 ? 0.6337 0.8137 0.7565 -0.0680 -0.0495 -0.0352 119 LYS B CE  
5067  N NZ  . LYS B 119 ? 0.6797 0.8616 0.8055 -0.0835 -0.0346 -0.0305 119 LYS B NZ  
5068  N N   . GLU B 120 ? 0.6004 0.8253 0.7319 0.0212  -0.1092 -0.0741 120 GLU B N   
5069  C CA  . GLU B 120 ? 0.5842 0.7796 0.6846 0.0442  -0.1224 -0.0748 120 GLU B CA  
5070  C C   . GLU B 120 ? 0.6029 0.7509 0.6681 0.0385  -0.1196 -0.0623 120 GLU B C   
5071  O O   . GLU B 120 ? 0.6597 0.7721 0.6900 0.0514  -0.1194 -0.0569 120 GLU B O   
5072  C CB  . GLU B 120 ? 0.5751 0.7942 0.6914 0.0557  -0.1413 -0.0888 120 GLU B CB  
5073  N N   . LYS B 121 ? 0.5655 0.7118 0.6380 0.0189  -0.1171 -0.0583 121 LYS B N   
5074  C CA  . LYS B 121 ? 0.5499 0.6576 0.5935 0.0122  -0.1134 -0.0480 121 LYS B CA  
5075  C C   . LYS B 121 ? 0.5849 0.6933 0.6371 -0.0097 -0.0996 -0.0408 121 LYS B C   
5076  O O   . LYS B 121 ? 0.6111 0.7474 0.6909 -0.0227 -0.0951 -0.0437 121 LYS B O   
5077  C CB  . LYS B 121 ? 0.5221 0.6202 0.5584 0.0140  -0.1272 -0.0511 121 LYS B CB  
5078  N N   . LEU B 122 ? 0.5646 0.6415 0.5913 -0.0138 -0.0928 -0.0321 122 LEU B N   
5079  C CA  . LEU B 122 ? 0.5182 0.5904 0.5466 -0.0305 -0.0809 -0.0257 122 LEU B CA  
5080  C C   . LEU B 122 ? 0.5068 0.5578 0.5203 -0.0375 -0.0841 -0.0226 122 LEU B C   
5081  O O   . LEU B 122 ? 0.5440 0.5720 0.5336 -0.0294 -0.0867 -0.0209 122 LEU B O   
5082  C CB  . LEU B 122 ? 0.4720 0.5300 0.4856 -0.0276 -0.0687 -0.0201 122 LEU B CB  
5083  C CG  . LEU B 122 ? 0.4827 0.5586 0.5080 -0.0207 -0.0637 -0.0224 122 LEU B CG  
5084  C CD1 . LEU B 122 ? 0.4630 0.5188 0.4690 -0.0183 -0.0528 -0.0168 122 LEU B CD1 
5085  C CD2 . LEU B 122 ? 0.4019 0.5081 0.4566 -0.0335 -0.0591 -0.0250 122 LEU B CD2 
5086  N N   . ASN B 123 ? 0.4746 0.5314 0.4995 -0.0525 -0.0833 -0.0222 123 ASN B N   
5087  C CA  . ASN B 123 ? 0.4635 0.5001 0.4734 -0.0580 -0.0869 -0.0201 123 ASN B CA  
5088  C C   . ASN B 123 ? 0.4194 0.4386 0.4135 -0.0617 -0.0762 -0.0145 123 ASN B C   
5089  O O   . ASN B 123 ? 0.4538 0.4746 0.4472 -0.0599 -0.0664 -0.0120 123 ASN B O   
5090  C CB  . ASN B 123 ? 0.4037 0.4490 0.4280 -0.0714 -0.0929 -0.0229 123 ASN B CB  
5091  C CG  . ASN B 123 ? 0.4276 0.4823 0.4645 -0.0864 -0.0828 -0.0207 123 ASN B CG  
5092  O OD1 . ASN B 123 ? 0.4111 0.4557 0.4383 -0.0882 -0.0726 -0.0157 123 ASN B OD1 
5093  N ND2 . ASN B 123 ? 0.4137 0.4872 0.4712 -0.0979 -0.0855 -0.0251 123 ASN B ND2 
5094  N N   . ARG B 124 ? 0.5021 0.3445 0.3760 0.0224  0.0049  -0.0373 124 ARG B N   
5095  C CA  . ARG B 124 ? 0.4987 0.3414 0.3674 0.0281  0.0083  -0.0339 124 ARG B CA  
5096  C C   . ARG B 124 ? 0.5696 0.4098 0.4402 0.0244  0.0113  -0.0279 124 ARG B C   
5097  O O   . ARG B 124 ? 0.5263 0.3735 0.3967 0.0271  0.0146  -0.0243 124 ARG B O   
5098  C CB  . ARG B 124 ? 0.5637 0.3953 0.4242 0.0347  0.0059  -0.0376 124 ARG B CB  
5099  C CG  . ARG B 124 ? 0.5741 0.4077 0.4311 0.0417  0.0085  -0.0361 124 ARG B CG  
5100  C CD  . ARG B 124 ? 0.6485 0.4693 0.4991 0.0481  0.0053  -0.0403 124 ARG B CD  
5101  N NE  . ARG B 124 ? 0.6489 0.4723 0.4984 0.0552  0.0068  -0.0398 124 ARG B NE  
5102  C CZ  . ARG B 124 ? 0.7105 0.5258 0.5588 0.0560  0.0057  -0.0358 124 ARG B CZ  
5103  N NH1 . ARG B 124 ? 0.6572 0.4609 0.5039 0.0491  0.0041  -0.0313 124 ARG B NH1 
5104  N NH2 . ARG B 124 ? 0.7335 0.5521 0.5816 0.0634  0.0060  -0.0366 124 ARG B NH2 
5105  N N   . GLU B 125 ? 0.6027 0.4319 0.4741 0.0178  0.0103  -0.0269 125 GLU B N   
5106  C CA  . GLU B 125 ? 0.6480 0.4720 0.5180 0.0134  0.0136  -0.0208 125 GLU B CA  
5107  C C   . GLU B 125 ? 0.5342 0.3738 0.4119 0.0089  0.0183  -0.0178 125 GLU B C   
5108  O O   . GLU B 125 ? 0.4524 0.2935 0.3272 0.0097  0.0215  -0.0129 125 GLU B O   
5109  C CB  . GLU B 125 ? 0.7534 0.5616 0.6219 0.0055  0.0123  -0.0205 125 GLU B CB  
5110  C CG  . GLU B 125 ? 0.9155 0.7075 0.7775 0.0092  0.0065  -0.0247 125 GLU B CG  
5111  C CD  . GLU B 125 ? 1.0284 0.8233 0.8970 0.0066  0.0029  -0.0313 125 GLU B CD  
5112  O OE1 . GLU B 125 ? 1.0650 0.8538 0.9383 -0.0022 0.0021  -0.0324 125 GLU B OE1 
5113  O OE2 . GLU B 125 ? 1.0208 0.8238 0.8894 0.0132  0.0008  -0.0357 125 GLU B OE2 
5114  N N   . GLU B 126 ? 0.5065 0.3574 0.3939 0.0049  0.0179  -0.0214 126 GLU B N   
5115  C CA  . GLU B 126 ? 0.5140 0.3803 0.4100 0.0012  0.0215  -0.0200 126 GLU B CA  
5116  C C   . GLU B 126 ? 0.4979 0.3747 0.3920 0.0083  0.0226  -0.0183 126 GLU B C   
5117  O O   . GLU B 126 ? 0.5025 0.3866 0.3983 0.0073  0.0263  -0.0146 126 GLU B O   
5118  C CB  . GLU B 126 ? 0.4928 0.3676 0.4001 -0.0035 0.0190  -0.0256 126 GLU B CB  
5119  C CG  . GLU B 126 ? 0.6262 0.4913 0.5371 -0.0116 0.0184  -0.0277 126 GLU B CG  
5120  C CD  . GLU B 126 ? 0.7675 0.6389 0.6897 -0.0149 0.0138  -0.0351 126 GLU B CD  
5121  O OE1 . GLU B 126 ? 0.7673 0.6401 0.6872 -0.0085 0.0083  -0.0391 126 GLU B OE1 
5122  O OE2 . GLU B 126 ? 0.9111 0.7846 0.8436 -0.0241 0.0156  -0.0373 126 GLU B OE2 
5123  N N   . LEU B 127 ? 0.4634 0.3405 0.3533 0.0150  0.0197  -0.0211 127 LEU B N   
5124  C CA  . LEU B 127 ? 0.4265 0.3125 0.3142 0.0208  0.0213  -0.0197 127 LEU B CA  
5125  C C   . LEU B 127 ? 0.3988 0.2813 0.2818 0.0241  0.0239  -0.0154 127 LEU B C   
5126  O O   . LEU B 127 ? 0.4897 0.3810 0.3744 0.0254  0.0264  -0.0126 127 LEU B O   
5127  C CB  . LEU B 127 ? 0.4108 0.2959 0.2931 0.0262  0.0188  -0.0239 127 LEU B CB  
5128  C CG  . LEU B 127 ? 0.4402 0.3293 0.3248 0.0245  0.0153  -0.0279 127 LEU B CG  
5129  C CD1 . LEU B 127 ? 0.4255 0.3102 0.3008 0.0295  0.0132  -0.0318 127 LEU B CD1 
5130  C CD2 . LEU B 127 ? 0.4319 0.3334 0.3220 0.0230  0.0162  -0.0263 127 LEU B CD2 
5131  N N   . LEU B 128 ? 0.4083 0.2769 0.2850 0.0259  0.0224  -0.0152 128 LEU B N   
5132  C CA  . LEU B 128 ? 0.4927 0.3556 0.3641 0.0297  0.0232  -0.0115 128 LEU B CA  
5133  C C   . LEU B 128 ? 0.4903 0.3551 0.3625 0.0246  0.0264  -0.0063 128 LEU B C   
5134  O O   . LEU B 128 ? 0.5293 0.3969 0.3992 0.0282  0.0275  -0.0034 128 LEU B O   
5135  C CB  . LEU B 128 ? 0.5255 0.3702 0.3892 0.0317  0.0198  -0.0123 128 LEU B CB  
5136  C CG  . LEU B 128 ? 0.5758 0.4174 0.4358 0.0410  0.0169  -0.0167 128 LEU B CG  
5137  C CD1 . LEU B 128 ? 0.5882 0.4096 0.4403 0.0427  0.0125  -0.0174 128 LEU B CD1 
5138  C CD2 . LEU B 128 ? 0.5841 0.4347 0.4451 0.0476  0.0182  -0.0160 128 LEU B CD2 
5139  N N   . ASP B 129 ? 0.5089 0.3724 0.3846 0.0160  0.0280  -0.0056 129 ASP B N   
5140  C CA  . ASP B 129 ? 0.4960 0.3625 0.3724 0.0103  0.0323  -0.0013 129 ASP B CA  
5141  C C   . ASP B 129 ? 0.4935 0.3785 0.3778 0.0114  0.0344  -0.0016 129 ASP B C   
5142  O O   . ASP B 129 ? 0.4948 0.3833 0.3769 0.0121  0.0370  0.0019  129 ASP B O   
5143  C CB  . ASP B 129 ? 0.5246 0.3867 0.4044 0.0000  0.0346  -0.0016 129 ASP B CB  
5144  C CG  . ASP B 129 ? 0.6060 0.4467 0.4749 -0.0029 0.0337  0.0011  129 ASP B CG  
5145  O OD1 . ASP B 129 ? 0.5992 0.4283 0.4586 0.0045  0.0300  0.0022  129 ASP B OD1 
5146  O OD2 . ASP B 129 ? 0.5824 0.4176 0.4526 -0.0127 0.0367  0.0017  129 ASP B OD2 
5147  N N   . LEU B 130 ? 0.4782 0.3735 0.3701 0.0120  0.0327  -0.0060 130 LEU B N   
5148  C CA  . LEU B 130 ? 0.4769 0.3876 0.3753 0.0132  0.0335  -0.0066 130 LEU B CA  
5149  C C   . LEU B 130 ? 0.4334 0.3472 0.3275 0.0202  0.0337  -0.0045 130 LEU B C   
5150  O O   . LEU B 130 ? 0.4739 0.3963 0.3702 0.0206  0.0356  -0.0025 130 LEU B O   
5151  C CB  . LEU B 130 ? 0.4913 0.4083 0.3953 0.0135  0.0301  -0.0117 130 LEU B CB  
5152  C CG  . LEU B 130 ? 0.5097 0.4405 0.4199 0.0143  0.0298  -0.0128 130 LEU B CG  
5153  C CD1 . LEU B 130 ? 0.5014 0.4402 0.4192 0.0091  0.0330  -0.0120 130 LEU B CD1 
5154  C CD2 . LEU B 130 ? 0.4966 0.4301 0.4094 0.0151  0.0249  -0.0177 130 LEU B CD2 
5155  N N   . GLN B 131 ? 0.3851 0.2929 0.2739 0.0257  0.0317  -0.0057 131 GLN B N   
5156  C CA  . GLN B 131 ? 0.4277 0.3393 0.3143 0.0321  0.0321  -0.0047 131 GLN B CA  
5157  C C   . GLN B 131 ? 0.4282 0.3356 0.3110 0.0328  0.0332  -0.0005 131 GLN B C   
5158  O O   . GLN B 131 ? 0.4145 0.3302 0.2992 0.0343  0.0344  0.0012  131 GLN B O   
5159  C CB  . GLN B 131 ? 0.4028 0.3090 0.2856 0.0377  0.0303  -0.0079 131 GLN B CB  
5160  C CG  . GLN B 131 ? 0.3677 0.2769 0.2508 0.0381  0.0295  -0.0122 131 GLN B CG  
5161  C CD  . GLN B 131 ? 0.4372 0.3394 0.3158 0.0431  0.0283  -0.0159 131 GLN B CD  
5162  O OE1 . GLN B 131 ? 0.4112 0.3019 0.2866 0.0440  0.0262  -0.0159 131 GLN B OE1 
5163  N NE2 . GLN B 131 ? 0.4780 0.3865 0.3559 0.0464  0.0297  -0.0192 131 GLN B NE2 
5164  N N   . THR B 132 ? 0.4631 0.3561 0.3392 0.0318  0.0322  0.0012  132 THR B N   
5165  C CA  . THR B 132 ? 0.4738 0.3586 0.3424 0.0337  0.0320  0.0052  132 THR B CA  
5166  C C   . THR B 132 ? 0.5225 0.4115 0.3911 0.0280  0.0357  0.0089  132 THR B C   
5167  O O   . THR B 132 ? 0.5078 0.3961 0.3715 0.0307  0.0358  0.0118  132 THR B O   
5168  C CB  . THR B 132 ? 0.4695 0.3345 0.3284 0.0336  0.0293  0.0063  132 THR B CB  
5169  O OG1 . THR B 132 ? 0.4650 0.3272 0.3250 0.0387  0.0261  0.0016  132 THR B OG1 
5170  C CG2 . THR B 132 ? 0.4434 0.2966 0.2915 0.0380  0.0271  0.0099  132 THR B CG2 
5171  N N   . LEU B 133 ? 0.5190 0.4127 0.3932 0.0203  0.0386  0.0082  133 LEU B N   
5172  C CA  . LEU B 133 ? 0.4934 0.3933 0.3690 0.0149  0.0430  0.0105  133 LEU B CA  
5173  C C   . LEU B 133 ? 0.4764 0.3926 0.3589 0.0184  0.0432  0.0094  133 LEU B C   
5174  O O   . LEU B 133 ? 0.3910 0.3105 0.2713 0.0177  0.0456  0.0118  133 LEU B O   
5175  C CB  . LEU B 133 ? 0.5165 0.4189 0.3988 0.0058  0.0460  0.0085  133 LEU B CB  
5176  C CG  . LEU B 133 ? 0.5826 0.4678 0.4569 -0.0004 0.0474  0.0106  133 LEU B CG  
5177  C CD1 . LEU B 133 ? 0.6177 0.5076 0.5024 -0.0088 0.0493  0.0066  133 LEU B CD1 
5178  C CD2 . LEU B 133 ? 0.5752 0.4510 0.4377 -0.0037 0.0513  0.0160  133 LEU B CD2 
5179  N N   . ASN B 134 ? 0.4393 0.3645 0.3289 0.0219  0.0408  0.0059  134 ASN B N   
5180  C CA  . ASN B 134 ? 0.4367 0.3744 0.3309 0.0254  0.0404  0.0053  134 ASN B CA  
5181  C C   . ASN B 134 ? 0.4679 0.4029 0.3564 0.0312  0.0394  0.0077  134 ASN B C   
5182  O O   . ASN B 134 ? 0.5556 0.4968 0.4446 0.0322  0.0402  0.0091  134 ASN B O   
5183  C CB  . ASN B 134 ? 0.4284 0.3724 0.3277 0.0276  0.0380  0.0017  134 ASN B CB  
5184  C CG  . ASN B 134 ? 0.4028 0.3538 0.3093 0.0233  0.0375  -0.0013 134 ASN B CG  
5185  O OD1 . ASN B 134 ? 0.3641 0.3247 0.2755 0.0233  0.0373  -0.0021 134 ASN B OD1 
5186  N ND2 . ASN B 134 ? 0.3877 0.3335 0.2952 0.0203  0.0365  -0.0035 134 ASN B ND2 
5187  N N   . LEU B 135 ? 0.4347 0.3602 0.3179 0.0355  0.0371  0.0076  135 LEU B N   
5188  C CA  . LEU B 135 ? 0.5117 0.4337 0.3901 0.0417  0.0349  0.0090  135 LEU B CA  
5189  C C   . LEU B 135 ? 0.4609 0.3752 0.3305 0.0399  0.0359  0.0133  135 LEU B C   
5190  O O   . LEU B 135 ? 0.4490 0.3685 0.3180 0.0424  0.0356  0.0144  135 LEU B O   
5191  C CB  . LEU B 135 ? 0.5237 0.4352 0.3980 0.0467  0.0316  0.0072  135 LEU B CB  
5192  C CG  . LEU B 135 ? 0.6471 0.5657 0.5278 0.0513  0.0305  0.0023  135 LEU B CG  
5193  C CD1 . LEU B 135 ? 0.6233 0.5319 0.4998 0.0580  0.0267  0.0003  135 LEU B CD1 
5194  C CD2 . LEU B 135 ? 0.5871 0.5208 0.4754 0.0533  0.0315  0.0008  135 LEU B CD2 
5195  N N   . LEU B 136 ? 0.4654 0.3660 0.3269 0.0353  0.0371  0.0157  136 LEU B N   
5196  C CA  . LEU B 136 ? 0.4410 0.3308 0.2904 0.0326  0.0386  0.0203  136 LEU B CA  
5197  C C   . LEU B 136 ? 0.4457 0.3473 0.2987 0.0280  0.0433  0.0211  136 LEU B C   
5198  O O   . LEU B 136 ? 0.4511 0.3479 0.2945 0.0282  0.0443  0.0242  136 LEU B O   
5199  C CB  . LEU B 136 ? 0.4347 0.3075 0.2750 0.0265  0.0401  0.0226  136 LEU B CB  
5200  C CG  . LEU B 136 ? 0.4689 0.3252 0.3014 0.0322  0.0343  0.0224  136 LEU B CG  
5201  C CD1 . LEU B 136 ? 0.4945 0.3339 0.3192 0.0253  0.0354  0.0243  136 LEU B CD1 
5202  C CD2 . LEU B 136 ? 0.5085 0.3539 0.3288 0.0397  0.0295  0.0249  136 LEU B CD2 
5203  N N   . ALA B 137 ? 0.4092 0.3254 0.2750 0.0242  0.0458  0.0178  137 ALA B N   
5204  C CA  . ALA B 137 ? 0.4595 0.3878 0.3301 0.0207  0.0496  0.0173  137 ALA B CA  
5205  C C   . ALA B 137 ? 0.4383 0.3728 0.3078 0.0269  0.0475  0.0178  137 ALA B C   
5206  O O   . ALA B 137 ? 0.4538 0.3915 0.3201 0.0251  0.0504  0.0189  137 ALA B O   
5207  C CB  . ALA B 137 ? 0.4599 0.4025 0.3451 0.0178  0.0503  0.0127  137 ALA B CB  
5208  N N   . TRP B 138 ? 0.4231 0.3596 0.2953 0.0339  0.0428  0.0166  138 TRP B N   
5209  C CA  . TRP B 138 ? 0.4378 0.3802 0.3104 0.0397  0.0401  0.0164  138 TRP B CA  
5210  C C   . TRP B 138 ? 0.4813 0.4108 0.3417 0.0450  0.0368  0.0190  138 TRP B C   
5211  O O   . TRP B 138 ? 0.4811 0.4146 0.3432 0.0514  0.0328  0.0177  138 TRP B O   
5212  C CB  . TRP B 138 ? 0.4026 0.3555 0.2861 0.0435  0.0374  0.0128  138 TRP B CB  
5213  C CG  . TRP B 138 ? 0.3854 0.3486 0.2780 0.0393  0.0393  0.0105  138 TRP B CG  
5214  C CD1 . TRP B 138 ? 0.3553 0.3180 0.2517 0.0358  0.0401  0.0089  138 TRP B CD1 
5215  C CD2 . TRP B 138 ? 0.4143 0.3887 0.3128 0.0386  0.0396  0.0091  138 TRP B CD2 
5216  N NE1 . TRP B 138 ? 0.4046 0.3773 0.3087 0.0334  0.0403  0.0064  138 TRP B NE1 
5217  C CE2 . TRP B 138 ? 0.4172 0.3969 0.3227 0.0351  0.0400  0.0065  138 TRP B CE2 
5218  C CE3 . TRP B 138 ? 0.3570 0.3365 0.2551 0.0411  0.0388  0.0093  138 TRP B CE3 
5219  C CZ2 . TRP B 138 ? 0.4102 0.3998 0.3224 0.0344  0.0392  0.0041  138 TRP B CZ2 
5220  C CZ3 . TRP B 138 ? 0.3914 0.3811 0.2963 0.0400  0.0386  0.0070  138 TRP B CZ3 
5221  C CH2 . TRP B 138 ? 0.4261 0.4205 0.3380 0.0368  0.0386  0.0044  138 TRP B CH2 
5222  N N   . CYS B 139 ? 0.4339 0.3473 0.2816 0.0424  0.0377  0.0223  139 CYS B N   
5223  C CA  . CYS B 139 ? 0.3985 0.2967 0.2325 0.0482  0.0329  0.0246  139 CYS B CA  
5224  C C   . CYS B 139 ? 0.4129 0.3107 0.2383 0.0495  0.0330  0.0267  139 CYS B C   
5225  O O   . CYS B 139 ? 0.4559 0.3560 0.2780 0.0430  0.0388  0.0284  139 CYS B O   
5226  C CB  . CYS B 139 ? 0.4610 0.3390 0.2816 0.0445  0.0334  0.0280  139 CYS B CB  
5227  S SG  . CYS B 139 ? 0.5374 0.3917 0.3380 0.0522  0.0258  0.0310  139 CYS B SG  
5228  N N   . GLY B 140 ? 0.4221 0.3177 0.2446 0.0581  0.0264  0.0257  140 GLY B N   
5229  C CA  . GLY B 140 ? 0.4423 0.3372 0.2563 0.0606  0.0251  0.0270  140 GLY B CA  
5230  C C   . GLY B 140 ? 0.4985 0.3708 0.2888 0.0604  0.0239  0.0320  140 GLY B C   
5231  O O   . GLY B 140 ? 0.5921 0.4475 0.3720 0.0588  0.0233  0.0346  140 GLY B O   
5232  N N   . ARG B 141 ? 0.4784 0.3489 0.2585 0.0622  0.0233  0.0333  141 ARG B N   
5233  C CA  . ARG B 141 ? 0.4901 0.3377 0.2439 0.0611  0.0230  0.0385  141 ARG B CA  
5234  C C   . ARG B 141 ? 0.5010 0.3269 0.2415 0.0683  0.0140  0.0399  141 ARG B C   
5235  O O   . ARG B 141 ? 0.5230 0.3270 0.2448 0.0641  0.0152  0.0447  141 ARG B O   
5236  C CB  . ARG B 141 ? 0.4823 0.3325 0.2280 0.0643  0.0219  0.0384  141 ARG B CB  
5237  C CG  . ARG B 141 ? 0.5869 0.4149 0.3036 0.0605  0.0246  0.0442  141 ARG B CG  
5238  C CD  . ARG B 141 ? 0.7156 0.5479 0.4251 0.0636  0.0239  0.0433  141 ARG B CD  
5239  N NE  . ARG B 141 ? 0.7881 0.6158 0.4953 0.0759  0.0115  0.0410  141 ARG B NE  
5240  C CZ  . ARG B 141 ? 0.7437 0.5485 0.4254 0.0813  0.0047  0.0439  141 ARG B CZ  
5241  N NH1 . ARG B 141 ? 0.8204 0.6039 0.4748 0.0747  0.0101  0.0501  141 ARG B NH1 
5242  N NH2 . ARG B 141 ? 0.7556 0.5587 0.4390 0.0931  -0.0075 0.0404  141 ARG B NH2 
5243  N N   . THR B 142 ? 0.4974 0.3291 0.2481 0.0789  0.0047  0.0352  142 THR B N   
5244  C CA  . THR B 142 ? 0.5986 0.4109 0.3383 0.0875  -0.0055 0.0350  142 THR B CA  
5245  C C   . THR B 142 ? 0.5796 0.3814 0.3187 0.0840  -0.0041 0.0362  142 THR B C   
5246  O O   . THR B 142 ? 0.6063 0.3821 0.3240 0.0840  -0.0073 0.0404  142 THR B O   
5247  C CB  . THR B 142 ? 0.6025 0.4289 0.3598 0.0988  -0.0145 0.0276  142 THR B CB  
5248  O OG1 . THR B 142 ? 0.6145 0.4487 0.3713 0.1023  -0.0169 0.0263  142 THR B OG1 
5249  C CG2 . THR B 142 ? 0.5568 0.3652 0.3055 0.1090  -0.0260 0.0256  142 THR B CG2 
5250  N N   . LEU B 143 ? 0.4928 0.3131 0.2539 0.0811  0.0002  0.0325  143 LEU B N   
5251  C CA  . LEU B 143 ? 0.5571 0.3689 0.3191 0.0782  0.0011  0.0327  143 LEU B CA  
5252  C C   . LEU B 143 ? 0.6081 0.4085 0.3581 0.0660  0.0097  0.0386  143 LEU B C   
5253  O O   . LEU B 143 ? 0.5237 0.3078 0.2661 0.0636  0.0090  0.0403  143 LEU B O   
5254  C CB  . LEU B 143 ? 0.4695 0.3042 0.2571 0.0789  0.0031  0.0267  143 LEU B CB  
5255  C CG  . LEU B 143 ? 0.4610 0.3058 0.2611 0.0902  -0.0049 0.0200  143 LEU B CG  
5256  C CD1 . LEU B 143 ? 0.4382 0.3025 0.2603 0.0899  -0.0019 0.0143  143 LEU B CD1 
5257  C CD2 . LEU B 143 ? 0.4974 0.3205 0.2839 0.0993  -0.0150 0.0193  143 LEU B CD2 
5258  N N   . ARG B 144 ? 0.5693 0.3775 0.3176 0.0582  0.0177  0.0411  144 ARG B N   
5259  C CA  . ARG B 144 ? 0.5835 0.3817 0.3211 0.0461  0.0265  0.0459  144 ARG B CA  
5260  C C   . ARG B 144 ? 0.6683 0.4341 0.3766 0.0448  0.0238  0.0520  144 ARG B C   
5261  O O   . ARG B 144 ? 0.6679 0.4212 0.3666 0.0344  0.0302  0.0558  144 ARG B O   
5262  C CB  . ARG B 144 ? 0.6277 0.4417 0.3697 0.0388  0.0355  0.0462  144 ARG B CB  
5263  C CG  . ARG B 144 ? 0.5583 0.3973 0.3255 0.0336  0.0414  0.0417  144 ARG B CG  
5264  C CD  . ARG B 144 ? 0.5862 0.4425 0.3596 0.0297  0.0478  0.0404  144 ARG B CD  
5265  N NE  . ARG B 144 ? 0.5960 0.4754 0.3926 0.0267  0.0513  0.0356  144 ARG B NE  
5266  C CZ  . ARG B 144 ? 0.6408 0.5278 0.4443 0.0171  0.0591  0.0345  144 ARG B CZ  
5267  N NH1 . ARG B 144 ? 0.6818 0.5561 0.4717 0.0085  0.0656  0.0379  144 ARG B NH1 
5268  N NH2 . ARG B 144 ? 0.6197 0.5264 0.4435 0.0160  0.0603  0.0296  144 ARG B NH2 
5269  N N   . LYS B 145 ? 0.6722 0.4230 0.3660 0.0551  0.0139  0.0527  145 LYS B N   
5270  C CA  . LYS B 145 ? 0.7480 0.4643 0.4126 0.0554  0.0091  0.0583  145 LYS B CA  
5271  C C   . LYS B 145 ? 0.7765 0.4803 0.4429 0.0619  0.0003  0.0560  145 LYS B C   
5272  O O   . LYS B 145 ? 0.8299 0.5114 0.4818 0.0559  0.0013  0.0601  145 LYS B O   
5273  C CB  . LYS B 145 ? 0.8824 0.5845 0.5263 0.0636  0.0015  0.0602  145 LYS B CB  
5274  C CG  . LYS B 145 ? 0.9724 0.6764 0.6042 0.0557  0.0105  0.0641  145 LYS B CG  
5275  C CD  . LYS B 145 ? 1.0137 0.7483 0.6674 0.0604  0.0111  0.0586  145 LYS B CD  
5276  C CE  . LYS B 145 ? 1.0168 0.7595 0.6647 0.0515  0.0220  0.0608  145 LYS B CE  
5277  N NZ  . LYS B 145 ? 0.9677 0.7439 0.6458 0.0474  0.0295  0.0556  145 LYS B NZ  
5278  N N   . ASP B 146 ? 0.7713 0.4894 0.4557 0.0738  -0.0080 0.0492  146 ASP B N   
5279  C CA  . ASP B 146 ? 0.8479 0.5567 0.5361 0.0812  -0.0164 0.0454  146 ASP B CA  
5280  C C   . ASP B 146 ? 0.8547 0.5663 0.5523 0.0721  -0.0094 0.0455  146 ASP B C   
5281  O O   . ASP B 146 ? 0.9587 0.6479 0.6446 0.0720  -0.0135 0.0470  146 ASP B O   
5282  C CB  . ASP B 146 ? 0.9072 0.6379 0.6181 0.0937  -0.0235 0.0367  146 ASP B CB  
5283  C CG  . ASP B 146 ? 0.9882 0.7178 0.6925 0.1032  -0.0314 0.0355  146 ASP B CG  
5284  O OD1 . ASP B 146 ? 1.0213 0.7390 0.7059 0.0992  -0.0293 0.0414  146 ASP B OD1 
5285  O OD2 . ASP B 146 ? 1.0882 0.8296 0.8073 0.1146  -0.0396 0.0280  146 ASP B OD2 
5286  N N   . LEU B 147 ? 0.7226 0.4604 0.4408 0.0649  0.0001  0.0434  147 LEU B N   
5287  C CA  . LEU B 147 ? 0.7280 0.4716 0.4578 0.0572  0.0058  0.0422  147 LEU B CA  
5288  C C   . LEU B 147 ? 0.7044 0.4401 0.4246 0.0425  0.0158  0.0479  147 LEU B C   
5289  O O   . LEU B 147 ? 0.6629 0.4087 0.3960 0.0347  0.0218  0.0462  147 LEU B O   
5290  C CB  . LEU B 147 ? 0.6516 0.4270 0.4091 0.0583  0.0093  0.0359  147 LEU B CB  
5291  C CG  . LEU B 147 ? 0.6486 0.4371 0.4185 0.0710  0.0020  0.0297  147 LEU B CG  
5292  C CD1 . LEU B 147 ? 0.5595 0.3775 0.3530 0.0699  0.0070  0.0249  147 LEU B CD1 
5293  C CD2 . LEU B 147 ? 0.7038 0.4793 0.4719 0.0794  -0.0065 0.0259  147 LEU B CD2 
5294  N N   . LYS B 148 ? 0.6523 0.3702 0.3499 0.0384  0.0176  0.0540  148 LYS B N   
5295  C CA  . LYS B 148 ? 0.6679 0.3808 0.3570 0.0234  0.0287  0.0588  148 LYS B CA  
5296  C C   . LYS B 148 ? 0.7608 0.4623 0.4503 0.0150  0.0312  0.0594  148 LYS B C   
5297  O O   . LYS B 148 ? 0.8014 0.5144 0.5012 0.0033  0.0408  0.0589  148 LYS B O   
5298  C CB  . LYS B 148 ? 0.6775 0.3654 0.3362 0.0209  0.0290  0.0658  148 LYS B CB  
5299  C CG  . LYS B 148 ? 0.6907 0.3646 0.3344 0.0046  0.0400  0.0713  148 LYS B CG  
5300  C CD  . LYS B 148 ? 0.8178 0.4685 0.4297 0.0021  0.0414  0.0782  148 LYS B CD  
5301  C CE  . LYS B 148 ? 0.9023 0.5435 0.5012 -0.0159 0.0552  0.0831  148 LYS B CE  
5302  N NZ  . LYS B 148 ? 1.0186 0.6474 0.5914 -0.0194 0.0600  0.0883  148 LYS B NZ  
5303  N N   . ASP B 149 ? 0.7947 0.4738 0.4737 0.0211  0.0220  0.0597  149 ASP B N   
5304  C CA  . ASP B 149 ? 0.8302 0.4960 0.5081 0.0134  0.0235  0.0602  149 ASP B CA  
5305  C C   . ASP B 149 ? 0.7852 0.4769 0.4917 0.0129  0.0258  0.0533  149 ASP B C   
5306  O O   . ASP B 149 ? 0.7667 0.4573 0.4782 0.0025  0.0311  0.0531  149 ASP B O   
5307  C CB  . ASP B 149 ? 0.9250 0.5595 0.5843 0.0214  0.0118  0.0616  149 ASP B CB  
5308  C CG  . ASP B 149 ? 1.0365 0.6421 0.6647 0.0234  0.0075  0.0683  149 ASP B CG  
5309  O OD1 . ASP B 149 ? 1.0495 0.6452 0.6617 0.0113  0.0163  0.0746  149 ASP B OD1 
5310  O OD2 . ASP B 149 ? 1.0552 0.6482 0.6748 0.0373  -0.0049 0.0668  149 ASP B OD2 
5311  N N   . LEU B 150 ? 0.7825 0.4967 0.5071 0.0236  0.0218  0.0476  150 LEU B N   
5312  C CA  . LEU B 150 ? 0.7243 0.4630 0.4738 0.0230  0.0243  0.0413  150 LEU B CA  
5313  C C   . LEU B 150 ? 0.7070 0.4667 0.4690 0.0127  0.0345  0.0412  150 LEU B C   
5314  O O   . LEU B 150 ? 0.6460 0.4156 0.4214 0.0062  0.0384  0.0381  150 LEU B O   
5315  C CB  . LEU B 150 ? 0.7172 0.4737 0.4809 0.0360  0.0185  0.0355  150 LEU B CB  
5316  C CG  . LEU B 150 ? 0.7616 0.5089 0.5246 0.0476  0.0088  0.0313  150 LEU B CG  
5317  C CD1 . LEU B 150 ? 0.7953 0.5405 0.5653 0.0446  0.0089  0.0280  150 LEU B CD1 
5318  C CD2 . LEU B 150 ? 0.8698 0.5883 0.6101 0.0521  0.0015  0.0353  150 LEU B CD2 
5319  N N   . LEU B 151 ? 0.6580 0.4254 0.4167 0.0121  0.0381  0.0435  151 LEU B N   
5320  C CA  . LEU B 151 ? 0.6782 0.4669 0.4497 0.0037  0.0472  0.0423  151 LEU B CA  
5321  C C   . LEU B 151 ? 0.7223 0.5026 0.4888 -0.0106 0.0553  0.0446  151 LEU B C   
5322  O O   . LEU B 151 ? 0.7363 0.5343 0.5198 -0.0178 0.0610  0.0408  151 LEU B O   
5323  C CB  . LEU B 151 ? 0.6610 0.4576 0.4280 0.0068  0.0488  0.0440  151 LEU B CB  
5324  C CG  . LEU B 151 ? 0.6538 0.4656 0.4323 0.0191  0.0422  0.0400  151 LEU B CG  
5325  C CD1 . LEU B 151 ? 0.7269 0.5287 0.4901 0.0267  0.0374  0.0429  151 LEU B CD1 
5326  C CD2 . LEU B 151 ? 0.5296 0.3695 0.3290 0.0173  0.0467  0.0356  151 LEU B CD2 
5327  N N   . ASN B 152 ? 0.7388 0.4918 0.4820 -0.0151 0.0557  0.0506  152 ASN B N   
5328  C CA  . ASN B 152 ? 0.8087 0.5518 0.5460 -0.0302 0.0642  0.0530  152 ASN B CA  
5329  C C   . ASN B 152 ? 0.7879 0.5295 0.5367 -0.0345 0.0629  0.0495  152 ASN B C   
5330  O O   . ASN B 152 ? 0.7842 0.5288 0.5390 -0.0474 0.0708  0.0486  152 ASN B O   
5331  C CB  . ASN B 152 ? 0.9402 0.6504 0.6460 -0.0341 0.0645  0.0609  152 ASN B CB  
5332  C CG  . ASN B 152 ? 1.0862 0.7965 0.7783 -0.0312 0.0665  0.0644  152 ASN B CG  
5333  O OD1 . ASN B 152 ? 1.2037 0.9398 0.9107 -0.0300 0.0706  0.0610  152 ASN B OD1 
5334  N ND2 . ASN B 152 ? 1.1400 0.8198 0.8023 -0.0298 0.0628  0.0710  152 ASN B ND2 
5335  N N   . LYS B 153 ? 0.7754 0.5130 0.5279 -0.0241 0.0534  0.0469  153 LYS B N   
5336  C CA  . LYS B 153 ? 0.7928 0.5328 0.5585 -0.0266 0.0516  0.0422  153 LYS B CA  
5337  C C   . LYS B 153 ? 0.7335 0.5024 0.5235 -0.0323 0.0576  0.0365  153 LYS B C   
5338  O O   . LYS B 153 ? 0.7155 0.4855 0.5128 -0.0431 0.0623  0.0345  153 LYS B O   
5339  C CB  . LYS B 153 ? 0.8369 0.5755 0.6061 -0.0127 0.0412  0.0387  153 LYS B CB  
5340  C CG  . LYS B 153 ? 0.8391 0.5483 0.5875 -0.0064 0.0331  0.0421  153 LYS B CG  
5341  C CD  . LYS B 153 ? 0.7953 0.5092 0.5500 0.0088  0.0238  0.0372  153 LYS B CD  
5342  C CE  . LYS B 153 ? 0.7435 0.4761 0.5191 0.0101  0.0236  0.0301  153 LYS B CE  
5343  N NZ  . LYS B 153 ? 0.7172 0.4399 0.4943 0.0018  0.0243  0.0287  153 LYS B NZ  
5344  N N   . GLY B 154 ? 0.7387 0.5306 0.5417 -0.0247 0.0568  0.0333  154 GLY B N   
5345  C CA  . GLY B 154 ? 0.7088 0.5271 0.5338 -0.0279 0.0605  0.0276  154 GLY B CA  
5346  C C   . GLY B 154 ? 0.6768 0.5005 0.5155 -0.0271 0.0564  0.0218  154 GLY B C   
5347  O O   . GLY B 154 ? 0.6594 0.5039 0.5154 -0.0274 0.0572  0.0166  154 GLY B O   
5348  N N   . ARG B 155 ? 0.6941 0.4984 0.5243 -0.0256 0.0514  0.0225  155 ARG B N   
5349  C CA  . ARG B 155 ? 0.6972 0.5034 0.5380 -0.0258 0.0477  0.0170  155 ARG B CA  
5350  C C   . ARG B 155 ? 0.6831 0.4722 0.5139 -0.0165 0.0397  0.0171  155 ARG B C   
5351  O O   . ARG B 155 ? 0.6782 0.4514 0.4936 -0.0114 0.0369  0.0214  155 ARG B O   
5352  C CB  . ARG B 155 ? 0.6979 0.4970 0.5415 -0.0392 0.0518  0.0160  155 ARG B CB  
5353  C CG  . ARG B 155 ? 0.7422 0.5422 0.5832 -0.0512 0.0612  0.0193  155 ARG B CG  
5354  C CD  . ARG B 155 ? 0.7595 0.5560 0.6074 -0.0648 0.0655  0.0166  155 ARG B CD  
5355  N NE  . ARG B 155 ? 0.7842 0.6015 0.6547 -0.0647 0.0634  0.0082  155 ARG B NE  
5356  C CZ  . ARG B 155 ? 0.8141 0.6530 0.7024 -0.0717 0.0688  0.0031  155 ARG B CZ  
5357  N NH1 . ARG B 155 ? 0.8353 0.6899 0.7421 -0.0699 0.0646  -0.0048 155 ARG B NH1 
5358  N NH2 . ARG B 155 ? 0.8147 0.6593 0.7021 -0.0799 0.0781  0.0053  155 ARG B NH2 
5359  N N   . ASN B 156 ? 0.6273 0.4196 0.4668 -0.0141 0.0355  0.0115  156 ASN B N   
5360  C CA  . ASN B 156 ? 0.6231 0.3980 0.4546 -0.0078 0.0285  0.0099  156 ASN B CA  
5361  C C   . ASN B 156 ? 0.6232 0.3945 0.4467 0.0049  0.0238  0.0109  156 ASN B C   
5362  O O   . ASN B 156 ? 0.6165 0.3666 0.4259 0.0088  0.0193  0.0133  156 ASN B O   
5363  C CB  . ASN B 156 ? 0.6809 0.4302 0.5002 -0.0160 0.0282  0.0132  156 ASN B CB  
5364  C CG  . ASN B 156 ? 0.6742 0.4276 0.5021 -0.0304 0.0343  0.0123  156 ASN B CG  
5365  O OD1 . ASN B 156 ? 0.7332 0.4757 0.5527 -0.0405 0.0397  0.0172  156 ASN B OD1 
5366  N ND2 . ASN B 156 ? 0.6256 0.3943 0.4697 -0.0317 0.0335  0.0057  156 ASN B ND2 
5367  N N   . TYR B 157 ? 0.5296 0.3210 0.3622 0.0115  0.0243  0.0086  157 TYR B N   
5368  C CA  . TYR B 157 ? 0.4948 0.2861 0.3228 0.0230  0.0204  0.0084  157 TYR B CA  
5369  C C   . TYR B 157 ? 0.5492 0.3394 0.3798 0.0315  0.0151  0.0023  157 TYR B C   
5370  O O   . TYR B 157 ? 0.5231 0.3208 0.3616 0.0297  0.0154  -0.0022 157 TYR B O   
5371  C CB  . TYR B 157 ? 0.4650 0.2776 0.3011 0.0255  0.0238  0.0088  157 TYR B CB  
5372  C CG  . TYR B 157 ? 0.5539 0.3662 0.3851 0.0192  0.0285  0.0145  157 TYR B CG  
5373  C CD1 . TYR B 157 ? 0.5576 0.3547 0.3744 0.0220  0.0266  0.0192  157 TYR B CD1 
5374  C CD2 . TYR B 157 ? 0.4942 0.3208 0.3346 0.0109  0.0344  0.0146  157 TYR B CD2 
5375  C CE1 . TYR B 157 ? 0.5628 0.3586 0.3728 0.0160  0.0313  0.0244  157 TYR B CE1 
5376  C CE2 . TYR B 157 ? 0.5420 0.3691 0.3779 0.0051  0.0395  0.0191  157 TYR B CE2 
5377  C CZ  . TYR B 157 ? 0.5815 0.3929 0.4014 0.0074  0.0384  0.0242  157 TYR B CZ  
5378  O OH  . TYR B 157 ? 0.5908 0.4019 0.4040 0.0015  0.0438  0.0285  157 TYR B OH  
5379  N N   . THR B 158 ? 0.5420 0.3222 0.3652 0.0409  0.0099  0.0015  158 THR B N   
5380  C CA  . THR B 158 ? 0.5738 0.3548 0.4000 0.0500  0.0054  -0.0053 158 THR B CA  
5381  C C   . THR B 158 ? 0.5478 0.3484 0.3824 0.0580  0.0064  -0.0086 158 THR B C   
5382  O O   . THR B 158 ? 0.5149 0.3233 0.3504 0.0584  0.0084  -0.0052 158 THR B O   
5383  C CB  . THR B 158 ? 0.6218 0.3787 0.4358 0.0560  -0.0020 -0.0060 158 THR B CB  
5384  O OG1 . THR B 158 ? 0.6078 0.3582 0.4140 0.0614  -0.0048 -0.0025 158 THR B OG1 
5385  C CG2 . THR B 158 ? 0.6001 0.3356 0.4049 0.0469  -0.0029 -0.0026 158 THR B CG2 
5386  N N   . GLN B 159 ? 0.5245 0.3332 0.3651 0.0640  0.0055  -0.0156 159 GLN B N   
5387  C CA  . GLN B 159 ? 0.5065 0.3337 0.3554 0.0708  0.0072  -0.0195 159 GLN B CA  
5388  C C   . GLN B 159 ? 0.4943 0.3175 0.3405 0.0789  0.0031  -0.0192 159 GLN B C   
5389  O O   . GLN B 159 ? 0.4569 0.2947 0.3094 0.0812  0.0052  -0.0191 159 GLN B O   
5390  C CB  . GLN B 159 ? 0.5249 0.3586 0.3783 0.0757  0.0073  -0.0276 159 GLN B CB  
5391  C CG  . GLN B 159 ? 0.5277 0.3805 0.3898 0.0817  0.0102  -0.0326 159 GLN B CG  
5392  C CD  . GLN B 159 ? 0.5765 0.4466 0.4445 0.0756  0.0166  -0.0306 159 GLN B CD  
5393  O OE1 . GLN B 159 ? 0.5229 0.3918 0.3893 0.0679  0.0183  -0.0269 159 GLN B OE1 
5394  N NE2 . GLN B 159 ? 0.5479 0.4339 0.4231 0.0791  0.0198  -0.0336 159 GLN B NE2 
5395  N N   . GLU B 160 ? 0.5320 0.3345 0.3686 0.0834  -0.0036 -0.0194 160 GLU B N   
5396  C CA  . GLU B 160 ? 0.5928 0.3883 0.4251 0.0921  -0.0096 -0.0196 160 GLU B CA  
5397  C C   . GLU B 160 ? 0.5352 0.3292 0.3620 0.0877  -0.0081 -0.0118 160 GLU B C   
5398  O O   . GLU B 160 ? 0.5344 0.3341 0.3631 0.0943  -0.0107 -0.0126 160 GLU B O   
5399  C CB  . GLU B 160 ? 0.6611 0.4304 0.4811 0.0974  -0.0182 -0.0207 160 GLU B CB  
5400  C CG  . GLU B 160 ? 0.7899 0.5478 0.6028 0.1070  -0.0264 -0.0208 160 GLU B CG  
5401  C CD  . GLU B 160 ? 0.9353 0.7061 0.7600 0.1202  -0.0307 -0.0314 160 GLU B CD  
5402  O OE1 . GLU B 160 ? 0.9570 0.7458 0.7945 0.1210  -0.0260 -0.0382 160 GLU B OE1 
5403  O OE2 . GLU B 160 ? 0.9953 0.7581 0.8163 0.1298  -0.0388 -0.0333 160 GLU B OE2 
5404  N N   . GLU B 161 ? 0.5542 0.3405 0.3742 0.0768  -0.0041 -0.0048 161 GLU B N   
5405  C CA  . GLU B 161 ? 0.5443 0.3299 0.3585 0.0721  -0.0016 0.0022  161 GLU B CA  
5406  C C   . GLU B 161 ? 0.5156 0.3272 0.3431 0.0705  0.0043  0.0015  161 GLU B C   
5407  O O   . GLU B 161 ? 0.4746 0.2908 0.3010 0.0729  0.0039  0.0037  161 GLU B O   
5408  C CB  . GLU B 161 ? 0.5401 0.3114 0.3444 0.0601  0.0020  0.0087  161 GLU B CB  
5409  C CG  . GLU B 161 ? 0.6314 0.3731 0.4192 0.0603  -0.0038 0.0110  161 GLU B CG  
5410  C CD  . GLU B 161 ? 0.7106 0.4407 0.4922 0.0469  0.0010  0.0157  161 GLU B CD  
5411  O OE1 . GLU B 161 ? 0.6858 0.4333 0.4788 0.0388  0.0082  0.0156  161 GLU B OE1 
5412  O OE2 . GLU B 161 ? 0.7348 0.4383 0.5004 0.0444  -0.0026 0.0192  161 GLU B OE2 
5413  N N   . LYS B 162 ? 0.5002 0.3272 0.3389 0.0668  0.0090  -0.0016 162 LYS B N   
5414  C CA  . LYS B 162 ? 0.4902 0.3400 0.3405 0.0657  0.0138  -0.0028 162 LYS B CA  
5415  C C   . LYS B 162 ? 0.4784 0.3389 0.3354 0.0753  0.0113  -0.0075 162 LYS B C   
5416  O O   . LYS B 162 ? 0.5489 0.4212 0.4105 0.0758  0.0129  -0.0063 162 LYS B O   
5417  C CB  . LYS B 162 ? 0.4379 0.2983 0.2960 0.0610  0.0178  -0.0057 162 LYS B CB  
5418  C CG  . LYS B 162 ? 0.4434 0.3246 0.3116 0.0600  0.0220  -0.0070 162 LYS B CG  
5419  C CD  . LYS B 162 ? 0.4163 0.3043 0.2889 0.0559  0.0246  -0.0099 162 LYS B CD  
5420  C CE  . LYS B 162 ? 0.4225 0.3089 0.2954 0.0613  0.0232  -0.0161 162 LYS B CE  
5421  N NZ  . LYS B 162 ? 0.3942 0.2862 0.2688 0.0582  0.0254  -0.0193 162 LYS B NZ  
5422  N N   . GLU B 163 ? 0.5361 0.3935 0.3947 0.0828  0.0075  -0.0137 163 GLU B N   
5423  C CA  . GLU B 163 ? 0.5251 0.3938 0.3921 0.0919  0.0051  -0.0195 163 GLU B CA  
5424  C C   . GLU B 163 ? 0.4828 0.3419 0.3432 0.0975  -0.0011 -0.0171 163 GLU B C   
5425  O O   . GLU B 163 ? 0.4804 0.3518 0.3488 0.1030  -0.0025 -0.0203 163 GLU B O   
5426  C CB  . GLU B 163 ? 0.5909 0.4592 0.4618 0.0989  0.0027  -0.0279 163 GLU B CB  
5427  C CG  . GLU B 163 ? 0.6480 0.5256 0.5236 0.0937  0.0088  -0.0307 163 GLU B CG  
5428  C CD  . GLU B 163 ? 0.7343 0.6104 0.6121 0.1002  0.0069  -0.0392 163 GLU B CD  
5429  O OE1 . GLU B 163 ? 0.7666 0.6323 0.6420 0.1086  0.0001  -0.0428 163 GLU B OE1 
5430  O OE2 . GLU B 163 ? 0.7102 0.5944 0.5910 0.0972  0.0119  -0.0425 163 GLU B OE2 
5431  N N   . TYR B 164 ? 0.4887 0.3254 0.3339 0.0958  -0.0050 -0.0115 164 TYR B N   
5432  C CA  . TYR B 164 ? 0.5972 0.4220 0.4324 0.1008  -0.0112 -0.0085 164 TYR B CA  
5433  C C   . TYR B 164 ? 0.5480 0.3837 0.3845 0.0958  -0.0067 -0.0036 164 TYR B C   
5434  O O   . TYR B 164 ? 0.6028 0.4426 0.4405 0.1020  -0.0106 -0.0047 164 TYR B O   
5435  C CB  . TYR B 164 ? 0.6258 0.4210 0.4412 0.0990  -0.0158 -0.0030 164 TYR B CB  
5436  C CG  . TYR B 164 ? 0.6772 0.4565 0.4782 0.1042  -0.0228 0.0007  164 TYR B CG  
5437  C CD1 . TYR B 164 ? 0.7119 0.4856 0.5126 0.1173  -0.0329 -0.0051 164 TYR B CD1 
5438  C CD2 . TYR B 164 ? 0.6987 0.4689 0.4863 0.0963  -0.0194 0.0093  164 TYR B CD2 
5439  C CE1 . TYR B 164 ? 0.7093 0.4665 0.4949 0.1228  -0.0407 -0.0019 164 TYR B CE1 
5440  C CE2 . TYR B 164 ? 0.7394 0.4931 0.5109 0.1010  -0.0259 0.0129  164 TYR B CE2 
5441  C CZ  . TYR B 164 ? 0.7422 0.4885 0.5120 0.1144  -0.0370 0.0075  164 TYR B CZ  
5442  O OH  . TYR B 164 ? 0.7587 0.4871 0.5108 0.1195  -0.0446 0.0110  164 TYR B OH  
5443  N N   . VAL B 165 ? 0.4821 0.3236 0.3196 0.0852  0.0010  0.0009  165 VAL B N   
5444  C CA  . VAL B 165 ? 0.5103 0.3635 0.3502 0.0805  0.0054  0.0047  165 VAL B CA  
5445  C C   . VAL B 165 ? 0.5134 0.3895 0.3693 0.0847  0.0065  -0.0006 165 VAL B C   
5446  O O   . VAL B 165 ? 0.4129 0.2952 0.2701 0.0873  0.0052  0.0000  165 VAL B O   
5447  C CB  . VAL B 165 ? 0.5099 0.3658 0.3497 0.0690  0.0128  0.0088  165 VAL B CB  
5448  C CG1 . VAL B 165 ? 0.5257 0.3975 0.3716 0.0652  0.0173  0.0107  165 VAL B CG1 
5449  C CG2 . VAL B 165 ? 0.4764 0.3104 0.3003 0.0633  0.0128  0.0145  165 VAL B CG2 
5450  N N   . LEU B 166 ? 0.4604 0.3484 0.3277 0.0849  0.0092  -0.0060 166 LEU B N   
5451  C CA  . LEU B 166 ? 0.4297 0.3386 0.3113 0.0872  0.0115  -0.0109 166 LEU B CA  
5452  C C   . LEU B 166 ? 0.4042 0.3161 0.2904 0.0969  0.0055  -0.0157 166 LEU B C   
5453  O O   . LEU B 166 ? 0.3819 0.3079 0.2767 0.0979  0.0063  -0.0174 166 LEU B O   
5454  C CB  . LEU B 166 ? 0.4445 0.3624 0.3343 0.0861  0.0154  -0.0161 166 LEU B CB  
5455  C CG  . LEU B 166 ? 0.4985 0.4221 0.3892 0.0771  0.0215  -0.0134 166 LEU B CG  
5456  C CD1 . LEU B 166 ? 0.5461 0.4705 0.4387 0.0769  0.0235  -0.0181 166 LEU B CD1 
5457  C CD2 . LEU B 166 ? 0.4418 0.3814 0.3402 0.0743  0.0250  -0.0129 166 LEU B CD2 
5458  N N   . ASN B 167 ? 0.4090 0.3081 0.2904 0.1044  -0.0010 -0.0188 167 ASN B N   
5459  C CA  . ASN B 167 ? 0.4624 0.3643 0.3492 0.1149  -0.0082 -0.0248 167 ASN B CA  
5460  C C   . ASN B 167 ? 0.4618 0.3572 0.3403 0.1165  -0.0126 -0.0200 167 ASN B C   
5461  O O   . ASN B 167 ? 0.4208 0.3274 0.3085 0.1222  -0.0160 -0.0245 167 ASN B O   
5462  C CB  . ASN B 167 ? 0.5663 0.4531 0.4481 0.1233  -0.0156 -0.0293 167 ASN B CB  
5463  C CG  . ASN B 167 ? 0.7174 0.6167 0.6123 0.1255  -0.0124 -0.0380 167 ASN B CG  
5464  O OD1 . ASN B 167 ? 0.7420 0.6631 0.6528 0.1260  -0.0080 -0.0441 167 ASN B OD1 
5465  N ND2 . ASN B 167 ? 0.7620 0.6469 0.6492 0.1263  -0.0141 -0.0386 167 ASN B ND2 
5466  N N   . LYS B 168 ? 0.4414 0.3188 0.3025 0.1113  -0.0125 -0.0115 168 LYS B N   
5467  C CA  . LYS B 168 ? 0.4643 0.3348 0.3151 0.1122  -0.0158 -0.0068 168 LYS B CA  
5468  C C   . LYS B 168 ? 0.4323 0.3227 0.2934 0.1070  -0.0098 -0.0058 168 LYS B C   
5469  O O   . LYS B 168 ? 0.4565 0.3504 0.3177 0.1109  -0.0135 -0.0062 168 LYS B O   
5470  C CB  . LYS B 168 ? 0.5193 0.3659 0.3481 0.1064  -0.0155 0.0020  168 LYS B CB  
5471  C CG  . LYS B 168 ? 0.5666 0.3901 0.3828 0.1100  -0.0212 0.0022  168 LYS B CG  
5472  C CD  . LYS B 168 ? 0.7174 0.5313 0.5299 0.1231  -0.0331 -0.0026 168 LYS B CD  
5473  C CE  . LYS B 168 ? 0.7989 0.5975 0.5932 0.1250  -0.0382 0.0029  168 LYS B CE  
5474  N NZ  . LYS B 168 ? 0.8570 0.6369 0.6408 0.1379  -0.0519 -0.0006 168 LYS B NZ  
5475  N N   . TYR B 169 ? 0.4289 0.3313 0.2980 0.0986  -0.0014 -0.0049 169 TYR B N   
5476  C CA  . TYR B 169 ? 0.3992 0.3186 0.2772 0.0938  0.0037  -0.0042 169 TYR B CA  
5477  C C   . TYR B 169 ? 0.4032 0.3401 0.2971 0.0993  0.0017  -0.0113 169 TYR B C   
5478  O O   . TYR B 169 ? 0.5051 0.4499 0.4025 0.1000  0.0007  -0.0112 169 TYR B O   
5479  C CB  . TYR B 169 ? 0.4445 0.3711 0.3267 0.0847  0.0116  -0.0024 169 TYR B CB  
5480  C CG  . TYR B 169 ? 0.4032 0.3195 0.2741 0.0771  0.0150  0.0042  169 TYR B CG  
5481  C CD1 . TYR B 169 ? 0.4849 0.3827 0.3401 0.0775  0.0122  0.0087  169 TYR B CD1 
5482  C CD2 . TYR B 169 ? 0.3957 0.3203 0.2714 0.0693  0.0210  0.0055  169 TYR B CD2 
5483  C CE1 . TYR B 169 ? 0.4663 0.3560 0.3121 0.0693  0.0167  0.0142  169 TYR B CE1 
5484  C CE2 . TYR B 169 ? 0.4136 0.3311 0.2818 0.0622  0.0244  0.0101  169 TYR B CE2 
5485  C CZ  . TYR B 169 ? 0.4441 0.3452 0.2981 0.0617  0.0230  0.0143  169 TYR B CZ  
5486  O OH  . TYR B 169 ? 0.4126 0.3085 0.2606 0.0534  0.0277  0.0182  169 TYR B OH  
5487  N N   . PHE B 170 ? 0.4406 0.3841 0.3447 0.1030  0.0015  -0.0180 170 PHE B N   
5488  C CA  . PHE B 170 ? 0.4540 0.4148 0.3745 0.1077  0.0003  -0.0257 170 PHE B CA  
5489  C C   . PHE B 170 ? 0.4599 0.4162 0.3794 0.1175  -0.0093 -0.0286 170 PHE B C   
5490  O O   . PHE B 170 ? 0.4164 0.3864 0.3476 0.1200  -0.0110 -0.0331 170 PHE B O   
5491  C CB  . PHE B 170 ? 0.4604 0.4302 0.3920 0.1092  0.0033  -0.0330 170 PHE B CB  
5492  C CG  . PHE B 170 ? 0.4954 0.4757 0.4317 0.1000  0.0126  -0.0320 170 PHE B CG  
5493  C CD1 . PHE B 170 ? 0.4952 0.4908 0.4410 0.0955  0.0169  -0.0329 170 PHE B CD1 
5494  C CD2 . PHE B 170 ? 0.4992 0.4721 0.4289 0.0960  0.0164  -0.0301 170 PHE B CD2 
5495  C CE1 . PHE B 170 ? 0.4530 0.4552 0.4002 0.0872  0.0246  -0.0316 170 PHE B CE1 
5496  C CE2 . PHE B 170 ? 0.4644 0.4451 0.3963 0.0881  0.0238  -0.0292 170 PHE B CE2 
5497  C CZ  . PHE B 170 ? 0.4146 0.4092 0.3544 0.0839  0.0278  -0.0298 170 PHE B CZ  
5498  N N   . GLU B 171 ? 0.4876 0.4235 0.3923 0.1229  -0.0163 -0.0263 171 GLU B N   
5499  C CA  . GLU B 171 ? 0.5138 0.4417 0.4133 0.1320  -0.0265 -0.0279 171 GLU B CA  
5500  C C   . GLU B 171 ? 0.5083 0.4389 0.4034 0.1285  -0.0258 -0.0231 171 GLU B C   
5501  O O   . GLU B 171 ? 0.4937 0.4318 0.3958 0.1345  -0.0316 -0.0275 171 GLU B O   
5502  C CB  . GLU B 171 ? 0.5915 0.4923 0.4706 0.1369  -0.0339 -0.0243 171 GLU B CB  
5503  C CG  . GLU B 171 ? 0.6784 0.5756 0.5626 0.1441  -0.0383 -0.0314 171 GLU B CG  
5504  C CD  . GLU B 171 ? 0.7920 0.6594 0.6544 0.1493  -0.0469 -0.0278 171 GLU B CD  
5505  O OE1 . GLU B 171 ? 0.7957 0.6453 0.6391 0.1495  -0.0514 -0.0210 171 GLU B OE1 
5506  O OE2 . GLU B 171 ? 0.8314 0.6920 0.6944 0.1529  -0.0491 -0.0316 171 GLU B OE2 
5507  N N   . ILE B 172 ? 0.4825 0.4082 0.3673 0.1191  -0.0189 -0.0148 172 ILE B N   
5508  C CA  . ILE B 172 ? 0.4701 0.3984 0.3503 0.1160  -0.0178 -0.0107 172 ILE B CA  
5509  C C   . ILE B 172 ? 0.4358 0.3875 0.3357 0.1143  -0.0148 -0.0156 172 ILE B C   
5510  O O   . ILE B 172 ? 0.3721 0.3290 0.2745 0.1173  -0.0188 -0.0172 172 ILE B O   
5511  C CB  . ILE B 172 ? 0.4675 0.3872 0.3345 0.1062  -0.0105 -0.0023 172 ILE B CB  
5512  C CG1 . ILE B 172 ? 0.4888 0.3830 0.3334 0.1072  -0.0138 0.0032  172 ILE B CG1 
5513  C CG2 . ILE B 172 ? 0.4192 0.3466 0.2857 0.1022  -0.0077 0.0005  172 ILE B CG2 
5514  C CD1 . ILE B 172 ? 0.5000 0.3806 0.3289 0.1132  -0.0214 0.0052  172 ILE B CD1 
5515  N N   . ILE B 173 ? 0.3994 0.3644 0.3125 0.1092  -0.0080 -0.0183 173 ILE B N   
5516  C CA  . ILE B 173 ? 0.4199 0.4047 0.3497 0.1062  -0.0045 -0.0224 173 ILE B CA  
5517  C C   . ILE B 173 ? 0.3811 0.3761 0.3246 0.1143  -0.0109 -0.0309 173 ILE B C   
5518  O O   . ILE B 173 ? 0.4120 0.4180 0.3643 0.1139  -0.0120 -0.0333 173 ILE B O   
5519  C CB  . ILE B 173 ? 0.4133 0.4072 0.3511 0.0992  0.0040  -0.0233 173 ILE B CB  
5520  C CG1 . ILE B 173 ? 0.4206 0.4076 0.3476 0.0911  0.0094  -0.0157 173 ILE B CG1 
5521  C CG2 . ILE B 173 ? 0.4077 0.4201 0.3618 0.0963  0.0073  -0.0283 173 ILE B CG2 
5522  C CD1 . ILE B 173 ? 0.4018 0.3943 0.3332 0.0846  0.0164  -0.0161 173 ILE B CD1 
5523  N N   . LYS B 174 ? 0.3783 0.3702 0.3249 0.1218  -0.0157 -0.0365 174 LYS B N   
5524  C CA  . LYS B 174 ? 0.4680 0.4721 0.4310 0.1298  -0.0219 -0.0465 174 LYS B CA  
5525  C C   . LYS B 174 ? 0.4314 0.4293 0.3889 0.1370  -0.0321 -0.0468 174 LYS B C   
5526  O O   . LYS B 174 ? 0.4413 0.4530 0.4149 0.1419  -0.0367 -0.0550 174 LYS B O   
5527  C CB  . LYS B 174 ? 0.5573 0.5591 0.5250 0.1374  -0.0257 -0.0535 174 LYS B CB  
5528  C CG  . LYS B 174 ? 0.6211 0.6303 0.5953 0.1314  -0.0161 -0.0551 174 LYS B CG  
5529  C CD  . LYS B 174 ? 0.6864 0.6834 0.6548 0.1381  -0.0202 -0.0578 174 LYS B CD  
5530  C CE  . LYS B 174 ? 0.7131 0.7232 0.6943 0.1356  -0.0126 -0.0644 174 LYS B CE  
5531  N NZ  . LYS B 174 ? 0.7454 0.7531 0.7186 0.1245  -0.0024 -0.0572 174 LYS B NZ  
5532  N N   . LYS B 175 ? 0.3933 0.3709 0.3285 0.1378  -0.0357 -0.0386 175 LYS B N   
5533  C CA  . LYS B 175 ? 0.4588 0.4283 0.3855 0.1450  -0.0456 -0.0387 175 LYS B CA  
5534  C C   . LYS B 175 ? 0.5157 0.4893 0.4389 0.1388  -0.0421 -0.0338 175 LYS B C   
5535  O O   . LYS B 175 ? 0.5453 0.5100 0.4573 0.1436  -0.0492 -0.0325 175 LYS B O   
5536  C CB  . LYS B 175 ? 0.5581 0.5001 0.4596 0.1507  -0.0530 -0.0334 175 LYS B CB  
5537  C CG  . LYS B 175 ? 0.6868 0.6179 0.5838 0.1529  -0.0533 -0.0338 175 LYS B CG  
5538  C CD  . LYS B 175 ? 0.8234 0.7677 0.7415 0.1615  -0.0585 -0.0458 175 LYS B CD  
5539  C CE  . LYS B 175 ? 0.8176 0.7583 0.7369 0.1605  -0.0546 -0.0470 175 LYS B CE  
5540  N NZ  . LYS B 175 ? 0.8835 0.7982 0.7774 0.1570  -0.0537 -0.0371 175 LYS B NZ  
5541  N N   . THR B 176 ? 0.4318 0.4181 0.3635 0.1288  -0.0318 -0.0316 176 THR B N   
5542  C CA  . THR B 176 ? 0.4689 0.4565 0.3948 0.1225  -0.0279 -0.0262 176 THR B CA  
5543  C C   . THR B 176 ? 0.4762 0.4765 0.4144 0.1252  -0.0326 -0.0316 176 THR B C   
5544  O O   . THR B 176 ? 0.4820 0.4761 0.4097 0.1269  -0.0366 -0.0290 176 THR B O   
5545  C CB  . THR B 176 ? 0.3950 0.3898 0.3250 0.1119  -0.0169 -0.0226 176 THR B CB  
5546  O OG1 . THR B 176 ? 0.3528 0.3332 0.2680 0.1091  -0.0135 -0.0164 176 THR B OG1 
5547  C CG2 . THR B 176 ? 0.3930 0.3937 0.3229 0.1062  -0.0138 -0.0196 176 THR B CG2 
5548  N N   . LEU B 177 ? 0.4017 0.4199 0.3620 0.1251  -0.0318 -0.0396 177 LEU B N   
5549  C CA  . LEU B 177 ? 0.3455 0.3758 0.3189 0.1274  -0.0368 -0.0456 177 LEU B CA  
5550  C C   . LEU B 177 ? 0.4280 0.4498 0.3958 0.1391  -0.0496 -0.0494 177 LEU B C   
5551  O O   . LEU B 177 ? 0.3669 0.3900 0.3343 0.1418  -0.0555 -0.0509 177 LEU B O   
5552  C CB  . LEU B 177 ? 0.3471 0.3985 0.3460 0.1241  -0.0327 -0.0540 177 LEU B CB  
5553  C CG  . LEU B 177 ? 0.3529 0.4114 0.3556 0.1121  -0.0209 -0.0502 177 LEU B CG  
5554  C CD1 . LEU B 177 ? 0.3985 0.4761 0.4240 0.1083  -0.0161 -0.0586 177 LEU B CD1 
5555  C CD2 . LEU B 177 ? 0.4057 0.4620 0.4011 0.1065  -0.0193 -0.0445 177 LEU B CD2 
5556  N N   . SER B 178 ? 0.3628 0.3741 0.3245 0.1465  -0.0549 -0.0510 178 SER B N   
5557  C CA  . SER B 178 ? 0.4574 0.4573 0.4110 0.1587  -0.0685 -0.0546 178 SER B CA  
5558  C C   . SER B 178 ? 0.3960 0.3771 0.3238 0.1595  -0.0720 -0.0466 178 SER B C   
5559  O O   . SER B 178 ? 0.4064 0.3841 0.3307 0.1669  -0.0822 -0.0499 178 SER B O   
5560  C CB  . SER B 178 ? 0.4971 0.4847 0.4445 0.1661  -0.0735 -0.0564 178 SER B CB  
5561  O OG  . SER B 178 ? 0.5865 0.5924 0.5595 0.1694  -0.0742 -0.0674 178 SER B OG  
5562  N N   . ILE B 179 ? 0.4455 0.4146 0.3550 0.1520  -0.0638 -0.0365 179 ILE B N   
5563  C CA  . ILE B 179 ? 0.5259 0.4766 0.4095 0.1526  -0.0662 -0.0293 179 ILE B CA  
5564  C C   . ILE B 179 ? 0.4544 0.4159 0.3431 0.1500  -0.0657 -0.0302 179 ILE B C   
5565  O O   . ILE B 179 ? 0.4648 0.4152 0.3378 0.1549  -0.0725 -0.0291 179 ILE B O   
5566  C CB  . ILE B 179 ? 0.5475 0.4837 0.4117 0.1448  -0.0571 -0.0194 179 ILE B CB  
5567  C CG1 . ILE B 179 ? 0.5914 0.5040 0.4255 0.1474  -0.0611 -0.0130 179 ILE B CG1 
5568  C CG2 . ILE B 179 ? 0.5085 0.4584 0.3814 0.1336  -0.0451 -0.0161 179 ILE B CG2 
5569  C CD1 . ILE B 179 ? 0.5898 0.4868 0.4047 0.1399  -0.0529 -0.0042 179 ILE B CD1 
5570  N N   . TYR B 180 ? 0.3845 0.3664 0.2942 0.1428  -0.0585 -0.0327 180 TYR B N   
5571  C CA  . TYR B 180 ? 0.4182 0.4101 0.3343 0.1406  -0.0589 -0.0345 180 TYR B CA  
5572  C C   . TYR B 180 ? 0.4450 0.4423 0.3712 0.1498  -0.0710 -0.0432 180 TYR B C   
5573  O O   . TYR B 180 ? 0.4051 0.3977 0.3223 0.1532  -0.0769 -0.0434 180 TYR B O   
5574  C CB  . TYR B 180 ? 0.3931 0.4028 0.3279 0.1306  -0.0492 -0.0351 180 TYR B CB  
5575  C CG  . TYR B 180 ? 0.3784 0.3828 0.3018 0.1220  -0.0390 -0.0268 180 TYR B CG  
5576  C CD1 . TYR B 180 ? 0.4270 0.4270 0.3383 0.1193  -0.0372 -0.0225 180 TYR B CD1 
5577  C CD2 . TYR B 180 ? 0.3843 0.3886 0.3095 0.1170  -0.0316 -0.0241 180 TYR B CD2 
5578  C CE1 . TYR B 180 ? 0.4193 0.4161 0.3223 0.1118  -0.0283 -0.0163 180 TYR B CE1 
5579  C CE2 . TYR B 180 ? 0.3764 0.3764 0.2926 0.1095  -0.0232 -0.0175 180 TYR B CE2 
5580  C CZ  . TYR B 180 ? 0.3814 0.3785 0.2876 0.1069  -0.0216 -0.0139 180 TYR B CZ  
5581  O OH  . TYR B 180 ? 0.3326 0.3273 0.2323 0.0999  -0.0138 -0.0088 180 TYR B OH  
5582  N N   . ARG B 181 ? 0.4513 0.4588 0.3965 0.1543  -0.0752 -0.0514 181 ARG B N   
5583  C CA  . ARG B 181 ? 0.4521 0.4628 0.4062 0.1649  -0.0885 -0.0607 181 ARG B CA  
5584  C C   . ARG B 181 ? 0.5145 0.5012 0.4412 0.1748  -0.0994 -0.0576 181 ARG B C   
5585  O O   . ARG B 181 ? 0.5269 0.5100 0.4482 0.1808  -0.1088 -0.0604 181 ARG B O   
5586  C CB  . ARG B 181 ? 0.4081 0.4320 0.3851 0.1690  -0.0909 -0.0702 181 ARG B CB  
5587  C CG  . ARG B 181 ? 0.4307 0.4790 0.4356 0.1597  -0.0810 -0.0752 181 ARG B CG  
5588  C CD  . ARG B 181 ? 0.4756 0.5378 0.5034 0.1651  -0.0841 -0.0865 181 ARG B CD  
5589  N NE  . ARG B 181 ? 0.5271 0.6094 0.5766 0.1547  -0.0719 -0.0896 181 ARG B NE  
5590  C CZ  . ARG B 181 ? 0.5498 0.6323 0.5986 0.1496  -0.0623 -0.0867 181 ARG B CZ  
5591  N NH1 . ARG B 181 ? 0.5336 0.5980 0.5629 0.1538  -0.0636 -0.0808 181 ARG B NH1 
5592  N NH2 . ARG B 181 ? 0.5317 0.6316 0.5983 0.1399  -0.0513 -0.0897 181 ARG B NH2 
5593  N N   . GLU B 182 ? 0.5416 0.5102 0.4497 0.1765  -0.0986 -0.0519 182 GLU B N   
5594  C CA  . GLU B 182 ? 0.6167 0.5580 0.4939 0.1843  -0.1075 -0.0472 182 GLU B CA  
5595  C C   . GLU B 182 ? 0.6025 0.5344 0.4595 0.1823  -0.1073 -0.0416 182 GLU B C   
5596  O O   . GLU B 182 ? 0.6159 0.5388 0.4627 0.1913  -0.1193 -0.0449 182 GLU B O   
5597  C CB  . GLU B 182 ? 0.7574 0.6813 0.6167 0.1812  -0.1017 -0.0392 182 GLU B CB  
5598  C CG  . GLU B 182 ? 0.8569 0.7498 0.6795 0.1852  -0.1071 -0.0316 182 GLU B CG  
5599  C CD  . GLU B 182 ? 0.8847 0.7574 0.6942 0.1916  -0.1135 -0.0308 182 GLU B CD  
5600  O OE1 . GLU B 182 ? 0.9220 0.7716 0.7085 0.2010  -0.1257 -0.0303 182 GLU B OE1 
5601  O OE2 . GLU B 182 ? 0.8685 0.7464 0.6882 0.1872  -0.1065 -0.0302 182 GLU B OE2 
5602  N N   . ILE B 183 ? 0.5031 0.4365 0.3536 0.1713  -0.0943 -0.0338 183 ILE B N   
5603  C CA  . ILE B 183 ? 0.5838 0.5066 0.4125 0.1697  -0.0933 -0.0286 183 ILE B CA  
5604  C C   . ILE B 183 ? 0.5612 0.4982 0.4035 0.1723  -0.0990 -0.0353 183 ILE B C   
5605  O O   . ILE B 183 ? 0.5437 0.4701 0.3679 0.1763  -0.1044 -0.0344 183 ILE B O   
5606  C CB  . ILE B 183 ? 0.5873 0.5102 0.4085 0.1576  -0.0783 -0.0201 183 ILE B CB  
5607  C CG1 . ILE B 183 ? 0.6009 0.5486 0.4505 0.1495  -0.0697 -0.0229 183 ILE B CG1 
5608  C CG2 . ILE B 183 ? 0.5798 0.4873 0.3870 0.1550  -0.0736 -0.0139 183 ILE B CG2 
5609  C CD1 . ILE B 183 ? 0.5489 0.5066 0.4022 0.1454  -0.0666 -0.0233 183 ILE B CD1 
5610  N N   . LYS B 184 ? 0.5273 0.4876 0.4008 0.1698  -0.0976 -0.0422 184 LYS B N   
5611  C CA  . LYS B 184 ? 0.5028 0.4773 0.3921 0.1714  -0.1030 -0.0493 184 LYS B CA  
5612  C C   . LYS B 184 ? 0.4454 0.4143 0.3334 0.1843  -0.1195 -0.0571 184 LYS B C   
5613  O O   . LYS B 184 ? 0.4504 0.4153 0.3301 0.1886  -0.1268 -0.0591 184 LYS B O   
5614  C CB  . LYS B 184 ? 0.5121 0.5111 0.4340 0.1644  -0.0967 -0.0546 184 LYS B CB  
5615  C CG  . LYS B 184 ? 0.5365 0.5508 0.4792 0.1665  -0.1037 -0.0637 184 LYS B CG  
5616  C CD  . LYS B 184 ? 0.5470 0.5830 0.5185 0.1576  -0.0954 -0.0677 184 LYS B CD  
5617  C CE  . LYS B 184 ? 0.5655 0.6117 0.5471 0.1524  -0.0948 -0.0700 184 LYS B CE  
5618  N NZ  . LYS B 184 ? 0.6292 0.6730 0.6094 0.1615  -0.1084 -0.0765 184 LYS B NZ  
5619  N N   . GLU B 185 ? 0.5076 0.4757 0.4035 0.1911  -0.1261 -0.0620 185 GLU B N   
5620  C CA  . GLU B 185 ? 0.5596 0.5237 0.4574 0.2043  -0.1430 -0.0710 185 GLU B CA  
5621  C C   . GLU B 185 ? 0.5695 0.5045 0.4299 0.2123  -0.1520 -0.0656 185 GLU B C   
5622  O O   . GLU B 185 ? 0.5822 0.5119 0.4377 0.2219  -0.1658 -0.0714 185 GLU B O   
5623  C CB  . GLU B 185 ? 0.6630 0.6336 0.5788 0.2098  -0.1474 -0.0781 185 GLU B CB  
5624  C CG  . GLU B 185 ? 0.7747 0.7282 0.6781 0.2252  -0.1651 -0.0834 185 GLU B CG  
5625  C CD  . GLU B 185 ? 0.8706 0.8384 0.8015 0.2316  -0.1710 -0.0947 185 GLU B CD  
5626  O OE1 . GLU B 185 ? 0.8948 0.8767 0.8476 0.2394  -0.1824 -0.1072 185 GLU B OE1 
5627  O OE2 . GLU B 185 ? 0.8864 0.8522 0.8179 0.2289  -0.1641 -0.0918 185 GLU B OE2 
5628  N N   . GLU B 186 ? 0.5459 0.4612 0.3790 0.2079  -0.1442 -0.0546 186 GLU B N   
5629  C CA  . GLU B 186 ? 0.6039 0.4894 0.3979 0.2133  -0.1503 -0.0481 186 GLU B CA  
5630  C C   . GLU B 186 ? 0.5991 0.4826 0.3784 0.2087  -0.1456 -0.0440 186 GLU B C   
5631  O O   . GLU B 186 ? 0.6640 0.5234 0.4093 0.2120  -0.1491 -0.0387 186 GLU B O   
5632  C CB  . GLU B 186 ? 0.5539 0.4189 0.3246 0.2091  -0.1429 -0.0382 186 GLU B CB  
5633  C CG  . GLU B 186 ? 0.6608 0.5219 0.4397 0.2157  -0.1496 -0.0420 186 GLU B CG  
5634  C CD  . GLU B 186 ? 0.7200 0.5599 0.4759 0.2108  -0.1423 -0.0322 186 GLU B CD  
5635  O OE1 . GLU B 186 ? 0.7042 0.5443 0.4521 0.1988  -0.1275 -0.0236 186 GLU B OE1 
5636  O OE2 . GLU B 186 ? 0.7740 0.5970 0.5205 0.2191  -0.1520 -0.0335 186 GLU B OE2 
5637  N N   . GLY B 187 ? 0.5599 0.4671 0.3629 0.2011  -0.1377 -0.0466 187 GLY B N   
5638  C CA  . GLY B 187 ? 0.5399 0.4473 0.3319 0.1969  -0.1333 -0.0439 187 GLY B CA  
5639  C C   . GLY B 187 ? 0.5975 0.4932 0.3657 0.1879  -0.1195 -0.0331 187 GLY B C   
5640  O O   . GLY B 187 ? 0.5998 0.4916 0.3529 0.1858  -0.1164 -0.0308 187 GLY B O   
5641  N N   . LYS B 188 ? 0.6266 0.5172 0.3918 0.1825  -0.1112 -0.0272 188 LYS B N   
5642  C CA  . LYS B 188 ? 0.6283 0.5108 0.3753 0.1727  -0.0972 -0.0179 188 LYS B CA  
5643  C C   . LYS B 188 ? 0.5725 0.4770 0.3401 0.1624  -0.0849 -0.0177 188 LYS B C   
5644  O O   . LYS B 188 ? 0.5563 0.4577 0.3118 0.1544  -0.0735 -0.0117 188 LYS B O   
5645  C CB  . LYS B 188 ? 0.5814 0.4509 0.3197 0.1705  -0.0935 -0.0124 188 LYS B CB  
5646  C CG  . LYS B 188 ? 0.6457 0.4865 0.3546 0.1798  -0.1049 -0.0105 188 LYS B CG  
5647  C CD  . LYS B 188 ? 0.6845 0.5120 0.3866 0.1783  -0.1027 -0.0059 188 LYS B CD  
5648  C CE  . LYS B 188 ? 0.7537 0.5466 0.4174 0.1844  -0.1108 -0.0009 188 LYS B CE  
5649  N NZ  . LYS B 188 ? 0.7824 0.5674 0.4495 0.1981  -0.1283 -0.0076 188 LYS B NZ  
5650  N N   . GLY B 189 ? 0.5595 0.4855 0.3572 0.1623  -0.0872 -0.0245 189 GLY B N   
5651  C CA  . GLY B 189 ? 0.5006 0.4452 0.3170 0.1530  -0.0770 -0.0244 189 GLY B CA  
5652  C C   . GLY B 189 ? 0.4683 0.4327 0.3150 0.1538  -0.0816 -0.0324 189 GLY B C   
5653  O O   . GLY B 189 ? 0.4736 0.4415 0.3329 0.1594  -0.0895 -0.0378 189 GLY B O   
5654  N N   . SER B 190 ? 0.4481 0.4254 0.3065 0.1483  -0.0773 -0.0339 190 SER B N   
5655  C CA  . SER B 190 ? 0.4242 0.4198 0.3111 0.1462  -0.0793 -0.0405 190 SER B CA  
5656  C C   . SER B 190 ? 0.4211 0.4267 0.3222 0.1366  -0.0682 -0.0375 190 SER B C   
5657  O O   . SER B 190 ? 0.3848 0.3855 0.2750 0.1312  -0.0593 -0.0311 190 SER B O   
5658  C CB  . SER B 190 ? 0.4851 0.4864 0.3754 0.1463  -0.0828 -0.0442 190 SER B CB  
5659  O OG  . SER B 190 ? 0.5464 0.5371 0.4209 0.1555  -0.0932 -0.0469 190 SER B OG  
5660  N N   . VAL B 191 ? 0.4327 0.4519 0.3577 0.1344  -0.0689 -0.0426 191 VAL B N   
5661  C CA  . VAL B 191 ? 0.3759 0.4042 0.3140 0.1254  -0.0590 -0.0404 191 VAL B CA  
5662  C C   . VAL B 191 ? 0.4304 0.4718 0.3870 0.1198  -0.0584 -0.0446 191 VAL B C   
5663  O O   . VAL B 191 ? 0.4487 0.4983 0.4202 0.1223  -0.0650 -0.0517 191 VAL B O   
5664  C CB  . VAL B 191 ? 0.3524 0.3843 0.3010 0.1261  -0.0580 -0.0423 191 VAL B CB  
5665  C CG1 . VAL B 191 ? 0.3181 0.3594 0.2795 0.1162  -0.0476 -0.0405 191 VAL B CG1 
5666  C CG2 . VAL B 191 ? 0.3834 0.4000 0.3129 0.1312  -0.0590 -0.0379 191 VAL B CG2 
5667  N N   . SER B 192 ? 0.3491 0.3917 0.3046 0.1122  -0.0508 -0.0405 192 SER B N   
5668  C CA  . SER B 192 ? 0.3142 0.3656 0.2838 0.1057  -0.0494 -0.0430 192 SER B CA  
5669  C C   . SER B 192 ? 0.3447 0.4013 0.3238 0.0974  -0.0407 -0.0409 192 SER B C   
5670  O O   . SER B 192 ? 0.3436 0.3974 0.3184 0.0971  -0.0359 -0.0376 192 SER B O   
5671  C CB  . SER B 192 ? 0.3193 0.3663 0.2787 0.1046  -0.0491 -0.0407 192 SER B CB  
5672  O OG  . SER B 192 ? 0.4020 0.4446 0.3518 0.1005  -0.0411 -0.0346 192 SER B OG  
5673  N N   . THR B 193 ? 0.3669 0.4296 0.3575 0.0905  -0.0390 -0.0427 193 THR B N   
5674  C CA  . THR B 193 ? 0.3189 0.3838 0.3146 0.0818  -0.0307 -0.0401 193 THR B CA  
5675  C C   . THR B 193 ? 0.3124 0.3742 0.3058 0.0761  -0.0299 -0.0383 193 THR B C   
5676  O O   . THR B 193 ? 0.3082 0.3673 0.2974 0.0792  -0.0354 -0.0395 193 THR B O   
5677  C CB  . THR B 193 ? 0.3312 0.4064 0.3446 0.0780  -0.0288 -0.0451 193 THR B CB  
5678  O OG1 . THR B 193 ? 0.3999 0.4750 0.4139 0.0699  -0.0200 -0.0419 193 THR B OG1 
5679  C CG2 . THR B 193 ? 0.3071 0.3891 0.3342 0.0753  -0.0333 -0.0511 193 THR B CG2 
5680  N N   . SER B 194 ? 0.2846 0.3456 0.2795 0.0682  -0.0235 -0.0356 194 SER B N   
5681  C CA  . SER B 194 ? 0.2955 0.3518 0.2882 0.0623  -0.0232 -0.0341 194 SER B CA  
5682  C C   . SER B 194 ? 0.3534 0.4131 0.3570 0.0534  -0.0198 -0.0360 194 SER B C   
5683  O O   . SER B 194 ? 0.2727 0.3394 0.2849 0.0516  -0.0156 -0.0380 194 SER B O   
5684  C CB  . SER B 194 ? 0.3046 0.3536 0.2853 0.0607  -0.0191 -0.0286 194 SER B CB  
5685  O OG  . SER B 194 ? 0.3489 0.3952 0.3199 0.0674  -0.0212 -0.0273 194 SER B OG  
5686  N N   . PRO B 195 ? 0.3889 0.4433 0.3919 0.0475  -0.0212 -0.0358 195 PRO B N   
5687  C CA  . PRO B 195 ? 0.4218 0.4759 0.4305 0.0371  -0.0160 -0.0360 195 PRO B CA  
5688  C C   . PRO B 195 ? 0.3576 0.4106 0.3615 0.0336  -0.0078 -0.0323 195 PRO B C   
5689  O O   . PRO B 195 ? 0.3382 0.3856 0.3311 0.0370  -0.0069 -0.0281 195 PRO B O   
5690  C CB  . PRO B 195 ? 0.4013 0.4436 0.4020 0.0329  -0.0196 -0.0340 195 PRO B CB  
5691  C CG  . PRO B 195 ? 0.4381 0.4805 0.4378 0.0411  -0.0281 -0.0364 195 PRO B CG  
5692  C CD  . PRO B 195 ? 0.4085 0.4564 0.4055 0.0502  -0.0280 -0.0360 195 PRO B CD  
5693  N N   . TYR B 196 ? 0.3391 0.3975 0.3515 0.0262  -0.0014 -0.0344 196 TYR B N   
5694  C CA  . TYR B 196 ? 0.2790 0.3425 0.2928 0.0257  0.0058  -0.0341 196 TYR B CA  
5695  C C   . TYR B 196 ? 0.3469 0.4005 0.3453 0.0264  0.0086  -0.0279 196 TYR B C   
5696  O O   . TYR B 196 ? 0.3036 0.3593 0.2996 0.0324  0.0094  -0.0269 196 TYR B O   
5697  C CB  . TYR B 196 ? 0.3098 0.3787 0.3325 0.0155  0.0135  -0.0371 196 TYR B CB  
5698  C CG  . TYR B 196 ? 0.3186 0.3990 0.3501 0.0174  0.0193  -0.0407 196 TYR B CG  
5699  C CD1 . TYR B 196 ? 0.3126 0.3885 0.3342 0.0173  0.0249  -0.0369 196 TYR B CD1 
5700  C CD2 . TYR B 196 ? 0.3315 0.4272 0.3818 0.0199  0.0183  -0.0485 196 TYR B CD2 
5701  C CE1 . TYR B 196 ? 0.3249 0.4107 0.3546 0.0198  0.0295  -0.0407 196 TYR B CE1 
5702  C CE2 . TYR B 196 ? 0.3276 0.4338 0.3867 0.0228  0.0226  -0.0528 196 TYR B CE2 
5703  C CZ  . TYR B 196 ? 0.3016 0.4025 0.3500 0.0227  0.0283  -0.0488 196 TYR B CZ  
5704  O OH  . TYR B 196 ? 0.3556 0.4667 0.4130 0.0261  0.0320  -0.0538 196 TYR B OH  
5705  N N   . TYR B 197 ? 0.3454 0.3873 0.3330 0.0201  0.0096  -0.0240 197 TYR B N   
5706  C CA  . TYR B 197 ? 0.3762 0.4092 0.3505 0.0200  0.0122  -0.0191 197 TYR B CA  
5707  C C   . TYR B 197 ? 0.3667 0.3915 0.3314 0.0252  0.0057  -0.0164 197 TYR B C   
5708  O O   . TYR B 197 ? 0.3692 0.3845 0.3229 0.0238  0.0060  -0.0129 197 TYR B O   
5709  C CB  . TYR B 197 ? 0.3564 0.3809 0.3234 0.0098  0.0180  -0.0170 197 TYR B CB  
5710  C CG  . TYR B 197 ? 0.3773 0.4117 0.3532 0.0052  0.0264  -0.0203 197 TYR B CG  
5711  C CD1 . TYR B 197 ? 0.2934 0.3324 0.2690 0.0085  0.0309  -0.0203 197 TYR B CD1 
5712  C CD2 . TYR B 197 ? 0.3032 0.3433 0.2890 -0.0024 0.0299  -0.0242 197 TYR B CD2 
5713  C CE1 . TYR B 197 ? 0.3486 0.3976 0.3333 0.0053  0.0383  -0.0243 197 TYR B CE1 
5714  C CE2 . TYR B 197 ? 0.3032 0.3549 0.2994 -0.0064 0.0381  -0.0285 197 TYR B CE2 
5715  C CZ  . TYR B 197 ? 0.3859 0.4421 0.3812 -0.0020 0.0421  -0.0287 197 TYR B CZ  
5716  O OH  . TYR B 197 ? 0.3945 0.4627 0.4003 -0.0048 0.0501  -0.0339 197 TYR B OH  
5717  N N   . HIS B 198 ? 0.3722 0.4013 0.3413 0.0317  -0.0002 -0.0185 198 HIS B N   
5718  C CA  . HIS B 198 ? 0.3309 0.3553 0.2929 0.0373  -0.0057 -0.0173 198 HIS B CA  
5719  C C   . HIS B 198 ? 0.3504 0.3627 0.3042 0.0335  -0.0093 -0.0158 198 HIS B C   
5720  O O   . HIS B 198 ? 0.3750 0.3813 0.3207 0.0353  -0.0105 -0.0139 198 HIS B O   
5721  C CB  . HIS B 198 ? 0.3360 0.3610 0.2926 0.0413  -0.0027 -0.0149 198 HIS B CB  
5722  C CG  . HIS B 198 ? 0.3352 0.3606 0.2881 0.0480  -0.0066 -0.0151 198 HIS B CG  
5723  N ND1 . HIS B 198 ? 0.3064 0.3261 0.2525 0.0486  -0.0083 -0.0140 198 HIS B ND1 
5724  C CD2 . HIS B 198 ? 0.3413 0.3720 0.2956 0.0542  -0.0087 -0.0167 198 HIS B CD2 
5725  C CE1 . HIS B 198 ? 0.3472 0.3703 0.2923 0.0543  -0.0104 -0.0154 198 HIS B CE1 
5726  N NE2 . HIS B 198 ? 0.3275 0.3564 0.2762 0.0576  -0.0104 -0.0166 198 HIS B NE2 
5727  N N   . PRO B 199 ? 0.3920 0.3998 0.3477 0.0280  -0.0115 -0.0170 199 PRO B N   
5728  C CA  . PRO B 199 ? 0.4032 0.3964 0.3488 0.0247  -0.0162 -0.0155 199 PRO B CA  
5729  C C   . PRO B 199 ? 0.4615 0.4526 0.4066 0.0311  -0.0249 -0.0180 199 PRO B C   
5730  O O   . PRO B 199 ? 0.4058 0.4068 0.3579 0.0374  -0.0267 -0.0208 199 PRO B O   
5731  C CB  . PRO B 199 ? 0.4266 0.4152 0.3740 0.0149  -0.0137 -0.0156 199 PRO B CB  
5732  C CG  . PRO B 199 ? 0.4623 0.4654 0.4249 0.0165  -0.0128 -0.0198 199 PRO B CG  
5733  C CD  . PRO B 199 ? 0.4333 0.4483 0.4003 0.0242  -0.0102 -0.0203 199 PRO B CD  
5734  N N   . LEU B 200 ? 0.4239 0.4012 0.3601 0.0298  -0.0307 -0.0173 200 LEU B N   
5735  C CA  . LEU B 200 ? 0.4691 0.4433 0.4050 0.0356  -0.0396 -0.0207 200 LEU B CA  
5736  C C   . LEU B 200 ? 0.5003 0.4696 0.4395 0.0305  -0.0431 -0.0223 200 LEU B C   
5737  O O   . LEU B 200 ? 0.4697 0.4236 0.4009 0.0247  -0.0464 -0.0209 200 LEU B O   
5738  C CB  . LEU B 200 ? 0.4900 0.4522 0.4154 0.0383  -0.0454 -0.0203 200 LEU B CB  
5739  C CG  . LEU B 200 ? 0.5021 0.4713 0.4270 0.0442  -0.0432 -0.0203 200 LEU B CG  
5740  C CD1 . LEU B 200 ? 0.5824 0.5387 0.4979 0.0456  -0.0494 -0.0205 200 LEU B CD1 
5741  C CD2 . LEU B 200 ? 0.4890 0.4716 0.4212 0.0526  -0.0443 -0.0244 200 LEU B CD2 
5742  N N   . ILE B 201 ? 0.4310 0.4189 0.3737 0.0352  0.0150  -0.0292 201 ILE B N   
5743  C CA  . ILE B 201 ? 0.3882 0.3638 0.3288 0.0318  0.0107  -0.0367 201 ILE B CA  
5744  C C   . ILE B 201 ? 0.4326 0.3922 0.3611 0.0374  0.0082  -0.0389 201 ILE B C   
5745  O O   . ILE B 201 ? 0.4345 0.3805 0.3626 0.0306  0.0059  -0.0418 201 ILE B O   
5746  C CB  . ILE B 201 ? 0.4300 0.4100 0.3723 0.0338  0.0065  -0.0422 201 ILE B CB  
5747  C CG1 . ILE B 201 ? 0.3744 0.3669 0.3299 0.0271  0.0078  -0.0415 201 ILE B CG1 
5748  C CG2 . ILE B 201 ? 0.3901 0.3566 0.3292 0.0323  -0.0004 -0.0504 201 ILE B CG2 
5749  C CD1 . ILE B 201 ? 0.3898 0.3815 0.3570 0.0158  0.0088  -0.0438 201 ILE B CD1 
5750  N N   . PRO B 202 ? 0.3603 0.3197 0.2786 0.0497  0.0088  -0.0376 202 PRO B N   
5751  C CA  . PRO B 202 ? 0.3603 0.3018 0.2658 0.0563  0.0057  -0.0408 202 PRO B CA  
5752  C C   . PRO B 202 ? 0.3548 0.2859 0.2607 0.0505  0.0064  -0.0373 202 PRO B C   
5753  O O   . PRO B 202 ? 0.4116 0.3227 0.3091 0.0500  0.0021  -0.0411 202 PRO B O   
5754  C CB  . PRO B 202 ? 0.3833 0.3325 0.2807 0.0715  0.0091  -0.0379 202 PRO B CB  
5755  C CG  . PRO B 202 ? 0.4376 0.4027 0.3390 0.0727  0.0112  -0.0369 202 PRO B CG  
5756  C CD  . PRO B 202 ? 0.4171 0.3912 0.3341 0.0589  0.0121  -0.0339 202 PRO B CD  
5757  N N   . ILE B 203 ? 0.3411 0.2833 0.2552 0.0460  0.0108  -0.0301 203 ILE B N   
5758  C CA  . ILE B 203 ? 0.3476 0.2793 0.2592 0.0413  0.0111  -0.0262 203 ILE B CA  
5759  C C   . ILE B 203 ? 0.4077 0.3296 0.3222 0.0276  0.0110  -0.0280 203 ILE B C   
5760  O O   . ILE B 203 ? 0.4339 0.3381 0.3414 0.0238  0.0097  -0.0272 203 ILE B O   
5761  C CB  . ILE B 203 ? 0.3671 0.3131 0.2850 0.0418  0.0142  -0.0184 203 ILE B CB  
5762  C CG1 . ILE B 203 ? 0.4180 0.3740 0.3356 0.0551  0.0149  -0.0152 203 ILE B CG1 
5763  C CG2 . ILE B 203 ? 0.3335 0.2671 0.2467 0.0357  0.0137  -0.0144 203 ILE B CG2 
5764  C CD1 . ILE B 203 ? 0.4301 0.4012 0.3571 0.0546  0.0162  -0.0074 203 ILE B CD1 
5765  N N   . LEU B 204 ? 0.4164 0.3498 0.3416 0.0202  0.0129  -0.0299 204 LEU B N   
5766  C CA  . LEU B 204 ? 0.3749 0.3024 0.3056 0.0077  0.0144  -0.0311 204 LEU B CA  
5767  C C   . LEU B 204 ? 0.3952 0.3070 0.3235 0.0051  0.0090  -0.0368 204 LEU B C   
5768  O O   . LEU B 204 ? 0.3588 0.2568 0.2861 -0.0038 0.0095  -0.0356 204 LEU B O   
5769  C CB  . LEU B 204 ? 0.3066 0.2516 0.2509 0.0021  0.0175  -0.0322 204 LEU B CB  
5770  C CG  . LEU B 204 ? 0.3360 0.2951 0.2831 0.0039  0.0212  -0.0276 204 LEU B CG  
5771  C CD1 . LEU B 204 ? 0.2709 0.2438 0.2304 -0.0007 0.0233  -0.0302 204 LEU B CD1 
5772  C CD2 . LEU B 204 ? 0.3709 0.3234 0.3108 0.0012  0.0242  -0.0217 204 LEU B CD2 
5773  N N   . LEU B 205 ? 0.4246 0.3362 0.3503 0.0128  0.0034  -0.0428 205 LEU B N   
5774  C CA  . LEU B 205 ? 0.4581 0.3515 0.3790 0.0114  -0.0042 -0.0493 205 LEU B CA  
5775  C C   . LEU B 205 ? 0.4994 0.3698 0.4050 0.0158  -0.0068 -0.0480 205 LEU B C   
5776  O O   . LEU B 205 ? 0.5556 0.4063 0.4586 0.0090  -0.0118 -0.0506 205 LEU B O   
5777  C CB  . LEU B 205 ? 0.4183 0.3148 0.3352 0.0210  -0.0103 -0.0564 205 LEU B CB  
5778  C CG  . LEU B 205 ? 0.4431 0.3574 0.3756 0.0151  -0.0108 -0.0591 205 LEU B CG  
5779  C CD1 . LEU B 205 ? 0.4231 0.3418 0.3489 0.0259  -0.0164 -0.0647 205 LEU B CD1 
5780  C CD2 . LEU B 205 ? 0.4381 0.3473 0.3842 0.0010  -0.0142 -0.0621 205 LEU B CD2 
5781  N N   . ASN B 206 ? 0.4826 0.3548 0.3789 0.0270  -0.0041 -0.0439 206 ASN B N   
5782  C CA  . ASN B 206 ? 0.5676 0.4183 0.4482 0.0352  -0.0078 -0.0437 206 ASN B CA  
5783  C C   . ASN B 206 ? 0.5284 0.3889 0.4056 0.0458  -0.0035 -0.0374 206 ASN B C   
5784  O O   . ASN B 206 ? 0.5129 0.3837 0.3873 0.0592  -0.0028 -0.0385 206 ASN B O   
5785  C CB  . ASN B 206 ? 0.6925 0.5293 0.5613 0.0455  -0.0154 -0.0525 206 ASN B CB  
5786  C CG  . ASN B 206 ? 0.7850 0.5936 0.6367 0.0526  -0.0209 -0.0539 206 ASN B CG  
5787  O OD1 . ASN B 206 ? 0.7299 0.5339 0.5773 0.0556  -0.0183 -0.0477 206 ASN B OD1 
5788  N ND2 . ASN B 206 ? 0.8668 0.6545 0.7078 0.0558  -0.0299 -0.0626 206 ASN B ND2 
5789  N N   . PRO B 207 ? 0.4938 0.3523 0.3715 0.0405  -0.0007 -0.0303 207 PRO B N   
5790  C CA  . PRO B 207 ? 0.4480 0.3176 0.3254 0.0499  0.0016  -0.0242 207 PRO B CA  
5791  C C   . PRO B 207 ? 0.4674 0.3278 0.3339 0.0664  -0.0019 -0.0257 207 PRO B C   
5792  O O   . PRO B 207 ? 0.5271 0.4039 0.3979 0.0767  0.0004  -0.0219 207 PRO B O   
5793  C CB  . PRO B 207 ? 0.4638 0.3248 0.3389 0.0405  0.0028  -0.0177 207 PRO B CB  
5794  C CG  . PRO B 207 ? 0.4295 0.2860 0.3091 0.0251  0.0051  -0.0193 207 PRO B CG  
5795  C CD  . PRO B 207 ? 0.4856 0.3331 0.3647 0.0255  0.0009  -0.0272 207 PRO B CD  
5796  N N   . ASN B 208 ? 0.4249 0.2598 0.2783 0.0694  -0.0075 -0.0312 208 ASN B N   
5797  C CA  . ASN B 208 ? 0.4800 0.3039 0.3209 0.0869  -0.0109 -0.0336 208 ASN B CA  
5798  C C   . ASN B 208 ? 0.5100 0.3504 0.3513 0.1009  -0.0083 -0.0379 208 ASN B C   
5799  O O   . ASN B 208 ? 0.4537 0.2924 0.2871 0.1180  -0.0085 -0.0389 208 ASN B O   
5800  C CB  . ASN B 208 ? 0.5066 0.2949 0.3315 0.0860  -0.0188 -0.0389 208 ASN B CB  
5801  C CG  . ASN B 208 ? 0.5915 0.3616 0.4137 0.0728  -0.0202 -0.0330 208 ASN B CG  
5802  O OD1 . ASN B 208 ? 0.5244 0.3019 0.3490 0.0729  -0.0175 -0.0253 208 ASN B OD1 
5803  N ND2 . ASN B 208 ? 0.6275 0.3739 0.4446 0.0611  -0.0247 -0.0359 208 ASN B ND2 
5804  N N   . CYS B 209 ? 0.5655 0.4227 0.4155 0.0950  -0.0053 -0.0397 209 CYS B N   
5805  C CA  . CYS B 209 ? 0.5196 0.3920 0.3677 0.1079  -0.0020 -0.0426 209 CYS B CA  
5806  C C   . CYS B 209 ? 0.5047 0.4026 0.3621 0.1182  0.0052  -0.0348 209 CYS B C   
5807  O O   . CYS B 209 ? 0.4578 0.3667 0.3113 0.1326  0.0094  -0.0357 209 CYS B O   
5808  C CB  . CYS B 209 ? 0.5191 0.4027 0.3743 0.0985  -0.0012 -0.0452 209 CYS B CB  
5809  S SG  . CYS B 209 ? 0.5281 0.4420 0.4045 0.0877  0.0059  -0.0364 209 CYS B SG  
5810  N N   . VAL B 210 ? 0.4970 0.4043 0.3664 0.1115  0.0066  -0.0268 210 VAL B N   
5811  C CA  . VAL B 210 ? 0.4738 0.4050 0.3549 0.1205  0.0115  -0.0192 210 VAL B CA  
5812  C C   . VAL B 210 ? 0.4613 0.3867 0.3335 0.1398  0.0111  -0.0206 210 VAL B C   
5813  O O   . VAL B 210 ? 0.4969 0.4453 0.3794 0.1509  0.0165  -0.0153 210 VAL B O   
5814  C CB  . VAL B 210 ? 0.4545 0.3922 0.3477 0.1092  0.0102  -0.0116 210 VAL B CB  
5815  C CG1 . VAL B 210 ? 0.4652 0.4093 0.3661 0.0925  0.0115  -0.0109 210 VAL B CG1 
5816  C CG2 . VAL B 210 ? 0.4662 0.3779 0.3482 0.1077  0.0038  -0.0121 210 VAL B CG2 
5817  N N   . TYR B 211 ? 0.4297 0.3246 0.2838 0.1442  0.0047  -0.0273 211 TYR B N   
5818  C CA  . TYR B 211 ? 0.4701 0.3560 0.3140 0.1639  0.0034  -0.0293 211 TYR B CA  
5819  C C   . TYR B 211 ? 0.4688 0.3561 0.3005 0.1807  0.0073  -0.0360 211 TYR B C   
5820  O O   . TYR B 211 ? 0.5247 0.4060 0.3467 0.1999  0.0075  -0.0385 211 TYR B O   
5821  C CB  . TYR B 211 ? 0.5194 0.3683 0.3468 0.1619  -0.0060 -0.0334 211 TYR B CB  
5822  C CG  . TYR B 211 ? 0.5274 0.3729 0.3623 0.1483  -0.0091 -0.0261 211 TYR B CG  
5823  C CD1 . TYR B 211 ? 0.5216 0.3838 0.3680 0.1541  -0.0083 -0.0182 211 TYR B CD1 
5824  C CD2 . TYR B 211 ? 0.5650 0.3918 0.3956 0.1297  -0.0126 -0.0268 211 TYR B CD2 
5825  C CE1 . TYR B 211 ? 0.5682 0.4248 0.4177 0.1426  -0.0122 -0.0119 211 TYR B CE1 
5826  C CE2 . TYR B 211 ? 0.6316 0.4545 0.4656 0.1181  -0.0143 -0.0198 211 TYR B CE2 
5827  C CZ  . TYR B 211 ? 0.6374 0.4737 0.4789 0.1251  -0.0145 -0.0127 211 TYR B CZ  
5828  O OH  . TYR B 211 ? 0.7228 0.5527 0.5639 0.1148  -0.0173 -0.0062 211 TYR B OH  
5829  N N   . GLU B 212 ? 0.4879 0.3820 0.3184 0.1752  0.0101  -0.0390 212 GLU B N   
5830  C CA  . GLU B 212 ? 0.5682 0.4657 0.3854 0.1918  0.0147  -0.0443 212 GLU B CA  
5831  C C   . GLU B 212 ? 0.5988 0.5311 0.4295 0.2046  0.0265  -0.0360 212 GLU B C   
5832  O O   . GLU B 212 ? 0.6314 0.5670 0.4495 0.2230  0.0322  -0.0392 212 GLU B O   
5833  C CB  . GLU B 212 ? 0.5693 0.4640 0.3811 0.1817  0.0132  -0.0493 212 GLU B CB  
5834  C CG  . GLU B 212 ? 0.6739 0.5361 0.4745 0.1699  0.0015  -0.0579 212 GLU B CG  
5835  C CD  . GLU B 212 ? 0.7527 0.6144 0.5508 0.1606  -0.0013 -0.0629 212 GLU B CD  
5836  O OE1 . GLU B 212 ? 0.7956 0.6405 0.5950 0.1454  -0.0096 -0.0671 212 GLU B OE1 
5837  O OE2 . GLU B 212 ? 0.7919 0.6706 0.5874 0.1684  0.0048  -0.0622 212 GLU B OE2 
5838  N N   . THR B 213 ? 0.6260 0.5841 0.4818 0.1954  0.0302  -0.0253 213 THR B N   
5839  C CA  . THR B 213 ? 0.6105 0.6047 0.4844 0.2040  0.0412  -0.0159 213 THR B CA  
5840  C C   . THR B 213 ? 0.5809 0.5910 0.4758 0.2053  0.0405  -0.0075 213 THR B C   
5841  O O   . THR B 213 ? 0.5303 0.5671 0.4392 0.2180  0.0485  -0.0010 213 THR B O   
5842  C CB  . THR B 213 ? 0.5220 0.5374 0.4092 0.1900  0.0464  -0.0098 213 THR B CB  
5843  O OG1 . THR B 213 ? 0.5300 0.5403 0.4278 0.1694  0.0394  -0.0078 213 THR B OG1 
5844  C CG2 . THR B 213 ? 0.5237 0.5280 0.3903 0.1925  0.0478  -0.0171 213 THR B CG2 
5845  N N   . THR B 214 ? 0.5453 0.5409 0.4435 0.1922  0.0312  -0.0069 214 THR B N   
5846  C CA  . THR B 214 ? 0.4705 0.4769 0.3855 0.1934  0.0279  0.0003  214 THR B CA  
5847  C C   . THR B 214 ? 0.4630 0.4346 0.3606 0.1944  0.0174  -0.0052 214 THR B C   
5848  O O   . THR B 214 ? 0.4528 0.4087 0.3482 0.1782  0.0106  -0.0046 214 THR B O   
5849  C CB  . THR B 214 ? 0.4671 0.4923 0.4039 0.1749  0.0266  0.0088  214 THR B CB  
5850  O OG1 . THR B 214 ? 0.4435 0.4474 0.3697 0.1572  0.0215  0.0048  214 THR B OG1 
5851  C CG2 . THR B 214 ? 0.4151 0.4747 0.3707 0.1740  0.0366  0.0159  214 THR B CG2 
5852  N N   . PRO B 215 ? 0.5016 0.4589 0.3850 0.2138  0.0163  -0.0105 215 PRO B N   
5853  C CA  . PRO B 215 ? 0.5800 0.4995 0.4442 0.2149  0.0057  -0.0157 215 PRO B CA  
5854  C C   . PRO B 215 ? 0.6480 0.5674 0.5224 0.2103  -0.0013 -0.0086 215 PRO B C   
5855  O O   . PRO B 215 ? 0.6789 0.5660 0.5377 0.2042  -0.0101 -0.0106 215 PRO B O   
5856  C CB  . PRO B 215 ? 0.6344 0.5427 0.4826 0.2399  0.0069  -0.0227 215 PRO B CB  
5857  C CG  . PRO B 215 ? 0.5513 0.4999 0.4170 0.2534  0.0193  -0.0180 215 PRO B CG  
5858  C CD  . PRO B 215 ? 0.4670 0.4376 0.3467 0.2354  0.0251  -0.0131 215 PRO B CD  
5859  N N   . ASN B 216 ? 0.6273 0.5808 0.5270 0.2122  0.0017  0.0001  216 ASN B N   
5860  C CA  . ASN B 216 ? 0.6752 0.6297 0.5844 0.2106  -0.0066 0.0066  216 ASN B CA  
5861  C C   . ASN B 216 ? 0.6496 0.6032 0.5640 0.1879  -0.0108 0.0114  216 ASN B C   
5862  O O   . ASN B 216 ? 0.6771 0.6254 0.5938 0.1851  -0.0192 0.0161  216 ASN B O   
5863  C CB  . ASN B 216 ? 0.6526 0.6452 0.5889 0.2246  -0.0031 0.0136  216 ASN B CB  
5864  C CG  . ASN B 216 ? 0.6784 0.6640 0.6079 0.2493  -0.0045 0.0103  216 ASN B CG  
5865  O OD1 . ASN B 216 ? 0.6551 0.6612 0.5915 0.2661  0.0049  0.0092  216 ASN B OD1 
5866  N ND2 . ASN B 216 ? 0.7450 0.7003 0.6593 0.2525  -0.0159 0.0087  216 ASN B ND2 
5867  N N   . VAL B 217 ? 0.6400 0.5973 0.5547 0.1727  -0.0057 0.0099  217 VAL B N   
5868  C CA  . VAL B 217 ? 0.5619 0.5226 0.4833 0.1532  -0.0083 0.0144  217 VAL B CA  
5869  C C   . VAL B 217 ? 0.5379 0.4634 0.4384 0.1435  -0.0157 0.0126  217 VAL B C   
5870  O O   . VAL B 217 ? 0.5052 0.4032 0.3864 0.1429  -0.0161 0.0065  217 VAL B O   
5871  C CB  . VAL B 217 ? 0.5320 0.5060 0.4592 0.1417  -0.0006 0.0130  217 VAL B CB  
5872  C CG1 . VAL B 217 ? 0.4773 0.4255 0.3841 0.1369  0.0007  0.0045  217 VAL B CG1 
5873  C CG2 . VAL B 217 ? 0.5176 0.5004 0.4550 0.1249  -0.0030 0.0180  217 VAL B CG2 
5874  N N   . LYS B 218 ? 0.5186 0.4438 0.4224 0.1359  -0.0220 0.0184  218 LYS B N   
5875  C CA  . LYS B 218 ? 0.4695 0.3645 0.3535 0.1239  -0.0267 0.0184  218 LYS B CA  
5876  C C   . LYS B 218 ? 0.4812 0.3794 0.3663 0.1060  -0.0214 0.0173  218 LYS B C   
5877  O O   . LYS B 218 ? 0.4774 0.4007 0.3794 0.1009  -0.0189 0.0199  218 LYS B O   
5878  C CB  . LYS B 218 ? 0.5356 0.4277 0.4192 0.1247  -0.0362 0.0249  218 LYS B CB  
5879  C CG  . LYS B 218 ? 0.6962 0.5988 0.5895 0.1435  -0.0417 0.0273  218 LYS B CG  
5880  C CD  . LYS B 218 ? 0.7759 0.6904 0.6799 0.1433  -0.0514 0.0342  218 LYS B CD  
5881  C CE  . LYS B 218 ? 0.8270 0.7073 0.7056 0.1393  -0.0605 0.0364  218 LYS B CE  
5882  N NZ  . LYS B 218 ? 0.8587 0.7176 0.7241 0.1553  -0.0665 0.0357  218 LYS B NZ  
5883  N N   . ILE B 219 ? 0.5122 0.3853 0.3805 0.0967  -0.0197 0.0137  219 ILE B N   
5884  C CA  . ILE B 219 ? 0.4735 0.3479 0.3421 0.0801  -0.0149 0.0129  219 ILE B CA  
5885  C C   . ILE B 219 ? 0.4748 0.3214 0.3246 0.0704  -0.0170 0.0152  219 ILE B C   
5886  O O   . ILE B 219 ? 0.4787 0.3008 0.3131 0.0754  -0.0216 0.0162  219 ILE B O   
5887  C CB  . ILE B 219 ? 0.4618 0.3383 0.3328 0.0768  -0.0087 0.0062  219 ILE B CB  
5888  C CG1 . ILE B 219 ? 0.5212 0.3670 0.3751 0.0754  -0.0104 0.0020  219 ILE B CG1 
5889  C CG2 . ILE B 219 ? 0.4103 0.3105 0.2949 0.0886  -0.0058 0.0042  219 ILE B CG2 
5890  C CD1 . ILE B 219 ? 0.5592 0.4038 0.4149 0.0682  -0.0064 -0.0045 219 ILE B CD1 
5891  N N   . PRO B 220 ? 0.4928 0.3415 0.3419 0.0569  -0.0133 0.0165  220 PRO B N   
5892  C CA  . PRO B 220 ? 0.5526 0.3761 0.3826 0.0475  -0.0130 0.0196  220 PRO B CA  
5893  C C   . PRO B 220 ? 0.5571 0.3609 0.3792 0.0409  -0.0090 0.0164  220 PRO B C   
5894  O O   . PRO B 220 ? 0.5326 0.3428 0.3638 0.0421  -0.0068 0.0106  220 PRO B O   
5895  C CB  . PRO B 220 ? 0.5544 0.3904 0.3881 0.0370  -0.0089 0.0209  220 PRO B CB  
5896  C CG  . PRO B 220 ? 0.4834 0.3462 0.3377 0.0376  -0.0057 0.0169  220 PRO B CG  
5897  C CD  . PRO B 220 ? 0.4813 0.3552 0.3458 0.0512  -0.0098 0.0162  220 PRO B CD  
5898  N N   . ASP B 221 ? 0.5751 0.3533 0.3791 0.0337  -0.0087 0.0207  221 ASP B N   
5899  C CA  . ASP B 221 ? 0.5304 0.2863 0.3264 0.0248  -0.0055 0.0198  221 ASP B CA  
5900  C C   . ASP B 221 ? 0.5367 0.3072 0.3454 0.0117  0.0034  0.0167  221 ASP B C   
5901  O O   . ASP B 221 ? 0.5510 0.3242 0.3567 0.0024  0.0096  0.0203  221 ASP B O   
5902  C CB  . ASP B 221 ? 0.6147 0.3410 0.3875 0.0204  -0.0068 0.0275  221 ASP B CB  
5903  C CG  . ASP B 221 ? 0.6811 0.3818 0.4458 0.0097  -0.0039 0.0285  221 ASP B CG  
5904  O OD1 . ASP B 221 ? 0.6762 0.3751 0.4497 0.0099  -0.0055 0.0224  221 ASP B OD1 
5905  O OD2 . ASP B 221 ? 0.7738 0.4551 0.5224 0.0006  -0.0002 0.0359  221 ASP B OD2 
5906  N N   . PHE B 222 ? 0.5174 0.2976 0.3399 0.0120  0.0039  0.0097  222 PHE B N   
5907  C CA  . PHE B 222 ? 0.4905 0.2863 0.3276 0.0011  0.0108  0.0060  222 PHE B CA  
5908  C C   . PHE B 222 ? 0.5446 0.3216 0.3775 -0.0127 0.0146  0.0081  222 PHE B C   
5909  O O   . PHE B 222 ? 0.6151 0.3836 0.4530 -0.0164 0.0122  0.0037  222 PHE B O   
5910  C CB  . PHE B 222 ? 0.4794 0.2916 0.3308 0.0075  0.0084  -0.0019 222 PHE B CB  
5911  C CG  . PHE B 222 ? 0.4420 0.2813 0.3043 0.0144  0.0094  -0.0025 222 PHE B CG  
5912  C CD1 . PHE B 222 ? 0.4686 0.3129 0.3286 0.0270  0.0050  -0.0004 222 PHE B CD1 
5913  C CD2 . PHE B 222 ? 0.4532 0.3126 0.3285 0.0080  0.0145  -0.0045 222 PHE B CD2 
5914  C CE1 . PHE B 222 ? 0.3771 0.2461 0.2488 0.0316  0.0058  0.0004  222 PHE B CE1 
5915  C CE2 . PHE B 222 ? 0.4640 0.3454 0.3485 0.0134  0.0147  -0.0042 222 PHE B CE2 
5916  C CZ  . PHE B 222 ? 0.4058 0.2919 0.2888 0.0244  0.0104  -0.0014 222 PHE B CZ  
5917  N N   . ALA B 223 ? 0.5690 0.3390 0.3921 -0.0207 0.0207  0.0152  223 ALA B N   
5918  C CA  . ALA B 223 ? 0.5935 0.3443 0.4103 -0.0342 0.0260  0.0202  223 ALA B CA  
5919  C C   . ALA B 223 ? 0.6580 0.4251 0.4944 -0.0471 0.0344  0.0177  223 ALA B C   
5920  O O   . ALA B 223 ? 0.7521 0.5064 0.5885 -0.0597 0.0392  0.0220  223 ALA B O   
5921  C CB  . ALA B 223 ? 0.5750 0.3123 0.3710 -0.0366 0.0306  0.0296  223 ALA B CB  
5922  N N   . VAL B 224 ? 0.5266 0.3217 0.3802 -0.0445 0.0362  0.0116  224 VAL B N   
5923  C CA  . VAL B 224 ? 0.5753 0.3887 0.4502 -0.0544 0.0425  0.0080  224 VAL B CA  
5924  C C   . VAL B 224 ? 0.6019 0.4295 0.4921 -0.0480 0.0351  -0.0013 224 VAL B C   
5925  O O   . VAL B 224 ? 0.6523 0.4807 0.5371 -0.0356 0.0281  -0.0043 224 VAL B O   
5926  C CB  . VAL B 224 ? 0.5318 0.3649 0.4106 -0.0568 0.0527  0.0098  224 VAL B CB  
5927  C CG1 . VAL B 224 ? 0.6080 0.4284 0.4736 -0.0656 0.0626  0.0187  224 VAL B CG1 
5928  C CG2 . VAL B 224 ? 0.4982 0.3411 0.3702 -0.0446 0.0488  0.0084  224 VAL B CG2 
5929  N N   . SER B 225 ? 0.5878 0.4283 0.4978 -0.0561 0.0370  -0.0056 225 SER B N   
5930  C CA  . SER B 225 ? 0.5068 0.3600 0.4301 -0.0508 0.0297  -0.0146 225 SER B CA  
5931  C C   . SER B 225 ? 0.5117 0.3928 0.4479 -0.0475 0.0338  -0.0176 225 SER B C   
5932  O O   . SER B 225 ? 0.4605 0.3542 0.4057 -0.0546 0.0426  -0.0153 225 SER B O   
5933  C CB  . SER B 225 ? 0.5503 0.3983 0.4877 -0.0612 0.0258  -0.0183 225 SER B CB  
5934  O OG  . SER B 225 ? 0.5203 0.3815 0.4697 -0.0560 0.0186  -0.0273 225 SER B OG  
5935  N N   . PHE B 226 ? 0.5063 0.3962 0.4426 -0.0363 0.0278  -0.0225 226 PHE B N   
5936  C CA  . PHE B 226 ? 0.4893 0.4029 0.4376 -0.0328 0.0295  -0.0258 226 PHE B CA  
5937  C C   . PHE B 226 ? 0.4749 0.3965 0.4361 -0.0319 0.0231  -0.0335 226 PHE B C   
5938  O O   . PHE B 226 ? 0.4369 0.3757 0.4060 -0.0273 0.0226  -0.0365 226 PHE B O   
5939  C CB  . PHE B 226 ? 0.4556 0.3745 0.3944 -0.0216 0.0283  -0.0238 226 PHE B CB  
5940  C CG  . PHE B 226 ? 0.4422 0.3557 0.3694 -0.0224 0.0331  -0.0169 226 PHE B CG  
5941  C CD1 . PHE B 226 ? 0.3455 0.2705 0.2758 -0.0252 0.0391  -0.0153 226 PHE B CD1 
5942  C CD2 . PHE B 226 ? 0.4260 0.3214 0.3378 -0.0194 0.0306  -0.0126 226 PHE B CD2 
5943  C CE1 . PHE B 226 ? 0.4524 0.3701 0.3689 -0.0252 0.0422  -0.0097 226 PHE B CE1 
5944  C CE2 . PHE B 226 ? 0.3888 0.2778 0.2881 -0.0196 0.0334  -0.0064 226 PHE B CE2 
5945  C CZ  . PHE B 226 ? 0.4172 0.3170 0.3182 -0.0227 0.0390  -0.0052 226 PHE B CZ  
5946  N N   . ARG B 227 ? 0.4596 0.3674 0.4220 -0.0363 0.0171  -0.0367 227 ARG B N   
5947  C CA  . ARG B 227 ? 0.4704 0.3824 0.4415 -0.0340 0.0083  -0.0448 227 ARG B CA  
5948  C C   . ARG B 227 ? 0.4953 0.4291 0.4884 -0.0404 0.0108  -0.0474 227 ARG B C   
5949  O O   . ARG B 227 ? 0.4215 0.3678 0.4196 -0.0338 0.0063  -0.0523 227 ARG B O   
5950  C CB  . ARG B 227 ? 0.4654 0.3551 0.4329 -0.0386 -0.0002 -0.0482 227 ARG B CB  
5951  C CG  . ARG B 227 ? 0.5173 0.3849 0.4619 -0.0285 -0.0046 -0.0477 227 ARG B CG  
5952  C CD  . ARG B 227 ? 0.5656 0.4076 0.5044 -0.0320 -0.0145 -0.0520 227 ARG B CD  
5953  N NE  . ARG B 227 ? 0.6085 0.4532 0.5549 -0.0312 -0.0246 -0.0612 227 ARG B NE  
5954  C CZ  . ARG B 227 ? 0.6241 0.4666 0.5579 -0.0168 -0.0315 -0.0678 227 ARG B CZ  
5955  N NH1 . ARG B 227 ? 0.5881 0.4281 0.5042 -0.0025 -0.0284 -0.0658 227 ARG B NH1 
5956  N NH2 . ARG B 227 ? 0.6599 0.5031 0.5988 -0.0165 -0.0415 -0.0763 227 ARG B NH2 
5957  N N   . GLU B 228 ? 0.5030 0.4422 0.5093 -0.0524 0.0184  -0.0436 228 GLU B N   
5958  C CA  . GLU B 228 ? 0.5250 0.4873 0.5543 -0.0569 0.0212  -0.0463 228 GLU B CA  
5959  C C   . GLU B 228 ? 0.4976 0.4760 0.5249 -0.0485 0.0266  -0.0455 228 GLU B C   
5960  O O   . GLU B 228 ? 0.4570 0.4526 0.4984 -0.0459 0.0245  -0.0499 228 GLU B O   
5961  C CB  . GLU B 228 ? 0.5922 0.5587 0.6374 -0.0712 0.0299  -0.0418 228 GLU B CB  
5962  C CG  . GLU B 228 ? 0.7453 0.6988 0.7997 -0.0820 0.0224  -0.0433 228 GLU B CG  
5963  C CD  . GLU B 228 ? 0.8858 0.8536 0.9647 -0.0850 0.0126  -0.0512 228 GLU B CD  
5964  O OE1 . GLU B 228 ? 0.9316 0.8850 1.0069 -0.0840 -0.0012 -0.0571 228 GLU B OE1 
5965  O OE2 . GLU B 228 ? 0.9316 0.9244 1.0327 -0.0874 0.0179  -0.0519 228 GLU B OE2 
5966  N N   . ASP B 229 ? 0.4570 0.4288 0.4668 -0.0438 0.0319  -0.0402 229 ASP B N   
5967  C CA  . ASP B 229 ? 0.3998 0.3834 0.4063 -0.0361 0.0348  -0.0395 229 ASP B CA  
5968  C C   . ASP B 229 ? 0.3597 0.3470 0.3633 -0.0260 0.0262  -0.0435 229 ASP B C   
5969  O O   . ASP B 229 ? 0.4054 0.4058 0.4144 -0.0215 0.0261  -0.0450 229 ASP B O   
5970  C CB  . ASP B 229 ? 0.3742 0.3482 0.3628 -0.0341 0.0401  -0.0329 229 ASP B CB  
5971  C CG  . ASP B 229 ? 0.4290 0.4040 0.4184 -0.0417 0.0508  -0.0288 229 ASP B CG  
5972  O OD1 . ASP B 229 ? 0.4548 0.4401 0.4611 -0.0487 0.0553  -0.0305 229 ASP B OD1 
5973  O OD2 . ASP B 229 ? 0.4015 0.3679 0.3748 -0.0403 0.0549  -0.0237 229 ASP B OD2 
5974  N N   . ALA B 230 ? 0.3663 0.3410 0.3598 -0.0217 0.0194  -0.0450 230 ALA B N   
5975  C CA  . ALA B 230 ? 0.3995 0.3774 0.3884 -0.0116 0.0125  -0.0484 230 ALA B CA  
5976  C C   . ALA B 230 ? 0.4103 0.3995 0.4138 -0.0125 0.0072  -0.0547 230 ALA B C   
5977  O O   . ALA B 230 ? 0.4459 0.4452 0.4502 -0.0060 0.0054  -0.0557 230 ALA B O   
5978  C CB  . ALA B 230 ? 0.3908 0.3519 0.3651 -0.0060 0.0066  -0.0500 230 ALA B CB  
5979  N N   . SER B 231 ? 0.3907 0.3783 0.4067 -0.0209 0.0042  -0.0585 231 SER B N   
5980  C CA  . SER B 231 ? 0.4360 0.4356 0.4687 -0.0220 -0.0025 -0.0647 231 SER B CA  
5981  C C   . SER B 231 ? 0.4114 0.4303 0.4577 -0.0221 0.0038  -0.0634 231 SER B C   
5982  O O   . SER B 231 ? 0.3029 0.3323 0.3560 -0.0169 -0.0017 -0.0673 231 SER B O   
5983  C CB  . SER B 231 ? 0.5239 0.5197 0.5717 -0.0330 -0.0069 -0.0680 231 SER B CB  
5984  O OG  . SER B 231 ? 0.6285 0.6030 0.6618 -0.0317 -0.0149 -0.0705 231 SER B OG  
5985  N N   . LYS B 232 ? 0.4190 0.4410 0.4672 -0.0272 0.0148  -0.0582 232 LYS B N   
5986  C CA  . LYS B 232 ? 0.3508 0.3890 0.4102 -0.0267 0.0214  -0.0576 232 LYS B CA  
5987  C C   . LYS B 232 ? 0.3214 0.3618 0.3702 -0.0164 0.0192  -0.0570 232 LYS B C   
5988  O O   . LYS B 232 ? 0.3660 0.4184 0.4247 -0.0125 0.0171  -0.0600 232 LYS B O   
5989  C CB  . LYS B 232 ? 0.3870 0.4239 0.4444 -0.0330 0.0337  -0.0521 232 LYS B CB  
5990  C CG  . LYS B 232 ? 0.4428 0.4865 0.5188 -0.0440 0.0394  -0.0519 232 LYS B CG  
5991  C CD  . LYS B 232 ? 0.5485 0.5976 0.6233 -0.0463 0.0532  -0.0474 232 LYS B CD  
5992  C CE  . LYS B 232 ? 0.6623 0.7095 0.7445 -0.0581 0.0619  -0.0430 232 LYS B CE  
5993  N NZ  . LYS B 232 ? 0.7493 0.7956 0.8197 -0.0580 0.0754  -0.0377 232 LYS B NZ  
5994  N N   . HIS B 233 ? 0.3251 0.3544 0.3549 -0.0121 0.0195  -0.0527 233 HIS B N   
5995  C CA  . HIS B 233 ? 0.3239 0.3549 0.3447 -0.0037 0.0173  -0.0507 233 HIS B CA  
5996  C C   . HIS B 233 ? 0.3315 0.3672 0.3558 0.0022  0.0086  -0.0552 233 HIS B C   
5997  O O   . HIS B 233 ? 0.3143 0.3570 0.3413 0.0067  0.0070  -0.0555 233 HIS B O   
5998  C CB  . HIS B 233 ? 0.3308 0.3513 0.3346 -0.0001 0.0176  -0.0455 233 HIS B CB  
5999  C CG  . HIS B 233 ? 0.3445 0.3603 0.3417 -0.0034 0.0242  -0.0402 233 HIS B CG  
6000  N ND1 . HIS B 233 ? 0.3322 0.3512 0.3270 -0.0018 0.0265  -0.0371 233 HIS B ND1 
6001  C CD2 . HIS B 233 ? 0.3891 0.3949 0.3796 -0.0076 0.0276  -0.0375 233 HIS B CD2 
6002  C CE1 . HIS B 233 ? 0.3623 0.3742 0.3491 -0.0048 0.0306  -0.0332 233 HIS B CE1 
6003  N NE2 . HIS B 233 ? 0.3830 0.3869 0.3667 -0.0081 0.0317  -0.0330 233 HIS B NE2 
6004  N N   . VAL B 234 ? 0.3278 0.3574 0.3502 0.0026  0.0020  -0.0590 234 VAL B N   
6005  C CA  . VAL B 234 ? 0.2994 0.3307 0.3210 0.0091  -0.0076 -0.0637 234 VAL B CA  
6006  C C   . VAL B 234 ? 0.3031 0.3475 0.3451 0.0067  -0.0112 -0.0688 234 VAL B C   
6007  O O   . VAL B 234 ? 0.3258 0.3759 0.3685 0.0131  -0.0159 -0.0701 234 VAL B O   
6008  C CB  . VAL B 234 ? 0.3365 0.3551 0.3484 0.0107  -0.0149 -0.0677 234 VAL B CB  
6009  C CG1 . VAL B 234 ? 0.2979 0.3160 0.3040 0.0190  -0.0256 -0.0727 234 VAL B CG1 
6010  C CG2 . VAL B 234 ? 0.3586 0.3650 0.3515 0.0146  -0.0109 -0.0631 234 VAL B CG2 
6011  N N   . GLU B 235 ? 0.3002 0.3500 0.3598 -0.0024 -0.0091 -0.0713 235 GLU B N   
6012  C CA  . GLU B 235 ? 0.3814 0.4469 0.4643 -0.0043 -0.0127 -0.0762 235 GLU B CA  
6013  C C   . GLU B 235 ? 0.4005 0.4777 0.4896 -0.0007 -0.0062 -0.0743 235 GLU B C   
6014  O O   . GLU B 235 ? 0.3348 0.4217 0.4335 0.0049  -0.0121 -0.0779 235 GLU B O   
6015  C CB  . GLU B 235 ? 0.4736 0.5444 0.5768 -0.0159 -0.0107 -0.0781 235 GLU B CB  
6016  C CG  . GLU B 235 ? 0.5624 0.6495 0.6924 -0.0177 -0.0190 -0.0844 235 GLU B CG  
6017  C CD  . GLU B 235 ? 0.6562 0.7348 0.7813 -0.0143 -0.0356 -0.0906 235 GLU B CD  
6018  O OE1 . GLU B 235 ? 0.6991 0.7855 0.8298 -0.0071 -0.0451 -0.0950 235 GLU B OE1 
6019  O OE2 . GLU B 235 ? 0.7026 0.7649 0.8167 -0.0180 -0.0399 -0.0914 235 GLU B OE2 
6020  N N   . LEU B 236 ? 0.3989 0.4735 0.4808 -0.0029 0.0049  -0.0690 236 LEU B N   
6021  C CA  . LEU B 236 ? 0.3548 0.4367 0.4390 0.0014  0.0102  -0.0680 236 LEU B CA  
6022  C C   . LEU B 236 ? 0.3471 0.4237 0.4180 0.0107  0.0037  -0.0668 236 LEU B C   
6023  O O   . LEU B 236 ? 0.3266 0.4095 0.4031 0.0162  0.0023  -0.0684 236 LEU B O   
6024  C CB  . LEU B 236 ? 0.3122 0.3888 0.3874 -0.0025 0.0219  -0.0630 236 LEU B CB  
6025  C CG  . LEU B 236 ? 0.3767 0.4596 0.4645 -0.0113 0.0313  -0.0628 236 LEU B CG  
6026  C CD1 . LEU B 236 ? 0.3350 0.4091 0.4076 -0.0135 0.0417  -0.0575 236 LEU B CD1 
6027  C CD2 . LEU B 236 ? 0.3778 0.4804 0.4903 -0.0109 0.0338  -0.0673 236 LEU B CD2 
6028  N N   . ALA B 237 ? 0.3628 0.4277 0.4161 0.0131  0.0001  -0.0635 237 ALA B N   
6029  C CA  . ALA B 237 ? 0.3346 0.3953 0.3759 0.0212  -0.0054 -0.0611 237 ALA B CA  
6030  C C   . ALA B 237 ? 0.3738 0.4401 0.4229 0.0266  -0.0155 -0.0665 237 ALA B C   
6031  O O   . ALA B 237 ? 0.3554 0.4235 0.4045 0.0326  -0.0189 -0.0663 237 ALA B O   
6032  C CB  . ALA B 237 ? 0.3048 0.3548 0.3277 0.0231  -0.0058 -0.0562 237 ALA B CB  
6033  N N   . LYS B 238 ? 0.3454 0.4132 0.4012 0.0246  -0.0216 -0.0717 238 LYS B N   
6034  C CA  . LYS B 238 ? 0.3857 0.4597 0.4513 0.0291  -0.0330 -0.0780 238 LYS B CA  
6035  C C   . LYS B 238 ? 0.3682 0.4567 0.4543 0.0304  -0.0323 -0.0808 238 LYS B C   
6036  O O   . LYS B 238 ? 0.3783 0.4690 0.4652 0.0384  -0.0405 -0.0828 238 LYS B O   
6037  C CB  . LYS B 238 ? 0.3946 0.4688 0.4691 0.0238  -0.0396 -0.0838 238 LYS B CB  
6038  C CG  . LYS B 238 ? 0.4389 0.4968 0.4906 0.0267  -0.0444 -0.0835 238 LYS B CG  
6039  C CD  . LYS B 238 ? 0.4314 0.4859 0.4910 0.0210  -0.0522 -0.0899 238 LYS B CD  
6040  C CE  . LYS B 238 ? 0.4912 0.5537 0.5661 0.0230  -0.0664 -0.0974 238 LYS B CE  
6041  N NZ  . LYS B 238 ? 0.5287 0.5886 0.6159 0.0146  -0.0745 -0.1035 238 LYS B NZ  
6042  N N   . GLU B 239 ? 0.3475 0.4454 0.4488 0.0238  -0.0223 -0.0808 239 GLU B N   
6043  C CA  . GLU B 239 ? 0.3257 0.4387 0.4467 0.0265  -0.0199 -0.0838 239 GLU B CA  
6044  C C   . GLU B 239 ? 0.3152 0.4220 0.4234 0.0344  -0.0179 -0.0807 239 GLU B C   
6045  O O   . GLU B 239 ? 0.3008 0.4141 0.4176 0.0420  -0.0229 -0.0839 239 GLU B O   
6046  C CB  . GLU B 239 ? 0.3371 0.4613 0.4751 0.0178  -0.0078 -0.0839 239 GLU B CB  
6047  C CG  . GLU B 239 ? 0.3833 0.5140 0.5380 0.0087  -0.0108 -0.0867 239 GLU B CG  
6048  C CD  . GLU B 239 ? 0.5369 0.6797 0.7100 -0.0007 0.0020  -0.0854 239 GLU B CD  
6049  O OE1 . GLU B 239 ? 0.5984 0.7413 0.7654 0.0002  0.0143  -0.0821 239 GLU B OE1 
6050  O OE2 . GLU B 239 ? 0.5858 0.7370 0.7787 -0.0093 -0.0005 -0.0874 239 GLU B OE2 
6051  N N   . LYS B 240 ? 0.3371 0.4304 0.4251 0.0328  -0.0117 -0.0745 240 LYS B N   
6052  C CA  . LYS B 240 ? 0.3607 0.4457 0.4365 0.0390  -0.0116 -0.0712 240 LYS B CA  
6053  C C   . LYS B 240 ? 0.3435 0.4212 0.4091 0.0467  -0.0227 -0.0698 240 LYS B C   
6054  O O   . LYS B 240 ? 0.3259 0.4013 0.3908 0.0537  -0.0268 -0.0702 240 LYS B O   
6055  C CB  . LYS B 240 ? 0.3321 0.4049 0.3907 0.0347  -0.0044 -0.0646 240 LYS B CB  
6056  C CG  . LYS B 240 ? 0.3169 0.3795 0.3641 0.0392  -0.0053 -0.0611 240 LYS B CG  
6057  C CD  . LYS B 240 ? 0.3423 0.4093 0.3976 0.0418  -0.0002 -0.0656 240 LYS B CD  
6058  C CE  . LYS B 240 ? 0.3699 0.4234 0.4129 0.0469  -0.0033 -0.0634 240 LYS B CE  
6059  N NZ  . LYS B 240 ? 0.3518 0.4073 0.3986 0.0501  0.0030  -0.0685 240 LYS B NZ  
6060  N N   . TYR B 241 ? 0.3859 0.4580 0.4409 0.0462  -0.0275 -0.0679 241 TYR B N   
6061  C CA  . TYR B 241 ? 0.3628 0.4276 0.4057 0.0540  -0.0375 -0.0663 241 TYR B CA  
6062  C C   . TYR B 241 ? 0.3440 0.4179 0.4020 0.0604  -0.0473 -0.0734 241 TYR B C   
6063  O O   . TYR B 241 ? 0.4079 0.4767 0.4605 0.0682  -0.0536 -0.0723 241 TYR B O   
6064  C CB  . TYR B 241 ? 0.3645 0.4226 0.3930 0.0533  -0.0399 -0.0644 241 TYR B CB  
6065  C CG  . TYR B 241 ? 0.3691 0.4173 0.3785 0.0616  -0.0479 -0.0610 241 TYR B CG  
6066  C CD1 . TYR B 241 ? 0.3526 0.4016 0.3628 0.0677  -0.0599 -0.0668 241 TYR B CD1 
6067  C CD2 . TYR B 241 ? 0.4068 0.4449 0.3971 0.0630  -0.0436 -0.0514 241 TYR B CD2 
6068  C CE1 . TYR B 241 ? 0.3951 0.4330 0.3835 0.0761  -0.0671 -0.0632 241 TYR B CE1 
6069  C CE2 . TYR B 241 ? 0.3489 0.3778 0.3199 0.0705  -0.0491 -0.0469 241 TYR B CE2 
6070  C CZ  . TYR B 241 ? 0.3652 0.3930 0.3335 0.0774  -0.0606 -0.0529 241 TYR B CZ  
6071  O OH  . TYR B 241 ? 0.4253 0.4422 0.3709 0.0855  -0.0658 -0.0480 241 TYR B OH  
6072  N N   . PHE B 242 ? 0.2935 0.3807 0.3716 0.0567  -0.0491 -0.0804 242 PHE B N   
6073  C CA  . PHE B 242 ? 0.3177 0.4183 0.4168 0.0618  -0.0581 -0.0876 242 PHE B CA  
6074  C C   . PHE B 242 ? 0.3819 0.4877 0.4901 0.0679  -0.0552 -0.0883 242 PHE B C   
6075  O O   . PHE B 242 ? 0.4163 0.5239 0.5288 0.0772  -0.0651 -0.0911 242 PHE B O   
6076  C CB  . PHE B 242 ? 0.2510 0.3675 0.3751 0.0536  -0.0571 -0.0934 242 PHE B CB  
6077  C CG  . PHE B 242 ? 0.2951 0.4300 0.4472 0.0574  -0.0663 -0.1008 242 PHE B CG  
6078  C CD1 . PHE B 242 ? 0.3088 0.4423 0.4607 0.0624  -0.0829 -0.1051 242 PHE B CD1 
6079  C CD2 . PHE B 242 ? 0.3274 0.4816 0.5061 0.0565  -0.0584 -0.1034 242 PHE B CD2 
6080  C CE1 . PHE B 242 ? 0.3769 0.5289 0.5573 0.0661  -0.0931 -0.1120 242 PHE B CE1 
6081  C CE2 . PHE B 242 ? 0.3581 0.5328 0.5666 0.0604  -0.0665 -0.1100 242 PHE B CE2 
6082  C CZ  . PHE B 242 ? 0.3743 0.5484 0.5850 0.0649  -0.0846 -0.1143 242 PHE B CZ  
6083  N N   . GLU B 243 ? 0.3758 0.4821 0.4847 0.0637  -0.0424 -0.0859 243 GLU B N   
6084  C CA  . GLU B 243 ? 0.4540 0.5622 0.5679 0.0706  -0.0394 -0.0874 243 GLU B CA  
6085  C C   . GLU B 243 ? 0.4515 0.5414 0.5448 0.0789  -0.0470 -0.0832 243 GLU B C   
6086  O O   . GLU B 243 ? 0.3717 0.4621 0.4702 0.0884  -0.0521 -0.0862 243 GLU B O   
6087  C CB  . GLU B 243 ? 0.5229 0.6306 0.6351 0.0649  -0.0250 -0.0856 243 GLU B CB  
6088  C CG  . GLU B 243 ? 0.6108 0.7382 0.7462 0.0589  -0.0155 -0.0897 243 GLU B CG  
6089  C CD  . GLU B 243 ? 0.7036 0.8265 0.8306 0.0537  -0.0014 -0.0869 243 GLU B CD  
6090  O OE1 . GLU B 243 ? 0.7532 0.8596 0.8602 0.0569  -0.0004 -0.0838 243 GLU B OE1 
6091  O OE2 . GLU B 243 ? 0.7013 0.8357 0.8407 0.0462  0.0080  -0.0875 243 GLU B OE2 
6092  N N   . ILE B 244 ? 0.4245 0.4981 0.4948 0.0755  -0.0473 -0.0756 244 ILE B N   
6093  C CA  . ILE B 244 ? 0.4155 0.4707 0.4661 0.0809  -0.0523 -0.0694 244 ILE B CA  
6094  C C   . ILE B 244 ? 0.4339 0.4846 0.4781 0.0890  -0.0654 -0.0692 244 ILE B C   
6095  O O   . ILE B 244 ? 0.4247 0.4665 0.4639 0.0975  -0.0728 -0.0685 244 ILE B O   
6096  C CB  . ILE B 244 ? 0.4757 0.5179 0.5073 0.0734  -0.0460 -0.0601 244 ILE B CB  
6097  C CG1 . ILE B 244 ? 0.4618 0.5057 0.4971 0.0665  -0.0350 -0.0603 244 ILE B CG1 
6098  C CG2 . ILE B 244 ? 0.4928 0.5169 0.5057 0.0772  -0.0515 -0.0521 244 ILE B CG2 
6099  C CD1 . ILE B 244 ? 0.4433 0.4865 0.4850 0.0714  -0.0336 -0.0650 244 ILE B CD1 
6100  N N   . PHE B 245 ? 0.4495 0.5042 0.4917 0.0870  -0.0692 -0.0701 245 PHE B N   
6101  C CA  . PHE B 245 ? 0.4649 0.5110 0.4929 0.0944  -0.0812 -0.0686 245 PHE B CA  
6102  C C   . PHE B 245 ? 0.4204 0.4792 0.4653 0.0997  -0.0929 -0.0780 245 PHE B C   
6103  O O   . PHE B 245 ? 0.4855 0.5365 0.5189 0.1081  -0.1053 -0.0779 245 PHE B O   
6104  C CB  . PHE B 245 ? 0.4504 0.4871 0.4568 0.0903  -0.0781 -0.0621 245 PHE B CB  
6105  C CG  . PHE B 245 ? 0.4395 0.4647 0.4303 0.0859  -0.0687 -0.0515 245 PHE B CG  
6106  C CD1 . PHE B 245 ? 0.4182 0.4284 0.3925 0.0905  -0.0720 -0.0433 245 PHE B CD1 
6107  C CD2 . PHE B 245 ? 0.3783 0.4072 0.3716 0.0767  -0.0574 -0.0492 245 PHE B CD2 
6108  C CE1 . PHE B 245 ? 0.4605 0.4613 0.4238 0.0849  -0.0642 -0.0330 245 PHE B CE1 
6109  C CE2 . PHE B 245 ? 0.4180 0.4380 0.3998 0.0723  -0.0502 -0.0396 245 PHE B CE2 
6110  C CZ  . PHE B 245 ? 0.4612 0.4680 0.4294 0.0759  -0.0536 -0.0314 245 PHE B CZ  
6111  N N   . GLY B 246 ? 0.4697 0.5891 0.5605 0.2089  -0.1201 -0.0728 246 GLY B N   
6112  C CA  . GLY B 246 ? 0.4592 0.6137 0.5734 0.2170  -0.1297 -0.0820 246 GLY B CA  
6113  C C   . GLY B 246 ? 0.4685 0.6380 0.5806 0.2073  -0.1356 -0.0807 246 GLY B C   
6114  O O   . GLY B 246 ? 0.4298 0.6293 0.5619 0.2138  -0.1452 -0.0891 246 GLY B O   
6115  N N   . GLU B 247 ? 0.4336 0.5840 0.5234 0.1928  -0.1307 -0.0714 247 GLU B N   
6116  C CA  . GLU B 247 ? 0.5042 0.6655 0.5902 0.1820  -0.1346 -0.0708 247 GLU B CA  
6117  C C   . GLU B 247 ? 0.4398 0.6017 0.5262 0.1607  -0.1205 -0.0720 247 GLU B C   
6118  O O   . GLU B 247 ? 0.4394 0.5833 0.5172 0.1547  -0.1096 -0.0686 247 GLU B O   
6119  C CB  . GLU B 247 ? 0.5600 0.6951 0.6148 0.1854  -0.1423 -0.0575 247 GLU B CB  
6120  C CG  . GLU B 247 ? 0.7341 0.8543 0.7761 0.2058  -0.1542 -0.0504 247 GLU B CG  
6121  C CD  . GLU B 247 ? 0.9011 0.9823 0.9093 0.2049  -0.1515 -0.0345 247 GLU B CD  
6122  O OE1 . GLU B 247 ? 0.9535 1.0282 0.9424 0.2001  -0.1546 -0.0278 247 GLU B OE1 
6123  O OE2 . GLU B 247 ? 0.9641 1.0215 0.9659 0.2087  -0.1456 -0.0295 247 GLU B OE2 
6124  N N   . HIS B 248 ? 0.4241 0.6052 0.5196 0.1495  -0.1215 -0.0770 248 HIS B N   
6125  C CA  . HIS B 248 ? 0.4380 0.6102 0.5243 0.1307  -0.1108 -0.0740 248 HIS B CA  
6126  C C   . HIS B 248 ? 0.4408 0.5841 0.4966 0.1297  -0.1135 -0.0618 248 HIS B C   
6127  O O   . HIS B 248 ? 0.4431 0.5819 0.4878 0.1399  -0.1249 -0.0577 248 HIS B O   
6128  C CB  . HIS B 248 ? 0.5194 0.7170 0.6236 0.1187  -0.1109 -0.0826 248 HIS B CB  
6129  C CG  . HIS B 248 ? 0.6135 0.8380 0.7471 0.1138  -0.1028 -0.0937 248 HIS B CG  
6130  N ND1 . HIS B 248 ? 0.6426 0.8619 0.7771 0.1068  -0.0883 -0.0936 248 HIS B ND1 
6131  C CD2 . HIS B 248 ? 0.6447 0.9026 0.8079 0.1148  -0.1068 -0.1056 248 HIS B CD2 
6132  C CE1 . HIS B 248 ? 0.6417 0.8896 0.8040 0.1035  -0.0824 -0.1043 248 HIS B CE1 
6133  N NE2 . HIS B 248 ? 0.6482 0.9206 0.8300 0.1078  -0.0933 -0.1119 248 HIS B NE2 
6134  N N   . PRO B 249 ? 0.4374 0.5613 0.4788 0.1184  -0.1032 -0.0559 249 PRO B N   
6135  C CA  . PRO B 249 ? 0.4359 0.5354 0.4510 0.1165  -0.1046 -0.0453 249 PRO B CA  
6136  C C   . PRO B 249 ? 0.4475 0.5547 0.4586 0.1097  -0.1096 -0.0464 249 PRO B C   
6137  O O   . PRO B 249 ? 0.4417 0.5648 0.4667 0.0992  -0.1067 -0.0535 249 PRO B O   
6138  C CB  . PRO B 249 ? 0.3919 0.4745 0.3988 0.1061  -0.0924 -0.0417 249 PRO B CB  
6139  C CG  . PRO B 249 ? 0.3748 0.4756 0.4007 0.0979  -0.0848 -0.0504 249 PRO B CG  
6140  C CD  . PRO B 249 ? 0.4077 0.5320 0.4556 0.1075  -0.0900 -0.0589 249 PRO B CD  
6141  N N   . VAL B 250 ? 0.4519 0.5469 0.4433 0.1158  -0.1169 -0.0394 250 VAL B N   
6142  C CA  . VAL B 250 ? 0.4028 0.5021 0.3863 0.1105  -0.1217 -0.0405 250 VAL B CA  
6143  C C   . VAL B 250 ? 0.3665 0.4441 0.3283 0.1028  -0.1151 -0.0323 250 VAL B C   
6144  O O   . VAL B 250 ? 0.4315 0.5118 0.3884 0.0959  -0.1163 -0.0346 250 VAL B O   
6145  C CB  . VAL B 250 ? 0.4797 0.5869 0.4572 0.1238  -0.1360 -0.0411 250 VAL B CB  
6146  C CG1 . VAL B 250 ? 0.4660 0.6012 0.4701 0.1302  -0.1438 -0.0523 250 VAL B CG1 
6147  C CG2 . VAL B 250 ? 0.4875 0.5726 0.4426 0.1364  -0.1387 -0.0292 250 VAL B CG2 
6148  N N   . TYR B 251 ? 0.3960 0.4532 0.3466 0.1035  -0.1083 -0.0240 251 TYR B N   
6149  C CA  . TYR B 251 ? 0.4292 0.4685 0.3639 0.0954  -0.1008 -0.0174 251 TYR B CA  
6150  C C   . TYR B 251 ? 0.3846 0.4183 0.3267 0.0871  -0.0906 -0.0184 251 TYR B C   
6151  O O   . TYR B 251 ? 0.4520 0.4848 0.4024 0.0911  -0.0885 -0.0196 251 TYR B O   
6152  C CB  . TYR B 251 ? 0.4642 0.4836 0.3779 0.1027  -0.1015 -0.0067 251 TYR B CB  
6153  C CG  . TYR B 251 ? 0.5063 0.5303 0.4114 0.1149  -0.1126 -0.0049 251 TYR B CG  
6154  C CD1 . TYR B 251 ? 0.4883 0.5244 0.3890 0.1142  -0.1191 -0.0091 251 TYR B CD1 
6155  C CD2 . TYR B 251 ? 0.5358 0.5518 0.4368 0.1280  -0.1174 0.0003  251 TYR B CD2 
6156  C CE1 . TYR B 251 ? 0.5317 0.5733 0.4230 0.1260  -0.1304 -0.0085 251 TYR B CE1 
6157  C CE2 . TYR B 251 ? 0.5082 0.5285 0.3992 0.1408  -0.1290 0.0022  251 TYR B CE2 
6158  C CZ  . TYR B 251 ? 0.5540 0.5882 0.4400 0.1396  -0.1357 -0.0024 251 TYR B CZ  
6159  O OH  . TYR B 251 ? 0.6145 0.6544 0.4891 0.1527  -0.1483 -0.0015 251 TYR B OH  
6160  N N   . MET B 252 ? 0.3332 0.3627 0.2712 0.0765  -0.0849 -0.0182 252 MET B N   
6161  C CA  . MET B 252 ? 0.3275 0.3495 0.2678 0.0696  -0.0763 -0.0182 252 MET B CA  
6162  C C   . MET B 252 ? 0.3571 0.3647 0.2835 0.0643  -0.0722 -0.0127 252 MET B C   
6163  O O   . MET B 252 ? 0.4404 0.4480 0.3586 0.0627  -0.0743 -0.0114 252 MET B O   
6164  C CB  . MET B 252 ? 0.3342 0.3687 0.2874 0.0615  -0.0727 -0.0250 252 MET B CB  
6165  C CG  . MET B 252 ? 0.4133 0.4616 0.3830 0.0649  -0.0723 -0.0309 252 MET B CG  
6166  S SD  . MET B 252 ? 0.4351 0.4945 0.4170 0.0538  -0.0642 -0.0369 252 MET B SD  
6167  C CE  . MET B 252 ? 0.4142 0.4918 0.4158 0.0609  -0.0640 -0.0438 252 MET B CE  
6168  N N   . TRP B 253 ? 0.3583 0.3548 0.2831 0.0618  -0.0664 -0.0108 253 TRP B N   
6169  C CA  . TRP B 253 ? 0.3389 0.3260 0.2557 0.0553  -0.0620 -0.0080 253 TRP B CA  
6170  C C   . TRP B 253 ? 0.3939 0.3859 0.3160 0.0480  -0.0587 -0.0127 253 TRP B C   
6171  O O   . TRP B 253 ? 0.3563 0.3491 0.2843 0.0473  -0.0557 -0.0157 253 TRP B O   
6172  C CB  . TRP B 253 ? 0.3686 0.3410 0.2813 0.0563  -0.0584 -0.0039 253 TRP B CB  
6173  C CG  . TRP B 253 ? 0.3737 0.3403 0.2834 0.0487  -0.0536 -0.0037 253 TRP B CG  
6174  C CD1 . TRP B 253 ? 0.4413 0.4050 0.3553 0.0444  -0.0502 -0.0074 253 TRP B CD1 
6175  C CD2 . TRP B 253 ? 0.4097 0.3745 0.3123 0.0452  -0.0523 -0.0006 253 TRP B CD2 
6176  N NE1 . TRP B 253 ? 0.4348 0.3960 0.3459 0.0387  -0.0479 -0.0069 253 TRP B NE1 
6177  C CE2 . TRP B 253 ? 0.4189 0.3811 0.3239 0.0390  -0.0486 -0.0027 253 TRP B CE2 
6178  C CE3 . TRP B 253 ? 0.4534 0.4198 0.3475 0.0474  -0.0541 0.0030  253 TRP B CE3 
6179  C CZ2 . TRP B 253 ? 0.4246 0.3870 0.3264 0.0350  -0.0463 -0.0016 253 TRP B CZ2 
6180  C CZ3 . TRP B 253 ? 0.4708 0.4365 0.3600 0.0432  -0.0508 0.0043  253 TRP B CZ3 
6181  C CH2 . TRP B 253 ? 0.4117 0.3759 0.3059 0.0371  -0.0468 0.0020  253 TRP B CH2 
6182  N N   . PRO B 254 ? 0.3662 0.3608 0.2853 0.0432  -0.0590 -0.0135 254 PRO B N   
6183  C CA  . PRO B 254 ? 0.3506 0.3462 0.2717 0.0370  -0.0561 -0.0163 254 PRO B CA  
6184  C C   . PRO B 254 ? 0.3691 0.3563 0.2864 0.0348  -0.0525 -0.0153 254 PRO B C   
6185  O O   . PRO B 254 ? 0.3665 0.3480 0.2789 0.0346  -0.0522 -0.0127 254 PRO B O   
6186  C CB  . PRO B 254 ? 0.3687 0.3659 0.2862 0.0343  -0.0584 -0.0168 254 PRO B CB  
6187  C CG  . PRO B 254 ? 0.3312 0.3263 0.2419 0.0384  -0.0608 -0.0138 254 PRO B CG  
6188  C CD  . PRO B 254 ? 0.3481 0.3439 0.2605 0.0443  -0.0625 -0.0119 254 PRO B CD  
6189  N N   . PRO B 255 ? 0.3966 0.3838 0.3162 0.0331  -0.0497 -0.0180 255 PRO B N   
6190  C CA  . PRO B 255 ? 0.3225 0.3029 0.2388 0.0313  -0.0477 -0.0187 255 PRO B CA  
6191  C C   . PRO B 255 ? 0.3390 0.3172 0.2507 0.0284  -0.0488 -0.0175 255 PRO B C   
6192  O O   . PRO B 255 ? 0.3350 0.3158 0.2448 0.0268  -0.0502 -0.0174 255 PRO B O   
6193  C CB  . PRO B 255 ? 0.3773 0.3602 0.2937 0.0298  -0.0451 -0.0223 255 PRO B CB  
6194  C CG  . PRO B 255 ? 0.3974 0.3884 0.3207 0.0318  -0.0442 -0.0236 255 PRO B CG  
6195  C CD  . PRO B 255 ? 0.3950 0.3894 0.3211 0.0338  -0.0480 -0.0212 255 PRO B CD  
6196  N N   . GLU B 256 ? 0.3451 0.3187 0.2565 0.0277  -0.0481 -0.0173 256 GLU B N   
6197  C CA  . GLU B 256 ? 0.3781 0.3523 0.2881 0.0255  -0.0489 -0.0173 256 GLU B CA  
6198  C C   . GLU B 256 ? 0.3932 0.3701 0.3011 0.0265  -0.0498 -0.0148 256 GLU B C   
6199  O O   . GLU B 256 ? 0.4439 0.4230 0.3508 0.0258  -0.0509 -0.0159 256 GLU B O   
6200  C CB  . GLU B 256 ? 0.3060 0.2816 0.2134 0.0242  -0.0506 -0.0203 256 GLU B CB  
6201  C CG  . GLU B 256 ? 0.3289 0.3027 0.2354 0.0238  -0.0500 -0.0238 256 GLU B CG  
6202  C CD  . GLU B 256 ? 0.3875 0.3584 0.2990 0.0227  -0.0490 -0.0263 256 GLU B CD  
6203  O OE1 . GLU B 256 ? 0.4905 0.4585 0.4022 0.0232  -0.0479 -0.0295 256 GLU B OE1 
6204  O OE2 . GLU B 256 ? 0.4703 0.4413 0.3859 0.0209  -0.0486 -0.0256 256 GLU B OE2 
6205  N N   . ALA B 257 ? 0.3813 0.3584 0.2881 0.0291  -0.0501 -0.0121 257 ALA B N   
6206  C CA  . ALA B 257 ? 0.4018 0.3821 0.3048 0.0309  -0.0519 -0.0109 257 ALA B CA  
6207  C C   . ALA B 257 ? 0.4153 0.3988 0.3183 0.0296  -0.0545 -0.0140 257 ALA B C   
6208  O O   . ALA B 257 ? 0.3770 0.3623 0.2770 0.0305  -0.0560 -0.0150 257 ALA B O   
6209  C CB  . ALA B 257 ? 0.4110 0.3905 0.3108 0.0305  -0.0493 -0.0088 257 ALA B CB  
6210  N N   . SER B 258 ? 0.4493 0.4324 0.3547 0.0277  -0.0545 -0.0157 258 SER B N   
6211  C CA  . SER B 258 ? 0.4265 0.4084 0.3304 0.0257  -0.0560 -0.0174 258 SER B CA  
6212  C C   . SER B 258 ? 0.3822 0.3672 0.2885 0.0250  -0.0578 -0.0187 258 SER B C   
6213  O O   . SER B 258 ? 0.3949 0.3843 0.3061 0.0247  -0.0573 -0.0191 258 SER B O   
6214  C CB  . SER B 258 ? 0.4483 0.4271 0.3510 0.0236  -0.0544 -0.0176 258 SER B CB  
6215  O OG  . SER B 258 ? 0.4652 0.4397 0.3643 0.0220  -0.0556 -0.0176 258 SER B OG  
6216  N N   . VAL B 259 ? 0.3601 0.3436 0.2644 0.0250  -0.0603 -0.0206 259 VAL B N   
6217  C CA  . VAL B 259 ? 0.3119 0.2981 0.2194 0.0235  -0.0629 -0.0236 259 VAL B CA  
6218  C C   . VAL B 259 ? 0.3523 0.3307 0.2578 0.0210  -0.0639 -0.0253 259 VAL B C   
6219  O O   . VAL B 259 ? 0.3775 0.3497 0.2783 0.0223  -0.0636 -0.0242 259 VAL B O   
6220  C CB  . VAL B 259 ? 0.3830 0.3750 0.2887 0.0274  -0.0662 -0.0253 259 VAL B CB  
6221  C CG1 . VAL B 259 ? 0.3222 0.3197 0.2293 0.0307  -0.0660 -0.0227 259 VAL B CG1 
6222  C CG2 . VAL B 259 ? 0.4400 0.4293 0.3386 0.0303  -0.0660 -0.0253 259 VAL B CG2 
6223  N N   . SER B 260 ? 0.4298 0.4085 0.3399 0.0175  -0.0656 -0.0286 260 SER B N   
6224  C CA  . SER B 260 ? 0.4434 0.4119 0.3523 0.0145  -0.0667 -0.0306 260 SER B CA  
6225  C C   . SER B 260 ? 0.3907 0.3641 0.3074 0.0109  -0.0695 -0.0363 260 SER B C   
6226  O O   . SER B 260 ? 0.4453 0.4307 0.3685 0.0108  -0.0703 -0.0378 260 SER B O   
6227  C CB  . SER B 260 ? 0.3916 0.3506 0.2981 0.0103  -0.0627 -0.0262 260 SER B CB  
6228  O OG  . SER B 260 ? 0.3665 0.3307 0.2802 0.0044  -0.0591 -0.0258 260 SER B OG  
6229  N N   . ASN B 261 ? 0.3628 0.3269 0.2794 0.0084  -0.0717 -0.0402 261 ASN B N   
6230  C CA  . ASN B 261 ? 0.4210 0.3902 0.3469 0.0038  -0.0749 -0.0472 261 ASN B CA  
6231  C C   . ASN B 261 ? 0.4478 0.4240 0.3852 -0.0036 -0.0710 -0.0462 261 ASN B C   
6232  O O   . ASN B 261 ? 0.4216 0.4129 0.3691 -0.0043 -0.0736 -0.0508 261 ASN B O   
6233  C CB  . ASN B 261 ? 0.4505 0.4052 0.3752 0.0013  -0.0774 -0.0521 261 ASN B CB  
6234  C CG  . ASN B 261 ? 0.4663 0.4190 0.3822 0.0095  -0.0817 -0.0562 261 ASN B CG  
6235  O OD1 . ASN B 261 ? 0.4219 0.3862 0.3337 0.0156  -0.0832 -0.0566 261 ASN B OD1 
6236  N ND2 . ASN B 261 ? 0.4530 0.3900 0.3655 0.0100  -0.0830 -0.0589 261 ASN B ND2 
6237  N N   . GLU B 262 ? 0.3986 0.3657 0.3340 -0.0083 -0.0647 -0.0400 262 GLU B N   
6238  C CA  . GLU B 262 ? 0.4272 0.4022 0.3735 -0.0157 -0.0592 -0.0393 262 GLU B CA  
6239  C C   . GLU B 262 ? 0.3701 0.3618 0.3206 -0.0112 -0.0582 -0.0384 262 GLU B C   
6240  O O   . GLU B 262 ? 0.3854 0.3918 0.3499 -0.0146 -0.0570 -0.0421 262 GLU B O   
6241  C CB  . GLU B 262 ? 0.4527 0.4126 0.3921 -0.0213 -0.0518 -0.0322 262 GLU B CB  
6242  C CG  . GLU B 262 ? 0.4702 0.4118 0.4079 -0.0274 -0.0520 -0.0328 262 GLU B CG  
6243  C CD  . GLU B 262 ? 0.5799 0.5046 0.5078 -0.0325 -0.0444 -0.0241 262 GLU B CD  
6244  O OE1 . GLU B 262 ? 0.6210 0.5537 0.5509 -0.0364 -0.0371 -0.0205 262 GLU B OE1 
6245  O OE2 . GLU B 262 ? 0.5636 0.4671 0.4809 -0.0317 -0.0458 -0.0210 262 GLU B OE2 
6246  N N   . ALA B 263 ? 0.3591 0.3493 0.2993 -0.0035 -0.0587 -0.0342 263 ALA B N   
6247  C CA  . ALA B 263 ? 0.3444 0.3470 0.2880 0.0012  -0.0579 -0.0334 263 ALA B CA  
6248  C C   . ALA B 263 ? 0.3747 0.3904 0.3252 0.0058  -0.0645 -0.0384 263 ALA B C   
6249  O O   . ALA B 263 ? 0.3844 0.4133 0.3449 0.0072  -0.0645 -0.0404 263 ALA B O   
6250  C CB  . ALA B 263 ? 0.3509 0.3469 0.2826 0.0070  -0.0569 -0.0283 263 ALA B CB  
6251  N N   . LEU B 264 ? 0.3908 0.4034 0.3355 0.0089  -0.0703 -0.0410 264 LEU B N   
6252  C CA  . LEU B 264 ? 0.3836 0.4081 0.3316 0.0139  -0.0773 -0.0458 264 LEU B CA  
6253  C C   . LEU B 264 ? 0.3838 0.4212 0.3487 0.0087  -0.0798 -0.0532 264 LEU B C   
6254  O O   . LEU B 264 ? 0.4022 0.4545 0.3750 0.0130  -0.0841 -0.0563 264 LEU B O   
6255  C CB  . LEU B 264 ? 0.4259 0.4446 0.3629 0.0176  -0.0820 -0.0481 264 LEU B CB  
6256  C CG  . LEU B 264 ? 0.4536 0.4648 0.3767 0.0235  -0.0797 -0.0418 264 LEU B CG  
6257  C CD1 . LEU B 264 ? 0.4119 0.4194 0.3250 0.0270  -0.0830 -0.0449 264 LEU B CD1 
6258  C CD2 . LEU B 264 ? 0.4442 0.4620 0.3657 0.0295  -0.0798 -0.0375 264 LEU B CD2 
6259  N N   . GLU B 265 ? 0.4168 0.4483 0.3880 -0.0007 -0.0772 -0.0561 265 GLU B N   
6260  C CA  . GLU B 265 ? 0.4321 0.4761 0.4226 -0.0084 -0.0776 -0.0633 265 GLU B CA  
6261  C C   . GLU B 265 ? 0.3776 0.4356 0.3801 -0.0091 -0.0724 -0.0618 265 GLU B C   
6262  O O   . GLU B 265 ? 0.3219 0.3991 0.3403 -0.0082 -0.0763 -0.0684 265 GLU B O   
6263  C CB  . GLU B 265 ? 0.4591 0.4896 0.4526 -0.0196 -0.0732 -0.0644 265 GLU B CB  
6264  C CG  . GLU B 265 ? 0.6002 0.6206 0.5884 -0.0198 -0.0798 -0.0703 265 GLU B CG  
6265  C CD  . GLU B 265 ? 0.6881 0.7244 0.6901 -0.0210 -0.0884 -0.0822 265 GLU B CD  
6266  O OE1 . GLU B 265 ? 0.6629 0.7174 0.6832 -0.0250 -0.0882 -0.0865 265 GLU B OE1 
6267  O OE2 . GLU B 265 ? 0.7474 0.7792 0.7422 -0.0174 -0.0956 -0.0882 265 GLU B OE2 
6268  N N   . LEU B 266 ? 0.4087 0.4581 0.4042 -0.0101 -0.0638 -0.0541 266 LEU B N   
6269  C CA  . LEU B 266 ? 0.4094 0.4713 0.4149 -0.0103 -0.0578 -0.0533 266 LEU B CA  
6270  C C   . LEU B 266 ? 0.3997 0.4750 0.4083 0.0010  -0.0638 -0.0550 266 LEU B C   
6271  O O   . LEU B 266 ? 0.4255 0.5197 0.4513 0.0020  -0.0644 -0.0603 266 LEU B O   
6272  C CB  . LEU B 266 ? 0.3889 0.4373 0.3815 -0.0115 -0.0489 -0.0453 266 LEU B CB  
6273  C CG  . LEU B 266 ? 0.3564 0.4170 0.3560 -0.0091 -0.0429 -0.0451 266 LEU B CG  
6274  C CD1 . LEU B 266 ? 0.3367 0.4121 0.3555 -0.0184 -0.0362 -0.0499 266 LEU B CD1 
6275  C CD2 . LEU B 266 ? 0.3984 0.4463 0.3819 -0.0071 -0.0366 -0.0382 266 LEU B CD2 
6276  N N   . TYR B 267 ? 0.3599 0.4255 0.3525 0.0096  -0.0680 -0.0505 267 TYR B N   
6277  C CA  . TYR B 267 ? 0.4004 0.4742 0.3927 0.0206  -0.0740 -0.0505 267 TYR B CA  
6278  C C   . TYR B 267 ? 0.4196 0.5104 0.4242 0.0234  -0.0832 -0.0584 267 TYR B C   
6279  O O   . TYR B 267 ? 0.3763 0.4809 0.3900 0.0309  -0.0871 -0.0608 267 TYR B O   
6280  C CB  . TYR B 267 ? 0.4025 0.4618 0.3752 0.0273  -0.0765 -0.0442 267 TYR B CB  
6281  C CG  . TYR B 267 ? 0.3967 0.4442 0.3606 0.0277  -0.0695 -0.0377 267 TYR B CG  
6282  C CD1 . TYR B 267 ? 0.4079 0.4594 0.3766 0.0318  -0.0666 -0.0368 267 TYR B CD1 
6283  C CD2 . TYR B 267 ? 0.4301 0.4631 0.3815 0.0246  -0.0665 -0.0337 267 TYR B CD2 
6284  C CE1 . TYR B 267 ? 0.4001 0.4410 0.3610 0.0320  -0.0609 -0.0325 267 TYR B CE1 
6285  C CE2 . TYR B 267 ? 0.3806 0.4047 0.3252 0.0250  -0.0615 -0.0292 267 TYR B CE2 
6286  C CZ  . TYR B 267 ? 0.4041 0.4320 0.3531 0.0283  -0.0587 -0.0288 267 TYR B CZ  
6287  O OH  . TYR B 267 ? 0.3375 0.3564 0.2796 0.0284  -0.0543 -0.0258 267 TYR B OH  
6288  N N   . TYR B 268 ? 0.4572 0.5473 0.4622 0.0184  -0.0875 -0.0633 268 TYR B N   
6289  C CA  . TYR B 268 ? 0.4066 0.5135 0.4231 0.0205  -0.0975 -0.0726 268 TYR B CA  
6290  C C   . TYR B 268 ? 0.3613 0.4889 0.4044 0.0145  -0.0958 -0.0803 268 TYR B C   
6291  O O   . TYR B 268 ? 0.3149 0.4623 0.3710 0.0209  -0.1037 -0.0868 268 TYR B O   
6292  C CB  . TYR B 268 ? 0.4633 0.5627 0.4741 0.0154  -0.1018 -0.0775 268 TYR B CB  
6293  C CG  . TYR B 268 ? 0.5122 0.6301 0.5397 0.0134  -0.1110 -0.0898 268 TYR B CG  
6294  C CD1 . TYR B 268 ? 0.4892 0.6205 0.5147 0.0247  -0.1226 -0.0939 268 TYR B CD1 
6295  C CD2 . TYR B 268 ? 0.4836 0.6051 0.5289 0.0002  -0.1084 -0.0974 268 TYR B CD2 
6296  C CE1 . TYR B 268 ? 0.5255 0.6757 0.5667 0.0236  -0.1326 -0.1064 268 TYR B CE1 
6297  C CE2 . TYR B 268 ? 0.4727 0.6124 0.5357 -0.0025 -0.1172 -0.1102 268 TYR B CE2 
6298  C CZ  . TYR B 268 ? 0.5348 0.6901 0.5961 0.0096  -0.1300 -0.1153 268 TYR B CZ  
6299  O OH  . TYR B 268 ? 0.5249 0.7004 0.6042 0.0077  -0.1405 -0.1294 268 TYR B OH  
6300  N N   . GLU B 269 ? 0.3474 0.4712 0.3989 0.0023  -0.0856 -0.0799 269 GLU B N   
6301  C CA  . GLU B 269 ? 0.4474 0.5912 0.5251 -0.0056 -0.0812 -0.0870 269 GLU B CA  
6302  C C   . GLU B 269 ? 0.4088 0.5665 0.4950 0.0019  -0.0778 -0.0858 269 GLU B C   
6303  O O   . GLU B 269 ? 0.4404 0.6216 0.5512 -0.0004 -0.0770 -0.0937 269 GLU B O   
6304  C CB  . GLU B 269 ? 0.5238 0.6559 0.6037 -0.0209 -0.0693 -0.0846 269 GLU B CB  
6305  C CG  . GLU B 269 ? 0.6354 0.7521 0.7088 -0.0281 -0.0728 -0.0867 269 GLU B CG  
6306  C CD  . GLU B 269 ? 0.7390 0.8363 0.8073 -0.0407 -0.0613 -0.0809 269 GLU B CD  
6307  O OE1 . GLU B 269 ? 0.7053 0.7994 0.7701 -0.0427 -0.0507 -0.0738 269 GLU B OE1 
6308  O OE2 . GLU B 269 ? 0.7886 0.8726 0.8549 -0.0478 -0.0632 -0.0835 269 GLU B OE2 
6309  N N   . LYS B 270 ? 0.3645 0.5089 0.4326 0.0108  -0.0759 -0.0771 270 LYS B N   
6310  C CA  . LYS B 270 ? 0.3371 0.4917 0.4117 0.0195  -0.0736 -0.0766 270 LYS B CA  
6311  C C   . LYS B 270 ? 0.3995 0.5620 0.4732 0.0348  -0.0859 -0.0782 270 LYS B C   
6312  O O   . LYS B 270 ? 0.3973 0.5633 0.4729 0.0445  -0.0854 -0.0767 270 LYS B O   
6313  C CB  . LYS B 270 ? 0.3615 0.4968 0.4182 0.0203  -0.0646 -0.0675 270 LYS B CB  
6314  C CG  . LYS B 270 ? 0.3321 0.4629 0.3904 0.0073  -0.0518 -0.0659 270 LYS B CG  
6315  C CD  . LYS B 270 ? 0.4385 0.5936 0.5234 0.0005  -0.0462 -0.0741 270 LYS B CD  
6316  C CE  . LYS B 270 ? 0.5265 0.6756 0.6101 -0.0125 -0.0318 -0.0710 270 LYS B CE  
6317  N NZ  . LYS B 270 ? 0.5759 0.7403 0.6818 -0.0258 -0.0271 -0.0776 270 LYS B NZ  
6318  N N   . GLY B 271 ? 0.3503 0.5145 0.4198 0.0379  -0.0971 -0.0811 271 GLY B N   
6319  C CA  . GLY B 271 ? 0.3229 0.4949 0.3898 0.0528  -0.1096 -0.0823 271 GLY B CA  
6320  C C   . GLY B 271 ? 0.3963 0.5465 0.4360 0.0631  -0.1118 -0.0716 271 GLY B C   
6321  O O   . GLY B 271 ? 0.4761 0.6295 0.5117 0.0767  -0.1204 -0.0702 271 GLY B O   
6322  N N   . ILE B 272 ? 0.3538 0.4822 0.3754 0.0573  -0.1044 -0.0638 272 ILE B N   
6323  C CA  . ILE B 272 ? 0.3684 0.4769 0.3659 0.0650  -0.1054 -0.0541 272 ILE B CA  
6324  C C   . ILE B 272 ? 0.3928 0.4989 0.3763 0.0680  -0.1141 -0.0545 272 ILE B C   
6325  O O   . ILE B 272 ? 0.3883 0.4942 0.3717 0.0595  -0.1140 -0.0587 272 ILE B O   
6326  C CB  . ILE B 272 ? 0.3601 0.4495 0.3465 0.0577  -0.0944 -0.0471 272 ILE B CB  
6327  C CG1 . ILE B 272 ? 0.2992 0.3928 0.2987 0.0533  -0.0855 -0.0486 272 ILE B CG1 
6328  C CG2 . ILE B 272 ? 0.3880 0.4593 0.3544 0.0649  -0.0940 -0.0378 272 ILE B CG2 
6329  C CD1 . ILE B 272 ? 0.3683 0.4663 0.3736 0.0639  -0.0865 -0.0482 272 ILE B CD1 
6330  N N   . ASN B 273 ? 0.4813 0.5847 0.4518 0.0806  -0.1218 -0.0503 273 ASN B N   
6331  C CA  . ASN B 273 ? 0.4991 0.6015 0.4535 0.0853  -0.1304 -0.0507 273 ASN B CA  
6332  C C   . ASN B 273 ? 0.5008 0.5825 0.4314 0.0832  -0.1246 -0.0422 273 ASN B C   
6333  O O   . ASN B 273 ? 0.4929 0.5739 0.4125 0.0820  -0.1280 -0.0450 273 ASN B O   
6334  C CB  . ASN B 273 ? 0.6257 0.7340 0.5736 0.1007  -0.1415 -0.0491 273 ASN B CB  
6335  C CG  . ASN B 273 ? 0.7601 0.8925 0.7333 0.1048  -0.1490 -0.0588 273 ASN B CG  
6336  O OD1 . ASN B 273 ? 0.8591 0.9937 0.8387 0.1138  -0.1501 -0.0563 273 ASN B OD1 
6337  N ND2 . ASN B 273 ? 0.7470 0.8980 0.7365 0.0981  -0.1540 -0.0708 273 ASN B ND2 
6338  N N   . MET B 274 ? 0.4663 0.5324 0.3898 0.0829  -0.1159 -0.0331 274 MET B N   
6339  C CA  . MET B 274 ? 0.4707 0.5193 0.3736 0.0818  -0.1103 -0.0249 274 MET B CA  
6340  C C   . MET B 274 ? 0.4112 0.4478 0.3171 0.0755  -0.0996 -0.0200 274 MET B C   
6341  O O   . MET B 274 ? 0.4542 0.4912 0.3704 0.0769  -0.0975 -0.0194 274 MET B O   
6342  C CB  . MET B 274 ? 0.5677 0.6081 0.4505 0.0933  -0.1146 -0.0167 274 MET B CB  
6343  C CG  . MET B 274 ? 0.7095 0.7338 0.5714 0.0915  -0.1076 -0.0083 274 MET B CG  
6344  S SD  . MET B 274 ? 0.8494 0.8543 0.7085 0.0901  -0.0972 0.0026  274 MET B SD  
6345  C CE  . MET B 274 ? 0.8713 0.8677 0.7148 0.1046  -0.1037 0.0116  274 MET B CE  
6346  N N   . LEU B 275 ? 0.3985 0.4256 0.2959 0.0690  -0.0934 -0.0177 275 LEU B N   
6347  C CA  . LEU B 275 ? 0.4571 0.4727 0.3546 0.0640  -0.0845 -0.0130 275 LEU B CA  
6348  C C   . LEU B 275 ? 0.4522 0.4575 0.3341 0.0629  -0.0803 -0.0076 275 LEU B C   
6349  O O   . LEU B 275 ? 0.5163 0.5233 0.3867 0.0659  -0.0834 -0.0077 275 LEU B O   
6350  C CB  . LEU B 275 ? 0.4779 0.4969 0.3883 0.0552  -0.0804 -0.0181 275 LEU B CB  
6351  C CG  . LEU B 275 ? 0.5700 0.5933 0.4827 0.0491  -0.0816 -0.0240 275 LEU B CG  
6352  C CD1 . LEU B 275 ? 0.6091 0.6230 0.5108 0.0464  -0.0778 -0.0216 275 LEU B CD1 
6353  C CD2 . LEU B 275 ? 0.5752 0.6027 0.5019 0.0420  -0.0785 -0.0282 275 LEU B CD2 
6354  N N   . ALA B 276 ? 0.4386 0.4344 0.3207 0.0586  -0.0729 -0.0039 276 ALA B N   
6355  C CA  . ALA B 276 ? 0.4628 0.4516 0.3348 0.0558  -0.0675 -0.0002 276 ALA B CA  
6356  C C   . ALA B 276 ? 0.4540 0.4426 0.3341 0.0484  -0.0631 -0.0036 276 ALA B C   
6357  O O   . ALA B 276 ? 0.4634 0.4530 0.3537 0.0455  -0.0627 -0.0063 276 ALA B O   
6358  C CB  . ALA B 276 ? 0.4999 0.4766 0.3637 0.0581  -0.0629 0.0085  276 ALA B CB  
6359  N N   . THR B 277 ? 0.4131 0.4008 0.2878 0.0460  -0.0598 -0.0037 277 THR B N   
6360  C CA  . THR B 277 ? 0.4006 0.3879 0.2819 0.0407  -0.0564 -0.0066 277 THR B CA  
6361  C C   . THR B 277 ? 0.4326 0.4184 0.3087 0.0394  -0.0508 -0.0041 277 THR B C   
6362  O O   . THR B 277 ? 0.4599 0.4421 0.3274 0.0414  -0.0479 0.0014  277 THR B O   
6363  C CB  . THR B 277 ? 0.3910 0.3829 0.2766 0.0391  -0.0603 -0.0130 277 THR B CB  
6364  O OG1 . THR B 277 ? 0.3905 0.3804 0.2805 0.0355  -0.0580 -0.0149 277 THR B OG1 
6365  C CG2 . THR B 277 ? 0.3981 0.3939 0.2763 0.0419  -0.0633 -0.0161 277 THR B CG2 
6366  N N   . ASP B 278 ? 0.3828 0.3711 0.2639 0.0363  -0.0490 -0.0079 278 ASP B N   
6367  C CA  . ASP B 278 ? 0.4528 0.4423 0.3343 0.0341  -0.0428 -0.0067 278 ASP B CA  
6368  C C   . ASP B 278 ? 0.4253 0.4211 0.3009 0.0364  -0.0415 -0.0097 278 ASP B C   
6369  O O   . ASP B 278 ? 0.3906 0.3890 0.2651 0.0388  -0.0462 -0.0149 278 ASP B O   
6370  C CB  . ASP B 278 ? 0.4276 0.4183 0.3202 0.0303  -0.0421 -0.0101 278 ASP B CB  
6371  C CG  . ASP B 278 ? 0.4551 0.4496 0.3526 0.0270  -0.0357 -0.0100 278 ASP B CG  
6372  O OD1 . ASP B 278 ? 0.4793 0.4703 0.3733 0.0251  -0.0301 -0.0047 278 ASP B OD1 
6373  O OD2 . ASP B 278 ? 0.4898 0.4909 0.3951 0.0262  -0.0361 -0.0151 278 ASP B OD2 
6374  N N   . GLU B 279 ? 0.3871 0.4107 0.2683 0.1132  -0.0224 -0.0155 279 GLU B N   
6375  C CA  . GLU B 279 ? 0.3977 0.4149 0.2699 0.1147  -0.0147 -0.0191 279 GLU B CA  
6376  C C   . GLU B 279 ? 0.4193 0.4411 0.3060 0.1191  -0.0095 -0.0203 279 GLU B C   
6377  O O   . GLU B 279 ? 0.4074 0.4210 0.2893 0.1212  -0.0056 -0.0253 279 GLU B O   
6378  C CB  . GLU B 279 ? 0.5103 0.5283 0.3743 0.1126  -0.0075 -0.0177 279 GLU B CB  
6379  C CG  . GLU B 279 ? 0.6238 0.6323 0.4718 0.1122  0.0008  -0.0228 279 GLU B CG  
6380  C CD  . GLU B 279 ? 0.6941 0.7015 0.5301 0.1080  0.0081  -0.0211 279 GLU B CD  
6381  O OE1 . GLU B 279 ? 0.6508 0.6631 0.4900 0.1053  0.0052  -0.0157 279 GLU B OE1 
6382  O OE2 . GLU B 279 ? 0.7247 0.7258 0.5479 0.1067  0.0177  -0.0259 279 GLU B OE2 
6383  N N   . VAL B 280 ? 0.3620 0.3958 0.2657 0.1205  -0.0101 -0.0159 280 VAL B N   
6384  C CA  . VAL B 280 ? 0.3668 0.4038 0.2846 0.1252  -0.0074 -0.0155 280 VAL B CA  
6385  C C   . VAL B 280 ? 0.3514 0.3779 0.2672 0.1260  -0.0113 -0.0180 280 VAL B C   
6386  O O   . VAL B 280 ? 0.3917 0.4119 0.3107 0.1300  -0.0074 -0.0210 280 VAL B O   
6387  C CB  . VAL B 280 ? 0.3945 0.4452 0.3281 0.1254  -0.0101 -0.0094 280 VAL B CB  
6388  C CG1 . VAL B 280 ? 0.3526 0.4040 0.2993 0.1304  -0.0100 -0.0077 280 VAL B CG1 
6389  C CG2 . VAL B 280 ? 0.4038 0.4654 0.3420 0.1244  -0.0053 -0.0078 280 VAL B CG2 
6390  N N   . ILE B 281 ? 0.4043 0.4286 0.3164 0.1220  -0.0186 -0.0174 281 ILE B N   
6391  C CA  . ILE B 281 ? 0.4143 0.4289 0.3248 0.1212  -0.0221 -0.0202 281 ILE B CA  
6392  C C   . ILE B 281 ? 0.4024 0.4042 0.3004 0.1220  -0.0192 -0.0272 281 ILE B C   
6393  O O   . ILE B 281 ? 0.4085 0.4013 0.3082 0.1243  -0.0169 -0.0303 281 ILE B O   
6394  C CB  . ILE B 281 ? 0.4379 0.4546 0.3480 0.1161  -0.0293 -0.0199 281 ILE B CB  
6395  C CG1 . ILE B 281 ? 0.5257 0.5546 0.4457 0.1143  -0.0308 -0.0145 281 ILE B CG1 
6396  C CG2 . ILE B 281 ? 0.3449 0.3527 0.2550 0.1138  -0.0324 -0.0232 281 ILE B CG2 
6397  C CD1 . ILE B 281 ? 0.5456 0.5778 0.4746 0.1160  -0.0290 -0.0097 281 ILE B CD1 
6398  N N   . LEU B 282 ? 0.4231 0.4219 0.3067 0.1196  -0.0199 -0.0297 282 LEU B N   
6399  C CA  . LEU B 282 ? 0.4326 0.4185 0.2998 0.1191  -0.0170 -0.0367 282 LEU B CA  
6400  C C   . LEU B 282 ? 0.4341 0.4171 0.3051 0.1239  -0.0064 -0.0401 282 LEU B C   
6401  O O   . LEU B 282 ? 0.4345 0.4058 0.3009 0.1249  -0.0038 -0.0465 282 LEU B O   
6402  C CB  . LEU B 282 ? 0.4529 0.4363 0.3022 0.1157  -0.0183 -0.0369 282 LEU B CB  
6403  C CG  . LEU B 282 ? 0.4213 0.3897 0.2483 0.1133  -0.0173 -0.0442 282 LEU B CG  
6404  C CD1 . LEU B 282 ? 0.3927 0.3533 0.2182 0.1110  -0.0260 -0.0484 282 LEU B CD1 
6405  C CD2 . LEU B 282 ? 0.4632 0.4271 0.2690 0.1091  -0.0196 -0.0427 282 LEU B CD2 
6406  N N   . LYS B 283 ? 0.4523 0.4462 0.3334 0.1270  0.0000  -0.0366 283 LYS B N   
6407  C CA  . LYS B 283 ? 0.4950 0.4887 0.3840 0.1322  0.0106  -0.0405 283 LYS B CA  
6408  C C   . LYS B 283 ? 0.4982 0.4884 0.4033 0.1375  0.0095  -0.0403 283 LYS B C   
6409  O O   . LYS B 283 ? 0.4474 0.4306 0.3564 0.1421  0.0169  -0.0463 283 LYS B O   
6410  C CB  . LYS B 283 ? 0.5380 0.5470 0.4389 0.1339  0.0164  -0.0364 283 LYS B CB  
6411  C CG  . LYS B 283 ? 0.6642 0.6740 0.5485 0.1287  0.0210  -0.0373 283 LYS B CG  
6412  C CD  . LYS B 283 ? 0.7388 0.7647 0.6379 0.1294  0.0268  -0.0333 283 LYS B CD  
6413  C CE  . LYS B 283 ? 0.8188 0.8432 0.7009 0.1238  0.0344  -0.0349 283 LYS B CE  
6414  N NZ  . LYS B 283 ? 0.9071 0.9249 0.7811 0.1244  0.0477  -0.0436 283 LYS B NZ  
6415  N N   . ASN B 284 ? 0.4765 0.4703 0.3904 0.1365  0.0008  -0.0337 284 ASN B N   
6416  C CA  . ASN B 284 ? 0.4584 0.4466 0.3849 0.1402  -0.0015 -0.0316 284 ASN B CA  
6417  C C   . ASN B 284 ? 0.4575 0.4286 0.3743 0.1376  -0.0038 -0.0372 284 ASN B C   
6418  O O   . ASN B 284 ? 0.4472 0.4085 0.3720 0.1412  -0.0031 -0.0378 284 ASN B O   
6419  C CB  . ASN B 284 ? 0.5070 0.5045 0.4430 0.1383  -0.0091 -0.0221 284 ASN B CB  
6420  C CG  . ASN B 284 ? 0.5273 0.5408 0.4765 0.1414  -0.0080 -0.0163 284 ASN B CG  
6421  O OD1 . ASN B 284 ? 0.5110 0.5288 0.4681 0.1465  -0.0012 -0.0188 284 ASN B OD1 
6422  N ND2 . ASN B 284 ? 0.5168 0.5396 0.4690 0.1378  -0.0142 -0.0093 284 ASN B ND2 
6423  N N   . SER B 285 ? 0.4438 0.4107 0.3442 0.1314  -0.0072 -0.0414 285 SER B N   
6424  C CA  . SER B 285 ? 0.4668 0.4203 0.3589 0.1270  -0.0116 -0.0465 285 SER B CA  
6425  C C   . SER B 285 ? 0.5045 0.4442 0.3802 0.1262  -0.0072 -0.0570 285 SER B C   
6426  O O   . SER B 285 ? 0.5148 0.4412 0.3862 0.1235  -0.0094 -0.0625 285 SER B O   
6427  C CB  . SER B 285 ? 0.5324 0.4918 0.4201 0.1202  -0.0207 -0.0442 285 SER B CB  
6428  O OG  . SER B 285 ? 0.5406 0.5133 0.4402 0.1199  -0.0236 -0.0358 285 SER B OG  
6429  N N   . VAL B 286 ? 0.4317 0.3736 0.2965 0.1270  -0.0011 -0.0603 286 VAL B N   
6430  C CA  . VAL B 286 ? 0.5692 0.4976 0.4141 0.1249  0.0042  -0.0707 286 VAL B CA  
6431  C C   . VAL B 286 ? 0.5582 0.4900 0.4037 0.1295  0.0173  -0.0738 286 VAL B C   
6432  O O   . VAL B 286 ? 0.5631 0.5094 0.4208 0.1325  0.0201  -0.0673 286 VAL B O   
6433  C CB  . VAL B 286 ? 0.6483 0.5738 0.4703 0.1173  -0.0037 -0.0724 286 VAL B CB  
6434  C CG1 . VAL B 286 ? 0.6202 0.5479 0.4477 0.1130  -0.0168 -0.0688 286 VAL B CG1 
6435  C CG2 . VAL B 286 ? 0.6517 0.5873 0.4661 0.1163  -0.0022 -0.0673 286 VAL B CG2 
6436  N N   . GLU B 287 ? 0.6662 0.5848 0.4987 0.1294  0.0260  -0.0847 287 GLU B N   
6437  C CA  . GLU B 287 ? 0.6852 0.6073 0.5194 0.1332  0.0408  -0.0896 287 GLU B CA  
6438  C C   . GLU B 287 ? 0.7300 0.6565 0.5425 0.1270  0.0436  -0.0887 287 GLU B C   
6439  O O   . GLU B 287 ? 0.7640 0.7047 0.5863 0.1286  0.0483  -0.0832 287 GLU B O   
6440  C CB  . GLU B 287 ? 0.7574 0.6633 0.5869 0.1354  0.0510  -0.1028 287 GLU B CB  
6441  C CG  . GLU B 287 ? 0.7873 0.6848 0.6360 0.1408  0.0473  -0.1032 287 GLU B CG  
6442  C CD  . GLU B 287 ? 0.8987 0.7778 0.7427 0.1429  0.0575  -0.1175 287 GLU B CD  
6443  O OE1 . GLU B 287 ? 0.9505 0.8237 0.8164 0.1505  0.0596  -0.1185 287 GLU B OE1 
6444  O OE2 . GLU B 287 ? 0.9199 0.7892 0.7373 0.1368  0.0633  -0.1277 287 GLU B OE2 
6445  N N   . ARG B 288 ? 0.6823 0.5957 0.4645 0.1193  0.0400  -0.0937 288 ARG B N   
6446  C CA  . ARG B 288 ? 0.7306 0.6441 0.4874 0.1124  0.0405  -0.0916 288 ARG B CA  
6447  C C   . ARG B 288 ? 0.7117 0.6340 0.4717 0.1102  0.0253  -0.0798 288 ARG B C   
6448  O O   . ARG B 288 ? 0.7715 0.6877 0.5229 0.1066  0.0120  -0.0789 288 ARG B O   
6449  C CB  . ARG B 288 ? 0.7942 0.6886 0.5156 0.1048  0.0413  -0.1014 288 ARG B CB  
6450  C CG  . ARG B 288 ? 0.8562 0.7429 0.5704 0.1058  0.0607  -0.1141 288 ARG B CG  
6451  C CD  . ARG B 288 ? 0.9055 0.7707 0.5868 0.0988  0.0624  -0.1270 288 ARG B CD  
6452  N NE  . ARG B 288 ? 0.9848 0.8414 0.6656 0.0974  0.0469  -0.1278 288 ARG B NE  
6453  C CZ  . ARG B 288 ? 1.0850 0.9366 0.7454 0.0902  0.0307  -0.1238 288 ARG B CZ  
6454  N NH1 . ARG B 288 ? 1.1219 0.9676 0.7865 0.0888  0.0181  -0.1258 288 ARG B NH1 
6455  N NH2 . ARG B 288 ? 1.1233 0.9762 0.7616 0.0846  0.0266  -0.1172 288 ARG B NH2 
6456  N N   . ALA B 289 ? 0.6805 0.6175 0.4543 0.1122  0.0275  -0.0716 289 ALA B N   
6457  C CA  . ALA B 289 ? 0.6933 0.6410 0.4797 0.1123  0.0152  -0.0612 289 ALA B CA  
6458  C C   . ALA B 289 ? 0.7230 0.6719 0.4930 0.1071  0.0129  -0.0553 289 ALA B C   
6459  O O   . ALA B 289 ? 0.8000 0.7610 0.5827 0.1082  0.0158  -0.0489 289 ALA B O   
6460  C CB  . ALA B 289 ? 0.5694 0.5327 0.3883 0.1191  0.0181  -0.0562 289 ALA B CB  
6461  N N   . SER B 290 ? 0.6814 0.6168 0.4229 0.1010  0.0067  -0.0570 290 SER B N   
6462  C CA  . SER B 290 ? 0.6435 0.5770 0.3678 0.0960  0.0030  -0.0500 290 SER B CA  
6463  C C   . SER B 290 ? 0.5700 0.5085 0.3045 0.0966  -0.0133 -0.0422 290 SER B C   
6464  O O   . SER B 290 ? 0.5773 0.5117 0.3117 0.0964  -0.0251 -0.0441 290 SER B O   
6465  C CB  . SER B 290 ? 0.6701 0.5854 0.3562 0.0887  0.0028  -0.0540 290 SER B CB  
6466  O OG  . SER B 290 ? 0.6269 0.5371 0.2956 0.0839  -0.0065 -0.0454 290 SER B OG  
6467  N N   . PRO B 291 ? 0.6082 0.5556 0.3527 0.0970  -0.0141 -0.0344 291 PRO B N   
6468  C CA  . PRO B 291 ? 0.6018 0.5539 0.3576 0.0979  -0.0283 -0.0282 291 PRO B CA  
6469  C C   . PRO B 291 ? 0.5752 0.5146 0.3079 0.0936  -0.0404 -0.0243 291 PRO B C   
6470  O O   . PRO B 291 ? 0.5030 0.4456 0.2459 0.0948  -0.0524 -0.0195 291 PRO B O   
6471  C CB  . PRO B 291 ? 0.6202 0.5858 0.3952 0.0998  -0.0223 -0.0226 291 PRO B CB  
6472  C CG  . PRO B 291 ? 0.6086 0.5710 0.3693 0.0965  -0.0084 -0.0232 291 PRO B CG  
6473  C CD  . PRO B 291 ? 0.6305 0.5845 0.3777 0.0962  -0.0011 -0.0317 291 PRO B CD  
6474  N N   . TYR B 292 ? 0.5702 0.4947 0.2717 0.0884  -0.0379 -0.0263 292 TYR B N   
6475  C CA  . TYR B 292 ? 0.5577 0.4681 0.2335 0.0837  -0.0500 -0.0207 292 TYR B CA  
6476  C C   . TYR B 292 ? 0.5974 0.4993 0.2628 0.0826  -0.0655 -0.0242 292 TYR B C   
6477  O O   . TYR B 292 ? 0.5495 0.4372 0.1891 0.0783  -0.0771 -0.0203 292 TYR B O   
6478  C CB  . TYR B 292 ? 0.6447 0.5423 0.2882 0.0769  -0.0388 -0.0196 292 TYR B CB  
6479  C CG  . TYR B 292 ? 0.6976 0.6062 0.3557 0.0775  -0.0235 -0.0168 292 TYR B CG  
6480  C CD1 . TYR B 292 ? 0.6857 0.6055 0.3686 0.0810  -0.0277 -0.0103 292 TYR B CD1 
6481  C CD2 . TYR B 292 ? 0.7864 0.6949 0.4351 0.0742  -0.0047 -0.0217 292 TYR B CD2 
6482  C CE1 . TYR B 292 ? 0.7092 0.6398 0.4064 0.0808  -0.0151 -0.0081 292 TYR B CE1 
6483  C CE2 . TYR B 292 ? 0.7579 0.6789 0.4239 0.0746  0.0084  -0.0195 292 TYR B CE2 
6484  C CZ  . TYR B 292 ? 0.7402 0.6720 0.4298 0.0776  0.0024  -0.0124 292 TYR B CZ  
6485  O OH  . TYR B 292 ? 0.7091 0.6536 0.4159 0.0771  0.0140  -0.0105 292 TYR B OH  
6486  N N   . LEU B 293 ? 0.5059 0.4157 0.1911 0.0860  -0.0667 -0.0309 293 LEU B N   
6487  C CA  . LEU B 293 ? 0.5740 0.4782 0.2540 0.0845  -0.0803 -0.0359 293 LEU B CA  
6488  C C   . LEU B 293 ? 0.5390 0.4570 0.2520 0.0889  -0.0913 -0.0347 293 LEU B C   
6489  O O   . LEU B 293 ? 0.4842 0.4159 0.2240 0.0931  -0.0841 -0.0337 293 LEU B O   
6490  C CB  . LEU B 293 ? 0.5261 0.4258 0.2002 0.0831  -0.0711 -0.0465 293 LEU B CB  
6491  C CG  . LEU B 293 ? 0.6705 0.5534 0.3080 0.0771  -0.0632 -0.0524 293 LEU B CG  
6492  C CD1 . LEU B 293 ? 0.7215 0.6034 0.3482 0.0761  -0.0467 -0.0494 293 LEU B CD1 
6493  C CD2 . LEU B 293 ? 0.6169 0.4973 0.2587 0.0775  -0.0560 -0.0638 293 LEU B CD2 
6494  N N   . ARG B 294 ? 0.5596 0.4742 0.2703 0.0873  -0.1088 -0.0352 294 ARG B N   
6495  C CA  . ARG B 294 ? 0.5683 0.4963 0.3107 0.0902  -0.1177 -0.0372 294 ARG B CA  
6496  C C   . ARG B 294 ? 0.5737 0.5036 0.3237 0.0889  -0.1121 -0.0463 294 ARG B C   
6497  O O   . ARG B 294 ? 0.6002 0.5180 0.3284 0.0845  -0.1132 -0.0523 294 ARG B O   
6498  C CB  . ARG B 294 ? 0.5598 0.4853 0.3010 0.0893  -0.1390 -0.0351 294 ARG B CB  
6499  C CG  . ARG B 294 ? 0.5576 0.4987 0.3339 0.0914  -0.1471 -0.0389 294 ARG B CG  
6500  C CD  . ARG B 294 ? 0.5598 0.5029 0.3446 0.0927  -0.1678 -0.0357 294 ARG B CD  
6501  N NE  . ARG B 294 ? 0.5914 0.5220 0.3516 0.0880  -0.1826 -0.0376 294 ARG B NE  
6502  C CZ  . ARG B 294 ? 0.6505 0.5686 0.3889 0.0868  -0.1954 -0.0307 294 ARG B CZ  
6503  N NH1 . ARG B 294 ? 0.6286 0.5452 0.3695 0.0899  -0.1935 -0.0214 294 ARG B NH1 
6504  N NH2 . ARG B 294 ? 0.7255 0.6341 0.4457 0.0798  -0.2053 -0.0322 294 ARG B NH2 
6505  N N   . TYR B 295 ? 0.5231 0.4664 0.3024 0.0919  -0.1058 -0.0473 295 TYR B N   
6506  C CA  . TYR B 295 ? 0.4583 0.4020 0.2463 0.0907  -0.0999 -0.0546 295 TYR B CA  
6507  C C   . TYR B 295 ? 0.4988 0.4518 0.3100 0.0891  -0.1107 -0.0576 295 TYR B C   
6508  O O   . TYR B 295 ? 0.5237 0.4883 0.3538 0.0910  -0.1176 -0.0538 295 TYR B O   
6509  C CB  . TYR B 295 ? 0.4812 0.4310 0.2825 0.0944  -0.0840 -0.0531 295 TYR B CB  
6510  C CG  . TYR B 295 ? 0.4686 0.4101 0.2508 0.0955  -0.0715 -0.0531 295 TYR B CG  
6511  C CD1 . TYR B 295 ? 0.4681 0.4115 0.2433 0.0969  -0.0677 -0.0466 295 TYR B CD1 
6512  C CD2 . TYR B 295 ? 0.5325 0.4641 0.3048 0.0947  -0.0630 -0.0602 295 TYR B CD2 
6513  C CE1 . TYR B 295 ? 0.4840 0.4213 0.2434 0.0970  -0.0552 -0.0474 295 TYR B CE1 
6514  C CE2 . TYR B 295 ? 0.5848 0.5101 0.3422 0.0958  -0.0503 -0.0617 295 TYR B CE2 
6515  C CZ  . TYR B 295 ? 0.5611 0.4902 0.3125 0.0966  -0.0461 -0.0553 295 TYR B CZ  
6516  O OH  . TYR B 295 ? 0.5190 0.4434 0.2575 0.0969  -0.0321 -0.0577 295 TYR B OH  
6517  N N   . TYR B 296 ? 0.4686 0.4164 0.2789 0.0851  -0.1116 -0.0652 296 TYR B N   
6518  C CA  . TYR B 296 ? 0.5068 0.4637 0.3406 0.0821  -0.1191 -0.0692 296 TYR B CA  
6519  C C   . TYR B 296 ? 0.4737 0.4303 0.3190 0.0813  -0.1068 -0.0723 296 TYR B C   
6520  O O   . TYR B 296 ? 0.4840 0.4272 0.3142 0.0798  -0.1004 -0.0771 296 TYR B O   
6521  C CB  . TYR B 296 ? 0.5875 0.5377 0.4107 0.0765  -0.1340 -0.0756 296 TYR B CB  
6522  C CG  . TYR B 296 ? 0.6523 0.5983 0.4577 0.0768  -0.1481 -0.0718 296 TYR B CG  
6523  C CD1 . TYR B 296 ? 0.6536 0.6103 0.4736 0.0812  -0.1555 -0.0647 296 TYR B CD1 
6524  C CD2 . TYR B 296 ? 0.7250 0.6545 0.4974 0.0724  -0.1542 -0.0753 296 TYR B CD2 
6525  C CE1 . TYR B 296 ? 0.6718 0.6220 0.4749 0.0818  -0.1697 -0.0600 296 TYR B CE1 
6526  C CE2 . TYR B 296 ? 0.7212 0.6444 0.4737 0.0719  -0.1684 -0.0705 296 TYR B CE2 
6527  C CZ  . TYR B 296 ? 0.7211 0.6543 0.4896 0.0770  -0.1765 -0.0622 296 TYR B CZ  
6528  O OH  . TYR B 296 ? 0.7300 0.6549 0.4789 0.0768  -0.1917 -0.0561 296 TYR B OH  
6529  N N   . PHE B 297 ? 0.4577 0.4276 0.3284 0.0821  -0.1030 -0.0694 297 PHE B N   
6530  C CA  . PHE B 297 ? 0.4365 0.4051 0.3178 0.0806  -0.0928 -0.0707 297 PHE B CA  
6531  C C   . PHE B 297 ? 0.4683 0.4355 0.3585 0.0734  -0.0990 -0.0780 297 PHE B C   
6532  O O   . PHE B 297 ? 0.4385 0.4187 0.3485 0.0703  -0.1060 -0.0792 297 PHE B O   
6533  C CB  . PHE B 297 ? 0.4420 0.4240 0.3428 0.0829  -0.0862 -0.0644 297 PHE B CB  
6534  C CG  . PHE B 297 ? 0.4272 0.4065 0.3368 0.0807  -0.0769 -0.0639 297 PHE B CG  
6535  C CD1 . PHE B 297 ? 0.4604 0.4290 0.3601 0.0843  -0.0677 -0.0616 297 PHE B CD1 
6536  C CD2 . PHE B 297 ? 0.3989 0.3859 0.3272 0.0748  -0.0775 -0.0654 297 PHE B CD2 
6537  C CE1 . PHE B 297 ? 0.4734 0.4374 0.3807 0.0828  -0.0608 -0.0597 297 PHE B CE1 
6538  C CE2 . PHE B 297 ? 0.3936 0.3758 0.3272 0.0718  -0.0692 -0.0635 297 PHE B CE2 
6539  C CZ  . PHE B 297 ? 0.4280 0.3976 0.3504 0.0761  -0.0618 -0.0601 297 PHE B CZ  
6540  N N   . ARG B 298 ? 0.5269 0.4784 0.4038 0.0706  -0.0960 -0.0838 298 ARG B N   
6541  C CA  . ARG B 298 ? 0.5575 0.5044 0.4406 0.0628  -0.1007 -0.0916 298 ARG B CA  
6542  C C   . ARG B 298 ? 0.5759 0.5308 0.4634 0.0583  -0.1168 -0.0960 298 ARG B C   
6543  O O   . ARG B 298 ? 0.6002 0.5608 0.5046 0.0514  -0.1221 -0.1011 298 ARG B O   
6544  C CB  . ARG B 298 ? 0.5432 0.4960 0.4487 0.0593  -0.0938 -0.0897 298 ARG B CB  
6545  C CG  . ARG B 298 ? 0.4868 0.4312 0.3890 0.0638  -0.0804 -0.0842 298 ARG B CG  
6546  C CD  . ARG B 298 ? 0.5162 0.4637 0.4362 0.0592  -0.0744 -0.0811 298 ARG B CD  
6547  N NE  . ARG B 298 ? 0.5585 0.4941 0.4729 0.0636  -0.0641 -0.0759 298 ARG B NE  
6548  C CZ  . ARG B 298 ? 0.5816 0.5182 0.5059 0.0621  -0.0578 -0.0693 298 ARG B CZ  
6549  N NH1 . ARG B 298 ? 0.5630 0.5123 0.5023 0.0554  -0.0585 -0.0680 298 ARG B NH1 
6550  N NH2 . ARG B 298 ? 0.5350 0.4597 0.4540 0.0672  -0.0508 -0.0642 298 ARG B NH2 
6551  N N   . GLU B 299 ? 0.5440 0.4990 0.4166 0.0618  -0.1251 -0.0939 299 GLU B N   
6552  C CA  . GLU B 299 ? 0.5437 0.5063 0.4206 0.0590  -0.1428 -0.0963 299 GLU B CA  
6553  C C   . GLU B 299 ? 0.5312 0.5150 0.4436 0.0581  -0.1470 -0.0955 299 GLU B C   
6554  O O   . GLU B 299 ? 0.5429 0.5354 0.4697 0.0537  -0.1603 -0.1004 299 GLU B O   
6555  C CB  . GLU B 299 ? 0.6437 0.5950 0.5074 0.0512  -0.1520 -0.1059 299 GLU B CB  
6556  C CG  . GLU B 299 ? 0.7271 0.6565 0.5551 0.0508  -0.1467 -0.1092 299 GLU B CG  
6557  C CD  . GLU B 299 ? 0.8153 0.7389 0.6163 0.0530  -0.1558 -0.1060 299 GLU B CD  
6558  O OE1 . GLU B 299 ? 0.8303 0.7660 0.6412 0.0565  -0.1657 -0.0994 299 GLU B OE1 
6559  O OE2 . GLU B 299 ? 0.8456 0.7514 0.6150 0.0508  -0.1530 -0.1104 299 GLU B OE2 
6560  N N   . LEU B 300 ? 0.5010 0.4939 0.4284 0.0619  -0.1354 -0.0899 300 LEU B N   
6561  C CA  . LEU B 300 ? 0.5073 0.5202 0.4671 0.0611  -0.1360 -0.0896 300 LEU B CA  
6562  C C   . LEU B 300 ? 0.5038 0.5270 0.4703 0.0685  -0.1382 -0.0833 300 LEU B C   
6563  O O   . LEU B 300 ? 0.4979 0.5362 0.4880 0.0691  -0.1467 -0.0849 300 LEU B O   
6564  C CB  . LEU B 300 ? 0.4843 0.4994 0.4562 0.0577  -0.1207 -0.0888 300 LEU B CB  
6565  C CG  . LEU B 300 ? 0.5547 0.5607 0.5267 0.0491  -0.1182 -0.0951 300 LEU B CG  
6566  C CD1 . LEU B 300 ? 0.5990 0.5988 0.5711 0.0476  -0.1025 -0.0911 300 LEU B CD1 
6567  C CD2 . LEU B 300 ? 0.5738 0.5939 0.5717 0.0414  -0.1267 -0.1024 300 LEU B CD2 
6568  N N   . ILE B 301 ? 0.5074 0.5226 0.4553 0.0742  -0.1308 -0.0766 301 ILE B N   
6569  C CA  . ILE B 301 ? 0.5149 0.5383 0.4692 0.0805  -0.1306 -0.0706 301 ILE B CA  
6570  C C   . ILE B 301 ? 0.4904 0.5000 0.4156 0.0851  -0.1284 -0.0648 301 ILE B C   
6571  O O   . ILE B 301 ? 0.5235 0.5213 0.4302 0.0844  -0.1196 -0.0647 301 ILE B O   
6572  C CB  . ILE B 301 ? 0.5244 0.5590 0.4975 0.0805  -0.1174 -0.0687 301 ILE B CB  
6573  C CG1 . ILE B 301 ? 0.4611 0.5024 0.4389 0.0866  -0.1160 -0.0632 301 ILE B CG1 
6574  C CG2 . ILE B 301 ? 0.4870 0.5115 0.4467 0.0789  -0.1041 -0.0667 301 ILE B CG2 
6575  C CD1 . ILE B 301 ? 0.4249 0.4767 0.4184 0.0856  -0.1038 -0.0622 301 ILE B CD1 
6576  N N   . SER B 302 ? 0.4732 0.4841 0.3959 0.0896  -0.1358 -0.0602 302 SER B N   
6577  C CA  . SER B 302 ? 0.4913 0.4893 0.3862 0.0926  -0.1338 -0.0544 302 SER B CA  
6578  C C   . SER B 302 ? 0.5083 0.5102 0.4065 0.0961  -0.1199 -0.0492 302 SER B C   
6579  O O   . SER B 302 ? 0.5333 0.5481 0.4542 0.0975  -0.1169 -0.0484 302 SER B O   
6580  C CB  . SER B 302 ? 0.5205 0.5152 0.4088 0.0949  -0.1493 -0.0509 302 SER B CB  
6581  O OG  . SER B 302 ? 0.5552 0.5534 0.4532 0.0921  -0.1642 -0.0562 302 SER B OG  
6582  N N   . VAL B 303 ? 0.4906 0.4821 0.3667 0.0970  -0.1112 -0.0464 303 VAL B N   
6583  C CA  . VAL B 303 ? 0.4918 0.4870 0.3700 0.0997  -0.0984 -0.0417 303 VAL B CA  
6584  C C   . VAL B 303 ? 0.4841 0.4692 0.3388 0.1013  -0.0962 -0.0371 303 VAL B C   
6585  O O   . VAL B 303 ? 0.4880 0.4607 0.3200 0.0994  -0.0961 -0.0390 303 VAL B O   
6586  C CB  . VAL B 303 ? 0.4421 0.4369 0.3230 0.0988  -0.0865 -0.0437 303 VAL B CB  
6587  C CG1 . VAL B 303 ? 0.4083 0.4084 0.2928 0.1018  -0.0756 -0.0383 303 VAL B CG1 
6588  C CG2 . VAL B 303 ? 0.4544 0.4569 0.3557 0.0955  -0.0878 -0.0479 303 VAL B CG2 
6589  N N   . PHE B 304 ? 0.4419 0.4317 0.3014 0.1037  -0.0937 -0.0315 304 PHE B N   
6590  C CA  . PHE B 304 ? 0.4755 0.4574 0.3155 0.1041  -0.0878 -0.0269 304 PHE B CA  
6591  C C   . PHE B 304 ? 0.4472 0.4368 0.2959 0.1056  -0.0741 -0.0251 304 PHE B C   
6592  O O   . PHE B 304 ? 0.4514 0.4525 0.3206 0.1066  -0.0717 -0.0250 304 PHE B O   
6593  C CB  . PHE B 304 ? 0.4841 0.4627 0.3203 0.1050  -0.0963 -0.0213 304 PHE B CB  
6594  C CG  . PHE B 304 ? 0.4777 0.4449 0.2978 0.1036  -0.1107 -0.0210 304 PHE B CG  
6595  C CD1 . PHE B 304 ? 0.5225 0.4742 0.3107 0.1004  -0.1103 -0.0194 304 PHE B CD1 
6596  C CD2 . PHE B 304 ? 0.4762 0.4484 0.3130 0.1050  -0.1247 -0.0227 304 PHE B CD2 
6597  C CE1 . PHE B 304 ? 0.5399 0.4798 0.3099 0.0982  -0.1252 -0.0184 304 PHE B CE1 
6598  C CE2 . PHE B 304 ? 0.5291 0.4912 0.3517 0.1038  -0.1405 -0.0219 304 PHE B CE2 
6599  C CZ  . PHE B 304 ? 0.5343 0.4796 0.3219 0.1002  -0.1414 -0.0193 304 PHE B CZ  
6600  N N   . PHE B 305 ? 0.3905 0.3741 0.2234 0.1053  -0.0651 -0.0240 305 PHE B N   
6601  C CA  . PHE B 305 ? 0.3922 0.3838 0.2342 0.1069  -0.0533 -0.0221 305 PHE B CA  
6602  C C   . PHE B 305 ? 0.4235 0.4145 0.2584 0.1060  -0.0505 -0.0168 305 PHE B C   
6603  O O   . PHE B 305 ? 0.3785 0.3582 0.1920 0.1037  -0.0507 -0.0156 305 PHE B O   
6604  C CB  . PHE B 305 ? 0.4197 0.4073 0.2557 0.1077  -0.0439 -0.0261 305 PHE B CB  
6605  C CG  . PHE B 305 ? 0.4491 0.4356 0.2928 0.1080  -0.0463 -0.0309 305 PHE B CG  
6606  C CD1 . PHE B 305 ? 0.4702 0.4467 0.3020 0.1056  -0.0536 -0.0357 305 PHE B CD1 
6607  C CD2 . PHE B 305 ? 0.3903 0.3848 0.2522 0.1099  -0.0423 -0.0303 305 PHE B CD2 
6608  C CE1 . PHE B 305 ? 0.4391 0.4139 0.2785 0.1047  -0.0557 -0.0405 305 PHE B CE1 
6609  C CE2 . PHE B 305 ? 0.3676 0.3589 0.2355 0.1092  -0.0443 -0.0342 305 PHE B CE2 
6610  C CZ  . PHE B 305 ? 0.3848 0.3666 0.2424 0.1064  -0.0505 -0.0396 305 PHE B CZ  
6611  N N   . ARG B 306 ? 0.3935 0.3951 0.2445 0.1069  -0.0484 -0.0136 306 ARG B N   
6612  C CA  . ARG B 306 ? 0.4392 0.4390 0.2848 0.1052  -0.0472 -0.0087 306 ARG B CA  
6613  C C   . ARG B 306 ? 0.4490 0.4472 0.2838 0.1036  -0.0356 -0.0080 306 ARG B C   
6614  O O   . ARG B 306 ? 0.3879 0.3909 0.2275 0.1053  -0.0279 -0.0110 306 ARG B O   
6615  C CB  . ARG B 306 ? 0.4294 0.4404 0.2945 0.1057  -0.0475 -0.0068 306 ARG B CB  
6616  C CG  . ARG B 306 ? 0.4465 0.4697 0.3248 0.1063  -0.0390 -0.0072 306 ARG B CG  
6617  C CD  . ARG B 306 ? 0.4126 0.4452 0.3049 0.1051  -0.0387 -0.0054 306 ARG B CD  
6618  N NE  . ARG B 306 ? 0.4295 0.4723 0.3296 0.1049  -0.0311 -0.0044 306 ARG B NE  
6619  C CZ  . ARG B 306 ? 0.3984 0.4498 0.3072 0.1027  -0.0286 -0.0026 306 ARG B CZ  
6620  N NH1 . ARG B 306 ? 0.3942 0.4441 0.3047 0.1004  -0.0316 -0.0020 306 ARG B NH1 
6621  N NH2 . ARG B 306 ? 0.4104 0.4714 0.3269 0.1030  -0.0234 -0.0016 306 ARG B NH2 
6622  N N   . ASP B 307 ? 0.4744 0.4650 0.2949 0.1003  -0.0343 -0.0040 307 ASP B N   
6623  C CA  . ASP B 307 ? 0.4979 0.4890 0.3106 0.0975  -0.0218 -0.0034 307 ASP B CA  
6624  C C   . ASP B 307 ? 0.4432 0.4496 0.2776 0.0980  -0.0162 -0.0017 307 ASP B C   
6625  O O   . ASP B 307 ? 0.4138 0.4209 0.2517 0.0956  -0.0184 0.0023  307 ASP B O   
6626  C CB  . ASP B 307 ? 0.5263 0.5024 0.3141 0.0922  -0.0222 0.0009  307 ASP B CB  
6627  C CG  . ASP B 307 ? 0.5522 0.5289 0.3313 0.0878  -0.0075 0.0008  307 ASP B CG  
6628  O OD1 . ASP B 307 ? 0.4965 0.4869 0.2940 0.0878  0.0003  0.0012  307 ASP B OD1 
6629  O OD2 . ASP B 307 ? 0.5327 0.4962 0.2858 0.0836  -0.0038 0.0002  307 ASP B OD2 
6630  N N   . LYS B 308 ? 0.3882 0.4062 0.2372 0.1009  -0.0094 -0.0048 308 LYS B N   
6631  C CA  . LYS B 308 ? 0.3940 0.4275 0.2646 0.1016  -0.0073 -0.0032 308 LYS B CA  
6632  C C   . LYS B 308 ? 0.4076 0.4452 0.2786 0.0970  0.0000  -0.0005 308 LYS B C   
6633  O O   . LYS B 308 ? 0.4327 0.4772 0.3142 0.0949  -0.0021 0.0021  308 LYS B O   
6634  C CB  . LYS B 308 ? 0.3886 0.4315 0.2737 0.1062  -0.0036 -0.0060 308 LYS B CB  
6635  C CG  . LYS B 308 ? 0.4378 0.4968 0.3439 0.1069  -0.0027 -0.0039 308 LYS B CG  
6636  C CD  . LYS B 308 ? 0.4730 0.5379 0.3915 0.1122  -0.0004 -0.0056 308 LYS B CD  
6637  C CE  . LYS B 308 ? 0.5365 0.6166 0.4728 0.1130  0.0048  -0.0042 308 LYS B CE  
6638  N NZ  . LYS B 308 ? 0.5842 0.6735 0.5278 0.1088  0.0006  -0.0006 308 LYS B NZ  
6639  N N   . THR B 309 ? 0.4343 0.4672 0.2929 0.0944  0.0094  -0.0015 309 THR B N   
6640  C CA  . THR B 309 ? 0.4240 0.4616 0.2841 0.0888  0.0179  0.0006  309 THR B CA  
6641  C C   . THR B 309 ? 0.4060 0.4334 0.2557 0.0836  0.0121  0.0059  309 THR B C   
6642  O O   . THR B 309 ? 0.4849 0.5198 0.3460 0.0802  0.0134  0.0081  309 THR B O   
6643  C CB  . THR B 309 ? 0.4368 0.4697 0.2832 0.0859  0.0305  -0.0023 309 THR B CB  
6644  O OG1 . THR B 309 ? 0.5843 0.5971 0.4014 0.0830  0.0271  -0.0012 309 THR B OG1 
6645  C CG2 . THR B 309 ? 0.3598 0.4012 0.2180 0.0918  0.0369  -0.0084 309 THR B CG2 
6646  N N   . LEU B 310 ? 0.4736 0.4832 0.3019 0.0829  0.0051  0.0079  310 LEU B N   
6647  C CA  . LEU B 310 ? 0.4615 0.4590 0.2804 0.0789  -0.0016 0.0134  310 LEU B CA  
6648  C C   . LEU B 310 ? 0.4398 0.4443 0.2783 0.0820  -0.0103 0.0136  310 LEU B C   
6649  O O   . LEU B 310 ? 0.4184 0.4205 0.2605 0.0785  -0.0115 0.0165  310 LEU B O   
6650  C CB  . LEU B 310 ? 0.4093 0.3866 0.2027 0.0787  -0.0098 0.0158  310 LEU B CB  
6651  C CG  . LEU B 310 ? 0.4281 0.3921 0.1929 0.0734  -0.0025 0.0165  310 LEU B CG  
6652  C CD1 . LEU B 310 ? 0.4654 0.4094 0.2060 0.0735  -0.0155 0.0197  310 LEU B CD1 
6653  C CD2 . LEU B 310 ? 0.4578 0.4184 0.2148 0.0650  0.0079  0.0207  310 LEU B CD2 
6654  N N   . SER B 311 ? 0.4281 0.4394 0.2778 0.0878  -0.0162 0.0100  311 SER B N   
6655  C CA  . SER B 311 ? 0.3742 0.3937 0.2423 0.0900  -0.0223 0.0088  311 SER B CA  
6656  C C   . SER B 311 ? 0.4021 0.4362 0.2860 0.0872  -0.0160 0.0084  311 SER B C   
6657  O O   . SER B 311 ? 0.4218 0.4570 0.3133 0.0848  -0.0185 0.0089  311 SER B O   
6658  C CB  . SER B 311 ? 0.3576 0.3824 0.2336 0.0952  -0.0273 0.0049  311 SER B CB  
6659  O OG  . SER B 311 ? 0.3839 0.3963 0.2481 0.0972  -0.0352 0.0048  311 SER B OG  
6660  N N   . ASP B 312 ? 0.4051 0.4507 0.2953 0.0875  -0.0084 0.0071  312 ASP B N   
6661  C CA  . ASP B 312 ? 0.3745 0.4357 0.2813 0.0849  -0.0043 0.0069  312 ASP B CA  
6662  C C   . ASP B 312 ? 0.4148 0.4735 0.3187 0.0778  0.0008  0.0093  312 ASP B C   
6663  O O   . ASP B 312 ? 0.3932 0.4611 0.3094 0.0741  0.0009  0.0091  312 ASP B O   
6664  C CB  . ASP B 312 ? 0.3921 0.4663 0.3092 0.0880  0.0016  0.0051  312 ASP B CB  
6665  C CG  . ASP B 312 ? 0.4307 0.5090 0.3549 0.0940  -0.0038 0.0034  312 ASP B CG  
6666  O OD1 . ASP B 312 ? 0.4307 0.5046 0.3534 0.0947  -0.0111 0.0031  312 ASP B OD1 
6667  O OD2 . ASP B 312 ? 0.4475 0.5332 0.3797 0.0977  -0.0004 0.0023  312 ASP B OD2 
6668  N N   . LEU B 313 ? 0.4015 0.4472 0.2878 0.0748  0.0053  0.0116  313 LEU B N   
6669  C CA  . LEU B 313 ? 0.3972 0.4381 0.2786 0.0667  0.0109  0.0145  313 LEU B CA  
6670  C C   . LEU B 313 ? 0.3649 0.3968 0.2468 0.0642  0.0034  0.0165  313 LEU B C   
6671  O O   . LEU B 313 ? 0.3803 0.4166 0.2705 0.0582  0.0064  0.0169  313 LEU B O   
6672  C CB  . LEU B 313 ? 0.4074 0.4323 0.2646 0.0632  0.0165  0.0173  313 LEU B CB  
6673  C CG  . LEU B 313 ? 0.4189 0.4527 0.2761 0.0613  0.0297  0.0146  313 LEU B CG  
6674  C CD1 . LEU B 313 ? 0.4200 0.4348 0.2475 0.0584  0.0336  0.0163  313 LEU B CD1 
6675  C CD2 . LEU B 313 ? 0.4215 0.4671 0.2918 0.0538  0.0392  0.0148  313 LEU B CD2 
6676  N N   . ILE B 314 ? 0.3653 0.3846 0.2399 0.0688  -0.0063 0.0172  314 ILE B N   
6677  C CA  . ILE B 314 ? 0.3557 0.3666 0.2343 0.0680  -0.0133 0.0177  314 ILE B CA  
6678  C C   . ILE B 314 ? 0.3725 0.3997 0.2717 0.0689  -0.0146 0.0126  314 ILE B C   
6679  O O   . ILE B 314 ? 0.3532 0.3807 0.2596 0.0642  -0.0143 0.0116  314 ILE B O   
6680  C CB  . ILE B 314 ? 0.3479 0.3430 0.2168 0.0735  -0.0237 0.0191  314 ILE B CB  
6681  C CG1 . ILE B 314 ? 0.3754 0.3504 0.2200 0.0705  -0.0242 0.0256  314 ILE B CG1 
6682  C CG2 . ILE B 314 ? 0.3721 0.3627 0.2523 0.0751  -0.0309 0.0173  314 ILE B CG2 
6683  C CD1 . ILE B 314 ? 0.3906 0.3504 0.2245 0.0761  -0.0364 0.0277  314 ILE B CD1 
6684  N N   . GLY B 315 ? 0.3229 0.3627 0.2301 0.0739  -0.0159 0.0094  315 GLY B N   
6685  C CA  . GLY B 315 ? 0.2936 0.3462 0.2158 0.0743  -0.0181 0.0052  315 GLY B CA  
6686  C C   . GLY B 315 ? 0.3331 0.4012 0.2659 0.0692  -0.0132 0.0045  315 GLY B C   
6687  O O   . GLY B 315 ? 0.3826 0.4579 0.3242 0.0665  -0.0153 0.0014  315 GLY B O   
6688  N N   . PHE B 316 ? 0.2965 0.3703 0.2290 0.0673  -0.0067 0.0068  316 PHE B N   
6689  C CA  . PHE B 316 ? 0.3579 0.4503 0.3047 0.0639  -0.0032 0.0060  316 PHE B CA  
6690  C C   . PHE B 316 ? 0.3431 0.4371 0.2913 0.0567  0.0043  0.0076  316 PHE B C   
6691  O O   . PHE B 316 ? 0.3663 0.4736 0.3276 0.0512  0.0054  0.0063  316 PHE B O   
6692  C CB  . PHE B 316 ? 0.4230 0.5272 0.3765 0.0698  -0.0021 0.0060  316 PHE B CB  
6693  C CG  . PHE B 316 ? 0.5196 0.6257 0.4748 0.0751  -0.0088 0.0047  316 PHE B CG  
6694  C CD1 . PHE B 316 ? 0.5740 0.6810 0.5314 0.0726  -0.0142 0.0027  316 PHE B CD1 
6695  C CD2 . PHE B 316 ? 0.5299 0.6361 0.4840 0.0818  -0.0089 0.0050  316 PHE B CD2 
6696  C CE1 . PHE B 316 ? 0.5765 0.6850 0.5342 0.0760  -0.0189 0.0014  316 PHE B CE1 
6697  C CE2 . PHE B 316 ? 0.5063 0.6130 0.4612 0.0853  -0.0145 0.0042  316 PHE B CE2 
6698  C CZ  . PHE B 316 ? 0.5319 0.6402 0.4884 0.0821  -0.0192 0.0026  316 PHE B CZ  
6699  N N   . SER B 317 ? 0.3495 0.4305 0.2837 0.0556  0.0096  0.0102  317 SER B N   
6700  C CA  . SER B 317 ? 0.3907 0.4748 0.3261 0.0481  0.0192  0.0115  317 SER B CA  
6701  C C   . SER B 317 ? 0.4323 0.5001 0.3573 0.0398  0.0202  0.0142  317 SER B C   
6702  O O   . SER B 317 ? 0.4363 0.5114 0.3709 0.0315  0.0248  0.0137  317 SER B O   
6703  C CB  . SER B 317 ? 0.4006 0.4821 0.3262 0.0506  0.0271  0.0122  317 SER B CB  
6704  O OG  . SER B 317 ? 0.5251 0.6147 0.4561 0.0435  0.0388  0.0121  317 SER B OG  
6705  N N   . TYR B 318 ? 0.3636 0.4091 0.2704 0.0417  0.0153  0.0172  318 TYR B N   
6706  C CA  . TYR B 318 ? 0.3800 0.4061 0.2739 0.0339  0.0171  0.0215  318 TYR B CA  
6707  C C   . TYR B 318 ? 0.4197 0.4453 0.3247 0.0285  0.0140  0.0194  318 TYR B C   
6708  O O   . TYR B 318 ? 0.4015 0.4129 0.2992 0.0204  0.0169  0.0227  318 TYR B O   
6709  C CB  . TYR B 318 ? 0.4124 0.4140 0.2848 0.0382  0.0103  0.0260  318 TYR B CB  
6710  C CG  . TYR B 318 ? 0.4455 0.4413 0.2996 0.0395  0.0149  0.0287  318 TYR B CG  
6711  C CD1 . TYR B 318 ? 0.4610 0.4655 0.3135 0.0334  0.0278  0.0285  318 TYR B CD1 
6712  C CD2 . TYR B 318 ? 0.4764 0.4584 0.3152 0.0462  0.0066  0.0307  318 TYR B CD2 
6713  C CE1 . TYR B 318 ? 0.4437 0.4417 0.2774 0.0337  0.0335  0.0297  318 TYR B CE1 
6714  C CE2 . TYR B 318 ? 0.4611 0.4365 0.2805 0.0464  0.0106  0.0324  318 TYR B CE2 
6715  C CZ  . TYR B 318 ? 0.4610 0.4438 0.2768 0.0400  0.0246  0.0316  318 TYR B CZ  
6716  O OH  . TYR B 318 ? 0.5185 0.4938 0.3133 0.0395  0.0298  0.0320  318 TYR B OH  
6717  N N   . HIS B 319 ? 0.3926 0.4320 0.3134 0.0318  0.0085  0.0141  319 HIS B N   
6718  C CA  . HIS B 319 ? 0.4493 0.4889 0.3796 0.0254  0.0068  0.0107  319 HIS B CA  
6719  C C   . HIS B 319 ? 0.4236 0.4728 0.3617 0.0144  0.0148  0.0109  319 HIS B C   
6720  O O   . HIS B 319 ? 0.3608 0.4022 0.3008 0.0063  0.0152  0.0097  319 HIS B O   
6721  C CB  . HIS B 319 ? 0.4356 0.4906 0.3792 0.0293  0.0009  0.0045  319 HIS B CB  
6722  C CG  . HIS B 319 ? 0.4263 0.5067 0.3834 0.0286  0.0029  0.0028  319 HIS B CG  
6723  N ND1 . HIS B 319 ? 0.4719 0.5667 0.4420 0.0202  0.0047  0.0003  319 HIS B ND1 
6724  C CD2 . HIS B 319 ? 0.4335 0.5269 0.3944 0.0356  0.0025  0.0034  319 HIS B CD2 
6725  C CE1 . HIS B 319 ? 0.4145 0.5308 0.3966 0.0227  0.0044  -0.0001 319 HIS B CE1 
6726  N NE2 . HIS B 319 ? 0.4032 0.5182 0.3799 0.0322  0.0034  0.0018  319 HIS B NE2 
6727  N N   . ALA B 320 ? 0.3780 0.4442 0.3224 0.0139  0.0214  0.0115  320 ALA B N   
6728  C CA  . ALA B 320 ? 0.4024 0.4825 0.3589 0.0039  0.0297  0.0108  320 ALA B CA  
6729  C C   . ALA B 320 ? 0.4358 0.5018 0.3781 -0.0032 0.0400  0.0157  320 ALA B C   
6730  O O   . ALA B 320 ? 0.4474 0.5259 0.4000 -0.0118 0.0494  0.0150  320 ALA B O   
6731  C CB  . ALA B 320 ? 0.4226 0.5311 0.3982 0.0078  0.0314  0.0080  320 ALA B CB  
6732  N N   . TRP B 321 ? 0.4436 0.4842 0.3626 -0.0002 0.0381  0.0207  321 TRP B N   
6733  C CA  . TRP B 321 ? 0.5568 0.5790 0.4557 -0.0076 0.0466  0.0268  321 TRP B CA  
6734  C C   . TRP B 321 ? 0.5809 0.5753 0.4662 -0.0135 0.0424  0.0313  321 TRP B C   
6735  O O   . TRP B 321 ? 0.6154 0.5996 0.5014 -0.0077 0.0316  0.0302  321 TRP B O   
6736  C CB  . TRP B 321 ? 0.5489 0.5597 0.4267 -0.0002 0.0465  0.0303  321 TRP B CB  
6737  C CG  . TRP B 321 ? 0.5687 0.6008 0.4556 0.0060  0.0516  0.0263  321 TRP B CG  
6738  C CD1 . TRP B 321 ? 0.5257 0.5815 0.4354 0.0133  0.0479  0.0207  321 TRP B CD1 
6739  C CD2 . TRP B 321 ? 0.6090 0.6382 0.4809 0.0055  0.0613  0.0274  321 TRP B CD2 
6740  N NE1 . TRP B 321 ? 0.5248 0.5925 0.4370 0.0182  0.0543  0.0185  321 TRP B NE1 
6741  C CE2 . TRP B 321 ? 0.5740 0.6262 0.4635 0.0135  0.0633  0.0217  321 TRP B CE2 
6742  C CE3 . TRP B 321 ? 0.6204 0.6285 0.4640 -0.0014 0.0686  0.0327  321 TRP B CE3 
6743  C CZ2 . TRP B 321 ? 0.5718 0.6269 0.4536 0.0153  0.0731  0.0198  321 TRP B CZ2 
6744  C CZ3 . TRP B 321 ? 0.6047 0.6162 0.4381 -0.0007 0.0787  0.0308  321 TRP B CZ3 
6745  C CH2 . TRP B 321 ? 0.5833 0.6185 0.4369 0.0079  0.0813  0.0238  321 TRP B CH2 
6746  N N   . ASN B 322 ? 0.5902 0.5717 0.4634 -0.0252 0.0516  0.0362  322 ASN B N   
6747  C CA  . ASN B 322 ? 0.6757 0.6234 0.5274 -0.0298 0.0477  0.0435  322 ASN B CA  
6748  C C   . ASN B 322 ? 0.6253 0.5537 0.4567 -0.0185 0.0373  0.0483  322 ASN B C   
6749  O O   . ASN B 322 ? 0.5824 0.5190 0.4074 -0.0120 0.0384  0.0479  322 ASN B O   
6750  C CB  . ASN B 322 ? 0.8242 0.7617 0.6613 -0.0446 0.0613  0.0491  322 ASN B CB  
6751  C CG  . ASN B 322 ? 0.9616 0.8602 0.7693 -0.0495 0.0577  0.0594  322 ASN B CG  
6752  O OD1 . ASN B 322 ? 1.0168 0.8975 0.8003 -0.0439 0.0527  0.0657  322 ASN B OD1 
6753  N ND2 . ASN B 322 ? 1.0081 0.8927 0.8174 -0.0607 0.0598  0.0616  322 ASN B ND2 
6754  N N   . ALA B 323 ? 0.5343 0.5140 0.4079 0.0251  0.0773  0.0474  323 ALA B N   
6755  C CA  . ALA B 323 ? 0.5225 0.4864 0.3791 0.0373  0.0704  0.0505  323 ALA B CA  
6756  C C   . ALA B 323 ? 0.5431 0.5014 0.3790 0.0374  0.0766  0.0566  323 ALA B C   
6757  O O   . ALA B 323 ? 0.5289 0.4902 0.3581 0.0481  0.0729  0.0553  323 ALA B O   
6758  C CB  . ALA B 323 ? 0.4835 0.4195 0.3303 0.0391  0.0623  0.0537  323 ALA B CB  
6759  N N   . GLU B 324 ? 0.5503 0.4995 0.3747 0.0251  0.0859  0.0634  324 GLU B N   
6760  C CA  . GLU B 324 ? 0.6069 0.5495 0.4077 0.0247  0.0927  0.0699  324 GLU B CA  
6761  C C   . GLU B 324 ? 0.5650 0.5375 0.3748 0.0288  0.0993  0.0635  324 GLU B C   
6762  O O   . GLU B 324 ? 0.5255 0.4957 0.3189 0.0374  0.0985  0.0643  324 GLU B O   
6763  C CB  . GLU B 324 ? 0.7346 0.6616 0.5211 0.0085  0.1030  0.0791  324 GLU B CB  
6764  C CG  . GLU B 324 ? 0.9619 0.8549 0.7127 0.0103  0.1008  0.0901  324 GLU B CG  
6765  C CD  . GLU B 324 ? 1.1127 0.9775 0.8486 -0.0048 0.1052  0.1003  324 GLU B CD  
6766  O OE1 . GLU B 324 ? 1.1428 1.0172 0.8822 -0.0211 0.1190  0.1031  324 GLU B OE1 
6767  O OE2 . GLU B 324 ? 1.1574 0.9899 0.8782 -0.0005 0.0945  0.1053  324 GLU B OE2 
6768  N N   . ASP B 325 ? 0.5129 0.5131 0.3485 0.0236  0.1046  0.0563  325 ASP B N   
6769  C CA  . ASP B 325 ? 0.4814 0.5100 0.3273 0.0290  0.1098  0.0490  325 ASP B CA  
6770  C C   . ASP B 325 ? 0.5000 0.5322 0.3497 0.0451  0.0984  0.0429  325 ASP B C   
6771  O O   . ASP B 325 ? 0.5039 0.5467 0.3491 0.0529  0.0999  0.0392  325 ASP B O   
6772  C CB  . ASP B 325 ? 0.4941 0.5515 0.3688 0.0210  0.1160  0.0419  325 ASP B CB  
6773  C CG  . ASP B 325 ? 0.6646 0.7248 0.5386 0.0033  0.1298  0.0467  325 ASP B CG  
6774  O OD1 . ASP B 325 ? 0.7303 0.7710 0.5787 -0.0026 0.1364  0.0561  325 ASP B OD1 
6775  O OD2 . ASP B 325 ? 0.6865 0.7682 0.5858 -0.0051 0.1335  0.0411  325 ASP B OD2 
6776  N N   . ALA B 326 ? 0.5077 0.5311 0.3655 0.0498  0.0872  0.0416  326 ALA B N   
6777  C CA  . ALA B 326 ? 0.4439 0.4714 0.3070 0.0629  0.0771  0.0362  326 ALA B CA  
6778  C C   . ALA B 326 ? 0.4780 0.4884 0.3191 0.0714  0.0721  0.0397  326 ALA B C   
6779  O O   . ALA B 326 ? 0.5003 0.5183 0.3407 0.0804  0.0689  0.0351  326 ALA B O   
6780  C CB  . ALA B 326 ? 0.4154 0.4393 0.2921 0.0644  0.0682  0.0340  326 ALA B CB  
6781  N N   . VAL B 327 ? 0.4566 0.4432 0.2795 0.0692  0.0703  0.0472  327 VAL B N   
6782  C CA  . VAL B 327 ? 0.5314 0.5013 0.3328 0.0779  0.0639  0.0502  327 VAL B CA  
6783  C C   . VAL B 327 ? 0.5305 0.5057 0.3156 0.0788  0.0714  0.0506  327 VAL B C   
6784  O O   . VAL B 327 ? 0.5528 0.5271 0.3288 0.0887  0.0657  0.0476  327 VAL B O   
6785  C CB  . VAL B 327 ? 0.6113 0.5529 0.3956 0.0761  0.0593  0.0582  327 VAL B CB  
6786  C CG1 . VAL B 327 ? 0.6788 0.6119 0.4549 0.0624  0.0697  0.0651  327 VAL B CG1 
6787  C CG2 . VAL B 327 ? 0.5761 0.5001 0.3353 0.0851  0.0525  0.0616  327 VAL B CG2 
6788  N N   . ARG B 328 ? 0.5326 0.5145 0.3141 0.0682  0.0847  0.0536  328 ARG B N   
6789  C CA  . ARG B 328 ? 0.5633 0.5523 0.3284 0.0687  0.0939  0.0534  328 ARG B CA  
6790  C C   . ARG B 328 ? 0.5298 0.5429 0.3101 0.0778  0.0928  0.0425  328 ARG B C   
6791  O O   . ARG B 328 ? 0.5111 0.5237 0.2761 0.0862  0.0916  0.0398  328 ARG B O   
6792  C CB  . ARG B 328 ? 0.6303 0.6260 0.3928 0.0539  0.1099  0.0580  328 ARG B CB  
6793  C CG  . ARG B 328 ? 0.7660 0.7835 0.5246 0.0546  0.1220  0.0532  328 ARG B CG  
6794  C CD  . ARG B 328 ? 0.8778 0.9008 0.6297 0.0388  0.1396  0.0590  328 ARG B CD  
6795  N NE  . ARG B 328 ? 0.9470 0.9847 0.7276 0.0272  0.1439  0.0572  328 ARG B NE  
6796  C CZ  . ARG B 328 ? 1.0301 1.0511 0.8077 0.0135  0.1466  0.0658  328 ARG B CZ  
6797  N NH1 . ARG B 328 ? 1.0777 1.0655 0.8240 0.0102  0.1454  0.0774  328 ARG B NH1 
6798  N NH2 . ARG B 328 ? 1.0193 1.0556 0.8247 0.0035  0.1495  0.0624  328 ARG B NH2 
6799  N N   . ASP B 329 ? 0.4806 0.5136 0.2896 0.0768  0.0924  0.0359  329 ASP B N   
6800  C CA  . ASP B 329 ? 0.4856 0.5378 0.3093 0.0864  0.0891  0.0257  329 ASP B CA  
6801  C C   . ASP B 329 ? 0.5021 0.5416 0.3192 0.0983  0.0754  0.0236  329 ASP B C   
6802  O O   . ASP B 329 ? 0.5151 0.5582 0.3249 0.1069  0.0734  0.0182  329 ASP B O   
6803  C CB  . ASP B 329 ? 0.5037 0.5742 0.3570 0.0835  0.0883  0.0205  329 ASP B CB  
6804  C CG  . ASP B 329 ? 0.4915 0.5811 0.3599 0.0931  0.0851  0.0103  329 ASP B CG  
6805  O OD1 . ASP B 329 ? 0.4739 0.5838 0.3487 0.0925  0.0942  0.0049  329 ASP B OD1 
6806  O OD2 . ASP B 329 ? 0.5036 0.5880 0.3778 0.1011  0.0736  0.0074  329 ASP B OD2 
6807  N N   . PHE B 330 ? 0.4711 0.4965 0.2918 0.0987  0.0658  0.0270  330 PHE B N   
6808  C CA  . PHE B 330 ? 0.4475 0.4627 0.2651 0.1082  0.0531  0.0250  330 PHE B CA  
6809  C C   . PHE B 330 ? 0.4560 0.4576 0.2473 0.1137  0.0509  0.0269  330 PHE B C   
6810  O O   . PHE B 330 ? 0.4939 0.4956 0.2821 0.1225  0.0437  0.0213  330 PHE B O   
6811  C CB  . PHE B 330 ? 0.4343 0.4381 0.2590 0.1067  0.0455  0.0286  330 PHE B CB  
6812  C CG  . PHE B 330 ? 0.5436 0.5438 0.3743 0.1147  0.0335  0.0250  330 PHE B CG  
6813  C CD1 . PHE B 330 ? 0.5585 0.5707 0.4085 0.1166  0.0300  0.0196  330 PHE B CD1 
6814  C CD2 . PHE B 330 ? 0.4425 0.4273 0.2599 0.1198  0.0254  0.0272  330 PHE B CD2 
6815  C CE1 . PHE B 330 ? 0.5066 0.5156 0.3627 0.1219  0.0200  0.0169  330 PHE B CE1 
6816  C CE2 . PHE B 330 ? 0.4461 0.4303 0.2721 0.1258  0.0147  0.0233  330 PHE B CE2 
6817  C CZ  . PHE B 330 ? 0.4274 0.4238 0.2729 0.1261  0.0127  0.0184  330 PHE B CZ  
6818  N N   . ILE B 331 ? 0.5271 0.5146 0.2980 0.1086  0.0560  0.0348  331 ILE B N   
6819  C CA  . ILE B 331 ? 0.6055 0.5780 0.3475 0.1141  0.0533  0.0372  331 ILE B CA  
6820  C C   . ILE B 331 ? 0.5779 0.5638 0.3118 0.1177  0.0604  0.0312  331 ILE B C   
6821  O O   . ILE B 331 ? 0.5769 0.5586 0.2986 0.1272  0.0532  0.0265  331 ILE B O   
6822  C CB  . ILE B 331 ? 0.6029 0.5549 0.3217 0.1072  0.0577  0.0482  331 ILE B CB  
6823  C CG1 . ILE B 331 ? 0.6351 0.5715 0.3606 0.1069  0.0480  0.0525  331 ILE B CG1 
6824  C CG2 . ILE B 331 ? 0.5934 0.5294 0.2777 0.1130  0.0557  0.0512  331 ILE B CG2 
6825  C CD1 . ILE B 331 ? 0.6582 0.5879 0.3857 0.1184  0.0322  0.0484  331 ILE B CD1 
6826  N N   . GLY B 332 ? 0.5777 0.5814 0.3201 0.1107  0.0741  0.0299  332 GLY B N   
6827  C CA  . GLY B 332 ? 0.5860 0.6054 0.3225 0.1146  0.0823  0.0229  332 GLY B CA  
6828  C C   . GLY B 332 ? 0.5877 0.6165 0.3373 0.1263  0.0728  0.0117  332 GLY B C   
6829  O O   . GLY B 332 ? 0.5193 0.5506 0.2550 0.1341  0.0732  0.0054  332 GLY B O   
6830  N N   . ARG B 333 ? 0.4778 0.5105 0.2526 0.1274  0.0642  0.0089  333 ARG B N   
6831  C CA  . ARG B 333 ? 0.5936 0.6314 0.3797 0.1373  0.0545  -0.0006 333 ARG B CA  
6832  C C   . ARG B 333 ? 0.5853 0.6050 0.3562 0.1449  0.0415  -0.0014 333 ARG B C   
6833  O O   . ARG B 333 ? 0.5637 0.5841 0.3309 0.1537  0.0357  -0.0096 333 ARG B O   
6834  C CB  . ARG B 333 ? 0.5810 0.6262 0.3951 0.1354  0.0494  -0.0021 333 ARG B CB  
6835  C CG  . ARG B 333 ? 0.5047 0.5709 0.3369 0.1307  0.0593  -0.0047 333 ARG B CG  
6836  C CD  . ARG B 333 ? 0.4345 0.5030 0.2886 0.1268  0.0542  -0.0031 333 ARG B CD  
6837  N NE  . ARG B 333 ? 0.3942 0.4831 0.2674 0.1239  0.0605  -0.0071 333 ARG B NE  
6838  C CZ  . ARG B 333 ? 0.4704 0.5725 0.3557 0.1314  0.0581  -0.0158 333 ARG B CZ  
6839  N NH1 . ARG B 333 ? 0.4867 0.5821 0.3657 0.1414  0.0503  -0.0212 333 ARG B NH1 
6840  N NH2 . ARG B 333 ? 0.5151 0.6366 0.4190 0.1292  0.0628  -0.0197 333 ARG B NH2 
6841  N N   . LEU B 334 ? 0.4793 0.4829 0.2421 0.1421  0.0361  0.0063  334 LEU B N   
6842  C CA  . LEU B 334 ? 0.5285 0.5168 0.2782 0.1493  0.0230  0.0051  334 LEU B CA  
6843  C C   . LEU B 334 ? 0.5636 0.5452 0.2833 0.1547  0.0251  0.0034  334 LEU B C   
6844  O O   . LEU B 334 ? 0.5299 0.5043 0.2403 0.1631  0.0144  -0.0024 334 LEU B O   
6845  C CB  . LEU B 334 ? 0.4902 0.4641 0.2384 0.1462  0.0168  0.0131  334 LEU B CB  
6846  C CG  . LEU B 334 ? 0.4628 0.4415 0.2384 0.1425  0.0125  0.0137  334 LEU B CG  
6847  C CD1 . LEU B 334 ? 0.4675 0.4323 0.2394 0.1411  0.0069  0.0203  334 LEU B CD1 
6848  C CD2 . LEU B 334 ? 0.5061 0.4899 0.2980 0.1475  0.0025  0.0060  334 LEU B CD2 
6849  N N   . LYS B 335 ? 0.5815 0.5654 0.2852 0.1494  0.0390  0.0083  335 LYS B N   
6850  C CA  . LYS B 335 ? 0.6066 0.5855 0.2790 0.1540  0.0434  0.0069  335 LYS B CA  
6851  C C   . LYS B 335 ? 0.6558 0.6497 0.3327 0.1619  0.0448  -0.0057 335 LYS B C   
6852  O O   . LYS B 335 ? 0.6673 0.6542 0.3231 0.1707  0.0395  -0.0116 335 LYS B O   
6853  C CB  . LYS B 335 ? 0.6893 0.6681 0.3446 0.1443  0.0600  0.0160  335 LYS B CB  
6854  C CG  . LYS B 335 ? 0.8744 0.8395 0.4889 0.1470  0.0637  0.0193  335 LYS B CG  
6855  C CD  . LYS B 335 ? 0.9573 0.8961 0.5493 0.1431  0.0590  0.0322  335 LYS B CD  
6856  C CE  . LYS B 335 ? 1.0295 0.9495 0.5781 0.1491  0.0566  0.0348  335 LYS B CE  
6857  N NZ  . LYS B 335 ? 1.0431 0.9424 0.5625 0.1404  0.0639  0.0496  335 LYS B NZ  
6858  N N   . LYS B 336 ? 0.6452 0.6588 0.3488 0.1598  0.0509  -0.0108 336 LYS B N   
6859  C CA  . LYS B 336 ? 0.6764 0.7034 0.3861 0.1687  0.0511  -0.0235 336 LYS B CA  
6860  C C   . LYS B 336 ? 0.6418 0.6584 0.3577 0.1777  0.0332  -0.0309 336 LYS B C   
6861  O O   . LYS B 336 ? 0.7297 0.7457 0.4356 0.1874  0.0290  -0.0410 336 LYS B O   
6862  C CB  . LYS B 336 ? 0.7107 0.7606 0.4484 0.1651  0.0603  -0.0270 336 LYS B CB  
6863  C CG  . LYS B 336 ? 0.7979 0.8643 0.5299 0.1579  0.0797  -0.0245 336 LYS B CG  
6864  C CD  . LYS B 336 ? 0.8153 0.9081 0.5769 0.1568  0.0872  -0.0312 336 LYS B CD  
6865  C CE  . LYS B 336 ? 0.8680 0.9751 0.6312 0.1695  0.0879  -0.0459 336 LYS B CE  
6866  N NZ  . LYS B 336 ? 0.9151 1.0241 0.6489 0.1728  0.0984  -0.0489 336 LYS B NZ  
6867  N N   . ILE B 337 ? 0.5643 0.5730 0.2969 0.1743  0.0228  -0.0265 337 ILE B N   
6868  C CA  . ILE B 337 ? 0.5486 0.5463 0.2860 0.1805  0.0060  -0.0321 337 ILE B CA  
6869  C C   . ILE B 337 ? 0.6134 0.5958 0.3228 0.1862  -0.0017 -0.0332 337 ILE B C   
6870  O O   . ILE B 337 ? 0.6621 0.6389 0.3649 0.1946  -0.0115 -0.0427 337 ILE B O   
6871  C CB  . ILE B 337 ? 0.5285 0.5227 0.2881 0.1743  -0.0013 -0.0263 337 ILE B CB  
6872  C CG1 . ILE B 337 ? 0.5018 0.5092 0.2874 0.1707  0.0030  -0.0273 337 ILE B CG1 
6873  C CG2 . ILE B 337 ? 0.5646 0.5469 0.3262 0.1787  -0.0177 -0.0306 337 ILE B CG2 
6874  C CD1 . ILE B 337 ? 0.5306 0.5369 0.3347 0.1631  0.0005  -0.0201 337 ILE B CD1 
6875  N N   . HIS B 338 ? 0.6023 0.5760 0.2940 0.1822  0.0016  -0.0236 338 HIS B N   
6876  C CA  . HIS B 338 ? 0.6390 0.5961 0.3020 0.1879  -0.0071 -0.0233 338 HIS B CA  
6877  C C   . HIS B 338 ? 0.6627 0.6204 0.2998 0.1959  -0.0034 -0.0315 338 HIS B C   
6878  O O   . HIS B 338 ? 0.6369 0.5831 0.2567 0.2042  -0.0157 -0.0378 338 HIS B O   
6879  C CB  . HIS B 338 ? 0.6205 0.5672 0.2678 0.1818  -0.0023 -0.0104 338 HIS B CB  
6880  C CG  . HIS B 338 ? 0.6897 0.6175 0.3038 0.1878  -0.0111 -0.0083 338 HIS B CG  
6881  N ND1 . HIS B 338 ? 0.7556 0.6754 0.3349 0.1873  -0.0013 -0.0025 338 HIS B ND1 
6882  C CD2 . HIS B 338 ? 0.7215 0.6368 0.3315 0.1945  -0.0292 -0.0111 338 HIS B CD2 
6883  C CE1 . HIS B 338 ? 0.7709 0.6721 0.3234 0.1942  -0.0138 -0.0016 338 HIS B CE1 
6884  N NE2 . HIS B 338 ? 0.7726 0.6717 0.3445 0.1991  -0.0313 -0.0074 338 HIS B NE2 
6885  N N   . GLU B 339 ? 0.7110 0.6833 0.3456 0.1939  0.0133  -0.0328 339 GLU B N   
6886  C CA  . GLU B 339 ? 0.7520 0.7275 0.3614 0.2017  0.0193  -0.0412 339 GLU B CA  
6887  C C   . GLU B 339 ? 0.7489 0.7338 0.3730 0.2107  0.0144  -0.0563 339 GLU B C   
6888  O O   . GLU B 339 ? 0.7678 0.7528 0.3709 0.2198  0.0153  -0.0661 339 GLU B O   
6889  C CB  . GLU B 339 ? 0.8049 0.7937 0.4035 0.1950  0.0412  -0.0358 339 GLU B CB  
6890  C CG  . GLU B 339 ? 0.8654 0.8427 0.4479 0.1847  0.0477  -0.0201 339 GLU B CG  
6891  C CD  . GLU B 339 ? 0.9220 0.9156 0.5057 0.1743  0.0697  -0.0143 339 GLU B CD  
6892  O OE1 . GLU B 339 ? 0.9488 0.9314 0.5096 0.1662  0.0779  -0.0023 339 GLU B OE1 
6893  O OE2 . GLU B 339 ? 0.9202 0.9371 0.5283 0.1740  0.0783  -0.0219 339 GLU B OE2 
6894  N N   . SER B 340 ? 0.7163 0.7076 0.3741 0.2089  0.0090  -0.0587 340 SER B N   
6895  C CA  . SER B 340 ? 0.6338 0.6321 0.3057 0.2172  0.0047  -0.0722 340 SER B CA  
6896  C C   . SER B 340 ? 0.6189 0.6005 0.2866 0.2252  -0.0146 -0.0811 340 SER B C   
6897  O O   . SER B 340 ? 0.6342 0.6166 0.3063 0.2339  -0.0197 -0.0937 340 SER B O   
6898  C CB  . SER B 340 ? 0.6486 0.6579 0.3554 0.2119  0.0061  -0.0702 340 SER B CB  
6899  O OG  . SER B 340 ? 0.6908 0.6896 0.4118 0.2050  -0.0040 -0.0620 340 SER B OG  
6900  N N   . VAL B 341 ? 0.6549 0.6215 0.3155 0.2226  -0.0260 -0.0754 341 VAL B N   
6901  C CA  . VAL B 341 ? 0.7170 0.6687 0.3775 0.2278  -0.0455 -0.0831 341 VAL B CA  
6902  C C   . VAL B 341 ? 0.7552 0.6941 0.3842 0.2314  -0.0516 -0.0816 341 VAL B C   
6903  O O   . VAL B 341 ? 0.7225 0.6599 0.3387 0.2264  -0.0448 -0.0702 341 VAL B O   
6904  C CB  . VAL B 341 ? 0.6798 0.6281 0.3708 0.2202  -0.0560 -0.0784 341 VAL B CB  
6905  C CG1 . VAL B 341 ? 0.6971 0.6546 0.4153 0.2177  -0.0520 -0.0801 341 VAL B CG1 
6906  C CG2 . VAL B 341 ? 0.6442 0.5930 0.3385 0.2115  -0.0524 -0.0646 341 VAL B CG2 
6907  N N   . ASP B 342 ? 0.8293 0.7571 0.4449 0.2402  -0.0657 -0.0931 342 ASP B N   
6908  C CA  . ASP B 342 ? 0.9087 0.8228 0.4937 0.2451  -0.0749 -0.0931 342 ASP B CA  
6909  C C   . ASP B 342 ? 0.8475 0.7521 0.4467 0.2418  -0.0929 -0.0903 342 ASP B C   
6910  O O   . ASP B 342 ? 0.8394 0.7329 0.4159 0.2457  -0.1024 -0.0891 342 ASP B O   
6911  C CB  . ASP B 342 ? 1.0513 0.9585 0.6109 0.2573  -0.0814 -0.1083 342 ASP B CB  
6912  C CG  . ASP B 342 ? 1.1307 1.0315 0.7104 0.2609  -0.0986 -0.1212 342 ASP B CG  
6913  O OD1 . ASP B 342 ? 1.1142 1.0221 0.7217 0.2580  -0.0956 -0.1237 342 ASP B OD1 
6914  O OD2 . ASP B 342 ? 1.1758 1.0633 0.7427 0.2664  -0.1159 -0.1290 342 ASP B OD2 
6915  N N   . PHE B 343 ? 0.7518 0.6613 0.3874 0.2349  -0.0978 -0.0894 343 PHE B N   
6916  C CA  . PHE B 343 ? 0.6998 0.6052 0.3536 0.2303  -0.1119 -0.0862 343 PHE B CA  
6917  C C   . PHE B 343 ? 0.7044 0.6168 0.3711 0.2216  -0.1022 -0.0718 343 PHE B C   
6918  O O   . PHE B 343 ? 0.7080 0.6261 0.3668 0.2188  -0.0857 -0.0640 343 PHE B O   
6919  C CB  . PHE B 343 ? 0.6770 0.5823 0.3610 0.2273  -0.1235 -0.0944 343 PHE B CB  
6920  C CG  . PHE B 343 ? 0.6532 0.5678 0.3624 0.2208  -0.1126 -0.0915 343 PHE B CG  
6921  C CD1 . PHE B 343 ? 0.6776 0.5928 0.3828 0.2259  -0.1073 -0.0992 343 PHE B CD1 
6922  C CD2 . PHE B 343 ? 0.6250 0.5473 0.3611 0.2106  -0.1088 -0.0818 343 PHE B CD2 
6923  C CE1 . PHE B 343 ? 0.6779 0.6003 0.4051 0.2213  -0.0993 -0.0968 343 PHE B CE1 
6924  C CE2 . PHE B 343 ? 0.6448 0.5741 0.4012 0.2053  -0.1000 -0.0790 343 PHE B CE2 
6925  C CZ  . PHE B 343 ? 0.6571 0.5861 0.4092 0.2107  -0.0959 -0.0863 343 PHE B CZ  
6926  N N   . GLN B 344 ? 0.6740 0.5864 0.3610 0.2172  -0.1126 -0.0688 344 GLN B N   
6927  C CA  . GLN B 344 ? 0.6391 0.5572 0.3383 0.2102  -0.1048 -0.0566 344 GLN B CA  
6928  C C   . GLN B 344 ? 0.5919 0.5212 0.3258 0.2014  -0.0992 -0.0548 344 GLN B C   
6929  O O   . GLN B 344 ? 0.6145 0.5460 0.3723 0.1979  -0.1096 -0.0586 344 GLN B O   
6930  C CB  . GLN B 344 ? 0.5987 0.5115 0.2985 0.2120  -0.1184 -0.0545 344 GLN B CB  
6931  C CG  . GLN B 344 ? 0.6366 0.5351 0.2970 0.2217  -0.1252 -0.0553 344 GLN B CG  
6932  C CD  . GLN B 344 ? 0.6561 0.5486 0.3144 0.2246  -0.1373 -0.0511 344 GLN B CD  
6933  O OE1 . GLN B 344 ? 0.6787 0.5613 0.3124 0.2269  -0.1331 -0.0420 344 GLN B OE1 
6934  N NE2 . GLN B 344 ? 0.6450 0.5428 0.3291 0.2245  -0.1528 -0.0579 344 GLN B NE2 
6935  N N   . PRO B 345 ? 0.5452 0.4820 0.2829 0.1971  -0.0835 -0.0493 345 PRO B N   
6936  C CA  . PRO B 345 ? 0.5679 0.5139 0.3355 0.1895  -0.0791 -0.0475 345 PRO B CA  
6937  C C   . PRO B 345 ? 0.5973 0.5479 0.3837 0.1826  -0.0792 -0.0396 345 PRO B C   
6938  O O   . PRO B 345 ? 0.5497 0.4981 0.3259 0.1829  -0.0768 -0.0330 345 PRO B O   
6939  C CB  . PRO B 345 ? 0.5647 0.5178 0.3270 0.1886  -0.0630 -0.0446 345 PRO B CB  
6940  C CG  . PRO B 345 ? 0.5812 0.5312 0.3174 0.1906  -0.0555 -0.0387 345 PRO B CG  
6941  C CD  . PRO B 345 ? 0.5675 0.5052 0.2826 0.1980  -0.0687 -0.0434 345 PRO B CD  
6942  N N   . VAL B 346 ? 0.5874 0.5437 0.4007 0.1763  -0.0817 -0.0403 346 VAL B N   
6943  C CA  . VAL B 346 ? 0.5729 0.5365 0.4060 0.1694  -0.0794 -0.0336 346 VAL B CA  
6944  C C   . VAL B 346 ? 0.5355 0.5063 0.3798 0.1633  -0.0667 -0.0284 346 VAL B C   
6945  O O   . VAL B 346 ? 0.4389 0.4104 0.2918 0.1615  -0.0663 -0.0316 346 VAL B O   
6946  C CB  . VAL B 346 ? 0.6116 0.5779 0.4666 0.1658  -0.0912 -0.0379 346 VAL B CB  
6947  C CG1 . VAL B 346 ? 0.6422 0.6060 0.5072 0.1631  -0.0955 -0.0440 346 VAL B CG1 
6948  C CG2 . VAL B 346 ? 0.5417 0.5182 0.4180 0.1588  -0.0864 -0.0317 346 VAL B CG2 
6949  N N   . VAL B 347 ? 0.4318 0.4064 0.2747 0.1606  -0.0575 -0.0209 347 VAL B N   
6950  C CA  . VAL B 347 ? 0.4679 0.4494 0.3179 0.1557  -0.0457 -0.0165 347 VAL B CA  
6951  C C   . VAL B 347 ? 0.4229 0.4105 0.2922 0.1490  -0.0439 -0.0116 347 VAL B C   
6952  O O   . VAL B 347 ? 0.3982 0.3857 0.2656 0.1484  -0.0418 -0.0071 347 VAL B O   
6953  C CB  . VAL B 347 ? 0.4883 0.4695 0.3201 0.1572  -0.0352 -0.0125 347 VAL B CB  
6954  C CG1 . VAL B 347 ? 0.5029 0.4932 0.3442 0.1525  -0.0244 -0.0098 347 VAL B CG1 
6955  C CG2 . VAL B 347 ? 0.4471 0.4230 0.2574 0.1644  -0.0367 -0.0179 347 VAL B CG2 
6956  N N   . PHE B 348 ? 0.4739 0.4656 0.3602 0.1443  -0.0449 -0.0128 348 PHE B N   
6957  C CA  . PHE B 348 ? 0.4351 0.4337 0.3388 0.1377  -0.0422 -0.0088 348 PHE B CA  
6958  C C   . PHE B 348 ? 0.3677 0.3707 0.2719 0.1345  -0.0316 -0.0041 348 PHE B C   
6959  O O   . PHE B 348 ? 0.3980 0.4014 0.3018 0.1343  -0.0289 -0.0049 348 PHE B O   
6960  C CB  . PHE B 348 ? 0.4417 0.4414 0.3613 0.1328  -0.0475 -0.0113 348 PHE B CB  
6961  C CG  . PHE B 348 ? 0.4460 0.4485 0.3768 0.1316  -0.0559 -0.0144 348 PHE B CG  
6962  C CD1 . PHE B 348 ? 0.3840 0.3812 0.3073 0.1373  -0.0658 -0.0199 348 PHE B CD1 
6963  C CD2 . PHE B 348 ? 0.4372 0.4489 0.3863 0.1248  -0.0541 -0.0125 348 PHE B CD2 
6964  C CE1 . PHE B 348 ? 0.4065 0.4083 0.3426 0.1364  -0.0748 -0.0239 348 PHE B CE1 
6965  C CE2 . PHE B 348 ? 0.4351 0.4530 0.3980 0.1235  -0.0614 -0.0164 348 PHE B CE2 
6966  C CZ  . PHE B 348 ? 0.4413 0.4545 0.3986 0.1294  -0.0725 -0.0224 348 PHE B CZ  
6967  N N   . VAL B 349 ? 0.3871 0.3929 0.2919 0.1328  -0.0267 0.0002  349 VAL B N   
6968  C CA  . VAL B 349 ? 0.4061 0.4164 0.3134 0.1288  -0.0178 0.0041  349 VAL B CA  
6969  C C   . VAL B 349 ? 0.3712 0.3872 0.2937 0.1239  -0.0173 0.0055  349 VAL B C   
6970  O O   . VAL B 349 ? 0.3941 0.4112 0.3205 0.1243  -0.0188 0.0059  349 VAL B O   
6971  C CB  . VAL B 349 ? 0.3929 0.4003 0.2883 0.1298  -0.0123 0.0075  349 VAL B CB  
6972  C CG1 . VAL B 349 ? 0.4135 0.4261 0.3136 0.1248  -0.0040 0.0106  349 VAL B CG1 
6973  C CG2 . VAL B 349 ? 0.4018 0.4043 0.2799 0.1341  -0.0115 0.0063  349 VAL B CG2 
6974  N N   . VAL B 350 ? 0.3291 0.3482 0.2589 0.1199  -0.0155 0.0061  350 VAL B N   
6975  C CA  . VAL B 350 ? 0.3318 0.3560 0.2740 0.1145  -0.0145 0.0074  350 VAL B CA  
6976  C C   . VAL B 350 ? 0.3417 0.3686 0.2842 0.1110  -0.0085 0.0103  350 VAL B C   
6977  O O   . VAL B 350 ? 0.3284 0.3527 0.2676 0.1114  -0.0088 0.0104  350 VAL B O   
6978  C CB  . VAL B 350 ? 0.3253 0.3480 0.2751 0.1117  -0.0205 0.0055  350 VAL B CB  
6979  C CG1 . VAL B 350 ? 0.3202 0.3500 0.2826 0.1048  -0.0177 0.0072  350 VAL B CG1 
6980  C CG2 . VAL B 350 ? 0.3337 0.3536 0.2828 0.1158  -0.0282 0.0012  350 VAL B CG2 
6981  N N   . LEU B 351 ? 0.3289 0.3609 0.2757 0.1082  -0.0040 0.0119  351 LEU B N   
6982  C CA  . LEU B 351 ? 0.3693 0.4037 0.3152 0.1053  0.0009  0.0140  351 LEU B CA  
6983  C C   . LEU B 351 ? 0.3896 0.4296 0.3411 0.1026  0.0046  0.0142  351 LEU B C   
6984  O O   . LEU B 351 ? 0.3496 0.3919 0.3059 0.1043  0.0035  0.0124  351 LEU B O   
6985  C CB  . LEU B 351 ? 0.3401 0.3738 0.2791 0.1074  0.0038  0.0141  351 LEU B CB  
6986  C CG  . LEU B 351 ? 0.3087 0.3407 0.2437 0.1090  0.0060  0.0142  351 LEU B CG  
6987  C CD1 . LEU B 351 ? 0.3614 0.3949 0.2937 0.1069  0.0108  0.0149  351 LEU B CD1 
6988  C CD2 . LEU B 351 ? 0.3202 0.3469 0.2480 0.1132  0.0031  0.0135  351 LEU B CD2 
6989  N N   . ASN B 352 ? 0.3526 0.3948 0.3029 0.0994  0.0084  0.0157  352 ASN B N   
6990  C CA  . ASN B 352 ? 0.3083 0.3557 0.2615 0.0982  0.0126  0.0146  352 ASN B CA  
6991  C C   . ASN B 352 ? 0.3396 0.3845 0.2907 0.1019  0.0130  0.0129  352 ASN B C   
6992  O O   . ASN B 352 ? 0.3558 0.3958 0.3008 0.1032  0.0126  0.0137  352 ASN B O   
6993  C CB  . ASN B 352 ? 0.3761 0.4246 0.3246 0.0950  0.0158  0.0160  352 ASN B CB  
6994  C CG  . ASN B 352 ? 0.4015 0.4518 0.3508 0.0903  0.0171  0.0184  352 ASN B CG  
6995  O OD1 . ASN B 352 ? 0.4329 0.4778 0.3790 0.0887  0.0140  0.0212  352 ASN B OD1 
6996  N ND2 . ASN B 352 ? 0.3991 0.4567 0.3523 0.0880  0.0219  0.0171  352 ASN B ND2 
6997  N N   . GLY B 353 ? 0.3381 0.3859 0.2942 0.1038  0.0138  0.0103  353 GLY B N   
6998  C CA  . GLY B 353 ? 0.3899 0.4313 0.3420 0.1075  0.0131  0.0092  353 GLY B CA  
6999  C C   . GLY B 353 ? 0.3416 0.3827 0.2930 0.1074  0.0164  0.0069  353 GLY B C   
7000  O O   . GLY B 353 ? 0.3480 0.3827 0.2978 0.1112  0.0150  0.0051  353 GLY B O   
7001  N N   . GLU B 354 ? 0.3134 0.3597 0.2644 0.1037  0.0201  0.0065  354 GLU B N   
7002  C CA  . GLU B 354 ? 0.3929 0.4385 0.3418 0.1039  0.0227  0.0032  354 GLU B CA  
7003  C C   . GLU B 354 ? 0.3873 0.4312 0.3296 0.1000  0.0238  0.0041  354 GLU B C   
7004  O O   . GLU B 354 ? 0.3661 0.4070 0.3052 0.0998  0.0247  0.0008  354 GLU B O   
7005  C CB  . GLU B 354 ? 0.4073 0.4632 0.3620 0.1045  0.0262  -0.0005 354 GLU B CB  
7006  C CG  . GLU B 354 ? 0.3109 0.3735 0.2627 0.0992  0.0299  0.0017  354 GLU B CG  
7007  C CD  . GLU B 354 ? 0.3073 0.3744 0.2642 0.0962  0.0293  0.0054  354 GLU B CD  
7008  O OE1 . GLU B 354 ? 0.3130 0.3894 0.2752 0.0935  0.0333  0.0048  354 GLU B OE1 
7009  O OE2 . GLU B 354 ? 0.3330 0.3942 0.2883 0.0959  0.0252  0.0088  354 GLU B OE2 
7010  N N   . ASN B 355 ? 0.3382 0.3833 0.2787 0.0975  0.0227  0.0075  355 ASN B N   
7011  C CA  . ASN B 355 ? 0.3289 0.3750 0.2650 0.0947  0.0225  0.0077  355 ASN B CA  
7012  C C   . ASN B 355 ? 0.3417 0.3849 0.2774 0.0935  0.0212  0.0078  355 ASN B C   
7013  O O   . ASN B 355 ? 0.3239 0.3686 0.2582 0.0914  0.0205  0.0060  355 ASN B O   
7014  C CB  . ASN B 355 ? 0.3497 0.3987 0.2841 0.0934  0.0213  0.0109  355 ASN B CB  
7015  C CG  . ASN B 355 ? 0.3524 0.4050 0.2855 0.0920  0.0242  0.0112  355 ASN B CG  
7016  O OD1 . ASN B 355 ? 0.3520 0.4069 0.2835 0.0922  0.0273  0.0079  355 ASN B OD1 
7017  N ND2 . ASN B 355 ? 0.3754 0.4284 0.3092 0.0902  0.0237  0.0148  355 ASN B ND2 
7018  N N   . CYS B 356 ? 0.3074 0.3473 0.2441 0.0946  0.0209  0.0097  356 CYS B N   
7019  C CA  . CYS B 356 ? 0.3084 0.3484 0.2451 0.0924  0.0213  0.0101  356 CYS B CA  
7020  C C   . CYS B 356 ? 0.3160 0.3489 0.2510 0.0896  0.0230  0.0092  356 CYS B C   
7021  O O   . CYS B 356 ? 0.4452 0.4801 0.3819 0.0854  0.0243  0.0085  356 CYS B O   
7022  C CB  . CYS B 356 ? 0.3725 0.4124 0.3085 0.0945  0.0210  0.0125  356 CYS B CB  
7023  S SG  . CYS B 356 ? 0.3395 0.3704 0.2715 0.0979  0.0202  0.0143  356 CYS B SG  
7024  N N   . TRP B 357 ? 0.3408 0.3655 0.2733 0.0918  0.0227  0.0087  357 TRP B N   
7025  C CA  . TRP B 357 ? 0.3594 0.3723 0.2881 0.0898  0.0232  0.0086  357 TRP B CA  
7026  C C   . TRP B 357 ? 0.3859 0.3980 0.3159 0.0851  0.0234  0.0050  357 TRP B C   
7027  O O   . TRP B 357 ? 0.3470 0.3516 0.2755 0.0799  0.0244  0.0057  357 TRP B O   
7028  C CB  . TRP B 357 ? 0.3546 0.3585 0.2808 0.0954  0.0210  0.0079  357 TRP B CB  
7029  C CG  . TRP B 357 ? 0.3733 0.3804 0.3002 0.1000  0.0195  0.0101  357 TRP B CG  
7030  C CD1 . TRP B 357 ? 0.3692 0.3831 0.3016 0.1046  0.0180  0.0081  357 TRP B CD1 
7031  C CD2 . TRP B 357 ? 0.4367 0.4414 0.3590 0.1000  0.0193  0.0142  357 TRP B CD2 
7032  N NE1 . TRP B 357 ? 0.3694 0.3844 0.3018 0.1072  0.0157  0.0104  357 TRP B NE1 
7033  C CE2 . TRP B 357 ? 0.4109 0.4197 0.3359 0.1050  0.0163  0.0141  357 TRP B CE2 
7034  C CE3 . TRP B 357 ? 0.4364 0.4368 0.3525 0.0958  0.0219  0.0176  357 TRP B CE3 
7035  C CZ2 . TRP B 357 ? 0.4109 0.4180 0.3312 0.1070  0.0146  0.0167  357 TRP B CZ2 
7036  C CZ3 . TRP B 357 ? 0.4117 0.4114 0.3223 0.0979  0.0216  0.0204  357 TRP B CZ3 
7037  C CH2 . TRP B 357 ? 0.4326 0.4347 0.3445 0.1038  0.0174  0.0197  357 TRP B CH2 
7038  N N   . GLU B 358 ? 0.3518 0.3711 0.2838 0.0861  0.0224  0.0011  358 GLU B N   
7039  C CA  . GLU B 358 ? 0.3398 0.3578 0.2719 0.0824  0.0212  -0.0036 358 GLU B CA  
7040  C C   . GLU B 358 ? 0.3412 0.3651 0.2781 0.0759  0.0212  -0.0036 358 GLU B C   
7041  O O   . GLU B 358 ? 0.3472 0.3680 0.2856 0.0711  0.0198  -0.0074 358 GLU B O   
7042  C CB  . GLU B 358 ? 0.3376 0.3627 0.2678 0.0853  0.0202  -0.0073 358 GLU B CB  
7043  C CG  . GLU B 358 ? 0.4208 0.4567 0.3519 0.0864  0.0201  -0.0043 358 GLU B CG  
7044  C CD  . GLU B 358 ? 0.3681 0.4081 0.2940 0.0890  0.0205  -0.0058 358 GLU B CD  
7045  O OE1 . GLU B 358 ? 0.3718 0.4112 0.2973 0.0921  0.0230  -0.0061 358 GLU B OE1 
7046  O OE2 . GLU B 358 ? 0.4326 0.4770 0.3548 0.0880  0.0182  -0.0068 358 GLU B OE2 
7047  N N   . TYR B 359 ? 0.3562 0.3894 0.2968 0.0758  0.0224  -0.0003 359 TYR B N   
7048  C CA  . TYR B 359 ? 0.3823 0.4242 0.3302 0.0703  0.0233  -0.0011 359 TYR B CA  
7049  C C   . TYR B 359 ? 0.3932 0.4288 0.3406 0.0650  0.0279  0.0024  359 TYR B C   
7050  O O   . TYR B 359 ? 0.4046 0.4478 0.3592 0.0585  0.0302  0.0014  359 TYR B O   
7051  C CB  . TYR B 359 ? 0.4155 0.4711 0.3677 0.0739  0.0220  -0.0006 359 TYR B CB  
7052  C CG  . TYR B 359 ? 0.3756 0.4346 0.3253 0.0780  0.0173  -0.0028 359 TYR B CG  
7053  C CD1 . TYR B 359 ? 0.3928 0.4571 0.3451 0.0761  0.0132  -0.0076 359 TYR B CD1 
7054  C CD2 . TYR B 359 ? 0.3856 0.4414 0.3291 0.0831  0.0169  0.0000  359 TYR B CD2 
7055  C CE1 . TYR B 359 ? 0.3308 0.3957 0.2764 0.0799  0.0088  -0.0089 359 TYR B CE1 
7056  C CE2 . TYR B 359 ? 0.3157 0.3727 0.2539 0.0855  0.0137  -0.0008 359 TYR B CE2 
7057  C CZ  . TYR B 359 ? 0.3559 0.4166 0.2936 0.0843  0.0098  -0.0049 359 TYR B CZ  
7058  O OH  . TYR B 359 ? 0.3902 0.4502 0.3188 0.0868  0.0068  -0.0049 359 TYR B OH  
7059  N N   . TYR B 360 ? 0.3837 0.4061 0.3226 0.0676  0.0292  0.0064  360 TYR B N   
7060  C CA  . TYR B 360 ? 0.4407 0.4535 0.3747 0.0626  0.0332  0.0109  360 TYR B CA  
7061  C C   . TYR B 360 ? 0.4599 0.4583 0.3918 0.0558  0.0328  0.0099  360 TYR B C   
7062  O O   . TYR B 360 ? 0.4579 0.4486 0.3884 0.0585  0.0287  0.0061  360 TYR B O   
7063  C CB  . TYR B 360 ? 0.4299 0.4318 0.3535 0.0689  0.0328  0.0155  360 TYR B CB  
7064  C CG  . TYR B 360 ? 0.4272 0.4383 0.3500 0.0733  0.0341  0.0176  360 TYR B CG  
7065  C CD1 . TYR B 360 ? 0.3709 0.3933 0.2990 0.0790  0.0312  0.0152  360 TYR B CD1 
7066  C CD2 . TYR B 360 ? 0.4653 0.4713 0.3795 0.0719  0.0378  0.0223  360 TYR B CD2 
7067  C CE1 . TYR B 360 ? 0.3970 0.4252 0.3239 0.0833  0.0313  0.0165  360 TYR B CE1 
7068  C CE2 . TYR B 360 ? 0.4560 0.4692 0.3680 0.0768  0.0383  0.0231  360 TYR B CE2 
7069  C CZ  . TYR B 360 ? 0.4305 0.4544 0.3496 0.0826  0.0346  0.0198  360 TYR B CZ  
7070  O OH  . TYR B 360 ? 0.4161 0.4448 0.3327 0.0874  0.0342  0.0200  360 TYR B OH  
7071  N N   . GLU B 361 ? 0.4487 0.4806 0.4966 0.0941  0.0496  -0.0129 361 GLU B N   
7072  C CA  . GLU B 361 ? 0.4866 0.5127 0.5486 0.0841  0.0537  -0.0071 361 GLU B CA  
7073  C C   . GLU B 361 ? 0.4545 0.4606 0.5015 0.0840  0.0554  0.0036  361 GLU B C   
7074  O O   . GLU B 361 ? 0.4206 0.4263 0.4529 0.0867  0.0594  0.0116  361 GLU B O   
7075  C CB  . GLU B 361 ? 0.5800 0.6240 0.6581 0.0751  0.0649  -0.0018 361 GLU B CB  
7076  C CG  . GLU B 361 ? 0.6676 0.7111 0.7696 0.0636  0.0670  -0.0022 361 GLU B CG  
7077  C CD  . GLU B 361 ? 0.7479 0.7941 0.8655 0.0655  0.0554  -0.0173 361 GLU B CD  
7078  O OE1 . GLU B 361 ? 0.7790 0.8065 0.8959 0.0646  0.0485  -0.0196 361 GLU B OE1 
7079  O OE2 . GLU B 361 ? 0.7695 0.8359 0.8992 0.0689  0.0523  -0.0278 361 GLU B OE2 
7080  N N   . GLU B 362 ? 0.4473 0.4371 0.4982 0.0820  0.0513  0.0023  362 GLU B N   
7081  C CA  . GLU B 362 ? 0.4392 0.4106 0.4809 0.0822  0.0527  0.0113  362 GLU B CA  
7082  C C   . GLU B 362 ? 0.4237 0.3903 0.4458 0.0910  0.0507  0.0126  362 GLU B C   
7083  O O   . GLU B 362 ? 0.4652 0.4268 0.4795 0.0920  0.0536  0.0221  362 GLU B O   
7084  C CB  . GLU B 362 ? 0.4926 0.4635 0.5382 0.0747  0.0612  0.0245  362 GLU B CB  
7085  C CG  . GLU B 362 ? 0.6786 0.6379 0.7395 0.0657  0.0624  0.0267  362 GLU B CG  
7086  C CD  . GLU B 362 ? 0.8417 0.7980 0.9036 0.0574  0.0717  0.0409  362 GLU B CD  
7087  O OE1 . GLU B 362 ? 0.8958 0.8581 0.9742 0.0468  0.0773  0.0415  362 GLU B OE1 
7088  O OE2 . GLU B 362 ? 0.8730 0.8205 0.9187 0.0614  0.0734  0.0515  362 GLU B OE2 
7089  N N   . ASN B 363 ? 0.4695 0.4372 0.4835 0.0972  0.0452  0.0030  363 ASN B N   
7090  C CA  . ASN B 363 ? 0.4437 0.4052 0.4404 0.1041  0.0435  0.0029  363 ASN B CA  
7091  C C   . ASN B 363 ? 0.4328 0.4042 0.4215 0.1054  0.0471  0.0099  363 ASN B C   
7092  O O   . ASN B 363 ? 0.4140 0.3808 0.3917 0.1091  0.0465  0.0121  363 ASN B O   
7093  C CB  . ASN B 363 ? 0.3564 0.3018 0.3507 0.1052  0.0435  0.0053  363 ASN B CB  
7094  C CG  . ASN B 363 ? 0.3164 0.2550 0.2960 0.1111  0.0423  0.0020  363 ASN B CG  
7095  O OD1 . ASN B 363 ? 0.4191 0.3588 0.3886 0.1143  0.0396  -0.0042 363 ASN B OD1 
7096  N ND2 . ASN B 363 ? 0.3249 0.2563 0.3043 0.1124  0.0444  0.0063  363 ASN B ND2 
7097  N N   . GLY B 364 ? 0.4124 0.3978 0.4068 0.1021  0.0511  0.0126  364 GLY B N   
7098  C CA  . GLY B 364 ? 0.4207 0.4148 0.4047 0.1041  0.0543  0.0177  364 GLY B CA  
7099  C C   . GLY B 364 ? 0.4135 0.4030 0.3930 0.1019  0.0579  0.0299  364 GLY B C   
7100  O O   . GLY B 364 ? 0.4062 0.4012 0.3742 0.1040  0.0594  0.0343  364 GLY B O   
7101  N N   . ILE B 365 ? 0.3697 0.3477 0.3566 0.0985  0.0583  0.0350  365 ILE B N   
7102  C CA  . ILE B 365 ? 0.3848 0.3554 0.3661 0.0980  0.0598  0.0468  365 ILE B CA  
7103  C C   . ILE B 365 ? 0.4249 0.4025 0.4020 0.0934  0.0669  0.0554  365 ILE B C   
7104  O O   . ILE B 365 ? 0.4424 0.4198 0.4049 0.0963  0.0669  0.0627  365 ILE B O   
7105  C CB  . ILE B 365 ? 0.4047 0.3591 0.3948 0.0966  0.0581  0.0494  365 ILE B CB  
7106  C CG1 . ILE B 365 ? 0.3891 0.3375 0.3793 0.1024  0.0529  0.0411  365 ILE B CG1 
7107  C CG2 . ILE B 365 ? 0.3647 0.3096 0.3489 0.0969  0.0587  0.0622  365 ILE B CG2 
7108  C CD1 . ILE B 365 ? 0.3443 0.2800 0.3448 0.1010  0.0516  0.0365  365 ILE B CD1 
7109  N N   . PRO B 366 ? 0.4319 0.4163 0.4206 0.0860  0.0732  0.0548  366 PRO B N   
7110  C CA  . PRO B 366 ? 0.4393 0.4315 0.4224 0.0810  0.0825  0.0630  366 PRO B CA  
7111  C C   . PRO B 366 ? 0.5171 0.5230 0.4857 0.0867  0.0835  0.0602  366 PRO B C   
7112  O O   . PRO B 366 ? 0.4880 0.4934 0.4404 0.0868  0.0880  0.0692  366 PRO B O   
7113  C CB  . PRO B 366 ? 0.3869 0.3884 0.3911 0.0720  0.0888  0.0586  366 PRO B CB  
7114  C CG  . PRO B 366 ? 0.4265 0.4161 0.4442 0.0710  0.0819  0.0531  366 PRO B CG  
7115  C CD  . PRO B 366 ? 0.3940 0.3787 0.4019 0.0811  0.0725  0.0468  366 PRO B CD  
7116  N N   . PHE B 367 ? 0.4537 0.4692 0.4252 0.0920  0.0787  0.0479  367 PHE B N   
7117  C CA  . PHE B 367 ? 0.4447 0.4707 0.4019 0.0981  0.0787  0.0441  367 PHE B CA  
7118  C C   . PHE B 367 ? 0.4243 0.4405 0.3622 0.1036  0.0730  0.0495  367 PHE B C   
7119  O O   . PHE B 367 ? 0.4463 0.4650 0.3678 0.1051  0.0759  0.0551  367 PHE B O   
7120  C CB  . PHE B 367 ? 0.4161 0.4498 0.3790 0.1033  0.0732  0.0301  367 PHE B CB  
7121  C CG  . PHE B 367 ? 0.3988 0.4379 0.3453 0.1107  0.0709  0.0254  367 PHE B CG  
7122  C CD1 . PHE B 367 ? 0.4285 0.4822 0.3705 0.1116  0.0781  0.0242  367 PHE B CD1 
7123  C CD2 . PHE B 367 ? 0.3619 0.3911 0.2976 0.1163  0.0622  0.0220  367 PHE B CD2 
7124  C CE1 . PHE B 367 ? 0.3962 0.4531 0.3221 0.1190  0.0753  0.0189  367 PHE B CE1 
7125  C CE2 . PHE B 367 ? 0.3603 0.3923 0.2811 0.1223  0.0594  0.0171  367 PHE B CE2 
7126  C CZ  . PHE B 367 ? 0.3680 0.4130 0.2832 0.1241  0.0653  0.0154  367 PHE B CZ  
7127  N N   . LEU B 368 ? 0.3409 0.3468 0.2806 0.1068  0.0647  0.0469  368 LEU B N   
7128  C CA  . LEU B 368 ? 0.3923 0.3919 0.3187 0.1118  0.0584  0.0502  368 LEU B CA  
7129  C C   . LEU B 368 ? 0.4072 0.3992 0.3249 0.1108  0.0594  0.0632  368 LEU B C   
7130  O O   . LEU B 368 ? 0.4277 0.4192 0.3296 0.1149  0.0556  0.0668  368 LEU B O   
7131  C CB  . LEU B 368 ? 0.3690 0.3604 0.3030 0.1141  0.0517  0.0451  368 LEU B CB  
7132  C CG  . LEU B 368 ? 0.3858 0.3800 0.3176 0.1173  0.0483  0.0337  368 LEU B CG  
7133  C CD1 . LEU B 368 ? 0.4227 0.4080 0.3584 0.1188  0.0437  0.0305  368 LEU B CD1 
7134  C CD2 . LEU B 368 ? 0.3616 0.3626 0.2785 0.1208  0.0467  0.0317  368 LEU B CD2 
7135  N N   . GLU B 369 ? 0.4045 0.3886 0.3311 0.1056  0.0634  0.0703  369 GLU B N   
7136  C CA  . GLU B 369 ? 0.4579 0.4307 0.3736 0.1053  0.0636  0.0836  369 GLU B CA  
7137  C C   . GLU B 369 ? 0.5096 0.4876 0.4072 0.1034  0.0711  0.0901  369 GLU B C   
7138  O O   . GLU B 369 ? 0.4275 0.3989 0.3052 0.1073  0.0679  0.0981  369 GLU B O   
7139  C CB  . GLU B 369 ? 0.4863 0.4460 0.4148 0.1000  0.0661  0.0894  369 GLU B CB  
7140  C CG  . GLU B 369 ? 0.5224 0.4723 0.4615 0.1045  0.0579  0.0865  369 GLU B CG  
7141  C CD  . GLU B 369 ? 0.5480 0.4828 0.4984 0.0999  0.0598  0.0915  369 GLU B CD  
7142  O OE1 . GLU B 369 ? 0.5610 0.4943 0.5133 0.0917  0.0679  0.0963  369 GLU B OE1 
7143  O OE2 . GLU B 369 ? 0.5515 0.4762 0.5098 0.1043  0.0539  0.0900  369 GLU B OE2 
7144  N N   . LYS B 370 ? 0.4881 0.4787 0.3919 0.0981  0.0809  0.0858  370 LYS B N   
7145  C CA  . LYS B 370 ? 0.5571 0.5552 0.4441 0.0965  0.0903  0.0903  370 LYS B CA  
7146  C C   . LYS B 370 ? 0.5244 0.5301 0.3936 0.1049  0.0849  0.0839  370 LYS B C   
7147  O O   . LYS B 370 ? 0.5099 0.5135 0.3552 0.1072  0.0874  0.0903  370 LYS B O   
7148  C CB  . LYS B 370 ? 0.6100 0.6232 0.5138 0.0889  0.1024  0.0854  370 LYS B CB  
7149  C CG  . LYS B 370 ? 0.7213 0.7263 0.6410 0.0786  0.1090  0.0926  370 LYS B CG  
7150  C CD  . LYS B 370 ? 0.8088 0.8279 0.7370 0.0692  0.1248  0.0936  370 LYS B CD  
7151  C CE  . LYS B 370 ? 0.8813 0.8941 0.7831 0.0662  0.1357  0.1074  370 LYS B CE  
7152  N NZ  . LYS B 370 ? 0.9320 0.9504 0.8073 0.0761  0.1333  0.1052  370 LYS B NZ  
7153  N N   . LEU B 371 ? 0.4732 0.4854 0.3518 0.1095  0.0775  0.0715  371 LEU B N   
7154  C CA  . LEU B 371 ? 0.4616 0.4787 0.3248 0.1169  0.0715  0.0643  371 LEU B CA  
7155  C C   . LEU B 371 ? 0.5183 0.5242 0.3651 0.1216  0.0614  0.0704  371 LEU B C   
7156  O O   . LEU B 371 ? 0.5846 0.5907 0.4088 0.1256  0.0601  0.0723  371 LEU B O   
7157  C CB  . LEU B 371 ? 0.4489 0.4706 0.3252 0.1198  0.0655  0.0509  371 LEU B CB  
7158  C CG  . LEU B 371 ? 0.4307 0.4542 0.2938 0.1265  0.0581  0.0422  371 LEU B CG  
7159  C CD1 . LEU B 371 ? 0.4217 0.4553 0.2700 0.1293  0.0645  0.0389  371 LEU B CD1 
7160  C CD2 . LEU B 371 ? 0.4039 0.4263 0.2789 0.1282  0.0524  0.0311  371 LEU B CD2 
7161  N N   . TYR B 372 ? 0.4443 0.4409 0.3028 0.1219  0.0539  0.0729  372 TYR B N   
7162  C CA  . TYR B 372 ? 0.4128 0.4017 0.2615 0.1272  0.0426  0.0767  372 TYR B CA  
7163  C C   . TYR B 372 ? 0.4444 0.4236 0.2725 0.1281  0.0436  0.0902  372 TYR B C   
7164  O O   . TYR B 372 ? 0.4954 0.4716 0.3041 0.1338  0.0355  0.0923  372 TYR B O   
7165  C CB  . TYR B 372 ? 0.4521 0.4354 0.3211 0.1276  0.0361  0.0753  372 TYR B CB  
7166  C CG  . TYR B 372 ? 0.4195 0.4089 0.3028 0.1276  0.0338  0.0627  372 TYR B CG  
7167  C CD1 . TYR B 372 ? 0.3777 0.3747 0.2534 0.1289  0.0336  0.0535  372 TYR B CD1 
7168  C CD2 . TYR B 372 ? 0.4412 0.4265 0.3433 0.1268  0.0319  0.0601  372 TYR B CD2 
7169  C CE1 . TYR B 372 ? 0.3950 0.3933 0.2809 0.1287  0.0313  0.0430  372 TYR B CE1 
7170  C CE2 . TYR B 372 ? 0.4218 0.4099 0.3332 0.1264  0.0309  0.0498  372 TYR B CE2 
7171  C CZ  . TYR B 372 ? 0.4112 0.4047 0.3139 0.1270  0.0304  0.0419  372 TYR B CZ  
7172  O OH  . TYR B 372 ? 0.3606 0.3527 0.2698 0.1264  0.0294  0.0329  372 TYR B OH  
7173  N N   . SER B 373 ? 0.4522 0.4246 0.2833 0.1222  0.0529  0.0996  373 SER B N   
7174  C CA  . SER B 373 ? 0.4858 0.4453 0.2940 0.1219  0.0559  0.1140  373 SER B CA  
7175  C C   . SER B 373 ? 0.5372 0.5026 0.3184 0.1230  0.0623  0.1147  373 SER B C   
7176  O O   . SER B 373 ? 0.5623 0.5173 0.3153 0.1275  0.0583  0.1231  373 SER B O   
7177  C CB  . SER B 373 ? 0.4925 0.4434 0.3112 0.1132  0.0667  0.1229  373 SER B CB  
7178  O OG  . SER B 373 ? 0.7147 0.6501 0.5086 0.1118  0.0711  0.1380  373 SER B OG  
7179  N N   . THR B 374 ? 0.6065 0.5880 0.3947 0.1199  0.0720  0.1054  374 THR B N   
7180  C CA  . THR B 374 ? 0.6191 0.6076 0.3827 0.1219  0.0792  0.1040  374 THR B CA  
7181  C C   . THR B 374 ? 0.6046 0.5941 0.3517 0.1313  0.0657  0.0962  374 THR B C   
7182  O O   . THR B 374 ? 0.5518 0.5353 0.2679 0.1358  0.0642  0.1008  374 THR B O   
7183  C CB  . THR B 374 ? 0.6104 0.6174 0.3899 0.1172  0.0927  0.0948  374 THR B CB  
7184  O OG1 . THR B 374 ? 0.4953 0.5018 0.2929 0.1074  0.1040  0.1015  374 THR B OG1 
7185  C CG2 . THR B 374 ? 0.6595 0.6747 0.4140 0.1197  0.1024  0.0932  374 THR B CG2 
7186  N N   . LEU B 375 ? 0.4846 0.4799 0.2508 0.1340  0.0557  0.0846  375 LEU B N   
7187  C CA  . LEU B 375 ? 0.5186 0.5145 0.2727 0.1412  0.0426  0.0762  375 LEU B CA  
7188  C C   . LEU B 375 ? 0.5952 0.5786 0.3317 0.1463  0.0299  0.0844  375 LEU B C   
7189  O O   . LEU B 375 ? 0.6349 0.6166 0.3475 0.1522  0.0222  0.0817  375 LEU B O   
7190  C CB  . LEU B 375 ? 0.4793 0.4805 0.2585 0.1412  0.0352  0.0643  375 LEU B CB  
7191  C CG  . LEU B 375 ? 0.4591 0.4711 0.2470 0.1405  0.0416  0.0522  375 LEU B CG  
7192  C CD1 . LEU B 375 ? 0.4121 0.4243 0.2225 0.1396  0.0349  0.0428  375 LEU B CD1 
7193  C CD2 . LEU B 375 ? 0.4851 0.5005 0.2493 0.1459  0.0408  0.0453  375 LEU B CD2 
7194  N N   . GLU B 376 ? 0.6099 0.5840 0.3577 0.1449  0.0264  0.0938  376 GLU B N   
7195  C CA  . GLU B 376 ? 0.6203 0.5832 0.3557 0.1513  0.0118  0.1004  376 GLU B CA  
7196  C C   . GLU B 376 ? 0.6858 0.6360 0.3836 0.1542  0.0141  0.1126  376 GLU B C   
7197  O O   . GLU B 376 ? 0.7518 0.6909 0.4336 0.1611  0.0003  0.1183  376 GLU B O   
7198  C CB  . GLU B 376 ? 0.5973 0.5532 0.3565 0.1504  0.0074  0.1060  376 GLU B CB  
7199  C CG  . GLU B 376 ? 0.6582 0.5990 0.4096 0.1471  0.0158  0.1214  376 GLU B CG  
7200  C CD  . GLU B 376 ? 0.7596 0.6920 0.5338 0.1482  0.0093  0.1253  376 GLU B CD  
7201  O OE1 . GLU B 376 ? 0.7864 0.7074 0.5646 0.1432  0.0178  0.1346  376 GLU B OE1 
7202  O OE2 . GLU B 376 ? 0.8013 0.7386 0.5907 0.1538  -0.0040 0.1182  376 GLU B OE2 
7203  N N   . LYS B 377 ? 0.7019 0.6536 0.3849 0.1493  0.0311  0.1164  377 LYS B N   
7204  C CA  . LYS B 377 ? 0.7796 0.7185 0.4231 0.1510  0.0365  0.1282  377 LYS B CA  
7205  C C   . LYS B 377 ? 0.7829 0.7304 0.4012 0.1536  0.0429  0.1205  377 LYS B C   
7206  O O   . LYS B 377 ? 0.8462 0.7830 0.4271 0.1556  0.0482  0.1293  377 LYS B O   
7207  C CB  . LYS B 377 ? 0.7932 0.7233 0.4377 0.1420  0.0537  0.1420  377 LYS B CB  
7208  C CG  . LYS B 377 ? 0.7756 0.6923 0.4395 0.1404  0.0471  0.1507  377 LYS B CG  
7209  C CD  . LYS B 377 ? 0.7606 0.6710 0.4331 0.1293  0.0649  0.1608  377 LYS B CD  
7210  C CE  . LYS B 377 ? 0.7205 0.6132 0.4073 0.1288  0.0578  0.1700  377 LYS B CE  
7211  N NZ  . LYS B 377 ? 0.6930 0.5983 0.4219 0.1262  0.0551  0.1586  377 LYS B NZ  
7212  N N   . GLU B 378 ? 0.7569 0.7213 0.3921 0.1540  0.0427  0.1045  378 GLU B N   
7213  C CA  . GLU B 378 ? 0.8201 0.7915 0.4315 0.1583  0.0467  0.0954  378 GLU B CA  
7214  C C   . GLU B 378 ? 0.8442 0.8082 0.4330 0.1677  0.0265  0.0903  378 GLU B C   
7215  O O   . GLU B 378 ? 0.8488 0.8167 0.4582 0.1698  0.0114  0.0808  378 GLU B O   
7216  C CB  . GLU B 378 ? 0.8115 0.8012 0.4484 0.1561  0.0534  0.0802  378 GLU B CB  
7217  C CG  . GLU B 378 ? 0.8495 0.8502 0.5038 0.1481  0.0742  0.0825  378 GLU B CG  
7218  C CD  . GLU B 378 ? 0.9871 0.9887 0.6127 0.1470  0.0917  0.0886  378 GLU B CD  
7219  O OE1 . GLU B 378 ? 1.0316 1.0231 0.6467 0.1414  0.1010  0.1039  378 GLU B OE1 
7220  O OE2 . GLU B 378 ? 1.0244 1.0359 0.6369 0.1517  0.0970  0.0780  378 GLU B OE2 
7221  N N   . GLU B 379 ? 0.7763 0.7293 0.3234 0.1726  0.0266  0.0961  379 GLU B N   
7222  C CA  . GLU B 379 ? 0.8044 0.7497 0.3350 0.1792  0.0059  0.0900  379 GLU B CA  
7223  C C   . GLU B 379 ? 0.8009 0.7573 0.3375 0.1827  -0.0016 0.0710  379 GLU B C   
7224  O O   . GLU B 379 ? 0.8120 0.7668 0.3520 0.1873  -0.0216 0.0633  379 GLU B O   
7225  C CB  . GLU B 379 ? 0.8316 0.7634 0.3261 0.1788  0.0092  0.0972  379 GLU B CB  
7226  N N   . TRP B 380 ? 0.7986 0.7662 0.3387 0.1803  0.0139  0.0627  380 TRP B N   
7227  C CA  . TRP B 380 ? 0.7909 0.7655 0.3339 0.1837  0.0077  0.0447  380 TRP B CA  
7228  C C   . TRP B 380 ? 0.6755 0.6590 0.2490 0.1834  0.0029  0.0359  380 TRP B C   
7229  O O   . TRP B 380 ? 0.6985 0.6851 0.2751 0.1859  -0.0032 0.0210  380 TRP B O   
7230  C CB  . TRP B 380 ? 0.7589 0.7405 0.2919 0.1824  0.0254  0.0389  380 TRP B CB  
7231  C CG  . TRP B 380 ? 0.7532 0.7463 0.3038 0.1769  0.0463  0.0444  380 TRP B CG  
7232  C CD1 . TRP B 380 ? 0.7598 0.7510 0.3054 0.1711  0.0614  0.0594  380 TRP B CD1 
7233  C CD2 . TRP B 380 ? 0.7728 0.7805 0.3509 0.1762  0.0536  0.0347  380 TRP B CD2 
7234  N NE1 . TRP B 380 ? 0.7984 0.8044 0.3685 0.1665  0.0780  0.0589  380 TRP B NE1 
7235  C CE2 . TRP B 380 ? 0.7701 0.7867 0.3603 0.1701  0.0730  0.0436  380 TRP B CE2 
7236  C CE3 . TRP B 380 ? 0.7621 0.7746 0.3553 0.1798  0.0453  0.0192  380 TRP B CE3 
7237  C CZ2 . TRP B 380 ? 0.7313 0.7634 0.3512 0.1679  0.0827  0.0364  380 TRP B CZ2 
7238  C CZ3 . TRP B 380 ? 0.7165 0.7418 0.3349 0.1784  0.0553  0.0130  380 TRP B CZ3 
7239  C CH2 . TRP B 380 ? 0.7269 0.7627 0.3609 0.1723  0.0729  0.0211  380 TRP B CH2 
7240  N N   . ILE B 381 ? 0.6058 0.5920 0.2107 0.1768  0.0056  0.0434  381 ILE B N   
7241  C CA  . ILE B 381 ? 0.5770 0.5697 0.2193 0.1727  0.0009  0.0352  381 ILE B CA  
7242  C C   . ILE B 381 ? 0.6119 0.5994 0.2675 0.1726  -0.0163 0.0380  381 ILE B C   
7243  O O   . ILE B 381 ? 0.6618 0.6438 0.3171 0.1722  -0.0176 0.0506  381 ILE B O   
7244  C CB  . ILE B 381 ? 0.5815 0.5819 0.2509 0.1658  0.0164  0.0393  381 ILE B CB  
7245  C CG1 . ILE B 381 ? 0.6411 0.6502 0.3015 0.1662  0.0335  0.0357  381 ILE B CG1 
7246  C CG2 . ILE B 381 ? 0.5058 0.5100 0.2086 0.1622  0.0111  0.0307  381 ILE B CG2 
7247  C CD1 . ILE B 381 ? 0.6024 0.6212 0.2923 0.1598  0.0465  0.0367  381 ILE B CD1 
7248  N N   . GLU B 382 ? 0.5504 0.5393 0.2182 0.1730  -0.0295 0.0261  382 GLU B N   
7249  C CA  . GLU B 382 ? 0.6213 0.6100 0.3111 0.1716  -0.0440 0.0262  382 GLU B CA  
7250  C C   . GLU B 382 ? 0.5047 0.4991 0.2284 0.1651  -0.0411 0.0187  382 GLU B C   
7251  O O   . GLU B 382 ? 0.5036 0.4983 0.2285 0.1642  -0.0429 0.0068  382 GLU B O   
7252  C CB  . GLU B 382 ? 0.7087 0.6942 0.3841 0.1767  -0.0634 0.0186  382 GLU B CB  
7253  C CG  . GLU B 382 ? 0.8203 0.8064 0.5117 0.1780  -0.0788 0.0228  382 GLU B CG  
7254  C CD  . GLU B 382 ? 0.9029 0.8902 0.5937 0.1808  -0.0996 0.0113  382 GLU B CD  
7255  O OE1 . GLU B 382 ? 0.9098 0.8919 0.5715 0.1850  -0.1049 0.0041  382 GLU B OE1 
7256  O OE2 . GLU B 382 ? 0.9034 0.8973 0.6237 0.1787  -0.1105 0.0087  382 GLU B OE2 
7257  N N   . THR B 383 ? 0.5448 0.5414 0.2938 0.1610  -0.0370 0.0256  383 THR B N   
7258  C CA  . THR B 383 ? 0.4558 0.4559 0.2344 0.1551  -0.0350 0.0189  383 THR B CA  
7259  C C   . THR B 383 ? 0.4733 0.4756 0.2675 0.1541  -0.0497 0.0125  383 THR B C   
7260  O O   . THR B 383 ? 0.4709 0.4741 0.2640 0.1579  -0.0610 0.0164  383 THR B O   
7261  C CB  . THR B 383 ? 0.4868 0.4879 0.2856 0.1513  -0.0248 0.0273  383 THR B CB  
7262  O OG1 . THR B 383 ? 0.4600 0.4595 0.2622 0.1537  -0.0304 0.0372  383 THR B OG1 
7263  C CG2 . THR B 383 ? 0.5416 0.5430 0.3309 0.1505  -0.0100 0.0313  383 THR B CG2 
7264  N N   . LEU B 384 ? 0.4614 0.4642 0.2703 0.1491  -0.0500 0.0023  384 LEU B N   
7265  C CA  . LEU B 384 ? 0.4653 0.4714 0.2914 0.1461  -0.0624 -0.0054 384 LEU B CA  
7266  C C   . LEU B 384 ? 0.4154 0.4245 0.2725 0.1388  -0.0563 -0.0070 384 LEU B C   
7267  O O   . LEU B 384 ? 0.4016 0.4064 0.2617 0.1356  -0.0441 -0.0065 384 LEU B O   
7268  C CB  . LEU B 384 ? 0.4520 0.4532 0.2647 0.1454  -0.0695 -0.0176 384 LEU B CB  
7269  C CG  . LEU B 384 ? 0.5078 0.5044 0.2856 0.1529  -0.0738 -0.0186 384 LEU B CG  
7270  C CD1 . LEU B 384 ? 0.4911 0.4813 0.2584 0.1521  -0.0816 -0.0324 384 LEU B CD1 
7271  C CD2 . LEU B 384 ? 0.4973 0.4968 0.2653 0.1591  -0.0854 -0.0121 384 LEU B CD2 
7272  N N   . THR B 385 ? 0.4550 0.4718 0.3351 0.1366  -0.0651 -0.0097 385 THR B N   
7273  C CA  . THR B 385 ? 0.4805 0.4997 0.3877 0.1283  -0.0595 -0.0147 385 THR B CA  
7274  C C   . THR B 385 ? 0.4475 0.4592 0.3493 0.1221  -0.0604 -0.0253 385 THR B C   
7275  O O   . THR B 385 ? 0.4374 0.4445 0.3187 0.1249  -0.0684 -0.0303 385 THR B O   
7276  C CB  . THR B 385 ? 0.4965 0.5288 0.4332 0.1273  -0.0677 -0.0161 385 THR B CB  
7277  O OG1 . THR B 385 ? 0.4741 0.5115 0.4128 0.1266  -0.0830 -0.0248 385 THR B OG1 
7278  C CG2 . THR B 385 ? 0.4896 0.5262 0.4270 0.1358  -0.0707 -0.0057 385 THR B CG2 
7279  N N   . LEU B 386 ? 0.4000 0.4083 0.3179 0.1139  -0.0516 -0.0286 386 LEU B N   
7280  C CA  . LEU B 386 ? 0.4260 0.4238 0.3394 0.1070  -0.0523 -0.0380 386 LEU B CA  
7281  C C   . LEU B 386 ? 0.4277 0.4315 0.3497 0.1040  -0.0671 -0.0466 386 LEU B C   
7282  O O   . LEU B 386 ? 0.4258 0.4195 0.3331 0.1022  -0.0731 -0.0545 386 LEU B O   
7283  C CB  . LEU B 386 ? 0.3865 0.3783 0.3155 0.0979  -0.0402 -0.0389 386 LEU B CB  
7284  C CG  . LEU B 386 ? 0.3754 0.3587 0.2959 0.1000  -0.0267 -0.0325 386 LEU B CG  
7285  C CD1 . LEU B 386 ? 0.3711 0.3468 0.3045 0.0907  -0.0159 -0.0341 386 LEU B CD1 
7286  C CD2 . LEU B 386 ? 0.3827 0.3532 0.2748 0.1054  -0.0259 -0.0334 386 LEU B CD2 
7287  N N   . GLU B 387 ? 0.4071 0.4273 0.3543 0.1037  -0.0738 -0.0461 387 GLU B N   
7288  C CA  . GLU B 387 ? 0.4795 0.5083 0.4393 0.1009  -0.0897 -0.0553 387 GLU B CA  
7289  C C   . GLU B 387 ? 0.4512 0.4767 0.3824 0.1102  -0.1041 -0.0568 387 GLU B C   
7290  O O   . GLU B 387 ? 0.4576 0.4800 0.3838 0.1076  -0.1161 -0.0669 387 GLU B O   
7291  C CB  . GLU B 387 ? 0.5762 0.6257 0.5717 0.1004  -0.0945 -0.0549 387 GLU B CB  
7292  C CG  . GLU B 387 ? 0.7212 0.7831 0.7281 0.1018  -0.1152 -0.0634 387 GLU B CG  
7293  C CD  . GLU B 387 ? 0.8367 0.9167 0.8884 0.0922  -0.1172 -0.0715 387 GLU B CD  
7294  O OE1 . GLU B 387 ? 0.8893 0.9718 0.9515 0.0844  -0.1272 -0.0828 387 GLU B OE1 
7295  O OE2 . GLU B 387 ? 0.8682 0.9605 0.9458 0.0922  -0.1086 -0.0672 387 GLU B OE2 
7296  N N   . GLU B 388 ? 0.4545 0.4796 0.3655 0.1207  -0.1028 -0.0471 388 GLU B N   
7297  C CA  . GLU B 388 ? 0.4897 0.5098 0.3687 0.1297  -0.1143 -0.0478 388 GLU B CA  
7298  C C   . GLU B 388 ? 0.5087 0.5135 0.3600 0.1295  -0.1099 -0.0534 388 GLU B C   
7299  O O   . GLU B 388 ? 0.5636 0.5632 0.3936 0.1334  -0.1216 -0.0605 388 GLU B O   
7300  C CB  . GLU B 388 ? 0.4671 0.4887 0.3304 0.1397  -0.1115 -0.0348 388 GLU B CB  
7301  C CG  . GLU B 388 ? 0.4667 0.5008 0.3509 0.1435  -0.1212 -0.0301 388 GLU B CG  
7302  C CD  . GLU B 388 ? 0.5833 0.6154 0.4590 0.1502  -0.1131 -0.0157 388 GLU B CD  
7303  O OE1 . GLU B 388 ? 0.5254 0.5487 0.3833 0.1502  -0.0986 -0.0097 388 GLU B OE1 
7304  O OE2 . GLU B 388 ? 0.6057 0.6447 0.4939 0.1555  -0.1218 -0.0109 388 GLU B OE2 
7305  N N   . ALA B 389 ? 0.4704 0.4672 0.3210 0.1259  -0.0940 -0.0509 389 ALA B N   
7306  C CA  . ALA B 389 ? 0.4849 0.4667 0.3126 0.1265  -0.0899 -0.0571 389 ALA B CA  
7307  C C   . ALA B 389 ? 0.4880 0.4615 0.3222 0.1185  -0.0982 -0.0697 389 ALA B C   
7308  O O   . ALA B 389 ? 0.5663 0.5284 0.3782 0.1213  -0.1043 -0.0781 389 ALA B O   
7309  C CB  . ALA B 389 ? 0.4519 0.4277 0.2803 0.1252  -0.0729 -0.0517 389 ALA B CB  
7310  N N   . MET B 390 ? 0.5379 0.5169 0.4031 0.1081  -0.0981 -0.0716 390 MET B N   
7311  C CA  . MET B 390 ? 0.6465 0.6180 0.5218 0.0981  -0.1053 -0.0832 390 MET B CA  
7312  C C   . MET B 390 ? 0.6204 0.5968 0.4906 0.1009  -0.1251 -0.0921 390 MET B C   
7313  O O   . MET B 390 ? 0.6313 0.5942 0.4875 0.0988  -0.1331 -0.1027 390 MET B O   
7314  C CB  . MET B 390 ? 0.7435 0.7232 0.6556 0.0858  -0.0988 -0.0826 390 MET B CB  
7315  C CG  . MET B 390 ? 0.8896 0.8656 0.8191 0.0731  -0.1063 -0.0942 390 MET B CG  
7316  S SD  . MET B 390 ? 1.0013 0.9456 0.9109 0.0654  -0.0986 -0.0998 390 MET B SD  
7317  C CE  . MET B 390 ? 1.0524 0.9845 0.9303 0.0735  -0.1162 -0.1106 390 MET B CE  
7318  N N   . ARG B 391 ? 0.5862 0.5801 0.4657 0.1064  -0.1344 -0.0883 391 ARG B N   
7319  C CA  . ARG B 391 ? 0.6518 0.6524 0.5311 0.1088  -0.1556 -0.0972 391 ARG B CA  
7320  C C   . ARG B 391 ? 0.7095 0.7030 0.5475 0.1223  -0.1644 -0.0969 391 ARG B C   
7321  O O   . ARG B 391 ? 0.6952 0.6906 0.5258 0.1255  -0.1834 -0.1053 391 ARG B O   
7322  C CB  . ARG B 391 ? 0.7039 0.7270 0.6164 0.1086  -0.1636 -0.0944 391 ARG B CB  
7323  C CG  . ARG B 391 ? 0.7460 0.7798 0.7030 0.0942  -0.1597 -0.0997 391 ARG B CG  
7324  C CD  . ARG B 391 ? 0.8128 0.8673 0.8010 0.0962  -0.1560 -0.0920 391 ARG B CD  
7325  N NE  . ARG B 391 ? 0.9269 1.0024 0.9489 0.0942  -0.1732 -0.1004 391 ARG B NE  
7326  C CZ  . ARG B 391 ? 0.9961 1.0911 1.0420 0.1006  -0.1780 -0.0959 391 ARG B CZ  
7327  N NH1 . ARG B 391 ? 0.9944 1.0884 1.0324 0.1086  -0.1665 -0.0826 391 ARG B NH1 
7328  N NH2 . ARG B 391 ? 1.0331 1.1485 1.1119 0.0993  -0.1952 -0.1053 391 ARG B NH2 
7329  N N   . LYS B 392 ? 0.6958 0.6816 0.5070 0.1299  -0.1511 -0.0882 392 LYS B N   
7330  C CA  . LYS B 392 ? 0.6970 0.6780 0.4691 0.1425  -0.1560 -0.0862 392 LYS B CA  
7331  C C   . LYS B 392 ? 0.6959 0.6641 0.4434 0.1446  -0.1687 -0.1006 392 LYS B C   
7332  O O   . LYS B 392 ? 0.6980 0.6533 0.4429 0.1397  -0.1642 -0.1089 392 LYS B O   
7333  C CB  . LYS B 392 ? 0.6654 0.6416 0.4190 0.1477  -0.1366 -0.0760 392 LYS B CB  
7334  C CG  . LYS B 392 ? 0.6693 0.6443 0.3873 0.1596  -0.1368 -0.0698 392 LYS B CG  
7335  C CD  . LYS B 392 ? 0.7223 0.7074 0.4454 0.1637  -0.1449 -0.0600 392 LYS B CD  
7336  C CE  . LYS B 392 ? 0.7007 0.6920 0.4377 0.1630  -0.1294 -0.0452 392 LYS B CE  
7337  N NZ  . LYS B 392 ? 0.7728 0.7676 0.4998 0.1705  -0.1367 -0.0345 392 LYS B NZ  
7338  N N   . GLU B 393 ? 0.7632 0.7329 0.4903 0.1527  -0.1855 -0.1039 393 GLU B N   
7339  C CA  . GLU B 393 ? 0.8323 0.7894 0.5355 0.1550  -0.1998 -0.1190 393 GLU B CA  
7340  C C   . GLU B 393 ? 0.8300 0.7737 0.4881 0.1657  -0.1914 -0.1196 393 GLU B C   
7341  O O   . GLU B 393 ? 0.8602 0.7896 0.5043 0.1653  -0.1926 -0.1318 393 GLU B O   
7342  C CB  . GLU B 393 ? 0.8958 0.8599 0.5973 0.1590  -0.2244 -0.1246 393 GLU B CB  
7343  C CG  . GLU B 393 ? 0.9281 0.9088 0.6785 0.1488  -0.2342 -0.1269 393 GLU B CG  
7344  C CD  . GLU B 393 ? 1.0104 0.9907 0.7717 0.1434  -0.2574 -0.1447 393 GLU B CD  
7345  O OE1 . GLU B 393 ? 1.0488 1.0333 0.8478 0.1293  -0.2569 -0.1521 393 GLU B OE1 
7346  O OE2 . GLU B 393 ? 1.0213 0.9965 0.7529 0.1529  -0.2758 -0.1515 393 GLU B OE2 
7347  N N   . ASP B 394 ? 0.8297 0.7772 0.4656 0.1749  -0.1820 -0.1070 394 ASP B N   
7348  C CA  . ASP B 394 ? 0.8488 0.7870 0.4449 0.1844  -0.1726 -0.1070 394 ASP B CA  
7349  C C   . ASP B 394 ? 0.8269 0.7621 0.4225 0.1842  -0.1513 -0.1048 394 ASP B C   
7350  O O   . ASP B 394 ? 0.8140 0.7529 0.3985 0.1885  -0.1341 -0.0946 394 ASP B O   
7351  C CB  . ASP B 394 ? 0.9690 0.9120 0.5475 0.1908  -0.1691 -0.0930 394 ASP B CB  
7352  C CG  . ASP B 394 ? 0.9969 0.9514 0.5919 0.1906  -0.1663 -0.0786 394 ASP B CG  
7353  O OD1 . ASP B 394 ? 1.0179 0.9803 0.6511 0.1823  -0.1703 -0.0796 394 ASP B OD1 
7354  O OD2 . ASP B 394 ? 0.9816 0.9372 0.5622 0.1947  -0.1555 -0.0647 394 ASP B OD2 
7355  N N   . VAL B 395 ? 0.7356 0.6640 0.3500 0.1770  -0.1511 -0.1140 395 VAL B N   
7356  C CA  . VAL B 395 ? 0.6773 0.6019 0.2986 0.1756  -0.1333 -0.1125 395 VAL B CA  
7357  C C   . VAL B 395 ? 0.7044 0.6110 0.3143 0.1761  -0.1387 -0.1289 395 VAL B C   
7358  O O   . VAL B 395 ? 0.7030 0.6012 0.3110 0.1731  -0.1555 -0.1403 395 VAL B O   
7359  C CB  . VAL B 395 ? 0.6371 0.5689 0.2979 0.1647  -0.1258 -0.1038 395 VAL B CB  
7360  C CG1 . VAL B 395 ? 0.6167 0.5393 0.2992 0.1539  -0.1349 -0.1137 395 VAL B CG1 
7361  C CG2 . VAL B 395 ? 0.6695 0.6027 0.3334 0.1663  -0.1066 -0.0966 395 VAL B CG2 
7362  N N   . LYS B 396 ? 0.6957 0.5967 0.3025 0.1792  -0.1241 -0.1293 396 LYS B N   
7363  C CA  . LYS B 396 ? 0.7686 0.6516 0.3719 0.1786  -0.1272 -0.1418 396 LYS B CA  
7364  C C   . LYS B 396 ? 0.7403 0.6100 0.3595 0.1707  -0.1290 -0.1467 396 LYS B C   
7365  O O   . LYS B 396 ? 0.7575 0.6350 0.3981 0.1658  -0.1176 -0.1356 396 LYS B O   
7366  C CB  . LYS B 396 ? 0.8581 0.7413 0.4513 0.1868  -0.1126 -0.1409 396 LYS B CB  
7367  C CG  . LYS B 396 ? 0.9776 0.8424 0.5633 0.1884  -0.1184 -0.1539 396 LYS B CG  
7368  C CD  . LYS B 396 ? 1.0568 0.9258 0.6293 0.1982  -0.1075 -0.1546 396 LYS B CD  
7369  C CE  . LYS B 396 ? 1.1173 0.9797 0.6694 0.2019  -0.1173 -0.1635 396 LYS B CE  
7370  N NZ  . LYS B 396 ? 1.1270 1.0024 0.6662 0.2036  -0.1184 -0.1566 396 LYS B NZ  
7371  N N   . THR B 397 ? 0.8112 0.5251 0.2911 0.0418  -0.0708 -0.0841 397 THR B N   
7372  C CA  . THR B 397 ? 0.7893 0.5168 0.3120 0.0437  -0.0764 -0.0891 397 THR B CA  
7373  C C   . THR B 397 ? 0.7798 0.5043 0.3013 0.0497  -0.0629 -0.1012 397 THR B C   
7374  O O   . THR B 397 ? 0.7701 0.4779 0.2571 0.0516  -0.0549 -0.1078 397 THR B O   
7375  C CB  . THR B 397 ? 0.7944 0.5138 0.3236 0.0394  -0.1031 -0.0906 397 THR B CB  
7376  O OG1 . THR B 397 ? 0.8957 0.5940 0.3920 0.0369  -0.1107 -0.0977 397 THR B OG1 
7377  C CG2 . THR B 397 ? 0.7874 0.5101 0.3217 0.0353  -0.1167 -0.0780 397 THR B CG2 
7378  N N   . GLU B 398 ? 0.7293 0.4708 0.2920 0.0524  -0.0600 -0.1031 398 GLU B N   
7379  C CA  . GLU B 398 ? 0.7910 0.5308 0.3594 0.0586  -0.0487 -0.1133 398 GLU B CA  
7380  C C   . GLU B 398 ? 0.7892 0.5387 0.3970 0.0577  -0.0594 -0.1155 398 GLU B C   
7381  O O   . GLU B 398 ? 0.7615 0.5277 0.3999 0.0548  -0.0666 -0.1076 398 GLU B O   
7382  C CB  . GLU B 398 ? 0.8802 0.6366 0.4585 0.0649  -0.0235 -0.1100 398 GLU B CB  
7383  C CG  . GLU B 398 ? 0.9857 0.7391 0.5672 0.0732  -0.0098 -0.1197 398 GLU B CG  
7384  C CD  . GLU B 398 ? 1.1851 0.9098 0.7247 0.0751  -0.0092 -0.1306 398 GLU B CD  
7385  O OE1 . GLU B 398 ? 1.2499 0.9683 0.7598 0.0744  -0.0007 -0.1280 398 GLU B OE1 
7386  O OE2 . GLU B 398 ? 1.2510 0.9661 0.7982 0.0747  -0.0169 -0.1385 398 GLU B OE2 
7387  N N   . VAL B 399 ? 0.7375 0.4750 0.3433 0.0604  -0.0598 -0.1262 399 VAL B N   
7388  C CA  . VAL B 399 ? 0.7641 0.5099 0.4063 0.0596  -0.0676 -0.1282 399 VAL B CA  
7389  C C   . VAL B 399 ? 0.7380 0.4993 0.4051 0.0669  -0.0490 -0.1280 399 VAL B C   
7390  O O   . VAL B 399 ? 0.7990 0.5554 0.4501 0.0736  -0.0323 -0.1320 399 VAL B O   
7391  C CB  . VAL B 399 ? 0.8391 0.5609 0.4656 0.0564  -0.0819 -0.1391 399 VAL B CB  
7392  C CG1 . VAL B 399 ? 0.7768 0.5075 0.4424 0.0551  -0.0881 -0.1403 399 VAL B CG1 
7393  C CG2 . VAL B 399 ? 0.8494 0.5613 0.4574 0.0480  -0.1017 -0.1362 399 VAL B CG2 
7394  N N   . ILE B 400 ? 0.6538 0.4340 0.3601 0.0659  -0.0516 -0.1228 400 ILE B N   
7395  C CA  . ILE B 400 ? 0.7267 0.5223 0.4600 0.0717  -0.0378 -0.1214 400 ILE B CA  
7396  C C   . ILE B 400 ? 0.7140 0.5073 0.4703 0.0703  -0.0467 -0.1251 400 ILE B C   
7397  O O   . ILE B 400 ? 0.7248 0.5211 0.4956 0.0641  -0.0612 -0.1225 400 ILE B O   
7398  C CB  . ILE B 400 ? 0.6891 0.5098 0.4463 0.0710  -0.0317 -0.1104 400 ILE B CB  
7399  C CG1 . ILE B 400 ? 0.7345 0.5602 0.4742 0.0733  -0.0180 -0.1062 400 ILE B CG1 
7400  C CG2 . ILE B 400 ? 0.7297 0.5662 0.5195 0.0745  -0.0248 -0.1081 400 ILE B CG2 
7401  C CD1 . ILE B 400 ? 0.7425 0.5921 0.5062 0.0718  -0.0114 -0.0957 400 ILE B CD1 
7402  N N   . GLU B 401 ? 0.6797 0.4679 0.4405 0.0762  -0.0376 -0.1305 401 GLU B N   
7403  C CA  . GLU B 401 ? 0.6438 0.4287 0.4262 0.0743  -0.0449 -0.1330 401 GLU B CA  
7404  C C   . GLU B 401 ? 0.5749 0.3797 0.3901 0.0780  -0.0360 -0.1266 401 GLU B C   
7405  O O   . GLU B 401 ? 0.5875 0.3925 0.4232 0.0755  -0.0418 -0.1263 401 GLU B O   
7406  C CB  . GLU B 401 ? 0.6671 0.4250 0.4291 0.0766  -0.0454 -0.1444 401 GLU B CB  
7407  C CG  . GLU B 401 ? 0.7788 0.5127 0.5014 0.0728  -0.0544 -0.1522 401 GLU B CG  
7408  C CD  . GLU B 401 ? 0.8572 0.5787 0.5811 0.0625  -0.0760 -0.1554 401 GLU B CD  
7409  O OE1 . GLU B 401 ? 0.8641 0.6021 0.6128 0.0565  -0.0870 -0.1480 401 GLU B OE1 
7410  O OE2 . GLU B 401 ? 0.9409 0.6434 0.6484 0.0588  -0.0801 -0.1615 401 GLU B OE2 
7411  N N   . SER B 402 ? 0.5394 0.3611 0.3603 0.0829  -0.0230 -0.1205 402 SER B N   
7412  C CA  . SER B 402 ? 0.5285 0.3686 0.3779 0.0861  -0.0156 -0.1140 402 SER B CA  
7413  C C   . SER B 402 ? 0.4931 0.3539 0.3478 0.0870  -0.0071 -0.1057 402 SER B C   
7414  O O   . SER B 402 ? 0.4913 0.3512 0.3275 0.0891  -0.0001 -0.1061 402 SER B O   
7415  C CB  . SER B 402 ? 0.5435 0.3756 0.3951 0.0946  -0.0061 -0.1181 402 SER B CB  
7416  O OG  . SER B 402 ? 0.6256 0.4747 0.5046 0.0969  -0.0018 -0.1109 402 SER B OG  
7417  N N   . VAL B 403 ? 0.4755 0.3539 0.3541 0.0846  -0.0078 -0.0981 403 VAL B N   
7418  C CA  . VAL B 403 ? 0.4583 0.3564 0.3451 0.0843  -0.0008 -0.0899 403 VAL B CA  
7419  C C   . VAL B 403 ? 0.4519 0.3637 0.3616 0.0877  0.0044  -0.0849 403 VAL B C   
7420  O O   . VAL B 403 ? 0.5038 0.4119 0.4256 0.0877  0.0000  -0.0857 403 VAL B O   
7421  C CB  . VAL B 403 ? 0.4444 0.3481 0.3329 0.0764  -0.0088 -0.0850 403 VAL B CB  
7422  C CG1 . VAL B 403 ? 0.4843 0.3734 0.3517 0.0731  -0.0167 -0.0889 403 VAL B CG1 
7423  C CG2 . VAL B 403 ? 0.3904 0.2981 0.2988 0.0733  -0.0155 -0.0827 403 VAL B CG2 
7424  N N   . LYS B 404 ? 0.4260 0.3544 0.3423 0.0902  0.0134  -0.0788 404 LYS B N   
7425  C CA  . LYS B 404 ? 0.4387 0.3828 0.3768 0.0926  0.0165  -0.0722 404 LYS B CA  
7426  C C   . LYS B 404 ? 0.4142 0.3693 0.3619 0.0845  0.0102  -0.0658 404 LYS B C   
7427  O O   . LYS B 404 ? 0.4637 0.4275 0.4081 0.0796  0.0109  -0.0617 404 LYS B O   
7428  C CB  . LYS B 404 ? 0.4886 0.4465 0.4323 0.0994  0.0284  -0.0683 404 LYS B CB  
7429  C CG  . LYS B 404 ? 0.6435 0.5893 0.5853 0.1105  0.0352  -0.0743 404 LYS B CG  
7430  C CD  . LYS B 404 ? 0.7465 0.6796 0.6963 0.1099  0.0264  -0.0767 404 LYS B CD  
7431  C CE  . LYS B 404 ? 0.8017 0.7093 0.7343 0.1074  0.0194  -0.0868 404 LYS B CE  
7432  N NZ  . LYS B 404 ? 0.8041 0.7106 0.7546 0.1040  0.0115  -0.0836 404 LYS B NZ  
7433  N N   . ALA B 405 ? 0.3718 0.3250 0.3299 0.0828  0.0046  -0.0649 405 ALA B N   
7434  C CA  . ALA B 405 ? 0.4293 0.3886 0.3926 0.0757  -0.0008 -0.0603 405 ALA B CA  
7435  C C   . ALA B 405 ? 0.3745 0.3506 0.3430 0.0727  0.0018  -0.0530 405 ALA B C   
7436  O O   . ALA B 405 ? 0.4256 0.4137 0.4032 0.0770  0.0072  -0.0491 405 ALA B O   
7437  C CB  . ALA B 405 ? 0.4205 0.3775 0.3942 0.0757  -0.0039 -0.0591 405 ALA B CB  
7438  N N   . GLY B 406 ? 0.3660 0.3430 0.3297 0.0651  -0.0023 -0.0508 406 GLY B N   
7439  C CA  . GLY B 406 ? 0.3277 0.3190 0.2965 0.0599  -0.0018 -0.0437 406 GLY B CA  
7440  C C   . GLY B 406 ? 0.3307 0.3158 0.2903 0.0516  -0.0069 -0.0431 406 GLY B C   
7441  O O   . GLY B 406 ? 0.3720 0.3436 0.3246 0.0511  -0.0109 -0.0475 406 GLY B O   
7442  N N   . THR B 407 ? 0.3021 0.2973 0.2632 0.0452  -0.0069 -0.0372 407 THR B N   
7443  C CA  . THR B 407 ? 0.3075 0.2952 0.2592 0.0368  -0.0115 -0.0360 407 THR B CA  
7444  C C   . THR B 407 ? 0.3466 0.3430 0.2963 0.0322  -0.0078 -0.0310 407 THR B C   
7445  O O   . THR B 407 ? 0.3559 0.3654 0.3126 0.0361  -0.0009 -0.0285 407 THR B O   
7446  C CB  . THR B 407 ? 0.3271 0.3149 0.2811 0.0304  -0.0171 -0.0333 407 THR B CB  
7447  O OG1 . THR B 407 ? 0.2906 0.2962 0.2549 0.0259  -0.0170 -0.0262 407 THR B OG1 
7448  C CG2 . THR B 407 ? 0.2956 0.2785 0.2530 0.0354  -0.0185 -0.0365 407 THR B CG2 
7449  N N   . TRP B 408 ? 0.3575 0.3463 0.2982 0.0238  -0.0117 -0.0288 408 TRP B N   
7450  C CA  . TRP B 408 ? 0.4022 0.3989 0.3413 0.0176  -0.0082 -0.0226 408 TRP B CA  
7451  C C   . TRP B 408 ? 0.4066 0.4216 0.3602 0.0101  -0.0091 -0.0149 408 TRP B C   
7452  O O   . TRP B 408 ? 0.4021 0.4260 0.3577 0.0030  -0.0064 -0.0083 408 TRP B O   
7453  C CB  . TRP B 408 ? 0.3489 0.3282 0.2720 0.0114  -0.0123 -0.0224 408 TRP B CB  
7454  C CG  . TRP B 408 ? 0.3788 0.3449 0.2975 0.0046  -0.0203 -0.0229 408 TRP B CG  
7455  C CD1 . TRP B 408 ? 0.3558 0.3228 0.2802 0.0028  -0.0245 -0.0241 408 TRP B CD1 
7456  C CD2 . TRP B 408 ? 0.3705 0.3180 0.2754 -0.0007 -0.0245 -0.0225 408 TRP B CD2 
7457  N NE1 . TRP B 408 ? 0.3468 0.2958 0.2603 -0.0032 -0.0303 -0.0253 408 TRP B NE1 
7458  C CE2 . TRP B 408 ? 0.3680 0.3050 0.2709 -0.0051 -0.0303 -0.0242 408 TRP B CE2 
7459  C CE3 . TRP B 408 ? 0.3931 0.3305 0.2857 -0.0020 -0.0240 -0.0203 408 TRP B CE3 
7460  C CZ2 . TRP B 408 ? 0.3839 0.2998 0.2741 -0.0097 -0.0348 -0.0246 408 TRP B CZ2 
7461  C CZ3 . TRP B 408 ? 0.4664 0.3839 0.3477 -0.0069 -0.0295 -0.0196 408 TRP B CZ3 
7462  C CH2 . TRP B 408 ? 0.4974 0.4041 0.3783 -0.0103 -0.0345 -0.0220 408 TRP B CH2 
7463  N N   . PHE B 409 ? 0.3678 0.3891 0.3316 0.0107  -0.0132 -0.0147 409 PHE B N   
7464  C CA  . PHE B 409 ? 0.4025 0.4451 0.3834 0.0053  -0.0148 -0.0067 409 PHE B CA  
7465  C C   . PHE B 409 ? 0.4003 0.4615 0.3981 0.0160  -0.0073 -0.0048 409 PHE B C   
7466  O O   . PHE B 409 ? 0.2971 0.3578 0.2997 0.0231  -0.0088 -0.0074 409 PHE B O   
7467  C CB  . PHE B 409 ? 0.4170 0.4546 0.3966 -0.0009 -0.0249 -0.0065 409 PHE B CB  
7468  C CG  . PHE B 409 ? 0.4618 0.5195 0.4566 -0.0097 -0.0299 0.0026  409 PHE B CG  
7469  C CD1 . PHE B 409 ? 0.5130 0.5925 0.5280 -0.0039 -0.0287 0.0077  409 PHE B CD1 
7470  C CD2 . PHE B 409 ? 0.5317 0.5868 0.5221 -0.0240 -0.0365 0.0068  409 PHE B CD2 
7471  C CE1 . PHE B 409 ? 0.5565 0.6573 0.5888 -0.0121 -0.0347 0.0173  409 PHE B CE1 
7472  C CE2 . PHE B 409 ? 0.5529 0.6280 0.5594 -0.0337 -0.0428 0.0158  409 PHE B CE2 
7473  C CZ  . PHE B 409 ? 0.5665 0.6659 0.5950 -0.0277 -0.0422 0.0214  409 PHE B CZ  
7474  N N   . ASP B 410 ? 0.3495 0.4263 0.3559 0.0174  0.0017  0.0000  410 ASP B N   
7475  C CA  . ASP B 410 ? 0.4023 0.4973 0.4258 0.0283  0.0110  0.0024  410 ASP B CA  
7476  C C   . ASP B 410 ? 0.3638 0.4443 0.3786 0.0414  0.0151  -0.0068 410 ASP B C   
7477  O O   . ASP B 410 ? 0.4507 0.5410 0.4783 0.0516  0.0209  -0.0062 410 ASP B O   
7478  C CB  . ASP B 410 ? 0.5234 0.6402 0.5707 0.0270  0.0059  0.0104  410 ASP B CB  
7479  C CG  . ASP B 410 ? 0.6172 0.7533 0.6783 0.0138  0.0021  0.0209  410 ASP B CG  
7480  O OD1 . ASP B 410 ? 0.6523 0.7913 0.7103 0.0085  0.0083  0.0236  410 ASP B OD1 
7481  O OD2 . ASP B 410 ? 0.6734 0.8212 0.7477 0.0079  -0.0079 0.0268  410 ASP B OD2 
7482  N N   . GLY B 411 ? 0.3254 0.3823 0.3197 0.0414  0.0119  -0.0150 411 GLY B N   
7483  C CA  . GLY B 411 ? 0.3359 0.3792 0.3230 0.0520  0.0146  -0.0233 411 GLY B CA  
7484  C C   . GLY B 411 ? 0.3874 0.4291 0.3834 0.0566  0.0099  -0.0247 411 GLY B C   
7485  O O   . GLY B 411 ? 0.4199 0.4545 0.4155 0.0661  0.0135  -0.0298 411 GLY B O   
7486  N N   . ASN B 412 ? 0.3420 0.3886 0.3443 0.0499  0.0019  -0.0203 412 ASN B N   
7487  C CA  . ASN B 412 ? 0.3164 0.3619 0.3257 0.0538  -0.0021 -0.0201 412 ASN B CA  
7488  C C   . ASN B 412 ? 0.3545 0.3909 0.3554 0.0449  -0.0114 -0.0200 412 ASN B C   
7489  O O   . ASN B 412 ? 0.3194 0.3490 0.3098 0.0367  -0.0145 -0.0209 412 ASN B O   
7490  C CB  . ASN B 412 ? 0.3109 0.3780 0.3413 0.0587  0.0002  -0.0121 412 ASN B CB  
7491  C CG  . ASN B 412 ? 0.3477 0.4341 0.3892 0.0490  -0.0049 -0.0027 412 ASN B CG  
7492  O OD1 . ASN B 412 ? 0.3812 0.4623 0.4151 0.0388  -0.0140 -0.0016 412 ASN B OD1 
7493  N ND2 . ASN B 412 ? 0.3284 0.4374 0.3891 0.0523  0.0010  0.0044  412 ASN B ND2 
7494  N N   . PHE B 413 ? 0.3315 0.3657 0.3353 0.0468  -0.0154 -0.0190 413 PHE B N   
7495  C CA  . PHE B 413 ? 0.2775 0.2993 0.2695 0.0403  -0.0220 -0.0204 413 PHE B CA  
7496  C C   . PHE B 413 ? 0.3257 0.3573 0.3209 0.0332  -0.0297 -0.0130 413 PHE B C   
7497  O O   . PHE B 413 ? 0.3269 0.3468 0.3098 0.0286  -0.0347 -0.0141 413 PHE B O   
7498  C CB  . PHE B 413 ? 0.2653 0.2732 0.2534 0.0465  -0.0205 -0.0252 413 PHE B CB  
7499  C CG  . PHE B 413 ? 0.3140 0.3094 0.2966 0.0504  -0.0164 -0.0328 413 PHE B CG  
7500  C CD1 . PHE B 413 ? 0.3116 0.2935 0.2828 0.0463  -0.0181 -0.0373 413 PHE B CD1 
7501  C CD2 . PHE B 413 ? 0.3419 0.3378 0.3302 0.0584  -0.0113 -0.0355 413 PHE B CD2 
7502  C CE1 . PHE B 413 ? 0.3288 0.3008 0.2970 0.0497  -0.0162 -0.0432 413 PHE B CE1 
7503  C CE2 . PHE B 413 ? 0.3686 0.3523 0.3503 0.0608  -0.0097 -0.0424 413 PHE B CE2 
7504  C CZ  . PHE B 413 ? 0.3200 0.2931 0.2929 0.0562  -0.0129 -0.0457 413 PHE B CZ  
7505  N N   . LEU B 414 ? 0.3483 0.4007 0.3589 0.0318  -0.0308 -0.0053 414 LEU B N   
7506  C CA  . LEU B 414 ? 0.4235 0.4879 0.4402 0.0253  -0.0401 0.0029  414 LEU B CA  
7507  C C   . LEU B 414 ? 0.3621 0.4173 0.3630 0.0114  -0.0488 0.0027  414 LEU B C   
7508  O O   . LEU B 414 ? 0.3587 0.4169 0.3573 0.0049  -0.0585 0.0078  414 LEU B O   
7509  C CB  . LEU B 414 ? 0.4206 0.5125 0.4622 0.0273  -0.0387 0.0119  414 LEU B CB  
7510  C CG  . LEU B 414 ? 0.4340 0.5343 0.4915 0.0420  -0.0312 0.0134  414 LEU B CG  
7511  C CD1 . LEU B 414 ? 0.3938 0.5236 0.4790 0.0449  -0.0296 0.0237  414 LEU B CD1 
7512  C CD2 . LEU B 414 ? 0.4222 0.5122 0.4746 0.0464  -0.0358 0.0138  414 LEU B CD2 
7513  N N   . LYS B 415 ? 0.3492 0.3911 0.3375 0.0067  -0.0465 -0.0030 415 LYS B N   
7514  C CA  . LYS B 415 ? 0.4029 0.4322 0.3746 -0.0060 -0.0547 -0.0038 415 LYS B CA  
7515  C C   . LYS B 415 ? 0.3636 0.3692 0.3135 -0.0056 -0.0564 -0.0103 415 LYS B C   
7516  O O   . LYS B 415 ? 0.4546 0.4460 0.3871 -0.0152 -0.0628 -0.0119 415 LYS B O   
7517  C CB  . LYS B 415 ? 0.4692 0.4914 0.4351 -0.0113 -0.0518 -0.0065 415 LYS B CB  
7518  C CG  . LYS B 415 ? 0.5360 0.5793 0.5179 -0.0188 -0.0531 0.0017  415 LYS B CG  
7519  C CD  . LYS B 415 ? 0.6415 0.6910 0.6242 -0.0324 -0.0655 0.0081  415 LYS B CD  
7520  C CE  . LYS B 415 ? 0.7050 0.7866 0.7156 -0.0317 -0.0678 0.0188  415 LYS B CE  
7521  N NZ  . LYS B 415 ? 0.7367 0.8240 0.7475 -0.0435 -0.0827 0.0251  415 LYS B NZ  
7522  N N   . TRP B 416 ? 0.3990 0.3990 0.3491 0.0050  -0.0502 -0.0140 416 TRP B N   
7523  C CA  . TRP B 416 ? 0.3443 0.3235 0.2762 0.0064  -0.0490 -0.0195 416 TRP B CA  
7524  C C   . TRP B 416 ? 0.3743 0.3559 0.3088 0.0126  -0.0484 -0.0167 416 TRP B C   
7525  O O   . TRP B 416 ? 0.3887 0.3543 0.3071 0.0127  -0.0473 -0.0197 416 TRP B O   
7526  C CB  . TRP B 416 ? 0.3461 0.3118 0.2744 0.0124  -0.0409 -0.0273 416 TRP B CB  
7527  C CG  . TRP B 416 ? 0.4438 0.4047 0.3682 0.0073  -0.0414 -0.0294 416 TRP B CG  
7528  C CD1 . TRP B 416 ? 0.4089 0.3516 0.3159 0.0007  -0.0438 -0.0330 416 TRP B CD1 
7529  C CD2 . TRP B 416 ? 0.4289 0.4012 0.3648 0.0082  -0.0390 -0.0277 416 TRP B CD2 
7530  N NE1 . TRP B 416 ? 0.4407 0.3829 0.3491 -0.0027 -0.0438 -0.0329 416 TRP B NE1 
7531  C CE2 . TRP B 416 ? 0.4223 0.3830 0.3476 0.0014  -0.0407 -0.0294 416 TRP B CE2 
7532  C CE3 . TRP B 416 ? 0.4026 0.3922 0.3552 0.0144  -0.0348 -0.0249 416 TRP B CE3 
7533  C CZ2 . TRP B 416 ? 0.3799 0.3464 0.3101 0.0000  -0.0386 -0.0276 416 TRP B CZ2 
7534  C CZ3 . TRP B 416 ? 0.3677 0.3629 0.3240 0.0135  -0.0317 -0.0239 416 TRP B CZ3 
7535  C CH2 . TRP B 416 ? 0.3383 0.3224 0.2833 0.0060  -0.0338 -0.0249 416 TRP B CH2 
7536  N N   . ILE B 417 ? 0.3456 0.3455 0.2993 0.0181  -0.0484 -0.0107 417 ILE B N   
7537  C CA  . ILE B 417 ? 0.4145 0.4155 0.3712 0.0243  -0.0483 -0.0069 417 ILE B CA  
7538  C C   . ILE B 417 ? 0.4242 0.4479 0.4016 0.0268  -0.0525 0.0023  417 ILE B C   
7539  O O   . ILE B 417 ? 0.4305 0.4695 0.4233 0.0272  -0.0511 0.0041  417 ILE B O   
7540  C CB  . ILE B 417 ? 0.4151 0.4070 0.3751 0.0339  -0.0387 -0.0124 417 ILE B CB  
7541  C CG1 . ILE B 417 ? 0.3859 0.3730 0.3442 0.0384  -0.0380 -0.0088 417 ILE B CG1 
7542  C CG2 . ILE B 417 ? 0.3805 0.3828 0.3576 0.0404  -0.0335 -0.0139 417 ILE B CG2 
7543  C CD1 . ILE B 417 ? 0.3729 0.3449 0.3263 0.0427  -0.0301 -0.0146 417 ILE B CD1 
7544  N N   . GLY B 418 ? 0.3900 0.4165 0.3681 0.0288  -0.0574 0.0090  418 GLY B N   
7545  C CA  . GLY B 418 ? 0.4074 0.4561 0.4082 0.0330  -0.0613 0.0187  418 GLY B CA  
7546  C C   . GLY B 418 ? 0.4865 0.5461 0.4877 0.0259  -0.0749 0.0288  418 GLY B C   
7547  O O   . GLY B 418 ? 0.6283 0.6992 0.6434 0.0323  -0.0782 0.0375  418 GLY B O   
7548  N N   . ASN B 419 ? 0.4240 0.4801 0.4105 0.0127  -0.0838 0.0285  419 ASN B N   
7549  C CA  . ASN B 419 ? 0.4366 0.5019 0.4216 0.0048  -0.0990 0.0384  419 ASN B CA  
7550  C C   . ASN B 419 ? 0.4097 0.4513 0.3627 0.0010  -0.1037 0.0366  419 ASN B C   
7551  O O   . ASN B 419 ? 0.4278 0.4477 0.3622 0.0041  -0.0940 0.0279  419 ASN B O   
7552  C CB  . ASN B 419 ? 0.4896 0.5666 0.4787 -0.0088 -0.1087 0.0409  419 ASN B CB  
7553  C CG  . ASN B 419 ? 0.5556 0.6079 0.5146 -0.0201 -0.1095 0.0310  419 ASN B CG  
7554  O OD1 . ASN B 419 ? 0.6268 0.6536 0.5583 -0.0196 -0.1062 0.0238  419 ASN B OD1 
7555  N ND2 . ASN B 419 ? 0.5223 0.5821 0.4874 -0.0302 -0.1134 0.0312  419 ASN B ND2 
7556  N N   . LYS B 420 ? 0.4388 0.4854 0.3855 -0.0060 -0.1186 0.0456  420 LYS B N   
7557  C CA  . LYS B 420 ? 0.4382 0.4625 0.3527 -0.0088 -0.1228 0.0456  420 LYS B CA  
7558  C C   . LYS B 420 ? 0.4984 0.4946 0.3787 -0.0165 -0.1185 0.0336  420 LYS B C   
7559  O O   . LYS B 420 ? 0.5324 0.5071 0.3907 -0.0126 -0.1097 0.0283  420 LYS B O   
7560  C CB  . LYS B 420 ? 0.5056 0.5400 0.4170 -0.0169 -0.1423 0.0576  420 LYS B CB  
7561  C CG  . LYS B 420 ? 0.6273 0.6407 0.5060 -0.0182 -0.1471 0.0603  420 LYS B CG  
7562  C CD  . LYS B 420 ? 0.6910 0.7217 0.5801 -0.0191 -0.1644 0.0761  420 LYS B CD  
7563  C CE  . LYS B 420 ? 0.7749 0.7858 0.6228 -0.0312 -0.1792 0.0785  420 LYS B CE  
7564  N NZ  . LYS B 420 ? 0.8175 0.8455 0.6756 -0.0320 -0.1980 0.0951  420 LYS B NZ  
7565  N N   . GLU B 421 ? 0.5131 0.5088 0.3896 -0.0272 -0.1236 0.0294  421 GLU B N   
7566  C CA  . GLU B 421 ? 0.5271 0.4938 0.3693 -0.0347 -0.1209 0.0184  421 GLU B CA  
7567  C C   . GLU B 421 ? 0.5087 0.4635 0.3519 -0.0255 -0.1027 0.0080  421 GLU B C   
7568  O O   . GLU B 421 ? 0.4830 0.4138 0.3010 -0.0235 -0.0946 0.0007  421 GLU B O   
7569  C CB  . GLU B 421 ? 0.5901 0.5577 0.4281 -0.0495 -0.1327 0.0176  421 GLU B CB  
7570  C CG  . GLU B 421 ? 0.7340 0.7009 0.5555 -0.0626 -0.1527 0.0248  421 GLU B CG  
7571  C CD  . GLU B 421 ? 0.8043 0.8067 0.6612 -0.0630 -0.1646 0.0391  421 GLU B CD  
7572  O OE1 . GLU B 421 ? 0.8172 0.8441 0.7104 -0.0568 -0.1580 0.0421  421 GLU B OE1 
7573  O OE2 . GLU B 421 ? 0.8449 0.8505 0.6930 -0.0691 -0.1804 0.0477  421 GLU B OE2 
7574  N N   . LYS B 422 ? 0.5105 0.4822 0.3827 -0.0197 -0.0961 0.0075  422 LYS B N   
7575  C CA  . LYS B 422 ? 0.4158 0.3777 0.2904 -0.0114 -0.0812 -0.0014 422 LYS B CA  
7576  C C   . LYS B 422 ? 0.4600 0.4156 0.3337 -0.0006 -0.0716 -0.0018 422 LYS B C   
7577  O O   . LYS B 422 ? 0.4612 0.3996 0.3230 0.0030  -0.0615 -0.0094 422 LYS B O   
7578  C CB  . LYS B 422 ? 0.3913 0.3724 0.2945 -0.0074 -0.0771 -0.0009 422 LYS B CB  
7579  C CG  . LYS B 422 ? 0.4312 0.4172 0.3361 -0.0183 -0.0838 -0.0006 422 LYS B CG  
7580  C CD  . LYS B 422 ? 0.4019 0.4055 0.3326 -0.0136 -0.0773 0.0001  422 LYS B CD  
7581  C CE  . LYS B 422 ? 0.4149 0.4269 0.3504 -0.0255 -0.0842 0.0030  422 LYS B CE  
7582  N NZ  . LYS B 422 ? 0.3798 0.3669 0.2905 -0.0346 -0.0858 -0.0044 422 LYS B NZ  
7583  N N   . ASN B 423 ? 0.4034 0.3732 0.2915 0.0045  -0.0748 0.0070  423 ASN B N   
7584  C CA  . ASN B 423 ? 0.4276 0.3907 0.3154 0.0136  -0.0666 0.0080  423 ASN B CA  
7585  C C   . ASN B 423 ? 0.4249 0.3658 0.2803 0.0098  -0.0657 0.0066  423 ASN B C   
7586  O O   . ASN B 423 ? 0.4313 0.3612 0.2819 0.0157  -0.0550 0.0043  423 ASN B O   
7587  C CB  . ASN B 423 ? 0.4256 0.4061 0.3339 0.0198  -0.0713 0.0187  423 ASN B CB  
7588  C CG  . ASN B 423 ? 0.4177 0.4153 0.3569 0.0283  -0.0658 0.0185  423 ASN B CG  
7589  O OD1 . ASN B 423 ? 0.3855 0.3824 0.3299 0.0289  -0.0593 0.0108  423 ASN B OD1 
7590  N ND2 . ASN B 423 ? 0.4417 0.4531 0.4001 0.0354  -0.0683 0.0271  423 ASN B ND2 
7591  N N   . GLU B 424 ? 0.5131 0.4469 0.3456 -0.0005 -0.0767 0.0081  424 GLU B N   
7592  C CA  . GLU B 424 ? 0.5817 0.4909 0.3779 -0.0043 -0.0745 0.0054  424 GLU B CA  
7593  C C   . GLU B 424 ? 0.5097 0.4004 0.2939 -0.0023 -0.0607 -0.0063 424 GLU B C   
7594  O O   . GLU B 424 ? 0.5216 0.3962 0.2890 0.0014  -0.0500 -0.0089 424 GLU B O   
7595  C CB  . GLU B 424 ? 0.6773 0.5799 0.4482 -0.0168 -0.0905 0.0082  424 GLU B CB  
7596  C CG  . GLU B 424 ? 0.7829 0.6552 0.5087 -0.0218 -0.0880 0.0033  424 GLU B CG  
7597  C CD  . GLU B 424 ? 0.8743 0.7397 0.5868 -0.0166 -0.0834 0.0099  424 GLU B CD  
7598  O OE1 . GLU B 424 ? 0.8786 0.7189 0.5537 -0.0191 -0.0778 0.0061  424 GLU B OE1 
7599  O OE2 . GLU B 424 ? 0.8840 0.7674 0.6221 -0.0098 -0.0843 0.0190  424 GLU B OE2 
7600  N N   . TYR B 425 ? 0.4961 0.3896 0.2906 -0.0041 -0.0602 -0.0126 425 TYR B N   
7601  C CA  . TYR B 425 ? 0.5246 0.4025 0.3125 -0.0007 -0.0477 -0.0227 425 TYR B CA  
7602  C C   . TYR B 425 ? 0.4894 0.3717 0.2962 0.0104  -0.0342 -0.0235 425 TYR B C   
7603  O O   . TYR B 425 ? 0.5291 0.3967 0.3244 0.0142  -0.0226 -0.0280 425 TYR B O   
7604  C CB  . TYR B 425 ? 0.4799 0.3616 0.2778 -0.0046 -0.0512 -0.0273 425 TYR B CB  
7605  C CG  . TYR B 425 ? 0.4852 0.3472 0.2545 -0.0150 -0.0576 -0.0323 425 TYR B CG  
7606  C CD1 . TYR B 425 ? 0.5276 0.3787 0.2694 -0.0236 -0.0674 -0.0298 425 TYR B CD1 
7607  C CD2 . TYR B 425 ? 0.4771 0.3293 0.2454 -0.0164 -0.0547 -0.0395 425 TYR B CD2 
7608  C CE1 . TYR B 425 ? 0.6195 0.4487 0.3321 -0.0340 -0.0740 -0.0355 425 TYR B CE1 
7609  C CE2 . TYR B 425 ? 0.4978 0.3284 0.2391 -0.0260 -0.0604 -0.0446 425 TYR B CE2 
7610  C CZ  . TYR B 425 ? 0.5357 0.3542 0.2487 -0.0351 -0.0700 -0.0431 425 TYR B CZ  
7611  O OH  . TYR B 425 ? 0.5487 0.3427 0.2328 -0.0454 -0.0763 -0.0492 425 TYR B OH  
7612  N N   . TRP B 426 ? 0.4326 0.3348 0.2687 0.0156  -0.0352 -0.0190 426 TRP B N   
7613  C CA  . TRP B 426 ? 0.4548 0.3598 0.3083 0.0246  -0.0244 -0.0195 426 TRP B CA  
7614  C C   . TRP B 426 ? 0.4778 0.3739 0.3190 0.0266  -0.0189 -0.0151 426 TRP B C   
7615  O O   . TRP B 426 ? 0.5203 0.4096 0.3639 0.0312  -0.0072 -0.0178 426 TRP B O   
7616  C CB  . TRP B 426 ? 0.4340 0.3585 0.3165 0.0293  -0.0274 -0.0157 426 TRP B CB  
7617  C CG  . TRP B 426 ? 0.3588 0.2902 0.2533 0.0289  -0.0285 -0.0207 426 TRP B CG  
7618  C CD1 . TRP B 426 ? 0.3781 0.3214 0.2787 0.0246  -0.0368 -0.0185 426 TRP B CD1 
7619  C CD2 . TRP B 426 ? 0.4205 0.3477 0.3226 0.0326  -0.0212 -0.0278 426 TRP B CD2 
7620  N NE1 . TRP B 426 ? 0.4003 0.3457 0.3098 0.0253  -0.0341 -0.0238 426 TRP B NE1 
7621  C CE2 . TRP B 426 ? 0.4657 0.4010 0.3757 0.0304  -0.0254 -0.0296 426 TRP B CE2 
7622  C CE3 . TRP B 426 ? 0.4499 0.3686 0.3545 0.0373  -0.0118 -0.0318 426 TRP B CE3 
7623  C CZ2 . TRP B 426 ? 0.5074 0.4402 0.4241 0.0329  -0.0214 -0.0353 426 TRP B CZ2 
7624  C CZ3 . TRP B 426 ? 0.5240 0.4425 0.4387 0.0399  -0.0086 -0.0375 426 TRP B CZ3 
7625  C CH2 . TRP B 426 ? 0.5438 0.4683 0.4629 0.0378  -0.0139 -0.0392 426 TRP B CH2 
7626  N N   . LYS B 427 ? 0.5166 0.4135 0.3458 0.0231  -0.0274 -0.0072 427 LYS B N   
7627  C CA  . LYS B 427 ? 0.5171 0.4031 0.3294 0.0241  -0.0225 -0.0020 427 LYS B CA  
7628  C C   . LYS B 427 ? 0.5258 0.3908 0.3100 0.0221  -0.0124 -0.0084 427 LYS B C   
7629  O O   . LYS B 427 ? 0.5520 0.4096 0.3338 0.0262  0.0003  -0.0078 427 LYS B O   
7630  C CB  . LYS B 427 ? 0.6065 0.4955 0.4067 0.0196  -0.0359 0.0078  427 LYS B CB  
7631  C CG  . LYS B 427 ? 0.6968 0.6005 0.5215 0.0257  -0.0392 0.0173  427 LYS B CG  
7632  C CD  . LYS B 427 ? 0.7427 0.6620 0.5754 0.0228  -0.0555 0.0250  427 LYS B CD  
7633  C CE  . LYS B 427 ? 0.8110 0.7204 0.6122 0.0148  -0.0663 0.0311  427 LYS B CE  
7634  N NZ  . LYS B 427 ? 0.8293 0.7567 0.6424 0.0123  -0.0836 0.0413  427 LYS B NZ  
7635  N N   . ILE B 428 ? 0.5184 0.3727 0.2806 0.0156  -0.0174 -0.0141 428 ILE B N   
7636  C CA  . ILE B 428 ? 0.5748 0.4069 0.3099 0.0150  -0.0066 -0.0220 428 ILE B CA  
7637  C C   . ILE B 428 ? 0.6032 0.4368 0.3590 0.0232  0.0088  -0.0276 428 ILE B C   
7638  O O   . ILE B 428 ? 0.6080 0.4305 0.3541 0.0271  0.0232  -0.0292 428 ILE B O   
7639  C CB  . ILE B 428 ? 0.6149 0.4351 0.3283 0.0070  -0.0157 -0.0285 428 ILE B CB  
7640  C CG1 . ILE B 428 ? 0.5369 0.3527 0.2250 -0.0024 -0.0312 -0.0227 428 ILE B CG1 
7641  C CG2 . ILE B 428 ? 0.6584 0.4544 0.3480 0.0088  -0.0026 -0.0385 428 ILE B CG2 
7642  C CD1 . ILE B 428 ? 0.5536 0.3598 0.2237 -0.0126 -0.0435 -0.0277 428 ILE B CD1 
7643  N N   . LEU B 429 ? 0.4862 0.3344 0.2712 0.0257  0.0058  -0.0301 429 LEU B N   
7644  C CA  . LEU B 429 ? 0.4290 0.2802 0.2354 0.0326  0.0170  -0.0350 429 LEU B CA  
7645  C C   . LEU B 429 ? 0.4721 0.3312 0.2974 0.0380  0.0256  -0.0299 429 LEU B C   
7646  O O   . LEU B 429 ? 0.5695 0.4251 0.4015 0.0426  0.0385  -0.0321 429 LEU B O   
7647  C CB  . LEU B 429 ? 0.4258 0.2897 0.2551 0.0329  0.0097  -0.0378 429 LEU B CB  
7648  C CG  . LEU B 429 ? 0.4447 0.3121 0.2960 0.0394  0.0181  -0.0424 429 LEU B CG  
7649  C CD1 . LEU B 429 ? 0.4423 0.2930 0.2785 0.0409  0.0260  -0.0493 429 LEU B CD1 
7650  C CD2 . LEU B 429 ? 0.3622 0.2435 0.2353 0.0397  0.0100  -0.0432 429 LEU B CD2 
7651  N N   . ILE B 430 ? 0.4706 0.3408 0.3068 0.0375  0.0185  -0.0225 430 ILE B N   
7652  C CA  . ILE B 430 ? 0.4747 0.3496 0.3269 0.0414  0.0255  -0.0168 430 ILE B CA  
7653  C C   . ILE B 430 ? 0.5053 0.3666 0.3360 0.0410  0.0369  -0.0138 430 ILE B C   
7654  O O   . ILE B 430 ? 0.5687 0.4296 0.4107 0.0444  0.0496  -0.0135 430 ILE B O   
7655  C CB  . ILE B 430 ? 0.4673 0.3527 0.3307 0.0415  0.0153  -0.0092 430 ILE B CB  
7656  C CG1 . ILE B 430 ? 0.4522 0.3515 0.3406 0.0438  0.0085  -0.0126 430 ILE B CG1 
7657  C CG2 . ILE B 430 ? 0.5082 0.3929 0.3812 0.0442  0.0221  -0.0023 430 ILE B CG2 
7658  C CD1 . ILE B 430 ? 0.4778 0.3871 0.3735 0.0442  -0.0020 -0.0061 430 ILE B CD1 
7659  N N   . GLU B 431 ? 0.5398 0.3899 0.3387 0.0364  0.0324  -0.0111 431 GLU B N   
7660  C CA  . GLU B 431 ? 0.6249 0.4598 0.3981 0.0359  0.0441  -0.0080 431 GLU B CA  
7661  C C   . GLU B 431 ? 0.6309 0.4556 0.3975 0.0391  0.0595  -0.0161 431 GLU B C   
7662  O O   . GLU B 431 ? 0.6330 0.4541 0.4007 0.0422  0.0753  -0.0138 431 GLU B O   
7663  C CB  . GLU B 431 ? 0.7372 0.5596 0.4729 0.0297  0.0345  -0.0042 431 GLU B CB  
7664  C CG  . GLU B 431 ? 0.8995 0.7300 0.6393 0.0280  0.0226  0.0072  431 GLU B CG  
7665  C CD  . GLU B 431 ? 0.9691 0.8055 0.7305 0.0326  0.0314  0.0149  431 GLU B CD  
7666  O OE1 . GLU B 431 ? 0.9245 0.7756 0.7169 0.0356  0.0253  0.0176  431 GLU B OE1 
7667  O OE2 . GLU B 431 ? 1.0143 0.8395 0.7608 0.0329  0.0447  0.0184  431 GLU B OE2 
7668  N N   . ALA B 432 ? 0.6203 0.4406 0.3815 0.0385  0.0559  -0.0251 432 ALA B N   
7669  C CA  . ALA B 432 ? 0.6441 0.4536 0.4001 0.0430  0.0704  -0.0328 432 ALA B CA  
7670  C C   . ALA B 432 ? 0.6325 0.4568 0.4272 0.0497  0.0806  -0.0328 432 ALA B C   
7671  O O   . ALA B 432 ? 0.6195 0.4388 0.4153 0.0547  0.0972  -0.0345 432 ALA B O   
7672  C CB  . ALA B 432 ? 0.6426 0.4430 0.3863 0.0408  0.0627  -0.0418 432 ALA B CB  
7673  N N   . LYS B 433 ? 0.5802 0.4224 0.4066 0.0499  0.0709  -0.0308 433 LYS B N   
7674  C CA  . LYS B 433 ? 0.5589 0.4146 0.4215 0.0548  0.0774  -0.0308 433 LYS B CA  
7675  C C   . LYS B 433 ? 0.5885 0.4466 0.4599 0.0563  0.0910  -0.0240 433 LYS B C   
7676  O O   . LYS B 433 ? 0.5259 0.3893 0.4174 0.0606  0.1030  -0.0246 433 LYS B O   
7677  C CB  . LYS B 433 ? 0.5541 0.4249 0.4422 0.0538  0.0636  -0.0301 433 LYS B CB  
7678  C CG  . LYS B 433 ? 0.4988 0.3827 0.4224 0.0570  0.0671  -0.0291 433 LYS B CG  
7679  C CD  . LYS B 433 ? 0.5176 0.4029 0.4539 0.0614  0.0729  -0.0349 433 LYS B CD  
7680  C CE  . LYS B 433 ? 0.4523 0.3520 0.4252 0.0633  0.0730  -0.0335 433 LYS B CE  
7681  N NZ  . LYS B 433 ? 0.4539 0.3567 0.4423 0.0685  0.0787  -0.0373 433 LYS B NZ  
7682  N N   . LYS B 434 ? 0.6623 0.5168 0.5195 0.0526  0.0895  -0.0164 434 LYS B N   
7683  C CA  . LYS B 434 ? 0.6693 0.5247 0.5334 0.0529  0.1025  -0.0084 434 LYS B CA  
7684  C C   . LYS B 434 ? 0.6820 0.5282 0.5326 0.0561  0.1223  -0.0098 434 LYS B C   
7685  O O   . LYS B 434 ? 0.7254 0.5780 0.5947 0.0576  0.1361  -0.0045 434 LYS B O   
7686  C CB  . LYS B 434 ? 0.7157 0.5649 0.5605 0.0485  0.0971  0.0006  434 LYS B CB  
7687  C CG  . LYS B 434 ? 0.7009 0.5563 0.5508 0.0464  0.0779  0.0019  434 LYS B CG  
7688  C CD  . LYS B 434 ? 0.7478 0.5947 0.5722 0.0430  0.0717  0.0107  434 LYS B CD  
7689  C CE  . LYS B 434 ? 0.7375 0.5940 0.5773 0.0428  0.0555  0.0144  434 LYS B CE  
7690  N NZ  . LYS B 434 ? 0.7573 0.6129 0.6043 0.0428  0.0563  0.0253  434 LYS B NZ  
7691  N N   . LYS B 435 ? 0.6283 0.4588 0.4465 0.0570  0.1245  -0.0165 435 LYS B N   
7692  C CA  . LYS B 435 ? 0.6451 0.4635 0.4459 0.0614  0.1448  -0.0190 435 LYS B CA  
7693  C C   . LYS B 435 ? 0.6942 0.5088 0.4986 0.0672  0.1479  -0.0295 435 LYS B C   
7694  O O   . LYS B 435 ? 0.7346 0.5323 0.5133 0.0711  0.1617  -0.0344 435 LYS B O   
7695  C CB  . LYS B 435 ? 0.6991 0.4949 0.4492 0.0578  0.1479  -0.0176 435 LYS B CB  
7696  C CG  . LYS B 435 ? 0.7284 0.5231 0.4635 0.0504  0.1301  -0.0112 435 LYS B CG  
7697  C CD  . LYS B 435 ? 0.8178 0.5897 0.5016 0.0466  0.1330  -0.0090 435 LYS B CD  
7698  C CE  . LYS B 435 ? 0.8785 0.6498 0.5474 0.0395  0.1126  -0.0021 435 LYS B CE  
7699  N NZ  . LYS B 435 ? 0.9863 0.7369 0.6076 0.0354  0.1161  0.0036  435 LYS B NZ  
7700  N N   . ALA B 436 ? 0.5830 0.5029 0.4220 -0.0439 0.0879  0.0243  436 ALA B N   
7701  C CA  . ALA B 436 ? 0.5827 0.5298 0.4491 -0.0338 0.0911  0.0176  436 ALA B CA  
7702  C C   . ALA B 436 ? 0.5748 0.5483 0.4745 -0.0394 0.1082  0.0168  436 ALA B C   
7703  O O   . ALA B 436 ? 0.5709 0.5500 0.4851 -0.0509 0.1112  0.0205  436 ALA B O   
7704  C CB  . ALA B 436 ? 0.5288 0.4878 0.4146 -0.0259 0.0721  0.0144  436 ALA B CB  
7705  N N   . LYS B 437 ? 0.5734 0.5632 0.4878 -0.0311 0.1195  0.0117  437 LYS B N   
7706  C CA  . LYS B 437 ? 0.6171 0.6354 0.5698 -0.0340 0.1366  0.0102  437 LYS B CA  
7707  C C   . LYS B 437 ? 0.6002 0.6454 0.5897 -0.0208 0.1332  0.0049  437 LYS B C   
7708  O O   . LYS B 437 ? 0.5756 0.6461 0.6016 -0.0202 0.1473  0.0029  437 LYS B O   
7709  C CB  . LYS B 437 ? 0.6718 0.6804 0.6050 -0.0397 0.1635  0.0098  437 LYS B CB  
7710  C CG  . LYS B 437 ? 0.7507 0.7205 0.6280 -0.0478 0.1643  0.0147  437 LYS B CG  
7711  C CD  . LYS B 437 ? 0.8213 0.7819 0.6779 -0.0571 0.1928  0.0154  437 LYS B CD  
7712  C CE  . LYS B 437 ? 0.8977 0.8152 0.6903 -0.0634 0.1910  0.0204  437 LYS B CE  
7713  N NZ  . LYS B 437 ? 0.9473 0.8512 0.7081 -0.0695 0.2196  0.0184  437 LYS B NZ  
7714  N N   . ASN B 438 ? 0.5665 0.6071 0.5495 -0.0103 0.1154  0.0031  438 ASN B N   
7715  C CA  . ASN B 438 ? 0.5576 0.6204 0.5734 0.0014  0.1096  0.0001  438 ASN B CA  
7716  C C   . ASN B 438 ? 0.5355 0.5921 0.5419 0.0067  0.0865  0.0011  438 ASN B C   
7717  O O   . ASN B 438 ? 0.5614 0.5982 0.5389 0.0030  0.0775  0.0027  438 ASN B O   
7718  C CB  . ASN B 438 ? 0.5315 0.5917 0.5451 0.0114  0.1252  -0.0054 438 ASN B CB  
7719  C CG  . ASN B 438 ? 0.5388 0.5666 0.5045 0.0140  0.1244  -0.0076 438 ASN B CG  
7720  O OD1 . ASN B 438 ? 0.5295 0.5478 0.4828 0.0193  0.1072  -0.0071 438 ASN B OD1 
7721  N ND2 . ASN B 438 ? 0.5897 0.6006 0.5281 0.0097  0.1430  -0.0101 438 ASN B ND2 
7722  N N   . ASP B 439 ? 0.4689 0.5424 0.5007 0.0158  0.0777  0.0005  439 ASP B N   
7723  C CA  . ASP B 439 ? 0.4483 0.5201 0.4751 0.0197  0.0575  0.0021  439 ASP B CA  
7724  C C   . ASP B 439 ? 0.3908 0.4409 0.3868 0.0260  0.0538  0.0007  439 ASP B C   
7725  O O   . ASP B 439 ? 0.4108 0.4594 0.4022 0.0291  0.0400  0.0021  439 ASP B O   
7726  C CB  . ASP B 439 ? 0.5282 0.6230 0.5900 0.0263  0.0487  0.0038  439 ASP B CB  
7727  C CG  . ASP B 439 ? 0.5923 0.7089 0.6840 0.0184  0.0421  0.0061  439 ASP B CG  
7728  O OD1 . ASP B 439 ? 0.5577 0.6685 0.6384 0.0075  0.0402  0.0063  439 ASP B OD1 
7729  O OD2 . ASP B 439 ? 0.6532 0.7921 0.7809 0.0231  0.0376  0.0078  439 ASP B OD2 
7730  N N   . TYR B 440 ? 0.4031 0.4362 0.3775 0.0271  0.0657  -0.0020 440 TYR B N   
7731  C CA  . TYR B 440 ? 0.4223 0.4344 0.3679 0.0308  0.0593  -0.0031 440 TYR B CA  
7732  C C   . TYR B 440 ? 0.4248 0.4247 0.3503 0.0249  0.0487  -0.0009 440 TYR B C   
7733  O O   . TYR B 440 ? 0.4405 0.4287 0.3506 0.0279  0.0399  -0.0012 440 TYR B O   
7734  C CB  . TYR B 440 ? 0.4713 0.4655 0.3948 0.0322  0.0725  -0.0071 440 TYR B CB  
7735  C CG  . TYR B 440 ? 0.5510 0.5463 0.4844 0.0423  0.0767  -0.0112 440 TYR B CG  
7736  C CD1 . TYR B 440 ? 0.5374 0.5258 0.4665 0.0479  0.0643  -0.0108 440 TYR B CD1 
7737  C CD2 . TYR B 440 ? 0.5717 0.5742 0.5205 0.0461  0.0942  -0.0156 440 TYR B CD2 
7738  C CE1 . TYR B 440 ? 0.5504 0.5360 0.4882 0.0568  0.0672  -0.0141 440 TYR B CE1 
7739  C CE2 . TYR B 440 ? 0.5662 0.5671 0.5255 0.0566  0.0979  -0.0201 440 TYR B CE2 
7740  C CZ  . TYR B 440 ? 0.5701 0.5609 0.5228 0.0618  0.0835  -0.0191 440 TYR B CZ  
7741  O OH  . TYR B 440 ? 0.6245 0.6101 0.5873 0.0719  0.0865  -0.0232 440 TYR B OH  
7742  N N   . ILE B 441 ? 0.4015 0.4038 0.3295 0.0167  0.0494  0.0010  441 ILE B N   
7743  C CA  . ILE B 441 ? 0.4543 0.4453 0.3683 0.0128  0.0383  0.0023  441 ILE B CA  
7744  C C   . ILE B 441 ? 0.4243 0.4261 0.3500 0.0165  0.0259  0.0016  441 ILE B C   
7745  O O   . ILE B 441 ? 0.4129 0.4054 0.3269 0.0180  0.0176  0.0008  441 ILE B O   
7746  C CB  . ILE B 441 ? 0.4471 0.4348 0.3609 0.0026  0.0418  0.0045  441 ILE B CB  
7747  C CG1 . ILE B 441 ? 0.3842 0.3527 0.2793 0.0001  0.0316  0.0055  441 ILE B CG1 
7748  C CG2 . ILE B 441 ? 0.3903 0.4006 0.3341 -0.0014 0.0400  0.0044  441 ILE B CG2 
7749  C CD1 . ILE B 441 ? 0.4343 0.3782 0.2999 0.0004  0.0324  0.0076  441 ILE B CD1 
7750  N N   . LEU B 442 ? 0.3693 0.3908 0.3182 0.0181  0.0245  0.0019  442 LEU B N   
7751  C CA  . LEU B 442 ? 0.3500 0.3790 0.3035 0.0208  0.0129  0.0020  442 LEU B CA  
7752  C C   . LEU B 442 ? 0.3443 0.3669 0.2883 0.0280  0.0106  0.0023  442 LEU B C   
7753  O O   . LEU B 442 ? 0.3135 0.3342 0.2504 0.0288  0.0033  0.0021  442 LEU B O   
7754  C CB  . LEU B 442 ? 0.2910 0.3407 0.2701 0.0205  0.0091  0.0039  442 LEU B CB  
7755  C CG  . LEU B 442 ? 0.3098 0.3693 0.3051 0.0119  0.0114  0.0038  442 LEU B CG  
7756  C CD1 . LEU B 442 ? 0.3730 0.4559 0.3998 0.0128  0.0062  0.0062  442 LEU B CD1 
7757  C CD2 . LEU B 442 ? 0.3575 0.4080 0.3402 0.0042  0.0038  0.0016  442 LEU B CD2 
7758  N N   . VAL B 443 ? 0.3542 0.3722 0.2971 0.0325  0.0178  0.0022  443 VAL B N   
7759  C CA  . VAL B 443 ? 0.3961 0.4058 0.3304 0.0379  0.0150  0.0023  443 VAL B CA  
7760  C C   . VAL B 443 ? 0.3905 0.3866 0.3064 0.0359  0.0108  0.0011  443 VAL B C   
7761  O O   . VAL B 443 ? 0.3902 0.3855 0.3040 0.0375  0.0050  0.0018  443 VAL B O   
7762  C CB  . VAL B 443 ? 0.3964 0.3998 0.3308 0.0427  0.0236  0.0006  443 VAL B CB  
7763  C CG1 . VAL B 443 ? 0.4226 0.4155 0.3488 0.0468  0.0188  0.0008  443 VAL B CG1 
7764  C CG2 . VAL B 443 ? 0.3789 0.3980 0.3386 0.0465  0.0286  0.0013  443 VAL B CG2 
7765  N N   . ALA B 444 ? 0.4199 0.4050 0.3237 0.0322  0.0138  0.0000  444 ALA B N   
7766  C CA  . ALA B 444 ? 0.4378 0.4093 0.3271 0.0311  0.0079  -0.0005 444 ALA B CA  
7767  C C   . ALA B 444 ? 0.4085 0.3848 0.3031 0.0299  0.0018  -0.0013 444 ALA B C   
7768  O O   . ALA B 444 ? 0.4026 0.3709 0.2921 0.0309  -0.0036 -0.0021 444 ALA B O   
7769  C CB  . ALA B 444 ? 0.4267 0.3819 0.2985 0.0272  0.0115  0.0001  444 ALA B CB  
7770  N N   . GLU B 445 ? 0.3654 0.3541 0.2707 0.0280  0.0019  -0.0017 445 GLU B N   
7771  C CA  . GLU B 445 ? 0.3664 0.3573 0.2728 0.0269  -0.0029 -0.0043 445 GLU B CA  
7772  C C   . GLU B 445 ? 0.3928 0.3919 0.3017 0.0299  -0.0053 -0.0046 445 GLU B C   
7773  O O   . GLU B 445 ? 0.3974 0.3984 0.3048 0.0291  -0.0071 -0.0079 445 GLU B O   
7774  C CB  . GLU B 445 ? 0.4046 0.4015 0.3169 0.0214  -0.0033 -0.0053 445 GLU B CB  
7775  C CG  . GLU B 445 ? 0.4208 0.4064 0.3290 0.0163  -0.0007 -0.0048 445 GLU B CG  
7776  C CD  . GLU B 445 ? 0.4538 0.4488 0.3735 0.0094  0.0010  -0.0042 445 GLU B CD  
7777  O OE1 . GLU B 445 ? 0.3922 0.4021 0.3231 0.0091  -0.0027 -0.0047 445 GLU B OE1 
7778  O OE2 . GLU B 445 ? 0.5124 0.4995 0.4302 0.0034  0.0051  -0.0025 445 GLU B OE2 
7779  N N   . GLY B 446 ? 0.3839 0.3857 0.2949 0.0328  -0.0043 -0.0016 446 GLY B N   
7780  C CA  . GLY B 446 ? 0.4136 0.4206 0.3251 0.0341  -0.0058 -0.0003 446 GLY B CA  
7781  C C   . GLY B 446 ? 0.4410 0.4445 0.3512 0.0349  -0.0059 -0.0031 446 GLY B C   
7782  O O   . GLY B 446 ? 0.3761 0.3714 0.2860 0.0361  -0.0072 -0.0044 446 GLY B O   
7783  N N   . SER B 447 ? 0.3726 0.3827 0.2822 0.0339  -0.0045 -0.0038 447 SER B N   
7784  C CA  . SER B 447 ? 0.3924 0.4033 0.3059 0.0349  -0.0019 -0.0077 447 SER B CA  
7785  C C   . SER B 447 ? 0.3937 0.4037 0.3156 0.0362  -0.0029 -0.0051 447 SER B C   
7786  O O   . SER B 447 ? 0.3516 0.3609 0.2829 0.0382  -0.0041 -0.0080 447 SER B O   
7787  C CB  . SER B 447 ? 0.3618 0.3797 0.2696 0.0325  0.0030  -0.0092 447 SER B CB  
7788  O OG  . SER B 447 ? 0.3979 0.4195 0.3043 0.0305  0.0041  -0.0026 447 SER B OG  
7789  N N   . ASP B 448 ? 0.3387 0.3482 0.2593 0.0351  -0.0038 0.0002  448 ASP B N   
7790  C CA  . ASP B 448 ? 0.2963 0.3036 0.2238 0.0344  -0.0055 0.0026  448 ASP B CA  
7791  C C   . ASP B 448 ? 0.3236 0.3228 0.2544 0.0361  -0.0114 0.0003  448 ASP B C   
7792  O O   . ASP B 448 ? 0.3323 0.3331 0.2742 0.0352  -0.0145 0.0002  448 ASP B O   
7793  C CB  . ASP B 448 ? 0.2917 0.2940 0.2149 0.0337  -0.0067 0.0078  448 ASP B CB  
7794  C CG  . ASP B 448 ? 0.3824 0.3899 0.3005 0.0323  -0.0044 0.0122  448 ASP B CG  
7795  O OD1 . ASP B 448 ? 0.3496 0.3590 0.2632 0.0337  -0.0053 0.0119  448 ASP B OD1 
7796  O OD2 . ASP B 448 ? 0.4262 0.4354 0.3447 0.0290  -0.0026 0.0167  448 ASP B OD2 
7797  N N   . TRP B 449 ? 0.3406 0.3304 0.2615 0.0375  -0.0137 -0.0008 449 TRP B N   
7798  C CA  . TRP B 449 ? 0.3778 0.3556 0.2948 0.0381  -0.0206 -0.0017 449 TRP B CA  
7799  C C   . TRP B 449 ? 0.3244 0.3052 0.2531 0.0399  -0.0249 -0.0039 449 TRP B C   
7800  O O   . TRP B 449 ? 0.3295 0.3059 0.2643 0.0402  -0.0334 -0.0035 449 TRP B O   
7801  C CB  . TRP B 449 ? 0.3870 0.3532 0.2878 0.0379  -0.0196 -0.0017 449 TRP B CB  
7802  C CG  . TRP B 449 ? 0.3684 0.3369 0.2652 0.0378  -0.0128 -0.0006 449 TRP B CG  
7803  C CD1 . TRP B 449 ? 0.3807 0.3554 0.2783 0.0376  -0.0076 -0.0005 449 TRP B CD1 
7804  C CD2 . TRP B 449 ? 0.3366 0.3014 0.2318 0.0385  -0.0114 0.0003  449 TRP B CD2 
7805  N NE1 . TRP B 449 ? 0.3931 0.3707 0.2928 0.0389  -0.0035 0.0009  449 TRP B NE1 
7806  C CE2 . TRP B 449 ? 0.3890 0.3591 0.2864 0.0401  -0.0052 0.0011  449 TRP B CE2 
7807  C CE3 . TRP B 449 ? 0.3446 0.3013 0.2384 0.0377  -0.0158 0.0003  449 TRP B CE3 
7808  C CZ2 . TRP B 449 ? 0.4039 0.3709 0.3030 0.0426  -0.0026 0.0019  449 TRP B CZ2 
7809  C CZ3 . TRP B 449 ? 0.3491 0.3002 0.2412 0.0390  -0.0129 0.0006  449 TRP B CZ3 
7810  C CH2 . TRP B 449 ? 0.3572 0.3131 0.2522 0.0423  -0.0060 0.0013  449 TRP B CH2 
7811  N N   . PHE B 450 ? 0.2822 0.2696 0.2152 0.0415  -0.0201 -0.0067 450 PHE B N   
7812  C CA  . PHE B 450 ? 0.2806 0.2701 0.2276 0.0451  -0.0229 -0.0101 450 PHE B CA  
7813  C C   . PHE B 450 ? 0.3271 0.3319 0.2953 0.0456  -0.0196 -0.0115 450 PHE B C   
7814  O O   . PHE B 450 ? 0.3612 0.3694 0.3486 0.0490  -0.0244 -0.0133 450 PHE B O   
7815  C CB  . PHE B 450 ? 0.3312 0.3192 0.2741 0.0465  -0.0183 -0.0143 450 PHE B CB  
7816  C CG  . PHE B 450 ? 0.3545 0.3294 0.2798 0.0440  -0.0202 -0.0122 450 PHE B CG  
7817  C CD1 . PHE B 450 ? 0.4176 0.3956 0.3329 0.0403  -0.0153 -0.0104 450 PHE B CD1 
7818  C CD2 . PHE B 450 ? 0.4106 0.3703 0.3313 0.0451  -0.0269 -0.0113 450 PHE B CD2 
7819  C CE1 . PHE B 450 ? 0.3966 0.3661 0.3009 0.0373  -0.0150 -0.0086 450 PHE B CE1 
7820  C CE2 . PHE B 450 ? 0.4163 0.3642 0.3207 0.0410  -0.0265 -0.0086 450 PHE B CE2 
7821  C CZ  . PHE B 450 ? 0.4200 0.3745 0.3180 0.0370  -0.0194 -0.0077 450 PHE B CZ  
7822  N N   . TRP B 451 ? 0.3332 0.3470 0.2996 0.0419  -0.0118 -0.0098 451 TRP B N   
7823  C CA  . TRP B 451 ? 0.3018 0.3300 0.2868 0.0401  -0.0062 -0.0100 451 TRP B CA  
7824  C C   . TRP B 451 ? 0.3209 0.3497 0.3229 0.0390  -0.0156 -0.0076 451 TRP B C   
7825  O O   . TRP B 451 ? 0.3563 0.3973 0.3844 0.0403  -0.0153 -0.0098 451 TRP B O   
7826  C CB  . TRP B 451 ? 0.3229 0.3552 0.2968 0.0348  0.0018  -0.0061 451 TRP B CB  
7827  C CG  . TRP B 451 ? 0.4398 0.4841 0.4297 0.0303  0.0080  -0.0039 451 TRP B CG  
7828  C CD1 . TRP B 451 ? 0.4543 0.4973 0.4504 0.0253  0.0040  0.0016  451 TRP B CD1 
7829  C CD2 . TRP B 451 ? 0.5411 0.5997 0.5427 0.0293  0.0207  -0.0074 451 TRP B CD2 
7830  N NE1 . TRP B 451 ? 0.4914 0.5481 0.5042 0.0203  0.0131  0.0029  451 TRP B NE1 
7831  C CE2 . TRP B 451 ? 0.5545 0.6219 0.5708 0.0228  0.0247  -0.0027 451 TRP B CE2 
7832  C CE3 . TRP B 451 ? 0.6159 0.6795 0.6163 0.0330  0.0302  -0.0150 451 TRP B CE3 
7833  C CZ2 . TRP B 451 ? 0.6138 0.6971 0.6447 0.0195  0.0396  -0.0046 451 TRP B CZ2 
7834  C CZ3 . TRP B 451 ? 0.6936 0.7714 0.7063 0.0308  0.0452  -0.0183 451 TRP B CZ3 
7835  C CH2 . TRP B 451 ? 0.6841 0.7728 0.7123 0.0239  0.0506  -0.0128 451 TRP B CH2 
7836  N N   . TRP B 452 ? 0.3439 0.3601 0.3326 0.0363  -0.0238 -0.0038 452 TRP B N   
7837  C CA  . TRP B 452 ? 0.3538 0.3675 0.3537 0.0332  -0.0345 -0.0018 452 TRP B CA  
7838  C C   . TRP B 452 ? 0.4305 0.4363 0.4351 0.0368  -0.0487 -0.0030 452 TRP B C   
7839  O O   . TRP B 452 ? 0.3639 0.3723 0.3862 0.0347  -0.0597 -0.0020 452 TRP B O   
7840  C CB  . TRP B 452 ? 0.3481 0.3474 0.3283 0.0290  -0.0374 0.0012  452 TRP B CB  
7841  C CG  . TRP B 452 ? 0.3929 0.3975 0.3706 0.0256  -0.0270 0.0043  452 TRP B CG  
7842  C CD1 . TRP B 452 ? 0.3816 0.3814 0.3416 0.0269  -0.0207 0.0059  452 TRP B CD1 
7843  C CD2 . TRP B 452 ? 0.3586 0.3739 0.3531 0.0197  -0.0226 0.0074  452 TRP B CD2 
7844  N NE1 . TRP B 452 ? 0.3993 0.4038 0.3613 0.0228  -0.0145 0.0103  452 TRP B NE1 
7845  C CE2 . TRP B 452 ? 0.3882 0.4013 0.3695 0.0178  -0.0144 0.0115  452 TRP B CE2 
7846  C CE3 . TRP B 452 ? 0.3149 0.3419 0.3362 0.0154  -0.0251 0.0076  452 TRP B CE3 
7847  C CZ2 . TRP B 452 ? 0.3614 0.3804 0.3502 0.0109  -0.0082 0.0167  452 TRP B CZ2 
7848  C CZ3 . TRP B 452 ? 0.3746 0.4102 0.4068 0.0081  -0.0170 0.0120  452 TRP B CZ3 
7849  C CH2 . TRP B 452 ? 0.3531 0.3831 0.3666 0.0056  -0.0084 0.0169  452 TRP B CH2 
7850  N N   . GLN B 453 ? 0.4265 0.4216 0.4157 0.0411  -0.0501 -0.0041 453 GLN B N   
7851  C CA  . GLN B 453 ? 0.4385 0.4219 0.4275 0.0441  -0.0648 -0.0034 453 GLN B CA  
7852  C C   . GLN B 453 ? 0.5248 0.5236 0.5505 0.0487  -0.0695 -0.0052 453 GLN B C   
7853  O O   . GLN B 453 ? 0.5318 0.5439 0.5739 0.0530  -0.0583 -0.0093 453 GLN B O   
7854  C CB  . GLN B 453 ? 0.4161 0.3852 0.3827 0.0468  -0.0628 -0.0035 453 GLN B CB  
7855  C CG  . GLN B 453 ? 0.4314 0.3857 0.3961 0.0501  -0.0777 -0.0013 453 GLN B CG  
7856  C CD  . GLN B 453 ? 0.4701 0.4043 0.4115 0.0457  -0.0922 0.0030  453 GLN B CD  
7857  O OE1 . GLN B 453 ? 0.4542 0.3880 0.3890 0.0408  -0.0929 0.0029  453 GLN B OE1 
7858  N NE2 . GLN B 453 ? 0.4822 0.3968 0.4083 0.0468  -0.1042 0.0068  453 GLN B NE2 
7859  N N   . GLY B 454 ? 0.5959 0.5928 0.6348 0.0474  -0.0863 -0.0028 454 GLY B N   
7860  C CA  . GLY B 454 ? 0.6860 0.6995 0.7669 0.0513  -0.0947 -0.0036 454 GLY B CA  
7861  C C   . GLY B 454 ? 0.7682 0.8046 0.8829 0.0578  -0.0800 -0.0090 454 GLY B C   
7862  O O   . GLY B 454 ? 0.8097 0.8401 0.9224 0.0653  -0.0776 -0.0117 454 GLY B O   
7863  N N   . GLU B 455 ? 0.7863 0.8468 0.9308 0.0548  -0.0689 -0.0109 455 GLU B N   
7864  C CA  . GLU B 455 ? 0.7700 0.8384 0.9183 0.0445  -0.0671 -0.0078 455 GLU B CA  
7865  C C   . GLU B 455 ? 0.8019 0.8670 0.9627 0.0392  -0.0892 -0.0038 455 GLU B C   
7866  O O   . GLU B 455 ? 0.8297 0.8740 0.9706 0.0400  -0.1082 -0.0013 455 GLU B O   
7867  C CB  . GLU B 455 ? 0.7139 0.7677 0.8205 0.0388  -0.0578 -0.0059 455 GLU B CB  
7868  C CG  . GLU B 455 ? 0.6496 0.7126 0.7483 0.0390  -0.0353 -0.0084 455 GLU B CG  
7869  C CD  . GLU B 455 ? 0.6513 0.7324 0.7766 0.0456  -0.0229 -0.0147 455 GLU B CD  
7870  O OE1 . GLU B 455 ? 0.6405 0.7151 0.7490 0.0507  -0.0153 -0.0188 455 GLU B OE1 
7871  O OE2 . GLU B 455 ? 0.6452 0.7469 0.8087 0.0453  -0.0195 -0.0161 455 GLU B OE2 
7872  N N   . GLU B 456 ? 0.8021 0.8869 0.9942 0.0321  -0.0860 -0.0030 456 GLU B N   
7873  C CA  . GLU B 456 ? 0.8176 0.9051 1.0332 0.0262  -0.1075 -0.0001 456 GLU B CA  
7874  C C   . GLU B 456 ? 0.8575 0.9186 1.0343 0.0172  -0.1199 0.0027  456 GLU B C   
7875  O O   . GLU B 456 ? 0.8906 0.9269 1.0219 0.0190  -0.1191 0.0027  456 GLU B O   
7876  C CB  . GLU B 456 ? 0.7908 0.9100 1.0566 0.0202  -0.0978 -0.0003 456 GLU B CB  
7877  N N   . LYS B 457 ? 0.8529 0.9191 1.0495 0.0070  -0.1307 0.0045  457 LYS B N   
7878  C CA  . LYS B 457 ? 0.8659 0.9056 1.0290 -0.0021 -0.1438 0.0055  457 LYS B CA  
7879  C C   . LYS B 457 ? 0.8405 0.8674 0.9693 -0.0050 -0.1246 0.0055  457 LYS B C   
7880  O O   . LYS B 457 ? 0.8848 0.8947 0.9761 0.0011  -0.1177 0.0043  457 LYS B O   
7881  C CB  . LYS B 457 ? 0.8998 0.9502 1.0979 -0.0136 -0.1588 0.0070  457 LYS B CB  
7882  N N   . ALA B 458 ? 0.7539 0.7886 0.8974 -0.0147 -0.1167 0.0074  458 ALA B N   
7883  C CA  . ALA B 458 ? 0.6861 0.7107 0.8047 -0.0178 -0.0996 0.0091  458 ALA B CA  
7884  C C   . ALA B 458 ? 0.6874 0.6775 0.7618 -0.0190 -0.1084 0.0070  458 ALA B C   
7885  O O   . ALA B 458 ? 0.6563 0.6305 0.7013 -0.0118 -0.1130 0.0042  458 ALA B O   
7886  C CB  . ALA B 458 ? 0.6253 0.6596 0.7348 -0.0091 -0.0787 0.0091  458 ALA B CB  
7887  N N   . PRO B 459 ? 0.6589 0.6357 0.7276 -0.0283 -0.1096 0.0081  459 PRO B N   
7888  C CA  . PRO B 459 ? 0.6110 0.5536 0.6383 -0.0284 -0.1153 0.0043  459 PRO B CA  
7889  C C   . PRO B 459 ? 0.5906 0.5245 0.5883 -0.0187 -0.0993 0.0039  459 PRO B C   
7890  O O   . PRO B 459 ? 0.4476 0.3982 0.4544 -0.0152 -0.0834 0.0078  459 PRO B O   
7891  C CB  . PRO B 459 ? 0.6087 0.5419 0.6439 -0.0401 -0.1167 0.0062  459 PRO B CB  
7892  C CG  . PRO B 459 ? 0.6193 0.5823 0.7022 -0.0485 -0.1171 0.0110  459 PRO B CG  
7893  C CD  . PRO B 459 ? 0.6360 0.6272 0.7362 -0.0394 -0.1045 0.0127  459 PRO B CD  
7894  N N   . PHE B 460 ? 0.5694 0.4768 0.5311 -0.0152 -0.1038 -0.0013 460 PHE B N   
7895  C CA  . PHE B 460 ? 0.5211 0.4174 0.4549 -0.0066 -0.0908 -0.0031 460 PHE B CA  
7896  C C   . PHE B 460 ? 0.4364 0.3477 0.3693 0.0018  -0.0832 -0.0020 460 PHE B C   
7897  O O   . PHE B 460 ? 0.4654 0.3699 0.3784 0.0082  -0.0732 -0.0034 460 PHE B O   
7898  C CB  . PHE B 460 ? 0.5913 0.4867 0.5277 -0.0063 -0.0777 0.0004  460 PHE B CB  
7899  C CG  . PHE B 460 ? 0.6175 0.4936 0.5532 -0.0145 -0.0843 -0.0005 460 PHE B CG  
7900  C CD1 . PHE B 460 ? 0.6666 0.5147 0.5790 -0.0169 -0.0954 -0.0083 460 PHE B CD1 
7901  C CD2 . PHE B 460 ? 0.6501 0.5337 0.6061 -0.0208 -0.0795 0.0065  460 PHE B CD2 
7902  C CE1 . PHE B 460 ? 0.6998 0.5267 0.6107 -0.0250 -0.1023 -0.0103 460 PHE B CE1 
7903  C CE2 . PHE B 460 ? 0.6607 0.5240 0.6169 -0.0294 -0.0862 0.0062  460 PHE B CE2 
7904  C CZ  . PHE B 460 ? 0.7055 0.5401 0.6401 -0.0313 -0.0980 -0.0028 460 PHE B CZ  
7905  N N   . VAL B 461 ? 0.4423 0.3730 0.3979 0.0021  -0.0880 0.0000  461 VAL B N   
7906  C CA  . VAL B 461 ? 0.5072 0.4474 0.4602 0.0099  -0.0825 0.0001  461 VAL B CA  
7907  C C   . VAL B 461 ? 0.5985 0.5162 0.5167 0.0131  -0.0865 -0.0030 461 VAL B C   
7908  O O   . VAL B 461 ? 0.6759 0.5947 0.5825 0.0187  -0.0768 -0.0030 461 VAL B O   
7909  C CB  . VAL B 461 ? 0.6111 0.5717 0.5956 0.0106  -0.0894 0.0015  461 VAL B CB  
7910  C CG1 . VAL B 461 ? 0.6206 0.5707 0.6064 0.0069  -0.1113 0.0006  461 VAL B CG1 
7911  C CG2 . VAL B 461 ? 0.6135 0.5820 0.5967 0.0188  -0.0823 0.0012  461 VAL B CG2 
7912  N N   . GLU B 462 ? 0.5525 0.4488 0.4519 0.0085  -0.1005 -0.0058 462 GLU B N   
7913  C CA  . GLU B 462 ? 0.6307 0.5024 0.4907 0.0101  -0.1019 -0.0090 462 GLU B CA  
7914  C C   . GLU B 462 ? 0.5896 0.4551 0.4319 0.0142  -0.0833 -0.0115 462 GLU B C   
7915  O O   . GLU B 462 ? 0.5685 0.4246 0.3874 0.0172  -0.0767 -0.0126 462 GLU B O   
7916  C CB  . GLU B 462 ? 0.7270 0.5728 0.5638 0.0031  -0.1186 -0.0130 462 GLU B CB  
7917  C CG  . GLU B 462 ? 0.8777 0.7263 0.7281 -0.0010 -0.1414 -0.0102 462 GLU B CG  
7918  C CD  . GLU B 462 ? 0.9823 0.8485 0.8724 -0.0066 -0.1491 -0.0089 462 GLU B CD  
7919  O OE1 . GLU B 462 ? 1.0146 0.8901 0.9278 -0.0093 -0.1673 -0.0063 462 GLU B OE1 
7920  O OE2 . GLU B 462 ? 0.9672 0.8377 0.8667 -0.0084 -0.1372 -0.0099 462 GLU B OE2 
7921  N N   . VAL B 463 ? 0.5196 0.3900 0.3743 0.0142  -0.0750 -0.0116 463 VAL B N   
7922  C CA  . VAL B 463 ? 0.5080 0.3733 0.3511 0.0193  -0.0595 -0.0137 463 VAL B CA  
7923  C C   . VAL B 463 ? 0.4783 0.3624 0.3298 0.0249  -0.0485 -0.0102 463 VAL B C   
7924  O O   . VAL B 463 ? 0.4668 0.3454 0.3030 0.0286  -0.0388 -0.0123 463 VAL B O   
7925  C CB  . VAL B 463 ? 0.5101 0.3743 0.3656 0.0186  -0.0556 -0.0130 463 VAL B CB  
7926  C CG1 . VAL B 463 ? 0.4857 0.3453 0.3336 0.0256  -0.0415 -0.0149 463 VAL B CG1 
7927  C CG2 . VAL B 463 ? 0.4978 0.3400 0.3440 0.0117  -0.0675 -0.0174 463 VAL B CG2 
7928  N N   . PHE B 464 ? 0.4940 0.3999 0.3699 0.0249  -0.0494 -0.0055 464 PHE B N   
7929  C CA  . PHE B 464 ? 0.4316 0.3528 0.3135 0.0292  -0.0407 -0.0034 464 PHE B CA  
7930  C C   . PHE B 464 ? 0.4242 0.3368 0.2890 0.0301  -0.0427 -0.0047 464 PHE B C   
7931  O O   . PHE B 464 ? 0.3974 0.3120 0.2555 0.0326  -0.0335 -0.0047 464 PHE B O   
7932  C CB  . PHE B 464 ? 0.4228 0.3656 0.3302 0.0286  -0.0407 -0.0001 464 PHE B CB  
7933  C CG  . PHE B 464 ? 0.3994 0.3504 0.3197 0.0266  -0.0357 0.0031  464 PHE B CG  
7934  C CD1 . PHE B 464 ? 0.4205 0.3789 0.3408 0.0292  -0.0264 0.0057  464 PHE B CD1 
7935  C CD2 . PHE B 464 ? 0.4059 0.3556 0.3374 0.0210  -0.0417 0.0044  464 PHE B CD2 
7936  C CE1 . PHE B 464 ? 0.4143 0.3766 0.3420 0.0267  -0.0233 0.0105  464 PHE B CE1 
7937  C CE2 . PHE B 464 ? 0.4182 0.3723 0.3589 0.0177  -0.0367 0.0088  464 PHE B CE2 
7938  C CZ  . PHE B 464 ? 0.3602 0.3195 0.2971 0.0208  -0.0276 0.0124  464 PHE B CZ  
7939  N N   . ASP B 465 ? 0.3944 0.2969 0.2527 0.0274  -0.0558 -0.0049 465 ASP B N   
7940  C CA  . ASP B 465 ? 0.4572 0.3465 0.2947 0.0272  -0.0599 -0.0044 465 ASP B CA  
7941  C C   . ASP B 465 ? 0.4675 0.3370 0.2725 0.0261  -0.0516 -0.0075 465 ASP B C   
7942  O O   . ASP B 465 ? 0.4911 0.3569 0.2830 0.0265  -0.0440 -0.0064 465 ASP B O   
7943  C CB  . ASP B 465 ? 0.4498 0.3303 0.2865 0.0245  -0.0790 -0.0030 465 ASP B CB  
7944  C CG  . ASP B 465 ? 0.4721 0.3329 0.2808 0.0234  -0.0858 -0.0009 465 ASP B CG  
7945  O OD1 . ASP B 465 ? 0.5110 0.3777 0.3272 0.0263  -0.0848 0.0024  465 ASP B OD1 
7946  O OD2 . ASP B 465 ? 0.5577 0.3946 0.3341 0.0190  -0.0919 -0.0025 465 ASP B OD2 
7947  N N   . LYS B 466 ? 0.5051 0.3607 0.2972 0.0242  -0.0521 -0.0118 466 LYS B N   
7948  C CA  . LYS B 466 ? 0.5417 0.3793 0.3051 0.0242  -0.0404 -0.0168 466 LYS B CA  
7949  C C   . LYS B 466 ? 0.5157 0.3689 0.2924 0.0292  -0.0223 -0.0166 466 LYS B C   
7950  O O   . LYS B 466 ? 0.5475 0.3951 0.3083 0.0291  -0.0108 -0.0178 466 LYS B O   
7951  C CB  . LYS B 466 ? 0.5828 0.4033 0.3349 0.0226  -0.0430 -0.0230 466 LYS B CB  
7952  C CG  . LYS B 466 ? 0.6810 0.4806 0.4023 0.0235  -0.0291 -0.0304 466 LYS B CG  
7953  C CD  . LYS B 466 ? 0.7322 0.5105 0.4403 0.0218  -0.0331 -0.0382 466 LYS B CD  
7954  C CE  . LYS B 466 ? 0.8349 0.5838 0.4998 0.0205  -0.0234 -0.0473 466 LYS B CE  
7955  N NZ  . LYS B 466 ? 0.9198 0.6404 0.5613 0.0156  -0.0349 -0.0552 466 LYS B NZ  
7956  N N   . LEU B 467 ? 0.4269 0.2996 0.2329 0.0326  -0.0200 -0.0145 467 LEU B N   
7957  C CA  . LEU B 467 ? 0.4254 0.3140 0.2466 0.0371  -0.0067 -0.0136 467 LEU B CA  
7958  C C   . LEU B 467 ? 0.4268 0.3260 0.2508 0.0362  -0.0035 -0.0102 467 LEU B C   
7959  O O   . LEU B 467 ? 0.4687 0.3691 0.2884 0.0367  0.0079  -0.0112 467 LEU B O   
7960  C CB  . LEU B 467 ? 0.4306 0.3352 0.2779 0.0397  -0.0083 -0.0103 467 LEU B CB  
7961  C CG  . LEU B 467 ? 0.3876 0.2813 0.2356 0.0414  -0.0082 -0.0128 467 LEU B CG  
7962  C CD1 . LEU B 467 ? 0.3903 0.2976 0.2602 0.0413  -0.0121 -0.0070 467 LEU B CD1 
7963  C CD2 . LEU B 467 ? 0.4334 0.3225 0.2793 0.0471  0.0044  -0.0169 467 LEU B CD2 
7964  N N   . PHE B 468 ? 0.3694 0.2770 0.2033 0.0348  -0.0128 -0.0067 468 PHE B N   
7965  C CA  . PHE B 468 ? 0.3877 0.3020 0.2242 0.0338  -0.0112 -0.0042 468 PHE B CA  
7966  C C   . PHE B 468 ? 0.4087 0.3060 0.2197 0.0304  -0.0065 -0.0044 468 PHE B C   
7967  O O   . PHE B 468 ? 0.4361 0.3385 0.2481 0.0292  0.0040  -0.0038 468 PHE B O   
7968  C CB  . PHE B 468 ? 0.3525 0.2712 0.1992 0.0336  -0.0226 -0.0021 468 PHE B CB  
7969  C CG  . PHE B 468 ? 0.4074 0.3265 0.2541 0.0328  -0.0228 -0.0003 468 PHE B CG  
7970  C CD1 . PHE B 468 ? 0.3637 0.2975 0.2241 0.0335  -0.0160 -0.0004 468 PHE B CD1 
7971  C CD2 . PHE B 468 ? 0.4472 0.3499 0.2796 0.0311  -0.0318 0.0020  468 PHE B CD2 
7972  C CE1 . PHE B 468 ? 0.4442 0.3756 0.3044 0.0320  -0.0168 0.0004  468 PHE B CE1 
7973  C CE2 . PHE B 468 ? 0.4284 0.3281 0.2611 0.0304  -0.0327 0.0041  468 PHE B CE2 
7974  C CZ  . PHE B 468 ? 0.4629 0.3766 0.3098 0.0307  -0.0246 0.0028  468 PHE B CZ  
7975  N N   . ARG B 469 ? 0.3966 0.2730 0.1836 0.0276  -0.0145 -0.0048 469 ARG B N   
7976  C CA  . ARG B 469 ? 0.4804 0.3367 0.2363 0.0228  -0.0111 -0.0036 469 ARG B CA  
7977  C C   . ARG B 469 ? 0.5098 0.3608 0.2517 0.0221  0.0069  -0.0080 469 ARG B C   
7978  O O   . ARG B 469 ? 0.5517 0.3943 0.2758 0.0177  0.0170  -0.0065 469 ARG B O   
7979  C CB  . ARG B 469 ? 0.4705 0.3039 0.2012 0.0196  -0.0274 -0.0024 469 ARG B CB  
7980  C CG  . ARG B 469 ? 0.5000 0.3387 0.2478 0.0210  -0.0447 0.0023  469 ARG B CG  
7981  C CD  . ARG B 469 ? 0.5168 0.3359 0.2463 0.0183  -0.0641 0.0036  469 ARG B CD  
7982  N NE  . ARG B 469 ? 0.4900 0.3152 0.2408 0.0209  -0.0811 0.0082  469 ARG B NE  
7983  C CZ  . ARG B 469 ? 0.5358 0.3478 0.2757 0.0201  -0.0900 0.0142  469 ARG B CZ  
7984  N NH1 . ARG B 469 ? 0.5452 0.3370 0.2504 0.0150  -0.0828 0.0173  469 ARG B NH1 
7985  N NH2 . ARG B 469 ? 0.5328 0.3512 0.2973 0.0243  -0.1056 0.0173  469 ARG B NH2 
7986  N N   . SER B 470 ? 0.5244 0.3793 0.2748 0.0264  0.0121  -0.0134 470 SER B N   
7987  C CA  . SER B 470 ? 0.5475 0.4010 0.2930 0.0281  0.0310  -0.0188 470 SER B CA  
7988  C C   . SER B 470 ? 0.5682 0.4458 0.3416 0.0298  0.0431  -0.0163 470 SER B C   
7989  O O   . SER B 470 ? 0.5686 0.4458 0.3359 0.0276  0.0592  -0.0179 470 SER B O   
7990  C CB  . SER B 470 ? 0.5699 0.4206 0.3221 0.0336  0.0320  -0.0250 470 SER B CB  
7991  O OG  . SER B 470 ? 0.6640 0.4872 0.3836 0.0305  0.0251  -0.0298 470 SER B OG  
7992  N N   . PHE B 471 ? 0.5190 0.4179 0.3230 0.0327  0.0355  -0.0127 471 PHE B N   
7993  C CA  . PHE B 471 ? 0.4508 0.3724 0.2814 0.0333  0.0426  -0.0102 471 PHE B CA  
7994  C C   . PHE B 471 ? 0.4627 0.3817 0.2843 0.0260  0.0449  -0.0065 471 PHE B C   
7995  O O   . PHE B 471 ? 0.4739 0.4044 0.3079 0.0234  0.0564  -0.0059 471 PHE B O   
7996  C CB  . PHE B 471 ? 0.4653 0.4049 0.3214 0.0366  0.0319  -0.0074 471 PHE B CB  
7997  C CG  . PHE B 471 ? 0.4325 0.3761 0.3012 0.0429  0.0303  -0.0089 471 PHE B CG  
7998  C CD1 . PHE B 471 ? 0.4256 0.3719 0.3039 0.0479  0.0410  -0.0120 471 PHE B CD1 
7999  C CD2 . PHE B 471 ? 0.4672 0.4116 0.3399 0.0438  0.0188  -0.0068 471 PHE B CD2 
8000  C CE1 . PHE B 471 ? 0.4721 0.4187 0.3620 0.0540  0.0383  -0.0126 471 PHE B CE1 
8001  C CE2 . PHE B 471 ? 0.4997 0.4449 0.3824 0.0482  0.0170  -0.0067 471 PHE B CE2 
8002  C CZ  . PHE B 471 ? 0.4462 0.3911 0.3367 0.0536  0.0258  -0.0093 471 PHE B CZ  
8003  N N   . VAL B 472 ? 0.4409 0.3452 0.2442 0.0225  0.0331  -0.0035 472 VAL B N   
8004  C CA  . VAL B 472 ? 0.4925 0.3877 0.2831 0.0155  0.0335  0.0011  472 VAL B CA  
8005  C C   . VAL B 472 ? 0.5663 0.4464 0.3310 0.0096  0.0486  0.0009  472 VAL B C   
8006  O O   . VAL B 472 ? 0.5258 0.4089 0.2923 0.0032  0.0590  0.0038  472 VAL B O   
8007  C CB  . VAL B 472 ? 0.5710 0.4506 0.3479 0.0149  0.0160  0.0045  472 VAL B CB  
8008  C CG1 . VAL B 472 ? 0.6467 0.5055 0.3982 0.0074  0.0157  0.0100  472 VAL B CG1 
8009  C CG2 . VAL B 472 ? 0.5331 0.4292 0.3375 0.0189  0.0058  0.0048  472 VAL B CG2 
8010  N N   . ARG B 473 ? 0.5952 0.4575 0.3337 0.0106  0.0505  -0.0029 473 ARG B N   
8011  C CA  . ARG B 473 ? 0.6372 0.4827 0.3454 0.0049  0.0674  -0.0047 473 ARG B CA  
8012  C C   . ARG B 473 ? 0.5811 0.4482 0.3152 0.0065  0.0893  -0.0086 473 ARG B C   
8013  O O   . ARG B 473 ? 0.6086 0.4771 0.3395 -0.0007 0.1045  -0.0062 473 ARG B O   
8014  C CB  . ARG B 473 ? 0.7936 0.6150 0.4681 0.0061  0.0642  -0.0102 473 ARG B CB  
8015  C CG  . ARG B 473 ? 0.9854 0.7743 0.6077 -0.0030 0.0683  -0.0083 473 ARG B CG  
8016  C CD  . ARG B 473 ? 1.1594 0.9223 0.7499 -0.0037 0.0467  -0.0085 473 ARG B CD  
8017  N NE  . ARG B 473 ? 1.2434 1.0073 0.8445 -0.0037 0.0227  -0.0001 473 ARG B NE  
8018  C CZ  . ARG B 473 ? 1.2742 1.0302 0.8730 -0.0014 0.0003  0.0001  473 ARG B CZ  
8019  N NH1 . ARG B 473 ? 1.2958 1.0405 0.8796 -0.0002 -0.0028 -0.0073 473 ARG B NH1 
8020  N NH2 . ARG B 473 ? 1.2363 0.9960 0.8504 -0.0003 -0.0187 0.0071  473 ARG B NH2 
8021  N N   . ARG B 474 ? 0.5828 0.4681 0.3466 0.0157  0.0902  -0.0138 474 ARG B N   
8022  C CA  . ARG B 474 ? 0.6254 0.5318 0.4184 0.0193  0.1092  -0.0179 474 ARG B CA  
8023  C C   . ARG B 474 ? 0.5774 0.5079 0.4019 0.0147  0.1120  -0.0124 474 ARG B C   
8024  O O   . ARG B 474 ? 0.5365 0.4825 0.3809 0.0133  0.1301  -0.0140 474 ARG B O   
8025  C CB  . ARG B 474 ? 0.6868 0.6042 0.5047 0.0307  0.1051  -0.0228 474 ARG B CB  
8026  C CG  . ARG B 474 ? 0.7837 0.7248 0.6395 0.0372  0.1208  -0.0265 474 ARG B CG  
8027  C CD  . ARG B 474 ? 0.8984 0.8292 0.7404 0.0383  0.1452  -0.0350 474 ARG B CD  
8028  N NE  . ARG B 474 ? 0.9863 0.9449 0.8679 0.0396  0.1631  -0.0357 474 ARG B NE  
8029  C CZ  . ARG B 474 ? 1.0092 0.9920 0.9370 0.0500  0.1636  -0.0374 474 ARG B CZ  
8030  N NH1 . ARG B 474 ? 1.0434 1.0233 0.9794 0.0595  0.1482  -0.0381 474 ARG B NH1 
8031  N NH2 . ARG B 474 ? 0.9721 0.9821 0.9393 0.0505  0.1786  -0.0377 474 ARG B NH2 
8032  N N   . ALA B 475 ? 0.5202 0.4539 0.3502 0.0119  0.0947  -0.0065 475 ALA B N   
8033  C CA  . ALA B 475 ? 0.5515 0.5047 0.4086 0.0065  0.0950  -0.0022 475 ALA B CA  
8034  C C   . ALA B 475 ? 0.5988 0.5420 0.4397 -0.0055 0.1076  0.0017  475 ALA B C   
8035  O O   . ALA B 475 ? 0.5866 0.5466 0.4524 -0.0118 0.1120  0.0046  475 ALA B O   
8036  C CB  . ALA B 475 ? 0.4948 0.4499 0.3580 0.0069  0.0744  0.0012  475 ALA B CB  
8037  N N   . GLN B 476 ? 0.6694 0.5843 0.4678 -0.0100 0.1125  0.0026  476 GLN B N   
8038  C CA  . GLN B 476 ? 0.7148 0.6145 0.4899 -0.0228 0.1236  0.0083  476 GLN B CA  
8039  C C   . GLN B 476 ? 0.7678 0.6663 0.5323 -0.0266 0.1510  0.0045  476 GLN B C   
8040  O O   . GLN B 476 ? 0.8059 0.6875 0.5427 -0.0385 0.1632  0.0095  476 GLN B O   
8041  C CB  . GLN B 476 ? 0.7190 0.5845 0.4497 -0.0268 0.1085  0.0139  476 GLN B CB  
8042  C CG  . GLN B 476 ? 0.6606 0.5280 0.4047 -0.0217 0.0838  0.0162  476 GLN B CG  
8043  C CD  . GLN B 476 ? 0.6680 0.5043 0.3757 -0.0236 0.0673  0.0216  476 GLN B CD  
8044  O OE1 . GLN B 476 ? 0.7515 0.5683 0.4386 -0.0327 0.0663  0.0294  476 GLN B OE1 
8045  N NE2 . GLN B 476 ? 0.6355 0.4663 0.3367 -0.0154 0.0531  0.0184  476 GLN B NE2 
8046  N N   . GLU B 477 ? 0.8337 0.7486 0.6194 -0.0168 0.1618  -0.0042 477 GLU B N   
8047  C CA  . GLU B 477 ? 0.9309 0.8459 0.7100 -0.0181 0.1905  -0.0104 477 GLU B CA  
8048  C C   . GLU B 477 ? 0.9404 0.8936 0.7759 -0.0170 0.2069  -0.0123 477 GLU B C   
8049  O O   . GLU B 477 ? 0.9300 0.9092 0.8097 -0.0093 0.1941  -0.0124 477 GLU B O   
8050  C CB  . GLU B 477 ? 0.9711 0.8730 0.7326 -0.0068 0.1924  -0.0205 477 GLU B CB  
8051  C CG  . GLU B 477 ? 0.9957 0.8694 0.7194 -0.0051 0.1680  -0.0190 477 GLU B CG  
8052  C CD  . GLU B 477 ? 1.0427 0.8897 0.7269 -0.0014 0.1741  -0.0281 477 GLU B CD  
8053  O OE1 . GLU B 477 ? 1.1214 0.9363 0.7527 -0.0101 0.1732  -0.0260 477 GLU B OE1 
8054  O OE2 . GLU B 477 ? 1.0161 0.8716 0.7203 0.0098  0.1783  -0.0372 477 GLU B OE2 
8055  N N   . LYS C 2   ? 1.0219 0.5397 0.3020 0.2739  -0.0662 0.0042  2   LYS C N   
8056  C CA  . LYS C 2   ? 1.0458 0.6041 0.3718 0.2684  -0.0769 -0.0046 2   LYS C CA  
8057  C C   . LYS C 2   ? 0.9872 0.5817 0.3595 0.2551  -0.0783 -0.0027 2   LYS C C   
8058  O O   . LYS C 2   ? 1.0164 0.6122 0.4026 0.2570  -0.0980 -0.0086 2   LYS C O   
8059  C CB  . LYS C 2   ? 1.1426 0.6942 0.4707 0.2807  -0.1077 -0.0208 2   LYS C CB  
8060  C CG  . LYS C 2   ? 1.1587 0.7487 0.5320 0.2750  -0.1165 -0.0302 2   LYS C CG  
8061  C CD  . LYS C 2   ? 1.1604 0.7681 0.5721 0.2751  -0.1444 -0.0438 2   LYS C CD  
8062  C CE  . LYS C 2   ? 1.2302 0.8123 0.6247 0.2908  -0.1697 -0.0579 2   LYS C CE  
8063  N NZ  . LYS C 2   ? 1.1958 0.7967 0.6333 0.2903  -0.1960 -0.0732 2   LYS C NZ  
8064  N N   . LYS C 3   ? 0.9418 0.5649 0.3384 0.2421  -0.0580 0.0048  3   LYS C N   
8065  C CA  . LYS C 3   ? 0.8709 0.5251 0.3064 0.2292  -0.0554 0.0087  3   LYS C CA  
8066  C C   . LYS C 3   ? 0.8455 0.5365 0.3258 0.2244  -0.0698 -0.0012 3   LYS C C   
8067  O O   . LYS C 3   ? 0.8396 0.5381 0.3238 0.2274  -0.0724 -0.0078 3   LYS C O   
8068  C CB  . LYS C 3   ? 0.8519 0.5147 0.2885 0.2175  -0.0241 0.0225  3   LYS C CB  
8069  C CG  . LYS C 3   ? 0.9384 0.5662 0.3330 0.2201  -0.0028 0.0326  3   LYS C CG  
8070  C CD  . LYS C 3   ? 0.9998 0.6134 0.3872 0.2170  -0.0002 0.0402  3   LYS C CD  
8071  C CE  . LYS C 3   ? 1.0932 0.6749 0.4443 0.2163  0.0265  0.0513  3   LYS C CE  
8072  N NZ  . LYS C 3   ? 1.1764 0.7190 0.4913 0.2255  0.0176  0.0530  3   LYS C NZ  
8073  N N   . LEU C 4   ? 0.8647 0.5771 0.3786 0.2170  -0.0784 -0.0021 4   LEU C N   
8074  C CA  . LEU C 4   ? 0.7801 0.5291 0.3384 0.2087  -0.0847 -0.0078 4   LEU C CA  
8075  C C   . LEU C 4   ? 0.7552 0.5236 0.3254 0.1966  -0.0616 0.0041  4   LEU C C   
8076  O O   . LEU C 4   ? 0.7581 0.5190 0.3201 0.1919  -0.0497 0.0144  4   LEU C O   
8077  C CB  . LEU C 4   ? 0.7825 0.5429 0.3726 0.2074  -0.1067 -0.0164 4   LEU C CB  
8078  C CG  . LEU C 4   ? 0.6889 0.4852 0.3272 0.1977  -0.1124 -0.0218 4   LEU C CG  
8079  C CD1 . LEU C 4   ? 0.6659 0.4676 0.3328 0.2007  -0.1372 -0.0370 4   LEU C CD1 
8080  C CD2 . LEU C 4   ? 0.6114 0.4236 0.2666 0.1867  -0.1001 -0.0109 4   LEU C CD2 
8081  N N   . PHE C 5   ? 0.7445 0.5363 0.3334 0.1918  -0.0554 0.0022  5   PHE C N   
8082  C CA  . PHE C 5   ? 0.6728 0.4845 0.2746 0.1812  -0.0341 0.0115  5   PHE C CA  
8083  C C   . PHE C 5   ? 0.6674 0.5114 0.3206 0.1694  -0.0421 0.0075  5   PHE C C   
8084  O O   . PHE C 5   ? 0.6286 0.4878 0.3055 0.1693  -0.0555 -0.0024 5   PHE C O   
8085  C CB  . PHE C 5   ? 0.6625 0.4798 0.2576 0.1822  -0.0190 0.0110  5   PHE C CB  
8086  C CG  . PHE C 5   ? 0.7613 0.5493 0.3177 0.1889  -0.0043 0.0154  5   PHE C CG  
8087  C CD1 . PHE C 5   ? 0.7311 0.5018 0.2688 0.1856  0.0139  0.0263  5   PHE C CD1 
8088  C CD2 . PHE C 5   ? 0.7858 0.5623 0.3251 0.1980  -0.0080 0.0085  5   PHE C CD2 
8089  C CE1 . PHE C 5   ? 0.8221 0.5644 0.3249 0.1909  0.0288  0.0304  5   PHE C CE1 
8090  C CE2 . PHE C 5   ? 0.8545 0.6022 0.3569 0.2042  0.0063  0.0129  5   PHE C CE2 
8091  C CZ  . PHE C 5   ? 0.8920 0.6223 0.3759 0.2005  0.0250  0.0238  5   PHE C CZ  
8092  N N   . LEU C 6   ? 0.6330 0.4859 0.3047 0.1584  -0.0325 0.0149  6   LEU C N   
8093  C CA  . LEU C 6   ? 0.5707 0.4490 0.2877 0.1466  -0.0384 0.0117  6   LEU C CA  
8094  C C   . LEU C 6   ? 0.5036 0.4052 0.2474 0.1327  -0.0194 0.0171  6   LEU C C   
8095  O O   . LEU C 6   ? 0.5186 0.4153 0.2519 0.1290  -0.0013 0.0258  6   LEU C O   
8096  C CB  . LEU C 6   ? 0.5484 0.4159 0.2643 0.1466  -0.0456 0.0143  6   LEU C CB  
8097  C CG  . LEU C 6   ? 0.5612 0.4508 0.3208 0.1355  -0.0518 0.0101  6   LEU C CG  
8098  C CD1 . LEU C 6   ? 0.4937 0.3964 0.2780 0.1370  -0.0680 -0.0025 6   LEU C CD1 
8099  C CD2 . LEU C 6   ? 0.5540 0.4304 0.3100 0.1372  -0.0581 0.0124  6   LEU C CD2 
8100  N N   . VAL C 7   ? 0.4930 0.4182 0.2706 0.1253  -0.0235 0.0114  7   VAL C N   
8101  C CA  . VAL C 7   ? 0.4725 0.4185 0.2744 0.1140  -0.0096 0.0150  7   VAL C CA  
8102  C C   . VAL C 7   ? 0.4618 0.4242 0.2966 0.1031  -0.0153 0.0125  7   VAL C C   
8103  O O   . VAL C 7   ? 0.4872 0.4568 0.3371 0.1027  -0.0260 0.0052  7   VAL C O   
8104  C CB  . VAL C 7   ? 0.4539 0.4085 0.2581 0.1172  -0.0068 0.0111  7   VAL C CB  
8105  C CG1 . VAL C 7   ? 0.4544 0.4296 0.2842 0.1072  0.0059  0.0142  7   VAL C CG1 
8106  C CG2 . VAL C 7   ? 0.5282 0.4631 0.2957 0.1293  -0.0010 0.0122  7   VAL C CG2 
8107  N N   . PHE C 8   ? 0.4468 0.4130 0.2916 0.0942  -0.0071 0.0184  8   PHE C N   
8108  C CA  . PHE C 8   ? 0.4264 0.4066 0.2991 0.0834  -0.0099 0.0164  8   PHE C CA  
8109  C C   . PHE C 8   ? 0.3780 0.3751 0.2681 0.0762  -0.0026 0.0172  8   PHE C C   
8110  O O   . PHE C 8   ? 0.3802 0.3808 0.2688 0.0750  0.0090  0.0218  8   PHE C O   
8111  C CB  . PHE C 8   ? 0.4217 0.3971 0.2972 0.0773  -0.0063 0.0210  8   PHE C CB  
8112  C CG  . PHE C 8   ? 0.4671 0.4275 0.3326 0.0839  -0.0170 0.0186  8   PHE C CG  
8113  C CD1 . PHE C 8   ? 0.4719 0.4369 0.3563 0.0817  -0.0275 0.0113  8   PHE C CD1 
8114  C CD2 . PHE C 8   ? 0.4623 0.4025 0.2994 0.0929  -0.0164 0.0229  8   PHE C CD2 
8115  C CE1 . PHE C 8   ? 0.4607 0.4140 0.3417 0.0884  -0.0387 0.0074  8   PHE C CE1 
8116  C CE2 . PHE C 8   ? 0.5069 0.4323 0.3348 0.1007  -0.0293 0.0199  8   PHE C CE2 
8117  C CZ  . PHE C 8   ? 0.4884 0.4219 0.3409 0.0987  -0.0413 0.0115  8   PHE C CZ  
8118  N N   . TRP C 9   ? 0.3513 0.3575 0.2582 0.0717  -0.0091 0.0124  9   TRP C N   
8119  C CA  . TRP C 9   ? 0.3547 0.3741 0.2766 0.0658  -0.0058 0.0126  9   TRP C CA  
8120  C C   . TRP C 9   ? 0.3445 0.3663 0.2799 0.0570  -0.0098 0.0107  9   TRP C C   
8121  O O   . TRP C 9   ? 0.3379 0.3564 0.2761 0.0571  -0.0164 0.0057  9   TRP C O   
8122  C CB  . TRP C 9   ? 0.3267 0.3490 0.2467 0.0724  -0.0092 0.0086  9   TRP C CB  
8123  C CG  . TRP C 9   ? 0.3039 0.3383 0.2360 0.0703  -0.0058 0.0090  9   TRP C CG  
8124  C CD1 . TRP C 9   ? 0.3276 0.3715 0.2743 0.0629  -0.0021 0.0115  9   TRP C CD1 
8125  C CD2 . TRP C 9   ? 0.2877 0.3255 0.2198 0.0768  -0.0078 0.0057  9   TRP C CD2 
8126  N NE1 . TRP C 9   ? 0.3059 0.3594 0.2628 0.0649  -0.0028 0.0096  9   TRP C NE1 
8127  C CE2 . TRP C 9   ? 0.2840 0.3338 0.2319 0.0734  -0.0056 0.0064  9   TRP C CE2 
8128  C CE3 . TRP C 9   ? 0.3313 0.3625 0.2520 0.0855  -0.0122 0.0014  9   TRP C CE3 
8129  C CZ2 . TRP C 9   ? 0.2964 0.3518 0.2496 0.0790  -0.0074 0.0034  9   TRP C CZ2 
8130  C CZ3 . TRP C 9   ? 0.3875 0.4238 0.3121 0.0903  -0.0127 -0.0013 9   TRP C CZ3 
8131  C CH2 . TRP C 9   ? 0.3728 0.4211 0.3138 0.0873  -0.0101 -0.0001 9   TRP C CH2 
8132  N N   . TRP C 10  ? 0.3058 0.3315 0.2491 0.0491  -0.0049 0.0142  10  TRP C N   
8133  C CA  . TRP C 10  ? 0.3278 0.3522 0.2792 0.0408  -0.0073 0.0126  10  TRP C CA  
8134  C C   . TRP C 10  ? 0.2961 0.3267 0.2542 0.0371  -0.0095 0.0115  10  TRP C C   
8135  O O   . TRP C 10  ? 0.3481 0.3873 0.3133 0.0355  -0.0068 0.0135  10  TRP C O   
8136  C CB  . TRP C 10  ? 0.2845 0.3070 0.2386 0.0348  -0.0022 0.0162  10  TRP C CB  
8137  C CG  . TRP C 10  ? 0.3798 0.3929 0.3252 0.0388  -0.0011 0.0179  10  TRP C CG  
8138  C CD1 . TRP C 10  ? 0.3909 0.3996 0.3278 0.0413  0.0055  0.0232  10  TRP C CD1 
8139  C CD2 . TRP C 10  ? 0.4054 0.4102 0.3497 0.0412  -0.0070 0.0140  10  TRP C CD2 
8140  N NE1 . TRP C 10  ? 0.4105 0.4065 0.3370 0.0461  0.0024  0.0234  10  TRP C NE1 
8141  C CE2 . TRP C 10  ? 0.4106 0.4058 0.3442 0.0463  -0.0062 0.0171  10  TRP C CE2 
8142  C CE3 . TRP C 10  ? 0.3780 0.3816 0.3306 0.0395  -0.0121 0.0076  10  TRP C CE3 
8143  C CZ2 . TRP C 10  ? 0.4298 0.4159 0.3625 0.0510  -0.0134 0.0134  10  TRP C CZ2 
8144  C CZ3 . TRP C 10  ? 0.3599 0.3566 0.3159 0.0428  -0.0168 0.0033  10  TRP C CZ3 
8145  C CH2 . TRP C 10  ? 0.3639 0.3528 0.3108 0.0491  -0.0190 0.0058  10  TRP C CH2 
8146  N N   . HIS C 11  ? 0.3104 0.3353 0.2669 0.0359  -0.0142 0.0079  11  HIS C N   
8147  C CA  . HIS C 11  ? 0.3325 0.3578 0.2891 0.0345  -0.0181 0.0070  11  HIS C CA  
8148  C C   . HIS C 11  ? 0.3065 0.3260 0.2623 0.0262  -0.0187 0.0071  11  HIS C C   
8149  O O   . HIS C 11  ? 0.3583 0.3676 0.3100 0.0218  -0.0165 0.0055  11  HIS C O   
8150  C CB  . HIS C 11  ? 0.3100 0.3275 0.2608 0.0382  -0.0216 0.0036  11  HIS C CB  
8151  C CG  . HIS C 11  ? 0.3754 0.3852 0.3202 0.0363  -0.0257 0.0029  11  HIS C CG  
8152  N ND1 . HIS C 11  ? 0.3576 0.3734 0.3042 0.0392  -0.0307 0.0039  11  HIS C ND1 
8153  C CD2 . HIS C 11  ? 0.3940 0.3880 0.3296 0.0325  -0.0254 0.0011  11  HIS C CD2 
8154  C CE1 . HIS C 11  ? 0.3969 0.3994 0.3326 0.0382  -0.0354 0.0031  11  HIS C CE1 
8155  N NE2 . HIS C 11  ? 0.3896 0.3775 0.3165 0.0338  -0.0310 0.0020  11  HIS C NE2 
8156  N N   . MET C 12  ? 0.3456 0.3709 0.3060 0.0244  -0.0219 0.0079  12  MET C N   
8157  C CA  . MET C 12  ? 0.3208 0.3393 0.2781 0.0176  -0.0246 0.0071  12  MET C CA  
8158  C C   . MET C 12  ? 0.3343 0.3460 0.2832 0.0195  -0.0338 0.0053  12  MET C C   
8159  O O   . MET C 12  ? 0.2960 0.3176 0.2532 0.0249  -0.0391 0.0048  12  MET C O   
8160  C CB  . MET C 12  ? 0.2960 0.3258 0.2675 0.0137  -0.0229 0.0082  12  MET C CB  
8161  C CG  . MET C 12  ? 0.3395 0.3747 0.3172 0.0137  -0.0137 0.0112  12  MET C CG  
8162  S SD  . MET C 12  ? 0.3104 0.3318 0.2785 0.0102  -0.0096 0.0110  12  MET C SD  
8163  C CE  . MET C 12  ? 0.3477 0.3733 0.3228 0.0093  -0.0019 0.0151  12  MET C CE  
8164  N N   . HIS C 13  ? 0.3553 0.3481 0.2867 0.0157  -0.0353 0.0042  13  HIS C N   
8165  C CA  . HIS C 13  ? 0.3176 0.2972 0.2335 0.0189  -0.0442 0.0032  13  HIS C CA  
8166  C C   . HIS C 13  ? 0.3972 0.3530 0.2900 0.0133  -0.0441 0.0023  13  HIS C C   
8167  O O   . HIS C 13  ? 0.3690 0.3160 0.2568 0.0077  -0.0339 0.0021  13  HIS C O   
8168  C CB  . HIS C 13  ? 0.3075 0.2812 0.2168 0.0247  -0.0432 0.0036  13  HIS C CB  
8169  C CG  . HIS C 13  ? 0.3907 0.3417 0.2764 0.0271  -0.0497 0.0034  13  HIS C CG  
8170  N ND1 . HIS C 13  ? 0.3794 0.3282 0.2603 0.0316  -0.0632 0.0026  13  HIS C ND1 
8171  C CD2 . HIS C 13  ? 0.3816 0.3090 0.2466 0.0258  -0.0446 0.0038  13  HIS C CD2 
8172  C CE1 . HIS C 13  ? 0.4157 0.3378 0.2690 0.0339  -0.0671 0.0033  13  HIS C CE1 
8173  N NE2 . HIS C 13  ? 0.4302 0.3382 0.2728 0.0298  -0.0544 0.0044  13  HIS C NE2 
8174  N N   . GLN C 14  ? 0.3991 0.3437 0.2779 0.0153  -0.0559 0.0010  14  GLN C N   
8175  C CA  . GLN C 14  ? 0.4435 0.3573 0.2895 0.0124  -0.0568 0.0004  14  GLN C CA  
8176  C C   . GLN C 14  ? 0.4724 0.3698 0.2980 0.0201  -0.0698 0.0005  14  GLN C C   
8177  O O   . GLN C 14  ? 0.4787 0.3914 0.3195 0.0264  -0.0831 -0.0010 14  GLN C O   
8178  C CB  . GLN C 14  ? 0.4515 0.3616 0.2940 0.0071  -0.0608 -0.0022 14  GLN C CB  
8179  C CG  . GLN C 14  ? 0.4148 0.3359 0.2736 -0.0004 -0.0481 -0.0023 14  GLN C CG  
8180  C CD  . GLN C 14  ? 0.4356 0.3398 0.2809 -0.0049 -0.0328 -0.0017 14  GLN C CD  
8181  O OE1 . GLN C 14  ? 0.4555 0.3328 0.2723 -0.0052 -0.0300 -0.0018 14  GLN C OE1 
8182  N NE2 . GLN C 14  ? 0.4435 0.3618 0.3095 -0.0081 -0.0223 -0.0016 14  GLN C NE2 
8183  N N   . PRO C 15  ? 0.4523 0.3177 0.2442 0.0201  -0.0656 0.0021  15  PRO C N   
8184  C CA  . PRO C 15  ? 0.5357 0.3770 0.2990 0.0277  -0.0798 0.0025  15  PRO C CA  
8185  C C   . PRO C 15  ? 0.5636 0.3962 0.3139 0.0291  -0.0961 -0.0008 15  PRO C C   
8186  O O   . PRO C 15  ? 0.5486 0.3861 0.3043 0.0224  -0.0931 -0.0031 15  PRO C O   
8187  C CB  . PRO C 15  ? 0.5025 0.3067 0.2294 0.0248  -0.0663 0.0054  15  PRO C CB  
8188  C CG  . PRO C 15  ? 0.4574 0.2623 0.1895 0.0143  -0.0483 0.0044  15  PRO C CG  
8189  C CD  . PRO C 15  ? 0.4484 0.2955 0.2263 0.0128  -0.0471 0.0030  15  PRO C CD  
8190  N N   . LEU C 16  ? 0.5974 0.4156 0.3303 0.0384  -0.1149 -0.0018 16  LEU C N   
8191  C CA  . LEU C 16  ? 0.6382 0.4500 0.3627 0.0416  -0.1351 -0.0068 16  LEU C CA  
8192  C C   . LEU C 16  ? 0.6656 0.4352 0.3402 0.0378  -0.1321 -0.0064 16  LEU C C   
8193  O O   . LEU C 16  ? 0.7318 0.4623 0.3616 0.0421  -0.1324 -0.0032 16  LEU C O   
8194  C CB  . LEU C 16  ? 0.6460 0.4559 0.3700 0.0544  -0.1586 -0.0092 16  LEU C CB  
8195  C CG  . LEU C 16  ? 0.6746 0.4784 0.3932 0.0597  -0.1842 -0.0162 16  LEU C CG  
8196  C CD1 . LEU C 16  ? 0.6045 0.4444 0.3676 0.0524  -0.1844 -0.0219 16  LEU C CD1 
8197  C CD2 . LEU C 16  ? 0.6519 0.4579 0.3804 0.0726  -0.2041 -0.0193 16  LEU C CD2 
8198  N N   . TYR C 17  ? 0.5546 0.3291 0.2344 0.0300  -0.1282 -0.0096 17  TYR C N   
8199  C CA  . TYR C 17  ? 0.6799 0.4149 0.3133 0.0258  -0.1229 -0.0101 17  TYR C CA  
8200  C C   . TYR C 17  ? 0.7325 0.4421 0.3341 0.0332  -0.1486 -0.0152 17  TYR C C   
8201  O O   . TYR C 17  ? 0.7001 0.3762 0.2649 0.0308  -0.1434 -0.0158 17  TYR C O   
8202  C CB  . TYR C 17  ? 0.6943 0.4441 0.3468 0.0145  -0.1067 -0.0119 17  TYR C CB  
8203  C CG  . TYR C 17  ? 0.6602 0.4279 0.3373 0.0077  -0.0822 -0.0079 17  TYR C CG  
8204  C CD1 . TYR C 17  ? 0.6231 0.3661 0.2757 0.0058  -0.0644 -0.0039 17  TYR C CD1 
8205  C CD2 . TYR C 17  ? 0.6212 0.4292 0.3463 0.0033  -0.0770 -0.0086 17  TYR C CD2 
8206  C CE1 . TYR C 17  ? 0.5476 0.3081 0.2269 0.0000  -0.0444 -0.0021 17  TYR C CE1 
8207  C CE2 . TYR C 17  ? 0.5293 0.3515 0.2749 -0.0014 -0.0578 -0.0058 17  TYR C CE2 
8208  C CZ  . TYR C 17  ? 0.5382 0.3382 0.2630 -0.0027 -0.0429 -0.0032 17  TYR C CZ  
8209  O OH  . TYR C 17  ? 0.5230 0.3384 0.2722 -0.0067 -0.0264 -0.0023 17  TYR C OH  
8210  N N   . ARG C 18  ? 0.7476 0.4775 0.3754 0.0419  -0.1717 -0.0193 18  ARG C N   
8211  C CA  . ARG C 18  ? 0.7921 0.5128 0.4164 0.0481  -0.1929 -0.0258 18  ARG C CA  
8212  C C   . ARG C 18  ? 0.8432 0.5275 0.4319 0.0581  -0.1981 -0.0228 18  ARG C C   
8213  O O   . ARG C 18  ? 0.8628 0.5562 0.4661 0.0665  -0.2072 -0.0223 18  ARG C O   
8214  C CB  . ARG C 18  ? 0.7587 0.5218 0.4370 0.0517  -0.2128 -0.0331 18  ARG C CB  
8215  C CG  . ARG C 18  ? 0.7906 0.5497 0.4745 0.0569  -0.2351 -0.0419 18  ARG C CG  
8216  C CD  . ARG C 18  ? 0.7135 0.5155 0.4564 0.0609  -0.2515 -0.0492 18  ARG C CD  
8217  N NE  . ARG C 18  ? 0.7031 0.5076 0.4613 0.0635  -0.2717 -0.0594 18  ARG C NE  
8218  C CZ  . ARG C 18  ? 0.7713 0.5554 0.5155 0.0745  -0.2898 -0.0635 18  ARG C CZ  
8219  N NH1 . ARG C 18  ? 0.7913 0.5500 0.5054 0.0835  -0.2896 -0.0579 18  ARG C NH1 
8220  N NH2 . ARG C 18  ? 0.8202 0.6079 0.5811 0.0766  -0.3084 -0.0737 18  ARG C NH2 
8221  N N   . GLU C 19  ? 0.8884 0.5298 0.4299 0.0573  -0.1921 -0.0214 19  GLU C N   
8222  C CA  . GLU C 19  ? 0.8841 0.4844 0.3861 0.0667  -0.1972 -0.0190 19  GLU C CA  
8223  C C   . GLU C 19  ? 0.8433 0.4518 0.3628 0.0786  -0.2268 -0.0261 19  GLU C C   
8224  O O   . GLU C 19  ? 0.8219 0.4444 0.3596 0.0788  -0.2424 -0.0337 19  GLU C O   
8225  C CB  . GLU C 19  ? 1.0108 0.5638 0.4607 0.0636  -0.1863 -0.0174 19  GLU C CB  
8226  C CG  . GLU C 19  ? 1.1413 0.6457 0.5437 0.0699  -0.1808 -0.0125 19  GLU C CG  
8227  C CD  . GLU C 19  ? 1.1961 0.6735 0.5756 0.0824  -0.2061 -0.0173 19  GLU C CD  
8228  O OE1 . GLU C 19  ? 1.1451 0.6427 0.5477 0.0855  -0.2270 -0.0248 19  GLU C OE1 
8229  O OE2 . GLU C 19  ? 1.2966 0.7319 0.6359 0.0893  -0.2051 -0.0141 19  GLU C OE2 
8230  N N   . PRO C 20  ? 0.8720 0.4733 0.3896 0.0885  -0.2352 -0.0248 20  PRO C N   
8231  C CA  . PRO C 20  ? 0.9166 0.5343 0.4626 0.0996  -0.2627 -0.0328 20  PRO C CA  
8232  C C   . PRO C 20  ? 1.0224 0.6042 0.5366 0.1084  -0.2825 -0.0385 20  PRO C C   
8233  O O   . PRO C 20  ? 1.0837 0.6811 0.6257 0.1168  -0.3066 -0.0473 20  PRO C O   
8234  C CB  . PRO C 20  ? 0.9077 0.5260 0.4581 0.1068  -0.2620 -0.0291 20  PRO C CB  
8235  C CG  . PRO C 20  ? 0.9111 0.4898 0.4129 0.1028  -0.2396 -0.0199 20  PRO C CG  
8236  C CD  . PRO C 20  ? 0.8598 0.4409 0.3547 0.0894  -0.2193 -0.0168 20  PRO C CD  
8237  N N   . TYR C 21  ? 1.0227 0.5564 0.4807 0.1070  -0.2731 -0.0346 21  TYR C N   
8238  C CA  . TYR C 21  ? 1.1148 0.6096 0.5372 0.1164  -0.2924 -0.0398 21  TYR C CA  
8239  C C   . TYR C 21  ? 1.1110 0.6133 0.5399 0.1112  -0.2986 -0.0459 21  TYR C C   
8240  O O   . TYR C 21  ? 1.1349 0.6399 0.5759 0.1189  -0.3239 -0.0552 21  TYR C O   
8241  C CB  . TYR C 21  ? 1.1946 0.6281 0.5492 0.1189  -0.2792 -0.0327 21  TYR C CB  
8242  C CG  . TYR C 21  ? 1.2952 0.7138 0.6385 0.1263  -0.2783 -0.0287 21  TYR C CG  
8243  C CD1 . TYR C 21  ? 1.3251 0.7505 0.6861 0.1394  -0.3041 -0.0349 21  TYR C CD1 
8244  C CD2 . TYR C 21  ? 1.3524 0.7514 0.6706 0.1200  -0.2515 -0.0195 21  TYR C CD2 
8245  C CE1 . TYR C 21  ? 1.3456 0.7571 0.6961 0.1464  -0.3037 -0.0317 21  TYR C CE1 
8246  C CE2 . TYR C 21  ? 1.3855 0.7706 0.6939 0.1265  -0.2506 -0.0163 21  TYR C CE2 
8247  C CZ  . TYR C 21  ? 1.3619 0.7530 0.6853 0.1398  -0.2771 -0.0222 21  TYR C CZ  
8248  O OH  . TYR C 21  ? 1.3263 0.7031 0.6394 0.1465  -0.2769 -0.0195 21  TYR C OH  
8249  N N   . THR C 22  ? 1.0490 0.5545 0.4713 0.0984  -0.2759 -0.0415 22  THR C N   
8250  C CA  . THR C 22  ? 1.1004 0.6136 0.5286 0.0919  -0.2786 -0.0470 22  THR C CA  
8251  C C   . THR C 22  ? 1.0430 0.6147 0.5350 0.0841  -0.2812 -0.0522 22  THR C C   
8252  O O   . THR C 22  ? 1.0281 0.6112 0.5342 0.0797  -0.2884 -0.0591 22  THR C O   
8253  C CB  . THR C 22  ? 1.1432 0.6259 0.5291 0.0821  -0.2517 -0.0406 22  THR C CB  
8254  O OG1 . THR C 22  ? 1.0647 0.5751 0.4738 0.0708  -0.2274 -0.0349 22  THR C OG1 
8255  C CG2 . THR C 22  ? 1.1923 0.6155 0.5154 0.0883  -0.2438 -0.0346 22  THR C CG2 
8256  N N   . GLY C 23  ? 1.0089 0.6160 0.5388 0.0821  -0.2750 -0.0494 23  GLY C N   
8257  C CA  . GLY C 23  ? 0.9669 0.6257 0.5540 0.0740  -0.2744 -0.0536 23  GLY C CA  
8258  C C   . GLY C 23  ? 0.9553 0.6196 0.5386 0.0602  -0.2534 -0.0510 23  GLY C C   
8259  O O   . GLY C 23  ? 0.9425 0.6436 0.5684 0.0528  -0.2545 -0.0559 23  GLY C O   
8260  N N   . GLU C 24  ? 0.9613 0.5890 0.4962 0.0563  -0.2331 -0.0439 24  GLU C N   
8261  C CA  . GLU C 24  ? 0.9715 0.5994 0.4995 0.0437  -0.2122 -0.0424 24  GLU C CA  
8262  C C   . GLU C 24  ? 0.9116 0.5602 0.4562 0.0366  -0.1910 -0.0359 24  GLU C C   
8263  O O   . GLU C 24  ? 0.8875 0.5230 0.4164 0.0400  -0.1812 -0.0289 24  GLU C O   
8264  C CB  . GLU C 24  ? 1.0826 0.6601 0.5527 0.0427  -0.1990 -0.0391 24  GLU C CB  
8265  C CG  . GLU C 24  ? 1.2074 0.7621 0.6569 0.0480  -0.2177 -0.0461 24  GLU C CG  
8266  C CD  . GLU C 24  ? 1.2912 0.8350 0.7254 0.0384  -0.2046 -0.0485 24  GLU C CD  
8267  O OE1 . GLU C 24  ? 1.2753 0.8369 0.7248 0.0275  -0.1838 -0.0465 24  GLU C OE1 
8268  O OE2 . GLU C 24  ? 1.3437 0.8598 0.7499 0.0424  -0.2153 -0.0529 24  GLU C OE2 
8269  N N   . TYR C 25  ? 0.8312 0.5102 0.4071 0.0269  -0.1844 -0.0386 25  TYR C N   
8270  C CA  . TYR C 25  ? 0.7584 0.4493 0.3414 0.0193  -0.1619 -0.0329 25  TYR C CA  
8271  C C   . TYR C 25  ? 0.7996 0.4537 0.3396 0.0134  -0.1369 -0.0286 25  TYR C C   
8272  O O   . TYR C 25  ? 0.8652 0.5082 0.3936 0.0071  -0.1306 -0.0325 25  TYR C O   
8273  C CB  . TYR C 25  ? 0.7479 0.4844 0.3880 0.0107  -0.1563 -0.0356 25  TYR C CB  
8274  C CG  . TYR C 25  ? 0.7153 0.4927 0.4066 0.0154  -0.1694 -0.0369 25  TYR C CG  
8275  C CD1 . TYR C 25  ? 0.7416 0.5252 0.4449 0.0225  -0.1982 -0.0451 25  TYR C CD1 
8276  C CD2 . TYR C 25  ? 0.6765 0.4848 0.4040 0.0133  -0.1535 -0.0310 25  TYR C CD2 
8277  C CE1 . TYR C 25  ? 0.7572 0.5783 0.5104 0.0266  -0.2082 -0.0473 25  TYR C CE1 
8278  C CE2 . TYR C 25  ? 0.6538 0.4971 0.4257 0.0177  -0.1632 -0.0324 25  TYR C CE2 
8279  C CZ  . TYR C 25  ? 0.7249 0.5751 0.5110 0.0240  -0.1894 -0.0406 25  TYR C CZ  
8280  O OH  . TYR C 25  ? 0.7269 0.6123 0.5604 0.0283  -0.1973 -0.0431 25  TYR C OH  
8281  N N   . LEU C 26  ? 0.8018 0.4368 0.3206 0.0153  -0.1220 -0.0213 26  LEU C N   
8282  C CA  . LEU C 26  ? 0.8496 0.4464 0.3292 0.0106  -0.0975 -0.0176 26  LEU C CA  
8283  C C   . LEU C 26  ? 0.8496 0.4572 0.3410 -0.0008 -0.0709 -0.0169 26  LEU C C   
8284  O O   . LEU C 26  ? 0.8943 0.4755 0.3622 -0.0066 -0.0491 -0.0163 26  LEU C O   
8285  C CB  . LEU C 26  ? 0.8654 0.4331 0.3177 0.0171  -0.0928 -0.0112 26  LEU C CB  
8286  C CG  . LEU C 26  ? 0.8673 0.4162 0.3016 0.0295  -0.1175 -0.0122 26  LEU C CG  
8287  C CD1 . LEU C 26  ? 0.9176 0.4318 0.3204 0.0346  -0.1091 -0.0062 26  LEU C CD1 
8288  C CD2 . LEU C 26  ? 0.9712 0.4952 0.3793 0.0313  -0.1277 -0.0171 26  LEU C CD2 
8289  N N   . LEU C 27  ? 0.7634 0.4171 0.3093 -0.0035 -0.0689 -0.0161 27  LEU C N   
8290  C CA  . LEU C 27  ? 0.7555 0.4316 0.3349 -0.0130 -0.0457 -0.0159 27  LEU C CA  
8291  C C   . LEU C 27  ? 0.7544 0.4747 0.3851 -0.0152 -0.0552 -0.0189 27  LEU C C   
8292  O O   . LEU C 27  ? 0.7828 0.5256 0.4356 -0.0098 -0.0746 -0.0195 27  LEU C O   
8293  C CB  . LEU C 27  ? 0.7820 0.4674 0.3783 -0.0142 -0.0281 -0.0108 27  LEU C CB  
8294  C CG  . LEU C 27  ? 0.8247 0.4673 0.3783 -0.0161 -0.0085 -0.0082 27  LEU C CG  
8295  C CD1 . LEU C 27  ? 0.7575 0.4142 0.3363 -0.0175 0.0062  -0.0047 27  LEU C CD1 
8296  C CD2 . LEU C 27  ? 0.8261 0.4465 0.3614 -0.0243 0.0116  -0.0118 27  LEU C CD2 
8297  N N   . PRO C 28  ? 0.6748 0.4069 0.3256 -0.0231 -0.0411 -0.0210 28  PRO C N   
8298  C CA  . PRO C 28  ? 0.6412 0.4093 0.3356 -0.0258 -0.0485 -0.0234 28  PRO C CA  
8299  C C   . PRO C 28  ? 0.5607 0.3662 0.3013 -0.0267 -0.0402 -0.0194 28  PRO C C   
8300  O O   . PRO C 28  ? 0.5331 0.3644 0.3068 -0.0297 -0.0417 -0.0205 28  PRO C O   
8301  C CB  . PRO C 28  ? 0.6555 0.4096 0.3403 -0.0330 -0.0372 -0.0277 28  PRO C CB  
8302  C CG  . PRO C 28  ? 0.6390 0.3716 0.3043 -0.0358 -0.0137 -0.0256 28  PRO C CG  
8303  C CD  . PRO C 28  ? 0.6711 0.3814 0.3048 -0.0298 -0.0171 -0.0218 28  PRO C CD  
8304  N N   . TRP C 29  ? 0.5489 0.3560 0.2909 -0.0239 -0.0322 -0.0151 29  TRP C N   
8305  C CA  . TRP C 29  ? 0.5777 0.4146 0.3576 -0.0247 -0.0228 -0.0123 29  TRP C CA  
8306  C C   . TRP C 29  ? 0.5510 0.4209 0.3648 -0.0217 -0.0351 -0.0113 29  TRP C C   
8307  O O   . TRP C 29  ? 0.4681 0.3606 0.3114 -0.0238 -0.0286 -0.0101 29  TRP C O   
8308  C CB  . TRP C 29  ? 0.5662 0.3959 0.3392 -0.0218 -0.0145 -0.0092 29  TRP C CB  
8309  C CG  . TRP C 29  ? 0.6409 0.4389 0.3860 -0.0261 0.0026  -0.0104 29  TRP C CG  
8310  C CD1 . TRP C 29  ? 0.6471 0.4139 0.3568 -0.0243 0.0062  -0.0089 29  TRP C CD1 
8311  C CD2 . TRP C 29  ? 0.6618 0.4549 0.4130 -0.0330 0.0200  -0.0136 29  TRP C CD2 
8312  N NE1 . TRP C 29  ? 0.7116 0.4545 0.4057 -0.0305 0.0270  -0.0110 29  TRP C NE1 
8313  C CE2 . TRP C 29  ? 0.7118 0.4718 0.4329 -0.0357 0.0353  -0.0145 29  TRP C CE2 
8314  C CE3 . TRP C 29  ? 0.6584 0.4708 0.4380 -0.0367 0.0247  -0.0160 29  TRP C CE3 
8315  C CZ2 . TRP C 29  ? 0.7264 0.4745 0.4486 -0.0423 0.0559  -0.0185 29  TRP C CZ2 
8316  C CZ3 . TRP C 29  ? 0.6244 0.4250 0.4044 -0.0423 0.0426  -0.0200 29  TRP C CZ3 
8317  C CH2 . TRP C 29  ? 0.6960 0.4660 0.4495 -0.0452 0.0584  -0.0217 29  TRP C CH2 
8318  N N   . THR C 30  ? 0.5352 0.4072 0.3455 -0.0162 -0.0521 -0.0119 30  THR C N   
8319  C CA  . THR C 30  ? 0.5236 0.4271 0.3695 -0.0140 -0.0611 -0.0120 30  THR C CA  
8320  C C   . THR C 30  ? 0.4950 0.4106 0.3612 -0.0205 -0.0600 -0.0148 30  THR C C   
8321  O O   . THR C 30  ? 0.4418 0.3810 0.3382 -0.0222 -0.0537 -0.0126 30  THR C O   
8322  C CB  . THR C 30  ? 0.5292 0.4318 0.3706 -0.0069 -0.0808 -0.0144 30  THR C CB  
8323  O OG1 . THR C 30  ? 0.5637 0.4584 0.3915 -0.0005 -0.0805 -0.0110 30  THR C OG1 
8324  C CG2 . THR C 30  ? 0.4802 0.4154 0.3625 -0.0058 -0.0886 -0.0164 30  THR C CG2 
8325  N N   . PHE C 31  ? 0.4628 0.3590 0.3095 -0.0240 -0.0654 -0.0194 31  PHE C N   
8326  C CA  . PHE C 31  ? 0.3747 0.2783 0.2382 -0.0307 -0.0642 -0.0228 31  PHE C CA  
8327  C C   . PHE C 31  ? 0.4090 0.3185 0.2844 -0.0355 -0.0455 -0.0194 31  PHE C C   
8328  O O   . PHE C 31  ? 0.3833 0.3122 0.2871 -0.0384 -0.0416 -0.0182 31  PHE C O   
8329  C CB  . PHE C 31  ? 0.4532 0.3290 0.2862 -0.0329 -0.0728 -0.0291 31  PHE C CB  
8330  C CG  . PHE C 31  ? 0.4575 0.3366 0.3045 -0.0403 -0.0706 -0.0332 31  PHE C CG  
8331  C CD1 . PHE C 31  ? 0.4452 0.3408 0.3191 -0.0422 -0.0837 -0.0381 31  PHE C CD1 
8332  C CD2 . PHE C 31  ? 0.4952 0.3611 0.3315 -0.0455 -0.0550 -0.0330 31  PHE C CD2 
8333  C CE1 . PHE C 31  ? 0.4647 0.3621 0.3524 -0.0495 -0.0811 -0.0420 31  PHE C CE1 
8334  C CE2 . PHE C 31  ? 0.4723 0.3397 0.3210 -0.0519 -0.0529 -0.0368 31  PHE C CE2 
8335  C CZ  . PHE C 31  ? 0.4647 0.3470 0.3380 -0.0541 -0.0660 -0.0411 31  PHE C CZ  
8336  N N   . PHE C 32  ? 0.4596 0.3514 0.3142 -0.0360 -0.0334 -0.0181 32  PHE C N   
8337  C CA  . PHE C 32  ? 0.4751 0.3711 0.3426 -0.0397 -0.0179 -0.0168 32  PHE C CA  
8338  C C   . PHE C 32  ? 0.4139 0.3343 0.3088 -0.0365 -0.0136 -0.0118 32  PHE C C   
8339  O O   . PHE C 32  ? 0.4154 0.3465 0.3294 -0.0385 -0.0077 -0.0105 32  PHE C O   
8340  C CB  . PHE C 32  ? 0.5219 0.3944 0.3660 -0.0411 -0.0052 -0.0183 32  PHE C CB  
8341  C CG  . PHE C 32  ? 0.5666 0.4143 0.3865 -0.0457 -0.0031 -0.0235 32  PHE C CG  
8342  C CD1 . PHE C 32  ? 0.5930 0.4450 0.4254 -0.0502 -0.0033 -0.0263 32  PHE C CD1 
8343  C CD2 . PHE C 32  ? 0.6176 0.4348 0.3994 -0.0453 -0.0009 -0.0255 32  PHE C CD2 
8344  C CE1 . PHE C 32  ? 0.6903 0.5183 0.4992 -0.0541 -0.0019 -0.0320 32  PHE C CE1 
8345  C CE2 . PHE C 32  ? 0.6692 0.4603 0.4240 -0.0490 0.0014  -0.0307 32  PHE C CE2 
8346  C CZ  . PHE C 32  ? 0.6829 0.4802 0.4520 -0.0533 0.0005  -0.0344 32  PHE C CZ  
8347  N N   . HIS C 33  ? 0.3703 0.2969 0.2648 -0.0309 -0.0167 -0.0091 33  HIS C N   
8348  C CA  . HIS C 33  ? 0.3615 0.3087 0.2780 -0.0271 -0.0133 -0.0050 33  HIS C CA  
8349  C C   . HIS C 33  ? 0.2756 0.2425 0.2133 -0.0266 -0.0192 -0.0034 33  HIS C C   
8350  O O   . HIS C 33  ? 0.3141 0.2951 0.2679 -0.0243 -0.0142 0.0002  33  HIS C O   
8351  C CB  . HIS C 33  ? 0.2858 0.2319 0.1949 -0.0213 -0.0139 -0.0034 33  HIS C CB  
8352  C CG  . HIS C 33  ? 0.3980 0.3308 0.2984 -0.0222 -0.0033 -0.0047 33  HIS C CG  
8353  N ND1 . HIS C 33  ? 0.3817 0.3219 0.2982 -0.0220 0.0049  -0.0048 33  HIS C ND1 
8354  C CD2 . HIS C 33  ? 0.3474 0.2587 0.2259 -0.0235 0.0011  -0.0067 33  HIS C CD2 
8355  C CE1 . HIS C 33  ? 0.3663 0.2935 0.2767 -0.0234 0.0135  -0.0078 33  HIS C CE1 
8356  N NE2 . HIS C 33  ? 0.3871 0.2959 0.2738 -0.0249 0.0132  -0.0086 33  HIS C NE2 
8357  N N   . ALA C 34  ? 0.3100 0.2768 0.2481 -0.0286 -0.0294 -0.0066 34  ALA C N   
8358  C CA  . ALA C 34  ? 0.3455 0.3317 0.3099 -0.0297 -0.0326 -0.0065 34  ALA C CA  
8359  C C   . ALA C 34  ? 0.4059 0.3933 0.3823 -0.0361 -0.0247 -0.0060 34  ALA C C   
8360  O O   . ALA C 34  ? 0.4277 0.4284 0.4231 -0.0365 -0.0180 -0.0024 34  ALA C O   
8361  C CB  . ALA C 34  ? 0.3450 0.3321 0.3116 -0.0293 -0.0481 -0.0120 34  ALA C CB  
8362  N N   . VAL C 35  ? 0.3849 0.3558 0.3479 -0.0410 -0.0247 -0.0096 35  VAL C N   
8363  C CA  . VAL C 35  ? 0.3935 0.3627 0.3665 -0.0470 -0.0177 -0.0097 35  VAL C CA  
8364  C C   . VAL C 35  ? 0.3980 0.3667 0.3722 -0.0449 -0.0054 -0.0047 35  VAL C C   
8365  O O   . VAL C 35  ? 0.4158 0.3869 0.4020 -0.0474 0.0009  -0.0022 35  VAL C O   
8366  C CB  . VAL C 35  ? 0.3771 0.3269 0.3337 -0.0521 -0.0213 -0.0160 35  VAL C CB  
8367  C CG1 . VAL C 35  ? 0.4054 0.3529 0.3583 -0.0528 -0.0372 -0.0223 35  VAL C CG1 
8368  C CG2 . VAL C 35  ? 0.3762 0.3075 0.3073 -0.0504 -0.0151 -0.0166 35  VAL C CG2 
8369  N N   . LYS C 36  ? 0.4048 0.3688 0.3670 -0.0401 -0.0026 -0.0036 36  LYS C N   
8370  C CA  . LYS C 36  ? 0.3866 0.3500 0.3519 -0.0370 0.0060  -0.0007 36  LYS C CA  
8371  C C   . LYS C 36  ? 0.3673 0.3440 0.3408 -0.0304 0.0068  0.0045  36  LYS C C   
8372  O O   . LYS C 36  ? 0.3629 0.3410 0.3424 -0.0280 0.0116  0.0079  36  LYS C O   
8373  C CB  . LYS C 36  ? 0.4187 0.3689 0.3708 -0.0362 0.0099  -0.0043 36  LYS C CB  
8374  C CG  . LYS C 36  ? 0.3679 0.3165 0.3282 -0.0336 0.0172  -0.0043 36  LYS C CG  
8375  C CD  . LYS C 36  ? 0.4413 0.3780 0.3948 -0.0340 0.0232  -0.0096 36  LYS C CD  
8376  C CE  . LYS C 36  ? 0.4032 0.3432 0.3537 -0.0297 0.0223  -0.0093 36  LYS C CE  
8377  N NZ  . LYS C 36  ? 0.3824 0.3351 0.3472 -0.0226 0.0202  -0.0069 36  LYS C NZ  
8378  N N   . ASP C 37  ? 0.3505 0.3348 0.3221 -0.0266 0.0019  0.0050  37  ASP C N   
8379  C CA  . ASP C 37  ? 0.3589 0.3520 0.3338 -0.0194 0.0034  0.0087  37  ASP C CA  
8380  C C   . ASP C 37  ? 0.4345 0.4416 0.4184 -0.0171 0.0011  0.0112  37  ASP C C   
8381  O O   . ASP C 37  ? 0.3801 0.3931 0.3677 -0.0125 0.0056  0.0152  37  ASP C O   
8382  C CB  . ASP C 37  ? 0.3669 0.3554 0.3326 -0.0153 0.0019  0.0066  37  ASP C CB  
8383  C CG  . ASP C 37  ? 0.3737 0.3492 0.3344 -0.0179 0.0064  0.0028  37  ASP C CG  
8384  O OD1 . ASP C 37  ? 0.3332 0.3074 0.3006 -0.0165 0.0102  0.0029  37  ASP C OD1 
8385  O OD2 . ASP C 37  ? 0.3632 0.3280 0.3125 -0.0210 0.0062  -0.0006 37  ASP C OD2 
8386  N N   . TYR C 38  ? 0.3506 0.3619 0.3374 -0.0192 -0.0059 0.0083  38  TYR C N   
8387  C CA  . TYR C 38  ? 0.3360 0.3619 0.3345 -0.0155 -0.0083 0.0092  38  TYR C CA  
8388  C C   . TYR C 38  ? 0.3254 0.3614 0.3426 -0.0186 -0.0013 0.0114  38  TYR C C   
8389  O O   . TYR C 38  ? 0.3280 0.3747 0.3544 -0.0146 0.0032  0.0137  38  TYR C O   
8390  C CB  . TYR C 38  ? 0.3434 0.3701 0.3411 -0.0154 -0.0201 0.0045  38  TYR C CB  
8391  C CG  . TYR C 38  ? 0.3506 0.3651 0.3273 -0.0112 -0.0246 0.0036  38  TYR C CG  
8392  C CD1 . TYR C 38  ? 0.3458 0.3587 0.3159 -0.0064 -0.0190 0.0062  38  TYR C CD1 
8393  C CD2 . TYR C 38  ? 0.4129 0.4151 0.3752 -0.0121 -0.0342 -0.0002 38  TYR C CD2 
8394  C CE1 . TYR C 38  ? 0.3868 0.3880 0.3409 -0.0038 -0.0212 0.0049  38  TYR C CE1 
8395  C CE2 . TYR C 38  ? 0.4130 0.4002 0.3537 -0.0089 -0.0357 -0.0003 38  TYR C CE2 
8396  C CZ  . TYR C 38  ? 0.4158 0.4033 0.3544 -0.0054 -0.0283 0.0022  38  TYR C CZ  
8397  O OH  . TYR C 38  ? 0.3954 0.3671 0.3152 -0.0034 -0.0280 0.0016  38  TYR C OH  
8398  N N   . TYR C 39  ? 0.3369 0.3683 0.3599 -0.0258 0.0011  0.0106  39  TYR C N   
8399  C CA  . TYR C 39  ? 0.3804 0.4175 0.4200 -0.0297 0.0108  0.0134  39  TYR C CA  
8400  C C   . TYR C 39  ? 0.3690 0.3962 0.3968 -0.0268 0.0214  0.0199  39  TYR C C   
8401  O O   . TYR C 39  ? 0.3317 0.3615 0.3628 -0.0246 0.0312  0.0247  39  TYR C O   
8402  C CB  . TYR C 39  ? 0.4262 0.4615 0.4786 -0.0390 0.0084  0.0091  39  TYR C CB  
8403  C CG  . TYR C 39  ? 0.4300 0.4676 0.4994 -0.0444 0.0209  0.0122  39  TYR C CG  
8404  C CD1 . TYR C 39  ? 0.4125 0.4654 0.5076 -0.0465 0.0256  0.0109  39  TYR C CD1 
8405  C CD2 . TYR C 39  ? 0.4374 0.4607 0.4981 -0.0473 0.0290  0.0162  39  TYR C CD2 
8406  C CE1 . TYR C 39  ? 0.4205 0.4730 0.5310 -0.0524 0.0401  0.0139  39  TYR C CE1 
8407  C CE2 . TYR C 39  ? 0.4647 0.4858 0.5376 -0.0523 0.0417  0.0199  39  TYR C CE2 
8408  C CZ  . TYR C 39  ? 0.4812 0.5164 0.5785 -0.0554 0.0483  0.0189  39  TYR C CZ  
8409  O OH  . TYR C 39  ? 0.5339 0.5647 0.6435 -0.0614 0.0639  0.0227  39  TYR C OH  
8410  N N   . ASP C 40  ? 0.3443 0.3587 0.3571 -0.0260 0.0193  0.0198  40  ASP C N   
8411  C CA  . ASP C 40  ? 0.3414 0.3442 0.3446 -0.0231 0.0261  0.0246  40  ASP C CA  
8412  C C   . ASP C 40  ? 0.3778 0.3798 0.3692 -0.0131 0.0274  0.0282  40  ASP C C   
8413  O O   . ASP C 40  ? 0.3615 0.3545 0.3445 -0.0093 0.0338  0.0335  40  ASP C O   
8414  C CB  . ASP C 40  ? 0.3591 0.3501 0.3554 -0.0250 0.0229  0.0213  40  ASP C CB  
8415  C CG  . ASP C 40  ? 0.4414 0.4266 0.4453 -0.0336 0.0255  0.0199  40  ASP C CG  
8416  O OD1 . ASP C 40  ? 0.4127 0.3924 0.4190 -0.0347 0.0332  0.0248  40  ASP C OD1 
8417  O OD2 . ASP C 40  ? 0.4110 0.3951 0.4166 -0.0392 0.0202  0.0142  40  ASP C OD2 
8418  N N   . MET C 41  ? 0.3554 0.3642 0.3438 -0.0084 0.0211  0.0255  41  MET C N   
8419  C CA  . MET C 41  ? 0.3605 0.3680 0.3378 0.0012  0.0212  0.0278  41  MET C CA  
8420  C C   . MET C 41  ? 0.3722 0.3832 0.3493 0.0040  0.0297  0.0326  41  MET C C   
8421  O O   . MET C 41  ? 0.4283 0.4284 0.3907 0.0103  0.0340  0.0370  41  MET C O   
8422  C CB  . MET C 41  ? 0.3436 0.3562 0.3189 0.0048  0.0133  0.0233  41  MET C CB  
8423  C CG  . MET C 41  ? 0.3222 0.3265 0.2942 0.0041  0.0089  0.0191  41  MET C CG  
8424  S SD  . MET C 41  ? 0.3500 0.3450 0.3143 0.0131  0.0074  0.0194  41  MET C SD  
8425  C CE  . MET C 41  ? 0.3181 0.3192 0.2778 0.0211  0.0025  0.0174  41  MET C CE  
8426  N N   . PRO C 42  ? 0.3336 0.3577 0.3258 0.0002  0.0327  0.0317  42  PRO C N   
8427  C CA  . PRO C 42  ? 0.3240 0.3499 0.3188 0.0014  0.0453  0.0361  42  PRO C CA  
8428  C C   . PRO C 42  ? 0.3887 0.4039 0.3843 -0.0044 0.0566  0.0408  42  PRO C C   
8429  O O   . PRO C 42  ? 0.4294 0.4363 0.4156 -0.0016 0.0693  0.0463  42  PRO C O   
8430  C CB  . PRO C 42  ? 0.2954 0.3403 0.3136 -0.0019 0.0442  0.0316  42  PRO C CB  
8431  C CG  . PRO C 42  ? 0.2937 0.3427 0.3206 -0.0074 0.0312  0.0259  42  PRO C CG  
8432  C CD  . PRO C 42  ? 0.2853 0.3217 0.2918 -0.0038 0.0245  0.0260  42  PRO C CD  
8433  N N   . ALA C 43  ? 0.4255 0.4379 0.4292 -0.0121 0.0533  0.0389  43  ALA C N   
8434  C CA  . ALA C 43  ? 0.4211 0.4211 0.4252 -0.0178 0.0638  0.0433  43  ALA C CA  
8435  C C   . ALA C 43  ? 0.4613 0.4395 0.4379 -0.0101 0.0677  0.0499  43  ALA C C   
8436  O O   . ALA C 43  ? 0.4315 0.3952 0.4023 -0.0125 0.0796  0.0557  43  ALA C O   
8437  C CB  . ALA C 43  ? 0.4127 0.4120 0.4284 -0.0266 0.0576  0.0389  43  ALA C CB  
8438  N N   . TYR C 44  ? 0.5074 0.4811 0.4672 -0.0006 0.0575  0.0488  44  TYR C N   
8439  C CA  . TYR C 44  ? 0.4654 0.4177 0.3987 0.0088  0.0581  0.0540  44  TYR C CA  
8440  C C   . TYR C 44  ? 0.5238 0.4650 0.4406 0.0129  0.0719  0.0611  44  TYR C C   
8441  O O   . TYR C 44  ? 0.5522 0.4695 0.4453 0.0179  0.0771  0.0675  44  TYR C O   
8442  C CB  . TYR C 44  ? 0.4170 0.3696 0.3401 0.0188  0.0442  0.0498  44  TYR C CB  
8443  C CG  . TYR C 44  ? 0.4412 0.3932 0.3721 0.0173  0.0337  0.0443  44  TYR C CG  
8444  C CD1 . TYR C 44  ? 0.4488 0.3832 0.3693 0.0222  0.0303  0.0457  44  TYR C CD1 
8445  C CD2 . TYR C 44  ? 0.4187 0.3857 0.3664 0.0118  0.0278  0.0376  44  TYR C CD2 
8446  C CE1 . TYR C 44  ? 0.4362 0.3710 0.3675 0.0210  0.0223  0.0396  44  TYR C CE1 
8447  C CE2 . TYR C 44  ? 0.3905 0.3551 0.3448 0.0101  0.0215  0.0322  44  TYR C CE2 
8448  C CZ  . TYR C 44  ? 0.4203 0.3701 0.3685 0.0145  0.0193  0.0328  44  TYR C CZ  
8449  O OH  . TYR C 44  ? 0.4341 0.3821 0.3923 0.0130  0.0147  0.0265  44  TYR C OH  
8450  N N   . LEU C 45  ? 0.4517 0.4076 0.3788 0.0115  0.0786  0.0600  45  LEU C N   
8451  C CA  . LEU C 45  ? 0.4592 0.4039 0.3705 0.0151  0.0949  0.0661  45  LEU C CA  
8452  C C   . LEU C 45  ? 0.5915 0.5232 0.5055 0.0068  0.1129  0.0722  45  LEU C C   
8453  O O   . LEU C 45  ? 0.6300 0.5420 0.5213 0.0105  0.1286  0.0792  45  LEU C O   
8454  C CB  . LEU C 45  ? 0.4291 0.3951 0.3573 0.0149  0.0988  0.0621  45  LEU C CB  
8455  C CG  . LEU C 45  ? 0.4282 0.4018 0.3482 0.0244  0.0832  0.0572  45  LEU C CG  
8456  C CD1 . LEU C 45  ? 0.4273 0.4239 0.3692 0.0232  0.0840  0.0521  45  LEU C CD1 
8457  C CD2 . LEU C 45  ? 0.4687 0.4197 0.3506 0.0375  0.0827  0.0611  45  LEU C CD2 
8458  N N   . LYS C 46  ? 0.5955 0.5353 0.5348 -0.0045 0.1119  0.0696  46  LYS C N   
8459  C CA  . LYS C 46  ? 0.6646 0.5900 0.6076 -0.0130 0.1288  0.0749  46  LYS C CA  
8460  C C   . LYS C 46  ? 0.6831 0.5742 0.5893 -0.0061 0.1308  0.0831  46  LYS C C   
8461  O O   . LYS C 46  ? 0.7299 0.5993 0.6237 -0.0089 0.1491  0.0906  46  LYS C O   
8462  C CB  . LYS C 46  ? 0.6928 0.6332 0.6701 -0.0259 0.1242  0.0688  46  LYS C CB  
8463  C CG  . LYS C 46  ? 0.6895 0.6605 0.7039 -0.0329 0.1217  0.0604  46  LYS C CG  
8464  C CD  . LYS C 46  ? 0.6976 0.6746 0.7447 -0.0468 0.1328  0.0579  46  LYS C CD  
8465  C CE  . LYS C 46  ? 0.7028 0.7083 0.7866 -0.0531 0.1199  0.0469  46  LYS C CE  
8466  N NZ  . LYS C 46  ? 0.7014 0.7063 0.8006 -0.0625 0.1119  0.0419  46  LYS C NZ  
8467  N N   . ASP C 47  ? 0.6587 0.5432 0.5481 0.0030  0.1125  0.0815  47  ASP C N   
8468  C CA  . ASP C 47  ? 0.6756 0.5284 0.5332 0.0112  0.1096  0.0876  47  ASP C CA  
8469  C C   . ASP C 47  ? 0.6833 0.5181 0.5032 0.0275  0.1024  0.0904  47  ASP C C   
8470  O O   . ASP C 47  ? 0.7209 0.5246 0.5089 0.0363  0.1006  0.0963  47  ASP C O   
8471  C CB  . ASP C 47  ? 0.6667 0.5233 0.5367 0.0099  0.0934  0.0821  47  ASP C CB  
8472  C CG  . ASP C 47  ? 0.6611 0.5311 0.5633 -0.0052 0.0983  0.0786  47  ASP C CG  
8473  O OD1 . ASP C 47  ? 0.6377 0.5073 0.5506 -0.0144 0.1150  0.0818  47  ASP C OD1 
8474  O OD2 . ASP C 47  ? 0.6620 0.5417 0.5791 -0.0077 0.0858  0.0719  47  ASP C OD2 
8475  N N   . PHE C 48  ? 0.5952 0.4468 0.4171 0.0326  0.0965  0.0858  48  PHE C N   
8476  C CA  . PHE C 48  ? 0.5746 0.4107 0.3627 0.0483  0.0870  0.0865  48  PHE C CA  
8477  C C   . PHE C 48  ? 0.6407 0.4826 0.4222 0.0499  0.0994  0.0875  48  PHE C C   
8478  O O   . PHE C 48  ? 0.6408 0.5121 0.4515 0.0440  0.0990  0.0815  48  PHE C O   
8479  C CB  . PHE C 48  ? 0.6179 0.4687 0.4168 0.0544  0.0634  0.0773  48  PHE C CB  
8480  C CG  . PHE C 48  ? 0.6488 0.4945 0.4564 0.0537  0.0520  0.0748  48  PHE C CG  
8481  C CD1 . PHE C 48  ? 0.6709 0.4886 0.4508 0.0658  0.0423  0.0773  48  PHE C CD1 
8482  C CD2 . PHE C 48  ? 0.5938 0.4608 0.4359 0.0418  0.0506  0.0696  48  PHE C CD2 
8483  C CE1 . PHE C 48  ? 0.6961 0.5099 0.4874 0.0657  0.0321  0.0742  48  PHE C CE1 
8484  C CE2 . PHE C 48  ? 0.6025 0.4643 0.4529 0.0412  0.0418  0.0667  48  PHE C CE2 
8485  C CZ  . PHE C 48  ? 0.6637 0.5000 0.4909 0.0531  0.0329  0.0688  48  PHE C CZ  
8486  N N   . GLU C 49  ? 0.7398 0.5513 0.4811 0.0584  0.1106  0.0950  49  GLU C N   
8487  C CA  . GLU C 49  ? 0.8160 0.6285 0.5487 0.0593  0.1277  0.0968  49  GLU C CA  
8488  C C   . GLU C 49  ? 0.7813 0.5946 0.4943 0.0731  0.1131  0.0916  49  GLU C C   
8489  O O   . GLU C 49  ? 0.8581 0.6445 0.5291 0.0844  0.1182  0.0956  49  GLU C O   
8490  C CB  . GLU C 49  ? 0.9386 0.7144 0.6357 0.0603  0.1514  0.1077  49  GLU C CB  
8491  C CG  . GLU C 49  ? 1.0540 0.8337 0.7545 0.0558  0.1772  0.1095  49  GLU C CG  
8492  C CD  . GLU C 49  ? 1.2396 0.9782 0.8825 0.0684  0.1888  0.1167  49  GLU C CD  
8493  O OE1 . GLU C 49  ? 1.3308 1.0469 0.9372 0.0826  0.1683  0.1163  49  GLU C OE1 
8494  O OE2 . GLU C 49  ? 1.2869 1.0217 0.9333 0.0632  0.2117  0.1174  49  GLU C OE2 
8495  N N   . ILE C 50  ? 0.7041 0.5467 0.4469 0.0719  0.0946  0.0824  50  ILE C N   
8496  C CA  . ILE C 50  ? 0.6766 0.5262 0.4113 0.0821  0.0813  0.0758  50  ILE C CA  
8497  C C   . ILE C 50  ? 0.6468 0.5291 0.4166 0.0741  0.0875  0.0707  50  ILE C C   
8498  O O   . ILE C 50  ? 0.5819 0.4808 0.3815 0.0616  0.1002  0.0717  50  ILE C O   
8499  C CB  . ILE C 50  ? 0.6571 0.5115 0.3977 0.0880  0.0549  0.0685  50  ILE C CB  
8500  C CG1 . ILE C 50  ? 0.6533 0.5327 0.4360 0.0750  0.0506  0.0648  50  ILE C CG1 
8501  C CG2 . ILE C 50  ? 0.7027 0.5239 0.4067 0.1002  0.0444  0.0715  50  ILE C CG2 
8502  C CD1 . ILE C 50  ? 0.6136 0.5049 0.4117 0.0781  0.0294  0.0558  50  ILE C CD1 
8503  N N   . LYS C 51  ? 0.6097 0.5017 0.3781 0.0815  0.0765  0.0643  51  LYS C N   
8504  C CA  . LYS C 51  ? 0.5287 0.4502 0.3291 0.0759  0.0782  0.0586  51  LYS C CA  
8505  C C   . LYS C 51  ? 0.5128 0.4536 0.3374 0.0737  0.0579  0.0510  51  LYS C C   
8506  O O   . LYS C 51  ? 0.5028 0.4353 0.3142 0.0819  0.0418  0.0472  51  LYS C O   
8507  C CB  . LYS C 51  ? 0.4671 0.3842 0.2487 0.0855  0.0834  0.0568  51  LYS C CB  
8508  C CG  . LYS C 51  ? 0.5383 0.4281 0.2849 0.0902  0.1040  0.0642  51  LYS C CG  
8509  C CD  . LYS C 51  ? 0.5183 0.4180 0.2884 0.0786  0.1292  0.0681  51  LYS C CD  
8510  C CE  . LYS C 51  ? 0.5555 0.4266 0.2877 0.0849  0.1527  0.0743  51  LYS C CE  
8511  N NZ  . LYS C 51  ? 0.6327 0.5089 0.3865 0.0736  0.1814  0.0780  51  LYS C NZ  
8512  N N   . LEU C 52  ? 0.4459 0.4106 0.3055 0.0628  0.0591  0.0483  52  LEU C N   
8513  C CA  . LEU C 52  ? 0.4536 0.4349 0.3349 0.0593  0.0437  0.0417  52  LEU C CA  
8514  C C   . LEU C 52  ? 0.4038 0.4071 0.3097 0.0549  0.0464  0.0382  52  LEU C C   
8515  O O   . LEU C 52  ? 0.4342 0.4461 0.3557 0.0486  0.0587  0.0402  52  LEU C O   
8516  C CB  . LEU C 52  ? 0.4730 0.4554 0.3681 0.0505  0.0398  0.0422  52  LEU C CB  
8517  C CG  . LEU C 52  ? 0.5170 0.4787 0.3936 0.0541  0.0361  0.0452  52  LEU C CG  
8518  C CD1 . LEU C 52  ? 0.5005 0.4651 0.3944 0.0438  0.0366  0.0457  52  LEU C CD1 
8519  C CD2 . LEU C 52  ? 0.4898 0.4451 0.3562 0.0636  0.0198  0.0397  52  LEU C CD2 
8520  N N   . ASN C 53  ? 0.3303 0.3418 0.2409 0.0584  0.0349  0.0324  53  ASN C N   
8521  C CA  . ASN C 53  ? 0.3408 0.3705 0.2722 0.0561  0.0348  0.0288  53  ASN C CA  
8522  C C   . ASN C 53  ? 0.3431 0.3814 0.2909 0.0496  0.0232  0.0250  53  ASN C C   
8523  O O   . ASN C 53  ? 0.3603 0.3909 0.3022 0.0486  0.0154  0.0239  53  ASN C O   
8524  C CB  . ASN C 53  ? 0.3171 0.3460 0.2376 0.0662  0.0324  0.0255  53  ASN C CB  
8525  C CG  . ASN C 53  ? 0.4130 0.4263 0.3074 0.0743  0.0426  0.0289  53  ASN C CG  
8526  O OD1 . ASN C 53  ? 0.4679 0.4826 0.3644 0.0733  0.0584  0.0319  53  ASN C OD1 
8527  N ND2 . ASN C 53  ? 0.3866 0.3830 0.2559 0.0823  0.0339  0.0281  53  ASN C ND2 
8528  N N   . PHE C 54  ? 0.3181 0.3710 0.2860 0.0458  0.0222  0.0225  54  PHE C N   
8529  C CA  . PHE C 54  ? 0.3661 0.4235 0.3454 0.0395  0.0123  0.0195  54  PHE C CA  
8530  C C   . PHE C 54  ? 0.3557 0.4227 0.3450 0.0423  0.0056  0.0154  54  PHE C C   
8531  O O   . PHE C 54  ? 0.4181 0.4957 0.4195 0.0452  0.0106  0.0145  54  PHE C O   
8532  C CB  . PHE C 54  ? 0.3698 0.4314 0.3636 0.0299  0.0159  0.0209  54  PHE C CB  
8533  C CG  . PHE C 54  ? 0.3682 0.4185 0.3523 0.0269  0.0220  0.0250  54  PHE C CG  
8534  C CD1 . PHE C 54  ? 0.3720 0.4182 0.3519 0.0280  0.0348  0.0297  54  PHE C CD1 
8535  C CD2 . PHE C 54  ? 0.3652 0.4066 0.3431 0.0235  0.0158  0.0243  54  PHE C CD2 
8536  C CE1 . PHE C 54  ? 0.4062 0.4383 0.3740 0.0263  0.0394  0.0340  54  PHE C CE1 
8537  C CE2 . PHE C 54  ? 0.3729 0.4033 0.3429 0.0219  0.0201  0.0276  54  PHE C CE2 
8538  C CZ  . PHE C 54  ? 0.4107 0.4357 0.3745 0.0237  0.0310  0.0327  54  PHE C CZ  
8539  N N   . ASN C 55  ? 0.3759 0.4376 0.3603 0.0418  -0.0048 0.0128  55  ASN C N   
8540  C CA  . ASN C 55  ? 0.3578 0.4240 0.3489 0.0437  -0.0133 0.0094  55  ASN C CA  
8541  C C   . ASN C 55  ? 0.3794 0.4442 0.3759 0.0364  -0.0199 0.0083  55  ASN C C   
8542  O O   . ASN C 55  ? 0.3588 0.4129 0.3455 0.0309  -0.0205 0.0091  55  ASN C O   
8543  C CB  . ASN C 55  ? 0.3564 0.4125 0.3335 0.0487  -0.0194 0.0074  55  ASN C CB  
8544  C CG  . ASN C 55  ? 0.3923 0.4503 0.3731 0.0530  -0.0275 0.0046  55  ASN C CG  
8545  O OD1 . ASN C 55  ? 0.3872 0.4562 0.3791 0.0586  -0.0262 0.0033  55  ASN C OD1 
8546  N ND2 . ASN C 55  ? 0.3413 0.3868 0.3121 0.0508  -0.0352 0.0037  55  ASN C ND2 
8547  N N   . LEU C 56  ? 0.3432 0.4183 0.3558 0.0368  -0.0252 0.0056  56  LEU C N   
8548  C CA  . LEU C 56  ? 0.3751 0.4474 0.3910 0.0321  -0.0355 0.0030  56  LEU C CA  
8549  C C   . LEU C 56  ? 0.3629 0.4325 0.3762 0.0387  -0.0481 -0.0003 56  LEU C C   
8550  O O   . LEU C 56  ? 0.3773 0.4606 0.4088 0.0444  -0.0502 -0.0030 56  LEU C O   
8551  C CB  . LEU C 56  ? 0.3842 0.4711 0.4255 0.0271  -0.0333 0.0011  56  LEU C CB  
8552  C CG  . LEU C 56  ? 0.3646 0.4530 0.4105 0.0201  -0.0209 0.0044  56  LEU C CG  
8553  C CD1 . LEU C 56  ? 0.3248 0.4287 0.4012 0.0155  -0.0194 0.0010  56  LEU C CD1 
8554  C CD2 . LEU C 56  ? 0.4143 0.4866 0.4416 0.0143  -0.0231 0.0059  56  LEU C CD2 
8555  N N   . THR C 57  ? 0.3219 0.3722 0.3122 0.0384  -0.0555 -0.0001 57  THR C N   
8556  C CA  . THR C 57  ? 0.3766 0.4189 0.3593 0.0451  -0.0684 -0.0025 57  THR C CA  
8557  C C   . THR C 57  ? 0.3978 0.4464 0.3948 0.0452  -0.0814 -0.0070 57  THR C C   
8558  O O   . THR C 57  ? 0.3234 0.3720 0.3238 0.0381  -0.0821 -0.0079 57  THR C O   
8559  C CB  . THR C 57  ? 0.3891 0.4042 0.3400 0.0441  -0.0710 -0.0008 57  THR C CB  
8560  O OG1 . THR C 57  ? 0.4080 0.4110 0.3470 0.0366  -0.0724 -0.0008 57  THR C OG1 
8561  C CG2 . THR C 57  ? 0.3804 0.3906 0.3229 0.0436  -0.0594 0.0017  57  THR C CG2 
8562  N N   . PRO C 58  ? 0.4488 0.5028 0.4562 0.0537  -0.0929 -0.0107 58  PRO C N   
8563  C CA  . PRO C 58  ? 0.4464 0.5083 0.4727 0.0550  -0.1081 -0.0169 58  PRO C CA  
8564  C C   . PRO C 58  ? 0.4458 0.4838 0.4451 0.0523  -0.1210 -0.0178 58  PRO C C   
8565  O O   . PRO C 58  ? 0.4776 0.5213 0.4910 0.0492  -0.1304 -0.0228 58  PRO C O   
8566  C CB  . PRO C 58  ? 0.4410 0.5090 0.4791 0.0667  -0.1187 -0.0208 58  PRO C CB  
8567  C CG  . PRO C 58  ? 0.4513 0.5238 0.4873 0.0697  -0.1036 -0.0168 58  PRO C CG  
8568  C CD  . PRO C 58  ? 0.4483 0.5024 0.4539 0.0629  -0.0933 -0.0106 58  PRO C CD  
8569  N N   . VAL C 59  ? 0.4506 0.4602 0.4108 0.0531  -0.1210 -0.0135 59  VAL C N   
8570  C CA  . VAL C 59  ? 0.3984 0.3804 0.3268 0.0507  -0.1309 -0.0140 59  VAL C CA  
8571  C C   . VAL C 59  ? 0.3915 0.3750 0.3209 0.0394  -0.1208 -0.0134 59  VAL C C   
8572  O O   . VAL C 59  ? 0.4317 0.4030 0.3498 0.0367  -0.1307 -0.0167 59  VAL C O   
8573  C CB  . VAL C 59  ? 0.3847 0.3331 0.2705 0.0537  -0.1295 -0.0094 59  VAL C CB  
8574  C CG1 . VAL C 59  ? 0.3530 0.3015 0.2350 0.0484  -0.1088 -0.0044 59  VAL C CG1 
8575  C CG2 . VAL C 59  ? 0.4258 0.3401 0.2720 0.0515  -0.1375 -0.0096 59  VAL C CG2 
8576  N N   . LEU C 60  ? 0.3402 0.3372 0.2823 0.0337  -0.1025 -0.0097 60  LEU C N   
8577  C CA  . LEU C 60  ? 0.3504 0.3507 0.2978 0.0239  -0.0938 -0.0094 60  LEU C CA  
8578  C C   . LEU C 60  ? 0.3730 0.3957 0.3545 0.0215  -0.0993 -0.0144 60  LEU C C   
8579  O O   . LEU C 60  ? 0.4170 0.4353 0.3984 0.0153  -0.1029 -0.0173 60  LEU C O   
8580  C CB  . LEU C 60  ? 0.3400 0.3469 0.2912 0.0201  -0.0750 -0.0046 60  LEU C CB  
8581  C CG  . LEU C 60  ? 0.2869 0.3008 0.2495 0.0114  -0.0653 -0.0039 60  LEU C CG  
8582  C CD1 . LEU C 60  ? 0.3811 0.3726 0.3199 0.0058  -0.0680 -0.0054 60  LEU C CD1 
8583  C CD2 . LEU C 60  ? 0.2600 0.2798 0.2264 0.0101  -0.0499 0.0004  60  LEU C CD2 
8584  N N   . ILE C 61  ? 0.3790 0.4254 0.3915 0.0261  -0.0989 -0.0161 61  ILE C N   
8585  C CA  . ILE C 61  ? 0.3909 0.4603 0.4421 0.0232  -0.1016 -0.0217 61  ILE C CA  
8586  C C   . ILE C 61  ? 0.3986 0.4613 0.4510 0.0247  -0.1237 -0.0295 61  ILE C C   
8587  O O   . ILE C 61  ? 0.4173 0.4877 0.4893 0.0182  -0.1268 -0.0345 61  ILE C O   
8588  C CB  . ILE C 61  ? 0.3618 0.4553 0.4447 0.0290  -0.0963 -0.0229 61  ILE C CB  
8589  C CG1 . ILE C 61  ? 0.3352 0.4334 0.4152 0.0272  -0.0747 -0.0158 61  ILE C CG1 
8590  C CG2 . ILE C 61  ? 0.3676 0.4844 0.4950 0.0264  -0.1000 -0.0307 61  ILE C CG2 
8591  C CD1 . ILE C 61  ? 0.3310 0.4496 0.4371 0.0328  -0.0661 -0.0168 61  ILE C CD1 
8592  N N   . ASP C 62  ? 0.4220 0.4689 0.4531 0.0338  -0.1403 -0.0313 62  ASP C N   
8593  C CA  . ASP C 62  ? 0.5018 0.5367 0.5265 0.0373  -0.1645 -0.0390 62  ASP C CA  
8594  C C   . ASP C 62  ? 0.5726 0.5877 0.5727 0.0290  -0.1648 -0.0392 62  ASP C C   
8595  O O   . ASP C 62  ? 0.5682 0.5887 0.5855 0.0256  -0.1764 -0.0470 62  ASP C O   
8596  C CB  . ASP C 62  ? 0.5470 0.5576 0.5382 0.0488  -0.1803 -0.0384 62  ASP C CB  
8597  C CG  . ASP C 62  ? 0.5559 0.5856 0.5758 0.0591  -0.1876 -0.0417 62  ASP C CG  
8598  O OD1 . ASP C 62  ? 0.5493 0.6108 0.6185 0.0583  -0.1870 -0.0478 62  ASP C OD1 
8599  O OD2 . ASP C 62  ? 0.5727 0.5846 0.5664 0.0680  -0.1930 -0.0384 62  ASP C OD2 
8600  N N   . GLN C 63  ? 0.5696 0.5618 0.5313 0.0254  -0.1518 -0.0318 63  GLN C N   
8601  C CA  . GLN C 63  ? 0.5875 0.5574 0.5219 0.0184  -0.1510 -0.0323 63  GLN C CA  
8602  C C   . GLN C 63  ? 0.5388 0.5284 0.5041 0.0082  -0.1411 -0.0343 63  GLN C C   
8603  O O   . GLN C 63  ? 0.4685 0.4504 0.4315 0.0038  -0.1502 -0.0401 63  GLN C O   
8604  C CB  . GLN C 63  ? 0.5321 0.4764 0.4262 0.0164  -0.1358 -0.0247 63  GLN C CB  
8605  C CG  . GLN C 63  ? 0.5869 0.5056 0.4457 0.0251  -0.1436 -0.0225 63  GLN C CG  
8606  C CD  . GLN C 63  ? 0.5986 0.4951 0.4257 0.0216  -0.1251 -0.0157 63  GLN C CD  
8607  O OE1 . GLN C 63  ? 0.5475 0.4213 0.3478 0.0158  -0.1184 -0.0155 63  GLN C OE1 
8608  N NE2 . GLN C 63  ? 0.4990 0.4024 0.3318 0.0249  -0.1160 -0.0112 63  GLN C NE2 
8609  N N   . ILE C 64  ? 0.5064 0.5186 0.4981 0.0046  -0.1227 -0.0295 64  ILE C N   
8610  C CA  . ILE C 64  ? 0.4859 0.5144 0.5060 -0.0046 -0.1121 -0.0305 64  ILE C CA  
8611  C C   . ILE C 64  ? 0.4462 0.4908 0.5014 -0.0058 -0.1268 -0.0402 64  ILE C C   
8612  O O   . ILE C 64  ? 0.3667 0.4097 0.4299 -0.0132 -0.1287 -0.0446 64  ILE C O   
8613  C CB  . ILE C 64  ? 0.4381 0.4851 0.4771 -0.0060 -0.0915 -0.0236 64  ILE C CB  
8614  C CG1 . ILE C 64  ? 0.3983 0.4289 0.4063 -0.0064 -0.0784 -0.0161 64  ILE C CG1 
8615  C CG2 . ILE C 64  ? 0.3954 0.4581 0.4650 -0.0145 -0.0808 -0.0244 64  ILE C CG2 
8616  C CD1 . ILE C 64  ? 0.3149 0.3590 0.3348 -0.0057 -0.0613 -0.0099 64  ILE C CD1 
8617  N N   . GLN C 65  ? 0.4717 0.5316 0.5501 0.0018  -0.1384 -0.0448 65  GLN C N   
8618  C CA  . GLN C 65  ? 0.4808 0.5583 0.5994 0.0013  -0.1539 -0.0561 65  GLN C CA  
8619  C C   . GLN C 65  ? 0.4612 0.5167 0.5578 0.0022  -0.1776 -0.0641 65  GLN C C   
8620  O O   . GLN C 65  ? 0.4333 0.4974 0.5569 -0.0033 -0.1863 -0.0731 65  GLN C O   
8621  C CB  . GLN C 65  ? 0.5500 0.6466 0.6970 0.0111  -0.1632 -0.0604 65  GLN C CB  
8622  C CG  . GLN C 65  ? 0.5915 0.7157 0.7754 0.0091  -0.1414 -0.0570 65  GLN C CG  
8623  C CD  . GLN C 65  ? 0.6058 0.7454 0.8122 0.0200  -0.1497 -0.0611 65  GLN C CD  
8624  O OE1 . GLN C 65  ? 0.6213 0.7451 0.7981 0.0299  -0.1623 -0.0595 65  GLN C OE1 
8625  N NE2 . GLN C 65  ? 0.5931 0.7622 0.8523 0.0182  -0.1415 -0.0668 65  GLN C NE2 
8626  N N   . GLU C 66  ? 0.4345 0.4595 0.4806 0.0091  -0.1877 -0.0612 66  GLU C N   
8627  C CA  . GLU C 66  ? 0.5308 0.5284 0.5463 0.0114  -0.2101 -0.0683 66  GLU C CA  
8628  C C   . GLU C 66  ? 0.5149 0.4994 0.5154 0.0005  -0.2006 -0.0681 66  GLU C C   
8629  O O   . GLU C 66  ? 0.4876 0.4634 0.4878 -0.0014 -0.2173 -0.0776 66  GLU C O   
8630  C CB  . GLU C 66  ? 0.6153 0.5784 0.5749 0.0213  -0.2190 -0.0638 66  GLU C CB  
8631  C CG  . GLU C 66  ? 0.7503 0.6833 0.6767 0.0281  -0.2477 -0.0722 66  GLU C CG  
8632  C CD  . GLU C 66  ? 0.8364 0.7513 0.7368 0.0424  -0.2647 -0.0715 66  GLU C CD  
8633  O OE1 . GLU C 66  ? 0.8077 0.7083 0.6785 0.0451  -0.2516 -0.0616 66  GLU C OE1 
8634  O OE2 . GLU C 66  ? 0.9155 0.8306 0.8296 0.0500  -0.2824 -0.0788 66  GLU C OE2 
8635  N N   . TYR C 67  ? 0.5102 0.4917 0.4977 -0.0061 -0.1751 -0.0582 67  TYR C N   
8636  C CA  . TYR C 67  ? 0.5214 0.4928 0.5000 -0.0161 -0.1650 -0.0584 67  TYR C CA  
8637  C C   . TYR C 67  ? 0.5501 0.5483 0.5794 -0.0243 -0.1628 -0.0641 67  TYR C C   
8638  O O   . TYR C 67  ? 0.6270 0.6173 0.6572 -0.0304 -0.1689 -0.0709 67  TYR C O   
8639  C CB  . TYR C 67  ? 0.5020 0.4669 0.4617 -0.0201 -0.1394 -0.0475 67  TYR C CB  
8640  C CG  . TYR C 67  ? 0.4760 0.4059 0.3818 -0.0171 -0.1378 -0.0440 67  TYR C CG  
8641  C CD1 . TYR C 67  ? 0.4881 0.3924 0.3644 -0.0221 -0.1361 -0.0466 67  TYR C CD1 
8642  C CD2 . TYR C 67  ? 0.4985 0.4195 0.3831 -0.0097 -0.1361 -0.0384 67  TYR C CD2 
8643  C CE1 . TYR C 67  ? 0.5220 0.3923 0.3487 -0.0200 -0.1310 -0.0436 67  TYR C CE1 
8644  C CE2 . TYR C 67  ? 0.5335 0.4208 0.3700 -0.0080 -0.1314 -0.0352 67  TYR C CE2 
8645  C CZ  . TYR C 67  ? 0.5261 0.3880 0.3337 -0.0133 -0.1279 -0.0377 67  TYR C CZ  
8646  O OH  . TYR C 67  ? 0.5553 0.3816 0.3147 -0.0120 -0.1203 -0.0348 67  TYR C OH  
8647  N N   . ALA C 68  ? 0.4736 0.5019 0.5443 -0.0247 -0.1522 -0.0616 68  ALA C N   
8648  C CA  . ALA C 68  ? 0.4269 0.4804 0.5483 -0.0329 -0.1464 -0.0665 68  ALA C CA  
8649  C C   . ALA C 68  ? 0.4651 0.5225 0.6101 -0.0329 -0.1714 -0.0811 68  ALA C C   
8650  O O   . ALA C 68  ? 0.5172 0.5738 0.6765 -0.0417 -0.1723 -0.0871 68  ALA C O   
8651  C CB  . ALA C 68  ? 0.3738 0.4554 0.5313 -0.0312 -0.1321 -0.0622 68  ALA C CB  
8652  N N   . GLN C 69  ? 0.4419 0.5886 0.5798 -0.0087 -0.1633 -0.0092 69  GLN C N   
8653  C CA  . GLN C 69  ? 0.4939 0.6535 0.6380 -0.0090 -0.1825 -0.0189 69  GLN C CA  
8654  C C   . GLN C 69  ? 0.5463 0.6750 0.6575 -0.0099 -0.1907 -0.0212 69  GLN C C   
8655  O O   . GLN C 69  ? 0.5436 0.6817 0.6593 -0.0120 -0.2068 -0.0302 69  GLN C O   
8656  C CB  . GLN C 69  ? 0.5550 0.7307 0.7045 0.0074  -0.1961 -0.0221 69  GLN C CB  
8657  C CG  . GLN C 69  ? 0.6263 0.8419 0.8154 0.0072  -0.1935 -0.0242 69  GLN C CG  
8658  C CD  . GLN C 69  ? 0.7205 0.9507 0.9129 0.0255  -0.2079 -0.0280 69  GLN C CD  
8659  O OE1 . GLN C 69  ? 0.7844 1.0498 1.0056 0.0264  -0.2198 -0.0374 69  GLN C OE1 
8660  N NE2 . GLN C 69  ? 0.7146 0.9170 0.8767 0.0404  -0.2068 -0.0214 69  GLN C NE2 
8661  N N   . GLY C 70  ? 0.5880 0.6817 0.6671 -0.0083 -0.1803 -0.0142 70  GLY C N   
8662  C CA  . GLY C 70  ? 0.6415 0.7046 0.6867 -0.0076 -0.1873 -0.0162 70  GLY C CA  
8663  C C   . GLY C 70  ? 0.6815 0.7287 0.6993 0.0087  -0.2010 -0.0172 70  GLY C C   
8664  O O   . GLY C 70  ? 0.7365 0.7619 0.7273 0.0106  -0.2108 -0.0207 70  GLY C O   
8665  N N   . LYS C 71  ? 0.6837 0.7391 0.7053 0.0213  -0.2020 -0.0142 71  LYS C N   
8666  C CA  . LYS C 71  ? 0.6646 0.7023 0.6576 0.0386  -0.2146 -0.0144 71  LYS C CA  
8667  C C   . LYS C 71  ? 0.6825 0.6837 0.6398 0.0458  -0.2012 -0.0048 71  LYS C C   
8668  O O   . LYS C 71  ? 0.7384 0.7221 0.6708 0.0606  -0.2080 -0.0030 71  LYS C O   
8669  C CB  . LYS C 71  ? 0.6518 0.7203 0.6695 0.0494  -0.2262 -0.0183 71  LYS C CB  
8670  N N   . ALA C 72  ? 0.6013 0.5903 0.5552 0.0358  -0.1823 0.0007  72  ALA C N   
8671  C CA  . ALA C 72  ? 0.6074 0.5655 0.5318 0.0402  -0.1675 0.0086  72  ALA C CA  
8672  C C   . ALA C 72  ? 0.6570 0.5798 0.5421 0.0394  -0.1672 0.0086  72  ALA C C   
8673  O O   . ALA C 72  ? 0.6393 0.5607 0.5264 0.0287  -0.1640 0.0061  72  ALA C O   
8674  C CB  . ALA C 72  ? 0.6297 0.5975 0.5740 0.0312  -0.1473 0.0133  72  ALA C CB  
8675  N N   . LYS C 73  ? 0.6431 0.5358 0.4907 0.0510  -0.1702 0.0114  73  LYS C N   
8676  C CA  . LYS C 73  ? 0.6309 0.4870 0.4364 0.0520  -0.1689 0.0120  73  LYS C CA  
8677  C C   . LYS C 73  ? 0.5983 0.4313 0.3851 0.0493  -0.1464 0.0190  73  LYS C C   
8678  O O   . LYS C 73  ? 0.6791 0.4928 0.4446 0.0574  -0.1413 0.0239  73  LYS C O   
8679  C CB  . LYS C 73  ? 0.6189 0.4544 0.3917 0.0668  -0.1865 0.0102  73  LYS C CB  
8680  C CG  . LYS C 73  ? 0.6711 0.5363 0.4684 0.0722  -0.2092 0.0024  73  LYS C CG  
8681  C CD  . LYS C 73  ? 0.8071 0.6503 0.5684 0.0866  -0.2294 -0.0017 73  LYS C CD  
8682  C CE  . LYS C 73  ? 0.8558 0.7006 0.6123 0.1040  -0.2403 -0.0007 73  LYS C CE  
8683  N NZ  . LYS C 73  ? 0.9563 0.8087 0.7073 0.1164  -0.2673 -0.0100 73  LYS C NZ  
8684  N N   . ASP C 74  ? 0.5628 0.3967 0.3560 0.0380  -0.1332 0.0188  74  ASP C N   
8685  C CA  . ASP C 74  ? 0.5845 0.4074 0.3717 0.0334  -0.1111 0.0234  74  ASP C CA  
8686  C C   . ASP C 74  ? 0.6587 0.4489 0.4076 0.0323  -0.1046 0.0232  74  ASP C C   
8687  O O   . ASP C 74  ? 0.7133 0.5037 0.4622 0.0263  -0.1063 0.0192  74  ASP C O   
8688  C CB  . ASP C 74  ? 0.5989 0.4503 0.4241 0.0233  -0.1013 0.0225  74  ASP C CB  
8689  C CG  . ASP C 74  ? 0.6565 0.5016 0.4797 0.0191  -0.0797 0.0255  74  ASP C CG  
8690  O OD1 . ASP C 74  ? 0.7025 0.5234 0.4979 0.0178  -0.0706 0.0254  74  ASP C OD1 
8691  O OD2 . ASP C 74  ? 0.6352 0.5010 0.4856 0.0170  -0.0718 0.0271  74  ASP C OD2 
8692  N N   . VAL C 75  ? 0.7404 0.5012 0.4554 0.0379  -0.0966 0.0273  75  VAL C N   
8693  C CA  . VAL C 75  ? 0.7725 0.4995 0.4461 0.0384  -0.0914 0.0271  75  VAL C CA  
8694  C C   . VAL C 75  ? 0.7325 0.4633 0.4134 0.0284  -0.0756 0.0249  75  VAL C C   
8695  O O   . VAL C 75  ? 0.7039 0.4222 0.3673 0.0267  -0.0782 0.0214  75  VAL C O   
8696  C CB  . VAL C 75  ? 0.8393 0.5333 0.4757 0.0449  -0.0825 0.0326  75  VAL C CB  
8697  C CG1 . VAL C 75  ? 0.8809 0.5834 0.5345 0.0402  -0.0638 0.0362  75  VAL C CG1 
8698  C CG2 . VAL C 75  ? 0.8991 0.5583 0.4923 0.0444  -0.0743 0.0325  75  VAL C CG2 
8699  N N   . PHE C 76  ? 0.7111 0.4604 0.4185 0.0224  -0.0603 0.0261  76  PHE C N   
8700  C CA  . PHE C 76  ? 0.6680 0.4228 0.3831 0.0148  -0.0463 0.0231  76  PHE C CA  
8701  C C   . PHE C 76  ? 0.6724 0.4446 0.4080 0.0108  -0.0568 0.0187  76  PHE C C   
8702  O O   . PHE C 76  ? 0.7167 0.4795 0.4404 0.0080  -0.0536 0.0152  76  PHE C O   
8703  C CB  . PHE C 76  ? 0.7027 0.4746 0.4419 0.0106  -0.0290 0.0244  76  PHE C CB  
8704  C CG  . PHE C 76  ? 0.8142 0.5896 0.5569 0.0050  -0.0138 0.0205  76  PHE C CG  
8705  C CD1 . PHE C 76  ? 0.9060 0.6604 0.6220 0.0039  0.0015  0.0197  76  PHE C CD1 
8706  C CD2 . PHE C 76  ? 0.9001 0.6986 0.6711 0.0014  -0.0148 0.0173  76  PHE C CD2 
8707  C CE1 . PHE C 76  ? 0.9690 0.7289 0.6891 0.0000  0.0151  0.0148  76  PHE C CE1 
8708  C CE2 . PHE C 76  ? 0.9461 0.7471 0.7185 -0.0015 -0.0020 0.0131  76  PHE C CE2 
8709  C CZ  . PHE C 76  ? 0.9723 0.7556 0.7204 -0.0018 0.0126  0.0113  76  PHE C CZ  
8710  N N   . LEU C 77  ? 0.6402 0.4368 0.4054 0.0104  -0.0691 0.0186  77  LEU C N   
8711  C CA  . LEU C 77  ? 0.6285 0.4406 0.4135 0.0048  -0.0782 0.0144  77  LEU C CA  
8712  C C   . LEU C 77  ? 0.7043 0.4976 0.4641 0.0059  -0.0919 0.0103  77  LEU C C   
8713  O O   . LEU C 77  ? 0.7077 0.4978 0.4662 0.0008  -0.0919 0.0065  77  LEU C O   
8714  C CB  . LEU C 77  ? 0.6421 0.4840 0.4629 0.0036  -0.0877 0.0149  77  LEU C CB  
8715  C CG  . LEU C 77  ? 0.6442 0.5094 0.4968 -0.0046 -0.0865 0.0128  77  LEU C CG  
8716  C CD1 . LEU C 77  ? 0.6281 0.4921 0.4831 -0.0079 -0.0687 0.0132  77  LEU C CD1 
8717  C CD2 . LEU C 77  ? 0.6281 0.5221 0.5140 -0.0045 -0.0908 0.0145  77  LEU C CD2 
8718  N N   . GLU C 78  ? 0.6741 0.4534 0.4122 0.0133  -0.1043 0.0107  78  GLU C N   
8719  C CA  . GLU C 78  ? 0.7562 0.5159 0.4673 0.0155  -0.1179 0.0062  78  GLU C CA  
8720  C C   . GLU C 78  ? 0.8061 0.5410 0.4886 0.0137  -0.1058 0.0051  78  GLU C C   
8721  O O   . GLU C 78  ? 0.8763 0.6026 0.5487 0.0111  -0.1129 0.0000  78  GLU C O   
8722  C CB  . GLU C 78  ? 0.8766 0.6197 0.5612 0.0264  -0.1308 0.0073  78  GLU C CB  
8723  C CG  . GLU C 78  ? 0.9900 0.7556 0.6988 0.0313  -0.1418 0.0085  78  GLU C CG  
8724  C CD  . GLU C 78  ? 1.1359 0.8790 0.8127 0.0444  -0.1483 0.0117  78  GLU C CD  
8725  O OE1 . GLU C 78  ? 1.1932 0.9018 0.8275 0.0489  -0.1442 0.0133  78  GLU C OE1 
8726  O OE2 . GLU C 78  ? 1.1548 0.9133 0.8473 0.0508  -0.1572 0.0127  78  GLU C OE2 
8727  N N   . ALA C 79  ? 0.7543 0.4784 0.4244 0.0148  -0.0870 0.0090  79  ALA C N   
8728  C CA  . ALA C 79  ? 0.7207 0.4252 0.3668 0.0132  -0.0734 0.0071  79  ALA C CA  
8729  C C   . ALA C 79  ? 0.7318 0.4520 0.4009 0.0063  -0.0668 0.0034  79  ALA C C   
8730  O O   . ALA C 79  ? 0.7702 0.4751 0.4201 0.0058  -0.0613 -0.0002 79  ALA C O   
8731  C CB  . ALA C 79  ? 0.6986 0.3910 0.3294 0.0147  -0.0538 0.0112  79  ALA C CB  
8732  N N   . ILE C 80  ? 0.6591 0.4075 0.3664 0.0020  -0.0666 0.0043  80  ILE C N   
8733  C CA  . ILE C 80  ? 0.6166 0.3770 0.3429 -0.0035 -0.0626 0.0011  80  ILE C CA  
8734  C C   . ILE C 80  ? 0.6040 0.3618 0.3304 -0.0071 -0.0793 -0.0033 80  ILE C C   
8735  O O   . ILE C 80  ? 0.6107 0.3568 0.3260 -0.0091 -0.0780 -0.0074 80  ILE C O   
8736  C CB  . ILE C 80  ? 0.6140 0.4032 0.3781 -0.0066 -0.0559 0.0037  80  ILE C CB  
8737  C CG1 . ILE C 80  ? 0.6695 0.4613 0.4341 -0.0042 -0.0380 0.0062  80  ILE C CG1 
8738  C CG2 . ILE C 80  ? 0.5928 0.3911 0.3734 -0.0115 -0.0548 0.0006  80  ILE C CG2 
8739  C CD1 . ILE C 80  ? 0.7163 0.5033 0.4739 -0.0044 -0.0232 0.0024  80  ILE C CD1 
8740  N N   . ARG C 81  ? 0.6802 0.4491 0.4195 -0.0079 -0.0952 -0.0032 81  ARG C N   
8741  C CA  . ARG C 81  ? 0.7748 0.5459 0.5201 -0.0134 -0.1111 -0.0084 81  ARG C CA  
8742  C C   . ARG C 81  ? 0.8319 0.5745 0.5412 -0.0111 -0.1188 -0.0134 81  ARG C C   
8743  O O   . ARG C 81  ? 0.8792 0.6170 0.5882 -0.0170 -0.1257 -0.0186 81  ARG C O   
8744  C CB  . ARG C 81  ? 0.8372 0.6284 0.6035 -0.0137 -0.1267 -0.0087 81  ARG C CB  
8745  C CG  . ARG C 81  ? 0.9005 0.7092 0.6933 -0.0237 -0.1375 -0.0136 81  ARG C CG  
8746  C CD  . ARG C 81  ? 0.9473 0.7822 0.7663 -0.0237 -0.1508 -0.0145 81  ARG C CD  
8747  N NE  . ARG C 81  ? 0.9718 0.8321 0.8270 -0.0348 -0.1520 -0.0166 81  ARG C NE  
8748  C CZ  . ARG C 81  ? 0.9434 0.8313 0.8305 -0.0361 -0.1480 -0.0133 81  ARG C CZ  
8749  N NH1 . ARG C 81  ? 0.9002 0.7937 0.7879 -0.0268 -0.1434 -0.0081 81  ARG C NH1 
8750  N NH2 . ARG C 81  ? 0.9630 0.8713 0.8798 -0.0470 -0.1482 -0.0154 81  ARG C NH2 
8751  N N   . LYS C 82  ? 0.7998 0.5214 0.4768 -0.0030 -0.1174 -0.0118 82  LYS C N   
8752  C CA  . LYS C 82  ? 0.8318 0.5251 0.4713 0.0007  -0.1257 -0.0164 82  LYS C CA  
8753  C C   . LYS C 82  ? 0.8650 0.5437 0.4915 -0.0024 -0.1170 -0.0202 82  LYS C C   
8754  O O   . LYS C 82  ? 0.8619 0.5440 0.4946 -0.0031 -0.0996 -0.0182 82  LYS C O   
8755  C CB  . LYS C 82  ? 0.8193 0.4903 0.4239 0.0102  -0.1206 -0.0126 82  LYS C CB  
8756  C CG  . LYS C 82  ? 0.7908 0.4583 0.3848 0.0173  -0.1375 -0.0121 82  LYS C CG  
8757  C CD  . LYS C 82  ? 0.8241 0.4661 0.3816 0.0262  -0.1283 -0.0068 82  LYS C CD  
8758  C CE  . LYS C 82  ? 0.9048 0.5372 0.4439 0.0359  -0.1468 -0.0066 82  LYS C CE  
8759  N NZ  . LYS C 82  ? 0.9536 0.5564 0.4531 0.0447  -0.1374 -0.0008 82  LYS C NZ  
8760  N N   . ASP C 83  ? 0.8995 0.5615 0.5071 -0.0033 -0.1299 -0.0265 83  ASP C N   
8761  C CA  . ASP C 83  ? 0.9047 0.5441 0.4869 -0.0026 -0.1225 -0.0305 83  ASP C CA  
8762  C C   . ASP C 83  ? 0.8875 0.5090 0.4397 0.0055  -0.1069 -0.0273 83  ASP C C   
8763  O O   . ASP C 83  ? 0.8602 0.4713 0.3924 0.0114  -0.1102 -0.0246 83  ASP C O   
8764  C CB  . ASP C 83  ? 0.9729 0.5936 0.5336 -0.0034 -0.1405 -0.0381 83  ASP C CB  
8765  C CG  . ASP C 83  ? 0.9548 0.5547 0.4957 -0.0043 -0.1348 -0.0432 83  ASP C CG  
8766  O OD1 . ASP C 83  ? 0.9475 0.5300 0.4616 0.0025  -0.1214 -0.0426 83  ASP C OD1 
8767  O OD2 . ASP C 83  ? 0.9456 0.5460 0.4972 -0.0118 -0.1433 -0.0484 83  ASP C OD2 
8768  N N   . PRO C 84  ? 0.8281 0.4457 0.3761 0.0060  -0.0894 -0.0280 84  PRO C N   
8769  C CA  . PRO C 84  ? 0.8284 0.4315 0.3502 0.0120  -0.0725 -0.0260 84  PRO C CA  
8770  C C   . PRO C 84  ? 0.9188 0.4908 0.3956 0.0183  -0.0783 -0.0279 84  PRO C C   
8771  O O   . PRO C 84  ? 0.9415 0.5008 0.3956 0.0226  -0.0662 -0.0246 84  PRO C O   
8772  C CB  . PRO C 84  ? 0.8226 0.4282 0.3487 0.0117  -0.0571 -0.0297 84  PRO C CB  
8773  C CG  . PRO C 84  ? 0.7757 0.4056 0.3409 0.0057  -0.0610 -0.0293 84  PRO C CG  
8774  C CD  . PRO C 84  ? 0.8146 0.4451 0.3863 0.0012  -0.0827 -0.0301 84  PRO C CD  
8775  N N   . ASP C 85  ? 0.9558 0.5136 0.4174 0.0185  -0.0956 -0.0335 85  ASP C N   
8776  C CA  . ASP C 85  ? 0.9853 0.5123 0.4018 0.0255  -0.1025 -0.0358 85  ASP C CA  
8777  C C   . ASP C 85  ? 0.9932 0.5162 0.3992 0.0303  -0.1126 -0.0312 85  ASP C C   
8778  O O   . ASP C 85  ? 1.0338 0.5294 0.3985 0.0378  -0.1126 -0.0307 85  ASP C O   
8779  C CB  . ASP C 85  ? 1.0447 0.5588 0.4496 0.0243  -0.1200 -0.0439 85  ASP C CB  
8780  C CG  . ASP C 85  ? 1.0570 0.5613 0.4536 0.0236  -0.1096 -0.0492 85  ASP C CG  
8781  O OD1 . ASP C 85  ? 1.0366 0.5368 0.4228 0.0271  -0.0893 -0.0477 85  ASP C OD1 
8782  O OD2 . ASP C 85  ? 1.0439 0.5440 0.4436 0.0196  -0.1220 -0.0555 85  ASP C OD2 
8783  N N   . ASP C 86  ? 0.9603 0.5086 0.4007 0.0270  -0.1210 -0.0281 86  ASP C N   
8784  C CA  . ASP C 86  ? 0.9713 0.5186 0.4052 0.0328  -0.1311 -0.0239 86  ASP C CA  
8785  C C   . ASP C 86  ? 0.9017 0.4513 0.3370 0.0347  -0.1128 -0.0157 86  ASP C C   
8786  O O   . ASP C 86  ? 0.9500 0.4948 0.3760 0.0406  -0.1191 -0.0114 86  ASP C O   
8787  C CB  . ASP C 86  ? 1.0675 0.6430 0.5391 0.0288  -0.1502 -0.0259 86  ASP C CB  
8788  C CG  . ASP C 86  ? 1.1859 0.7616 0.6609 0.0244  -0.1684 -0.0349 86  ASP C CG  
8789  O OD1 . ASP C 86  ? 1.1980 0.7467 0.6366 0.0286  -0.1734 -0.0397 86  ASP C OD1 
8790  O OD2 . ASP C 86  ? 1.2284 0.8307 0.7417 0.0163  -0.1770 -0.0376 86  ASP C OD2 
8791  N N   . LEU C 87  ? 0.8813 0.4386 0.3285 0.0300  -0.0911 -0.0139 87  LEU C N   
8792  C CA  . LEU C 87  ? 0.8767 0.4376 0.3278 0.0301  -0.0731 -0.0073 87  LEU C CA  
8793  C C   . LEU C 87  ? 0.9067 0.4330 0.3093 0.0368  -0.0654 -0.0042 87  LEU C C   
8794  O O   . LEU C 87  ? 0.9186 0.4211 0.2874 0.0393  -0.0611 -0.0075 87  LEU C O   
8795  C CB  . LEU C 87  ? 0.8009 0.3787 0.2750 0.0239  -0.0522 -0.0082 87  LEU C CB  
8796  C CG  . LEU C 87  ? 0.7797 0.3918 0.3025 0.0177  -0.0554 -0.0086 87  LEU C CG  
8797  C CD1 . LEU C 87  ? 0.8074 0.4307 0.3443 0.0142  -0.0368 -0.0113 87  LEU C CD1 
8798  C CD2 . LEU C 87  ? 0.7326 0.3622 0.2787 0.0173  -0.0563 -0.0026 87  LEU C CD2 
8799  N N   . GLU C 88  ? 0.9464 0.4680 0.3436 0.0399  -0.0633 0.0023  88  GLU C N   
8800  C CA  . GLU C 88  ? 0.9846 0.4735 0.3384 0.0442  -0.0496 0.0068  88  GLU C CA  
8801  C C   . GLU C 88  ? 0.9799 0.4744 0.3416 0.0367  -0.0210 0.0078  88  GLU C C   
8802  O O   . GLU C 88  ? 0.8616 0.3876 0.2656 0.0299  -0.0134 0.0068  88  GLU C O   
8803  C CB  . GLU C 88  ? 1.0091 0.4887 0.3532 0.0504  -0.0571 0.0134  88  GLU C CB  
8804  C CG  . GLU C 88  ? 1.0560 0.5392 0.4022 0.0583  -0.0864 0.0116  88  GLU C CG  
8805  C CD  . GLU C 88  ? 1.0984 0.5799 0.4444 0.0649  -0.0930 0.0176  88  GLU C CD  
8806  O OE1 . GLU C 88  ? 1.1928 0.6657 0.5237 0.0752  -0.1151 0.0165  88  GLU C OE1 
8807  O OE2 . GLU C 88  ? 1.0736 0.5618 0.4336 0.0605  -0.0762 0.0227  88  GLU C OE2 
8808  N N   . LYS C 89  ? 0.9443 0.4082 0.2642 0.0381  -0.0050 0.0091  89  LYS C N   
8809  C CA  . LYS C 89  ? 1.0627 0.5314 0.3881 0.0305  0.0233  0.0090  89  LYS C CA  
8810  C C   . LYS C 89  ? 0.9882 0.4760 0.3442 0.0254  0.0315  0.0138  89  LYS C C   
8811  O O   . LYS C 89  ? 0.9802 0.4951 0.3704 0.0179  0.0463  0.0112  89  LYS C O   
8812  C CB  . LYS C 89  ? 1.1389 0.5682 0.4107 0.0325  0.0389  0.0106  89  LYS C CB  
8813  C CG  . LYS C 89  ? 1.1542 0.5885 0.4262 0.0259  0.0643  0.0051  89  LYS C CG  
8814  C CD  . LYS C 89  ? 1.2733 0.6750 0.5046 0.0285  0.0750  0.0055  89  LYS C CD  
8815  C CE  . LYS C 89  ? 1.3517 0.7370 0.5721 0.0245  0.0912  0.0119  89  LYS C CE  
8816  N NZ  . LYS C 89  ? 1.2865 0.6973 0.5397 0.0146  0.1071  0.0123  89  LYS C NZ  
8817  N N   . GLU C 90  ? 0.9802 0.4544 0.3241 0.0304  0.0210  0.0203  90  GLU C N   
8818  C CA  . GLU C 90  ? 1.0175 0.5089 0.3900 0.0267  0.0259  0.0247  90  GLU C CA  
8819  C C   . GLU C 90  ? 0.8867 0.4226 0.3158 0.0224  0.0193  0.0213  90  GLU C C   
8820  O O   . GLU C 90  ? 0.8611 0.4189 0.3206 0.0157  0.0329  0.0215  90  GLU C O   
8821  C CB  . GLU C 90  ? 1.1509 0.6217 0.5019 0.0358  0.0099  0.0311  90  GLU C CB  
8822  C CG  . GLU C 90  ? 1.2902 0.7618 0.6507 0.0331  0.0202  0.0368  90  GLU C CG  
8823  C CD  . GLU C 90  ? 1.3866 0.8905 0.7903 0.0354  0.0035  0.0376  90  GLU C CD  
8824  O OE1 . GLU C 90  ? 1.4064 0.9425 0.8466 0.0335  -0.0073 0.0329  90  GLU C OE1 
8825  O OE2 . GLU C 90  ? 1.4324 0.9278 0.8319 0.0391  0.0018  0.0429  90  GLU C OE2 
8826  N N   . GLU C 91  ? 0.8609 0.4097 0.3037 0.0257  -0.0013 0.0179  91  GLU C N   
8827  C CA  . GLU C 91  ? 0.8207 0.4084 0.3138 0.0216  -0.0081 0.0153  91  GLU C CA  
8828  C C   . GLU C 91  ? 0.8160 0.4219 0.3297 0.0151  0.0076  0.0099  91  GLU C C   
8829  O O   . GLU C 91  ? 0.7099 0.3460 0.2633 0.0107  0.0120  0.0089  91  GLU C O   
8830  C CB  . GLU C 91  ? 0.8376 0.4316 0.3376 0.0256  -0.0336 0.0127  91  GLU C CB  
8831  C CG  . GLU C 91  ? 0.8854 0.4709 0.3749 0.0333  -0.0525 0.0163  91  GLU C CG  
8832  C CD  . GLU C 91  ? 0.9361 0.5325 0.4367 0.0356  -0.0770 0.0116  91  GLU C CD  
8833  O OE1 . GLU C 91  ? 0.9602 0.5399 0.4368 0.0373  -0.0837 0.0071  91  GLU C OE1 
8834  O OE2 . GLU C 91  ? 0.9001 0.5226 0.4344 0.0351  -0.0889 0.0117  91  GLU C OE2 
8835  N N   . VAL C 92  ? 0.8155 0.4035 0.3018 0.0157  0.0154  0.0058  92  VAL C N   
8836  C CA  . VAL C 92  ? 0.8553 0.4594 0.3580 0.0114  0.0306  -0.0003 92  VAL C CA  
8837  C C   . VAL C 92  ? 0.8463 0.4627 0.3637 0.0058  0.0531  0.0001  92  VAL C C   
8838  O O   . VAL C 92  ? 0.7887 0.4346 0.3423 0.0023  0.0599  -0.0033 92  VAL C O   
8839  C CB  . VAL C 92  ? 0.8488 0.4296 0.3161 0.0143  0.0345  -0.0053 92  VAL C CB  
8840  C CG1 . VAL C 92  ? 0.8225 0.4201 0.3052 0.0116  0.0515  -0.0124 92  VAL C CG1 
8841  C CG2 . VAL C 92  ? 0.8406 0.4126 0.2985 0.0189  0.0112  -0.0072 92  VAL C CG2 
8842  N N   . GLU C 93  ? 0.8395 0.4326 0.3286 0.0048  0.0644  0.0042  93  GLU C N   
8843  C CA  . GLU C 93  ? 0.8752 0.4788 0.3779 -0.0023 0.0865  0.0039  93  GLU C CA  
8844  C C   . GLU C 93  ? 0.7755 0.4050 0.3171 -0.0045 0.0817  0.0069  93  GLU C C   
8845  O O   . GLU C 93  ? 0.7515 0.4047 0.3215 -0.0101 0.0960  0.0035  93  GLU C O   
8846  C CB  . GLU C 93  ? 0.9398 0.5083 0.4001 -0.0040 0.1005  0.0079  93  GLU C CB  
8847  C CG  . GLU C 93  ? 1.0983 0.6567 0.5371 -0.0074 0.1211  0.0018  93  GLU C CG  
8848  C CD  . GLU C 93  ? 1.2129 0.7542 0.6319 -0.0153 0.1460  0.0032  93  GLU C CD  
8849  O OE1 . GLU C 93  ? 1.2796 0.7839 0.6515 -0.0141 0.1527  0.0059  93  GLU C OE1 
8850  O OE2 . GLU C 93  ? 1.2200 0.7837 0.6693 -0.0231 0.1593  0.0012  93  GLU C OE2 
8851  N N   . LYS C 94  ? 0.7474 0.3743 0.2913 0.0004  0.0617  0.0125  94  LYS C N   
8852  C CA  . LYS C 94  ? 0.7669 0.4203 0.3488 -0.0009 0.0566  0.0149  94  LYS C CA  
8853  C C   . LYS C 94  ? 0.7008 0.3891 0.3233 -0.0027 0.0541  0.0096  94  LYS C C   
8854  O O   . LYS C 94  ? 0.6637 0.3774 0.3188 -0.0062 0.0615  0.0084  94  LYS C O   
8855  C CB  . LYS C 94  ? 0.8508 0.4958 0.4269 0.0057  0.0351  0.0208  94  LYS C CB  
8856  C CG  . LYS C 94  ? 0.9538 0.6298 0.5720 0.0053  0.0268  0.0224  94  LYS C CG  
8857  C CD  . LYS C 94  ? 1.0164 0.6830 0.6294 0.0083  0.0245  0.0286  94  LYS C CD  
8858  C CE  . LYS C 94  ? 0.9431 0.6438 0.6009 0.0068  0.0215  0.0290  94  LYS C CE  
8859  N NZ  . LYS C 94  ? 0.9224 0.6231 0.5832 0.0139  0.0050  0.0336  94  LYS C NZ  
8860  N N   . LEU C 95  ? 0.7448 0.4327 0.3634 -0.0001 0.0441  0.0061  95  LEU C N   
8861  C CA  . LEU C 95  ? 0.7139 0.4289 0.3645 -0.0011 0.0426  0.0011  95  LEU C CA  
8862  C C   . LEU C 95  ? 0.6583 0.3874 0.3206 -0.0043 0.0634  -0.0050 95  LEU C C   
8863  O O   . LEU C 95  ? 0.5636 0.3202 0.2597 -0.0056 0.0669  -0.0074 95  LEU C O   
8864  C CB  . LEU C 95  ? 0.7009 0.4054 0.3375 0.0020  0.0294  -0.0019 95  LEU C CB  
8865  C CG  . LEU C 95  ? 0.7938 0.5193 0.4581 0.0016  0.0224  -0.0056 95  LEU C CG  
8866  C CD1 . LEU C 95  ? 0.8108 0.5601 0.5096 -0.0002 0.0141  -0.0017 95  LEU C CD1 
8867  C CD2 . LEU C 95  ? 0.8158 0.5244 0.4605 0.0038  0.0076  -0.0077 95  LEU C CD2 
8868  N N   . ILE C 96  ? 0.6419 0.3530 0.2764 -0.0052 0.0777  -0.0081 96  ILE C N   
8869  C CA  . ILE C 96  ? 0.6649 0.3917 0.3111 -0.0082 0.0979  -0.0156 96  ILE C CA  
8870  C C   . ILE C 96  ? 0.6740 0.4167 0.3418 -0.0140 0.1108  -0.0150 96  ILE C C   
8871  O O   . ILE C 96  ? 0.6546 0.4255 0.3527 -0.0154 0.1195  -0.0212 96  ILE C O   
8872  C CB  . ILE C 96  ? 0.7704 0.4742 0.3809 -0.0084 0.1110  -0.0195 96  ILE C CB  
8873  C CG1 . ILE C 96  ? 0.7934 0.4805 0.3816 -0.0022 0.0976  -0.0209 96  ILE C CG1 
8874  C CG2 . ILE C 96  ? 0.7850 0.5095 0.4109 -0.0113 0.1321  -0.0291 96  ILE C CG2 
8875  C CD1 . ILE C 96  ? 0.8894 0.5444 0.4330 -0.0013 0.1053  -0.0214 96  ILE C CD1 
8876  N N   . GLU C 97  ? 0.6643 0.3879 0.3155 -0.0166 0.1115  -0.0080 97  GLU C N   
8877  C CA  . GLU C 97  ? 0.6494 0.3841 0.3183 -0.0226 0.1232  -0.0072 97  GLU C CA  
8878  C C   . GLU C 97  ? 0.6672 0.4329 0.3772 -0.0211 0.1135  -0.0068 97  GLU C C   
8879  O O   . GLU C 97  ? 0.6422 0.4314 0.3793 -0.0249 0.1245  -0.0115 97  GLU C O   
8880  C CB  . GLU C 97  ? 0.8646 0.5679 0.5037 -0.0239 0.1231  0.0011  97  GLU C CB  
8881  C CG  . GLU C 97  ? 1.0567 0.7575 0.6966 -0.0328 0.1440  0.0001  97  GLU C CG  
8882  C CD  . GLU C 97  ? 1.2224 0.9030 0.8498 -0.0325 0.1388  0.0090  97  GLU C CD  
8883  O OE1 . GLU C 97  ? 1.2770 0.9517 0.9008 -0.0246 0.1182  0.0152  97  GLU C OE1 
8884  O OE2 . GLU C 97  ? 1.2734 0.9439 0.8941 -0.0402 0.1555  0.0091  97  GLU C OE2 
8885  N N   . PHE C 98  ? 0.6337 0.3998 0.3482 -0.0156 0.0930  -0.0019 98  PHE C N   
8886  C CA  . PHE C 98  ? 0.5699 0.3639 0.3212 -0.0141 0.0834  -0.0011 98  PHE C CA  
8887  C C   . PHE C 98  ? 0.5463 0.3668 0.3232 -0.0133 0.0886  -0.0089 98  PHE C C   
8888  O O   . PHE C 98  ? 0.5994 0.4453 0.4072 -0.0136 0.0907  -0.0108 98  PHE C O   
8889  C CB  . PHE C 98  ? 0.5680 0.3566 0.3169 -0.0094 0.0616  0.0044  98  PHE C CB  
8890  C CG  . PHE C 98  ? 0.5792 0.3937 0.3630 -0.0084 0.0520  0.0065  98  PHE C CG  
8891  C CD1 . PHE C 98  ? 0.6274 0.4455 0.4205 -0.0085 0.0504  0.0112  98  PHE C CD1 
8892  C CD2 . PHE C 98  ? 0.5815 0.4144 0.3863 -0.0070 0.0451  0.0039  98  PHE C CD2 
8893  C CE1 . PHE C 98  ? 0.5880 0.4304 0.4127 -0.0072 0.0422  0.0129  98  PHE C CE1 
8894  C CE2 . PHE C 98  ? 0.4866 0.3419 0.3215 -0.0064 0.0374  0.0061  98  PHE C CE2 
8895  C CZ  . PHE C 98  ? 0.5338 0.3949 0.3792 -0.0065 0.0362  0.0104  98  PHE C CZ  
8896  N N   . THR C 99  ? 0.5441 0.3579 0.3071 -0.0109 0.0895  -0.0136 99  THR C N   
8897  C CA  . THR C 99  ? 0.5433 0.3790 0.3261 -0.0082 0.0946  -0.0217 99  THR C CA  
8898  C C   . THR C 99  ? 0.5573 0.4104 0.3541 -0.0117 0.1141  -0.0291 99  THR C C   
8899  O O   . THR C 99  ? 0.5056 0.3858 0.3321 -0.0101 0.1166  -0.0337 99  THR C O   
8900  C CB  . THR C 99  ? 0.5991 0.4200 0.3596 -0.0042 0.0915  -0.0254 99  THR C CB  
8901  O OG1 . THR C 99  ? 0.6395 0.4464 0.3903 -0.0022 0.0727  -0.0195 99  THR C OG1 
8902  C CG2 . THR C 99  ? 0.5941 0.4353 0.3724 0.0007  0.0954  -0.0339 99  THR C CG2 
8903  N N   . LYS C 100 ? 0.6137 0.4516 0.3891 -0.0166 0.1283  -0.0308 100 LYS C N   
8904  C CA  . LYS C 100 ? 0.6888 0.5450 0.4792 -0.0216 0.1480  -0.0394 100 LYS C CA  
8905  C C   . LYS C 100 ? 0.6196 0.4920 0.4355 -0.0260 0.1500  -0.0375 100 LYS C C   
8906  O O   . LYS C 100 ? 0.5850 0.4841 0.4270 -0.0278 0.1604  -0.0461 100 LYS C O   
8907  C CB  . LYS C 100 ? 0.7863 0.6206 0.5467 -0.0278 0.1644  -0.0412 100 LYS C CB  
8908  C CG  . LYS C 100 ? 0.8516 0.6896 0.6033 -0.0248 0.1736  -0.0509 100 LYS C CG  
8909  C CD  . LYS C 100 ? 0.9135 0.7896 0.7006 -0.0210 0.1787  -0.0626 100 LYS C CD  
8910  C CE  . LYS C 100 ? 0.9757 0.8574 0.7546 -0.0180 0.1909  -0.0740 100 LYS C CE  
8911  N NZ  . LYS C 100 ? 0.9596 0.8802 0.7729 -0.0156 0.2002  -0.0874 100 LYS C NZ  
8912  N N   . LEU C 101 ? 0.5482 0.4057 0.3573 -0.0268 0.1395  -0.0273 101 LEU C N   
8913  C CA  . LEU C 101 ? 0.6035 0.4746 0.4354 -0.0298 0.1401  -0.0253 101 LEU C CA  
8914  C C   . LEU C 101 ? 0.5432 0.4465 0.4108 -0.0245 0.1325  -0.0288 101 LEU C C   
8915  O O   . LEU C 101 ? 0.5018 0.4261 0.3942 -0.0268 0.1388  -0.0328 101 LEU C O   
8916  C CB  . LEU C 101 ? 0.6608 0.5090 0.4764 -0.0292 0.1284  -0.0140 101 LEU C CB  
8917  C CG  . LEU C 101 ? 0.7208 0.5779 0.5551 -0.0312 0.1276  -0.0108 101 LEU C CG  
8918  C CD1 . LEU C 101 ? 0.7524 0.6016 0.5801 -0.0403 0.1470  -0.0141 101 LEU C CD1 
8919  C CD2 . LEU C 101 ? 0.7710 0.6107 0.5927 -0.0266 0.1108  -0.0004 101 LEU C CD2 
8920  N N   . ASN C 102 ? 0.5507 0.5348 0.3758 -0.0422 0.0365  -0.0156 102 ASN C N   
8921  C CA  . ASN C 102 ? 0.5160 0.5295 0.3756 -0.0287 0.0265  -0.0103 102 ASN C CA  
8922  C C   . ASN C 102 ? 0.5168 0.5535 0.4049 -0.0170 0.0402  -0.0134 102 ASN C C   
8923  O O   . ASN C 102 ? 0.4321 0.4922 0.3477 -0.0040 0.0335  -0.0090 102 ASN C O   
8924  C CB  . ASN C 102 ? 0.5211 0.5117 0.3658 -0.0239 0.0114  -0.0061 102 ASN C CB  
8925  C CG  . ASN C 102 ? 0.5464 0.5192 0.3679 -0.0328 -0.0055 -0.0042 102 ASN C CG  
8926  O OD1 . ASN C 102 ? 0.4923 0.4856 0.3275 -0.0355 -0.0152 -0.0010 102 ASN C OD1 
8927  N ND2 . ASN C 102 ? 0.4785 0.4136 0.2652 -0.0364 -0.0098 -0.0071 102 ASN C ND2 
8928  N N   . TYR C 103 ? 0.4951 0.5259 0.3766 -0.0213 0.0592  -0.0212 103 TYR C N   
8929  C CA  . TYR C 103 ? 0.5034 0.5488 0.4058 -0.0101 0.0728  -0.0261 103 TYR C CA  
8930  C C   . TYR C 103 ? 0.4449 0.5366 0.3915 0.0022  0.0709  -0.0259 103 TYR C C   
8931  O O   . TYR C 103 ? 0.4422 0.5448 0.4073 0.0177  0.0719  -0.0253 103 TYR C O   
8932  C CB  . TYR C 103 ? 0.5712 0.6061 0.4598 -0.0203 0.0942  -0.0363 103 TYR C CB  
8933  C CG  . TYR C 103 ? 0.6625 0.7107 0.5706 -0.0100 0.1095  -0.0438 103 TYR C CG  
8934  C CD1 . TYR C 103 ? 0.7071 0.7279 0.5977 -0.0046 0.1138  -0.0446 103 TYR C CD1 
8935  C CD2 . TYR C 103 ? 0.6912 0.7802 0.6360 -0.0051 0.1195  -0.0514 103 TYR C CD2 
8936  C CE1 . TYR C 103 ? 0.7656 0.7980 0.6739 0.0053  0.1275  -0.0519 103 TYR C CE1 
8937  C CE2 . TYR C 103 ? 0.7396 0.8417 0.7030 0.0055  0.1326  -0.0596 103 TYR C CE2 
8938  C CZ  . TYR C 103 ? 0.8220 0.8949 0.7666 0.0107  0.1366  -0.0594 103 TYR C CZ  
8939  O OH  . TYR C 103 ? 0.9825 1.0679 0.9456 0.0218  0.1493  -0.0681 103 TYR C OH  
8940  N N   . GLU C 104 ? 0.4442 0.5626 0.4073 -0.0037 0.0683  -0.0269 104 GLU C N   
8941  C CA  . GLU C 104 ? 0.4466 0.6114 0.4520 0.0078  0.0679  -0.0293 104 GLU C CA  
8942  C C   . GLU C 104 ? 0.4189 0.5993 0.4393 0.0179  0.0479  -0.0191 104 GLU C C   
8943  O O   . GLU C 104 ? 0.4168 0.6358 0.4701 0.0274  0.0445  -0.0204 104 GLU C O   
8944  C CB  . GLU C 104 ? 0.4262 0.6163 0.4462 -0.0038 0.0783  -0.0385 104 GLU C CB  
8945  C CG  . GLU C 104 ? 0.4426 0.6212 0.4512 -0.0143 0.1012  -0.0503 104 GLU C CG  
8946  C CD  . GLU C 104 ? 0.5348 0.7362 0.5703 -0.0007 0.1140  -0.0599 104 GLU C CD  
8947  O OE1 . GLU C 104 ? 0.5984 0.8290 0.6646 0.0176  0.1057  -0.0584 104 GLU C OE1 
8948  O OE2 . GLU C 104 ? 0.6404 0.8294 0.6650 -0.0081 0.1326  -0.0695 104 GLU C OE2 
8949  N N   . LYS C 105 ? 0.4235 0.5764 0.4214 0.0164  0.0351  -0.0105 105 LYS C N   
8950  C CA  . LYS C 105 ? 0.3416 0.5083 0.3532 0.0255  0.0177  -0.0015 105 LYS C CA  
8951  C C   . LYS C 105 ? 0.3403 0.5066 0.3618 0.0438  0.0171  0.0023  105 LYS C C   
8952  O O   . LYS C 105 ? 0.3034 0.4452 0.3104 0.0465  0.0258  0.0003  105 LYS C O   
8953  C CB  . LYS C 105 ? 0.3287 0.4681 0.3138 0.0153  0.0036  0.0047  105 LYS C CB  
8954  C CG  . LYS C 105 ? 0.3447 0.4819 0.3176 -0.0014 0.0021  0.0019  105 LYS C CG  
8955  C CD  . LYS C 105 ? 0.3193 0.4198 0.2575 -0.0117 -0.0086 0.0046  105 LYS C CD  
8956  C CE  . LYS C 105 ? 0.3869 0.4839 0.3118 -0.0267 -0.0104 0.0022  105 LYS C CE  
8957  N NZ  . LYS C 105 ? 0.4491 0.5120 0.3405 -0.0347 -0.0239 0.0042  105 LYS C NZ  
8958  N N   . PRO C 106 ? 0.2976 0.4894 0.3423 0.0572  0.0073  0.0078  106 PRO C N   
8959  C CA  . PRO C 106 ? 0.2846 0.4715 0.3346 0.0753  0.0069  0.0122  106 PRO C CA  
8960  C C   . PRO C 106 ? 0.2928 0.4391 0.3157 0.0731  0.0035  0.0180  106 PRO C C   
8961  O O   . PRO C 106 ? 0.3644 0.4955 0.3839 0.0843  0.0092  0.0188  106 PRO C O   
8962  C CB  . PRO C 106 ? 0.3318 0.5499 0.4055 0.0871  -0.0056 0.0181  106 PRO C CB  
8963  C CG  . PRO C 106 ? 0.3017 0.5530 0.3938 0.0790  -0.0056 0.0120  106 PRO C CG  
8964  C CD  . PRO C 106 ? 0.2928 0.5209 0.3610 0.0575  -0.0017 0.0087  106 PRO C CD  
8965  N N   . ILE C 107 ? 0.3311 0.4593 0.3350 0.0593  -0.0058 0.0208  107 ILE C N   
8966  C CA  . ILE C 107 ? 0.3640 0.4569 0.3453 0.0574  -0.0095 0.0241  107 ILE C CA  
8967  C C   . ILE C 107 ? 0.4167 0.4798 0.3766 0.0525  0.0027  0.0176  107 ILE C C   
8968  O O   . ILE C 107 ? 0.4017 0.4362 0.3456 0.0536  0.0030  0.0183  107 ILE C O   
8969  C CB  . ILE C 107 ? 0.3318 0.4164 0.3009 0.0450  -0.0241 0.0268  107 ILE C CB  
8970  C CG1 . ILE C 107 ? 0.3038 0.3912 0.2641 0.0304  -0.0248 0.0218  107 ILE C CG1 
8971  C CG2 . ILE C 107 ? 0.3003 0.4078 0.2878 0.0516  -0.0363 0.0342  107 ILE C CG2 
8972  C CD1 . ILE C 107 ? 0.3813 0.4467 0.3191 0.0181  -0.0376 0.0216  107 ILE C CD1 
8973  N N   . TYR C 108 ? 0.4102 0.4794 0.3694 0.0468  0.0136  0.0104  108 TYR C N   
8974  C CA  . TYR C 108 ? 0.4422 0.4858 0.3820 0.0427  0.0269  0.0036  108 TYR C CA  
8975  C C   . TYR C 108 ? 0.4543 0.5084 0.4105 0.0562  0.0406  -0.0003 108 TYR C C   
8976  O O   . TYR C 108 ? 0.4676 0.5041 0.4108 0.0537  0.0532  -0.0069 108 TYR C O   
8977  C CB  . TYR C 108 ? 0.4255 0.4643 0.3497 0.0268  0.0320  -0.0025 108 TYR C CB  
8978  C CG  . TYR C 108 ? 0.4660 0.4731 0.3584 0.0146  0.0223  -0.0018 108 TYR C CG  
8979  C CD1 . TYR C 108 ? 0.4102 0.4218 0.3026 0.0104  0.0054  0.0034  108 TYR C CD1 
8980  C CD2 . TYR C 108 ? 0.4675 0.4404 0.3298 0.0082  0.0293  -0.0072 108 TYR C CD2 
8981  C CE1 . TYR C 108 ? 0.3941 0.3775 0.2579 0.0006  -0.0049 0.0022  108 TYR C CE1 
8982  C CE2 . TYR C 108 ? 0.4966 0.4410 0.3294 -0.0010 0.0190  -0.0079 108 TYR C CE2 
8983  C CZ  . TYR C 108 ? 0.4670 0.4169 0.3009 -0.0045 0.0017  -0.0036 108 TYR C CZ  
8984  O OH  . TYR C 108 ? 0.4792 0.4014 0.2842 -0.0124 -0.0096 -0.0062 108 TYR C OH  
8985  N N   . ARG C 109 ? 0.4625 0.5443 0.4460 0.0714  0.0380  0.0030  109 ARG C N   
8986  C CA  . ARG C 109 ? 0.5297 0.6246 0.5308 0.0864  0.0493  -0.0019 109 ARG C CA  
8987  C C   . ARG C 109 ? 0.5577 0.6205 0.5441 0.0946  0.0531  0.0001  109 ARG C C   
8988  O O   . ARG C 109 ? 0.5203 0.5795 0.5118 0.1082  0.0474  0.0071  109 ARG C O   
8989  C CB  . ARG C 109 ? 0.5940 0.7263 0.6260 0.1019  0.0429  0.0009  109 ARG C CB  
8990  C CG  . ARG C 109 ? 0.6936 0.8408 0.7449 0.1207  0.0520  -0.0049 109 ARG C CG  
8991  C CD  . ARG C 109 ? 0.7448 0.9268 0.8238 0.1384  0.0429  -0.0020 109 ARG C CD  
8992  N NE  . ARG C 109 ? 0.7887 0.9544 0.8621 0.1549  0.0352  0.0083  109 ARG C NE  
8993  C CZ  . ARG C 109 ? 0.8312 0.9756 0.8977 0.1683  0.0416  0.0083  109 ARG C CZ  
8994  N NH1 . ARG C 109 ? 0.8311 0.9699 0.8972 0.1678  0.0554  -0.0019 109 ARG C NH1 
8995  N NH2 . ARG C 109 ? 0.8479 0.9752 0.9069 0.1820  0.0348  0.0184  109 ARG C NH2 
8996  N N   . PHE C 110 ? 0.5762 0.6132 0.5420 0.0856  0.0632  -0.0062 110 PHE C N   
8997  C CA  . PHE C 110 ? 0.5706 0.5773 0.5226 0.0918  0.0697  -0.0070 110 PHE C CA  
8998  C C   . PHE C 110 ? 0.5683 0.5770 0.5231 0.0938  0.0865  -0.0177 110 PHE C C   
8999  O O   . PHE C 110 ? 0.5805 0.5903 0.5269 0.0804  0.0939  -0.0248 110 PHE C O   
9000  C CB  . PHE C 110 ? 0.5505 0.5208 0.4720 0.0785  0.0654  -0.0062 110 PHE C CB  
9001  C CG  . PHE C 110 ? 0.4572 0.4210 0.3750 0.0769  0.0502  0.0024  110 PHE C CG  
9002  C CD1 . PHE C 110 ? 0.4224 0.3726 0.3415 0.0875  0.0479  0.0078  110 PHE C CD1 
9003  C CD2 . PHE C 110 ? 0.4083 0.3774 0.3198 0.0640  0.0390  0.0042  110 PHE C CD2 
9004  C CE1 . PHE C 110 ? 0.4574 0.4012 0.3729 0.0845  0.0356  0.0144  110 PHE C CE1 
9005  C CE2 . PHE C 110 ? 0.4223 0.3866 0.3316 0.0620  0.0254  0.0104  110 PHE C CE2 
9006  C CZ  . PHE C 110 ? 0.4538 0.4062 0.3657 0.0718  0.0242  0.0153  110 PHE C CZ  
9007  N N   . GLU C 111 ? 0.5936 0.6006 0.5584 0.1103  0.0928  -0.0192 111 GLU C N   
9008  C CA  . GLU C 111 ? 0.6725 0.6812 0.6412 0.1133  0.1090  -0.0305 111 GLU C CA  
9009  C C   . GLU C 111 ? 0.6194 0.5985 0.5591 0.0965  0.1174  -0.0363 111 GLU C C   
9010  O O   . GLU C 111 ? 0.6003 0.5863 0.5392 0.0888  0.1300  -0.0461 111 GLU C O   
9011  C CB  . GLU C 111 ? 0.8454 0.8464 0.8222 0.1334  0.1127  -0.0303 111 GLU C CB  
9012  C CG  . GLU C 111 ? 0.9726 0.9883 0.9665 0.1511  0.1011  -0.0211 111 GLU C CG  
9013  C CD  . GLU C 111 ? 1.0697 1.0826 1.0739 0.1735  0.1061  -0.0228 111 GLU C CD  
9014  O OE1 . GLU C 111 ? 1.1238 1.1026 1.1112 0.1778  0.1075  -0.0187 111 GLU C OE1 
9015  O OE2 . GLU C 111 ? 1.0671 1.1117 1.0964 0.1872  0.1084  -0.0293 111 GLU C OE2 
9016  N N   . ARG C 112 ? 0.5824 0.5283 0.4975 0.0904  0.1108  -0.0312 112 ARG C N   
9017  C CA  . ARG C 112 ? 0.6511 0.5664 0.5368 0.0772  0.1176  -0.0374 112 ARG C CA  
9018  C C   . ARG C 112 ? 0.6220 0.5393 0.4928 0.0594  0.1171  -0.0400 112 ARG C C   
9019  O O   . ARG C 112 ? 0.6227 0.5240 0.4735 0.0497  0.1278  -0.0477 112 ARG C O   
9020  C CB  . ARG C 112 ? 0.6651 0.5473 0.5310 0.0761  0.1094  -0.0330 112 ARG C CB  
9021  C CG  . ARG C 112 ? 0.6411 0.4904 0.4757 0.0645  0.1144  -0.0401 112 ARG C CG  
9022  C CD  . ARG C 112 ? 0.6805 0.5200 0.5137 0.0703  0.1307  -0.0487 112 ARG C CD  
9023  N NE  . ARG C 112 ? 0.7040 0.5076 0.5094 0.0643  0.1324  -0.0537 112 ARG C NE  
9024  C CZ  . ARG C 112 ? 0.7275 0.5159 0.5177 0.0608  0.1454  -0.0631 112 ARG C CZ  
9025  N NH1 . ARG C 112 ? 0.7329 0.5390 0.5334 0.0618  0.1591  -0.0690 112 ARG C NH1 
9026  N NH2 . ARG C 112 ? 0.7680 0.5243 0.5329 0.0559  0.1450  -0.0678 112 ARG C NH2 
9027  N N   . ILE C 113 ? 0.5633 0.4978 0.4414 0.0550  0.1050  -0.0337 113 ILE C N   
9028  C CA  . ILE C 113 ? 0.5859 0.5211 0.4494 0.0387  0.1045  -0.0358 113 ILE C CA  
9029  C C   . ILE C 113 ? 0.6576 0.6134 0.5326 0.0355  0.1211  -0.0448 113 ILE C C   
9030  O O   . ILE C 113 ? 0.6924 0.6344 0.5452 0.0214  0.1297  -0.0505 113 ILE C O   
9031  C CB  . ILE C 113 ? 0.5618 0.5136 0.4343 0.0360  0.0879  -0.0275 113 ILE C CB  
9032  C CG1 . ILE C 113 ? 0.6062 0.5339 0.4626 0.0353  0.0730  -0.0214 113 ILE C CG1 
9033  C CG2 . ILE C 113 ? 0.5295 0.4854 0.3906 0.0206  0.0880  -0.0296 113 ILE C CG2 
9034  C CD1 . ILE C 113 ? 0.6210 0.5612 0.4819 0.0305  0.0567  -0.0147 113 ILE C CD1 
9035  N N   . ARG C 114 ? 0.6914 0.6792 0.6003 0.0487  0.1263  -0.0472 114 ARG C N   
9036  C CA  . ARG C 114 ? 0.7221 0.7324 0.6465 0.0468  0.1432  -0.0586 114 ARG C CA  
9037  C C   . ARG C 114 ? 0.7150 0.6998 0.6181 0.0416  0.1595  -0.0677 114 ARG C C   
9038  O O   . ARG C 114 ? 0.7057 0.6932 0.6027 0.0299  0.1742  -0.0770 114 ARG C O   
9039  C CB  . ARG C 114 ? 0.7672 0.8145 0.7316 0.0657  0.1441  -0.0612 114 ARG C CB  
9040  C CG  . ARG C 114 ? 0.8169 0.8927 0.8041 0.0725  0.1288  -0.0533 114 ARG C CG  
9041  C CD  . ARG C 114 ? 0.8700 0.9855 0.8960 0.0907  0.1314  -0.0592 114 ARG C CD  
9042  N NE  . ARG C 114 ? 0.9196 1.0697 0.9688 0.0922  0.1212  -0.0565 114 ARG C NE  
9043  C CZ  . ARG C 114 ? 0.9467 1.1036 1.0039 0.1033  0.1046  -0.0454 114 ARG C CZ  
9044  N NH1 . ARG C 114 ? 0.9679 1.0982 1.0115 0.1131  0.0973  -0.0359 114 ARG C NH1 
9045  N NH2 . ARG C 114 ? 0.9328 1.1225 1.0111 0.1040  0.0961  -0.0442 114 ARG C NH2 
9046  N N   . GLU C 115 ? 0.7512 0.7106 0.6426 0.0498  0.1579  -0.0656 115 GLU C N   
9047  C CA  . GLU C 115 ? 0.7510 0.6869 0.6236 0.0465  0.1730  -0.0746 115 GLU C CA  
9048  C C   . GLU C 115 ? 0.7460 0.6475 0.5770 0.0285  0.1740  -0.0752 115 GLU C C   
9049  O O   . GLU C 115 ? 0.7929 0.6842 0.6077 0.0188  0.1896  -0.0843 115 GLU C O   
9050  C CB  . GLU C 115 ? 0.7725 0.6916 0.6462 0.0611  0.1708  -0.0726 115 GLU C CB  
9051  C CG  . GLU C 115 ? 0.8004 0.7472 0.7097 0.0807  0.1735  -0.0746 115 GLU C CG  
9052  C CD  . GLU C 115 ? 0.8499 0.7788 0.7592 0.0953  0.1651  -0.0673 115 GLU C CD  
9053  O OE1 . GLU C 115 ? 0.8409 0.7888 0.7759 0.1132  0.1628  -0.0656 115 GLU C OE1 
9054  O OE2 . GLU C 115 ? 0.8975 0.7926 0.7804 0.0891  0.1609  -0.0639 115 GLU C OE2 
9055  N N   . LEU C 116 ? 0.7772 0.6596 0.5894 0.0244  0.1573  -0.0663 116 LEU C N   
9056  C CA  . LEU C 116 ? 0.7912 0.6393 0.5617 0.0097  0.1553  -0.0672 116 LEU C CA  
9057  C C   . LEU C 116 ? 0.8141 0.6674 0.5735 -0.0050 0.1633  -0.0706 116 LEU C C   
9058  O O   . LEU C 116 ? 0.8539 0.6817 0.5813 -0.0160 0.1741  -0.0766 116 LEU C O   
9059  C CB  . LEU C 116 ? 0.7522 0.5855 0.5107 0.0094  0.1342  -0.0585 116 LEU C CB  
9060  C CG  . LEU C 116 ? 0.7283 0.5530 0.4956 0.0219  0.1274  -0.0557 116 LEU C CG  
9061  C CD1 . LEU C 116 ? 0.7126 0.5273 0.4720 0.0203  0.1075  -0.0488 116 LEU C CD1 
9062  C CD2 . LEU C 116 ? 0.7628 0.5587 0.5091 0.0224  0.1378  -0.0636 116 LEU C CD2 
9063  N N   . MET C 117 ? 0.7624 0.6470 0.5464 -0.0058 0.1589  -0.0670 117 MET C N   
9064  C CA  . MET C 117 ? 0.8034 0.6945 0.5797 -0.0204 0.1673  -0.0705 117 MET C CA  
9065  C C   . MET C 117 ? 0.8890 0.7947 0.6769 -0.0239 0.1912  -0.0826 117 MET C C   
9066  O O   . MET C 117 ? 0.9516 0.8573 0.7285 -0.0383 0.2026  -0.0876 117 MET C O   
9067  C CB  . MET C 117 ? 0.7965 0.7191 0.5991 -0.0194 0.1551  -0.0641 117 MET C CB  
9068  C CG  . MET C 117 ? 0.7757 0.6865 0.5689 -0.0168 0.1319  -0.0532 117 MET C CG  
9069  S SD  . MET C 117 ? 0.7844 0.6482 0.5230 -0.0319 0.1242  -0.0515 117 MET C SD  
9070  C CE  . MET C 117 ? 0.8036 0.6323 0.5189 -0.0249 0.1217  -0.0534 117 MET C CE  
9071  N N   . ASN C 118 ? 0.8691 0.7867 0.6786 -0.0113 0.1994  -0.0883 118 ASN C N   
9072  C CA  . ASN C 118 ? 0.9402 0.8685 0.7585 -0.0142 0.2225  -0.1019 118 ASN C CA  
9073  C C   . ASN C 118 ? 0.9775 0.8666 0.7578 -0.0211 0.2342  -0.1073 118 ASN C C   
9074  O O   . ASN C 118 ? 1.0064 0.8998 0.7883 -0.0261 0.2550  -0.1194 118 ASN C O   
9075  C CB  . ASN C 118 ? 0.9899 0.9526 0.8522 0.0045  0.2254  -0.1069 118 ASN C CB  
9076  C CG  . ASN C 118 ? 1.0380 1.0441 0.9402 0.0121  0.2172  -0.1048 118 ASN C CG  
9077  O OD1 . ASN C 118 ? 1.0563 1.0715 0.9572 0.0011  0.2136  -0.1022 118 ASN C OD1 
9078  N ND2 . ASN C 118 ? 1.0453 1.0772 0.9819 0.0319  0.2135  -0.1061 118 ASN C ND2 
9079  N N   . LYS C 119 ? 0.9768 0.8294 0.7243 -0.0211 0.2217  -0.1001 119 LYS C N   
9080  C CA  . LYS C 119 ? 0.9931 0.8098 0.7074 -0.0239 0.2303  -0.1055 119 LYS C CA  
9081  C C   . LYS C 119 ? 1.0450 0.8266 0.7107 -0.0416 0.2350  -0.1065 119 LYS C C   
9082  O O   . LYS C 119 ? 1.0656 0.8353 0.7125 -0.0480 0.2211  -0.0987 119 LYS C O   
9083  C CB  . LYS C 119 ? 0.9530 0.7509 0.6616 -0.0121 0.2145  -0.0994 119 LYS C CB  
9084  C CG  . LYS C 119 ? 0.9444 0.7623 0.6880 0.0047  0.2186  -0.1024 119 LYS C CG  
9085  C CD  . LYS C 119 ? 0.9534 0.7524 0.6930 0.0154  0.2045  -0.0965 119 LYS C CD  
9086  C CE  . LYS C 119 ? 0.9597 0.7657 0.7215 0.0300  0.2133  -0.1018 119 LYS C CE  
9087  N NZ  . LYS C 119 ? 0.9371 0.7839 0.7422 0.0418  0.2169  -0.1027 119 LYS C NZ  
9088  N N   . GLU C 120 ? 1.0757 0.8393 0.7196 -0.0489 0.2548  -0.1166 120 GLU C N   
9089  C CA  . GLU C 120 ? 1.1225 0.8519 0.7180 -0.0661 0.2638  -0.1188 120 GLU C CA  
9090  C C   . GLU C 120 ? 1.1391 0.8237 0.6879 -0.0665 0.2478  -0.1132 120 GLU C C   
9091  O O   . GLU C 120 ? 1.2086 0.8691 0.7238 -0.0766 0.2403  -0.1082 120 GLU C O   
9092  C CB  . GLU C 120 ? 1.1363 0.8621 0.7254 -0.0733 0.2901  -0.1317 120 GLU C CB  
9093  N N   . LYS C 121 ? 1.0793 0.7538 0.6292 -0.0549 0.2406  -0.1139 121 LYS C N   
9094  C CA  . LYS C 121 ? 1.0852 0.7230 0.5984 -0.0530 0.2234  -0.1105 121 LYS C CA  
9095  C C   . LYS C 121 ? 1.0772 0.7294 0.6207 -0.0382 0.2061  -0.1057 121 LYS C C   
9096  O O   . LYS C 121 ? 1.0601 0.7346 0.6386 -0.0282 0.2128  -0.1082 121 LYS C O   
9097  C CB  . LYS C 121 ? 1.1056 0.7147 0.5912 -0.0557 0.2303  -0.1161 121 LYS C CB  
9098  N N   . LEU C 122 ? 1.0428 0.6813 0.5724 -0.0369 0.1842  -0.0995 122 LEU C N   
9099  C CA  . LEU C 122 ? 0.9962 0.6459 0.5517 -0.0251 0.1678  -0.0950 122 LEU C CA  
9100  C C   . LEU C 122 ? 1.0203 0.6373 0.5487 -0.0218 0.1601  -0.1003 122 LEU C C   
9101  O O   . LEU C 122 ? 1.0405 0.6273 0.5279 -0.0279 0.1518  -0.1025 122 LEU C O   
9102  C CB  . LEU C 122 ? 0.8899 0.5524 0.4551 -0.0260 0.1484  -0.0859 122 LEU C CB  
9103  C CG  . LEU C 122 ? 0.8765 0.5792 0.4814 -0.0249 0.1506  -0.0798 122 LEU C CG  
9104  C CD1 . LEU C 122 ? 0.8207 0.5352 0.4393 -0.0219 0.1290  -0.0712 122 LEU C CD1 
9105  C CD2 . LEU C 122 ? 0.8768 0.6067 0.5211 -0.0143 0.1632  -0.0820 122 LEU C CD2 
9106  N N   . ASN C 123 ? 1.0090 0.6315 0.5597 -0.0116 0.1624  -0.1030 123 ASN C N   
9107  C CA  . ASN C 123 ? 0.9705 0.5660 0.5022 -0.0079 0.1549  -0.1090 123 ASN C CA  
9108  C C   . ASN C 123 ? 0.9028 0.5009 0.4445 -0.0042 0.1331  -0.1044 123 ASN C C   
9109  O O   . ASN C 123 ? 0.8670 0.4852 0.4260 -0.0051 0.1236  -0.0961 123 ASN C O   
9110  C CB  . ASN C 123 ? 0.9602 0.5572 0.5089 0.0003  0.1691  -0.1151 123 ASN C CB  
9111  C CG  . ASN C 123 ? 0.9234 0.5506 0.5191 0.0111  0.1699  -0.1092 123 ASN C CG  
9112  O OD1 . ASN C 123 ? 0.8439 0.4858 0.4583 0.0138  0.1563  -0.1012 123 ASN C OD1 
9113  N ND2 . ASN C 123 ? 0.9092 0.5444 0.5226 0.0179  0.1860  -0.1137 123 ASN C ND2 
9114  N N   . ARG C 124 ? 1.0371 0.4373 0.3640 0.0801  0.0331  -0.0772 124 ARG C N   
9115  C CA  . ARG C 124 ? 0.9597 0.3762 0.3075 0.0646  0.0033  -0.0745 124 ARG C CA  
9116  C C   . ARG C 124 ? 0.9453 0.3892 0.3464 0.0659  0.0030  -0.0710 124 ARG C C   
9117  O O   . ARG C 124 ? 0.8580 0.3413 0.3033 0.0588  -0.0095 -0.0624 124 ARG C O   
9118  C CB  . ARG C 124 ? 1.0163 0.3974 0.3246 0.0510  -0.0184 -0.0822 124 ARG C CB  
9119  C CG  . ARG C 124 ? 1.0171 0.4118 0.3468 0.0346  -0.0477 -0.0817 124 ARG C CG  
9120  C CD  . ARG C 124 ? 1.1113 0.4789 0.4159 0.0201  -0.0678 -0.0876 124 ARG C CD  
9121  N NE  . ARG C 124 ? 1.1434 0.5297 0.4754 0.0032  -0.0946 -0.0863 124 ARG C NE  
9122  C CZ  . ARG C 124 ? 1.1290 0.5161 0.4847 -0.0026 -0.0982 -0.0885 124 ARG C CZ  
9123  N NH1 . ARG C 124 ? 1.1254 0.4949 0.4806 0.0087  -0.0781 -0.0919 124 ARG C NH1 
9124  N NH2 . ARG C 124 ? 1.0850 0.4932 0.4691 -0.0192 -0.1212 -0.0860 124 ARG C NH2 
9125  N N   . GLU C 125 ? 0.9193 0.3406 0.3148 0.0755  0.0165  -0.0775 125 GLU C N   
9126  C CA  . GLU C 125 ? 0.9887 0.4287 0.4268 0.0759  0.0133  -0.0739 125 GLU C CA  
9127  C C   . GLU C 125 ? 0.8831 0.3720 0.3751 0.0859  0.0260  -0.0633 125 GLU C C   
9128  O O   . GLU C 125 ? 0.8266 0.3459 0.3600 0.0814  0.0167  -0.0564 125 GLU C O   
9129  C CB  . GLU C 125 ? 1.1210 0.5189 0.5351 0.0849  0.0238  -0.0833 125 GLU C CB  
9130  C CG  . GLU C 125 ? 1.2858 0.6421 0.6609 0.0705  0.0063  -0.0920 125 GLU C CG  
9131  C CD  . GLU C 125 ? 1.3818 0.7227 0.7164 0.0600  -0.0039 -0.0951 125 GLU C CD  
9132  O OE1 . GLU C 125 ? 1.4347 0.7803 0.7672 0.0424  -0.0292 -0.0947 125 GLU C OE1 
9133  O OE2 . GLU C 125 ? 1.4229 0.7483 0.7300 0.0685  0.0116  -0.0973 125 GLU C OE2 
9134  N N   . GLU C 126 ? 0.8851 0.3816 0.3759 0.0984  0.0474  -0.0621 126 GLU C N   
9135  C CA  . GLU C 126 ? 0.8496 0.3935 0.3904 0.1053  0.0579  -0.0526 126 GLU C CA  
9136  C C   . GLU C 126 ? 0.8350 0.4122 0.3982 0.0926  0.0419  -0.0443 126 GLU C C   
9137  O O   . GLU C 126 ? 0.7357 0.3519 0.3454 0.0922  0.0395  -0.0369 126 GLU C O   
9138  C CB  . GLU C 126 ? 0.8703 0.4129 0.4035 0.1195  0.0853  -0.0536 126 GLU C CB  
9139  C CG  . GLU C 126 ? 0.8971 0.4196 0.4260 0.1362  0.1048  -0.0600 126 GLU C CG  
9140  C CD  . GLU C 126 ? 0.9938 0.4959 0.4924 0.1477  0.1314  -0.0653 126 GLU C CD  
9141  O OE1 . GLU C 126 ? 0.9936 0.4904 0.4657 0.1412  0.1338  -0.0642 126 GLU C OE1 
9142  O OE2 . GLU C 126 ? 1.0361 0.5317 0.5420 0.1615  0.1486  -0.0685 126 GLU C OE2 
9143  N N   . LEU C 127 ? 0.8286 0.3901 0.3586 0.0828  0.0306  -0.0456 127 LEU C N   
9144  C CA  . LEU C 127 ? 0.7678 0.3586 0.3192 0.0720  0.0141  -0.0378 127 LEU C CA  
9145  C C   . LEU C 127 ? 0.7502 0.3575 0.3296 0.0611  -0.0066 -0.0361 127 LEU C C   
9146  O O   . LEU C 127 ? 0.7176 0.3615 0.3359 0.0569  -0.0132 -0.0288 127 LEU C O   
9147  C CB  . LEU C 127 ? 0.7588 0.3264 0.2662 0.0651  0.0041  -0.0391 127 LEU C CB  
9148  C CG  . LEU C 127 ? 0.8066 0.3683 0.2931 0.0729  0.0232  -0.0363 127 LEU C CG  
9149  C CD1 . LEU C 127 ? 0.8349 0.3644 0.2667 0.0667  0.0119  -0.0379 127 LEU C CD1 
9150  C CD2 . LEU C 127 ? 0.7271 0.3311 0.2596 0.0741  0.0287  -0.0261 127 LEU C CD2 
9151  N N   . LEU C 128 ? 0.7965 0.3753 0.3551 0.0557  -0.0161 -0.0429 128 LEU C N   
9152  C CA  . LEU C 128 ? 0.7836 0.3761 0.3684 0.0445  -0.0329 -0.0409 128 LEU C CA  
9153  C C   . LEU C 128 ? 0.7263 0.3500 0.3561 0.0512  -0.0236 -0.0347 128 LEU C C   
9154  O O   . LEU C 128 ? 0.6157 0.2683 0.2786 0.0433  -0.0338 -0.0291 128 LEU C O   
9155  C CB  . LEU C 128 ? 0.8435 0.3950 0.3965 0.0380  -0.0410 -0.0497 128 LEU C CB  
9156  C CG  . LEU C 128 ? 0.9200 0.4558 0.4502 0.0207  -0.0649 -0.0539 128 LEU C CG  
9157  C CD1 . LEU C 128 ? 0.9997 0.4893 0.4946 0.0150  -0.0698 -0.0641 128 LEU C CD1 
9158  C CD2 . LEU C 128 ? 0.9054 0.4792 0.4776 0.0078  -0.0818 -0.0468 128 LEU C CD2 
9159  N N   . ASP C 129 ? 0.7137 0.3319 0.3446 0.0663  -0.0044 -0.0357 129 ASP C N   
9160  C CA  . ASP C 129 ? 0.7519 0.3998 0.4240 0.0740  0.0031  -0.0296 129 ASP C CA  
9161  C C   . ASP C 129 ? 0.7308 0.4206 0.4363 0.0737  0.0050  -0.0226 129 ASP C C   
9162  O O   . ASP C 129 ? 0.6634 0.3828 0.4036 0.0714  0.0005  -0.0170 129 ASP C O   
9163  C CB  . ASP C 129 ? 0.8006 0.4341 0.4682 0.0914  0.0223  -0.0325 129 ASP C CB  
9164  C CG  . ASP C 129 ? 0.8329 0.4298 0.4797 0.0934  0.0202  -0.0377 129 ASP C CG  
9165  O OD1 . ASP C 129 ? 0.7854 0.3634 0.4154 0.0793  0.0043  -0.0401 129 ASP C OD1 
9166  O OD2 . ASP C 129 ? 0.9040 0.4913 0.5535 0.1091  0.0345  -0.0390 129 ASP C OD2 
9167  N N   . LEU C 130 ? 0.6532 0.3431 0.3458 0.0757  0.0119  -0.0228 130 LEU C N   
9168  C CA  . LEU C 130 ? 0.6435 0.3684 0.3651 0.0747  0.0141  -0.0163 130 LEU C CA  
9169  C C   . LEU C 130 ? 0.6161 0.3590 0.3529 0.0618  -0.0048 -0.0126 130 LEU C C   
9170  O O   . LEU C 130 ? 0.5826 0.3574 0.3548 0.0602  -0.0065 -0.0078 130 LEU C O   
9171  C CB  . LEU C 130 ? 0.6434 0.3582 0.3425 0.0786  0.0261  -0.0166 130 LEU C CB  
9172  C CG  . LEU C 130 ? 0.6184 0.3643 0.3457 0.0792  0.0334  -0.0101 130 LEU C CG  
9173  C CD1 . LEU C 130 ? 0.5916 0.3644 0.3573 0.0874  0.0462  -0.0082 130 LEU C CD1 
9174  C CD2 . LEU C 130 ? 0.6371 0.3661 0.3345 0.0811  0.0448  -0.0094 130 LEU C CD2 
9175  N N   . GLN C 131 ? 0.5971 0.3201 0.3083 0.0525  -0.0195 -0.0154 131 GLN C N   
9176  C CA  . GLN C 131 ? 0.5406 0.2823 0.2702 0.0407  -0.0375 -0.0123 131 GLN C CA  
9177  C C   . GLN C 131 ? 0.5513 0.3100 0.3103 0.0368  -0.0411 -0.0106 131 GLN C C   
9178  O O   . GLN C 131 ? 0.5095 0.2986 0.3003 0.0334  -0.0445 -0.0060 131 GLN C O   
9179  C CB  . GLN C 131 ? 0.5577 0.2747 0.2561 0.0311  -0.0542 -0.0162 131 GLN C CB  
9180  C CG  . GLN C 131 ? 0.6067 0.3012 0.2672 0.0343  -0.0527 -0.0177 131 GLN C CG  
9181  C CD  . GLN C 131 ? 0.6437 0.3094 0.2688 0.0247  -0.0709 -0.0232 131 GLN C CD  
9182  O OE1 . GLN C 131 ? 0.6691 0.3136 0.2807 0.0201  -0.0751 -0.0294 131 GLN C OE1 
9183  N NE2 . GLN C 131 ? 0.7073 0.3713 0.3175 0.0211  -0.0835 -0.0207 131 GLN C NE2 
9184  N N   . THR C 132 ? 0.6001 0.3370 0.3463 0.0377  -0.0396 -0.0141 132 THR C N   
9185  C CA  . THR C 132 ? 0.6361 0.3837 0.4040 0.0321  -0.0444 -0.0115 132 THR C CA  
9186  C C   . THR C 132 ? 0.6621 0.4366 0.4599 0.0407  -0.0341 -0.0065 132 THR C C   
9187  O O   . THR C 132 ? 0.6146 0.4126 0.4376 0.0352  -0.0386 -0.0023 132 THR C O   
9188  C CB  . THR C 132 ? 0.6201 0.3326 0.3640 0.0306  -0.0457 -0.0160 132 THR C CB  
9189  O OG1 . THR C 132 ? 0.6657 0.3504 0.3775 0.0226  -0.0556 -0.0222 132 THR C OG1 
9190  C CG2 . THR C 132 ? 0.6076 0.3283 0.3704 0.0212  -0.0525 -0.0122 132 THR C CG2 
9191  N N   . LEU C 133 ? 0.6467 0.4188 0.4425 0.0541  -0.0203 -0.0071 133 LEU C N   
9192  C CA  . LEU C 133 ? 0.5688 0.3671 0.3938 0.0620  -0.0128 -0.0028 133 LEU C CA  
9193  C C   . LEU C 133 ? 0.5153 0.3468 0.3659 0.0584  -0.0138 0.0005  133 LEU C C   
9194  O O   . LEU C 133 ? 0.4970 0.3524 0.3727 0.0588  -0.0141 0.0039  133 LEU C O   
9195  C CB  . LEU C 133 ? 0.5473 0.3378 0.3684 0.0769  0.0021  -0.0046 133 LEU C CB  
9196  C CG  . LEU C 133 ? 0.5347 0.2981 0.3415 0.0841  0.0043  -0.0064 133 LEU C CG  
9197  C CD1 . LEU C 133 ? 0.5880 0.3382 0.3853 0.0994  0.0205  -0.0100 133 LEU C CD1 
9198  C CD2 . LEU C 133 ? 0.5345 0.3139 0.3646 0.0861  0.0001  -0.0006 133 LEU C CD2 
9199  N N   . ASN C 134 ? 0.4726 0.3038 0.3150 0.0550  -0.0150 -0.0003 134 ASN C N   
9200  C CA  . ASN C 134 ? 0.4845 0.3429 0.3497 0.0507  -0.0177 0.0028  134 ASN C CA  
9201  C C   . ASN C 134 ? 0.4922 0.3640 0.3725 0.0411  -0.0291 0.0044  134 ASN C C   
9202  O O   . ASN C 134 ? 0.5452 0.4408 0.4498 0.0403  -0.0283 0.0067  134 ASN C O   
9203  C CB  . ASN C 134 ? 0.5148 0.3658 0.3650 0.0492  -0.0184 0.0027  134 ASN C CB  
9204  C CG  . ASN C 134 ? 0.4965 0.3511 0.3484 0.0570  -0.0036 0.0037  134 ASN C CG  
9205  O OD1 . ASN C 134 ? 0.5502 0.4282 0.4273 0.0575  0.0008  0.0062  134 ASN C OD1 
9206  N ND2 . ASN C 134 ? 0.5132 0.3438 0.3375 0.0625  0.0051  0.0013  134 ASN C ND2 
9207  N N   . LEU C 135 ? 0.4553 0.3114 0.3213 0.0331  -0.0393 0.0029  135 LEU C N   
9208  C CA  . LEU C 135 ? 0.4492 0.3185 0.3314 0.0231  -0.0479 0.0046  135 LEU C CA  
9209  C C   . LEU C 135 ? 0.4368 0.3135 0.3308 0.0250  -0.0431 0.0070  135 LEU C C   
9210  O O   . LEU C 135 ? 0.3991 0.2989 0.3143 0.0223  -0.0427 0.0094  135 LEU C O   
9211  C CB  . LEU C 135 ? 0.4914 0.3407 0.3569 0.0133  -0.0590 0.0023  135 LEU C CB  
9212  C CG  . LEU C 135 ? 0.5012 0.3466 0.3574 0.0085  -0.0696 0.0006  135 LEU C CG  
9213  C CD1 . LEU C 135 ? 0.4682 0.2944 0.3098 -0.0028 -0.0820 -0.0024 135 LEU C CD1 
9214  C CD2 . LEU C 135 ? 0.5290 0.4051 0.4136 0.0063  -0.0736 0.0039  135 LEU C CD2 
9215  N N   . LEU C 136 ? 0.4484 0.3038 0.3267 0.0304  -0.0392 0.0064  136 LEU C N   
9216  C CA  . LEU C 136 ? 0.4626 0.3205 0.3479 0.0326  -0.0369 0.0099  136 LEU C CA  
9217  C C   . LEU C 136 ? 0.3962 0.2802 0.3024 0.0399  -0.0314 0.0123  136 LEU C C   
9218  O O   . LEU C 136 ? 0.3627 0.2570 0.2781 0.0383  -0.0325 0.0159  136 LEU C O   
9219  C CB  . LEU C 136 ? 0.4051 0.2325 0.2693 0.0399  -0.0338 0.0090  136 LEU C CB  
9220  C CG  . LEU C 136 ? 0.5035 0.3014 0.3463 0.0300  -0.0406 0.0068  136 LEU C CG  
9221  C CD1 . LEU C 136 ? 0.4843 0.2475 0.3044 0.0385  -0.0365 0.0052  136 LEU C CD1 
9222  C CD2 . LEU C 136 ? 0.4856 0.2926 0.3394 0.0165  -0.0469 0.0108  136 LEU C CD2 
9223  N N   . ALA C 137 ? 0.4414 0.3349 0.3538 0.0470  -0.0255 0.0106  137 ALA C N   
9224  C CA  . ALA C 137 ? 0.4731 0.3920 0.4073 0.0518  -0.0215 0.0120  137 ALA C CA  
9225  C C   . ALA C 137 ? 0.4223 0.3623 0.3718 0.0434  -0.0257 0.0129  137 ALA C C   
9226  O O   . ALA C 137 ? 0.3391 0.2954 0.3014 0.0449  -0.0253 0.0142  137 ALA C O   
9227  C CB  . ALA C 137 ? 0.4603 0.3856 0.3997 0.0576  -0.0138 0.0099  137 ALA C CB  
9228  N N   . TRP C 138 ? 0.4420 0.3823 0.3908 0.0353  -0.0297 0.0118  138 TRP C N   
9229  C CA  . TRP C 138 ? 0.4255 0.3856 0.3903 0.0287  -0.0317 0.0120  138 TRP C CA  
9230  C C   . TRP C 138 ? 0.4419 0.4005 0.4053 0.0206  -0.0352 0.0141  138 TRP C C   
9231  O O   . TRP C 138 ? 0.4040 0.3763 0.3793 0.0140  -0.0361 0.0138  138 TRP C O   
9232  C CB  . TRP C 138 ? 0.4355 0.3998 0.4051 0.0259  -0.0339 0.0104  138 TRP C CB  
9233  C CG  . TRP C 138 ? 0.4608 0.4269 0.4320 0.0324  -0.0287 0.0094  138 TRP C CG  
9234  C CD1 . TRP C 138 ? 0.4803 0.4306 0.4364 0.0374  -0.0255 0.0091  138 TRP C CD1 
9235  C CD2 . TRP C 138 ? 0.4652 0.4482 0.4530 0.0337  -0.0246 0.0085  138 TRP C CD2 
9236  N NE1 . TRP C 138 ? 0.4486 0.4061 0.4122 0.0413  -0.0188 0.0090  138 TRP C NE1 
9237  C CE2 . TRP C 138 ? 0.4947 0.4716 0.4781 0.0386  -0.0189 0.0085  138 TRP C CE2 
9238  C CE3 . TRP C 138 ? 0.4235 0.4238 0.4276 0.0307  -0.0243 0.0071  138 TRP C CE3 
9239  C CZ2 . TRP C 138 ? 0.5327 0.5204 0.5295 0.0395  -0.0137 0.0078  138 TRP C CZ2 
9240  C CZ3 . TRP C 138 ? 0.4692 0.4788 0.4847 0.0323  -0.0199 0.0054  138 TRP C CZ3 
9241  C CH2 . TRP C 138 ? 0.4786 0.4820 0.4914 0.0361  -0.0150 0.0060  138 TRP C CH2 
9242  N N   . CYS C 139 ? 0.4201 0.3612 0.3693 0.0212  -0.0360 0.0164  139 CYS C N   
9243  C CA  . CYS C 139 ? 0.4248 0.3614 0.3706 0.0125  -0.0378 0.0195  139 CYS C CA  
9244  C C   . CYS C 139 ? 0.4019 0.3570 0.3575 0.0114  -0.0346 0.0213  139 CYS C C   
9245  O O   . CYS C 139 ? 0.3649 0.3269 0.3221 0.0191  -0.0330 0.0216  139 CYS C O   
9246  C CB  . CYS C 139 ? 0.3961 0.3060 0.3224 0.0148  -0.0387 0.0223  139 CYS C CB  
9247  S SG  . CYS C 139 ? 0.5093 0.4078 0.4283 0.0019  -0.0399 0.0274  139 CYS C SG  
9248  N N   . GLY C 140 ? 0.3845 0.3482 0.3470 0.0013  -0.0334 0.0222  140 GLY C N   
9249  C CA  . GLY C 140 ? 0.3226 0.3008 0.2896 -0.0006 -0.0288 0.0232  140 GLY C CA  
9250  C C   . GLY C 140 ? 0.3818 0.3463 0.3317 -0.0028 -0.0277 0.0292  140 GLY C C   
9251  O O   . GLY C 140 ? 0.4932 0.4361 0.4298 -0.0044 -0.0302 0.0328  140 GLY C O   
9252  N N   . ARG C 141 ? 0.3799 0.3543 0.3273 -0.0032 -0.0240 0.0302  141 ARG C N   
9253  C CA  . ARG C 141 ? 0.3653 0.3258 0.2922 -0.0041 -0.0236 0.0370  141 ARG C CA  
9254  C C   . ARG C 141 ? 0.4248 0.3692 0.3434 -0.0152 -0.0206 0.0423  141 ARG C C   
9255  O O   . ARG C 141 ? 0.3756 0.2962 0.2758 -0.0143 -0.0231 0.0486  141 ARG C O   
9256  C CB  . ARG C 141 ? 0.4007 0.3743 0.3235 -0.0049 -0.0197 0.0361  141 ARG C CB  
9257  C CG  . ARG C 141 ? 0.4920 0.4497 0.3890 -0.0042 -0.0212 0.0440  141 ARG C CG  
9258  C CD  . ARG C 141 ? 0.6054 0.5738 0.4931 -0.0050 -0.0184 0.0422  141 ARG C CD  
9259  N NE  . ARG C 141 ? 0.6834 0.6570 0.5713 -0.0163 -0.0064 0.0415  141 ARG C NE  
9260  C CZ  . ARG C 141 ? 0.6450 0.6064 0.5105 -0.0233 0.0001  0.0482  141 ARG C CZ  
9261  N NH1 . ARG C 141 ? 0.6767 0.6176 0.5153 -0.0196 -0.0062 0.0568  141 ARG C NH1 
9262  N NH2 . ARG C 141 ? 0.6780 0.6474 0.5485 -0.0335 0.0134  0.0469  141 ARG C NH2 
9263  N N   . THR C 142 ? 0.4297 0.3868 0.3636 -0.0258 -0.0151 0.0399  142 THR C N   
9264  C CA  . THR C 142 ? 0.5187 0.4641 0.4495 -0.0390 -0.0116 0.0446  142 THR C CA  
9265  C C   . THR C 142 ? 0.6281 0.5492 0.5510 -0.0395 -0.0191 0.0459  142 THR C C   
9266  O O   . THR C 142 ? 0.8141 0.7106 0.7193 -0.0449 -0.0187 0.0521  142 THR C O   
9267  C CB  . THR C 142 ? 0.5386 0.5075 0.4955 -0.0490 -0.0057 0.0408  142 THR C CB  
9268  O OG1 . THR C 142 ? 0.5898 0.5782 0.5519 -0.0474 0.0031  0.0385  142 THR C OG1 
9269  C CG2 . THR C 142 ? 0.5703 0.5303 0.5279 -0.0647 -0.0012 0.0458  142 THR C CG2 
9270  N N   . LEU C 143 ? 0.5645 0.4890 0.4971 -0.0340 -0.0257 0.0399  143 LEU C N   
9271  C CA  . LEU C 143 ? 0.5227 0.4237 0.4467 -0.0365 -0.0321 0.0392  143 LEU C CA  
9272  C C   . LEU C 143 ? 0.5251 0.3983 0.4259 -0.0256 -0.0348 0.0420  143 LEU C C   
9273  O O   . LEU C 143 ? 0.5240 0.3717 0.4128 -0.0277 -0.0387 0.0413  143 LEU C O   
9274  C CB  . LEU C 143 ? 0.5137 0.4255 0.4516 -0.0348 -0.0380 0.0321  143 LEU C CB  
9275  C CG  . LEU C 143 ? 0.4753 0.4030 0.4340 -0.0484 -0.0397 0.0302  143 LEU C CG  
9276  C CD1 . LEU C 143 ? 0.3638 0.2909 0.3268 -0.0471 -0.0494 0.0247  143 LEU C CD1 
9277  C CD2 . LEU C 143 ? 0.4931 0.4059 0.4470 -0.0635 -0.0385 0.0345  143 LEU C CD2 
9278  N N   . ARG C 144 ? 0.5830 0.4599 0.4779 -0.0139 -0.0334 0.0447  144 ARG C N   
9279  C CA  . ARG C 144 ? 0.6486 0.5020 0.5265 -0.0015 -0.0364 0.0477  144 ARG C CA  
9280  C C   . ARG C 144 ? 0.6639 0.4838 0.5207 -0.0073 -0.0365 0.0544  144 ARG C C   
9281  O O   . ARG C 144 ? 0.7176 0.5106 0.5603 0.0008  -0.0390 0.0551  144 ARG C O   
9282  C CB  . ARG C 144 ? 0.6890 0.5549 0.5668 0.0108  -0.0370 0.0504  144 ARG C CB  
9283  C CG  . ARG C 144 ? 0.7221 0.6208 0.6182 0.0114  -0.0354 0.0457  144 ARG C CG  
9284  C CD  . ARG C 144 ? 0.7588 0.6652 0.6490 0.0184  -0.0374 0.0497  144 ARG C CD  
9285  N NE  . ARG C 144 ? 0.7372 0.6373 0.6119 0.0096  -0.0344 0.0561  144 ARG C NE  
9286  C CZ  . ARG C 144 ? 0.7476 0.6458 0.6076 0.0143  -0.0375 0.0615  144 ARG C CZ  
9287  N NH1 . ARG C 144 ? 0.7783 0.6836 0.6420 0.0276  -0.0451 0.0611  144 ARG C NH1 
9288  N NH2 . ARG C 144 ? 0.6776 0.5674 0.5193 0.0055  -0.0332 0.0677  144 ARG C NH2 
9289  N N   . LYS C 145 ? 0.6249 0.4443 0.4789 -0.0213 -0.0323 0.0595  145 LYS C N   
9290  C CA  . LYS C 145 ? 0.6820 0.4673 0.5153 -0.0292 -0.0313 0.0668  145 LYS C CA  
9291  C C   . LYS C 145 ? 0.6806 0.4452 0.5127 -0.0380 -0.0345 0.0619  145 LYS C C   
9292  O O   . LYS C 145 ? 0.6726 0.4025 0.4856 -0.0332 -0.0373 0.0631  145 LYS C O   
9293  C CB  . LYS C 145 ? 0.8155 0.6079 0.6478 -0.0438 -0.0237 0.0732  145 LYS C CB  
9294  C CG  . LYS C 145 ? 0.9412 0.7629 0.7793 -0.0388 -0.0198 0.0738  145 LYS C CG  
9295  C CD  . LYS C 145 ? 1.0210 0.8389 0.8461 -0.0203 -0.0257 0.0768  145 LYS C CD  
9296  C CE  . LYS C 145 ? 1.0557 0.8853 0.8704 -0.0201 -0.0224 0.0817  145 LYS C CE  
9297  N NZ  . LYS C 145 ? 1.0599 0.9238 0.8952 -0.0260 -0.0164 0.0740  145 LYS C NZ  
9298  N N   . ASP C 146 ? 0.5989 0.3836 0.4507 -0.0507 -0.0349 0.0560  146 ASP C N   
9299  C CA  . ASP C 146 ? 0.6942 0.4605 0.5444 -0.0621 -0.0402 0.0511  146 ASP C CA  
9300  C C   . ASP C 146 ? 0.6458 0.3995 0.4879 -0.0499 -0.0466 0.0433  146 ASP C C   
9301  O O   . ASP C 146 ? 0.6942 0.4202 0.5234 -0.0563 -0.0515 0.0393  146 ASP C O   
9302  C CB  . ASP C 146 ? 0.8501 0.6456 0.7274 -0.0783 -0.0408 0.0475  146 ASP C CB  
9303  C CG  . ASP C 146 ? 1.0117 0.8265 0.9008 -0.0888 -0.0310 0.0541  146 ASP C CG  
9304  O OD1 . ASP C 146 ? 1.0806 0.8740 0.9581 -0.1007 -0.0264 0.0610  146 ASP C OD1 
9305  O OD2 . ASP C 146 ? 1.0269 0.8759 0.9353 -0.0852 -0.0269 0.0525  146 ASP C OD2 
9306  N N   . LEU C 147 ? 0.5828 0.3553 0.4312 -0.0336 -0.0460 0.0406  147 LEU C N   
9307  C CA  . LEU C 147 ? 0.5476 0.3111 0.3890 -0.0218 -0.0491 0.0334  147 LEU C CA  
9308  C C   . LEU C 147 ? 0.6240 0.3662 0.4491 -0.0038 -0.0462 0.0357  147 LEU C C   
9309  O O   . LEU C 147 ? 0.6238 0.3616 0.4448 0.0083  -0.0455 0.0302  147 LEU C O   
9310  C CB  . LEU C 147 ? 0.5015 0.3001 0.3629 -0.0165 -0.0492 0.0289  147 LEU C CB  
9311  C CG  . LEU C 147 ? 0.5026 0.3226 0.3820 -0.0300 -0.0538 0.0253  147 LEU C CG  
9312  C CD1 . LEU C 147 ? 0.4858 0.3336 0.3806 -0.0214 -0.0534 0.0218  147 LEU C CD1 
9313  C CD2 . LEU C 147 ? 0.5514 0.3473 0.4182 -0.0401 -0.0618 0.0203  147 LEU C CD2 
9314  N N   . LYS C 148 ? 0.6519 0.3805 0.4677 -0.0016 -0.0440 0.0442  148 LYS C N   
9315  C CA  . LYS C 148 ? 0.6667 0.3818 0.4730 0.0177  -0.0425 0.0479  148 LYS C CA  
9316  C C   . LYS C 148 ? 0.6695 0.3473 0.4567 0.0261  -0.0422 0.0432  148 LYS C C   
9317  O O   . LYS C 148 ? 0.6740 0.3502 0.4615 0.0447  -0.0396 0.0416  148 LYS C O   
9318  C CB  . LYS C 148 ? 0.6249 0.3290 0.4212 0.0171  -0.0422 0.0591  148 LYS C CB  
9319  C CG  . LYS C 148 ? 0.6764 0.3582 0.4600 0.0365  -0.0430 0.0644  148 LYS C CG  
9320  C CD  . LYS C 148 ? 0.7460 0.4300 0.5235 0.0390  -0.0447 0.0762  148 LYS C CD  
9321  C CE  . LYS C 148 ? 0.8498 0.5317 0.6205 0.0176  -0.0422 0.0814  148 LYS C CE  
9322  N NZ  . LYS C 148 ? 0.8837 0.5695 0.6447 0.0189  -0.0427 0.0926  148 LYS C NZ  
9323  N N   . ASP C 149 ? 0.6607 0.3079 0.4318 0.0127  -0.0443 0.0405  149 ASP C N   
9324  C CA  . ASP C 149 ? 0.8212 0.4295 0.5705 0.0201  -0.0437 0.0341  149 ASP C CA  
9325  C C   . ASP C 149 ? 0.7069 0.3279 0.4599 0.0279  -0.0422 0.0240  149 ASP C C   
9326  O O   . ASP C 149 ? 0.7061 0.3107 0.4491 0.0449  -0.0370 0.0202  149 ASP C O   
9327  C CB  . ASP C 149 ? 1.0282 0.6006 0.7588 0.0012  -0.0476 0.0320  149 ASP C CB  
9328  C CG  . ASP C 149 ? 1.2112 0.7599 0.9315 -0.0043 -0.0466 0.0429  149 ASP C CG  
9329  O OD1 . ASP C 149 ? 1.2394 0.8002 0.9653 0.0078  -0.0440 0.0519  149 ASP C OD1 
9330  O OD2 . ASP C 149 ? 1.2805 0.7982 0.9865 -0.0212 -0.0489 0.0428  149 ASP C OD2 
9331  N N   . LEU C 150 ? 0.6719 0.3220 0.4394 0.0167  -0.0457 0.0201  150 LEU C N   
9332  C CA  . LEU C 150 ? 0.6468 0.3092 0.4161 0.0242  -0.0439 0.0123  150 LEU C CA  
9333  C C   . LEU C 150 ? 0.6765 0.3663 0.4634 0.0421  -0.0369 0.0149  150 LEU C C   
9334  O O   . LEU C 150 ? 0.6604 0.3478 0.4431 0.0545  -0.0310 0.0098  150 LEU C O   
9335  C CB  . LEU C 150 ? 0.6064 0.2925 0.3874 0.0086  -0.0509 0.0090  150 LEU C CB  
9336  C CG  . LEU C 150 ? 0.6678 0.3309 0.4358 -0.0106 -0.0598 0.0055  150 LEU C CG  
9337  C CD1 . LEU C 150 ? 0.6620 0.3537 0.4470 -0.0236 -0.0680 0.0030  150 LEU C CD1 
9338  C CD2 . LEU C 150 ? 0.7022 0.3198 0.4366 -0.0073 -0.0603 -0.0026 150 LEU C CD2 
9339  N N   . LEU C 151 ? 0.6476 0.3634 0.4536 0.0428  -0.0373 0.0226  151 LEU C N   
9340  C CA  . LEU C 151 ? 0.6700 0.4136 0.4948 0.0578  -0.0328 0.0247  151 LEU C CA  
9341  C C   . LEU C 151 ? 0.7370 0.4614 0.5550 0.0768  -0.0279 0.0261  151 LEU C C   
9342  O O   . LEU C 151 ? 0.7360 0.4745 0.5655 0.0905  -0.0218 0.0234  151 LEU C O   
9343  C CB  . LEU C 151 ? 0.6528 0.4248 0.4949 0.0529  -0.0358 0.0317  151 LEU C CB  
9344  C CG  . LEU C 151 ? 0.5697 0.3703 0.4269 0.0394  -0.0378 0.0293  151 LEU C CG  
9345  C CD1 . LEU C 151 ? 0.5654 0.3858 0.4328 0.0325  -0.0393 0.0355  151 LEU C CD1 
9346  C CD2 . LEU C 151 ? 0.5407 0.3649 0.4125 0.0461  -0.0346 0.0242  151 LEU C CD2 
9347  N N   . ASN C 152 ? 0.7759 0.4675 0.5764 0.0780  -0.0297 0.0304  152 ASN C N   
9348  C CA  . ASN C 152 ? 0.8204 0.4903 0.6144 0.0977  -0.0255 0.0322  152 ASN C CA  
9349  C C   . ASN C 152 ? 0.8583 0.4979 0.6340 0.1050  -0.0182 0.0228  152 ASN C C   
9350  O O   . ASN C 152 ? 0.8812 0.5114 0.6582 0.1246  -0.0112 0.0221  152 ASN C O   
9351  C CB  . ASN C 152 ? 0.8729 0.5134 0.6516 0.0969  -0.0300 0.0410  152 ASN C CB  
9352  C CG  . ASN C 152 ? 0.8479 0.5140 0.6392 0.0927  -0.0360 0.0512  152 ASN C CG  
9353  O OD1 . ASN C 152 ? 0.7899 0.4943 0.6036 0.0978  -0.0369 0.0520  152 ASN C OD1 
9354  N ND2 . ASN C 152 ? 0.8820 0.5246 0.6565 0.0826  -0.0397 0.0587  152 ASN C ND2 
9355  N N   . LYS C 153 ? 0.8139 0.4374 0.5720 0.0899  -0.0200 0.0155  153 LYS C N   
9356  C CA  . LYS C 153 ? 0.8293 0.4228 0.5646 0.0954  -0.0135 0.0054  153 LYS C CA  
9357  C C   . LYS C 153 ? 0.7795 0.3973 0.5289 0.1101  -0.0032 0.0015  153 LYS C C   
9358  O O   . LYS C 153 ? 0.8412 0.4426 0.5847 0.1279  0.0074  -0.0019 153 LYS C O   
9359  C CB  . LYS C 153 ? 0.7817 0.3613 0.4983 0.0745  -0.0207 -0.0014 153 LYS C CB  
9360  C CG  . LYS C 153 ? 0.8499 0.3906 0.5341 0.0772  -0.0164 -0.0125 153 LYS C CG  
9361  C CD  . LYS C 153 ? 0.8709 0.3926 0.5350 0.0547  -0.0280 -0.0181 153 LYS C CD  
9362  C CE  . LYS C 153 ? 0.9428 0.4254 0.5700 0.0567  -0.0250 -0.0304 153 LYS C CE  
9363  N NZ  . LYS C 153 ? 0.9596 0.4166 0.5638 0.0346  -0.0387 -0.0368 153 LYS C NZ  
9364  N N   . GLY C 154 ? 0.7191 0.3756 0.4882 0.1029  -0.0049 0.0021  154 GLY C N   
9365  C CA  . GLY C 154 ? 0.6945 0.3793 0.4820 0.1139  0.0046  0.0003  154 GLY C CA  
9366  C C   . GLY C 154 ? 0.7692 0.4374 0.5356 0.1161  0.0138  -0.0087 154 GLY C C   
9367  O O   . GLY C 154 ? 0.7687 0.4611 0.5493 0.1216  0.0223  -0.0097 154 GLY C O   
9368  N N   . ARG C 155 ? 0.8259 0.4521 0.5570 0.1112  0.0123  -0.0154 155 ARG C N   
9369  C CA  . ARG C 155 ? 0.8712 0.4757 0.5750 0.1149  0.0218  -0.0246 155 ARG C CA  
9370  C C   . ARG C 155 ? 0.8800 0.4394 0.5437 0.1028  0.0134  -0.0319 155 ARG C C   
9371  O O   . ARG C 155 ? 0.8698 0.4117 0.5288 0.0945  0.0035  -0.0300 155 ARG C O   
9372  C CB  . ARG C 155 ? 0.8679 0.4638 0.5728 0.1374  0.0403  -0.0273 155 ARG C CB  
9373  C CG  . ARG C 155 ? 0.8930 0.4551 0.5877 0.1488  0.0423  -0.0277 155 ARG C CG  
9374  C CD  . ARG C 155 ? 0.9335 0.4912 0.6342 0.1730  0.0619  -0.0307 155 ARG C CD  
9375  N NE  . ARG C 155 ? 0.9261 0.5339 0.6724 0.1831  0.0673  -0.0234 155 ARG C NE  
9376  C CZ  . ARG C 155 ? 0.9714 0.6000 0.7317 0.1930  0.0837  -0.0259 155 ARG C CZ  
9377  N NH1 . ARG C 155 ? 0.9228 0.5979 0.7276 0.1997  0.0863  -0.0192 155 ARG C NH1 
9378  N NH2 . ARG C 155 ? 1.0244 0.6261 0.7528 0.1954  0.0978  -0.0352 155 ARG C NH2 
9379  N N   . ASN C 156 ? 0.8738 0.4136 0.5072 0.1013  0.0175  -0.0404 156 ASN C N   
9380  C CA  . ASN C 156 ? 0.9545 0.4480 0.5443 0.0908  0.0100  -0.0497 156 ASN C CA  
9381  C C   . ASN C 156 ? 0.7647 0.2614 0.3580 0.0682  -0.0111 -0.0473 156 ASN C C   
9382  O O   . ASN C 156 ? 0.8739 0.3396 0.4519 0.0599  -0.0188 -0.0497 156 ASN C O   
9383  C CB  . ASN C 156 ? 1.0464 0.4939 0.6115 0.1038  0.0201  -0.0559 156 ASN C CB  
9384  C CG  . ASN C 156 ? 1.1552 0.6000 0.7174 0.1266  0.0430  -0.0596 156 ASN C CG  
9385  O OD1 . ASN C 156 ? 1.1929 0.6585 0.7574 0.1292  0.0512  -0.0601 156 ASN C OD1 
9386  N ND2 . ASN C 156 ? 1.2200 0.6378 0.7770 0.1432  0.0540  -0.0619 156 ASN C ND2 
9387  N N   . TYR C 157 ? 0.7264 0.2600 0.3397 0.0582  -0.0196 -0.0428 157 TYR C N   
9388  C CA  . TYR C 157 ? 0.8140 0.3598 0.4370 0.0376  -0.0383 -0.0404 157 TYR C CA  
9389  C C   . TYR C 157 ? 0.8746 0.3951 0.4632 0.0247  -0.0506 -0.0490 157 TYR C C   
9390  O O   . TYR C 157 ? 0.8913 0.3960 0.4515 0.0314  -0.0450 -0.0549 157 TYR C O   
9391  C CB  . TYR C 157 ? 0.7435 0.3410 0.4056 0.0351  -0.0409 -0.0318 157 TYR C CB  
9392  C CG  . TYR C 157 ? 0.7343 0.3583 0.4296 0.0449  -0.0325 -0.0236 157 TYR C CG  
9393  C CD1 . TYR C 157 ? 0.6678 0.2959 0.3785 0.0373  -0.0385 -0.0180 157 TYR C CD1 
9394  C CD2 . TYR C 157 ? 0.7279 0.3723 0.4383 0.0610  -0.0189 -0.0212 157 TYR C CD2 
9395  C CE1 . TYR C 157 ? 0.6423 0.2923 0.3784 0.0462  -0.0326 -0.0103 157 TYR C CE1 
9396  C CE2 . TYR C 157 ? 0.6745 0.3434 0.4146 0.0692  -0.0140 -0.0141 157 TYR C CE2 
9397  C CZ  . TYR C 157 ? 0.6418 0.3125 0.3927 0.0622  -0.0216 -0.0087 157 TYR C CZ  
9398  O OH  . TYR C 157 ? 0.5490 0.2418 0.3247 0.0704  -0.0185 -0.0014 157 TYR C OH  
9399  N N   . THR C 158 ? 0.8555 0.3727 0.4467 0.0054  -0.0679 -0.0493 158 THR C N   
9400  C CA  . THR C 158 ? 0.8956 0.3935 0.4596 -0.0097 -0.0846 -0.0569 158 THR C CA  
9401  C C   . THR C 158 ? 0.8287 0.3689 0.4206 -0.0203 -0.0985 -0.0513 158 THR C C   
9402  O O   . THR C 158 ? 0.7938 0.3746 0.4267 -0.0197 -0.0962 -0.0424 158 THR C O   
9403  C CB  . THR C 158 ? 0.9095 0.3740 0.4589 -0.0260 -0.0962 -0.0621 158 THR C CB  
9404  O OG1 . THR C 158 ? 0.8408 0.3359 0.4309 -0.0381 -0.1025 -0.0534 158 THR C OG1 
9405  C CG2 . THR C 158 ? 0.9297 0.3485 0.4516 -0.0146 -0.0824 -0.0673 158 THR C CG2 
9406  N N   . GLN C 159 ? 0.7757 0.3038 0.3430 -0.0296 -0.1137 -0.0571 159 GLN C N   
9407  C CA  . GLN C 159 ? 0.7776 0.3416 0.3704 -0.0406 -0.1307 -0.0524 159 GLN C CA  
9408  C C   . GLN C 159 ? 0.7790 0.3684 0.4124 -0.0559 -0.1399 -0.0476 159 GLN C C   
9409  O O   . GLN C 159 ? 0.7393 0.3719 0.4127 -0.0573 -0.1420 -0.0398 159 GLN C O   
9410  C CB  . GLN C 159 ? 0.8374 0.3778 0.3931 -0.0497 -0.1494 -0.0600 159 GLN C CB  
9411  C CG  . GLN C 159 ? 0.8942 0.4710 0.4770 -0.0598 -0.1695 -0.0549 159 GLN C CG  
9412  C CD  . GLN C 159 ? 0.8448 0.4544 0.4464 -0.0460 -0.1609 -0.0464 159 GLN C CD  
9413  O OE1 . GLN C 159 ? 0.8980 0.4961 0.4794 -0.0308 -0.1435 -0.0462 159 GLN C OE1 
9414  N NE2 . GLN C 159 ? 0.7467 0.3969 0.3881 -0.0516 -0.1726 -0.0395 159 GLN C NE2 
9415  N N   . GLU C 160 ? 0.8600 0.4213 0.4830 -0.0675 -0.1439 -0.0520 160 GLU C N   
9416  C CA  . GLU C 160 ? 0.8656 0.4488 0.5256 -0.0837 -0.1505 -0.0469 160 GLU C CA  
9417  C C   . GLU C 160 ? 0.7954 0.4111 0.4915 -0.0742 -0.1344 -0.0367 160 GLU C C   
9418  O O   . GLU C 160 ? 0.7757 0.4305 0.5109 -0.0818 -0.1377 -0.0301 160 GLU C O   
9419  C CB  . GLU C 160 ? 0.9541 0.4950 0.5925 -0.0971 -0.1545 -0.0531 160 GLU C CB  
9420  C CG  . GLU C 160 ? 1.1053 0.6140 0.7094 -0.1110 -0.1738 -0.0643 160 GLU C CG  
9421  C CD  . GLU C 160 ? 1.2093 0.6706 0.7581 -0.0974 -0.1672 -0.0740 160 GLU C CD  
9422  O OE1 . GLU C 160 ? 1.2219 0.6879 0.7535 -0.0880 -0.1689 -0.0758 160 GLU C OE1 
9423  O OE2 . GLU C 160 ? 1.2937 0.7109 0.8151 -0.0960 -0.1591 -0.0797 160 GLU C OE2 
9424  N N   . GLU C 161 ? 0.7667 0.3671 0.4501 -0.0571 -0.1170 -0.0355 161 GLU C N   
9425  C CA  . GLU C 161 ? 0.6871 0.3152 0.4008 -0.0483 -0.1038 -0.0262 161 GLU C CA  
9426  C C   . GLU C 161 ? 0.7247 0.3972 0.4660 -0.0411 -0.1017 -0.0212 161 GLU C C   
9427  O O   . GLU C 161 ? 0.6802 0.3859 0.4547 -0.0431 -0.0986 -0.0141 161 GLU C O   
9428  C CB  . GLU C 161 ? 0.7158 0.3183 0.4110 -0.0308 -0.0881 -0.0262 161 GLU C CB  
9429  C CG  . GLU C 161 ? 0.7603 0.3176 0.4313 -0.0365 -0.0883 -0.0295 161 GLU C CG  
9430  C CD  . GLU C 161 ? 0.8371 0.3658 0.4873 -0.0163 -0.0737 -0.0310 161 GLU C CD  
9431  O OE1 . GLU C 161 ? 0.8579 0.3912 0.5007 -0.0004 -0.0651 -0.0337 161 GLU C OE1 
9432  O OE2 . GLU C 161 ? 0.9789 0.4808 0.6216 -0.0161 -0.0701 -0.0288 161 GLU C OE2 
9433  N N   . LYS C 162 ? 0.7629 0.4338 0.4883 -0.0330 -0.1028 -0.0248 162 LYS C N   
9434  C CA  . LYS C 162 ? 0.6786 0.3872 0.4280 -0.0276 -0.1022 -0.0202 162 LYS C CA  
9435  C C   . LYS C 162 ? 0.6421 0.3808 0.4220 -0.0421 -0.1160 -0.0172 162 LYS C C   
9436  O O   . LYS C 162 ? 0.6240 0.3986 0.4371 -0.0400 -0.1121 -0.0113 162 LYS C O   
9437  C CB  . LYS C 162 ? 0.6327 0.3278 0.3540 -0.0190 -0.1023 -0.0241 162 LYS C CB  
9438  C CG  . LYS C 162 ? 0.5544 0.2816 0.2958 -0.0113 -0.0988 -0.0189 162 LYS C CG  
9439  C CD  . LYS C 162 ? 0.5869 0.2944 0.2947 -0.0028 -0.0962 -0.0219 162 LYS C CD  
9440  C CE  . LYS C 162 ? 0.6245 0.3090 0.3025 -0.0132 -0.1149 -0.0272 162 LYS C CE  
9441  N NZ  . LYS C 162 ? 0.6592 0.3278 0.3036 -0.0057 -0.1138 -0.0282 162 LYS C NZ  
9442  N N   . GLU C 163 ? 0.6887 0.4134 0.4585 -0.0570 -0.1323 -0.0218 163 GLU C N   
9443  C CA  . GLU C 163 ? 0.7135 0.4687 0.5164 -0.0713 -0.1462 -0.0193 163 GLU C CA  
9444  C C   . GLU C 163 ? 0.6868 0.4616 0.5222 -0.0795 -0.1391 -0.0140 163 GLU C C   
9445  O O   . GLU C 163 ? 0.6917 0.5035 0.5644 -0.0850 -0.1417 -0.0097 163 GLU C O   
9446  C CB  . GLU C 163 ? 0.7297 0.4643 0.5142 -0.0864 -0.1668 -0.0260 163 GLU C CB  
9447  C CG  . GLU C 163 ? 0.7617 0.4908 0.5238 -0.0809 -0.1789 -0.0289 163 GLU C CG  
9448  C CD  . GLU C 163 ? 0.8557 0.5492 0.5812 -0.0929 -0.1973 -0.0378 163 GLU C CD  
9449  O OE1 . GLU C 163 ? 0.8298 0.5077 0.5236 -0.0873 -0.2057 -0.0409 163 GLU C OE1 
9450  O OE2 . GLU C 163 ? 0.8691 0.5484 0.5955 -0.1085 -0.2035 -0.0417 163 GLU C OE2 
9451  N N   . TYR C 164 ? 0.7083 0.4579 0.5293 -0.0799 -0.1293 -0.0139 164 TYR C N   
9452  C CA  . TYR C 164 ? 0.6841 0.4491 0.5307 -0.0871 -0.1212 -0.0077 164 TYR C CA  
9453  C C   . TYR C 164 ? 0.6602 0.4586 0.5306 -0.0746 -0.1086 -0.0013 164 TYR C C   
9454  O O   . TYR C 164 ? 0.6117 0.4386 0.5123 -0.0815 -0.1052 0.0035  164 TYR C O   
9455  C CB  . TYR C 164 ? 0.7005 0.4268 0.5223 -0.0882 -0.1139 -0.0077 164 TYR C CB  
9456  C CG  . TYR C 164 ? 0.7228 0.4611 0.5651 -0.0945 -0.1044 0.0003  164 TYR C CG  
9457  C CD1 . TYR C 164 ? 0.7792 0.5228 0.6387 -0.1155 -0.1094 0.0021  164 TYR C CD1 
9458  C CD2 . TYR C 164 ? 0.7232 0.4683 0.5673 -0.0802 -0.0906 0.0063  164 TYR C CD2 
9459  C CE1 . TYR C 164 ? 0.7869 0.5397 0.6617 -0.1218 -0.0987 0.0101  164 TYR C CE1 
9460  C CE2 . TYR C 164 ? 0.7542 0.5080 0.6116 -0.0860 -0.0823 0.0141  164 TYR C CE2 
9461  C CZ  . TYR C 164 ? 0.7827 0.5390 0.6537 -0.1066 -0.0853 0.0162  164 TYR C CZ  
9462  O OH  . TYR C 164 ? 0.7634 0.5261 0.6439 -0.1127 -0.0750 0.0245  164 TYR C OH  
9463  N N   . VAL C 165 ? 0.6147 0.4089 0.4714 -0.0570 -0.1008 -0.0018 165 VAL C N   
9464  C CA  . VAL C 165 ? 0.5366 0.3601 0.4141 -0.0460 -0.0901 0.0031  165 VAL C CA  
9465  C C   . VAL C 165 ? 0.5118 0.3700 0.4167 -0.0480 -0.0957 0.0039  165 VAL C C   
9466  O O   . VAL C 165 ? 0.4304 0.3174 0.3619 -0.0476 -0.0895 0.0077  165 VAL C O   
9467  C CB  . VAL C 165 ? 0.5198 0.3312 0.3788 -0.0281 -0.0810 0.0020  165 VAL C CB  
9468  C CG1 . VAL C 165 ? 0.4100 0.2527 0.2915 -0.0185 -0.0723 0.0060  165 VAL C CG1 
9469  C CG2 . VAL C 165 ? 0.4944 0.2742 0.3314 -0.0237 -0.0747 0.0021  165 VAL C CG2 
9470  N N   . LEU C 166 ? 0.5044 0.3583 0.4010 -0.0492 -0.1076 0.0002  166 LEU C N   
9471  C CA  . LEU C 166 ? 0.5062 0.3908 0.4286 -0.0498 -0.1147 0.0016  166 LEU C CA  
9472  C C   . LEU C 166 ? 0.5200 0.4299 0.4763 -0.0637 -0.1190 0.0037  166 LEU C C   
9473  O O   . LEU C 166 ? 0.5368 0.4789 0.5241 -0.0614 -0.1155 0.0066  166 LEU C O   
9474  C CB  . LEU C 166 ? 0.5116 0.3824 0.4139 -0.0490 -0.1291 -0.0019 166 LEU C CB  
9475  C CG  . LEU C 166 ? 0.5032 0.3589 0.3795 -0.0338 -0.1221 -0.0025 166 LEU C CG  
9476  C CD1 . LEU C 166 ? 0.5616 0.3919 0.4051 -0.0351 -0.1355 -0.0066 166 LEU C CD1 
9477  C CD2 . LEU C 166 ? 0.5221 0.4060 0.4219 -0.0244 -0.1159 0.0018  166 LEU C CD2 
9478  N N   . ASN C 167 ? 0.5184 0.4132 0.4695 -0.0783 -0.1254 0.0020  167 ASN C N   
9479  C CA  . ASN C 167 ? 0.5609 0.4799 0.5461 -0.0936 -0.1276 0.0042  167 ASN C CA  
9480  C C   . ASN C 167 ? 0.5307 0.4672 0.5337 -0.0916 -0.1096 0.0094  167 ASN C C   
9481  O O   . ASN C 167 ? 0.5134 0.4838 0.5510 -0.0941 -0.1057 0.0118  167 ASN C O   
9482  C CB  . ASN C 167 ? 0.6217 0.5157 0.5942 -0.1111 -0.1366 0.0013  167 ASN C CB  
9483  C CG  . ASN C 167 ? 0.7391 0.6255 0.7036 -0.1178 -0.1581 -0.0041 167 ASN C CG  
9484  O OD1 . ASN C 167 ? 0.7191 0.6307 0.7021 -0.1135 -0.1678 -0.0037 167 ASN C OD1 
9485  N ND2 . ASN C 167 ? 0.7873 0.6371 0.7223 -0.1281 -0.1665 -0.0093 167 ASN C ND2 
9486  N N   . LYS C 168 ? 0.5358 0.4488 0.5146 -0.0861 -0.0985 0.0110  168 LYS C N   
9487  C CA  . LYS C 168 ? 0.5229 0.4490 0.5120 -0.0836 -0.0831 0.0161  168 LYS C CA  
9488  C C   . LYS C 168 ? 0.4898 0.4446 0.4966 -0.0710 -0.0770 0.0165  168 LYS C C   
9489  O O   . LYS C 168 ? 0.5048 0.4835 0.5333 -0.0729 -0.0675 0.0191  168 LYS C O   
9490  C CB  . LYS C 168 ? 0.4742 0.3689 0.4325 -0.0772 -0.0754 0.0181  168 LYS C CB  
9491  C CG  . LYS C 168 ? 0.5004 0.3611 0.4387 -0.0891 -0.0798 0.0178  168 LYS C CG  
9492  C CD  . LYS C 168 ? 0.5808 0.4516 0.5390 -0.1081 -0.0772 0.0218  168 LYS C CD  
9493  C CE  . LYS C 168 ? 0.6612 0.5399 0.6223 -0.1060 -0.0618 0.0290  168 LYS C CE  
9494  N NZ  . LYS C 168 ? 0.7371 0.6236 0.7151 -0.1252 -0.0560 0.0337  168 LYS C NZ  
9495  N N   . TYR C 169 ? 0.4625 0.4135 0.4587 -0.0586 -0.0813 0.0137  169 TYR C N   
9496  C CA  . TYR C 169 ? 0.3799 0.3538 0.3910 -0.0471 -0.0757 0.0139  169 TYR C CA  
9497  C C   . TYR C 169 ? 0.4302 0.4350 0.4754 -0.0515 -0.0797 0.0139  169 TYR C C   
9498  O O   . TYR C 169 ? 0.4136 0.4411 0.4791 -0.0478 -0.0703 0.0147  169 TYR C O   
9499  C CB  . TYR C 169 ? 0.3329 0.2936 0.3248 -0.0347 -0.0789 0.0116  169 TYR C CB  
9500  C CG  . TYR C 169 ? 0.3375 0.2799 0.3070 -0.0253 -0.0701 0.0119  169 TYR C CG  
9501  C CD1 . TYR C 169 ? 0.3752 0.3088 0.3379 -0.0277 -0.0632 0.0144  169 TYR C CD1 
9502  C CD2 . TYR C 169 ? 0.3500 0.2844 0.3063 -0.0139 -0.0685 0.0104  169 TYR C CD2 
9503  C CE1 . TYR C 169 ? 0.3837 0.3028 0.3293 -0.0176 -0.0570 0.0152  169 TYR C CE1 
9504  C CE2 . TYR C 169 ? 0.3669 0.2888 0.3085 -0.0049 -0.0604 0.0106  169 TYR C CE2 
9505  C CZ  . TYR C 169 ? 0.3861 0.3015 0.3237 -0.0062 -0.0556 0.0129  169 TYR C CZ  
9506  O OH  . TYR C 169 ? 0.4410 0.3463 0.3674 0.0042  -0.0493 0.0136  169 TYR C OH  
9507  N N   . PHE C 170 ? 0.4369 0.4427 0.4887 -0.0586 -0.0941 0.0125  170 PHE C N   
9508  C CA  . PHE C 170 ? 0.4228 0.4608 0.5120 -0.0617 -0.0992 0.0130  170 PHE C CA  
9509  C C   . PHE C 170 ? 0.3942 0.4528 0.5105 -0.0731 -0.0893 0.0149  170 PHE C C   
9510  O O   . PHE C 170 ? 0.4212 0.5101 0.5702 -0.0709 -0.0836 0.0155  170 PHE C O   
9511  C CB  . PHE C 170 ? 0.4511 0.4861 0.5411 -0.0672 -0.1198 0.0114  170 PHE C CB  
9512  C CG  . PHE C 170 ? 0.5200 0.5475 0.5951 -0.0540 -0.1282 0.0109  170 PHE C CG  
9513  C CD1 . PHE C 170 ? 0.5128 0.5652 0.6140 -0.0452 -0.1304 0.0127  170 PHE C CD1 
9514  C CD2 . PHE C 170 ? 0.5627 0.5566 0.5967 -0.0496 -0.1320 0.0090  170 PHE C CD2 
9515  C CE1 . PHE C 170 ? 0.5204 0.5628 0.6056 -0.0335 -0.1375 0.0136  170 PHE C CE1 
9516  C CE2 . PHE C 170 ? 0.5944 0.5800 0.6124 -0.0382 -0.1374 0.0095  170 PHE C CE2 
9517  C CZ  . PHE C 170 ? 0.5762 0.5853 0.6191 -0.0306 -0.1406 0.0123  170 PHE C CZ  
9518  N N   . GLU C 171 ? 0.3662 0.4072 0.4687 -0.0847 -0.0857 0.0161  171 GLU C N   
9519  C CA  . GLU C 171 ? 0.4754 0.5315 0.5973 -0.0953 -0.0723 0.0192  171 GLU C CA  
9520  C C   . GLU C 171 ? 0.4869 0.5559 0.6118 -0.0846 -0.0552 0.0203  171 GLU C C   
9521  O O   . GLU C 171 ? 0.5508 0.6469 0.7041 -0.0874 -0.0448 0.0211  171 GLU C O   
9522  C CB  . GLU C 171 ? 0.5859 0.6124 0.6830 -0.1070 -0.0696 0.0215  171 GLU C CB  
9523  C CG  . GLU C 171 ? 0.7180 0.7296 0.8124 -0.1217 -0.0850 0.0196  171 GLU C CG  
9524  C CD  . GLU C 171 ? 0.8223 0.8009 0.8915 -0.1331 -0.0803 0.0222  171 GLU C CD  
9525  O OE1 . GLU C 171 ? 0.8620 0.8297 0.9335 -0.1496 -0.0899 0.0208  171 GLU C OE1 
9526  O OE2 . GLU C 171 ? 0.8574 0.8201 0.9045 -0.1258 -0.0678 0.0257  171 GLU C OE2 
9527  N N   . ILE C 172 ? 0.4374 0.4872 0.5332 -0.0725 -0.0519 0.0199  172 ILE C N   
9528  C CA  . ILE C 172 ? 0.4082 0.4672 0.5030 -0.0632 -0.0381 0.0200  172 ILE C CA  
9529  C C   . ILE C 172 ? 0.4089 0.4954 0.5316 -0.0551 -0.0369 0.0171  172 ILE C C   
9530  O O   . ILE C 172 ? 0.3804 0.4848 0.5178 -0.0536 -0.0241 0.0164  172 ILE C O   
9531  C CB  . ILE C 172 ? 0.4081 0.4434 0.4705 -0.0522 -0.0380 0.0199  172 ILE C CB  
9532  C CG1 . ILE C 172 ? 0.4347 0.4453 0.4719 -0.0578 -0.0347 0.0239  172 ILE C CG1 
9533  C CG2 . ILE C 172 ? 0.3645 0.4116 0.4288 -0.0412 -0.0290 0.0180  172 ILE C CG2 
9534  C CD1 . ILE C 172 ? 0.4521 0.4687 0.4880 -0.0618 -0.0209 0.0275  172 ILE C CD1 
9535  N N   . ILE C 173 ? 0.4208 0.5087 0.5493 -0.0496 -0.0501 0.0153  173 ILE C N   
9536  C CA  . ILE C 173 ? 0.3529 0.4632 0.5066 -0.0403 -0.0501 0.0133  173 ILE C CA  
9537  C C   . ILE C 173 ? 0.3337 0.4743 0.5266 -0.0472 -0.0459 0.0137  173 ILE C C   
9538  O O   . ILE C 173 ? 0.3643 0.5245 0.5776 -0.0410 -0.0344 0.0119  173 ILE C O   
9539  C CB  . ILE C 173 ? 0.3482 0.4503 0.4962 -0.0335 -0.0664 0.0130  173 ILE C CB  
9540  C CG1 . ILE C 173 ? 0.3882 0.4625 0.4999 -0.0262 -0.0665 0.0125  173 ILE C CG1 
9541  C CG2 . ILE C 173 ? 0.2935 0.4155 0.4667 -0.0233 -0.0671 0.0122  173 ILE C CG2 
9542  C CD1 . ILE C 173 ? 0.4096 0.4725 0.5098 -0.0191 -0.0793 0.0127  173 ILE C CD1 
9543  N N   . LYS C 174 ? 0.3307 0.4753 0.5355 -0.0605 -0.0543 0.0154  174 LYS C N   
9544  C CA  . LYS C 174 ? 0.3995 0.5761 0.6468 -0.0689 -0.0508 0.0161  174 LYS C CA  
9545  C C   . LYS C 174 ? 0.3248 0.5125 0.5799 -0.0736 -0.0281 0.0167  174 LYS C C   
9546  O O   . LYS C 174 ? 0.3365 0.5540 0.6299 -0.0787 -0.0206 0.0168  174 LYS C O   
9547  C CB  . LYS C 174 ? 0.4314 0.6074 0.6876 -0.0855 -0.0644 0.0176  174 LYS C CB  
9548  C CG  . LYS C 174 ? 0.4806 0.6601 0.7460 -0.0829 -0.0879 0.0167  174 LYS C CG  
9549  C CD  . LYS C 174 ? 0.5771 0.7979 0.8946 -0.0784 -0.0910 0.0168  174 LYS C CD  
9550  C CE  . LYS C 174 ? 0.5576 0.8123 0.9186 -0.0883 -0.0750 0.0176  174 LYS C CE  
9551  N NZ  . LYS C 174 ? 0.5265 0.8150 0.9296 -0.0746 -0.0751 0.0170  174 LYS C NZ  
9552  N N   . LYS C 175 ? 0.3956 0.5604 0.6155 -0.0722 -0.0175 0.0173  175 LYS C N   
9553  C CA  . LYS C 175 ? 0.4504 0.6194 0.6672 -0.0766 0.0034  0.0184  175 LYS C CA  
9554  C C   . LYS C 175 ? 0.3600 0.5309 0.5678 -0.0626 0.0151  0.0146  175 LYS C C   
9555  O O   . LYS C 175 ? 0.3237 0.4975 0.5257 -0.0648 0.0329  0.0145  175 LYS C O   
9556  C CB  . LYS C 175 ? 0.5000 0.6392 0.6804 -0.0860 0.0059  0.0228  175 LYS C CB  
9557  C CG  . LYS C 175 ? 0.5629 0.6960 0.7490 -0.1032 -0.0010 0.0266  175 LYS C CG  
9558  C CD  . LYS C 175 ? 0.6506 0.7594 0.8070 -0.1128 0.0100  0.0320  175 LYS C CD  
9559  C CE  . LYS C 175 ? 0.7203 0.8018 0.8598 -0.1243 -0.0022 0.0349  175 LYS C CE  
9560  N NZ  . LYS C 175 ? 0.7830 0.8289 0.8793 -0.1232 0.0024  0.0396  175 LYS C NZ  
9561  N N   . THR C 176 ? 0.2847 0.4525 0.4898 -0.0491 0.0059  0.0113  176 THR C N   
9562  C CA  . THR C 176 ? 0.3328 0.4930 0.5199 -0.0375 0.0139  0.0074  176 THR C CA  
9563  C C   . THR C 176 ? 0.3739 0.5560 0.5846 -0.0323 0.0295  0.0029  176 THR C C   
9564  O O   . THR C 176 ? 0.3700 0.5476 0.5642 -0.0314 0.0442  0.0004  176 THR C O   
9565  C CB  . THR C 176 ? 0.2858 0.4341 0.4630 -0.0266 0.0002  0.0058  176 THR C CB  
9566  O OG1 . THR C 176 ? 0.3094 0.4342 0.4590 -0.0302 -0.0101 0.0089  176 THR C OG1 
9567  C CG2 . THR C 176 ? 0.2586 0.4018 0.4236 -0.0159 0.0081  0.0010  176 THR C CG2 
9568  N N   . LEU C 177 ? 0.3563 0.5613 0.6046 -0.0277 0.0264  0.0016  177 LEU C N   
9569  C CA  . LEU C 177 ? 0.3646 0.5905 0.6376 -0.0216 0.0433  -0.0030 177 LEU C CA  
9570  C C   . LEU C 177 ? 0.3704 0.6074 0.6489 -0.0332 0.0620  -0.0018 177 LEU C C   
9571  O O   . LEU C 177 ? 0.2991 0.5418 0.5773 -0.0295 0.0815  -0.0064 177 LEU C O   
9572  C CB  . LEU C 177 ? 0.3460 0.5963 0.6627 -0.0135 0.0354  -0.0034 177 LEU C CB  
9573  C CG  . LEU C 177 ? 0.3335 0.5703 0.6421 -0.0014 0.0185  -0.0037 177 LEU C CG  
9574  C CD1 . LEU C 177 ? 0.3379 0.5979 0.6885 0.0070  0.0094  -0.0026 177 LEU C CD1 
9575  C CD2 . LEU C 177 ? 0.3387 0.5574 0.6224 0.0088  0.0272  -0.0092 177 LEU C CD2 
9576  N N   . SER C 178 ? 0.4321 0.6691 0.7123 -0.0479 0.0575  0.0041  178 SER C N   
9577  C CA  . SER C 178 ? 0.4486 0.6950 0.7342 -0.0607 0.0765  0.0066  178 SER C CA  
9578  C C   . SER C 178 ? 0.4107 0.6324 0.6502 -0.0623 0.0900  0.0066  178 SER C C   
9579  O O   . SER C 178 ? 0.4269 0.6558 0.6659 -0.0667 0.1115  0.0060  178 SER C O   
9580  C CB  . SER C 178 ? 0.4863 0.7349 0.7833 -0.0776 0.0671  0.0131  178 SER C CB  
9581  O OG  . SER C 178 ? 0.5068 0.7871 0.8545 -0.0789 0.0596  0.0129  178 SER C OG  
9582  N N   . ILE C 179 ? 0.4033 0.5966 0.6039 -0.0583 0.0779  0.0073  179 ILE C N   
9583  C CA  . ILE C 179 ? 0.4469 0.6181 0.6047 -0.0589 0.0878  0.0077  179 ILE C CA  
9584  C C   . ILE C 179 ? 0.3987 0.5736 0.5511 -0.0474 0.0997  -0.0007 179 ILE C C   
9585  O O   . ILE C 179 ? 0.3715 0.5388 0.4996 -0.0498 0.1155  -0.0020 179 ILE C O   
9586  C CB  . ILE C 179 ? 0.4288 0.5710 0.5506 -0.0578 0.0713  0.0113  179 ILE C CB  
9587  C CG1 . ILE C 179 ? 0.4792 0.6000 0.5594 -0.0616 0.0799  0.0147  179 ILE C CG1 
9588  C CG2 . ILE C 179 ? 0.3893 0.5265 0.5071 -0.0441 0.0587  0.0060  179 ILE C CG2 
9589  C CD1 . ILE C 179 ? 0.4518 0.5459 0.5016 -0.0627 0.0657  0.0207  179 ILE C CD1 
9590  N N   . TYR C 180 ? 0.2773 0.4613 0.4497 -0.0353 0.0927  -0.0067 180 TYR C N   
9591  C CA  . TYR C 180 ? 0.3226 0.5091 0.4933 -0.0249 0.1052  -0.0157 180 TYR C CA  
9592  C C   . TYR C 180 ? 0.3987 0.6059 0.5916 -0.0271 0.1284  -0.0184 180 TYR C C   
9593  O O   . TYR C 180 ? 0.4031 0.6033 0.5743 -0.0256 0.1456  -0.0239 180 TYR C O   
9594  C CB  . TYR C 180 ? 0.2826 0.4730 0.4728 -0.0120 0.0935  -0.0203 180 TYR C CB  
9595  C CG  . TYR C 180 ? 0.2852 0.4530 0.4473 -0.0086 0.0767  -0.0197 180 TYR C CG  
9596  C CD1 . TYR C 180 ? 0.3106 0.4614 0.4422 -0.0048 0.0796  -0.0254 180 TYR C CD1 
9597  C CD2 . TYR C 180 ? 0.3108 0.4744 0.4767 -0.0100 0.0584  -0.0138 180 TYR C CD2 
9598  C CE1 . TYR C 180 ? 0.2864 0.4201 0.3973 -0.0024 0.0650  -0.0247 180 TYR C CE1 
9599  C CE2 . TYR C 180 ? 0.2436 0.3880 0.3857 -0.0068 0.0459  -0.0133 180 TYR C CE2 
9600  C CZ  . TYR C 180 ? 0.2421 0.3734 0.3594 -0.0030 0.0495  -0.0185 180 TYR C CZ  
9601  O OH  . TYR C 180 ? 0.2365 0.3526 0.3356 -0.0003 0.0377  -0.0178 180 TYR C OH  
9602  N N   . ARG C 181 ? 0.4260 0.6592 0.6625 -0.0310 0.1295  -0.0150 181 ARG C N   
9603  C CA  . ARG C 181 ? 0.4342 0.6906 0.6965 -0.0351 0.1533  -0.0163 181 ARG C CA  
9604  C C   . ARG C 181 ? 0.4412 0.6836 0.6684 -0.0481 0.1699  -0.0125 181 ARG C C   
9605  O O   . ARG C 181 ? 0.4265 0.6730 0.6480 -0.0478 0.1943  -0.0168 181 ARG C O   
9606  C CB  . ARG C 181 ? 0.4184 0.7059 0.7341 -0.0406 0.1478  -0.0114 181 ARG C CB  
9607  C CG  . ARG C 181 ? 0.4476 0.7570 0.8069 -0.0260 0.1389  -0.0155 181 ARG C CG  
9608  C CD  . ARG C 181 ? 0.4633 0.8081 0.8783 -0.0327 0.1353  -0.0108 181 ARG C CD  
9609  N NE  . ARG C 181 ? 0.4797 0.8393 0.9291 -0.0202 0.1157  -0.0113 181 ARG C NE  
9610  C CZ  . ARG C 181 ? 0.4925 0.8467 0.9427 -0.0232 0.0887  -0.0063 181 ARG C CZ  
9611  N NH1 . ARG C 181 ? 0.5010 0.8356 0.9215 -0.0379 0.0790  -0.0012 181 ARG C NH1 
9612  N NH2 . ARG C 181 ? 0.5005 0.8669 0.9791 -0.0110 0.0717  -0.0063 181 ARG C NH2 
9613  N N   . GLU C 182 ? 0.4652 0.6885 0.6663 -0.0590 0.1576  -0.0042 182 GLU C N   
9614  C CA  . GLU C 182 ? 0.5118 0.7203 0.6808 -0.0723 0.1717  0.0020  182 GLU C CA  
9615  C C   . GLU C 182 ? 0.5315 0.7158 0.6500 -0.0672 0.1815  -0.0024 182 GLU C C   
9616  O O   . GLU C 182 ? 0.5639 0.7466 0.6662 -0.0723 0.2046  -0.0027 182 GLU C O   
9617  C CB  . GLU C 182 ? 0.5514 0.7415 0.7042 -0.0832 0.1541  0.0119  182 GLU C CB  
9618  C CG  . GLU C 182 ? 0.6405 0.8115 0.7592 -0.0972 0.1677  0.0202  182 GLU C CG  
9619  C CD  . GLU C 182 ? 0.6673 0.8147 0.7663 -0.1064 0.1506  0.0297  182 GLU C CD  
9620  O OE1 . GLU C 182 ? 0.6538 0.7944 0.7545 -0.0998 0.1281  0.0286  182 GLU C OE1 
9621  O OE2 . GLU C 182 ? 0.7014 0.8347 0.7811 -0.1200 0.1610  0.0382  182 GLU C OE2 
9622  N N   . ILE C 183 ? 0.4999 0.6651 0.5920 -0.0577 0.1641  -0.0059 183 ILE C N   
9623  C CA  . ILE C 183 ? 0.5227 0.6655 0.5673 -0.0536 0.1696  -0.0107 183 ILE C CA  
9624  C C   . ILE C 183 ? 0.5266 0.6792 0.5780 -0.0453 0.1889  -0.0224 183 ILE C C   
9625  O O   . ILE C 183 ? 0.5785 0.7147 0.5903 -0.0453 0.2011  -0.0268 183 ILE C O   
9626  C CB  . ILE C 183 ? 0.5511 0.6748 0.5724 -0.0463 0.1457  -0.0119 183 ILE C CB  
9627  C CG1 . ILE C 183 ? 0.5894 0.7251 0.6410 -0.0343 0.1358  -0.0200 183 ILE C CG1 
9628  C CG2 . ILE C 183 ? 0.4649 0.5765 0.4774 -0.0529 0.1286  -0.0010 183 ILE C CG2 
9629  C CD1 . ILE C 183 ? 0.6075 0.7343 0.6405 -0.0250 0.1400  -0.0316 183 ILE C CD1 
9630  N N   . LYS C 184 ? 0.4566 0.6338 0.5555 -0.0375 0.1915  -0.0278 184 LYS C N   
9631  C CA  . LYS C 184 ? 0.5193 0.7054 0.6280 -0.0283 0.2119  -0.0391 184 LYS C CA  
9632  C C   . LYS C 184 ? 0.5707 0.7686 0.6835 -0.0362 0.2414  -0.0380 184 LYS C C   
9633  O O   . LYS C 184 ? 0.5959 0.7821 0.6781 -0.0343 0.2614  -0.0452 184 LYS C O   
9634  C CB  . LYS C 184 ? 0.4710 0.6792 0.6310 -0.0163 0.2051  -0.0437 184 LYS C CB  
9635  C CG  . LYS C 184 ? 0.4843 0.6994 0.6571 -0.0040 0.2246  -0.0559 184 LYS C CG  
9636  C CD  . LYS C 184 ? 0.5177 0.7477 0.7346 0.0094  0.2122  -0.0587 184 LYS C CD  
9637  C CE  . LYS C 184 ? 0.5483 0.8028 0.8071 0.0195  0.2343  -0.0654 184 LYS C CE  
9638  N NZ  . LYS C 184 ? 0.5974 0.8327 0.8279 0.0288  0.2522  -0.0789 184 LYS C NZ  
9639  N N   . GLU C 185 ? 0.5850 0.8056 0.7347 -0.0459 0.2450  -0.0291 185 GLU C N   
9640  C CA  . GLU C 185 ? 0.5897 0.8238 0.7473 -0.0556 0.2744  -0.0266 185 GLU C CA  
9641  C C   . GLU C 185 ? 0.5906 0.7938 0.6856 -0.0662 0.2845  -0.0218 185 GLU C C   
9642  O O   . GLU C 185 ? 0.6648 0.8661 0.7420 -0.0692 0.3128  -0.0246 185 GLU C O   
9643  C CB  . GLU C 185 ? 0.6276 0.8906 0.8367 -0.0668 0.2721  -0.0171 185 GLU C CB  
9644  C CG  . GLU C 185 ? 0.7608 1.0308 0.9692 -0.0835 0.2988  -0.0100 185 GLU C CG  
9645  C CD  . GLU C 185 ? 0.8551 1.0999 1.0278 -0.1003 0.2883  0.0028  185 GLU C CD  
9646  O OE1 . GLU C 185 ? 0.8612 1.0940 1.0289 -0.1000 0.2592  0.0068  185 GLU C OE1 
9647  O OE2 . GLU C 185 ? 0.8925 1.1277 1.0409 -0.1135 0.3100  0.0091  185 GLU C OE2 
9648  N N   . GLU C 186 ? 0.6236 0.5072 0.6514 -0.0132 0.1665  -0.0001 186 GLU C N   
9649  C CA  . GLU C 186 ? 0.6732 0.5204 0.6624 -0.0044 0.1891  0.0195  186 GLU C CA  
9650  C C   . GLU C 186 ? 0.6848 0.5345 0.6337 0.0160  0.1819  0.0341  186 GLU C C   
9651  O O   . GLU C 186 ? 0.7434 0.5648 0.6546 0.0278  0.1970  0.0509  186 GLU C O   
9652  C CB  . GLU C 186 ? 0.7208 0.5382 0.6948 -0.0038 0.1910  0.0241  186 GLU C CB  
9653  C CG  . GLU C 186 ? 0.8325 0.6321 0.8363 -0.0234 0.2115  0.0147  186 GLU C CG  
9654  C CD  . GLU C 186 ? 0.9242 0.7069 0.9264 -0.0260 0.2036  0.0103  186 GLU C CD  
9655  O OE1 . GLU C 186 ? 0.9314 0.7025 0.8979 -0.0098 0.1922  0.0219  186 GLU C OE1 
9656  O OE2 . GLU C 186 ? 0.9722 0.7539 1.0098 -0.0443 0.2097  -0.0056 186 GLU C OE2 
9657  N N   . GLY C 187 ? 0.6087 0.4903 0.5636 0.0211  0.1594  0.0274  187 GLY C N   
9658  C CA  . GLY C 187 ? 0.6012 0.4879 0.5223 0.0385  0.1527  0.0378  187 GLY C CA  
9659  C C   . GLY C 187 ? 0.6559 0.5301 0.5412 0.0534  0.1413  0.0480  187 GLY C C   
9660  O O   . GLY C 187 ? 0.7321 0.6080 0.5864 0.0692  0.1375  0.0569  187 GLY C O   
9661  N N   . LYS C 188 ? 0.5998 0.4631 0.4898 0.0493  0.1353  0.0455  188 LYS C N   
9662  C CA  . LYS C 188 ? 0.6129 0.4656 0.4716 0.0636  0.1252  0.0542  188 LYS C CA  
9663  C C   . LYS C 188 ? 0.6305 0.5112 0.4890 0.0695  0.0980  0.0478  188 LYS C C   
9664  O O   . LYS C 188 ? 0.6349 0.5144 0.4675 0.0833  0.0890  0.0541  188 LYS C O   
9665  C CB  . LYS C 188 ? 0.6628 0.4925 0.5259 0.0574  0.1298  0.0533  188 LYS C CB  
9666  C CG  . LYS C 188 ? 0.7069 0.4973 0.5468 0.0620  0.1561  0.0672  188 LYS C CG  
9667  C CD  . LYS C 188 ? 0.7639 0.5331 0.6271 0.0453  0.1692  0.0603  188 LYS C CD  
9668  C CE  . LYS C 188 ? 0.8473 0.5707 0.6828 0.0513  0.1961  0.0755  188 LYS C CE  
9669  N NZ  . LYS C 188 ? 0.9251 0.6357 0.7242 0.0678  0.2105  0.0927  188 LYS C NZ  
9670  N N   . GLY C 189 ? 0.5542 0.4594 0.4412 0.0597  0.0857  0.0349  189 GLY C N   
9671  C CA  . GLY C 189 ? 0.5087 0.4365 0.3949 0.0643  0.0631  0.0293  189 GLY C CA  
9672  C C   . GLY C 189 ? 0.5023 0.4522 0.4180 0.0551  0.0547  0.0169  189 GLY C C   
9673  O O   . GLY C 189 ? 0.5206 0.4716 0.4629 0.0437  0.0622  0.0097  189 GLY C O   
9674  N N   . SER C 190 ? 0.4624 0.4299 0.3737 0.0605  0.0394  0.0138  190 SER C N   
9675  C CA  . SER C 190 ? 0.4156 0.4022 0.3505 0.0549  0.0283  0.0026  190 SER C CA  
9676  C C   . SER C 190 ? 0.4895 0.4792 0.4301 0.0525  0.0110  -0.0039 190 SER C C   
9677  O O   . SER C 190 ? 0.5422 0.5249 0.4646 0.0573  0.0049  0.0005  190 SER C O   
9678  C CB  . SER C 190 ? 0.4474 0.4474 0.3730 0.0621  0.0231  0.0025  190 SER C CB  
9679  O OG  . SER C 190 ? 0.4731 0.4701 0.3897 0.0660  0.0391  0.0084  190 SER C OG  
9680  N N   . VAL C 191 ? 0.4497 0.4503 0.4152 0.0460  0.0034  -0.0147 191 VAL C N   
9681  C CA  . VAL C 191 ? 0.4710 0.4745 0.4401 0.0452  -0.0134 -0.0215 191 VAL C CA  
9682  C C   . VAL C 191 ? 0.4657 0.4838 0.4409 0.0487  -0.0258 -0.0275 191 VAL C C   
9683  O O   . VAL C 191 ? 0.5319 0.5619 0.5264 0.0470  -0.0233 -0.0333 191 VAL C O   
9684  C CB  . VAL C 191 ? 0.4391 0.4408 0.4299 0.0365  -0.0132 -0.0304 191 VAL C CB  
9685  C CG1 . VAL C 191 ? 0.5156 0.5186 0.5038 0.0381  -0.0311 -0.0369 191 VAL C CG1 
9686  C CG2 . VAL C 191 ? 0.4024 0.3854 0.3867 0.0329  0.0022  -0.0241 191 VAL C CG2 
9687  N N   . SER C 192 ? 0.4511 0.4672 0.4097 0.0538  -0.0375 -0.0259 192 SER C N   
9688  C CA  . SER C 192 ? 0.4328 0.4565 0.3924 0.0579  -0.0485 -0.0303 192 SER C CA  
9689  C C   . SER C 192 ? 0.4400 0.4607 0.3989 0.0591  -0.0625 -0.0356 192 SER C C   
9690  O O   . SER C 192 ? 0.4234 0.4381 0.3820 0.0561  -0.0642 -0.0369 192 SER C O   
9691  C CB  . SER C 192 ? 0.3695 0.3911 0.3090 0.0627  -0.0485 -0.0247 192 SER C CB  
9692  O OG  . SER C 192 ? 0.4220 0.4347 0.3440 0.0636  -0.0518 -0.0205 192 SER C OG  
9693  N N   . THR C 193 ? 0.4139 0.4366 0.3695 0.0644  -0.0720 -0.0384 193 THR C N   
9694  C CA  . THR C 193 ? 0.3425 0.3589 0.2896 0.0684  -0.0850 -0.0415 193 THR C CA  
9695  C C   . THR C 193 ? 0.4056 0.4131 0.3333 0.0738  -0.0884 -0.0374 193 THR C C   
9696  O O   . THR C 193 ? 0.4333 0.4420 0.3575 0.0735  -0.0819 -0.0341 193 THR C O   
9697  C CB  . THR C 193 ? 0.4898 0.5174 0.4575 0.0708  -0.0942 -0.0523 193 THR C CB  
9698  O OG1 . THR C 193 ? 0.5097 0.5305 0.4675 0.0741  -0.1057 -0.0556 193 THR C OG1 
9699  C CG2 . THR C 193 ? 0.4924 0.5266 0.4651 0.0783  -0.0993 -0.0554 193 THR C CG2 
9700  N N   . SER C 194 ? 0.4413 0.4383 0.3549 0.0786  -0.0978 -0.0379 194 SER C N   
9701  C CA  . SER C 194 ? 0.4980 0.4815 0.3920 0.0836  -0.1002 -0.0344 194 SER C CA  
9702  C C   . SER C 194 ? 0.4913 0.4715 0.3839 0.0935  -0.1118 -0.0390 194 SER C C   
9703  O O   . SER C 194 ? 0.4245 0.4136 0.3285 0.0963  -0.1202 -0.0457 194 SER C O   
9704  C CB  . SER C 194 ? 0.5004 0.4694 0.3726 0.0818  -0.0985 -0.0291 194 SER C CB  
9705  O OG  . SER C 194 ? 0.4872 0.4597 0.3586 0.0752  -0.0889 -0.0252 194 SER C OG  
9706  N N   . PRO C 195 ? 0.5146 0.4818 0.3932 0.0997  -0.1126 -0.0364 195 PRO C N   
9707  C CA  . PRO C 195 ? 0.4940 0.4515 0.3616 0.1125  -0.1240 -0.0386 195 PRO C CA  
9708  C C   . PRO C 195 ? 0.5032 0.4548 0.3578 0.1158  -0.1321 -0.0393 195 PRO C C   
9709  O O   . PRO C 195 ? 0.5271 0.4718 0.3710 0.1088  -0.1266 -0.0351 195 PRO C O   
9710  C CB  . PRO C 195 ? 0.4803 0.4146 0.3254 0.1156  -0.1183 -0.0321 195 PRO C CB  
9711  C CG  . PRO C 195 ? 0.5640 0.5070 0.4218 0.1058  -0.1069 -0.0317 195 PRO C CG  
9712  C CD  . PRO C 195 ? 0.5220 0.4822 0.3939 0.0960  -0.1028 -0.0324 195 PRO C CD  
9713  N N   . TYR C 196 ? 0.4957 0.4512 0.3512 0.1278  -0.1460 -0.0458 196 TYR C N   
9714  C CA  . TYR C 196 ? 0.5099 0.4746 0.3697 0.1289  -0.1559 -0.0530 196 TYR C CA  
9715  C C   . TYR C 196 ? 0.5518 0.4977 0.3840 0.1269  -0.1535 -0.0470 196 TYR C C   
9716  O O   . TYR C 196 ? 0.5372 0.4899 0.3771 0.1184  -0.1515 -0.0497 196 TYR C O   
9717  C CB  . TYR C 196 ? 0.5133 0.4853 0.3746 0.1450  -0.1732 -0.0621 196 TYR C CB  
9718  C CG  . TYR C 196 ? 0.5062 0.4996 0.3875 0.1440  -0.1842 -0.0755 196 TYR C CG  
9719  C CD1 . TYR C 196 ? 0.5305 0.5147 0.3930 0.1449  -0.1895 -0.0767 196 TYR C CD1 
9720  C CD2 . TYR C 196 ? 0.4878 0.5105 0.4078 0.1417  -0.1884 -0.0884 196 TYR C CD2 
9721  C CE1 . TYR C 196 ? 0.5484 0.5518 0.4301 0.1433  -0.1996 -0.0911 196 TYR C CE1 
9722  C CE2 . TYR C 196 ? 0.5567 0.5997 0.4985 0.1391  -0.1977 -0.1030 196 TYR C CE2 
9723  C CZ  . TYR C 196 ? 0.5714 0.6043 0.4938 0.1399  -0.2038 -0.1048 196 TYR C CZ  
9724  O OH  . TYR C 196 ? 0.5822 0.6354 0.5278 0.1365  -0.2130 -0.1215 196 TYR C OH  
9725  N N   . TYR C 197 ? 0.5742 0.4948 0.3734 0.1353  -0.1530 -0.0392 197 TYR C N   
9726  C CA  . TYR C 197 ? 0.5585 0.4611 0.3306 0.1345  -0.1499 -0.0340 197 TYR C CA  
9727  C C   . TYR C 197 ? 0.5132 0.4027 0.2757 0.1233  -0.1328 -0.0244 197 TYR C C   
9728  O O   . TYR C 197 ? 0.5626 0.4324 0.2986 0.1241  -0.1274 -0.0185 197 TYR C O   
9729  C CB  . TYR C 197 ? 0.5940 0.4758 0.3326 0.1518  -0.1596 -0.0322 197 TYR C CB  
9730  C CG  . TYR C 197 ? 0.6033 0.5029 0.3521 0.1633  -0.1788 -0.0446 197 TYR C CG  
9731  C CD1 . TYR C 197 ? 0.6036 0.5119 0.3558 0.1608  -0.1841 -0.0523 197 TYR C CD1 
9732  C CD2 . TYR C 197 ? 0.5906 0.5013 0.3533 0.1738  -0.1880 -0.0502 197 TYR C CD2 
9733  C CE1 . TYR C 197 ? 0.5569 0.4847 0.3267 0.1675  -0.1979 -0.0659 197 TYR C CE1 
9734  C CE2 . TYR C 197 ? 0.6310 0.5627 0.4120 0.1811  -0.2014 -0.0637 197 TYR C CE2 
9735  C CZ  . TYR C 197 ? 0.5854 0.5260 0.3703 0.1775  -0.2064 -0.0719 197 TYR C CZ  
9736  O OH  . TYR C 197 ? 0.6704 0.6335 0.4753 0.1842  -0.2201 -0.0872 197 TYR C OH  
9737  N N   . HIS C 198 ? 0.5162 0.4180 0.3003 0.1133  -0.1241 -0.0239 198 HIS C N   
9738  C CA  . HIS C 198 ? 0.5029 0.3994 0.2836 0.1026  -0.1096 -0.0180 198 HIS C CA  
9739  C C   . HIS C 198 ? 0.5406 0.4111 0.2960 0.1054  -0.1022 -0.0114 198 HIS C C   
9740  O O   . HIS C 198 ? 0.6029 0.4615 0.3435 0.1002  -0.0928 -0.0072 198 HIS C O   
9741  C CB  . HIS C 198 ? 0.4987 0.3986 0.2773 0.0962  -0.1061 -0.0176 198 HIS C CB  
9742  C CG  . HIS C 198 ? 0.4254 0.3320 0.2117 0.0856  -0.0938 -0.0148 198 HIS C CG  
9743  N ND1 . HIS C 198 ? 0.4559 0.3504 0.2267 0.0817  -0.0839 -0.0106 198 HIS C ND1 
9744  C CD2 . HIS C 198 ? 0.4219 0.3469 0.2289 0.0790  -0.0899 -0.0164 198 HIS C CD2 
9745  C CE1 . HIS C 198 ? 0.4909 0.3992 0.2751 0.0737  -0.0761 -0.0111 198 HIS C CE1 
9746  N NE2 . HIS C 198 ? 0.4090 0.3347 0.2128 0.0729  -0.0799 -0.0138 198 HIS C NE2 
9747  N N   . PRO C 199 ? 0.5425 0.4026 0.2932 0.1129  -0.1043 -0.0107 199 PRO C N   
9748  C CA  . PRO C 199 ? 0.6341 0.4648 0.3602 0.1146  -0.0945 -0.0042 199 PRO C CA  
9749  C C   . PRO C 199 ? 0.7039 0.5369 0.4427 0.1025  -0.0815 -0.0047 199 PRO C C   
9750  O O   . PRO C 199 ? 0.6591 0.5166 0.4234 0.0952  -0.0814 -0.0095 199 PRO C O   
9751  C CB  . PRO C 199 ? 0.6261 0.4444 0.3412 0.1310  -0.1045 -0.0041 199 PRO C CB  
9752  C CG  . PRO C 199 ? 0.5888 0.4372 0.3371 0.1306  -0.1129 -0.0120 199 PRO C CG  
9753  C CD  . PRO C 199 ? 0.5396 0.4135 0.3082 0.1203  -0.1142 -0.0162 199 PRO C CD  
9754  N N   . LEU C 200 ? 0.7213 0.5270 0.4407 0.1009  -0.0699 -0.0001 200 LEU C N   
9755  C CA  . LEU C 200 ? 0.6201 0.4247 0.3501 0.0897  -0.0575 -0.0027 200 LEU C CA  
9756  C C   . LEU C 200 ? 0.6408 0.4364 0.3722 0.0979  -0.0609 -0.0041 200 LEU C C   
9757  O O   . LEU C 200 ? 0.6666 0.4304 0.3760 0.1045  -0.0557 0.0005  200 LEU C O   
9758  C CB  . LEU C 200 ? 0.5644 0.3436 0.2760 0.0818  -0.0411 0.0011  200 LEU C CB  
9759  C CG  . LEU C 200 ? 0.5842 0.3774 0.3007 0.0716  -0.0354 0.0002  200 LEU C CG  
9760  C CD1 . LEU C 200 ? 0.6640 0.4301 0.3610 0.0648  -0.0179 0.0040  200 LEU C CD1 
9761  C CD2 . LEU C 200 ? 0.5436 0.3716 0.2915 0.0606  -0.0352 -0.0079 200 LEU C CD2 
9762  N N   . ILE C 201 ? 0.5748 0.3974 0.3314 0.0980  -0.0684 -0.0101 201 ILE C N   
9763  C CA  . ILE C 201 ? 0.5314 0.3501 0.2926 0.1068  -0.0723 -0.0126 201 ILE C CA  
9764  C C   . ILE C 201 ? 0.5377 0.3305 0.2892 0.1029  -0.0595 -0.0126 201 ILE C C   
9765  O O   . ILE C 201 ? 0.5661 0.3340 0.3019 0.1149  -0.0604 -0.0097 201 ILE C O   
9766  C CB  . ILE C 201 ? 0.5014 0.3543 0.2924 0.1048  -0.0785 -0.0196 201 ILE C CB  
9767  C CG1 . ILE C 201 ? 0.4957 0.3677 0.2954 0.1107  -0.0909 -0.0203 201 ILE C CG1 
9768  C CG2 . ILE C 201 ? 0.5192 0.3689 0.3166 0.1123  -0.0798 -0.0234 201 ILE C CG2 
9769  C CD1 . ILE C 201 ? 0.5427 0.4016 0.3281 0.1276  -0.1024 -0.0188 201 ILE C CD1 
9770  N N   . PRO C 202 ? 0.5527 0.3495 0.3128 0.0872  -0.0474 -0.0166 202 PRO C N   
9771  C CA  . PRO C 202 ? 0.5963 0.3690 0.3507 0.0822  -0.0348 -0.0193 202 PRO C CA  
9772  C C   . PRO C 202 ? 0.6216 0.3503 0.3447 0.0867  -0.0253 -0.0109 202 PRO C C   
9773  O O   . PRO C 202 ? 0.6430 0.3426 0.3548 0.0904  -0.0181 -0.0104 202 PRO C O   
9774  C CB  . PRO C 202 ? 0.5318 0.3244 0.3044 0.0640  -0.0256 -0.0275 202 PRO C CB  
9775  C CG  . PRO C 202 ? 0.5173 0.3489 0.3085 0.0635  -0.0362 -0.0294 202 PRO C CG  
9776  C CD  . PRO C 202 ? 0.5127 0.3382 0.2902 0.0744  -0.0453 -0.0208 202 PRO C CD  
9777  N N   . ILE C 203 ? 0.6053 0.3261 0.3120 0.0872  -0.0242 -0.0040 203 ILE C N   
9778  C CA  . ILE C 203 ? 0.6817 0.3579 0.3537 0.0933  -0.0141 0.0055  203 ILE C CA  
9779  C C   . ILE C 203 ? 0.7375 0.3934 0.3875 0.1164  -0.0257 0.0121  203 ILE C C   
9780  O O   . ILE C 203 ? 0.8095 0.4248 0.4342 0.1245  -0.0171 0.0180  203 ILE C O   
9781  C CB  . ILE C 203 ? 0.6946 0.3697 0.3542 0.0883  -0.0095 0.0105  203 ILE C CB  
9782  C CG1 . ILE C 203 ? 0.6672 0.3564 0.3467 0.0664  0.0053  0.0033  203 ILE C CG1 
9783  C CG2 . ILE C 203 ? 0.7824 0.4098 0.3991 0.0994  -0.0009 0.0225  203 ILE C CG2 
9784  C CD1 . ILE C 203 ? 0.7315 0.4137 0.3976 0.0605  0.0149  0.0078  203 ILE C CD1 
9785  N N   . LEU C 204 ? 0.7033 0.3870 0.3635 0.1276  -0.0451 0.0105  204 LEU C N   
9786  C CA  . LEU C 204 ? 0.7287 0.4006 0.3731 0.1507  -0.0586 0.0139  204 LEU C CA  
9787  C C   . LEU C 204 ? 0.7605 0.4226 0.4113 0.1565  -0.0569 0.0106  204 LEU C C   
9788  O O   . LEU C 204 ? 0.7873 0.4178 0.4127 0.1746  -0.0584 0.0162  204 LEU C O   
9789  C CB  . LEU C 204 ? 0.7056 0.4160 0.3688 0.1580  -0.0788 0.0088  204 LEU C CB  
9790  C CG  . LEU C 204 ? 0.7014 0.4227 0.3586 0.1551  -0.0834 0.0106  204 LEU C CG  
9791  C CD1 . LEU C 204 ? 0.6727 0.4294 0.3506 0.1630  -0.1031 0.0035  204 LEU C CD1 
9792  C CD2 . LEU C 204 ? 0.6849 0.3667 0.2983 0.1663  -0.0790 0.0209  204 LEU C CD2 
9793  N N   . LEU C 205 ? 0.6918 0.3795 0.3743 0.1431  -0.0540 0.0013  205 LEU C N   
9794  C CA  . LEU C 205 ? 0.6646 0.3448 0.3545 0.1483  -0.0522 -0.0033 205 LEU C CA  
9795  C C   . LEU C 205 ? 0.7059 0.3402 0.3739 0.1442  -0.0334 0.0002  205 LEU C C   
9796  O O   . LEU C 205 ? 0.7382 0.3450 0.3922 0.1580  -0.0322 0.0022  205 LEU C O   
9797  C CB  . LEU C 205 ? 0.6278 0.3471 0.3546 0.1352  -0.0531 -0.0145 205 LEU C CB  
9798  C CG  . LEU C 205 ? 0.6273 0.3878 0.3780 0.1413  -0.0694 -0.0189 205 LEU C CG  
9799  C CD1 . LEU C 205 ? 0.5658 0.3590 0.3464 0.1274  -0.0664 -0.0280 205 LEU C CD1 
9800  C CD2 . LEU C 205 ? 0.6778 0.4349 0.4263 0.1626  -0.0808 -0.0194 205 LEU C CD2 
9801  N N   . ASN C 206 ? 0.7070 0.3327 0.3734 0.1251  -0.0179 0.0001  206 ASN C N   
9802  C CA  . ASN C 206 ? 0.7578 0.3388 0.4057 0.1182  0.0028  0.0023  206 ASN C CA  
9803  C C   . ASN C 206 ? 0.7513 0.3261 0.3953 0.0995  0.0181  0.0036  206 ASN C C   
9804  O O   . ASN C 206 ? 0.7375 0.3396 0.4090 0.0797  0.0236  -0.0068 206 ASN C O   
9805  C CB  . ASN C 206 ? 0.8237 0.4086 0.4932 0.1091  0.0093  -0.0095 206 ASN C CB  
9806  C CG  . ASN C 206 ? 0.8851 0.4241 0.5397 0.0985  0.0325  -0.0100 206 ASN C CG  
9807  O OD1 . ASN C 206 ? 0.9338 0.4286 0.5557 0.1040  0.0438  0.0013  206 ASN C OD1 
9808  N ND2 . ASN C 206 ? 0.9094 0.4576 0.5873 0.0836  0.0404  -0.0236 206 ASN C ND2 
9809  N N   . PRO C 207 ? 0.8319 0.3719 0.4418 0.1061  0.0255  0.0157  207 PRO C N   
9810  C CA  . PRO C 207 ? 0.8253 0.3608 0.4322 0.0887  0.0413  0.0169  207 PRO C CA  
9811  C C   . PRO C 207 ? 0.8361 0.3608 0.4581 0.0656  0.0636  0.0077  207 PRO C C   
9812  O O   . PRO C 207 ? 0.9196 0.4570 0.5534 0.0477  0.0745  0.0034  207 PRO C O   
9813  C CB  . PRO C 207 ? 0.8986 0.3876 0.4585 0.1041  0.0475  0.0327  207 PRO C CB  
9814  C CG  . PRO C 207 ? 0.9518 0.4421 0.4976 0.1310  0.0255  0.0381  207 PRO C CG  
9815  C CD  . PRO C 207 ? 0.9249 0.4307 0.4967 0.1318  0.0188  0.0285  207 PRO C CD  
9816  N N   . ASN C 208 ? 0.8591 0.3615 0.4824 0.0655  0.0707  0.0031  208 ASN C N   
9817  C CA  . ASN C 208 ? 0.8942 0.3877 0.5351 0.0424  0.0914  -0.0089 208 ASN C CA  
9818  C C   . ASN C 208 ? 0.8158 0.3655 0.5007 0.0252  0.0844  -0.0263 208 ASN C C   
9819  O O   . ASN C 208 ? 0.7809 0.3323 0.4851 0.0048  0.0996  -0.0394 208 ASN C O   
9820  C CB  . ASN C 208 ? 0.9123 0.3661 0.5421 0.0483  0.0999  -0.0100 208 ASN C CB  
9821  C CG  . ASN C 208 ? 1.0634 0.4528 0.6458 0.0635  0.1128  0.0072  208 ASN C CG  
9822  O OD1 . ASN C 208 ? 1.0753 0.4287 0.6412 0.0518  0.1364  0.0114  208 ASN C OD1 
9823  N ND2 . ASN C 208 ? 1.1567 0.5317 0.7164 0.0906  0.0977  0.0170  208 ASN C ND2 
9824  N N   . CYS C 209 ? 0.7986 0.3932 0.4989 0.0332  0.0625  -0.0271 209 CYS C N   
9825  C CA  . CYS C 209 ? 0.7730 0.4193 0.5096 0.0201  0.0554  -0.0415 209 CYS C CA  
9826  C C   . CYS C 209 ? 0.7566 0.4207 0.5046 0.0036  0.0643  -0.0455 209 CYS C C   
9827  O O   . CYS C 209 ? 0.7357 0.4366 0.5130 -0.0097 0.0634  -0.0599 209 CYS C O   
9828  C CB  . CYS C 209 ? 0.7288 0.4123 0.4749 0.0339  0.0323  -0.0393 209 CYS C CB  
9829  S SG  . CYS C 209 ? 0.8016 0.4962 0.5346 0.0428  0.0220  -0.0265 209 CYS C SG  
9830  N N   . VAL C 210 ? 0.7947 0.4343 0.5194 0.0054  0.0729  -0.0338 210 VAL C N   
9831  C CA  . VAL C 210 ? 0.7861 0.4411 0.5217 -0.0102 0.0836  -0.0379 210 VAL C CA  
9832  C C   . VAL C 210 ? 0.7793 0.4264 0.5327 -0.0321 0.1050  -0.0521 210 VAL C C   
9833  O O   . VAL C 210 ? 0.7889 0.4631 0.5649 -0.0476 0.1119  -0.0625 210 VAL C O   
9834  C CB  . VAL C 210 ? 0.7704 0.3972 0.4737 -0.0026 0.0899  -0.0220 210 VAL C CB  
9835  C CG1 . VAL C 210 ? 0.7283 0.3666 0.4173 0.0184  0.0674  -0.0112 210 VAL C CG1 
9836  C CG2 . VAL C 210 ? 0.8218 0.3880 0.4925 -0.0010 0.1103  -0.0128 210 VAL C CG2 
9837  N N   . TYR C 211 ? 0.8428 0.4548 0.5885 -0.0337 0.1155  -0.0544 211 TYR C N   
9838  C CA  . TYR C 211 ? 0.8748 0.4781 0.6398 -0.0560 0.1365  -0.0703 211 TYR C CA  
9839  C C   . TYR C 211 ? 0.8451 0.4992 0.6509 -0.0676 0.1272  -0.0924 211 TYR C C   
9840  O O   . TYR C 211 ? 0.8605 0.5199 0.6896 -0.0882 0.1424  -0.1097 211 TYR C O   
9841  C CB  . TYR C 211 ? 0.9245 0.4714 0.6671 -0.0530 0.1506  -0.0661 211 TYR C CB  
9842  C CG  . TYR C 211 ? 1.0107 0.5027 0.7127 -0.0461 0.1671  -0.0470 211 TYR C CG  
9843  C CD1 . TYR C 211 ? 1.0438 0.5330 0.7434 -0.0579 0.1830  -0.0443 211 TYR C CD1 
9844  C CD2 . TYR C 211 ? 1.0530 0.4967 0.7175 -0.0259 0.1666  -0.0315 211 TYR C CD2 
9845  C CE1 . TYR C 211 ? 1.1384 0.5760 0.7971 -0.0506 0.1992  -0.0262 211 TYR C CE1 
9846  C CE2 . TYR C 211 ? 1.1344 0.5264 0.7570 -0.0169 0.1812  -0.0133 211 TYR C CE2 
9847  C CZ  . TYR C 211 ? 1.2194 0.6074 0.8379 -0.0296 0.1981  -0.0104 211 TYR C CZ  
9848  O OH  . TYR C 211 ? 1.4226 0.7570 0.9955 -0.0199 0.2142  0.0084  211 TYR C OH  
9849  N N   . GLU C 212 ? 0.8220 0.5136 0.6369 -0.0550 0.1033  -0.0931 212 GLU C N   
9850  C CA  . GLU C 212 ? 0.7548 0.4898 0.6020 -0.0627 0.0943  -0.1132 212 GLU C CA  
9851  C C   . GLU C 212 ? 0.7560 0.5358 0.6308 -0.0759 0.0942  -0.1261 212 GLU C C   
9852  O O   . GLU C 212 ? 0.7843 0.5951 0.6870 -0.0869 0.0929  -0.1468 212 GLU C O   
9853  C CB  . GLU C 212 ? 0.6821 0.4400 0.5276 -0.0445 0.0715  -0.1087 212 GLU C CB  
9854  C CG  . GLU C 212 ? 0.6881 0.4078 0.5119 -0.0311 0.0706  -0.0997 212 GLU C CG  
9855  C CD  . GLU C 212 ? 0.7748 0.5191 0.6001 -0.0142 0.0500  -0.0963 212 GLU C CD  
9856  O OE1 . GLU C 212 ? 0.8479 0.5667 0.6552 0.0007  0.0460  -0.0863 212 GLU C OE1 
9857  O OE2 . GLU C 212 ? 0.7718 0.5608 0.6161 -0.0153 0.0385  -0.1037 212 GLU C OE2 
9858  N N   . THR C 213 ? 0.7487 0.5333 0.6162 -0.0741 0.0953  -0.1155 213 THR C N   
9859  C CA  . THR C 213 ? 0.7076 0.5326 0.6005 -0.0852 0.0966  -0.1271 213 THR C CA  
9860  C C   . THR C 213 ? 0.7341 0.5371 0.6231 -0.0981 0.1188  -0.1244 213 THR C C   
9861  O O   . THR C 213 ? 0.7424 0.5749 0.6590 -0.1129 0.1263  -0.1400 213 THR C O   
9862  C CB  . THR C 213 ? 0.6607 0.5218 0.5532 -0.0705 0.0760  -0.1191 213 THR C CB  
9863  O OG1 . THR C 213 ? 0.7038 0.5359 0.5654 -0.0565 0.0730  -0.0973 213 THR C OG1 
9864  C CG2 . THR C 213 ? 0.5946 0.4850 0.4966 -0.0608 0.0567  -0.1253 213 THR C CG2 
9865  N N   . THR C 214 ? 0.7817 0.5348 0.6370 -0.0921 0.1297  -0.1059 214 THR C N   
9866  C CA  . THR C 214 ? 0.8661 0.5902 0.7117 -0.1037 0.1543  -0.1016 214 THR C CA  
9867  C C   . THR C 214 ? 0.9439 0.6059 0.7640 -0.1061 0.1738  -0.0944 214 THR C C   
9868  O O   . THR C 214 ? 0.9838 0.6029 0.7645 -0.0915 0.1761  -0.0738 214 THR C O   
9869  C CB  . THR C 214 ? 0.9024 0.6241 0.7248 -0.0911 0.1496  -0.0837 214 THR C CB  
9870  O OG1 . THR C 214 ? 0.9645 0.6570 0.7514 -0.0698 0.1370  -0.0646 214 THR C OG1 
9871  C CG2 . THR C 214 ? 0.8397 0.6199 0.6867 -0.0880 0.1314  -0.0909 214 THR C CG2 
9872  N N   . PRO C 215 ? 0.9332 0.5881 0.7741 -0.1235 0.1878  -0.1117 215 PRO C N   
9873  C CA  . PRO C 215 ? 0.9620 0.5550 0.7778 -0.1239 0.2054  -0.1051 215 PRO C CA  
9874  C C   . PRO C 215 ? 1.0536 0.5912 0.8387 -0.1284 0.2335  -0.0905 215 PRO C C   
9875  O O   . PRO C 215 ? 1.1015 0.5806 0.8532 -0.1210 0.2455  -0.0780 215 PRO C O   
9876  C CB  . PRO C 215 ? 0.9339 0.5399 0.7859 -0.1450 0.2146  -0.1315 215 PRO C CB  
9877  C CG  . PRO C 215 ? 0.8981 0.5659 0.7925 -0.1598 0.2103  -0.1514 215 PRO C CG  
9878  C CD  . PRO C 215 ? 0.9054 0.6096 0.7927 -0.1406 0.1851  -0.1391 215 PRO C CD  
9879  N N   . ASN C 216 ? 1.0656 0.6172 0.8582 -0.1386 0.2453  -0.0909 216 ASN C N   
9880  C CA  . ASN C 216 ? 1.1164 0.6143 0.8804 -0.1450 0.2761  -0.0785 216 ASN C CA  
9881  C C   . ASN C 216 ? 1.1019 0.5866 0.8269 -0.1254 0.2699  -0.0552 216 ASN C C   
9882  O O   . ASN C 216 ? 1.1429 0.5867 0.8413 -0.1289 0.2949  -0.0439 216 ASN C O   
9883  C CB  . ASN C 216 ? 1.1366 0.6529 0.9386 -0.1749 0.3015  -0.0986 216 ASN C CB  
9884  C CG  . ASN C 216 ? 1.1600 0.6828 0.9986 -0.1959 0.3110  -0.1234 216 ASN C CG  
9885  O OD1 . ASN C 216 ? 1.1442 0.7201 1.0315 -0.2140 0.3093  -0.1485 216 ASN C OD1 
9886  N ND2 . ASN C 216 ? 1.1976 0.6668 1.0126 -0.1925 0.3201  -0.1175 216 ASN C ND2 
9887  N N   . VAL C 217 ? 1.0656 0.5826 0.7859 -0.1049 0.2384  -0.0482 217 VAL C N   
9888  C CA  . VAL C 217 ? 1.0691 0.5742 0.7527 -0.0856 0.2305  -0.0280 217 VAL C CA  
9889  C C   . VAL C 217 ? 1.0755 0.5133 0.7057 -0.0680 0.2383  -0.0073 217 VAL C C   
9890  O O   . VAL C 217 ? 1.0523 0.4676 0.6743 -0.0604 0.2333  -0.0061 217 VAL C O   
9891  C CB  . VAL C 217 ? 1.0427 0.5980 0.7374 -0.0694 0.1955  -0.0278 217 VAL C CB  
9892  C CG1 . VAL C 217 ? 1.0382 0.5951 0.7339 -0.0571 0.1756  -0.0285 217 VAL C CG1 
9893  C CG2 . VAL C 217 ? 1.0236 0.5687 0.6832 -0.0506 0.1868  -0.0098 217 VAL C CG2 
9894  N N   . LYS C 218 ? 1.0748 0.4790 0.6664 -0.0601 0.2509  0.0090  218 LYS C N   
9895  C CA  . LYS C 218 ? 1.1396 0.4809 0.6742 -0.0386 0.2557  0.0303  218 LYS C CA  
9896  C C   . LYS C 218 ? 1.1632 0.5212 0.6751 -0.0109 0.2242  0.0420  218 LYS C C   
9897  O O   . LYS C 218 ? 1.2345 0.6189 0.7466 -0.0086 0.2170  0.0437  218 LYS C O   
9898  C CB  . LYS C 218 ? 1.2008 0.4897 0.7020 -0.0458 0.2911  0.0412  218 LYS C CB  
9899  C CG  . LYS C 218 ? 1.2283 0.5166 0.7654 -0.0791 0.3231  0.0246  218 LYS C CG  
9900  C CD  . LYS C 218 ? 1.3120 0.5565 0.8217 -0.0888 0.3598  0.0340  218 LYS C CD  
9901  C CE  . LYS C 218 ? 1.4155 0.5764 0.8619 -0.0725 0.3787  0.0562  218 LYS C CE  
9902  N NZ  . LYS C 218 ? 1.4699 0.6063 0.8927 -0.0744 0.4067  0.0625  218 LYS C NZ  
9903  N N   . ILE C 219 ? 1.1413 0.4868 0.6372 0.0093  0.2053  0.0480  219 ILE C N   
9904  C CA  . ILE C 219 ? 1.1344 0.4947 0.6107 0.0359  0.1752  0.0572  219 ILE C CA  
9905  C C   . ILE C 219 ? 1.2167 0.5159 0.6362 0.0608  0.1784  0.0755  219 ILE C C   
9906  O O   . ILE C 219 ? 1.2332 0.4844 0.6361 0.0586  0.1985  0.0793  219 ILE C O   
9907  C CB  . ILE C 219 ? 1.1091 0.5199 0.6230 0.0394  0.1463  0.0456  219 ILE C CB  
9908  C CG1 . ILE C 219 ? 1.1455 0.5311 0.6582 0.0441  0.1472  0.0441  219 ILE C CG1 
9909  C CG2 . ILE C 219 ? 1.0414 0.5083 0.6076 0.0164  0.1447  0.0279  219 ILE C CG2 
9910  C CD1 . ILE C 219 ? 1.1309 0.5598 0.6729 0.0514  0.1198  0.0351  219 ILE C CD1 
9911  N N   . PRO C 220 ? 1.2637 0.5618 0.6509 0.0860  0.1587  0.0866  220 PRO C N   
9912  C CA  . PRO C 220 ? 1.3514 0.5912 0.6798 0.1131  0.1608  0.1042  220 PRO C CA  
9913  C C   . PRO C 220 ? 1.3724 0.5963 0.6997 0.1265  0.1512  0.1041  220 PRO C C   
9914  O O   . PRO C 220 ? 1.3269 0.5859 0.6990 0.1146  0.1424  0.0902  220 PRO C O   
9915  C CB  . PRO C 220 ? 1.3627 0.6224 0.6694 0.1358  0.1352  0.1099  220 PRO C CB  
9916  C CG  . PRO C 220 ? 1.2622 0.5918 0.6221 0.1237  0.1140  0.0945  220 PRO C CG  
9917  C CD  . PRO C 220 ? 1.2302 0.5774 0.6307 0.0914  0.1352  0.0830  220 PRO C CD  
9918  N N   . ASP C 221 ? 1.4520 0.6446 0.7418 0.1495  0.1506  0.1130  221 ASP C N   
9919  C CA  . ASP C 221 ? 1.4290 0.6101 0.7178 0.1639  0.1420  0.1121  221 ASP C CA  
9920  C C   . ASP C 221 ? 1.2816 0.5034 0.5799 0.1865  0.1047  0.1087  221 ASP C C   
9921  O O   . ASP C 221 ? 1.2025 0.4347 0.4797 0.2072  0.0890  0.1117  221 ASP C O   
9922  C CB  . ASP C 221 ? 1.5525 0.6886 0.8010 0.1777  0.1586  0.1209  221 ASP C CB  
9923  C CG  . ASP C 221 ? 1.6374 0.7570 0.8853 0.1891  0.1552  0.1200  221 ASP C CG  
9924  O OD1 . ASP C 221 ? 1.6089 0.7342 0.8892 0.1734  0.1583  0.1118  221 ASP C OD1 
9925  O OD2 . ASP C 221 ? 1.7380 0.8387 0.9532 0.2138  0.1500  0.1265  221 ASP C OD2 
9926  N N   . PHE C 222 ? 1.2110 0.4572 0.5434 0.1819  0.0909  0.1003  222 PHE C N   
9927  C CA  . PHE C 222 ? 1.1588 0.4466 0.5060 0.2016  0.0571  0.0951  222 PHE C CA  
9928  C C   . PHE C 222 ? 1.2526 0.5255 0.5850 0.2238  0.0505  0.0965  222 PHE C C   
9929  O O   . PHE C 222 ? 1.2401 0.5105 0.5900 0.2238  0.0494  0.0915  222 PHE C O   
9930  C CB  . PHE C 222 ? 1.0529 0.3965 0.4576 0.1830  0.0457  0.0791  222 PHE C CB  
9931  C CG  . PHE C 222 ? 1.0082 0.3976 0.4397 0.1652  0.0412  0.0724  222 PHE C CG  
9932  C CD1 . PHE C 222 ? 1.0154 0.4013 0.4566 0.1395  0.0641  0.0702  222 PHE C CD1 
9933  C CD2 . PHE C 222 ? 0.9445 0.3806 0.3936 0.1738  0.0150  0.0671  222 PHE C CD2 
9934  C CE1 . PHE C 222 ? 1.0134 0.4405 0.4785 0.1253  0.0600  0.0640  222 PHE C CE1 
9935  C CE2 . PHE C 222 ? 0.9850 0.4594 0.4574 0.1582  0.0120  0.0613  222 PHE C CE2 
9936  C CZ  . PHE C 222 ? 1.0063 0.4761 0.4857 0.1350  0.0340  0.0601  222 PHE C CZ  
9937  N N   . ALA C 223 ? 1.3055 0.5680 0.6046 0.2436  0.0464  0.1023  223 ALA C N   
9938  C CA  . ALA C 223 ? 1.3534 0.5995 0.6312 0.2676  0.0403  0.1046  223 ALA C CA  
9939  C C   . ALA C 223 ? 1.3495 0.6406 0.6475 0.2874  0.0073  0.0957  223 ALA C C   
9940  O O   . ALA C 223 ? 1.3781 0.6607 0.6603 0.3091  -0.0004 0.0962  223 ALA C O   
9941  C CB  . ALA C 223 ? 1.3927 0.6057 0.6237 0.2811  0.0512  0.1137  223 ALA C CB  
9942  N N   . VAL C 224 ? 1.2779 0.6166 0.6102 0.2806  -0.0114 0.0870  224 VAL C N   
9943  C CA  . VAL C 224 ? 1.2354 0.6214 0.5945 0.2951  -0.0407 0.0763  224 VAL C CA  
9944  C C   . VAL C 224 ? 1.1586 0.5745 0.5614 0.2802  -0.0467 0.0685  224 VAL C C   
9945  O O   . VAL C 224 ? 1.1682 0.5723 0.5788 0.2595  -0.0314 0.0707  224 VAL C O   
9946  C CB  . VAL C 224 ? 1.2755 0.6944 0.6341 0.3033  -0.0590 0.0713  224 VAL C CB  
9947  C CG1 . VAL C 224 ? 1.2866 0.7435 0.6634 0.3231  -0.0855 0.0601  224 VAL C CG1 
9948  C CG2 . VAL C 224 ? 1.3297 0.7128 0.6430 0.3108  -0.0461 0.0803  224 VAL C CG2 
9949  N N   . SER C 225 ? 1.0734 0.5281 0.5050 0.2913  -0.0684 0.0583  225 SER C N   
9950  C CA  . SER C 225 ? 1.0435 0.5301 0.5172 0.2806  -0.0760 0.0495  225 SER C CA  
9951  C C   . SER C 225 ? 1.0116 0.5498 0.5127 0.2765  -0.0952 0.0412  225 SER C C   
9952  O O   . SER C 225 ? 1.0545 0.6194 0.5589 0.2895  -0.1120 0.0351  225 SER C O   
9953  C CB  . SER C 225 ? 1.0083 0.5055 0.5003 0.2937  -0.0846 0.0425  225 SER C CB  
9954  O OG  . SER C 225 ? 0.9866 0.5199 0.5219 0.2818  -0.0906 0.0322  225 SER C OG  
9955  N N   . PHE C 226 ? 0.8777 0.4392 0.4074 0.2520  -0.0891 0.0367  226 PHE C N   
9956  C CA  . PHE C 226 ? 0.8382 0.4510 0.4000 0.2430  -0.1035 0.0275  226 PHE C CA  
9957  C C   . PHE C 226 ? 0.7520 0.4092 0.3626 0.2340  -0.1103 0.0148  226 PHE C C   
9958  O O   . PHE C 226 ? 0.7252 0.4231 0.3658 0.2229  -0.1181 0.0071  226 PHE C O   
9959  C CB  . PHE C 226 ? 0.8490 0.4634 0.4110 0.2200  -0.0902 0.0300  226 PHE C CB  
9960  C CG  . PHE C 226 ? 0.9685 0.5488 0.4855 0.2292  -0.0861 0.0410  226 PHE C CG  
9961  C CD1 . PHE C 226 ? 0.9962 0.5941 0.5053 0.2405  -0.1031 0.0391  226 PHE C CD1 
9962  C CD2 . PHE C 226 ? 1.0258 0.5566 0.5090 0.2257  -0.0638 0.0520  226 PHE C CD2 
9963  C CE1 . PHE C 226 ? 1.0388 0.6144 0.5153 0.2442  -0.0956 0.0449  226 PHE C CE1 
9964  C CE2 . PHE C 226 ? 1.0895 0.5874 0.5290 0.2343  -0.0577 0.0627  226 PHE C CE2 
9965  C CZ  . PHE C 226 ? 1.0687 0.5951 0.5097 0.2417  -0.0731 0.0571  226 PHE C CZ  
9966  N N   . ARG C 227 ? 0.7330 0.3517 0.3343 0.2134  -0.1950 -0.0733 227 ARG C N   
9967  C CA  . ARG C 227 ? 0.8017 0.4649 0.4521 0.2106  -0.1842 -0.0749 227 ARG C CA  
9968  C C   . ARG C 227 ? 0.8003 0.5149 0.5104 0.2238  -0.1967 -0.0818 227 ARG C C   
9969  O O   . ARG C 227 ? 0.7943 0.5551 0.5536 0.2139  -0.1860 -0.0815 227 ARG C O   
9970  C CB  . ARG C 227 ? 0.8820 0.5181 0.5064 0.2193  -0.1775 -0.0748 227 ARG C CB  
9971  C CG  . ARG C 227 ? 0.9736 0.5595 0.5422 0.2031  -0.1636 -0.0690 227 ARG C CG  
9972  C CD  . ARG C 227 ? 1.0074 0.5604 0.5472 0.2122  -0.1584 -0.0702 227 ARG C CD  
9973  N NE  . ARG C 227 ? 1.0031 0.5988 0.5879 0.2206  -0.1548 -0.0750 227 ARG C NE  
9974  C CZ  . ARG C 227 ? 1.0103 0.6305 0.6142 0.2054  -0.1372 -0.0745 227 ARG C CZ  
9975  N NH1 . ARG C 227 ? 0.9993 0.6083 0.5849 0.1809  -0.1228 -0.0705 227 ARG C NH1 
9976  N NH2 . ARG C 227 ? 1.0012 0.6589 0.6430 0.2153  -0.1340 -0.0787 227 ARG C NH2 
9977  N N   . GLU C 228 ? 0.7829 0.4939 0.4922 0.2419  -0.2163 -0.0887 228 GLU C N   
9978  C CA  . GLU C 228 ? 0.7730 0.5384 0.5448 0.2474  -0.2252 -0.0972 228 GLU C CA  
9979  C C   . GLU C 228 ? 0.7780 0.5673 0.5774 0.2336  -0.2282 -0.0970 228 GLU C C   
9980  O O   . GLU C 228 ? 0.7441 0.5825 0.6026 0.2304  -0.2281 -0.1007 228 GLU C O   
9981  C CB  . GLU C 228 ? 0.9113 0.6717 0.6776 0.2647  -0.2409 -0.1071 228 GLU C CB  
9982  C CG  . GLU C 228 ? 1.0281 0.8442 0.8594 0.2704  -0.2499 -0.1174 228 GLU C CG  
9983  C CD  . GLU C 228 ? 1.1375 0.9985 1.0204 0.2711  -0.2381 -0.1174 228 GLU C CD  
9984  O OE1 . GLU C 228 ? 1.1544 1.0643 1.0962 0.2650  -0.2375 -0.1214 228 GLU C OE1 
9985  O OE2 . GLU C 228 ? 1.1809 1.0281 1.0459 0.2770  -0.2283 -0.1139 228 GLU C OE2 
9986  N N   . ASP C 229 ? 0.7341 0.4893 0.4921 0.2243  -0.2292 -0.0931 229 ASP C N   
9987  C CA  . ASP C 229 ? 0.7073 0.4836 0.4886 0.2100  -0.2304 -0.0929 229 ASP C CA  
9988  C C   . ASP C 229 ? 0.6796 0.4869 0.4947 0.1883  -0.2075 -0.0866 229 ASP C C   
9989  O O   . ASP C 229 ? 0.6558 0.4994 0.5165 0.1785  -0.2060 -0.0883 229 ASP C O   
9990  C CB  . ASP C 229 ? 0.7035 0.4371 0.4315 0.2018  -0.2303 -0.0902 229 ASP C CB  
9991  C CG  . ASP C 229 ? 0.7614 0.4803 0.4775 0.2135  -0.2450 -0.0989 229 ASP C CG  
9992  O OD1 . ASP C 229 ? 0.6672 0.4026 0.4055 0.2288  -0.2565 -0.1075 229 ASP C OD1 
9993  O OD2 . ASP C 229 ? 0.8079 0.5015 0.4941 0.2070  -0.2440 -0.0972 229 ASP C OD2 
9994  N N   . ALA C 230 ? 0.6293 0.4207 0.4211 0.1811  -0.1900 -0.0797 230 ALA C N   
9995  C CA  . ALA C 230 ? 0.6350 0.4564 0.4567 0.1637  -0.1698 -0.0741 230 ALA C CA  
9996  C C   . ALA C 230 ? 0.5565 0.4267 0.4386 0.1692  -0.1692 -0.0769 230 ALA C C   
9997  O O   . ALA C 230 ? 0.4610 0.3645 0.3831 0.1566  -0.1613 -0.0745 230 ALA C O   
9998  C CB  . ALA C 230 ? 0.6072 0.4041 0.3936 0.1579  -0.1541 -0.0688 230 ALA C CB  
9999  N N   . SER C 231 ? 0.5831 0.4574 0.4727 0.1886  -0.1777 -0.0825 231 SER C N   
10000 C CA  . SER C 231 ? 0.5509 0.4735 0.4997 0.1948  -0.1771 -0.0868 231 SER C CA  
10001 C C   . SER C 231 ? 0.5411 0.4931 0.5335 0.1908  -0.1881 -0.0920 231 SER C C   
10002 O O   . SER C 231 ? 0.5142 0.5061 0.5569 0.1810  -0.1784 -0.0908 231 SER C O   
10003 C CB  . SER C 231 ? 0.5863 0.5064 0.5337 0.2192  -0.1879 -0.0943 231 SER C CB  
10004 O OG  . SER C 231 ? 0.6221 0.5323 0.5511 0.2215  -0.1732 -0.0906 231 SER C OG  
10005 N N   . LYS C 232 ? 0.5747 0.5056 0.5467 0.1981  -0.2081 -0.0982 232 LYS C N   
10006 C CA  . LYS C 232 ? 0.5311 0.4893 0.5445 0.1965  -0.2217 -0.1063 232 LYS C CA  
10007 C C   . LYS C 232 ? 0.4584 0.4294 0.4910 0.1734  -0.2089 -0.1004 232 LYS C C   
10008 O O   . LYS C 232 ? 0.4774 0.4847 0.5635 0.1664  -0.2088 -0.1041 232 LYS C O   
10009 C CB  . LYS C 232 ? 0.6040 0.5319 0.5820 0.2066  -0.2421 -0.1141 232 LYS C CB  
10010 C CG  . LYS C 232 ? 0.7411 0.6610 0.7069 0.2251  -0.2513 -0.1216 232 LYS C CG  
10011 C CD  . LYS C 232 ? 0.8321 0.8024 0.8605 0.2300  -0.2499 -0.1287 232 LYS C CD  
10012 C CE  . LYS C 232 ? 0.8891 0.8690 0.9237 0.2349  -0.2344 -0.1225 232 LYS C CE  
10013 N NZ  . LYS C 232 ? 0.8480 0.8803 0.9458 0.2357  -0.2260 -0.1266 232 LYS C NZ  
10014 N N   . HIS C 233 ? 0.4441 0.3853 0.4345 0.1612  -0.1978 -0.0918 233 HIS C N   
10015 C CA  . HIS C 233 ? 0.4605 0.4124 0.4666 0.1413  -0.1857 -0.0862 233 HIS C CA  
10016 C C   . HIS C 233 ? 0.4287 0.4188 0.4833 0.1326  -0.1688 -0.0805 233 HIS C C   
10017 O O   . HIS C 233 ? 0.4354 0.4492 0.5297 0.1221  -0.1661 -0.0805 233 HIS C O   
10018 C CB  . HIS C 233 ? 0.5359 0.4541 0.4909 0.1311  -0.1744 -0.0785 233 HIS C CB  
10019 C CG  . HIS C 233 ? 0.6214 0.5039 0.5321 0.1337  -0.1868 -0.0826 233 HIS C CG  
10020 N ND1 . HIS C 233 ? 0.6021 0.4860 0.5198 0.1265  -0.1932 -0.0866 233 HIS C ND1 
10021 C CD2 . HIS C 233 ? 0.6465 0.4884 0.5024 0.1423  -0.1927 -0.0829 233 HIS C CD2 
10022 C CE1 . HIS C 233 ? 0.6665 0.5143 0.5353 0.1311  -0.2023 -0.0894 233 HIS C CE1 
10023 N NE2 . HIS C 233 ? 0.6687 0.4896 0.4987 0.1403  -0.2017 -0.0865 233 HIS C NE2 
10024 N N   . VAL C 234 ? 0.4713 0.4659 0.5215 0.1373  -0.1572 -0.0759 234 VAL C N   
10025 C CA  . VAL C 234 ? 0.4485 0.4774 0.5388 0.1303  -0.1396 -0.0697 234 VAL C CA  
10026 C C   . VAL C 234 ? 0.4552 0.5211 0.6015 0.1367  -0.1459 -0.0773 234 VAL C C   
10027 O O   . VAL C 234 ? 0.3754 0.4709 0.5658 0.1258  -0.1354 -0.0739 234 VAL C O   
10028 C CB  . VAL C 234 ? 0.4639 0.4845 0.5280 0.1345  -0.1259 -0.0641 234 VAL C CB  
10029 C CG1 . VAL C 234 ? 0.3434 0.3961 0.4404 0.1270  -0.1059 -0.0563 234 VAL C CG1 
10030 C CG2 . VAL C 234 ? 0.5320 0.5157 0.5423 0.1273  -0.1219 -0.0594 234 VAL C CG2 
10031 N N   . GLU C 235 ? 0.5146 0.5791 0.6602 0.1544  -0.1629 -0.0880 235 GLU C N   
10032 C CA  . GLU C 235 ? 0.5886 0.6927 0.7903 0.1619  -0.1693 -0.0974 235 GLU C CA  
10033 C C   . GLU C 235 ? 0.5558 0.6775 0.7966 0.1522  -0.1794 -0.1039 235 GLU C C   
10034 O O   . GLU C 235 ? 0.5264 0.6853 0.8231 0.1437  -0.1714 -0.1052 235 GLU C O   
10035 C CB  . GLU C 235 ? 0.6659 0.7626 0.8543 0.1859  -0.1878 -0.1084 235 GLU C CB  
10036 C CG  . GLU C 235 ? 0.7654 0.9066 1.0098 0.1953  -0.1888 -0.1176 235 GLU C CG  
10037 C CD  . GLU C 235 ? 0.8238 0.9903 1.0905 0.1914  -0.1639 -0.1101 235 GLU C CD  
10038 O OE1 . GLU C 235 ? 0.8902 1.0446 1.1297 0.2046  -0.1591 -0.1090 235 GLU C OE1 
10039 O OE2 . GLU C 235 ? 0.7879 0.9838 1.0963 0.1747  -0.1483 -0.1050 235 GLU C OE2 
10040 N N   . LEU C 236 ? 0.4992 0.5936 0.7110 0.1528  -0.1964 -0.1086 236 LEU C N   
10041 C CA  . LEU C 236 ? 0.4645 0.5723 0.7099 0.1436  -0.2069 -0.1163 236 LEU C CA  
10042 C C   . LEU C 236 ? 0.4469 0.5629 0.7126 0.1216  -0.1870 -0.1056 236 LEU C C   
10043 O O   . LEU C 236 ? 0.4435 0.5861 0.7602 0.1114  -0.1861 -0.1097 236 LEU C O   
10044 C CB  . LEU C 236 ? 0.4395 0.5130 0.6418 0.1500  -0.2280 -0.1232 236 LEU C CB  
10045 C CG  . LEU C 236 ? 0.4723 0.5298 0.6460 0.1683  -0.2432 -0.1322 236 LEU C CG  
10046 C CD1 . LEU C 236 ? 0.5243 0.5423 0.6472 0.1717  -0.2578 -0.1364 236 LEU C CD1 
10047 C CD2 . LEU C 236 ? 0.4403 0.5337 0.6648 0.1715  -0.2488 -0.1442 236 LEU C CD2 
10048 N N   . ALA C 237 ? 0.4429 0.5361 0.6700 0.1143  -0.1712 -0.0923 237 ALA C N   
10049 C CA  . ALA C 237 ? 0.4496 0.5503 0.6933 0.0965  -0.1521 -0.0811 237 ALA C CA  
10050 C C   . ALA C 237 ? 0.4020 0.5395 0.6976 0.0913  -0.1366 -0.0769 237 ALA C C   
10051 O O   . ALA C 237 ? 0.4450 0.5981 0.7791 0.0780  -0.1298 -0.0748 237 ALA C O   
10052 C CB  . ALA C 237 ? 0.4559 0.5317 0.6515 0.0926  -0.1382 -0.0688 237 ALA C CB  
10053 N N   . LYS C 238 ? 0.3948 0.5451 0.6913 0.1016  -0.1302 -0.0760 238 LYS C N   
10054 C CA  . LYS C 238 ? 0.4164 0.6031 0.7604 0.0978  -0.1137 -0.0726 238 LYS C CA  
10055 C C   . LYS C 238 ? 0.4524 0.6699 0.8568 0.0940  -0.1226 -0.0844 238 LYS C C   
10056 O O   . LYS C 238 ? 0.4512 0.6922 0.8988 0.0804  -0.1071 -0.0794 238 LYS C O   
10057 C CB  . LYS C 238 ? 0.3778 0.5720 0.7102 0.1130  -0.1089 -0.0735 238 LYS C CB  
10058 C CG  . LYS C 238 ? 0.3692 0.5420 0.6542 0.1131  -0.0935 -0.0610 238 LYS C CG  
10059 C CD  . LYS C 238 ? 0.3742 0.5530 0.6487 0.1295  -0.0904 -0.0645 238 LYS C CD  
10060 C CE  . LYS C 238 ? 0.3279 0.5502 0.6570 0.1314  -0.0792 -0.0672 238 LYS C CE  
10061 N NZ  . LYS C 238 ? 0.3611 0.5907 0.6856 0.1514  -0.0827 -0.0758 238 LYS C NZ  
10062 N N   . GLU C 239 ? 0.4723 0.6899 0.8803 0.1058  -0.1474 -0.1004 239 GLU C N   
10063 C CA  . GLU C 239 ? 0.5459 0.7963 1.0142 0.1027  -0.1583 -0.1146 239 GLU C CA  
10064 C C   . GLU C 239 ? 0.5418 0.7867 1.0293 0.0837  -0.1583 -0.1139 239 GLU C C   
10065 O O   . GLU C 239 ? 0.5376 0.8089 1.0782 0.0698  -0.1490 -0.1155 239 GLU C O   
10066 C CB  . GLU C 239 ? 0.6076 0.8488 1.0562 0.1186  -0.1824 -0.1297 239 GLU C CB  
10067 C CG  . GLU C 239 ? 0.6879 0.9628 1.1749 0.1243  -0.1821 -0.1397 239 GLU C CG  
10068 C CD  . GLU C 239 ? 0.7639 1.0650 1.3053 0.1086  -0.1818 -0.1482 239 GLU C CD  
10069 O OE1 . GLU C 239 ? 0.7994 1.1325 1.3789 0.1102  -0.1791 -0.1561 239 GLU C OE1 
10070 O OE2 . GLU C 239 ? 0.7971 1.0859 1.3429 0.0946  -0.1842 -0.1477 239 GLU C OE2 
10071 N N   . LYS C 240 ? 0.5371 0.7454 0.9791 0.0823  -0.1669 -0.1115 240 LYS C N   
10072 C CA  . LYS C 240 ? 0.5254 0.7243 0.9803 0.0663  -0.1676 -0.1116 240 LYS C CA  
10073 C C   . LYS C 240 ? 0.5203 0.7255 0.9954 0.0490  -0.1405 -0.0952 240 LYS C C   
10074 O O   . LYS C 240 ? 0.5441 0.7595 1.0607 0.0344  -0.1366 -0.0970 240 LYS C O   
10075 C CB  . LYS C 240 ? 0.4967 0.6553 0.8935 0.0699  -0.1789 -0.1111 240 LYS C CB  
10076 C CG  . LYS C 240 ? 0.4901 0.6351 0.8935 0.0559  -0.1802 -0.1120 240 LYS C CG  
10077 C CD  . LYS C 240 ? 0.4869 0.6240 0.8882 0.0618  -0.2078 -0.1310 240 LYS C CD  
10078 C CE  . LYS C 240 ? 0.4357 0.5713 0.8668 0.0466  -0.2096 -0.1365 240 LYS C CE  
10079 N NZ  . LYS C 240 ? 0.4129 0.5442 0.8460 0.0509  -0.2291 -0.1550 240 LYS C NZ  
10080 N N   . TYR C 241 ? 0.5096 0.7072 0.9547 0.0508  -0.1217 -0.0794 241 TYR C N   
10081 C CA  . TYR C 241 ? 0.5260 0.7272 0.9835 0.0370  -0.0962 -0.0625 241 TYR C CA  
10082 C C   . TYR C 241 ? 0.5402 0.7771 1.0590 0.0282  -0.0834 -0.0632 241 TYR C C   
10083 O O   . TYR C 241 ? 0.5478 0.7869 1.0951 0.0123  -0.0706 -0.0562 241 TYR C O   
10084 C CB  . TYR C 241 ? 0.5296 0.7193 0.9429 0.0430  -0.0809 -0.0479 241 TYR C CB  
10085 C CG  . TYR C 241 ? 0.4978 0.6878 0.9148 0.0315  -0.0563 -0.0297 241 TYR C CG  
10086 C CD1 . TYR C 241 ? 0.4657 0.6819 0.9163 0.0270  -0.0367 -0.0225 241 TYR C CD1 
10087 C CD2 . TYR C 241 ? 0.4967 0.6609 0.8826 0.0261  -0.0524 -0.0198 241 TYR C CD2 
10088 C CE1 . TYR C 241 ? 0.4727 0.6859 0.9219 0.0177  -0.0142 -0.0048 241 TYR C CE1 
10089 C CE2 . TYR C 241 ? 0.4746 0.6374 0.8612 0.0180  -0.0315 -0.0028 241 TYR C CE2 
10090 C CZ  . TYR C 241 ? 0.4804 0.6661 0.8967 0.0139  -0.0126 0.0053  241 TYR C CZ  
10091 O OH  . TYR C 241 ? 0.5105 0.6917 0.9226 0.0071  0.0084  0.0233  241 TYR C OH  
10092 N N   . PHE C 242 ? 0.5502 0.8147 1.0899 0.0384  -0.0856 -0.0715 242 PHE C N   
10093 C CA  . PHE C 242 ? 0.5510 0.8543 1.1527 0.0300  -0.0725 -0.0741 242 PHE C CA  
10094 C C   . PHE C 242 ? 0.5408 0.8558 1.1934 0.0169  -0.0836 -0.0872 242 PHE C C   
10095 O O   . PHE C 242 ? 0.5204 0.8508 1.2160 -0.0003 -0.0660 -0.0823 242 PHE C O   
10096 C CB  . PHE C 242 ? 0.5309 0.8627 1.1459 0.0465  -0.0770 -0.0846 242 PHE C CB  
10097 C CG  . PHE C 242 ? 0.5429 0.9158 1.2171 0.0382  -0.0613 -0.0877 242 PHE C CG  
10098 C CD1 . PHE C 242 ? 0.5503 0.9390 1.2364 0.0325  -0.0315 -0.0729 242 PHE C CD1 
10099 C CD2 . PHE C 242 ? 0.5592 0.9481 1.2638 0.0353  -0.0741 -0.1038 242 PHE C CD2 
10100 C CE1 . PHE C 242 ? 0.5574 0.9783 1.2865 0.0235  -0.0143 -0.0742 242 PHE C CE1 
10101 C CE2 . PHE C 242 ? 0.5709 0.9933 1.3208 0.0261  -0.0580 -0.1059 242 PHE C CE2 
10102 C CZ  . PHE C 242 ? 0.5672 1.0054 1.3289 0.0198  -0.0277 -0.0909 242 PHE C CZ  
10103 N N   . GLU C 243 ? 0.5613 0.8642 1.2013 0.0243  -0.1113 -0.1034 243 GLU C N   
10104 C CA  . GLU C 243 ? 0.6145 0.9166 1.2814 0.0125  -0.1215 -0.1159 243 GLU C CA  
10105 C C   . GLU C 243 ? 0.6151 0.8997 1.2932 -0.0065 -0.1103 -0.1059 243 GLU C C   
10106 O O   . GLU C 243 ? 0.6463 0.9388 1.3632 -0.0228 -0.1017 -0.1079 243 GLU C O   
10107 C CB  . GLU C 243 ? 0.6668 0.9503 1.3023 0.0259  -0.1517 -0.1325 243 GLU C CB  
10108 C CG  . GLU C 243 ? 0.7385 1.0123 1.3908 0.0152  -0.1639 -0.1449 243 GLU C CG  
10109 C CD  . GLU C 243 ? 0.8014 1.0413 1.4067 0.0243  -0.1859 -0.1518 243 GLU C CD  
10110 O OE1 . GLU C 243 ? 0.8272 1.0495 1.4353 0.0137  -0.1894 -0.1547 243 GLU C OE1 
10111 O OE2 . GLU C 243 ? 0.8230 1.0519 1.3864 0.0421  -0.1985 -0.1541 243 GLU C OE2 
10112 N N   . ILE C 244 ? 0.5536 0.8090 1.1894 -0.0043 -0.1086 -0.0938 244 ILE C N   
10113 C CA  . ILE C 244 ? 0.4936 0.7242 1.1264 -0.0196 -0.0979 -0.0832 244 ILE C CA  
10114 C C   . ILE C 244 ? 0.4801 0.7179 1.1312 -0.0320 -0.0666 -0.0633 244 ILE C C   
10115 O O   . ILE C 244 ? 0.4969 0.7281 1.1760 -0.0488 -0.0559 -0.0584 244 ILE C O   
10116 C CB  . ILE C 244 ? 0.4535 0.6461 1.0225 -0.0115 -0.1046 -0.0767 244 ILE C CB  
10117 C CG1 . ILE C 244 ? 0.4483 0.6318 0.9940 0.0014  -0.1336 -0.0952 244 ILE C CG1 
10118 C CG2 . ILE C 244 ? 0.4393 0.6066 1.0068 -0.0247 -0.0963 -0.0680 244 ILE C CG2 
10119 C CD1 . ILE C 244 ? 0.4309 0.6155 1.0098 -0.0059 -0.1525 -0.1139 244 ILE C CD1 
10120 N N   . PHE C 245 ? 0.4614 0.7105 1.0951 -0.0239 -0.0512 -0.0517 245 PHE C N   
10121 C CA  . PHE C 245 ? 0.4772 0.7232 1.1071 -0.0322 -0.0217 -0.0295 245 PHE C CA  
10122 C C   . PHE C 245 ? 0.5572 0.8385 1.2232 -0.0351 -0.0014 -0.0257 245 PHE C C   
10123 O O   . PHE C 245 ? 0.6026 0.8827 1.2756 -0.0457 0.0245  -0.0083 245 PHE C O   
10124 C CB  . PHE C 245 ? 0.4385 0.6596 1.0040 -0.0209 -0.0169 -0.0150 245 PHE C CB  
10125 C CG  . PHE C 245 ? 0.4395 0.6259 0.9705 -0.0210 -0.0284 -0.0138 245 PHE C CG  
10126 C CD1 . PHE C 245 ? 0.4386 0.6062 0.9779 -0.0336 -0.0190 -0.0040 245 PHE C CD1 
10127 C CD2 . PHE C 245 ? 0.4212 0.5928 0.9109 -0.0083 -0.0477 -0.0225 245 PHE C CD2 
10128 C CE1 . PHE C 245 ? 0.4472 0.5847 0.9563 -0.0322 -0.0295 -0.0042 245 PHE C CE1 
10129 C CE2 . PHE C 245 ? 0.4085 0.5509 0.8680 -0.0085 -0.0566 -0.0224 245 PHE C CE2 
10130 C CZ  . PHE C 245 ? 0.4301 0.5570 0.9004 -0.0198 -0.0479 -0.0138 245 PHE C CZ  
10131 N N   . GLY C 246 ? 0.6052 0.9170 1.2924 -0.0250 -0.0113 -0.0409 246 GLY C N   
10132 C CA  . GLY C 246 ? 0.6456 0.9946 1.3736 -0.0285 0.0090  -0.0392 246 GLY C CA  
10133 C C   . GLY C 246 ? 0.6663 1.0184 1.3597 -0.0174 0.0277  -0.0251 246 GLY C C   
10134 O O   . GLY C 246 ? 0.7140 1.0892 1.4331 -0.0238 0.0528  -0.0168 246 GLY C O   
10135 N N   . GLU C 247 ? 0.6317 0.9604 1.2665 -0.0017 0.0172  -0.0222 247 GLU C N   
10136 C CA  . GLU C 247 ? 0.6197 0.9547 1.2236 0.0124  0.0280  -0.0160 247 GLU C CA  
10137 C C   . GLU C 247 ? 0.6227 0.9394 1.1818 0.0304  0.0038  -0.0259 247 GLU C C   
10138 O O   . GLU C 247 ? 0.6248 0.9174 1.1652 0.0303  -0.0159 -0.0314 247 GLU C O   
10139 C CB  . GLU C 247 ? 0.6565 0.9734 1.2240 0.0084  0.0522  0.0070  247 GLU C CB  
10140 C CG  . GLU C 247 ? 0.7065 1.0159 1.2948 -0.0109 0.0710  0.0218  247 GLU C CG  
10141 C CD  . GLU C 247 ? 0.7627 1.0466 1.3027 -0.0104 0.0877  0.0437  247 GLU C CD  
10142 O OE1 . GLU C 247 ? 0.7772 1.0628 1.2817 0.0020  0.0942  0.0484  247 GLU C OE1 
10143 O OE2 . GLU C 247 ? 0.7850 1.0467 1.3222 -0.0217 0.0936  0.0554  247 GLU C OE2 
10144 N N   . HIS C 248 ? 0.6131 0.9394 1.1542 0.0456  0.0062  -0.0282 248 HIS C N   
10145 C CA  . HIS C 248 ? 0.6073 0.9076 1.0959 0.0610  -0.0120 -0.0332 248 HIS C CA  
10146 C C   . HIS C 248 ? 0.5655 0.8350 1.0014 0.0580  -0.0019 -0.0168 248 HIS C C   
10147 O O   . HIS C 248 ? 0.5493 0.8248 0.9783 0.0553  0.0204  -0.0035 248 HIS C O   
10148 C CB  . HIS C 248 ? 0.6515 0.9681 1.1363 0.0794  -0.0143 -0.0423 248 HIS C CB  
10149 C CG  . HIS C 248 ? 0.6624 0.9907 1.1697 0.0909  -0.0393 -0.0623 248 HIS C CG  
10150 N ND1 . HIS C 248 ? 0.6780 1.0334 1.2062 0.1064  -0.0418 -0.0737 248 HIS C ND1 
10151 C CD2 . HIS C 248 ? 0.6695 0.9862 1.1800 0.0908  -0.0638 -0.0733 248 HIS C CD2 
10152 C CE1 . HIS C 248 ? 0.6842 1.0441 1.2276 0.1160  -0.0678 -0.0907 248 HIS C CE1 
10153 N NE2 . HIS C 248 ? 0.6796 1.0159 1.2114 0.1066  -0.0815 -0.0907 248 HIS C NE2 
10154 N N   . PRO C 249 ? 0.5200 0.7584 0.9194 0.0583  -0.0174 -0.0178 249 PRO C N   
10155 C CA  . PRO C 249 ? 0.4826 0.6961 0.8388 0.0543  -0.0083 -0.0037 249 PRO C CA  
10156 C C   . PRO C 249 ? 0.4786 0.6883 0.7961 0.0651  0.0000  0.0004  249 PRO C C   
10157 O O   . PRO C 249 ? 0.5285 0.7338 0.8279 0.0776  -0.0113 -0.0099 249 PRO C O   
10158 C CB  . PRO C 249 ? 0.4665 0.6523 0.7972 0.0538  -0.0286 -0.0102 249 PRO C CB  
10159 C CG  . PRO C 249 ? 0.4781 0.6676 0.8161 0.0642  -0.0488 -0.0271 249 PRO C CG  
10160 C CD  . PRO C 249 ? 0.5019 0.7270 0.8947 0.0641  -0.0438 -0.0327 249 PRO C CD  
10161 N N   . VAL C 250 ? 0.4255 0.6354 0.7290 0.0610  0.0195  0.0151  250 VAL C N   
10162 C CA  . VAL C 250 ? 0.4351 0.6413 0.7007 0.0705  0.0279  0.0186  250 VAL C CA  
10163 C C   . VAL C 250 ? 0.4143 0.5934 0.6317 0.0696  0.0238  0.0234  250 VAL C C   
10164 O O   . VAL C 250 ? 0.4096 0.5825 0.5922 0.0767  0.0277  0.0239  250 VAL C O   
10165 C CB  . VAL C 250 ? 0.4711 0.6987 0.7498 0.0692  0.0528  0.0300  250 VAL C CB  
10166 C CG1 . VAL C 250 ? 0.4759 0.7339 0.8098 0.0668  0.0591  0.0251  250 VAL C CG1 
10167 C CG2 . VAL C 250 ? 0.4493 0.6676 0.7183 0.0592  0.0657  0.0471  250 VAL C CG2 
10168 N N   . TYR C 251 ? 0.3927 0.5568 0.6084 0.0612  0.0159  0.0257  251 TYR C N   
10169 C CA  . TYR C 251 ? 0.4203 0.5617 0.5950 0.0605  0.0096  0.0269  251 TYR C CA  
10170 C C   . TYR C 251 ? 0.4420 0.5666 0.6144 0.0581  -0.0094 0.0167  251 TYR C C   
10171 O O   . TYR C 251 ? 0.3752 0.5047 0.5799 0.0541  -0.0164 0.0123  251 TYR C O   
10172 C CB  . TYR C 251 ? 0.4806 0.6196 0.6482 0.0543  0.0213  0.0414  251 TYR C CB  
10173 C CG  . TYR C 251 ? 0.5214 0.6717 0.7272 0.0467  0.0323  0.0511  251 TYR C CG  
10174 C CD1 . TYR C 251 ? 0.5493 0.6935 0.7809 0.0387  0.0238  0.0483  251 TYR C CD1 
10175 C CD2 . TYR C 251 ? 0.5480 0.7132 0.7625 0.0469  0.0520  0.0628  251 TYR C CD2 
10176 C CE1 . TYR C 251 ? 0.6090 0.7606 0.8762 0.0300  0.0345  0.0567  251 TYR C CE1 
10177 C CE2 . TYR C 251 ? 0.5909 0.7636 0.8395 0.0382  0.0642  0.0725  251 TYR C CE2 
10178 C CZ  . TYR C 251 ? 0.6416 0.8068 0.9174 0.0291  0.0554  0.0694  251 TYR C CZ  
10179 O OH  . TYR C 251 ? 0.6936 0.8636 1.0039 0.0188  0.0684  0.0788  251 TYR C OH  
10180 N N   . MET C 252 ? 0.3886 0.4934 0.5221 0.0600  -0.0172 0.0122  252 MET C N   
10181 C CA  . MET C 252 ? 0.3986 0.4849 0.5215 0.0586  -0.0336 0.0027  252 MET C CA  
10182 C C   . MET C 252 ? 0.4184 0.4881 0.5063 0.0546  -0.0338 0.0043  252 MET C C   
10183 O O   . MET C 252 ? 0.3459 0.4159 0.4104 0.0558  -0.0255 0.0083  252 MET C O   
10184 C CB  . MET C 252 ? 0.3503 0.4282 0.4621 0.0677  -0.0457 -0.0091 252 MET C CB  
10185 C CG  . MET C 252 ? 0.3346 0.4275 0.4850 0.0717  -0.0534 -0.0157 252 MET C CG  
10186 S SD  . MET C 252 ? 0.4676 0.5425 0.5981 0.0839  -0.0741 -0.0305 252 MET C SD  
10187 C CE  . MET C 252 ? 0.4396 0.5439 0.6261 0.0888  -0.0812 -0.0382 252 MET C CE  
10188 N N   . TRP C 253 ? 0.2986 0.3558 0.3846 0.0498  -0.0432 0.0001  253 TRP C N   
10189 C CA  . TRP C 253 ? 0.3480 0.3908 0.4024 0.0461  -0.0443 -0.0014 253 TRP C CA  
10190 C C   . TRP C 253 ? 0.4102 0.4327 0.4357 0.0484  -0.0545 -0.0120 253 TRP C C   
10191 O O   . TRP C 253 ? 0.4355 0.4486 0.4661 0.0496  -0.0660 -0.0190 253 TRP C O   
10192 C CB  . TRP C 253 ? 0.3037 0.3440 0.3699 0.0402  -0.0467 0.0000  253 TRP C CB  
10193 C CG  . TRP C 253 ? 0.3207 0.3473 0.3566 0.0369  -0.0496 -0.0051 253 TRP C CG  
10194 C CD1 . TRP C 253 ? 0.3321 0.3433 0.3573 0.0346  -0.0591 -0.0141 253 TRP C CD1 
10195 C CD2 . TRP C 253 ? 0.3038 0.3331 0.3172 0.0352  -0.0422 -0.0026 253 TRP C CD2 
10196 N NE1 . TRP C 253 ? 0.3255 0.3303 0.3242 0.0308  -0.0562 -0.0168 253 TRP C NE1 
10197 C CE2 . TRP C 253 ? 0.3195 0.3364 0.3124 0.0309  -0.0466 -0.0105 253 TRP C CE2 
10198 C CE3 . TRP C 253 ? 0.3335 0.3756 0.3419 0.0372  -0.0325 0.0048  253 TRP C CE3 
10199 C CZ2 . TRP C 253 ? 0.2763 0.2959 0.2487 0.0274  -0.0415 -0.0120 253 TRP C CZ2 
10200 C CZ3 . TRP C 253 ? 0.3114 0.3551 0.2976 0.0349  -0.0294 0.0030  253 TRP C CZ3 
10201 C CH2 . TRP C 253 ? 0.3279 0.3618 0.2985 0.0296  -0.0338 -0.0057 253 TRP C CH2 
10202 N N   . PRO C 254 ? 0.4510 0.4641 0.4444 0.0491  -0.0509 -0.0138 254 PRO C N   
10203 C CA  . PRO C 254 ? 0.4471 0.4350 0.4085 0.0502  -0.0590 -0.0226 254 PRO C CA  
10204 C C   . PRO C 254 ? 0.3888 0.3634 0.3360 0.0429  -0.0628 -0.0266 254 PRO C C   
10205 O O   . PRO C 254 ? 0.3346 0.3152 0.2767 0.0362  -0.0559 -0.0243 254 PRO C O   
10206 C CB  . PRO C 254 ? 0.3912 0.3735 0.3249 0.0504  -0.0513 -0.0228 254 PRO C CB  
10207 C CG  . PRO C 254 ? 0.4665 0.4705 0.4117 0.0468  -0.0405 -0.0153 254 PRO C CG  
10208 C CD  . PRO C 254 ? 0.4547 0.4781 0.4381 0.0490  -0.0393 -0.0082 254 PRO C CD  
10209 N N   . PRO C 255 ? 0.4121 0.3695 0.3513 0.0450  -0.0740 -0.0332 255 PRO C N   
10210 C CA  . PRO C 255 ? 0.3966 0.3417 0.3219 0.0386  -0.0768 -0.0376 255 PRO C CA  
10211 C C   . PRO C 255 ? 0.3705 0.3069 0.2654 0.0306  -0.0677 -0.0387 255 PRO C C   
10212 O O   . PRO C 255 ? 0.4326 0.3553 0.3016 0.0305  -0.0647 -0.0401 255 PRO C O   
10213 C CB  . PRO C 255 ? 0.4003 0.3232 0.3099 0.0447  -0.0901 -0.0448 255 PRO C CB  
10214 C CG  . PRO C 255 ? 0.4678 0.4024 0.4034 0.0543  -0.0968 -0.0443 255 PRO C CG  
10215 C CD  . PRO C 255 ? 0.4043 0.3535 0.3460 0.0548  -0.0851 -0.0377 255 PRO C CD  
10216 N N   . GLU C 256 ? 0.4206 0.3660 0.3208 0.0239  -0.0632 -0.0389 256 GLU C N   
10217 C CA  . GLU C 256 ? 0.4676 0.4115 0.3460 0.0152  -0.0543 -0.0416 256 GLU C CA  
10218 C C   . GLU C 256 ? 0.4573 0.4145 0.3353 0.0144  -0.0464 -0.0378 256 GLU C C   
10219 O O   . GLU C 256 ? 0.4889 0.4409 0.3446 0.0072  -0.0402 -0.0420 256 GLU C O   
10220 C CB  . GLU C 256 ? 0.4881 0.4027 0.3281 0.0105  -0.0548 -0.0485 256 GLU C CB  
10221 C CG  . GLU C 256 ? 0.4781 0.3765 0.3110 0.0125  -0.0630 -0.0530 256 GLU C CG  
10222 C CD  . GLU C 256 ? 0.5045 0.4183 0.3561 0.0093  -0.0617 -0.0551 256 GLU C CD  
10223 O OE1 . GLU C 256 ? 0.4941 0.4018 0.3524 0.0134  -0.0704 -0.0581 256 GLU C OE1 
10224 O OE2 . GLU C 256 ? 0.4853 0.4173 0.3451 0.0036  -0.0530 -0.0546 256 GLU C OE2 
10225 N N   . ALA C 257 ? 0.4275 0.4018 0.3295 0.0211  -0.0459 -0.0304 257 ALA C N   
10226 C CA  . ALA C 257 ? 0.3688 0.3552 0.2687 0.0227  -0.0389 -0.0268 257 ALA C CA  
10227 C C   . ALA C 257 ? 0.4218 0.3881 0.2920 0.0220  -0.0382 -0.0322 257 ALA C C   
10228 O O   . ALA C 257 ? 0.4384 0.4091 0.2968 0.0199  -0.0322 -0.0333 257 ALA C O   
10229 C CB  . ALA C 257 ? 0.3218 0.3263 0.2226 0.0177  -0.0325 -0.0262 257 ALA C CB  
10230 N N   A SER C 258 ? 0.4695 0.4115 0.3254 0.0243  -0.0450 -0.0360 258 SER C N   
10231 N N   B SER C 258 ? 0.4702 0.4124 0.3264 0.0244  -0.0451 -0.0360 258 SER C N   
10232 C CA  A SER C 258 ? 0.5073 0.4222 0.3293 0.0232  -0.0445 -0.0412 258 SER C CA  
10233 C CA  B SER C 258 ? 0.5141 0.4293 0.3366 0.0235  -0.0446 -0.0411 258 SER C CA  
10234 C C   A SER C 258 ? 0.4867 0.4024 0.3112 0.0335  -0.0450 -0.0393 258 SER C C   
10235 C C   B SER C 258 ? 0.4830 0.3995 0.3081 0.0336  -0.0449 -0.0392 258 SER C C   
10236 O O   A SER C 258 ? 0.4883 0.4108 0.3331 0.0436  -0.0509 -0.0366 258 SER C O   
10237 O O   B SER C 258 ? 0.4939 0.4175 0.3396 0.0437  -0.0507 -0.0364 258 SER C O   
10238 C CB  A SER C 258 ? 0.5546 0.4396 0.3550 0.0238  -0.0521 -0.0452 258 SER C CB  
10239 C CB  B SER C 258 ? 0.5537 0.4391 0.3551 0.0244  -0.0524 -0.0450 258 SER C CB  
10240 O OG  A SER C 258 ? 0.6022 0.4851 0.4162 0.0361  -0.0626 -0.0438 258 SER C OG  
10241 O OG  B SER C 258 ? 0.5836 0.4384 0.3479 0.0219  -0.0500 -0.0489 258 SER C OG  
10242 N N   . VAL C 259 ? 0.4481 0.3582 0.2532 0.0307  -0.0384 -0.0421 259 VAL C N   
10243 C CA  . VAL C 259 ? 0.5050 0.4144 0.3084 0.0406  -0.0375 -0.0419 259 VAL C CA  
10244 C C   . VAL C 259 ? 0.5356 0.4122 0.3007 0.0372  -0.0357 -0.0489 259 VAL C C   
10245 O O   . VAL C 259 ? 0.6599 0.5214 0.4035 0.0245  -0.0321 -0.0532 259 VAL C O   
10246 C CB  . VAL C 259 ? 0.4682 0.4090 0.2903 0.0422  -0.0297 -0.0377 259 VAL C CB  
10247 C CG1 . VAL C 259 ? 0.4844 0.4527 0.3436 0.0466  -0.0303 -0.0293 259 VAL C CG1 
10248 C CG2 . VAL C 259 ? 0.4690 0.4167 0.2789 0.0304  -0.0234 -0.0411 259 VAL C CG2 
10249 N N   . SER C 260 ? 0.5494 0.4141 0.3068 0.0489  -0.0378 -0.0503 260 SER C N   
10250 C CA  . SER C 260 ? 0.5618 0.3966 0.2851 0.0478  -0.0349 -0.0568 260 SER C CA  
10251 C C   . SER C 260 ? 0.5408 0.3856 0.2732 0.0626  -0.0342 -0.0571 260 SER C C   
10252 O O   . SER C 260 ? 0.4965 0.3698 0.2607 0.0721  -0.0355 -0.0521 260 SER C O   
10253 C CB  . SER C 260 ? 0.5147 0.3049 0.2053 0.0484  -0.0409 -0.0593 260 SER C CB  
10254 O OG  . SER C 260 ? 0.5275 0.3140 0.2277 0.0654  -0.0515 -0.0570 260 SER C OG  
10255 N N   . ASN C 261 ? 0.5395 0.3603 0.2442 0.0639  -0.0312 -0.0637 261 ASN C N   
10256 C CA  . ASN C 261 ? 0.6002 0.4281 0.3106 0.0796  -0.0302 -0.0656 261 ASN C CA  
10257 C C   . ASN C 261 ? 0.5915 0.4156 0.3146 0.0971  -0.0395 -0.0636 261 ASN C C   
10258 O O   . ASN C 261 ? 0.5299 0.3830 0.2821 0.1092  -0.0387 -0.0615 261 ASN C O   
10259 C CB  . ASN C 261 ? 0.6086 0.4048 0.2835 0.0785  -0.0265 -0.0746 261 ASN C CB  
10260 C CG  . ASN C 261 ? 0.6523 0.4596 0.3197 0.0629  -0.0179 -0.0792 261 ASN C CG  
10261 O OD1 . ASN C 261 ? 0.6175 0.4629 0.3083 0.0598  -0.0140 -0.0754 261 ASN C OD1 
10262 N ND2 . ASN C 261 ? 0.6935 0.4663 0.3277 0.0532  -0.0155 -0.0879 261 ASN C ND2 
10263 N N   . GLU C 262 ? 0.6006 0.3905 0.3027 0.0986  -0.0485 -0.0645 262 GLU C N   
10264 C CA  . GLU C 262 ? 0.6076 0.3945 0.3210 0.1167  -0.0600 -0.0642 262 GLU C CA  
10265 C C   . GLU C 262 ? 0.5329 0.3577 0.2888 0.1171  -0.0640 -0.0588 262 GLU C C   
10266 O O   . GLU C 262 ? 0.5832 0.4302 0.3687 0.1311  -0.0687 -0.0591 262 GLU C O   
10267 C CB  . GLU C 262 ? 0.7495 0.4868 0.4239 0.1197  -0.0694 -0.0661 262 GLU C CB  
10268 C CG  . GLU C 262 ? 0.8545 0.5498 0.4885 0.1238  -0.0668 -0.0716 262 GLU C CG  
10269 C CD  . GLU C 262 ? 0.9468 0.5890 0.5394 0.1292  -0.0759 -0.0717 262 GLU C CD  
10270 O OE1 . GLU C 262 ? 0.9447 0.5871 0.5452 0.1422  -0.0889 -0.0697 262 GLU C OE1 
10271 O OE2 . GLU C 262 ? 0.9931 0.5926 0.5447 0.1202  -0.0701 -0.0740 262 GLU C OE2 
10272 N N   . ALA C 263 ? 0.5466 0.3800 0.3079 0.1015  -0.0615 -0.0548 263 ALA C N   
10273 C CA  . ALA C 263 ? 0.5272 0.3939 0.3285 0.1006  -0.0647 -0.0501 263 ALA C CA  
10274 C C   . ALA C 263 ? 0.4934 0.4011 0.3314 0.1035  -0.0558 -0.0463 263 ALA C C   
10275 O O   . ALA C 263 ? 0.4767 0.4095 0.3507 0.1107  -0.0591 -0.0445 263 ALA C O   
10276 C CB  . ALA C 263 ? 0.4886 0.3546 0.2857 0.0841  -0.0627 -0.0474 263 ALA C CB  
10277 N N   . LEU C 264 ? 0.4942 0.4090 0.3230 0.0979  -0.0443 -0.0455 264 LEU C N   
10278 C CA  . LEU C 264 ? 0.4637 0.4139 0.3206 0.1019  -0.0346 -0.0412 264 LEU C CA  
10279 C C   . LEU C 264 ? 0.5278 0.4853 0.3983 0.1190  -0.0358 -0.0446 264 LEU C C   
10280 O O   . LEU C 264 ? 0.5479 0.5372 0.4552 0.1238  -0.0318 -0.0407 264 LEU C O   
10281 C CB  . LEU C 264 ? 0.4790 0.4321 0.3168 0.0947  -0.0239 -0.0414 264 LEU C CB  
10282 C CG  . LEU C 264 ? 0.5000 0.4556 0.3321 0.0790  -0.0220 -0.0385 264 LEU C CG  
10283 C CD1 . LEU C 264 ? 0.4773 0.4277 0.2829 0.0724  -0.0155 -0.0433 264 LEU C CD1 
10284 C CD2 . LEU C 264 ? 0.4839 0.4717 0.3503 0.0761  -0.0184 -0.0287 264 LEU C CD2 
10285 N N   . GLU C 265 ? 0.5389 0.4667 0.3807 0.1284  -0.0409 -0.0523 265 GLU C N   
10286 C CA  . GLU C 265 ? 0.6261 0.5605 0.4811 0.1471  -0.0436 -0.0571 265 GLU C CA  
10287 C C   . GLU C 265 ? 0.5994 0.5502 0.4892 0.1543  -0.0542 -0.0568 265 GLU C C   
10288 O O   . GLU C 265 ? 0.6374 0.6188 0.5627 0.1645  -0.0518 -0.0578 265 GLU C O   
10289 C CB  . GLU C 265 ? 0.6906 0.5834 0.5051 0.1570  -0.0493 -0.0654 265 GLU C CB  
10290 C CG  . GLU C 265 ? 0.7427 0.6223 0.5276 0.1529  -0.0386 -0.0690 265 GLU C CG  
10291 C CD  . GLU C 265 ? 0.8041 0.6344 0.5456 0.1596  -0.0445 -0.0769 265 GLU C CD  
10292 O OE1 . GLU C 265 ? 0.8827 0.6835 0.6092 0.1636  -0.0563 -0.0774 265 GLU C OE1 
10293 O OE2 . GLU C 265 ? 0.8265 0.6451 0.5467 0.1612  -0.0374 -0.0827 265 GLU C OE2 
10294 N N   . LEU C 266 ? 0.5539 0.4862 0.4350 0.1485  -0.0657 -0.0563 266 LEU C N   
10295 C CA  . LEU C 266 ? 0.4916 0.4370 0.4029 0.1556  -0.0785 -0.0581 266 LEU C CA  
10296 C C   . LEU C 266 ? 0.4696 0.4589 0.4306 0.1484  -0.0711 -0.0527 266 LEU C C   
10297 O O   . LEU C 266 ? 0.4279 0.4450 0.4277 0.1576  -0.0736 -0.0557 266 LEU C O   
10298 C CB  . LEU C 266 ? 0.4968 0.4118 0.3834 0.1500  -0.0912 -0.0587 266 LEU C CB  
10299 C CG  . LEU C 266 ? 0.5226 0.4506 0.4382 0.1556  -0.1061 -0.0617 266 LEU C CG  
10300 C CD1 . LEU C 266 ? 0.5893 0.5282 0.5242 0.1767  -0.1163 -0.0694 266 LEU C CD1 
10301 C CD2 . LEU C 266 ? 0.5620 0.4539 0.4425 0.1522  -0.1181 -0.0629 266 LEU C CD2 
10302 N N   . TYR C 267 ? 0.4554 0.4510 0.4166 0.1319  -0.0620 -0.0450 267 TYR C N   
10303 C CA  . TYR C 267 ? 0.4827 0.5141 0.4860 0.1241  -0.0532 -0.0380 267 TYR C CA  
10304 C C   . TYR C 267 ? 0.4338 0.4948 0.4625 0.1317  -0.0406 -0.0366 267 TYR C C   
10305 O O   . TYR C 267 ? 0.3808 0.4713 0.4531 0.1331  -0.0384 -0.0358 267 TYR C O   
10306 C CB  . TYR C 267 ? 0.5125 0.5421 0.5036 0.1085  -0.0443 -0.0299 267 TYR C CB  
10307 C CG  . TYR C 267 ? 0.4812 0.4930 0.4620 0.0993  -0.0542 -0.0304 267 TYR C CG  
10308 C CD1 . TYR C 267 ? 0.4449 0.4663 0.4554 0.0979  -0.0629 -0.0313 267 TYR C CD1 
10309 C CD2 . TYR C 267 ? 0.4867 0.4733 0.4290 0.0914  -0.0539 -0.0311 267 TYR C CD2 
10310 C CE1 . TYR C 267 ? 0.4755 0.4804 0.4748 0.0904  -0.0715 -0.0328 267 TYR C CE1 
10311 C CE2 . TYR C 267 ? 0.5108 0.4829 0.4436 0.0833  -0.0610 -0.0320 267 TYR C CE2 
10312 C CZ  . TYR C 267 ? 0.4842 0.4647 0.4440 0.0835  -0.0699 -0.0328 267 TYR C CZ  
10313 O OH  . TYR C 267 ? 0.4304 0.3959 0.3785 0.0762  -0.0765 -0.0347 267 TYR C OH  
10314 N N   . TYR C 268 ? 0.4587 0.5123 0.4609 0.1362  -0.0315 -0.0373 268 TYR C N   
10315 C CA  . TYR C 268 ? 0.4230 0.5030 0.4442 0.1451  -0.0186 -0.0372 268 TYR C CA  
10316 C C   . TYR C 268 ? 0.3972 0.4911 0.4474 0.1603  -0.0264 -0.0458 268 TYR C C   
10317 O O   . TYR C 268 ? 0.3711 0.5002 0.4630 0.1625  -0.0176 -0.0445 268 TYR C O   
10318 C CB  . TYR C 268 ? 0.4648 0.5289 0.4473 0.1498  -0.0111 -0.0399 268 TYR C CB  
10319 C CG  . TYR C 268 ? 0.5039 0.5915 0.5016 0.1627  0.0006  -0.0426 268 TYR C CG  
10320 C CD1 . TYR C 268 ? 0.5339 0.6556 0.5592 0.1587  0.0173  -0.0342 268 TYR C CD1 
10321 C CD2 . TYR C 268 ? 0.5402 0.6150 0.5243 0.1794  -0.0042 -0.0534 268 TYR C CD2 
10322 C CE1 . TYR C 268 ? 0.5830 0.7277 0.6219 0.1700  0.0303  -0.0366 268 TYR C CE1 
10323 C CE2 . TYR C 268 ? 0.6210 0.7195 0.6204 0.1921  0.0074  -0.0570 268 TYR C CE2 
10324 C CZ  . TYR C 268 ? 0.6676 0.8025 0.6948 0.1869  0.0254  -0.0487 268 TYR C CZ  
10325 O OH  . TYR C 268 ? 0.7293 0.8896 0.7712 0.1990  0.0395  -0.0521 268 TYR C OH  
10326 N N   . GLU C 269 ? 0.4216 0.4882 0.4499 0.1714  -0.0423 -0.0548 269 GLU C N   
10327 C CA  . GLU C 269 ? 0.4748 0.5553 0.5291 0.1891  -0.0515 -0.0644 269 GLU C CA  
10328 C C   . GLU C 269 ? 0.4669 0.5771 0.5713 0.1851  -0.0580 -0.0649 269 GLU C C   
10329 O O   . GLU C 269 ? 0.4835 0.6252 0.6285 0.1954  -0.0583 -0.0713 269 GLU C O   
10330 C CB  . GLU C 269 ? 0.5749 0.6149 0.5909 0.2029  -0.0690 -0.0729 269 GLU C CB  
10331 C CG  . GLU C 269 ? 0.7314 0.7443 0.7048 0.2102  -0.0625 -0.0756 269 GLU C CG  
10332 C CD  . GLU C 269 ? 0.8188 0.8547 0.8113 0.2282  -0.0553 -0.0825 269 GLU C CD  
10333 O OE1 . GLU C 269 ? 0.8568 0.8665 0.8148 0.2392  -0.0544 -0.0880 269 GLU C OE1 
10334 O OE2 . GLU C 269 ? 0.8322 0.9121 0.8743 0.2313  -0.0498 -0.0832 269 GLU C OE2 
10335 N N   . LYS C 270 ? 0.4872 0.5899 0.5918 0.1700  -0.0627 -0.0594 270 LYS C N   
10336 C CA  . LYS C 270 ? 0.5330 0.6608 0.6840 0.1645  -0.0695 -0.0609 270 LYS C CA  
10337 C C   . LYS C 270 ? 0.4828 0.6440 0.6722 0.1504  -0.0504 -0.0516 270 LYS C C   
10338 O O   . LYS C 270 ? 0.4447 0.6220 0.6697 0.1409  -0.0536 -0.0510 270 LYS C O   
10339 C CB  . LYS C 270 ? 0.5379 0.6389 0.6697 0.1569  -0.0853 -0.0613 270 LYS C CB  
10340 C CG  . LYS C 270 ? 0.6330 0.6911 0.7141 0.1675  -0.1013 -0.0672 270 LYS C CG  
10341 C CD  . LYS C 270 ? 0.6946 0.7492 0.7708 0.1901  -0.1104 -0.0770 270 LYS C CD  
10342 C CE  . LYS C 270 ? 0.7309 0.8174 0.8559 0.2016  -0.1234 -0.0870 270 LYS C CE  
10343 N NZ  . LYS C 270 ? 0.7614 0.8480 0.9002 0.1936  -0.1378 -0.0892 270 LYS C NZ  
10344 N N   . GLY C 271 ? 0.4799 0.6495 0.6606 0.1492  -0.0309 -0.0444 271 GLY C N   
10345 C CA  . GLY C 271 ? 0.4152 0.6152 0.6289 0.1386  -0.0108 -0.0346 271 GLY C CA  
10346 C C   . GLY C 271 ? 0.3910 0.5805 0.5909 0.1220  -0.0026 -0.0215 271 GLY C C   
10347 O O   . GLY C 271 ? 0.4622 0.6727 0.6899 0.1124  0.0127  -0.0120 271 GLY C O   
10348 N N   . ILE C 272 ? 0.3590 0.5166 0.5173 0.1184  -0.0114 -0.0204 272 ILE C N   
10349 C CA  . ILE C 272 ? 0.4074 0.5569 0.5535 0.1045  -0.0048 -0.0092 272 ILE C CA  
10350 C C   . ILE C 272 ? 0.4442 0.5950 0.5644 0.1051  0.0117  -0.0014 272 ILE C C   
10351 O O   . ILE C 272 ? 0.5032 0.6384 0.5881 0.1122  0.0099  -0.0066 272 ILE C O   
10352 C CB  . ILE C 272 ? 0.3905 0.5094 0.5063 0.1000  -0.0203 -0.0127 272 ILE C CB  
10353 C CG1 . ILE C 272 ? 0.4251 0.5412 0.5619 0.1015  -0.0379 -0.0215 272 ILE C CG1 
10354 C CG2 . ILE C 272 ? 0.3591 0.4730 0.4658 0.0876  -0.0139 -0.0025 272 ILE C CG2 
10355 C CD1 . ILE C 272 ? 0.4160 0.5576 0.6037 0.0944  -0.0353 -0.0193 272 ILE C CD1 
10356 N N   . ASN C 273 ? 0.3899 0.5577 0.5259 0.0980  0.0276  0.0107  273 ASN C N   
10357 C CA  . ASN C 273 ? 0.4166 0.5887 0.5288 0.1003  0.0436  0.0183  273 ASN C CA  
10358 C C   . ASN C 273 ? 0.4390 0.5944 0.5179 0.0937  0.0429  0.0250  273 ASN C C   
10359 O O   . ASN C 273 ? 0.4711 0.6244 0.5199 0.0973  0.0502  0.0270  273 ASN C O   
10360 C CB  . ASN C 273 ? 0.4303 0.6291 0.5732 0.0980  0.0634  0.0290  273 ASN C CB  
10361 C CG  . ASN C 273 ? 0.4662 0.6879 0.6416 0.1058  0.0679  0.0214  273 ASN C CG  
10362 O OD1 . ASN C 273 ? 0.5516 0.7720 0.7122 0.1181  0.0649  0.0113  273 ASN C OD1 
10363 N ND2 . ASN C 273 ? 0.4701 0.7131 0.6919 0.0989  0.0749  0.0251  273 ASN C ND2 
10364 N N   . MET C 274 ? 0.4249 0.5700 0.5093 0.0847  0.0339  0.0272  274 MET C N   
10365 C CA  . MET C 274 ? 0.4662 0.5996 0.5242 0.0792  0.0332  0.0329  274 MET C CA  
10366 C C   . MET C 274 ? 0.3957 0.5120 0.4523 0.0729  0.0176  0.0270  274 MET C C   
10367 O O   . MET C 274 ? 0.3878 0.5054 0.4725 0.0698  0.0112  0.0250  274 MET C O   
10368 C CB  . MET C 274 ? 0.5098 0.6548 0.5791 0.0753  0.0470  0.0485  274 MET C CB  
10369 C CG  . MET C 274 ? 0.6344 0.7710 0.6745 0.0733  0.0465  0.0542  274 MET C CG  
10370 S SD  . MET C 274 ? 0.7101 0.8356 0.7641 0.0643  0.0368  0.0573  274 MET C SD  
10371 C CE  . MET C 274 ? 0.7148 0.8499 0.7922 0.0621  0.0530  0.0761  274 MET C CE  
10372 N N   . LEU C 275 ? 0.3819 0.4830 0.4058 0.0709  0.0118  0.0230  275 LEU C N   
10373 C CA  . LEU C 275 ? 0.3815 0.4681 0.4005 0.0640  0.0006  0.0192  275 LEU C CA  
10374 C C   . LEU C 275 ? 0.3866 0.4701 0.3798 0.0605  0.0024  0.0212  275 LEU C C   
10375 O O   . LEU C 275 ? 0.3301 0.4210 0.3067 0.0639  0.0101  0.0241  275 LEU C O   
10376 C CB  . LEU C 275 ? 0.4231 0.4910 0.4295 0.0652  -0.0120 0.0068  275 LEU C CB  
10377 C CG  . LEU C 275 ? 0.4355 0.4899 0.4082 0.0693  -0.0128 -0.0011 275 LEU C CG  
10378 C CD1 . LEU C 275 ? 0.4528 0.4944 0.3950 0.0620  -0.0141 -0.0044 275 LEU C CD1 
10379 C CD2 . LEU C 275 ? 0.4611 0.4997 0.4313 0.0749  -0.0234 -0.0101 275 LEU C CD2 
10380 N N   . ALA C 276 ? 0.3789 0.4528 0.3687 0.0543  -0.0053 0.0181  276 ALA C N   
10381 C CA  . ALA C 276 ? 0.3628 0.4361 0.3318 0.0508  -0.0055 0.0170  276 ALA C CA  
10382 C C   . ALA C 276 ? 0.3426 0.3986 0.2925 0.0449  -0.0141 0.0051  276 ALA C C   
10383 O O   . ALA C 276 ? 0.4003 0.4429 0.3540 0.0437  -0.0211 -0.0001 276 ALA C O   
10384 C CB  . ALA C 276 ? 0.2862 0.3675 0.2706 0.0493  -0.0038 0.0262  276 ALA C CB  
10385 N N   . THR C 277 ? 0.3887 0.4455 0.3171 0.0411  -0.0133 0.0004  277 THR C N   
10386 C CA  . THR C 277 ? 0.4505 0.4925 0.3610 0.0332  -0.0185 -0.0103 277 THR C CA  
10387 C C   . THR C 277 ? 0.4390 0.4942 0.3438 0.0289  -0.0170 -0.0123 277 THR C C   
10388 O O   . THR C 277 ? 0.4659 0.5381 0.3833 0.0334  -0.0147 -0.0042 277 THR C O   
10389 C CB  . THR C 277 ? 0.4818 0.5056 0.3677 0.0322  -0.0190 -0.0187 277 THR C CB  
10390 O OG1 . THR C 277 ? 0.4110 0.4184 0.2769 0.0227  -0.0215 -0.0281 277 THR C OG1 
10391 C CG2 . THR C 277 ? 0.5170 0.5504 0.3904 0.0354  -0.0131 -0.0190 277 THR C CG2 
10392 N N   . ASP C 278 ? 0.4219 0.4690 0.3077 0.0203  -0.0180 -0.0231 278 ASP C N   
10393 C CA  . ASP C 278 ? 0.4173 0.4787 0.3033 0.0152  -0.0180 -0.0279 278 ASP C CA  
10394 C C   . ASP C 278 ? 0.4582 0.5329 0.3303 0.0137  -0.0154 -0.0335 278 ASP C C   
10395 O O   . ASP C 278 ? 0.5417 0.6061 0.3964 0.0119  -0.0135 -0.0383 278 ASP C O   
10396 C CB  . ASP C 278 ? 0.4120 0.4592 0.2895 0.0048  -0.0194 -0.0376 278 ASP C CB  
10397 C CG  . ASP C 278 ? 0.4742 0.5399 0.3587 0.0004  -0.0190 -0.0430 278 ASP C CG  
10398 O OD1 . ASP C 278 ? 0.4745 0.5570 0.3777 0.0079  -0.0209 -0.0364 278 ASP C OD1 
10399 O OD2 . ASP C 278 ? 0.5288 0.5920 0.4001 -0.0104 -0.0164 -0.0542 278 ASP C OD2 
10400 N N   . GLU C 279 ? 0.3918 0.5234 0.4858 0.0294  -0.0832 -0.0685 279 GLU C N   
10401 C CA  . GLU C 279 ? 0.3897 0.5182 0.4892 0.0291  -0.0928 -0.0755 279 GLU C CA  
10402 C C   . GLU C 279 ? 0.4097 0.5402 0.5252 0.0218  -0.0900 -0.0783 279 GLU C C   
10403 O O   . GLU C 279 ? 0.4409 0.5635 0.5547 0.0202  -0.0953 -0.0829 279 GLU C O   
10404 C CB  . GLU C 279 ? 0.3922 0.5290 0.5010 0.0323  -0.1013 -0.0802 279 GLU C CB  
10405 C CG  . GLU C 279 ? 0.4515 0.5854 0.5621 0.0342  -0.1141 -0.0879 279 GLU C CG  
10406 C CD  . GLU C 279 ? 0.4724 0.6145 0.5892 0.0397  -0.1228 -0.0917 279 GLU C CD  
10407 O OE1 . GLU C 279 ? 0.4757 0.6237 0.5936 0.0423  -0.1183 -0.0881 279 GLU C OE1 
10408 O OE2 . GLU C 279 ? 0.5186 0.6611 0.6387 0.0418  -0.1344 -0.0986 279 GLU C OE2 
10409 N N   . VAL C 280 ? 0.3819 0.5212 0.5119 0.0173  -0.0812 -0.0760 280 VAL C N   
10410 C CA  . VAL C 280 ? 0.4077 0.5473 0.5530 0.0103  -0.0767 -0.0784 280 VAL C CA  
10411 C C   . VAL C 280 ? 0.3989 0.5243 0.5294 0.0093  -0.0716 -0.0756 280 VAL C C   
10412 O O   . VAL C 280 ? 0.4236 0.5424 0.5591 0.0047  -0.0725 -0.0799 280 VAL C O   
10413 C CB  . VAL C 280 ? 0.4733 0.6232 0.6343 0.0069  -0.0666 -0.0754 280 VAL C CB  
10414 C CG1 . VAL C 280 ? 0.4229 0.5704 0.5975 -0.0003 -0.0594 -0.0769 280 VAL C CG1 
10415 C CG2 . VAL C 280 ? 0.5074 0.6711 0.6846 0.0080  -0.0714 -0.0785 280 VAL C CG2 
10416 N N   . ILE C 281 ? 0.3486 0.4689 0.4606 0.0137  -0.0661 -0.0686 281 ILE C N   
10417 C CA  . ILE C 281 ? 0.3282 0.4349 0.4242 0.0147  -0.0615 -0.0652 281 ILE C CA  
10418 C C   . ILE C 281 ? 0.4147 0.5096 0.4993 0.0168  -0.0709 -0.0698 281 ILE C C   
10419 O O   . ILE C 281 ? 0.3702 0.4529 0.4495 0.0147  -0.0696 -0.0714 281 ILE C O   
10420 C CB  . ILE C 281 ? 0.3444 0.4515 0.4249 0.0197  -0.0546 -0.0568 281 ILE C CB  
10421 C CG1 . ILE C 281 ? 0.3889 0.5058 0.4790 0.0176  -0.0455 -0.0530 281 ILE C CG1 
10422 C CG2 . ILE C 281 ? 0.2754 0.3690 0.3379 0.0226  -0.0504 -0.0528 281 ILE C CG2 
10423 C CD1 . ILE C 281 ? 0.4355 0.5519 0.5117 0.0212  -0.0371 -0.0451 281 ILE C CD1 
10424 N N   . LEU C 282 ? 0.4225 0.5194 0.5021 0.0214  -0.0803 -0.0722 282 LEU C N   
10425 C CA  . LEU C 282 ? 0.4356 0.5208 0.5035 0.0243  -0.0902 -0.0771 282 LEU C CA  
10426 C C   . LEU C 282 ? 0.3983 0.4826 0.4807 0.0181  -0.0965 -0.0859 282 LEU C C   
10427 O O   . LEU C 282 ? 0.4176 0.4879 0.4907 0.0169  -0.0986 -0.0889 282 LEU C O   
10428 C CB  . LEU C 282 ? 0.4480 0.5357 0.5088 0.0309  -0.0986 -0.0782 282 LEU C CB  
10429 C CG  . LEU C 282 ? 0.4505 0.5249 0.4966 0.0355  -0.1093 -0.0833 282 LEU C CG  
10430 C CD1 . LEU C 282 ? 0.4728 0.5301 0.4960 0.0390  -0.1044 -0.0787 282 LEU C CD1 
10431 C CD2 . LEU C 282 ? 0.4606 0.5378 0.5007 0.0425  -0.1164 -0.0842 282 LEU C CD2 
10432 N N   . LYS C 283 ? 0.3683 0.4678 0.4745 0.0137  -0.0990 -0.0901 283 LYS C N   
10433 C CA  . LYS C 283 ? 0.4760 0.5780 0.6001 0.0069  -0.1054 -0.0992 283 LYS C CA  
10434 C C   . LYS C 283 ? 0.4749 0.5683 0.6035 -0.0008 -0.0960 -0.0991 283 LYS C C   
10435 O O   . LYS C 283 ? 0.4792 0.5669 0.6140 -0.0064 -0.1012 -0.1067 283 LYS C O   
10436 C CB  . LYS C 283 ? 0.4969 0.6190 0.6474 0.0043  -0.1085 -0.1027 283 LYS C CB  
10437 C CG  . LYS C 283 ? 0.5851 0.7147 0.7310 0.0125  -0.1170 -0.1027 283 LYS C CG  
10438 C CD  . LYS C 283 ? 0.6945 0.8175 0.8300 0.0171  -0.1318 -0.1096 283 LYS C CD  
10439 C CE  . LYS C 283 ? 0.7429 0.8755 0.8791 0.0250  -0.1408 -0.1111 283 LYS C CE  
10440 N NZ  . LYS C 283 ? 0.7340 0.8871 0.8987 0.0219  -0.1411 -0.1137 283 LYS C NZ  
10441 N N   . ASN C 284 ? 0.4621 0.5539 0.5868 -0.0010 -0.0823 -0.0909 284 ASN C N   
10442 C CA  . ASN C 284 ? 0.4880 0.5693 0.6135 -0.0067 -0.0717 -0.0896 284 ASN C CA  
10443 C C   . ASN C 284 ? 0.5073 0.5678 0.6075 -0.0035 -0.0705 -0.0877 284 ASN C C   
10444 O O   . ASN C 284 ? 0.5652 0.6131 0.6645 -0.0086 -0.0646 -0.0893 284 ASN C O   
10445 C CB  . ASN C 284 ? 0.4896 0.5760 0.6178 -0.0064 -0.0574 -0.0812 284 ASN C CB  
10446 C CG  . ASN C 284 ? 0.4799 0.5833 0.6336 -0.0107 -0.0551 -0.0828 284 ASN C CG  
10447 O OD1 . ASN C 284 ? 0.4856 0.5968 0.6595 -0.0160 -0.0619 -0.0906 284 ASN C OD1 
10448 N ND2 . ASN C 284 ? 0.4706 0.5802 0.6236 -0.0081 -0.0456 -0.0756 284 ASN C ND2 
10449 N N   . SER C 285 ? 0.4833 0.5392 0.5628 0.0050  -0.0750 -0.0841 285 SER C N   
10450 C CA  . SER C 285 ? 0.5165 0.5536 0.5705 0.0098  -0.0717 -0.0802 285 SER C CA  
10451 C C   . SER C 285 ? 0.5337 0.5573 0.5747 0.0117  -0.0833 -0.0870 285 SER C C   
10452 O O   . SER C 285 ? 0.4966 0.5012 0.5201 0.0129  -0.0803 -0.0863 285 SER C O   
10453 C CB  . SER C 285 ? 0.4750 0.5151 0.5136 0.0184  -0.0670 -0.0707 285 SER C CB  
10454 O OG  . SER C 285 ? 0.4251 0.4771 0.4732 0.0173  -0.0573 -0.0647 285 SER C OG  
10455 N N   . VAL C 286 ? 0.5294 0.5612 0.5766 0.0130  -0.0962 -0.0932 286 VAL C N   
10456 C CA  . VAL C 286 ? 0.6092 0.6282 0.6415 0.0165  -0.1084 -0.0996 286 VAL C CA  
10457 C C   . VAL C 286 ? 0.6175 0.6466 0.6700 0.0109  -0.1213 -0.1108 286 VAL C C   
10458 O O   . VAL C 286 ? 0.5945 0.6432 0.6707 0.0075  -0.1222 -0.1123 286 VAL C O   
10459 C CB  . VAL C 286 ? 0.6386 0.6550 0.6509 0.0274  -0.1124 -0.0950 286 VAL C CB  
10460 C CG1 . VAL C 286 ? 0.6197 0.6342 0.6195 0.0323  -0.0996 -0.0836 286 VAL C CG1 
10461 C CG2 . VAL C 286 ? 0.6843 0.7184 0.7104 0.0293  -0.1202 -0.0974 286 VAL C CG2 
10462 N N   . GLU C 287 ? 0.6695 0.6850 0.7120 0.0105  -0.1316 -0.1189 287 GLU C N   
10463 C CA  . GLU C 287 ? 0.7473 0.7728 0.8070 0.0065  -0.1464 -0.1305 287 GLU C CA  
10464 C C   . GLU C 287 ? 0.8028 0.8348 0.8548 0.0166  -0.1583 -0.1314 287 GLU C C   
10465 O O   . GLU C 287 ? 0.8620 0.9141 0.9345 0.0163  -0.1642 -0.1343 287 GLU C O   
10466 C CB  . GLU C 287 ? 0.7604 0.7681 0.8119 0.0015  -0.1534 -0.1398 287 GLU C CB  
10467 C CG  . GLU C 287 ? 0.7870 0.7762 0.8283 -0.0033 -0.1398 -0.1359 287 GLU C CG  
10468 C CD  . GLU C 287 ? 0.8390 0.8089 0.8715 -0.0089 -0.1466 -0.1458 287 GLU C CD  
10469 O OE1 . GLU C 287 ? 0.8437 0.8109 0.8910 -0.0202 -0.1405 -0.1499 287 GLU C OE1 
10470 O OE2 . GLU C 287 ? 0.8748 0.8309 0.8845 -0.0020 -0.1574 -0.1496 287 GLU C OE2 
10471 N N   . ARG C 288 ? 0.8373 0.8515 0.8589 0.0262  -0.1609 -0.1286 288 ARG C N   
10472 C CA  . ARG C 288 ? 0.8825 0.8975 0.8906 0.0373  -0.1699 -0.1282 288 ARG C CA  
10473 C C   . ARG C 288 ? 0.8517 0.8806 0.8653 0.0414  -0.1616 -0.1191 288 ARG C C   
10474 O O   . ARG C 288 ? 0.8862 0.9061 0.8790 0.0495  -0.1563 -0.1115 288 ARG C O   
10475 C CB  . ARG C 288 ? 0.9098 0.8990 0.8825 0.0461  -0.1710 -0.1260 288 ARG C CB  
10476 C CG  . ARG C 288 ? 0.9203 0.9041 0.8744 0.0580  -0.1815 -0.1274 288 ARG C CG  
10477 C CD  . ARG C 288 ? 0.8798 0.8373 0.8036 0.0640  -0.1879 -0.1310 288 ARG C CD  
10478 N NE  . ARG C 288 ? 0.8671 0.8225 0.7986 0.0573  -0.2005 -0.1435 288 ARG C NE  
10479 C CZ  . ARG C 288 ? 0.8351 0.7790 0.7665 0.0486  -0.1969 -0.1468 288 ARG C CZ  
10480 N NH1 . ARG C 288 ? 0.7494 0.6921 0.6890 0.0417  -0.2093 -0.1592 288 ARG C NH1 
10481 N NH2 . ARG C 288 ? 0.8519 0.7860 0.7755 0.0469  -0.1809 -0.1377 288 ARG C NH2 
10482 N N   . ALA C 289 ? 0.7893 0.8397 0.8309 0.0357  -0.1601 -0.1200 289 ALA C N   
10483 C CA  . ALA C 289 ? 0.7724 0.8341 0.8202 0.0367  -0.1488 -0.1110 289 ALA C CA  
10484 C C   . ALA C 289 ? 0.7428 0.8120 0.7873 0.0454  -0.1547 -0.1101 289 ALA C C   
10485 O O   . ALA C 289 ? 0.7979 0.8845 0.8627 0.0442  -0.1579 -0.1126 289 ALA C O   
10486 C CB  . ALA C 289 ? 0.7373 0.8152 0.8139 0.0267  -0.1418 -0.1113 289 ALA C CB  
10487 N N   . SER C 290 ? 0.6496 0.7044 0.6674 0.0547  -0.1546 -0.1058 290 SER C N   
10488 C CA  . SER C 290 ? 0.5609 0.6186 0.5713 0.0636  -0.1574 -0.1036 290 SER C CA  
10489 C C   . SER C 290 ? 0.4863 0.5450 0.4910 0.0646  -0.1440 -0.0936 290 SER C C   
10490 O O   . SER C 290 ? 0.4560 0.5016 0.4424 0.0669  -0.1369 -0.0880 290 SER C O   
10491 C CB  . SER C 290 ? 0.5497 0.5897 0.5337 0.0739  -0.1666 -0.1061 290 SER C CB  
10492 O OG  . SER C 290 ? 0.5035 0.5425 0.4764 0.0830  -0.1656 -0.1020 290 SER C OG  
10493 N N   . PRO C 291 ? 0.4636 0.5374 0.4830 0.0633  -0.1401 -0.0914 291 PRO C N   
10494 C CA  . PRO C 291 ? 0.4485 0.5239 0.4632 0.0634  -0.1281 -0.0830 291 PRO C CA  
10495 C C   . PRO C 291 ? 0.4814 0.5457 0.4742 0.0725  -0.1273 -0.0792 291 PRO C C   
10496 O O   . PRO C 291 ? 0.4648 0.5317 0.4553 0.0721  -0.1181 -0.0732 291 PRO C O   
10497 C CB  . PRO C 291 ? 0.4840 0.5778 0.5216 0.0589  -0.1258 -0.0834 291 PRO C CB  
10498 C CG  . PRO C 291 ? 0.4590 0.5587 0.5059 0.0621  -0.1381 -0.0909 291 PRO C CG  
10499 C CD  . PRO C 291 ? 0.4563 0.5466 0.4977 0.0618  -0.1470 -0.0969 291 PRO C CD  
10500 N N   . TYR C 292 ? 0.4693 0.5206 0.4452 0.0806  -0.1360 -0.0826 292 TYR C N   
10501 C CA  . TYR C 292 ? 0.4587 0.4980 0.4134 0.0899  -0.1342 -0.0790 292 TYR C CA  
10502 C C   . TYR C 292 ? 0.4281 0.4490 0.3595 0.0940  -0.1294 -0.0746 292 TYR C C   
10503 O O   . TYR C 292 ? 0.4122 0.4203 0.3240 0.1021  -0.1271 -0.0714 292 TYR C O   
10504 C CB  . TYR C 292 ? 0.4968 0.5334 0.4463 0.0985  -0.1463 -0.0849 292 TYR C CB  
10505 C CG  . TYR C 292 ? 0.5491 0.6055 0.5235 0.0949  -0.1504 -0.0888 292 TYR C CG  
10506 C CD1 . TYR C 292 ? 0.5699 0.6372 0.5558 0.0911  -0.1411 -0.0843 292 TYR C CD1 
10507 C CD2 . TYR C 292 ? 0.5398 0.6045 0.5272 0.0947  -0.1631 -0.0970 292 TYR C CD2 
10508 C CE1 . TYR C 292 ? 0.5817 0.6662 0.5897 0.0883  -0.1436 -0.0872 292 TYR C CE1 
10509 C CE2 . TYR C 292 ? 0.6004 0.6846 0.6126 0.0916  -0.1658 -0.1001 292 TYR C CE2 
10510 C CZ  . TYR C 292 ? 0.6257 0.7192 0.6475 0.0888  -0.1555 -0.0947 292 TYR C CZ  
10511 O OH  . TYR C 292 ? 0.6579 0.7696 0.7033 0.0863  -0.1568 -0.0971 292 TYR C OH  
10512 N N   . LEU C 293 ? 0.3989 0.4175 0.3316 0.0888  -0.1266 -0.0738 293 LEU C N   
10513 C CA  . LEU C 293 ? 0.4621 0.4639 0.3741 0.0926  -0.1213 -0.0693 293 LEU C CA  
10514 C C   . LEU C 293 ? 0.4675 0.4756 0.3833 0.0881  -0.1077 -0.0610 293 LEU C C   
10515 O O   . LEU C 293 ? 0.4359 0.4604 0.3711 0.0805  -0.1036 -0.0600 293 LEU C O   
10516 C CB  . LEU C 293 ? 0.4946 0.4881 0.4038 0.0904  -0.1268 -0.0739 293 LEU C CB  
10517 C CG  . LEU C 293 ? 0.5654 0.5457 0.4619 0.0963  -0.1404 -0.0819 293 LEU C CG  
10518 C CD1 . LEU C 293 ? 0.5439 0.5337 0.4493 0.0991  -0.1512 -0.0880 293 LEU C CD1 
10519 C CD2 . LEU C 293 ? 0.6045 0.5820 0.5068 0.0896  -0.1446 -0.0873 293 LEU C CD2 
10520 N N   . ARG C 294 ? 0.4431 0.4385 0.3404 0.0934  -0.1008 -0.0552 294 ARG C N   
10521 C CA  . ARG C 294 ? 0.4305 0.4315 0.3307 0.0898  -0.0891 -0.0478 294 ARG C CA  
10522 C C   . ARG C 294 ? 0.4378 0.4328 0.3354 0.0880  -0.0886 -0.0479 294 ARG C C   
10523 O O   . ARG C 294 ? 0.4661 0.4430 0.3456 0.0938  -0.0917 -0.0491 294 ARG C O   
10524 C CB  . ARG C 294 ? 0.4289 0.4210 0.3132 0.0958  -0.0807 -0.0411 294 ARG C CB  
10525 C CG  . ARG C 294 ? 0.4603 0.4602 0.3485 0.0927  -0.0694 -0.0335 294 ARG C CG  
10526 C CD  . ARG C 294 ? 0.5178 0.5161 0.3986 0.0959  -0.0603 -0.0274 294 ARG C CD  
10527 N NE  . ARG C 294 ? 0.5803 0.5571 0.4380 0.1053  -0.0588 -0.0252 294 ARG C NE  
10528 C CZ  . ARG C 294 ? 0.6209 0.5853 0.4650 0.1116  -0.0581 -0.0250 294 ARG C CZ  
10529 N NH1 . ARG C 294 ? 0.5772 0.5482 0.4285 0.1094  -0.0588 -0.0269 294 ARG C NH1 
10530 N NH2 . ARG C 294 ? 0.6552 0.5986 0.4769 0.1208  -0.0559 -0.0227 294 ARG C NH2 
10531 N N   . TYR C 295 ? 0.4210 0.4295 0.3352 0.0806  -0.0845 -0.0467 295 TYR C N   
10532 C CA  . TYR C 295 ? 0.4778 0.4799 0.3897 0.0786  -0.0826 -0.0465 295 TYR C CA  
10533 C C   . TYR C 295 ? 0.4961 0.4982 0.4012 0.0808  -0.0712 -0.0376 295 TYR C C   
10534 O O   . TYR C 295 ? 0.4496 0.4647 0.3615 0.0797  -0.0648 -0.0325 295 TYR C O   
10535 C CB  . TYR C 295 ? 0.4801 0.4945 0.4129 0.0699  -0.0842 -0.0504 295 TYR C CB  
10536 C CG  . TYR C 295 ? 0.4283 0.4418 0.3684 0.0677  -0.0958 -0.0598 295 TYR C CG  
10537 C CD1 . TYR C 295 ? 0.3941 0.4189 0.3457 0.0671  -0.1015 -0.0633 295 TYR C CD1 
10538 C CD2 . TYR C 295 ? 0.5008 0.5021 0.4365 0.0663  -0.1013 -0.0654 295 TYR C CD2 
10539 C CE1 . TYR C 295 ? 0.3968 0.4232 0.3569 0.0657  -0.1126 -0.0718 295 TYR C CE1 
10540 C CE2 . TYR C 295 ? 0.4962 0.4988 0.4407 0.0638  -0.1130 -0.0748 295 TYR C CE2 
10541 C CZ  . TYR C 295 ? 0.4880 0.5043 0.4453 0.0638  -0.1188 -0.0778 295 TYR C CZ  
10542 O OH  . TYR C 295 ? 0.4512 0.4713 0.4189 0.0620  -0.1307 -0.0869 295 TYR C OH  
10543 N N   . TYR C 296 ? 0.5235 0.5106 0.4147 0.0841  -0.0689 -0.0361 296 TYR C N   
10544 C CA  . TYR C 296 ? 0.4875 0.4740 0.3718 0.0873  -0.0581 -0.0276 296 TYR C CA  
10545 C C   . TYR C 296 ? 0.4762 0.4633 0.3666 0.0830  -0.0552 -0.0277 296 TYR C C   
10546 O O   . TYR C 296 ? 0.4783 0.4496 0.3603 0.0829  -0.0588 -0.0321 296 TYR C O   
10547 C CB  . TYR C 296 ? 0.5093 0.4754 0.3695 0.0965  -0.0558 -0.0243 296 TYR C CB  
10548 C CG  . TYR C 296 ? 0.5154 0.4773 0.3669 0.1018  -0.0573 -0.0237 296 TYR C CG  
10549 C CD1 . TYR C 296 ? 0.5380 0.5159 0.3999 0.1002  -0.0524 -0.0198 296 TYR C CD1 
10550 C CD2 . TYR C 296 ? 0.5996 0.5401 0.4311 0.1085  -0.0632 -0.0273 296 TYR C CD2 
10551 C CE1 . TYR C 296 ? 0.5369 0.5088 0.3901 0.1048  -0.0522 -0.0191 296 TYR C CE1 
10552 C CE2 . TYR C 296 ? 0.5443 0.4787 0.3657 0.1144  -0.0634 -0.0264 296 TYR C CE2 
10553 C CZ  . TYR C 296 ? 0.5475 0.4972 0.3800 0.1124  -0.0573 -0.0220 296 TYR C CZ  
10554 O OH  . TYR C 296 ? 0.5863 0.5283 0.4084 0.1179  -0.0560 -0.0209 296 TYR C OH  
10555 N N   . PHE C 297 ? 0.4540 0.4581 0.3580 0.0793  -0.0487 -0.0234 297 PHE C N   
10556 C CA  . PHE C 297 ? 0.4589 0.4625 0.3671 0.0762  -0.0441 -0.0226 297 PHE C CA  
10557 C C   . PHE C 297 ? 0.4576 0.4495 0.3488 0.0834  -0.0357 -0.0154 297 PHE C C   
10558 O O   . PHE C 297 ? 0.4385 0.4405 0.3290 0.0876  -0.0286 -0.0077 297 PHE C O   
10559 C CB  . PHE C 297 ? 0.4195 0.4440 0.3464 0.0709  -0.0403 -0.0206 297 PHE C CB  
10560 C CG  . PHE C 297 ? 0.4266 0.4490 0.3555 0.0691  -0.0339 -0.0187 297 PHE C CG  
10561 C CD1 . PHE C 297 ? 0.4705 0.4857 0.4060 0.0631  -0.0368 -0.0252 297 PHE C CD1 
10562 C CD2 . PHE C 297 ? 0.4331 0.4595 0.3565 0.0739  -0.0245 -0.0103 297 PHE C CD2 
10563 C CE1 . PHE C 297 ? 0.4789 0.4894 0.4149 0.0615  -0.0293 -0.0232 297 PHE C CE1 
10564 C CE2 . PHE C 297 ? 0.4216 0.4437 0.3443 0.0736  -0.0176 -0.0081 297 PHE C CE2 
10565 C CZ  . PHE C 297 ? 0.4267 0.4395 0.3550 0.0672  -0.0195 -0.0145 297 PHE C CZ  
10566 N N   . ARG C 298 ? 0.4946 0.4655 0.3724 0.0849  -0.0366 -0.0182 298 ARG C N   
10567 C CA  . ARG C 298 ? 0.5368 0.4924 0.3957 0.0924  -0.0284 -0.0119 298 ARG C CA  
10568 C C   . ARG C 298 ? 0.5826 0.5367 0.4292 0.1010  -0.0250 -0.0055 298 ARG C C   
10569 O O   . ARG C 298 ? 0.5402 0.4937 0.3785 0.1078  -0.0157 0.0029  298 ARG C O   
10570 C CB  . ARG C 298 ? 0.5600 0.5235 0.4241 0.0923  -0.0186 -0.0057 298 ARG C CB  
10571 C CG  . ARG C 298 ? 0.5421 0.5051 0.4180 0.0838  -0.0200 -0.0116 298 ARG C CG  
10572 C CD  . ARG C 298 ? 0.5521 0.5171 0.4282 0.0852  -0.0092 -0.0054 298 ARG C CD  
10573 N NE  . ARG C 298 ? 0.5019 0.4641 0.3889 0.0768  -0.0094 -0.0112 298 ARG C NE  
10574 C CZ  . ARG C 298 ? 0.5351 0.5027 0.4280 0.0758  -0.0011 -0.0075 298 ARG C CZ  
10575 N NH1 . ARG C 298 ? 0.5245 0.5021 0.4133 0.0832  0.0070  0.0019  298 ARG C NH1 
10576 N NH2 . ARG C 298 ? 0.4957 0.4591 0.3989 0.0677  -0.0007 -0.0131 298 ARG C NH2 
10577 N N   . GLU C 299 ? 0.5663 0.5201 0.4121 0.1013  -0.0321 -0.0093 299 GLU C N   
10578 C CA  . GLU C 299 ? 0.5617 0.5133 0.3971 0.1087  -0.0288 -0.0040 299 GLU C CA  
10579 C C   . GLU C 299 ? 0.6136 0.5865 0.4597 0.1100  -0.0198 0.0046  299 GLU C C   
10580 O O   . GLU C 299 ? 0.6572 0.6286 0.4949 0.1167  -0.0135 0.0110  299 GLU C O   
10581 C CB  . GLU C 299 ? 0.5879 0.5132 0.3973 0.1176  -0.0257 -0.0017 299 GLU C CB  
10582 C CG  . GLU C 299 ? 0.6538 0.5572 0.4493 0.1178  -0.0360 -0.0107 299 GLU C CG  
10583 C CD  . GLU C 299 ? 0.7601 0.6621 0.5520 0.1204  -0.0422 -0.0135 299 GLU C CD  
10584 O OE1 . GLU C 299 ? 0.8601 0.7416 0.6348 0.1241  -0.0496 -0.0192 299 GLU C OE1 
10585 O OE2 . GLU C 299 ? 0.7615 0.6818 0.5665 0.1190  -0.0396 -0.0103 299 GLU C OE2 
10586 N N   . LEU C 300 ? 0.5719 0.5651 0.4368 0.1035  -0.0194 0.0045  300 LEU C N   
10587 C CA  . LEU C 300 ? 0.5858 0.6009 0.4618 0.1041  -0.0122 0.0117  300 LEU C CA  
10588 C C   . LEU C 300 ? 0.4971 0.5333 0.3912 0.0974  -0.0156 0.0093  300 LEU C C   
10589 O O   . LEU C 300 ? 0.5422 0.5935 0.4424 0.0984  -0.0111 0.0143  300 LEU C O   
10590 C CB  . LEU C 300 ? 0.6183 0.6385 0.4977 0.1041  -0.0071 0.0150  300 LEU C CB  
10591 C CG  . LEU C 300 ? 0.6478 0.6514 0.5092 0.1127  0.0003  0.0207  300 LEU C CG  
10592 C CD1 . LEU C 300 ? 0.7258 0.7355 0.5908 0.1131  0.0060  0.0243  300 LEU C CD1 
10593 C CD2 . LEU C 300 ? 0.6727 0.6791 0.5269 0.1211  0.0069  0.0286  300 LEU C CD2 
10594 N N   . ILE C 301 ? 0.4704 0.5080 0.3735 0.0905  -0.0232 0.0019  301 ILE C N   
10595 C CA  . ILE C 301 ? 0.4282 0.4832 0.3465 0.0844  -0.0261 -0.0006 301 ILE C CA  
10596 C C   . ILE C 301 ? 0.4673 0.5137 0.3861 0.0813  -0.0349 -0.0085 301 ILE C C   
10597 O O   . ILE C 301 ? 0.4698 0.5058 0.3871 0.0798  -0.0401 -0.0137 301 ILE C O   
10598 C CB  . ILE C 301 ? 0.3664 0.4394 0.2999 0.0792  -0.0244 0.0000  301 ILE C CB  
10599 C CG1 . ILE C 301 ? 0.3303 0.4201 0.2777 0.0732  -0.0268 -0.0024 301 ILE C CG1 
10600 C CG2 . ILE C 301 ? 0.3513 0.4164 0.2870 0.0759  -0.0274 -0.0046 301 ILE C CG2 
10601 C CD1 . ILE C 301 ? 0.3306 0.4387 0.2902 0.0694  -0.0241 -0.0007 301 ILE C CD1 
10602 N N   . SER C 302 ? 0.4307 0.4818 0.3521 0.0804  -0.0365 -0.0096 302 SER C N   
10603 C CA  . SER C 302 ? 0.4708 0.5155 0.3927 0.0787  -0.0447 -0.0166 302 SER C CA  
10604 C C   . SER C 302 ? 0.4354 0.4939 0.3750 0.0712  -0.0483 -0.0209 302 SER C C   
10605 O O   . SER C 302 ? 0.3991 0.4738 0.3499 0.0672  -0.0441 -0.0183 302 SER C O   
10606 C CB  . SER C 302 ? 0.4872 0.5296 0.4037 0.0812  -0.0437 -0.0157 302 SER C CB  
10607 O OG  . SER C 302 ? 0.4885 0.5161 0.3878 0.0888  -0.0398 -0.0117 302 SER C OG  
10608 N N   . VAL C 303 ? 0.4088 0.4611 0.3509 0.0696  -0.0561 -0.0276 303 VAL C N   
10609 C CA  . VAL C 303 ? 0.3793 0.4432 0.3385 0.0631  -0.0592 -0.0319 303 VAL C CA  
10610 C C   . VAL C 303 ? 0.3581 0.4186 0.3193 0.0633  -0.0677 -0.0383 303 VAL C C   
10611 O O   . VAL C 303 ? 0.3236 0.3708 0.2756 0.0669  -0.0742 -0.0423 303 VAL C O   
10612 C CB  . VAL C 303 ? 0.3746 0.4364 0.3390 0.0600  -0.0590 -0.0335 303 VAL C CB  
10613 C CG1 . VAL C 303 ? 0.3901 0.4631 0.3731 0.0534  -0.0617 -0.0382 303 VAL C CG1 
10614 C CG2 . VAL C 303 ? 0.3460 0.4116 0.3078 0.0610  -0.0499 -0.0266 303 VAL C CG2 
10615 N N   . PHE C 304 ? 0.3298 0.4019 0.3018 0.0601  -0.0679 -0.0394 304 PHE C N   
10616 C CA  . PHE C 304 ? 0.2973 0.3693 0.2742 0.0604  -0.0755 -0.0454 304 PHE C CA  
10617 C C   . PHE C 304 ? 0.3852 0.4694 0.3815 0.0540  -0.0767 -0.0487 304 PHE C C   
10618 O O   . PHE C 304 ? 0.3049 0.3992 0.3098 0.0496  -0.0704 -0.0456 304 PHE C O   
10619 C CB  . PHE C 304 ? 0.3103 0.3837 0.2834 0.0623  -0.0737 -0.0441 304 PHE C CB  
10620 C CG  . PHE C 304 ? 0.3269 0.3852 0.2808 0.0696  -0.0736 -0.0423 304 PHE C CG  
10621 C CD1 . PHE C 304 ? 0.3532 0.3988 0.2969 0.0757  -0.0815 -0.0466 304 PHE C CD1 
10622 C CD2 . PHE C 304 ? 0.4144 0.4718 0.3607 0.0706  -0.0653 -0.0364 304 PHE C CD2 
10623 C CE1 . PHE C 304 ? 0.3539 0.3836 0.2778 0.0834  -0.0806 -0.0446 304 PHE C CE1 
10624 C CE2 . PHE C 304 ? 0.4203 0.4627 0.3489 0.0775  -0.0637 -0.0343 304 PHE C CE2 
10625 C CZ  . PHE C 304 ? 0.3719 0.3995 0.2883 0.0842  -0.0711 -0.0382 304 PHE C CZ  
10626 N N   . PHE C 305 ? 0.4238 0.5072 0.4268 0.0541  -0.0849 -0.0550 305 PHE C N   
10627 C CA  . PHE C 305 ? 0.3744 0.4696 0.3974 0.0484  -0.0860 -0.0585 305 PHE C CA  
10628 C C   . PHE C 305 ? 0.3560 0.4574 0.3850 0.0501  -0.0898 -0.0611 305 PHE C C   
10629 O O   . PHE C 305 ? 0.3877 0.4825 0.4098 0.0556  -0.0974 -0.0646 305 PHE C O   
10630 C CB  . PHE C 305 ? 0.3976 0.4891 0.4272 0.0462  -0.0919 -0.0640 305 PHE C CB  
10631 C CG  . PHE C 305 ? 0.4671 0.5500 0.4890 0.0449  -0.0873 -0.0613 305 PHE C CG  
10632 C CD1 . PHE C 305 ? 0.4649 0.5325 0.4675 0.0501  -0.0894 -0.0606 305 PHE C CD1 
10633 C CD2 . PHE C 305 ? 0.4529 0.5414 0.4852 0.0394  -0.0799 -0.0592 305 PHE C CD2 
10634 C CE1 . PHE C 305 ? 0.4452 0.5038 0.4396 0.0498  -0.0844 -0.0578 305 PHE C CE1 
10635 C CE2 . PHE C 305 ? 0.4266 0.5059 0.4503 0.0392  -0.0749 -0.0563 305 PHE C CE2 
10636 C CZ  . PHE C 305 ? 0.4481 0.5125 0.4529 0.0444  -0.0772 -0.0556 305 PHE C CZ  
10637 N N   . ARG C 306 ? 0.2921 0.4047 0.3320 0.0464  -0.0843 -0.0592 306 ARG C N   
10638 C CA  . ARG C 306 ? 0.2947 0.4123 0.3389 0.0482  -0.0859 -0.0608 306 ARG C CA  
10639 C C   . ARG C 306 ? 0.4000 0.5219 0.4571 0.0492  -0.0944 -0.0671 306 ARG C C   
10640 O O   . ARG C 306 ? 0.3521 0.4772 0.4208 0.0456  -0.0972 -0.0703 306 ARG C O   
10641 C CB  . ARG C 306 ? 0.3620 0.4896 0.4148 0.0435  -0.0777 -0.0578 306 ARG C CB  
10642 C CG  . ARG C 306 ? 0.3765 0.5141 0.4485 0.0386  -0.0765 -0.0597 306 ARG C CG  
10643 C CD  . ARG C 306 ? 0.3660 0.5119 0.4446 0.0354  -0.0689 -0.0572 306 ARG C CD  
10644 N NE  . ARG C 306 ? 0.3026 0.4565 0.3993 0.0315  -0.0669 -0.0588 306 ARG C NE  
10645 C CZ  . ARG C 306 ? 0.3159 0.4770 0.4228 0.0300  -0.0628 -0.0587 306 ARG C CZ  
10646 N NH1 . ARG C 306 ? 0.3125 0.4735 0.4126 0.0319  -0.0606 -0.0574 306 ARG C NH1 
10647 N NH2 . ARG C 306 ? 0.3606 0.5281 0.4844 0.0267  -0.0601 -0.0600 306 ARG C NH2 
10648 N N   . ASP C 307 ? 0.4075 0.5296 0.4628 0.0543  -0.0982 -0.0688 307 ASP C N   
10649 C CA  . ASP C 307 ? 0.3998 0.5298 0.4697 0.0562  -0.1059 -0.0743 307 ASP C CA  
10650 C C   . ASP C 307 ? 0.3570 0.5004 0.4458 0.0510  -0.0998 -0.0735 307 ASP C C   
10651 O O   . ASP C 307 ? 0.3179 0.4631 0.4048 0.0523  -0.0948 -0.0710 307 ASP C O   
10652 C CB  . ASP C 307 ? 0.3981 0.5222 0.4565 0.0653  -0.1117 -0.0758 307 ASP C CB  
10653 C CG  . ASP C 307 ? 0.4435 0.5758 0.5152 0.0690  -0.1222 -0.0820 307 ASP C CG  
10654 O OD1 . ASP C 307 ? 0.4440 0.5907 0.5377 0.0648  -0.1213 -0.0838 307 ASP C OD1 
10655 O OD2 . ASP C 307 ? 0.4741 0.5988 0.5344 0.0764  -0.1314 -0.0853 307 ASP C OD2 
10656 N N   . LYS C 308 ? 0.3849 0.5363 0.4915 0.0450  -0.0995 -0.0757 308 LYS C N   
10657 C CA  . LYS C 308 ? 0.3265 0.4892 0.4506 0.0401  -0.0922 -0.0744 308 LYS C CA  
10658 C C   . LYS C 308 ? 0.3378 0.5092 0.4729 0.0441  -0.0949 -0.0767 308 LYS C C   
10659 O O   . LYS C 308 ? 0.2790 0.4551 0.4187 0.0433  -0.0875 -0.0738 308 LYS C O   
10660 C CB  . LYS C 308 ? 0.2914 0.4591 0.4321 0.0333  -0.0911 -0.0767 308 LYS C CB  
10661 C CG  . LYS C 308 ? 0.3363 0.5136 0.4941 0.0285  -0.0820 -0.0749 308 LYS C CG  
10662 C CD  . LYS C 308 ? 0.4031 0.5861 0.5812 0.0224  -0.0820 -0.0786 308 LYS C CD  
10663 C CE  . LYS C 308 ? 0.4227 0.6170 0.6214 0.0195  -0.0745 -0.0779 308 LYS C CE  
10664 N NZ  . LYS C 308 ? 0.4076 0.5995 0.5965 0.0199  -0.0637 -0.0714 308 LYS C NZ  
10665 N N   . THR C 309 ? 0.3308 0.5043 0.4696 0.0491  -0.1057 -0.0817 309 THR C N   
10666 C CA  . THR C 309 ? 0.3374 0.5208 0.4880 0.0539  -0.1085 -0.0837 309 THR C CA  
10667 C C   . THR C 309 ? 0.3251 0.5010 0.4584 0.0603  -0.1043 -0.0797 309 THR C C   
10668 O O   . THR C 309 ? 0.3053 0.4868 0.4456 0.0612  -0.0986 -0.0779 309 THR C O   
10669 C CB  . THR C 309 ? 0.4044 0.5926 0.5622 0.0587  -0.1222 -0.0904 309 THR C CB  
10670 O OG1 . THR C 309 ? 0.4206 0.6168 0.5977 0.0511  -0.1251 -0.0948 309 THR C OG1 
10671 C CG2 . THR C 309 ? 0.4025 0.6017 0.5715 0.0655  -0.1255 -0.0920 309 THR C CG2 
10672 N N   . LEU C 310 ? 0.3277 0.4895 0.4376 0.0646  -0.1061 -0.0782 310 LEU C N   
10673 C CA  . LEU C 310 ? 0.3524 0.5051 0.4453 0.0698  -0.1012 -0.0747 310 LEU C CA  
10674 C C   . LEU C 310 ? 0.3317 0.4837 0.4225 0.0633  -0.0892 -0.0700 310 LEU C C   
10675 O O   . LEU C 310 ? 0.3174 0.4675 0.4039 0.0652  -0.0835 -0.0680 310 LEU C O   
10676 C CB  . LEU C 310 ? 0.3557 0.4927 0.4246 0.0753  -0.1045 -0.0740 310 LEU C CB  
10677 C CG  . LEU C 310 ? 0.3573 0.4923 0.4233 0.0836  -0.1170 -0.0788 310 LEU C CG  
10678 C CD1 . LEU C 310 ? 0.3418 0.4590 0.3822 0.0885  -0.1179 -0.0771 310 LEU C CD1 
10679 C CD2 . LEU C 310 ? 0.3642 0.5044 0.4348 0.0920  -0.1206 -0.0805 310 LEU C CD2 
10680 N N   . SER C 311 ? 0.3770 0.5298 0.4695 0.0560  -0.0854 -0.0683 311 SER C N   
10681 C CA  . SER C 311 ? 0.3764 0.5295 0.4664 0.0503  -0.0752 -0.0643 311 SER C CA  
10682 C C   . SER C 311 ? 0.3477 0.5110 0.4543 0.0479  -0.0702 -0.0642 311 SER C C   
10683 O O   . SER C 311 ? 0.3524 0.5138 0.4538 0.0473  -0.0632 -0.0619 311 SER C O   
10684 C CB  . SER C 311 ? 0.3842 0.5365 0.4720 0.0447  -0.0730 -0.0624 311 SER C CB  
10685 O OG  . SER C 311 ? 0.4069 0.5488 0.4774 0.0472  -0.0753 -0.0612 311 SER C OG  
10686 N N   . ASP C 312 ? 0.3597 0.5330 0.4861 0.0464  -0.0733 -0.0670 312 ASP C N   
10687 C CA  . ASP C 312 ? 0.3582 0.5412 0.5019 0.0444  -0.0675 -0.0667 312 ASP C CA  
10688 C C   . ASP C 312 ? 0.3785 0.5632 0.5235 0.0510  -0.0679 -0.0672 312 ASP C C   
10689 O O   . ASP C 312 ? 0.3643 0.5514 0.5136 0.0506  -0.0602 -0.0652 312 ASP C O   
10690 C CB  . ASP C 312 ? 0.3298 0.5233 0.4961 0.0409  -0.0705 -0.0699 312 ASP C CB  
10691 C CG  . ASP C 312 ? 0.3196 0.5106 0.4857 0.0342  -0.0666 -0.0685 312 ASP C CG  
10692 O OD1 . ASP C 312 ? 0.3340 0.5176 0.4841 0.0326  -0.0612 -0.0645 312 ASP C OD1 
10693 O OD2 . ASP C 312 ? 0.3345 0.5310 0.5165 0.0306  -0.0688 -0.0714 312 ASP C OD2 
10694 N N   . LEU C 313 ? 0.3974 0.5801 0.5379 0.0580  -0.0767 -0.0699 313 LEU C N   
10695 C CA  . LEU C 313 ? 0.3806 0.5634 0.5196 0.0660  -0.0769 -0.0700 313 LEU C CA  
10696 C C   . LEU C 313 ? 0.3833 0.5546 0.5040 0.0661  -0.0675 -0.0660 313 LEU C C   
10697 O O   . LEU C 313 ? 0.3779 0.5509 0.5022 0.0680  -0.0613 -0.0646 313 LEU C O   
10698 C CB  . LEU C 313 ? 0.3793 0.5585 0.5104 0.0746  -0.0877 -0.0730 313 LEU C CB  
10699 C CG  . LEU C 313 ? 0.3611 0.5542 0.5126 0.0769  -0.0986 -0.0782 313 LEU C CG  
10700 C CD1 . LEU C 313 ? 0.3418 0.5282 0.4799 0.0850  -0.1100 -0.0812 313 LEU C CD1 
10701 C CD2 . LEU C 313 ? 0.3695 0.5772 0.5420 0.0806  -0.0975 -0.0790 313 LEU C CD2 
10702 N N   . ILE C 314 ? 0.3371 0.4965 0.4382 0.0638  -0.0661 -0.0644 314 ILE C N   
10703 C CA  . ILE C 314 ? 0.3497 0.4986 0.4344 0.0623  -0.0575 -0.0615 314 ILE C CA  
10704 C C   . ILE C 314 ? 0.3754 0.5295 0.4675 0.0552  -0.0492 -0.0596 314 ILE C C   
10705 O O   . ILE C 314 ? 0.3721 0.5226 0.4600 0.0556  -0.0422 -0.0583 314 ILE C O   
10706 C CB  . ILE C 314 ? 0.3100 0.4471 0.3752 0.0605  -0.0576 -0.0604 314 ILE C CB  
10707 C CG1 . ILE C 314 ? 0.3596 0.4871 0.4124 0.0692  -0.0633 -0.0615 314 ILE C CG1 
10708 C CG2 . ILE C 314 ? 0.3304 0.4594 0.3824 0.0558  -0.0484 -0.0581 314 ILE C CG2 
10709 C CD1 . ILE C 314 ? 0.3301 0.4450 0.3639 0.0678  -0.0618 -0.0600 314 ILE C CD1 
10710 N N   . GLY C 315 ? 0.3654 0.5268 0.4675 0.0494  -0.0497 -0.0595 315 GLY C N   
10711 C CA  . GLY C 315 ? 0.3808 0.5452 0.4862 0.0436  -0.0416 -0.0573 315 GLY C CA  
10712 C C   . GLY C 315 ? 0.3767 0.5490 0.4989 0.0445  -0.0371 -0.0572 315 GLY C C   
10713 O O   . GLY C 315 ? 0.4063 0.5769 0.5258 0.0423  -0.0289 -0.0551 315 GLY C O   
10714 N N   . PHE C 316 ? 0.3453 0.5268 0.4855 0.0479  -0.0423 -0.0595 316 PHE C N   
10715 C CA  . PHE C 316 ? 0.3170 0.5086 0.4778 0.0479  -0.0376 -0.0594 316 PHE C CA  
10716 C C   . PHE C 316 ? 0.3680 0.5642 0.5372 0.0554  -0.0386 -0.0603 316 PHE C C   
10717 O O   . PHE C 316 ? 0.3901 0.5912 0.5705 0.0563  -0.0313 -0.0588 316 PHE C O   
10718 C CB  . PHE C 316 ? 0.3494 0.5514 0.5304 0.0439  -0.0414 -0.0616 316 PHE C CB  
10719 C CG  . PHE C 316 ? 0.4041 0.6024 0.5796 0.0372  -0.0379 -0.0598 316 PHE C CG  
10720 C CD1 . PHE C 316 ? 0.4466 0.6380 0.6083 0.0347  -0.0294 -0.0562 316 PHE C CD1 
10721 C CD2 . PHE C 316 ? 0.4288 0.6300 0.6122 0.0337  -0.0431 -0.0620 316 PHE C CD2 
10722 C CE1 . PHE C 316 ? 0.4452 0.6339 0.6013 0.0299  -0.0264 -0.0542 316 PHE C CE1 
10723 C CE2 . PHE C 316 ? 0.4613 0.6582 0.6385 0.0286  -0.0390 -0.0598 316 PHE C CE2 
10724 C CZ  . PHE C 316 ? 0.4408 0.6321 0.6045 0.0272  -0.0308 -0.0557 316 PHE C CZ  
10725 N N   . SER C 317 ? 0.3470 0.5413 0.5103 0.0618  -0.0469 -0.0624 317 SER C N   
10726 C CA  . SER C 317 ? 0.4083 0.6108 0.5842 0.0699  -0.0496 -0.0637 317 SER C CA  
10727 C C   . SER C 317 ? 0.3586 0.5499 0.5158 0.0784  -0.0483 -0.0624 317 SER C C   
10728 O O   . SER C 317 ? 0.3359 0.5303 0.4992 0.0843  -0.0438 -0.0611 317 SER C O   
10729 C CB  . SER C 317 ? 0.5486 0.7627 0.7402 0.0720  -0.0619 -0.0682 317 SER C CB  
10730 O OG  . SER C 317 ? 0.6430 0.8723 0.8619 0.0672  -0.0605 -0.0696 317 SER C OG  
10731 N N   . TYR C 318 ? 0.3675 0.5450 0.5019 0.0794  -0.0512 -0.0624 318 TYR C N   
10732 C CA  . TYR C 318 ? 0.3916 0.5568 0.5075 0.0881  -0.0502 -0.0614 318 TYR C CA  
10733 C C   . TYR C 318 ? 0.3782 0.5339 0.4840 0.0881  -0.0383 -0.0584 318 TYR C C   
10734 O O   . TYR C 318 ? 0.3796 0.5266 0.4742 0.0965  -0.0358 -0.0574 318 TYR C O   
10735 C CB  . TYR C 318 ? 0.3718 0.5226 0.4652 0.0876  -0.0536 -0.0617 318 TYR C CB  
10736 C CG  . TYR C 318 ? 0.3740 0.5289 0.4702 0.0926  -0.0658 -0.0647 318 TYR C CG  
10737 C CD1 . TYR C 318 ? 0.3870 0.5570 0.5028 0.0987  -0.0739 -0.0675 318 TYR C CD1 
10738 C CD2 . TYR C 318 ? 0.3764 0.5202 0.4556 0.0913  -0.0692 -0.0650 318 TYR C CD2 
10739 C CE1 . TYR C 318 ? 0.3497 0.5228 0.4665 0.1034  -0.0862 -0.0711 318 TYR C CE1 
10740 C CE2 . TYR C 318 ? 0.4059 0.5511 0.4848 0.0966  -0.0803 -0.0678 318 TYR C CE2 
10741 C CZ  . TYR C 318 ? 0.4074 0.5670 0.5045 0.1026  -0.0893 -0.0711 318 TYR C CZ  
10742 O OH  . TYR C 318 ? 0.4302 0.5910 0.5260 0.1078  -0.1013 -0.0747 318 TYR C OH  
10743 N N   . HIS C 319 ? 0.3766 0.5327 0.4845 0.0797  -0.0307 -0.0569 319 HIS C N   
10744 C CA  . HIS C 319 ? 0.3816 0.5280 0.4792 0.0796  -0.0197 -0.0545 319 HIS C CA  
10745 C C   . HIS C 319 ? 0.4055 0.5570 0.5137 0.0890  -0.0166 -0.0535 319 HIS C C   
10746 O O   . HIS C 319 ? 0.3942 0.5331 0.4878 0.0933  -0.0089 -0.0517 319 HIS C O   
10747 C CB  . HIS C 319 ? 0.3180 0.4669 0.4195 0.0705  -0.0132 -0.0533 319 HIS C CB  
10748 C CG  . HIS C 319 ? 0.3447 0.5093 0.4717 0.0704  -0.0118 -0.0528 319 HIS C CG  
10749 N ND1 . HIS C 319 ? 0.3625 0.5402 0.5076 0.0665  -0.0180 -0.0544 319 HIS C ND1 
10750 C CD2 . HIS C 319 ? 0.3883 0.5569 0.5259 0.0736  -0.0040 -0.0509 319 HIS C CD2 
10751 C CE1 . HIS C 319 ? 0.3740 0.5634 0.5409 0.0667  -0.0139 -0.0537 319 HIS C CE1 
10752 N NE2 . HIS C 319 ? 0.3662 0.5509 0.5294 0.0712  -0.0053 -0.0514 319 HIS C NE2 
10753 N N   . ALA C 320 ? 0.3316 0.5014 0.4652 0.0922  -0.0222 -0.0546 320 ALA C N   
10754 C CA  . ALA C 320 ? 0.3867 0.5654 0.5348 0.1011  -0.0194 -0.0535 320 ALA C CA  
10755 C C   . ALA C 320 ? 0.4510 0.6295 0.5950 0.1131  -0.0266 -0.0544 320 ALA C C   
10756 O O   . ALA C 320 ? 0.4635 0.6496 0.6183 0.1224  -0.0248 -0.0532 320 ALA C O   
10757 C CB  . ALA C 320 ? 0.4039 0.6043 0.5845 0.0982  -0.0210 -0.0544 320 ALA C CB  
10758 N N   . TRP C 321 ? 0.4849 0.6546 0.6128 0.1139  -0.0341 -0.0562 321 TRP C N   
10759 C CA  . TRP C 321 ? 0.5040 0.6719 0.6250 0.1259  -0.0417 -0.0572 321 TRP C CA  
10760 C C   . TRP C 321 ? 0.4849 0.6288 0.5754 0.1317  -0.0343 -0.0547 321 TRP C C   
10761 O O   . TRP C 321 ? 0.4918 0.6195 0.5638 0.1238  -0.0267 -0.0536 321 TRP C O   
10762 C CB  . TRP C 321 ? 0.5346 0.7048 0.6542 0.1245  -0.0542 -0.0607 321 TRP C CB  
10763 C CG  . TRP C 321 ? 0.5470 0.7382 0.6939 0.1192  -0.0630 -0.0641 321 TRP C CG  
10764 C CD1 . TRP C 321 ? 0.5474 0.7506 0.7149 0.1096  -0.0589 -0.0642 321 TRP C CD1 
10765 C CD2 . TRP C 321 ? 0.5639 0.7648 0.7188 0.1230  -0.0771 -0.0684 321 TRP C CD2 
10766 N NE1 . TRP C 321 ? 0.5624 0.7819 0.7513 0.1065  -0.0690 -0.0682 321 TRP C NE1 
10767 C CE2 . TRP C 321 ? 0.5827 0.8015 0.7645 0.1144  -0.0809 -0.0712 321 TRP C CE2 
10768 C CE3 . TRP C 321 ? 0.5812 0.7760 0.7219 0.1332  -0.0866 -0.0702 321 TRP C CE3 
10769 C CZ2 . TRP C 321 ? 0.5921 0.8232 0.7874 0.1147  -0.0943 -0.0764 321 TRP C CZ2 
10770 C CZ3 . TRP C 321 ? 0.5868 0.7940 0.7400 0.1345  -0.1006 -0.0751 321 TRP C CZ3 
10771 C CH2 . TRP C 321 ? 0.5933 0.8186 0.7738 0.1248  -0.1046 -0.0784 321 TRP C CH2 
10772 N N   . ASN C 322 ? 0.4884 0.6303 0.5737 0.1456  -0.0365 -0.0540 322 ASN C N   
10773 C CA  . ASN C 322 ? 0.5572 0.6745 0.6113 0.1523  -0.0320 -0.0524 322 ASN C CA  
10774 C C   . ASN C 322 ? 0.5702 0.6767 0.6087 0.1465  -0.0370 -0.0541 322 ASN C C   
10775 O O   . ASN C 322 ? 0.5941 0.7132 0.6448 0.1441  -0.0478 -0.0569 322 ASN C O   
10776 C CB  . ASN C 322 ? 0.6202 0.7396 0.6728 0.1699  -0.0360 -0.0515 322 ASN C CB  
10777 C CG  . ASN C 322 ? 0.7137 0.8055 0.7329 0.1782  -0.0295 -0.0492 322 ASN C CG  
10778 O OD1 . ASN C 322 ? 0.7588 0.8407 0.7623 0.1823  -0.0351 -0.0502 322 ASN C OD1 
10779 N ND2 . ASN C 322 ? 0.8006 0.8782 0.8073 0.1808  -0.0166 -0.0461 322 ASN C ND2 
10780 N N   . ALA C 323 ? 0.6275 0.6762 0.6771 0.2173  -0.1087 -0.0681 323 ALA C N   
10781 C CA  . ALA C 323 ? 0.5896 0.6137 0.6009 0.2116  -0.1063 -0.0543 323 ALA C CA  
10782 C C   . ALA C 323 ? 0.6570 0.6749 0.6434 0.2332  -0.1252 -0.0493 323 ALA C C   
10783 O O   . ALA C 323 ? 0.6644 0.6827 0.6344 0.2272  -0.1303 -0.0468 323 ALA C O   
10784 C CB  . ALA C 323 ? 0.5303 0.5169 0.5150 0.2059  -0.0876 -0.0402 323 ALA C CB  
10785 N N   . GLU C 324 ? 0.7017 0.7124 0.6831 0.2588  -0.1356 -0.0474 324 GLU C N   
10786 C CA  . GLU C 324 ? 0.7423 0.7456 0.6963 0.2802  -0.1545 -0.0418 324 GLU C CA  
10787 C C   . GLU C 324 ? 0.6489 0.6932 0.6255 0.2803  -0.1731 -0.0565 324 GLU C C   
10788 O O   . GLU C 324 ? 0.6251 0.6663 0.5777 0.2834  -0.1838 -0.0531 324 GLU C O   
10789 C CB  . GLU C 324 ? 0.8976 0.8832 0.8405 0.3093  -0.1618 -0.0360 324 GLU C CB  
10790 C CG  . GLU C 324 ? 1.0062 0.9492 0.9263 0.3082  -0.1413 -0.0227 324 GLU C CG  
10791 C CD  . GLU C 324 ? 1.1373 1.0374 1.0097 0.3315  -0.1454 -0.0066 324 GLU C CD  
10792 O OE1 . GLU C 324 ? 1.1856 1.0673 1.0549 0.3501  -0.1431 -0.0026 324 GLU C OE1 
10793 O OE2 . GLU C 324 ? 1.1681 1.0509 1.0051 0.3309  -0.1497 0.0019  324 GLU C OE2 
10794 N N   . ASP C 325 ? 0.5810 0.6637 0.6032 0.2753  -0.1756 -0.0739 325 ASP C N   
10795 C CA  . ASP C 325 ? 0.5847 0.7077 0.6305 0.2708  -0.1901 -0.0903 325 ASP C CA  
10796 C C   . ASP C 325 ? 0.5637 0.6856 0.6007 0.2456  -0.1815 -0.0900 325 ASP C C   
10797 O O   . ASP C 325 ? 0.4896 0.6237 0.5186 0.2454  -0.1934 -0.0944 325 ASP C O   
10798 C CB  . ASP C 325 ? 0.6131 0.7754 0.7102 0.2672  -0.1905 -0.1100 325 ASP C CB  
10799 C CG  . ASP C 325 ? 0.7442 0.9101 0.8541 0.2931  -0.1987 -0.1115 325 ASP C CG  
10800 O OD1 . ASP C 325 ? 0.8463 0.9893 0.9247 0.3155  -0.2087 -0.0988 325 ASP C OD1 
10801 O OD2 . ASP C 325 ? 0.7435 0.9325 0.8931 0.2896  -0.1933 -0.1248 325 ASP C OD2 
10802 N N   . ALA C 326 ? 0.5136 0.6215 0.5519 0.2246  -0.1609 -0.0853 326 ALA C N   
10803 C CA  . ALA C 326 ? 0.4937 0.5991 0.5237 0.2023  -0.1521 -0.0838 326 ALA C CA  
10804 C C   . ALA C 326 ? 0.5052 0.5845 0.4927 0.2078  -0.1563 -0.0701 326 ALA C C   
10805 O O   . ALA C 326 ? 0.5035 0.5912 0.4853 0.2000  -0.1609 -0.0738 326 ALA C O   
10806 C CB  . ALA C 326 ? 0.4863 0.5794 0.5218 0.1818  -0.1304 -0.0791 326 ALA C CB  
10807 N N   . VAL C 327 ? 0.5356 0.5811 0.4918 0.2201  -0.1531 -0.0547 327 VAL C N   
10808 C CA  . VAL C 327 ? 0.5625 0.5800 0.4766 0.2231  -0.1541 -0.0417 327 VAL C CA  
10809 C C   . VAL C 327 ? 0.5682 0.5955 0.4702 0.2404  -0.1757 -0.0456 327 VAL C C   
10810 O O   . VAL C 327 ? 0.5473 0.5684 0.4273 0.2362  -0.1790 -0.0430 327 VAL C O   
10811 C CB  . VAL C 327 ? 0.6311 0.6078 0.5134 0.2299  -0.1426 -0.0252 327 VAL C CB  
10812 C CG1 . VAL C 327 ? 0.6832 0.6298 0.5199 0.2356  -0.1447 -0.0129 327 VAL C CG1 
10813 C CG2 . VAL C 327 ? 0.6152 0.5837 0.5063 0.2090  -0.1207 -0.0217 327 VAL C CG2 
10814 N N   . ARG C 328 ? 0.5839 0.6281 0.5008 0.2602  -0.1909 -0.0526 328 ARG C N   
10815 C CA  . ARG C 328 ? 0.5804 0.6400 0.4887 0.2765  -0.2135 -0.0581 328 ARG C CA  
10816 C C   . ARG C 328 ? 0.6192 0.7125 0.5490 0.2603  -0.2184 -0.0737 328 ARG C C   
10817 O O   . ARG C 328 ? 0.6053 0.6983 0.5136 0.2618  -0.2283 -0.0740 328 ARG C O   
10818 C CB  . ARG C 328 ? 0.6219 0.6974 0.5487 0.2961  -0.2252 -0.0643 328 ARG C CB  
10819 C CG  . ARG C 328 ? 0.7224 0.8194 0.6490 0.3028  -0.2419 -0.0732 328 ARG C CG  
10820 C CD  . ARG C 328 ? 0.7503 0.8674 0.7013 0.3186  -0.2510 -0.0809 328 ARG C CD  
10821 N NE  . ARG C 328 ? 0.8386 0.9326 0.7889 0.3282  -0.2410 -0.0710 328 ARG C NE  
10822 C CZ  . ARG C 328 ? 0.8345 0.9493 0.8241 0.3288  -0.2371 -0.0805 328 ARG C CZ  
10823 N NH1 . ARG C 328 ? 0.8051 0.9648 0.8380 0.3196  -0.2421 -0.1007 328 ARG C NH1 
10824 N NH2 . ARG C 328 ? 0.8272 0.9165 0.8123 0.3376  -0.2266 -0.0707 328 ARG C NH2 
10825 N N   . ASP C 329 ? 0.5621 0.6819 0.5319 0.2433  -0.2097 -0.0867 329 ASP C N   
10826 C CA  . ASP C 329 ? 0.5292 0.6779 0.5190 0.2261  -0.2112 -0.1022 329 ASP C CA  
10827 C C   . ASP C 329 ? 0.5366 0.6628 0.4993 0.2099  -0.2003 -0.0934 329 ASP C C   
10828 O O   . ASP C 329 ? 0.4901 0.6271 0.4474 0.2042  -0.2066 -0.1006 329 ASP C O   
10829 C CB  . ASP C 329 ? 0.5058 0.6802 0.5396 0.2104  -0.2009 -0.1163 329 ASP C CB  
10830 C CG  . ASP C 329 ? 0.5489 0.7527 0.6046 0.1924  -0.2012 -0.1341 329 ASP C CG  
10831 O OD1 . ASP C 329 ? 0.5216 0.7134 0.5699 0.1727  -0.1871 -0.1310 329 ASP C OD1 
10832 O OD2 . ASP C 329 ? 0.5555 0.7943 0.6357 0.1979  -0.2151 -0.1518 329 ASP C OD2 
10833 N N   . PHE C 330 ? 0.5738 0.6691 0.5197 0.2025  -0.1834 -0.0784 330 PHE C N   
10834 C CA  . PHE C 330 ? 0.5451 0.6206 0.4688 0.1874  -0.1715 -0.0701 330 PHE C CA  
10835 C C   . PHE C 330 ? 0.5544 0.6090 0.4382 0.1985  -0.1803 -0.0613 330 PHE C C   
10836 O O   . PHE C 330 ? 0.5546 0.6110 0.4283 0.1901  -0.1812 -0.0645 330 PHE C O   
10837 C CB  . PHE C 330 ? 0.4689 0.5209 0.3874 0.1777  -0.1523 -0.0575 330 PHE C CB  
10838 C CG  . PHE C 330 ? 0.4604 0.4980 0.3644 0.1613  -0.1390 -0.0506 330 PHE C CG  
10839 C CD1 . PHE C 330 ? 0.4411 0.4935 0.3675 0.1425  -0.1295 -0.0576 330 PHE C CD1 
10840 C CD2 . PHE C 330 ? 0.5044 0.5122 0.3719 0.1649  -0.1351 -0.0369 330 PHE C CD2 
10841 C CE1 . PHE C 330 ? 0.4821 0.5212 0.3956 0.1294  -0.1176 -0.0506 330 PHE C CE1 
10842 C CE2 . PHE C 330 ? 0.5356 0.5321 0.3922 0.1508  -0.1228 -0.0311 330 PHE C CE2 
10843 C CZ  . PHE C 330 ? 0.5011 0.5139 0.3814 0.1338  -0.1145 -0.0377 330 PHE C CZ  
10844 N N   . ILE C 331 ? 0.6084 0.6406 0.4671 0.2171  -0.1859 -0.0502 331 ILE C N   
10845 C CA  . ILE C 331 ? 0.6977 0.7077 0.5150 0.2291  -0.1949 -0.0419 331 ILE C CA  
10846 C C   . ILE C 331 ? 0.6923 0.7295 0.5143 0.2363  -0.2152 -0.0550 331 ILE C C   
10847 O O   . ILE C 331 ? 0.6591 0.6866 0.4542 0.2352  -0.2193 -0.0534 331 ILE C O   
10848 C CB  . ILE C 331 ? 0.7955 0.7752 0.5852 0.2491  -0.1970 -0.0282 331 ILE C CB  
10849 C CG1 . ILE C 331 ? 0.7925 0.7458 0.5773 0.2398  -0.1754 -0.0167 331 ILE C CG1 
10850 C CG2 . ILE C 331 ? 0.8590 0.8125 0.6058 0.2568  -0.2016 -0.0199 331 ILE C CG2 
10851 C CD1 . ILE C 331 ? 0.7561 0.6834 0.5134 0.2259  -0.1606 -0.0070 331 ILE C CD1 
10852 N N   . GLY C 332 ? 0.7007 0.7733 0.5578 0.2425  -0.2269 -0.0693 332 GLY C N   
10853 C CA  . GLY C 332 ? 0.7230 0.8239 0.5906 0.2436  -0.2409 -0.0836 332 GLY C CA  
10854 C C   . GLY C 332 ? 0.6515 0.7694 0.5262 0.2253  -0.2394 -0.0952 332 GLY C C   
10855 O O   . GLY C 332 ? 0.5765 0.7014 0.4405 0.2236  -0.2466 -0.1012 332 GLY C O   
10856 N N   . ARG C 333 ? 0.5812 0.7006 0.4759 0.2058  -0.2221 -0.0972 333 ARG C N   
10857 C CA  . ARG C 333 ? 0.5815 0.7083 0.4808 0.1854  -0.2140 -0.1058 333 ARG C CA  
10858 C C   . ARG C 333 ? 0.5820 0.6759 0.4413 0.1819  -0.2071 -0.0927 333 ARG C C   
10859 O O   . ARG C 333 ? 0.5869 0.6853 0.4373 0.1738  -0.2089 -0.0999 333 ARG C O   
10860 C CB  . ARG C 333 ? 0.5800 0.7139 0.5095 0.1663  -0.1962 -0.1100 333 ARG C CB  
10861 C CG  . ARG C 333 ? 0.5565 0.7247 0.5274 0.1661  -0.2010 -0.1261 333 ARG C CG  
10862 C CD  . ARG C 333 ? 0.5142 0.6857 0.5097 0.1460  -0.1826 -0.1299 333 ARG C CD  
10863 N NE  . ARG C 333 ? 0.5317 0.7308 0.5647 0.1465  -0.1848 -0.1431 333 ARG C NE  
10864 C CZ  . ARG C 333 ? 0.5316 0.7632 0.5948 0.1368  -0.1872 -0.1641 333 ARG C CZ  
10865 N NH1 . ARG C 333 ? 0.5013 0.7403 0.5599 0.1256  -0.1875 -0.1739 333 ARG C NH1 
10866 N NH2 . ARG C 333 ? 0.5426 0.7984 0.6403 0.1374  -0.1880 -0.1762 333 ARG C NH2 
10867 N N   . LEU C 334 ? 0.5338 0.5944 0.3692 0.1865  -0.1977 -0.0746 334 LEU C N   
10868 C CA  . LEU C 334 ? 0.5515 0.5805 0.3479 0.1846  -0.1912 -0.0626 334 LEU C CA  
10869 C C   . LEU C 334 ? 0.6635 0.6881 0.4296 0.1990  -0.2088 -0.0633 334 LEU C C   
10870 O O   . LEU C 334 ? 0.7053 0.7188 0.4480 0.1930  -0.2072 -0.0631 334 LEU C O   
10871 C CB  . LEU C 334 ? 0.5546 0.5512 0.3330 0.1872  -0.1780 -0.0450 334 LEU C CB  
10872 C CG  . LEU C 334 ? 0.5213 0.5183 0.3227 0.1718  -0.1595 -0.0421 334 LEU C CG  
10873 C CD1 . LEU C 334 ? 0.5490 0.5149 0.3294 0.1748  -0.1477 -0.0260 334 LEU C CD1 
10874 C CD2 . LEU C 334 ? 0.5034 0.5035 0.3099 0.1540  -0.1487 -0.0459 334 LEU C CD2 
10875 N N   . LYS C 335 ? 0.6818 0.7139 0.4495 0.2167  -0.2231 -0.0638 335 LYS C N   
10876 C CA  . LYS C 335 ? 0.7766 0.8077 0.5261 0.2253  -0.2344 -0.0650 335 LYS C CA  
10877 C C   . LYS C 335 ? 0.7550 0.8152 0.5172 0.2148  -0.2418 -0.0820 335 LYS C C   
10878 O O   . LYS C 335 ? 0.7652 0.8146 0.5016 0.2116  -0.2432 -0.0813 335 LYS C O   
10879 C CB  . LYS C 335 ? 0.8473 0.8882 0.6082 0.2431  -0.2455 -0.0652 335 LYS C CB  
10880 C CG  . LYS C 335 ? 0.9563 0.9592 0.6885 0.2565  -0.2402 -0.0473 335 LYS C CG  
10881 C CD  . LYS C 335 ? 1.0194 1.0323 0.7612 0.2753  -0.2524 -0.0486 335 LYS C CD  
10882 C CE  . LYS C 335 ? 1.0101 1.0066 0.7566 0.2839  -0.2444 -0.0394 335 LYS C CE  
10883 N NZ  . LYS C 335 ? 1.0259 0.9743 0.7306 0.2890  -0.2333 -0.0212 335 LYS C NZ  
10884 N N   . LYS C 336 ? 0.7232 0.8201 0.5254 0.2079  -0.2451 -0.0984 336 LYS C N   
10885 C CA  . LYS C 336 ? 0.6991 0.8254 0.5166 0.1961  -0.2503 -0.1170 336 LYS C CA  
10886 C C   . LYS C 336 ? 0.6951 0.8064 0.4942 0.1798  -0.2393 -0.1175 336 LYS C C   
10887 O O   . LYS C 336 ? 0.7184 0.8358 0.5078 0.1723  -0.2422 -0.1263 336 LYS C O   
10888 C CB  . LYS C 336 ? 0.6502 0.8159 0.5154 0.1902  -0.2524 -0.1347 336 LYS C CB  
10889 C CG  . LYS C 336 ? 0.6852 0.8811 0.5702 0.1738  -0.2532 -0.1560 336 LYS C CG  
10890 C CD  . LYS C 336 ? 0.7252 0.9504 0.6542 0.1626  -0.2479 -0.1717 336 LYS C CD  
10891 C CE  . LYS C 336 ? 0.7338 0.9362 0.6660 0.1575  -0.2313 -0.1587 336 LYS C CE  
10892 N NZ  . LYS C 336 ? 0.7350 0.9603 0.7094 0.1482  -0.2237 -0.1699 336 LYS C NZ  
10893 N N   . ILE C 337 ? 0.6362 0.7252 0.4333 0.1716  -0.2219 -0.1068 337 ILE C N   
10894 C CA  . ILE C 337 ? 0.6457 0.7149 0.4279 0.1553  -0.2056 -0.1037 337 ILE C CA  
10895 C C   . ILE C 337 ? 0.6326 0.6726 0.3688 0.1624  -0.2085 -0.0933 337 ILE C C   
10896 O O   . ILE C 337 ? 0.6165 0.6517 0.3376 0.1529  -0.2052 -0.0985 337 ILE C O   
10897 C CB  . ILE C 337 ? 0.5892 0.6421 0.3828 0.1450  -0.1846 -0.0931 337 ILE C CB  
10898 C CG1 . ILE C 337 ? 0.5330 0.6126 0.3693 0.1346  -0.1796 -0.1046 337 ILE C CG1 
10899 C CG2 . ILE C 337 ? 0.5692 0.5986 0.3433 0.1324  -0.1687 -0.0874 337 ILE C CG2 
10900 C CD1 . ILE C 337 ? 0.4951 0.5612 0.3431 0.1274  -0.1621 -0.0934 337 ILE C CD1 
10901 N N   . HIS C 338 ? 0.6917 0.7091 0.4037 0.1781  -0.2127 -0.0784 338 HIS C N   
10902 C CA  . HIS C 338 ? 0.7625 0.7479 0.4331 0.1823  -0.2105 -0.0668 338 HIS C CA  
10903 C C   . HIS C 338 ? 0.8136 0.8118 0.4759 0.1847  -0.2238 -0.0755 338 HIS C C   
10904 O O   . HIS C 338 ? 0.8896 0.8685 0.5216 0.1806  -0.2206 -0.0724 338 HIS C O   
10905 C CB  . HIS C 338 ? 0.8014 0.7605 0.4568 0.1951  -0.2073 -0.0499 338 HIS C CB  
10906 C CG  . HIS C 338 ? 0.8224 0.7490 0.4380 0.1998  -0.2048 -0.0388 338 HIS C CG  
10907 N ND1 . HIS C 338 ? 0.8458 0.7681 0.4489 0.2137  -0.2160 -0.0355 338 HIS C ND1 
10908 C CD2 . HIS C 338 ? 0.8214 0.7173 0.4067 0.1923  -0.1915 -0.0306 338 HIS C CD2 
10909 C CE1 . HIS C 338 ? 0.8753 0.7651 0.4411 0.2140  -0.2100 -0.0258 338 HIS C CE1 
10910 N NE2 . HIS C 338 ? 0.8674 0.7413 0.4229 0.2006  -0.1948 -0.0231 338 HIS C NE2 
10911 N N   . GLU C 339 ? 0.8264 0.8583 0.5161 0.1904  -0.2380 -0.0871 339 GLU C N   
10912 C CA  . GLU C 339 ? 0.9011 0.9511 0.5871 0.1927  -0.2519 -0.0968 339 GLU C CA  
10913 C C   . GLU C 339 ? 0.8920 0.9675 0.5927 0.1757  -0.2517 -0.1157 339 GLU C C   
10914 O O   . GLU C 339 ? 0.9245 1.0141 0.6192 0.1743  -0.2614 -0.1245 339 GLU C O   
10915 C CB  . GLU C 339 ? 0.9862 1.0618 0.6958 0.2075  -0.2668 -0.1010 339 GLU C CB  
10916 C CG  . GLU C 339 ? 1.1177 1.1673 0.8045 0.2262  -0.2704 -0.0843 339 GLU C CG  
10917 C CD  . GLU C 339 ? 1.2371 1.3107 0.9519 0.2410  -0.2818 -0.0885 339 GLU C CD  
10918 O OE1 . GLU C 339 ? 1.2608 1.3746 1.0103 0.2372  -0.2898 -0.1056 339 GLU C OE1 
10919 O OE2 . GLU C 339 ? 1.2977 1.3496 0.9999 0.2557  -0.2816 -0.0754 339 GLU C OE2 
10920 N N   . SER C 340 ? 0.8353 0.9160 0.5535 0.1623  -0.2404 -0.1226 340 SER C N   
10921 C CA  . SER C 340 ? 0.7931 0.8985 0.5288 0.1454  -0.2385 -0.1428 340 SER C CA  
10922 C C   . SER C 340 ? 0.8092 0.8918 0.5159 0.1324  -0.2272 -0.1435 340 SER C C   
10923 O O   . SER C 340 ? 0.8205 0.9197 0.5353 0.1182  -0.2253 -0.1605 340 SER C O   
10924 C CB  . SER C 340 ? 0.7037 0.8290 0.4767 0.1366  -0.2316 -0.1531 340 SER C CB  
10925 O OG  . SER C 340 ? 0.7331 0.8288 0.5017 0.1318  -0.2125 -0.1375 340 SER C OG  
10926 N N   . VAL C 341 ? 0.7751 0.8198 0.4490 0.1359  -0.2180 -0.1265 341 VAL C N   
10927 C CA  . VAL C 341 ? 0.7798 0.7997 0.4270 0.1241  -0.2043 -0.1257 341 VAL C CA  
10928 C C   . VAL C 341 ? 0.8780 0.8673 0.4845 0.1329  -0.2059 -0.1106 341 VAL C C   
10929 O O   . VAL C 341 ? 0.9130 0.8927 0.5132 0.1468  -0.2116 -0.0972 341 VAL C O   
10930 C CB  . VAL C 341 ? 0.7045 0.7064 0.3662 0.1123  -0.1796 -0.1171 341 VAL C CB  
10931 C CG1 . VAL C 341 ? 0.6259 0.6536 0.3297 0.1000  -0.1728 -0.1299 341 VAL C CG1 
10932 C CG2 . VAL C 341 ? 0.6746 0.6567 0.3313 0.1233  -0.1755 -0.0980 341 VAL C CG2 
10933 N N   . ASP C 342 ? 0.9805 0.9521 0.5600 0.1232  -0.1981 -0.1130 342 ASP C N   
10934 C CA  . ASP C 342 ? 1.1041 1.0452 0.6456 0.1280  -0.1961 -0.0997 342 ASP C CA  
10935 C C   . ASP C 342 ? 1.0948 0.9989 0.6163 0.1259  -0.1770 -0.0857 342 ASP C C   
10936 O O   . ASP C 342 ? 1.1861 1.0631 0.6794 0.1306  -0.1732 -0.0729 342 ASP C O   
10937 C CB  . ASP C 342 ? 1.1970 1.1406 0.7188 0.1185  -0.1991 -0.1105 342 ASP C CB  
10938 C CG  . ASP C 342 ? 1.2356 1.1722 0.7543 0.1017  -0.1835 -0.1216 342 ASP C CG  
10939 O OD1 . ASP C 342 ? 1.1941 1.1387 0.7385 0.0964  -0.1747 -0.1265 342 ASP C OD1 
10940 O OD2 . ASP C 342 ? 1.2954 1.2182 0.7878 0.0932  -0.1785 -0.1253 342 ASP C OD2 
10941 N N   . PHE C 343 ? 0.9371 0.8410 0.4779 0.1174  -0.1625 -0.0872 343 PHE C N   
10942 C CA  . PHE C 343 ? 0.8387 0.7143 0.3732 0.1144  -0.1424 -0.0728 343 PHE C CA  
10943 C C   . PHE C 343 ? 0.7868 0.6640 0.3388 0.1237  -0.1428 -0.0613 343 PHE C C   
10944 O O   . PHE C 343 ? 0.7982 0.6958 0.3655 0.1331  -0.1582 -0.0639 343 PHE C O   
10945 C CB  . PHE C 343 ? 0.7979 0.6738 0.3528 0.0984  -0.1225 -0.0778 343 PHE C CB  
10946 C CG  . PHE C 343 ? 0.7503 0.6546 0.3483 0.0926  -0.1221 -0.0863 343 PHE C CG  
10947 C CD1 . PHE C 343 ? 0.7425 0.6707 0.3540 0.0854  -0.1294 -0.1039 343 PHE C CD1 
10948 C CD2 . PHE C 343 ? 0.7384 0.6454 0.3622 0.0933  -0.1137 -0.0776 343 PHE C CD2 
10949 C CE1 . PHE C 343 ? 0.6808 0.6330 0.3300 0.0788  -0.1275 -0.1126 343 PHE C CE1 
10950 C CE2 . PHE C 343 ? 0.7067 0.6375 0.3673 0.0873  -0.1126 -0.0854 343 PHE C CE2 
10951 C CZ  . PHE C 343 ? 0.6786 0.6310 0.3517 0.0799  -0.1189 -0.1029 343 PHE C CZ  
10952 N N   . GLN C 344 ? 0.7362 0.5929 0.2871 0.1206  -0.1252 -0.0493 344 GLN C N   
10953 C CA  . GLN C 344 ? 0.7057 0.5608 0.2698 0.1275  -0.1231 -0.0383 344 GLN C CA  
10954 C C   . GLN C 344 ? 0.6860 0.5619 0.2932 0.1189  -0.1141 -0.0411 344 GLN C C   
10955 O O   . GLN C 344 ? 0.6900 0.5585 0.3051 0.1093  -0.0969 -0.0381 344 GLN C O   
10956 C CB  . GLN C 344 ? 0.7176 0.5395 0.2541 0.1287  -0.1094 -0.0244 344 GLN C CB  
10957 C CG  . GLN C 344 ? 0.8248 0.6225 0.3182 0.1373  -0.1170 -0.0198 344 GLN C CG  
10958 C CD  . GLN C 344 ? 0.8565 0.6239 0.3315 0.1367  -0.1015 -0.0067 344 GLN C CD  
10959 O OE1 . GLN C 344 ? 0.9408 0.6966 0.4063 0.1450  -0.1051 0.0007  344 GLN C OE1 
10960 N NE2 . GLN C 344 ? 0.8473 0.6018 0.3175 0.1269  -0.0833 -0.0048 344 GLN C NE2 
10961 N N   . PRO C 345 ? 0.6578 0.5595 0.2930 0.1222  -0.1250 -0.0472 345 PRO C N   
10962 C CA  . PRO C 345 ? 0.6571 0.5771 0.3305 0.1128  -0.1162 -0.0508 345 PRO C CA  
10963 C C   . PRO C 345 ? 0.6403 0.5507 0.3228 0.1123  -0.1036 -0.0379 345 PRO C C   
10964 O O   . PRO C 345 ? 0.5959 0.4927 0.2637 0.1209  -0.1050 -0.0279 345 PRO C O   
10965 C CB  . PRO C 345 ? 0.6361 0.5853 0.3331 0.1174  -0.1322 -0.0616 345 PRO C CB  
10966 C CG  . PRO C 345 ? 0.6603 0.6037 0.3350 0.1332  -0.1478 -0.0572 345 PRO C CG  
10967 C CD  . PRO C 345 ? 0.6416 0.5579 0.2749 0.1349  -0.1459 -0.0518 345 PRO C CD  
10968 N N   . VAL C 346 ? 0.6538 0.5714 0.3603 0.1018  -0.0910 -0.0387 346 VAL C N   
10969 C CA  . VAL C 346 ? 0.5882 0.5037 0.3093 0.0997  -0.0801 -0.0287 346 VAL C CA  
10970 C C   . VAL C 346 ? 0.6109 0.5501 0.3654 0.0964  -0.0835 -0.0349 346 VAL C C   
10971 O O   . VAL C 346 ? 0.5885 0.5405 0.3601 0.0882  -0.0817 -0.0445 346 VAL C O   
10972 C CB  . VAL C 346 ? 0.5638 0.4678 0.2839 0.0915  -0.0628 -0.0233 346 VAL C CB  
10973 C CG1 . VAL C 346 ? 0.5095 0.4153 0.2452 0.0893  -0.0531 -0.0139 346 VAL C CG1 
10974 C CG2 . VAL C 346 ? 0.5660 0.4467 0.2534 0.0942  -0.0585 -0.0186 346 VAL C CG2 
10975 N N   . VAL C 347 ? 0.5638 0.5071 0.3260 0.1022  -0.0875 -0.0299 347 VAL C N   
10976 C CA  . VAL C 347 ? 0.5640 0.5291 0.3560 0.1003  -0.0918 -0.0363 347 VAL C CA  
10977 C C   . VAL C 347 ? 0.5137 0.4770 0.3193 0.0944  -0.0793 -0.0274 347 VAL C C   
10978 O O   . VAL C 347 ? 0.4816 0.4351 0.2792 0.0992  -0.0771 -0.0181 347 VAL C O   
10979 C CB  . VAL C 347 ? 0.5569 0.5296 0.3484 0.1125  -0.1070 -0.0390 347 VAL C CB  
10980 C CG1 . VAL C 347 ? 0.5076 0.5053 0.3325 0.1094  -0.1109 -0.0485 347 VAL C CG1 
10981 C CG2 . VAL C 347 ? 0.5974 0.5698 0.3691 0.1203  -0.1207 -0.0456 347 VAL C CG2 
10982 N N   . PHE C 348 ? 0.4532 0.4247 0.2773 0.0838  -0.0707 -0.0304 348 PHE C N   
10983 C CA  . PHE C 348 ? 0.4742 0.4468 0.3117 0.0777  -0.0599 -0.0228 348 PHE C CA  
10984 C C   . PHE C 348 ? 0.4577 0.4475 0.3192 0.0754  -0.0640 -0.0287 348 PHE C C   
10985 O O   . PHE C 348 ? 0.4801 0.4838 0.3573 0.0710  -0.0677 -0.0404 348 PHE C O   
10986 C CB  . PHE C 348 ? 0.4238 0.3936 0.2657 0.0690  -0.0485 -0.0215 348 PHE C CB  
10987 C CG  . PHE C 348 ? 0.4397 0.3942 0.2657 0.0701  -0.0389 -0.0105 348 PHE C CG  
10988 C CD1 . PHE C 348 ? 0.4387 0.3790 0.2415 0.0749  -0.0399 -0.0096 348 PHE C CD1 
10989 C CD2 . PHE C 348 ? 0.4299 0.3855 0.2642 0.0659  -0.0290 -0.0018 348 PHE C CD2 
10990 C CE1 . PHE C 348 ? 0.4571 0.3845 0.2469 0.0752  -0.0299 -0.0010 348 PHE C CE1 
10991 C CE2 . PHE C 348 ? 0.4295 0.3750 0.2523 0.0669  -0.0203 0.0067  348 PHE C CE2 
10992 C CZ  . PHE C 348 ? 0.4598 0.3910 0.2611 0.0713  -0.0201 0.0068  348 PHE C CZ  
10993 N N   . VAL C 349 ? 0.4034 0.3919 0.2673 0.0779  -0.0625 -0.0218 349 VAL C N   
10994 C CA  . VAL C 349 ? 0.4177 0.4206 0.3043 0.0746  -0.0634 -0.0263 349 VAL C CA  
10995 C C   . VAL C 349 ? 0.4448 0.4463 0.3384 0.0653  -0.0509 -0.0182 349 VAL C C   
10996 O O   . VAL C 349 ? 0.4278 0.4195 0.3107 0.0666  -0.0454 -0.0081 349 VAL C O   
10997 C CB  . VAL C 349 ? 0.4344 0.4366 0.3182 0.0852  -0.0715 -0.0256 349 VAL C CB  
10998 C CG1 . VAL C 349 ? 0.3825 0.3978 0.2901 0.0806  -0.0694 -0.0295 349 VAL C CG1 
10999 C CG2 . VAL C 349 ? 0.4719 0.4793 0.3503 0.0956  -0.0862 -0.0344 349 VAL C CG2 
11000 N N   . VAL C 350 ? 0.4304 0.4415 0.3408 0.0554  -0.0462 -0.0232 350 VAL C N   
11001 C CA  . VAL C 350 ? 0.4267 0.4368 0.3416 0.0467  -0.0353 -0.0156 350 VAL C CA  
11002 C C   . VAL C 350 ? 0.4028 0.4250 0.3383 0.0380  -0.0332 -0.0218 350 VAL C C   
11003 O O   . VAL C 350 ? 0.4278 0.4576 0.3748 0.0339  -0.0354 -0.0330 350 VAL C O   
11004 C CB  . VAL C 350 ? 0.3876 0.3910 0.2962 0.0434  -0.0292 -0.0131 350 VAL C CB  
11005 C CG1 . VAL C 350 ? 0.4296 0.4322 0.3401 0.0376  -0.0194 -0.0031 350 VAL C CG1 
11006 C CG2 . VAL C 350 ? 0.4171 0.4089 0.3062 0.0513  -0.0314 -0.0101 350 VAL C CG2 
11007 N N   . LEU C 351 ? 0.3570 0.3808 0.2965 0.0340  -0.0280 -0.0155 351 LEU C N   
11008 C CA  . LEU C 351 ? 0.2929 0.3264 0.2498 0.0245  -0.0243 -0.0206 351 LEU C CA  
11009 C C   . LEU C 351 ? 0.2963 0.3287 0.2509 0.0195  -0.0170 -0.0108 351 LEU C C   
11010 O O   . LEU C 351 ? 0.3339 0.3598 0.2759 0.0240  -0.0155 -0.0021 351 LEU C O   
11011 C CB  . LEU C 351 ? 0.2935 0.3367 0.2643 0.0275  -0.0313 -0.0319 351 LEU C CB  
11012 C CG  . LEU C 351 ? 0.3034 0.3433 0.2695 0.0368  -0.0352 -0.0284 351 LEU C CG  
11013 C CD1 . LEU C 351 ? 0.3147 0.3663 0.3004 0.0366  -0.0381 -0.0386 351 LEU C CD1 
11014 C CD2 . LEU C 351 ? 0.3442 0.3757 0.2934 0.0504  -0.0440 -0.0265 351 LEU C CD2 
11015 N N   . ASN C 352 ? 0.2770 0.3159 0.2433 0.0089  -0.0118 -0.0132 352 ASN C N   
11016 C CA  . ASN C 352 ? 0.2706 0.3110 0.2357 0.0026  -0.0052 -0.0058 352 ASN C CA  
11017 C C   . ASN C 352 ? 0.2735 0.3119 0.2366 0.0081  -0.0067 -0.0052 352 ASN C C   
11018 O O   . ASN C 352 ? 0.2775 0.3171 0.2475 0.0140  -0.0122 -0.0130 352 ASN C O   
11019 C CB  . ASN C 352 ? 0.2763 0.3232 0.2536 -0.0099 0.0000  -0.0106 352 ASN C CB  
11020 C CG  . ASN C 352 ? 0.3995 0.4440 0.3710 -0.0161 0.0048  -0.0047 352 ASN C CG  
11021 O OD1 . ASN C 352 ? 0.3856 0.4258 0.3565 -0.0159 0.0044  -0.0083 352 ASN C OD1 
11022 N ND2 . ASN C 352 ? 0.3571 0.4040 0.3232 -0.0213 0.0097  0.0044  352 ASN C ND2 
11023 N N   . GLY C 353 ? 0.3017 0.3365 0.2544 0.0070  -0.0016 0.0038  353 GLY C N   
11024 C CA  . GLY C 353 ? 0.2978 0.3261 0.2449 0.0119  -0.0009 0.0048  353 GLY C CA  
11025 C C   . GLY C 353 ? 0.3006 0.3323 0.2552 0.0031  0.0061  0.0033  353 GLY C C   
11026 O O   . GLY C 353 ? 0.3900 0.4133 0.3374 0.0062  0.0092  0.0051  353 GLY C O   
11027 N N   . GLU C 354 ? 0.2666 0.3081 0.2339 -0.0083 0.0095  -0.0004 354 GLU C N   
11028 C CA  . GLU C 354 ? 0.2915 0.3363 0.2641 -0.0190 0.0176  -0.0016 354 GLU C CA  
11029 C C   . GLU C 354 ? 0.2742 0.3259 0.2645 -0.0260 0.0186  -0.0117 354 GLU C C   
11030 O O   . GLU C 354 ? 0.2757 0.3286 0.2711 -0.0344 0.0257  -0.0143 354 GLU C O   
11031 C CB  . GLU C 354 ? 0.3748 0.4254 0.3404 -0.0298 0.0241  0.0062  354 GLU C CB  
11032 C CG  . GLU C 354 ? 0.4026 0.4612 0.3742 -0.0389 0.0245  0.0056  354 GLU C CG  
11033 C CD  . GLU C 354 ? 0.3728 0.4302 0.3391 -0.0324 0.0193  0.0098  354 GLU C CD  
11034 O OE1 . GLU C 354 ? 0.3601 0.4217 0.3200 -0.0360 0.0212  0.0173  354 GLU C OE1 
11035 O OE2 . GLU C 354 ? 0.3272 0.3798 0.2959 -0.0238 0.0135  0.0051  354 GLU C OE2 
11036 N N   . ASN C 355 ? 0.3020 0.3576 0.3017 -0.0238 0.0129  -0.0188 355 ASN C N   
11037 C CA  . ASN C 355 ? 0.3286 0.3914 0.3450 -0.0332 0.0159  -0.0294 355 ASN C CA  
11038 C C   . ASN C 355 ? 0.2985 0.3654 0.3312 -0.0260 0.0116  -0.0412 355 ASN C C   
11039 O O   . ASN C 355 ? 0.2778 0.3508 0.3259 -0.0343 0.0165  -0.0504 355 ASN C O   
11040 C CB  . ASN C 355 ? 0.3487 0.4134 0.3657 -0.0381 0.0148  -0.0315 355 ASN C CB  
11041 C CG  . ASN C 355 ? 0.3809 0.4429 0.3843 -0.0456 0.0196  -0.0206 355 ASN C CG  
11042 O OD1 . ASN C 355 ? 0.3824 0.4461 0.3819 -0.0540 0.0256  -0.0158 355 ASN C OD1 
11043 N ND2 . ASN C 355 ? 0.3270 0.3852 0.3228 -0.0422 0.0168  -0.0168 355 ASN C ND2 
11044 N N   . CYS C 356 ? 0.2616 0.3260 0.2915 -0.0105 0.0024  -0.0415 356 CYS C N   
11045 C CA  . CYS C 356 ? 0.2708 0.3426 0.3177 -0.0018 -0.0041 -0.0534 356 CYS C CA  
11046 C C   . CYS C 356 ? 0.2858 0.3527 0.3351 0.0046  -0.0018 -0.0532 356 CYS C C   
11047 O O   . CYS C 356 ? 0.3878 0.4631 0.4561 0.0086  -0.0038 -0.0641 356 CYS C O   
11048 C CB  . CYS C 356 ? 0.3328 0.4056 0.3750 0.0124  -0.0165 -0.0548 356 CYS C CB  
11049 S SG  . CYS C 356 ? 0.3266 0.3819 0.3407 0.0261  -0.0205 -0.0401 356 CYS C SG  
11050 N N   . TRP C 357 ? 0.3096 0.3632 0.3409 0.0051  0.0036  -0.0418 357 TRP C N   
11051 C CA  . TRP C 357 ? 0.3818 0.4251 0.4101 0.0140  0.0059  -0.0406 357 TRP C CA  
11052 C C   . TRP C 357 ? 0.3851 0.4328 0.4306 0.0047  0.0153  -0.0483 357 TRP C C   
11053 O O   . TRP C 357 ? 0.3662 0.4100 0.4190 0.0147  0.0150  -0.0525 357 TRP C O   
11054 C CB  . TRP C 357 ? 0.3891 0.4157 0.3923 0.0144  0.0115  -0.0277 357 TRP C CB  
11055 C CG  . TRP C 357 ? 0.3847 0.4075 0.3721 0.0212  0.0042  -0.0208 357 TRP C CG  
11056 C CD1 . TRP C 357 ? 0.4029 0.4250 0.3779 0.0132  0.0079  -0.0129 357 TRP C CD1 
11057 C CD2 . TRP C 357 ? 0.4364 0.4566 0.4187 0.0375  -0.0083 -0.0219 357 TRP C CD2 
11058 N NE1 . TRP C 357 ? 0.4110 0.4287 0.3741 0.0232  -0.0002 -0.0091 357 TRP C NE1 
11059 C CE2 . TRP C 357 ? 0.4049 0.4208 0.3709 0.0375  -0.0102 -0.0145 357 TRP C CE2 
11060 C CE3 . TRP C 357 ? 0.4524 0.4746 0.4426 0.0525  -0.0185 -0.0288 357 TRP C CE3 
11061 C CZ2 . TRP C 357 ? 0.4499 0.4616 0.4055 0.0504  -0.0209 -0.0139 357 TRP C CZ2 
11062 C CZ3 . TRP C 357 ? 0.4575 0.4772 0.4369 0.0659  -0.0306 -0.0278 357 TRP C CZ3 
11063 C CH2 . TRP C 357 ? 0.4230 0.4366 0.3845 0.0640  -0.0312 -0.0205 357 TRP C CH2 
11064 N N   . GLU C 358 ? 0.3907 0.4454 0.4419 -0.0139 0.0240  -0.0502 358 GLU C N   
11065 C CA  . GLU C 358 ? 0.3399 0.3978 0.4058 -0.0251 0.0345  -0.0581 358 GLU C CA  
11066 C C   . GLU C 358 ? 0.2788 0.3486 0.3708 -0.0192 0.0303  -0.0727 358 GLU C C   
11067 O O   . GLU C 358 ? 0.2858 0.3570 0.3920 -0.0243 0.0386  -0.0804 358 GLU C O   
11068 C CB  . GLU C 358 ? 0.3361 0.3993 0.4004 -0.0462 0.0432  -0.0574 358 GLU C CB  
11069 C CG  . GLU C 358 ? 0.3243 0.3976 0.3954 -0.0506 0.0378  -0.0621 358 GLU C CG  
11070 C CD  . GLU C 358 ? 0.4252 0.4979 0.4831 -0.0656 0.0430  -0.0548 358 GLU C CD  
11071 O OE1 . GLU C 358 ? 0.4277 0.5047 0.4928 -0.0800 0.0495  -0.0613 358 GLU C OE1 
11072 O OE2 . GLU C 358 ? 0.4045 0.4726 0.4446 -0.0625 0.0406  -0.0429 358 GLU C OE2 
11073 N N   . TYR C 359 ? 0.2714 0.3509 0.3710 -0.0091 0.0180  -0.0779 359 TYR C N   
11074 C CA  . TYR C 359 ? 0.3056 0.4004 0.4317 -0.0021 0.0125  -0.0931 359 TYR C CA  
11075 C C   . TYR C 359 ? 0.3292 0.4216 0.4565 0.0212  0.0020  -0.0930 359 TYR C C   
11076 O O   . TYR C 359 ? 0.3000 0.4064 0.4512 0.0294  -0.0027 -0.1056 359 TYR C O   
11077 C CB  . TYR C 359 ? 0.3034 0.4129 0.4390 -0.0067 0.0061  -0.1016 359 TYR C CB  
11078 C CG  . TYR C 359 ? 0.3289 0.4383 0.4622 -0.0287 0.0167  -0.1023 359 TYR C CG  
11079 C CD1 . TYR C 359 ? 0.3890 0.5063 0.5412 -0.0433 0.0267  -0.1147 359 TYR C CD1 
11080 C CD2 . TYR C 359 ? 0.3142 0.4145 0.4254 -0.0342 0.0171  -0.0903 359 TYR C CD2 
11081 C CE1 . TYR C 359 ? 0.4032 0.5172 0.5492 -0.0631 0.0365  -0.1145 359 TYR C CE1 
11082 C CE2 . TYR C 359 ? 0.3596 0.4580 0.4662 -0.0522 0.0259  -0.0896 359 TYR C CE2 
11083 C CZ  . TYR C 359 ? 0.4238 0.5280 0.5462 -0.0667 0.0355  -0.1014 359 TYR C CZ  
11084 O OH  . TYR C 359 ? 0.4301 0.5294 0.5437 -0.0843 0.0443  -0.0998 359 TYR C OH  
11085 N N   . TYR C 360 ? 0.2971 0.3722 0.3990 0.0322  -0.0017 -0.0793 360 TYR C N   
11086 C CA  . TYR C 360 ? 0.3967 0.4635 0.4933 0.0546  -0.0103 -0.0768 360 TYR C CA  
11087 C C   . TYR C 360 ? 0.3924 0.4459 0.4904 0.0567  0.0006  -0.0757 360 TYR C C   
11088 O O   . TYR C 360 ? 0.3824 0.4265 0.4739 0.0409  0.0153  -0.0717 360 TYR C O   
11089 C CB  . TYR C 360 ? 0.3895 0.4382 0.4545 0.0642  -0.0158 -0.0625 360 TYR C CB  
11090 C CG  . TYR C 360 ? 0.3733 0.4309 0.4335 0.0694  -0.0289 -0.0630 360 TYR C CG  
11091 C CD1 . TYR C 360 ? 0.3673 0.4348 0.4304 0.0541  -0.0269 -0.0648 360 TYR C CD1 
11092 C CD2 . TYR C 360 ? 0.4244 0.4777 0.4737 0.0899  -0.0428 -0.0608 360 TYR C CD2 
11093 C CE1 . TYR C 360 ? 0.3455 0.4185 0.4025 0.0584  -0.0373 -0.0654 360 TYR C CE1 
11094 C CE2 . TYR C 360 ? 0.3418 0.4025 0.3851 0.0936  -0.0541 -0.0619 360 TYR C CE2 
11095 C CZ  . TYR C 360 ? 0.3326 0.4030 0.3804 0.0774  -0.0506 -0.0645 360 TYR C CZ  
11096 O OH  . TYR C 360 ? 0.3338 0.4096 0.3748 0.0804  -0.0602 -0.0660 360 TYR C OH  
11097 N N   . GLU C 361 ? 0.3601 0.4710 0.4635 0.0303  -0.0673 -0.1158 361 GLU C N   
11098 C CA  . GLU C 361 ? 0.4248 0.5173 0.5281 0.0371  -0.0618 -0.1162 361 GLU C CA  
11099 C C   . GLU C 361 ? 0.4162 0.4822 0.4984 0.0333  -0.0569 -0.1012 361 GLU C C   
11100 O O   . GLU C 361 ? 0.4011 0.4584 0.4686 0.0395  -0.0614 -0.0893 361 GLU C O   
11101 C CB  . GLU C 361 ? 0.5198 0.6110 0.6298 0.0608  -0.0709 -0.1190 361 GLU C CB  
11102 C CG  . GLU C 361 ? 0.6806 0.7553 0.7951 0.0700  -0.0664 -0.1230 361 GLU C CG  
11103 C CD  . GLU C 361 ? 0.7757 0.8709 0.9170 0.0684  -0.0619 -0.1416 361 GLU C CD  
11104 O OE1 . GLU C 361 ? 0.7470 0.8657 0.8995 0.0534  -0.0583 -0.1503 361 GLU C OE1 
11105 O OE2 . GLU C 361 ? 0.8524 0.9389 1.0028 0.0821  -0.0613 -0.1476 361 GLU C OE2 
11106 N N   . GLU C 362 ? 0.4215 0.4751 0.5021 0.0221  -0.0471 -0.1024 362 GLU C N   
11107 C CA  . GLU C 362 ? 0.4458 0.4747 0.5094 0.0166  -0.0415 -0.0897 362 GLU C CA  
11108 C C   . GLU C 362 ? 0.3752 0.4079 0.4293 0.0065  -0.0425 -0.0786 362 GLU C C   
11109 O O   . GLU C 362 ? 0.3533 0.3705 0.3937 0.0096  -0.0415 -0.0660 362 GLU C O   
11110 C CB  . GLU C 362 ? 0.5071 0.5118 0.5594 0.0349  -0.0438 -0.0821 362 GLU C CB  
11111 C CG  . GLU C 362 ? 0.6397 0.6390 0.7025 0.0477  -0.0441 -0.0929 362 GLU C CG  
11112 C CD  . GLU C 362 ? 0.7728 0.7435 0.8211 0.0660  -0.0476 -0.0843 362 GLU C CD  
11113 O OE1 . GLU C 362 ? 0.7863 0.7582 0.8426 0.0849  -0.0554 -0.0903 362 GLU C OE1 
11114 O OE2 . GLU C 362 ? 0.8394 0.7862 0.8682 0.0611  -0.0428 -0.0715 362 GLU C OE2 
11115 N N   . ASN C 363 ? 0.3538 0.4068 0.4151 -0.0058 -0.0439 -0.0837 363 ASN C N   
11116 C CA  . ASN C 363 ? 0.3018 0.3586 0.3565 -0.0165 -0.0447 -0.0746 363 ASN C CA  
11117 C C   . ASN C 363 ? 0.3209 0.3758 0.3665 -0.0032 -0.0501 -0.0649 363 ASN C C   
11118 O O   . ASN C 363 ? 0.3229 0.3726 0.3607 -0.0075 -0.0481 -0.0545 363 ASN C O   
11119 C CB  . ASN C 363 ? 0.3317 0.3742 0.3806 -0.0304 -0.0375 -0.0676 363 ASN C CB  
11120 C CG  . ASN C 363 ? 0.3130 0.3641 0.3610 -0.0442 -0.0390 -0.0616 363 ASN C CG  
11121 O OD1 . ASN C 363 ? 0.3297 0.3964 0.3817 -0.0485 -0.0439 -0.0660 363 ASN C OD1 
11122 N ND2 . ASN C 363 ? 0.3176 0.3584 0.3613 -0.0507 -0.0350 -0.0516 363 ASN C ND2 
11123 N N   . GLY C 364 ? 0.3051 0.3644 0.3518 0.0128  -0.0571 -0.0688 364 GLY C N   
11124 C CA  . GLY C 364 ? 0.2967 0.3538 0.3318 0.0248  -0.0630 -0.0610 364 GLY C CA  
11125 C C   . GLY C 364 ? 0.3543 0.3875 0.3723 0.0345  -0.0600 -0.0491 364 GLY C C   
11126 O O   . GLY C 364 ? 0.3344 0.3625 0.3387 0.0441  -0.0636 -0.0420 364 GLY C O   
11127 N N   . ILE C 365 ? 0.3368 0.3532 0.3530 0.0319  -0.0530 -0.0468 365 ILE C N   
11128 C CA  . ILE C 365 ? 0.4247 0.4156 0.4226 0.0377  -0.0482 -0.0345 365 ILE C CA  
11129 C C   . ILE C 365 ? 0.4637 0.4418 0.4489 0.0585  -0.0561 -0.0328 365 ILE C C   
11130 O O   . ILE C 365 ? 0.4790 0.4431 0.4445 0.0654  -0.0560 -0.0224 365 ILE C O   
11131 C CB  . ILE C 365 ? 0.4828 0.4568 0.4808 0.0280  -0.0390 -0.0329 365 ILE C CB  
11132 C CG1 . ILE C 365 ? 0.4408 0.4252 0.4469 0.0074  -0.0327 -0.0314 365 ILE C CG1 
11133 C CG2 . ILE C 365 ? 0.3986 0.3426 0.3758 0.0360  -0.0347 -0.0211 365 ILE C CG2 
11134 C CD1 . ILE C 365 ? 0.4376 0.4193 0.4526 -0.0058 -0.0279 -0.0382 365 ILE C CD1 
11135 N N   . PRO C 366 ? 0.4746 0.4566 0.4698 0.0693  -0.0633 -0.0427 366 PRO C N   
11136 C CA  . PRO C 366 ? 0.5266 0.4980 0.5100 0.0902  -0.0740 -0.0407 366 PRO C CA  
11137 C C   . PRO C 366 ? 0.4971 0.4801 0.4724 0.0953  -0.0820 -0.0385 366 PRO C C   
11138 O O   . PRO C 366 ? 0.5354 0.4999 0.4870 0.1062  -0.0856 -0.0291 366 PRO C O   
11139 C CB  . PRO C 366 ? 0.4049 0.3877 0.4094 0.0986  -0.0804 -0.0547 366 PRO C CB  
11140 C CG  . PRO C 366 ? 0.4582 0.4395 0.4744 0.0841  -0.0688 -0.0595 366 PRO C CG  
11141 C CD  . PRO C 366 ? 0.4662 0.4571 0.4814 0.0641  -0.0610 -0.0551 366 PRO C CD  
11142 N N   . PHE C 367 ? 0.4521 0.4626 0.4437 0.0867  -0.0845 -0.0469 367 PHE C N   
11143 C CA  . PHE C 367 ? 0.4370 0.4574 0.4208 0.0911  -0.0924 -0.0460 367 PHE C CA  
11144 C C   . PHE C 367 ? 0.4324 0.4377 0.3934 0.0882  -0.0856 -0.0328 367 PHE C C   
11145 O O   . PHE C 367 ? 0.3945 0.3889 0.3348 0.0993  -0.0910 -0.0273 367 PHE C O   
11146 C CB  . PHE C 367 ? 0.3619 0.4115 0.3658 0.0798  -0.0947 -0.0567 367 PHE C CB  
11147 C CG  . PHE C 367 ? 0.3741 0.4313 0.3684 0.0819  -0.1014 -0.0555 367 PHE C CG  
11148 C CD1 . PHE C 367 ? 0.4102 0.4696 0.3990 0.0965  -0.1146 -0.0589 367 PHE C CD1 
11149 C CD2 . PHE C 367 ? 0.3753 0.4359 0.3653 0.0702  -0.0953 -0.0511 367 PHE C CD2 
11150 C CE1 . PHE C 367 ? 0.4246 0.4884 0.4017 0.0980  -0.1209 -0.0583 367 PHE C CE1 
11151 C CE2 . PHE C 367 ? 0.4068 0.4717 0.3865 0.0728  -0.1011 -0.0505 367 PHE C CE2 
11152 C CZ  . PHE C 367 ? 0.4091 0.4748 0.3813 0.0862  -0.1135 -0.0542 367 PHE C CZ  
11153 N N   . LEU C 368 ? 0.4297 0.4346 0.3945 0.0732  -0.0737 -0.0283 368 LEU C N   
11154 C CA  . LEU C 368 ? 0.3999 0.3957 0.3488 0.0695  -0.0660 -0.0174 368 LEU C CA  
11155 C C   . LEU C 368 ? 0.4141 0.3804 0.3387 0.0776  -0.0608 -0.0061 368 LEU C C   
11156 O O   . LEU C 368 ? 0.4649 0.4202 0.3686 0.0824  -0.0582 0.0018  368 LEU C O   
11157 C CB  . LEU C 368 ? 0.3491 0.3552 0.3125 0.0513  -0.0563 -0.0163 368 LEU C CB  
11158 C CG  . LEU C 368 ? 0.3212 0.3519 0.3003 0.0422  -0.0605 -0.0239 368 LEU C CG  
11159 C CD1 . LEU C 368 ? 0.3054 0.3429 0.2969 0.0250  -0.0525 -0.0215 368 LEU C CD1 
11160 C CD2 . LEU C 368 ? 0.4640 0.4985 0.4317 0.0495  -0.0655 -0.0225 368 LEU C CD2 
11161 N N   . GLU C 369 ? 0.4229 0.3737 0.3479 0.0788  -0.0582 -0.0051 369 GLU C N   
11162 C CA  . GLU C 369 ? 0.4730 0.3917 0.3721 0.0856  -0.0531 0.0061  369 GLU C CA  
11163 C C   . GLU C 369 ? 0.5390 0.4440 0.4158 0.1047  -0.0650 0.0080  369 GLU C C   
11164 O O   . GLU C 369 ? 0.5450 0.4284 0.3933 0.1096  -0.0615 0.0183  369 GLU C O   
11165 C CB  . GLU C 369 ? 0.5052 0.4081 0.4090 0.0825  -0.0485 0.0060  369 GLU C CB  
11166 C CG  . GLU C 369 ? 0.4924 0.3974 0.4063 0.0630  -0.0346 0.0093  369 GLU C CG  
11167 C CD  . GLU C 369 ? 0.5234 0.4112 0.4404 0.0585  -0.0299 0.0084  369 GLU C CD  
11168 O OE1 . GLU C 369 ? 0.5669 0.4435 0.4820 0.0710  -0.0372 0.0037  369 GLU C OE1 
11169 O OE2 . GLU C 369 ? 0.4870 0.3721 0.4088 0.0425  -0.0190 0.0121  369 GLU C OE2 
11170 N N   . LYS C 370 ? 0.5066 0.4250 0.3960 0.1148  -0.0791 -0.0023 370 LYS C N   
11171 C CA  . LYS C 370 ? 0.4965 0.4058 0.3672 0.1327  -0.0934 -0.0017 370 LYS C CA  
11172 C C   . LYS C 370 ? 0.5898 0.5055 0.4460 0.1322  -0.0945 0.0009  370 LYS C C   
11173 O O   . LYS C 370 ? 0.5618 0.4552 0.3863 0.1418  -0.0973 0.0091  370 LYS C O   
11174 C CB  . LYS C 370 ? 0.5263 0.4552 0.4204 0.1421  -0.1083 -0.0149 370 LYS C CB  
11175 C CG  . LYS C 370 ? 0.6847 0.5992 0.5609 0.1629  -0.1252 -0.0138 370 LYS C CG  
11176 C CD  . LYS C 370 ? 0.8291 0.7152 0.6964 0.1741  -0.1271 -0.0094 370 LYS C CD  
11177 C CE  . LYS C 370 ? 0.8911 0.7944 0.7937 0.1726  -0.1267 -0.0215 370 LYS C CE  
11178 N NZ  . LYS C 370 ? 0.9465 0.8215 0.8428 0.1732  -0.1184 -0.0164 370 LYS C NZ  
11179 N N   . LEU C 371 ? 0.5363 0.4801 0.4132 0.1208  -0.0923 -0.0060 371 LEU C N   
11180 C CA  . LEU C 371 ? 0.5383 0.4891 0.4038 0.1202  -0.0935 -0.0053 371 LEU C CA  
11181 C C   . LEU C 371 ? 0.5564 0.4856 0.3953 0.1177  -0.0801 0.0073  371 LEU C C   
11182 O O   . LEU C 371 ? 0.5459 0.4593 0.3559 0.1268  -0.0831 0.0122  371 LEU C O   
11183 C CB  . LEU C 371 ? 0.4923 0.4733 0.3850 0.1069  -0.0918 -0.0139 371 LEU C CB  
11184 C CG  . LEU C 371 ? 0.4546 0.4434 0.3393 0.1041  -0.0913 -0.0140 371 LEU C CG  
11185 C CD1 . LEU C 371 ? 0.5116 0.5012 0.3838 0.1165  -0.1069 -0.0193 371 LEU C CD1 
11186 C CD2 . LEU C 371 ? 0.4852 0.4987 0.3962 0.0893  -0.0880 -0.0207 371 LEU C CD2 
11187 N N   . TYR C 372 ? 0.5570 0.4849 0.4050 0.1050  -0.0649 0.0124  372 TYR C N   
11188 C CA  . TYR C 372 ? 0.5849 0.4974 0.4138 0.1004  -0.0500 0.0231  372 TYR C CA  
11189 C C   . TYR C 372 ? 0.6812 0.5585 0.4741 0.1107  -0.0486 0.0330  372 TYR C C   
11190 O O   . TYR C 372 ? 0.6596 0.5217 0.4252 0.1134  -0.0421 0.0400  372 TYR C O   
11191 C CB  . TYR C 372 ? 0.5412 0.4616 0.3913 0.0841  -0.0359 0.0256  372 TYR C CB  
11192 C CG  . TYR C 372 ? 0.4523 0.4033 0.3315 0.0731  -0.0359 0.0182  372 TYR C CG  
11193 C CD1 . TYR C 372 ? 0.4751 0.4412 0.3556 0.0769  -0.0437 0.0122  372 TYR C CD1 
11194 C CD2 . TYR C 372 ? 0.4109 0.3734 0.3143 0.0586  -0.0291 0.0173  372 TYR C CD2 
11195 C CE1 . TYR C 372 ? 0.4567 0.4472 0.3611 0.0668  -0.0443 0.0062  372 TYR C CE1 
11196 C CE2 . TYR C 372 ? 0.3748 0.3623 0.3017 0.0486  -0.0306 0.0114  372 TYR C CE2 
11197 C CZ  . TYR C 372 ? 0.4157 0.4163 0.3426 0.0530  -0.0381 0.0062  372 TYR C CZ  
11198 O OH  . TYR C 372 ? 0.3442 0.3657 0.2915 0.0432  -0.0400 0.0011  372 TYR C OH  
11199 N N   . SER C 373 ? 0.6910 0.5531 0.4819 0.1167  -0.0545 0.0337  373 SER C N   
11200 C CA  . SER C 373 ? 0.7102 0.5348 0.4645 0.1269  -0.0551 0.0437  373 SER C CA  
11201 C C   . SER C 373 ? 0.7052 0.5204 0.4329 0.1427  -0.0699 0.0433  373 SER C C   
11202 O O   . SER C 373 ? 0.7683 0.5557 0.4580 0.1473  -0.0658 0.0528  373 SER C O   
11203 C CB  . SER C 373 ? 0.7289 0.5393 0.4892 0.1311  -0.0598 0.0434  373 SER C CB  
11204 O OG  . SER C 373 ? 0.7592 0.5867 0.5383 0.1417  -0.0777 0.0323  373 SER C OG  
11205 N N   . THR C 374 ? 0.6796 0.5171 0.4256 0.1502  -0.0871 0.0322  374 THR C N   
11206 C CA  . THR C 374 ? 0.7454 0.5767 0.4684 0.1642  -0.1032 0.0306  374 THR C CA  
11207 C C   . THR C 374 ? 0.7458 0.5777 0.4496 0.1598  -0.0954 0.0330  374 THR C C   
11208 O O   . THR C 374 ? 0.7766 0.5843 0.4418 0.1686  -0.0993 0.0388  374 THR C O   
11209 C CB  . THR C 374 ? 0.7255 0.5859 0.4781 0.1702  -0.1217 0.0167  374 THR C CB  
11210 O OG1 . THR C 374 ? 0.6979 0.5598 0.4718 0.1738  -0.1262 0.0132  374 THR C OG1 
11211 C CG2 . THR C 374 ? 0.7973 0.6494 0.5262 0.1856  -0.1413 0.0151  374 THR C CG2 
11212 N N   . LEU C 375 ? 0.6273 0.4848 0.3559 0.1466  -0.0846 0.0286  375 LEU C N   
11213 C CA  . LEU C 375 ? 0.6498 0.5077 0.3627 0.1429  -0.0754 0.0305  375 LEU C CA  
11214 C C   . LEU C 375 ? 0.6989 0.5267 0.3790 0.1409  -0.0581 0.0432  375 LEU C C   
11215 O O   . LEU C 375 ? 0.6876 0.5004 0.3359 0.1448  -0.0544 0.0466  375 LEU C O   
11216 C CB  . LEU C 375 ? 0.5980 0.4874 0.3459 0.1295  -0.0671 0.0241  375 LEU C CB  
11217 C CG  . LEU C 375 ? 0.5777 0.4961 0.3515 0.1290  -0.0814 0.0113  375 LEU C CG  
11218 C CD1 . LEU C 375 ? 0.5345 0.4789 0.3417 0.1144  -0.0724 0.0070  375 LEU C CD1 
11219 C CD2 . LEU C 375 ? 0.5880 0.5030 0.3394 0.1371  -0.0912 0.0076  375 LEU C CD2 
11220 N N   . GLU C 376 ? 0.6902 0.5078 0.3762 0.1341  -0.0467 0.0499  376 GLU C N   
11221 C CA  . GLU C 376 ? 0.8080 0.5978 0.4651 0.1296  -0.0284 0.0619  376 GLU C CA  
11222 C C   . GLU C 376 ? 0.8763 0.6281 0.4832 0.1425  -0.0352 0.0694  376 GLU C C   
11223 O O   . GLU C 376 ? 0.9304 0.6584 0.5039 0.1401  -0.0207 0.0780  376 GLU C O   
11224 C CB  . GLU C 376 ? 0.8738 0.6580 0.5465 0.1198  -0.0178 0.0670  376 GLU C CB  
11225 C CG  . GLU C 376 ? 0.8932 0.6920 0.5866 0.1029  0.0035  0.0695  376 GLU C CG  
11226 C CD  . GLU C 376 ? 0.9329 0.7206 0.6355 0.0930  0.0130  0.0751  376 GLU C CD  
11227 O OE1 . GLU C 376 ? 0.9352 0.7102 0.6363 0.0992  0.0015  0.0744  376 GLU C OE1 
11228 O OE2 . GLU C 376 ? 0.9620 0.7536 0.6740 0.0791  0.0315  0.0796  376 GLU C OE2 
11229 N N   . LYS C 377 ? 0.9051 0.6505 0.5059 0.1561  -0.0573 0.0660  377 LYS C N   
11230 C CA  . LYS C 377 ? 0.9697 0.6769 0.5231 0.1695  -0.0677 0.0734  377 LYS C CA  
11231 C C   . LYS C 377 ? 1.0222 0.7313 0.5558 0.1803  -0.0840 0.0680  377 LYS C C   
11232 O O   . LYS C 377 ? 1.1108 0.7923 0.6090 0.1935  -0.0994 0.0720  377 LYS C O   
11233 C CB  . LYS C 377 ? 0.9820 0.6761 0.5401 0.1791  -0.0825 0.0745  377 LYS C CB  
11234 C CG  . LYS C 377 ? 1.0224 0.6966 0.5803 0.1705  -0.0668 0.0834  377 LYS C CG  
11235 C CD  . LYS C 377 ? 1.0609 0.7199 0.6222 0.1819  -0.0824 0.0835  377 LYS C CD  
11236 C CE  . LYS C 377 ? 1.0356 0.7343 0.6494 0.1820  -0.0923 0.0696  377 LYS C CE  
11237 N NZ  . LYS C 377 ? 1.0892 0.7786 0.7052 0.1994  -0.1140 0.0662  377 LYS C NZ  
11238 N N   . GLU C 378 ? 0.9393 0.6782 0.4931 0.1749  -0.0819 0.0590  378 GLU C N   
11239 C CA  . GLU C 378 ? 0.8753 0.6153 0.4093 0.1832  -0.0960 0.0532  378 GLU C CA  
11240 C C   . GLU C 378 ? 0.8485 0.5743 0.3515 0.1776  -0.0770 0.0578  378 GLU C C   
11241 O O   . GLU C 378 ? 0.8727 0.6211 0.3995 0.1673  -0.0619 0.0538  378 GLU C O   
11242 C CB  . GLU C 378 ? 0.8060 0.5869 0.3828 0.1816  -0.1084 0.0389  378 GLU C CB  
11243 C CG  . GLU C 378 ? 0.8560 0.6524 0.4638 0.1874  -0.1264 0.0329  378 GLU C CG  
11244 C CD  . GLU C 378 ? 0.9914 0.7789 0.5813 0.2032  -0.1526 0.0294  378 GLU C CD  
11245 O OE1 . GLU C 378 ? 1.0048 0.8124 0.6258 0.2084  -0.1683 0.0213  378 GLU C OE1 
11246 O OE2 . GLU C 378 ? 1.0109 0.7719 0.5563 0.2103  -0.1577 0.0343  378 GLU C OE2 
11247 N N   . GLU C 379 ? 0.8907 0.5780 0.3399 0.1847  -0.0775 0.0661  379 GLU C N   
11248 C CA  . GLU C 379 ? 0.9024 0.5729 0.3190 0.1789  -0.0563 0.0707  379 GLU C CA  
11249 C C   . GLU C 379 ? 0.9331 0.6238 0.3550 0.1787  -0.0580 0.0600  379 GLU C C   
11250 O O   . GLU C 379 ? 0.9526 0.6432 0.3669 0.1718  -0.0370 0.0603  379 GLU C O   
11251 C CB  . GLU C 379 ? 0.9500 0.5714 0.3025 0.1863  -0.0575 0.0816  379 GLU C CB  
11252 N N   . TRP C 380 ? 0.8843 0.5923 0.3198 0.1858  -0.0822 0.0500  380 TRP C N   
11253 C CA  . TRP C 380 ? 0.8672 0.5903 0.3038 0.1857  -0.0861 0.0396  380 TRP C CA  
11254 C C   . TRP C 380 ? 0.8400 0.6032 0.3299 0.1759  -0.0788 0.0310  380 TRP C C   
11255 O O   . TRP C 380 ? 0.8491 0.6251 0.3431 0.1749  -0.0810 0.0222  380 TRP C O   
11256 C CB  . TRP C 380 ? 0.8618 0.5881 0.2982 0.1933  -0.1134 0.0313  380 TRP C CB  
11257 C CG  . TRP C 380 ? 0.8772 0.6247 0.3510 0.1966  -0.1316 0.0274  380 TRP C CG  
11258 C CD1 . TRP C 380 ? 0.9344 0.6688 0.4070 0.2023  -0.1389 0.0340  380 TRP C CD1 
11259 C CD2 . TRP C 380 ? 0.8649 0.6500 0.3838 0.1938  -0.1434 0.0155  380 TRP C CD2 
11260 N NE1 . TRP C 380 ? 0.9329 0.6958 0.4482 0.2043  -0.1542 0.0262  380 TRP C NE1 
11261 C CE2 . TRP C 380 ? 0.8919 0.6867 0.4362 0.1982  -0.1567 0.0148  380 TRP C CE2 
11262 C CE3 . TRP C 380 ? 0.8503 0.6605 0.3903 0.1874  -0.1433 0.0051  380 TRP C CE3 
11263 C CZ2 . TRP C 380 ? 0.8245 0.6547 0.4149 0.1956  -0.1682 0.0037  380 TRP C CZ2 
11264 C CZ3 . TRP C 380 ? 0.8317 0.6751 0.4160 0.1839  -0.1554 -0.0051 380 TRP C CZ3 
11265 C CH2 . TRP C 380 ? 0.8279 0.6818 0.4372 0.1875  -0.1669 -0.0059 380 TRP C CH2 
11266 N N   . ILE C 381 ? 0.7881 0.5688 0.3162 0.1687  -0.0712 0.0333  381 ILE C N   
11267 C CA  . ILE C 381 ? 0.7288 0.5443 0.3049 0.1584  -0.0635 0.0268  381 ILE C CA  
11268 C C   . ILE C 381 ? 0.7533 0.5673 0.3359 0.1489  -0.0368 0.0341  381 ILE C C   
11269 O O   . ILE C 381 ? 0.7822 0.5809 0.3575 0.1467  -0.0278 0.0434  381 ILE C O   
11270 C CB  . ILE C 381 ? 0.6491 0.4885 0.2662 0.1564  -0.0769 0.0221  381 ILE C CB  
11271 C CG1 . ILE C 381 ? 0.7135 0.5620 0.3320 0.1641  -0.1020 0.0124  381 ILE C CG1 
11272 C CG2 . ILE C 381 ? 0.6007 0.4708 0.2629 0.1439  -0.0664 0.0179  381 ILE C CG2 
11273 C CD1 . ILE C 381 ? 0.6705 0.5392 0.3242 0.1642  -0.1157 0.0073  381 ILE C CD1 
11274 N N   . GLU C 382 ? 0.7722 0.6020 0.3693 0.1434  -0.0246 0.0297  382 GLU C N   
11275 C CA  . GLU C 382 ? 0.7671 0.6045 0.3818 0.1338  -0.0006 0.0344  382 GLU C CA  
11276 C C   . GLU C 382 ? 0.6887 0.5615 0.3540 0.1257  -0.0019 0.0277  382 GLU C C   
11277 O O   . GLU C 382 ? 0.6517 0.5382 0.3266 0.1266  -0.0066 0.0195  382 GLU C O   
11278 C CB  . GLU C 382 ? 0.7849 0.6084 0.3716 0.1353  0.0171  0.0354  382 GLU C CB  
11279 C CG  . GLU C 382 ? 0.8455 0.6771 0.4504 0.1259  0.0431  0.0402  382 GLU C CG  
11280 C CD  . GLU C 382 ? 0.9622 0.7788 0.5376 0.1282  0.0624  0.0405  382 GLU C CD  
11281 O OE1 . GLU C 382 ? 0.9877 0.8200 0.5868 0.1218  0.0823  0.0403  382 GLU C OE1 
11282 O OE2 . GLU C 382 ? 0.9860 0.7752 0.5147 0.1363  0.0575  0.0407  382 GLU C OE2 
11283 N N   . THR C 383 ? 0.5983 0.4833 0.2933 0.1174  0.0017  0.0312  383 THR C N   
11284 C CA  . THR C 383 ? 0.5736 0.4892 0.3131 0.1085  0.0020  0.0260  383 THR C CA  
11285 C C   . THR C 383 ? 0.5720 0.4954 0.3220 0.1034  0.0223  0.0279  383 THR C C   
11286 O O   . THR C 383 ? 0.6071 0.5166 0.3417 0.1018  0.0399  0.0352  383 THR C O   
11287 C CB  . THR C 383 ? 0.5490 0.4747 0.3158 0.1007  -0.0014 0.0282  383 THR C CB  
11288 O OG1 . THR C 383 ? 0.5776 0.4888 0.3367 0.0961  0.0140  0.0379  383 THR C OG1 
11289 C CG2 . THR C 383 ? 0.5120 0.4337 0.2735 0.1069  -0.0212 0.0245  383 THR C CG2 
11290 N N   . LEU C 384 ? 0.5071 0.4521 0.2828 0.1011  0.0198  0.0210  384 LEU C N   
11291 C CA  . LEU C 384 ? 0.5048 0.4601 0.2943 0.0986  0.0365  0.0209  384 LEU C CA  
11292 C C   . LEU C 384 ? 0.4660 0.4487 0.3013 0.0886  0.0362  0.0198  384 LEU C C   
11293 O O   . LEU C 384 ? 0.4518 0.4462 0.3049 0.0849  0.0206  0.0158  384 LEU C O   
11294 C CB  . LEU C 384 ? 0.5137 0.4664 0.2891 0.1069  0.0332  0.0133  384 LEU C CB  
11295 C CG  . LEU C 384 ? 0.5541 0.4792 0.2814 0.1169  0.0307  0.0127  384 LEU C CG  
11296 C CD1 . LEU C 384 ? 0.5585 0.4830 0.2762 0.1235  0.0251  0.0036  384 LEU C CD1 
11297 C CD2 . LEU C 384 ? 0.5906 0.4971 0.2931 0.1175  0.0525  0.0204  384 LEU C CD2 
11298 N N   . THR C 385 ? 0.4774 0.4704 0.3315 0.0838  0.0537  0.0230  385 THR C N   
11299 C CA  . THR C 385 ? 0.4709 0.4903 0.3667 0.0770  0.0519  0.0203  385 THR C CA  
11300 C C   . THR C 385 ? 0.4842 0.5099 0.3831 0.0839  0.0445  0.0122  385 THR C C   
11301 O O   . THR C 385 ? 0.5061 0.5164 0.3758 0.0934  0.0446  0.0088  385 THR C O   
11302 C CB  . THR C 385 ? 0.4388 0.4698 0.3569 0.0706  0.0718  0.0252  385 THR C CB  
11303 O OG1 . THR C 385 ? 0.4650 0.4903 0.3692 0.0783  0.0876  0.0238  385 THR C OG1 
11304 C CG2 . THR C 385 ? 0.4785 0.4992 0.3895 0.0627  0.0806  0.0334  385 THR C CG2 
11305 N N   . LEU C 386 ? 0.4358 0.4822 0.3686 0.0788  0.0372  0.0093  386 LEU C N   
11306 C CA  . LEU C 386 ? 0.3919 0.4432 0.3302 0.0848  0.0312  0.0024  386 LEU C CA  
11307 C C   . LEU C 386 ? 0.4141 0.4630 0.3479 0.0931  0.0490  0.0015  386 LEU C C   
11308 O O   . LEU C 386 ? 0.4499 0.4892 0.3665 0.1023  0.0474  -0.0045 386 LEU C O   
11309 C CB  . LEU C 386 ? 0.3615 0.4335 0.3368 0.0772  0.0212  0.0011  386 LEU C CB  
11310 C CG  . LEU C 386 ? 0.3468 0.4214 0.3266 0.0685  0.0035  0.0000  386 LEU C CG  
11311 C CD1 . LEU C 386 ? 0.3157 0.4079 0.3282 0.0602  -0.0052 -0.0005 386 LEU C CD1 
11312 C CD2 . LEU C 386 ? 0.4149 0.4763 0.3688 0.0736  -0.0098 -0.0063 386 LEU C CD2 
11313 N N   . GLU C 387 ? 0.4192 0.4773 0.3695 0.0893  0.0669  0.0067  387 GLU C N   
11314 C CA  . GLU C 387 ? 0.4896 0.5480 0.4388 0.0963  0.0869  0.0052  387 GLU C CA  
11315 C C   . GLU C 387 ? 0.4974 0.5285 0.3990 0.1043  0.0953  0.0046  387 GLU C C   
11316 O O   . GLU C 387 ? 0.5077 0.5316 0.3959 0.1137  0.1036  -0.0008 387 GLU C O   
11317 C CB  . GLU C 387 ? 0.6374 0.7122 0.6146 0.0882  0.1048  0.0110  387 GLU C CB  
11318 C CG  . GLU C 387 ? 0.8331 0.9259 0.8383 0.0928  0.1202  0.0076  387 GLU C CG  
11319 C CD  . GLU C 387 ? 0.9895 1.0996 1.0225 0.0833  0.1387  0.0130  387 GLU C CD  
11320 O OE1 . GLU C 387 ? 0.9935 1.1260 1.0651 0.0745  0.1310  0.0151  387 GLU C OE1 
11321 O OE2 . GLU C 387 ? 1.1016 1.2021 1.1166 0.0837  0.1608  0.0151  387 GLU C OE2 
11322 N N   . GLU C 388 ? 0.5420 0.5559 0.4161 0.1011  0.0928  0.0099  388 GLU C N   
11323 C CA  . GLU C 388 ? 0.5666 0.5517 0.3915 0.1085  0.0972  0.0100  388 GLU C CA  
11324 C C   . GLU C 388 ? 0.5680 0.5424 0.3717 0.1169  0.0792  0.0021  388 GLU C C   
11325 O O   . GLU C 388 ? 0.6091 0.5655 0.3807 0.1253  0.0850  -0.0018 388 GLU C O   
11326 C CB  . GLU C 388 ? 0.5698 0.5385 0.3723 0.1038  0.0956  0.0180  388 GLU C CB  
11327 C CG  . GLU C 388 ? 0.6308 0.6042 0.4467 0.0946  0.1156  0.0260  388 GLU C CG  
11328 C CD  . GLU C 388 ? 0.7353 0.6920 0.5330 0.0891  0.1119  0.0341  388 GLU C CD  
11329 O OE1 . GLU C 388 ? 0.6750 0.6288 0.4701 0.0899  0.0913  0.0333  388 GLU C OE1 
11330 O OE2 . GLU C 388 ? 0.7922 0.7376 0.5778 0.0841  0.1305  0.0412  388 GLU C OE2 
11331 N N   . ALA C 389 ? 0.5451 0.5299 0.3658 0.1137  0.0580  -0.0007 389 ALA C N   
11332 C CA  . ALA C 389 ? 0.5547 0.5312 0.3586 0.1195  0.0409  -0.0087 389 ALA C CA  
11333 C C   . ALA C 389 ? 0.6188 0.5986 0.4297 0.1258  0.0460  -0.0158 389 ALA C C   
11334 O O   . ALA C 389 ? 0.6324 0.5959 0.4153 0.1331  0.0409  -0.0222 389 ALA C O   
11335 C CB  . ALA C 389 ? 0.5509 0.5396 0.3743 0.1128  0.0197  -0.0105 389 ALA C CB  
11336 N N   . MET C 390 ? 0.6238 0.6237 0.4718 0.1234  0.0553  -0.0149 390 MET C N   
11337 C CA  . MET C 390 ? 0.6229 0.6257 0.4803 0.1310  0.0599  -0.0218 390 MET C CA  
11338 C C   . MET C 390 ? 0.6915 0.6782 0.5209 0.1399  0.0802  -0.0241 390 MET C C   
11339 O O   . MET C 390 ? 0.7200 0.6950 0.5335 0.1487  0.0803  -0.0319 390 MET C O   
11340 C CB  . MET C 390 ? 0.6532 0.6826 0.5592 0.1271  0.0638  -0.0201 390 MET C CB  
11341 C CG  . MET C 390 ? 0.7373 0.7706 0.6581 0.1357  0.0637  -0.0274 390 MET C CG  
11342 S SD  . MET C 390 ? 0.7778 0.8430 0.7564 0.1334  0.0703  -0.0249 390 MET C SD  
11343 C CE  . MET C 390 ? 0.7735 0.8528 0.7701 0.1172  0.0611  -0.0158 390 MET C CE  
11344 N N   . ARG C 391 ? 0.6432 0.6272 0.4645 0.1372  0.0983  -0.0176 391 ARG C N   
11345 C CA  . ARG C 391 ? 0.6708 0.6425 0.4703 0.1439  0.1220  -0.0194 391 ARG C CA  
11346 C C   . ARG C 391 ? 0.7003 0.6398 0.4429 0.1469  0.1238  -0.0182 391 ARG C C   
11347 O O   . ARG C 391 ? 0.7468 0.6709 0.4627 0.1523  0.1430  -0.0205 391 ARG C O   
11348 C CB  . ARG C 391 ? 0.6957 0.6857 0.5242 0.1380  0.1448  -0.0136 391 ARG C CB  
11349 C CG  . ARG C 391 ? 0.7301 0.7525 0.6154 0.1364  0.1445  -0.0155 391 ARG C CG  
11350 C CD  . ARG C 391 ? 0.8053 0.8491 0.7241 0.1251  0.1552  -0.0076 391 ARG C CD  
11351 N NE  . ARG C 391 ? 0.8894 0.9476 0.8297 0.1268  0.1816  -0.0091 391 ARG C NE  
11352 C CZ  . ARG C 391 ? 0.9791 1.0266 0.8977 0.1242  0.2058  -0.0060 391 ARG C CZ  
11353 N NH1 . ARG C 391 ? 1.0261 1.0457 0.8984 0.1207  0.2052  -0.0003 391 ARG C NH1 
11354 N NH2 . ARG C 391 ? 1.0008 1.0650 0.9438 0.1252  0.2307  -0.0086 391 ARG C NH2 
11355 N N   . LYS C 392 ? 0.6777 0.6066 0.4011 0.1437  0.1044  -0.0150 392 LYS C N   
11356 C CA  . LYS C 392 ? 0.7477 0.6459 0.4176 0.1469  0.1030  -0.0130 392 LYS C CA  
11357 C C   . LYS C 392 ? 0.8447 0.7225 0.4797 0.1565  0.1017  -0.0223 392 LYS C C   
11358 O O   . LYS C 392 ? 0.8575 0.7411 0.5039 0.1597  0.0879  -0.0303 392 LYS C O   
11359 C CB  . LYS C 392 ? 0.7004 0.5954 0.3642 0.1433  0.0790  -0.0095 392 LYS C CB  
11360 C CG  . LYS C 392 ? 0.8168 0.6813 0.4288 0.1466  0.0747  -0.0057 392 LYS C CG  
11361 C CD  . LYS C 392 ? 0.9006 0.7540 0.4987 0.1426  0.0946  0.0046  392 LYS C CD  
11362 C CE  . LYS C 392 ? 0.8609 0.7255 0.4831 0.1347  0.0875  0.0126  392 LYS C CE  
11363 N NZ  . LYS C 392 ? 0.8761 0.7266 0.4823 0.1298  0.1076  0.0226  392 LYS C NZ  
11364 N N   . GLU C 393 ? 0.9125 0.7640 0.5024 0.1605  0.1167  -0.0215 393 GLU C N   
11365 C CA  . GLU C 393 ? 0.9336 0.7641 0.4886 0.1692  0.1189  -0.0310 393 GLU C CA  
11366 C C   . GLU C 393 ? 0.9514 0.7541 0.4569 0.1723  0.0985  -0.0327 393 GLU C C   
11367 O O   . GLU C 393 ? 0.9323 0.7257 0.4229 0.1774  0.0865  -0.0421 393 GLU C O   
11368 C CB  . GLU C 393 ? 1.0504 0.8689 0.5856 0.1721  0.1504  -0.0315 393 GLU C CB  
11369 C CG  . GLU C 393 ? 1.1967 0.9964 0.7026 0.1816  0.1584  -0.0431 393 GLU C CG  
11370 C CD  . GLU C 393 ? 1.2585 1.0651 0.7809 0.1864  0.1378  -0.0532 393 GLU C CD  
11371 O OE1 . GLU C 393 ? 1.2996 1.0807 0.7811 0.1922  0.1310  -0.0612 393 GLU C OE1 
11372 O OE2 . GLU C 393 ? 1.2134 1.0483 0.7865 0.1839  0.1287  -0.0532 393 GLU C OE2 
11373 N N   . ASP C 394 ? 1.0125 0.8013 0.4930 0.1694  0.0928  -0.0240 394 ASP C N   
11374 C CA  . ASP C 394 ? 1.0661 0.8290 0.5002 0.1732  0.0721  -0.0253 394 ASP C CA  
11375 C C   . ASP C 394 ? 1.0127 0.7919 0.4710 0.1716  0.0422  -0.0290 394 ASP C C   
11376 O O   . ASP C 394 ? 1.0286 0.8010 0.4731 0.1712  0.0237  -0.0251 394 ASP C O   
11377 C CB  . ASP C 394 ? 1.1783 0.9186 0.5765 0.1718  0.0754  -0.0143 394 ASP C CB  
11378 C CG  . ASP C 394 ? 1.2269 0.9865 0.6619 0.1643  0.0815  -0.0041 394 ASP C CG  
11379 O OD1 . ASP C 394 ? 1.2509 0.9952 0.6647 0.1630  0.0755  0.0049  394 ASP C OD1 
11380 O OD2 . ASP C 394 ? 1.2146 1.0034 0.6990 0.1599  0.0914  -0.0051 394 ASP C OD2 
11381 N N   . VAL C 395 ? 0.9244 0.7244 0.4185 0.1707  0.0373  -0.0367 395 VAL C N   
11382 C CA  . VAL C 395 ? 0.8584 0.6736 0.3749 0.1677  0.0114  -0.0415 395 VAL C CA  
11383 C C   . VAL C 395 ? 0.8613 0.6683 0.3660 0.1714  0.0043  -0.0534 395 VAL C C   
11384 O O   . VAL C 395 ? 0.9148 0.7097 0.4044 0.1765  0.0209  -0.0579 395 VAL C O   
11385 C CB  . VAL C 395 ? 0.7378 0.5858 0.3113 0.1604  0.0103  -0.0383 395 VAL C CB  
11386 C CG1 . VAL C 395 ? 0.7601 0.6145 0.3449 0.1560  0.0179  -0.0270 395 VAL C CG1 
11387 C CG2 . VAL C 395 ? 0.6747 0.5350 0.2754 0.1611  0.0262  -0.0418 395 VAL C CG2 
11388 N N   . LYS C 396 ? 0.8136 0.6269 0.3256 0.1684  -0.0200 -0.0591 396 LYS C N   
11389 C CA  . LYS C 396 ? 0.8078 0.6123 0.3088 0.1701  -0.0294 -0.0707 396 LYS C CA  
11390 C C   . LYS C 396 ? 0.8013 0.6266 0.3461 0.1664  -0.0279 -0.0742 396 LYS C C   
11391 O O   . LYS C 396 ? 0.7150 0.5647 0.2999 0.1601  -0.0305 -0.0691 396 LYS C O   
11392 C CB  . LYS C 396 ? 0.8010 0.6005 0.2854 0.1676  -0.0565 -0.0757 396 LYS C CB  
11393 C CG  . LYS C 396 ? 0.8298 0.6219 0.3110 0.1650  -0.0663 -0.0862 396 LYS C CG  
11394 C CD  . LYS C 396 ? 0.8224 0.6039 0.2884 0.1602  -0.0822 -0.0874 396 LYS C CD  
11395 C CE  . LYS C 396 ? 0.7929 0.5815 0.2770 0.1519  -0.0977 -0.0959 396 LYS C CE  
11396 N NZ  . LYS C 396 ? 0.8372 0.6082 0.2978 0.1496  -0.1052 -0.1006 396 LYS C NZ  
11397 N N   . THR C 397 ? 0.3808 0.6625 0.4101 0.1332  -0.1004 0.0080  397 THR C N   
11398 C CA  . THR C 397 ? 0.4432 0.6911 0.4558 0.1390  -0.1016 0.0049  397 THR C CA  
11399 C C   . THR C 397 ? 0.4336 0.6926 0.4132 0.1360  -0.1168 -0.0176 397 THR C C   
11400 O O   . THR C 397 ? 0.4389 0.7262 0.4000 0.1299  -0.1253 -0.0315 397 THR C O   
11401 C CB  . THR C 397 ? 0.5579 0.7788 0.5591 0.1533  -0.0934 0.0140  397 THR C CB  
11402 O OG1 . THR C 397 ? 0.5815 0.7798 0.6117 0.1453  -0.0832 0.0298  397 THR C OG1 
11403 C CG2 . THR C 397 ? 0.6141 0.8026 0.5825 0.1661  -0.0966 0.0071  397 THR C CG2 
11404 N N   . GLU C 398 ? 0.4670 0.6973 0.4332 0.1350  -0.1214 -0.0240 398 GLU C N   
11405 C CA  . GLU C 398 ? 0.4872 0.6847 0.4138 0.1116  -0.1205 -0.0479 398 GLU C CA  
11406 C C   . GLU C 398 ? 0.4539 0.5828 0.3580 0.1138  -0.1105 -0.0466 398 GLU C C   
11407 O O   . GLU C 398 ? 0.4513 0.5712 0.3773 0.1247  -0.1097 -0.0318 398 GLU C O   
11408 C CB  . GLU C 398 ? 0.5116 0.7370 0.4534 0.0830  -0.1237 -0.0605 398 GLU C CB  
11409 C CG  . GLU C 398 ? 0.6412 0.8317 0.5462 0.0518  -0.1193 -0.0854 398 GLU C CG  
11410 C CD  . GLU C 398 ? 0.8517 1.0488 0.7253 0.0459  -0.1238 -0.1006 398 GLU C CD  
11411 O OE1 . GLU C 398 ? 0.8973 1.1556 0.7884 0.0439  -0.1349 -0.1015 398 GLU C OE1 
11412 O OE2 . GLU C 398 ? 0.9255 1.0657 0.7551 0.0445  -0.1161 -0.1111 398 GLU C OE2 
11413 N N   . VAL C 399 ? 0.4734 0.5530 0.3327 0.1038  -0.1029 -0.0619 399 VAL C N   
11414 C CA  . VAL C 399 ? 0.5270 0.5396 0.3613 0.1047  -0.0920 -0.0612 399 VAL C CA  
11415 C C   . VAL C 399 ? 0.5744 0.5639 0.3972 0.0733  -0.0873 -0.0780 399 VAL C C   
11416 O O   . VAL C 399 ? 0.6434 0.6434 0.4531 0.0482  -0.0885 -0.0977 399 VAL C O   
11417 C CB  . VAL C 399 ? 0.5976 0.5633 0.3882 0.1154  -0.0830 -0.0658 399 VAL C CB  
11418 C CG1 . VAL C 399 ? 0.5870 0.4841 0.3520 0.1162  -0.0708 -0.0643 399 VAL C CG1 
11419 C CG2 . VAL C 399 ? 0.5663 0.5554 0.3702 0.1481  -0.0854 -0.0467 399 VAL C CG2 
11420 N N   . ILE C 400 ? 0.5443 0.5038 0.3722 0.0742  -0.0824 -0.0699 400 ILE C N   
11421 C CA  . ILE C 400 ? 0.6322 0.5644 0.4487 0.0476  -0.0751 -0.0822 400 ILE C CA  
11422 C C   . ILE C 400 ? 0.6258 0.4845 0.4061 0.0521  -0.0627 -0.0806 400 ILE C C   
11423 O O   . ILE C 400 ? 0.6374 0.4781 0.4192 0.0777  -0.0626 -0.0632 400 ILE C O   
11424 C CB  . ILE C 400 ? 0.6317 0.5980 0.4864 0.0444  -0.0795 -0.0734 400 ILE C CB  
11425 C CG1 . ILE C 400 ? 0.7430 0.6795 0.5851 0.0188  -0.0696 -0.0839 400 ILE C CG1 
11426 C CG2 . ILE C 400 ? 0.5825 0.5453 0.4559 0.0716  -0.0832 -0.0516 400 ILE C CG2 
11427 C CD1 . ILE C 400 ? 0.7515 0.7181 0.6268 0.0169  -0.0715 -0.0757 400 ILE C CD1 
11428 N N   . GLU C 401 ? 0.6059 0.4227 0.3541 0.0277  -0.0519 -0.0979 401 GLU C N   
11429 C CA  . GLU C 401 ? 0.7035 0.4474 0.4132 0.0327  -0.0380 -0.0966 401 GLU C CA  
11430 C C   . GLU C 401 ? 0.7402 0.4539 0.4483 0.0242  -0.0305 -0.0919 401 GLU C C   
11431 O O   . GLU C 401 ? 0.7564 0.4206 0.4435 0.0387  -0.0225 -0.0813 401 GLU C O   
11432 C CB  . GLU C 401 ? 0.7473 0.4503 0.4144 0.0138  -0.0277 -0.1182 401 GLU C CB  
11433 C CG  . GLU C 401 ? 0.8655 0.5796 0.5192 0.0271  -0.0316 -0.1224 401 GLU C CG  
11434 C CD  . GLU C 401 ? 0.9499 0.6431 0.5983 0.0641  -0.0285 -0.1017 401 GLU C CD  
11435 O OE1 . GLU C 401 ? 1.0334 0.6655 0.6528 0.0723  -0.0150 -0.0971 401 GLU C OE1 
11436 O OE2 . GLU C 401 ? 0.9468 0.6862 0.6223 0.0856  -0.0389 -0.0885 401 GLU C OE2 
11437 N N   . SER C 402 ? 0.7249 0.4681 0.4542 0.0027  -0.0323 -0.0981 402 SER C N   
11438 C CA  . SER C 402 ? 0.6866 0.3995 0.4100 -0.0072 -0.0228 -0.0951 402 SER C CA  
11439 C C   . SER C 402 ? 0.6811 0.4479 0.4438 -0.0147 -0.0297 -0.0919 402 SER C C   
11440 O O   . SER C 402 ? 0.6330 0.4535 0.4210 -0.0264 -0.0372 -0.0997 402 SER C O   
11441 C CB  . SER C 402 ? 0.7376 0.4030 0.4277 -0.0356 -0.0071 -0.1125 402 SER C CB  
11442 O OG  . SER C 402 ? 0.8189 0.4521 0.5009 -0.0431 0.0040  -0.1076 402 SER C OG  
11443 N N   . VAL C 403 ? 0.6376 0.3903 0.4040 -0.0066 -0.0272 -0.0798 403 VAL C N   
11444 C CA  . VAL C 403 ? 0.6551 0.4462 0.4508 -0.0157 -0.0284 -0.0781 403 VAL C CA  
11445 C C   . VAL C 403 ? 0.6995 0.4485 0.4735 -0.0330 -0.0124 -0.0815 403 VAL C C   
11446 O O   . VAL C 403 ? 0.7714 0.4607 0.5097 -0.0310 -0.0024 -0.0802 403 VAL C O   
11447 C CB  . VAL C 403 ? 0.6206 0.4388 0.4425 0.0092  -0.0400 -0.0612 403 VAL C CB  
11448 C CG1 . VAL C 403 ? 0.5496 0.4106 0.3955 0.0261  -0.0540 -0.0562 403 VAL C CG1 
11449 C CG2 . VAL C 403 ? 0.6866 0.4538 0.4846 0.0266  -0.0382 -0.0486 403 VAL C CG2 
11450 N N   . LYS C 404 ? 0.6736 0.4551 0.4701 -0.0493 -0.0084 -0.0848 404 LYS C N   
11451 C CA  . LYS C 404 ? 0.7352 0.4841 0.5166 -0.0631 0.0078  -0.0848 404 LYS C CA  
11452 C C   . LYS C 404 ? 0.6708 0.4217 0.4590 -0.0431 0.0051  -0.0701 404 LYS C C   
11453 O O   . LYS C 404 ? 0.5932 0.3942 0.4147 -0.0353 -0.0037 -0.0657 404 LYS C O   
11454 C CB  . LYS C 404 ? 0.7824 0.5640 0.5840 -0.0938 0.0161  -0.0966 404 LYS C CB  
11455 C CG  . LYS C 404 ? 0.8401 0.6098 0.6284 -0.1187 0.0196  -0.1136 404 LYS C CG  
11456 C CD  . LYS C 404 ? 0.8783 0.6440 0.6693 -0.1522 0.0354  -0.1232 404 LYS C CD  
11457 C CE  . LYS C 404 ? 0.9044 0.6522 0.6790 -0.1788 0.0378  -0.1419 404 LYS C CE  
11458 N NZ  . LYS C 404 ? 0.9188 0.6831 0.7096 -0.2156 0.0486  -0.1523 404 LYS C NZ  
11459 N N   . ALA C 405 ? 0.7266 0.4218 0.4815 -0.0343 0.0126  -0.0625 405 ALA C N   
11460 C CA  . ALA C 405 ? 0.7113 0.4010 0.4648 -0.0138 0.0073  -0.0493 405 ALA C CA  
11461 C C   . ALA C 405 ? 0.6752 0.3968 0.4499 -0.0213 0.0134  -0.0494 405 ALA C C   
11462 O O   . ALA C 405 ? 0.7554 0.4788 0.5313 -0.0432 0.0289  -0.0562 405 ALA C O   
11463 C CB  . ALA C 405 ? 0.7581 0.3819 0.4680 -0.0060 0.0155  -0.0418 405 ALA C CB  
11464 N N   . GLY C 406 ? 0.6193 0.3643 0.4110 -0.0030 0.0024  -0.0411 406 GLY C N   
11465 C CA  . GLY C 406 ? 0.6315 0.4039 0.4414 -0.0058 0.0094  -0.0399 406 GLY C CA  
11466 C C   . GLY C 406 ? 0.6004 0.3897 0.4243 0.0168  -0.0043 -0.0313 406 GLY C C   
11467 O O   . GLY C 406 ? 0.6067 0.3796 0.4221 0.0340  -0.0189 -0.0250 406 GLY C O   
11468 N N   . THR C 407 ? 0.5231 0.3451 0.3696 0.0163  0.0014  -0.0306 407 THR C N   
11469 C CA  . THR C 407 ? 0.5604 0.3997 0.4225 0.0355  -0.0085 -0.0239 407 THR C CA  
11470 C C   . THR C 407 ? 0.5410 0.4425 0.4478 0.0323  -0.0059 -0.0248 407 THR C C   
11471 O O   . THR C 407 ? 0.5754 0.5052 0.4984 0.0143  0.0038  -0.0303 407 THR C O   
11472 C CB  . THR C 407 ? 0.5783 0.3813 0.4117 0.0422  0.0000  -0.0206 407 THR C CB  
11473 O OG1 . THR C 407 ? 0.5188 0.3359 0.3585 0.0284  0.0209  -0.0237 407 THR C OG1 
11474 C CG2 . THR C 407 ? 0.7092 0.4511 0.4953 0.0442  -0.0002 -0.0187 407 THR C CG2 
11475 N N   . TRP C 408 ? 0.4849 0.4073 0.4115 0.0495  -0.0138 -0.0188 408 TRP C N   
11476 C CA  . TRP C 408 ? 0.4526 0.4330 0.4211 0.0498  -0.0092 -0.0171 408 TRP C CA  
11477 C C   . TRP C 408 ? 0.4933 0.4769 0.4613 0.0433  0.0114  -0.0173 408 TRP C C   
11478 O O   . TRP C 408 ? 0.5044 0.5341 0.5065 0.0469  0.0174  -0.0136 408 TRP C O   
11479 C CB  . TRP C 408 ? 0.4599 0.4605 0.4515 0.0709  -0.0222 -0.0096 408 TRP C CB  
11480 C CG  . TRP C 408 ? 0.5127 0.4730 0.4819 0.0860  -0.0247 -0.0060 408 TRP C CG  
11481 C CD1 . TRP C 408 ? 0.5149 0.4229 0.4422 0.0846  -0.0175 -0.0084 408 TRP C CD1 
11482 C CD2 . TRP C 408 ? 0.5069 0.4746 0.4927 0.1043  -0.0356 0.0003  408 TRP C CD2 
11483 N NE1 . TRP C 408 ? 0.5220 0.4055 0.4375 0.1001  -0.0251 -0.0054 408 TRP C NE1 
11484 C CE2 . TRP C 408 ? 0.5373 0.4555 0.4891 0.1115  -0.0360 -0.0004 408 TRP C CE2 
11485 C CE3 . TRP C 408 ? 0.4694 0.4796 0.4945 0.1150  -0.0450 0.0066  408 TRP C CE3 
11486 C CZ2 . TRP C 408 ? 0.4812 0.3899 0.4378 0.1269  -0.0462 0.0035  408 TRP C CZ2 
11487 C CZ3 . TRP C 408 ? 0.4582 0.4586 0.4899 0.1313  -0.0531 0.0121  408 TRP C CZ3 
11488 C CH2 . TRP C 408 ? 0.4862 0.4355 0.4841 0.1360  -0.0541 0.0098  408 TRP C CH2 
11489 N N   . PHE C 409 ? 0.5241 0.4602 0.4544 0.0357  0.0236  -0.0199 409 PHE C N   
11490 C CA  . PHE C 409 ? 0.5664 0.5050 0.4951 0.0271  0.0465  -0.0196 409 PHE C CA  
11491 C C   . PHE C 409 ? 0.5864 0.5326 0.5180 0.0015  0.0567  -0.0253 409 PHE C C   
11492 O O   . PHE C 409 ? 0.5628 0.4616 0.4589 -0.0076 0.0606  -0.0286 409 PHE C O   
11493 C CB  . PHE C 409 ? 0.5880 0.4686 0.4714 0.0366  0.0550  -0.0178 409 PHE C CB  
11494 C CG  . PHE C 409 ? 0.6598 0.5471 0.5447 0.0357  0.0791  -0.0150 409 PHE C CG  
11495 C CD1 . PHE C 409 ? 0.7132 0.6057 0.5996 0.0161  0.0993  -0.0159 409 PHE C CD1 
11496 C CD2 . PHE C 409 ? 0.7063 0.5943 0.5920 0.0543  0.0828  -0.0111 409 PHE C CD2 
11497 C CE1 . PHE C 409 ? 0.7507 0.6518 0.6411 0.0162  0.1234  -0.0115 409 PHE C CE1 
11498 C CE2 . PHE C 409 ? 0.7485 0.6416 0.6343 0.0556  0.1074  -0.0077 409 PHE C CE2 
11499 C CZ  . PHE C 409 ? 0.7689 0.6703 0.6582 0.0371  0.1280  -0.0070 409 PHE C CZ  
11500 N N   . ASP C 410 ? 0.6063 0.6127 0.5808 -0.0104 0.0601  -0.0262 410 ASP C N   
11501 C CA  . ASP C 410 ? 0.6659 0.6895 0.6513 -0.0380 0.0695  -0.0323 410 ASP C CA  
11502 C C   . ASP C 410 ? 0.6435 0.6395 0.6081 -0.0501 0.0581  -0.0410 410 ASP C C   
11503 O O   . ASP C 410 ? 0.6757 0.6688 0.6385 -0.0746 0.0665  -0.0480 410 ASP C O   
11504 C CB  . ASP C 410 ? 0.7306 0.7279 0.6986 -0.0496 0.0948  -0.0306 410 ASP C CB  
11505 C CG  . ASP C 410 ? 0.7933 0.8277 0.7885 -0.0413 0.1106  -0.0221 410 ASP C CG  
11506 O OD1 . ASP C 410 ? 0.7866 0.8554 0.8065 -0.0229 0.1017  -0.0173 410 ASP C OD1 
11507 O OD2 . ASP C 410 ? 0.8268 0.8546 0.8185 -0.0519 0.1335  -0.0192 410 ASP C OD2 
11508 N N   . GLY C 411 ? 0.5777 0.5527 0.5272 -0.0335 0.0401  -0.0405 411 GLY C N   
11509 C CA  . GLY C 411 ? 0.5865 0.5316 0.5137 -0.0413 0.0314  -0.0473 411 GLY C CA  
11510 C C   . GLY C 411 ? 0.6473 0.5234 0.5277 -0.0471 0.0422  -0.0487 411 GLY C C   
11511 O O   . GLY C 411 ? 0.7080 0.5582 0.5702 -0.0581 0.0408  -0.0552 411 GLY C O   
11512 N N   . ASN C 412 ? 0.6420 0.4856 0.4998 -0.0390 0.0538  -0.0425 412 ASN C N   
11513 C CA  . ASN C 412 ? 0.6903 0.4686 0.5017 -0.0428 0.0653  -0.0416 412 ASN C CA  
11514 C C   . ASN C 412 ? 0.6832 0.4256 0.4651 -0.0198 0.0630  -0.0331 412 ASN C C   
11515 O O   . ASN C 412 ? 0.6804 0.4451 0.4775 -0.0026 0.0515  -0.0293 412 ASN C O   
11516 C CB  . ASN C 412 ? 0.7208 0.4958 0.5322 -0.0675 0.0893  -0.0447 412 ASN C CB  
11517 C CG  . ASN C 412 ? 0.7138 0.5209 0.5469 -0.0664 0.1034  -0.0396 412 ASN C CG  
11518 O OD1 . ASN C 412 ? 0.7626 0.5494 0.5768 -0.0479 0.1068  -0.0326 412 ASN C OD1 
11519 N ND2 . ASN C 412 ? 0.6558 0.5133 0.5281 -0.0865 0.1120  -0.0429 412 ASN C ND2 
11520 N N   . PHE C 413 ? 0.6936 0.3785 0.4313 -0.0200 0.0739  -0.0301 413 PHE C N   
11521 C CA  . PHE C 413 ? 0.6670 0.3101 0.3674 0.0005  0.0695  -0.0226 413 PHE C CA  
11522 C C   . PHE C 413 ? 0.6963 0.3190 0.3745 -0.0007 0.0911  -0.0191 413 PHE C C   
11523 O O   . PHE C 413 ? 0.7498 0.3278 0.3861 0.0128  0.0912  -0.0136 413 PHE C O   
11524 C CB  . PHE C 413 ? 0.7381 0.3286 0.3997 0.0061  0.0629  -0.0192 413 PHE C CB  
11525 C CG  . PHE C 413 ? 0.7409 0.3450 0.4185 0.0127  0.0420  -0.0203 413 PHE C CG  
11526 C CD1 . PHE C 413 ? 0.7348 0.3450 0.4164 0.0334  0.0202  -0.0149 413 PHE C CD1 
11527 C CD2 . PHE C 413 ? 0.7579 0.3672 0.4454 -0.0022 0.0448  -0.0267 413 PHE C CD2 
11528 C CE1 . PHE C 413 ? 0.7164 0.3404 0.4144 0.0405  0.0030  -0.0140 413 PHE C CE1 
11529 C CE2 . PHE C 413 ? 0.7082 0.3287 0.4078 0.0058  0.0275  -0.0271 413 PHE C CE2 
11530 C CZ  . PHE C 413 ? 0.6784 0.3072 0.3842 0.0278  0.0074  -0.0198 413 PHE C CZ  
11531 N N   . LEU C 414 ? 0.6929 0.3491 0.3984 -0.0159 0.1095  -0.0214 414 LEU C N   
11532 C CA  . LEU C 414 ? 0.8438 0.4777 0.5272 -0.0189 0.1346  -0.0168 414 LEU C CA  
11533 C C   . LEU C 414 ? 0.8547 0.4811 0.5217 0.0029  0.1339  -0.0125 414 LEU C C   
11534 O O   . LEU C 414 ? 0.8787 0.4694 0.5098 0.0071  0.1517  -0.0078 414 LEU C O   
11535 C CB  . LEU C 414 ? 0.8187 0.4959 0.5415 -0.0414 0.1544  -0.0190 414 LEU C CB  
11536 C CG  . LEU C 414 ? 0.8212 0.4927 0.5500 -0.0673 0.1603  -0.0244 414 LEU C CG  
11537 C CD1 . LEU C 414 ? 0.8225 0.5314 0.5861 -0.0916 0.1820  -0.0252 414 LEU C CD1 
11538 C CD2 . LEU C 414 ? 0.8327 0.4330 0.5079 -0.0664 0.1678  -0.0211 414 LEU C CD2 
11539 N N   . LYS C 415 ? 0.7604 0.4160 0.4500 0.0171  0.1145  -0.0140 415 LYS C N   
11540 C CA  . LYS C 415 ? 0.8191 0.4605 0.4889 0.0370  0.1134  -0.0115 415 LYS C CA  
11541 C C   . LYS C 415 ? 0.8631 0.4489 0.4814 0.0520  0.0978  -0.0096 415 LYS C C   
11542 O O   . LYS C 415 ? 0.7544 0.3217 0.3493 0.0677  0.0939  -0.0092 415 LYS C O   
11543 C CB  . LYS C 415 ? 0.7953 0.4866 0.5089 0.0463  0.1011  -0.0131 415 LYS C CB  
11544 C CG  . LYS C 415 ? 0.8334 0.5702 0.5831 0.0419  0.1226  -0.0114 415 LYS C CG  
11545 C CD  . LYS C 415 ? 0.9713 0.6780 0.6876 0.0533  0.1433  -0.0081 415 LYS C CD  
11546 C CE  . LYS C 415 ? 1.0284 0.7604 0.7643 0.0412  0.1746  -0.0037 415 LYS C CE  
11547 N NZ  . LYS C 415 ? 1.0077 0.8008 0.7959 0.0452  0.1815  -0.0009 415 LYS C NZ  
11548 N N   . TRP C 416 ? 0.8176 0.3757 0.4166 0.0478  0.0888  -0.0083 416 TRP C N   
11549 C CA  . TRP C 416 ? 0.8590 0.3679 0.4106 0.0622  0.0739  -0.0043 416 TRP C CA  
11550 C C   . TRP C 416 ? 0.8922 0.3533 0.4018 0.0567  0.0866  0.0009  416 TRP C C   
11551 O O   . TRP C 416 ? 0.9067 0.3259 0.3728 0.0693  0.0762  0.0061  416 TRP C O   
11552 C CB  . TRP C 416 ? 0.7633 0.2852 0.3335 0.0702  0.0438  -0.0043 416 TRP C CB  
11553 C CG  . TRP C 416 ? 0.7465 0.3118 0.3570 0.0771  0.0305  -0.0078 416 TRP C CG  
11554 C CD1 . TRP C 416 ? 0.7444 0.3027 0.3459 0.0921  0.0159  -0.0080 416 TRP C CD1 
11555 C CD2 . TRP C 416 ? 0.7068 0.3275 0.3716 0.0692  0.0311  -0.0112 416 TRP C CD2 
11556 N NE1 . TRP C 416 ? 0.6544 0.2586 0.3026 0.0946  0.0090  -0.0105 416 TRP C NE1 
11557 C CE2 . TRP C 416 ? 0.6409 0.2856 0.3282 0.0817  0.0181  -0.0117 416 TRP C CE2 
11558 C CE3 . TRP C 416 ? 0.6655 0.3177 0.3611 0.0523  0.0407  -0.0139 416 TRP C CE3 
11559 C CZ2 . TRP C 416 ? 0.5768 0.2764 0.3160 0.0799  0.0156  -0.0130 416 TRP C CZ2 
11560 C CZ3 . TRP C 416 ? 0.5922 0.3013 0.3385 0.0497  0.0361  -0.0164 416 TRP C CZ3 
11561 C CH2 . TRP C 416 ? 0.5962 0.3288 0.3638 0.0644  0.0242  -0.0150 416 TRP C CH2 
11562 N N   . ILE C 417 ? 0.9064 0.3725 0.4277 0.0380  0.1083  0.0002  417 ILE C N   
11563 C CA  . ILE C 417 ? 0.9907 0.4100 0.4751 0.0315  0.1224  0.0055  417 ILE C CA  
11564 C C   . ILE C 417 ? 1.0037 0.4362 0.5076 0.0087  0.1511  0.0035  417 ILE C C   
11565 O O   . ILE C 417 ? 1.0075 0.4900 0.5602 -0.0048 0.1525  -0.0030 417 ILE C O   
11566 C CB  . ILE C 417 ? 0.9711 0.3765 0.4534 0.0331  0.1047  0.0068  417 ILE C CB  
11567 C CG1 . ILE C 417 ? 1.0454 0.3930 0.4802 0.0331  0.1180  0.0151  417 ILE C CG1 
11568 C CG2 . ILE C 417 ? 0.9155 0.3634 0.4473 0.0166  0.1017  -0.0014 417 ILE C CG2 
11569 C CD1 . ILE C 417 ? 1.0820 0.4040 0.4969 0.0476  0.0973  0.0214  417 ILE C CD1 
11570 N N   . GLY C 418 ? 1.0421 0.4309 0.5083 0.0043  0.1741  0.0101  418 GLY C N   
11571 C CA  . GLY C 418 ? 1.0473 0.4429 0.5312 -0.0199 0.2015  0.0094  418 GLY C CA  
11572 C C   . GLY C 418 ? 1.1670 0.5573 0.6394 -0.0219 0.2302  0.0152  418 GLY C C   
11573 O O   . GLY C 418 ? 1.2390 0.6313 0.7248 -0.0429 0.2550  0.0166  418 GLY C O   
11574 N N   . ASN C 419 ? 1.1858 0.5691 0.6344 -0.0017 0.2291  0.0185  419 ASN C N   
11575 C CA  . ASN C 419 ? 1.2443 0.6112 0.6701 0.0001  0.2590  0.0258  419 ASN C CA  
11576 C C   . ASN C 419 ? 1.2977 0.6020 0.6525 0.0210  0.2585  0.0337  419 ASN C C   
11577 O O   . ASN C 419 ? 1.2777 0.5607 0.6081 0.0348  0.2321  0.0330  419 ASN C O   
11578 C CB  . ASN C 419 ? 1.2395 0.6529 0.6972 0.0054  0.2645  0.0231  419 ASN C CB  
11579 C CG  . ASN C 419 ? 1.2440 0.6539 0.6829 0.0303  0.2410  0.0194  419 ASN C CG  
11580 O OD1 . ASN C 419 ? 1.2538 0.6222 0.6474 0.0451  0.2232  0.0204  419 ASN C OD1 
11581 N ND2 . ASN C 419 ? 1.2476 0.7014 0.7219 0.0347  0.2417  0.0158  419 ASN C ND2 
11582 N N   . LYS C 420 ? 1.3484 0.6256 0.6711 0.0234  0.2881  0.0422  420 LYS C N   
11583 C CA  . LYS C 420 ? 1.4394 0.6545 0.6901 0.0415  0.2920  0.0514  420 LYS C CA  
11584 C C   . LYS C 420 ? 1.4152 0.6185 0.6348 0.0654  0.2601  0.0473  420 LYS C C   
11585 O O   . LYS C 420 ? 1.4057 0.5730 0.5864 0.0765  0.2418  0.0513  420 LYS C O   
11586 C CB  . LYS C 420 ? 1.5439 0.7414 0.7686 0.0440  0.3286  0.0602  420 LYS C CB  
11587 C CG  . LYS C 420 ? 1.5744 0.8073 0.8507 0.0191  0.3593  0.0622  420 LYS C CG  
11588 C CD  . LYS C 420 ? 1.5822 0.8469 0.8763 0.0243  0.3794  0.0630  420 LYS C CD  
11589 C CE  . LYS C 420 ? 1.5532 0.8693 0.9139 -0.0022 0.4025  0.0642  420 LYS C CE  
11590 N NZ  . LYS C 420 ? 1.5397 0.8870 0.9188 0.0043  0.4266  0.0685  420 LYS C NZ  
11591 N N   . GLU C 421 ? 1.4330 0.6676 0.6717 0.0729  0.2529  0.0396  421 GLU C N   
11592 C CA  . GLU C 421 ? 1.5043 0.7219 0.7074 0.0947  0.2280  0.0353  421 GLU C CA  
11593 C C   . GLU C 421 ? 1.4219 0.6568 0.6482 0.0968  0.1892  0.0292  421 GLU C C   
11594 O O   . GLU C 421 ? 1.4732 0.6783 0.6599 0.1111  0.1654  0.0304  421 GLU C O   
11595 C CB  . GLU C 421 ? 1.5934 0.8341 0.8084 0.1017  0.2385  0.0297  421 GLU C CB  
11596 C CG  . GLU C 421 ? 1.6378 0.9418 0.9289 0.0862  0.2447  0.0250  421 GLU C CG  
11597 C CD  . GLU C 421 ? 1.7308 1.0524 1.0465 0.0702  0.2825  0.0318  421 GLU C CD  
11598 O OE1 . GLU C 421 ? 1.7811 1.0790 1.0832 0.0585  0.2969  0.0389  421 GLU C OE1 
11599 O OE2 . GLU C 421 ? 1.7434 1.1039 1.0949 0.0692  0.2979  0.0307  421 GLU C OE2 
11600 N N   . LYS C 422 ? 1.2649 0.5493 0.5552 0.0830  0.1821  0.0234  422 LYS C N   
11601 C CA  . LYS C 422 ? 1.1781 0.4788 0.4918 0.0847  0.1486  0.0195  422 LYS C CA  
11602 C C   . LYS C 422 ? 1.1758 0.4439 0.4663 0.0831  0.1423  0.0268  422 LYS C C   
11603 O O   . LYS C 422 ? 1.1728 0.4314 0.4527 0.0939  0.1144  0.0281  422 LYS C O   
11604 C CB  . LYS C 422 ? 1.1074 0.4680 0.4914 0.0712  0.1450  0.0124  422 LYS C CB  
11605 C CG  . LYS C 422 ? 1.1186 0.5154 0.5305 0.0755  0.1494  0.0068  422 LYS C CG  
11606 C CD  . LYS C 422 ? 1.0483 0.5001 0.5215 0.0579  0.1643  0.0043  422 LYS C CD  
11607 C CE  . LYS C 422 ? 0.9640 0.4658 0.4847 0.0628  0.1489  -0.0015 422 LYS C CE  
11608 N NZ  . LYS C 422 ? 0.9900 0.4895 0.4984 0.0791  0.1534  -0.0029 422 LYS C NZ  
11609 N N   . ASN C 423 ? 1.1703 0.4201 0.4533 0.0703  0.1686  0.0325  423 ASN C N   
11610 C CA  . ASN C 423 ? 1.1846 0.3949 0.4382 0.0713  0.1668  0.0411  423 ASN C CA  
11611 C C   . ASN C 423 ? 1.2860 0.4611 0.4862 0.0923  0.1544  0.0458  423 ASN C C   
11612 O O   . ASN C 423 ? 1.3142 0.4903 0.5143 0.0990  0.1353  0.0454  423 ASN C O   
11613 C CB  . ASN C 423 ? 1.2217 0.4145 0.4740 0.0534  0.2009  0.0461  423 ASN C CB  
11614 C CG  . ASN C 423 ? 1.1837 0.4137 0.4932 0.0302  0.2045  0.0382  423 ASN C CG  
11615 O OD1 . ASN C 423 ? 1.1834 0.4465 0.5282 0.0298  0.1809  0.0308  423 ASN C OD1 
11616 N ND2 . ASN C 423 ? 1.1645 0.3892 0.4830 0.0103  0.2343  0.0398  423 ASN C ND2 
11617 N N   . GLU C 424 ? 1.2982 0.4571 0.4653 0.1020  0.1640  0.0460  424 GLU C N   
11618 C CA  . GLU C 424 ? 1.3402 0.4761 0.4692 0.1201  0.1496  0.0450  424 GLU C CA  
11619 C C   . GLU C 424 ? 1.2716 0.4252 0.4090 0.1309  0.1102  0.0386  424 GLU C C   
11620 O O   . GLU C 424 ? 1.2181 0.3649 0.3421 0.1405  0.0920  0.0389  424 GLU C O   
11621 C CB  . GLU C 424 ? 1.4509 0.5663 0.5472 0.1278  0.1678  0.0453  424 GLU C CB  
11622 C CG  . GLU C 424 ? 1.5671 0.6512 0.6202 0.1444  0.1591  0.0466  424 GLU C CG  
11623 C CD  . GLU C 424 ? 1.7454 0.8059 0.7821 0.1430  0.1790  0.0550  424 GLU C CD  
11624 O OE1 . GLU C 424 ? 1.7784 0.8434 0.8364 0.1276  0.2027  0.0591  424 GLU C OE1 
11625 O OE2 . GLU C 424 ? 1.8163 0.8538 0.8194 0.1565  0.1714  0.0577  424 GLU C OE2 
11626 N N   . TYR C 425 ? 1.2354 0.4148 0.3990 0.1287  0.0971  0.0338  425 TYR C N   
11627 C CA  . TYR C 425 ? 1.1977 0.3995 0.3789 0.1363  0.0601  0.0277  425 TYR C CA  
11628 C C   . TYR C 425 ? 1.1967 0.4210 0.4086 0.1324  0.0451  0.0299  425 TYR C C   
11629 O O   . TYR C 425 ? 1.2062 0.4388 0.4199 0.1402  0.0209  0.0287  425 TYR C O   
11630 C CB  . TYR C 425 ? 1.1167 0.3429 0.3254 0.1345  0.0517  0.0232  425 TYR C CB  
11631 C CG  . TYR C 425 ? 1.1901 0.4009 0.3686 0.1452  0.0466  0.0172  425 TYR C CG  
11632 C CD1 . TYR C 425 ? 1.2763 0.4528 0.4110 0.1525  0.0595  0.0177  425 TYR C CD1 
11633 C CD2 . TYR C 425 ? 1.2212 0.4560 0.4250 0.1476  0.0294  0.0098  425 TYR C CD2 
11634 C CE1 . TYR C 425 ? 1.3241 0.4884 0.4377 0.1613  0.0544  0.0124  425 TYR C CE1 
11635 C CE2 . TYR C 425 ? 1.3005 0.5210 0.4779 0.1563  0.0258  0.0022  425 TYR C CE2 
11636 C CZ  . TYR C 425 ? 1.3450 0.5320 0.4813 0.1624  0.0378  0.0049  425 TYR C CZ  
11637 O OH  . TYR C 425 ? 1.3512 0.5294 0.4718 0.1695  0.0331  -0.0007 425 TYR C OH  
11638 N N   . TRP C 426 ? 1.1834 0.4184 0.4221 0.1198  0.0603  0.0335  426 TRP C N   
11639 C CA  . TRP C 426 ? 1.1453 0.3984 0.4104 0.1169  0.0502  0.0358  426 TRP C CA  
11640 C C   . TRP C 426 ? 1.1528 0.3813 0.3873 0.1244  0.0539  0.0411  426 TRP C C   
11641 O O   . TRP C 426 ? 1.1434 0.3867 0.3893 0.1315  0.0339  0.0428  426 TRP C O   
11642 C CB  . TRP C 426 ? 1.1123 0.3732 0.4062 0.1008  0.0684  0.0369  426 TRP C CB  
11643 C CG  . TRP C 426 ? 1.0222 0.3159 0.3577 0.0959  0.0573  0.0316  426 TRP C CG  
11644 C CD1 . TRP C 426 ? 1.0141 0.3124 0.3621 0.0887  0.0709  0.0276  426 TRP C CD1 
11645 C CD2 . TRP C 426 ? 0.9259 0.2589 0.3023 0.0987  0.0311  0.0289  426 TRP C CD2 
11646 N NE1 . TRP C 426 ? 0.9442 0.2893 0.3422 0.0868  0.0534  0.0205  426 TRP C NE1 
11647 C CE2 . TRP C 426 ? 0.9666 0.3215 0.3751 0.0942  0.0292  0.0235  426 TRP C CE2 
11648 C CE3 . TRP C 426 ? 0.9072 0.2603 0.2995 0.1049  0.0112  0.0307  426 TRP C CE3 
11649 C CZ2 . TRP C 426 ? 0.9650 0.3610 0.4182 0.0960  0.0074  0.0205  426 TRP C CZ2 
11650 C CZ3 . TRP C 426 ? 0.9192 0.3136 0.3570 0.1055  -0.0088 0.0281  426 TRP C CZ3 
11651 C CH2 . TRP C 426 ? 0.9309 0.3462 0.3974 0.1012  -0.0109 0.0234  426 TRP C CH2 
11652 N N   . LYS C 427 ? 1.1707 0.3631 0.3685 0.1237  0.0803  0.0449  427 LYS C N   
11653 C CA  . LYS C 427 ? 1.2531 0.4207 0.4210 0.1328  0.0848  0.0509  427 LYS C CA  
11654 C C   . LYS C 427 ? 1.2751 0.4430 0.4252 0.1483  0.0586  0.0496  427 LYS C C   
11655 O O   . LYS C 427 ? 1.3350 0.5071 0.4857 0.1560  0.0455  0.0545  427 LYS C O   
11656 C CB  . LYS C 427 ? 1.3367 0.4673 0.4713 0.1294  0.1188  0.0553  427 LYS C CB  
11657 C CG  . LYS C 427 ? 1.4379 0.5478 0.5598 0.1304  0.1336  0.0631  427 LYS C CG  
11658 C CD  . LYS C 427 ? 1.5654 0.6425 0.6628 0.1241  0.1696  0.0676  427 LYS C CD  
11659 C CE  . LYS C 427 ? 1.5751 0.6614 0.6966 0.1047  0.1898  0.0641  427 LYS C CE  
11660 N NZ  . LYS C 427 ? 1.6358 0.6955 0.7401 0.0972  0.2258  0.0692  427 LYS C NZ  
11661 N N   . ILE C 428 ? 1.2871 0.4499 0.4216 0.1526  0.0515  0.0435  428 ILE C N   
11662 C CA  . ILE C 428 ? 1.2688 0.4336 0.3912 0.1641  0.0234  0.0402  428 ILE C CA  
11663 C C   . ILE C 428 ? 1.2118 0.4166 0.3775 0.1632  -0.0054 0.0394  428 ILE C C   
11664 O O   . ILE C 428 ? 1.1993 0.4100 0.3638 0.1706  -0.0241 0.0431  428 ILE C O   
11665 C CB  . ILE C 428 ? 1.2728 0.4277 0.3785 0.1666  0.0202  0.0320  428 ILE C CB  
11666 C CG1 . ILE C 428 ? 1.3156 0.4312 0.3766 0.1705  0.0485  0.0347  428 ILE C CG1 
11667 C CG2 . ILE C 428 ? 1.2338 0.3953 0.3363 0.1745  -0.0127 0.0268  428 ILE C CG2 
11668 C CD1 . ILE C 428 ? 1.2887 0.3991 0.3436 0.1698  0.0572  0.0289  428 ILE C CD1 
11669 N N   . LEU C 429 ? 1.1793 0.4146 0.3866 0.1539  -0.0084 0.0360  429 LEU C N   
11670 C CA  . LEU C 429 ? 1.1218 0.3984 0.3754 0.1527  -0.0335 0.0357  429 LEU C CA  
11671 C C   . LEU C 429 ? 1.0981 0.3826 0.3654 0.1540  -0.0307 0.0450  429 LEU C C   
11672 O O   . LEU C 429 ? 1.1007 0.4087 0.3901 0.1585  -0.0506 0.0489  429 LEU C O   
11673 C CB  . LEU C 429 ? 1.0820 0.3887 0.3761 0.1436  -0.0354 0.0306  429 LEU C CB  
11674 C CG  . LEU C 429 ? 1.0396 0.3928 0.3875 0.1416  -0.0583 0.0303  429 LEU C CG  
11675 C CD1 . LEU C 429 ? 1.0879 0.4519 0.4404 0.1464  -0.0843 0.0259  429 LEU C CD1 
11676 C CD2 . LEU C 429 ? 1.0340 0.4136 0.4194 0.1329  -0.0540 0.0272  429 LEU C CD2 
11677 N N   . ILE C 430 ? 1.0862 0.3510 0.3416 0.1496  -0.0048 0.0493  430 ILE C N   
11678 C CA  . ILE C 430 ? 1.1427 0.4094 0.4077 0.1514  0.0009  0.0579  430 ILE C CA  
11679 C C   . ILE C 430 ? 1.2582 0.5090 0.4958 0.1641  -0.0050 0.0660  430 ILE C C   
11680 O O   . ILE C 430 ? 1.2760 0.5451 0.5333 0.1697  -0.0162 0.0736  430 ILE C O   
11681 C CB  . ILE C 430 ? 1.1241 0.3669 0.3786 0.1420  0.0317  0.0595  430 ILE C CB  
11682 C CG1 . ILE C 430 ? 1.0573 0.3222 0.3467 0.1288  0.0344  0.0536  430 ILE C CG1 
11683 C CG2 . ILE C 430 ? 1.1255 0.3581 0.3774 0.1462  0.0408  0.0685  430 ILE C CG2 
11684 C CD1 . ILE C 430 ? 1.1010 0.3400 0.3755 0.1156  0.0642  0.0520  430 ILE C CD1 
11685 N N   . GLU C 431 ? 1.2886 0.5058 0.4809 0.1694  0.0033  0.0657  431 GLU C N   
11686 C CA  . GLU C 431 ? 1.3507 0.5536 0.5155 0.1822  -0.0038 0.0741  431 GLU C CA  
11687 C C   . GLU C 431 ? 1.3390 0.5708 0.5221 0.1871  -0.0370 0.0734  431 GLU C C   
11688 O O   . GLU C 431 ? 1.3589 0.6016 0.5470 0.1948  -0.0489 0.0835  431 GLU C O   
11689 C CB  . GLU C 431 ? 1.4347 0.5951 0.5462 0.1872  0.0133  0.0739  431 GLU C CB  
11690 C CG  . GLU C 431 ? 1.5151 0.6481 0.6120 0.1797  0.0484  0.0747  431 GLU C CG  
11691 C CD  . GLU C 431 ? 1.5665 0.6838 0.6563 0.1827  0.0660  0.0858  431 GLU C CD  
11692 O OE1 . GLU C 431 ? 1.5346 0.6722 0.6566 0.1796  0.0622  0.0888  431 GLU C OE1 
11693 O OE2 . GLU C 431 ? 1.6197 0.7029 0.6710 0.1888  0.0848  0.0917  431 GLU C OE2 
11694 N N   . ALA C 432 ? 1.3166 0.5623 0.5127 0.1819  -0.0515 0.0626  432 ALA C N   
11695 C CA  . ALA C 432 ? 1.2909 0.5631 0.5066 0.1840  -0.0823 0.0612  432 ALA C CA  
11696 C C   . ALA C 432 ? 1.2387 0.5558 0.5098 0.1812  -0.0952 0.0678  432 ALA C C   
11697 O O   . ALA C 432 ? 1.2335 0.5719 0.5195 0.1850  -0.1160 0.0743  432 ALA C O   
11698 C CB  . ALA C 432 ? 1.2823 0.5552 0.4991 0.1788  -0.0922 0.0478  432 ALA C CB  
11699 N N   . LYS C 433 ? 1.1445 0.4770 0.4466 0.1742  -0.0826 0.0670  433 LYS C N   
11700 C CA  . LYS C 433 ? 1.0995 0.4725 0.4530 0.1724  -0.0908 0.0740  433 LYS C CA  
11701 C C   . LYS C 433 ? 1.1665 0.5386 0.5164 0.1816  -0.0891 0.0892  433 LYS C C   
11702 O O   . LYS C 433 ? 1.1065 0.5132 0.4937 0.1835  -0.1030 0.0984  433 LYS C O   
11703 C CB  . LYS C 433 ? 1.1005 0.4826 0.4786 0.1641  -0.0751 0.0698  433 LYS C CB  
11704 C CG  . LYS C 433 ? 1.0646 0.4847 0.4927 0.1630  -0.0798 0.0769  433 LYS C CG  
11705 C CD  . LYS C 433 ? 0.9912 0.4541 0.4637 0.1596  -0.1020 0.0752  433 LYS C CD  
11706 C CE  . LYS C 433 ? 0.9003 0.4011 0.4229 0.1589  -0.1031 0.0837  433 LYS C CE  
11707 N NZ  . LYS C 433 ? 0.8628 0.4055 0.4284 0.1562  -0.1226 0.0858  433 LYS C NZ  
11708 N N   . LYS C 434 ? 1.2414 0.5751 0.5486 0.1874  -0.0704 0.0937  434 LYS C N   
11709 C CA  . LYS C 434 ? 1.3020 0.6315 0.6014 0.1979  -0.0683 0.1092  434 LYS C CA  
11710 C C   . LYS C 434 ? 1.3427 0.6925 0.6464 0.2045  -0.0942 0.1173  434 LYS C C   
11711 O O   . LYS C 434 ? 1.3453 0.7215 0.6764 0.2095  -0.1032 0.1314  434 LYS C O   
11712 C CB  . LYS C 434 ? 1.3975 0.6791 0.6446 0.2035  -0.0447 0.1120  434 LYS C CB  
11713 C CG  . LYS C 434 ? 1.4075 0.6670 0.6495 0.1963  -0.0164 0.1074  434 LYS C CG  
11714 C CD  . LYS C 434 ? 1.4781 0.6897 0.6680 0.1992  0.0076  0.1084  434 LYS C CD  
11715 C CE  . LYS C 434 ? 1.5082 0.6994 0.6835 0.2079  0.0242  0.1218  434 LYS C CE  
11716 N NZ  . LYS C 434 ? 1.5627 0.7462 0.7115 0.2227  0.0143  0.1341  434 LYS C NZ  
11717 N N   . LYS C 435 ? 1.4717 0.7196 0.6508 0.3620  -0.1186 -0.0060 435 LYS C N   
11718 C CA  . LYS C 435 ? 1.4875 0.7546 0.6751 0.3789  -0.1486 -0.0108 435 LYS C CA  
11719 C C   . LYS C 435 ? 1.4027 0.7259 0.6448 0.3716  -0.1706 -0.0168 435 LYS C C   
11720 O O   . LYS C 435 ? 1.4203 0.7539 0.6639 0.3750  -0.1911 -0.0215 435 LYS C O   
11721 C CB  . LYS C 435 ? 1.5436 0.7679 0.6761 0.3818  -0.1466 -0.0106 435 LYS C CB  
11722 C CG  . LYS C 435 ? 1.6115 0.7791 0.6887 0.3755  -0.1151 -0.0040 435 LYS C CG  
11723 C CD  . LYS C 435 ? 1.7031 0.8294 0.7274 0.3869  -0.1177 -0.0046 435 LYS C CD  
11724 C CE  . LYS C 435 ? 1.7929 0.8620 0.7623 0.3857  -0.0877 0.0025  435 LYS C CE  
11725 N NZ  . LYS C 435 ? 1.8744 0.9044 0.7960 0.4082  -0.0950 0.0034  435 LYS C NZ  
11726 N N   . ALA C 436 ? 1.2777 0.6350 0.5636 0.3610  -0.1660 -0.0169 436 ALA C N   
11727 C CA  . ALA C 436 ? 1.2212 0.6325 0.5597 0.3520  -0.1847 -0.0217 436 ALA C CA  
11728 C C   . ALA C 436 ? 1.2124 0.6706 0.6025 0.3682  -0.2091 -0.0261 436 ALA C C   
11729 O O   . ALA C 436 ? 1.1167 0.5754 0.5167 0.3826  -0.2046 -0.0246 436 ALA C O   
11730 C CB  . ALA C 436 ? 1.1778 0.6036 0.5384 0.3328  -0.1684 -0.0193 436 ALA C CB  
11731 N N   . LYS C 437 ? 1.1773 0.6758 0.6032 0.3647  -0.2336 -0.0319 437 LYS C N   
11732 C CA  . LYS C 437 ? 1.2007 0.7469 0.6799 0.3775  -0.2583 -0.0364 437 LYS C CA  
11733 C C   . LYS C 437 ? 1.0986 0.7065 0.6442 0.3640  -0.2715 -0.0410 437 LYS C C   
11734 O O   . LYS C 437 ? 1.0574 0.7101 0.6556 0.3725  -0.2893 -0.0444 437 LYS C O   
11735 C CB  . LYS C 437 ? 1.2980 0.8321 0.7578 0.3898  -0.2807 -0.0399 437 LYS C CB  
11736 C CG  . LYS C 437 ? 1.4196 0.8997 0.8208 0.4078  -0.2727 -0.0355 437 LYS C CG  
11737 C CD  . LYS C 437 ? 1.4704 0.8949 0.8054 0.3987  -0.2560 -0.0335 437 LYS C CD  
11738 C CE  . LYS C 437 ? 1.5114 0.8933 0.7944 0.4152  -0.2649 -0.0338 437 LYS C CE  
11739 N NZ  . LYS C 437 ? 1.5128 0.8327 0.7274 0.4106  -0.2383 -0.0291 437 LYS C NZ  
11740 N N   . ASN C 438 ? 1.0634 0.6764 0.6105 0.3430  -0.2630 -0.0408 438 ASN C N   
11741 C CA  . ASN C 438 ? 0.9883 0.6582 0.5963 0.3286  -0.2752 -0.0450 438 ASN C CA  
11742 C C   . ASN C 438 ? 0.9412 0.6126 0.5489 0.3097  -0.2551 -0.0414 438 ASN C C   
11743 O O   . ASN C 438 ? 0.9736 0.6055 0.5394 0.3034  -0.2295 -0.0372 438 ASN C O   
11744 C CB  . ASN C 438 ? 1.0331 0.7125 0.6465 0.3198  -0.2959 -0.0511 438 ASN C CB  
11745 C CG  . ASN C 438 ? 1.0643 0.6943 0.6178 0.3113  -0.2854 -0.0500 438 ASN C CG  
11746 O OD1 . ASN C 438 ? 1.0460 0.6713 0.5918 0.2945  -0.2703 -0.0472 438 ASN C OD1 
11747 N ND2 . ASN C 438 ? 1.1120 0.7050 0.6232 0.3233  -0.2929 -0.0518 438 ASN C ND2 
11748 N N   . ASP C 439 ? 0.8448 0.5683 0.5079 0.2900  -0.2585 -0.0455 439 ASP C N   
11749 C CA  . ASP C 439 ? 0.8596 0.6009 0.5410 0.2623  -0.2315 -0.0448 439 ASP C CA  
11750 C C   . ASP C 439 ? 0.8744 0.5892 0.5206 0.2444  -0.2222 -0.0427 439 ASP C C   
11751 O O   . ASP C 439 ? 0.8196 0.5498 0.4811 0.2212  -0.2026 -0.0417 439 ASP C O   
11752 C CB  . ASP C 439 ? 0.8730 0.6784 0.6264 0.2489  -0.2368 -0.0485 439 ASP C CB  
11753 C CG  . ASP C 439 ? 0.9465 0.7801 0.7371 0.2565  -0.2260 -0.0491 439 ASP C CG  
11754 O OD1 . ASP C 439 ? 1.0019 0.8037 0.7612 0.2694  -0.2119 -0.0470 439 ASP C OD1 
11755 O OD2 . ASP C 439 ? 0.9527 0.8383 0.8032 0.2496  -0.2300 -0.0515 439 ASP C OD2 
11756 N N   . TYR C 440 ? 0.9108 0.5859 0.5097 0.2553  -0.2354 -0.0419 440 TYR C N   
11757 C CA  . TYR C 440 ? 0.9470 0.5943 0.5110 0.2400  -0.2224 -0.0395 440 TYR C CA  
11758 C C   . TYR C 440 ? 0.9186 0.5293 0.4456 0.2334  -0.1912 -0.0339 440 TYR C C   
11759 O O   . TYR C 440 ? 0.8536 0.4511 0.3646 0.2165  -0.1747 -0.0314 440 TYR C O   
11760 C CB  . TYR C 440 ? 0.9557 0.5701 0.4809 0.2508  -0.2387 -0.0416 440 TYR C CB  
11761 C CG  . TYR C 440 ? 0.9927 0.6404 0.5549 0.2400  -0.2569 -0.0484 440 TYR C CG  
11762 C CD1 . TYR C 440 ? 0.9657 0.6156 0.5280 0.2215  -0.2490 -0.0479 440 TYR C CD1 
11763 C CD2 . TYR C 440 ? 1.0118 0.6878 0.6095 0.2476  -0.2813 -0.0552 440 TYR C CD2 
11764 C CE1 . TYR C 440 ? 0.9797 0.6553 0.5738 0.2118  -0.2644 -0.0540 440 TYR C CE1 
11765 C CE2 . TYR C 440 ? 1.0108 0.7133 0.6412 0.2361  -0.2970 -0.0613 440 TYR C CE2 
11766 C CZ  . TYR C 440 ? 1.0211 0.7215 0.6483 0.2185  -0.2882 -0.0607 440 TYR C CZ  
11767 O OH  . TYR C 440 ? 1.0291 0.7517 0.6869 0.2073  -0.3029 -0.0667 440 TYR C OH  
11768 N N   . ILE C 441 ? 0.8839 0.4776 0.3984 0.2465  -0.1830 -0.0320 441 ILE C N   
11769 C CA  . ILE C 441 ? 0.9129 0.4744 0.3985 0.2373  -0.1531 -0.0279 441 ILE C CA  
11770 C C   . ILE C 441 ? 0.8379 0.4377 0.3645 0.2102  -0.1353 -0.0296 441 ILE C C   
11771 O O   . ILE C 441 ? 0.8222 0.4035 0.3312 0.1935  -0.1128 -0.0269 441 ILE C O   
11772 C CB  . ILE C 441 ? 0.9701 0.5035 0.4342 0.2585  -0.1493 -0.0264 441 ILE C CB  
11773 C CG1 . ILE C 441 ? 1.0219 0.5034 0.4384 0.2521  -0.1211 -0.0216 441 ILE C CG1 
11774 C CG2 . ILE C 441 ? 0.9352 0.5129 0.4511 0.2589  -0.1490 -0.0307 441 ILE C CG2 
11775 C CD1 . ILE C 441 ? 1.1098 0.5358 0.4655 0.2606  -0.1196 -0.0157 441 ILE C CD1 
11776 N N   . LEU C 442 ? 0.7973 0.4504 0.3789 0.2051  -0.1453 -0.0336 442 LEU C N   
11777 C CA  . LEU C 442 ? 0.7810 0.4705 0.3990 0.1801  -0.1309 -0.0345 442 LEU C CA  
11778 C C   . LEU C 442 ? 0.7504 0.4473 0.3713 0.1613  -0.1297 -0.0326 442 LEU C C   
11779 O O   . LEU C 442 ? 0.7274 0.4330 0.3559 0.1406  -0.1125 -0.0310 442 LEU C O   
11780 C CB  . LEU C 442 ? 0.7370 0.4792 0.4109 0.1805  -0.1405 -0.0381 442 LEU C CB  
11781 C CG  . LEU C 442 ? 0.7886 0.5337 0.4718 0.2016  -0.1441 -0.0404 442 LEU C CG  
11782 C CD1 . LEU C 442 ? 0.7206 0.5217 0.4637 0.1969  -0.1470 -0.0433 442 LEU C CD1 
11783 C CD2 . LEU C 442 ? 0.8437 0.5517 0.4920 0.2035  -0.1217 -0.0396 442 LEU C CD2 
11784 N N   . VAL C 443 ? 0.8006 0.4941 0.4158 0.1687  -0.1484 -0.0333 443 VAL C N   
11785 C CA  . VAL C 443 ? 0.7823 0.4784 0.3974 0.1532  -0.1461 -0.0317 443 VAL C CA  
11786 C C   . VAL C 443 ? 0.8249 0.4801 0.3975 0.1466  -0.1241 -0.0270 443 VAL C C   
11787 O O   . VAL C 443 ? 0.7843 0.4497 0.3675 0.1276  -0.1108 -0.0246 443 VAL C O   
11788 C CB  . VAL C 443 ? 0.8104 0.5034 0.4206 0.1641  -0.1708 -0.0347 443 VAL C CB  
11789 C CG1 . VAL C 443 ? 0.7544 0.4567 0.3738 0.1476  -0.1682 -0.0340 443 VAL C CG1 
11790 C CG2 . VAL C 443 ? 0.8138 0.5443 0.4662 0.1724  -0.1938 -0.0396 443 VAL C CG2 
11791 N N   . ALA C 444 ? 0.8373 0.4459 0.3629 0.1624  -0.1197 -0.0251 444 ALA C N   
11792 C CA  . ALA C 444 ? 0.8898 0.4557 0.3739 0.1567  -0.0969 -0.0201 444 ALA C CA  
11793 C C   . ALA C 444 ? 0.8916 0.4635 0.3876 0.1389  -0.0743 -0.0190 444 ALA C C   
11794 O O   . ALA C 444 ? 0.8852 0.4310 0.3589 0.1281  -0.0540 -0.0151 444 ALA C O   
11795 C CB  . ALA C 444 ? 0.8855 0.3961 0.3130 0.1798  -0.0987 -0.0175 444 ALA C CB  
11796 N N   . GLU C 445 ? 0.8503 0.4550 0.3805 0.1351  -0.0768 -0.0226 445 GLU C N   
11797 C CA  . GLU C 445 ? 0.8284 0.4399 0.3689 0.1172  -0.0578 -0.0231 445 GLU C CA  
11798 C C   . GLU C 445 ? 0.7800 0.4329 0.3586 0.0934  -0.0543 -0.0228 445 GLU C C   
11799 O O   . GLU C 445 ? 0.7467 0.4071 0.3339 0.0765  -0.0407 -0.0234 445 GLU C O   
11800 C CB  . GLU C 445 ? 0.8432 0.4637 0.3948 0.1263  -0.0598 -0.0274 445 GLU C CB  
11801 C CG  . GLU C 445 ? 0.9048 0.4778 0.4150 0.1482  -0.0581 -0.0267 445 GLU C CG  
11802 C CD  . GLU C 445 ? 0.9875 0.5753 0.5147 0.1656  -0.0674 -0.0306 445 GLU C CD  
11803 O OE1 . GLU C 445 ? 0.9418 0.5771 0.5132 0.1587  -0.0729 -0.0340 445 GLU C OE1 
11804 O OE2 . GLU C 445 ? 1.0863 0.6377 0.5829 0.1866  -0.0680 -0.0298 445 GLU C OE2 
11805 N N   . GLY C 446 ? 0.8092 0.4864 0.4085 0.0920  -0.0669 -0.0218 446 GLY C N   
11806 C CA  . GLY C 446 ? 0.7738 0.4862 0.4062 0.0712  -0.0635 -0.0201 446 GLY C CA  
11807 C C   . GLY C 446 ? 0.7427 0.4379 0.3614 0.0560  -0.0447 -0.0162 446 GLY C C   
11808 O O   . GLY C 446 ? 0.7392 0.3973 0.3248 0.0620  -0.0367 -0.0136 446 GLY C O   
11809 N N   . SER C 447 ? 0.6822 0.4055 0.3274 0.0360  -0.0375 -0.0155 447 SER C N   
11810 C CA  . SER C 447 ? 0.6884 0.4017 0.3285 0.0194  -0.0206 -0.0124 447 SER C CA  
11811 C C   . SER C 447 ? 0.6720 0.3797 0.3107 0.0184  -0.0168 -0.0074 447 SER C C   
11812 O O   . SER C 447 ? 0.6828 0.3685 0.3071 0.0114  -0.0005 -0.0043 447 SER C O   
11813 C CB  . SER C 447 ? 0.6413 0.3907 0.3126 -0.0009 -0.0189 -0.0130 447 SER C CB  
11814 O OG  . SER C 447 ? 0.5967 0.3826 0.3001 -0.0058 -0.0288 -0.0097 447 SER C OG  
11815 N N   . ASP C 448 ? 0.6312 0.3580 0.2858 0.0247  -0.0304 -0.0066 448 ASP C N   
11816 C CA  . ASP C 448 ? 0.6602 0.3844 0.3164 0.0235  -0.0263 -0.0024 448 ASP C CA  
11817 C C   . ASP C 448 ? 0.7146 0.3911 0.3282 0.0336  -0.0135 -0.0005 448 ASP C C   
11818 O O   . ASP C 448 ? 0.6699 0.3390 0.2826 0.0269  0.0016  0.0039  448 ASP C O   
11819 C CB  . ASP C 448 ? 0.6265 0.3680 0.2974 0.0320  -0.0443 -0.0036 448 ASP C CB  
11820 C CG  . ASP C 448 ? 0.5835 0.3696 0.2953 0.0223  -0.0551 -0.0041 448 ASP C CG  
11821 O OD1 . ASP C 448 ? 0.5620 0.3573 0.2786 0.0267  -0.0637 -0.0079 448 ASP C OD1 
11822 O OD2 . ASP C 448 ? 0.5924 0.4031 0.3307 0.0112  -0.0537 0.0000  448 ASP C OD2 
11823 N N   . TRP C 449 ? 0.7224 0.3665 0.3007 0.0511  -0.0194 -0.0033 449 TRP C N   
11824 C CA  . TRP C 449 ? 0.7980 0.3918 0.3288 0.0628  -0.0077 -0.0007 449 TRP C CA  
11825 C C   . TRP C 449 ? 0.8300 0.4055 0.3523 0.0491  0.0178  0.0035  449 TRP C C   
11826 O O   . TRP C 449 ? 0.8178 0.3693 0.3220 0.0484  0.0349  0.0082  449 TRP C O   
11827 C CB  . TRP C 449 ? 0.8429 0.4056 0.3373 0.0842  -0.0200 -0.0037 449 TRP C CB  
11828 C CG  . TRP C 449 ? 0.8197 0.4096 0.3343 0.0945  -0.0469 -0.0090 449 TRP C CG  
11829 C CD1 . TRP C 449 ? 0.8291 0.4333 0.3559 0.1010  -0.0596 -0.0129 449 TRP C CD1 
11830 C CD2 . TRP C 449 ? 0.7781 0.3847 0.3061 0.0984  -0.0631 -0.0111 449 TRP C CD2 
11831 N NE1 . TRP C 449 ? 0.7780 0.4098 0.3287 0.1078  -0.0825 -0.0169 449 TRP C NE1 
11832 C CE2 . TRP C 449 ? 0.7437 0.3757 0.2941 0.1058  -0.0858 -0.0162 449 TRP C CE2 
11833 C CE3 . TRP C 449 ? 0.7768 0.3777 0.3000 0.0965  -0.0597 -0.0095 449 TRP C CE3 
11834 C CZ2 . TRP C 449 ? 0.7289 0.3808 0.2981 0.1094  -0.1061 -0.0199 449 TRP C CZ2 
11835 C CZ3 . TRP C 449 ? 0.7696 0.3872 0.3078 0.1012  -0.0799 -0.0136 449 TRP C CZ3 
11836 C CH2 . TRP C 449 ? 0.7294 0.3719 0.2905 0.1066  -0.1033 -0.0188 449 TRP C CH2 
11837 N N   . PHE C 450 ? 0.8643 0.4520 0.4017 0.0370  0.0215  0.0016  450 PHE C N   
11838 C CA  . PHE C 450 ? 0.8726 0.4434 0.4047 0.0216  0.0438  0.0041  450 PHE C CA  
11839 C C   . PHE C 450 ? 0.8106 0.4142 0.3814 0.0011  0.0533  0.0074  450 PHE C C   
11840 O O   . PHE C 450 ? 0.8477 0.4343 0.4138 -0.0086 0.0741  0.0117  450 PHE C O   
11841 C CB  . PHE C 450 ? 0.8453 0.4159 0.3783 0.0158  0.0425  -0.0008 450 PHE C CB  
11842 C CG  . PHE C 450 ? 0.8503 0.3926 0.3507 0.0379  0.0325  -0.0037 450 PHE C CG  
11843 C CD1 . PHE C 450 ? 0.7841 0.3530 0.3002 0.0498  0.0107  -0.0077 450 PHE C CD1 
11844 C CD2 . PHE C 450 ? 0.8895 0.3788 0.3450 0.0474  0.0450  -0.0016 450 PHE C CD2 
11845 C CE1 . PHE C 450 ? 0.8534 0.3998 0.3445 0.0712  0.0005  -0.0100 450 PHE C CE1 
11846 C CE2 . PHE C 450 ? 0.9092 0.3723 0.3350 0.0700  0.0345  -0.0034 450 PHE C CE2 
11847 C CZ  . PHE C 450 ? 0.8980 0.3914 0.3433 0.0823  0.0116  -0.0078 450 PHE C CZ  
11848 N N   . TRP C 451 ? 0.7633 0.4140 0.3739 -0.0052 0.0387  0.0062  451 TRP C N   
11849 C CA  . TRP C 451 ? 0.6826 0.3674 0.3322 -0.0217 0.0443  0.0102  451 TRP C CA  
11850 C C   . TRP C 451 ? 0.7254 0.3914 0.3650 -0.0168 0.0598  0.0159  451 TRP C C   
11851 O O   . TRP C 451 ? 0.7264 0.3943 0.3801 -0.0300 0.0780  0.0200  451 TRP C O   
11852 C CB  . TRP C 451 ? 0.6573 0.3874 0.3423 -0.0232 0.0249  0.0094  451 TRP C CB  
11853 C CG  . TRP C 451 ? 0.6507 0.4123 0.3723 -0.0346 0.0289  0.0148  451 TRP C CG  
11854 C CD1 . TRP C 451 ? 0.6317 0.4002 0.3626 -0.0267 0.0272  0.0184  451 TRP C CD1 
11855 C CD2 . TRP C 451 ? 0.7484 0.5374 0.5022 -0.0550 0.0349  0.0172  451 TRP C CD2 
11856 N NE1 . TRP C 451 ? 0.6432 0.4426 0.4117 -0.0397 0.0328  0.0237  451 TRP C NE1 
11857 C CE2 . TRP C 451 ? 0.7168 0.5312 0.5013 -0.0574 0.0364  0.0232  451 TRP C CE2 
11858 C CE3 . TRP C 451 ? 0.7965 0.5903 0.5558 -0.0715 0.0380  0.0142  451 TRP C CE3 
11859 C CZ2 . TRP C 451 ? 0.7160 0.5635 0.5391 -0.0747 0.0396  0.0271  451 TRP C CZ2 
11860 C CZ3 . TRP C 451 ? 0.7958 0.6211 0.5912 -0.0903 0.0402  0.0171  451 TRP C CZ3 
11861 C CH2 . TRP C 451 ? 0.7733 0.6267 0.6017 -0.0914 0.0404  0.0239  451 TRP C CH2 
11862 N N   . TRP C 452 ? 0.7703 0.4177 0.3857 0.0023  0.0529  0.0157  452 TRP C N   
11863 C CA  . TRP C 452 ? 0.8226 0.4496 0.4237 0.0094  0.0672  0.0202  452 TRP C CA  
11864 C C   . TRP C 452 ? 0.9132 0.4877 0.4683 0.0156  0.0887  0.0231  452 TRP C C   
11865 O O   . TRP C 452 ? 0.9028 0.4605 0.4484 0.0178  0.1078  0.0279  452 TRP C O   
11866 C CB  . TRP C 452 ? 0.8507 0.4731 0.4383 0.0272  0.0507  0.0176  452 TRP C CB  
11867 C CG  . TRP C 452 ? 0.7932 0.4625 0.4245 0.0215  0.0327  0.0162  452 TRP C CG  
11868 C CD1 . TRP C 452 ? 0.8017 0.4897 0.4427 0.0255  0.0094  0.0114  452 TRP C CD1 
11869 C CD2 . TRP C 452 ? 0.7739 0.4771 0.4463 0.0111  0.0374  0.0206  452 TRP C CD2 
11870 N NE1 . TRP C 452 ? 0.7633 0.4918 0.4458 0.0175  0.0002  0.0128  452 TRP C NE1 
11871 C CE2 . TRP C 452 ? 0.7263 0.4642 0.4277 0.0093  0.0162  0.0186  452 TRP C CE2 
11872 C CE3 . TRP C 452 ? 0.7959 0.5040 0.4853 0.0037  0.0581  0.0267  452 TRP C CE3 
11873 C CZ2 . TRP C 452 ? 0.7014 0.4751 0.4437 0.0012  0.0141  0.0228  452 TRP C CZ2 
11874 C CZ3 . TRP C 452 ? 0.7386 0.4856 0.4722 -0.0035 0.0552  0.0304  452 TRP C CZ3 
11875 C CH2 . TRP C 452 ? 0.7053 0.4831 0.4628 -0.0044 0.0329  0.0287  452 TRP C CH2 
11876 N N   . GLN C 453 ? 0.9719 0.5180 0.4965 0.0199  0.0875  0.0207  453 GLN C N   
11877 C CA  . GLN C 453 ? 1.0357 0.5261 0.5109 0.0277  0.1080  0.0247  453 GLN C CA  
11878 C C   . GLN C 453 ? 1.1007 0.5915 0.5941 0.0094  0.1369  0.0306  453 GLN C C   
11879 O O   . GLN C 453 ? 1.0433 0.5561 0.5686 -0.0108 0.1417  0.0299  453 GLN C O   
11880 C CB  . GLN C 453 ? 1.0916 0.5516 0.5347 0.0341  0.1034  0.0220  453 GLN C CB  
11881 C CG  . GLN C 453 ? 1.2500 0.6493 0.6413 0.0405  0.1276  0.0278  453 GLN C CG  
11882 C CD  . GLN C 453 ? 1.3760 0.7423 0.7284 0.0575  0.1358  0.0323  453 GLN C CD  
11883 O OE1 . GLN C 453 ? 1.4265 0.7951 0.7900 0.0494  0.1569  0.0372  453 GLN C OE1 
11884 N NE2 . GLN C 453 ? 1.4259 0.7623 0.7335 0.0813  0.1188  0.0303  453 GLN C NE2 
11885 N N   . GLY C 454 ? 1.2155 0.6821 0.6890 0.0168  0.1557  0.0361  454 GLY C N   
11886 C CA  . GLY C 454 ? 1.3094 0.7815 0.8059 0.0030  0.1844  0.0426  454 GLY C CA  
11887 C C   . GLY C 454 ? 1.3577 0.8568 0.8985 -0.0236 0.1954  0.0436  454 GLY C C   
11888 O O   . GLY C 454 ? 1.3648 0.8372 0.8850 -0.0294 0.2011  0.0427  454 GLY C O   
11889 N N   . GLU C 455 ? 1.3853 0.9353 0.9856 -0.0400 0.1969  0.0450  455 GLU C N   
11890 C CA  . GLU C 455 ? 1.3343 0.9244 0.9697 -0.0358 0.1870  0.0459  455 GLU C CA  
11891 C C   . GLU C 455 ? 1.3656 0.9326 0.9823 -0.0218 0.2076  0.0514  455 GLU C C   
11892 O O   . GLU C 455 ? 1.4082 0.9345 0.9724 -0.0009 0.2055  0.0502  455 GLU C O   
11893 C CB  . GLU C 455 ? 1.3107 0.9181 0.9430 -0.0246 0.1540  0.0395  455 GLU C CB  
11894 C CG  . GLU C 455 ? 1.3147 0.9431 0.9620 -0.0364 0.1353  0.0339  455 GLU C CG  
11895 C CD  . GLU C 455 ? 1.2907 0.9669 0.9947 -0.0606 0.1353  0.0348  455 GLU C CD  
11896 O OE1 . GLU C 455 ? 1.2548 0.9365 0.9642 -0.0741 0.1295  0.0306  455 GLU C OE1 
11897 O OE2 . GLU C 455 ? 1.2976 1.0049 1.0397 -0.0652 0.1403  0.0394  455 GLU C OE2 
11898 N N   . GLU C 456 ? 1.3511 0.9453 1.0125 -0.0336 0.2273  0.0570  456 GLU C N   
11899 C CA  . GLU C 456 ? 1.3255 0.9070 0.9813 -0.0220 0.2498  0.0625  456 GLU C CA  
11900 C C   . GLU C 456 ? 1.2685 0.8394 0.8958 0.0003  0.2315  0.0586  456 GLU C C   
11901 O O   . GLU C 456 ? 1.2148 0.8205 0.8675 0.0004  0.2036  0.0542  456 GLU C O   
11902 C CB  . GLU C 456 ? 1.2603 0.8942 0.9876 -0.0370 0.2615  0.0677  456 GLU C CB  
11903 N N   . LYS C 457 ? 1.2741 0.7938 0.8461 0.0188  0.2476  0.0599  457 LYS C N   
11904 C CA  . LYS C 457 ? 1.2915 0.7910 0.8264 0.0404  0.2305  0.0548  457 LYS C CA  
11905 C C   . LYS C 457 ? 1.3015 0.8433 0.8835 0.0410  0.2224  0.0544  457 LYS C C   
11906 O O   . LYS C 457 ? 1.3409 0.8849 0.9381 0.0437  0.2466  0.0594  457 LYS C O   
11907 C CB  . LYS C 457 ? 1.3427 0.7778 0.8089 0.0589  0.2535  0.0569  457 LYS C CB  
11908 N N   . ALA C 458 ? 1.2397 0.8150 0.8461 0.0387  0.1900  0.0492  458 ALA C N   
11909 C CA  . ALA C 458 ? 1.1384 0.7433 0.7754 0.0433  0.1757  0.0476  458 ALA C CA  
11910 C C   . ALA C 458 ? 1.1041 0.6719 0.6894 0.0631  0.1589  0.0402  458 ALA C C   
11911 O O   . ALA C 458 ? 1.1478 0.6781 0.6821 0.0714  0.1507  0.0359  458 ALA C O   
11912 C CB  . ALA C 458 ? 1.0675 0.7276 0.7583 0.0281  0.1507  0.0469  458 ALA C CB  
11913 N N   . PRO C 459 ? 1.0320 0.6070 0.6278 0.0714  0.1527  0.0383  459 PRO C N   
11914 C CA  . PRO C 459 ? 1.0612 0.5989 0.6072 0.0889  0.1353  0.0297  459 PRO C CA  
11915 C C   . PRO C 459 ? 1.0682 0.6117 0.6055 0.0876  0.1015  0.0229  459 PRO C C   
11916 O O   . PRO C 459 ? 0.9317 0.5193 0.5141 0.0741  0.0861  0.0238  459 PRO C O   
11917 C CB  . PRO C 459 ? 1.0604 0.6170 0.6364 0.0926  0.1326  0.0293  459 PRO C CB  
11918 C CG  . PRO C 459 ? 1.0322 0.6167 0.6542 0.0845  0.1606  0.0389  459 PRO C CG  
11919 C CD  . PRO C 459 ? 1.0063 0.6193 0.6569 0.0666  0.1628  0.0438  459 PRO C CD  
11920 N N   . PHE C 460 ? 1.1453 0.6432 0.6229 0.1026  0.0903  0.0161  460 PHE C N   
11921 C CA  . PHE C 460 ? 1.1424 0.6408 0.6074 0.1059  0.0572  0.0086  460 PHE C CA  
11922 C C   . PHE C 460 ? 1.0808 0.5925 0.5538 0.0974  0.0521  0.0105  460 PHE C C   
11923 O O   . PHE C 460 ? 1.0848 0.6067 0.5597 0.0988  0.0255  0.0051  460 PHE C O   
11924 C CB  . PHE C 460 ? 1.0760 0.6133 0.5843 0.1004  0.0321  0.0044  460 PHE C CB  
11925 C CG  . PHE C 460 ? 1.0978 0.6205 0.5985 0.1090  0.0324  0.0008  460 PHE C CG  
11926 C CD1 . PHE C 460 ? 1.1898 0.6624 0.6316 0.1257  0.0253  -0.0073 460 PHE C CD1 
11927 C CD2 . PHE C 460 ? 1.0216 0.5789 0.5723 0.1010  0.0384  0.0052  460 PHE C CD2 
11928 C CE1 . PHE C 460 ? 1.1550 0.6104 0.5870 0.1334  0.0258  -0.0119 460 PHE C CE1 
11929 C CE2 . PHE C 460 ? 1.0404 0.5814 0.5836 0.1097  0.0395  0.0017  460 PHE C CE2 
11930 C CZ  . PHE C 460 ? 1.0872 0.5767 0.5709 0.1254  0.0335  -0.0075 460 PHE C CZ  
11931 N N   . VAL C 461 ? 1.0704 0.5820 0.5497 0.0883  0.0768  0.0177  461 VAL C N   
11932 C CA  . VAL C 461 ? 1.0703 0.5867 0.5500 0.0815  0.0716  0.0183  461 VAL C CA  
11933 C C   . VAL C 461 ? 1.1256 0.5912 0.5413 0.0985  0.0643  0.0149  461 VAL C C   
11934 O O   . VAL C 461 ? 1.1683 0.6368 0.5806 0.0990  0.0486  0.0124  461 VAL C O   
11935 C CB  . VAL C 461 ? 1.1229 0.6503 0.6260 0.0655  0.0986  0.0259  461 VAL C CB  
11936 C CG1 . VAL C 461 ? 1.0853 0.6681 0.6552 0.0486  0.1005  0.0292  461 VAL C CG1 
11937 C CG2 . VAL C 461 ? 1.2221 0.7033 0.6844 0.0724  0.1302  0.0312  461 VAL C CG2 
11938 N N   . GLU C 462 ? 1.1052 0.5219 0.4672 0.1139  0.0757  0.0150  462 GLU C N   
11939 C CA  . GLU C 462 ? 1.1585 0.5236 0.4541 0.1323  0.0664  0.0122  462 GLU C CA  
11940 C C   . GLU C 462 ? 1.0905 0.4680 0.3873 0.1405  0.0273  0.0033  462 GLU C C   
11941 O O   . GLU C 462 ? 1.0410 0.3935 0.3023 0.1522  0.0132  0.0014  462 GLU C O   
11942 C CB  . GLU C 462 ? 1.2711 0.5822 0.5070 0.1479  0.0835  0.0130  462 GLU C CB  
11943 C CG  . GLU C 462 ? 1.3930 0.6947 0.6105 0.1605  0.0608  0.0039  462 GLU C CG  
11944 C CD  . GLU C 462 ? 1.4822 0.7980 0.7258 0.1558  0.0776  0.0045  462 GLU C CD  
11945 O OE1 . GLU C 462 ? 1.4237 0.7864 0.7299 0.1389  0.0894  0.0095  462 GLU C OE1 
11946 O OE2 . GLU C 462 ? 1.5726 0.8511 0.7724 0.1699  0.0785  -0.0002 462 GLU C OE2 
11947 N N   . VAL C 463 ? 1.0497 0.4660 0.3891 0.1347  0.0099  -0.0017 463 VAL C N   
11948 C CA  . VAL C 463 ? 1.0216 0.4560 0.3724 0.1394  -0.0259 -0.0099 463 VAL C CA  
11949 C C   . VAL C 463 ? 0.9977 0.4619 0.3785 0.1319  -0.0350 -0.0088 463 VAL C C   
11950 O O   . VAL C 463 ? 1.0350 0.4943 0.4028 0.1422  -0.0581 -0.0135 463 VAL C O   
11951 C CB  . VAL C 463 ? 1.0001 0.4692 0.3935 0.1321  -0.0385 -0.0142 463 VAL C CB  
11952 C CG1 . VAL C 463 ? 1.0055 0.4827 0.4013 0.1388  -0.0743 -0.0235 463 VAL C CG1 
11953 C CG2 . VAL C 463 ? 1.0640 0.5051 0.4330 0.1376  -0.0217 -0.0141 463 VAL C CG2 
11954 N N   . PHE C 464 ? 0.9064 0.4023 0.3286 0.1144  -0.0175 -0.0029 464 PHE C N   
11955 C CA  . PHE C 464 ? 0.8136 0.3322 0.2586 0.1072  -0.0227 -0.0024 464 PHE C CA  
11956 C C   . PHE C 464 ? 0.9085 0.3827 0.3033 0.1196  -0.0174 -0.0008 464 PHE C C   
11957 O O   . PHE C 464 ? 0.8961 0.3747 0.2911 0.1253  -0.0332 -0.0037 464 PHE C O   
11958 C CB  . PHE C 464 ? 0.7721 0.3273 0.2641 0.0857  -0.0046 0.0030  464 PHE C CB  
11959 C CG  . PHE C 464 ? 0.7296 0.3343 0.2755 0.0740  -0.0149 0.0022  464 PHE C CG  
11960 C CD1 . PHE C 464 ? 0.7182 0.3596 0.2980 0.0688  -0.0347 -0.0012 464 PHE C CD1 
11961 C CD2 . PHE C 464 ? 0.7185 0.3311 0.2800 0.0693  -0.0035 0.0054  464 PHE C CD2 
11962 C CE1 . PHE C 464 ? 0.6630 0.3464 0.2891 0.0581  -0.0431 -0.0006 464 PHE C CE1 
11963 C CE2 . PHE C 464 ? 0.7139 0.3683 0.3223 0.0598  -0.0130 0.0058  464 PHE C CE2 
11964 C CZ  . PHE C 464 ? 0.6320 0.3209 0.2714 0.0538  -0.0329 0.0031  464 PHE C CZ  
11965 N N   . ASP C 465 ? 0.9479 0.3771 0.2983 0.1250  0.0058  0.0042  465 ASP C N   
11966 C CA  . ASP C 465 ? 0.9831 0.3641 0.2805 0.1377  0.0118  0.0070  465 ASP C CA  
11967 C C   . ASP C 465 ? 1.0289 0.3863 0.2919 0.1599  -0.0159 0.0012  465 ASP C C   
11968 O O   . ASP C 465 ? 1.0713 0.4176 0.3247 0.1696  -0.0259 0.0003  465 ASP C O   
11969 C CB  . ASP C 465 ? 1.0326 0.3702 0.2916 0.1375  0.0454  0.0146  465 ASP C CB  
11970 C CG  . ASP C 465 ? 1.2016 0.4891 0.4151 0.1519  0.0507  0.0168  465 ASP C CG  
11971 O OD1 . ASP C 465 ? 1.2207 0.5005 0.4332 0.1452  0.0630  0.0207  465 ASP C OD1 
11972 O OD2 . ASP C 465 ? 1.2612 0.5185 0.4443 0.1693  0.0413  0.0140  465 ASP C OD2 
11973 N N   . LYS C 466 ? 1.0192 0.3761 0.2792 0.1666  -0.0289 -0.0037 466 LYS C N   
11974 C CA  . LYS C 466 ? 1.0863 0.4299 0.3323 0.1841  -0.0562 -0.0106 466 LYS C CA  
11975 C C   . LYS C 466 ? 1.0143 0.3971 0.2962 0.1846  -0.0857 -0.0167 466 LYS C C   
11976 O O   . LYS C 466 ? 1.0155 0.3883 0.2881 0.1983  -0.1019 -0.0200 466 LYS C O   
11977 C CB  . LYS C 466 ? 1.1440 0.4780 0.3798 0.1885  -0.0631 -0.0151 466 LYS C CB  
11978 C CG  . LYS C 466 ? 1.2319 0.5711 0.4718 0.2002  -0.0984 -0.0247 466 LYS C CG  
11979 C CD  . LYS C 466 ? 1.2910 0.5900 0.4918 0.2124  -0.1009 -0.0275 466 LYS C CD  
11980 C CE  . LYS C 466 ? 1.2538 0.5459 0.4483 0.2047  -0.0800 -0.0246 466 LYS C CE  
11981 N NZ  . LYS C 466 ? 1.3469 0.5874 0.4910 0.2178  -0.0707 -0.0231 466 LYS C NZ  
11982 N N   . LEU C 467 ? 0.9433 0.3710 0.2668 0.1705  -0.0925 -0.0183 467 LEU C N   
11983 C CA  . LEU C 467 ? 0.9366 0.4051 0.2995 0.1693  -0.1175 -0.0230 467 LEU C CA  
11984 C C   . LEU C 467 ? 0.9699 0.4344 0.3285 0.1732  -0.1128 -0.0195 467 LEU C C   
11985 O O   . LEU C 467 ? 0.9566 0.4255 0.3208 0.1856  -0.1321 -0.0235 467 LEU C O   
11986 C CB  . LEU C 467 ? 0.8449 0.3675 0.2708 0.1486  -0.1157 -0.0234 467 LEU C CB  
11987 C CG  . LEU C 467 ? 0.8630 0.3941 0.2998 0.1462  -0.1274 -0.0284 467 LEU C CG  
11988 C CD1 . LEU C 467 ? 0.8361 0.4112 0.3281 0.1256  -0.1170 -0.0256 467 LEU C CD1 
11989 C CD2 . LEU C 467 ? 0.8492 0.3899 0.2928 0.1560  -0.1620 -0.0371 467 LEU C CD2 
11990 N N   . PHE C 468 ? 0.9278 0.3884 0.2887 0.1609  -0.0847 -0.0130 468 PHE C N   
11991 C CA  . PHE C 468 ? 0.9957 0.4493 0.3527 0.1627  -0.0775 -0.0104 468 PHE C CA  
11992 C C   . PHE C 468 ? 1.0101 0.4160 0.3155 0.1859  -0.0848 -0.0099 468 PHE C C   
11993 O O   . PHE C 468 ? 1.0531 0.4664 0.3655 0.1979  -0.1023 -0.0130 468 PHE C O   
11994 C CB  . PHE C 468 ? 0.9741 0.4222 0.3350 0.1449  -0.0452 -0.0042 468 PHE C CB  
11995 C CG  . PHE C 468 ? 0.9786 0.4057 0.3236 0.1469  -0.0344 -0.0016 468 PHE C CG  
11996 C CD1 . PHE C 468 ? 0.9206 0.3805 0.3016 0.1421  -0.0422 -0.0051 468 PHE C CD1 
11997 C CD2 . PHE C 468 ? 0.9992 0.3707 0.2912 0.1540  -0.0149 0.0044  468 PHE C CD2 
11998 C CE1 . PHE C 468 ? 0.9677 0.4046 0.3320 0.1445  -0.0314 -0.0036 468 PHE C CE1 
11999 C CE2 . PHE C 468 ? 1.0683 0.4164 0.3443 0.1556  -0.0043 0.0067  468 PHE C CE2 
12000 C CZ  . PHE C 468 ? 1.0665 0.4470 0.3787 0.1511  -0.0130 0.0023  468 PHE C CZ  
12001 N N   . ARG C 469 ? 1.0234 0.3872 0.2911 0.1916  -0.0700 -0.0073 469 ARG C N   
12002 C CA  . ARG C 469 ? 1.0894 0.4113 0.3185 0.2114  -0.0737 -0.0084 469 ARG C CA  
12003 C C   . ARG C 469 ? 1.0932 0.4280 0.3309 0.2269  -0.1072 -0.0175 469 ARG C C   
12004 O O   . ARG C 469 ? 1.1347 0.4518 0.3541 0.2433  -0.1179 -0.0201 469 ARG C O   
12005 C CB  . ARG C 469 ? 1.1114 0.3858 0.2983 0.2136  -0.0502 -0.0041 469 ARG C CB  
12006 C CG  . ARG C 469 ? 1.1765 0.4329 0.3537 0.1999  -0.0159 0.0045  469 ARG C CG  
12007 C CD  . ARG C 469 ? 1.2367 0.4552 0.3826 0.1992  0.0092  0.0089  469 ARG C CD  
12008 N NE  . ARG C 469 ? 1.2524 0.4550 0.3934 0.1842  0.0436  0.0166  469 ARG C NE  
12009 C CZ  . ARG C 469 ? 1.2732 0.4406 0.3879 0.1873  0.0593  0.0193  469 ARG C CZ  
12010 N NH1 . ARG C 469 ? 1.3138 0.4579 0.4020 0.2065  0.0438  0.0153  469 ARG C NH1 
12011 N NH2 . ARG C 469 ? 1.2742 0.4313 0.3908 0.1704  0.0909  0.0253  469 ARG C NH2 
12012 N N   . SER C 470 ? 1.0806 0.4470 0.3473 0.2212  -0.1240 -0.0227 470 SER C N   
12013 C CA  . SER C 470 ? 1.1239 0.5079 0.4068 0.2324  -0.1563 -0.0318 470 SER C CA  
12014 C C   . SER C 470 ? 1.0899 0.5124 0.4110 0.2343  -0.1727 -0.0339 470 SER C C   
12015 O O   . SER C 470 ? 1.1357 0.5576 0.4560 0.2494  -0.1919 -0.0388 470 SER C O   
12016 C CB  . SER C 470 ? 1.1614 0.5681 0.4674 0.2237  -0.1686 -0.0369 470 SER C CB  
12017 O OG  . SER C 470 ? 1.2730 0.6399 0.5396 0.2265  -0.1562 -0.0357 470 SER C OG  
12018 N N   . PHE C 471 ? 0.9747 0.4312 0.3293 0.2196  -0.1652 -0.0303 471 PHE C N   
12019 C CA  . PHE C 471 ? 0.9320 0.4226 0.3210 0.2223  -0.1776 -0.0313 471 PHE C CA  
12020 C C   . PHE C 471 ? 0.9695 0.4282 0.3275 0.2371  -0.1695 -0.0278 471 PHE C C   
12021 O O   . PHE C 471 ? 0.9927 0.4642 0.3649 0.2510  -0.1865 -0.0310 471 PHE C O   
12022 C CB  . PHE C 471 ? 0.8781 0.4058 0.3026 0.2029  -0.1679 -0.0281 471 PHE C CB  
12023 C CG  . PHE C 471 ? 0.9067 0.4725 0.3716 0.1880  -0.1769 -0.0322 471 PHE C CG  
12024 C CD1 . PHE C 471 ? 0.9358 0.5232 0.4246 0.1940  -0.2045 -0.0393 471 PHE C CD1 
12025 C CD2 . PHE C 471 ? 0.8044 0.3857 0.2892 0.1667  -0.1560 -0.0292 471 PHE C CD2 
12026 C CE1 . PHE C 471 ? 0.9105 0.5274 0.4322 0.1805  -0.2130 -0.0428 471 PHE C CE1 
12027 C CE2 . PHE C 471 ? 0.8076 0.4198 0.3269 0.1546  -0.1638 -0.0321 471 PHE C CE2 
12028 C CZ  . PHE C 471 ? 0.8217 0.4495 0.3572 0.1615  -0.1921 -0.0388 471 PHE C CZ  
12029 N N   . VAL C 472 ? 0.9965 0.4140 0.3143 0.2338  -0.1423 -0.0209 472 VAL C N   
12030 C CA  . VAL C 472 ? 1.0535 0.4340 0.3375 0.2463  -0.1312 -0.0173 472 VAL C CA  
12031 C C   . VAL C 472 ? 1.1469 0.5055 0.4070 0.2679  -0.1481 -0.0227 472 VAL C C   
12032 O O   . VAL C 472 ? 1.1958 0.5494 0.4510 0.2829  -0.1555 -0.0233 472 VAL C O   
12033 C CB  . VAL C 472 ? 1.1091 0.4480 0.3562 0.2357  -0.0976 -0.0097 472 VAL C CB  
12034 C CG1 . VAL C 472 ? 1.2061 0.4993 0.4122 0.2488  -0.0853 -0.0071 472 VAL C CG1 
12035 C CG2 . VAL C 472 ? 1.0673 0.4303 0.3386 0.2131  -0.0813 -0.0048 472 VAL C CG2 
12036 N N   . ARG C 473 ? 1.1333 0.4782 0.3771 0.2704  -0.1550 -0.0267 473 ARG C N   
12037 C CA  . ARG C 473 ? 1.2962 0.6175 0.5126 0.2904  -0.1722 -0.0320 473 ARG C CA  
12038 C C   . ARG C 473 ? 1.2501 0.6155 0.5095 0.2984  -0.2046 -0.0389 473 ARG C C   
12039 O O   . ARG C 473 ? 1.2127 0.5729 0.4651 0.3152  -0.2164 -0.0404 473 ARG C O   
12040 C CB  . ARG C 473 ? 1.3838 0.6751 0.5687 0.2913  -0.1710 -0.0343 473 ARG C CB  
12041 C CG  . ARG C 473 ? 1.4862 0.7237 0.6196 0.2905  -0.1394 -0.0275 473 ARG C CG  
12042 C CD  . ARG C 473 ? 1.5869 0.7847 0.6784 0.3005  -0.1420 -0.0304 473 ARG C CD  
12043 N NE  . ARG C 473 ? 1.5923 0.8145 0.7081 0.2937  -0.1577 -0.0353 473 ARG C NE  
12044 C CZ  . ARG C 473 ? 1.5940 0.8179 0.7152 0.2795  -0.1413 -0.0317 473 ARG C CZ  
12045 N NH1 . ARG C 473 ? 1.5794 0.7848 0.6870 0.2698  -0.1088 -0.0230 473 ARG C NH1 
12046 N NH2 . ARG C 473 ? 1.5970 0.8414 0.7381 0.2745  -0.1570 -0.0369 473 ARG C NH2 
12047 N N   . ARG C 474 ? 1.1889 0.5995 0.4958 0.2861  -0.2182 -0.0429 474 ARG C N   
12048 C CA  . ARG C 474 ? 1.1818 0.6371 0.5357 0.2911  -0.2478 -0.0496 474 ARG C CA  
12049 C C   . ARG C 474 ? 1.1984 0.6788 0.5801 0.2980  -0.2494 -0.0469 474 ARG C C   
12050 O O   . ARG C 474 ? 1.2000 0.7035 0.6072 0.3102  -0.2710 -0.0510 474 ARG C O   
12051 C CB  . ARG C 474 ? 1.1128 0.6098 0.5124 0.2735  -0.2574 -0.0535 474 ARG C CB  
12052 C CG  . ARG C 474 ? 1.1429 0.6956 0.6045 0.2726  -0.2817 -0.0588 474 ARG C CG  
12053 C CD  . ARG C 474 ? 1.2326 0.7848 0.6950 0.2857  -0.3087 -0.0663 474 ARG C CD  
12054 N NE  . ARG C 474 ? 1.3791 0.9103 0.8200 0.2816  -0.3163 -0.0715 474 ARG C NE  
12055 C CZ  . ARG C 474 ? 1.4204 0.9821 0.8989 0.2727  -0.3363 -0.0783 474 ARG C CZ  
12056 N NH1 . ARG C 474 ? 1.3716 0.9880 0.9134 0.2659  -0.3489 -0.0803 474 ARG C NH1 
12057 N NH2 . ARG C 474 ? 1.4243 0.9605 0.8771 0.2705  -0.3425 -0.0830 474 ARG C NH2 
12058 N N   . ALA C 475 ? 1.2058 0.6799 0.5824 0.2911  -0.2261 -0.0397 475 ALA C N   
12059 C CA  . ALA C 475 ? 1.1618 0.6537 0.5606 0.2989  -0.2247 -0.0367 475 ALA C CA  
12060 C C   . ALA C 475 ? 1.2162 0.6772 0.5836 0.3210  -0.2270 -0.0360 475 ALA C C   
12061 O O   . ALA C 475 ? 1.1274 0.6083 0.5203 0.3324  -0.2327 -0.0353 475 ALA C O   
12062 C CB  . ALA C 475 ? 1.1833 0.6663 0.5752 0.2858  -0.1983 -0.0292 475 ALA C CB  
12063 N N   . GLN C 476 ? 1.2912 0.7040 0.6044 0.3282  -0.2222 -0.0359 476 GLN C N   
12064 C CA  . GLN C 476 ? 1.3673 0.7459 0.6438 0.3488  -0.2232 -0.0345 476 GLN C CA  
12065 C C   . GLN C 476 ? 1.4436 0.8280 0.7213 0.3639  -0.2525 -0.0410 476 GLN C C   
12066 O O   . GLN C 476 ? 1.5401 0.8897 0.7783 0.3815  -0.2551 -0.0400 476 GLN C O   
12067 C CB  . GLN C 476 ? 1.4027 0.7197 0.6141 0.3477  -0.1961 -0.0292 476 GLN C CB  
12068 C CG  . GLN C 476 ? 1.3797 0.6870 0.5875 0.3303  -0.1661 -0.0225 476 GLN C CG  
12069 C CD  . GLN C 476 ? 1.4234 0.6757 0.5751 0.3247  -0.1391 -0.0181 476 GLN C CD  
12070 O OE1 . GLN C 476 ? 1.4651 0.6768 0.5757 0.3344  -0.1260 -0.0145 476 GLN C OE1 
12071 N NE2 . GLN C 476 ? 1.4034 0.6546 0.5547 0.3089  -0.1295 -0.0180 476 GLN C NE2 
12072 N N   . GLU C 477 ? 1.4633 0.8889 0.7840 0.3569  -0.2746 -0.0476 477 GLU C N   
12073 C CA  . GLU C 477 ? 1.5320 0.9614 0.8536 0.3686  -0.3033 -0.0543 477 GLU C CA  
12074 C C   . GLU C 477 ? 1.4760 0.9662 0.8664 0.3713  -0.3287 -0.0583 477 GLU C C   
12075 O O   . GLU C 477 ? 1.3958 0.9306 0.8384 0.3579  -0.3265 -0.0583 477 GLU C O   
12076 C CB  . GLU C 477 ? 1.5639 0.9787 0.8679 0.3581  -0.3077 -0.0593 477 GLU C CB  
12077 C CG  . GLU C 477 ? 1.6374 0.9888 0.8713 0.3598  -0.2851 -0.0558 477 GLU C CG  
12078 C CD  . GLU C 477 ? 1.6636 1.0023 0.8845 0.3491  -0.2855 -0.0597 477 GLU C CD  
12079 O OE1 . GLU C 477 ? 1.7233 1.0099 0.8879 0.3529  -0.2698 -0.0575 477 GLU C OE1 
12080 O OE2 . GLU C 477 ? 1.6168 0.9966 0.8838 0.3371  -0.3004 -0.0647 477 GLU C OE2 
12081 N N   . MET D 1   ? 1.0216 0.7474 0.5933 -0.0613 0.1433  0.0129  1   MET D N   
12082 C CA  . MET D 1   ? 1.0488 0.7993 0.6698 -0.0547 0.1523  0.0129  1   MET D CA  
12083 C C   . MET D 1   ? 1.0353 0.7833 0.6666 -0.0516 0.1680  0.0050  1   MET D C   
12084 O O   . MET D 1   ? 1.1286 0.8740 0.7712 -0.0475 0.1889  0.0053  1   MET D O   
12085 C CB  . MET D 1   ? 1.0887 0.8676 0.7453 -0.0535 0.1326  0.0144  1   MET D CB  
12086 C CG  . MET D 1   ? 1.1251 0.9279 0.8283 -0.0475 0.1388  0.0172  1   MET D CG  
12087 S SD  . MET D 1   ? 1.1852 0.9824 0.8906 -0.0454 0.1562  0.0249  1   MET D SD  
12088 C CE  . MET D 1   ? 1.1199 0.9475 0.8722 -0.0417 0.1439  0.0304  1   MET D CE  
12089 N N   . LYS D 2   ? 0.8981 0.6479 0.5280 -0.0536 0.1563  -0.0013 2   LYS D N   
12090 C CA  . LYS D 2   ? 0.8293 0.5893 0.4857 -0.0500 0.1614  -0.0078 2   LYS D CA  
12091 C C   . LYS D 2   ? 0.7370 0.5288 0.4434 -0.0454 0.1549  -0.0040 2   LYS D C   
12092 O O   . LYS D 2   ? 0.7562 0.5576 0.4863 -0.0413 0.1653  0.0005  2   LYS D O   
12093 C CB  . LYS D 2   ? 0.7834 0.5276 0.4350 -0.0464 0.1869  -0.0122 2   LYS D CB  
12094 C CG  . LYS D 2   ? 0.7898 0.5519 0.4826 -0.0410 0.1919  -0.0157 2   LYS D CG  
12095 C CD  . LYS D 2   ? 0.8986 0.6428 0.5829 -0.0381 0.2127  -0.0223 2   LYS D CD  
12096 C CE  . LYS D 2   ? 0.8927 0.6570 0.6241 -0.0317 0.2186  -0.0234 2   LYS D CE  
12097 N NZ  . LYS D 2   ? 0.8926 0.6508 0.6357 -0.0263 0.2444  -0.0223 2   LYS D NZ  
12098 N N   . LYS D 3   ? 0.6341 0.4413 0.3556 -0.0465 0.1374  -0.0056 3   LYS D N   
12099 C CA  . LYS D 3   ? 0.5359 0.3708 0.2983 -0.0430 0.1285  -0.0021 3   LYS D CA  
12100 C C   . LYS D 3   ? 0.5414 0.3874 0.3322 -0.0393 0.1323  -0.0070 3   LYS D C   
12101 O O   . LYS D 3   ? 0.5632 0.3975 0.3420 -0.0403 0.1369  -0.0133 3   LYS D O   
12102 C CB  . LYS D 3   ? 0.5107 0.3563 0.2719 -0.0463 0.1063  0.0005  3   LYS D CB  
12103 C CG  . LYS D 3   ? 0.6623 0.4999 0.3999 -0.0496 0.0986  0.0066  3   LYS D CG  
12104 C CD  . LYS D 3   ? 0.7606 0.6134 0.5223 -0.0460 0.0979  0.0137  3   LYS D CD  
12105 C CE  . LYS D 3   ? 0.8478 0.6910 0.5855 -0.0490 0.0907  0.0205  3   LYS D CE  
12106 N NZ  . LYS D 3   ? 0.8919 0.7465 0.6334 -0.0508 0.0694  0.0239  3   LYS D NZ  
12107 N N   . LEU D 4   ? 0.5268 0.3943 0.3545 -0.0352 0.1299  -0.0039 4   LEU D N   
12108 C CA  . LEU D 4   ? 0.4692 0.3511 0.3246 -0.0326 0.1258  -0.0070 4   LEU D CA  
12109 C C   . LEU D 4   ? 0.4647 0.3620 0.3281 -0.0343 0.1063  -0.0055 4   LEU D C   
12110 O O   . LEU D 4   ? 0.5000 0.4076 0.3717 -0.0338 0.0990  -0.0003 4   LEU D O   
12111 C CB  . LEU D 4   ? 0.4778 0.3723 0.3685 -0.0271 0.1350  -0.0046 4   LEU D CB  
12112 C CG  . LEU D 4   ? 0.4501 0.3577 0.3687 -0.0242 0.1311  -0.0074 4   LEU D CG  
12113 C CD1 . LEU D 4   ? 0.4924 0.4012 0.4351 -0.0195 0.1461  -0.0073 4   LEU D CD1 
12114 C CD2 . LEU D 4   ? 0.3453 0.2724 0.2846 -0.0235 0.1158  -0.0044 4   LEU D CD2 
12115 N N   . PHE D 5   ? 0.4453 0.3439 0.3071 -0.0363 0.0987  -0.0098 5   PHE D N   
12116 C CA  . PHE D 5   ? 0.3596 0.2727 0.2302 -0.0380 0.0818  -0.0085 5   PHE D CA  
12117 C C   . PHE D 5   ? 0.3961 0.3264 0.2993 -0.0338 0.0802  -0.0087 5   PHE D C   
12118 O O   . PHE D 5   ? 0.4385 0.3667 0.3490 -0.0326 0.0852  -0.0125 5   PHE D O   
12119 C CB  . PHE D 5   ? 0.3749 0.2789 0.2241 -0.0436 0.0735  -0.0123 5   PHE D CB  
12120 C CG  . PHE D 5   ? 0.4846 0.3712 0.2992 -0.0486 0.0710  -0.0116 5   PHE D CG  
12121 C CD1 . PHE D 5   ? 0.5015 0.3921 0.3116 -0.0493 0.0637  -0.0056 5   PHE D CD1 
12122 C CD2 . PHE D 5   ? 0.4740 0.3385 0.2594 -0.0526 0.0758  -0.0168 5   PHE D CD2 
12123 C CE1 . PHE D 5   ? 0.5080 0.3814 0.2847 -0.0542 0.0601  -0.0042 5   PHE D CE1 
12124 C CE2 . PHE D 5   ? 0.5017 0.3479 0.2518 -0.0578 0.0723  -0.0161 5   PHE D CE2 
12125 C CZ  . PHE D 5   ? 0.4692 0.3204 0.2154 -0.0586 0.0640  -0.0095 5   PHE D CZ  
12126 N N   . LEU D 6   ? 0.3524 0.2981 0.2737 -0.0315 0.0729  -0.0044 6   LEU D N   
12127 C CA  . LEU D 6   ? 0.2837 0.2442 0.2333 -0.0276 0.0707  -0.0040 6   LEU D CA  
12128 C C   . LEU D 6   ? 0.3195 0.2916 0.2739 -0.0288 0.0573  -0.0034 6   LEU D C   
12129 O O   . LEU D 6   ? 0.2939 0.2693 0.2412 -0.0303 0.0495  -0.0005 6   LEU D O   
12130 C CB  . LEU D 6   ? 0.3163 0.2831 0.2823 -0.0240 0.0740  0.0001  6   LEU D CB  
12131 C CG  . LEU D 6   ? 0.3244 0.3035 0.3185 -0.0200 0.0721  0.0007  6   LEU D CG  
12132 C CD1 . LEU D 6   ? 0.3296 0.3060 0.3345 -0.0185 0.0794  -0.0023 6   LEU D CD1 
12133 C CD2 . LEU D 6   ? 0.3186 0.3013 0.3252 -0.0177 0.0746  0.0049  6   LEU D CD2 
12134 N N   . VAL D 7   ? 0.3519 0.3302 0.3190 -0.0279 0.0549  -0.0057 7   VAL D N   
12135 C CA  . VAL D 7   ? 0.3106 0.2990 0.2818 -0.0293 0.0442  -0.0053 7   VAL D CA  
12136 C C   . VAL D 7   ? 0.2993 0.2982 0.2922 -0.0254 0.0429  -0.0049 7   VAL D C   
12137 O O   . VAL D 7   ? 0.2689 0.2659 0.2687 -0.0246 0.0460  -0.0072 7   VAL D O   
12138 C CB  . VAL D 7   ? 0.3394 0.3213 0.2981 -0.0340 0.0418  -0.0086 7   VAL D CB  
12139 C CG1 . VAL D 7   ? 0.3409 0.3334 0.3029 -0.0364 0.0308  -0.0069 7   VAL D CG1 
12140 C CG2 . VAL D 7   ? 0.4210 0.3865 0.3543 -0.0381 0.0452  -0.0104 7   VAL D CG2 
12141 N N   . PHE D 8   ? 0.2451 0.2536 0.2478 -0.0228 0.0381  -0.0018 8   PHE D N   
12142 C CA  . PHE D 8   ? 0.2499 0.2664 0.2687 -0.0196 0.0353  -0.0017 8   PHE D CA  
12143 C C   . PHE D 8   ? 0.2928 0.3155 0.3107 -0.0213 0.0290  -0.0021 8   PHE D C   
12144 O O   . PHE D 8   ? 0.2291 0.2563 0.2419 -0.0230 0.0241  -0.0003 8   PHE D O   
12145 C CB  . PHE D 8   ? 0.3099 0.3319 0.3377 -0.0161 0.0331  0.0010  8   PHE D CB  
12146 C CG  . PHE D 8   ? 0.3385 0.3559 0.3724 -0.0144 0.0392  0.0020  8   PHE D CG  
12147 C CD1 . PHE D 8   ? 0.3591 0.3767 0.4077 -0.0122 0.0412  0.0014  8   PHE D CD1 
12148 C CD2 . PHE D 8   ? 0.2774 0.2899 0.3027 -0.0153 0.0427  0.0040  8   PHE D CD2 
12149 C CE1 . PHE D 8   ? 0.3465 0.3610 0.4042 -0.0109 0.0470  0.0029  8   PHE D CE1 
12150 C CE2 . PHE D 8   ? 0.3046 0.3130 0.3367 -0.0140 0.0495  0.0054  8   PHE D CE2 
12151 C CZ  . PHE D 8   ? 0.3089 0.3191 0.3588 -0.0118 0.0519  0.0049  8   PHE D CZ  
12152 N N   . TRP D 9   ? 0.2375 0.2607 0.2618 -0.0210 0.0290  -0.0037 9   TRP D N   
12153 C CA  . TRP D 9   ? 0.2277 0.2568 0.2527 -0.0224 0.0242  -0.0035 9   TRP D CA  
12154 C C   . TRP D 9   ? 0.2357 0.2683 0.2711 -0.0189 0.0229  -0.0030 9   TRP D C   
12155 O O   . TRP D 9   ? 0.2554 0.2837 0.2949 -0.0184 0.0245  -0.0043 9   TRP D O   
12156 C CB  . TRP D 9   ? 0.2380 0.2613 0.2558 -0.0268 0.0251  -0.0057 9   TRP D CB  
12157 C CG  . TRP D 9   ? 0.2492 0.2783 0.2660 -0.0301 0.0201  -0.0047 9   TRP D CG  
12158 C CD1 . TRP D 9   ? 0.2889 0.3285 0.3121 -0.0289 0.0165  -0.0021 9   TRP D CD1 
12159 C CD2 . TRP D 9   ? 0.2751 0.2994 0.2851 -0.0353 0.0191  -0.0062 9   TRP D CD2 
12160 N NE1 . TRP D 9   ? 0.2430 0.2858 0.2654 -0.0331 0.0136  -0.0013 9   TRP D NE1 
12161 C CE2 . TRP D 9   ? 0.2603 0.2938 0.2746 -0.0374 0.0145  -0.0038 9   TRP D CE2 
12162 C CE3 . TRP D 9   ? 0.2464 0.2587 0.2470 -0.0383 0.0222  -0.0095 9   TRP D CE3 
12163 C CZ2 . TRP D 9   ? 0.2733 0.3049 0.2839 -0.0432 0.0119  -0.0042 9   TRP D CZ2 
12164 C CZ3 . TRP D 9   ? 0.3127 0.3217 0.3076 -0.0438 0.0193  -0.0104 9   TRP D CZ3 
12165 C CH2 . TRP D 9   ? 0.2732 0.2921 0.2736 -0.0465 0.0137  -0.0076 9   TRP D CH2 
12166 N N   . TRP D 10  ? 0.2518 0.2909 0.2909 -0.0162 0.0199  -0.0013 10  TRP D N   
12167 C CA  . TRP D 10  ? 0.2504 0.2903 0.2955 -0.0129 0.0182  -0.0012 10  TRP D CA  
12168 C C   . TRP D 10  ? 0.2239 0.2670 0.2670 -0.0141 0.0166  -0.0008 10  TRP D C   
12169 O O   . TRP D 10  ? 0.2497 0.2994 0.2914 -0.0149 0.0158  0.0006  10  TRP D O   
12170 C CB  . TRP D 10  ? 0.2051 0.2478 0.2531 -0.0093 0.0165  0.0000  10  TRP D CB  
12171 C CG  . TRP D 10  ? 0.2554 0.2951 0.3060 -0.0083 0.0181  0.0005  10  TRP D CG  
12172 C CD1 . TRP D 10  ? 0.1990 0.2405 0.2469 -0.0083 0.0184  0.0022  10  TRP D CD1 
12173 C CD2 . TRP D 10  ? 0.2638 0.2983 0.3216 -0.0073 0.0196  0.0001  10  TRP D CD2 
12174 N NE1 . TRP D 10  ? 0.2492 0.2862 0.3005 -0.0075 0.0209  0.0027  10  TRP D NE1 
12175 C CE2 . TRP D 10  ? 0.2470 0.2804 0.3057 -0.0069 0.0219  0.0015  10  TRP D CE2 
12176 C CE3 . TRP D 10  ? 0.2545 0.2853 0.3192 -0.0067 0.0189  -0.0007 10  TRP D CE3 
12177 C CZ2 . TRP D 10  ? 0.2375 0.2670 0.3051 -0.0062 0.0244  0.0020  10  TRP D CZ2 
12178 C CZ3 . TRP D 10  ? 0.2772 0.3049 0.3521 -0.0058 0.0204  -0.0001 10  TRP D CZ3 
12179 C CH2 . TRP D 10  ? 0.2754 0.3028 0.3523 -0.0057 0.0236  0.0013  10  TRP D CH2 
12180 N N   . HIS D 11  ? 0.2340 0.2726 0.2780 -0.0141 0.0163  -0.0015 11  HIS D N   
12181 C CA  . HIS D 11  ? 0.2413 0.2810 0.2822 -0.0156 0.0156  -0.0007 11  HIS D CA  
12182 C C   . HIS D 11  ? 0.2864 0.3260 0.3259 -0.0122 0.0141  0.0001  11  HIS D C   
12183 O O   . HIS D 11  ? 0.2453 0.2791 0.2859 -0.0097 0.0119  -0.0005 11  HIS D O   
12184 C CB  . HIS D 11  ? 0.2474 0.2802 0.2881 -0.0179 0.0161  -0.0015 11  HIS D CB  
12185 C CG  . HIS D 11  ? 0.2579 0.2893 0.2954 -0.0192 0.0152  -0.0002 11  HIS D CG  
12186 N ND1 . HIS D 11  ? 0.1775 0.2146 0.2122 -0.0218 0.0162  0.0014  11  HIS D ND1 
12187 C CD2 . HIS D 11  ? 0.2272 0.2517 0.2639 -0.0185 0.0134  0.0004  11  HIS D CD2 
12188 C CE1 . HIS D 11  ? 0.2666 0.2999 0.2980 -0.0226 0.0161  0.0028  11  HIS D CE1 
12189 N NE2 . HIS D 11  ? 0.2438 0.2690 0.2753 -0.0206 0.0139  0.0022  11  HIS D NE2 
12190 N N   . MET D 12  ? 0.2666 0.3118 0.3037 -0.0122 0.0155  0.0015  12  MET D N   
12191 C CA  . MET D 12  ? 0.2465 0.2902 0.2794 -0.0086 0.0159  0.0019  12  MET D CA  
12192 C C   . MET D 12  ? 0.2278 0.2710 0.2557 -0.0105 0.0180  0.0034  12  MET D C   
12193 O O   . MET D 12  ? 0.1893 0.2397 0.2202 -0.0134 0.0205  0.0052  12  MET D O   
12194 C CB  . MET D 12  ? 0.2681 0.3189 0.3038 -0.0057 0.0175  0.0025  12  MET D CB  
12195 C CG  . MET D 12  ? 0.3264 0.3785 0.3668 -0.0047 0.0158  0.0019  12  MET D CG  
12196 S SD  . MET D 12  ? 0.5195 0.5621 0.5599 -0.0022 0.0126  -0.0001 12  MET D SD  
12197 C CE  . MET D 12  ? 0.4976 0.5438 0.5423 0.0006  0.0126  0.0004  12  MET D CE  
12198 N N   . HIS D 13  ? 0.2782 0.3121 0.2984 -0.0093 0.0166  0.0033  13  HIS D N   
12199 C CA  . HIS D 13  ? 0.2496 0.2807 0.2630 -0.0113 0.0188  0.0052  13  HIS D CA  
12200 C C   . HIS D 13  ? 0.2594 0.2796 0.2602 -0.0084 0.0176  0.0050  13  HIS D C   
12201 O O   . HIS D 13  ? 0.2126 0.2250 0.2112 -0.0065 0.0121  0.0034  13  HIS D O   
12202 C CB  . HIS D 13  ? 0.2232 0.2505 0.2385 -0.0155 0.0167  0.0058  13  HIS D CB  
12203 C CG  . HIS D 13  ? 0.2942 0.3156 0.3013 -0.0175 0.0178  0.0083  13  HIS D CG  
12204 N ND1 . HIS D 13  ? 0.2670 0.2934 0.2720 -0.0193 0.0234  0.0108  13  HIS D ND1 
12205 C CD2 . HIS D 13  ? 0.3072 0.3176 0.3082 -0.0182 0.0142  0.0093  13  HIS D CD2 
12206 C CE1 . HIS D 13  ? 0.2829 0.3011 0.2793 -0.0211 0.0237  0.0131  13  HIS D CE1 
12207 N NE2 . HIS D 13  ? 0.3361 0.3441 0.3293 -0.0205 0.0176  0.0122  13  HIS D NE2 
12208 N N   . GLN D 14  ? 0.2888 0.3079 0.2810 -0.0083 0.0227  0.0069  14  GLN D N   
12209 C CA  . GLN D 14  ? 0.2816 0.2870 0.2569 -0.0070 0.0218  0.0073  14  GLN D CA  
12210 C C   . GLN D 14  ? 0.3245 0.3293 0.2944 -0.0104 0.0268  0.0109  14  GLN D C   
12211 O O   . GLN D 14  ? 0.2514 0.2671 0.2287 -0.0118 0.0338  0.0127  14  GLN D O   
12212 C CB  . GLN D 14  ? 0.2872 0.2878 0.2519 -0.0022 0.0250  0.0056  14  GLN D CB  
12213 C CG  . GLN D 14  ? 0.2615 0.2606 0.2301 0.0011  0.0198  0.0022  14  GLN D CG  
12214 C CD  . GLN D 14  ? 0.3333 0.3210 0.2981 0.0003  0.0098  0.0012  14  GLN D CD  
12215 O OE1 . GLN D 14  ? 0.3159 0.2921 0.2680 -0.0010 0.0064  0.0024  14  GLN D OE1 
12216 N NE2 . GLN D 14  ? 0.2942 0.2850 0.2710 0.0008  0.0048  -0.0004 14  GLN D NE2 
12217 N N   . PRO D 15  ? 0.3527 0.3448 0.3107 -0.0120 0.0230  0.0124  15  PRO D N   
12218 C CA  . PRO D 15  ? 0.3487 0.3371 0.2973 -0.0148 0.0287  0.0163  15  PRO D CA  
12219 C C   . PRO D 15  ? 0.3481 0.3343 0.2844 -0.0117 0.0375  0.0167  15  PRO D C   
12220 O O   . PRO D 15  ? 0.3219 0.3041 0.2518 -0.0072 0.0372  0.0136  15  PRO D O   
12221 C CB  . PRO D 15  ? 0.3635 0.3360 0.2998 -0.0161 0.0209  0.0178  15  PRO D CB  
12222 C CG  . PRO D 15  ? 0.3433 0.3089 0.2770 -0.0126 0.0124  0.0145  15  PRO D CG  
12223 C CD  . PRO D 15  ? 0.3400 0.3197 0.2923 -0.0112 0.0132  0.0113  15  PRO D CD  
12224 N N   . LEU D 16  ? 0.3579 0.3459 0.2910 -0.0141 0.0460  0.0206  16  LEU D N   
12225 C CA  . LEU D 16  ? 0.4250 0.4114 0.3477 -0.0111 0.0572  0.0216  16  LEU D CA  
12226 C C   . LEU D 16  ? 0.4361 0.4008 0.3300 -0.0086 0.0558  0.0207  16  LEU D C   
12227 O O   . LEU D 16  ? 0.3799 0.3326 0.2590 -0.0116 0.0547  0.0240  16  LEU D O   
12228 C CB  . LEU D 16  ? 0.4430 0.4376 0.3723 -0.0151 0.0670  0.0268  16  LEU D CB  
12229 C CG  . LEU D 16  ? 0.4024 0.3973 0.3246 -0.0119 0.0811  0.0286  16  LEU D CG  
12230 C CD1 . LEU D 16  ? 0.4107 0.4174 0.3464 -0.0065 0.0846  0.0255  16  LEU D CD1 
12231 C CD2 . LEU D 16  ? 0.4170 0.4208 0.3488 -0.0167 0.0906  0.0346  16  LEU D CD2 
12232 N N   . TYR D 17  ? 0.4016 0.3599 0.2862 -0.0034 0.0555  0.0165  17  TYR D N   
12233 C CA  . TYR D 17  ? 0.3978 0.3333 0.2526 -0.0011 0.0529  0.0149  17  TYR D CA  
12234 C C   . TYR D 17  ? 0.4685 0.3958 0.3040 0.0010  0.0673  0.0164  17  TYR D C   
12235 O O   . TYR D 17  ? 0.4230 0.3290 0.2292 0.0030  0.0670  0.0148  17  TYR D O   
12236 C CB  . TYR D 17  ? 0.4346 0.3645 0.2868 0.0031  0.0455  0.0093  17  TYR D CB  
12237 C CG  . TYR D 17  ? 0.4240 0.3591 0.2927 0.0011  0.0317  0.0080  17  TYR D CG  
12238 C CD1 . TYR D 17  ? 0.4667 0.3909 0.3289 -0.0021 0.0202  0.0096  17  TYR D CD1 
12239 C CD2 . TYR D 17  ? 0.3541 0.3044 0.2453 0.0027  0.0307  0.0056  17  TYR D CD2 
12240 C CE1 . TYR D 17  ? 0.4604 0.3899 0.3402 -0.0034 0.0092  0.0087  17  TYR D CE1 
12241 C CE2 . TYR D 17  ? 0.3760 0.3303 0.2819 0.0011  0.0199  0.0046  17  TYR D CE2 
12242 C CZ  . TYR D 17  ? 0.4170 0.3615 0.3181 -0.0018 0.0098  0.0062  17  TYR D CZ  
12243 O OH  . TYR D 17  ? 0.3738 0.3226 0.2915 -0.0030 0.0006  0.0056  17  TYR D OH  
12244 N N   . ARG D 18  ? 0.4877 0.4306 0.3386 0.0005  0.0801  0.0197  18  ARG D N   
12245 C CA  . ARG D 18  ? 0.5133 0.4519 0.3516 0.0035  0.0964  0.0212  18  ARG D CA  
12246 C C   . ARG D 18  ? 0.5359 0.4644 0.3580 -0.0010 0.1013  0.0268  18  ARG D C   
12247 O O   . ARG D 18  ? 0.5170 0.4588 0.3570 -0.0059 0.1039  0.0317  18  ARG D O   
12248 C CB  . ARG D 18  ? 0.4950 0.4573 0.3624 0.0055  0.1074  0.0225  18  ARG D CB  
12249 C CG  . ARG D 18  ? 0.5098 0.4698 0.3695 0.0103  0.1255  0.0236  18  ARG D CG  
12250 C CD  . ARG D 18  ? 0.4895 0.4756 0.3836 0.0110  0.1349  0.0267  18  ARG D CD  
12251 N NE  . ARG D 18  ? 0.5510 0.5372 0.4425 0.0162  0.1540  0.0284  18  ARG D NE  
12252 C CZ  . ARG D 18  ? 0.5677 0.5488 0.4491 0.0143  0.1673  0.0334  18  ARG D CZ  
12253 N NH1 . ARG D 18  ? 0.6177 0.5927 0.4898 0.0072  0.1624  0.0372  18  ARG D NH1 
12254 N NH2 . ARG D 18  ? 0.6260 0.6076 0.5069 0.0196  0.1862  0.0348  18  ARG D NH2 
12255 N N   . GLU D 19  ? 0.4904 0.3939 0.2772 0.0002  0.1018  0.0261  19  GLU D N   
12256 C CA  . GLU D 19  ? 0.5488 0.4388 0.3149 -0.0039 0.1065  0.0317  19  GLU D CA  
12257 C C   . GLU D 19  ? 0.5395 0.4407 0.3146 -0.0038 0.1269  0.0364  19  GLU D C   
12258 O O   . GLU D 19  ? 0.5547 0.4575 0.3283 0.0018  0.1400  0.0342  19  GLU D O   
12259 C CB  . GLU D 19  ? 0.5847 0.4435 0.3078 -0.0021 0.1032  0.0297  19  GLU D CB  
12260 C CG  . GLU D 19  ? 0.5893 0.4312 0.2908 -0.0076 0.0972  0.0353  19  GLU D CG  
12261 C CD  . GLU D 19  ? 0.7492 0.5832 0.4327 -0.0087 0.1155  0.0408  19  GLU D CD  
12262 O OE1 . GLU D 19  ? 0.7627 0.6033 0.4496 -0.0046 0.1332  0.0400  19  GLU D OE1 
12263 O OE2 . GLU D 19  ? 0.8446 0.6654 0.5113 -0.0135 0.1124  0.0464  19  GLU D OE2 
12264 N N   . PRO D 20  ? 0.5063 0.4158 0.2930 -0.0098 0.1302  0.0430  20  PRO D N   
12265 C CA  . PRO D 20  ? 0.5603 0.4865 0.3661 -0.0104 0.1484  0.0480  20  PRO D CA  
12266 C C   . PRO D 20  ? 0.6516 0.5622 0.4305 -0.0082 0.1669  0.0510  20  PRO D C   
12267 O O   . PRO D 20  ? 0.7027 0.6275 0.4988 -0.0069 0.1841  0.0544  20  PRO D O   
12268 C CB  . PRO D 20  ? 0.5611 0.4989 0.3869 -0.0186 0.1433  0.0538  20  PRO D CB  
12269 C CG  . PRO D 20  ? 0.5288 0.4472 0.3329 -0.0216 0.1278  0.0536  20  PRO D CG  
12270 C CD  . PRO D 20  ? 0.4845 0.3913 0.2736 -0.0163 0.1167  0.0463  20  PRO D CD  
12271 N N   . TYR D 21  ? 0.6850 0.5666 0.4227 -0.0076 0.1642  0.0500  21  TYR D N   
12272 C CA  . TYR D 21  ? 0.7323 0.5961 0.4400 -0.0053 0.1830  0.0526  21  TYR D CA  
12273 C C   . TYR D 21  ? 0.7673 0.6195 0.4565 0.0033  0.1910  0.0457  21  TYR D C   
12274 O O   . TYR D 21  ? 0.8258 0.6759 0.5085 0.0073  0.2122  0.0470  21  TYR D O   
12275 C CB  . TYR D 21  ? 0.6891 0.5249 0.3581 -0.0098 0.1770  0.0564  21  TYR D CB  
12276 C CG  . TYR D 21  ? 0.6996 0.5451 0.3852 -0.0179 0.1753  0.0645  21  TYR D CG  
12277 C CD1 . TYR D 21  ? 0.7466 0.5977 0.4373 -0.0207 0.1945  0.0721  21  TYR D CD1 
12278 C CD2 . TYR D 21  ? 0.6174 0.4672 0.3160 -0.0226 0.1550  0.0648  21  TYR D CD2 
12279 C CE1 . TYR D 21  ? 0.7395 0.5990 0.4464 -0.0285 0.1925  0.0795  21  TYR D CE1 
12280 C CE2 . TYR D 21  ? 0.6283 0.4858 0.3421 -0.0297 0.1535  0.0717  21  TYR D CE2 
12281 C CZ  . TYR D 21  ? 0.6856 0.5477 0.4033 -0.0329 0.1716  0.0790  21  TYR D CZ  
12282 O OH  . TYR D 21  ? 0.6387 0.5073 0.3716 -0.0405 0.1694  0.0860  21  TYR D OH  
12283 N N   . THR D 22  ? 0.7567 0.6010 0.4382 0.0062  0.1750  0.0384  22  THR D N   
12284 C CA  . THR D 22  ? 0.7445 0.5775 0.4101 0.0141  0.1808  0.0311  22  THR D CA  
12285 C C   . THR D 22  ? 0.7373 0.5964 0.4419 0.0186  0.1814  0.0275  22  THR D C   
12286 O O   . THR D 22  ? 0.7762 0.6311 0.4757 0.0259  0.1913  0.0227  22  THR D O   
12287 C CB  . THR D 22  ? 0.7425 0.5475 0.3727 0.0144  0.1628  0.0253  22  THR D CB  
12288 O OG1 . THR D 22  ? 0.7199 0.5370 0.3728 0.0112  0.1410  0.0237  22  THR D OG1 
12289 C CG2 . THR D 22  ? 0.7643 0.5405 0.3520 0.0102  0.1614  0.0292  22  THR D CG2 
12290 N N   . GLY D 23  ? 0.6631 0.5477 0.4053 0.0145  0.1713  0.0298  23  GLY D N   
12291 C CA  . GLY D 23  ? 0.6704 0.5773 0.4463 0.0182  0.1692  0.0266  23  GLY D CA  
12292 C C   . GLY D 23  ? 0.6872 0.5830 0.4523 0.0221  0.1556  0.0187  23  GLY D C   
12293 O O   . GLY D 23  ? 0.7602 0.6679 0.5445 0.0272  0.1573  0.0152  23  GLY D O   
12294 N N   . GLU D 24  ? 0.6212 0.4944 0.3572 0.0197  0.1414  0.0163  24  GLU D N   
12295 C CA  . GLU D 24  ? 0.6264 0.4878 0.3523 0.0224  0.1271  0.0093  24  GLU D CA  
12296 C C   . GLU D 24  ? 0.6108 0.4849 0.3593 0.0176  0.1076  0.0095  24  GLU D C   
12297 O O   . GLU D 24  ? 0.5570 0.4332 0.3084 0.0117  0.1006  0.0140  24  GLU D O   
12298 C CB  . GLU D 24  ? 0.6909 0.5174 0.3695 0.0229  0.1231  0.0062  24  GLU D CB  
12299 C CG  . GLU D 24  ? 0.7937 0.6040 0.4458 0.0285  0.1432  0.0046  24  GLU D CG  
12300 C CD  . GLU D 24  ? 0.9165 0.6897 0.5169 0.0276  0.1401  0.0027  24  GLU D CD  
12301 O OE1 . GLU D 24  ? 1.0077 0.7646 0.5815 0.0316  0.1581  0.0021  24  GLU D OE1 
12302 O OE2 . GLU D 24  ? 0.9619 0.7217 0.5479 0.0231  0.1200  0.0022  24  GLU D OE2 
12303 N N   . TYR D 25  ? 0.5280 0.4104 0.2930 0.0206  0.1001  0.0049  25  TYR D N   
12304 C CA  . TYR D 25  ? 0.4939 0.3834 0.2752 0.0170  0.0820  0.0040  25  TYR D CA  
12305 C C   . TYR D 25  ? 0.4637 0.3280 0.2167 0.0153  0.0672  0.0016  25  TYR D C   
12306 O O   . TYR D 25  ? 0.4825 0.3298 0.2160 0.0189  0.0645  -0.0036 25  TYR D O   
12307 C CB  . TYR D 25  ? 0.4829 0.3878 0.2893 0.0207  0.0798  0.0004  25  TYR D CB  
12308 C CG  . TYR D 25  ? 0.5141 0.4469 0.3547 0.0201  0.0874  0.0040  25  TYR D CG  
12309 C CD1 . TYR D 25  ? 0.5070 0.4486 0.3540 0.0232  0.1045  0.0064  25  TYR D CD1 
12310 C CD2 . TYR D 25  ? 0.4446 0.3944 0.3110 0.0162  0.0773  0.0053  25  TYR D CD2 
12311 C CE1 . TYR D 25  ? 0.4486 0.4159 0.3284 0.0221  0.1095  0.0102  25  TYR D CE1 
12312 C CE2 . TYR D 25  ? 0.4202 0.3933 0.3152 0.0150  0.0826  0.0085  25  TYR D CE2 
12313 C CZ  . TYR D 25  ? 0.4177 0.3998 0.3199 0.0177  0.0977  0.0111  25  TYR D CZ  
12314 O OH  . TYR D 25  ? 0.3903 0.3957 0.3223 0.0160  0.1011  0.0147  25  TYR D OH  
12315 N N   . LEU D 26  ? 0.4612 0.3229 0.2132 0.0097  0.0566  0.0054  26  LEU D N   
12316 C CA  . LEU D 26  ? 0.5561 0.3932 0.2806 0.0076  0.0423  0.0046  26  LEU D CA  
12317 C C   . LEU D 26  ? 0.5676 0.4054 0.3047 0.0070  0.0246  0.0014  26  LEU D C   
12318 O O   . LEU D 26  ? 0.6245 0.4414 0.3401 0.0060  0.0117  -0.0002 26  LEU D O   
12319 C CB  . LEU D 26  ? 0.5897 0.4218 0.3068 0.0022  0.0390  0.0109  26  LEU D CB  
12320 C CG  . LEU D 26  ? 0.5936 0.4240 0.2979 0.0020  0.0569  0.0151  26  LEU D CG  
12321 C CD1 . LEU D 26  ? 0.6006 0.4211 0.2923 -0.0035 0.0521  0.0215  26  LEU D CD1 
12322 C CD2 . LEU D 26  ? 0.6560 0.4667 0.3277 0.0066  0.0685  0.0117  26  LEU D CD2 
12323 N N   . LEU D 27  ? 0.5420 0.4028 0.3131 0.0074  0.0236  0.0007  27  LEU D N   
12324 C CA  . LEU D 27  ? 0.5139 0.3778 0.3002 0.0076  0.0104  -0.0025 27  LEU D CA  
12325 C C   . LEU D 27  ? 0.5218 0.4013 0.3274 0.0117  0.0183  -0.0058 27  LEU D C   
12326 O O   . LEU D 27  ? 0.5213 0.4162 0.3394 0.0132  0.0314  -0.0042 27  LEU D O   
12327 C CB  . LEU D 27  ? 0.5080 0.3840 0.3180 0.0034  0.0002  0.0010  27  LEU D CB  
12328 C CG  . LEU D 27  ? 0.5639 0.4237 0.3580 -0.0004 -0.0112 0.0045  27  LEU D CG  
12329 C CD1 . LEU D 27  ? 0.5213 0.3949 0.3415 -0.0038 -0.0176 0.0082  27  LEU D CD1 
12330 C CD2 . LEU D 27  ? 0.5697 0.4091 0.3460 -0.0002 -0.0255 0.0016  27  LEU D CD2 
12331 N N   . PRO D 28  ? 0.4812 0.3566 0.2899 0.0136  0.0101  -0.0099 28  PRO D N   
12332 C CA  . PRO D 28  ? 0.4500 0.3378 0.2751 0.0178  0.0170  -0.0128 28  PRO D CA  
12333 C C   . PRO D 28  ? 0.4131 0.3222 0.2713 0.0163  0.0126  -0.0115 28  PRO D C   
12334 O O   . PRO D 28  ? 0.4164 0.3335 0.2873 0.0193  0.0151  -0.0137 28  PRO D O   
12335 C CB  . PRO D 28  ? 0.4073 0.2745 0.2135 0.0202  0.0099  -0.0180 28  PRO D CB  
12336 C CG  . PRO D 28  ? 0.4639 0.3181 0.2619 0.0155  -0.0070 -0.0171 28  PRO D CG  
12337 C CD  . PRO D 28  ? 0.4955 0.3511 0.2887 0.0120  -0.0056 -0.0120 28  PRO D CD  
12338 N N   . TRP D 29  ? 0.4067 0.3239 0.2775 0.0118  0.0070  -0.0080 29  TRP D N   
12339 C CA  . TRP D 29  ? 0.4119 0.3447 0.3099 0.0102  0.0018  -0.0073 29  TRP D CA  
12340 C C   . TRP D 29  ? 0.3335 0.2858 0.2505 0.0118  0.0116  -0.0068 29  TRP D C   
12341 O O   . TRP D 29  ? 0.3950 0.3562 0.3286 0.0124  0.0089  -0.0077 29  TRP D O   
12342 C CB  . TRP D 29  ? 0.3971 0.3321 0.3023 0.0056  -0.0047 -0.0038 29  TRP D CB  
12343 C CG  . TRP D 29  ? 0.4473 0.3641 0.3382 0.0038  -0.0174 -0.0035 29  TRP D CG  
12344 C CD1 . TRP D 29  ? 0.4715 0.3785 0.3497 0.0011  -0.0213 -0.0004 29  TRP D CD1 
12345 C CD2 . TRP D 29  ? 0.4896 0.3958 0.3786 0.0041  -0.0290 -0.0059 29  TRP D CD2 
12346 N NE1 . TRP D 29  ? 0.5374 0.4286 0.4059 -0.0001 -0.0351 -0.0005 29  TRP D NE1 
12347 C CE2 . TRP D 29  ? 0.5500 0.4406 0.4256 0.0015  -0.0403 -0.0039 29  TRP D CE2 
12348 C CE3 . TRP D 29  ? 0.4860 0.3942 0.3844 0.0060  -0.0316 -0.0091 29  TRP D CE3 
12349 C CZ2 . TRP D 29  ? 0.5439 0.4215 0.4159 0.0005  -0.0547 -0.0051 29  TRP D CZ2 
12350 C CZ3 . TRP D 29  ? 0.4883 0.3834 0.3831 0.0049  -0.0449 -0.0104 29  TRP D CZ3 
12351 C CH2 . TRP D 29  ? 0.5349 0.4152 0.4173 0.0020  -0.0567 -0.0084 29  TRP D CH2 
12352 N N   . THR D 30  ? 0.3420 0.3011 0.2575 0.0124  0.0226  -0.0048 30  THR D N   
12353 C CA  . THR D 30  ? 0.3854 0.3627 0.3197 0.0140  0.0304  -0.0039 30  THR D CA  
12354 C C   . THR D 30  ? 0.4090 0.3841 0.3430 0.0193  0.0326  -0.0071 30  THR D C   
12355 O O   . THR D 30  ? 0.3825 0.3694 0.3340 0.0203  0.0320  -0.0071 30  THR D O   
12356 C CB  . THR D 30  ? 0.3666 0.3519 0.3017 0.0135  0.0416  -0.0006 30  THR D CB  
12357 O OG1 . THR D 30  ? 0.3578 0.3456 0.2952 0.0081  0.0392  0.0025  30  THR D OG1 
12358 C CG2 . THR D 30  ? 0.3105 0.3149 0.2671 0.0150  0.0477  0.0008  30  THR D CG2 
12359 N N   . PHE D 31  ? 0.3811 0.3395 0.2939 0.0228  0.0350  -0.0099 31  PHE D N   
12360 C CA  . PHE D 31  ? 0.3792 0.3330 0.2904 0.0282  0.0373  -0.0134 31  PHE D CA  
12361 C C   . PHE D 31  ? 0.4249 0.3769 0.3446 0.0273  0.0258  -0.0154 31  PHE D C   
12362 O O   . PHE D 31  ? 0.4573 0.4176 0.3913 0.0298  0.0268  -0.0158 31  PHE D O   
12363 C CB  . PHE D 31  ? 0.3844 0.3165 0.2672 0.0318  0.0414  -0.0168 31  PHE D CB  
12364 C CG  . PHE D 31  ? 0.3698 0.2926 0.2477 0.0374  0.0427  -0.0213 31  PHE D CG  
12365 C CD1 . PHE D 31  ? 0.3805 0.3108 0.2660 0.0433  0.0552  -0.0213 31  PHE D CD1 
12366 C CD2 . PHE D 31  ? 0.3615 0.2673 0.2277 0.0368  0.0313  -0.0252 31  PHE D CD2 
12367 C CE1 . PHE D 31  ? 0.3996 0.3197 0.2803 0.0490  0.0568  -0.0255 31  PHE D CE1 
12368 C CE2 . PHE D 31  ? 0.3731 0.2684 0.2338 0.0417  0.0324  -0.0295 31  PHE D CE2 
12369 C CZ  . PHE D 31  ? 0.3735 0.2756 0.2409 0.0480  0.0454  -0.0298 31  PHE D CZ  
12370 N N   . PHE D 32  ? 0.3993 0.3401 0.3111 0.0236  0.0148  -0.0160 32  PHE D N   
12371 C CA  . PHE D 32  ? 0.3662 0.3030 0.2852 0.0227  0.0042  -0.0178 32  PHE D CA  
12372 C C   . PHE D 32  ? 0.3447 0.3002 0.2899 0.0207  0.0030  -0.0152 32  PHE D C   
12373 O O   . PHE D 32  ? 0.3825 0.3409 0.3382 0.0222  0.0012  -0.0161 32  PHE D O   
12374 C CB  . PHE D 32  ? 0.3889 0.3100 0.2953 0.0191  -0.0078 -0.0183 32  PHE D CB  
12375 C CG  . PHE D 32  ? 0.4538 0.3512 0.3327 0.0211  -0.0108 -0.0223 32  PHE D CG  
12376 C CD1 . PHE D 32  ? 0.5004 0.3895 0.3754 0.0245  -0.0110 -0.0262 32  PHE D CD1 
12377 C CD2 . PHE D 32  ? 0.4620 0.3436 0.3171 0.0193  -0.0138 -0.0221 32  PHE D CD2 
12378 C CE1 . PHE D 32  ? 0.5474 0.4121 0.3944 0.0262  -0.0140 -0.0306 32  PHE D CE1 
12379 C CE2 . PHE D 32  ? 0.5286 0.3859 0.3547 0.0207  -0.0170 -0.0261 32  PHE D CE2 
12380 C CZ  . PHE D 32  ? 0.5356 0.3839 0.3572 0.0241  -0.0170 -0.0307 32  PHE D CZ  
12381 N N   . HIS D 33  ? 0.3684 0.3353 0.3231 0.0173  0.0044  -0.0120 33  HIS D N   
12382 C CA  . HIS D 33  ? 0.3292 0.3117 0.3052 0.0154  0.0043  -0.0099 33  HIS D CA  
12383 C C   . HIS D 33  ? 0.3589 0.3539 0.3438 0.0182  0.0124  -0.0091 33  HIS D C   
12384 O O   . HIS D 33  ? 0.2657 0.2701 0.2649 0.0176  0.0116  -0.0080 33  HIS D O   
12385 C CB  . HIS D 33  ? 0.2376 0.2263 0.2194 0.0110  0.0034  -0.0073 33  HIS D CB  
12386 C CG  . HIS D 33  ? 0.2971 0.2768 0.2781 0.0083  -0.0059 -0.0072 33  HIS D CG  
12387 N ND1 . HIS D 33  ? 0.3506 0.3308 0.3443 0.0074  -0.0121 -0.0074 33  HIS D ND1 
12388 C CD2 . HIS D 33  ? 0.3583 0.3282 0.3285 0.0064  -0.0104 -0.0063 33  HIS D CD2 
12389 C CE1 . HIS D 33  ? 0.3085 0.2807 0.3015 0.0052  -0.0202 -0.0066 33  HIS D CE1 
12390 N NE2 . HIS D 33  ? 0.3656 0.3311 0.3438 0.0046  -0.0198 -0.0059 33  HIS D NE2 
12391 N N   . ALA D 34  ? 0.2877 0.2828 0.2649 0.0213  0.0203  -0.0091 34  ALA D N   
12392 C CA  . ALA D 34  ? 0.3215 0.3282 0.3097 0.0246  0.0271  -0.0079 34  ALA D CA  
12393 C C   . ALA D 34  ? 0.3431 0.3445 0.3330 0.0285  0.0248  -0.0100 34  ALA D C   
12394 O O   . ALA D 34  ? 0.2881 0.2993 0.2922 0.0289  0.0240  -0.0083 34  ALA D O   
12395 C CB  . ALA D 34  ? 0.3416 0.3496 0.3236 0.0276  0.0372  -0.0071 34  ALA D CB  
12396 N N   . VAL D 35  ? 0.2976 0.2821 0.2719 0.0311  0.0229  -0.0137 35  VAL D N   
12397 C CA  . VAL D 35  ? 0.3217 0.2998 0.2975 0.0347  0.0207  -0.0158 35  VAL D CA  
12398 C C   . VAL D 35  ? 0.3323 0.3112 0.3184 0.0311  0.0115  -0.0152 35  VAL D C   
12399 O O   . VAL D 35  ? 0.3433 0.3231 0.3376 0.0329  0.0102  -0.0151 35  VAL D O   
12400 C CB  . VAL D 35  ? 0.3506 0.3080 0.3049 0.0383  0.0212  -0.0204 35  VAL D CB  
12401 C CG1 . VAL D 35  ? 0.3051 0.2605 0.2471 0.0413  0.0318  -0.0207 35  VAL D CG1 
12402 C CG2 . VAL D 35  ? 0.4130 0.3549 0.3552 0.0343  0.0101  -0.0227 35  VAL D CG2 
12403 N N   . LYS D 36  ? 0.3428 0.3222 0.3304 0.0260  0.0058  -0.0143 36  LYS D N   
12404 C CA  . LYS D 36  ? 0.3340 0.3135 0.3325 0.0227  -0.0018 -0.0135 36  LYS D CA  
12405 C C   . LYS D 36  ? 0.3179 0.3131 0.3328 0.0201  0.0003  -0.0101 36  LYS D C   
12406 O O   . LYS D 36  ? 0.3582 0.3560 0.3834 0.0195  -0.0017 -0.0090 36  LYS D O   
12407 C CB  . LYS D 36  ? 0.2831 0.2527 0.2757 0.0191  -0.0099 -0.0143 36  LYS D CB  
12408 C CG  . LYS D 36  ? 0.3105 0.2770 0.3144 0.0165  -0.0180 -0.0139 36  LYS D CG  
12409 C CD  . LYS D 36  ? 0.2662 0.2226 0.2664 0.0133  -0.0275 -0.0142 36  LYS D CD  
12410 C CE  . LYS D 36  ? 0.2820 0.2470 0.2902 0.0102  -0.0272 -0.0114 36  LYS D CE  
12411 N NZ  . LYS D 36  ? 0.3078 0.2862 0.3362 0.0086  -0.0239 -0.0088 36  LYS D NZ  
12412 N N   . ASP D 37  ? 0.2955 0.2998 0.3116 0.0184  0.0043  -0.0084 37  ASP D N   
12413 C CA  . ASP D 37  ? 0.3561 0.3714 0.3840 0.0149  0.0049  -0.0059 37  ASP D CA  
12414 C C   . ASP D 37  ? 0.3573 0.3850 0.3894 0.0151  0.0106  -0.0037 37  ASP D C   
12415 O O   . ASP D 37  ? 0.2883 0.3231 0.3286 0.0140  0.0109  -0.0018 37  ASP D O   
12416 C CB  . ASP D 37  ? 0.2674 0.2807 0.2952 0.0110  0.0020  -0.0056 37  ASP D CB  
12417 C CG  . ASP D 37  ? 0.3170 0.3184 0.3420 0.0106  -0.0051 -0.0071 37  ASP D CG  
12418 O OD1 . ASP D 37  ? 0.2942 0.2942 0.3283 0.0101  -0.0085 -0.0068 37  ASP D OD1 
12419 O OD2 . ASP D 37  ? 0.3172 0.3100 0.3306 0.0107  -0.0077 -0.0082 37  ASP D OD2 
12420 N N   . TYR D 38  ? 0.2402 0.2701 0.2669 0.0161  0.0148  -0.0035 38  TYR D N   
12421 C CA  . TYR D 38  ? 0.3051 0.3478 0.3385 0.0146  0.0188  -0.0007 38  TYR D CA  
12422 C C   . TYR D 38  ? 0.2733 0.3238 0.3153 0.0175  0.0204  0.0012  38  TYR D C   
12423 O O   . TYR D 38  ? 0.2467 0.3071 0.2964 0.0149  0.0201  0.0039  38  TYR D O   
12424 C CB  . TYR D 38  ? 0.2907 0.3342 0.3183 0.0147  0.0237  -0.0003 38  TYR D CB  
12425 C CG  . TYR D 38  ? 0.3066 0.3438 0.3268 0.0110  0.0215  -0.0010 38  TYR D CG  
12426 C CD1 . TYR D 38  ? 0.2935 0.3306 0.3180 0.0070  0.0171  -0.0009 38  TYR D CD1 
12427 C CD2 . TYR D 38  ? 0.2978 0.3276 0.3061 0.0118  0.0243  -0.0015 38  TYR D CD2 
12428 C CE1 . TYR D 38  ? 0.3883 0.4193 0.4077 0.0041  0.0148  -0.0011 38  TYR D CE1 
12429 C CE2 . TYR D 38  ? 0.3474 0.3704 0.3486 0.0084  0.0214  -0.0014 38  TYR D CE2 
12430 C CZ  . TYR D 38  ? 0.3741 0.3981 0.3819 0.0048  0.0164  -0.0011 38  TYR D CZ  
12431 O OH  . TYR D 38  ? 0.3716 0.3886 0.3737 0.0020  0.0134  -0.0006 38  TYR D OH  
12432 N N   . TYR D 39  ? 0.2475 0.2929 0.2877 0.0226  0.0215  0.0000  39  TYR D N   
12433 C CA  . TYR D 39  ? 0.2260 0.2776 0.2753 0.0256  0.0219  0.0023  39  TYR D CA  
12434 C C   . TYR D 39  ? 0.2800 0.3288 0.3321 0.0238  0.0168  0.0028  39  TYR D C   
12435 O O   . TYR D 39  ? 0.2376 0.2935 0.2969 0.0230  0.0155  0.0059  39  TYR D O   
12436 C CB  . TYR D 39  ? 0.2309 0.2763 0.2772 0.0324  0.0258  0.0007  39  TYR D CB  
12437 C CG  . TYR D 39  ? 0.2293 0.2791 0.2856 0.0362  0.0254  0.0032  39  TYR D CG  
12438 C CD1 . TYR D 39  ? 0.2577 0.3203 0.3258 0.0382  0.0285  0.0071  39  TYR D CD1 
12439 C CD2 . TYR D 39  ? 0.2007 0.2420 0.2560 0.0375  0.0214  0.0023  39  TYR D CD2 
12440 C CE1 . TYR D 39  ? 0.2997 0.3661 0.3776 0.0419  0.0272  0.0101  39  TYR D CE1 
12441 C CE2 . TYR D 39  ? 0.2142 0.2586 0.2780 0.0408  0.0207  0.0052  39  TYR D CE2 
12442 C CZ  . TYR D 39  ? 0.3096 0.3664 0.3845 0.0432  0.0233  0.0091  39  TYR D CZ  
12443 O OH  . TYR D 39  ? 0.3507 0.4106 0.4351 0.0469  0.0218  0.0127  39  TYR D OH  
12444 N N   . ASP D 40  ? 0.2306 0.2688 0.2773 0.0228  0.0138  0.0001  40  ASP D N   
12445 C CA  . ASP D 40  ? 0.2560 0.2906 0.3067 0.0222  0.0104  0.0009  40  ASP D CA  
12446 C C   . ASP D 40  ? 0.2822 0.3208 0.3367 0.0171  0.0092  0.0026  40  ASP D C   
12447 O O   . ASP D 40  ? 0.3384 0.3767 0.3968 0.0166  0.0082  0.0046  40  ASP D O   
12448 C CB  . ASP D 40  ? 0.2287 0.2505 0.2745 0.0232  0.0072  -0.0022 40  ASP D CB  
12449 C CG  . ASP D 40  ? 0.3715 0.3868 0.4141 0.0285  0.0081  -0.0035 40  ASP D CG  
12450 O OD1 . ASP D 40  ? 0.3549 0.3708 0.4035 0.0301  0.0074  -0.0015 40  ASP D OD1 
12451 O OD2 . ASP D 40  ? 0.3384 0.3470 0.3717 0.0312  0.0098  -0.0064 40  ASP D OD2 
12452 N N   . MET D 41  ? 0.2084 0.2492 0.2611 0.0136  0.0097  0.0019  41  MET D N   
12453 C CA  . MET D 41  ? 0.2422 0.2857 0.2974 0.0093  0.0098  0.0032  41  MET D CA  
12454 C C   . MET D 41  ? 0.2349 0.2858 0.2913 0.0083  0.0106  0.0062  41  MET D C   
12455 O O   . MET D 41  ? 0.2081 0.2575 0.2651 0.0068  0.0104  0.0078  41  MET D O   
12456 C CB  . MET D 41  ? 0.2116 0.2550 0.2645 0.0061  0.0104  0.0018  41  MET D CB  
12457 C CG  . MET D 41  ? 0.2726 0.3077 0.3260 0.0060  0.0079  -0.0001 41  MET D CG  
12458 S SD  . MET D 41  ? 0.3385 0.3701 0.4005 0.0041  0.0076  0.0008  41  MET D SD  
12459 C CE  . MET D 41  ? 0.1991 0.2334 0.2614 0.0002  0.0109  0.0008  41  MET D CE  
12460 N N   . PRO D 42  ? 0.1874 0.2460 0.2445 0.0089  0.0112  0.0075  42  PRO D N   
12461 C CA  . PRO D 42  ? 0.1655 0.2307 0.2251 0.0080  0.0097  0.0110  42  PRO D CA  
12462 C C   . PRO D 42  ? 0.2899 0.3540 0.3528 0.0120  0.0084  0.0133  42  PRO D C   
12463 O O   . PRO D 42  ? 0.2359 0.3020 0.2988 0.0107  0.0060  0.0166  42  PRO D O   
12464 C CB  . PRO D 42  ? 0.2161 0.2906 0.2793 0.0077  0.0104  0.0122  42  PRO D CB  
12465 C CG  . PRO D 42  ? 0.1651 0.2368 0.2272 0.0108  0.0136  0.0095  42  PRO D CG  
12466 C CD  . PRO D 42  ? 0.2240 0.2858 0.2803 0.0096  0.0131  0.0064  42  PRO D CD  
12467 N N   . ALA D 43  ? 0.2301 0.2893 0.2943 0.0168  0.0094  0.0116  43  ALA D N   
12468 C CA  . ALA D 43  ? 0.2633 0.3202 0.3309 0.0208  0.0081  0.0138  43  ALA D CA  
12469 C C   . ALA D 43  ? 0.2601 0.3102 0.3257 0.0186  0.0065  0.0151  43  ALA D C   
12470 O O   . ALA D 43  ? 0.2347 0.2831 0.3025 0.0208  0.0050  0.0181  43  ALA D O   
12471 C CB  . ALA D 43  ? 0.2242 0.2750 0.2917 0.0264  0.0098  0.0110  43  ALA D CB  
12472 N N   . TYR D 44  ? 0.2168 0.2630 0.2794 0.0146  0.0074  0.0133  44  TYR D N   
12473 C CA  . TYR D 44  ? 0.2701 0.3109 0.3318 0.0121  0.0077  0.0151  44  TYR D CA  
12474 C C   . TYR D 44  ? 0.3032 0.3469 0.3609 0.0101  0.0068  0.0193  44  TYR D C   
12475 O O   . TYR D 44  ? 0.3370 0.3756 0.3929 0.0094  0.0070  0.0222  44  TYR D O   
12476 C CB  . TYR D 44  ? 0.2092 0.2471 0.2702 0.0083  0.0100  0.0129  44  TYR D CB  
12477 C CG  . TYR D 44  ? 0.2414 0.2734 0.3073 0.0091  0.0093  0.0103  44  TYR D CG  
12478 C CD1 . TYR D 44  ? 0.2540 0.2798 0.3251 0.0086  0.0095  0.0115  44  TYR D CD1 
12479 C CD2 . TYR D 44  ? 0.2073 0.2392 0.2725 0.0100  0.0080  0.0070  44  TYR D CD2 
12480 C CE1 . TYR D 44  ? 0.2333 0.2538 0.3104 0.0086  0.0072  0.0095  44  TYR D CE1 
12481 C CE2 . TYR D 44  ? 0.2302 0.2554 0.2986 0.0102  0.0055  0.0049  44  TYR D CE2 
12482 C CZ  . TYR D 44  ? 0.2192 0.2391 0.2944 0.0094  0.0046  0.0061  44  TYR D CZ  
12483 O OH  . TYR D 44  ? 0.2230 0.2365 0.3032 0.0090  0.0006  0.0045  44  TYR D OH  
12484 N N   . LEU D 45  ? 0.2729 0.3239 0.3286 0.0086  0.0055  0.0199  45  LEU D N   
12485 C CA  . LEU D 45  ? 0.2715 0.3243 0.3216 0.0058  0.0028  0.0239  45  LEU D CA  
12486 C C   . LEU D 45  ? 0.2546 0.3087 0.3085 0.0094  -0.0009 0.0284  45  LEU D C   
12487 O O   . LEU D 45  ? 0.3029 0.3553 0.3507 0.0073  -0.0041 0.0326  45  LEU D O   
12488 C CB  . LEU D 45  ? 0.2707 0.3309 0.3194 0.0027  0.0009  0.0234  45  LEU D CB  
12489 C CG  . LEU D 45  ? 0.2644 0.3215 0.3068 -0.0019 0.0041  0.0197  45  LEU D CG  
12490 C CD1 . LEU D 45  ? 0.2297 0.2940 0.2734 -0.0043 0.0025  0.0187  45  LEU D CD1 
12491 C CD2 . LEU D 45  ? 0.2384 0.2874 0.2689 -0.0061 0.0051  0.0208  45  LEU D CD2 
12492 N N   . LYS D 46  ? 0.2132 0.2689 0.2759 0.0151  -0.0007 0.0277  46  LYS D N   
12493 C CA  . LYS D 46  ? 0.3329 0.3882 0.4006 0.0195  -0.0036 0.0319  46  LYS D CA  
12494 C C   . LYS D 46  ? 0.3370 0.3820 0.4002 0.0189  -0.0034 0.0341  46  LYS D C   
12495 O O   . LYS D 46  ? 0.2641 0.3074 0.3281 0.0208  -0.0068 0.0391  46  LYS D O   
12496 C CB  . LYS D 46  ? 0.3389 0.3955 0.4155 0.0261  -0.0017 0.0296  46  LYS D CB  
12497 C CG  . LYS D 46  ? 0.3668 0.4340 0.4498 0.0276  -0.0005 0.0287  46  LYS D CG  
12498 C CD  . LYS D 46  ? 0.4802 0.5549 0.5742 0.0323  -0.0031 0.0336  46  LYS D CD  
12499 C CE  . LYS D 46  ? 0.5155 0.6001 0.6191 0.0354  0.0005  0.0325  46  LYS D CE  
12500 N NZ  . LYS D 46  ? 0.5691 0.6466 0.6696 0.0395  0.0068  0.0269  46  LYS D NZ  
12501 N N   . ASP D 47  ? 0.3014 0.3396 0.3614 0.0164  0.0003  0.0311  47  ASP D N   
12502 C CA  . ASP D 47  ? 0.3501 0.3788 0.4090 0.0160  0.0015  0.0332  47  ASP D CA  
12503 C C   . ASP D 47  ? 0.3511 0.3751 0.4012 0.0104  0.0047  0.0348  47  ASP D C   
12504 O O   . ASP D 47  ? 0.3948 0.4111 0.4436 0.0095  0.0065  0.0377  47  ASP D O   
12505 C CB  . ASP D 47  ? 0.3358 0.3590 0.4010 0.0179  0.0033  0.0291  47  ASP D CB  
12506 C CG  . ASP D 47  ? 0.4697 0.4933 0.5403 0.0238  0.0014  0.0271  47  ASP D CG  
12507 O OD1 . ASP D 47  ? 0.5056 0.5297 0.5785 0.0276  -0.0008 0.0305  47  ASP D OD1 
12508 O OD2 . ASP D 47  ? 0.5009 0.5231 0.5728 0.0248  0.0022  0.0222  47  ASP D OD2 
12509 N N   . PHE D 48  ? 0.3569 0.3843 0.4009 0.0067  0.0062  0.0328  48  PHE D N   
12510 C CA  . PHE D 48  ? 0.3018 0.3234 0.3371 0.0019  0.0112  0.0329  48  PHE D CA  
12511 C C   . PHE D 48  ? 0.3025 0.3252 0.3247 -0.0016 0.0092  0.0342  48  PHE D C   
12512 O O   . PHE D 48  ? 0.3514 0.3816 0.3750 -0.0018 0.0057  0.0323  48  PHE D O   
12513 C CB  . PHE D 48  ? 0.2927 0.3144 0.3339 0.0008  0.0160  0.0280  48  PHE D CB  
12514 C CG  . PHE D 48  ? 0.3039 0.3224 0.3567 0.0029  0.0170  0.0273  48  PHE D CG  
12515 C CD1 . PHE D 48  ? 0.3178 0.3294 0.3724 0.0015  0.0209  0.0304  48  PHE D CD1 
12516 C CD2 . PHE D 48  ? 0.3481 0.3695 0.4092 0.0060  0.0138  0.0238  48  PHE D CD2 
12517 C CE1 . PHE D 48  ? 0.3475 0.3558 0.4141 0.0027  0.0206  0.0300  48  PHE D CE1 
12518 C CE2 . PHE D 48  ? 0.3453 0.3618 0.4155 0.0073  0.0131  0.0230  48  PHE D CE2 
12519 C CZ  . PHE D 48  ? 0.2897 0.3001 0.3638 0.0055  0.0160  0.0262  48  PHE D CZ  
12520 N N   . GLU D 49  ? 0.3253 0.3396 0.3343 -0.0048 0.0111  0.0377  49  GLU D N   
12521 C CA  . GLU D 49  ? 0.3655 0.3774 0.3583 -0.0088 0.0075  0.0394  49  GLU D CA  
12522 C C   . GLU D 49  ? 0.3294 0.3373 0.3129 -0.0130 0.0134  0.0349  49  GLU D C   
12523 O O   . GLU D 49  ? 0.3702 0.3674 0.3382 -0.0164 0.0186  0.0356  49  GLU D O   
12524 C CB  . GLU D 49  ? 0.4639 0.4661 0.4431 -0.0103 0.0062  0.0456  49  GLU D CB  
12525 C CG  . GLU D 49  ? 0.6367 0.6408 0.6085 -0.0111 -0.0044 0.0501  49  GLU D CG  
12526 C CD  . GLU D 49  ? 0.7599 0.7765 0.7509 -0.0059 -0.0112 0.0511  49  GLU D CD  
12527 O OE1 . GLU D 49  ? 0.7897 0.8066 0.7920 -0.0013 -0.0098 0.0524  49  GLU D OE1 
12528 O OE2 . GLU D 49  ? 0.8364 0.8620 0.8316 -0.0064 -0.0172 0.0505  49  GLU D OE2 
12529 N N   . ILE D 50  ? 0.2820 0.2976 0.2748 -0.0124 0.0133  0.0303  50  ILE D N   
12530 C CA  . ILE D 50  ? 0.2799 0.2924 0.2659 -0.0158 0.0179  0.0258  50  ILE D CA  
12531 C C   . ILE D 50  ? 0.3236 0.3449 0.3130 -0.0167 0.0117  0.0236  50  ILE D C   
12532 O O   . ILE D 50  ? 0.2752 0.3058 0.2742 -0.0142 0.0054  0.0255  50  ILE D O   
12533 C CB  . ILE D 50  ? 0.2629 0.2742 0.2595 -0.0143 0.0262  0.0224  50  ILE D CB  
12534 C CG1 . ILE D 50  ? 0.2614 0.2821 0.2762 -0.0103 0.0231  0.0207  50  ILE D CG1 
12535 C CG2 . ILE D 50  ? 0.2571 0.2597 0.2519 -0.0143 0.0336  0.0250  50  ILE D CG2 
12536 C CD1 . ILE D 50  ? 0.2401 0.2601 0.2653 -0.0096 0.0285  0.0174  50  ILE D CD1 
12537 N N   . LYS D 51  ? 0.3037 0.3216 0.2858 -0.0202 0.0144  0.0198  51  LYS D N   
12538 C CA  . LYS D 51  ? 0.2282 0.2536 0.2145 -0.0217 0.0099  0.0175  51  LYS D CA  
12539 C C   . LYS D 51  ? 0.3137 0.3425 0.3122 -0.0195 0.0148  0.0135  51  LYS D C   
12540 O O   . LYS D 51  ? 0.2311 0.2530 0.2286 -0.0196 0.0220  0.0112  51  LYS D O   
12541 C CB  . LYS D 51  ? 0.3289 0.3467 0.2980 -0.0277 0.0083  0.0160  51  LYS D CB  
12542 C CG  . LYS D 51  ? 0.3635 0.3746 0.3162 -0.0308 0.0026  0.0200  51  LYS D CG  
12543 C CD  . LYS D 51  ? 0.3390 0.3620 0.3019 -0.0297 -0.0081 0.0246  51  LYS D CD  
12544 C CE  . LYS D 51  ? 0.4068 0.4230 0.3544 -0.0326 -0.0157 0.0297  51  LYS D CE  
12545 N NZ  . LYS D 51  ? 0.3934 0.3913 0.3151 -0.0367 -0.0112 0.0286  51  LYS D NZ  
12546 N N   . LEU D 52  ? 0.2506 0.2894 0.2606 -0.0176 0.0111  0.0132  52  LEU D N   
12547 C CA  . LEU D 52  ? 0.2182 0.2589 0.2366 -0.0163 0.0143  0.0097  52  LEU D CA  
12548 C C   . LEU D 52  ? 0.2973 0.3452 0.3182 -0.0181 0.0105  0.0092  52  LEU D C   
12549 O O   . LEU D 52  ? 0.2973 0.3532 0.3226 -0.0175 0.0057  0.0119  52  LEU D O   
12550 C CB  . LEU D 52  ? 0.2524 0.2961 0.2827 -0.0112 0.0151  0.0099  52  LEU D CB  
12551 C CG  . LEU D 52  ? 0.3081 0.3459 0.3406 -0.0092 0.0185  0.0108  52  LEU D CG  
12552 C CD1 . LEU D 52  ? 0.2805 0.3213 0.3236 -0.0047 0.0166  0.0110  52  LEU D CD1 
12553 C CD2 . LEU D 52  ? 0.2669 0.2978 0.2993 -0.0108 0.0248  0.0086  52  LEU D CD2 
12554 N N   . ASN D 53  ? 0.3125 0.3576 0.3320 -0.0204 0.0129  0.0061  53  ASN D N   
12555 C CA  . ASN D 53  ? 0.1871 0.2376 0.2088 -0.0230 0.0101  0.0057  53  ASN D CA  
12556 C C   . ASN D 53  ? 0.2638 0.3175 0.2945 -0.0199 0.0121  0.0044  53  ASN D C   
12557 O O   . ASN D 53  ? 0.2860 0.3354 0.3196 -0.0171 0.0151  0.0030  53  ASN D O   
12558 C CB  . ASN D 53  ? 0.2023 0.2451 0.2135 -0.0285 0.0107  0.0033  53  ASN D CB  
12559 C CG  . ASN D 53  ? 0.2965 0.3318 0.2942 -0.0314 0.0095  0.0039  53  ASN D CG  
12560 O OD1 . ASN D 53  ? 0.2875 0.3268 0.2826 -0.0336 0.0031  0.0068  53  ASN D OD1 
12561 N ND2 . ASN D 53  ? 0.2922 0.3165 0.2818 -0.0312 0.0158  0.0017  53  ASN D ND2 
12562 N N   . PHE D 54  ? 0.2559 0.3168 0.2910 -0.0209 0.0101  0.0054  54  PHE D N   
12563 C CA  . PHE D 54  ? 0.1946 0.2580 0.2355 -0.0182 0.0118  0.0049  54  PHE D CA  
12564 C C   . PHE D 54  ? 0.2053 0.2711 0.2464 -0.0222 0.0115  0.0051  54  PHE D C   
12565 O O   . PHE D 54  ? 0.2685 0.3394 0.3104 -0.0261 0.0087  0.0068  54  PHE D O   
12566 C CB  . PHE D 54  ? 0.1848 0.2554 0.2324 -0.0134 0.0114  0.0070  54  PHE D CB  
12567 C CG  . PHE D 54  ? 0.2778 0.3452 0.3256 -0.0095 0.0114  0.0071  54  PHE D CG  
12568 C CD1 . PHE D 54  ? 0.3452 0.4144 0.3923 -0.0098 0.0091  0.0094  54  PHE D CD1 
12569 C CD2 . PHE D 54  ? 0.2923 0.3537 0.3405 -0.0063 0.0130  0.0052  54  PHE D CD2 
12570 C CE1 . PHE D 54  ? 0.3652 0.4304 0.4124 -0.0065 0.0093  0.0099  54  PHE D CE1 
12571 C CE2 . PHE D 54  ? 0.3181 0.3760 0.3676 -0.0034 0.0127  0.0054  54  PHE D CE2 
12572 C CZ  . PHE D 54  ? 0.3174 0.3772 0.3665 -0.0035 0.0114  0.0078  54  PHE D CZ  
12573 N N   . ASN D 55  ? 0.2075 0.2693 0.2485 -0.0216 0.0137  0.0036  55  ASN D N   
12574 C CA  . ASN D 55  ? 0.2475 0.3116 0.2895 -0.0245 0.0142  0.0046  55  ASN D CA  
12575 C C   . ASN D 55  ? 0.2477 0.3157 0.2929 -0.0205 0.0163  0.0060  55  ASN D C   
12576 O O   . ASN D 55  ? 0.2654 0.3282 0.3084 -0.0164 0.0171  0.0046  55  ASN D O   
12577 C CB  . ASN D 55  ? 0.2883 0.3430 0.3258 -0.0270 0.0151  0.0024  55  ASN D CB  
12578 C CG  . ASN D 55  ? 0.2561 0.3123 0.2941 -0.0309 0.0154  0.0038  55  ASN D CG  
12579 O OD1 . ASN D 55  ? 0.2617 0.3221 0.3010 -0.0356 0.0135  0.0050  55  ASN D OD1 
12580 N ND2 . ASN D 55  ? 0.2374 0.2895 0.2744 -0.0295 0.0170  0.0040  55  ASN D ND2 
12581 N N   . LEU D 56  ? 0.2378 0.3140 0.2878 -0.0220 0.0174  0.0087  56  LEU D N   
12582 C CA  . LEU D 56  ? 0.2421 0.3205 0.2932 -0.0185 0.0215  0.0101  56  LEU D CA  
12583 C C   . LEU D 56  ? 0.2221 0.3011 0.2731 -0.0228 0.0236  0.0119  56  LEU D C   
12584 O O   . LEU D 56  ? 0.2522 0.3394 0.3107 -0.0270 0.0230  0.0144  56  LEU D O   
12585 C CB  . LEU D 56  ? 0.2899 0.3788 0.3496 -0.0152 0.0231  0.0126  56  LEU D CB  
12586 C CG  . LEU D 56  ? 0.2941 0.3836 0.3554 -0.0106 0.0213  0.0119  56  LEU D CG  
12587 C CD1 . LEU D 56  ? 0.3226 0.4234 0.3950 -0.0077 0.0232  0.0153  56  LEU D CD1 
12588 C CD2 . LEU D 56  ? 0.3158 0.3953 0.3691 -0.0059 0.0225  0.0090  56  LEU D CD2 
12589 N N   . THR D 57  ? 0.3008 0.3710 0.3439 -0.0220 0.0255  0.0111  57  THR D N   
12590 C CA  . THR D 57  ? 0.3076 0.3777 0.3501 -0.0260 0.0282  0.0136  57  THR D CA  
12591 C C   . THR D 57  ? 0.3378 0.4171 0.3860 -0.0244 0.0341  0.0171  57  THR D C   
12592 O O   . THR D 57  ? 0.1883 0.2686 0.2355 -0.0187 0.0372  0.0167  57  THR D O   
12593 C CB  . THR D 57  ? 0.2948 0.3521 0.3265 -0.0255 0.0281  0.0127  57  THR D CB  
12594 O OG1 . THR D 57  ? 0.2464 0.2992 0.2706 -0.0201 0.0305  0.0124  57  THR D OG1 
12595 C CG2 . THR D 57  ? 0.2797 0.3290 0.3092 -0.0259 0.0233  0.0096  57  THR D CG2 
12596 N N   . PRO D 58  ? 0.1897 0.2757 0.2453 -0.0294 0.0363  0.0206  58  PRO D N   
12597 C CA  . PRO D 58  ? 0.1990 0.2950 0.2632 -0.0278 0.0434  0.0245  58  PRO D CA  
12598 C C   . PRO D 58  ? 0.2506 0.3384 0.3028 -0.0229 0.0506  0.0245  58  PRO D C   
12599 O O   . PRO D 58  ? 0.2465 0.3397 0.3025 -0.0182 0.0573  0.0259  58  PRO D O   
12600 C CB  . PRO D 58  ? 0.1977 0.2999 0.2713 -0.0354 0.0436  0.0285  58  PRO D CB  
12601 C CG  . PRO D 58  ? 0.2125 0.3110 0.2850 -0.0406 0.0348  0.0260  58  PRO D CG  
12602 C CD  . PRO D 58  ? 0.2425 0.3275 0.3004 -0.0368 0.0325  0.0212  58  PRO D CD  
12603 N N   . VAL D 59  ? 0.2672 0.3412 0.3044 -0.0238 0.0494  0.0232  59  VAL D N   
12604 C CA  . VAL D 59  ? 0.2755 0.3391 0.2975 -0.0197 0.0552  0.0232  59  VAL D CA  
12605 C C   . VAL D 59  ? 0.2924 0.3514 0.3079 -0.0127 0.0542  0.0194  59  VAL D C   
12606 O O   . VAL D 59  ? 0.2419 0.2963 0.2486 -0.0081 0.0608  0.0193  59  VAL D O   
12607 C CB  . VAL D 59  ? 0.2314 0.2803 0.2387 -0.0225 0.0521  0.0232  59  VAL D CB  
12608 C CG1 . VAL D 59  ? 0.3180 0.3594 0.3221 -0.0220 0.0426  0.0192  59  VAL D CG1 
12609 C CG2 . VAL D 59  ? 0.2498 0.2863 0.2382 -0.0191 0.0581  0.0241  59  VAL D CG2 
12610 N N   . LEU D 60  ? 0.2122 0.2716 0.2316 -0.0120 0.0466  0.0162  60  LEU D N   
12611 C CA  . LEU D 60  ? 0.2124 0.2684 0.2281 -0.0059 0.0458  0.0132  60  LEU D CA  
12612 C C   . LEU D 60  ? 0.2098 0.2779 0.2372 -0.0023 0.0517  0.0147  60  LEU D C   
12613 O O   . LEU D 60  ? 0.2596 0.3233 0.2809 0.0035  0.0562  0.0134  60  LEU D O   
12614 C CB  . LEU D 60  ? 0.2149 0.2688 0.2333 -0.0061 0.0374  0.0102  60  LEU D CB  
12615 C CG  . LEU D 60  ? 0.2506 0.3026 0.2686 -0.0007 0.0358  0.0076  60  LEU D CG  
12616 C CD1 . LEU D 60  ? 0.3246 0.3622 0.3263 0.0032  0.0362  0.0053  60  LEU D CD1 
12617 C CD2 . LEU D 60  ? 0.2244 0.2766 0.2479 -0.0021 0.0288  0.0058  60  LEU D CD2 
12618 N N   . ILE D 61  ? 0.2874 0.3698 0.3317 -0.0057 0.0511  0.0176  61  ILE D N   
12619 C CA  . ILE D 61  ? 0.2165 0.3118 0.2757 -0.0025 0.0556  0.0201  61  ILE D CA  
12620 C C   . ILE D 61  ? 0.2098 0.3050 0.2668 0.0011  0.0670  0.0221  61  ILE D C   
12621 O O   . ILE D 61  ? 0.2385 0.3349 0.2977 0.0076  0.0726  0.0217  61  ILE D O   
12622 C CB  . ILE D 61  ? 0.2340 0.3438 0.3111 -0.0082 0.0515  0.0236  61  ILE D CB  
12623 C CG1 . ILE D 61  ? 0.2488 0.3563 0.3246 -0.0107 0.0415  0.0210  61  ILE D CG1 
12624 C CG2 . ILE D 61  ? 0.2624 0.3870 0.3584 -0.0051 0.0556  0.0274  61  ILE D CG2 
12625 C CD1 . ILE D 61  ? 0.2035 0.3209 0.2915 -0.0172 0.0360  0.0237  61  ILE D CD1 
12626 N N   . ASP D 62  ? 0.2368 0.3291 0.2885 -0.0030 0.0712  0.0244  62  ASP D N   
12627 C CA  . ASP D 62  ? 0.3239 0.4153 0.3722 -0.0002 0.0838  0.0270  62  ASP D CA  
12628 C C   . ASP D 62  ? 0.3229 0.3990 0.3512 0.0070  0.0881  0.0229  62  ASP D C   
12629 O O   . ASP D 62  ? 0.3861 0.4636 0.4161 0.0127  0.0984  0.0235  62  ASP D O   
12630 C CB  . ASP D 62  ? 0.3146 0.4011 0.3555 -0.0062 0.0865  0.0298  62  ASP D CB  
12631 C CG  . ASP D 62  ? 0.3618 0.4643 0.4243 -0.0128 0.0865  0.0350  62  ASP D CG  
12632 O OD1 . ASP D 62  ? 0.3925 0.5109 0.4765 -0.0117 0.0890  0.0379  62  ASP D OD1 
12633 O OD2 . ASP D 62  ? 0.4035 0.5019 0.4620 -0.0194 0.0834  0.0365  62  ASP D OD2 
12634 N N   . GLN D 63  ? 0.3684 0.4290 0.3782 0.0067  0.0801  0.0188  63  GLN D N   
12635 C CA  . GLN D 63  ? 0.3556 0.3991 0.3440 0.0123  0.0817  0.0146  63  GLN D CA  
12636 C C   . GLN D 63  ? 0.3180 0.3643 0.3134 0.0186  0.0815  0.0118  63  GLN D C   
12637 O O   . GLN D 63  ? 0.3454 0.3838 0.3311 0.0247  0.0893  0.0100  63  GLN D O   
12638 C CB  . GLN D 63  ? 0.3484 0.3765 0.3198 0.0096  0.0711  0.0117  63  GLN D CB  
12639 C CG  . GLN D 63  ? 0.3882 0.4100 0.3500 0.0042  0.0708  0.0144  63  GLN D CG  
12640 C CD  . GLN D 63  ? 0.3961 0.4037 0.3446 0.0022  0.0595  0.0120  63  GLN D CD  
12641 O OE1 . GLN D 63  ? 0.3958 0.3871 0.3246 0.0051  0.0572  0.0094  63  GLN D OE1 
12642 N NE2 . GLN D 63  ? 0.3154 0.3287 0.2751 -0.0026 0.0520  0.0129  63  GLN D NE2 
12643 N N   . ILE D 64  ? 0.3271 0.3828 0.3374 0.0172  0.0728  0.0114  64  ILE D N   
12644 C CA  . ILE D 64  ? 0.2967 0.3559 0.3153 0.0229  0.0724  0.0097  64  ILE D CA  
12645 C C   . ILE D 64  ? 0.2417 0.3118 0.2737 0.0275  0.0838  0.0128  64  ILE D C   
12646 O O   . ILE D 64  ? 0.3375 0.4022 0.3663 0.0346  0.0893  0.0107  64  ILE D O   
12647 C CB  . ILE D 64  ? 0.3011 0.3700 0.3342 0.0198  0.0623  0.0102  64  ILE D CB  
12648 C CG1 . ILE D 64  ? 0.2519 0.3088 0.2730 0.0172  0.0527  0.0066  64  ILE D CG1 
12649 C CG2 . ILE D 64  ? 0.2613 0.3375 0.3074 0.0253  0.0634  0.0106  64  ILE D CG2 
12650 C CD1 . ILE D 64  ? 0.2722 0.3371 0.3054 0.0134  0.0443  0.0072  64  ILE D CD1 
12651 N N   . GLN D 65  ? 0.2352 0.3207 0.2841 0.0237  0.0875  0.0179  65  GLN D N   
12652 C CA  . GLN D 65  ? 0.2389 0.3366 0.3049 0.0279  0.0988  0.0219  65  GLN D CA  
12653 C C   . GLN D 65  ? 0.3217 0.4064 0.3707 0.0337  0.1123  0.0202  65  GLN D C   
12654 O O   . GLN D 65  ? 0.2687 0.3557 0.3248 0.0410  0.1217  0.0204  65  GLN D O   
12655 C CB  . GLN D 65  ? 0.2566 0.3713 0.3423 0.0214  0.1000  0.0280  65  GLN D CB  
12656 C CG  . GLN D 65  ? 0.3267 0.4567 0.4337 0.0174  0.0888  0.0305  65  GLN D CG  
12657 C CD  . GLN D 65  ? 0.3249 0.4704 0.4512 0.0103  0.0886  0.0364  65  GLN D CD  
12658 O OE1 . GLN D 65  ? 0.2886 0.4298 0.4066 0.0042  0.0884  0.0370  65  GLN D OE1 
12659 N NE2 . GLN D 65  ? 0.2822 0.4455 0.4351 0.0110  0.0881  0.0413  65  GLN D NE2 
12660 N N   . GLU D 66  ? 0.3045 0.3741 0.3299 0.0307  0.1135  0.0186  66  GLU D N   
12661 C CA  . GLU D 66  ? 0.3689 0.4234 0.3733 0.0355  0.1266  0.0171  66  GLU D CA  
12662 C C   . GLU D 66  ? 0.3893 0.4264 0.3754 0.0426  0.1261  0.0108  66  GLU D C   
12663 O O   . GLU D 66  ? 0.3412 0.3733 0.3235 0.0498  0.1386  0.0097  66  GLU D O   
12664 C CB  . GLU D 66  ? 0.3800 0.4212 0.3620 0.0299  0.1262  0.0176  66  GLU D CB  
12665 C CG  . GLU D 66  ? 0.4966 0.5202 0.4532 0.0339  0.1401  0.0166  66  GLU D CG  
12666 C CD  . GLU D 66  ? 0.5696 0.5841 0.5091 0.0277  0.1416  0.0195  66  GLU D CD  
12667 O OE1 . GLU D 66  ? 0.5919 0.5930 0.5109 0.0302  0.1546  0.0201  66  GLU D OE1 
12668 O OE2 . GLU D 66  ? 0.5059 0.5252 0.4511 0.0206  0.1305  0.0213  66  GLU D OE2 
12669 N N   . TYR D 67  ? 0.3666 0.3939 0.3420 0.0406  0.1120  0.0066  67  TYR D N   
12670 C CA  . TYR D 67  ? 0.4386 0.4500 0.3993 0.0463  0.1093  0.0008  67  TYR D CA  
12671 C C   . TYR D 67  ? 0.4415 0.4639 0.4228 0.0530  0.1141  0.0012  67  TYR D C   
12672 O O   . TYR D 67  ? 0.4734 0.4838 0.4441 0.0603  0.1219  -0.0022 67  TYR D O   
12673 C CB  . TYR D 67  ? 0.4383 0.4424 0.3923 0.0421  0.0928  -0.0023 67  TYR D CB  
12674 C CG  . TYR D 67  ? 0.4310 0.4159 0.3582 0.0382  0.0871  -0.0044 67  TYR D CG  
12675 C CD1 . TYR D 67  ? 0.3641 0.3250 0.2631 0.0416  0.0874  -0.0093 67  TYR D CD1 
12676 C CD2 . TYR D 67  ? 0.3758 0.3653 0.3053 0.0311  0.0808  -0.0015 67  TYR D CD2 
12677 C CE1 . TYR D 67  ? 0.3835 0.3265 0.2582 0.0377  0.0804  -0.0106 67  TYR D CE1 
12678 C CE2 . TYR D 67  ? 0.3301 0.3019 0.2362 0.0278  0.0748  -0.0027 67  TYR D CE2 
12679 C CZ  . TYR D 67  ? 0.3952 0.3443 0.2745 0.0310  0.0739  -0.0070 67  TYR D CZ  
12680 O OH  . TYR D 67  ? 0.4115 0.3429 0.2681 0.0273  0.0661  -0.0076 67  TYR D OH  
12681 N N   . ALA D 68  ? 0.3920 0.4359 0.4017 0.0507  0.1092  0.0054  68  ALA D N   
12682 C CA  . ALA D 68  ? 0.3618 0.4167 0.3925 0.0568  0.1116  0.0067  68  ALA D CA  
12683 C C   . ALA D 68  ? 0.3644 0.4245 0.4043 0.0634  0.1285  0.0092  68  ALA D C   
12684 O O   . ALA D 68  ? 0.4437 0.5030 0.4909 0.0713  0.1339  0.0082  68  ALA D O   
12685 C CB  . ALA D 68  ? 0.3491 0.4250 0.4063 0.0520  0.1020  0.0114  68  ALA D CB  
12686 N N   . GLN D 69  ? 0.4325 0.4976 0.4732 0.0606  0.1377  0.0127  69  GLN D N   
12687 C CA  . GLN D 69  ? 0.4897 0.5584 0.5382 0.0672  0.1560  0.0152  69  GLN D CA  
12688 C C   . GLN D 69  ? 0.5034 0.5460 0.5187 0.0730  0.1671  0.0094  69  GLN D C   
12689 O O   . GLN D 69  ? 0.5072 0.5493 0.5251 0.0795  0.1845  0.0106  69  GLN D O   
12690 C CB  . GLN D 69  ? 0.5422 0.6269 0.6063 0.0617  0.1628  0.0220  69  GLN D CB  
12691 C CG  . GLN D 69  ? 0.6224 0.7335 0.7220 0.0566  0.1539  0.0284  69  GLN D CG  
12692 C CD  . GLN D 69  ? 0.7294 0.8503 0.8355 0.0473  0.1529  0.0333  69  GLN D CD  
12693 O OE1 . GLN D 69  ? 0.7533 0.8894 0.8783 0.0407  0.1416  0.0368  69  GLN D OE1 
12694 N NE2 . GLN D 69  ? 0.7842 0.8949 0.8730 0.0467  0.1648  0.0336  69  GLN D NE2 
12695 N N   . GLY D 70  ? 0.5179 0.5385 0.5025 0.0709  0.1577  0.0033  70  GLY D N   
12696 C CA  . GLY D 70  ? 0.5489 0.5419 0.4978 0.0752  0.1659  -0.0024 70  GLY D CA  
12697 C C   . GLY D 70  ? 0.5917 0.5764 0.5215 0.0723  0.1765  -0.0005 70  GLY D C   
12698 O O   . GLY D 70  ? 0.6480 0.6096 0.5477 0.0766  0.1868  -0.0045 70  GLY D O   
12699 N N   . LYS D 71  ? 0.5867 0.5878 0.5313 0.0649  0.1742  0.0055  71  LYS D N   
12700 C CA  . LYS D 71  ? 0.6237 0.6189 0.5533 0.0613  0.1842  0.0087  71  LYS D CA  
12701 C C   . LYS D 71  ? 0.6526 0.6305 0.5536 0.0540  0.1714  0.0067  71  LYS D C   
12702 O O   . LYS D 71  ? 0.7059 0.6787 0.5942 0.0498  0.1770  0.0101  71  LYS D O   
12703 C CB  . LYS D 71  ? 0.5649 0.5878 0.5292 0.0571  0.1897  0.0171  71  LYS D CB  
12704 N N   . ALA D 72  ? 0.5726 0.5416 0.4647 0.0525  0.1544  0.0019  72  ALA D N   
12705 C CA  . ALA D 72  ? 0.5264 0.4810 0.3964 0.0459  0.1406  0.0006  72  ALA D CA  
12706 C C   . ALA D 72  ? 0.5986 0.5215 0.4277 0.0488  0.1412  -0.0051 72  ALA D C   
12707 O O   . ALA D 72  ? 0.6050 0.5164 0.4253 0.0539  0.1387  -0.0108 72  ALA D O   
12708 C CB  . ALA D 72  ? 0.5023 0.4653 0.3875 0.0423  0.1220  -0.0009 72  ALA D CB  
12709 N N   . LYS D 73  ? 0.6230 0.5305 0.4258 0.0453  0.1441  -0.0034 73  LYS D N   
12710 C CA  . LYS D 73  ? 0.6326 0.5073 0.3921 0.0469  0.1430  -0.0084 73  LYS D CA  
12711 C C   . LYS D 73  ? 0.6400 0.5044 0.3878 0.0403  0.1216  -0.0093 73  LYS D C   
12712 O O   . LYS D 73  ? 0.6893 0.5535 0.4326 0.0343  0.1172  -0.0049 73  LYS D O   
12713 C CB  . LYS D 73  ? 0.7287 0.5902 0.4637 0.0476  0.1603  -0.0056 73  LYS D CB  
12714 C CG  . LYS D 73  ? 0.7816 0.6657 0.5444 0.0506  0.1802  -0.0004 73  LYS D CG  
12715 C CD  . LYS D 73  ? 0.9216 0.7936 0.6616 0.0503  0.1977  0.0035  73  LYS D CD  
12716 C CE  . LYS D 73  ? 0.9534 0.8537 0.7287 0.0479  0.2098  0.0117  73  LYS D CE  
12717 N NZ  . LYS D 73  ? 0.9949 0.8835 0.7481 0.0448  0.2229  0.0168  73  LYS D NZ  
12718 N N   . ASP D 74  ? 0.6143 0.4705 0.3590 0.0416  0.1085  -0.0147 74  ASP D N   
12719 C CA  . ASP D 74  ? 0.5616 0.4133 0.3054 0.0359  0.0876  -0.0153 74  ASP D CA  
12720 C C   . ASP D 74  ? 0.5685 0.3869 0.2711 0.0358  0.0800  -0.0198 74  ASP D C   
12721 O O   . ASP D 74  ? 0.5967 0.4002 0.2855 0.0402  0.0798  -0.0257 74  ASP D O   
12722 C CB  . ASP D 74  ? 0.4971 0.3646 0.2698 0.0370  0.0784  -0.0175 74  ASP D CB  
12723 C CG  . ASP D 74  ? 0.5718 0.4377 0.3493 0.0315  0.0583  -0.0176 74  ASP D CG  
12724 O OD1 . ASP D 74  ? 0.5936 0.4377 0.3456 0.0289  0.0477  -0.0192 74  ASP D OD1 
12725 O OD2 . ASP D 74  ? 0.5616 0.4483 0.3696 0.0299  0.0530  -0.0160 74  ASP D OD2 
12726 N N   . VAL D 75  ? 0.6386 0.4437 0.3204 0.0305  0.0731  -0.0168 75  VAL D N   
12727 C CA  . VAL D 75  ? 0.7162 0.4869 0.3536 0.0303  0.0677  -0.0203 75  VAL D CA  
12728 C C   . VAL D 75  ? 0.7101 0.4689 0.3439 0.0299  0.0495  -0.0258 75  VAL D C   
12729 O O   . VAL D 75  ? 0.7065 0.4399 0.3104 0.0328  0.0489  -0.0316 75  VAL D O   
12730 C CB  . VAL D 75  ? 0.7292 0.4881 0.3461 0.0243  0.0619  -0.0150 75  VAL D CB  
12731 C CG1 . VAL D 75  ? 0.7410 0.5130 0.3647 0.0241  0.0802  -0.0090 75  VAL D CG1 
12732 C CG2 . VAL D 75  ? 0.6800 0.4475 0.3156 0.0184  0.0415  -0.0121 75  VAL D CG2 
12733 N N   . PHE D 76  ? 0.6862 0.4627 0.3506 0.0265  0.0352  -0.0241 76  PHE D N   
12734 C CA  . PHE D 76  ? 0.7112 0.4778 0.3754 0.0255  0.0181  -0.0284 76  PHE D CA  
12735 C C   . PHE D 76  ? 0.6609 0.4295 0.3327 0.0315  0.0252  -0.0340 76  PHE D C   
12736 O O   . PHE D 76  ? 0.6715 0.4193 0.3250 0.0324  0.0170  -0.0394 76  PHE D O   
12737 C CB  . PHE D 76  ? 0.7583 0.5439 0.4549 0.0206  0.0032  -0.0247 76  PHE D CB  
12738 C CG  . PHE D 76  ? 0.8611 0.6367 0.5592 0.0186  -0.0152 -0.0279 76  PHE D CG  
12739 C CD1 . PHE D 76  ? 0.9280 0.6806 0.6025 0.0143  -0.0317 -0.0277 76  PHE D CD1 
12740 C CD2 . PHE D 76  ? 0.8809 0.6694 0.6043 0.0207  -0.0166 -0.0305 76  PHE D CD2 
12741 C CE1 . PHE D 76  ? 0.9652 0.7091 0.6436 0.0119  -0.0494 -0.0302 76  PHE D CE1 
12742 C CE2 . PHE D 76  ? 0.9096 0.6891 0.6361 0.0183  -0.0331 -0.0329 76  PHE D CE2 
12743 C CZ  . PHE D 76  ? 0.9569 0.7146 0.6620 0.0139  -0.0496 -0.0328 76  PHE D CZ  
12744 N N   . LEU D 77  ? 0.6275 0.4200 0.3257 0.0354  0.0400  -0.0324 77  LEU D N   
12745 C CA  . LEU D 77  ? 0.6368 0.4331 0.3456 0.0415  0.0469  -0.0367 77  LEU D CA  
12746 C C   . LEU D 77  ? 0.7008 0.4719 0.3759 0.0474  0.0590  -0.0420 77  LEU D C   
12747 O O   . LEU D 77  ? 0.7695 0.5306 0.4409 0.0516  0.0586  -0.0475 77  LEU D O   
12748 C CB  . LEU D 77  ? 0.6286 0.4570 0.3748 0.0438  0.0584  -0.0326 77  LEU D CB  
12749 C CG  . LEU D 77  ? 0.6296 0.4689 0.3979 0.0487  0.0607  -0.0350 77  LEU D CG  
12750 C CD1 . LEU D 77  ? 0.5982 0.4293 0.3687 0.0462  0.0431  -0.0382 77  LEU D CD1 
12751 C CD2 . LEU D 77  ? 0.6229 0.4944 0.4286 0.0485  0.0667  -0.0296 77  LEU D CD2 
12752 N N   . GLU D 78  ? 0.7227 0.4818 0.3719 0.0479  0.0705  -0.0406 78  GLU D N   
12753 C CA  . GLU D 78  ? 0.8158 0.5465 0.4275 0.0533  0.0824  -0.0461 78  GLU D CA  
12754 C C   . GLU D 78  ? 0.7924 0.4892 0.3675 0.0504  0.0655  -0.0518 78  GLU D C   
12755 O O   . GLU D 78  ? 0.8212 0.4950 0.3729 0.0550  0.0687  -0.0587 78  GLU D O   
12756 C CB  . GLU D 78  ? 0.9468 0.6724 0.5390 0.0541  0.0998  -0.0426 78  GLU D CB  
12757 C CG  . GLU D 78  ? 1.0445 0.7915 0.6608 0.0608  0.1233  -0.0403 78  GLU D CG  
12758 C CD  . GLU D 78  ? 1.1502 0.9164 0.7805 0.0577  0.1335  -0.0321 78  GLU D CD  
12759 O OE1 . GLU D 78  ? 1.1858 0.9435 0.7993 0.0511  0.1251  -0.0289 78  GLU D OE1 
12760 O OE2 . GLU D 78  ? 1.1624 0.9525 0.8222 0.0615  0.1491  -0.0287 78  GLU D OE2 
12761 N N   . ALA D 79  ? 0.7695 0.4622 0.3399 0.0428  0.0467  -0.0489 79  ALA D N   
12762 C CA  . ALA D 79  ? 0.7755 0.4395 0.3187 0.0390  0.0266  -0.0534 79  ALA D CA  
12763 C C   . ALA D 79  ? 0.7604 0.4285 0.3237 0.0405  0.0175  -0.0579 79  ALA D C   
12764 O O   . ALA D 79  ? 0.8124 0.4528 0.3495 0.0405  0.0085  -0.0642 79  ALA D O   
12765 C CB  . ALA D 79  ? 0.7315 0.3963 0.2760 0.0307  0.0075  -0.0480 79  ALA D CB  
12766 N N   . ILE D 80  ? 0.7490 0.4498 0.3572 0.0415  0.0198  -0.0548 80  ILE D N   
12767 C CA  . ILE D 80  ? 0.7041 0.4095 0.3322 0.0435  0.0139  -0.0584 80  ILE D CA  
12768 C C   . ILE D 80  ? 0.6881 0.3817 0.3031 0.0518  0.0300  -0.0643 80  ILE D C   
12769 O O   . ILE D 80  ? 0.7618 0.4359 0.3644 0.0533  0.0235  -0.0704 80  ILE D O   
12770 C CB  . ILE D 80  ? 0.6696 0.4118 0.3463 0.0424  0.0130  -0.0531 80  ILE D CB  
12771 C CG1 . ILE D 80  ? 0.6816 0.4330 0.3723 0.0345  -0.0042 -0.0482 80  ILE D CG1 
12772 C CG2 . ILE D 80  ? 0.5862 0.3338 0.2826 0.0462  0.0126  -0.0564 80  ILE D CG2 
12773 C CD1 . ILE D 80  ? 0.6844 0.4216 0.3726 0.0301  -0.0247 -0.0506 80  ILE D CD1 
12774 N N   . ARG D 81  ? 0.6709 0.3761 0.2903 0.0575  0.0514  -0.0624 81  ARG D N   
12775 C CA  . ARG D 81  ? 0.7707 0.4712 0.3883 0.0665  0.0684  -0.0668 81  ARG D CA  
12776 C C   . ARG D 81  ? 0.8589 0.5189 0.4278 0.0696  0.0719  -0.0747 81  ARG D C   
12777 O O   . ARG D 81  ? 0.8874 0.5339 0.4502 0.0754  0.0761  -0.0808 81  ARG D O   
12778 C CB  . ARG D 81  ? 0.8026 0.5269 0.4400 0.0714  0.0900  -0.0619 81  ARG D CB  
12779 C CG  . ARG D 81  ? 0.8838 0.6101 0.5299 0.0813  0.1081  -0.0648 81  ARG D CG  
12780 C CD  . ARG D 81  ? 0.9502 0.7006 0.6176 0.0853  0.1285  -0.0589 81  ARG D CD  
12781 N NE  . ARG D 81  ? 0.9769 0.7573 0.6747 0.0787  0.1218  -0.0510 81  ARG D NE  
12782 C CZ  . ARG D 81  ? 0.9872 0.7973 0.7261 0.0780  0.1172  -0.0469 81  ARG D CZ  
12783 N NH1 . ARG D 81  ? 0.9960 0.8112 0.7526 0.0834  0.1181  -0.0490 81  ARG D NH1 
12784 N NH2 . ARG D 81  ? 0.9381 0.7712 0.6989 0.0717  0.1116  -0.0404 81  ARG D NH2 
12785 N N   . LYS D 82  ? 0.8779 0.5036 0.3771 0.0536  0.0687  -0.0414 82  LYS D N   
12786 C CA  . LYS D 82  ? 0.8952 0.4953 0.3496 0.0566  0.0670  -0.0451 82  LYS D CA  
12787 C C   . LYS D 82  ? 0.8920 0.4791 0.3377 0.0563  0.0503  -0.0532 82  LYS D C   
12788 O O   . LYS D 82  ? 0.8392 0.4340 0.3084 0.0521  0.0347  -0.0540 82  LYS D O   
12789 C CB  . LYS D 82  ? 0.9192 0.5021 0.3450 0.0559  0.0610  -0.0378 82  LYS D CB  
12790 C CG  . LYS D 82  ? 0.9574 0.5466 0.3836 0.0543  0.0784  -0.0299 82  LYS D CG  
12791 C CD  . LYS D 82  ? 0.9562 0.5212 0.3469 0.0548  0.0719  -0.0239 82  LYS D CD  
12792 C CE  . LYS D 82  ? 0.9524 0.5204 0.3441 0.0509  0.0868  -0.0151 82  LYS D CE  
12793 N NZ  . LYS D 82  ? 0.9548 0.4956 0.3093 0.0524  0.0809  -0.0104 82  LYS D NZ  
12794 N N   . ASP D 83  ? 0.8794 0.4567 0.3078 0.0587  0.0525  -0.0566 83  ASP D N   
12795 C CA  . ASP D 83  ? 0.9263 0.4843 0.3353 0.0572  0.0355  -0.0632 83  ASP D CA  
12796 C C   . ASP D 83  ? 0.9344 0.4757 0.3182 0.0556  0.0174  -0.0612 83  ASP D C   
12797 O O   . ASP D 83  ? 0.9566 0.4916 0.3229 0.0581  0.0215  -0.0542 83  ASP D O   
12798 C CB  . ASP D 83  ? 0.9975 0.5468 0.3902 0.0611  0.0419  -0.0651 83  ASP D CB  
12799 C CG  . ASP D 83  ? 1.0637 0.5949 0.4414 0.0586  0.0268  -0.0726 83  ASP D CG  
12800 O OD1 . ASP D 83  ? 1.0862 0.6013 0.4434 0.0554  0.0091  -0.0744 83  ASP D OD1 
12801 O OD2 . ASP D 83  ? 1.1203 0.6538 0.5070 0.0600  0.0321  -0.0768 83  ASP D OD2 
12802 N N   . PRO D 84  ? 0.9267 0.4659 0.3161 0.0508  -0.0032 -0.0662 84  PRO D N   
12803 C CA  . PRO D 84  ? 0.9528 0.4873 0.3325 0.0501  -0.0230 -0.0629 84  PRO D CA  
12804 C C   . PRO D 84  ? 1.0504 0.5560 0.3795 0.0550  -0.0270 -0.0628 84  PRO D C   
12805 O O   . PRO D 84  ? 1.0972 0.5954 0.4098 0.0579  -0.0374 -0.0576 84  PRO D O   
12806 C CB  . PRO D 84  ? 0.9494 0.4928 0.3511 0.0427  -0.0429 -0.0703 84  PRO D CB  
12807 C CG  . PRO D 84  ? 0.8526 0.4146 0.2921 0.0390  -0.0306 -0.0724 84  PRO D CG  
12808 C CD  . PRO D 84  ? 0.8508 0.4019 0.2709 0.0450  -0.0082 -0.0728 84  PRO D CD  
12809 N N   . ASP D 85  ? 1.0780 0.5743 0.3955 0.0561  -0.0186 -0.0655 85  ASP D N   
12810 C CA  . ASP D 85  ? 1.1100 0.5863 0.3943 0.0605  -0.0202 -0.0629 85  ASP D CA  
12811 C C   . ASP D 85  ? 1.0839 0.5596 0.3598 0.0648  -0.0040 -0.0530 85  ASP D C   
12812 O O   . ASP D 85  ? 1.0781 0.5356 0.3255 0.0684  -0.0065 -0.0496 85  ASP D O   
12813 C CB  . ASP D 85  ? 1.1297 0.5962 0.4036 0.0615  -0.0137 -0.0679 85  ASP D CB  
12814 C CG  . ASP D 85  ? 1.1464 0.6063 0.4200 0.0559  -0.0312 -0.0773 85  ASP D CG  
12815 O OD1 . ASP D 85  ? 1.1653 0.6260 0.4406 0.0514  -0.0517 -0.0805 85  ASP D OD1 
12816 O OD2 . ASP D 85  ? 1.1789 0.6338 0.4515 0.0558  -0.0248 -0.0817 85  ASP D OD2 
12817 N N   . ASP D 86  ? 1.0295 0.5242 0.3300 0.0638  0.0130  -0.0488 86  ASP D N   
12818 C CA  . ASP D 86  ? 1.0655 0.5624 0.3630 0.0650  0.0295  -0.0399 86  ASP D CA  
12819 C C   . ASP D 86  ? 1.0359 0.5328 0.3344 0.0644  0.0227  -0.0331 86  ASP D C   
12820 O O   . ASP D 86  ? 1.0303 0.5262 0.3250 0.0640  0.0356  -0.0252 86  ASP D O   
12821 C CB  . ASP D 86  ? 1.0812 0.6017 0.4070 0.0638  0.0525  -0.0395 86  ASP D CB  
12822 C CG  . ASP D 86  ? 1.1024 0.6254 0.4298 0.0664  0.0587  -0.0459 86  ASP D CG  
12823 O OD1 . ASP D 86  ? 1.1254 0.6282 0.4253 0.0690  0.0516  -0.0484 86  ASP D OD1 
12824 O OD2 . ASP D 86  ? 1.0945 0.6394 0.4503 0.0665  0.0704  -0.0484 86  ASP D OD2 
12825 N N   . LEU D 87  ? 1.0054 0.5040 0.3095 0.0640  0.0026  -0.0360 87  LEU D N   
12826 C CA  . LEU D 87  ? 0.9712 0.4723 0.2793 0.0651  -0.0056 -0.0292 87  LEU D CA  
12827 C C   . LEU D 87  ? 0.9968 0.4757 0.2721 0.0703  -0.0167 -0.0236 87  LEU D C   
12828 O O   . LEU D 87  ? 1.0022 0.4681 0.2580 0.0731  -0.0336 -0.0284 87  LEU D O   
12829 C CB  . LEU D 87  ? 0.9323 0.4570 0.2818 0.0622  -0.0247 -0.0329 87  LEU D CB  
12830 C CG  . LEU D 87  ? 0.9147 0.4659 0.3095 0.0567  -0.0153 -0.0367 87  LEU D CG  
12831 C CD1 . LEU D 87  ? 0.8785 0.4501 0.3094 0.0535  -0.0348 -0.0398 87  LEU D CD1 
12832 C CD2 . LEU D 87  ? 0.8979 0.4630 0.3132 0.0559  0.0057  -0.0293 87  LEU D CD2 
12833 N N   . GLU D 88  ? 0.9988 0.4736 0.2703 0.0716  -0.0082 -0.0139 88  GLU D N   
12834 C CA  . GLU D 88  ? 1.0880 0.5425 0.3327 0.0779  -0.0204 -0.0081 88  GLU D CA  
12835 C C   . GLU D 88  ? 1.1165 0.5772 0.3672 0.0831  -0.0478 -0.0094 88  GLU D C   
12836 O O   . GLU D 88  ? 1.0455 0.5341 0.3380 0.0795  -0.0533 -0.0123 88  GLU D O   
12837 C CB  . GLU D 88  ? 1.0647 0.5124 0.3060 0.0766  -0.0029 0.0023  88  GLU D CB  
12838 C CG  . GLU D 88  ? 1.0888 0.5390 0.3330 0.0698  0.0244  0.0031  88  GLU D CG  
12839 C CD  . GLU D 88  ? 1.1785 0.6324 0.4332 0.0645  0.0427  0.0113  88  GLU D CD  
12840 O OE1 . GLU D 88  ? 1.2259 0.6814 0.4806 0.0586  0.0637  0.0123  88  GLU D OE1 
12841 O OE2 . GLU D 88  ? 1.1596 0.6157 0.4231 0.0658  0.0358  0.0165  88  GLU D OE2 
12842 N N   . LYS D 89  ? 1.0451 0.4889 0.2714 0.0909  -0.0639 -0.0074 89  LYS D N   
12843 C CA  . LYS D 89  ? 1.0687 0.5217 0.3024 0.0979  -0.0910 -0.0085 89  LYS D CA  
12844 C C   . LYS D 89  ? 1.0558 0.5247 0.3166 0.0990  -0.0881 -0.0008 89  LYS D C   
12845 O O   . LYS D 89  ? 1.0685 0.5682 0.3727 0.0985  -0.1016 -0.0040 89  LYS D O   
12846 C CB  . LYS D 89  ? 1.1213 0.5529 0.3243 0.1080  -0.1052 -0.0068 89  LYS D CB  
12847 C CG  . LYS D 89  ? 1.1812 0.6053 0.3676 0.1087  -0.1193 -0.0161 89  LYS D CG  
12848 C CD  . LYS D 89  ? 1.2323 0.6396 0.3926 0.1206  -0.1372 -0.0148 89  LYS D CD  
12849 C CE  . LYS D 89  ? 1.2755 0.6756 0.4193 0.1212  -0.1524 -0.0243 89  LYS D CE  
12850 N NZ  . LYS D 89  ? 1.3560 0.7363 0.4703 0.1335  -0.1670 -0.0229 89  LYS D NZ  
12851 N N   . GLU D 90  ? 1.0451 0.4992 0.2935 0.0986  -0.0684 0.0088  90  GLU D N   
12852 C CA  . GLU D 90  ? 1.0533 0.5201 0.3270 0.0992  -0.0642 0.0166  90  GLU D CA  
12853 C C   . GLU D 90  ? 0.9802 0.4836 0.3110 0.0892  -0.0537 0.0131  90  GLU D C   
12854 O O   . GLU D 90  ? 0.9313 0.4572 0.2993 0.0902  -0.0589 0.0156  90  GLU D O   
12855 C CB  . GLU D 90  ? 1.1943 0.6386 0.4480 0.0976  -0.0434 0.0260  90  GLU D CB  
12856 C CG  . GLU D 90  ? 1.3801 0.8118 0.6179 0.0895  -0.0213 0.0245  90  GLU D CG  
12857 C CD  . GLU D 90  ? 1.5776 0.9828 0.7784 0.0955  -0.0284 0.0227  90  GLU D CD  
12858 O OE1 . GLU D 90  ? 1.6220 1.0285 0.8159 0.1011  -0.0487 0.0159  90  GLU D OE1 
12859 O OE2 . GLU D 90  ? 1.6498 1.0331 0.8288 0.0941  -0.0142 0.0276  90  GLU D OE2 
12860 N N   . GLU D 91  ? 0.9626 0.4712 0.2991 0.0809  -0.0391 0.0073  91  GLU D N   
12861 C CA  . GLU D 91  ? 0.8757 0.4165 0.2628 0.0730  -0.0300 0.0033  91  GLU D CA  
12862 C C   . GLU D 91  ? 0.8574 0.4225 0.2781 0.0729  -0.0507 -0.0045 91  GLU D C   
12863 O O   . GLU D 91  ? 0.8037 0.3959 0.2691 0.0703  -0.0515 -0.0044 91  GLU D O   
12864 C CB  . GLU D 91  ? 0.8757 0.4140 0.2558 0.0666  -0.0098 -0.0014 91  GLU D CB  
12865 C CG  . GLU D 91  ? 0.8903 0.4185 0.2554 0.0631  0.0153  0.0052  91  GLU D CG  
12866 C CD  . GLU D 91  ? 1.0160 0.5477 0.3785 0.0586  0.0343  -0.0007 91  GLU D CD  
12867 O OE1 . GLU D 91  ? 1.0872 0.6077 0.4278 0.0608  0.0285  -0.0076 91  GLU D OE1 
12868 O OE2 . GLU D 91  ? 0.9983 0.5449 0.3807 0.0533  0.0543  0.0010  91  GLU D OE2 
12869 N N   . VAL D 92  ? 0.8931 0.4486 0.2923 0.0749  -0.0670 -0.0118 92  VAL D N   
12870 C CA  . VAL D 92  ? 0.9101 0.4875 0.3374 0.0737  -0.0889 -0.0196 92  VAL D CA  
12871 C C   . VAL D 92  ? 0.8986 0.4915 0.3459 0.0806  -0.1043 -0.0146 92  VAL D C   
12872 O O   . VAL D 92  ? 0.9045 0.5278 0.3964 0.0776  -0.1117 -0.0175 92  VAL D O   
12873 C CB  . VAL D 92  ? 0.9660 0.5260 0.3590 0.0749  -0.1050 -0.0280 92  VAL D CB  
12874 C CG1 . VAL D 92  ? 0.9209 0.5052 0.3427 0.0722  -0.1288 -0.0366 92  VAL D CG1 
12875 C CG2 . VAL D 92  ? 0.9701 0.5146 0.3436 0.0691  -0.0895 -0.0334 92  VAL D CG2 
12876 N N   . GLU D 93  ? 0.9070 0.4779 0.3196 0.0907  -0.1085 -0.0070 93  GLU D N   
12877 C CA  . GLU D 93  ? 0.9191 0.5008 0.3445 0.1003  -0.1228 -0.0017 93  GLU D CA  
12878 C C   . GLU D 93  ? 0.9014 0.5068 0.3716 0.0968  -0.1106 0.0034  93  GLU D C   
12879 O O   . GLU D 93  ? 0.8564 0.4915 0.3660 0.0981  -0.1227 0.0011  93  GLU D O   
12880 C CB  . GLU D 93  ? 0.9925 0.5387 0.3662 0.1120  -0.1244 0.0069  93  GLU D CB  
12881 C CG  . GLU D 93  ? 1.1053 0.6440 0.4529 0.1245  -0.1522 0.0033  93  GLU D CG  
12882 C CD  . GLU D 93  ? 1.2452 0.7381 0.5275 0.1343  -0.1509 0.0095  93  GLU D CD  
12883 O OE1 . GLU D 93  ? 1.2866 0.7695 0.5467 0.1386  -0.1645 0.0035  93  GLU D OE1 
12884 O OE2 . GLU D 93  ? 1.2682 0.7423 0.5381 0.1344  -0.1318 0.0192  93  GLU D OE2 
12885 N N   . LYS D 94  ? 0.9301 0.5240 0.3954 0.0919  -0.0865 0.0098  94  LYS D N   
12886 C CA  . LYS D 94  ? 0.9308 0.5444 0.4352 0.0887  -0.0747 0.0147  94  LYS D CA  
12887 C C   . LYS D 94  ? 0.8343 0.4805 0.3876 0.0802  -0.0732 0.0071  94  LYS D C   
12888 O O   . LYS D 94  ? 0.7513 0.4205 0.3432 0.0803  -0.0735 0.0091  94  LYS D O   
12889 C CB  . LYS D 94  ? 1.0433 0.6384 0.5307 0.0838  -0.0493 0.0218  94  LYS D CB  
12890 C CG  . LYS D 94  ? 1.1966 0.7538 0.6296 0.0896  -0.0468 0.0289  94  LYS D CG  
12891 C CD  . LYS D 94  ? 1.2559 0.7967 0.6720 0.0812  -0.0199 0.0339  94  LYS D CD  
12892 C CE  . LYS D 94  ? 1.3292 0.8310 0.6939 0.0862  -0.0162 0.0430  94  LYS D CE  
12893 N NZ  . LYS D 94  ? 1.3224 0.8139 0.6721 0.1005  -0.0394 0.0464  94  LYS D NZ  
12894 N N   . LEU D 95  ? 0.8381 0.4843 0.3883 0.0732  -0.0710 -0.0015 95  LEU D N   
12895 C CA  . LEU D 95  ? 0.7990 0.4713 0.3904 0.0654  -0.0708 -0.0090 95  LEU D CA  
12896 C C   . LEU D 95  ? 0.7498 0.4447 0.3667 0.0669  -0.0935 -0.0139 95  LEU D C   
12897 O O   . LEU D 95  ? 0.7115 0.4324 0.3706 0.0628  -0.0933 -0.0158 95  LEU D O   
12898 C CB  . LEU D 95  ? 0.8634 0.5248 0.4387 0.0587  -0.0632 -0.0170 95  LEU D CB  
12899 C CG  . LEU D 95  ? 0.9459 0.6256 0.5546 0.0505  -0.0581 -0.0246 95  LEU D CG  
12900 C CD1 . LEU D 95  ? 1.0009 0.6693 0.5971 0.0476  -0.0366 -0.0260 95  LEU D CD1 
12901 C CD2 . LEU D 95  ? 0.9863 0.6673 0.5917 0.0465  -0.0763 -0.0344 95  LEU D CD2 
12902 N N   . ILE D 96  ? 0.7267 0.4134 0.3188 0.0732  -0.1130 -0.0159 96  ILE D N   
12903 C CA  . ILE D 96  ? 0.7397 0.4522 0.3572 0.0759  -0.1355 -0.0205 96  ILE D CA  
12904 C C   . ILE D 96  ? 0.7442 0.4716 0.3838 0.0850  -0.1376 -0.0122 96  ILE D C   
12905 O O   . ILE D 96  ? 0.7326 0.4912 0.4147 0.0833  -0.1435 -0.0146 96  ILE D O   
12906 C CB  . ILE D 96  ? 0.7658 0.4662 0.3492 0.0817  -0.1571 -0.0255 96  ILE D CB  
12907 C CG1 . ILE D 96  ? 0.7867 0.4805 0.3596 0.0708  -0.1592 -0.0365 96  ILE D CG1 
12908 C CG2 . ILE D 96  ? 0.7633 0.4920 0.3706 0.0888  -0.1804 -0.0281 96  ILE D CG2 
12909 C CD1 . ILE D 96  ? 0.8436 0.5225 0.3793 0.0758  -0.1797 -0.0421 96  ILE D CD1 
12910 N N   . GLU D 97  ? 0.7879 0.4915 0.3963 0.0950  -0.1328 -0.0024 97  GLU D N   
12911 C CA  . GLU D 97  ? 0.8468 0.5564 0.4683 0.1042  -0.1318 0.0067  97  GLU D CA  
12912 C C   . GLU D 97  ? 0.7795 0.5138 0.4484 0.0970  -0.1187 0.0076  97  GLU D C   
12913 O O   . GLU D 97  ? 0.6413 0.4005 0.3433 0.1018  -0.1263 0.0086  97  GLU D O   
12914 C CB  . GLU D 97  ? 1.0070 0.6798 0.5854 0.1097  -0.1187 0.0171  97  GLU D CB  
12915 C CG  . GLU D 97  ? 1.2263 0.8712 0.7553 0.1220  -0.1325 0.0198  97  GLU D CG  
12916 C CD  . GLU D 97  ? 1.3711 1.0371 0.9111 0.1324  -0.1600 0.0143  97  GLU D CD  
12917 O OE1 . GLU D 97  ? 1.4151 1.0953 0.9727 0.1429  -0.1680 0.0185  97  GLU D OE1 
12918 O OE2 . GLU D 97  ? 1.4276 1.0969 0.9588 0.1302  -0.1736 0.0053  97  GLU D OE2 
12919 N N   . PHE D 98  ? 0.7135 0.4405 0.3844 0.0865  -0.0985 0.0071  98  PHE D N   
12920 C CA  . PHE D 98  ? 0.6169 0.3620 0.3266 0.0806  -0.0840 0.0084  98  PHE D CA  
12921 C C   . PHE D 98  ? 0.6097 0.3863 0.3616 0.0749  -0.0924 0.0002  98  PHE D C   
12922 O O   . PHE D 98  ? 0.6228 0.4200 0.4106 0.0751  -0.0892 0.0022  98  PHE D O   
12923 C CB  . PHE D 98  ? 0.5990 0.3294 0.2971 0.0722  -0.0622 0.0083  98  PHE D CB  
12924 C CG  . PHE D 98  ? 0.6163 0.3603 0.3470 0.0678  -0.0457 0.0105  98  PHE D CG  
12925 C CD1 . PHE D 98  ? 0.6041 0.3404 0.3323 0.0708  -0.0347 0.0194  98  PHE D CD1 
12926 C CD2 . PHE D 98  ? 0.6144 0.3757 0.3746 0.0604  -0.0408 0.0034  98  PHE D CD2 
12927 C CE1 . PHE D 98  ? 0.5901 0.3387 0.3469 0.0669  -0.0203 0.0207  98  PHE D CE1 
12928 C CE2 . PHE D 98  ? 0.6110 0.3829 0.3980 0.0576  -0.0261 0.0050  98  PHE D CE2 
12929 C CZ  . PHE D 98  ? 0.6124 0.3793 0.3987 0.0611  -0.0164 0.0136  98  PHE D CZ  
12930 N N   . THR D 99  ? 0.6297 0.4088 0.3762 0.0691  -0.1028 -0.0093 99  THR D N   
12931 C CA  . THR D 99  ? 0.6367 0.4444 0.4205 0.0619  -0.1118 -0.0177 99  THR D CA  
12932 C C   . THR D 99  ? 0.6459 0.4792 0.4531 0.0702  -0.1290 -0.0165 99  THR D C   
12933 O O   . THR D 99  ? 0.6134 0.4731 0.4609 0.0676  -0.1279 -0.0175 99  THR D O   
12934 C CB  . THR D 99  ? 0.6478 0.4495 0.4156 0.0536  -0.1211 -0.0284 99  THR D CB  
12935 O OG1 . THR D 99  ? 0.6539 0.4324 0.4000 0.0476  -0.1044 -0.0297 99  THR D OG1 
12936 C CG2 . THR D 99  ? 0.5722 0.4024 0.3779 0.0436  -0.1295 -0.0375 99  THR D CG2 
12937 N N   . LYS D 100 ? 0.6434 0.4692 0.4244 0.0812  -0.1450 -0.0146 100 LYS D N   
12938 C CA  . LYS D 100 ? 0.6509 0.5016 0.4507 0.0923  -0.1630 -0.0139 100 LYS D CA  
12939 C C   . LYS D 100 ? 0.5780 0.4377 0.4008 0.0996  -0.1534 -0.0048 100 LYS D C   
12940 O O   . LYS D 100 ? 0.5523 0.4439 0.4124 0.1023  -0.1607 -0.0065 100 LYS D O   
12941 C CB  . LYS D 100 ? 0.6401 0.4729 0.3987 0.1062  -0.1796 -0.0118 100 LYS D CB  
12942 C CG  . LYS D 100 ? 0.8223 0.6488 0.5580 0.1014  -0.1936 -0.0214 100 LYS D CG  
12943 C CD  . LYS D 100 ? 0.8684 0.6758 0.5616 0.1181  -0.2104 -0.0184 100 LYS D CD  
12944 C CE  . LYS D 100 ? 0.9116 0.7365 0.6037 0.1189  -0.2360 -0.0298 100 LYS D CE  
12945 N NZ  . LYS D 100 ? 0.9132 0.7091 0.5522 0.1336  -0.2501 -0.0278 100 LYS D NZ  
12946 N N   . LEU D 101 ? 0.5911 0.4227 0.3907 0.1028  -0.1373 0.0046  101 LEU D N   
12947 C CA  . LEU D 101 ? 0.6307 0.4655 0.4473 0.1088  -0.1269 0.0134  101 LEU D CA  
12948 C C   . LEU D 101 ? 0.5952 0.4573 0.4595 0.0996  -0.1178 0.0100  101 LEU D C   
12949 O O   . LEU D 101 ? 0.5926 0.4738 0.4844 0.1062  -0.1192 0.0134  101 LEU D O   
12950 C CB  . LEU D 101 ? 0.6771 0.4768 0.4610 0.1084  -0.1088 0.0218  101 LEU D CB  
12951 C CG  . LEU D 101 ? 0.7131 0.5059 0.5029 0.1136  -0.0964 0.0316  101 LEU D CG  
12952 C CD1 . LEU D 101 ? 0.7409 0.5278 0.5155 0.1308  -0.1099 0.0382  101 LEU D CD1 
12953 C CD2 . LEU D 101 ? 0.7071 0.4702 0.4695 0.1066  -0.0765 0.0363  101 LEU D CD2 
12954 N N   . ASN D 102 ? 0.6039 0.4664 0.4762 0.0854  -0.1083 0.0033  102 ASN D N   
12955 C CA  . ASN D 102 ? 0.5564 0.4374 0.4671 0.0765  -0.0969 0.0005  102 ASN D CA  
12956 C C   . ASN D 102 ? 0.5395 0.4483 0.4794 0.0681  -0.1077 -0.0097 102 ASN D C   
12957 O O   . ASN D 102 ? 0.4448 0.3678 0.4152 0.0599  -0.0987 -0.0127 102 ASN D O   
12958 C CB  . ASN D 102 ? 0.4902 0.3519 0.3900 0.0672  -0.0777 -0.0003 102 ASN D CB  
12959 C CG  . ASN D 102 ? 0.6094 0.4496 0.4892 0.0725  -0.0642 0.0090  102 ASN D CG  
12960 O OD1 . ASN D 102 ? 0.7290 0.5746 0.6257 0.0771  -0.0574 0.0152  102 ASN D OD1 
12961 N ND2 . ASN D 102 ? 0.5568 0.3722 0.3997 0.0713  -0.0595 0.0097  102 ASN D ND2 
12962 N N   . TYR D 103 ? 0.5665 0.4834 0.4973 0.0699  -0.1270 -0.0152 103 TYR D N   
12963 C CA  . TYR D 103 ? 0.5869 0.5252 0.5370 0.0582  -0.1375 -0.0268 103 TYR D CA  
12964 C C   . TYR D 103 ? 0.5236 0.4978 0.5218 0.0546  -0.1381 -0.0295 103 TYR D C   
12965 O O   . TYR D 103 ? 0.4964 0.4833 0.5149 0.0398  -0.1365 -0.0383 103 TYR D O   
12966 C CB  . TYR D 103 ? 0.6722 0.6134 0.6015 0.0638  -0.1600 -0.0314 103 TYR D CB  
12967 C CG  . TYR D 103 ? 0.7402 0.7059 0.6882 0.0518  -0.1745 -0.0443 103 TYR D CG  
12968 C CD1 . TYR D 103 ? 0.7749 0.7812 0.7596 0.0536  -0.1882 -0.0486 103 TYR D CD1 
12969 C CD2 . TYR D 103 ? 0.8269 0.7756 0.7547 0.0387  -0.1747 -0.0526 103 TYR D CD2 
12970 C CE1 . TYR D 103 ? 0.8204 0.8515 0.8235 0.0405  -0.2013 -0.0613 103 TYR D CE1 
12971 C CE2 . TYR D 103 ? 0.8747 0.8436 0.8174 0.0259  -0.1880 -0.0649 103 TYR D CE2 
12972 C CZ  . TYR D 103 ? 0.8850 0.8960 0.8663 0.0259  -0.2013 -0.0695 103 TYR D CZ  
12973 O OH  . TYR D 103 ? 0.9275 0.9609 0.9252 0.0109  -0.2143 -0.0827 103 TYR D OH  
12974 N N   . GLU D 104 ? 0.4307 0.4201 0.4455 0.0678  -0.1400 -0.0223 104 GLU D N   
12975 C CA  . GLU D 104 ? 0.4567 0.4831 0.5167 0.0666  -0.1420 -0.0248 104 GLU D CA  
12976 C C   . GLU D 104 ? 0.4222 0.4465 0.5039 0.0623  -0.1213 -0.0203 104 GLU D C   
12977 O O   . GLU D 104 ? 0.4030 0.4557 0.5217 0.0601  -0.1200 -0.0223 104 GLU D O   
12978 C CB  . GLU D 104 ? 0.5392 0.5857 0.6064 0.0853  -0.1565 -0.0201 104 GLU D CB  
12979 C CG  . GLU D 104 ? 0.6715 0.7348 0.7310 0.0899  -0.1806 -0.0273 104 GLU D CG  
12980 C CD  . GLU D 104 ? 0.8162 0.8479 0.8274 0.1039  -0.1887 -0.0215 104 GLU D CD  
12981 O OE1 . GLU D 104 ? 0.8729 0.9122 0.8703 0.1089  -0.2087 -0.0272 104 GLU D OE1 
12982 O OE2 . GLU D 104 ? 0.8584 0.8573 0.8443 0.1095  -0.1750 -0.0115 104 GLU D OE2 
12983 N N   . LYS D 105 ? 0.4135 0.4064 0.4733 0.0616  -0.1053 -0.0148 105 LYS D N   
12984 C CA  . LYS D 105 ? 0.4041 0.3928 0.4811 0.0585  -0.0862 -0.0112 105 LYS D CA  
12985 C C   . LYS D 105 ? 0.4324 0.4236 0.5233 0.0415  -0.0784 -0.0202 105 LYS D C   
12986 O O   . LYS D 105 ? 0.4176 0.3967 0.4897 0.0321  -0.0815 -0.0271 105 LYS D O   
12987 C CB  . LYS D 105 ? 0.3914 0.3482 0.4399 0.0635  -0.0729 -0.0034 105 LYS D CB  
12988 C CG  . LYS D 105 ? 0.3778 0.3250 0.4061 0.0789  -0.0791 0.0058  105 LYS D CG  
12989 C CD  . LYS D 105 ? 0.4473 0.3617 0.4423 0.0798  -0.0669 0.0115  105 LYS D CD  
12990 C CE  . LYS D 105 ? 0.4589 0.3589 0.4308 0.0935  -0.0711 0.0211  105 LYS D CE  
12991 N NZ  . LYS D 105 ? 0.4939 0.3627 0.4332 0.0915  -0.0579 0.0258  105 LYS D NZ  
12992 N N   . PRO D 106 ? 0.4070 0.4110 0.5280 0.0378  -0.0679 -0.0202 106 PRO D N   
12993 C CA  . PRO D 106 ? 0.4004 0.4046 0.5327 0.0215  -0.0605 -0.0289 106 PRO D CA  
12994 C C   . PRO D 106 ? 0.3722 0.3435 0.4755 0.0155  -0.0493 -0.0311 106 PRO D C   
12995 O O   . PRO D 106 ? 0.3868 0.3518 0.4861 0.0023  -0.0483 -0.0398 106 PRO D O   
12996 C CB  . PRO D 106 ? 0.3833 0.4014 0.5476 0.0225  -0.0490 -0.0258 106 PRO D CB  
12997 C CG  . PRO D 106 ? 0.3623 0.4026 0.5417 0.0369  -0.0583 -0.0193 106 PRO D CG  
12998 C CD  . PRO D 106 ? 0.3669 0.3879 0.5132 0.0482  -0.0647 -0.0133 106 PRO D CD  
12999 N N   . ILE D 107 ? 0.3477 0.2978 0.4299 0.0247  -0.0406 -0.0241 107 ILE D N   
13000 C CA  . ILE D 107 ? 0.3492 0.2718 0.4048 0.0206  -0.0299 -0.0268 107 ILE D CA  
13001 C C   . ILE D 107 ? 0.4371 0.3475 0.4634 0.0161  -0.0400 -0.0322 107 ILE D C   
13002 O O   . ILE D 107 ? 0.3610 0.2499 0.3651 0.0113  -0.0326 -0.0367 107 ILE D O   
13003 C CB  . ILE D 107 ? 0.3337 0.2413 0.3769 0.0306  -0.0176 -0.0187 107 ILE D CB  
13004 C CG1 . ILE D 107 ? 0.3706 0.2786 0.4014 0.0409  -0.0258 -0.0110 107 ILE D CG1 
13005 C CG2 . ILE D 107 ? 0.3341 0.2479 0.4020 0.0337  -0.0055 -0.0150 107 ILE D CG2 
13006 C CD1 . ILE D 107 ? 0.3300 0.2181 0.3386 0.0464  -0.0142 -0.0053 107 ILE D CD1 
13007 N N   . TYR D 108 ? 0.4378 0.3608 0.4621 0.0188  -0.0570 -0.0323 108 TYR D N   
13008 C CA  . TYR D 108 ? 0.4878 0.4010 0.4855 0.0145  -0.0689 -0.0384 108 TYR D CA  
13009 C C   . TYR D 108 ? 0.5207 0.4498 0.5333 0.0012  -0.0801 -0.0490 108 TYR D C   
13010 O O   . TYR D 108 ? 0.4719 0.3980 0.4663 -0.0024 -0.0939 -0.0548 108 TYR D O   
13011 C CB  . TYR D 108 ? 0.4991 0.4130 0.4799 0.0263  -0.0818 -0.0327 108 TYR D CB  
13012 C CG  . TYR D 108 ? 0.5001 0.3858 0.4463 0.0332  -0.0725 -0.0265 108 TYR D CG  
13013 C CD1 . TYR D 108 ? 0.4523 0.3313 0.4021 0.0392  -0.0571 -0.0185 108 TYR D CD1 
13014 C CD2 . TYR D 108 ? 0.4697 0.3358 0.3794 0.0330  -0.0786 -0.0291 108 TYR D CD2 
13015 C CE1 . TYR D 108 ? 0.4740 0.3300 0.3940 0.0435  -0.0476 -0.0137 108 TYR D CE1 
13016 C CE2 . TYR D 108 ? 0.4796 0.3211 0.3581 0.0383  -0.0684 -0.0237 108 TYR D CE2 
13017 C CZ  . TYR D 108 ? 0.5152 0.3531 0.3999 0.0429  -0.0528 -0.0162 108 TYR D CZ  
13018 O OH  . TYR D 108 ? 0.5388 0.3553 0.3946 0.0463  -0.0418 -0.0116 108 TYR D OH  
13019 N N   . ARG D 109 ? 0.5055 0.4506 0.5497 -0.0071 -0.0742 -0.0521 109 ARG D N   
13020 C CA  . ARG D 109 ? 0.5683 0.5312 0.6291 -0.0220 -0.0843 -0.0626 109 ARG D CA  
13021 C C   . ARG D 109 ? 0.5645 0.5000 0.6019 -0.0358 -0.0781 -0.0712 109 ARG D C   
13022 O O   . ARG D 109 ? 0.4979 0.4249 0.5431 -0.0451 -0.0651 -0.0744 109 ARG D O   
13023 C CB  . ARG D 109 ? 0.5702 0.5621 0.6734 -0.0261 -0.0804 -0.0627 109 ARG D CB  
13024 C CG  . ARG D 109 ? 0.6311 0.6574 0.7587 -0.0356 -0.0973 -0.0712 109 ARG D CG  
13025 C CD  . ARG D 109 ? 0.6646 0.7236 0.8356 -0.0383 -0.0931 -0.0708 109 ARG D CD  
13026 N NE  . ARG D 109 ? 0.7025 0.7449 0.8783 -0.0369 -0.0720 -0.0651 109 ARG D NE  
13027 C CZ  . ARG D 109 ? 0.7159 0.7700 0.9113 -0.0245 -0.0649 -0.0563 109 ARG D CZ  
13028 N NH1 . ARG D 109 ? 0.6668 0.7483 0.8780 -0.0117 -0.0768 -0.0519 109 ARG D NH1 
13029 N NH2 . ARG D 109 ? 0.7389 0.7756 0.9359 -0.0237 -0.0463 -0.0521 109 ARG D NH2 
13030 N N   . PHE D 110 ? 0.5869 0.5052 0.5913 -0.0359 -0.0875 -0.0747 110 PHE D N   
13031 C CA  . PHE D 110 ? 0.6093 0.5026 0.5876 -0.0487 -0.0868 -0.0842 110 PHE D CA  
13032 C C   . PHE D 110 ? 0.6003 0.5063 0.5748 -0.0571 -0.1081 -0.0930 110 PHE D C   
13033 O O   . PHE D 110 ? 0.5544 0.4713 0.5228 -0.0469 -0.1224 -0.0900 110 PHE D O   
13034 C CB  . PHE D 110 ? 0.5902 0.4479 0.5274 -0.0404 -0.0777 -0.0812 110 PHE D CB  
13035 C CG  . PHE D 110 ? 0.5371 0.3833 0.4760 -0.0317 -0.0577 -0.0740 110 PHE D CG  
13036 C CD1 . PHE D 110 ? 0.5060 0.3635 0.4561 -0.0181 -0.0540 -0.0635 110 PHE D CD1 
13037 C CD2 . PHE D 110 ? 0.5449 0.3676 0.4720 -0.0367 -0.0431 -0.0780 110 PHE D CD2 
13038 C CE1 . PHE D 110 ? 0.4961 0.3446 0.4484 -0.0109 -0.0366 -0.0577 110 PHE D CE1 
13039 C CE2 . PHE D 110 ? 0.4821 0.2962 0.4108 -0.0274 -0.0260 -0.0721 110 PHE D CE2 
13040 C CZ  . PHE D 110 ? 0.4705 0.2990 0.4132 -0.0151 -0.0230 -0.0622 110 PHE D CZ  
13041 N N   . GLU D 111 ? 0.6242 0.5274 0.6006 -0.0758 -0.1104 -0.1041 111 GLU D N   
13042 C CA  . GLU D 111 ? 0.7224 0.6395 0.6970 -0.0861 -0.1312 -0.1141 111 GLU D CA  
13043 C C   . GLU D 111 ? 0.7591 0.6509 0.6897 -0.0787 -0.1410 -0.1148 111 GLU D C   
13044 O O   . GLU D 111 ? 0.7564 0.6633 0.6836 -0.0775 -0.1612 -0.1189 111 GLU D O   
13045 C CB  . GLU D 111 ? 0.8502 0.7629 0.8306 -0.1100 -0.1293 -0.1262 111 GLU D CB  
13046 C CG  . GLU D 111 ? 1.0251 0.9572 1.0097 -0.1244 -0.1510 -0.1384 111 GLU D CG  
13047 C CD  . GLU D 111 ? 1.1305 1.1143 1.1551 -0.1194 -0.1670 -0.1379 111 GLU D CD  
13048 O OE1 . GLU D 111 ? 1.1706 1.1621 1.1865 -0.1011 -0.1785 -0.1319 111 GLU D OE1 
13049 O OE2 . GLU D 111 ? 1.1628 1.1788 1.2260 -0.1333 -0.1676 -0.1436 111 GLU D OE2 
13050 N N   . ARG D 112 ? 0.7558 0.6102 0.6522 -0.0725 -0.1269 -0.1110 112 ARG D N   
13051 C CA  . ARG D 112 ? 0.7900 0.6182 0.6425 -0.0653 -0.1336 -0.1114 112 ARG D CA  
13052 C C   . ARG D 112 ? 0.7893 0.6287 0.6381 -0.0472 -0.1416 -0.1020 112 ARG D C   
13053 O O   . ARG D 112 ? 0.7592 0.5903 0.5807 -0.0425 -0.1558 -0.1040 112 ARG D O   
13054 C CB  . ARG D 112 ? 0.7715 0.5604 0.5912 -0.0623 -0.1147 -0.1099 112 ARG D CB  
13055 C CG  . ARG D 112 ? 0.7871 0.5471 0.5597 -0.0543 -0.1182 -0.1099 112 ARG D CG  
13056 C CD  . ARG D 112 ? 0.7798 0.5300 0.5308 -0.0661 -0.1355 -0.1216 112 ARG D CD  
13057 N NE  . ARG D 112 ? 0.8077 0.5203 0.5087 -0.0604 -0.1326 -0.1230 112 ARG D NE  
13058 C CZ  . ARG D 112 ? 0.9029 0.6018 0.5739 -0.0643 -0.1485 -0.1305 112 ARG D CZ  
13059 N NH1 . ARG D 112 ? 0.9261 0.6481 0.6140 -0.0745 -0.1693 -0.1379 112 ARG D NH1 
13060 N NH2 . ARG D 112 ? 0.9132 0.5766 0.5377 -0.0578 -0.1438 -0.1311 112 ARG D NH2 
13061 N N   . ILE D 113 ? 0.7585 0.6137 0.6316 -0.0366 -0.1327 -0.0919 113 ILE D N   
13062 C CA  . ILE D 113 ? 0.7731 0.6350 0.6399 -0.0197 -0.1394 -0.0826 113 ILE D CA  
13063 C C   . ILE D 113 ? 0.7959 0.6866 0.6764 -0.0185 -0.1633 -0.0868 113 ILE D C   
13064 O O   . ILE D 113 ? 0.8413 0.7265 0.6979 -0.0071 -0.1758 -0.0840 113 ILE D O   
13065 C CB  . ILE D 113 ? 0.7271 0.5977 0.6160 -0.0098 -0.1244 -0.0714 113 ILE D CB  
13066 C CG1 . ILE D 113 ? 0.7061 0.5464 0.5708 -0.0058 -0.1040 -0.0665 113 ILE D CG1 
13067 C CG2 . ILE D 113 ? 0.7406 0.6251 0.6320 0.0055  -0.1346 -0.0631 113 ILE D CG2 
13068 C CD1 . ILE D 113 ? 0.6676 0.5153 0.5559 -0.0001 -0.0877 -0.0582 113 ILE D CD1 
13069 N N   . ARG D 114 ? 0.7648 0.6866 0.6829 -0.0302 -0.1700 -0.0940 114 ARG D N   
13070 C CA  . ARG D 114 ? 0.7799 0.7352 0.7152 -0.0290 -0.1934 -0.0994 114 ARG D CA  
13071 C C   . ARG D 114 ? 0.8186 0.7597 0.7198 -0.0325 -0.2111 -0.1082 114 ARG D C   
13072 O O   . ARG D 114 ? 0.8036 0.7607 0.7008 -0.0230 -0.2315 -0.1096 114 ARG D O   
13073 C CB  . ARG D 114 ? 0.7670 0.7597 0.7500 -0.0439 -0.1954 -0.1070 114 ARG D CB  
13074 C CG  . ARG D 114 ? 0.8189 0.8497 0.8210 -0.0474 -0.2207 -0.1168 114 ARG D CG  
13075 C CD  . ARG D 114 ? 0.8793 0.9333 0.9127 -0.0719 -0.2219 -0.1297 114 ARG D CD  
13076 N NE  . ARG D 114 ? 0.9645 1.0356 0.9953 -0.0821 -0.2453 -0.1432 114 ARG D NE  
13077 C CZ  . ARG D 114 ? 1.0036 1.0461 1.0014 -0.0951 -0.2500 -0.1521 114 ARG D CZ  
13078 N NH1 . ARG D 114 ? 0.9951 0.9905 0.9591 -0.0986 -0.2326 -0.1489 114 ARG D NH1 
13079 N NH2 . ARG D 114 ? 1.0447 1.1063 1.0429 -0.1041 -0.2727 -0.1647 114 ARG D NH2 
13080 N N   . GLU D 115 ? 0.8563 0.7652 0.7294 -0.0443 -0.2039 -0.1140 115 GLU D N   
13081 C CA  . GLU D 115 ? 0.9195 0.8118 0.7580 -0.0488 -0.2202 -0.1231 115 GLU D CA  
13082 C C   . GLU D 115 ? 0.9564 0.8205 0.7504 -0.0307 -0.2227 -0.1156 115 GLU D C   
13083 O O   . GLU D 115 ? 1.0032 0.8705 0.7793 -0.0241 -0.2432 -0.1190 115 GLU D O   
13084 C CB  . GLU D 115 ? 0.9431 0.8070 0.7637 -0.0669 -0.2107 -0.1319 115 GLU D CB  
13085 C CG  . GLU D 115 ? 0.9355 0.8204 0.7942 -0.0869 -0.2062 -0.1396 115 GLU D CG  
13086 C CD  . GLU D 115 ? 0.9653 0.8138 0.8007 -0.1021 -0.1926 -0.1460 115 GLU D CD  
13087 O OE1 . GLU D 115 ? 0.9505 0.7610 0.7402 -0.0977 -0.1907 -0.1465 115 GLU D OE1 
13088 O OE2 . GLU D 115 ? 0.9752 0.8316 0.8359 -0.1179 -0.1835 -0.1506 115 GLU D OE2 
13089 N N   . LEU D 116 ? 0.9346 0.7708 0.7092 -0.0228 -0.2019 -0.1058 116 LEU D N   
13090 C CA  . LEU D 116 ? 0.9858 0.7933 0.7166 -0.0077 -0.2013 -0.0987 116 LEU D CA  
13091 C C   . LEU D 116 ? 0.9931 0.8173 0.7277 0.0091  -0.2137 -0.0912 116 LEU D C   
13092 O O   . LEU D 116 ? 1.0704 0.8756 0.7672 0.0201  -0.2233 -0.0890 116 LEU D O   
13093 C CB  . LEU D 116 ? 0.9480 0.7287 0.6637 -0.0038 -0.1753 -0.0903 116 LEU D CB  
13094 C CG  . LEU D 116 ? 0.9228 0.6904 0.6412 -0.0177 -0.1608 -0.0967 116 LEU D CG  
13095 C CD1 . LEU D 116 ? 0.8939 0.6474 0.6106 -0.0119 -0.1357 -0.0882 116 LEU D CD1 
13096 C CD2 . LEU D 116 ? 0.9326 0.6715 0.6108 -0.0246 -0.1675 -0.1063 116 LEU D CD2 
13097 N N   . MET D 117 ? 0.9333 0.7907 0.7104 0.0120  -0.2138 -0.0872 117 MET D N   
13098 C CA  . MET D 117 ? 0.9549 0.8276 0.7353 0.0293  -0.2258 -0.0802 117 MET D CA  
13099 C C   . MET D 117 ? 0.9876 0.8835 0.7706 0.0316  -0.2542 -0.0894 117 MET D C   
13100 O O   . MET D 117 ? 0.9783 0.8812 0.7532 0.0488  -0.2672 -0.0846 117 MET D O   
13101 C CB  . MET D 117 ? 0.9018 0.8013 0.7253 0.0329  -0.2161 -0.0732 117 MET D CB  
13102 C CG  . MET D 117 ? 0.9370 0.8136 0.7544 0.0349  -0.1903 -0.0629 117 MET D CG  
13103 S SD  . MET D 117 ? 1.0141 0.8495 0.7761 0.0502  -0.1850 -0.0525 117 MET D SD  
13104 C CE  . MET D 117 ? 0.9864 0.7871 0.7157 0.0387  -0.1701 -0.0572 117 MET D CE  
13105 N N   . ASN D 118 ? 1.0359 0.9431 0.8286 0.0147  -0.2640 -0.1028 118 ASN D N   
13106 C CA  . ASN D 118 ? 1.0830 1.0118 0.8757 0.0146  -0.2918 -0.1136 118 ASN D CA  
13107 C C   . ASN D 118 ? 1.1430 1.0363 0.8830 0.0153  -0.3016 -0.1186 118 ASN D C   
13108 O O   . ASN D 118 ? 1.1990 1.1038 0.9286 0.0205  -0.3262 -0.1259 118 ASN D O   
13109 C CB  . ASN D 118 ? 1.0800 1.0462 0.9172 -0.0064 -0.2984 -0.1267 118 ASN D CB  
13110 C CG  . ASN D 118 ? 1.0744 1.0878 0.9650 -0.0033 -0.2995 -0.1246 118 ASN D CG  
13111 O OD1 . ASN D 118 ? 1.0935 1.1240 0.9897 0.0165  -0.3089 -0.1182 118 ASN D OD1 
13112 N ND2 . ASN D 118 ? 1.0469 1.0799 0.9753 -0.0224 -0.2892 -0.1301 118 ASN D ND2 
13113 N N   . LYS D 119 ? 1.1090 0.9600 0.8146 0.0117  -0.2833 -0.1149 119 LYS D N   
13114 C CA  . LYS D 119 ? 1.1051 0.9198 0.7589 0.0118  -0.2905 -0.1198 119 LYS D CA  
13115 C C   . LYS D 119 ? 1.1176 0.9081 0.7288 0.0335  -0.2952 -0.1105 119 LYS D C   
13116 O O   . LYS D 119 ? 1.0563 0.8367 0.6635 0.0453  -0.2799 -0.0975 119 LYS D O   
13117 C CB  . LYS D 119 ? 1.0444 0.8234 0.6764 0.0007  -0.2683 -0.1200 119 LYS D CB  
13118 C CG  . LYS D 119 ? 1.0011 0.7914 0.6614 -0.0216 -0.2634 -0.1303 119 LYS D CG  
13119 C CD  . LYS D 119 ? 1.0173 0.7663 0.6435 -0.0312 -0.2480 -0.1340 119 LYS D CD  
13120 C CE  . LYS D 119 ? 1.0123 0.7717 0.6683 -0.0526 -0.2416 -0.1431 119 LYS D CE  
13121 N NZ  . LYS D 119 ? 1.0413 0.8205 0.7094 -0.0686 -0.2642 -0.1577 119 LYS D NZ  
13122 N N   . GLU D 120 ? 1.1761 0.9545 0.7523 0.0383  -0.3163 -0.1174 120 GLU D N   
13123 C CA  . GLU D 120 ? 1.2255 0.9763 0.7552 0.0590  -0.3217 -0.1092 120 GLU D CA  
13124 C C   . GLU D 120 ? 1.2553 0.9584 0.7415 0.0609  -0.2979 -0.1009 120 GLU D C   
13125 O O   . GLU D 120 ? 1.2775 0.9620 0.7435 0.0747  -0.2866 -0.0884 120 GLU D O   
13126 C CB  . GLU D 120 ? 1.2791 1.0291 0.7817 0.0639  -0.3514 -0.1198 120 GLU D CB  
13127 N N   . LYS D 121 ? 1.2458 0.9286 0.7167 0.0470  -0.2897 -0.1079 121 LYS D N   
13128 C CA  . LYS D 121 ? 1.2468 0.8890 0.6805 0.0478  -0.2662 -0.1017 121 LYS D CA  
13129 C C   . LYS D 121 ? 1.1947 0.8400 0.6535 0.0316  -0.2470 -0.1051 121 LYS D C   
13130 O O   . LYS D 121 ? 1.2063 0.8726 0.6946 0.0171  -0.2552 -0.1153 121 LYS D O   
13131 C CB  . LYS D 121 ? 1.2987 0.9030 0.6737 0.0516  -0.2754 -0.1068 121 LYS D CB  
13132 N N   . LEU D 122 ? 1.0896 0.7135 0.5355 0.0341  -0.2211 -0.0968 122 LEU D N   
13133 C CA  . LEU D 122 ? 1.0144 0.6388 0.4808 0.0225  -0.2010 -0.0986 122 LEU D CA  
13134 C C   . LEU D 122 ? 1.0143 0.5993 0.4349 0.0234  -0.1860 -0.0995 122 LEU D C   
13135 O O   . LEU D 122 ? 1.0877 0.6508 0.4751 0.0345  -0.1763 -0.0916 122 LEU D O   
13136 C CB  . LEU D 122 ? 0.8941 0.5379 0.3973 0.0256  -0.1827 -0.0881 122 LEU D CB  
13137 C CG  . LEU D 122 ? 0.8959 0.5803 0.4489 0.0240  -0.1945 -0.0877 122 LEU D CG  
13138 C CD1 . LEU D 122 ? 0.9301 0.6277 0.5112 0.0294  -0.1767 -0.0764 122 LEU D CD1 
13139 C CD2 . LEU D 122 ? 0.8973 0.6015 0.4818 0.0072  -0.2014 -0.0994 122 LEU D CD2 
13140 N N   . ASN D 123 ? 0.9885 0.5635 0.4057 0.0117  -0.1834 -0.1092 123 ASN D N   
13141 C CA  . ASN D 123 ? 1.0556 0.5941 0.4305 0.0135  -0.1682 -0.1106 123 ASN D CA  
13142 C C   . ASN D 123 ? 0.9858 0.5260 0.3774 0.0149  -0.1406 -0.1044 123 ASN D C   
13143 O O   . ASN D 123 ? 0.9745 0.5415 0.4073 0.0145  -0.1336 -0.0984 123 ASN D O   
13144 C CB  . ASN D 123 ? 1.0936 0.6144 0.4487 0.0021  -0.1791 -0.1243 123 ASN D CB  
13145 C CG  . ASN D 123 ? 1.0795 0.6150 0.4710 -0.0131 -0.1749 -0.1311 123 ASN D CG  
13146 O OD1 . ASN D 123 ? 1.0246 0.5702 0.4423 -0.0129 -0.1561 -0.1259 123 ASN D OD1 
13147 N ND2 . ASN D 123 ? 1.1297 0.6644 0.5205 -0.0267 -0.1924 -0.1432 123 ASN D ND2 
13148 N N   . ARG D 124 ? 0.9193 0.3461 0.3553 0.0117  -0.0939 -0.0558 124 ARG D N   
13149 C CA  . ARG D 124 ? 0.9652 0.4124 0.4169 0.0219  -0.0728 -0.0520 124 ARG D CA  
13150 C C   . ARG D 124 ? 0.9840 0.4549 0.4699 0.0167  -0.0718 -0.0512 124 ARG D C   
13151 O O   . ARG D 124 ? 0.9641 0.4699 0.4843 0.0188  -0.0623 -0.0472 124 ARG D O   
13152 C CB  . ARG D 124 ? 0.9782 0.3927 0.3892 0.0344  -0.0589 -0.0533 124 ARG D CB  
13153 C CG  . ARG D 124 ? 0.9462 0.3807 0.3714 0.0463  -0.0372 -0.0494 124 ARG D CG  
13154 C CD  . ARG D 124 ? 0.9553 0.3574 0.3445 0.0577  -0.0252 -0.0513 124 ARG D CD  
13155 N NE  . ARG D 124 ? 0.9716 0.3975 0.3814 0.0683  -0.0063 -0.0474 124 ARG D NE  
13156 C CZ  . ARG D 124 ? 0.9488 0.3866 0.3779 0.0683  -0.0037 -0.0469 124 ARG D CZ  
13157 N NH1 . ARG D 124 ? 0.9328 0.3590 0.3615 0.0580  -0.0177 -0.0501 124 ARG D NH1 
13158 N NH2 . ARG D 124 ? 0.9039 0.3640 0.3515 0.0785  0.0127  -0.0432 124 ARG D NH2 
13159 N N   . GLU D 125 ? 0.9889 0.4394 0.4642 0.0097  -0.0815 -0.0550 125 GLU D N   
13160 C CA  . GLU D 125 ? 0.9653 0.4347 0.4696 0.0045  -0.0802 -0.0542 125 GLU D CA  
13161 C C   . GLU D 125 ? 0.9462 0.4541 0.4956 -0.0057 -0.0881 -0.0519 125 GLU D C   
13162 O O   . GLU D 125 ? 0.8725 0.4080 0.4532 -0.0061 -0.0806 -0.0490 125 GLU D O   
13163 C CB  . GLU D 125 ? 1.0380 0.4751 0.5199 -0.0024 -0.0899 -0.0588 125 GLU D CB  
13164 C CG  . GLU D 125 ? 1.1439 0.5943 0.6501 -0.0079 -0.0877 -0.0581 125 GLU D CG  
13165 C CD  . GLU D 125 ? 1.2423 0.7029 0.7538 0.0049  -0.0681 -0.0548 125 GLU D CD  
13166 O OE1 . GLU D 125 ? 1.1908 0.6865 0.7327 0.0091  -0.0592 -0.0504 125 GLU D OE1 
13167 O OE2 . GLU D 125 ? 1.3074 0.7405 0.7926 0.0107  -0.0622 -0.0565 125 GLU D OE2 
13168 N N   . GLU D 126 ? 0.9722 0.4819 0.5245 -0.0132 -0.1028 -0.0530 126 GLU D N   
13169 C CA  . GLU D 126 ? 0.9310 0.4764 0.5253 -0.0221 -0.1104 -0.0509 126 GLU D CA  
13170 C C   . GLU D 126 ? 0.8907 0.4669 0.5074 -0.0147 -0.0980 -0.0461 126 GLU D C   
13171 O O   . GLU D 126 ? 0.8521 0.4608 0.5057 -0.0179 -0.0948 -0.0433 126 GLU D O   
13172 C CB  . GLU D 126 ? 0.9528 0.4894 0.5427 -0.0315 -0.1309 -0.0537 126 GLU D CB  
13173 C CG  . GLU D 126 ? 0.9929 0.5076 0.5725 -0.0425 -0.1453 -0.0582 126 GLU D CG  
13174 C CD  . GLU D 126 ? 1.0502 0.5420 0.6077 -0.0484 -0.1648 -0.0618 126 GLU D CD  
13175 O OE1 . GLU D 126 ? 1.0670 0.5489 0.6041 -0.0415 -0.1651 -0.0613 126 GLU D OE1 
13176 O OE2 . GLU D 126 ? 1.0662 0.5490 0.6262 -0.0603 -0.1800 -0.0652 126 GLU D OE2 
13177 N N   . LEU D 127 ? 0.8228 0.3883 0.4167 -0.0051 -0.0906 -0.0450 127 LEU D N   
13178 C CA  . LEU D 127 ? 0.7606 0.3537 0.3740 0.0019  -0.0772 -0.0403 127 LEU D CA  
13179 C C   . LEU D 127 ? 0.7354 0.3452 0.3652 0.0076  -0.0614 -0.0379 127 LEU D C   
13180 O O   . LEU D 127 ? 0.6622 0.3040 0.3231 0.0083  -0.0544 -0.0342 127 LEU D O   
13181 C CB  . LEU D 127 ? 0.8121 0.3873 0.3949 0.0110  -0.0704 -0.0397 127 LEU D CB  
13182 C CG  . LEU D 127 ? 0.8059 0.3635 0.3694 0.0069  -0.0854 -0.0415 127 LEU D CG  
13183 C CD1 . LEU D 127 ? 0.7973 0.3290 0.3222 0.0166  -0.0769 -0.0412 127 LEU D CD1 
13184 C CD2 . LEU D 127 ? 0.7784 0.3666 0.3758 0.0008  -0.0930 -0.0390 127 LEU D CD2 
13185 N N   . LEU D 128 ? 0.6908 0.2779 0.2988 0.0120  -0.0563 -0.0399 128 LEU D N   
13186 C CA  . LEU D 128 ? 0.6740 0.2746 0.2956 0.0182  -0.0426 -0.0377 128 LEU D CA  
13187 C C   . LEU D 128 ? 0.6990 0.3252 0.3566 0.0090  -0.0474 -0.0366 128 LEU D C   
13188 O O   . LEU D 128 ? 0.6395 0.2914 0.3215 0.0124  -0.0375 -0.0333 128 LEU D O   
13189 C CB  . LEU D 128 ? 0.7692 0.3369 0.3580 0.0247  -0.0376 -0.0403 128 LEU D CB  
13190 C CG  . LEU D 128 ? 0.7883 0.3495 0.3594 0.0399  -0.0200 -0.0385 128 LEU D CG  
13191 C CD1 . LEU D 128 ? 0.8132 0.3403 0.3515 0.0468  -0.0156 -0.0413 128 LEU D CD1 
13192 C CD2 . LEU D 128 ? 0.8056 0.4031 0.4096 0.0454  -0.0073 -0.0338 128 LEU D CD2 
13193 N N   . ASP D 129 ? 0.6951 0.3149 0.3567 -0.0029 -0.0625 -0.0394 129 ASP D N   
13194 C CA  . ASP D 129 ? 0.6819 0.3265 0.3786 -0.0123 -0.0667 -0.0384 129 ASP D CA  
13195 C C   . ASP D 129 ? 0.6653 0.3438 0.3939 -0.0144 -0.0669 -0.0352 129 ASP D C   
13196 O O   . ASP D 129 ? 0.5697 0.2743 0.3275 -0.0160 -0.0616 -0.0325 129 ASP D O   
13197 C CB  . ASP D 129 ? 0.7262 0.3560 0.4201 -0.0250 -0.0826 -0.0422 129 ASP D CB  
13198 C CG  . ASP D 129 ? 0.7881 0.3903 0.4600 -0.0253 -0.0812 -0.0447 129 ASP D CG  
13199 O OD1 . ASP D 129 ? 0.8404 0.4348 0.4984 -0.0144 -0.0679 -0.0435 129 ASP D OD1 
13200 O OD2 . ASP D 129 ? 0.8256 0.4138 0.4941 -0.0363 -0.0932 -0.0479 129 ASP D OD2 
13201 N N   . LEU D 130 ? 0.5989 0.2755 0.3204 -0.0141 -0.0727 -0.0353 130 LEU D N   
13202 C CA  . LEU D 130 ? 0.6059 0.3120 0.3552 -0.0157 -0.0731 -0.0323 130 LEU D CA  
13203 C C   . LEU D 130 ? 0.6886 0.4142 0.4489 -0.0069 -0.0568 -0.0283 130 LEU D C   
13204 O O   . LEU D 130 ? 0.6992 0.4532 0.4898 -0.0091 -0.0540 -0.0256 130 LEU D O   
13205 C CB  . LEU D 130 ? 0.6135 0.3101 0.3492 -0.0164 -0.0829 -0.0332 130 LEU D CB  
13206 C CG  . LEU D 130 ? 0.5938 0.3163 0.3575 -0.0207 -0.0889 -0.0311 130 LEU D CG  
13207 C CD1 . LEU D 130 ? 0.6031 0.3455 0.3994 -0.0305 -0.0963 -0.0314 130 LEU D CD1 
13208 C CD2 . LEU D 130 ? 0.6679 0.3743 0.4125 -0.0215 -0.1012 -0.0325 130 LEU D CD2 
13209 N N   . GLN D 131 ? 0.6489 0.3598 0.3853 0.0032  -0.0459 -0.0279 131 GLN D N   
13210 C CA  . GLN D 131 ? 0.6030 0.3336 0.3514 0.0114  -0.0306 -0.0241 131 GLN D CA  
13211 C C   . GLN D 131 ? 0.6245 0.3715 0.3945 0.0109  -0.0253 -0.0228 131 GLN D C   
13212 O O   . GLN D 131 ? 0.6445 0.4185 0.4401 0.0113  -0.0195 -0.0197 131 GLN D O   
13213 C CB  . GLN D 131 ? 0.5873 0.2989 0.3067 0.0226  -0.0195 -0.0240 131 GLN D CB  
13214 C CG  . GLN D 131 ? 0.5917 0.2842 0.2851 0.0245  -0.0223 -0.0250 131 GLN D CG  
13215 C CD  . GLN D 131 ? 0.6436 0.3121 0.3049 0.0353  -0.0113 -0.0257 131 GLN D CD  
13216 O OE1 . GLN D 131 ? 0.6576 0.3094 0.3049 0.0387  -0.0090 -0.0276 131 GLN D OE1 
13217 N NE2 . GLN D 131 ? 0.6426 0.3087 0.2918 0.0410  -0.0035 -0.0239 131 GLN D NE2 
13218 N N   . THR D 132 ? 0.5712 0.3003 0.3293 0.0100  -0.0273 -0.0251 132 THR D N   
13219 C CA  . THR D 132 ? 0.6185 0.3585 0.3914 0.0113  -0.0209 -0.0237 132 THR D CA  
13220 C C   . THR D 132 ? 0.5909 0.3520 0.3940 0.0009  -0.0273 -0.0230 132 THR D C   
13221 O O   . THR D 132 ? 0.5911 0.3736 0.4157 0.0021  -0.0208 -0.0202 132 THR D O   
13222 C CB  . THR D 132 ? 0.5572 0.2684 0.3051 0.0139  -0.0205 -0.0263 132 THR D CB  
13223 O OG1 . THR D 132 ? 0.5938 0.2838 0.3118 0.0240  -0.0143 -0.0271 132 THR D OG1 
13224 C CG2 . THR D 132 ? 0.5443 0.2646 0.3038 0.0175  -0.0126 -0.0243 132 THR D CG2 
13225 N N   . LEU D 133 ? 0.5758 0.3312 0.3812 -0.0093 -0.0400 -0.0254 133 LEU D N   
13226 C CA  . LEU D 133 ? 0.5499 0.3258 0.3851 -0.0190 -0.0453 -0.0247 133 LEU D CA  
13227 C C   . LEU D 133 ? 0.5141 0.3185 0.3735 -0.0184 -0.0426 -0.0217 133 LEU D C   
13228 O O   . LEU D 133 ? 0.4754 0.3007 0.3604 -0.0225 -0.0409 -0.0199 133 LEU D O   
13229 C CB  . LEU D 133 ? 0.5226 0.2868 0.3560 -0.0297 -0.0599 -0.0281 133 LEU D CB  
13230 C CG  . LEU D 133 ? 0.5882 0.3266 0.4032 -0.0335 -0.0633 -0.0311 133 LEU D CG  
13231 C CD1 . LEU D 133 ? 0.5266 0.2536 0.3396 -0.0447 -0.0791 -0.0345 133 LEU D CD1 
13232 C CD2 . LEU D 133 ? 0.5792 0.3260 0.4090 -0.0357 -0.0566 -0.0295 133 LEU D CD2 
13233 N N   . ASN D 134 ? 0.4849 0.2890 0.3353 -0.0134 -0.0415 -0.0209 134 ASN D N   
13234 C CA  . ASN D 134 ? 0.4672 0.2964 0.3381 -0.0121 -0.0373 -0.0178 134 ASN D CA  
13235 C C   . ASN D 134 ? 0.4994 0.3442 0.3812 -0.0062 -0.0247 -0.0148 134 ASN D C   
13236 O O   . ASN D 134 ? 0.5214 0.3883 0.4273 -0.0089 -0.0226 -0.0128 134 ASN D O   
13237 C CB  . ASN D 134 ? 0.5699 0.3928 0.4260 -0.0081 -0.0380 -0.0175 134 ASN D CB  
13238 C CG  . ASN D 134 ? 0.5660 0.3886 0.4267 -0.0149 -0.0512 -0.0188 134 ASN D CG  
13239 O OD1 . ASN D 134 ? 0.5049 0.3480 0.3889 -0.0184 -0.0533 -0.0172 134 ASN D OD1 
13240 N ND2 . ASN D 134 ? 0.6301 0.4287 0.4681 -0.0165 -0.0606 -0.0218 134 ASN D ND2 
13241 N N   . LEU D 135 ? 0.4713 0.3039 0.3348 0.0021  -0.0166 -0.0147 135 LEU D N   
13242 C CA  . LEU D 135 ? 0.4275 0.2730 0.3006 0.0081  -0.0061 -0.0122 135 LEU D CA  
13243 C C   . LEU D 135 ? 0.4427 0.2959 0.3323 0.0025  -0.0080 -0.0120 135 LEU D C   
13244 O O   . LEU D 135 ? 0.3639 0.2383 0.2743 0.0018  -0.0042 -0.0095 135 LEU D O   
13245 C CB  . LEU D 135 ? 0.4536 0.2807 0.3029 0.0179  0.0011  -0.0127 135 LEU D CB  
13246 C CG  . LEU D 135 ? 0.5445 0.3681 0.3797 0.0265  0.0087  -0.0117 135 LEU D CG  
13247 C CD1 . LEU D 135 ? 0.6446 0.4546 0.4622 0.0372  0.0177  -0.0117 135 LEU D CD1 
13248 C CD2 . LEU D 135 ? 0.5032 0.3545 0.3606 0.0271  0.0143  -0.0082 135 LEU D CD2 
13249 N N   . LEU D 136 ? 0.5048 0.3391 0.3835 -0.0017 -0.0135 -0.0146 136 LEU D N   
13250 C CA  . LEU D 136 ? 0.3979 0.2351 0.2879 -0.0066 -0.0138 -0.0144 136 LEU D CA  
13251 C C   . LEU D 136 ? 0.4101 0.2670 0.3266 -0.0160 -0.0183 -0.0137 136 LEU D C   
13252 O O   . LEU D 136 ? 0.3627 0.2291 0.2931 -0.0187 -0.0153 -0.0123 136 LEU D O   
13253 C CB  . LEU D 136 ? 0.4619 0.2721 0.3325 -0.0101 -0.0189 -0.0175 136 LEU D CB  
13254 C CG  . LEU D 136 ? 0.4489 0.2378 0.2931 0.0000  -0.0128 -0.0181 136 LEU D CG  
13255 C CD1 . LEU D 136 ? 0.4793 0.2383 0.3011 -0.0045 -0.0195 -0.0217 136 LEU D CD1 
13256 C CD2 . LEU D 136 ? 0.4394 0.2368 0.2900 0.0068  -0.0035 -0.0152 136 LEU D CD2 
13257 N N   . ALA D 137 ? 0.3913 0.2537 0.3142 -0.0207 -0.0254 -0.0146 137 ALA D N   
13258 C CA  . ALA D 137 ? 0.4802 0.3623 0.4292 -0.0283 -0.0289 -0.0137 137 ALA D CA  
13259 C C   . ALA D 137 ? 0.4363 0.3404 0.4021 -0.0248 -0.0208 -0.0104 137 ALA D C   
13260 O O   . ALA D 137 ? 0.4252 0.3434 0.4107 -0.0299 -0.0203 -0.0094 137 ALA D O   
13261 C CB  . ALA D 137 ? 0.4679 0.3516 0.4195 -0.0320 -0.0381 -0.0150 137 ALA D CB  
13262 N N   . TRP D 138 ? 0.4299 0.3368 0.3880 -0.0164 -0.0140 -0.0088 138 TRP D N   
13263 C CA  . TRP D 138 ? 0.3833 0.3103 0.3559 -0.0131 -0.0071 -0.0057 138 TRP D CA  
13264 C C   . TRP D 138 ? 0.3901 0.3176 0.3611 -0.0081 0.0000  -0.0042 138 TRP D C   
13265 O O   . TRP D 138 ? 0.3251 0.2670 0.3043 -0.0040 0.0058  -0.0018 138 TRP D O   
13266 C CB  . TRP D 138 ? 0.3387 0.2702 0.3061 -0.0079 -0.0043 -0.0046 138 TRP D CB  
13267 C CG  . TRP D 138 ? 0.3681 0.3011 0.3390 -0.0125 -0.0113 -0.0054 138 TRP D CG  
13268 C CD1 . TRP D 138 ? 0.4204 0.3374 0.3770 -0.0141 -0.0187 -0.0078 138 TRP D CD1 
13269 C CD2 . TRP D 138 ? 0.3272 0.2776 0.3164 -0.0160 -0.0124 -0.0040 138 TRP D CD2 
13270 N NE1 . TRP D 138 ? 0.3657 0.2899 0.3312 -0.0179 -0.0246 -0.0077 138 TRP D NE1 
13271 C CE2 . TRP D 138 ? 0.3919 0.3364 0.3774 -0.0189 -0.0205 -0.0053 138 TRP D CE2 
13272 C CE3 . TRP D 138 ? 0.2858 0.2547 0.2926 -0.0167 -0.0076 -0.0017 138 TRP D CE3 
13273 C CZ2 . TRP D 138 ? 0.3118 0.2687 0.3112 -0.0218 -0.0235 -0.0043 138 TRP D CZ2 
13274 C CZ3 . TRP D 138 ? 0.2664 0.2466 0.2860 -0.0200 -0.0102 -0.0009 138 TRP D CZ3 
13275 C CH2 . TRP D 138 ? 0.3055 0.2799 0.3218 -0.0222 -0.0178 -0.0021 138 TRP D CH2 
13276 N N   . CYS D 139 ? 0.3255 0.2364 0.2851 -0.0085 -0.0008 -0.0057 139 CYS D N   
13277 C CA  . CYS D 139 ? 0.3588 0.2670 0.3139 -0.0030 0.0052  -0.0043 139 CYS D CA  
13278 C C   . CYS D 139 ? 0.3422 0.2658 0.3159 -0.0069 0.0070  -0.0023 139 CYS D C   
13279 O O   . CYS D 139 ? 0.3268 0.2526 0.3110 -0.0154 0.0035  -0.0031 139 CYS D O   
13280 C CB  . CYS D 139 ? 0.4067 0.2909 0.3443 -0.0037 0.0032  -0.0064 139 CYS D CB  
13281 S SG  . CYS D 139 ? 0.4956 0.3730 0.4245 0.0043  0.0101  -0.0045 139 CYS D SG  
13282 N N   . GLY D 140 ? 0.3471 0.2809 0.3247 -0.0009 0.0125  0.0001  140 GLY D N   
13283 C CA  . GLY D 140 ? 0.3328 0.2773 0.3243 -0.0049 0.0137  0.0016  140 GLY D CA  
13284 C C   . GLY D 140 ? 0.4717 0.4035 0.4553 -0.0044 0.0156  0.0020  140 GLY D C   
13285 O O   . GLY D 140 ? 0.4650 0.3787 0.4319 -0.0007 0.0159  0.0011  140 GLY D O   
13286 N N   . ARG D 141 ? 0.7142 0.6556 0.7092 -0.0076 0.0174  0.0036  141 ARG D N   
13287 C CA  . ARG D 141 ? 0.4089 0.3395 0.3983 -0.0088 0.0195  0.0044  141 ARG D CA  
13288 C C   . ARG D 141 ? 0.3043 0.2230 0.2771 0.0011  0.0219  0.0054  141 ARG D C   
13289 O O   . ARG D 141 ? 0.3799 0.2790 0.3389 0.0007  0.0221  0.0047  141 ARG D O   
13290 C CB  . ARG D 141 ? 0.3249 0.2688 0.3275 -0.0120 0.0217  0.0063  141 ARG D CB  
13291 C CG  . ARG D 141 ? 0.3632 0.2936 0.3592 -0.0152 0.0242  0.0070  141 ARG D CG  
13292 C CD  . ARG D 141 ? 0.4481 0.3882 0.4535 -0.0180 0.0272  0.0089  141 ARG D CD  
13293 N NE  . ARG D 141 ? 0.5469 0.4921 0.5479 -0.0093 0.0282  0.0111  141 ARG D NE  
13294 C CZ  . ARG D 141 ? 0.4806 0.4177 0.4722 -0.0058 0.0302  0.0130  141 ARG D CZ  
13295 N NH1 . ARG D 141 ? 0.4812 0.4033 0.4655 -0.0108 0.0328  0.0133  141 ARG D NH1 
13296 N NH2 . ARG D 141 ? 0.4701 0.4145 0.4599 0.0025  0.0295  0.0149  141 ARG D NH2 
13297 N N   . THR D 142 ? 0.2983 0.2283 0.2726 0.0100  0.0239  0.0071  142 THR D N   
13298 C CA  . THR D 142 ? 0.3527 0.2738 0.3138 0.0206  0.0262  0.0085  142 THR D CA  
13299 C C   . THR D 142 ? 0.4097 0.3105 0.3525 0.0247  0.0262  0.0065  142 THR D C   
13300 O O   . THR D 142 ? 0.4404 0.3220 0.3674 0.0284  0.0271  0.0065  142 THR D O   
13301 C CB  . THR D 142 ? 0.4012 0.3416 0.3710 0.0290  0.0280  0.0106  142 THR D CB  
13302 O OG1 . THR D 142 ? 0.3790 0.3355 0.3631 0.0253  0.0275  0.0124  142 THR D OG1 
13303 C CG2 . THR D 142 ? 0.4365 0.3695 0.3947 0.0412  0.0302  0.0121  142 THR D CG2 
13304 N N   . LEU D 143 ? 0.4621 0.3651 0.4048 0.0244  0.0252  0.0048  143 LEU D N   
13305 C CA  . LEU D 143 ? 0.4920 0.3744 0.4154 0.0284  0.0251  0.0027  143 LEU D CA  
13306 C C   . LEU D 143 ? 0.4804 0.3427 0.3943 0.0190  0.0208  0.0000  143 LEU D C   
13307 O O   . LEU D 143 ? 0.5350 0.3750 0.4291 0.0218  0.0204  -0.0019 143 LEU D O   
13308 C CB  . LEU D 143 ? 0.3509 0.2412 0.2755 0.0313  0.0256  0.0019  143 LEU D CB  
13309 C CG  . LEU D 143 ? 0.4026 0.3064 0.3303 0.0427  0.0311  0.0042  143 LEU D CG  
13310 C CD1 . LEU D 143 ? 0.3470 0.2544 0.2729 0.0443  0.0325  0.0032  143 LEU D CD1 
13311 C CD2 . LEU D 143 ? 0.4188 0.3074 0.3304 0.0538  0.0346  0.0047  143 LEU D CD2 
13312 N N   . ARG D 144 ? 0.5756 0.4448 0.5031 0.0078  0.0179  -0.0003 144 ARG D N   
13313 C CA  . ARG D 144 ? 0.6416 0.4939 0.5632 -0.0020 0.0138  -0.0028 144 ARG D CA  
13314 C C   . ARG D 144 ? 0.7206 0.5494 0.6243 -0.0007 0.0156  -0.0028 144 ARG D C   
13315 O O   . ARG D 144 ? 0.7578 0.5686 0.6528 -0.0084 0.0123  -0.0050 144 ARG D O   
13316 C CB  . ARG D 144 ? 0.6383 0.5050 0.5807 -0.0135 0.0116  -0.0027 144 ARG D CB  
13317 C CG  . ARG D 144 ? 0.6302 0.5091 0.5845 -0.0184 0.0067  -0.0043 144 ARG D CG  
13318 C CD  . ARG D 144 ? 0.6339 0.5274 0.6098 -0.0286 0.0050  -0.0040 144 ARG D CD  
13319 N NE  . ARG D 144 ? 0.6417 0.5485 0.6297 -0.0315 0.0004  -0.0050 144 ARG D NE  
13320 C CZ  . ARG D 144 ? 0.6591 0.5639 0.6532 -0.0399 -0.0061 -0.0072 144 ARG D CZ  
13321 N NH1 . ARG D 144 ? 0.6743 0.5653 0.6647 -0.0471 -0.0084 -0.0088 144 ARG D NH1 
13322 N NH2 . ARG D 144 ? 0.6069 0.5234 0.6108 -0.0411 -0.0106 -0.0078 144 ARG D NH2 
13323 N N   . LYS D 145 ? 0.7318 0.5593 0.6293 0.0088  0.0202  -0.0003 145 LYS D N   
13324 C CA  . LYS D 145 ? 0.7249 0.5269 0.6018 0.0120  0.0219  -0.0002 145 LYS D CA  
13325 C C   . LYS D 145 ? 0.8223 0.6071 0.6776 0.0233  0.0231  -0.0012 145 LYS D C   
13326 O O   . LYS D 145 ? 0.8797 0.6374 0.7145 0.0221  0.0221  -0.0031 145 LYS D O   
13327 C CB  . LYS D 145 ? 0.7661 0.5728 0.6457 0.0161  0.0255  0.0031  145 LYS D CB  
13328 C CG  . LYS D 145 ? 0.7875 0.5910 0.6559 0.0313  0.0286  0.0052  145 LYS D CG  
13329 C CD  . LYS D 145 ? 0.8115 0.6121 0.6774 0.0340  0.0306  0.0082  145 LYS D CD  
13330 C CE  . LYS D 145 ? 0.8665 0.6690 0.7256 0.0501  0.0324  0.0105  145 LYS D CE  
13331 N NZ  . LYS D 145 ? 0.9176 0.6995 0.7563 0.0591  0.0336  0.0090  145 LYS D NZ  
13332 N N   . ASP D 146 ? 0.7611 0.5602 0.6203 0.0339  0.0255  -0.0002 146 ASP D N   
13333 C CA  . ASP D 146 ? 0.7495 0.5330 0.5889 0.0454  0.0281  -0.0011 146 ASP D CA  
13334 C C   . ASP D 146 ? 0.7373 0.5067 0.5653 0.0405  0.0246  -0.0048 146 ASP D C   
13335 O O   . ASP D 146 ? 0.6786 0.4240 0.4832 0.0466  0.0257  -0.0065 146 ASP D O   
13336 C CB  . ASP D 146 ? 0.8067 0.6119 0.6562 0.0575  0.0325  0.0012  146 ASP D CB  
13337 C CG  . ASP D 146 ? 0.8549 0.6792 0.7202 0.0604  0.0339  0.0047  146 ASP D CG  
13338 O OD1 . ASP D 146 ? 0.7674 0.6036 0.6476 0.0503  0.0314  0.0054  146 ASP D OD1 
13339 O OD2 . ASP D 146 ? 0.9201 0.7476 0.7826 0.0732  0.0373  0.0069  146 ASP D OD2 
13340 N N   . LEU D 147 ? 0.6842 0.4669 0.5271 0.0298  0.0202  -0.0060 147 LEU D N   
13341 C CA  . LEU D 147 ? 0.6559 0.4261 0.4889 0.0244  0.0153  -0.0094 147 LEU D CA  
13342 C C   . LEU D 147 ? 0.6888 0.4439 0.5190 0.0106  0.0088  -0.0118 147 LEU D C   
13343 O O   . LEU D 147 ? 0.7728 0.5237 0.6021 0.0028  0.0024  -0.0145 147 LEU D O   
13344 C CB  . LEU D 147 ? 0.5997 0.3931 0.4495 0.0226  0.0140  -0.0091 147 LEU D CB  
13345 C CG  . LEU D 147 ? 0.5934 0.4043 0.4489 0.0347  0.0210  -0.0065 147 LEU D CG  
13346 C CD1 . LEU D 147 ? 0.5545 0.3879 0.4274 0.0310  0.0197  -0.0060 147 LEU D CD1 
13347 C CD2 . LEU D 147 ? 0.6613 0.4531 0.4929 0.0466  0.0255  -0.0075 147 LEU D CD2 
13348 N N   . LYS D 148 ? 0.6450 0.3912 0.4734 0.0074  0.0101  -0.0108 148 LYS D N   
13349 C CA  . LYS D 148 ? 0.6407 0.3752 0.4698 -0.0068 0.0050  -0.0126 148 LYS D CA  
13350 C C   . LYS D 148 ? 0.6501 0.3562 0.4564 -0.0105 -0.0005 -0.0165 148 LYS D C   
13351 O O   . LYS D 148 ? 0.6626 0.3671 0.4750 -0.0230 -0.0077 -0.0189 148 LYS D O   
13352 C CB  . LYS D 148 ? 0.6614 0.3876 0.4881 -0.0082 0.0090  -0.0105 148 LYS D CB  
13353 C CG  . LYS D 148 ? 0.7077 0.4199 0.5342 -0.0232 0.0052  -0.0122 148 LYS D CG  
13354 C CD  . LYS D 148 ? 0.7362 0.4508 0.5702 -0.0271 0.0101  -0.0094 148 LYS D CD  
13355 C CE  . LYS D 148 ? 0.7334 0.4434 0.5765 -0.0441 0.0071  -0.0107 148 LYS D CE  
13356 N NZ  . LYS D 148 ? 0.7284 0.4374 0.5756 -0.0480 0.0132  -0.0078 148 LYS D NZ  
13357 N N   . ASP D 149 ? 0.6816 0.3644 0.4611 0.0003  0.0025  -0.0172 149 ASP D N   
13358 C CA  . ASP D 149 ? 0.7957 0.4483 0.5498 -0.0026 -0.0027 -0.0212 149 ASP D CA  
13359 C C   . ASP D 149 ? 0.7626 0.4212 0.5179 -0.0042 -0.0081 -0.0235 149 ASP D C   
13360 O O   . ASP D 149 ? 0.7506 0.3936 0.4969 -0.0138 -0.0165 -0.0269 149 ASP D O   
13361 C CB  . ASP D 149 ? 0.9133 0.5389 0.6372 0.0109  0.0029  -0.0213 149 ASP D CB  
13362 C CG  . ASP D 149 ? 1.0274 0.6420 0.7455 0.0128  0.0074  -0.0192 149 ASP D CG  
13363 O OD1 . ASP D 149 ? 1.0961 0.7072 0.8211 -0.0003 0.0043  -0.0193 149 ASP D OD1 
13364 O OD2 . ASP D 149 ? 1.0504 0.6597 0.7571 0.0276  0.0141  -0.0172 149 ASP D OD2 
13365 N N   . LEU D 150 ? 0.7261 0.4059 0.4911 0.0052  -0.0038 -0.0216 150 LEU D N   
13366 C CA  . LEU D 150 ? 0.7229 0.4085 0.4888 0.0039  -0.0084 -0.0233 150 LEU D CA  
13367 C C   . LEU D 150 ? 0.7405 0.4455 0.5315 -0.0099 -0.0164 -0.0238 150 LEU D C   
13368 O O   . LEU D 150 ? 0.7988 0.4986 0.5858 -0.0157 -0.0245 -0.0263 150 LEU D O   
13369 C CB  . LEU D 150 ? 0.7101 0.4140 0.4811 0.0167  -0.0007 -0.0208 150 LEU D CB  
13370 C CG  . LEU D 150 ? 0.7290 0.4136 0.4736 0.0313  0.0065  -0.0212 150 LEU D CG  
13371 C CD1 . LEU D 150 ? 0.6320 0.3408 0.3890 0.0427  0.0151  -0.0180 150 LEU D CD1 
13372 C CD2 . LEU D 150 ? 0.7866 0.4428 0.5034 0.0299  0.0013  -0.0252 150 LEU D CD2 
13373 N N   . LEU D 151 ? 0.6429 0.3697 0.4590 -0.0146 -0.0142 -0.0212 151 LEU D N   
13374 C CA  . LEU D 151 ? 0.5995 0.3454 0.4409 -0.0269 -0.0207 -0.0214 151 LEU D CA  
13375 C C   . LEU D 151 ? 0.6263 0.3555 0.4642 -0.0402 -0.0288 -0.0243 151 LEU D C   
13376 O O   . LEU D 151 ? 0.6726 0.4087 0.5223 -0.0496 -0.0375 -0.0260 151 LEU D O   
13377 C CB  . LEU D 151 ? 0.6099 0.3817 0.4767 -0.0274 -0.0148 -0.0178 151 LEU D CB  
13378 C CG  . LEU D 151 ? 0.5704 0.3679 0.4518 -0.0195 -0.0100 -0.0151 151 LEU D CG  
13379 C CD1 . LEU D 151 ? 0.5243 0.3394 0.4225 -0.0181 -0.0033 -0.0117 151 LEU D CD1 
13380 C CD2 . LEU D 151 ? 0.5076 0.3208 0.4048 -0.0256 -0.0163 -0.0159 151 LEU D CD2 
13381 N N   . ASN D 152 ? 0.6310 0.3381 0.4533 -0.0414 -0.0264 -0.0247 152 ASN D N   
13382 C CA  . ASN D 152 ? 0.6947 0.3847 0.5133 -0.0551 -0.0338 -0.0274 152 ASN D CA  
13383 C C   . ASN D 152 ? 0.7409 0.4028 0.5325 -0.0561 -0.0418 -0.0315 152 ASN D C   
13384 O O   . ASN D 152 ? 0.7764 0.4267 0.5671 -0.0689 -0.0508 -0.0343 152 ASN D O   
13385 C CB  . ASN D 152 ? 0.7332 0.4082 0.5441 -0.0572 -0.0280 -0.0262 152 ASN D CB  
13386 C CG  . ASN D 152 ? 0.7507 0.4500 0.5867 -0.0586 -0.0213 -0.0225 152 ASN D CG  
13387 O OD1 . ASN D 152 ? 0.7546 0.4806 0.6176 -0.0638 -0.0230 -0.0216 152 ASN D OD1 
13388 N ND2 . ASN D 152 ? 0.7608 0.4493 0.5863 -0.0536 -0.0136 -0.0203 152 ASN D ND2 
13389 N N   . LYS D 153 ? 0.7577 0.4074 0.5265 -0.0431 -0.0385 -0.0320 153 LYS D N   
13390 C CA  . LYS D 153 ? 0.8164 0.4398 0.5582 -0.0432 -0.0460 -0.0359 153 LYS D CA  
13391 C C   . LYS D 153 ? 0.8233 0.4590 0.5793 -0.0526 -0.0576 -0.0378 153 LYS D C   
13392 O O   . LYS D 153 ? 0.8996 0.5183 0.6470 -0.0632 -0.0686 -0.0413 153 LYS D O   
13393 C CB  . LYS D 153 ? 0.8158 0.4300 0.5353 -0.0264 -0.0384 -0.0354 153 LYS D CB  
13394 C CG  . LYS D 153 ? 0.8855 0.4648 0.5691 -0.0240 -0.0431 -0.0393 153 LYS D CG  
13395 C CD  . LYS D 153 ? 0.9007 0.4709 0.5631 -0.0063 -0.0324 -0.0383 153 LYS D CD  
13396 C CE  . LYS D 153 ? 0.9606 0.4958 0.5858 -0.0031 -0.0364 -0.0423 153 LYS D CE  
13397 N NZ  . LYS D 153 ? 0.9883 0.5165 0.5944 0.0148  -0.0248 -0.0411 153 LYS D NZ  
13398 N N   . GLY D 154 ? 0.7798 0.4447 0.5574 -0.0489 -0.0558 -0.0355 154 GLY D N   
13399 C CA  . GLY D 154 ? 0.7650 0.4456 0.5606 -0.0571 -0.0662 -0.0365 154 GLY D CA  
13400 C C   . GLY D 154 ? 0.7686 0.4310 0.5413 -0.0555 -0.0749 -0.0396 154 GLY D C   
13401 O O   . GLY D 154 ? 0.7768 0.4534 0.5631 -0.0596 -0.0832 -0.0399 154 GLY D O   
13402 N N   . ARG D 155 ? 0.7591 0.3897 0.4963 -0.0491 -0.0734 -0.0418 155 ARG D N   
13403 C CA  . ARG D 155 ? 0.8161 0.4250 0.5270 -0.0475 -0.0815 -0.0449 155 ARG D CA  
13404 C C   . ARG D 155 ? 0.8654 0.4430 0.5382 -0.0357 -0.0737 -0.0461 155 ARG D C   
13405 O O   . ARG D 155 ? 0.8919 0.4612 0.5583 -0.0311 -0.0648 -0.0451 155 ARG D O   
13406 C CB  . ARG D 155 ? 0.8369 0.4325 0.5459 -0.0623 -0.0982 -0.0488 155 ARG D CB  
13407 C CG  . ARG D 155 ? 0.8830 0.4548 0.5797 -0.0702 -0.1002 -0.0511 155 ARG D CG  
13408 C CD  . ARG D 155 ? 0.9479 0.5074 0.6437 -0.0858 -0.1179 -0.0551 155 ARG D CD  
13409 N NE  . ARG D 155 ? 0.9907 0.5835 0.7275 -0.0968 -0.1248 -0.0538 155 ARG D NE  
13410 C CZ  . ARG D 155 ? 1.0305 0.6346 0.7790 -0.1018 -0.1376 -0.0549 155 ARG D CZ  
13411 N NH1 . ARG D 155 ? 0.9718 0.6072 0.7592 -0.1108 -0.1424 -0.0535 155 ARG D NH1 
13412 N NH2 . ARG D 155 ? 1.1229 0.7062 0.8432 -0.0974 -0.1454 -0.0575 155 ARG D NH2 
13413 N N   . ASN D 156 ? 0.8964 0.4563 0.5435 -0.0301 -0.0766 -0.0481 156 ASN D N   
13414 C CA  . ASN D 156 ? 0.9057 0.4318 0.5126 -0.0191 -0.0702 -0.0499 156 ASN D CA  
13415 C C   . ASN D 156 ? 0.8560 0.3927 0.4642 -0.0036 -0.0525 -0.0462 156 ASN D C   
13416 O O   . ASN D 156 ? 0.8980 0.4160 0.4881 0.0036  -0.0447 -0.0464 156 ASN D O   
13417 C CB  . ASN D 156 ? 0.9495 0.4412 0.5323 -0.0257 -0.0762 -0.0536 156 ASN D CB  
13418 C CG  . ASN D 156 ? 1.0220 0.4990 0.5979 -0.0398 -0.0944 -0.0577 156 ASN D CG  
13419 O OD1 . ASN D 156 ? 1.0639 0.5388 0.6505 -0.0532 -0.1030 -0.0593 156 ASN D OD1 
13420 N ND2 . ASN D 156 ? 1.0885 0.5561 0.6475 -0.0372 -0.1005 -0.0594 156 ASN D ND2 
13421 N N   . TYR D 157 ? 0.7741 0.3402 0.4032 0.0016  -0.0467 -0.0429 157 TYR D N   
13422 C CA  . TYR D 157 ? 0.7839 0.3649 0.4186 0.0155  -0.0310 -0.0392 157 TYR D CA  
13423 C C   . TYR D 157 ? 0.8239 0.3859 0.4285 0.0282  -0.0233 -0.0398 157 TYR D C   
13424 O O   . TYR D 157 ? 0.8394 0.3898 0.4285 0.0264  -0.0293 -0.0417 157 TYR D O   
13425 C CB  . TYR D 157 ? 0.7422 0.3639 0.4142 0.0141  -0.0282 -0.0353 157 TYR D CB  
13426 C CG  . TYR D 157 ? 0.7323 0.3746 0.4349 0.0032  -0.0330 -0.0341 157 TYR D CG  
13427 C CD1 . TYR D 157 ? 0.7531 0.4060 0.4684 0.0066  -0.0249 -0.0317 157 TYR D CD1 
13428 C CD2 . TYR D 157 ? 0.6940 0.3454 0.4128 -0.0099 -0.0455 -0.0354 157 TYR D CD2 
13429 C CE1 . TYR D 157 ? 0.6916 0.3621 0.4333 -0.0033 -0.0282 -0.0305 157 TYR D CE1 
13430 C CE2 . TYR D 157 ? 0.6787 0.3493 0.4260 -0.0195 -0.0486 -0.0343 157 TYR D CE2 
13431 C CZ  . TYR D 157 ? 0.6569 0.3363 0.4147 -0.0163 -0.0395 -0.0318 157 TYR D CZ  
13432 O OH  . TYR D 157 ? 0.6786 0.3753 0.4627 -0.0259 -0.0415 -0.0307 157 TYR D OH  
13433 N N   . THR D 158 ? 0.8002 0.3595 0.3968 0.0415  -0.0096 -0.0380 158 THR D N   
13434 C CA  . THR D 158 ? 0.7587 0.3021 0.3290 0.0552  0.0007  -0.0381 158 THR D CA  
13435 C C   . THR D 158 ? 0.7375 0.3136 0.3303 0.0629  0.0116  -0.0338 158 THR D C   
13436 O O   . THR D 158 ? 0.7384 0.3477 0.3655 0.0598  0.0128  -0.0306 158 THR D O   
13437 C CB  . THR D 158 ? 0.8138 0.3332 0.3606 0.0666  0.0098  -0.0388 158 THR D CB  
13438 O OG1 . THR D 158 ? 0.8004 0.3459 0.3735 0.0724  0.0184  -0.0349 158 THR D OG1 
13439 C CG2 . THR D 158 ? 0.7895 0.2745 0.3129 0.0582  -0.0008 -0.0431 158 THR D CG2 
13440 N N   . GLN D 159 ? 0.7216 0.2866 0.2935 0.0727  0.0200  -0.0337 159 GLN D N   
13441 C CA  . GLN D 159 ? 0.7228 0.3160 0.3130 0.0809  0.0325  -0.0296 159 GLN D CA  
13442 C C   . GLN D 159 ? 0.6817 0.2978 0.2948 0.0890  0.0427  -0.0262 159 GLN D C   
13443 O O   . GLN D 159 ? 0.6611 0.3120 0.3060 0.0885  0.0465  -0.0225 159 GLN D O   
13444 C CB  . GLN D 159 ? 0.7967 0.3687 0.3560 0.0916  0.0422  -0.0302 159 GLN D CB  
13445 C CG  . GLN D 159 ? 0.8209 0.4199 0.3973 0.1005  0.0568  -0.0259 159 GLN D CG  
13446 C CD  . GLN D 159 ? 0.7625 0.3837 0.3581 0.0916  0.0520  -0.0241 159 GLN D CD  
13447 O OE1 . GLN D 159 ? 0.7931 0.4032 0.3811 0.0812  0.0386  -0.0265 159 GLN D OE1 
13448 N NE2 . GLN D 159 ? 0.6999 0.3526 0.3209 0.0957  0.0625  -0.0199 159 GLN D NE2 
13449 N N   . GLU D 160 ? 0.7077 0.3035 0.3040 0.0963  0.0463  -0.0274 160 GLU D N   
13450 C CA  . GLU D 160 ? 0.7263 0.3407 0.3410 0.1054  0.0553  -0.0242 160 GLU D CA  
13451 C C   . GLU D 160 ? 0.7189 0.3597 0.3666 0.0953  0.0481  -0.0223 160 GLU D C   
13452 O O   . GLU D 160 ? 0.7185 0.3882 0.3923 0.1000  0.0542  -0.0186 160 GLU D O   
13453 C CB  . GLU D 160 ? 0.7181 0.3008 0.3046 0.1150  0.0591  -0.0261 160 GLU D CB  
13454 C CG  . GLU D 160 ? 0.9401 0.5361 0.5354 0.1312  0.0728  -0.0228 160 GLU D CG  
13455 C CD  . GLU D 160 ? 1.1528 0.7261 0.7325 0.1371  0.0728  -0.0238 160 GLU D CD  
13456 O OE1 . GLU D 160 ? 1.2253 0.7984 0.8013 0.1529  0.0840  -0.0219 160 GLU D OE1 
13457 O OE2 . GLU D 160 ? 1.2406 0.7962 0.8120 0.1259  0.0618  -0.0263 160 GLU D OE2 
13458 N N   . GLU D 161 ? 0.7165 0.3475 0.3633 0.0815  0.0351  -0.0249 161 GLU D N   
13459 C CA  . GLU D 161 ? 0.7389 0.3929 0.4155 0.0718  0.0291  -0.0232 161 GLU D CA  
13460 C C   . GLU D 161 ? 0.6716 0.3600 0.3783 0.0662  0.0282  -0.0206 161 GLU D C   
13461 O O   . GLU D 161 ? 0.5618 0.2774 0.2961 0.0651  0.0300  -0.0176 161 GLU D O   
13462 C CB  . GLU D 161 ? 0.7756 0.4096 0.4436 0.0584  0.0165  -0.0266 161 GLU D CB  
13463 C CG  . GLU D 161 ? 0.8219 0.4221 0.4621 0.0624  0.0171  -0.0288 161 GLU D CG  
13464 C CD  . GLU D 161 ? 0.8933 0.4718 0.5234 0.0479  0.0043  -0.0325 161 GLU D CD  
13465 O OE1 . GLU D 161 ? 0.9281 0.5092 0.5627 0.0371  -0.0054 -0.0343 161 GLU D OE1 
13466 O OE2 . GLU D 161 ? 0.9363 0.4947 0.5538 0.0474  0.0038  -0.0335 161 GLU D OE2 
13467 N N   . LYS D 162 ? 0.5871 0.2728 0.2867 0.0632  0.0254  -0.0217 162 LYS D N   
13468 C CA  . LYS D 162 ? 0.5915 0.3069 0.3163 0.0591  0.0254  -0.0192 162 LYS D CA  
13469 C C   . LYS D 162 ? 0.6090 0.3475 0.3481 0.0699  0.0386  -0.0153 162 LYS D C   
13470 O O   . LYS D 162 ? 0.5561 0.3247 0.3238 0.0669  0.0396  -0.0124 162 LYS D O   
13471 C CB  . LYS D 162 ? 0.6236 0.3266 0.3328 0.0550  0.0199  -0.0212 162 LYS D CB  
13472 C CG  . LYS D 162 ? 0.6165 0.3458 0.3462 0.0525  0.0215  -0.0185 162 LYS D CG  
13473 C CD  . LYS D 162 ? 0.5886 0.3017 0.2990 0.0491  0.0155  -0.0204 162 LYS D CD  
13474 C CE  . LYS D 162 ? 0.6221 0.3055 0.2963 0.0590  0.0226  -0.0220 162 LYS D CE  
13475 N NZ  . LYS D 162 ? 0.6151 0.2894 0.2732 0.0587  0.0219  -0.0222 162 LYS D NZ  
13476 N N   . GLU D 163 ? 0.5925 0.3174 0.3123 0.0827  0.0488  -0.0152 163 GLU D N   
13477 C CA  . GLU D 163 ? 0.5780 0.3263 0.3134 0.0932  0.0613  -0.0115 163 GLU D CA  
13478 C C   . GLU D 163 ? 0.5918 0.3586 0.3492 0.0953  0.0622  -0.0092 163 GLU D C   
13479 O O   . GLU D 163 ? 0.5646 0.3608 0.3469 0.0983  0.0677  -0.0057 163 GLU D O   
13480 C CB  . GLU D 163 ? 0.5812 0.3104 0.2913 0.1070  0.0726  -0.0120 163 GLU D CB  
13481 C CG  . GLU D 163 ? 0.6811 0.4010 0.3752 0.1070  0.0758  -0.0127 163 GLU D CG  
13482 C CD  . GLU D 163 ? 0.8215 0.5104 0.4806 0.1185  0.0842  -0.0146 163 GLU D CD  
13483 O OE1 . GLU D 163 ? 0.7692 0.4445 0.4090 0.1189  0.0870  -0.0155 163 GLU D OE1 
13484 O OE2 . GLU D 163 ? 0.9061 0.5825 0.5552 0.1274  0.0882  -0.0152 163 GLU D OE2 
13485 N N   . TYR D 164 ? 0.6184 0.3671 0.3657 0.0936  0.0567  -0.0110 164 TYR D N   
13486 C CA  . TYR D 164 ? 0.6168 0.3788 0.3810 0.0954  0.0569  -0.0089 164 TYR D CA  
13487 C C   . TYR D 164 ? 0.5744 0.3635 0.3682 0.0840  0.0507  -0.0072 164 TYR D C   
13488 O O   . TYR D 164 ? 0.5279 0.3417 0.3440 0.0867  0.0538  -0.0041 164 TYR D O   
13489 C CB  . TYR D 164 ? 0.6525 0.3847 0.3955 0.0950  0.0524  -0.0114 164 TYR D CB  
13490 C CG  . TYR D 164 ? 0.6865 0.4288 0.4442 0.0953  0.0514  -0.0093 164 TYR D CG  
13491 C CD1 . TYR D 164 ? 0.7327 0.4821 0.4935 0.1090  0.0594  -0.0066 164 TYR D CD1 
13492 C CD2 . TYR D 164 ? 0.7219 0.4672 0.4907 0.0822  0.0428  -0.0097 164 TYR D CD2 
13493 C CE1 . TYR D 164 ? 0.7434 0.5006 0.5157 0.1097  0.0578  -0.0045 164 TYR D CE1 
13494 C CE2 . TYR D 164 ? 0.7470 0.4996 0.5269 0.0825  0.0425  -0.0076 164 TYR D CE2 
13495 C CZ  . TYR D 164 ? 0.7512 0.5088 0.5317 0.0963  0.0496  -0.0050 164 TYR D CZ  
13496 O OH  . TYR D 164 ? 0.7629 0.5260 0.5522 0.0971  0.0486  -0.0028 164 TYR D OH  
13497 N N   . VAL D 165 ? 0.5479 0.3322 0.3418 0.0713  0.0415  -0.0093 165 VAL D N   
13498 C CA  . VAL D 165 ? 0.4584 0.2673 0.2792 0.0607  0.0361  -0.0080 165 VAL D CA  
13499 C C   . VAL D 165 ? 0.4824 0.3185 0.3218 0.0637  0.0420  -0.0050 165 VAL D C   
13500 O O   . VAL D 165 ? 0.4520 0.3126 0.3153 0.0614  0.0425  -0.0025 165 VAL D O   
13501 C CB  . VAL D 165 ? 0.4616 0.2596 0.2782 0.0480  0.0255  -0.0109 165 VAL D CB  
13502 C CG1 . VAL D 165 ? 0.4459 0.2698 0.2906 0.0382  0.0208  -0.0094 165 VAL D CG1 
13503 C CG2 . VAL D 165 ? 0.5063 0.2792 0.3073 0.0438  0.0197  -0.0136 165 VAL D CG2 
13504 N N   . LEU D 166 ? 0.4628 0.2938 0.2903 0.0684  0.0469  -0.0053 166 LEU D N   
13505 C CA  . LEU D 166 ? 0.4575 0.3131 0.3017 0.0706  0.0534  -0.0024 166 LEU D CA  
13506 C C   . LEU D 166 ? 0.4205 0.2959 0.2804 0.0797  0.0615  0.0008  166 LEU D C   
13507 O O   . LEU D 166 ? 0.5082 0.4104 0.3919 0.0774  0.0630  0.0035  166 LEU D O   
13508 C CB  . LEU D 166 ? 0.4830 0.3259 0.3080 0.0749  0.0587  -0.0031 166 LEU D CB  
13509 C CG  . LEU D 166 ? 0.5354 0.3682 0.3521 0.0651  0.0502  -0.0052 166 LEU D CG  
13510 C CD1 . LEU D 166 ? 0.6042 0.4169 0.3944 0.0704  0.0553  -0.0063 166 LEU D CD1 
13511 C CD2 . LEU D 166 ? 0.5125 0.3711 0.3546 0.0569  0.0473  -0.0031 166 LEU D CD2 
13512 N N   . ASN D 167 ? 0.4525 0.3144 0.2986 0.0904  0.0665  0.0005  167 ASN D N   
13513 C CA  . ASN D 167 ? 0.4811 0.3611 0.3420 0.1001  0.0730  0.0036  167 ASN D CA  
13514 C C   . ASN D 167 ? 0.4316 0.3283 0.3135 0.0940  0.0666  0.0050  167 ASN D C   
13515 O O   . ASN D 167 ? 0.4148 0.3378 0.3192 0.0957  0.0690  0.0080  167 ASN D O   
13516 C CB  . ASN D 167 ? 0.5466 0.4050 0.3865 0.1128  0.0780  0.0027  167 ASN D CB  
13517 C CG  . ASN D 167 ? 0.7350 0.5813 0.5566 0.1224  0.0877  0.0021  167 ASN D CG  
13518 O OD1 . ASN D 167 ? 0.7617 0.6240 0.5928 0.1228  0.0938  0.0037  167 ASN D OD1 
13519 N ND2 . ASN D 167 ? 0.7837 0.6001 0.5776 0.1302  0.0898  -0.0002 167 ASN D ND2 
13520 N N   . LYS D 168 ? 0.4119 0.2929 0.2863 0.0865  0.0586  0.0030  168 LYS D N   
13521 C CA  . LYS D 168 ? 0.4298 0.3236 0.3212 0.0810  0.0535  0.0044  168 LYS D CA  
13522 C C   . LYS D 168 ? 0.4068 0.3251 0.3212 0.0714  0.0507  0.0057  168 LYS D C   
13523 O O   . LYS D 168 ? 0.3470 0.2849 0.2799 0.0706  0.0501  0.0080  168 LYS D O   
13524 C CB  . LYS D 168 ? 0.4143 0.2851 0.2923 0.0742  0.0467  0.0019  168 LYS D CB  
13525 C CG  . LYS D 168 ? 0.4675 0.3112 0.3210 0.0831  0.0490  0.0006  168 LYS D CG  
13526 C CD  . LYS D 168 ? 0.5514 0.4040 0.4103 0.0953  0.0542  0.0035  168 LYS D CD  
13527 C CE  . LYS D 168 ? 0.5999 0.4672 0.4763 0.0904  0.0501  0.0056  168 LYS D CE  
13528 N NZ  . LYS D 168 ? 0.6011 0.4766 0.4816 0.1032  0.0541  0.0085  168 LYS D NZ  
13529 N N   . TYR D 169 ? 0.4561 0.3723 0.3680 0.0647  0.0487  0.0042  169 TYR D N   
13530 C CA  . TYR D 169 ? 0.3947 0.3313 0.3260 0.0559  0.0460  0.0053  169 TYR D CA  
13531 C C   . TYR D 169 ? 0.4240 0.3850 0.3718 0.0608  0.0525  0.0084  169 TYR D C   
13532 O O   . TYR D 169 ? 0.4294 0.4105 0.3967 0.0562  0.0508  0.0102  169 TYR D O   
13533 C CB  . TYR D 169 ? 0.4031 0.3295 0.3255 0.0491  0.0422  0.0032  169 TYR D CB  
13534 C CG  . TYR D 169 ? 0.3908 0.3028 0.3081 0.0400  0.0332  0.0005  169 TYR D CG  
13535 C CD1 . TYR D 169 ? 0.3725 0.2768 0.2888 0.0388  0.0306  0.0000  169 TYR D CD1 
13536 C CD2 . TYR D 169 ? 0.3843 0.2906 0.2983 0.0325  0.0274  -0.0012 169 TYR D CD2 
13537 C CE1 . TYR D 169 ? 0.3688 0.2613 0.2824 0.0297  0.0231  -0.0023 169 TYR D CE1 
13538 C CE2 . TYR D 169 ? 0.3855 0.2811 0.2977 0.0241  0.0189  -0.0035 169 TYR D CE2 
13539 C CZ  . TYR D 169 ? 0.3835 0.2732 0.2966 0.0222  0.0171  -0.0041 169 TYR D CZ  
13540 O OH  . TYR D 169 ? 0.4166 0.2968 0.3298 0.0129  0.0092  -0.0063 169 TYR D OH  
13541 N N   . PHE D 170 ? 0.4383 0.3977 0.3782 0.0698  0.0603  0.0091  170 PHE D N   
13542 C CA  . PHE D 170 ? 0.4136 0.3974 0.3707 0.0742  0.0672  0.0121  170 PHE D CA  
13543 C C   . PHE D 170 ? 0.3908 0.3896 0.3623 0.0798  0.0675  0.0143  170 PHE D C   
13544 O O   . PHE D 170 ? 0.4052 0.4285 0.3974 0.0790  0.0690  0.0168  170 PHE D O   
13545 C CB  . PHE D 170 ? 0.3456 0.3238 0.2910 0.0829  0.0768  0.0124  170 PHE D CB  
13546 C CG  . PHE D 170 ? 0.3505 0.3243 0.2892 0.0767  0.0777  0.0117  170 PHE D CG  
13547 C CD1 . PHE D 170 ? 0.3832 0.3780 0.3402 0.0698  0.0782  0.0137  170 PHE D CD1 
13548 C CD2 . PHE D 170 ? 0.4435 0.3907 0.3566 0.0769  0.0769  0.0089  170 PHE D CD2 
13549 C CE1 . PHE D 170 ? 0.3444 0.3337 0.2941 0.0640  0.0785  0.0132  170 PHE D CE1 
13550 C CE2 . PHE D 170 ? 0.4475 0.3894 0.3531 0.0711  0.0766  0.0084  170 PHE D CE2 
13551 C CZ  . PHE D 170 ? 0.3808 0.3434 0.3044 0.0650  0.0776  0.0107  170 PHE D CZ  
13552 N N   . GLU D 171 ? 0.4721 0.4556 0.4322 0.0854  0.0657  0.0135  171 GLU D N   
13553 C CA  . GLU D 171 ? 0.4738 0.4689 0.4457 0.0900  0.0641  0.0155  171 GLU D CA  
13554 C C   . GLU D 171 ? 0.4288 0.4368 0.4163 0.0794  0.0572  0.0162  171 GLU D C   
13555 O O   . GLU D 171 ? 0.4019 0.4297 0.4063 0.0807  0.0563  0.0186  171 GLU D O   
13556 C CB  . GLU D 171 ? 0.5039 0.4756 0.4572 0.0966  0.0628  0.0143  171 GLU D CB  
13557 C CG  . GLU D 171 ? 0.6491 0.6071 0.5861 0.1097  0.0700  0.0139  171 GLU D CG  
13558 C CD  . GLU D 171 ? 0.7097 0.6426 0.6272 0.1154  0.0679  0.0127  171 GLU D CD  
13559 O OE1 . GLU D 171 ? 0.7107 0.6404 0.6302 0.1094  0.0613  0.0128  171 GLU D OE1 
13560 O OE2 . GLU D 171 ? 0.7463 0.6616 0.6456 0.1257  0.0731  0.0118  171 GLU D OE2 
13561 N N   . ILE D 172 ? 0.3283 0.3249 0.3101 0.0690  0.0520  0.0141  172 ILE D N   
13562 C CA  . ILE D 172 ? 0.2825 0.2891 0.2775 0.0591  0.0463  0.0145  172 ILE D CA  
13563 C C   . ILE D 172 ? 0.3413 0.3710 0.3543 0.0546  0.0476  0.0161  172 ILE D C   
13564 O O   . ILE D 172 ? 0.3150 0.3606 0.3428 0.0515  0.0452  0.0177  172 ILE D O   
13565 C CB  . ILE D 172 ? 0.3340 0.3233 0.3196 0.0498  0.0412  0.0118  172 ILE D CB  
13566 C CG1 . ILE D 172 ? 0.3855 0.3553 0.3579 0.0515  0.0389  0.0108  172 ILE D CG1 
13567 C CG2 . ILE D 172 ? 0.3360 0.3377 0.3364 0.0393  0.0371  0.0120  172 ILE D CG2 
13568 C CD1 . ILE D 172 ? 0.4051 0.3819 0.3863 0.0503  0.0366  0.0125  172 ILE D CD1 
13569 N N   . ILE D 173 ? 0.2786 0.3086 0.2888 0.0541  0.0512  0.0156  173 ILE D N   
13570 C CA  . ILE D 173 ? 0.3092 0.3591 0.3345 0.0499  0.0534  0.0173  173 ILE D CA  
13571 C C   . ILE D 173 ? 0.3254 0.3962 0.3657 0.0563  0.0573  0.0201  173 ILE D C   
13572 O O   . ILE D 173 ? 0.3618 0.4514 0.4189 0.0514  0.0558  0.0218  173 ILE D O   
13573 C CB  . ILE D 173 ? 0.3299 0.3727 0.3456 0.0493  0.0576  0.0165  173 ILE D CB  
13574 C CG1 . ILE D 173 ? 0.2700 0.2949 0.2738 0.0418  0.0516  0.0138  173 ILE D CG1 
13575 C CG2 . ILE D 173 ? 0.2674 0.3302 0.2977 0.0462  0.0616  0.0187  173 ILE D CG2 
13576 C CD1 . ILE D 173 ? 0.2962 0.3114 0.2877 0.0409  0.0542  0.0129  173 ILE D CD1 
13577 N N   . LYS D 174 ? 0.2606 0.3282 0.2953 0.0674  0.0619  0.0207  174 LYS D N   
13578 C CA  . LYS D 174 ? 0.2568 0.3456 0.3075 0.0747  0.0654  0.0235  174 LYS D CA  
13579 C C   . LYS D 174 ? 0.2827 0.3819 0.3450 0.0731  0.0585  0.0247  174 LYS D C   
13580 O O   . LYS D 174 ? 0.3044 0.4256 0.3846 0.0750  0.0586  0.0271  174 LYS D O   
13581 C CB  . LYS D 174 ? 0.2780 0.3587 0.3187 0.0883  0.0715  0.0237  174 LYS D CB  
13582 C CG  . LYS D 174 ? 0.3151 0.3936 0.3495 0.0925  0.0811  0.0236  174 LYS D CG  
13583 C CD  . LYS D 174 ? 0.4637 0.5359 0.4898 0.1076  0.0879  0.0241  174 LYS D CD  
13584 C CE  . LYS D 174 ? 0.5999 0.6647 0.6149 0.1122  0.0983  0.0236  174 LYS D CE  
13585 N NZ  . LYS D 174 ? 0.6769 0.7300 0.6791 0.1272  0.1052  0.0235  174 LYS D NZ  
13586 N N   . LYS D 175 ? 0.2781 0.3613 0.3301 0.0697  0.0525  0.0232  175 LYS D N   
13587 C CA  . LYS D 175 ? 0.3245 0.4133 0.3833 0.0687  0.0464  0.0243  175 LYS D CA  
13588 C C   . LYS D 175 ? 0.3516 0.4463 0.4183 0.0564  0.0416  0.0240  175 LYS D C   
13589 O O   . LYS D 175 ? 0.4087 0.5044 0.4779 0.0541  0.0365  0.0245  175 LYS D O   
13590 C CB  . LYS D 175 ? 0.3376 0.4042 0.3792 0.0734  0.0441  0.0233  175 LYS D CB  
13591 C CG  . LYS D 175 ? 0.4535 0.5129 0.4861 0.0867  0.0487  0.0237  175 LYS D CG  
13592 C CD  . LYS D 175 ? 0.5855 0.6208 0.5994 0.0912  0.0463  0.0228  175 LYS D CD  
13593 C CE  . LYS D 175 ? 0.6690 0.6945 0.6715 0.1051  0.0516  0.0230  175 LYS D CE  
13594 N NZ  . LYS D 175 ? 0.7176 0.7228 0.7039 0.1120  0.0492  0.0231  175 LYS D NZ  
13595 N N   . THR D 176 ? 0.3047 0.4025 0.3745 0.0489  0.0433  0.0232  176 THR D N   
13596 C CA  . THR D 176 ? 0.2953 0.3938 0.3691 0.0379  0.0390  0.0224  176 THR D CA  
13597 C C   . THR D 176 ? 0.3273 0.4456 0.4174 0.0342  0.0365  0.0243  176 THR D C   
13598 O O   . THR D 176 ? 0.2991 0.4164 0.3904 0.0297  0.0317  0.0242  176 THR D O   
13599 C CB  . THR D 176 ? 0.3064 0.3995 0.3764 0.0320  0.0409  0.0209  176 THR D CB  
13600 O OG1 . THR D 176 ? 0.3154 0.3878 0.3692 0.0338  0.0409  0.0188  176 THR D OG1 
13601 C CG2 . THR D 176 ? 0.2551 0.3512 0.3313 0.0215  0.0370  0.0204  176 THR D CG2 
13602 N N   . LEU D 177 ? 0.2593 0.3951 0.3613 0.0355  0.0398  0.0259  177 LEU D N   
13603 C CA  . LEU D 177 ? 0.2440 0.3982 0.3614 0.0308  0.0366  0.0275  177 LEU D CA  
13604 C C   . LEU D 177 ? 0.2079 0.3669 0.3287 0.0364  0.0317  0.0288  177 LEU D C   
13605 O O   . LEU D 177 ? 0.2208 0.3872 0.3482 0.0314  0.0263  0.0294  177 LEU D O   
13606 C CB  . LEU D 177 ? 0.2591 0.4316 0.3898 0.0304  0.0417  0.0292  177 LEU D CB  
13607 C CG  . LEU D 177 ? 0.2456 0.4128 0.3720 0.0238  0.0458  0.0283  177 LEU D CG  
13608 C CD1 . LEU D 177 ? 0.2598 0.4445 0.3987 0.0233  0.0519  0.0303  177 LEU D CD1 
13609 C CD2 . LEU D 177 ? 0.1967 0.3588 0.3218 0.0133  0.0409  0.0272  177 LEU D CD2 
13610 N N   . SER D 178 ? 0.1946 0.3477 0.3090 0.0469  0.0333  0.0292  178 SER D N   
13611 C CA  . SER D 178 ? 0.1992 0.3541 0.3142 0.0535  0.0283  0.0305  178 SER D CA  
13612 C C   . SER D 178 ? 0.2543 0.3927 0.3574 0.0488  0.0230  0.0294  178 SER D C   
13613 O O   . SER D 178 ? 0.2712 0.4134 0.3766 0.0489  0.0171  0.0305  178 SER D O   
13614 C CB  . SER D 178 ? 0.3566 0.5055 0.4649 0.0665  0.0318  0.0310  178 SER D CB  
13615 O OG  . SER D 178 ? 0.4102 0.5800 0.5341 0.0728  0.0356  0.0329  178 SER D OG  
13616 N N   . ILE D 179 ? 0.2028 0.3227 0.2930 0.0445  0.0249  0.0273  179 ILE D N   
13617 C CA  . ILE D 179 ? 0.2234 0.3283 0.3032 0.0407  0.0210  0.0265  179 ILE D CA  
13618 C C   . ILE D 179 ? 0.2831 0.3954 0.3701 0.0309  0.0176  0.0265  179 ILE D C   
13619 O O   . ILE D 179 ? 0.2656 0.3721 0.3478 0.0292  0.0136  0.0268  179 ILE D O   
13620 C CB  . ILE D 179 ? 0.2698 0.3531 0.3349 0.0388  0.0235  0.0244  179 ILE D CB  
13621 C CG1 . ILE D 179 ? 0.4018 0.4700 0.4566 0.0362  0.0205  0.0242  179 ILE D CG1 
13622 C CG2 . ILE D 179 ? 0.3198 0.4033 0.3880 0.0302  0.0254  0.0226  179 ILE D CG2 
13623 C CD1 . ILE D 179 ? 0.4891 0.5354 0.5281 0.0385  0.0224  0.0229  179 ILE D CD1 
13624 N N   . TYR D 180 ? 0.2070 0.3306 0.3040 0.0248  0.0194  0.0261  180 TYR D N   
13625 C CA  . TYR D 180 ? 0.1890 0.3196 0.2925 0.0161  0.0162  0.0262  180 TYR D CA  
13626 C C   . TYR D 180 ? 0.2222 0.3670 0.3343 0.0181  0.0111  0.0281  180 TYR D C   
13627 O O   . TYR D 180 ? 0.2298 0.3720 0.3394 0.0137  0.0065  0.0281  180 TYR D O   
13628 C CB  . TYR D 180 ? 0.1736 0.3117 0.2845 0.0096  0.0192  0.0256  180 TYR D CB  
13629 C CG  . TYR D 180 ? 0.2264 0.3502 0.3291 0.0057  0.0218  0.0235  180 TYR D CG  
13630 C CD1 . TYR D 180 ? 0.2097 0.3249 0.3088 -0.0011 0.0202  0.0223  180 TYR D CD1 
13631 C CD2 . TYR D 180 ? 0.2487 0.3671 0.3470 0.0092  0.0258  0.0228  180 TYR D CD2 
13632 C CE1 . TYR D 180 ? 0.2454 0.3495 0.3395 -0.0043 0.0220  0.0206  180 TYR D CE1 
13633 C CE2 . TYR D 180 ? 0.2222 0.3279 0.3134 0.0055  0.0267  0.0209  180 TYR D CE2 
13634 C CZ  . TYR D 180 ? 0.2177 0.3174 0.3082 -0.0012 0.0246  0.0199  180 TYR D CZ  
13635 O OH  . TYR D 180 ? 0.1664 0.2554 0.2523 -0.0044 0.0249  0.0180  180 TYR D OH  
13636 N N   . ARG D 181 ? 0.2197 0.3798 0.3422 0.0246  0.0119  0.0297  181 ARG D N   
13637 C CA  . ARG D 181 ? 0.2020 0.3766 0.3340 0.0273  0.0058  0.0316  181 ARG D CA  
13638 C C   . ARG D 181 ? 0.2794 0.4407 0.3989 0.0323  0.0006  0.0320  181 ARG D C   
13639 O O   . ARG D 181 ? 0.2565 0.4206 0.3766 0.0300  -0.0063 0.0327  181 ARG D O   
13640 C CB  . ARG D 181 ? 0.2103 0.4030 0.3560 0.0356  0.0083  0.0335  181 ARG D CB  
13641 C CG  . ARG D 181 ? 0.2844 0.4948 0.4456 0.0308  0.0131  0.0340  181 ARG D CG  
13642 C CD  . ARG D 181 ? 0.2700 0.5004 0.4467 0.0400  0.0155  0.0362  181 ARG D CD  
13643 N NE  . ARG D 181 ? 0.3562 0.6023 0.5467 0.0360  0.0221  0.0369  181 ARG D NE  
13644 C CZ  . ARG D 181 ? 0.4341 0.6764 0.6211 0.0395  0.0313  0.0365  181 ARG D CZ  
13645 N NH1 . ARG D 181 ? 0.4395 0.6626 0.6098 0.0467  0.0344  0.0353  181 ARG D NH1 
13646 N NH2 . ARG D 181 ? 0.4704 0.7265 0.6692 0.0353  0.0376  0.0375  181 ARG D NH2 
13647 N N   . GLU D 182 ? 0.2916 0.4371 0.3984 0.0391  0.0036  0.0315  182 GLU D N   
13648 C CA  . GLU D 182 ? 0.3095 0.4403 0.4026 0.0446  -0.0005 0.0322  182 GLU D CA  
13649 C C   . GLU D 182 ? 0.2902 0.4073 0.3725 0.0363  -0.0032 0.0312  182 GLU D C   
13650 O O   . GLU D 182 ? 0.2611 0.3759 0.3386 0.0372  -0.0095 0.0323  182 GLU D O   
13651 C CB  . GLU D 182 ? 0.3592 0.4732 0.4393 0.0522  0.0042  0.0317  182 GLU D CB  
13652 C CG  . GLU D 182 ? 0.4627 0.5867 0.5493 0.0641  0.0059  0.0331  182 GLU D CG  
13653 C CD  . GLU D 182 ? 0.5964 0.7045 0.6710 0.0696  0.0123  0.0319  182 GLU D CD  
13654 O OE1 . GLU D 182 ? 0.6053 0.7210 0.6849 0.0789  0.0157  0.0327  182 GLU D OE1 
13655 O OE2 . GLU D 182 ? 0.6382 0.7261 0.6985 0.0647  0.0141  0.0302  182 GLU D OE2 
13656 N N   . ILE D 183 ? 0.2556 0.3630 0.3335 0.0285  0.0014  0.0293  183 ILE D N   
13657 C CA  . ILE D 183 ? 0.3183 0.4121 0.3861 0.0215  0.0004  0.0284  183 ILE D CA  
13658 C C   . ILE D 183 ? 0.3225 0.4271 0.3973 0.0150  -0.0042 0.0286  183 ILE D C   
13659 O O   . ILE D 183 ? 0.3719 0.4662 0.4368 0.0117  -0.0070 0.0285  183 ILE D O   
13660 C CB  . ILE D 183 ? 0.3388 0.4206 0.4020 0.0154  0.0064  0.0263  183 ILE D CB  
13661 C CG1 . ILE D 183 ? 0.3447 0.4390 0.4205 0.0096  0.0088  0.0252  183 ILE D CG1 
13662 C CG2 . ILE D 183 ? 0.3020 0.3712 0.3566 0.0210  0.0100  0.0259  183 ILE D CG2 
13663 C CD1 . ILE D 183 ? 0.3367 0.4285 0.4128 0.0006  0.0091  0.0241  183 ILE D CD1 
13664 N N   . LYS D 184 ? 0.2416 0.3658 0.3322 0.0132  -0.0050 0.0290  184 LYS D N   
13665 C CA  . LYS D 184 ? 0.2426 0.3769 0.3397 0.0069  -0.0102 0.0293  184 LYS D CA  
13666 C C   . LYS D 184 ? 0.2946 0.4327 0.3902 0.0118  -0.0186 0.0310  184 LYS D C   
13667 O O   . LYS D 184 ? 0.2415 0.3726 0.3289 0.0078  -0.0238 0.0308  184 LYS D O   
13668 C CB  . LYS D 184 ? 0.2866 0.4404 0.4010 0.0034  -0.0084 0.0294  184 LYS D CB  
13669 C CG  . LYS D 184 ? 0.3410 0.5047 0.4623 -0.0045 -0.0137 0.0296  184 LYS D CG  
13670 C CD  . LYS D 184 ? 0.3707 0.5544 0.5096 -0.0074 -0.0116 0.0303  184 LYS D CD  
13671 C CE  . LYS D 184 ? 0.4079 0.6035 0.5553 -0.0147 -0.0183 0.0308  184 LYS D CE  
13672 N NZ  . LYS D 184 ? 0.4496 0.6319 0.5866 -0.0240 -0.0190 0.0291  184 LYS D NZ  
13673 N N   . GLU D 185 ? 0.3373 0.4859 0.4403 0.0211  -0.0201 0.0326  185 GLU D N   
13674 C CA  . GLU D 185 ? 0.3365 0.4913 0.4406 0.0270  -0.0290 0.0345  185 GLU D CA  
13675 C C   . GLU D 185 ? 0.3559 0.4874 0.4380 0.0304  -0.0320 0.0347  185 GLU D C   
13676 O O   . GLU D 185 ? 0.3524 0.4822 0.4289 0.0310  -0.0407 0.0357  185 GLU D O   
13677 C CB  . GLU D 185 ? 0.3736 0.5447 0.4911 0.0375  -0.0286 0.0363  185 GLU D CB  
13678 C CG  . GLU D 185 ? 0.4574 0.6523 0.5971 0.0345  -0.0249 0.0365  185 GLU D CG  
13679 C CD  . GLU D 185 ? 0.5417 0.7553 0.6961 0.0274  -0.0322 0.0372  185 GLU D CD  
13680 O OE1 . GLU D 185 ? 0.5642 0.7928 0.7293 0.0330  -0.0396 0.0391  185 GLU D OE1 
13681 O OE2 . GLU D 185 ? 0.5732 0.7862 0.7282 0.0163  -0.0311 0.0359  185 GLU D OE2 
13682 N N   . GLU D 186 ? 0.2924 0.4052 0.3610 0.0325  -0.0253 0.0339  186 GLU D N   
13683 C CA  . GLU D 186 ? 0.3686 0.4573 0.4152 0.0346  -0.0264 0.0342  186 GLU D CA  
13684 C C   . GLU D 186 ? 0.3912 0.4663 0.4268 0.0247  -0.0251 0.0327  186 GLU D C   
13685 O O   . GLU D 186 ? 0.4643 0.5180 0.4809 0.0251  -0.0241 0.0328  186 GLU D O   
13686 C CB  . GLU D 186 ? 0.3938 0.4670 0.4304 0.0400  -0.0194 0.0339  186 GLU D CB  
13687 C CG  . GLU D 186 ? 0.4891 0.5707 0.5318 0.0516  -0.0202 0.0354  186 GLU D CG  
13688 C CD  . GLU D 186 ? 0.5677 0.6375 0.6043 0.0545  -0.0121 0.0343  186 GLU D CD  
13689 O OE1 . GLU D 186 ? 0.5929 0.6468 0.6197 0.0477  -0.0070 0.0327  186 GLU D OE1 
13690 O OE2 . GLU D 186 ? 0.5654 0.6422 0.6076 0.0634  -0.0108 0.0351  186 GLU D OE2 
13691 N N   . GLY D 187 ? 0.3581 0.4441 0.4045 0.0160  -0.0244 0.0314  187 GLY D N   
13692 C CA  . GLY D 187 ? 0.3250 0.3985 0.3616 0.0073  -0.0224 0.0299  187 GLY D CA  
13693 C C   . GLY D 187 ? 0.3559 0.4104 0.3809 0.0053  -0.0137 0.0288  187 GLY D C   
13694 O O   . GLY D 187 ? 0.3490 0.3879 0.3607 0.0009  -0.0119 0.0281  187 GLY D O   
13695 N N   . LYS D 188 ? 0.2624 0.3173 0.2920 0.0084  -0.0082 0.0285  188 LYS D N   
13696 C CA  . LYS D 188 ? 0.2803 0.3201 0.3028 0.0047  -0.0003 0.0271  188 LYS D CA  
13697 C C   . LYS D 188 ? 0.3239 0.3703 0.3568 -0.0033 0.0039  0.0252  188 LYS D C   
13698 O O   . LYS D 188 ? 0.2834 0.3193 0.3127 -0.0073 0.0099  0.0240  188 LYS D O   
13699 C CB  . LYS D 188 ? 0.3224 0.3576 0.3439 0.0102  0.0032  0.0272  188 LYS D CB  
13700 C CG  . LYS D 188 ? 0.3255 0.3532 0.3363 0.0195  -0.0007 0.0292  188 LYS D CG  
13701 C CD  . LYS D 188 ? 0.4265 0.4406 0.4292 0.0237  0.0039  0.0290  188 LYS D CD  
13702 C CE  . LYS D 188 ? 0.4593 0.4596 0.4461 0.0323  0.0005  0.0311  188 LYS D CE  
13703 N NZ  . LYS D 188 ? 0.5512 0.5335 0.5208 0.0290  0.0000  0.0318  188 LYS D NZ  
13704 N N   . GLY D 189 ? 0.3433 0.4068 0.3892 -0.0055 0.0009  0.0251  189 GLY D N   
13705 C CA  . GLY D 189 ? 0.3022 0.3718 0.3573 -0.0121 0.0044  0.0236  189 GLY D CA  
13706 C C   . GLY D 189 ? 0.3108 0.3974 0.3775 -0.0146 0.0001  0.0239  189 GLY D C   
13707 O O   . GLY D 189 ? 0.3131 0.4116 0.3860 -0.0103 -0.0044 0.0253  189 GLY D O   
13708 N N   . SER D 190 ? 0.2633 0.3511 0.3331 -0.0216 0.0016  0.0228  190 SER D N   
13709 C CA  . SER D 190 ? 0.2212 0.3241 0.3020 -0.0253 -0.0013 0.0230  190 SER D CA  
13710 C C   . SER D 190 ? 0.1687 0.2793 0.2598 -0.0258 0.0034  0.0226  190 SER D C   
13711 O O   . SER D 190 ? 0.2572 0.3595 0.3458 -0.0257 0.0081  0.0215  190 SER D O   
13712 C CB  . SER D 190 ? 0.2342 0.3314 0.3098 -0.0324 -0.0029 0.0221  190 SER D CB  
13713 O OG  . SER D 190 ? 0.3072 0.3971 0.3718 -0.0318 -0.0083 0.0226  190 SER D OG  
13714 N N   . VAL D 191 ? 0.2317 0.3581 0.3343 -0.0260 0.0019  0.0235  191 VAL D N   
13715 C CA  . VAL D 191 ? 0.1986 0.3314 0.3090 -0.0267 0.0064  0.0233  191 VAL D CA  
13716 C C   . VAL D 191 ? 0.1869 0.3266 0.3030 -0.0341 0.0056  0.0233  191 VAL D C   
13717 O O   . VAL D 191 ? 0.2631 0.4137 0.3853 -0.0364 0.0015  0.0244  191 VAL D O   
13718 C CB  . VAL D 191 ? 0.1836 0.3276 0.3014 -0.0200 0.0075  0.0247  191 VAL D CB  
13719 C CG1 . VAL D 191 ? 0.2173 0.3653 0.3401 -0.0212 0.0125  0.0244  191 VAL D CG1 
13720 C CG2 . VAL D 191 ? 0.2005 0.3352 0.3105 -0.0123 0.0083  0.0246  191 VAL D CG2 
13721 N N   . SER D 192 ? 0.1876 0.3203 0.3015 -0.0382 0.0091  0.0222  192 SER D N   
13722 C CA  . SER D 192 ? 0.1496 0.2863 0.2671 -0.0450 0.0092  0.0222  192 SER D CA  
13723 C C   . SER D 192 ? 0.2150 0.3588 0.3390 -0.0444 0.0132  0.0229  192 SER D C   
13724 O O   . SER D 192 ? 0.1853 0.3297 0.3099 -0.0386 0.0158  0.0231  192 SER D O   
13725 C CB  . SER D 192 ? 0.1771 0.3001 0.2867 -0.0493 0.0104  0.0206  192 SER D CB  
13726 O OG  . SER D 192 ? 0.1713 0.2865 0.2786 -0.0465 0.0143  0.0197  192 SER D OG  
13727 N N   . THR D 193 ? 0.1585 0.3057 0.2854 -0.0505 0.0140  0.0233  193 THR D N   
13728 C CA  . THR D 193 ? 0.1911 0.3399 0.3200 -0.0508 0.0185  0.0238  193 THR D CA  
13729 C C   . THR D 193 ? 0.2410 0.3806 0.3647 -0.0569 0.0193  0.0232  193 THR D C   
13730 O O   . THR D 193 ? 0.1868 0.3187 0.3055 -0.0604 0.0169  0.0222  193 THR D O   
13731 C CB  . THR D 193 ? 0.2158 0.3808 0.3551 -0.0509 0.0202  0.0258  193 THR D CB  
13732 O OG1 . THR D 193 ? 0.2586 0.4222 0.3967 -0.0495 0.0257  0.0263  193 THR D OG1 
13733 C CG2 . THR D 193 ? 0.2045 0.3772 0.3494 -0.0591 0.0178  0.0267  193 THR D CG2 
13734 N N   . SER D 194 ? 0.2121 0.3504 0.3350 -0.0576 0.0229  0.0238  194 SER D N   
13735 C CA  . SER D 194 ? 0.2149 0.3440 0.3321 -0.0626 0.0240  0.0236  194 SER D CA  
13736 C C   . SER D 194 ? 0.2117 0.3480 0.3324 -0.0676 0.0268  0.0254  194 SER D C   
13737 O O   . SER D 194 ? 0.1895 0.3380 0.3176 -0.0657 0.0292  0.0268  194 SER D O   
13738 C CB  . SER D 194 ? 0.1995 0.3174 0.3101 -0.0586 0.0255  0.0226  194 SER D CB  
13739 O OG  . SER D 194 ? 0.2020 0.3144 0.3112 -0.0547 0.0237  0.0210  194 SER D OG  
13740 N N   . PRO D 195 ? 0.2394 0.3680 0.3548 -0.0738 0.0272  0.0256  195 PRO D N   
13741 C CA  . PRO D 195 ? 0.2919 0.4235 0.4080 -0.0784 0.0314  0.0276  195 PRO D CA  
13742 C C   . PRO D 195 ? 0.1976 0.3299 0.3124 -0.0725 0.0360  0.0283  195 PRO D C   
13743 O O   . PRO D 195 ? 0.1632 0.2863 0.2716 -0.0666 0.0353  0.0271  195 PRO D O   
13744 C CB  . PRO D 195 ? 0.3457 0.4614 0.4509 -0.0832 0.0310  0.0272  195 PRO D CB  
13745 C CG  . PRO D 195 ? 0.3235 0.4334 0.4263 -0.0837 0.0263  0.0252  195 PRO D CG  
13746 C CD  . PRO D 195 ? 0.2852 0.4003 0.3925 -0.0765 0.0246  0.0242  195 PRO D CD  
13747 N N   . TYR D 196 ? 0.1650 0.3076 0.2855 -0.0745 0.0408  0.0304  196 TYR D N   
13748 C CA  . TYR D 196 ? 0.1863 0.3352 0.3092 -0.0680 0.0455  0.0312  196 TYR D CA  
13749 C C   . TYR D 196 ? 0.2459 0.3797 0.3558 -0.0619 0.0465  0.0302  196 TYR D C   
13750 O O   . TYR D 196 ? 0.1793 0.3136 0.2889 -0.0546 0.0461  0.0293  196 TYR D O   
13751 C CB  . TYR D 196 ? 0.1742 0.3333 0.3031 -0.0724 0.0523  0.0338  196 TYR D CB  
13752 C CG  . TYR D 196 ? 0.2345 0.4073 0.3721 -0.0658 0.0570  0.0349  196 TYR D CG  
13753 C CD1 . TYR D 196 ? 0.2373 0.4018 0.3653 -0.0584 0.0615  0.0347  196 TYR D CD1 
13754 C CD2 . TYR D 196 ? 0.2550 0.4482 0.4097 -0.0664 0.0565  0.0359  196 TYR D CD2 
13755 C CE1 . TYR D 196 ? 0.2776 0.4529 0.4120 -0.0515 0.0663  0.0355  196 TYR D CE1 
13756 C CE2 . TYR D 196 ? 0.2468 0.4527 0.4100 -0.0591 0.0610  0.0369  196 TYR D CE2 
13757 C CZ  . TYR D 196 ? 0.2689 0.4652 0.4213 -0.0515 0.0664  0.0366  196 TYR D CZ  
13758 O OH  . TYR D 196 ? 0.1965 0.4037 0.3559 -0.0437 0.0716  0.0376  196 TYR D OH  
13759 N N   . TYR D 197 ? 0.2121 0.3318 0.3105 -0.0646 0.0475  0.0305  197 TYR D N   
13760 C CA  . TYR D 197 ? 0.1830 0.2887 0.2689 -0.0591 0.0476  0.0298  197 TYR D CA  
13761 C C   . TYR D 197 ? 0.2723 0.3656 0.3525 -0.0577 0.0412  0.0278  197 TYR D C   
13762 O O   . TYR D 197 ? 0.2462 0.3263 0.3155 -0.0550 0.0400  0.0273  197 TYR D O   
13763 C CB  . TYR D 197 ? 0.1969 0.2941 0.2721 -0.0613 0.0533  0.0317  197 TYR D CB  
13764 C CG  . TYR D 197 ? 0.2267 0.3361 0.3078 -0.0607 0.0608  0.0336  197 TYR D CG  
13765 C CD1 . TYR D 197 ? 0.2129 0.3239 0.2926 -0.0529 0.0630  0.0331  197 TYR D CD1 
13766 C CD2 . TYR D 197 ? 0.2685 0.3889 0.3582 -0.0678 0.0657  0.0358  197 TYR D CD2 
13767 C CE1 . TYR D 197 ? 0.2064 0.3290 0.2923 -0.0511 0.0706  0.0347  197 TYR D CE1 
13768 C CE2 . TYR D 197 ? 0.2696 0.4038 0.3678 -0.0668 0.0732  0.0376  197 TYR D CE2 
13769 C CZ  . TYR D 197 ? 0.2037 0.3389 0.2998 -0.0579 0.0758  0.0371  197 TYR D CZ  
13770 O OH  . TYR D 197 ? 0.2421 0.3909 0.3468 -0.0556 0.0839  0.0388  197 TYR D OH  
13771 N N   . HIS D 198 ? 0.1727 0.2701 0.2600 -0.0593 0.0372  0.0265  198 HIS D N   
13772 C CA  . HIS D 198 ? 0.2377 0.3256 0.3222 -0.0577 0.0323  0.0247  198 HIS D CA  
13773 C C   . HIS D 198 ? 0.2601 0.3347 0.3351 -0.0604 0.0318  0.0251  198 HIS D C   
13774 O O   . HIS D 198 ? 0.3136 0.3779 0.3826 -0.0566 0.0290  0.0243  198 HIS D O   
13775 C CB  . HIS D 198 ? 0.1780 0.2627 0.2612 -0.0509 0.0302  0.0232  198 HIS D CB  
13776 C CG  . HIS D 198 ? 0.2193 0.3007 0.3056 -0.0489 0.0259  0.0212  198 HIS D CG  
13777 N ND1 . HIS D 198 ? 0.2042 0.2753 0.2864 -0.0472 0.0227  0.0202  198 HIS D ND1 
13778 C CD2 . HIS D 198 ? 0.1697 0.2565 0.2629 -0.0481 0.0247  0.0201  198 HIS D CD2 
13779 C CE1 . HIS D 198 ? 0.2085 0.2803 0.2967 -0.0458 0.0204  0.0186  198 HIS D CE1 
13780 N NE2 . HIS D 198 ? 0.1661 0.2463 0.2599 -0.0465 0.0219  0.0185  198 HIS D NE2 
13781 N N   . PRO D 199 ? 0.2844 0.3583 0.3575 -0.0670 0.0339  0.0265  199 PRO D N   
13782 C CA  . PRO D 199 ? 0.3276 0.3866 0.3901 -0.0693 0.0333  0.0270  199 PRO D CA  
13783 C C   . PRO D 199 ? 0.3822 0.4353 0.4451 -0.0693 0.0295  0.0253  199 PRO D C   
13784 O O   . PRO D 199 ? 0.3611 0.4212 0.4318 -0.0688 0.0278  0.0240  199 PRO D O   
13785 C CB  . PRO D 199 ? 0.2694 0.3304 0.3303 -0.0773 0.0376  0.0291  199 PRO D CB  
13786 C CG  . PRO D 199 ? 0.2157 0.2934 0.2900 -0.0802 0.0374  0.0288  199 PRO D CG  
13787 C CD  . PRO D 199 ? 0.2349 0.3213 0.3160 -0.0728 0.0365  0.0277  199 PRO D CD  
13788 N N   . LEU D 200 ? 0.3692 0.4077 0.4220 -0.0698 0.0286  0.0257  200 LEU D N   
13789 C CA  . LEU D 200 ? 0.3413 0.3718 0.3925 -0.0698 0.0263  0.0244  200 LEU D CA  
13790 C C   . LEU D 200 ? 0.3752 0.4027 0.4222 -0.0782 0.0282  0.0252  200 LEU D C   
13791 O O   . LEU D 200 ? 0.3434 0.3582 0.3795 -0.0813 0.0293  0.0264  200 LEU D O   
13792 C CB  . LEU D 200 ? 0.3491 0.3651 0.3919 -0.0648 0.0238  0.0243  200 LEU D CB  
13793 C CG  . LEU D 200 ? 0.3060 0.3244 0.3546 -0.0570 0.0202  0.0229  200 LEU D CG  
13794 C CD1 . LEU D 200 ? 0.3135 0.3186 0.3543 -0.0522 0.0168  0.0232  200 LEU D CD1 
13795 C CD2 . LEU D 200 ? 0.3014 0.3270 0.3609 -0.0552 0.0194  0.0209  200 LEU D CD2 
13796 N N   . ILE D 201 ? 0.2791 0.2883 0.2582 -0.0310 0.0323  0.0131  201 ILE D N   
13797 C CA  . ILE D 201 ? 0.2652 0.2685 0.2464 -0.0379 0.0296  0.0129  201 ILE D CA  
13798 C C   . ILE D 201 ? 0.3362 0.3212 0.3057 -0.0363 0.0254  0.0094  201 ILE D C   
13799 O O   . ILE D 201 ? 0.3159 0.2887 0.2850 -0.0425 0.0241  0.0113  201 ILE D O   
13800 C CB  . ILE D 201 ? 0.2689 0.2839 0.2581 -0.0405 0.0263  0.0108  201 ILE D CB  
13801 C CG1 . ILE D 201 ? 0.2923 0.3229 0.2937 -0.0422 0.0301  0.0147  201 ILE D CG1 
13802 C CG2 . ILE D 201 ? 0.3052 0.3125 0.2964 -0.0471 0.0196  0.0085  201 ILE D CG2 
13803 C CD1 . ILE D 201 ? 0.3585 0.3921 0.3713 -0.0491 0.0334  0.0196  201 ILE D CD1 
13804 N N   . PRO D 202 ? 0.3384 0.3207 0.2992 -0.0283 0.0232  0.0047  202 PRO D N   
13805 C CA  . PRO D 202 ? 0.3707 0.3335 0.3186 -0.0251 0.0190  0.0009  202 PRO D CA  
13806 C C   . PRO D 202 ? 0.3775 0.3240 0.3187 -0.0253 0.0199  0.0043  202 PRO D C   
13807 O O   . PRO D 202 ? 0.3318 0.2582 0.2646 -0.0274 0.0159  0.0031  202 PRO D O   
13808 C CB  . PRO D 202 ? 0.3474 0.3154 0.2897 -0.0139 0.0197  -0.0033 202 PRO D CB  
13809 C CG  . PRO D 202 ? 0.3318 0.3204 0.2843 -0.0147 0.0228  -0.0019 202 PRO D CG  
13810 C CD  . PRO D 202 ? 0.2271 0.2234 0.1904 -0.0217 0.0252  0.0033  202 PRO D CD  
13811 N N   . ILE D 203 ? 0.2658 0.2173 0.2081 -0.0228 0.0243  0.0086  203 ILE D N   
13812 C CA  . ILE D 203 ? 0.3544 0.2879 0.2857 -0.0214 0.0253  0.0125  203 ILE D CA  
13813 C C   . ILE D 203 ? 0.4112 0.3381 0.3465 -0.0324 0.0290  0.0191  203 ILE D C   
13814 O O   . ILE D 203 ? 0.4658 0.3721 0.3932 -0.0354 0.0281  0.0218  203 ILE D O   
13815 C CB  . ILE D 203 ? 0.4244 0.3631 0.3523 -0.0138 0.0271  0.0142  203 ILE D CB  
13816 C CG1 . ILE D 203 ? 0.4596 0.4047 0.3878 -0.0036 0.0229  0.0085  203 ILE D CG1 
13817 C CG2 . ILE D 203 ? 0.4283 0.3465 0.3409 -0.0118 0.0286  0.0196  203 ILE D CG2 
13818 C CD1 . ILE D 203 ? 0.5013 0.4507 0.4284 0.0037  0.0212  0.0090  203 ILE D CD1 
13819 N N   . LEU D 204 ? 0.4088 0.3532 0.3579 -0.0383 0.0334  0.0222  204 LEU D N   
13820 C CA  . LEU D 204 ? 0.3884 0.3318 0.3471 -0.0489 0.0383  0.0293  204 LEU D CA  
13821 C C   . LEU D 204 ? 0.3502 0.2828 0.3147 -0.0579 0.0318  0.0274  204 LEU D C   
13822 O O   . LEU D 204 ? 0.3694 0.2904 0.3378 -0.0665 0.0342  0.0337  204 LEU D O   
13823 C CB  . LEU D 204 ? 0.3415 0.3084 0.3162 -0.0517 0.0431  0.0315  204 LEU D CB  
13824 C CG  . LEU D 204 ? 0.3332 0.3081 0.3014 -0.0431 0.0483  0.0328  204 LEU D CG  
13825 C CD1 . LEU D 204 ? 0.3050 0.2994 0.2880 -0.0458 0.0535  0.0356  204 LEU D CD1 
13826 C CD2 . LEU D 204 ? 0.3134 0.2720 0.2651 -0.0389 0.0539  0.0387  204 LEU D CD2 
13827 N N   . LEU D 205 ? 0.3515 0.2867 0.3162 -0.0561 0.0233  0.0189  205 LEU D N   
13828 C CA  . LEU D 205 ? 0.3434 0.2648 0.3099 -0.0632 0.0143  0.0150  205 LEU D CA  
13829 C C   . LEU D 205 ? 0.3903 0.2827 0.3386 -0.0597 0.0102  0.0131  205 LEU D C   
13830 O O   . LEU D 205 ? 0.4251 0.2989 0.3749 -0.0684 0.0047  0.0137  205 LEU D O   
13831 C CB  . LEU D 205 ? 0.3710 0.3011 0.3370 -0.0596 0.0064  0.0062  205 LEU D CB  
13832 C CG  . LEU D 205 ? 0.2841 0.2376 0.2680 -0.0645 0.0061  0.0069  205 LEU D CG  
13833 C CD1 . LEU D 205 ? 0.2842 0.2398 0.2592 -0.0581 -0.0018 -0.0017 205 LEU D CD1 
13834 C CD2 . LEU D 205 ? 0.3258 0.2796 0.3295 -0.0786 0.0029  0.0110  205 LEU D CD2 
13835 N N   . ASN D 206 ? 0.4021 0.2899 0.3344 -0.0470 0.0117  0.0104  206 ASN D N   
13836 C CA  . ASN D 206 ? 0.4332 0.2940 0.3470 -0.0405 0.0067  0.0071  206 ASN D CA  
13837 C C   . ASN D 206 ? 0.4245 0.2875 0.3272 -0.0267 0.0104  0.0071  206 ASN D C   
13838 O O   . ASN D 206 ? 0.3962 0.2692 0.2961 -0.0165 0.0089  0.0007  206 ASN D O   
13839 C CB  . ASN D 206 ? 0.4336 0.2844 0.3392 -0.0365 -0.0030 -0.0032 206 ASN D CB  
13840 C CG  . ASN D 206 ? 0.5893 0.4070 0.4760 -0.0316 -0.0093 -0.0066 206 ASN D CG  
13841 O OD1 . ASN D 206 ? 0.5884 0.3929 0.4659 -0.0271 -0.0062 -0.0019 206 ASN D OD1 
13842 N ND2 . ASN D 206 ? 0.6606 0.4625 0.5389 -0.0311 -0.0193 -0.0151 206 ASN D ND2 
13843 N N   . PRO D 207 ? 0.4422 0.2964 0.3387 -0.0258 0.0151  0.0143  207 PRO D N   
13844 C CA  . PRO D 207 ? 0.4502 0.3073 0.3373 -0.0124 0.0160  0.0136  207 PRO D CA  
13845 C C   . PRO D 207 ? 0.4392 0.2838 0.3141 0.0002  0.0095  0.0064  207 PRO D C   
13846 O O   . PRO D 207 ? 0.5049 0.3604 0.3796 0.0118  0.0089  0.0037  207 PRO D O   
13847 C CB  . PRO D 207 ? 0.4950 0.3372 0.3721 -0.0139 0.0207  0.0230  207 PRO D CB  
13848 C CG  . PRO D 207 ? 0.4665 0.3115 0.3557 -0.0289 0.0266  0.0300  207 PRO D CG  
13849 C CD  . PRO D 207 ? 0.4657 0.3086 0.3642 -0.0366 0.0202  0.0242  207 PRO D CD  
13850 N N   . ASN D 208 ? 0.4292 0.2518 0.2955 -0.0013 0.0043  0.0029  208 ASN D N   
13851 C CA  . ASN D 208 ? 0.4893 0.2991 0.3424 0.0128  -0.0012 -0.0045 208 ASN D CA  
13852 C C   . ASN D 208 ? 0.4627 0.2952 0.3228 0.0210  -0.0007 -0.0121 208 ASN D C   
13853 O O   . ASN D 208 ? 0.4734 0.3038 0.3262 0.0355  -0.0023 -0.0172 208 ASN D O   
13854 C CB  . ASN D 208 ? 0.5930 0.3689 0.4324 0.0093  -0.0080 -0.0069 208 ASN D CB  
13855 C CG  . ASN D 208 ? 0.7003 0.4477 0.5273 0.0072  -0.0083 0.0010  208 ASN D CG  
13856 O OD1 . ASN D 208 ? 0.7210 0.4745 0.5496 0.0056  -0.0024 0.0093  208 ASN D OD1 
13857 N ND2 . ASN D 208 ? 0.8125 0.5258 0.6244 0.0079  -0.0154 -0.0016 208 ASN D ND2 
13858 N N   . CYS D 209 ? 0.4659 0.3210 0.3401 0.0131  0.0025  -0.0119 209 CYS D N   
13859 C CA  . CYS D 209 ? 0.4751 0.3507 0.3543 0.0210  0.0047  -0.0172 209 CYS D CA  
13860 C C   . CYS D 209 ? 0.4643 0.3593 0.3517 0.0320  0.0087  -0.0164 209 CYS D C   
13861 O O   . CYS D 209 ? 0.3902 0.3001 0.2816 0.0409  0.0117  -0.0199 209 CYS D O   
13862 C CB  . CYS D 209 ? 0.4922 0.3867 0.3841 0.0105  0.0070  -0.0159 209 CYS D CB  
13863 S SG  . CYS D 209 ? 0.5454 0.4648 0.4559 0.0037  0.0133  -0.0082 209 CYS D SG  
13864 N N   . VAL D 210 ? 0.4373 0.3320 0.3273 0.0322  0.0084  -0.0116 210 VAL D N   
13865 C CA  . VAL D 210 ? 0.4423 0.3534 0.3413 0.0430  0.0088  -0.0118 210 VAL D CA  
13866 C C   . VAL D 210 ? 0.4113 0.3137 0.3022 0.0585  0.0062  -0.0168 210 VAL D C   
13867 O O   . VAL D 210 ? 0.4468 0.3692 0.3507 0.0686  0.0077  -0.0183 210 VAL D O   
13868 C CB  . VAL D 210 ? 0.4960 0.4040 0.3945 0.0413  0.0066  -0.0067 210 VAL D CB  
13869 C CG1 . VAL D 210 ? 0.5313 0.4444 0.4343 0.0278  0.0102  -0.0017 210 VAL D CG1 
13870 C CG2 . VAL D 210 ? 0.5532 0.4314 0.4318 0.0461  0.0021  -0.0053 210 VAL D CG2 
13871 N N   . TYR D 211 ? 0.4085 0.2818 0.2799 0.0610  0.0023  -0.0195 211 TYR D N   
13872 C CA  . TYR D 211 ? 0.5044 0.3675 0.3662 0.0780  -0.0002 -0.0249 211 TYR D CA  
13873 C C   . TYR D 211 ? 0.5027 0.3801 0.3674 0.0867  0.0047  -0.0305 211 TYR D C   
13874 O O   . TYR D 211 ? 0.4807 0.3572 0.3415 0.1032  0.0050  -0.0348 211 TYR D O   
13875 C CB  . TYR D 211 ? 0.5617 0.3852 0.3995 0.0786  -0.0066 -0.0264 211 TYR D CB  
13876 C CG  . TYR D 211 ? 0.5793 0.3852 0.4102 0.0730  -0.0098 -0.0194 211 TYR D CG  
13877 C CD1 . TYR D 211 ? 0.5378 0.3549 0.3747 0.0798  -0.0109 -0.0160 211 TYR D CD1 
13878 C CD2 . TYR D 211 ? 0.6147 0.3920 0.4329 0.0610  -0.0120 -0.0158 211 TYR D CD2 
13879 C CE1 . TYR D 211 ? 0.5615 0.3595 0.3864 0.0767  -0.0135 -0.0092 211 TYR D CE1 
13880 C CE2 . TYR D 211 ? 0.6037 0.3641 0.4136 0.0564  -0.0125 -0.0076 211 TYR D CE2 
13881 C CZ  . TYR D 211 ? 0.5794 0.3489 0.3900 0.0652  -0.0130 -0.0044 211 TYR D CZ  
13882 O OH  . TYR D 211 ? 0.6057 0.3551 0.4026 0.0625  -0.0131 0.0040  211 TYR D OH  
13883 N N   . GLU D 212 ? 0.5751 0.4654 0.4455 0.0773  0.0091  -0.0303 212 GLU D N   
13884 C CA  . GLU D 212 ? 0.5745 0.4741 0.4416 0.0864  0.0145  -0.0350 212 GLU D CA  
13885 C C   . GLU D 212 ? 0.5795 0.5118 0.4673 0.0968  0.0227  -0.0329 212 GLU D C   
13886 O O   . GLU D 212 ? 0.6078 0.5455 0.4913 0.1113  0.0285  -0.0364 212 GLU D O   
13887 C CB  . GLU D 212 ? 0.4884 0.3913 0.3542 0.0739  0.0157  -0.0347 212 GLU D CB  
13888 C CG  . GLU D 212 ? 0.5414 0.4134 0.3897 0.0644  0.0067  -0.0379 212 GLU D CG  
13889 C CD  . GLU D 212 ? 0.6163 0.4941 0.4662 0.0527  0.0060  -0.0379 212 GLU D CD  
13890 O OE1 . GLU D 212 ? 0.6495 0.5114 0.4971 0.0397  -0.0012 -0.0377 212 GLU D OE1 
13891 O OE2 . GLU D 212 ? 0.5937 0.4925 0.4486 0.0564  0.0127  -0.0374 212 GLU D OE2 
13892 N N   . THR D 213 ? 0.5193 0.4729 0.4299 0.0903  0.0233  -0.0271 213 THR D N   
13893 C CA  . THR D 213 ? 0.4984 0.4836 0.4343 0.0980  0.0293  -0.0245 213 THR D CA  
13894 C C   . THR D 213 ? 0.5353 0.5249 0.4837 0.1035  0.0225  -0.0235 213 THR D C   
13895 O O   . THR D 213 ? 0.5830 0.5962 0.5526 0.1136  0.0254  -0.0228 213 THR D O   
13896 C CB  . THR D 213 ? 0.4886 0.4989 0.4446 0.0858  0.0350  -0.0190 213 THR D CB  
13897 O OG1 . THR D 213 ? 0.5549 0.5577 0.5109 0.0714  0.0287  -0.0164 213 THR D OG1 
13898 C CG2 . THR D 213 ? 0.4695 0.4801 0.4143 0.0846  0.0427  -0.0197 213 THR D CG2 
13899 N N   . THR D 214 ? 0.5205 0.4886 0.4569 0.0977  0.0136  -0.0228 214 THR D N   
13900 C CA  . THR D 214 ? 0.4729 0.4381 0.4131 0.1052  0.0052  -0.0224 214 THR D CA  
13901 C C   . THR D 214 ? 0.5230 0.4514 0.4344 0.1113  -0.0010 -0.0248 214 THR D C   
13902 O O   . THR D 214 ? 0.5848 0.4922 0.4821 0.1036  -0.0062 -0.0218 214 THR D O   
13903 C CB  . THR D 214 ? 0.4559 0.4276 0.4054 0.0940  0.0003  -0.0182 214 THR D CB  
13904 O OG1 . THR D 214 ? 0.4641 0.4172 0.3968 0.0803  0.0014  -0.0158 214 THR D OG1 
13905 C CG2 . THR D 214 ? 0.4409 0.4469 0.4207 0.0891  0.0045  -0.0160 214 THR D CG2 
13906 N N   . PRO D 215 ? 0.5122 0.4305 0.4131 0.1257  -0.0001 -0.0298 215 PRO D N   
13907 C CA  . PRO D 215 ? 0.5295 0.4079 0.4013 0.1307  -0.0067 -0.0321 215 PRO D CA  
13908 C C   . PRO D 215 ? 0.5908 0.4557 0.4570 0.1354  -0.0159 -0.0291 215 PRO D C   
13909 O O   . PRO D 215 ? 0.6305 0.4606 0.4726 0.1322  -0.0207 -0.0274 215 PRO D O   
13910 C CB  . PRO D 215 ? 0.5470 0.4216 0.4112 0.1489  -0.0040 -0.0388 215 PRO D CB  
13911 C CG  . PRO D 215 ? 0.5416 0.4582 0.4357 0.1570  0.0036  -0.0384 215 PRO D CG  
13912 C CD  . PRO D 215 ? 0.5252 0.4661 0.4391 0.1390  0.0076  -0.0330 215 PRO D CD  
13913 N N   . ASN D 216 ? 0.5591 0.4495 0.4467 0.1419  -0.0190 -0.0279 216 ASN D N   
13914 C CA  . ASN D 216 ? 0.6296 0.5068 0.5096 0.1498  -0.0297 -0.0261 216 ASN D CA  
13915 C C   . ASN D 216 ? 0.6033 0.4800 0.4825 0.1369  -0.0332 -0.0206 216 ASN D C   
13916 O O   . ASN D 216 ? 0.5782 0.4458 0.4501 0.1439  -0.0427 -0.0190 216 ASN D O   
13917 C CB  . ASN D 216 ? 0.6490 0.5524 0.5526 0.1673  -0.0342 -0.0292 216 ASN D CB  
13918 C CG  . ASN D 216 ? 0.6990 0.6002 0.5999 0.1845  -0.0306 -0.0345 216 ASN D CG  
13919 O OD1 . ASN D 216 ? 0.6782 0.6125 0.6062 0.1939  -0.0256 -0.0366 216 ASN D OD1 
13920 N ND2 . ASN D 216 ? 0.7407 0.6022 0.6091 0.1892  -0.0326 -0.0365 216 ASN D ND2 
13921 N N   . VAL D 217 ? 0.5753 0.4606 0.4596 0.1198  -0.0261 -0.0179 217 VAL D N   
13922 C CA  . VAL D 217 ? 0.5941 0.4774 0.4749 0.1092  -0.0282 -0.0130 217 VAL D CA  
13923 C C   . VAL D 217 ? 0.5727 0.4176 0.4216 0.1071  -0.0300 -0.0081 217 VAL D C   
13924 O O   . VAL D 217 ? 0.6119 0.4326 0.4446 0.1057  -0.0273 -0.0077 217 VAL D O   
13925 C CB  . VAL D 217 ? 0.6116 0.5132 0.5059 0.0928  -0.0196 -0.0114 217 VAL D CB  
13926 C CG1 . VAL D 217 ? 0.5768 0.4603 0.4569 0.0827  -0.0126 -0.0102 217 VAL D CG1 
13927 C CG2 . VAL D 217 ? 0.5930 0.4971 0.4866 0.0855  -0.0221 -0.0076 217 VAL D CG2 
13928 N N   . LYS D 218 ? 0.5326 0.3703 0.3715 0.1073  -0.0349 -0.0041 218 LYS D N   
13929 C CA  . LYS D 218 ? 0.6231 0.4275 0.4325 0.1030  -0.0333 0.0033  218 LYS D CA  
13930 C C   . LYS D 218 ? 0.5869 0.3991 0.3990 0.0875  -0.0251 0.0080  218 LYS D C   
13931 O O   . LYS D 218 ? 0.6457 0.4774 0.4684 0.0869  -0.0275 0.0068  218 LYS D O   
13932 C CB  . LYS D 218 ? 0.7089 0.4948 0.4980 0.1171  -0.0437 0.0053  218 LYS D CB  
13933 C CG  . LYS D 218 ? 0.8494 0.5927 0.6033 0.1178  -0.0418 0.0135  218 LYS D CG  
13934 C CD  . LYS D 218 ? 0.9566 0.6907 0.6973 0.1046  -0.0322 0.0226  218 LYS D CD  
13935 C CE  . LYS D 218 ? 1.0275 0.7273 0.7321 0.1124  -0.0341 0.0313  218 LYS D CE  
13936 N NZ  . LYS D 218 ? 1.0264 0.7228 0.7197 0.1022  -0.0232 0.0400  218 LYS D NZ  
13937 N N   . ILE D 219 ? 0.5825 0.3794 0.3861 0.0753  -0.0164 0.0132  219 ILE D N   
13938 C CA  . ILE D 219 ? 0.6370 0.4418 0.4446 0.0612  -0.0074 0.0184  219 ILE D CA  
13939 C C   . ILE D 219 ? 0.6143 0.3887 0.3972 0.0573  -0.0019 0.0286  219 ILE D C   
13940 O O   . ILE D 219 ? 0.6676 0.4138 0.4331 0.0614  -0.0041 0.0314  219 ILE D O   
13941 C CB  . ILE D 219 ? 0.6320 0.4538 0.4600 0.0485  -0.0012 0.0157  219 ILE D CB  
13942 C CG1 . ILE D 219 ? 0.6600 0.4591 0.4800 0.0444  -0.0003 0.0162  219 ILE D CG1 
13943 C CG2 . ILE D 219 ? 0.6380 0.4884 0.4879 0.0533  -0.0046 0.0076  219 ILE D CG2 
13944 C CD1 . ILE D 219 ? 0.6663 0.4744 0.5001 0.0294  0.0054  0.0162  219 ILE D CD1 
13945 N N   . PRO D 220 ? 0.6008 0.3790 0.3805 0.0501  0.0059  0.0350  220 PRO D N   
13946 C CA  . PRO D 220 ? 0.6405 0.3919 0.3979 0.0463  0.0143  0.0468  220 PRO D CA  
13947 C C   . PRO D 220 ? 0.6610 0.3998 0.4246 0.0326  0.0206  0.0515  220 PRO D C   
13948 O O   . PRO D 220 ? 0.5975 0.3495 0.3815 0.0252  0.0189  0.0452  220 PRO D O   
13949 C CB  . PRO D 220 ? 0.5886 0.3548 0.3474 0.0419  0.0228  0.0510  220 PRO D CB  
13950 C CG  . PRO D 220 ? 0.6011 0.4001 0.3873 0.0381  0.0200  0.0420  220 PRO D CG  
13951 C CD  . PRO D 220 ? 0.5891 0.3945 0.3832 0.0475  0.0076  0.0322  220 PRO D CD  
13952 N N   . ASP D 221 ? 0.6764 0.3879 0.4211 0.0292  0.0277  0.0632  221 ASP D N   
13953 C CA  . ASP D 221 ? 0.6947 0.3918 0.4467 0.0140  0.0338  0.0697  221 ASP D CA  
13954 C C   . ASP D 221 ? 0.6543 0.3754 0.4286 -0.0011 0.0452  0.0744  221 ASP D C   
13955 O O   . ASP D 221 ? 0.6507 0.3722 0.4175 -0.0025 0.0567  0.0846  221 ASP D O   
13956 C CB  . ASP D 221 ? 0.7750 0.4331 0.4997 0.0157  0.0378  0.0821  221 ASP D CB  
13957 C CG  . ASP D 221 ? 0.8079 0.4532 0.5433 -0.0034 0.0474  0.0929  221 ASP D CG  
13958 O OD1 . ASP D 221 ? 0.7670 0.4261 0.5287 -0.0163 0.0454  0.0876  221 ASP D OD1 
13959 O OD2 . ASP D 221 ? 0.8377 0.4586 0.5549 -0.0053 0.0570  0.1074  221 ASP D OD2 
13960 N N   . PHE D 222 ? 0.5659 0.3064 0.3664 -0.0108 0.0421  0.0669  222 PHE D N   
13961 C CA  . PHE D 222 ? 0.5716 0.3369 0.3970 -0.0246 0.0504  0.0697  222 PHE D CA  
13962 C C   . PHE D 222 ? 0.6435 0.3928 0.4758 -0.0401 0.0582  0.0814  222 PHE D C   
13963 O O   . PHE D 222 ? 0.7041 0.4522 0.5543 -0.0522 0.0534  0.0786  222 PHE D O   
13964 C CB  . PHE D 222 ? 0.4715 0.2607 0.3188 -0.0274 0.0425  0.0573  222 PHE D CB  
13965 C CG  . PHE D 222 ? 0.4380 0.2520 0.2881 -0.0172 0.0401  0.0499  222 PHE D CG  
13966 C CD1 . PHE D 222 ? 0.4342 0.2453 0.2728 -0.0030 0.0316  0.0426  222 PHE D CD1 
13967 C CD2 . PHE D 222 ? 0.4215 0.2614 0.2872 -0.0219 0.0462  0.0507  222 PHE D CD2 
13968 C CE1 . PHE D 222 ? 0.4958 0.3294 0.3405 0.0045  0.0288  0.0366  222 PHE D CE1 
13969 C CE2 . PHE D 222 ? 0.4914 0.3511 0.3599 -0.0135 0.0433  0.0442  222 PHE D CE2 
13970 C CZ  . PHE D 222 ? 0.5085 0.3650 0.3675 -0.0012 0.0344  0.0374  222 PHE D CZ  
13971 N N   . ALA D 223 ? 0.6593 0.3950 0.4766 -0.0395 0.0701  0.0951  223 ALA D N   
13972 C CA  . ALA D 223 ? 0.7085 0.4262 0.5315 -0.0541 0.0794  0.1090  223 ALA D CA  
13973 C C   . ALA D 223 ? 0.6968 0.4414 0.5550 -0.0709 0.0881  0.1139  223 ALA D C   
13974 O O   . ALA D 223 ? 0.7439 0.4786 0.6152 -0.0855 0.0958  0.1259  223 ALA D O   
13975 C CB  . ALA D 223 ? 0.7441 0.4389 0.5377 -0.0468 0.0918  0.1239  223 ALA D CB  
13976 N N   . VAL D 224 ? 0.6559 0.4342 0.5311 -0.0691 0.0870  0.1055  224 VAL D N   
13977 C CA  . VAL D 224 ? 0.5996 0.4069 0.5084 -0.0821 0.0944  0.1091  224 VAL D CA  
13978 C C   . VAL D 224 ? 0.5065 0.3338 0.4347 -0.0844 0.0802  0.0939  224 VAL D C   
13979 O O   . VAL D 224 ? 0.4955 0.3212 0.4099 -0.0732 0.0695  0.0819  224 VAL D O   
13980 C CB  . VAL D 224 ? 0.6224 0.4500 0.5278 -0.0746 0.1098  0.1159  224 VAL D CB  
13981 C CG1 . VAL D 224 ? 0.5969 0.4431 0.4959 -0.0613 0.1021  0.1026  224 VAL D CG1 
13982 C CG2 . VAL D 224 ? 0.6914 0.5431 0.6304 -0.0883 0.1223  0.1255  224 VAL D CG2 
13983 N N   . SER D 225 ? 0.5016 0.3481 0.4625 -0.0987 0.0803  0.0949  225 SER D N   
13984 C CA  . SER D 225 ? 0.4916 0.3554 0.4694 -0.1012 0.0668  0.0816  225 SER D CA  
13985 C C   . SER D 225 ? 0.5034 0.4010 0.4932 -0.0960 0.0717  0.0788  225 SER D C   
13986 O O   . SER D 225 ? 0.5371 0.4529 0.5442 -0.1009 0.0838  0.0880  225 SER D O   
13987 C CB  . SER D 225 ? 0.4567 0.3191 0.4624 -0.1192 0.0598  0.0826  225 SER D CB  
13988 O OG  . SER D 225 ? 0.4607 0.3384 0.4791 -0.1201 0.0462  0.0696  225 SER D OG  
13989 N N   . PHE D 226 ? 0.4622 0.3679 0.4437 -0.0861 0.0626  0.0666  226 PHE D N   
13990 C CA  . PHE D 226 ? 0.3940 0.3281 0.3855 -0.0811 0.0649  0.0630  226 PHE D CA  
13991 C C   . PHE D 226 ? 0.3641 0.3144 0.3765 -0.0874 0.0545  0.0550  226 PHE D C   
13992 O O   . PHE D 226 ? 0.3451 0.3146 0.3616 -0.0818 0.0531  0.0499  226 PHE D O   
13993 C CB  . PHE D 226 ? 0.3724 0.3052 0.3415 -0.0658 0.0629  0.0565  226 PHE D CB  
13994 C CG  . PHE D 226 ? 0.3908 0.3130 0.3392 -0.0572 0.0726  0.0637  226 PHE D CG  
13995 C CD1 . PHE D 226 ? 0.4375 0.3740 0.3881 -0.0540 0.0838  0.0695  226 PHE D CD1 
13996 C CD2 . PHE D 226 ? 0.4503 0.3469 0.3748 -0.0508 0.0699  0.0643  226 PHE D CD2 
13997 C CE1 . PHE D 226 ? 0.4288 0.3526 0.3552 -0.0442 0.0923  0.0756  226 PHE D CE1 
13998 C CE2 . PHE D 226 ? 0.4396 0.3242 0.3413 -0.0415 0.0774  0.0707  226 PHE D CE2 
13999 C CZ  . PHE D 226 ? 0.4952 0.3928 0.3967 -0.0381 0.0885  0.0762  226 PHE D CZ  
14000 N N   . ARG D 227 ? 0.4284 0.3687 0.4523 -0.0986 0.0461  0.0538  227 ARG D N   
14001 C CA  . ARG D 227 ? 0.3827 0.3332 0.4200 -0.1025 0.0331  0.0446  227 ARG D CA  
14002 C C   . ARG D 227 ? 0.3596 0.3400 0.4254 -0.1081 0.0365  0.0480  227 ARG D C   
14003 O O   . ARG D 227 ? 0.3036 0.2996 0.3728 -0.1033 0.0305  0.0410  227 ARG D O   
14004 C CB  . ARG D 227 ? 0.4369 0.3652 0.4766 -0.1124 0.0208  0.0412  227 ARG D CB  
14005 C CG  . ARG D 227 ? 0.5635 0.4619 0.5737 -0.1042 0.0152  0.0354  227 ARG D CG  
14006 C CD  . ARG D 227 ? 0.6717 0.5473 0.6816 -0.1117 -0.0002 0.0286  227 ARG D CD  
14007 N NE  . ARG D 227 ? 0.7136 0.6017 0.7313 -0.1119 -0.0124 0.0186  227 ARG D NE  
14008 C CZ  . ARG D 227 ? 0.7092 0.5931 0.7063 -0.0995 -0.0197 0.0074  227 ARG D CZ  
14009 N NH1 . ARG D 227 ? 0.6321 0.5026 0.6041 -0.0867 -0.0162 0.0048  227 ARG D NH1 
14010 N NH2 . ARG D 227 ? 0.7672 0.6608 0.7689 -0.0993 -0.0303 -0.0004 227 ARG D NH2 
14011 N N   . GLU D 228 ? 0.3571 0.3462 0.4439 -0.1173 0.0469  0.0594  228 GLU D N   
14012 C CA  . GLU D 228 ? 0.3760 0.3959 0.4930 -0.1214 0.0505  0.0629  228 GLU D CA  
14013 C C   . GLU D 228 ? 0.3522 0.3895 0.4604 -0.1079 0.0598  0.0627  228 GLU D C   
14014 O O   . GLU D 228 ? 0.3581 0.4180 0.4826 -0.1063 0.0571  0.0600  228 GLU D O   
14015 C CB  . GLU D 228 ? 0.5145 0.5418 0.6593 -0.1343 0.0615  0.0766  228 GLU D CB  
14016 C CG  . GLU D 228 ? 0.6958 0.7572 0.8801 -0.1405 0.0626  0.0799  228 GLU D CG  
14017 C CD  . GLU D 228 ? 0.8177 0.8871 1.0130 -0.1425 0.0419  0.0674  228 GLU D CD  
14018 O OE1 . GLU D 228 ? 0.8788 0.9346 1.0822 -0.1533 0.0267  0.0628  228 GLU D OE1 
14019 O OE2 . GLU D 228 ? 0.8111 0.8978 1.0045 -0.1325 0.0402  0.0621  228 GLU D OE2 
14020 N N   . ASP D 229 ? 0.2725 0.2978 0.3541 -0.0976 0.0690  0.0649  229 ASP D N   
14021 C CA  . ASP D 229 ? 0.2904 0.3267 0.3600 -0.0845 0.0741  0.0625  229 ASP D CA  
14022 C C   . ASP D 229 ? 0.3067 0.3462 0.3699 -0.0790 0.0614  0.0510  229 ASP D C   
14023 O O   . ASP D 229 ? 0.3249 0.3807 0.3927 -0.0731 0.0619  0.0487  229 ASP D O   
14024 C CB  . ASP D 229 ? 0.2895 0.3081 0.3298 -0.0746 0.0823  0.0654  229 ASP D CB  
14025 C CG  . ASP D 229 ? 0.3494 0.3682 0.3908 -0.0753 0.0992  0.0783  229 ASP D CG  
14026 O OD1 . ASP D 229 ? 0.2964 0.3332 0.3650 -0.0831 0.1065  0.0855  229 ASP D OD1 
14027 O OD2 . ASP D 229 ? 0.3435 0.3446 0.3583 -0.0671 0.1054  0.0815  229 ASP D OD2 
14028 N N   . ALA D 230 ? 0.3486 0.3715 0.3997 -0.0798 0.0507  0.0441  230 ALA D N   
14029 C CA  . ALA D 230 ? 0.3624 0.3884 0.4065 -0.0741 0.0409  0.0347  230 ALA D CA  
14030 C C   . ALA D 230 ? 0.3077 0.3521 0.3725 -0.0785 0.0345  0.0326  230 ALA D C   
14031 O O   . ALA D 230 ? 0.2639 0.3205 0.3285 -0.0721 0.0335  0.0298  230 ALA D O   
14032 C CB  . ALA D 230 ? 0.3931 0.3983 0.4206 -0.0730 0.0320  0.0283  230 ALA D CB  
14033 N N   . SER D 231 ? 0.3091 0.3557 0.3937 -0.0896 0.0299  0.0346  231 SER D N   
14034 C CA  . SER D 231 ? 0.3093 0.3755 0.4167 -0.0934 0.0227  0.0330  231 SER D CA  
14035 C C   . SER D 231 ? 0.2799 0.3695 0.4014 -0.0889 0.0332  0.0388  231 SER D C   
14036 O O   . SER D 231 ? 0.2669 0.3708 0.3949 -0.0845 0.0282  0.0356  231 SER D O   
14037 C CB  . SER D 231 ? 0.3991 0.4648 0.5301 -0.1074 0.0152  0.0348  231 SER D CB  
14038 O OG  . SER D 231 ? 0.5032 0.5456 0.6190 -0.1099 0.0018  0.0269  231 SER D OG  
14039 N N   . LYS D 232 ? 0.2539 0.3456 0.3775 -0.0884 0.0480  0.0473  232 LYS D N   
14040 C CA  . LYS D 232 ? 0.2101 0.3231 0.3464 -0.0828 0.0586  0.0526  232 LYS D CA  
14041 C C   . LYS D 232 ? 0.1956 0.3077 0.3114 -0.0697 0.0589  0.0476  232 LYS D C   
14042 O O   . LYS D 232 ? 0.2231 0.3516 0.3487 -0.0641 0.0595  0.0473  232 LYS D O   
14043 C CB  . LYS D 232 ? 0.3286 0.4421 0.4681 -0.0838 0.0757  0.0634  232 LYS D CB  
14044 C CG  . LYS D 232 ? 0.3964 0.5371 0.5684 -0.0864 0.0848  0.0714  232 LYS D CG  
14045 C CD  . LYS D 232 ? 0.4135 0.5544 0.5879 -0.0874 0.1042  0.0838  232 LYS D CD  
14046 C CE  . LYS D 232 ? 0.4436 0.6095 0.6332 -0.0789 0.1181  0.0899  232 LYS D CE  
14047 N NZ  . LYS D 232 ? 0.4409 0.6072 0.6335 -0.0807 0.1324  0.0984  232 LYS D NZ  
14048 N N   . HIS D 233 ? 0.1975 0.2904 0.2865 -0.0646 0.0582  0.0440  233 HIS D N   
14049 C CA  . HIS D 233 ? 0.2191 0.3106 0.2925 -0.0544 0.0562  0.0391  233 HIS D CA  
14050 C C   . HIS D 233 ? 0.1926 0.2931 0.2733 -0.0542 0.0457  0.0340  233 HIS D C   
14051 O O   . HIS D 233 ? 0.2198 0.3281 0.3002 -0.0473 0.0460  0.0331  233 HIS D O   
14052 C CB  . HIS D 233 ? 0.2519 0.3238 0.3014 -0.0508 0.0540  0.0354  233 HIS D CB  
14053 C CG  . HIS D 233 ? 0.2544 0.3162 0.2895 -0.0458 0.0630  0.0392  233 HIS D CG  
14054 N ND1 . HIS D 233 ? 0.2520 0.3156 0.2787 -0.0368 0.0682  0.0396  233 HIS D ND1 
14055 C CD2 . HIS D 233 ? 0.2813 0.3281 0.3057 -0.0475 0.0665  0.0423  233 HIS D CD2 
14056 C CE1 . HIS D 233 ? 0.2985 0.3491 0.3089 -0.0326 0.0741  0.0425  233 HIS D CE1 
14057 N NE2 . HIS D 233 ? 0.2755 0.3161 0.2844 -0.0390 0.0737  0.0448  233 HIS D NE2 
14058 N N   . VAL D 234 ? 0.2292 0.3265 0.3144 -0.0609 0.0358  0.0306  234 VAL D N   
14059 C CA  . VAL D 234 ? 0.2366 0.3392 0.3233 -0.0591 0.0250  0.0257  234 VAL D CA  
14060 C C   . VAL D 234 ? 0.2263 0.3494 0.3376 -0.0606 0.0227  0.0280  234 VAL D C   
14061 O O   . VAL D 234 ? 0.2156 0.3466 0.3270 -0.0542 0.0191  0.0266  234 VAL D O   
14062 C CB  . VAL D 234 ? 0.2052 0.2943 0.2831 -0.0633 0.0141  0.0200  234 VAL D CB  
14063 C CG1 . VAL D 234 ? 0.1922 0.2850 0.2670 -0.0597 0.0029  0.0151  234 VAL D CG1 
14064 C CG2 . VAL D 234 ? 0.2218 0.2930 0.2771 -0.0597 0.0171  0.0178  234 VAL D CG2 
14065 N N   . GLU D 235 ? 0.2172 0.3494 0.3511 -0.0691 0.0246  0.0322  235 GLU D N   
14066 C CA  . GLU D 235 ? 0.2361 0.3915 0.3995 -0.0710 0.0220  0.0349  235 GLU D CA  
14067 C C   . GLU D 235 ? 0.2695 0.4390 0.4370 -0.0613 0.0334  0.0392  235 GLU D C   
14068 O O   . GLU D 235 ? 0.2157 0.3996 0.3942 -0.0558 0.0286  0.0382  235 GLU D O   
14069 C CB  . GLU D 235 ? 0.3601 0.5230 0.5507 -0.0836 0.0232  0.0399  235 GLU D CB  
14070 C CG  . GLU D 235 ? 0.4914 0.6751 0.7151 -0.0893 0.0117  0.0393  235 GLU D CG  
14071 C CD  . GLU D 235 ? 0.6203 0.7922 0.8343 -0.0913 -0.0092 0.0297  235 GLU D CD  
14072 O OE1 . GLU D 235 ? 0.6557 0.8085 0.8607 -0.0990 -0.0162 0.0262  235 GLU D OE1 
14073 O OE2 . GLU D 235 ? 0.6493 0.8288 0.8618 -0.0839 -0.0187 0.0256  235 GLU D OE2 
14074 N N   . LEU D 236 ? 0.2482 0.4116 0.4044 -0.0576 0.0476  0.0434  236 LEU D N   
14075 C CA  . LEU D 236 ? 0.2639 0.4358 0.4181 -0.0464 0.0579  0.0463  236 LEU D CA  
14076 C C   . LEU D 236 ? 0.2770 0.4412 0.4127 -0.0371 0.0513  0.0406  236 LEU D C   
14077 O O   . LEU D 236 ? 0.2442 0.4184 0.3849 -0.0284 0.0530  0.0411  236 LEU D O   
14078 C CB  . LEU D 236 ? 0.2004 0.3618 0.3393 -0.0432 0.0724  0.0508  236 LEU D CB  
14079 C CG  . LEU D 236 ? 0.2164 0.3884 0.3758 -0.0504 0.0836  0.0597  236 LEU D CG  
14080 C CD1 . LEU D 236 ? 0.2717 0.4282 0.4082 -0.0457 0.0971  0.0641  236 LEU D CD1 
14081 C CD2 . LEU D 236 ? 0.2257 0.4259 0.4155 -0.0475 0.0895  0.0646  236 LEU D CD2 
14082 N N   . ALA D 237 ? 0.2769 0.4232 0.3918 -0.0385 0.0444  0.0358  237 ALA D N   
14083 C CA  . ALA D 237 ? 0.2402 0.3796 0.3402 -0.0313 0.0389  0.0321  237 ALA D CA  
14084 C C   . ALA D 237 ? 0.2497 0.4007 0.3617 -0.0298 0.0293  0.0309  237 ALA D C   
14085 O O   . ALA D 237 ? 0.1937 0.3474 0.3036 -0.0215 0.0285  0.0310  237 ALA D O   
14086 C CB  . ALA D 237 ? 0.2183 0.3400 0.2982 -0.0335 0.0347  0.0284  237 ALA D CB  
14087 N N   . LYS D 238 ? 0.1877 0.3437 0.3112 -0.0372 0.0205  0.0294  238 LYS D N   
14088 C CA  . LYS D 238 ? 0.2395 0.4053 0.3728 -0.0352 0.0086  0.0274  238 LYS D CA  
14089 C C   . LYS D 238 ? 0.2509 0.4375 0.4066 -0.0295 0.0119  0.0310  238 LYS D C   
14090 O O   . LYS D 238 ? 0.2492 0.4395 0.4039 -0.0214 0.0058  0.0302  238 LYS D O   
14091 C CB  . LYS D 238 ? 0.1941 0.3609 0.3377 -0.0446 -0.0030 0.0243  238 LYS D CB  
14092 C CG  . LYS D 238 ? 0.1789 0.3239 0.2969 -0.0470 -0.0080 0.0195  238 LYS D CG  
14093 C CD  . LYS D 238 ? 0.2793 0.4212 0.4064 -0.0567 -0.0191 0.0159  238 LYS D CD  
14094 C CE  . LYS D 238 ? 0.3859 0.5389 0.5277 -0.0566 -0.0351 0.0128  238 LYS D CE  
14095 N NZ  . LYS D 238 ? 0.4241 0.5737 0.5783 -0.0672 -0.0479 0.0087  238 LYS D NZ  
14096 N N   . GLU D 239 ? 0.2287 0.4284 0.4039 -0.0324 0.0227  0.0357  239 GLU D N   
14097 C CA  . GLU D 239 ? 0.2069 0.4288 0.4052 -0.0255 0.0284  0.0397  239 GLU D CA  
14098 C C   . GLU D 239 ? 0.2373 0.4518 0.4172 -0.0118 0.0349  0.0395  239 GLU D C   
14099 O O   . GLU D 239 ? 0.1612 0.3866 0.3499 -0.0025 0.0319  0.0397  239 GLU D O   
14100 C CB  . GLU D 239 ? 0.3177 0.5542 0.5385 -0.0311 0.0417  0.0462  239 GLU D CB  
14101 C CG  . GLU D 239 ? 0.4627 0.7095 0.7100 -0.0455 0.0346  0.0474  239 GLU D CG  
14102 C CD  . GLU D 239 ? 0.6013 0.8526 0.8617 -0.0534 0.0496  0.0551  239 GLU D CD  
14103 O OE1 . GLU D 239 ? 0.6532 0.8994 0.9224 -0.0669 0.0443  0.0555  239 GLU D OE1 
14104 O OE2 . GLU D 239 ? 0.5683 0.8262 0.8281 -0.0455 0.0666  0.0608  239 GLU D OE2 
14105 N N   . LYS D 240 ? 0.2324 0.4275 0.3872 -0.0101 0.0426  0.0390  240 LYS D N   
14106 C CA  . LYS D 240 ? 0.2680 0.4523 0.4047 0.0019  0.0467  0.0379  240 LYS D CA  
14107 C C   . LYS D 240 ? 0.2525 0.4264 0.3767 0.0056  0.0351  0.0348  240 LYS D C   
14108 O O   . LYS D 240 ? 0.2355 0.4081 0.3564 0.0162  0.0342  0.0347  240 LYS D O   
14109 C CB  . LYS D 240 ? 0.2434 0.4083 0.3571 0.0016  0.0542  0.0372  240 LYS D CB  
14110 C CG  . LYS D 240 ? 0.3223 0.4740 0.4177 0.0135  0.0575  0.0354  240 LYS D CG  
14111 C CD  . LYS D 240 ? 0.4070 0.5706 0.5104 0.0237  0.0689  0.0383  240 LYS D CD  
14112 C CE  . LYS D 240 ? 0.4340 0.5817 0.5172 0.0373  0.0696  0.0350  240 LYS D CE  
14113 N NZ  . LYS D 240 ? 0.4051 0.5631 0.4925 0.0504  0.0816  0.0373  240 LYS D NZ  
14114 N N   . TYR D 241 ? 0.1735 0.3377 0.2883 -0.0020 0.0269  0.0326  241 TYR D N   
14115 C CA  . TYR D 241 ? 0.1999 0.3541 0.3017 0.0015  0.0175  0.0313  241 TYR D CA  
14116 C C   . TYR D 241 ? 0.2172 0.3861 0.3340 0.0076  0.0094  0.0319  241 TYR D C   
14117 O O   . TYR D 241 ? 0.2188 0.3813 0.3269 0.0166  0.0060  0.0326  241 TYR D O   
14118 C CB  . TYR D 241 ? 0.2338 0.3779 0.3238 -0.0065 0.0116  0.0292  241 TYR D CB  
14119 C CG  . TYR D 241 ? 0.1891 0.3209 0.2615 -0.0027 0.0047  0.0293  241 TYR D CG  
14120 C CD1 . TYR D 241 ? 0.1861 0.3230 0.2607 0.0007  -0.0061 0.0289  241 TYR D CD1 
14121 C CD2 . TYR D 241 ? 0.2102 0.3253 0.2642 -0.0025 0.0088  0.0303  241 TYR D CD2 
14122 C CE1 . TYR D 241 ? 0.2964 0.4197 0.3508 0.0053  -0.0113 0.0302  241 TYR D CE1 
14123 C CE2 . TYR D 241 ? 0.2748 0.3788 0.3132 0.0005  0.0047  0.0323  241 TYR D CE2 
14124 C CZ  . TYR D 241 ? 0.3254 0.4325 0.3620 0.0049  -0.0046 0.0326  241 TYR D CZ  
14125 O OH  . TYR D 241 ? 0.3009 0.3949 0.3181 0.0090  -0.0073 0.0359  241 TYR D OH  
14126 N N   . PHE D 242 ? 0.2189 0.4075 0.3600 0.0030  0.0060  0.0320  242 PHE D N   
14127 C CA  . PHE D 242 ? 0.2325 0.4384 0.3927 0.0088  -0.0034 0.0322  242 PHE D CA  
14128 C C   . PHE D 242 ? 0.2213 0.4362 0.3896 0.0214  0.0035  0.0347  242 PHE D C   
14129 O O   . PHE D 242 ? 0.1850 0.4023 0.3540 0.0312  -0.0045 0.0346  242 PHE D O   
14130 C CB  . PHE D 242 ? 0.1716 0.3993 0.3627 -0.0002 -0.0081 0.0322  242 PHE D CB  
14131 C CG  . PHE D 242 ? 0.2266 0.4741 0.4407 0.0054  -0.0207 0.0318  242 PHE D CG  
14132 C CD1 . PHE D 242 ? 0.1954 0.4664 0.4362 0.0134  -0.0146 0.0352  242 PHE D CD1 
14133 C CD2 . PHE D 242 ? 0.2227 0.4642 0.4293 0.0047  -0.0389 0.0278  242 PHE D CD2 
14134 C CE1 . PHE D 242 ? 0.2081 0.4990 0.4723 0.0197  -0.0272 0.0347  242 PHE D CE1 
14135 C CE2 . PHE D 242 ? 0.1996 0.4587 0.4266 0.0109  -0.0528 0.0269  242 PHE D CE2 
14136 C CZ  . PHE D 242 ? 0.2042 0.4890 0.4618 0.0182  -0.0473 0.0304  242 PHE D CZ  
14137 N N   . GLU D 243 ? 0.2463 0.4651 0.4190 0.0228  0.0181  0.0368  243 GLU D N   
14138 C CA  . GLU D 243 ? 0.2816 0.5071 0.4587 0.0369  0.0258  0.0384  243 GLU D CA  
14139 C C   . GLU D 243 ? 0.2451 0.4467 0.3950 0.0468  0.0216  0.0365  243 GLU D C   
14140 O O   . GLU D 243 ? 0.2127 0.4177 0.3658 0.0598  0.0195  0.0368  243 GLU D O   
14141 C CB  . GLU D 243 ? 0.3101 0.5378 0.4876 0.0377  0.0428  0.0406  243 GLU D CB  
14142 C CG  . GLU D 243 ? 0.4246 0.6521 0.5971 0.0544  0.0521  0.0411  243 GLU D CG  
14143 C CD  . GLU D 243 ? 0.5517 0.7686 0.7083 0.0567  0.0671  0.0418  243 GLU D CD  
14144 O OE1 . GLU D 243 ? 0.5754 0.7780 0.7128 0.0703  0.0717  0.0396  243 GLU D OE1 
14145 O OE2 . GLU D 243 ? 0.5527 0.7731 0.7136 0.0456  0.0732  0.0442  243 GLU D OE2 
14146 N N   . ILE D 244 ? 0.1974 0.3745 0.3219 0.0408  0.0206  0.0350  244 ILE D N   
14147 C CA  . ILE D 244 ? 0.2536 0.4067 0.3547 0.0478  0.0175  0.0344  244 ILE D CA  
14148 C C   . ILE D 244 ? 0.2334 0.3812 0.3287 0.0488  0.0052  0.0354  244 ILE D C   
14149 O O   . ILE D 244 ? 0.2255 0.3629 0.3121 0.0590  0.0009  0.0365  244 ILE D O   
14150 C CB  . ILE D 244 ? 0.2811 0.4125 0.3615 0.0408  0.0218  0.0331  244 ILE D CB  
14151 C CG1 . ILE D 244 ? 0.2805 0.4140 0.3616 0.0419  0.0331  0.0319  244 ILE D CG1 
14152 C CG2 . ILE D 244 ? 0.2372 0.3435 0.2973 0.0454  0.0175  0.0333  244 ILE D CG2 
14153 C CD1 . ILE D 244 ? 0.3038 0.4334 0.3806 0.0564  0.0380  0.0308  244 ILE D CD1 
14154 N N   . PHE D 245 ? 0.2018 0.3545 0.2995 0.0396  -0.0011 0.0352  245 PHE D N   
14155 C CA  . PHE D 245 ? 0.2449 0.3855 0.3271 0.0405  -0.0115 0.0364  245 PHE D CA  
14156 C C   . PHE D 245 ? 0.2264 0.3834 0.3224 0.0428  -0.0237 0.0355  245 PHE D C   
14157 O O   . PHE D 245 ? 0.3040 0.4505 0.3849 0.0475  -0.0335 0.0368  245 PHE D O   
14158 C CB  . PHE D 245 ? 0.2333 0.3587 0.2975 0.0304  -0.0097 0.0364  245 PHE D CB  
14159 C CG  . PHE D 245 ? 0.2375 0.3448 0.2880 0.0286  -0.0010 0.0376  245 PHE D CG  
14160 C CD1 . PHE D 245 ? 0.2694 0.3581 0.3053 0.0345  -0.0019 0.0409  245 PHE D CD1 
14161 C CD2 . PHE D 245 ? 0.2408 0.3485 0.2934 0.0210  0.0067  0.0355  245 PHE D CD2 
14162 C CE1 . PHE D 245 ? 0.2977 0.3698 0.3246 0.0316  0.0039  0.0415  245 PHE D CE1 
14163 C CE2 . PHE D 245 ? 0.2404 0.3322 0.2822 0.0196  0.0121  0.0357  245 PHE D CE2 
14164 C CZ  . PHE D 245 ? 0.3293 0.4041 0.3599 0.0243  0.0103  0.0384  245 PHE D CZ  
14165 N N   . GLY D 246 ? 0.2102 0.4235 0.4125 0.0006  0.0558  0.0429  246 GLY D N   
14166 C CA  . GLY D 246 ? 0.2714 0.5123 0.4897 0.0040  0.0521  0.0425  246 GLY D CA  
14167 C C   . GLY D 246 ? 0.2673 0.5199 0.4910 -0.0014 0.0421  0.0379  246 GLY D C   
14168 O O   . GLY D 246 ? 0.2767 0.5513 0.5111 0.0038  0.0363  0.0366  246 GLY D O   
14169 N N   . GLU D 247 ? 0.2594 0.4976 0.4748 -0.0103 0.0394  0.0350  247 GLU D N   
14170 C CA  . GLU D 247 ? 0.2525 0.4983 0.4707 -0.0159 0.0302  0.0299  247 GLU D CA  
14171 C C   . GLU D 247 ? 0.2212 0.4523 0.4349 -0.0279 0.0316  0.0266  247 GLU D C   
14172 O O   . GLU D 247 ? 0.1770 0.3895 0.3805 -0.0297 0.0380  0.0286  247 GLU D O   
14173 C CB  . GLU D 247 ? 0.3561 0.5973 0.5617 -0.0085 0.0248  0.0318  247 GLU D CB  
14174 C CG  . GLU D 247 ? 0.4616 0.6794 0.6520 -0.0126 0.0266  0.0333  247 GLU D CG  
14175 C CD  . GLU D 247 ? 0.5804 0.7949 0.7606 -0.0047 0.0234  0.0369  247 GLU D CD  
14176 O OE1 . GLU D 247 ? 0.5904 0.8181 0.7721 0.0057  0.0205  0.0388  247 GLU D OE1 
14177 O OE2 . GLU D 247 ? 0.6097 0.8089 0.7804 -0.0078 0.0242  0.0384  247 GLU D OE2 
14178 N N   . HIS D 248 ? 0.2297 0.4682 0.4499 -0.0352 0.0251  0.0210  248 HIS D N   
14179 C CA  . HIS D 248 ? 0.2299 0.4519 0.4414 -0.0447 0.0253  0.0182  248 HIS D CA  
14180 C C   . HIS D 248 ? 0.2251 0.4323 0.4181 -0.0412 0.0220  0.0196  248 HIS D C   
14181 O O   . HIS D 248 ? 0.2140 0.4285 0.4042 -0.0342 0.0158  0.0201  248 HIS D O   
14182 C CB  . HIS D 248 ? 0.3610 0.5930 0.5841 -0.0532 0.0188  0.0115  248 HIS D CB  
14183 C CG  . HIS D 248 ? 0.5318 0.7787 0.7774 -0.0590 0.0229  0.0104  248 HIS D CG  
14184 N ND1 . HIS D 248 ? 0.5818 0.8195 0.8299 -0.0643 0.0343  0.0134  248 HIS D ND1 
14185 C CD2 . HIS D 248 ? 0.5820 0.8535 0.8500 -0.0598 0.0175  0.0067  248 HIS D CD2 
14186 C CE1 . HIS D 248 ? 0.5820 0.8379 0.8541 -0.0686 0.0372  0.0128  248 HIS D CE1 
14187 N NE2 . HIS D 248 ? 0.5814 0.8589 0.8675 -0.0667 0.0265  0.0083  248 HIS D NE2 
14188 N N   . PRO D 249 ? 0.2143 0.4020 0.3948 -0.0448 0.0260  0.0206  249 PRO D N   
14189 C CA  . PRO D 249 ? 0.2030 0.3792 0.3696 -0.0416 0.0234  0.0225  249 PRO D CA  
14190 C C   . PRO D 249 ? 0.2438 0.4219 0.4056 -0.0435 0.0158  0.0189  249 PRO D C   
14191 O O   . PRO D 249 ? 0.2991 0.4758 0.4623 -0.0509 0.0141  0.0141  249 PRO D O   
14192 C CB  . PRO D 249 ? 0.2361 0.3935 0.3932 -0.0455 0.0286  0.0227  249 PRO D CB  
14193 C CG  . PRO D 249 ? 0.1641 0.3210 0.3257 -0.0523 0.0326  0.0197  249 PRO D CG  
14194 C CD  . PRO D 249 ? 0.2044 0.3804 0.3829 -0.0510 0.0332  0.0199  249 PRO D CD  
14195 N N   . VAL D 250 ? 0.2138 0.3936 0.3690 -0.0359 0.0121  0.0218  250 VAL D N   
14196 C CA  . VAL D 250 ? 0.2284 0.4080 0.3750 -0.0350 0.0050  0.0189  250 VAL D CA  
14197 C C   . VAL D 250 ? 0.2218 0.3868 0.3552 -0.0347 0.0067  0.0219  250 VAL D C   
14198 O O   . VAL D 250 ? 0.2092 0.3712 0.3328 -0.0338 0.0019  0.0197  250 VAL D O   
14199 C CB  . VAL D 250 ? 0.2835 0.4767 0.4297 -0.0243 -0.0011 0.0197  250 VAL D CB  
14200 C CG1 . VAL D 250 ? 0.3158 0.5260 0.4758 -0.0255 -0.0063 0.0138  250 VAL D CG1 
14201 C CG2 . VAL D 250 ? 0.2927 0.4860 0.4376 -0.0146 0.0043  0.0281  250 VAL D CG2 
14202 N N   . TYR D 251 ? 0.1809 0.3371 0.3141 -0.0350 0.0128  0.0263  251 TYR D N   
14203 C CA  . TYR D 251 ? 0.1916 0.3360 0.3164 -0.0358 0.0143  0.0284  251 TYR D CA  
14204 C C   . TYR D 251 ? 0.2343 0.3674 0.3582 -0.0427 0.0178  0.0257  251 TYR D C   
14205 O O   . TYR D 251 ? 0.1877 0.3203 0.3178 -0.0438 0.0215  0.0256  251 TYR D O   
14206 C CB  . TYR D 251 ? 0.2640 0.4081 0.3910 -0.0290 0.0174  0.0360  251 TYR D CB  
14207 C CG  . TYR D 251 ? 0.3387 0.4939 0.4659 -0.0194 0.0158  0.0399  251 TYR D CG  
14208 C CD1 . TYR D 251 ? 0.3803 0.5401 0.4985 -0.0147 0.0104  0.0385  251 TYR D CD1 
14209 C CD2 . TYR D 251 ? 0.2964 0.4567 0.4308 -0.0136 0.0194  0.0443  251 TYR D CD2 
14210 C CE1 . TYR D 251 ? 0.4372 0.6067 0.5527 -0.0037 0.0081  0.0412  251 TYR D CE1 
14211 C CE2 . TYR D 251 ? 0.3055 0.4760 0.4377 -0.0026 0.0179  0.0478  251 TYR D CE2 
14212 C CZ  . TYR D 251 ? 0.3749 0.5501 0.4973 0.0026  0.0120  0.0461  251 TYR D CZ  
14213 O OH  . TYR D 251 ? 0.4075 0.5923 0.5248 0.0156  0.0095  0.0488  251 TYR D OH  
14214 N N   . MET D 252 ? 0.2044 0.3281 0.3187 -0.0457 0.0168  0.0236  252 MET D N   
14215 C CA  . MET D 252 ? 0.2457 0.3577 0.3558 -0.0494 0.0196  0.0213  252 MET D CA  
14216 C C   . MET D 252 ? 0.2759 0.3814 0.3800 -0.0480 0.0181  0.0225  252 MET D C   
14217 O O   . MET D 252 ? 0.2547 0.3628 0.3543 -0.0455 0.0156  0.0244  252 MET D O   
14218 C CB  . MET D 252 ? 0.2812 0.3873 0.3853 -0.0546 0.0209  0.0166  252 MET D CB  
14219 C CG  . MET D 252 ? 0.3221 0.4337 0.4357 -0.0570 0.0245  0.0156  252 MET D CG  
14220 S SD  . MET D 252 ? 0.2976 0.3989 0.4058 -0.0630 0.0298  0.0122  252 MET D SD  
14221 C CE  . MET D 252 ? 0.2875 0.4011 0.4130 -0.0645 0.0347  0.0133  252 MET D CE  
14222 N N   . TRP D 253 ? 0.2591 0.3567 0.3633 -0.0487 0.0193  0.0212  253 TRP D N   
14223 C CA  . TRP D 253 ? 0.2582 0.3501 0.3573 -0.0481 0.0169  0.0204  253 TRP D CA  
14224 C C   . TRP D 253 ? 0.3020 0.3837 0.3866 -0.0493 0.0170  0.0154  253 TRP D C   
14225 O O   . TRP D 253 ? 0.2257 0.3002 0.3066 -0.0500 0.0196  0.0123  253 TRP D O   
14226 C CB  . TRP D 253 ? 0.2132 0.3021 0.3214 -0.0478 0.0164  0.0203  253 TRP D CB  
14227 C CG  . TRP D 253 ? 0.1726 0.2566 0.2773 -0.0475 0.0126  0.0173  253 TRP D CG  
14228 C CD1 . TRP D 253 ? 0.2154 0.2895 0.3135 -0.0471 0.0103  0.0111  253 TRP D CD1 
14229 C CD2 . TRP D 253 ? 0.1701 0.2599 0.2777 -0.0462 0.0103  0.0203  253 TRP D CD2 
14230 N NE1 . TRP D 253 ? 0.2375 0.3120 0.3350 -0.0460 0.0055  0.0092  253 TRP D NE1 
14231 C CE2 . TRP D 253 ? 0.1965 0.2812 0.3008 -0.0458 0.0060  0.0152  253 TRP D CE2 
14232 C CE3 . TRP D 253 ? 0.1967 0.2958 0.3082 -0.0439 0.0117  0.0270  253 TRP D CE3 
14233 C CZ2 . TRP D 253 ? 0.1934 0.2841 0.3012 -0.0442 0.0031  0.0167  253 TRP D CZ2 
14234 C CZ3 . TRP D 253 ? 0.1828 0.2865 0.2961 -0.0417 0.0100  0.0294  253 TRP D CZ3 
14235 C CH2 . TRP D 253 ? 0.2273 0.3278 0.3404 -0.0424 0.0057  0.0244  253 TRP D CH2 
14236 N N   . PRO D 254 ? 0.3286 0.4083 0.4029 -0.0485 0.0153  0.0151  254 PRO D N   
14237 C CA  . PRO D 254 ? 0.2986 0.3663 0.3572 -0.0485 0.0165  0.0111  254 PRO D CA  
14238 C C   . PRO D 254 ? 0.2507 0.3122 0.3048 -0.0454 0.0144  0.0083  254 PRO D C   
14239 O O   . PRO D 254 ? 0.2799 0.3470 0.3402 -0.0435 0.0103  0.0094  254 PRO D O   
14240 C CB  . PRO D 254 ? 0.3019 0.3692 0.3508 -0.0472 0.0148  0.0120  254 PRO D CB  
14241 C CG  . PRO D 254 ? 0.2941 0.3729 0.3526 -0.0443 0.0118  0.0166  254 PRO D CG  
14242 C CD  . PRO D 254 ? 0.2907 0.3776 0.3655 -0.0458 0.0129  0.0189  254 PRO D CD  
14243 N N   . PRO D 255 ? 0.2479 0.2987 0.2928 -0.0441 0.0169  0.0047  255 PRO D N   
14244 C CA  . PRO D 255 ? 0.2088 0.2537 0.2487 -0.0397 0.0132  0.0004  255 PRO D CA  
14245 C C   . PRO D 255 ? 0.2554 0.3010 0.2884 -0.0361 0.0083  -0.0007 255 PRO D C   
14246 O O   . PRO D 255 ? 0.2255 0.2675 0.2461 -0.0348 0.0102  0.0005  255 PRO D O   
14247 C CB  . PRO D 255 ? 0.2523 0.2835 0.2767 -0.0365 0.0184  -0.0023 255 PRO D CB  
14248 C CG  . PRO D 255 ? 0.2448 0.2795 0.2776 -0.0415 0.0251  0.0012  255 PRO D CG  
14249 C CD  . PRO D 255 ? 0.2504 0.2954 0.2913 -0.0461 0.0236  0.0046  255 PRO D CD  
14250 N N   . GLU D 256 ? 0.2097 0.2605 0.2522 -0.0347 0.0018  -0.0031 256 GLU D N   
14251 C CA  . GLU D 256 ? 0.2706 0.3270 0.3127 -0.0313 -0.0035 -0.0036 256 GLU D CA  
14252 C C   . GLU D 256 ? 0.2906 0.3563 0.3368 -0.0326 -0.0014 0.0030  256 GLU D C   
14253 O O   . GLU D 256 ? 0.2408 0.3079 0.2782 -0.0282 -0.0030 0.0037  256 GLU D O   
14254 C CB  . GLU D 256 ? 0.2847 0.3300 0.3033 -0.0239 -0.0046 -0.0084 256 GLU D CB  
14255 C CG  . GLU D 256 ? 0.2670 0.2997 0.2741 -0.0197 -0.0051 -0.0145 256 GLU D CG  
14256 C CD  . GLU D 256 ? 0.2964 0.3333 0.3182 -0.0199 -0.0134 -0.0201 256 GLU D CD  
14257 O OE1 . GLU D 256 ? 0.2653 0.3147 0.3044 -0.0219 -0.0200 -0.0204 256 GLU D OE1 
14258 O OE2 . GLU D 256 ? 0.3152 0.3423 0.3313 -0.0177 -0.0130 -0.0242 256 GLU D OE2 
14259 N N   . ALA D 257 ? 0.2225 0.2940 0.2799 -0.0369 0.0021  0.0080  257 ALA D N   
14260 C CA  . ALA D 257 ? 0.1923 0.2709 0.2500 -0.0361 0.0039  0.0138  257 ALA D CA  
14261 C C   . ALA D 257 ? 0.2451 0.3142 0.2811 -0.0335 0.0055  0.0125  257 ALA D C   
14262 O O   . ALA D 257 ? 0.2282 0.3005 0.2590 -0.0304 0.0055  0.0159  257 ALA D O   
14263 C CB  . ALA D 257 ? 0.2093 0.2999 0.2793 -0.0335 0.0014  0.0180  257 ALA D CB  
14264 N N   A SER D 258 ? 0.2978 0.3539 0.3201 -0.0339 0.0077  0.0081  258 SER D N   
14265 N N   B SER D 258 ? 0.3060 0.3621 0.3285 -0.0340 0.0078  0.0082  258 SER D N   
14266 C CA  A SER D 258 ? 0.3154 0.3593 0.3164 -0.0309 0.0099  0.0069  258 SER D CA  
14267 C CA  B SER D 258 ? 0.3207 0.3646 0.3218 -0.0310 0.0099  0.0069  258 SER D CA  
14268 C C   A SER D 258 ? 0.3111 0.3520 0.3094 -0.0349 0.0129  0.0083  258 SER D C   
14269 C C   B SER D 258 ? 0.3132 0.3541 0.3116 -0.0349 0.0129  0.0083  258 SER D C   
14270 O O   A SER D 258 ? 0.3089 0.3503 0.3155 -0.0404 0.0155  0.0079  258 SER D O   
14271 O O   B SER D 258 ? 0.3092 0.3506 0.3158 -0.0405 0.0155  0.0079  258 SER D O   
14272 C CB  A SER D 258 ? 0.3199 0.3495 0.3066 -0.0286 0.0127  0.0027  258 SER D CB  
14273 C CB  B SER D 258 ? 0.3059 0.3354 0.2927 -0.0288 0.0128  0.0027  258 SER D CB  
14274 O OG  A SER D 258 ? 0.3768 0.4037 0.3701 -0.0335 0.0169  0.0021  258 SER D OG  
14275 O OG  B SER D 258 ? 0.2890 0.3051 0.2545 -0.0249 0.0159  0.0024  258 SER D OG  
14276 N N   . VAL D 259 ? 0.2828 0.3208 0.2696 -0.0315 0.0119  0.0096  259 VAL D N   
14277 C CA  . VAL D 259 ? 0.3161 0.3498 0.2988 -0.0345 0.0127  0.0093  259 VAL D CA  
14278 C C   . VAL D 259 ? 0.3249 0.3423 0.2848 -0.0307 0.0141  0.0078  259 VAL D C   
14279 O O   . VAL D 259 ? 0.2945 0.3083 0.2422 -0.0236 0.0137  0.0085  259 VAL D O   
14280 C CB  . VAL D 259 ? 0.3291 0.3765 0.3216 -0.0329 0.0090  0.0127  259 VAL D CB  
14281 C CG1 . VAL D 259 ? 0.2951 0.3560 0.3090 -0.0365 0.0089  0.0146  259 VAL D CG1 
14282 C CG2 . VAL D 259 ? 0.3241 0.3771 0.3114 -0.0245 0.0071  0.0168  259 VAL D CG2 
14283 N N   . SER D 260 ? 0.3052 0.3127 0.2604 -0.0355 0.0155  0.0054  260 SER D N   
14284 C CA  . SER D 260 ? 0.3725 0.3630 0.3071 -0.0328 0.0163  0.0037  260 SER D CA  
14285 C C   . SER D 260 ? 0.3660 0.3563 0.3059 -0.0383 0.0129  0.0007  260 SER D C   
14286 O O   . SER D 260 ? 0.3653 0.3688 0.3243 -0.0438 0.0110  0.0002  260 SER D O   
14287 C CB  . SER D 260 ? 0.3218 0.2924 0.2427 -0.0339 0.0234  0.0022  260 SER D CB  
14288 O OG  . SER D 260 ? 0.3894 0.3569 0.3225 -0.0436 0.0279  0.0005  260 SER D OG  
14289 N N   . ASN D 261 ? 0.3184 0.2935 0.2409 -0.0361 0.0116  -0.0018 261 ASN D N   
14290 C CA  . ASN D 261 ? 0.3445 0.3172 0.2709 -0.0412 0.0067  -0.0067 261 ASN D CA  
14291 C C   . ASN D 261 ? 0.3514 0.3238 0.2959 -0.0537 0.0098  -0.0099 261 ASN D C   
14292 O O   . ASN D 261 ? 0.3314 0.3165 0.2930 -0.0587 0.0048  -0.0127 261 ASN D O   
14293 C CB  . ASN D 261 ? 0.3976 0.3487 0.3000 -0.0372 0.0052  -0.0100 261 ASN D CB  
14294 C CG  . ASN D 261 ? 0.4045 0.3595 0.2911 -0.0239 0.0010  -0.0069 261 ASN D CG  
14295 O OD1 . ASN D 261 ? 0.3805 0.3547 0.2770 -0.0193 -0.0027 -0.0036 261 ASN D OD1 
14296 N ND2 . ASN D 261 ? 0.4105 0.3468 0.2723 -0.0167 0.0026  -0.0070 261 ASN D ND2 
14297 N N   . GLU D 262 ? 0.3358 0.2947 0.2770 -0.0576 0.0185  -0.0090 262 GLU D N   
14298 C CA  . GLU D 262 ? 0.3397 0.2983 0.2989 -0.0687 0.0238  -0.0105 262 GLU D CA  
14299 C C   . GLU D 262 ? 0.2875 0.2674 0.2677 -0.0705 0.0245  -0.0077 262 GLU D C   
14300 O O   . GLU D 262 ? 0.3428 0.3311 0.3433 -0.0789 0.0253  -0.0094 262 GLU D O   
14301 C CB  . GLU D 262 ? 0.4056 0.3422 0.3527 -0.0700 0.0351  -0.0086 262 GLU D CB  
14302 C CG  . GLU D 262 ? 0.5005 0.4126 0.4270 -0.0690 0.0361  -0.0111 262 GLU D CG  
14303 C CD  . GLU D 262 ? 0.5888 0.4777 0.5042 -0.0702 0.0491  -0.0083 262 GLU D CD  
14304 O OE1 . GLU D 262 ? 0.5885 0.4799 0.5198 -0.0770 0.0571  -0.0061 262 GLU D OE1 
14305 O OE2 . GLU D 262 ? 0.6626 0.5304 0.5524 -0.0633 0.0520  -0.0076 262 GLU D OE2 
14306 N N   . ALA D 263 ? 0.2740 0.2622 0.2507 -0.0630 0.0244  -0.0038 263 ALA D N   
14307 C CA  . ALA D 263 ? 0.3267 0.3328 0.3224 -0.0644 0.0245  -0.0017 263 ALA D CA  
14308 C C   . ALA D 263 ? 0.2889 0.3131 0.2996 -0.0654 0.0167  -0.0027 263 ALA D C   
14309 O O   . ALA D 263 ? 0.2932 0.3296 0.3225 -0.0700 0.0169  -0.0030 263 ALA D O   
14310 C CB  . ALA D 263 ? 0.3262 0.3353 0.3157 -0.0567 0.0251  0.0016  263 ALA D CB  
14311 N N   . LEU D 264 ? 0.2671 0.2928 0.2684 -0.0595 0.0102  -0.0030 264 LEU D N   
14312 C CA  . LEU D 264 ? 0.2931 0.3344 0.3046 -0.0577 0.0031  -0.0036 264 LEU D CA  
14313 C C   . LEU D 264 ? 0.3459 0.3884 0.3681 -0.0653 -0.0005 -0.0098 264 LEU D C   
14314 O O   . LEU D 264 ? 0.3095 0.3681 0.3484 -0.0667 -0.0039 -0.0105 264 LEU D O   
14315 C CB  . LEU D 264 ? 0.2688 0.3091 0.2647 -0.0479 -0.0018 -0.0020 264 LEU D CB  
14316 C CG  . LEU D 264 ? 0.3044 0.3486 0.2962 -0.0407 0.0011  0.0044  264 LEU D CG  
14317 C CD1 . LEU D 264 ? 0.3233 0.3647 0.2984 -0.0306 -0.0017 0.0067  264 LEU D CD1 
14318 C CD2 . LEU D 264 ? 0.3754 0.4372 0.3859 -0.0401 0.0016  0.0087  264 LEU D CD2 
14319 N N   . GLU D 265 ? 0.3101 0.3356 0.3236 -0.0703 0.0001  -0.0144 265 GLU D N   
14320 C CA  . GLU D 265 ? 0.3735 0.3995 0.4015 -0.0800 -0.0030 -0.0210 265 GLU D CA  
14321 C C   . GLU D 265 ? 0.3358 0.3733 0.3877 -0.0880 0.0032  -0.0194 265 GLU D C   
14322 O O   . GLU D 265 ? 0.3076 0.3591 0.3794 -0.0931 -0.0015 -0.0233 265 GLU D O   
14323 C CB  . GLU D 265 ? 0.4128 0.4147 0.4282 -0.0850 -0.0008 -0.0252 265 GLU D CB  
14324 C CG  . GLU D 265 ? 0.5051 0.5054 0.5394 -0.0976 -0.0024 -0.0321 265 GLU D CG  
14325 C CD  . GLU D 265 ? 0.5597 0.5690 0.5990 -0.0969 -0.0169 -0.0405 265 GLU D CD  
14326 O OE1 . GLU D 265 ? 0.5374 0.5561 0.6001 -0.1064 -0.0211 -0.0466 265 GLU D OE1 
14327 O OE2 . GLU D 265 ? 0.5154 0.5229 0.5349 -0.0857 -0.0240 -0.0410 265 GLU D OE2 
14328 N N   . LEU D 266 ? 0.3083 0.3400 0.3578 -0.0880 0.0136  -0.0139 266 LEU D N   
14329 C CA  . LEU D 266 ? 0.3010 0.3414 0.3702 -0.0939 0.0210  -0.0116 266 LEU D CA  
14330 C C   . LEU D 266 ? 0.3072 0.3699 0.3908 -0.0901 0.0172  -0.0095 266 LEU D C   
14331 O O   . LEU D 266 ? 0.2284 0.3053 0.3333 -0.0950 0.0176  -0.0104 266 LEU D O   
14332 C CB  . LEU D 266 ? 0.2551 0.2815 0.3134 -0.0920 0.0325  -0.0065 266 LEU D CB  
14333 C CG  . LEU D 266 ? 0.2496 0.2839 0.3236 -0.0944 0.0413  -0.0027 266 LEU D CG  
14334 C CD1 . LEU D 266 ? 0.2569 0.2945 0.3524 -0.1051 0.0461  -0.0042 266 LEU D CD1 
14335 C CD2 . LEU D 266 ? 0.2563 0.2756 0.3135 -0.0886 0.0512  0.0018  266 LEU D CD2 
14336 N N   . TYR D 267 ? 0.2455 0.3117 0.3187 -0.0812 0.0142  -0.0063 267 TYR D N   
14337 C CA  . TYR D 267 ? 0.2456 0.3302 0.3305 -0.0768 0.0114  -0.0036 267 TYR D CA  
14338 C C   . TYR D 267 ? 0.2996 0.3986 0.3958 -0.0771 0.0026  -0.0078 267 TYR D C   
14339 O O   . TYR D 267 ? 0.2370 0.3519 0.3505 -0.0776 0.0021  -0.0074 267 TYR D O   
14340 C CB  . TYR D 267 ? 0.2126 0.2967 0.2857 -0.0680 0.0099  0.0007  267 TYR D CB  
14341 C CG  . TYR D 267 ? 0.2926 0.3681 0.3593 -0.0664 0.0164  0.0040  267 TYR D CG  
14342 C CD1 . TYR D 267 ? 0.3099 0.3898 0.3868 -0.0672 0.0214  0.0060  267 TYR D CD1 
14343 C CD2 . TYR D 267 ? 0.3346 0.3979 0.3842 -0.0628 0.0168  0.0045  267 TYR D CD2 
14344 C CE1 . TYR D 267 ? 0.3527 0.4237 0.4219 -0.0645 0.0257  0.0075  267 TYR D CE1 
14345 C CE2 . TYR D 267 ? 0.3918 0.4482 0.4353 -0.0602 0.0208  0.0061  267 TYR D CE2 
14346 C CZ  . TYR D 267 ? 0.4046 0.4642 0.4574 -0.0611 0.0248  0.0071  267 TYR D CZ  
14347 O OH  . TYR D 267 ? 0.3470 0.3985 0.3916 -0.0573 0.0271  0.0072  267 TYR D OH  
14348 N N   . TYR D 268 ? 0.3108 0.4041 0.3962 -0.0754 -0.0048 -0.0122 268 TYR D N   
14349 C CA  . TYR D 268 ? 0.2585 0.3639 0.3521 -0.0746 -0.0150 -0.0180 268 TYR D CA  
14350 C C   . TYR D 268 ? 0.2741 0.3870 0.3905 -0.0855 -0.0149 -0.0231 268 TYR D C   
14351 O O   . TYR D 268 ? 0.2207 0.3530 0.3544 -0.0848 -0.0195 -0.0249 268 TYR D O   
14352 C CB  . TYR D 268 ? 0.3194 0.4130 0.3943 -0.0708 -0.0229 -0.0230 268 TYR D CB  
14353 C CG  . TYR D 268 ? 0.3316 0.4303 0.4153 -0.0745 -0.0338 -0.0329 268 TYR D CG  
14354 C CD1 . TYR D 268 ? 0.3555 0.4729 0.4464 -0.0674 -0.0431 -0.0355 268 TYR D CD1 
14355 C CD2 . TYR D 268 ? 0.3992 0.4837 0.4843 -0.0847 -0.0352 -0.0401 268 TYR D CD2 
14356 C CE1 . TYR D 268 ? 0.2603 0.3840 0.3600 -0.0700 -0.0552 -0.0462 268 TYR D CE1 
14357 C CE2 . TYR D 268 ? 0.3801 0.4695 0.4759 -0.0891 -0.0468 -0.0508 268 TYR D CE2 
14358 C CZ  . TYR D 268 ? 0.3575 0.4675 0.4609 -0.0816 -0.0576 -0.0543 268 TYR D CZ  
14359 O OH  . TYR D 268 ? 0.3849 0.5013 0.4996 -0.0852 -0.0711 -0.0663 268 TYR D OH  
14360 N N   . GLU D 269 ? 0.2359 0.3341 0.3535 -0.0952 -0.0089 -0.0249 269 GLU D N   
14361 C CA  . GLU D 269 ? 0.2827 0.3878 0.4251 -0.1067 -0.0075 -0.0292 269 GLU D CA  
14362 C C   . GLU D 269 ? 0.2847 0.4078 0.4475 -0.1073 -0.0008 -0.0241 269 GLU D C   
14363 O O   . GLU D 269 ? 0.3567 0.4954 0.5447 -0.1139 -0.0025 -0.0274 269 GLU D O   
14364 C CB  . GLU D 269 ? 0.3260 0.4090 0.4644 -0.1159 0.0012  -0.0295 269 GLU D CB  
14365 C CG  . GLU D 269 ? 0.4299 0.4977 0.5581 -0.1191 -0.0070 -0.0375 269 GLU D CG  
14366 C CD  . GLU D 269 ? 0.6047 0.6488 0.7293 -0.1280 0.0031  -0.0370 269 GLU D CD  
14367 O OE1 . GLU D 269 ? 0.6572 0.6815 0.7644 -0.1282 -0.0010 -0.0417 269 GLU D OE1 
14368 O OE2 . GLU D 269 ? 0.6477 0.6916 0.7851 -0.1337 0.0160  -0.0314 269 GLU D OE2 
14369 N N   . LYS D 270 ? 0.2473 0.3690 0.4005 -0.1004 0.0063  -0.0165 270 LYS D N   
14370 C CA  . LYS D 270 ? 0.2669 0.4024 0.4349 -0.0990 0.0129  -0.0115 270 LYS D CA  
14371 C C   . LYS D 270 ? 0.2797 0.4335 0.4514 -0.0899 0.0059  -0.0104 270 LYS D C   
14372 O O   . LYS D 270 ? 0.1872 0.3497 0.3660 -0.0862 0.0112  -0.0055 270 LYS D O   
14373 C CB  . LYS D 270 ? 0.2928 0.4136 0.4470 -0.0960 0.0242  -0.0048 270 LYS D CB  
14374 C CG  . LYS D 270 ? 0.3013 0.4042 0.4513 -0.1028 0.0337  -0.0042 270 LYS D CG  
14375 C CD  . LYS D 270 ? 0.3967 0.5091 0.5713 -0.1105 0.0413  -0.0033 270 LYS D CD  
14376 C CE  . LYS D 270 ? 0.4839 0.5775 0.6560 -0.1175 0.0523  -0.0018 270 LYS D CE  
14377 N NZ  . LYS D 270 ? 0.5170 0.6222 0.7194 -0.1277 0.0576  -0.0021 270 LYS D NZ  
14378 N N   . GLY D 271 ? 0.2934 0.4515 0.4585 -0.0850 -0.0054 -0.0146 271 GLY D N   
14379 C CA  . GLY D 271 ? 0.2410 0.4161 0.4091 -0.0751 -0.0115 -0.0133 271 GLY D CA  
14380 C C   . GLY D 271 ? 0.2683 0.4375 0.4195 -0.0650 -0.0089 -0.0063 271 GLY D C   
14381 O O   . GLY D 271 ? 0.2687 0.4499 0.4225 -0.0563 -0.0108 -0.0031 271 GLY D O   
14382 N N   . ILE D 272 ? 0.2419 0.3933 0.3772 -0.0657 -0.0044 -0.0037 272 ILE D N   
14383 C CA  . ILE D 272 ? 0.2447 0.3917 0.3679 -0.0573 -0.0023 0.0027  272 ILE D CA  
14384 C C   . ILE D 272 ? 0.2559 0.4036 0.3667 -0.0493 -0.0100 0.0019  272 ILE D C   
14385 O O   . ILE D 272 ? 0.3225 0.4611 0.4226 -0.0511 -0.0142 -0.0025 272 ILE D O   
14386 C CB  . ILE D 272 ? 0.2436 0.3740 0.3562 -0.0601 0.0045  0.0053  272 ILE D CB  
14387 C CG1 . ILE D 272 ? 0.2851 0.4130 0.4064 -0.0658 0.0124  0.0060  272 ILE D CG1 
14388 C CG2 . ILE D 272 ? 0.2263 0.3546 0.3312 -0.0525 0.0056  0.0113  272 ILE D CG2 
14389 C CD1 . ILE D 272 ? 0.3135 0.4546 0.4488 -0.0628 0.0149  0.0091  272 ILE D CD1 
14390 N N   . ASN D 273 ? 0.2087 0.3658 0.3195 -0.0394 -0.0111 0.0068  273 ASN D N   
14391 C CA  . ASN D 273 ? 0.2291 0.3887 0.3277 -0.0288 -0.0174 0.0073  273 ASN D CA  
14392 C C   . ASN D 273 ? 0.2678 0.4181 0.3532 -0.0227 -0.0130 0.0145  273 ASN D C   
14393 O O   . ASN D 273 ? 0.2947 0.4422 0.3658 -0.0147 -0.0170 0.0148  273 ASN D O   
14394 C CB  . ASN D 273 ? 0.3103 0.4859 0.4156 -0.0191 -0.0200 0.0095  273 ASN D CB  
14395 C CG  . ASN D 273 ? 0.4534 0.6417 0.5696 -0.0216 -0.0286 0.0006  273 ASN D CG  
14396 O OD1 . ASN D 273 ? 0.5456 0.7305 0.6591 -0.0265 -0.0361 -0.0078 273 ASN D OD1 
14397 N ND2 . ASN D 273 ? 0.4779 0.6811 0.6074 -0.0182 -0.0280 0.0022  273 ASN D ND2 
14398 N N   . MET D 274 ? 0.2419 0.3879 0.3324 -0.0257 -0.0051 0.0201  274 MET D N   
14399 C CA  . MET D 274 ? 0.2422 0.3820 0.3254 -0.0212 -0.0009 0.0269  274 MET D CA  
14400 C C   . MET D 274 ? 0.2984 0.4301 0.3866 -0.0291 0.0045  0.0276  274 MET D C   
14401 O O   . MET D 274 ? 0.2994 0.4319 0.3977 -0.0342 0.0073  0.0265  274 MET D O   
14402 C CB  . MET D 274 ? 0.2792 0.4265 0.3655 -0.0107 0.0023  0.0356  274 MET D CB  
14403 C CG  . MET D 274 ? 0.4038 0.5470 0.4856 -0.0056 0.0070  0.0435  274 MET D CG  
14404 S SD  . MET D 274 ? 0.5571 0.6964 0.6546 -0.0125 0.0145  0.0481  274 MET D SD  
14405 C CE  . MET D 274 ? 0.5259 0.6725 0.6332 -0.0044 0.0196  0.0564  274 MET D CE  
14406 N N   . LEU D 275 ? 0.3382 0.4622 0.4180 -0.0287 0.0055  0.0291  275 LEU D N   
14407 C CA  . LEU D 275 ? 0.3272 0.4448 0.4107 -0.0332 0.0092  0.0300  275 LEU D CA  
14408 C C   . LEU D 275 ? 0.3195 0.4378 0.4012 -0.0277 0.0107  0.0361  275 LEU D C   
14409 O O   . LEU D 275 ? 0.2824 0.4049 0.3581 -0.0200 0.0101  0.0403  275 LEU D O   
14410 C CB  . LEU D 275 ? 0.3105 0.4175 0.3862 -0.0401 0.0087  0.0233  275 LEU D CB  
14411 C CG  . LEU D 275 ? 0.3389 0.4389 0.3992 -0.0395 0.0055  0.0197  275 LEU D CG  
14412 C CD1 . LEU D 275 ? 0.2822 0.3775 0.3327 -0.0350 0.0058  0.0225  275 LEU D CD1 
14413 C CD2 . LEU D 275 ? 0.3991 0.4894 0.4559 -0.0472 0.0066  0.0135  275 LEU D CD2 
14414 N N   . ALA D 276 ? 0.2688 0.3837 0.3562 -0.0310 0.0126  0.0366  276 ALA D N   
14415 C CA  . ALA D 276 ? 0.2336 0.3504 0.3221 -0.0273 0.0136  0.0413  276 ALA D CA  
14416 C C   . ALA D 276 ? 0.2387 0.3477 0.3196 -0.0307 0.0115  0.0359  276 ALA D C   
14417 O O   . ALA D 276 ? 0.2169 0.3183 0.2942 -0.0358 0.0106  0.0297  276 ALA D O   
14418 C CB  . ALA D 276 ? 0.2230 0.3456 0.3306 -0.0272 0.0174  0.0477  276 ALA D CB  
14419 N N   . THR D 277 ? 0.2204 0.3317 0.2980 -0.0264 0.0112  0.0389  277 THR D N   
14420 C CA  . THR D 277 ? 0.2779 0.3834 0.3477 -0.0270 0.0089  0.0346  277 THR D CA  
14421 C C   . THR D 277 ? 0.2702 0.3857 0.3508 -0.0229 0.0096  0.0404  277 THR D C   
14422 O O   . THR D 277 ? 0.2665 0.3914 0.3637 -0.0218 0.0128  0.0475  277 THR D O   
14423 C CB  . THR D 277 ? 0.2750 0.3700 0.3218 -0.0252 0.0076  0.0303  277 THR D CB  
14424 O OG1 . THR D 277 ? 0.2891 0.3782 0.3269 -0.0239 0.0061  0.0269  277 THR D OG1 
14425 C CG2 . THR D 277 ? 0.2973 0.3946 0.3339 -0.0179 0.0077  0.0346  277 THR D CG2 
14426 N N   . ASP D 278 ? 0.2885 0.4024 0.3606 -0.0201 0.0072  0.0380  278 ASP D N   
14427 C CA  . ASP D 278 ? 0.2525 0.3781 0.3398 -0.0177 0.0069  0.0421  278 ASP D CA  
14428 C C   . ASP D 278 ? 0.2311 0.3637 0.3118 -0.0085 0.0098  0.0496  278 ASP D C   
14429 O O   . ASP D 278 ? 0.2312 0.3556 0.2886 -0.0032 0.0097  0.0486  278 ASP D O   
14430 C CB  . ASP D 278 ? 0.2556 0.3781 0.3405 -0.0189 0.0015  0.0345  278 ASP D CB  
14431 C CG  . ASP D 278 ? 0.3104 0.4476 0.4180 -0.0184 -0.0006 0.0369  278 ASP D CG  
14432 O OD1 . ASP D 278 ? 0.3605 0.5057 0.4932 -0.0232 0.0010  0.0406  278 ASP D OD1 
14433 O OD2 . ASP D 278 ? 0.3465 0.4874 0.4481 -0.0132 -0.0037 0.0352  278 ASP D OD2 
14434 N N   . GLU D 279 ? 0.2225 0.3626 0.3712 -0.0204 0.0213  0.0024  279 GLU D N   
14435 C CA  . GLU D 279 ? 0.2398 0.3670 0.3982 -0.0188 0.0323  0.0037  279 GLU D CA  
14436 C C   . GLU D 279 ? 0.2712 0.4036 0.4491 -0.0178 0.0320  0.0106  279 GLU D C   
14437 O O   . GLU D 279 ? 0.3358 0.4558 0.5179 -0.0162 0.0412  0.0115  279 GLU D O   
14438 C CB  . GLU D 279 ? 0.2705 0.3961 0.4384 -0.0184 0.0371  0.0015  279 GLU D CB  
14439 C CG  . GLU D 279 ? 0.3422 0.4490 0.5086 -0.0179 0.0513  -0.0007 279 GLU D CG  
14440 C CD  . GLU D 279 ? 0.4059 0.5111 0.5820 -0.0185 0.0571  -0.0025 279 GLU D CD  
14441 O OE1 . GLU D 279 ? 0.3935 0.5086 0.5714 -0.0195 0.0493  -0.0035 279 GLU D OE1 
14442 O OE2 . GLU D 279 ? 0.4619 0.5550 0.6440 -0.0183 0.0704  -0.0033 279 GLU D OE2 
14443 N N   . VAL D 280 ? 0.2734 0.4228 0.4628 -0.0189 0.0215  0.0156  280 VAL D N   
14444 C CA  . VAL D 280 ? 0.2764 0.4302 0.4850 -0.0181 0.0191  0.0234  280 VAL D CA  
14445 C C   . VAL D 280 ? 0.2621 0.4079 0.4594 -0.0185 0.0200  0.0251  280 VAL D C   
14446 O O   . VAL D 280 ? 0.1849 0.3237 0.3949 -0.0164 0.0243  0.0292  280 VAL D O   
14447 C CB  . VAL D 280 ? 0.3037 0.4756 0.5226 -0.0207 0.0058  0.0290  280 VAL D CB  
14448 C CG1 . VAL D 280 ? 0.3437 0.5187 0.5800 -0.0205 0.0009  0.0383  280 VAL D CG1 
14449 C CG2 . VAL D 280 ? 0.2980 0.4762 0.5318 -0.0206 0.0049  0.0282  280 VAL D CG2 
14450 N N   . ILE D 281 ? 0.2694 0.4163 0.4441 -0.0212 0.0158  0.0219  281 ILE D N   
14451 C CA  . ILE D 281 ? 0.2231 0.3620 0.3856 -0.0226 0.0164  0.0230  281 ILE D CA  
14452 C C   . ILE D 281 ? 0.2437 0.3615 0.4006 -0.0206 0.0284  0.0192  281 ILE D C   
14453 O O   . ILE D 281 ? 0.3162 0.4237 0.4759 -0.0201 0.0323  0.0220  281 ILE D O   
14454 C CB  . ILE D 281 ? 0.2537 0.3992 0.3959 -0.0260 0.0102  0.0197  281 ILE D CB  
14455 C CG1 . ILE D 281 ? 0.2955 0.4605 0.4403 -0.0288 0.0002  0.0220  281 ILE D CG1 
14456 C CG2 . ILE D 281 ? 0.2770 0.4150 0.4086 -0.0284 0.0103  0.0215  281 ILE D CG2 
14457 C CD1 . ILE D 281 ? 0.3429 0.5145 0.4983 -0.0309 -0.0059 0.0306  281 ILE D CD1 
14458 N N   . LEU D 282 ? 0.2677 0.3771 0.4146 -0.0200 0.0345  0.0127  282 LEU D N   
14459 C CA  . LEU D 282 ? 0.2713 0.3588 0.4102 -0.0192 0.0469  0.0088  282 LEU D CA  
14460 C C   . LEU D 282 ? 0.2610 0.3429 0.4221 -0.0160 0.0560  0.0119  282 LEU D C   
14461 O O   . LEU D 282 ? 0.2306 0.2976 0.3889 -0.0156 0.0627  0.0119  282 LEU D O   
14462 C CB  . LEU D 282 ? 0.2924 0.3724 0.4199 -0.0196 0.0515  0.0027  282 LEU D CB  
14463 C CG  . LEU D 282 ? 0.2793 0.3341 0.3918 -0.0206 0.0644  -0.0017 282 LEU D CG  
14464 C CD1 . LEU D 282 ? 0.2918 0.3330 0.3824 -0.0235 0.0629  -0.0028 282 LEU D CD1 
14465 C CD2 . LEU D 282 ? 0.3321 0.3793 0.4320 -0.0220 0.0675  -0.0066 282 LEU D CD2 
14466 N N   . LYS D 283 ? 0.3036 0.3973 0.4887 -0.0137 0.0558  0.0145  283 LYS D N   
14467 C CA  . LYS D 283 ? 0.3534 0.4436 0.5651 -0.0100 0.0647  0.0173  283 LYS D CA  
14468 C C   . LYS D 283 ? 0.3596 0.4497 0.5814 -0.0087 0.0607  0.0236  283 LYS D C   
14469 O O   . LYS D 283 ? 0.3553 0.4327 0.5884 -0.0057 0.0709  0.0236  283 LYS D O   
14470 C CB  . LYS D 283 ? 0.4035 0.5101 0.6420 -0.0084 0.0616  0.0205  283 LYS D CB  
14471 C CG  . LYS D 283 ? 0.5104 0.6169 0.7415 -0.0100 0.0654  0.0150  283 LYS D CG  
14472 C CD  . LYS D 283 ? 0.6132 0.6977 0.8293 -0.0103 0.0818  0.0081  283 LYS D CD  
14473 C CE  . LYS D 283 ? 0.6572 0.7361 0.8469 -0.0137 0.0805  0.0025  283 LYS D CE  
14474 N NZ  . LYS D 283 ? 0.6739 0.7549 0.8749 -0.0142 0.0864  0.0006  283 LYS D NZ  
14475 N N   . ASN D 284 ? 0.3617 0.4653 0.5795 -0.0112 0.0462  0.0287  284 ASN D N   
14476 C CA  . ASN D 284 ? 0.2869 0.3903 0.5119 -0.0111 0.0405  0.0356  284 ASN D CA  
14477 C C   . ASN D 284 ? 0.2988 0.3833 0.5034 -0.0125 0.0464  0.0325  284 ASN D C   
14478 O O   . ASN D 284 ? 0.3440 0.4215 0.5571 -0.0115 0.0463  0.0371  284 ASN D O   
14479 C CB  . ASN D 284 ? 0.2698 0.3914 0.4907 -0.0152 0.0242  0.0416  284 ASN D CB  
14480 C CG  . ASN D 284 ? 0.2173 0.3557 0.4618 -0.0146 0.0158  0.0475  284 ASN D CG  
14481 O OD1 . ASN D 284 ? 0.1738 0.3118 0.4431 -0.0105 0.0211  0.0486  284 ASN D OD1 
14482 N ND2 . ASN D 284 ? 0.2280 0.3808 0.4650 -0.0191 0.0025  0.0515  284 ASN D ND2 
14483 N N   . SER D 285 ? 0.2902 0.3654 0.4680 -0.0153 0.0502  0.0253  285 SER D N   
14484 C CA  . SER D 285 ? 0.3104 0.3694 0.4656 -0.0183 0.0521  0.0228  285 SER D CA  
14485 C C   . SER D 285 ? 0.3298 0.3636 0.4764 -0.0172 0.0675  0.0164  285 SER D C   
14486 O O   . SER D 285 ? 0.2935 0.3109 0.4302 -0.0186 0.0707  0.0159  285 SER D O   
14487 C CB  . SER D 285 ? 0.2829 0.3476 0.4136 -0.0230 0.0443  0.0197  285 SER D CB  
14488 O OG  . SER D 285 ? 0.3831 0.4702 0.5198 -0.0246 0.0320  0.0245  285 SER D OG  
14489 N N   . VAL D 286 ? 0.3346 0.3637 0.4831 -0.0154 0.0773  0.0114  286 VAL D N   
14490 C CA  . VAL D 286 ? 0.4258 0.4296 0.5627 -0.0155 0.0935  0.0046  286 VAL D CA  
14491 C C   . VAL D 286 ? 0.5054 0.5103 0.6674 -0.0110 0.1059  0.0034  286 VAL D C   
14492 O O   . VAL D 286 ? 0.4748 0.4988 0.6555 -0.0092 0.1012  0.0062  286 VAL D O   
14493 C CB  . VAL D 286 ? 0.4226 0.4134 0.5254 -0.0207 0.0943  -0.0018 286 VAL D CB  
14494 C CG1 . VAL D 286 ? 0.4193 0.4129 0.5019 -0.0251 0.0809  -0.0002 286 VAL D CG1 
14495 C CG2 . VAL D 286 ? 0.4440 0.4462 0.5494 -0.0203 0.0930  -0.0033 286 VAL D CG2 
14496 N N   . GLU D 287 ? 0.6265 0.6100 0.7888 -0.0097 0.1226  -0.0012 287 GLU D N   
14497 C CA  . GLU D 287 ? 0.6573 0.6379 0.8414 -0.0061 0.1386  -0.0042 287 GLU D CA  
14498 C C   . GLU D 287 ? 0.5700 0.5479 0.7384 -0.0096 0.1441  -0.0093 287 GLU D C   
14499 O O   . GLU D 287 ? 0.5146 0.5105 0.7034 -0.0079 0.1415  -0.0069 287 GLU D O   
14500 C CB  . GLU D 287 ? 0.7745 0.7298 0.9574 -0.0047 0.1569  -0.0095 287 GLU D CB  
14501 C CG  . GLU D 287 ? 0.8781 0.8306 1.0727 -0.0017 0.1522  -0.0051 287 GLU D CG  
14502 C CD  . GLU D 287 ? 0.9614 0.8825 1.1304 -0.0044 0.1642  -0.0120 287 GLU D CD  
14503 O OE1 . GLU D 287 ? 0.9891 0.8911 1.1237 -0.0102 0.1719  -0.0193 287 GLU D OE1 
14504 O OE2 . GLU D 287 ? 0.9800 0.8942 1.1622 -0.0011 0.1652  -0.0098 287 GLU D OE2 
14505 N N   . ARG D 288 ? 0.6621 0.6165 0.7937 -0.0151 0.1509  -0.0159 288 ARG D N   
14506 C CA  . ARG D 288 ? 0.7874 0.7334 0.8987 -0.0195 0.1567  -0.0207 288 ARG D CA  
14507 C C   . ARG D 288 ? 0.7596 0.7208 0.8583 -0.0218 0.1380  -0.0178 288 ARG D C   
14508 O O   . ARG D 288 ? 0.8107 0.7620 0.8790 -0.0263 0.1301  -0.0194 288 ARG D O   
14509 C CB  . ARG D 288 ? 0.9021 0.8149 0.9765 -0.0253 0.1695  -0.0280 288 ARG D CB  
14510 C CG  . ARG D 288 ? 0.9962 0.8901 1.0757 -0.0235 0.1859  -0.0317 288 ARG D CG  
14511 C CD  . ARG D 288 ? 1.0896 0.9484 1.1251 -0.0310 0.1958  -0.0391 288 ARG D CD  
14512 N NE  . ARG D 288 ? 1.1488 1.0012 1.1582 -0.0349 0.1802  -0.0374 288 ARG D NE  
14513 C CZ  . ARG D 288 ? 1.2036 1.0551 1.1852 -0.0405 0.1660  -0.0365 288 ARG D CZ  
14514 N NH1 . ARG D 288 ? 1.2203 1.0675 1.1832 -0.0439 0.1526  -0.0348 288 ARG D NH1 
14515 N NH2 . ARG D 288 ? 1.2086 1.0639 1.1828 -0.0427 0.1648  -0.0370 288 ARG D NH2 
14516 N N   . ALA D 289 ? 0.6488 0.6340 0.7721 -0.0189 0.1307  -0.0139 289 ALA D N   
14517 C CA  . ALA D 289 ? 0.6382 0.6417 0.7570 -0.0196 0.1122  -0.0107 289 ALA D CA  
14518 C C   . ALA D 289 ? 0.6080 0.6136 0.7202 -0.0217 0.1117  -0.0131 289 ALA D C   
14519 O O   . ALA D 289 ? 0.6348 0.6569 0.7706 -0.0196 0.1103  -0.0109 289 ALA D O   
14520 C CB  . ALA D 289 ? 0.6220 0.6506 0.7712 -0.0154 0.1017  -0.0039 289 ALA D CB  
14521 N N   . SER D 290 ? 0.5083 0.4966 0.5881 -0.0263 0.1115  -0.0171 290 SER D N   
14522 C CA  . SER D 290 ? 0.4577 0.4466 0.5288 -0.0286 0.1085  -0.0188 290 SER D CA  
14523 C C   . SER D 290 ? 0.3997 0.4010 0.4615 -0.0286 0.0904  -0.0176 290 SER D C   
14524 O O   . SER D 290 ? 0.4350 0.4282 0.4764 -0.0306 0.0841  -0.0183 290 SER D O   
14525 C CB  . SER D 290 ? 0.4268 0.3870 0.4683 -0.0342 0.1196  -0.0236 290 SER D CB  
14526 O OG  . SER D 290 ? 0.4421 0.4013 0.4709 -0.0368 0.1129  -0.0244 290 SER D OG  
14527 N N   . PRO D 291 ? 0.4209 0.4413 0.4974 -0.0267 0.0821  -0.0163 291 PRO D N   
14528 C CA  . PRO D 291 ? 0.3823 0.4143 0.4511 -0.0264 0.0666  -0.0163 291 PRO D CA  
14529 C C   . PRO D 291 ? 0.3308 0.3476 0.3743 -0.0295 0.0632  -0.0196 291 PRO D C   
14530 O O   . PRO D 291 ? 0.2962 0.3223 0.3358 -0.0286 0.0510  -0.0203 291 PRO D O   
14531 C CB  . PRO D 291 ? 0.3341 0.3882 0.4267 -0.0239 0.0612  -0.0145 291 PRO D CB  
14532 C CG  . PRO D 291 ? 0.3644 0.4113 0.4675 -0.0247 0.0736  -0.0150 291 PRO D CG  
14533 C CD  . PRO D 291 ? 0.3951 0.4255 0.4951 -0.0254 0.0873  -0.0153 291 PRO D CD  
14534 N N   . TYR D 292 ? 0.3909 0.3841 0.4170 -0.0333 0.0734  -0.0217 292 TYR D N   
14535 C CA  . TYR D 292 ? 0.3476 0.3250 0.3501 -0.0368 0.0692  -0.0238 292 TYR D CA  
14536 C C   . TYR D 292 ? 0.3364 0.2963 0.3114 -0.0403 0.0639  -0.0244 292 TYR D C   
14537 O O   . TYR D 292 ? 0.3656 0.3080 0.3179 -0.0442 0.0600  -0.0254 292 TYR D O   
14538 C CB  . TYR D 292 ? 0.3667 0.3274 0.3638 -0.0405 0.0827  -0.0252 292 TYR D CB  
14539 C CG  . TYR D 292 ? 0.3507 0.3295 0.3774 -0.0377 0.0871  -0.0241 292 TYR D CG  
14540 C CD1 . TYR D 292 ? 0.3916 0.3926 0.4351 -0.0341 0.0750  -0.0231 292 TYR D CD1 
14541 C CD2 . TYR D 292 ? 0.3675 0.3407 0.4055 -0.0391 0.1036  -0.0244 292 TYR D CD2 
14542 C CE1 . TYR D 292 ? 0.3573 0.3736 0.4264 -0.0326 0.0774  -0.0219 292 TYR D CE1 
14543 C CE2 . TYR D 292 ? 0.3802 0.3706 0.4474 -0.0370 0.1064  -0.0229 292 TYR D CE2 
14544 C CZ  . TYR D 292 ? 0.4049 0.4163 0.4867 -0.0341 0.0924  -0.0214 292 TYR D CZ  
14545 O OH  . TYR D 292 ? 0.5029 0.5304 0.6127 -0.0331 0.0939  -0.0196 292 TYR D OH  
14546 N N   . LEU D 293 ? 0.3789 0.3421 0.3552 -0.0396 0.0628  -0.0234 293 LEU D N   
14547 C CA  . LEU D 293 ? 0.3314 0.2779 0.2830 -0.0437 0.0578  -0.0237 293 LEU D CA  
14548 C C   . LEU D 293 ? 0.3108 0.2766 0.2696 -0.0412 0.0420  -0.0222 293 LEU D C   
14549 O O   . LEU D 293 ? 0.3165 0.3073 0.2988 -0.0365 0.0383  -0.0210 293 LEU D O   
14550 C CB  . LEU D 293 ? 0.4079 0.3428 0.3557 -0.0454 0.0686  -0.0239 293 LEU D CB  
14551 C CG  . LEU D 293 ? 0.5250 0.4331 0.4569 -0.0497 0.0859  -0.0268 293 LEU D CG  
14552 C CD1 . LEU D 293 ? 0.5727 0.4853 0.5203 -0.0480 0.0968  -0.0276 293 LEU D CD1 
14553 C CD2 . LEU D 293 ? 0.5390 0.4407 0.4742 -0.0495 0.0955  -0.0274 293 LEU D CD2 
14554 N N   . ARG D 294 ? 0.3612 0.3150 0.2995 -0.0448 0.0325  -0.0222 294 ARG D N   
14555 C CA  . ARG D 294 ? 0.3306 0.3004 0.2754 -0.0435 0.0197  -0.0209 294 ARG D CA  
14556 C C   . ARG D 294 ? 0.3410 0.3071 0.2832 -0.0458 0.0236  -0.0196 294 ARG D C   
14557 O O   . ARG D 294 ? 0.3636 0.3045 0.2832 -0.0512 0.0279  -0.0202 294 ARG D O   
14558 C CB  . ARG D 294 ? 0.2998 0.2594 0.2276 -0.0465 0.0066  -0.0209 294 ARG D CB  
14559 C CG  . ARG D 294 ? 0.3433 0.3224 0.2822 -0.0451 -0.0061 -0.0197 294 ARG D CG  
14560 C CD  . ARG D 294 ? 0.3211 0.2966 0.2532 -0.0458 -0.0204 -0.0197 294 ARG D CD  
14561 N NE  . ARG D 294 ? 0.3703 0.3151 0.2726 -0.0531 -0.0234 -0.0184 294 ARG D NE  
14562 C CZ  . ARG D 294 ? 0.3830 0.3087 0.2683 -0.0556 -0.0285 -0.0181 294 ARG D CZ  
14563 N NH1 . ARG D 294 ? 0.4587 0.3929 0.3554 -0.0508 -0.0313 -0.0192 294 ARG D NH1 
14564 N NH2 . ARG D 294 ? 0.4951 0.3915 0.3503 -0.0636 -0.0314 -0.0166 294 ARG D NH2 
14565 N N   . TYR D 295 ? 0.2723 0.2611 0.2358 -0.0424 0.0221  -0.0177 295 TYR D N   
14566 C CA  . TYR D 295 ? 0.3393 0.3255 0.3027 -0.0444 0.0252  -0.0158 295 TYR D CA  
14567 C C   . TYR D 295 ? 0.3306 0.3243 0.2906 -0.0470 0.0128  -0.0143 295 TYR D C   
14568 O O   . TYR D 295 ? 0.3453 0.3573 0.3148 -0.0450 0.0030  -0.0144 295 TYR D O   
14569 C CB  . TYR D 295 ? 0.3238 0.3284 0.3120 -0.0400 0.0308  -0.0135 295 TYR D CB  
14570 C CG  . TYR D 295 ? 0.2996 0.2950 0.2940 -0.0380 0.0446  -0.0144 295 TYR D CG  
14571 C CD1 . TYR D 295 ? 0.2815 0.2841 0.2857 -0.0352 0.0468  -0.0156 295 TYR D CD1 
14572 C CD2 . TYR D 295 ? 0.3446 0.3236 0.3361 -0.0391 0.0557  -0.0145 295 TYR D CD2 
14573 C CE1 . TYR D 295 ? 0.2591 0.2545 0.2716 -0.0338 0.0598  -0.0163 295 TYR D CE1 
14574 C CE2 . TYR D 295 ? 0.3232 0.2950 0.3240 -0.0370 0.0696  -0.0158 295 TYR D CE2 
14575 C CZ  . TYR D 295 ? 0.3229 0.3039 0.3349 -0.0345 0.0714  -0.0165 295 TYR D CZ  
14576 O OH  . TYR D 295 ? 0.4078 0.3837 0.4319 -0.0328 0.0852  -0.0175 295 TYR D OH  
14577 N N   . TYR D 296 ? 0.3299 0.3090 0.2771 -0.0517 0.0136  -0.0134 296 TYR D N   
14578 C CA  . TYR D 296 ? 0.3682 0.3542 0.3137 -0.0553 0.0025  -0.0114 296 TYR D CA  
14579 C C   . TYR D 296 ? 0.4002 0.3942 0.3570 -0.0554 0.0062  -0.0085 296 TYR D C   
14580 O O   . TYR D 296 ? 0.3735 0.3481 0.3206 -0.0578 0.0142  -0.0086 296 TYR D O   
14581 C CB  . TYR D 296 ? 0.4217 0.3811 0.3395 -0.0624 -0.0025 -0.0122 296 TYR D CB  
14582 C CG  . TYR D 296 ? 0.5327 0.4826 0.4377 -0.0634 -0.0093 -0.0137 296 TYR D CG  
14583 C CD1 . TYR D 296 ? 0.5179 0.4888 0.4395 -0.0584 -0.0166 -0.0140 296 TYR D CD1 
14584 C CD2 . TYR D 296 ? 0.6297 0.5473 0.5044 -0.0697 -0.0083 -0.0150 296 TYR D CD2 
14585 C CE1 . TYR D 296 ? 0.5428 0.5035 0.4535 -0.0590 -0.0237 -0.0149 296 TYR D CE1 
14586 C CE2 . TYR D 296 ? 0.6541 0.5610 0.5155 -0.0713 -0.0159 -0.0154 296 TYR D CE2 
14587 C CZ  . TYR D 296 ? 0.6114 0.5403 0.4922 -0.0655 -0.0239 -0.0150 296 TYR D CZ  
14588 O OH  . TYR D 296 ? 0.6054 0.5227 0.4743 -0.0667 -0.0322 -0.0149 296 TYR D OH  
14589 N N   . PHE D 297 ? 0.4019 0.4231 0.3783 -0.0534 0.0006  -0.0060 297 PHE D N   
14590 C CA  . PHE D 297 ? 0.2527 0.2819 0.2396 -0.0541 0.0028  -0.0021 297 PHE D CA  
14591 C C   . PHE D 297 ? 0.3503 0.3715 0.3260 -0.0608 -0.0034 -0.0005 297 PHE D C   
14592 O O   . PHE D 297 ? 0.3132 0.3483 0.2920 -0.0632 -0.0131 0.0002  297 PHE D O   
14593 C CB  . PHE D 297 ? 0.2299 0.2891 0.2383 -0.0509 -0.0005 0.0002  297 PHE D CB  
14594 C CG  . PHE D 297 ? 0.2575 0.3244 0.2750 -0.0527 0.0002  0.0053  297 PHE D CG  
14595 C CD1 . PHE D 297 ? 0.3219 0.3844 0.3480 -0.0498 0.0075  0.0078  297 PHE D CD1 
14596 C CD2 . PHE D 297 ? 0.2368 0.3154 0.2558 -0.0575 -0.0069 0.0080  297 PHE D CD2 
14597 C CE1 . PHE D 297 ? 0.2285 0.2970 0.2634 -0.0516 0.0066  0.0135  297 PHE D CE1 
14598 C CE2 . PHE D 297 ? 0.2805 0.3650 0.3065 -0.0600 -0.0068 0.0134  297 PHE D CE2 
14599 C CZ  . PHE D 297 ? 0.2413 0.3200 0.2746 -0.0570 -0.0006 0.0164  297 PHE D CZ  
14600 N N   . ARG D 298 ? 0.3370 0.3354 0.3007 -0.0638 0.0027  -0.0001 298 ARG D N   
14601 C CA  . ARG D 298 ? 0.3382 0.3243 0.2891 -0.0711 -0.0024 0.0014  298 ARG D CA  
14602 C C   . ARG D 298 ? 0.3758 0.3544 0.3107 -0.0762 -0.0126 -0.0004 298 ARG D C   
14603 O O   . ARG D 298 ? 0.3965 0.3759 0.3276 -0.0823 -0.0213 0.0016  298 ARG D O   
14604 C CB  . ARG D 298 ? 0.3175 0.3246 0.2845 -0.0727 -0.0071 0.0065  298 ARG D CB  
14605 C CG  . ARG D 298 ? 0.3773 0.3877 0.3582 -0.0685 0.0012  0.0095  298 ARG D CG  
14606 C CD  . ARG D 298 ? 0.3155 0.3446 0.3100 -0.0710 -0.0037 0.0155  298 ARG D CD  
14607 N NE  . ARG D 298 ? 0.3402 0.3682 0.3467 -0.0672 0.0028  0.0191  298 ARG D NE  
14608 C CZ  . ARG D 298 ? 0.3546 0.3928 0.3713 -0.0693 -0.0001 0.0254  298 ARG D CZ  
14609 N NH1 . ARG D 298 ? 0.3410 0.3920 0.3567 -0.0756 -0.0080 0.0283  298 ARG D NH1 
14610 N NH2 . ARG D 298 ? 0.3792 0.4145 0.4078 -0.0654 0.0045  0.0291  298 ARG D NH2 
14611 N N   . GLU D 299 ? 0.3410 0.3116 0.2670 -0.0741 -0.0123 -0.0038 299 GLU D N   
14612 C CA  . GLU D 299 ? 0.3752 0.3387 0.2877 -0.0783 -0.0236 -0.0047 299 GLU D CA  
14613 C C   . GLU D 299 ? 0.4217 0.4141 0.3535 -0.0781 -0.0359 -0.0025 299 GLU D C   
14614 O O   . GLU D 299 ? 0.4385 0.4277 0.3639 -0.0831 -0.0475 -0.0017 299 GLU D O   
14615 C CB  . GLU D 299 ? 0.4570 0.3892 0.3411 -0.0872 -0.0262 -0.0052 299 GLU D CB  
14616 C CG  . GLU D 299 ? 0.6650 0.5667 0.5289 -0.0883 -0.0119 -0.0084 299 GLU D CG  
14617 C CD  . GLU D 299 ? 0.9013 0.7818 0.7442 -0.0890 -0.0086 -0.0119 299 GLU D CD  
14618 O OE1 . GLU D 299 ? 0.9928 0.8875 0.8462 -0.0841 -0.0114 -0.0120 299 GLU D OE1 
14619 O OE2 . GLU D 299 ? 1.0197 0.8675 0.8338 -0.0952 -0.0029 -0.0147 299 GLU D OE2 
14620 N N   . LEU D 300 ? 0.3369 0.3574 0.2927 -0.0727 -0.0332 -0.0015 300 LEU D N   
14621 C CA  . LEU D 300 ? 0.3429 0.3923 0.3185 -0.0721 -0.0417 -0.0004 300 LEU D CA  
14622 C C   . LEU D 300 ? 0.3799 0.4463 0.3690 -0.0651 -0.0426 -0.0034 300 LEU D C   
14623 O O   . LEU D 300 ? 0.3668 0.4452 0.3646 -0.0646 -0.0516 -0.0044 300 LEU D O   
14624 C CB  . LEU D 300 ? 0.3160 0.3846 0.3066 -0.0729 -0.0383 0.0028  300 LEU D CB  
14625 C CG  . LEU D 300 ? 0.2644 0.3196 0.2458 -0.0796 -0.0373 0.0063  300 LEU D CG  
14626 C CD1 . LEU D 300 ? 0.2504 0.3266 0.2479 -0.0800 -0.0346 0.0102  300 LEU D CD1 
14627 C CD2 . LEU D 300 ? 0.3707 0.4180 0.3431 -0.0872 -0.0480 0.0072  300 LEU D CD2 
14628 N N   . ILE D 301 ? 0.4232 0.4910 0.4159 -0.0595 -0.0338 -0.0050 301 ILE D N   
14629 C CA  . ILE D 301 ? 0.3056 0.3907 0.3121 -0.0531 -0.0339 -0.0079 301 ILE D CA  
14630 C C   . ILE D 301 ? 0.3114 0.3815 0.3102 -0.0495 -0.0261 -0.0097 301 ILE D C   
14631 O O   . ILE D 301 ? 0.3792 0.4361 0.3714 -0.0503 -0.0177 -0.0084 301 ILE D O   
14632 C CB  . ILE D 301 ? 0.2499 0.3636 0.2762 -0.0513 -0.0317 -0.0072 301 ILE D CB  
14633 C CG1 . ILE D 301 ? 0.2224 0.3520 0.2610 -0.0451 -0.0307 -0.0110 301 ILE D CG1 
14634 C CG2 . ILE D 301 ? 0.2301 0.3404 0.2557 -0.0523 -0.0239 -0.0037 301 ILE D CG2 
14635 C CD1 . ILE D 301 ? 0.1953 0.3525 0.2501 -0.0448 -0.0289 -0.0109 301 ILE D CD1 
14636 N N   . SER D 302 ? 0.3050 0.3767 0.3058 -0.0455 -0.0286 -0.0128 302 SER D N   
14637 C CA  . SER D 302 ? 0.3286 0.3872 0.3231 -0.0426 -0.0215 -0.0146 302 SER D CA  
14638 C C   . SER D 302 ? 0.3109 0.3876 0.3224 -0.0380 -0.0152 -0.0150 302 SER D C   
14639 O O   . SER D 302 ? 0.2632 0.3632 0.2900 -0.0359 -0.0184 -0.0157 302 SER D O   
14640 C CB  . SER D 302 ? 0.2929 0.3435 0.2813 -0.0411 -0.0281 -0.0171 302 SER D CB  
14641 O OG  . SER D 302 ? 0.3445 0.3755 0.3148 -0.0463 -0.0352 -0.0158 302 SER D OG  
14642 N N   . VAL D 303 ? 0.3063 0.3717 0.3151 -0.0370 -0.0059 -0.0146 303 VAL D N   
14643 C CA  . VAL D 303 ? 0.2776 0.3576 0.3024 -0.0336 -0.0005 -0.0140 303 VAL D CA  
14644 C C   . VAL D 303 ? 0.2752 0.3433 0.2976 -0.0315 0.0058  -0.0158 303 VAL D C   
14645 O O   . VAL D 303 ? 0.2927 0.3395 0.3033 -0.0334 0.0130  -0.0157 303 VAL D O   
14646 C CB  . VAL D 303 ? 0.3374 0.4195 0.3684 -0.0349 0.0046  -0.0098 303 VAL D CB  
14647 C CG1 . VAL D 303 ? 0.2817 0.3789 0.3299 -0.0318 0.0077  -0.0082 303 VAL D CG1 
14648 C CG2 . VAL D 303 ? 0.2771 0.3702 0.3094 -0.0382 -0.0015 -0.0073 303 VAL D CG2 
14649 N N   . PHE D 304 ? 0.2544 0.3352 0.2869 -0.0282 0.0037  -0.0180 304 PHE D N   
14650 C CA  . PHE D 304 ? 0.2041 0.2780 0.2389 -0.0265 0.0098  -0.0191 304 PHE D CA  
14651 C C   . PHE D 304 ? 0.2774 0.3673 0.3310 -0.0246 0.0133  -0.0170 304 PHE D C   
14652 O O   . PHE D 304 ? 0.3113 0.4205 0.3748 -0.0241 0.0083  -0.0160 304 PHE D O   
14653 C CB  . PHE D 304 ? 0.1991 0.2736 0.2317 -0.0247 0.0041  -0.0229 304 PHE D CB  
14654 C CG  . PHE D 304 ? 0.2214 0.2745 0.2349 -0.0270 0.0014  -0.0239 304 PHE D CG  
14655 C CD1 . PHE D 304 ? 0.2644 0.2949 0.2644 -0.0295 0.0089  -0.0236 304 PHE D CD1 
14656 C CD2 . PHE D 304 ? 0.2436 0.2988 0.2526 -0.0271 -0.0088 -0.0248 304 PHE D CD2 
14657 C CE1 . PHE D 304 ? 0.3216 0.3300 0.3002 -0.0330 0.0056  -0.0240 304 PHE D CE1 
14658 C CE2 . PHE D 304 ? 0.3039 0.3379 0.2945 -0.0299 -0.0135 -0.0247 304 PHE D CE2 
14659 C CZ  . PHE D 304 ? 0.3335 0.3432 0.3070 -0.0332 -0.0066 -0.0241 304 PHE D CZ  
14660 N N   . PHE D 305 ? 0.3009 0.3826 0.3593 -0.0243 0.0218  -0.0159 305 PHE D N   
14661 C CA  . PHE D 305 ? 0.2526 0.3484 0.3309 -0.0228 0.0238  -0.0131 305 PHE D CA  
14662 C C   . PHE D 305 ? 0.2728 0.3713 0.3574 -0.0216 0.0241  -0.0154 305 PHE D C   
14663 O O   . PHE D 305 ? 0.2896 0.3724 0.3675 -0.0223 0.0302  -0.0171 305 PHE D O   
14664 C CB  . PHE D 305 ? 0.1938 0.2804 0.2789 -0.0229 0.0333  -0.0097 305 PHE D CB  
14665 C CG  . PHE D 305 ? 0.2438 0.3274 0.3239 -0.0243 0.0326  -0.0071 305 PHE D CG  
14666 C CD1 . PHE D 305 ? 0.2639 0.3637 0.3565 -0.0242 0.0274  -0.0026 305 PHE D CD1 
14667 C CD2 . PHE D 305 ? 0.2500 0.3136 0.3112 -0.0267 0.0362  -0.0089 305 PHE D CD2 
14668 C CE1 . PHE D 305 ? 0.2858 0.3821 0.3736 -0.0260 0.0265  0.0002  305 PHE D CE1 
14669 C CE2 . PHE D 305 ? 0.2934 0.3533 0.3496 -0.0286 0.0351  -0.0066 305 PHE D CE2 
14670 C CZ  . PHE D 305 ? 0.3351 0.4116 0.4051 -0.0281 0.0303  -0.0021 305 PHE D CZ  
14671 N N   . ARG D 306 ? 0.2247 0.3417 0.3202 -0.0206 0.0175  -0.0155 306 ARG D N   
14672 C CA  . ARG D 306 ? 0.2281 0.3474 0.3287 -0.0200 0.0164  -0.0182 306 ARG D CA  
14673 C C   . ARG D 306 ? 0.2147 0.3288 0.3280 -0.0205 0.0245  -0.0155 306 ARG D C   
14674 O O   . ARG D 306 ? 0.3336 0.4496 0.4584 -0.0204 0.0289  -0.0112 306 ARG D O   
14675 C CB  . ARG D 306 ? 0.2467 0.3856 0.3550 -0.0198 0.0081  -0.0192 306 ARG D CB  
14676 C CG  . ARG D 306 ? 0.2504 0.4021 0.3748 -0.0209 0.0069  -0.0141 306 ARG D CG  
14677 C CD  . ARG D 306 ? 0.2564 0.4240 0.3839 -0.0222 -0.0012 -0.0159 306 ARG D CD  
14678 N NE  . ARG D 306 ? 0.2118 0.3897 0.3535 -0.0242 -0.0040 -0.0098 306 ARG D NE  
14679 C CZ  . ARG D 306 ? 0.1973 0.3853 0.3456 -0.0265 -0.0102 -0.0095 306 ARG D CZ  
14680 N NH1 . ARG D 306 ? 0.2481 0.4372 0.3898 -0.0268 -0.0132 -0.0158 306 ARG D NH1 
14681 N NH2 . ARG D 306 ? 0.2656 0.4615 0.4271 -0.0287 -0.0140 -0.0026 306 ARG D NH2 
14682 N N   . ASP D 307 ? 0.2085 0.3157 0.3209 -0.0210 0.0267  -0.0181 307 ASP D N   
14683 C CA  . ASP D 307 ? 0.2480 0.3540 0.3761 -0.0219 0.0337  -0.0161 307 ASP D CA  
14684 C C   . ASP D 307 ? 0.2543 0.3800 0.4009 -0.0219 0.0262  -0.0139 307 ASP D C   
14685 O O   . ASP D 307 ? 0.2100 0.3410 0.3550 -0.0226 0.0197  -0.0169 307 ASP D O   
14686 C CB  . ASP D 307 ? 0.2593 0.3502 0.3779 -0.0236 0.0381  -0.0193 307 ASP D CB  
14687 C CG  . ASP D 307 ? 0.3661 0.4551 0.5014 -0.0253 0.0474  -0.0173 307 ASP D CG  
14688 O OD1 . ASP D 307 ? 0.3653 0.4704 0.5227 -0.0251 0.0441  -0.0146 307 ASP D OD1 
14689 O OD2 . ASP D 307 ? 0.3009 0.3721 0.4272 -0.0275 0.0579  -0.0184 307 ASP D OD2 
14690 N N   . LYS D 308 ? 0.2527 0.3879 0.4163 -0.0216 0.0266  -0.0086 308 LYS D N   
14691 C CA  . LYS D 308 ? 0.2037 0.3569 0.3827 -0.0226 0.0174  -0.0053 308 LYS D CA  
14692 C C   . LYS D 308 ? 0.1753 0.3313 0.3663 -0.0245 0.0165  -0.0060 308 LYS D C   
14693 O O   . LYS D 308 ? 0.1620 0.3272 0.3518 -0.0263 0.0073  -0.0076 308 LYS D O   
14694 C CB  . LYS D 308 ? 0.1446 0.3045 0.3415 -0.0220 0.0180  0.0019  308 LYS D CB  
14695 C CG  . LYS D 308 ? 0.1841 0.3616 0.3944 -0.0241 0.0061  0.0069  308 LYS D CG  
14696 C CD  . LYS D 308 ? 0.2549 0.4365 0.4890 -0.0231 0.0069  0.0150  308 LYS D CD  
14697 C CE  . LYS D 308 ? 0.2977 0.4949 0.5420 -0.0262 -0.0069 0.0214  308 LYS D CE  
14698 N NZ  . LYS D 308 ? 0.2613 0.4655 0.4950 -0.0300 -0.0157 0.0176  308 LYS D NZ  
14699 N N   . THR D 309 ? 0.1862 0.3339 0.3890 -0.0246 0.0267  -0.0049 309 THR D N   
14700 C CA  . THR D 309 ? 0.2054 0.3555 0.4224 -0.0271 0.0270  -0.0049 309 THR D CA  
14701 C C   . THR D 309 ? 0.2199 0.3659 0.4199 -0.0288 0.0215  -0.0108 309 THR D C   
14702 O O   . THR D 309 ? 0.2121 0.3669 0.4195 -0.0312 0.0134  -0.0110 309 THR D O   
14703 C CB  . THR D 309 ? 0.3173 0.4560 0.5445 -0.0273 0.0420  -0.0043 309 THR D CB  
14704 O OG1 . THR D 309 ? 0.3521 0.4961 0.6008 -0.0252 0.0471  0.0010  309 THR D OG1 
14705 C CG2 . THR D 309 ? 0.3578 0.4979 0.5986 -0.0307 0.0434  -0.0046 309 THR D CG2 
14706 N N   . LEU D 310 ? 0.1837 0.3149 0.3611 -0.0277 0.0252  -0.0154 310 LEU D N   
14707 C CA  . LEU D 310 ? 0.1947 0.3197 0.3577 -0.0286 0.0202  -0.0208 310 LEU D CA  
14708 C C   . LEU D 310 ? 0.1998 0.3373 0.3576 -0.0278 0.0081  -0.0237 310 LEU D C   
14709 O O   . LEU D 310 ? 0.1955 0.3354 0.3531 -0.0294 0.0020  -0.0269 310 LEU D O   
14710 C CB  . LEU D 310 ? 0.1905 0.2964 0.3310 -0.0277 0.0251  -0.0241 310 LEU D CB  
14711 C CG  . LEU D 310 ? 0.3014 0.3899 0.4396 -0.0303 0.0375  -0.0230 310 LEU D CG  
14712 C CD1 . LEU D 310 ? 0.3533 0.4219 0.4651 -0.0303 0.0394  -0.0256 310 LEU D CD1 
14713 C CD2 . LEU D 310 ? 0.2465 0.3336 0.3946 -0.0339 0.0387  -0.0233 310 LEU D CD2 
14714 N N   . SER D 311 ? 0.1565 0.3007 0.3088 -0.0258 0.0055  -0.0229 311 SER D N   
14715 C CA  . SER D 311 ? 0.1522 0.3088 0.2993 -0.0257 -0.0039 -0.0257 311 SER D CA  
14716 C C   . SER D 311 ? 0.1499 0.3195 0.3105 -0.0292 -0.0106 -0.0231 311 SER D C   
14717 O O   . SER D 311 ? 0.1750 0.3494 0.3300 -0.0308 -0.0175 -0.0276 311 SER D O   
14718 C CB  . SER D 311 ? 0.2232 0.3852 0.3645 -0.0241 -0.0042 -0.0238 311 SER D CB  
14719 O OG  . SER D 311 ? 0.2456 0.3952 0.3747 -0.0218 0.0007  -0.0255 311 SER D OG  
14720 N N   . ASP D 312 ? 0.2392 0.4139 0.4181 -0.0306 -0.0089 -0.0160 312 ASP D N   
14721 C CA  . ASP D 312 ? 0.2267 0.4138 0.4197 -0.0346 -0.0173 -0.0122 312 ASP D CA  
14722 C C   . ASP D 312 ? 0.2356 0.4199 0.4350 -0.0376 -0.0192 -0.0146 312 ASP D C   
14723 O O   . ASP D 312 ? 0.2813 0.4739 0.4848 -0.0418 -0.0286 -0.0141 312 ASP D O   
14724 C CB  . ASP D 312 ? 0.1425 0.3360 0.3575 -0.0348 -0.0159 -0.0032 312 ASP D CB  
14725 C CG  . ASP D 312 ? 0.2154 0.4140 0.4254 -0.0335 -0.0179 0.0005  312 ASP D CG  
14726 O OD1 . ASP D 312 ? 0.2378 0.4385 0.4288 -0.0336 -0.0215 -0.0032 312 ASP D OD1 
14727 O OD2 . ASP D 312 ? 0.1962 0.3969 0.4230 -0.0324 -0.0156 0.0074  312 ASP D OD2 
14728 N N   . LEU D 313 ? 0.1990 0.3707 0.3982 -0.0364 -0.0106 -0.0168 313 LEU D N   
14729 C CA  . LEU D 313 ? 0.2182 0.3857 0.4220 -0.0399 -0.0121 -0.0191 313 LEU D CA  
14730 C C   . LEU D 313 ? 0.2365 0.4033 0.4235 -0.0409 -0.0208 -0.0263 313 LEU D C   
14731 O O   . LEU D 313 ? 0.2651 0.4361 0.4571 -0.0454 -0.0283 -0.0272 313 LEU D O   
14732 C CB  . LEU D 313 ? 0.2200 0.3714 0.4205 -0.0390 -0.0010 -0.0206 313 LEU D CB  
14733 C CG  . LEU D 313 ? 0.1966 0.3477 0.4187 -0.0402 0.0090  -0.0149 313 LEU D CG  
14734 C CD1 . LEU D 313 ? 0.2100 0.3421 0.4201 -0.0398 0.0212  -0.0172 313 LEU D CD1 
14735 C CD2 . LEU D 313 ? 0.1663 0.3265 0.4115 -0.0451 0.0047  -0.0117 313 LEU D CD2 
14736 N N   . ILE D 314 ? 0.2045 0.3654 0.3723 -0.0370 -0.0197 -0.0319 314 ILE D N   
14737 C CA  . ILE D 314 ? 0.2268 0.3867 0.3801 -0.0369 -0.0264 -0.0397 314 ILE D CA  
14738 C C   . ILE D 314 ? 0.2684 0.4427 0.4206 -0.0399 -0.0345 -0.0397 314 ILE D C   
14739 O O   . ILE D 314 ? 0.2594 0.4352 0.4080 -0.0436 -0.0413 -0.0437 314 ILE D O   
14740 C CB  . ILE D 314 ? 0.1943 0.3458 0.3317 -0.0315 -0.0231 -0.0450 314 ILE D CB  
14741 C CG1 . ILE D 314 ? 0.1775 0.3119 0.3125 -0.0303 -0.0166 -0.0446 314 ILE D CG1 
14742 C CG2 . ILE D 314 ? 0.2211 0.3736 0.3465 -0.0303 -0.0288 -0.0538 314 ILE D CG2 
14743 C CD1 . ILE D 314 ? 0.2112 0.3361 0.3314 -0.0255 -0.0153 -0.0483 314 ILE D CD1 
14744 N N   . GLY D 315 ? 0.2282 0.4117 0.3823 -0.0391 -0.0340 -0.0348 315 GLY D N   
14745 C CA  . GLY D 315 ? 0.2824 0.4777 0.4310 -0.0427 -0.0416 -0.0344 315 GLY D CA  
14746 C C   . GLY D 315 ? 0.2433 0.4460 0.4041 -0.0491 -0.0499 -0.0285 315 GLY D C   
14747 O O   . GLY D 315 ? 0.2616 0.4701 0.4131 -0.0541 -0.0580 -0.0303 315 GLY D O   
14748 N N   . PHE D 316 ? 0.2011 0.4037 0.3829 -0.0497 -0.0482 -0.0214 316 PHE D N   
14749 C CA  . PHE D 316 ? 0.2141 0.4257 0.4130 -0.0555 -0.0571 -0.0138 316 PHE D CA  
14750 C C   . PHE D 316 ? 0.2376 0.4465 0.4525 -0.0589 -0.0587 -0.0130 316 PHE D C   
14751 O O   . PHE D 316 ? 0.2139 0.4293 0.4371 -0.0653 -0.0696 -0.0094 316 PHE D O   
14752 C CB  . PHE D 316 ? 0.2977 0.5159 0.5155 -0.0536 -0.0549 -0.0037 316 PHE D CB  
14753 C CG  . PHE D 316 ? 0.4184 0.6405 0.6236 -0.0519 -0.0552 -0.0022 316 PHE D CG  
14754 C CD1 . PHE D 316 ? 0.4872 0.7121 0.6699 -0.0549 -0.0611 -0.0070 316 PHE D CD1 
14755 C CD2 . PHE D 316 ? 0.4559 0.6782 0.6718 -0.0477 -0.0488 0.0036  316 PHE D CD2 
14756 C CE1 . PHE D 316 ? 0.5075 0.7364 0.6791 -0.0543 -0.0607 -0.0052 316 PHE D CE1 
14757 C CE2 . PHE D 316 ? 0.4856 0.7108 0.6899 -0.0468 -0.0494 0.0054  316 PHE D CE2 
14758 C CZ  . PHE D 316 ? 0.4958 0.7249 0.6784 -0.0504 -0.0554 0.0013  316 PHE D CZ  
14759 N N   . SER D 317 ? 0.1690 0.3683 0.3886 -0.0557 -0.0488 -0.0154 317 SER D N   
14760 C CA  . SER D 317 ? 0.2481 0.4460 0.4872 -0.0595 -0.0488 -0.0129 317 SER D CA  
14761 C C   . SER D 317 ? 0.2751 0.4624 0.5012 -0.0620 -0.0506 -0.0209 317 SER D C   
14762 O O   . SER D 317 ? 0.2659 0.4557 0.4985 -0.0684 -0.0595 -0.0206 317 SER D O   
14763 C CB  . SER D 317 ? 0.2559 0.4501 0.5126 -0.0559 -0.0355 -0.0086 317 SER D CB  
14764 O OG  . SER D 317 ? 0.3094 0.5089 0.5938 -0.0602 -0.0362 -0.0032 317 SER D OG  
14765 N N   . TYR D 318 ? 0.2503 0.4251 0.4581 -0.0574 -0.0434 -0.0279 318 TYR D N   
14766 C CA  . TYR D 318 ? 0.1924 0.3539 0.3915 -0.0589 -0.0430 -0.0343 318 TYR D CA  
14767 C C   . TYR D 318 ? 0.2711 0.4323 0.4592 -0.0634 -0.0542 -0.0404 318 TYR D C   
14768 O O   . TYR D 318 ? 0.2127 0.3641 0.3996 -0.0666 -0.0559 -0.0441 318 TYR D O   
14769 C CB  . TYR D 318 ? 0.2836 0.4318 0.4643 -0.0525 -0.0355 -0.0399 318 TYR D CB  
14770 C CG  . TYR D 318 ? 0.1900 0.3308 0.3773 -0.0503 -0.0239 -0.0355 318 TYR D CG  
14771 C CD1 . TYR D 318 ? 0.2541 0.3973 0.4630 -0.0541 -0.0189 -0.0290 318 TYR D CD1 
14772 C CD2 . TYR D 318 ? 0.1963 0.3272 0.3683 -0.0449 -0.0176 -0.0379 318 TYR D CD2 
14773 C CE1 . TYR D 318 ? 0.2711 0.4059 0.4839 -0.0527 -0.0061 -0.0260 318 TYR D CE1 
14774 C CE2 . TYR D 318 ? 0.2190 0.3404 0.3929 -0.0440 -0.0068 -0.0343 318 TYR D CE2 
14775 C CZ  . TYR D 318 ? 0.2633 0.3862 0.4564 -0.0480 -0.0002 -0.0288 318 TYR D CZ  
14776 O OH  . TYR D 318 ? 0.3188 0.4308 0.5114 -0.0476 0.0124  -0.0262 318 TYR D OH  
14777 N N   . HIS D 319 ? 0.2738 0.4440 0.4523 -0.0644 -0.0614 -0.0419 319 HIS D N   
14778 C CA  . HIS D 319 ? 0.3345 0.5026 0.4989 -0.0694 -0.0709 -0.0489 319 HIS D CA  
14779 C C   . HIS D 319 ? 0.3537 0.5211 0.5308 -0.0777 -0.0787 -0.0463 319 HIS D C   
14780 O O   . HIS D 319 ? 0.4972 0.6563 0.6621 -0.0816 -0.0845 -0.0536 319 HIS D O   
14781 C CB  . HIS D 319 ? 0.2955 0.4743 0.4486 -0.0714 -0.0771 -0.0489 319 HIS D CB  
14782 C CG  . HIS D 319 ? 0.3502 0.5416 0.5196 -0.0772 -0.0849 -0.0382 319 HIS D CG  
14783 N ND1 . HIS D 319 ? 0.3589 0.5529 0.5311 -0.0864 -0.0973 -0.0362 319 HIS D ND1 
14784 C CD2 . HIS D 319 ? 0.3490 0.5503 0.5333 -0.0752 -0.0831 -0.0286 319 HIS D CD2 
14785 C CE1 . HIS D 319 ? 0.3408 0.5465 0.5305 -0.0896 -0.1035 -0.0252 319 HIS D CE1 
14786 N NE2 . HIS D 319 ? 0.3644 0.5747 0.5621 -0.0826 -0.0947 -0.0207 319 HIS D NE2 
14787 N N   . ALA D 320 ? 0.3334 0.5090 0.5359 -0.0804 -0.0789 -0.0363 320 ALA D N   
14788 C CA  . ALA D 320 ? 0.3305 0.5078 0.5502 -0.0887 -0.0866 -0.0324 320 ALA D CA  
14789 C C   . ALA D 320 ? 0.3661 0.5342 0.5986 -0.0885 -0.0780 -0.0319 320 ALA D C   
14790 O O   . ALA D 320 ? 0.4108 0.5814 0.6623 -0.0955 -0.0825 -0.0277 320 ALA D O   
14791 C CB  . ALA D 320 ? 0.3726 0.5663 0.6166 -0.0926 -0.0934 -0.0211 320 ALA D CB  
14792 N N   . TRP D 321 ? 0.3496 0.5069 0.5719 -0.0816 -0.0662 -0.0357 321 TRP D N   
14793 C CA  . TRP D 321 ? 0.3763 0.5223 0.6061 -0.0821 -0.0572 -0.0350 321 TRP D CA  
14794 C C   . TRP D 321 ? 0.3698 0.4980 0.5788 -0.0826 -0.0592 -0.0441 321 TRP D C   
14795 O O   . TRP D 321 ? 0.4196 0.5423 0.6070 -0.0780 -0.0615 -0.0517 321 TRP D O   
14796 C CB  . TRP D 321 ? 0.3661 0.5086 0.5963 -0.0753 -0.0432 -0.0325 321 TRP D CB  
14797 C CG  . TRP D 321 ? 0.3941 0.5506 0.6454 -0.0736 -0.0382 -0.0241 321 TRP D CG  
14798 C CD1 . TRP D 321 ? 0.3749 0.5471 0.6353 -0.0737 -0.0457 -0.0197 321 TRP D CD1 
14799 C CD2 . TRP D 321 ? 0.3692 0.5233 0.6337 -0.0715 -0.0242 -0.0195 321 TRP D CD2 
14800 N NE1 . TRP D 321 ? 0.3959 0.5760 0.6771 -0.0710 -0.0375 -0.0124 321 TRP D NE1 
14801 C CE2 . TRP D 321 ? 0.3872 0.5565 0.6713 -0.0696 -0.0235 -0.0127 321 TRP D CE2 
14802 C CE3 . TRP D 321 ? 0.3967 0.5359 0.6572 -0.0716 -0.0118 -0.0204 321 TRP D CE3 
14803 C CZ2 . TRP D 321 ? 0.4199 0.5902 0.7208 -0.0671 -0.0100 -0.0079 321 TRP D CZ2 
14804 C CZ3 . TRP D 321 ? 0.4073 0.5472 0.6820 -0.0701 0.0019  -0.0156 321 TRP D CZ3 
14805 C CH2 . TRP D 321 ? 0.4250 0.5806 0.7205 -0.0675 0.0033  -0.0099 321 TRP D CH2 
14806 N N   . ASN D 322 ? 0.3728 0.4918 0.5899 -0.0880 -0.0579 -0.0432 322 ASN D N   
14807 C CA  . ASN D 322 ? 0.3883 0.4868 0.5874 -0.0873 -0.0568 -0.0502 322 ASN D CA  
14808 C C   . ASN D 322 ? 0.3747 0.4636 0.5582 -0.0785 -0.0477 -0.0524 322 ASN D C   
14809 O O   . ASN D 322 ? 0.4528 0.5453 0.6437 -0.0759 -0.0381 -0.0467 322 ASN D O   
14810 C CB  . ASN D 322 ? 0.4815 0.5717 0.6940 -0.0948 -0.0536 -0.0464 322 ASN D CB  
14811 C CG  . ASN D 322 ? 0.5363 0.6031 0.7303 -0.0946 -0.0529 -0.0524 322 ASN D CG  
14812 O OD1 . ASN D 322 ? 0.5604 0.6147 0.7458 -0.0909 -0.0437 -0.0515 322 ASN D OD1 
14813 N ND2 . ASN D 322 ? 0.5368 0.5957 0.7232 -0.0990 -0.0631 -0.0584 322 ASN D ND2 
14814 N N   . ALA D 323 ? 0.2918 0.3996 0.5710 -0.1073 -0.0049 -0.0203 323 ALA D N   
14815 C CA  . ALA D 323 ? 0.2912 0.3863 0.5547 -0.1032 0.0021  -0.0174 323 ALA D CA  
14816 C C   . ALA D 323 ? 0.3257 0.4183 0.5828 -0.1103 0.0154  -0.0085 323 ALA D C   
14817 O O   . ALA D 323 ? 0.3121 0.4068 0.5613 -0.1045 0.0249  -0.0054 323 ALA D O   
14818 C CB  . ALA D 323 ? 0.2870 0.3584 0.5403 -0.1031 -0.0081 -0.0214 323 ALA D CB  
14819 N N   . GLU D 324 ? 0.3284 0.4160 0.5880 -0.1231 0.0158  -0.0041 324 GLU D N   
14820 C CA  . GLU D 324 ? 0.4238 0.5078 0.6754 -0.1302 0.0281  0.0047  324 GLU D CA  
14821 C C   . GLU D 324 ? 0.3589 0.4690 0.6193 -0.1258 0.0395  0.0077  324 GLU D C   
14822 O O   . GLU D 324 ? 0.3243 0.4323 0.5744 -0.1225 0.0502  0.0123  324 GLU D O   
14823 C CB  . GLU D 324 ? 0.5373 0.6113 0.7895 -0.1465 0.0257  0.0092  324 GLU D CB  
14824 C CG  . GLU D 324 ? 0.6890 0.7316 0.9290 -0.1501 0.0136  0.0060  324 GLU D CG  
14825 C CD  . GLU D 324 ? 0.8200 0.8461 1.0551 -0.1671 0.0117  0.0109  324 GLU D CD  
14826 O OE1 . GLU D 324 ? 0.8727 0.9002 1.1180 -0.1741 0.0021  0.0068  324 GLU D OE1 
14827 O OE2 . GLU D 324 ? 0.8595 0.8699 1.0794 -0.1735 0.0197  0.0186  324 GLU D OE2 
14828 N N   . ASP D 325 ? 0.3192 0.4530 0.5980 -0.1244 0.0365  0.0043  325 ASP D N   
14829 C CA  . ASP D 325 ? 0.3539 0.5134 0.6425 -0.1183 0.0459  0.0057  325 ASP D CA  
14830 C C   . ASP D 325 ? 0.3552 0.5126 0.6342 -0.1038 0.0496  0.0031  325 ASP D C   
14831 O O   . ASP D 325 ? 0.3593 0.5246 0.6354 -0.0991 0.0604  0.0062  325 ASP D O   
14832 C CB  . ASP D 325 ? 0.4361 0.6202 0.7465 -0.1183 0.0396  0.0014  325 ASP D CB  
14833 C CG  . ASP D 325 ? 0.5292 0.7175 0.8506 -0.1345 0.0356  0.0040  325 ASP D CG  
14834 O OD1 . ASP D 325 ? 0.5722 0.7503 0.8859 -0.1461 0.0415  0.0111  325 ASP D OD1 
14835 O OD2 . ASP D 325 ? 0.5760 0.7773 0.9131 -0.1361 0.0263  -0.0009 325 ASP D OD2 
14836 N N   . ALA D 326 ? 0.2863 0.4336 0.5603 -0.0969 0.0406  -0.0027 326 ALA D N   
14837 C CA  . ALA D 326 ? 0.2395 0.3846 0.5045 -0.0852 0.0432  -0.0047 326 ALA D CA  
14838 C C   . ALA D 326 ? 0.2279 0.3555 0.4747 -0.0856 0.0511  0.0001  326 ALA D C   
14839 O O   . ALA D 326 ? 0.2165 0.3462 0.4576 -0.0789 0.0586  0.0012  326 ALA D O   
14840 C CB  . ALA D 326 ? 0.2309 0.3711 0.4947 -0.0792 0.0320  -0.0110 326 ALA D CB  
14841 N N   . VAL D 327 ? 0.1905 0.2992 0.4279 -0.0931 0.0490  0.0023  327 VAL D N   
14842 C CA  . VAL D 327 ? 0.2660 0.3571 0.4858 -0.0935 0.0559  0.0068  327 VAL D CA  
14843 C C   . VAL D 327 ? 0.2732 0.3705 0.4915 -0.0960 0.0686  0.0129  327 VAL D C   
14844 O O   . VAL D 327 ? 0.3059 0.3985 0.5132 -0.0906 0.0766  0.0150  327 VAL D O   
14845 C CB  . VAL D 327 ? 0.2771 0.3457 0.4878 -0.1006 0.0501  0.0075  327 VAL D CB  
14846 C CG1 . VAL D 327 ? 0.3089 0.3584 0.5006 -0.1008 0.0573  0.0122  327 VAL D CG1 
14847 C CG2 . VAL D 327 ? 0.2690 0.3334 0.4818 -0.0962 0.0382  0.0005  327 VAL D CG2 
14848 N N   . ARG D 328 ? 0.2907 0.3999 0.5205 -0.1042 0.0705  0.0160  328 ARG D N   
14849 C CA  . ARG D 328 ? 0.3527 0.4735 0.5834 -0.1060 0.0833  0.0218  328 ARG D CA  
14850 C C   . ARG D 328 ? 0.3302 0.4685 0.5659 -0.0939 0.0896  0.0190  328 ARG D C   
14851 O O   . ARG D 328 ? 0.2573 0.3934 0.4829 -0.0891 0.1004  0.0220  328 ARG D O   
14852 C CB  . ARG D 328 ? 0.4592 0.5961 0.7053 -0.1176 0.0835  0.0253  328 ARG D CB  
14853 C CG  . ARG D 328 ? 0.5639 0.7085 0.8072 -0.1231 0.0970  0.0337  328 ARG D CG  
14854 C CD  . ARG D 328 ? 0.6393 0.7972 0.8966 -0.1383 0.0959  0.0385  328 ARG D CD  
14855 N NE  . ARG D 328 ? 0.7027 0.8407 0.9582 -0.1480 0.0829  0.0369  328 ARG D NE  
14856 C CZ  . ARG D 328 ? 0.7737 0.8863 1.0148 -0.1590 0.0815  0.0427  328 ARG D CZ  
14857 N NH1 . ARG D 328 ? 0.7782 0.8827 1.0053 -0.1618 0.0925  0.0512  328 ARG D NH1 
14858 N NH2 . ARG D 328 ? 0.7895 0.8830 1.0286 -0.1664 0.0688  0.0397  328 ARG D NH2 
14859 N N   . ASP D 329 ? 0.3049 0.4586 0.5548 -0.0880 0.0827  0.0129  329 ASP D N   
14860 C CA  . ASP D 329 ? 0.2817 0.4498 0.5362 -0.0757 0.0874  0.0096  329 ASP D CA  
14861 C C   . ASP D 329 ? 0.2671 0.4163 0.5042 -0.0682 0.0898  0.0088  329 ASP D C   
14862 O O   . ASP D 329 ? 0.3087 0.4606 0.5411 -0.0606 0.0994  0.0095  329 ASP D O   
14863 C CB  . ASP D 329 ? 0.2553 0.4396 0.5262 -0.0707 0.0778  0.0031  329 ASP D CB  
14864 C CG  . ASP D 329 ? 0.2710 0.4684 0.5464 -0.0571 0.0818  -0.0007 329 ASP D CG  
14865 O OD1 . ASP D 329 ? 0.2873 0.5070 0.5740 -0.0533 0.0887  -0.0004 329 ASP D OD1 
14866 O OD2 . ASP D 329 ? 0.2365 0.4224 0.5041 -0.0500 0.0781  -0.0039 329 ASP D OD2 
14867 N N   . PHE D 330 ? 0.2238 0.3553 0.4519 -0.0697 0.0809  0.0070  330 PHE D N   
14868 C CA  . PHE D 330 ? 0.2205 0.3337 0.4290 -0.0637 0.0805  0.0070  330 PHE D CA  
14869 C C   . PHE D 330 ? 0.2870 0.3856 0.4771 -0.0643 0.0897  0.0121  330 PHE D C   
14870 O O   . PHE D 330 ? 0.2983 0.3895 0.4726 -0.0558 0.0927  0.0122  330 PHE D O   
14871 C CB  . PHE D 330 ? 0.1964 0.2960 0.3978 -0.0661 0.0696  0.0050  330 PHE D CB  
14872 C CG  . PHE D 330 ? 0.2435 0.3301 0.4260 -0.0590 0.0651  0.0042  330 PHE D CG  
14873 C CD1 . PHE D 330 ? 0.2843 0.3771 0.4679 -0.0519 0.0601  0.0012  330 PHE D CD1 
14874 C CD2 . PHE D 330 ? 0.2433 0.3114 0.4067 -0.0600 0.0652  0.0067  330 PHE D CD2 
14875 C CE1 . PHE D 330 ? 0.2788 0.3594 0.4455 -0.0479 0.0558  0.0016  330 PHE D CE1 
14876 C CE2 . PHE D 330 ? 0.3037 0.3622 0.4523 -0.0554 0.0604  0.0062  330 PHE D CE2 
14877 C CZ  . PHE D 330 ? 0.3035 0.3683 0.4541 -0.0503 0.0560  0.0041  330 PHE D CZ  
14878 N N   . ILE D 331 ? 0.3143 0.4056 0.5035 -0.0742 0.0932  0.0164  331 ILE D N   
14879 C CA  . ILE D 331 ? 0.3707 0.4464 0.5400 -0.0747 0.1018  0.0217  331 ILE D CA  
14880 C C   . ILE D 331 ? 0.3733 0.4641 0.5458 -0.0702 0.1148  0.0241  331 ILE D C   
14881 O O   . ILE D 331 ? 0.4371 0.5162 0.5889 -0.0636 0.1209  0.0262  331 ILE D O   
14882 C CB  . ILE D 331 ? 0.4370 0.4995 0.6032 -0.0865 0.1022  0.0263  331 ILE D CB  
14883 C CG1 . ILE D 331 ? 0.4159 0.4632 0.5768 -0.0881 0.0887  0.0228  331 ILE D CG1 
14884 C CG2 . ILE D 331 ? 0.4758 0.5210 0.6190 -0.0863 0.1115  0.0323  331 ILE D CG2 
14885 C CD1 . ILE D 331 ? 0.4067 0.4371 0.5458 -0.0797 0.0830  0.0207  331 ILE D CD1 
14886 N N   . GLY D 332 ? 0.3523 0.4698 0.5485 -0.0721 0.1176  0.0233  332 GLY D N   
14887 C CA  . GLY D 332 ? 0.3359 0.4730 0.5368 -0.0654 0.1298  0.0246  332 GLY D CA  
14888 C C   . GLY D 332 ? 0.3757 0.5090 0.5637 -0.0492 0.1290  0.0199  332 GLY D C   
14889 O O   . GLY D 332 ? 0.3365 0.4699 0.5113 -0.0403 0.1383  0.0212  332 GLY D O   
14890 N N   . ARG D 333 ? 0.3628 0.4904 0.5508 -0.0447 0.1165  0.0145  333 ARG D N   
14891 C CA  . ARG D 333 ? 0.3663 0.4849 0.5378 -0.0304 0.1130  0.0106  333 ARG D CA  
14892 C C   . ARG D 333 ? 0.3314 0.4201 0.4725 -0.0278 0.1118  0.0125  333 ARG D C   
14893 O O   . ARG D 333 ? 0.3297 0.4092 0.4528 -0.0165 0.1139  0.0112  333 ARG D O   
14894 C CB  . ARG D 333 ? 0.3669 0.4866 0.5452 -0.0275 0.1004  0.0055  333 ARG D CB  
14895 C CG  . ARG D 333 ? 0.3943 0.5431 0.5990 -0.0249 0.1006  0.0020  333 ARG D CG  
14896 C CD  . ARG D 333 ? 0.4202 0.5691 0.6326 -0.0257 0.0880  -0.0019 333 ARG D CD  
14897 N NE  . ARG D 333 ? 0.4427 0.6190 0.6837 -0.0279 0.0867  -0.0048 333 ARG D NE  
14898 C CZ  . ARG D 333 ? 0.4381 0.6335 0.6903 -0.0174 0.0863  -0.0092 333 ARG D CZ  
14899 N NH1 . ARG D 333 ? 0.5046 0.6917 0.7393 -0.0032 0.0869  -0.0111 333 ARG D NH1 
14900 N NH2 . ARG D 333 ? 0.4363 0.6581 0.7164 -0.0205 0.0842  -0.0121 333 ARG D NH2 
14901 N N   . LEU D 334 ? 0.3431 0.4160 0.4776 -0.0372 0.1074  0.0149  334 LEU D N   
14902 C CA  . LEU D 334 ? 0.2865 0.3331 0.3939 -0.0354 0.1060  0.0167  334 LEU D CA  
14903 C C   . LEU D 334 ? 0.3083 0.3518 0.4029 -0.0323 0.1185  0.0206  334 LEU D C   
14904 O O   . LEU D 334 ? 0.3462 0.3715 0.4164 -0.0242 0.1186  0.0202  334 LEU D O   
14905 C CB  . LEU D 334 ? 0.2692 0.3033 0.3742 -0.0451 0.0991  0.0181  334 LEU D CB  
14906 C CG  . LEU D 334 ? 0.2516 0.2875 0.3645 -0.0467 0.0869  0.0145  334 LEU D CG  
14907 C CD1 . LEU D 334 ? 0.2126 0.2369 0.3205 -0.0533 0.0805  0.0152  334 LEU D CD1 
14908 C CD2 . LEU D 334 ? 0.2384 0.2662 0.3391 -0.0386 0.0809  0.0119  334 LEU D CD2 
14909 N N   . LYS D 335 ? 0.3154 0.3766 0.4256 -0.0389 0.1288  0.0245  335 LYS D N   
14910 C CA  . LYS D 335 ? 0.3552 0.4180 0.4543 -0.0357 0.1429  0.0291  335 LYS D CA  
14911 C C   . LYS D 335 ? 0.3766 0.4485 0.4695 -0.0198 0.1477  0.0255  335 LYS D C   
14912 O O   . LYS D 335 ? 0.3183 0.3768 0.3866 -0.0105 0.1534  0.0265  335 LYS D O   
14913 C CB  . LYS D 335 ? 0.3444 0.4285 0.4650 -0.0478 0.1533  0.0349  335 LYS D CB  
14914 C CG  . LYS D 335 ? 0.4412 0.5267 0.5488 -0.0469 0.1694  0.0418  335 LYS D CG  
14915 C CD  . LYS D 335 ? 0.4293 0.5524 0.5633 -0.0496 0.1826  0.0446  335 LYS D CD  
14916 C CE  . LYS D 335 ? 0.4649 0.5901 0.5858 -0.0533 0.1950  0.0528  335 LYS D CE  
14917 N NZ  . LYS D 335 ? 0.4923 0.6151 0.5904 -0.0363 0.2076  0.0528  335 LYS D NZ  
14918 N N   . LYS D 336 ? 0.3540 0.4470 0.4670 -0.0150 0.1446  0.0208  336 LYS D N   
14919 C CA  . LYS D 336 ? 0.4233 0.5247 0.5298 0.0020  0.1482  0.0165  336 LYS D CA  
14920 C C   . LYS D 336 ? 0.4009 0.4706 0.4769 0.0131  0.1381  0.0124  336 LYS D C   
14921 O O   . LYS D 336 ? 0.4285 0.4911 0.4844 0.0274  0.1422  0.0105  336 LYS D O   
14922 C CB  . LYS D 336 ? 0.4735 0.6031 0.6074 0.0054  0.1454  0.0118  336 LYS D CB  
14923 C CG  . LYS D 336 ? 0.5441 0.7115 0.7017 0.0059  0.1595  0.0137  336 LYS D CG  
14924 C CD  . LYS D 336 ? 0.5512 0.7352 0.7356 -0.0140 0.1626  0.0190  336 LYS D CD  
14925 C CE  . LYS D 336 ? 0.5781 0.8055 0.7968 -0.0149 0.1698  0.0183  336 LYS D CE  
14926 N NZ  . LYS D 336 ? 0.5886 0.8246 0.8280 -0.0320 0.1586  0.0190  336 LYS D NZ  
14927 N N   . ILE D 337 ? 0.4004 0.4513 0.4724 0.0065  0.1246  0.0112  337 ILE D N   
14928 C CA  . ILE D 337 ? 0.3885 0.4084 0.4325 0.0128  0.1143  0.0087  337 ILE D CA  
14929 C C   . ILE D 337 ? 0.3874 0.3869 0.4059 0.0144  0.1191  0.0116  337 ILE D C   
14930 O O   . ILE D 337 ? 0.3770 0.3590 0.3703 0.0268  0.1181  0.0091  337 ILE D O   
14931 C CB  . ILE D 337 ? 0.3648 0.3741 0.4131 0.0028  0.1008  0.0082  337 ILE D CB  
14932 C CG1 . ILE D 337 ? 0.3673 0.3936 0.4362 0.0032  0.0953  0.0052  337 ILE D CG1 
14933 C CG2 . ILE D 337 ? 0.4040 0.3830 0.4255 0.0059  0.0903  0.0069  337 ILE D CG2 
14934 C CD1 . ILE D 337 ? 0.3167 0.3370 0.3910 -0.0065 0.0836  0.0054  337 ILE D CD1 
14935 N N   . HIS D 338 ? 0.3545 0.3535 0.3769 0.0026  0.1230  0.0165  338 HIS D N   
14936 C CA  . HIS D 338 ? 0.4880 0.4658 0.4849 0.0037  0.1265  0.0196  338 HIS D CA  
14937 C C   . HIS D 338 ? 0.5260 0.5067 0.5075 0.0165  0.1392  0.0203  338 HIS D C   
14938 O O   . HIS D 338 ? 0.5943 0.5513 0.5459 0.0247  0.1384  0.0197  338 HIS D O   
14939 C CB  . HIS D 338 ? 0.5061 0.4858 0.5115 -0.0103 0.1303  0.0253  338 HIS D CB  
14940 C CG  . HIS D 338 ? 0.5999 0.5564 0.5781 -0.0095 0.1332  0.0288  338 HIS D CG  
14941 N ND1 . HIS D 338 ? 0.6396 0.6004 0.6122 -0.0108 0.1476  0.0350  338 HIS D ND1 
14942 C CD2 . HIS D 338 ? 0.6211 0.5503 0.5760 -0.0076 0.1231  0.0272  338 HIS D CD2 
14943 C CE1 . HIS D 338 ? 0.6883 0.6229 0.6328 -0.0088 0.1462  0.0370  338 HIS D CE1 
14944 N NE2 . HIS D 338 ? 0.6563 0.5720 0.5904 -0.0065 0.1309  0.0318  338 HIS D NE2 
14945 N N   . GLU D 339 ? 0.5022 0.5129 0.5034 0.0193  0.1507  0.0210  339 GLU D N   
14946 C CA  . GLU D 339 ? 0.6267 0.6468 0.6161 0.0318  0.1650  0.0222  339 GLU D CA  
14947 C C   . GLU D 339 ? 0.6660 0.6806 0.6398 0.0517  0.1608  0.0148  339 GLU D C   
14948 O O   . GLU D 339 ? 0.7440 0.7566 0.6972 0.0659  0.1698  0.0143  339 GLU D O   
14949 C CB  . GLU D 339 ? 0.6940 0.7533 0.7136 0.0253  0.1801  0.0268  339 GLU D CB  
14950 C CG  . GLU D 339 ? 0.7853 0.8488 0.8184 0.0053  0.1854  0.0351  339 GLU D CG  
14951 C CD  . GLU D 339 ? 0.9536 0.9930 0.9577 0.0033  0.1918  0.0414  339 GLU D CD  
14952 O OE1 . GLU D 339 ? 1.0253 1.0400 0.9972 0.0163  0.1891  0.0387  339 GLU D OE1 
14953 O OE2 . GLU D 339 ? 1.0053 1.0487 1.0175 -0.0115 0.1987  0.0491  339 GLU D OE2 
14954 N N   . SER D 340 ? 0.6350 0.6452 0.6155 0.0539  0.1472  0.0091  340 SER D N   
14955 C CA  . SER D 340 ? 0.6473 0.6514 0.6138 0.0728  0.1420  0.0019  340 SER D CA  
14956 C C   . SER D 340 ? 0.6623 0.6243 0.5922 0.0806  0.1287  -0.0019 340 SER D C   
14957 O O   . SER D 340 ? 0.7293 0.6789 0.6422 0.0967  0.1222  -0.0081 340 SER D O   
14958 C CB  . SER D 340 ? 0.6491 0.6678 0.6391 0.0717  0.1336  -0.0019 340 SER D CB  
14959 O OG  . SER D 340 ? 0.6393 0.6405 0.6322 0.0580  0.1198  -0.0011 340 SER D OG  
14960 N N   . VAL D 341 ? 0.6145 0.5537 0.5317 0.0701  0.1233  0.0012  341 VAL D N   
14961 C CA  . VAL D 341 ? 0.6494 0.5498 0.5344 0.0750  0.1093  -0.0022 341 VAL D CA  
14962 C C   . VAL D 341 ? 0.6683 0.5533 0.5306 0.0756  0.1148  0.0009  341 VAL D C   
14963 O O   . VAL D 341 ? 0.6679 0.5657 0.5425 0.0643  0.1241  0.0069  341 VAL D O   
14964 C CB  . VAL D 341 ? 0.6403 0.5277 0.5335 0.0605  0.0930  -0.0022 341 VAL D CB  
14965 C CG1 . VAL D 341 ? 0.6651 0.5606 0.5722 0.0625  0.0861  -0.0053 341 VAL D CG1 
14966 C CG2 . VAL D 341 ? 0.5757 0.4780 0.4914 0.0428  0.0967  0.0034  341 VAL D CG2 
14967 N N   . ASP D 342 ? 0.7329 0.5880 0.5600 0.0892  0.1084  -0.0034 342 ASP D N   
14968 C CA  . ASP D 342 ? 0.8179 0.6528 0.6185 0.0912  0.1107  -0.0014 342 ASP D CA  
14969 C C   . ASP D 342 ? 0.7933 0.6035 0.5872 0.0787  0.0946  -0.0013 342 ASP D C   
14970 O O   . ASP D 342 ? 0.8344 0.6265 0.6071 0.0793  0.0940  0.0001  342 ASP D O   
14971 C CB  . ASP D 342 ? 0.9701 0.7841 0.7336 0.1135  0.1109  -0.0068 342 ASP D CB  
14972 C CG  . ASP D 342 ? 1.0869 0.8636 0.8260 0.1188  0.0894  -0.0138 342 ASP D CG  
14973 O OD1 . ASP D 342 ? 1.0929 0.8696 0.8455 0.1146  0.0787  -0.0164 342 ASP D OD1 
14974 O OD2 . ASP D 342 ? 1.1604 0.9067 0.8662 0.1264  0.0827  -0.0164 342 ASP D OD2 
14975 N N   . PHE D 343 ? 0.7008 0.5112 0.5122 0.0678  0.0818  -0.0026 343 PHE D N   
14976 C CA  . PHE D 343 ? 0.6385 0.4326 0.4488 0.0551  0.0671  -0.0023 343 PHE D CA  
14977 C C   . PHE D 343 ? 0.6244 0.4436 0.4685 0.0383  0.0699  0.0024  343 PHE D C   
14978 O O   . PHE D 343 ? 0.6369 0.4828 0.5039 0.0359  0.0818  0.0051  343 PHE D O   
14979 C CB  . PHE D 343 ? 0.5809 0.3526 0.3803 0.0561  0.0489  -0.0072 343 PHE D CB  
14980 C CG  . PHE D 343 ? 0.5510 0.3382 0.3723 0.0528  0.0471  -0.0075 343 PHE D CG  
14981 C CD1 . PHE D 343 ? 0.5606 0.3516 0.3772 0.0674  0.0522  -0.0108 343 PHE D CD1 
14982 C CD2 . PHE D 343 ? 0.4835 0.2822 0.3289 0.0366  0.0404  -0.0048 343 PHE D CD2 
14983 C CE1 . PHE D 343 ? 0.5863 0.3897 0.4211 0.0656  0.0493  -0.0114 343 PHE D CE1 
14984 C CE2 . PHE D 343 ? 0.5182 0.3294 0.3812 0.0342  0.0384  -0.0049 343 PHE D CE2 
14985 C CZ  . PHE D 343 ? 0.5437 0.3560 0.4009 0.0485  0.0424  -0.0082 343 PHE D CZ  
14986 N N   . GLN D 344 ? 0.5845 0.3956 0.4317 0.0270  0.0583  0.0028  344 GLN D N   
14987 C CA  . GLN D 344 ? 0.4915 0.3241 0.3672 0.0130  0.0594  0.0063  344 GLN D CA  
14988 C C   . GLN D 344 ? 0.4644 0.3078 0.3596 0.0068  0.0519  0.0052  344 GLN D C   
14989 O O   . GLN D 344 ? 0.4267 0.2569 0.3163 0.0024  0.0381  0.0035  344 GLN D O   
14990 C CB  . GLN D 344 ? 0.4057 0.2279 0.2757 0.0058  0.0511  0.0070  344 GLN D CB  
14991 C CG  . GLN D 344 ? 0.4474 0.2542 0.2933 0.0129  0.0572  0.0082  344 GLN D CG  
14992 C CD  . GLN D 344 ? 0.4686 0.2695 0.3125 0.0064  0.0507  0.0092  344 GLN D CD  
14993 O OE1 . GLN D 344 ? 0.5288 0.3364 0.3774 0.0032  0.0591  0.0131  344 GLN D OE1 
14994 N NE2 . GLN D 344 ? 0.4714 0.2596 0.3082 0.0041  0.0348  0.0056  344 GLN D NE2 
14995 N N   . PRO D 345 ? 0.4353 0.3025 0.3533 0.0053  0.0600  0.0065  345 PRO D N   
14996 C CA  . PRO D 345 ? 0.4055 0.2814 0.3392 0.0007  0.0530  0.0056  345 PRO D CA  
14997 C C   . PRO D 345 ? 0.3560 0.2425 0.3076 -0.0128 0.0465  0.0076  345 PRO D C   
14998 O O   . PRO D 345 ? 0.3794 0.2765 0.3413 -0.0183 0.0510  0.0096  345 PRO D O   
14999 C CB  . PRO D 345 ? 0.4192 0.3186 0.3709 0.0052  0.0646  0.0058  345 PRO D CB  
15000 C CG  . PRO D 345 ? 0.3650 0.2765 0.3237 0.0026  0.0767  0.0090  345 PRO D CG  
15001 C CD  . PRO D 345 ? 0.4303 0.3180 0.3614 0.0066  0.0756  0.0092  345 PRO D CD  
15002 N N   . VAL D 346 ? 0.4455 0.3289 0.3998 -0.0176 0.0360  0.0073  346 VAL D N   
15003 C CA  . VAL D 346 ? 0.3924 0.2907 0.3652 -0.0292 0.0309  0.0092  346 VAL D CA  
15004 C C   . VAL D 346 ? 0.3795 0.2955 0.3704 -0.0295 0.0339  0.0097  346 VAL D C   
15005 O O   . VAL D 346 ? 0.3503 0.2585 0.3349 -0.0251 0.0305  0.0088  346 VAL D O   
15006 C CB  . VAL D 346 ? 0.3705 0.2556 0.3345 -0.0363 0.0175  0.0097  346 VAL D CB  
15007 C CG1 . VAL D 346 ? 0.3999 0.3054 0.3838 -0.0472 0.0139  0.0120  346 VAL D CG1 
15008 C CG2 . VAL D 346 ? 0.3815 0.2476 0.3262 -0.0343 0.0130  0.0083  346 VAL D CG2 
15009 N N   . VAL D 347 ? 0.3661 0.3038 0.3777 -0.0338 0.0391  0.0105  347 VAL D N   
15010 C CA  . VAL D 347 ? 0.3327 0.2887 0.3624 -0.0334 0.0422  0.0103  347 VAL D CA  
15011 C C   . VAL D 347 ? 0.3238 0.2923 0.3665 -0.0418 0.0364  0.0116  347 VAL D C   
15012 O O   . VAL D 347 ? 0.2666 0.2460 0.3193 -0.0461 0.0377  0.0118  347 VAL D O   
15013 C CB  . VAL D 347 ? 0.2727 0.2441 0.3158 -0.0308 0.0530  0.0098  347 VAL D CB  
15014 C CG1 . VAL D 347 ? 0.3361 0.3258 0.3975 -0.0294 0.0544  0.0086  347 VAL D CG1 
15015 C CG2 . VAL D 347 ? 0.2948 0.2570 0.3244 -0.0225 0.0607  0.0093  347 VAL D CG2 
15016 N N   . PHE D 348 ? 0.3592 0.3255 0.4002 -0.0436 0.0299  0.0127  348 PHE D N   
15017 C CA  . PHE D 348 ? 0.3085 0.2885 0.3605 -0.0509 0.0255  0.0147  348 PHE D CA  
15018 C C   . PHE D 348 ? 0.2541 0.2514 0.3219 -0.0480 0.0289  0.0134  348 PHE D C   
15019 O O   . PHE D 348 ? 0.2839 0.2785 0.3501 -0.0425 0.0289  0.0126  348 PHE D O   
15020 C CB  . PHE D 348 ? 0.2590 0.2274 0.2999 -0.0561 0.0169  0.0180  348 PHE D CB  
15021 C CG  . PHE D 348 ? 0.2864 0.2505 0.3218 -0.0639 0.0114  0.0198  348 PHE D CG  
15022 C CD1 . PHE D 348 ? 0.2884 0.2362 0.3109 -0.0617 0.0104  0.0181  348 PHE D CD1 
15023 C CD2 . PHE D 348 ? 0.2788 0.2566 0.3219 -0.0728 0.0071  0.0232  348 PHE D CD2 
15024 C CE1 . PHE D 348 ? 0.2919 0.2363 0.3099 -0.0685 0.0038  0.0191  348 PHE D CE1 
15025 C CE2 . PHE D 348 ? 0.3394 0.3170 0.3799 -0.0800 0.0016  0.0246  348 PHE D CE2 
15026 C CZ  . PHE D 348 ? 0.3298 0.2902 0.3581 -0.0779 -0.0007 0.0223  348 PHE D CZ  
15027 N N   . VAL D 349 ? 0.2183 0.2322 0.3001 -0.0507 0.0305  0.0126  349 VAL D N   
15028 C CA  . VAL D 349 ? 0.2361 0.2666 0.3329 -0.0490 0.0314  0.0109  349 VAL D CA  
15029 C C   . VAL D 349 ? 0.2495 0.2888 0.3479 -0.0534 0.0260  0.0129  349 VAL D C   
15030 O O   . VAL D 349 ? 0.2679 0.3149 0.3696 -0.0567 0.0248  0.0129  349 VAL D O   
15031 C CB  . VAL D 349 ? 0.2263 0.2666 0.3357 -0.0487 0.0360  0.0083  349 VAL D CB  
15032 C CG1 . VAL D 349 ? 0.2838 0.3401 0.4083 -0.0473 0.0346  0.0058  349 VAL D CG1 
15033 C CG2 . VAL D 349 ? 0.2329 0.2669 0.3405 -0.0455 0.0431  0.0076  349 VAL D CG2 
15034 N N   . VAL D 350 ? 0.2450 0.2832 0.3398 -0.0527 0.0228  0.0149  350 VAL D N   
15035 C CA  . VAL D 350 ? 0.2655 0.3112 0.3589 -0.0575 0.0187  0.0185  350 VAL D CA  
15036 C C   . VAL D 350 ? 0.2942 0.3497 0.3933 -0.0529 0.0178  0.0174  350 VAL D C   
15037 O O   . VAL D 350 ? 0.2646 0.3116 0.3593 -0.0482 0.0167  0.0171  350 VAL D O   
15038 C CB  . VAL D 350 ? 0.2217 0.2522 0.3001 -0.0636 0.0143  0.0239  350 VAL D CB  
15039 C CG1 . VAL D 350 ? 0.1874 0.2308 0.2665 -0.0709 0.0117  0.0291  350 VAL D CG1 
15040 C CG2 . VAL D 350 ? 0.1784 0.1957 0.2489 -0.0668 0.0136  0.0240  350 VAL D CG2 
15041 N N   . LEU D 351 ? 0.2772 0.3497 0.3844 -0.0530 0.0173  0.0165  351 LEU D N   
15042 C CA  . LEU D 351 ? 0.2511 0.3323 0.3613 -0.0481 0.0153  0.0154  351 LEU D CA  
15043 C C   . LEU D 351 ? 0.2166 0.3147 0.3292 -0.0492 0.0144  0.0162  351 LEU D C   
15044 O O   . LEU D 351 ? 0.1857 0.2904 0.2997 -0.0529 0.0153  0.0169  351 LEU D O   
15045 C CB  . LEU D 351 ? 0.2212 0.3062 0.3432 -0.0413 0.0161  0.0090  351 LEU D CB  
15046 C CG  . LEU D 351 ? 0.2623 0.3551 0.3960 -0.0414 0.0178  0.0045  351 LEU D CG  
15047 C CD1 . LEU D 351 ? 0.2770 0.3785 0.4234 -0.0363 0.0158  -0.0011 351 LEU D CD1 
15048 C CD2 . LEU D 351 ? 0.1918 0.2745 0.3252 -0.0443 0.0223  0.0047  351 LEU D CD2 
15049 N N   . ASN D 352 ? 0.1960 0.3016 0.3080 -0.0444 0.0123  0.0157  352 ASN D N   
15050 C CA  . ASN D 352 ? 0.1695 0.2925 0.2827 -0.0428 0.0117  0.0154  352 ASN D CA  
15051 C C   . ASN D 352 ? 0.1782 0.3083 0.3020 -0.0388 0.0113  0.0083  352 ASN D C   
15052 O O   . ASN D 352 ? 0.1731 0.2973 0.3046 -0.0360 0.0105  0.0032  352 ASN D O   
15053 C CB  . ASN D 352 ? 0.1783 0.3062 0.2866 -0.0367 0.0091  0.0155  352 ASN D CB  
15054 C CG  . ASN D 352 ? 0.1901 0.3163 0.2849 -0.0420 0.0099  0.0244  352 ASN D CG  
15055 O OD1 . ASN D 352 ? 0.2110 0.3205 0.2968 -0.0446 0.0086  0.0285  352 ASN D OD1 
15056 N ND2 . ASN D 352 ? 0.1755 0.3190 0.2677 -0.0436 0.0118  0.0279  352 ASN D ND2 
15057 N N   . GLY D 353 ? 0.1179 0.2603 0.2416 -0.0388 0.0116  0.0082  353 GLY D N   
15058 C CA  . GLY D 353 ? 0.1237 0.2688 0.2536 -0.0345 0.0098  0.0016  353 GLY D CA  
15059 C C   . GLY D 353 ? 0.1863 0.3411 0.3173 -0.0252 0.0056  -0.0043 353 GLY D C   
15060 O O   . GLY D 353 ? 0.2099 0.3647 0.3432 -0.0211 0.0027  -0.0099 353 GLY D O   
15061 N N   . GLU D 354 ? 0.2257 0.3860 0.3527 -0.0211 0.0042  -0.0036 354 GLU D N   
15062 C CA  . GLU D 354 ? 0.2128 0.3821 0.3376 -0.0109 -0.0006 -0.0096 354 GLU D CA  
15063 C C   . GLU D 354 ? 0.2381 0.4031 0.3629 -0.0058 -0.0049 -0.0125 354 GLU D C   
15064 O O   . GLU D 354 ? 0.2324 0.4015 0.3551 0.0033  -0.0106 -0.0189 354 GLU D O   
15065 C CB  . GLU D 354 ? 0.2127 0.4011 0.3290 -0.0075 0.0019  -0.0060 354 GLU D CB  
15066 C CG  . GLU D 354 ? 0.1327 0.3264 0.2400 -0.0090 0.0046  0.0013  354 GLU D CG  
15067 C CD  . GLU D 354 ? 0.1702 0.3590 0.2756 -0.0216 0.0097  0.0112  354 GLU D CD  
15068 O OE1 . GLU D 354 ? 0.1459 0.3485 0.2462 -0.0263 0.0139  0.0185  354 GLU D OE1 
15069 O OE2 . GLU D 354 ? 0.1902 0.3615 0.2989 -0.0268 0.0093  0.0116  354 GLU D OE2 
15070 N N   . ASN D 355 ? 0.2158 0.3720 0.3418 -0.0100 -0.0035 -0.0090 355 ASN D N   
15071 C CA  . ASN D 355 ? 0.2052 0.3592 0.3299 -0.0038 -0.0084 -0.0118 355 ASN D CA  
15072 C C   . ASN D 355 ? 0.2266 0.3739 0.3654 -0.0031 -0.0128 -0.0185 355 ASN D C   
15073 O O   . ASN D 355 ? 0.2386 0.3868 0.3790 0.0036  -0.0192 -0.0234 355 ASN D O   
15074 C CB  . ASN D 355 ? 0.2169 0.3656 0.3317 -0.0065 -0.0057 -0.0041 355 ASN D CB  
15075 C CG  . ASN D 355 ? 0.2383 0.3958 0.3392 -0.0079 -0.0020 0.0034  355 ASN D CG  
15076 O OD1 . ASN D 355 ? 0.2404 0.4110 0.3375 -0.0018 -0.0028 0.0011  355 ASN D OD1 
15077 N ND2 . ASN D 355 ? 0.2139 0.3647 0.3069 -0.0162 0.0020  0.0124  355 ASN D ND2 
15078 N N   . CYS D 356 ? 0.1952 0.3369 0.3443 -0.0098 -0.0097 -0.0189 356 CYS D N   
15079 C CA  . CYS D 356 ? 0.1394 0.2783 0.3032 -0.0106 -0.0126 -0.0239 356 CYS D CA  
15080 C C   . CYS D 356 ? 0.1213 0.2602 0.2935 -0.0099 -0.0185 -0.0309 356 CYS D C   
15081 O O   . CYS D 356 ? 0.1952 0.3349 0.3800 -0.0099 -0.0235 -0.0358 356 CYS D O   
15082 C CB  . CYS D 356 ? 0.2463 0.3793 0.4165 -0.0178 -0.0057 -0.0203 356 CYS D CB  
15083 S SG  . CYS D 356 ? 0.2482 0.3750 0.4152 -0.0252 0.0003  -0.0170 356 CYS D SG  
15084 N N   . TRP D 357 ? 0.1555 0.2935 0.3205 -0.0090 -0.0191 -0.0317 357 TRP D N   
15085 C CA  . TRP D 357 ? 0.1885 0.3203 0.3584 -0.0094 -0.0250 -0.0377 357 TRP D CA  
15086 C C   . TRP D 357 ? 0.2161 0.3489 0.3870 -0.0019 -0.0361 -0.0455 357 TRP D C   
15087 O O   . TRP D 357 ? 0.2969 0.4228 0.4773 -0.0050 -0.0427 -0.0507 357 TRP D O   
15088 C CB  . TRP D 357 ? 0.1894 0.3190 0.3488 -0.0080 -0.0236 -0.0370 357 TRP D CB  
15089 C CG  . TRP D 357 ? 0.1888 0.3179 0.3460 -0.0148 -0.0140 -0.0296 357 TRP D CG  
15090 C CD1 . TRP D 357 ? 0.1584 0.2951 0.3061 -0.0136 -0.0098 -0.0251 357 TRP D CD1 
15091 C CD2 . TRP D 357 ? 0.2043 0.3253 0.3689 -0.0237 -0.0082 -0.0260 357 TRP D CD2 
15092 N NE1 . TRP D 357 ? 0.2206 0.3523 0.3690 -0.0213 -0.0031 -0.0195 357 TRP D NE1 
15093 C CE2 . TRP D 357 ? 0.2032 0.3245 0.3605 -0.0267 -0.0018 -0.0202 357 TRP D CE2 
15094 C CE3 . TRP D 357 ? 0.2252 0.3400 0.4019 -0.0295 -0.0077 -0.0271 357 TRP D CE3 
15095 C CZ2 . TRP D 357 ? 0.2220 0.3350 0.3811 -0.0336 0.0044  -0.0161 357 TRP D CZ2 
15096 C CZ3 . TRP D 357 ? 0.1974 0.3068 0.3766 -0.0364 0.0002  -0.0224 357 TRP D CZ3 
15097 C CH2 . TRP D 357 ? 0.2231 0.3302 0.3922 -0.0376 0.0057  -0.0173 357 TRP D CH2 
15098 N N   . GLU D 358 ? 0.2059 0.3461 0.3663 0.0074  -0.0388 -0.0463 358 GLU D N   
15099 C CA  . GLU D 358 ? 0.2084 0.3482 0.3665 0.0163  -0.0504 -0.0545 358 GLU D CA  
15100 C C   . GLU D 358 ? 0.2466 0.3852 0.4216 0.0127  -0.0564 -0.0585 358 GLU D C   
15101 O O   . GLU D 358 ? 0.2504 0.3861 0.4274 0.0176  -0.0682 -0.0664 358 GLU D O   
15102 C CB  . GLU D 358 ? 0.1999 0.3483 0.3415 0.0272  -0.0505 -0.0532 358 GLU D CB  
15103 C CG  . GLU D 358 ? 0.2133 0.3661 0.3542 0.0249  -0.0442 -0.0462 358 GLU D CG  
15104 C CD  . GLU D 358 ? 0.2763 0.4365 0.3979 0.0314  -0.0401 -0.0407 358 GLU D CD  
15105 O OE1 . GLU D 358 ? 0.3162 0.4771 0.4296 0.0388  -0.0444 -0.0415 358 GLU D OE1 
15106 O OE2 . GLU D 358 ? 0.2793 0.4452 0.3941 0.0288  -0.0327 -0.0351 358 GLU D OE2 
15107 N N   . TYR D 359 ? 0.2083 0.3501 0.3956 0.0050  -0.0493 -0.0537 359 TYR D N   
15108 C CA  . TYR D 359 ? 0.2129 0.3587 0.4195 0.0014  -0.0538 -0.0572 359 TYR D CA  
15109 C C   . TYR D 359 ? 0.2177 0.3600 0.4414 -0.0104 -0.0529 -0.0578 359 TYR D C   
15110 O O   . TYR D 359 ? 0.2108 0.3593 0.4536 -0.0149 -0.0571 -0.0610 359 TYR D O   
15111 C CB  . TYR D 359 ? 0.2676 0.4201 0.4770 0.0019  -0.0470 -0.0523 359 TYR D CB  
15112 C CG  . TYR D 359 ? 0.3311 0.4843 0.5222 0.0123  -0.0486 -0.0507 359 TYR D CG  
15113 C CD1 . TYR D 359 ? 0.3648 0.5212 0.5548 0.0216  -0.0590 -0.0567 359 TYR D CD1 
15114 C CD2 . TYR D 359 ? 0.3358 0.4862 0.5100 0.0124  -0.0403 -0.0431 359 TYR D CD2 
15115 C CE1 . TYR D 359 ? 0.4015 0.5566 0.5718 0.0313  -0.0603 -0.0545 359 TYR D CE1 
15116 C CE2 . TYR D 359 ? 0.3888 0.5393 0.5450 0.0204  -0.0413 -0.0402 359 TYR D CE2 
15117 C CZ  . TYR D 359 ? 0.4049 0.5570 0.5580 0.0301  -0.0509 -0.0457 359 TYR D CZ  
15118 O OH  . TYR D 359 ? 0.3957 0.5461 0.5282 0.0382  -0.0517 -0.0422 359 TYR D OH  
15119 N N   . TYR D 360 ? 0.1809 0.3141 0.3983 -0.0157 -0.0476 -0.0544 360 TYR D N   
15120 C CA  . TYR D 360 ? 0.2851 0.4116 0.5147 -0.0273 -0.0465 -0.0538 360 TYR D CA  
15121 C C   . TYR D 360 ? 0.2962 0.4111 0.5235 -0.0268 -0.0594 -0.0608 360 TYR D C   
15122 O O   . TYR D 360 ? 0.3201 0.4297 0.5308 -0.0164 -0.0661 -0.0650 360 TYR D O   
15123 C CB  . TYR D 360 ? 0.1980 0.3166 0.4189 -0.0324 -0.0360 -0.0472 360 TYR D CB  
15124 C CG  . TYR D 360 ? 0.2138 0.3383 0.4374 -0.0360 -0.0234 -0.0401 360 TYR D CG  
15125 C CD1 . TYR D 360 ? 0.2183 0.3496 0.4342 -0.0294 -0.0197 -0.0375 360 TYR D CD1 
15126 C CD2 . TYR D 360 ? 0.1890 0.3094 0.4194 -0.0458 -0.0154 -0.0356 360 TYR D CD2 
15127 C CE1 . TYR D 360 ? 0.2230 0.3556 0.4383 -0.0319 -0.0099 -0.0317 360 TYR D CE1 
15128 C CE2 . TYR D 360 ? 0.2270 0.3510 0.4568 -0.0473 -0.0045 -0.0298 360 TYR D CE2 
15129 C CZ  . TYR D 360 ? 0.2616 0.3908 0.4837 -0.0400 -0.0025 -0.0284 360 TYR D CZ  
15130 O OH  . TYR D 360 ? 0.2761 0.4051 0.4950 -0.0407 0.0064  -0.0234 360 TYR D OH  
15131 N N   . GLU D 361 ? 0.3168 0.3634 0.4755 -0.0273 -0.0457 -0.0323 361 GLU D N   
15132 C CA  . GLU D 361 ? 0.3909 0.4039 0.5258 -0.0319 -0.0534 -0.0331 361 GLU D CA  
15133 C C   . GLU D 361 ? 0.4094 0.4030 0.5189 -0.0216 -0.0446 -0.0288 361 GLU D C   
15134 O O   . GLU D 361 ? 0.3212 0.3296 0.4388 -0.0200 -0.0324 -0.0239 361 GLU D O   
15135 C CB  . GLU D 361 ? 0.5149 0.5313 0.6667 -0.0524 -0.0555 -0.0321 361 GLU D CB  
15136 C CG  . GLU D 361 ? 0.7378 0.7171 0.8654 -0.0599 -0.0658 -0.0337 361 GLU D CG  
15137 C CD  . GLU D 361 ? 0.8733 0.8468 1.0065 -0.0694 -0.0835 -0.0396 361 GLU D CD  
15138 O OE1 . GLU D 361 ? 0.9668 0.9119 1.0846 -0.0793 -0.0938 -0.0414 361 GLU D OE1 
15139 O OE2 . GLU D 361 ? 0.8775 0.8764 1.0319 -0.0668 -0.0876 -0.0424 361 GLU D OE2 
15140 N N   . GLU D 362 ? 0.4828 0.4421 0.5604 -0.0137 -0.0514 -0.0306 362 GLU D N   
15141 C CA  . GLU D 362 ? 0.4804 0.4179 0.5316 -0.0019 -0.0444 -0.0266 362 GLU D CA  
15142 C C   . GLU D 362 ? 0.3975 0.3566 0.4559 0.0115  -0.0320 -0.0222 362 GLU D C   
15143 O O   . GLU D 362 ? 0.3875 0.3456 0.4408 0.0156  -0.0233 -0.0169 362 GLU D O   
15144 C CB  . GLU D 362 ? 0.5277 0.4532 0.5751 -0.0135 -0.0414 -0.0230 362 GLU D CB  
15145 C CG  . GLU D 362 ? 0.6418 0.5321 0.6684 -0.0225 -0.0530 -0.0261 362 GLU D CG  
15146 C CD  . GLU D 362 ? 0.7703 0.6474 0.7916 -0.0334 -0.0483 -0.0216 362 GLU D CD  
15147 O OE1 . GLU D 362 ? 0.7681 0.6482 0.7844 -0.0254 -0.0374 -0.0161 362 GLU D OE1 
15148 O OE2 . GLU D 362 ? 0.8536 0.7179 0.8766 -0.0504 -0.0559 -0.0233 362 GLU D OE2 
15149 N N   . ASN D 363 ? 0.3584 0.3366 0.4288 0.0179  -0.0317 -0.0242 363 ASN D N   
15150 C CA  . ASN D 363 ? 0.3428 0.3393 0.4191 0.0303  -0.0212 -0.0203 363 ASN D CA  
15151 C C   . ASN D 363 ? 0.3176 0.3389 0.4153 0.0231  -0.0115 -0.0157 363 ASN D C   
15152 O O   . ASN D 363 ? 0.2704 0.3007 0.3687 0.0316  -0.0031 -0.0111 363 ASN D O   
15153 C CB  . ASN D 363 ? 0.3254 0.3005 0.3749 0.0473  -0.0173 -0.0172 363 ASN D CB  
15154 C CG  . ASN D 363 ? 0.2808 0.2746 0.3375 0.0601  -0.0078 -0.0134 363 ASN D CG  
15155 O OD1 . ASN D 363 ? 0.2886 0.3005 0.3594 0.0605  -0.0074 -0.0152 363 ASN D OD1 
15156 N ND2 . ASN D 363 ? 0.2759 0.2660 0.3237 0.0705  -0.0001 -0.0075 363 ASN D ND2 
15157 N N   . GLY D 364 ? 0.3095 0.3419 0.4249 0.0075  -0.0127 -0.0167 364 GLY D N   
15158 C CA  . GLY D 364 ? 0.2954 0.3491 0.4284 0.0012  -0.0034 -0.0129 364 GLY D CA  
15159 C C   . GLY D 364 ? 0.3014 0.3425 0.4223 -0.0004 0.0014  -0.0079 364 GLY D C   
15160 O O   . GLY D 364 ? 0.3077 0.3630 0.4387 -0.0047 0.0088  -0.0045 364 GLY D O   
15161 N N   . ILE D 365 ? 0.3329 0.3454 0.4298 0.0037  -0.0029 -0.0076 365 ILE D N   
15162 C CA  . ILE D 365 ? 0.3417 0.3392 0.4243 0.0036  0.0010  -0.0027 365 ILE D CA  
15163 C C   . ILE D 365 ? 0.3132 0.3117 0.4044 -0.0135 0.0029  -0.0015 365 ILE D C   
15164 O O   . ILE D 365 ? 0.3140 0.3183 0.4065 -0.0151 0.0100  0.0031  365 ILE D O   
15165 C CB  . ILE D 365 ? 0.3387 0.3025 0.3913 0.0132  -0.0040 -0.0027 365 ILE D CB  
15166 C CG1 . ILE D 365 ? 0.3405 0.3061 0.3854 0.0321  -0.0022 -0.0020 365 ILE D CG1 
15167 C CG2 . ILE D 365 ? 0.2817 0.2276 0.3181 0.0133  -0.0007 0.0023  365 ILE D CG2 
15168 C CD1 . ILE D 365 ? 0.3626 0.2943 0.3773 0.0429  -0.0079 -0.0040 365 ILE D CD1 
15169 N N   . PRO D 366 ? 0.2929 0.2856 0.3897 -0.0268 -0.0030 -0.0050 366 PRO D N   
15170 C CA  . PRO D 366 ? 0.2944 0.2922 0.4034 -0.0434 0.0015  -0.0027 366 PRO D CA  
15171 C C   . PRO D 366 ? 0.3408 0.3691 0.4717 -0.0455 0.0111  -0.0005 366 PRO D C   
15172 O O   . PRO D 366 ? 0.3215 0.3495 0.4498 -0.0497 0.0190  0.0040  366 PRO D O   
15173 C CB  . PRO D 366 ? 0.3309 0.3266 0.4507 -0.0563 -0.0075 -0.0073 366 PRO D CB  
15174 C CG  . PRO D 366 ? 0.3314 0.3019 0.4285 -0.0467 -0.0182 -0.0113 366 PRO D CG  
15175 C CD  . PRO D 366 ? 0.3095 0.2877 0.3999 -0.0277 -0.0143 -0.0105 366 PRO D CD  
15176 N N   . PHE D 367 ? 0.2314 0.2836 0.3805 -0.0413 0.0107  -0.0037 367 PHE D N   
15177 C CA  . PHE D 367 ? 0.1901 0.2686 0.3577 -0.0426 0.0195  -0.0021 367 PHE D CA  
15178 C C   . PHE D 367 ? 0.2100 0.2867 0.3654 -0.0345 0.0260  0.0024  367 PHE D C   
15179 O O   . PHE D 367 ? 0.2412 0.3206 0.3972 -0.0403 0.0334  0.0059  367 PHE D O   
15180 C CB  . PHE D 367 ? 0.1445 0.2442 0.3288 -0.0369 0.0172  -0.0062 367 PHE D CB  
15181 C CG  . PHE D 367 ? 0.1902 0.3127 0.3885 -0.0357 0.0259  -0.0049 367 PHE D CG  
15182 C CD1 . PHE D 367 ? 0.2068 0.3434 0.4217 -0.0462 0.0327  -0.0039 367 PHE D CD1 
15183 C CD2 . PHE D 367 ? 0.2040 0.3323 0.3978 -0.0243 0.0281  -0.0041 367 PHE D CD2 
15184 C CE1 . PHE D 367 ? 0.2537 0.3990 0.4591 -0.0414 0.0377  -0.0017 367 PHE D CE1 
15185 C CE2 . PHE D 367 ? 0.2678 0.4093 0.4631 -0.0231 0.0339  -0.0027 367 PHE D CE2 
15186 C CZ  . PHE D 367 ? 0.2489 0.3948 0.4430 -0.0306 0.0373  -0.0015 367 PHE D CZ  
15187 N N   . LEU D 368 ? 0.2054 0.2765 0.3490 -0.0211 0.0232  0.0027  368 LEU D N   
15188 C CA  . LEU D 368 ? 0.2038 0.2780 0.3407 -0.0133 0.0278  0.0071  368 LEU D CA  
15189 C C   . LEU D 368 ? 0.2446 0.2995 0.3638 -0.0157 0.0295  0.0116  368 LEU D C   
15190 O O   . LEU D 368 ? 0.2255 0.2848 0.3427 -0.0159 0.0341  0.0152  368 LEU D O   
15191 C CB  . LEU D 368 ? 0.2187 0.2935 0.3502 0.0014  0.0250  0.0073  368 LEU D CB  
15192 C CG  . LEU D 368 ? 0.1975 0.2942 0.3457 0.0051  0.0261  0.0046  368 LEU D CG  
15193 C CD1 . LEU D 368 ? 0.1479 0.2444 0.2903 0.0195  0.0251  0.0060  368 LEU D CD1 
15194 C CD2 . LEU D 368 ? 0.2298 0.3450 0.3907 0.0000  0.0320  0.0058  368 LEU D CD2 
15195 N N   . GLU D 369 ? 0.2495 0.2802 0.3531 -0.0170 0.0251  0.0115  369 GLU D N   
15196 C CA  . GLU D 369 ? 0.2946 0.3034 0.3787 -0.0189 0.0266  0.0160  369 GLU D CA  
15197 C C   . GLU D 369 ? 0.3005 0.3119 0.3904 -0.0334 0.0330  0.0178  369 GLU D C   
15198 O O   . GLU D 369 ? 0.2814 0.2846 0.3593 -0.0336 0.0372  0.0223  369 GLU D O   
15199 C CB  . GLU D 369 ? 0.3038 0.2829 0.3680 -0.0177 0.0205  0.0151  369 GLU D CB  
15200 C CG  . GLU D 369 ? 0.3373 0.3064 0.3869 -0.0004 0.0166  0.0155  369 GLU D CG  
15201 C CD  . GLU D 369 ? 0.4092 0.3433 0.4333 0.0018  0.0111  0.0148  369 GLU D CD  
15202 O OE1 . GLU D 369 ? 0.4056 0.3246 0.4263 -0.0120 0.0084  0.0128  369 GLU D OE1 
15203 O OE2 . GLU D 369 ? 0.4141 0.3356 0.4215 0.0175  0.0098  0.0166  369 GLU D OE2 
15204 N N   . LYS D 370 ? 0.2986 0.3211 0.4067 -0.0450 0.0340  0.0146  370 LYS D N   
15205 C CA  . LYS D 370 ? 0.2884 0.3168 0.4052 -0.0581 0.0422  0.0169  370 LYS D CA  
15206 C C   . LYS D 370 ? 0.3178 0.3671 0.4434 -0.0548 0.0495  0.0181  370 LYS D C   
15207 O O   . LYS D 370 ? 0.3094 0.3544 0.4276 -0.0591 0.0570  0.0220  370 LYS D O   
15208 C CB  . LYS D 370 ? 0.3036 0.3418 0.4412 -0.0707 0.0410  0.0136  370 LYS D CB  
15209 C CG  . LYS D 370 ? 0.4223 0.4671 0.5710 -0.0847 0.0512  0.0169  370 LYS D CG  
15210 C CD  . LYS D 370 ? 0.5057 0.5223 0.6370 -0.0946 0.0523  0.0209  370 LYS D CD  
15211 C CE  . LYS D 370 ? 0.5551 0.5744 0.6903 -0.1057 0.0655  0.0261  370 LYS D CE  
15212 N NZ  . LYS D 370 ? 0.5706 0.5572 0.6787 -0.1104 0.0680  0.0313  370 LYS D NZ  
15213 N N   . LEU D 371 ? 0.2296 0.2987 0.3683 -0.0470 0.0473  0.0148  371 LEU D N   
15214 C CA  . LEU D 371 ? 0.2296 0.3151 0.3738 -0.0436 0.0529  0.0157  371 LEU D CA  
15215 C C   . LEU D 371 ? 0.2471 0.3208 0.3713 -0.0370 0.0529  0.0200  371 LEU D C   
15216 O O   . LEU D 371 ? 0.2298 0.3010 0.3469 -0.0405 0.0589  0.0229  371 LEU D O   
15217 C CB  . LEU D 371 ? 0.2446 0.3495 0.4035 -0.0361 0.0498  0.0117  371 LEU D CB  
15218 C CG  . LEU D 371 ? 0.2392 0.3586 0.4020 -0.0322 0.0541  0.0121  371 LEU D CG  
15219 C CD1 . LEU D 371 ? 0.2109 0.3361 0.3779 -0.0404 0.0629  0.0126  371 LEU D CD1 
15220 C CD2 . LEU D 371 ? 0.2246 0.3579 0.3964 -0.0250 0.0497  0.0082  371 LEU D CD2 
15221 N N   . TYR D 372 ? 0.1932 0.2586 0.3074 -0.0269 0.0461  0.0209  372 TYR D N   
15222 C CA  . TYR D 372 ? 0.2385 0.2966 0.3374 -0.0191 0.0444  0.0253  372 TYR D CA  
15223 C C   . TYR D 372 ? 0.2857 0.3210 0.3641 -0.0238 0.0469  0.0295  372 TYR D C   
15224 O O   . TYR D 372 ? 0.2972 0.3286 0.3642 -0.0220 0.0481  0.0330  372 TYR D O   
15225 C CB  . TYR D 372 ? 0.2274 0.2836 0.3230 -0.0064 0.0377  0.0259  372 TYR D CB  
15226 C CG  . TYR D 372 ? 0.2314 0.3094 0.3447 -0.0006 0.0364  0.0230  372 TYR D CG  
15227 C CD1 . TYR D 372 ? 0.1971 0.2935 0.3250 -0.0053 0.0399  0.0207  372 TYR D CD1 
15228 C CD2 . TYR D 372 ? 0.2492 0.3271 0.3625 0.0103  0.0324  0.0229  372 TYR D CD2 
15229 C CE1 . TYR D 372 ? 0.2025 0.3160 0.3443 -0.0002 0.0389  0.0184  372 TYR D CE1 
15230 C CE2 . TYR D 372 ? 0.1927 0.2884 0.3203 0.0154  0.0323  0.0211  372 TYR D CE2 
15231 C CZ  . TYR D 372 ? 0.2372 0.3503 0.3790 0.0098  0.0351  0.0188  372 TYR D CZ  
15232 O OH  . TYR D 372 ? 0.1872 0.3153 0.3412 0.0150  0.0351  0.0173  372 TYR D OH  
15233 N N   . SER D 373 ? 0.2713 0.2895 0.3433 -0.0301 0.0471  0.0294  373 SER D N   
15234 C CA  . SER D 373 ? 0.2974 0.2916 0.3491 -0.0358 0.0504  0.0337  373 SER D CA  
15235 C C   . SER D 373 ? 0.2890 0.2881 0.3433 -0.0459 0.0600  0.0353  373 SER D C   
15236 O O   . SER D 373 ? 0.3080 0.2919 0.3429 -0.0463 0.0634  0.0397  373 SER D O   
15237 C CB  . SER D 373 ? 0.3668 0.3415 0.4128 -0.0424 0.0484  0.0328  373 SER D CB  
15238 O OG  . SER D 373 ? 0.5351 0.4869 0.5633 -0.0506 0.0534  0.0372  373 SER D OG  
15239 N N   . THR D 374 ? 0.3505 0.3701 0.4273 -0.0530 0.0647  0.0319  374 THR D N   
15240 C CA  . THR D 374 ? 0.3651 0.3922 0.4456 -0.0600 0.0752  0.0333  374 THR D CA  
15241 C C   . THR D 374 ? 0.3759 0.4087 0.4481 -0.0519 0.0751  0.0340  374 THR D C   
15242 O O   . THR D 374 ? 0.3600 0.3803 0.4141 -0.0533 0.0804  0.0377  374 THR D O   
15243 C CB  . THR D 374 ? 0.3306 0.3804 0.4391 -0.0671 0.0794  0.0294  374 THR D CB  
15244 O OG1 . THR D 374 ? 0.2544 0.2973 0.3698 -0.0761 0.0776  0.0290  374 THR D OG1 
15245 C CG2 . THR D 374 ? 0.3801 0.4383 0.4928 -0.0729 0.0922  0.0313  374 THR D CG2 
15246 N N   . LEU D 375 ? 0.3268 0.3763 0.4103 -0.0437 0.0686  0.0308  375 LEU D N   
15247 C CA  . LEU D 375 ? 0.2719 0.3278 0.3501 -0.0376 0.0671  0.0311  375 LEU D CA  
15248 C C   . LEU D 375 ? 0.3890 0.4261 0.4423 -0.0326 0.0627  0.0358  375 LEU D C   
15249 O O   . LEU D 375 ? 0.4431 0.4751 0.4829 -0.0325 0.0646  0.0375  375 LEU D O   
15250 C CB  . LEU D 375 ? 0.3075 0.3825 0.4021 -0.0302 0.0603  0.0277  375 LEU D CB  
15251 C CG  . LEU D 375 ? 0.2857 0.3799 0.4026 -0.0337 0.0645  0.0230  375 LEU D CG  
15252 C CD1 . LEU D 375 ? 0.2657 0.3755 0.3955 -0.0259 0.0581  0.0202  375 LEU D CD1 
15253 C CD2 . LEU D 375 ? 0.2444 0.3422 0.3604 -0.0388 0.0738  0.0228  375 LEU D CD2 
15254 N N   . GLU D 376 ? 0.3115 0.3358 0.3561 -0.0277 0.0565  0.0381  376 GLU D N   
15255 C CA  . GLU D 376 ? 0.3230 0.3314 0.3454 -0.0208 0.0509  0.0428  376 GLU D CA  
15256 C C   . GLU D 376 ? 0.3522 0.3376 0.3507 -0.0267 0.0575  0.0466  376 GLU D C   
15257 O O   . GLU D 376 ? 0.3665 0.3396 0.3448 -0.0214 0.0532  0.0502  376 GLU D O   
15258 C CB  . GLU D 376 ? 0.3307 0.3306 0.3490 -0.0121 0.0436  0.0445  376 GLU D CB  
15259 C CG  . GLU D 376 ? 0.3265 0.3031 0.3322 -0.0169 0.0466  0.0458  376 GLU D CG  
15260 C CD  . GLU D 376 ? 0.4290 0.3926 0.4249 -0.0062 0.0395  0.0478  376 GLU D CD  
15261 O OE1 . GLU D 376 ? 0.4331 0.3743 0.4162 -0.0101 0.0410  0.0486  376 GLU D OE1 
15262 O OE2 . GLU D 376 ? 0.4447 0.4195 0.4455 0.0058  0.0328  0.0488  376 GLU D OE2 
15263 N N   . LYS D 377 ? 0.3063 0.2865 0.3073 -0.0375 0.0677  0.0462  377 LYS D N   
15264 C CA  . LYS D 377 ? 0.3897 0.3481 0.3688 -0.0442 0.0766  0.0505  377 LYS D CA  
15265 C C   . LYS D 377 ? 0.4128 0.3781 0.3914 -0.0484 0.0859  0.0499  377 LYS D C   
15266 O O   . LYS D 377 ? 0.4580 0.4035 0.4117 -0.0497 0.0916  0.0539  377 LYS D O   
15267 C CB  . LYS D 377 ? 0.4390 0.3867 0.4214 -0.0549 0.0838  0.0516  377 LYS D CB  
15268 C CG  . LYS D 377 ? 0.5395 0.4681 0.5107 -0.0514 0.0762  0.0532  377 LYS D CG  
15269 C CD  . LYS D 377 ? 0.6371 0.5572 0.6155 -0.0637 0.0812  0.0531  377 LYS D CD  
15270 C CE  . LYS D 377 ? 0.7301 0.6474 0.7138 -0.0592 0.0710  0.0501  377 LYS D CE  
15271 N NZ  . LYS D 377 ? 0.7378 0.6783 0.7517 -0.0652 0.0703  0.0445  377 LYS D NZ  
15272 N N   . GLU D 378 ? 0.4060 0.3961 0.4088 -0.0499 0.0884  0.0453  378 GLU D N   
15273 C CA  . GLU D 378 ? 0.4227 0.4179 0.4236 -0.0525 0.0981  0.0446  378 GLU D CA  
15274 C C   . GLU D 378 ? 0.4460 0.4330 0.4255 -0.0449 0.0914  0.0451  378 GLU D C   
15275 O O   . GLU D 378 ? 0.4619 0.4600 0.4486 -0.0382 0.0797  0.0428  378 GLU D O   
15276 C CB  . GLU D 378 ? 0.3493 0.3721 0.3805 -0.0542 0.1011  0.0394  378 GLU D CB  
15277 C CG  . GLU D 378 ? 0.3631 0.3966 0.4181 -0.0617 0.1048  0.0383  378 GLU D CG  
15278 C CD  . GLU D 378 ? 0.5165 0.5428 0.5703 -0.0719 0.1193  0.0421  378 GLU D CD  
15279 O OE1 . GLU D 378 ? 0.5630 0.5725 0.5934 -0.0723 0.1275  0.0460  378 GLU D OE1 
15280 O OE2 . GLU D 378 ? 0.5436 0.5804 0.6194 -0.0798 0.1224  0.0415  378 GLU D OE2 
15281 N N   . GLU D 379 ? 0.4219 0.3888 0.3747 -0.0463 0.0988  0.0484  379 GLU D N   
15282 C CA  . GLU D 379 ? 0.4186 0.3733 0.3465 -0.0397 0.0910  0.0490  379 GLU D CA  
15283 C C   . GLU D 379 ? 0.4335 0.3983 0.3640 -0.0388 0.0937  0.0449  379 GLU D C   
15284 O O   . GLU D 379 ? 0.4854 0.4465 0.4035 -0.0336 0.0828  0.0437  379 GLU D O   
15285 C CB  . GLU D 379 ? 0.4115 0.3343 0.3027 -0.0401 0.0963  0.0545  379 GLU D CB  
15286 N N   . TRP D 380 ? 0.3655 0.3424 0.3119 -0.0435 0.1072  0.0428  380 TRP D N   
15287 C CA  . TRP D 380 ? 0.3439 0.3298 0.2931 -0.0416 0.1106  0.0387  380 TRP D CA  
15288 C C   . TRP D 380 ? 0.3160 0.3272 0.2934 -0.0391 0.1009  0.0336  380 TRP D C   
15289 O O   . TRP D 380 ? 0.3528 0.3704 0.3322 -0.0371 0.1021  0.0299  380 TRP D O   
15290 C CB  . TRP D 380 ? 0.4108 0.4002 0.3660 -0.0460 0.1302  0.0393  380 TRP D CB  
15291 C CG  . TRP D 380 ? 0.4094 0.4191 0.3975 -0.0518 0.1354  0.0393  380 TRP D CG  
15292 C CD1 . TRP D 380 ? 0.4425 0.4470 0.4346 -0.0578 0.1378  0.0431  380 TRP D CD1 
15293 C CD2 . TRP D 380 ? 0.4387 0.4758 0.4597 -0.0522 0.1371  0.0349  380 TRP D CD2 
15294 N NE1 . TRP D 380 ? 0.4433 0.4706 0.4692 -0.0627 0.1402  0.0412  380 TRP D NE1 
15295 C CE2 . TRP D 380 ? 0.4221 0.4702 0.4662 -0.0587 0.1392  0.0362  380 TRP D CE2 
15296 C CE3 . TRP D 380 ? 0.4343 0.4856 0.4654 -0.0475 0.1363  0.0301  380 TRP D CE3 
15297 C CZ2 . TRP D 380 ? 0.3883 0.4613 0.4616 -0.0578 0.1323  0.0320  380 TRP D CZ2 
15298 C CZ3 . TRP D 380 ? 0.4095 0.4853 0.4707 -0.0469 0.1325  0.0266  380 TRP D CZ3 
15299 C CH2 . TRP D 380 ? 0.3713 0.4576 0.4516 -0.0513 0.1286  0.0275  380 TRP D CH2 
15300 N N   . ILE D 381 ? 0.2925 0.3157 0.2891 -0.0387 0.0922  0.0336  381 ILE D N   
15301 C CA  . ILE D 381 ? 0.2762 0.3207 0.2966 -0.0354 0.0825  0.0298  381 ILE D CA  
15302 C C   . ILE D 381 ? 0.2767 0.3172 0.2898 -0.0303 0.0673  0.0317  381 ILE D C   
15303 O O   . ILE D 381 ? 0.3389 0.3703 0.3457 -0.0291 0.0638  0.0352  381 ILE D O   
15304 C CB  . ILE D 381 ? 0.2606 0.3224 0.3092 -0.0378 0.0853  0.0282  381 ILE D CB  
15305 C CG1 . ILE D 381 ? 0.3596 0.4287 0.4195 -0.0432 0.0997  0.0271  381 ILE D CG1 
15306 C CG2 . ILE D 381 ? 0.2208 0.3018 0.2904 -0.0334 0.0758  0.0248  381 ILE D CG2 
15307 C CD1 . ILE D 381 ? 0.3379 0.4243 0.4261 -0.0461 0.1000  0.0252  381 ILE D CD1 
15308 N N   . GLU D 382 ? 0.2770 0.3242 0.2918 -0.0272 0.0583  0.0298  382 GLU D N   
15309 C CA  . GLU D 382 ? 0.2476 0.2984 0.2642 -0.0223 0.0437  0.0319  382 GLU D CA  
15310 C C   . GLU D 382 ? 0.2228 0.2972 0.2678 -0.0204 0.0398  0.0293  382 GLU D C   
15311 O O   . GLU D 382 ? 0.1939 0.2764 0.2454 -0.0217 0.0400  0.0259  382 GLU D O   
15312 C CB  . GLU D 382 ? 0.3736 0.4124 0.3688 -0.0213 0.0345  0.0327  382 GLU D CB  
15313 C CG  . GLU D 382 ? 0.5081 0.5530 0.5077 -0.0164 0.0188  0.0359  382 GLU D CG  
15314 C CD  . GLU D 382 ? 0.7080 0.7378 0.6834 -0.0161 0.0080  0.0372  382 GLU D CD  
15315 O OE1 . GLU D 382 ? 0.7787 0.8179 0.7620 -0.0133 -0.0064 0.0393  382 GLU D OE1 
15316 O OE2 . GLU D 382 ? 0.7369 0.7453 0.6854 -0.0185 0.0137  0.0364  382 GLU D OE2 
15317 N N   . THR D 383 ? 0.1804 0.2635 0.2397 -0.0168 0.0366  0.0309  383 THR D N   
15318 C CA  . THR D 383 ? 0.1454 0.2488 0.2284 -0.0135 0.0324  0.0294  383 THR D CA  
15319 C C   . THR D 383 ? 0.1556 0.2649 0.2398 -0.0102 0.0206  0.0320  383 THR D C   
15320 O O   . THR D 383 ? 0.2216 0.3219 0.2928 -0.0077 0.0133  0.0360  383 THR D O   
15321 C CB  . THR D 383 ? 0.1883 0.2967 0.2834 -0.0095 0.0332  0.0304  383 THR D CB  
15322 O OG1 . THR D 383 ? 0.2029 0.3002 0.2860 -0.0050 0.0278  0.0351  383 THR D OG1 
15323 C CG2 . THR D 383 ? 0.1688 0.2739 0.2667 -0.0143 0.0430  0.0276  383 THR D CG2 
15324 N N   . LEU D 384 ? 0.1982 0.3232 0.2993 -0.0103 0.0183  0.0302  384 LEU D N   
15325 C CA  . LEU D 384 ? 0.1861 0.3187 0.2916 -0.0097 0.0072  0.0325  384 LEU D CA  
15326 C C   . LEU D 384 ? 0.1865 0.3398 0.3173 -0.0054 0.0050  0.0343  384 LEU D C   
15327 O O   . LEU D 384 ? 0.2000 0.3608 0.3429 -0.0046 0.0122  0.0316  384 LEU D O   
15328 C CB  . LEU D 384 ? 0.1637 0.2916 0.2613 -0.0159 0.0061  0.0290  384 LEU D CB  
15329 C CG  . LEU D 384 ? 0.2247 0.3303 0.2941 -0.0196 0.0090  0.0271  384 LEU D CG  
15330 C CD1 . LEU D 384 ? 0.2332 0.3332 0.2946 -0.0244 0.0087  0.0230  384 LEU D CD1 
15331 C CD2 . LEU D 384 ? 0.2415 0.3350 0.2932 -0.0178 -0.0010 0.0315  384 LEU D CD2 
15332 N N   . THR D 385 ? 0.1825 0.3452 0.3213 -0.0025 -0.0050 0.0392  385 THR D N   
15333 C CA  . THR D 385 ? 0.1267 0.3101 0.2900 0.0000  -0.0066 0.0414  385 THR D CA  
15334 C C   . THR D 385 ? 0.2014 0.3880 0.3689 -0.0076 -0.0069 0.0379  385 THR D C   
15335 O O   . THR D 385 ? 0.2196 0.3920 0.3698 -0.0138 -0.0072 0.0341  385 THR D O   
15336 C CB  . THR D 385 ? 0.1847 0.3801 0.3584 0.0048  -0.0170 0.0484  385 THR D CB  
15337 O OG1 . THR D 385 ? 0.2073 0.3977 0.3716 -0.0013 -0.0282 0.0490  385 THR D OG1 
15338 C CG2 . THR D 385 ? 0.2376 0.4264 0.4036 0.0138  -0.0166 0.0519  385 THR D CG2 
15339 N N   . LEU D 386 ? 0.1736 0.3654 0.3521 -0.0063 -0.0055 0.0359  386 LEU D N   
15340 C CA  . LEU D 386 ? 0.1694 0.3607 0.3497 -0.0130 -0.0069 0.0327  386 LEU D CA  
15341 C C   . LEU D 386 ? 0.1326 0.3333 0.3187 -0.0200 -0.0202 0.0384  386 LEU D C   
15342 O O   . LEU D 386 ? 0.1801 0.3743 0.3590 -0.0282 -0.0238 0.0360  386 LEU D O   
15343 C CB  . LEU D 386 ? 0.1281 0.3153 0.3106 -0.0096 -0.0026 0.0281  386 LEU D CB  
15344 C CG  . LEU D 386 ? 0.1414 0.3182 0.3157 -0.0041 0.0065  0.0218  386 LEU D CG  
15345 C CD1 . LEU D 386 ? 0.0874 0.2627 0.2629 -0.0017 0.0089  0.0191  386 LEU D CD1 
15346 C CD2 . LEU D 386 ? 0.1336 0.3034 0.3005 -0.0072 0.0119  0.0169  386 LEU D CD2 
15347 N N   . GLU D 387 ? 0.1733 0.3807 0.3655 -0.0161 -0.0279 0.0432  387 GLU D N   
15348 C CA  . GLU D 387 ? 0.1741 0.3881 0.3697 -0.0224 -0.0437 0.0480  387 GLU D CA  
15349 C C   . GLU D 387 ? 0.1858 0.3752 0.3502 -0.0262 -0.0475 0.0439  387 GLU D C   
15350 O O   . GLU D 387 ? 0.2171 0.3957 0.3692 -0.0343 -0.0560 0.0416  387 GLU D O   
15351 C CB  . GLU D 387 ? 0.1718 0.3931 0.3747 -0.0145 -0.0492 0.0526  387 GLU D CB  
15352 C CG  . GLU D 387 ? 0.3846 0.6120 0.5927 -0.0199 -0.0655 0.0561  387 GLU D CG  
15353 C CD  . GLU D 387 ? 0.5867 0.8203 0.7971 -0.0115 -0.0734 0.0618  387 GLU D CD  
15354 O OE1 . GLU D 387 ? 0.6463 0.8740 0.8430 -0.0095 -0.0802 0.0651  387 GLU D OE1 
15355 O OE2 . GLU D 387 ? 0.6509 0.8938 0.8746 -0.0066 -0.0726 0.0630  387 GLU D OE2 
15356 N N   . GLU D 388 ? 0.1681 0.3450 0.3162 -0.0206 -0.0403 0.0425  388 GLU D N   
15357 C CA  . GLU D 388 ? 0.2798 0.4308 0.3956 -0.0234 -0.0413 0.0389  388 GLU D CA  
15358 C C   . GLU D 388 ? 0.2784 0.4158 0.3808 -0.0293 -0.0336 0.0322  388 GLU D C   
15359 O O   . GLU D 388 ? 0.4015 0.5209 0.4816 -0.0345 -0.0394 0.0296  388 GLU D O   
15360 C CB  . GLU D 388 ? 0.2395 0.3805 0.3427 -0.0168 -0.0339 0.0398  388 GLU D CB  
15361 C CG  . GLU D 388 ? 0.2704 0.4168 0.3768 -0.0102 -0.0436 0.0462  388 GLU D CG  
15362 C CD  . GLU D 388 ? 0.3413 0.4791 0.4391 -0.0032 -0.0351 0.0475  388 GLU D CD  
15363 O OE1 . GLU D 388 ? 0.3022 0.4368 0.4004 -0.0036 -0.0222 0.0440  388 GLU D OE1 
15364 O OE2 . GLU D 388 ? 0.4169 0.5501 0.5068 0.0026  -0.0421 0.0521  388 GLU D OE2 
15365 N N   . ALA D 389 ? 0.2162 0.3608 0.3306 -0.0278 -0.0210 0.0295  389 ALA D N   
15366 C CA  . ALA D 389 ? 0.2021 0.3360 0.3063 -0.0317 -0.0131 0.0236  389 ALA D CA  
15367 C C   . ALA D 389 ? 0.2696 0.4010 0.3730 -0.0386 -0.0221 0.0223  389 ALA D C   
15368 O O   . ALA D 389 ? 0.2625 0.3749 0.3444 -0.0423 -0.0208 0.0178  389 ALA D O   
15369 C CB  . ALA D 389 ? 0.2166 0.3622 0.3379 -0.0279 -0.0006 0.0216  389 ALA D CB  
15370 N N   . MET D 390 ? 0.2757 0.4251 0.4016 -0.0406 -0.0311 0.0267  390 MET D N   
15371 C CA  . MET D 390 ? 0.3313 0.4780 0.4576 -0.0491 -0.0407 0.0260  390 MET D CA  
15372 C C   . MET D 390 ? 0.3032 0.4318 0.4058 -0.0544 -0.0551 0.0257  390 MET D C   
15373 O O   . MET D 390 ? 0.3366 0.4471 0.4212 -0.0612 -0.0599 0.0217  390 MET D O   
15374 C CB  . MET D 390 ? 0.3733 0.5462 0.5329 -0.0506 -0.0456 0.0319  390 MET D CB  
15375 C CG  . MET D 390 ? 0.5750 0.7469 0.7373 -0.0611 -0.0601 0.0332  390 MET D CG  
15376 S SD  . MET D 390 ? 0.7007 0.8991 0.8998 -0.0635 -0.0614 0.0390  390 MET D SD  
15377 C CE  . MET D 390 ? 0.7697 0.9558 0.9617 -0.0803 -0.0760 0.0377  390 MET D CE  
15378 N N   . ARG D 391 ? 0.2576 0.3883 0.3574 -0.0509 -0.0627 0.0296  391 ARG D N   
15379 C CA  . ARG D 391 ? 0.3073 0.4228 0.3865 -0.0551 -0.0792 0.0303  391 ARG D CA  
15380 C C   . ARG D 391 ? 0.3480 0.4317 0.3864 -0.0531 -0.0755 0.0259  391 ARG D C   
15381 O O   . ARG D 391 ? 0.4149 0.4791 0.4285 -0.0569 -0.0887 0.0250  391 ARG D O   
15382 C CB  . ARG D 391 ? 0.3722 0.5064 0.4690 -0.0510 -0.0904 0.0376  391 ARG D CB  
15383 C CG  . ARG D 391 ? 0.4342 0.6014 0.5722 -0.0518 -0.0937 0.0434  391 ARG D CG  
15384 C CD  . ARG D 391 ? 0.5449 0.7170 0.6923 -0.0629 -0.1103 0.0448  391 ARG D CD  
15385 N NE  . ARG D 391 ? 0.6320 0.8374 0.8200 -0.0625 -0.1134 0.0520  391 ARG D NE  
15386 C CZ  . ARG D 391 ? 0.7338 0.9458 0.9304 -0.0635 -0.1253 0.0545  391 ARG D CZ  
15387 N NH1 . ARG D 391 ? 0.7720 0.9709 0.9502 -0.0695 -0.1446 0.0545  391 ARG D NH1 
15388 N NH2 . ARG D 391 ? 0.7657 0.9959 0.9869 -0.0584 -0.1179 0.0566  391 ARG D NH2 
15389 N N   . LYS D 392 ? 0.3693 0.4472 0.4000 -0.0473 -0.0581 0.0236  392 LYS D N   
15390 C CA  . LYS D 392 ? 0.4293 0.4798 0.4243 -0.0446 -0.0523 0.0212  392 LYS D CA  
15391 C C   . LYS D 392 ? 0.4866 0.5088 0.4491 -0.0495 -0.0560 0.0160  392 LYS D C   
15392 O O   . LYS D 392 ? 0.4819 0.5027 0.4472 -0.0531 -0.0523 0.0121  392 LYS D O   
15393 C CB  . LYS D 392 ? 0.4016 0.4548 0.4005 -0.0394 -0.0320 0.0196  392 LYS D CB  
15394 C CG  . LYS D 392 ? 0.5073 0.5389 0.4775 -0.0359 -0.0237 0.0195  392 LYS D CG  
15395 C CD  . LYS D 392 ? 0.5935 0.6247 0.5600 -0.0324 -0.0318 0.0249  392 LYS D CD  
15396 C CE  . LYS D 392 ? 0.5716 0.6222 0.5630 -0.0277 -0.0238 0.0280  392 LYS D CE  
15397 N NZ  . LYS D 392 ? 0.6331 0.6747 0.6115 -0.0232 -0.0283 0.0328  392 LYS D NZ  
15398 N N   . GLU D 393 ? 0.5524 0.5496 0.4812 -0.0491 -0.0637 0.0160  393 GLU D N   
15399 C CA  . GLU D 393 ? 0.6540 0.6198 0.5466 -0.0531 -0.0693 0.0112  393 GLU D CA  
15400 C C   . GLU D 393 ? 0.6183 0.5605 0.4818 -0.0485 -0.0498 0.0071  393 GLU D C   
15401 O O   . GLU D 393 ? 0.6795 0.6025 0.5231 -0.0503 -0.0467 0.0021  393 GLU D O   
15402 C CB  . GLU D 393 ? 0.7816 0.7292 0.6487 -0.0547 -0.0892 0.0131  393 GLU D CB  
15403 C CG  . GLU D 393 ? 0.9009 0.8630 0.7878 -0.0624 -0.1125 0.0153  393 GLU D CG  
15404 C CD  . GLU D 393 ? 1.0526 0.9958 0.9128 -0.0634 -0.1338 0.0170  393 GLU D CD  
15405 O OE1 . GLU D 393 ? 1.1078 1.0330 0.9409 -0.0564 -0.1300 0.0183  393 GLU D OE1 
15406 O OE2 . GLU D 393 ? 1.0927 1.0383 0.9585 -0.0715 -0.1549 0.0174  393 GLU D OE2 
15407 N N   . ASP D 394 ? 0.5701 0.5130 0.4311 -0.0424 -0.0362 0.0095  394 ASP D N   
15408 C CA  . ASP D 394 ? 0.6302 0.5521 0.4647 -0.0381 -0.0170 0.0070  394 ASP D CA  
15409 C C   . ASP D 394 ? 0.5778 0.5187 0.4380 -0.0362 0.0013  0.0050  394 ASP D C   
15410 O O   . ASP D 394 ? 0.5939 0.5388 0.4579 -0.0324 0.0181  0.0062  394 ASP D O   
15411 C CB  . ASP D 394 ? 0.7343 0.6451 0.5514 -0.0337 -0.0113 0.0111  394 ASP D CB  
15412 C CG  . ASP D 394 ? 0.7492 0.6858 0.5972 -0.0327 -0.0157 0.0163  394 ASP D CG  
15413 O OD1 . ASP D 394 ? 0.7270 0.6919 0.6115 -0.0345 -0.0194 0.0167  394 ASP D OD1 
15414 O OD2 . ASP D 394 ? 0.7691 0.6960 0.6031 -0.0295 -0.0146 0.0203  394 ASP D OD2 
15415 N N   . VAL D 395 ? 0.5415 0.4943 0.4202 -0.0394 -0.0025 0.0021  395 VAL D N   
15416 C CA  . VAL D 395 ? 0.5440 0.5121 0.4439 -0.0370 0.0127  -0.0003 395 VAL D CA  
15417 C C   . VAL D 395 ? 0.5058 0.4546 0.3860 -0.0379 0.0132  -0.0056 395 VAL D C   
15418 O O   . VAL D 395 ? 0.5498 0.4797 0.4092 -0.0425 -0.0015 -0.0073 395 VAL D O   
15419 C CB  . VAL D 395 ? 0.5016 0.5035 0.4449 -0.0385 0.0092  0.0018  395 VAL D CB  
15420 C CG1 . VAL D 395 ? 0.5273 0.5445 0.4863 -0.0365 0.0097  0.0067  395 VAL D CG1 
15421 C CG2 . VAL D 395 ? 0.4900 0.4965 0.4418 -0.0447 -0.0087 0.0022  395 VAL D CG2 
15422 N N   . LYS D 396 ? 0.4736 0.4264 0.3600 -0.0333 0.0296  -0.0083 396 LYS D N   
15423 C CA  . LYS D 396 ? 0.4211 0.3558 0.2897 -0.0324 0.0319  -0.0133 396 LYS D CA  
15424 C C   . LYS D 396 ? 0.4304 0.3826 0.3263 -0.0364 0.0245  -0.0143 396 LYS D C   
15425 O O   . LYS D 396 ? 0.3316 0.3131 0.2629 -0.0357 0.0279  -0.0121 396 LYS D O   
15426 C CB  . LYS D 396 ? 0.5223 0.4521 0.3832 -0.0238 0.0536  -0.0154 396 LYS D CB  
15427 C CG  . LYS D 396 ? 0.6813 0.5827 0.5114 -0.0206 0.0568  -0.0205 396 LYS D CG  
15428 C CD  . LYS D 396 ? 0.6799 0.5895 0.5196 -0.0118 0.0764  -0.0223 396 LYS D CD  
15429 C CE  . LYS D 396 ? 0.6653 0.5716 0.4945 -0.0048 0.0949  -0.0202 396 LYS D CE  
15430 N NZ  . LYS D 396 ? 0.7175 0.5864 0.4992 -0.0029 0.0954  -0.0209 396 LYS D NZ  
15431 N N   . THR D 397 ? 0.5192 0.4502 0.3952 -0.0404 0.0154  -0.0177 397 THR D N   
15432 C CA  . THR D 397 ? 0.5507 0.4913 0.4457 -0.0471 0.0044  -0.0180 397 THR D CA  
15433 C C   . THR D 397 ? 0.5266 0.4474 0.4044 -0.0445 0.0111  -0.0230 397 THR D C   
15434 O O   . THR D 397 ? 0.5352 0.4271 0.3776 -0.0394 0.0181  -0.0267 397 THR D O   
15435 C CB  . THR D 397 ? 0.6288 0.5610 0.5160 -0.0572 -0.0177 -0.0162 397 THR D CB  
15436 O OG1 . THR D 397 ? 0.6382 0.5984 0.5544 -0.0588 -0.0240 -0.0106 397 THR D OG1 
15437 C CG2 . THR D 397 ? 0.6633 0.5901 0.5539 -0.0657 -0.0293 -0.0177 397 THR D CG2 
15438 N N   . GLU D 398 ? 0.4698 0.4048 0.3711 -0.0469 0.0100  -0.0230 398 GLU D N   
15439 C CA  . GLU D 398 ? 0.4487 0.3640 0.3338 -0.0443 0.0155  -0.0275 398 GLU D CA  
15440 C C   . GLU D 398 ? 0.4484 0.3732 0.3543 -0.0527 0.0054  -0.0261 398 GLU D C   
15441 O O   . GLU D 398 ? 0.3780 0.3340 0.3199 -0.0547 0.0040  -0.0218 398 GLU D O   
15442 C CB  . GLU D 398 ? 0.5449 0.4699 0.4379 -0.0318 0.0358  -0.0290 398 GLU D CB  
15443 C CG  . GLU D 398 ? 0.7685 0.6649 0.6325 -0.0249 0.0444  -0.0341 398 GLU D CG  
15444 C CD  . GLU D 398 ? 0.8819 0.7939 0.7612 -0.0122 0.0630  -0.0348 398 GLU D CD  
15445 O OE1 . GLU D 398 ? 0.9189 0.8203 0.7918 -0.0074 0.0674  -0.0376 398 GLU D OE1 
15446 O OE2 . GLU D 398 ? 0.8985 0.8328 0.7960 -0.0072 0.0727  -0.0325 398 GLU D OE2 
15447 N N   . VAL D 399 ? 0.4510 0.3471 0.3326 -0.0572 -0.0006 -0.0297 399 VAL D N   
15448 C CA  . VAL D 399 ? 0.5011 0.4024 0.3998 -0.0652 -0.0075 -0.0283 399 VAL D CA  
15449 C C   . VAL D 399 ? 0.5045 0.4108 0.4115 -0.0553 0.0081  -0.0299 399 VAL D C   
15450 O O   . VAL D 399 ? 0.5170 0.4062 0.4016 -0.0445 0.0204  -0.0341 399 VAL D O   
15451 C CB  . VAL D 399 ? 0.5104 0.3766 0.3788 -0.0762 -0.0226 -0.0312 399 VAL D CB  
15452 C CG1 . VAL D 399 ? 0.5008 0.3690 0.3847 -0.0845 -0.0272 -0.0296 399 VAL D CG1 
15453 C CG2 . VAL D 399 ? 0.4919 0.3587 0.3585 -0.0865 -0.0405 -0.0288 399 VAL D CG2 
15454 N N   . ILE D 400 ? 0.4547 0.3851 0.3941 -0.0580 0.0080  -0.0262 400 ILE D N   
15455 C CA  . ILE D 400 ? 0.4359 0.3703 0.3837 -0.0497 0.0200  -0.0272 400 ILE D CA  
15456 C C   . ILE D 400 ? 0.3858 0.3114 0.3367 -0.0599 0.0118  -0.0256 400 ILE D C   
15457 O O   . ILE D 400 ? 0.3952 0.3353 0.3664 -0.0715 0.0006  -0.0208 400 ILE D O   
15458 C CB  . ILE D 400 ? 0.4489 0.4201 0.4314 -0.0418 0.0293  -0.0240 400 ILE D CB  
15459 C CG1 . ILE D 400 ? 0.4221 0.3975 0.4131 -0.0329 0.0397  -0.0249 400 ILE D CG1 
15460 C CG2 . ILE D 400 ? 0.4476 0.4459 0.4611 -0.0502 0.0203  -0.0179 400 ILE D CG2 
15461 C CD1 . ILE D 400 ? 0.3536 0.3582 0.3698 -0.0227 0.0496  -0.0236 400 ILE D CD1 
15462 N N   . GLU D 401 ? 0.4080 0.3084 0.3380 -0.0558 0.0171  -0.0292 401 GLU D N   
15463 C CA  . GLU D 401 ? 0.4194 0.3056 0.3476 -0.0669 0.0093  -0.0276 401 GLU D CA  
15464 C C   . GLU D 401 ? 0.3843 0.2888 0.3376 -0.0630 0.0173  -0.0241 401 GLU D C   
15465 O O   . GLU D 401 ? 0.4310 0.3356 0.3953 -0.0741 0.0110  -0.0201 401 GLU D O   
15466 C CB  . GLU D 401 ? 0.5451 0.3851 0.4295 -0.0669 0.0080  -0.0335 401 GLU D CB  
15467 C CG  . GLU D 401 ? 0.7131 0.5280 0.5645 -0.0687 0.0013  -0.0377 401 GLU D CG  
15468 C CD  . GLU D 401 ? 0.8285 0.6438 0.6839 -0.0865 -0.0184 -0.0351 401 GLU D CD  
15469 O OE1 . GLU D 401 ? 0.9105 0.7061 0.7389 -0.0879 -0.0254 -0.0382 401 GLU D OE1 
15470 O OE2 . GLU D 401 ? 0.8466 0.6817 0.7316 -0.0986 -0.0268 -0.0296 401 GLU D OE2 
15471 N N   . SER D 402 ? 0.3417 0.2619 0.3049 -0.0479 0.0305  -0.0250 402 SER D N   
15472 C CA  . SER D 402 ? 0.3615 0.2932 0.3417 -0.0422 0.0380  -0.0225 402 SER D CA  
15473 C C   . SER D 402 ? 0.3442 0.3047 0.3452 -0.0286 0.0479  -0.0223 402 SER D C   
15474 O O   . SER D 402 ? 0.3496 0.3132 0.3447 -0.0213 0.0522  -0.0254 402 SER D O   
15475 C CB  . SER D 402 ? 0.4145 0.3127 0.3662 -0.0369 0.0429  -0.0263 402 SER D CB  
15476 O OG  . SER D 402 ? 0.4892 0.3973 0.4538 -0.0276 0.0514  -0.0244 402 SER D OG  
15477 N N   . VAL D 403 ? 0.3236 0.3048 0.3488 -0.0259 0.0512  -0.0184 403 VAL D N   
15478 C CA  . VAL D 403 ? 0.3588 0.3635 0.4014 -0.0129 0.0596  -0.0187 403 VAL D CA  
15479 C C   . VAL D 403 ? 0.3389 0.3397 0.3821 -0.0044 0.0658  -0.0182 403 VAL D C   
15480 O O   . VAL D 403 ? 0.3553 0.3428 0.3938 -0.0108 0.0636  -0.0156 403 VAL D O   
15481 C CB  . VAL D 403 ? 0.2600 0.2963 0.3316 -0.0159 0.0568  -0.0143 403 VAL D CB  
15482 C CG1 . VAL D 403 ? 0.2190 0.2574 0.2880 -0.0236 0.0501  -0.0144 403 VAL D CG1 
15483 C CG2 . VAL D 403 ? 0.2364 0.2827 0.3258 -0.0229 0.0536  -0.0081 403 VAL D CG2 
15484 N N   . LYS D 404 ? 0.3622 0.3734 0.4103 0.0098  0.0733  -0.0207 404 LYS D N   
15485 C CA  . LYS D 404 ? 0.3920 0.4033 0.4430 0.0197  0.0782  -0.0201 404 LYS D CA  
15486 C C   . LYS D 404 ? 0.3523 0.3900 0.4295 0.0197  0.0772  -0.0157 404 LYS D C   
15487 O O   . LYS D 404 ? 0.3431 0.4025 0.4362 0.0224  0.0772  -0.0161 404 LYS D O   
15488 C CB  . LYS D 404 ? 0.4244 0.4344 0.4684 0.0356  0.0853  -0.0248 404 LYS D CB  
15489 C CG  . LYS D 404 ? 0.5678 0.5463 0.5816 0.0395  0.0883  -0.0286 404 LYS D CG  
15490 C CD  . LYS D 404 ? 0.6094 0.5843 0.6175 0.0571  0.0955  -0.0312 404 LYS D CD  
15491 C CE  . LYS D 404 ? 0.6488 0.5939 0.6265 0.0635  0.1000  -0.0353 404 LYS D CE  
15492 N NZ  . LYS D 404 ? 0.7000 0.6545 0.6807 0.0818  0.1080  -0.0381 404 LYS D NZ  
15493 N N   . ALA D 405 ? 0.3495 0.3834 0.4297 0.0165  0.0770  -0.0113 405 ALA D N   
15494 C CA  . ALA D 405 ? 0.2956 0.3511 0.3975 0.0160  0.0767  -0.0064 405 ALA D CA  
15495 C C   . ALA D 405 ? 0.2808 0.3520 0.3921 0.0297  0.0797  -0.0086 405 ALA D C   
15496 O O   . ALA D 405 ? 0.2896 0.3533 0.3914 0.0409  0.0830  -0.0123 405 ALA D O   
15497 C CB  . ALA D 405 ? 0.2594 0.3051 0.3598 0.0123  0.0784  -0.0010 405 ALA D CB  
15498 N N   . GLY D 406 ? 0.3034 0.3714 0.4108 0.0323  0.0219  -0.0211 406 GLY D N   
15499 C CA  . GLY D 406 ? 0.2545 0.3351 0.3727 0.0256  0.0136  -0.0142 406 GLY D CA  
15500 C C   . GLY D 406 ? 0.2398 0.3116 0.3492 0.0123  0.0119  -0.0124 406 GLY D C   
15501 O O   . GLY D 406 ? 0.2445 0.2991 0.3387 0.0101  0.0162  -0.0159 406 GLY D O   
15502 N N   . THR D 407 ? 0.2339 0.3180 0.3544 0.0035  0.0050  -0.0070 407 THR D N   
15503 C CA  . THR D 407 ? 0.2506 0.3237 0.3637 -0.0097 0.0020  -0.0052 407 THR D CA  
15504 C C   . THR D 407 ? 0.1497 0.2475 0.2839 -0.0182 0.0025  0.0015  407 THR D C   
15505 O O   . THR D 407 ? 0.2181 0.3439 0.3728 -0.0133 0.0054  0.0046  407 THR D O   
15506 C CB  . THR D 407 ? 0.2233 0.2776 0.3231 -0.0155 -0.0099 -0.0065 407 THR D CB  
15507 O OG1 . THR D 407 ? 0.2418 0.3157 0.3581 -0.0178 -0.0204 -0.0026 407 THR D OG1 
15508 C CG2 . THR D 407 ? 0.1967 0.2296 0.2770 -0.0074 -0.0095 -0.0110 407 THR D CG2 
15509 N N   . TRP D 408 ? 0.2466 0.3337 0.3765 -0.0311 0.0000  0.0040  408 TRP D N   
15510 C CA  . TRP D 408 ? 0.2325 0.3419 0.3838 -0.0422 -0.0004 0.0116  408 TRP D CA  
15511 C C   . TRP D 408 ? 0.2174 0.3408 0.3844 -0.0499 -0.0139 0.0134  408 TRP D C   
15512 O O   . TRP D 408 ? 0.1870 0.3317 0.3757 -0.0615 -0.0158 0.0199  408 TRP D O   
15513 C CB  . TRP D 408 ? 0.2327 0.3237 0.3750 -0.0540 0.0022  0.0150  408 TRP D CB  
15514 C CG  . TRP D 408 ? 0.2828 0.3382 0.4035 -0.0605 -0.0059 0.0096  408 TRP D CG  
15515 C CD1 . TRP D 408 ? 0.3314 0.3707 0.4379 -0.0584 -0.0153 0.0024  408 TRP D CD1 
15516 C CD2 . TRP D 408 ? 0.3175 0.3477 0.4262 -0.0688 -0.0042 0.0112  408 TRP D CD2 
15517 N NE1 . TRP D 408 ? 0.3010 0.3080 0.3872 -0.0648 -0.0187 -0.0018 408 TRP D NE1 
15518 C CE2 . TRP D 408 ? 0.3002 0.3000 0.3882 -0.0707 -0.0122 0.0031  408 TRP D CE2 
15519 C CE3 . TRP D 408 ? 0.3310 0.3599 0.4430 -0.0739 0.0036  0.0192  408 TRP D CE3 
15520 C CZ2 . TRP D 408 ? 0.3003 0.2680 0.3722 -0.0764 -0.0123 0.0013  408 TRP D CZ2 
15521 C CZ3 . TRP D 408 ? 0.3230 0.3188 0.4194 -0.0799 0.0025  0.0190  408 TRP D CZ3 
15522 C CH2 . TRP D 408 ? 0.3228 0.2881 0.4001 -0.0806 -0.0053 0.0094  408 TRP D CH2 
15523 N N   . PHE D 409 ? 0.1757 0.2889 0.3327 -0.0445 -0.0239 0.0086  409 PHE D N   
15524 C CA  . PHE D 409 ? 0.2744 0.4064 0.4477 -0.0497 -0.0382 0.0109  409 PHE D CA  
15525 C C   . PHE D 409 ? 0.2819 0.4427 0.4747 -0.0339 -0.0360 0.0132  409 PHE D C   
15526 O O   . PHE D 409 ? 0.2761 0.4245 0.4555 -0.0202 -0.0362 0.0098  409 PHE D O   
15527 C CB  . PHE D 409 ? 0.4223 0.5261 0.5711 -0.0548 -0.0523 0.0053  409 PHE D CB  
15528 C CG  . PHE D 409 ? 0.6301 0.7527 0.7936 -0.0631 -0.0703 0.0074  409 PHE D CG  
15529 C CD1 . PHE D 409 ? 0.8189 0.9816 1.0144 -0.0574 -0.0740 0.0135  409 PHE D CD1 
15530 C CD2 . PHE D 409 ? 0.7058 0.8084 0.8535 -0.0774 -0.0833 0.0031  409 PHE D CD2 
15531 C CE1 . PHE D 409 ? 0.8772 1.0617 1.0888 -0.0643 -0.0928 0.0159  409 PHE D CE1 
15532 C CE2 . PHE D 409 ? 0.7867 0.9087 0.9483 -0.0867 -0.1023 0.0044  409 PHE D CE2 
15533 C CZ  . PHE D 409 ? 0.8313 0.9965 1.0267 -0.0808 -0.1077 0.0114  409 PHE D CZ  
15534 N N   . ASP D 410 ? 0.2698 0.4682 0.4943 -0.0352 -0.0313 0.0195  410 ASP D N   
15535 C CA  . ASP D 410 ? 0.3069 0.5378 0.5553 -0.0196 -0.0281 0.0220  410 ASP D CA  
15536 C C   . ASP D 410 ? 0.3149 0.5344 0.5500 -0.0011 -0.0144 0.0170  410 ASP D C   
15537 O O   . ASP D 410 ? 0.3686 0.6067 0.6182 0.0148  -0.0114 0.0171  410 ASP D O   
15538 C CB  . ASP D 410 ? 0.3764 0.6164 0.6327 -0.0150 -0.0456 0.0230  410 ASP D CB  
15539 C CG  . ASP D 410 ? 0.5005 0.7628 0.7780 -0.0330 -0.0604 0.0277  410 ASP D CG  
15540 O OD1 . ASP D 410 ? 0.5536 0.8298 0.8464 -0.0482 -0.0550 0.0315  410 ASP D OD1 
15541 O OD2 . ASP D 410 ? 0.5443 0.8106 0.8232 -0.0324 -0.0781 0.0282  410 ASP D OD2 
15542 N N   . GLY D 411 ? 0.2892 0.4789 0.4982 -0.0026 -0.0065 0.0123  411 GLY D N   
15543 C CA  . GLY D 411 ? 0.3093 0.4878 0.5056 0.0124  0.0046  0.0065  411 GLY D CA  
15544 C C   . GLY D 411 ? 0.3635 0.5190 0.5443 0.0237  -0.0011 0.0018  411 GLY D C   
15545 O O   . GLY D 411 ? 0.3087 0.4588 0.4852 0.0372  0.0066  -0.0029 411 GLY D O   
15546 N N   . ASN D 412 ? 0.3605 0.5006 0.5310 0.0181  -0.0144 0.0029  412 ASN D N   
15547 C CA  . ASN D 412 ? 0.3154 0.4322 0.4688 0.0280  -0.0193 0.0007  412 ASN D CA  
15548 C C   . ASN D 412 ? 0.2711 0.3605 0.3995 0.0172  -0.0280 -0.0002 412 ASN D C   
15549 O O   . ASN D 412 ? 0.2446 0.3301 0.3684 0.0039  -0.0289 -0.0009 412 ASN D O   
15550 C CB  . ASN D 412 ? 0.2855 0.4229 0.4585 0.0406  -0.0269 0.0052  412 ASN D CB  
15551 C CG  . ASN D 412 ? 0.3010 0.4614 0.4906 0.0318  -0.0419 0.0114  412 ASN D CG  
15552 O OD1 . ASN D 412 ? 0.3616 0.5055 0.5341 0.0208  -0.0529 0.0115  412 ASN D OD1 
15553 N ND2 . ASN D 412 ? 0.3141 0.5134 0.5370 0.0372  -0.0428 0.0160  412 ASN D ND2 
15554 N N   . PHE D 413 ? 0.3336 0.4021 0.4443 0.0236  -0.0337 0.0000  413 PHE D N   
15555 C CA  . PHE D 413 ? 0.3197 0.3588 0.4011 0.0161  -0.0378 -0.0019 413 PHE D CA  
15556 C C   . PHE D 413 ? 0.3287 0.3672 0.4023 0.0131  -0.0546 0.0020  413 PHE D C   
15557 O O   . PHE D 413 ? 0.3074 0.3205 0.3527 0.0099  -0.0581 0.0008  413 PHE D O   
15558 C CB  . PHE D 413 ? 0.3253 0.3380 0.3873 0.0235  -0.0292 -0.0043 413 PHE D CB  
15559 C CG  . PHE D 413 ? 0.3530 0.3630 0.4173 0.0237  -0.0148 -0.0098 413 PHE D CG  
15560 C CD1 . PHE D 413 ? 0.3436 0.3417 0.3955 0.0149  -0.0091 -0.0137 413 PHE D CD1 
15561 C CD2 . PHE D 413 ? 0.3615 0.3811 0.4396 0.0337  -0.0076 -0.0116 413 PHE D CD2 
15562 C CE1 . PHE D 413 ? 0.3551 0.3536 0.4096 0.0155  0.0021  -0.0181 413 PHE D CE1 
15563 C CE2 . PHE D 413 ? 0.3769 0.3949 0.4546 0.0334  0.0038  -0.0174 413 PHE D CE2 
15564 C CZ  . PHE D 413 ? 0.3692 0.3779 0.4357 0.0240  0.0079  -0.0201 413 PHE D CZ  
15565 N N   . LEU D 414 ? 0.3162 0.3838 0.4139 0.0139  -0.0653 0.0067  414 LEU D N   
15566 C CA  . LEU D 414 ? 0.3427 0.4129 0.4342 0.0139  -0.0834 0.0111  414 LEU D CA  
15567 C C   . LEU D 414 ? 0.4206 0.4785 0.4925 -0.0023 -0.0940 0.0074  414 LEU D C   
15568 O O   . LEU D 414 ? 0.4289 0.4821 0.4857 -0.0029 -0.1095 0.0097  414 LEU D O   
15569 C CB  . LEU D 414 ? 0.3301 0.4402 0.4576 0.0199  -0.0927 0.0172  414 LEU D CB  
15570 C CG  . LEU D 414 ? 0.3436 0.4639 0.4878 0.0400  -0.0852 0.0208  414 LEU D CG  
15571 C CD1 . LEU D 414 ? 0.3640 0.5262 0.5446 0.0473  -0.0954 0.0273  414 LEU D CD1 
15572 C CD2 . LEU D 414 ? 0.3306 0.4177 0.4465 0.0515  -0.0859 0.0230  414 LEU D CD2 
15573 N N   . LYS D 415 ? 0.3687 0.4194 0.4384 -0.0148 -0.0868 0.0018  415 LYS D N   
15574 C CA  . LYS D 415 ? 0.4055 0.4375 0.4527 -0.0290 -0.0957 -0.0036 415 LYS D CA  
15575 C C   . LYS D 415 ? 0.3619 0.3562 0.3693 -0.0271 -0.0895 -0.0086 415 LYS D C   
15576 O O   . LYS D 415 ? 0.4456 0.4209 0.4296 -0.0367 -0.0958 -0.0145 415 LYS D O   
15577 C CB  . LYS D 415 ? 0.4572 0.4930 0.5175 -0.0429 -0.0910 -0.0069 415 LYS D CB  
15578 C CG  . LYS D 415 ? 0.5081 0.5794 0.6036 -0.0515 -0.1002 -0.0023 415 LYS D CG  
15579 C CD  . LYS D 415 ? 0.5902 0.6736 0.6864 -0.0566 -0.1225 -0.0011 415 LYS D CD  
15580 C CE  . LYS D 415 ? 0.6547 0.7167 0.7304 -0.0748 -0.1341 -0.0086 415 LYS D CE  
15581 N NZ  . LYS D 415 ? 0.6848 0.7558 0.7548 -0.0798 -0.1577 -0.0089 415 LYS D NZ  
15582 N N   . TRP D 416 ? 0.3038 0.2869 0.3037 -0.0156 -0.0766 -0.0071 416 TRP D N   
15583 C CA  . TRP D 416 ? 0.3729 0.3248 0.3388 -0.0137 -0.0689 -0.0104 416 TRP D CA  
15584 C C   . TRP D 416 ? 0.4267 0.3692 0.3788 -0.0025 -0.0687 -0.0042 416 TRP D C   
15585 O O   . TRP D 416 ? 0.4373 0.3553 0.3589 -0.0021 -0.0639 -0.0052 416 TRP D O   
15586 C CB  . TRP D 416 ? 0.4048 0.3481 0.3732 -0.0137 -0.0508 -0.0148 416 TRP D CB  
15587 C CG  . TRP D 416 ? 0.3770 0.3254 0.3568 -0.0236 -0.0501 -0.0191 416 TRP D CG  
15588 C CD1 . TRP D 416 ? 0.4075 0.3365 0.3688 -0.0318 -0.0507 -0.0255 416 TRP D CD1 
15589 C CD2 . TRP D 416 ? 0.3500 0.3227 0.3609 -0.0261 -0.0485 -0.0165 416 TRP D CD2 
15590 N NE1 . TRP D 416 ? 0.3643 0.3014 0.3436 -0.0398 -0.0501 -0.0263 416 TRP D NE1 
15591 C CE2 . TRP D 416 ? 0.3305 0.2956 0.3401 -0.0371 -0.0484 -0.0202 416 TRP D CE2 
15592 C CE3 . TRP D 416 ? 0.2399 0.2389 0.2783 -0.0194 -0.0459 -0.0114 416 TRP D CE3 
15593 C CZ2 . TRP D 416 ? 0.2834 0.2665 0.3179 -0.0430 -0.0459 -0.0172 416 TRP D CZ2 
15594 C CZ3 . TRP D 416 ? 0.2480 0.2677 0.3110 -0.0246 -0.0425 -0.0095 416 TRP D CZ3 
15595 C CH2 . TRP D 416 ? 0.2923 0.3039 0.3529 -0.0371 -0.0425 -0.0116 416 TRP D CH2 
15596 N N   . ILE D 417 ? 0.3804 0.3405 0.3535 0.0070  -0.0728 0.0026  417 ILE D N   
15597 C CA  . ILE D 417 ? 0.4724 0.4198 0.4334 0.0185  -0.0723 0.0097  417 ILE D CA  
15598 C C   . ILE D 417 ? 0.4368 0.4083 0.4221 0.0282  -0.0844 0.0169  417 ILE D C   
15599 O O   . ILE D 417 ? 0.4248 0.4249 0.4416 0.0273  -0.0867 0.0157  417 ILE D O   
15600 C CB  . ILE D 417 ? 0.4810 0.4147 0.4431 0.0230  -0.0537 0.0079  417 ILE D CB  
15601 C CG1 . ILE D 417 ? 0.4707 0.3823 0.4139 0.0315  -0.0516 0.0153  417 ILE D CG1 
15602 C CG2 . ILE D 417 ? 0.4345 0.3903 0.4305 0.0272  -0.0472 0.0055  417 ILE D CG2 
15603 C CD1 . ILE D 417 ? 0.4418 0.3352 0.3791 0.0303  -0.0341 0.0124  417 ILE D CD1 
15604 N N   . GLY D 418 ? 0.4242 0.3852 0.3953 0.0381  -0.0920 0.0255  418 GLY D N   
15605 C CA  . GLY D 418 ? 0.4711 0.4527 0.4653 0.0514  -0.1026 0.0335  418 GLY D CA  
15606 C C   . GLY D 418 ? 0.5574 0.5484 0.5429 0.0531  -0.1248 0.0408  418 GLY D C   
15607 O O   . GLY D 418 ? 0.6700 0.6725 0.6689 0.0676  -0.1339 0.0499  418 GLY D O   
15608 N N   . ASN D 419 ? 0.5959 0.5828 0.5595 0.0397  -0.1348 0.0369  419 ASN D N   
15609 C CA  . ASN D 419 ? 0.6191 0.6118 0.5677 0.0412  -0.1576 0.0435  419 ASN D CA  
15610 C C   . ASN D 419 ? 0.6468 0.6023 0.5437 0.0400  -0.1571 0.0460  419 ASN D C   
15611 O O   . ASN D 419 ? 0.6606 0.5892 0.5372 0.0366  -0.1388 0.0420  419 ASN D O   
15612 C CB  . ASN D 419 ? 0.6160 0.6361 0.5797 0.0268  -0.1739 0.0373  419 ASN D CB  
15613 C CG  . ASN D 419 ? 0.6183 0.6173 0.5540 0.0088  -0.1704 0.0253  419 ASN D CG  
15614 O OD1 . ASN D 419 ? 0.6056 0.5712 0.5057 0.0080  -0.1585 0.0224  419 ASN D OD1 
15615 N ND2 . ASN D 419 ? 0.5981 0.6170 0.5508 -0.0057 -0.1812 0.0185  419 ASN D ND2 
15616 N N   . LYS D 420 ? 0.6728 0.6289 0.5482 0.0427  -0.1775 0.0531  420 LYS D N   
15617 C CA  . LYS D 420 ? 0.7290 0.6506 0.5534 0.0445  -0.1765 0.0585  420 LYS D CA  
15618 C C   . LYS D 420 ? 0.6782 0.5778 0.4700 0.0295  -0.1663 0.0461  420 LYS D C   
15619 O O   . LYS D 420 ? 0.6577 0.5282 0.4208 0.0300  -0.1492 0.0472  420 LYS D O   
15620 C CB  . LYS D 420 ? 0.8380 0.7667 0.6433 0.0504  -0.2025 0.0686  420 LYS D CB  
15621 C CG  . LYS D 420 ? 0.9602 0.8531 0.7089 0.0531  -0.2013 0.0765  420 LYS D CG  
15622 C CD  . LYS D 420 ? 1.0258 0.8917 0.7687 0.0636  -0.1804 0.0867  420 LYS D CD  
15623 C CE  . LYS D 420 ? 1.1008 0.9352 0.7906 0.0688  -0.1823 0.1002  420 LYS D CE  
15624 N NZ  . LYS D 420 ? 1.1018 0.9097 0.7890 0.0785  -0.1644 0.1126  420 LYS D NZ  
15625 N N   . GLU D 421 ? 0.7108 0.6236 0.5072 0.0161  -0.1763 0.0344  421 GLU D N   
15626 C CA  . GLU D 421 ? 0.8026 0.6921 0.5665 0.0037  -0.1678 0.0216  421 GLU D CA  
15627 C C   . GLU D 421 ? 0.7515 0.6314 0.5295 0.0014  -0.1417 0.0149  421 GLU D C   
15628 O O   . GLU D 421 ? 0.7921 0.6461 0.5403 0.0000  -0.1259 0.0112  421 GLU D O   
15629 C CB  . GLU D 421 ? 0.8718 0.7744 0.6380 -0.0106 -0.1863 0.0103  421 GLU D CB  
15630 C CG  . GLU D 421 ? 0.9764 0.8996 0.7417 -0.0097 -0.2158 0.0165  421 GLU D CG  
15631 C CD  . GLU D 421 ? 1.1259 1.0256 0.8341 -0.0073 -0.2264 0.0194  421 GLU D CD  
15632 O OE1 . GLU D 421 ? 1.1967 1.1041 0.8892 -0.0151 -0.2506 0.0148  421 GLU D OE1 
15633 O OE2 . GLU D 421 ? 1.1766 1.0507 0.8551 0.0017  -0.2109 0.0264  421 GLU D OE2 
15634 N N   . LYS D 422 ? 0.6718 0.5740 0.4951 0.0014  -0.1367 0.0135  422 LYS D N   
15635 C CA  . LYS D 422 ? 0.6245 0.5193 0.4605 -0.0001 -0.1139 0.0077  422 LYS D CA  
15636 C C   . LYS D 422 ? 0.5867 0.4639 0.4126 0.0095  -0.0976 0.0151  422 LYS D C   
15637 O O   . LYS D 422 ? 0.5526 0.4126 0.3658 0.0068  -0.0799 0.0104  422 LYS D O   
15638 C CB  . LYS D 422 ? 0.5381 0.4611 0.4213 -0.0015 -0.1126 0.0059  422 LYS D CB  
15639 C CG  . LYS D 422 ? 0.5242 0.4597 0.4180 -0.0153 -0.1232 -0.0025 422 LYS D CG  
15640 C CD  . LYS D 422 ? 0.4260 0.3915 0.3659 -0.0172 -0.1209 -0.0019 422 LYS D CD  
15641 C CE  . LYS D 422 ? 0.4324 0.4143 0.3861 -0.0318 -0.1361 -0.0066 422 LYS D CE  
15642 N NZ  . LYS D 422 ? 0.4134 0.3708 0.3456 -0.0448 -0.1321 -0.0178 422 LYS D NZ  
15643 N N   . ASN D 423 ? 0.5109 0.3917 0.3427 0.0208  -0.1035 0.0269  423 ASN D N   
15644 C CA  . ASN D 423 ? 0.5535 0.4132 0.3737 0.0284  -0.0893 0.0348  423 ASN D CA  
15645 C C   . ASN D 423 ? 0.5726 0.4046 0.3464 0.0248  -0.0833 0.0366  423 ASN D C   
15646 O O   . ASN D 423 ? 0.5272 0.3412 0.2912 0.0248  -0.0653 0.0388  423 ASN D O   
15647 C CB  . ASN D 423 ? 0.5564 0.4204 0.3879 0.0422  -0.0989 0.0479  423 ASN D CB  
15648 C CG  . ASN D 423 ? 0.5149 0.3993 0.3912 0.0491  -0.0947 0.0464  423 ASN D CG  
15649 O OD1 . ASN D 423 ? 0.4900 0.3844 0.3869 0.0430  -0.0838 0.0366  423 ASN D OD1 
15650 N ND2 . ASN D 423 ? 0.4906 0.3801 0.3801 0.0633  -0.1029 0.0565  423 ASN D ND2 
15651 N N   . GLU D 424 ? 0.6553 0.4844 0.3997 0.0212  -0.0981 0.0356  424 GLU D N   
15652 C CA  . GLU D 424 ? 0.7397 0.5433 0.4359 0.0180  -0.0914 0.0359  424 GLU D CA  
15653 C C   . GLU D 424 ? 0.6445 0.4389 0.3376 0.0107  -0.0701 0.0243  424 GLU D C   
15654 O O   . GLU D 424 ? 0.6371 0.4130 0.3062 0.0108  -0.0535 0.0275  424 GLU D O   
15655 C CB  . GLU D 424 ? 0.8108 0.6145 0.4760 0.0143  -0.1123 0.0328  424 GLU D CB  
15656 C CG  . GLU D 424 ? 0.9594 0.7365 0.5692 0.0122  -0.1055 0.0326  424 GLU D CG  
15657 C CD  . GLU D 424 ? 1.1268 0.8880 0.7102 0.0211  -0.1039 0.0509  424 GLU D CD  
15658 O OE1 . GLU D 424 ? 1.1744 0.9168 0.7407 0.0212  -0.0822 0.0554  424 GLU D OE1 
15659 O OE2 . GLU D 424 ? 1.2095 0.9775 0.7904 0.0280  -0.1244 0.0619  424 GLU D OE2 
15660 N N   . TYR D 425 ? 0.5560 0.3644 0.2749 0.0047  -0.0699 0.0119  425 TYR D N   
15661 C CA  . TYR D 425 ? 0.5710 0.3719 0.2896 -0.0002 -0.0509 0.0015  425 TYR D CA  
15662 C C   . TYR D 425 ? 0.5700 0.3709 0.3092 0.0030  -0.0316 0.0061  425 TYR D C   
15663 O O   . TYR D 425 ? 0.5735 0.3630 0.2993 0.0016  -0.0138 0.0040  425 TYR D O   
15664 C CB  . TYR D 425 ? 0.5656 0.3797 0.3081 -0.0068 -0.0564 -0.0104 425 TYR D CB  
15665 C CG  . TYR D 425 ? 0.5642 0.3660 0.2770 -0.0137 -0.0645 -0.0215 425 TYR D CG  
15666 C CD1 . TYR D 425 ? 0.5409 0.3303 0.2135 -0.0137 -0.0764 -0.0199 425 TYR D CD1 
15667 C CD2 . TYR D 425 ? 0.5510 0.3513 0.2740 -0.0199 -0.0606 -0.0338 425 TYR D CD2 
15668 C CE1 . TYR D 425 ? 0.6449 0.4205 0.2874 -0.0204 -0.0846 -0.0324 425 TYR D CE1 
15669 C CE2 . TYR D 425 ? 0.5791 0.3637 0.2744 -0.0262 -0.0680 -0.0453 425 TYR D CE2 
15670 C CZ  . TYR D 425 ? 0.6182 0.3902 0.2727 -0.0267 -0.0799 -0.0457 425 TYR D CZ  
15671 O OH  . TYR D 425 ? 0.6590 0.4128 0.2835 -0.0335 -0.0877 -0.0597 425 TYR D OH  
15672 N N   . TRP D 426 ? 0.5399 0.3543 0.3121 0.0074  -0.0346 0.0117  426 TRP D N   
15673 C CA  . TRP D 426 ? 0.5127 0.3245 0.3019 0.0095  -0.0183 0.0152  426 TRP D CA  
15674 C C   . TRP D 426 ? 0.5304 0.3209 0.2921 0.0114  -0.0099 0.0260  426 TRP D C   
15675 O O   . TRP D 426 ? 0.5535 0.3367 0.3152 0.0083  0.0077  0.0262  426 TRP D O   
15676 C CB  . TRP D 426 ? 0.5098 0.3375 0.3353 0.0148  -0.0238 0.0177  426 TRP D CB  
15677 C CG  . TRP D 426 ? 0.4329 0.2816 0.2868 0.0116  -0.0258 0.0079  426 TRP D CG  
15678 C CD1 . TRP D 426 ? 0.3582 0.2245 0.2257 0.0108  -0.0407 0.0058  426 TRP D CD1 
15679 C CD2 . TRP D 426 ? 0.3779 0.2328 0.2498 0.0079  -0.0125 0.0001  426 TRP D CD2 
15680 N NE1 . TRP D 426 ? 0.3637 0.2445 0.2551 0.0065  -0.0362 -0.0019 426 TRP D NE1 
15681 C CE2 . TRP D 426 ? 0.4487 0.3224 0.3420 0.0056  -0.0195 -0.0054 426 TRP D CE2 
15682 C CE3 . TRP D 426 ? 0.4250 0.2731 0.2981 0.0061  0.0040  -0.0020 426 TRP D CE3 
15683 C CZ2 . TRP D 426 ? 0.4511 0.3344 0.3636 0.0026  -0.0105 -0.0121 426 TRP D CZ2 
15684 C CZ3 . TRP D 426 ? 0.3898 0.2502 0.2840 0.0036  0.0116  -0.0097 426 TRP D CZ3 
15685 C CH2 . TRP D 426 ? 0.4041 0.2805 0.3159 0.0025  0.0042  -0.0142 426 TRP D CH2 
15686 N N   . LYS D 427 ? 0.5763 0.3577 0.3147 0.0160  -0.0226 0.0362  427 LYS D N   
15687 C CA  . LYS D 427 ? 0.6363 0.3949 0.3433 0.0172  -0.0147 0.0485  427 LYS D CA  
15688 C C   . LYS D 427 ? 0.6109 0.3593 0.2875 0.0107  0.0003  0.0436  427 LYS D C   
15689 O O   . LYS D 427 ? 0.6722 0.4092 0.3406 0.0078  0.0184  0.0491  427 LYS D O   
15690 C CB  . LYS D 427 ? 0.6827 0.4341 0.3661 0.0243  -0.0335 0.0605  427 LYS D CB  
15691 C CG  . LYS D 427 ? 0.7559 0.5149 0.4679 0.0339  -0.0457 0.0683  427 LYS D CG  
15692 C CD  . LYS D 427 ? 0.8905 0.6376 0.5759 0.0428  -0.0611 0.0842  427 LYS D CD  
15693 C CE  . LYS D 427 ? 0.9567 0.7248 0.6442 0.0462  -0.0859 0.0816  427 LYS D CE  
15694 N NZ  . LYS D 427 ? 1.0293 0.7860 0.6821 0.0539  -0.1022 0.0968  427 LYS D NZ  
15695 N N   . ILE D 428 ? 0.5769 0.3291 0.2369 0.0083  -0.0066 0.0330  428 ILE D N   
15696 C CA  . ILE D 428 ? 0.6608 0.4036 0.2928 0.0043  0.0087  0.0260  428 ILE D CA  
15697 C C   . ILE D 428 ? 0.6382 0.3892 0.2986 0.0012  0.0293  0.0197  428 ILE D C   
15698 O O   . ILE D 428 ? 0.6313 0.3757 0.2794 -0.0008 0.0487  0.0223  428 ILE D O   
15699 C CB  . ILE D 428 ? 0.6465 0.3898 0.2595 0.0024  -0.0036 0.0127  428 ILE D CB  
15700 C CG1 . ILE D 428 ? 0.6455 0.3803 0.2228 0.0046  -0.0237 0.0191  428 ILE D CG1 
15701 C CG2 . ILE D 428 ? 0.6696 0.4050 0.2631 0.0003  0.0146  0.0016  428 ILE D CG2 
15702 C CD1 . ILE D 428 ? 0.7134 0.4503 0.2775 0.0007  -0.0412 0.0054  428 ILE D CD1 
15703 N N   . LEU D 429 ? 0.5778 0.3454 0.2775 0.0007  0.0251  0.0124  429 LEU D N   
15704 C CA  . LEU D 429 ? 0.6047 0.3828 0.3327 -0.0016 0.0413  0.0061  429 LEU D CA  
15705 C C   . LEU D 429 ? 0.5198 0.2953 0.2591 -0.0034 0.0546  0.0158  429 LEU D C   
15706 O O   . LEU D 429 ? 0.5465 0.3242 0.2889 -0.0067 0.0726  0.0145  429 LEU D O   
15707 C CB  . LEU D 429 ? 0.5971 0.3927 0.3616 -0.0014 0.0323  -0.0014 429 LEU D CB  
15708 C CG  . LEU D 429 ? 0.5754 0.3836 0.3708 -0.0030 0.0460  -0.0062 429 LEU D CG  
15709 C CD1 . LEU D 429 ? 0.5974 0.4048 0.3830 -0.0036 0.0595  -0.0143 429 LEU D CD1 
15710 C CD2 . LEU D 429 ? 0.5010 0.3257 0.3293 -0.0023 0.0367  -0.0109 429 LEU D CD2 
15711 N N   . ILE D 430 ? 0.5262 0.2962 0.2719 -0.0012 0.0459  0.0258  430 ILE D N   
15712 C CA  . ILE D 430 ? 0.5435 0.3066 0.3013 -0.0038 0.0566  0.0345  430 ILE D CA  
15713 C C   . ILE D 430 ? 0.6222 0.3700 0.3505 -0.0082 0.0719  0.0439  430 ILE D C   
15714 O O   . ILE D 430 ? 0.6311 0.3810 0.3715 -0.0148 0.0888  0.0450  430 ILE D O   
15715 C CB  . ILE D 430 ? 0.5463 0.3022 0.3129 0.0019  0.0428  0.0429  430 ILE D CB  
15716 C CG1 . ILE D 430 ? 0.4716 0.2467 0.2749 0.0050  0.0343  0.0332  430 ILE D CG1 
15717 C CG2 . ILE D 430 ? 0.5070 0.2440 0.2722 -0.0010 0.0525  0.0548  430 ILE D CG2 
15718 C CD1 . ILE D 430 ? 0.4987 0.2745 0.3087 0.0140  0.0168  0.0383  430 ILE D CD1 
15719 N N   . GLU D 431 ? 0.7179 0.4512 0.4070 -0.0052 0.0661  0.0512  431 GLU D N   
15720 C CA  . GLU D 431 ? 0.7559 0.4745 0.4126 -0.0092 0.0820  0.0614  431 GLU D CA  
15721 C C   . GLU D 431 ? 0.6674 0.3978 0.3227 -0.0130 0.1008  0.0514  431 GLU D C   
15722 O O   . GLU D 431 ? 0.7182 0.4484 0.3743 -0.0192 0.1207  0.0572  431 GLU D O   
15723 C CB  . GLU D 431 ? 0.8946 0.5964 0.5050 -0.0041 0.0706  0.0705  431 GLU D CB  
15724 C CG  . GLU D 431 ? 1.0078 0.7014 0.6199 0.0028  0.0490  0.0802  431 GLU D CG  
15725 C CD  . GLU D 431 ? 1.1144 0.7910 0.7350 0.0019  0.0546  0.0961  431 GLU D CD  
15726 O OE1 . GLU D 431 ? 1.1673 0.8459 0.8183 0.0063  0.0444  0.0964  431 GLU D OE1 
15727 O OE2 . GLU D 431 ? 1.1296 0.7898 0.7262 -0.0033 0.0698  0.1083  431 GLU D OE2 
15728 N N   . ALA D 432 ? 0.6471 0.3879 0.3024 -0.0094 0.0950  0.0366  432 ALA D N   
15729 C CA  . ALA D 432 ? 0.6943 0.4455 0.3499 -0.0102 0.1124  0.0262  432 ALA D CA  
15730 C C   . ALA D 432 ? 0.6996 0.4694 0.3988 -0.0147 0.1256  0.0236  432 ALA D C   
15731 O O   . ALA D 432 ? 0.7639 0.5425 0.4656 -0.0171 0.1456  0.0228  432 ALA D O   
15732 C CB  . ALA D 432 ? 0.6740 0.4283 0.3237 -0.0052 0.1016  0.0107  432 ALA D CB  
15733 N N   . LYS D 433 ? 0.6329 0.4111 0.3671 -0.0154 0.1144  0.0217  433 LYS D N   
15734 C CA  . LYS D 433 ? 0.5790 0.3751 0.3531 -0.0202 0.1239  0.0185  433 LYS D CA  
15735 C C   . LYS D 433 ? 0.6650 0.4573 0.4422 -0.0289 0.1394  0.0300  433 LYS D C   
15736 O O   . LYS D 433 ? 0.6630 0.4726 0.4651 -0.0344 0.1532  0.0275  433 LYS D O   
15737 C CB  . LYS D 433 ? 0.5735 0.3759 0.3775 -0.0189 0.1083  0.0147  433 LYS D CB  
15738 C CG  . LYS D 433 ? 0.5428 0.3611 0.3849 -0.0244 0.1148  0.0117  433 LYS D CG  
15739 C CD  . LYS D 433 ? 0.5304 0.3703 0.3895 -0.0237 0.1246  0.0022  433 LYS D CD  
15740 C CE  . LYS D 433 ? 0.5628 0.4214 0.4599 -0.0292 0.1277  -0.0011 433 LYS D CE  
15741 N NZ  . LYS D 433 ? 0.5569 0.4389 0.4713 -0.0271 0.1372  -0.0087 433 LYS D NZ  
15742 N N   . LYS D 434 ? 0.7127 0.4828 0.4658 -0.0308 0.1370  0.0435  434 LYS D N   
15743 C CA  . LYS D 434 ? 0.7492 0.5117 0.5031 -0.0408 0.1523  0.0563  434 LYS D CA  
15744 C C   . LYS D 434 ? 0.7734 0.5459 0.5149 -0.0447 0.1749  0.0578  434 LYS D C   
15745 O O   . LYS D 434 ? 0.7956 0.5752 0.5539 -0.0550 0.1903  0.0644  434 LYS D O   
15746 C CB  . LYS D 434 ? 0.7626 0.4954 0.4878 -0.0403 0.1451  0.0723  434 LYS D CB  
15747 C CG  . LYS D 434 ? 0.7836 0.5064 0.5198 -0.0341 0.1237  0.0720  434 LYS D CG  
15748 C CD  . LYS D 434 ? 0.8578 0.5503 0.5708 -0.0337 0.1196  0.0902  434 LYS D CD  
15749 C CE  . LYS D 434 ? 0.8573 0.5414 0.5797 -0.0239 0.0982  0.0900  434 LYS D CE  
15750 N NZ  . LYS D 434 ? 0.8685 0.5228 0.5634 -0.0190 0.0909  0.1083  434 LYS D NZ  
15751 N N   . LYS D 435 ? 0.7412 0.5159 0.4554 -0.0365 0.1769  0.0511  435 LYS D N   
15752 C CA  . LYS D 435 ? 0.7656 0.5554 0.4736 -0.0359 0.1943  0.0491  435 LYS D CA  
15753 C C   . LYS D 435 ? 0.7550 0.5644 0.4756 -0.0277 0.1966  0.0321  435 LYS D C   
15754 O O   . LYS D 435 ? 0.7783 0.5963 0.4866 -0.0222 0.2047  0.0276  435 LYS D O   
15755 C CB  . LYS D 435 ? 0.7963 0.5699 0.4586 -0.0322 0.1937  0.0565  435 LYS D CB  
15756 C CG  . LYS D 435 ? 0.8951 0.6422 0.5348 -0.0348 0.1826  0.0719  435 LYS D CG  
15757 C CD  . LYS D 435 ? 0.9889 0.7242 0.5849 -0.0311 0.1819  0.0793  435 LYS D CD  
15758 C CE  . LYS D 435 ? 1.0414 0.7525 0.6190 -0.0328 0.1710  0.0968  435 LYS D CE  
15759 N NZ  . LYS D 435 ? 1.0739 0.7801 0.6190 -0.0332 0.1779  0.1080  435 LYS D NZ  
15760 N N   . ALA D 436 ? 0.6173 0.4291 0.3787 -0.1148 0.1328  0.0426  436 ALA D N   
15761 C CA  . ALA D 436 ? 0.5766 0.4350 0.3822 -0.1046 0.1296  0.0416  436 ALA D CA  
15762 C C   . ALA D 436 ? 0.5579 0.4594 0.4080 -0.1187 0.1436  0.0389  436 ALA D C   
15763 O O   . ALA D 436 ? 0.5950 0.5046 0.4553 -0.1370 0.1466  0.0367  436 ALA D O   
15764 C CB  . ALA D 436 ? 0.4243 0.3027 0.2483 -0.0932 0.1064  0.0419  436 ALA D CB  
15765 N N   . LYS D 437 ? 0.5347 0.4640 0.4128 -0.1100 0.1522  0.0384  437 LYS D N   
15766 C CA  . LYS D 437 ? 0.5690 0.5423 0.4940 -0.1206 0.1668  0.0355  437 LYS D CA  
15767 C C   . LYS D 437 ? 0.5480 0.5703 0.5223 -0.1056 0.1580  0.0357  437 LYS D C   
15768 O O   . LYS D 437 ? 0.5420 0.6060 0.5613 -0.1104 0.1685  0.0332  437 LYS D O   
15769 C CB  . LYS D 437 ? 0.6628 0.6182 0.5727 -0.1279 0.1966  0.0340  437 LYS D CB  
15770 C CG  . LYS D 437 ? 0.7814 0.6860 0.6418 -0.1405 0.2040  0.0343  437 LYS D CG  
15771 C CD  . LYS D 437 ? 0.8564 0.7699 0.7303 -0.1617 0.2012  0.0320  437 LYS D CD  
15772 C CE  . LYS D 437 ? 0.9157 0.7912 0.7582 -0.1727 0.2132  0.0300  437 LYS D CE  
15773 N NZ  . LYS D 437 ? 0.9433 0.7751 0.7446 -0.1765 0.1999  0.0309  437 LYS D NZ  
15774 N N   . ASN D 438 ? 0.4785 0.4970 0.4470 -0.0875 0.1395  0.0387  438 ASN D N   
15775 C CA  . ASN D 438 ? 0.4281 0.4864 0.4379 -0.0726 0.1304  0.0404  438 ASN D CA  
15776 C C   . ASN D 438 ? 0.4251 0.4739 0.4223 -0.0607 0.1074  0.0440  438 ASN D C   
15777 O O   . ASN D 438 ? 0.4606 0.4759 0.4217 -0.0634 0.0998  0.0442  438 ASN D O   
15778 C CB  . ASN D 438 ? 0.4869 0.5458 0.5038 -0.0593 0.1466  0.0396  438 ASN D CB  
15779 C CG  . ASN D 438 ? 0.4477 0.4579 0.4159 -0.0504 0.1481  0.0397  438 ASN D CG  
15780 O OD1 . ASN D 438 ? 0.4685 0.4643 0.4219 -0.0401 0.1307  0.0418  438 ASN D OD1 
15781 N ND2 . ASN D 438 ? 0.4625 0.4470 0.4051 -0.0549 0.1690  0.0368  438 ASN D ND2 
15782 N N   . ASP D 439 ? 0.3610 0.4379 0.3877 -0.0464 0.0977  0.0470  439 ASP D N   
15783 C CA  . ASP D 439 ? 0.3592 0.4330 0.3799 -0.0368 0.0778  0.0510  439 ASP D CA  
15784 C C   . ASP D 439 ? 0.3306 0.3697 0.3219 -0.0247 0.0761  0.0518  439 ASP D C   
15785 O O   . ASP D 439 ? 0.3694 0.4037 0.3555 -0.0176 0.0623  0.0546  439 ASP D O   
15786 C CB  . ASP D 439 ? 0.3834 0.4972 0.4437 -0.0264 0.0684  0.0551  439 ASP D CB  
15787 C CG  . ASP D 439 ? 0.4640 0.6090 0.5451 -0.0378 0.0565  0.0549  439 ASP D CG  
15788 O OD1 . ASP D 439 ? 0.4930 0.6276 0.5586 -0.0550 0.0570  0.0508  439 ASP D OD1 
15789 O OD2 . ASP D 439 ? 0.4882 0.6663 0.5996 -0.0293 0.0457  0.0586  439 ASP D OD2 
15790 N N   . TYR D 440 ? 0.4236 0.4374 0.3943 -0.0232 0.0896  0.0488  440 TYR D N   
15791 C CA  . TYR D 440 ? 0.3696 0.3496 0.3100 -0.0144 0.0845  0.0479  440 TYR D CA  
15792 C C   . TYR D 440 ? 0.3908 0.3466 0.3026 -0.0199 0.0728  0.0475  440 TYR D C   
15793 O O   . TYR D 440 ? 0.4489 0.3865 0.3458 -0.0120 0.0634  0.0470  440 TYR D O   
15794 C CB  . TYR D 440 ? 0.4252 0.3806 0.3441 -0.0122 0.1002  0.0439  440 TYR D CB  
15795 C CG  . TYR D 440 ? 0.4469 0.4130 0.3855 0.0009  0.1071  0.0434  440 TYR D CG  
15796 C CD1 . TYR D 440 ? 0.4772 0.4325 0.4126 0.0125  0.0971  0.0436  440 TYR D CD1 
15797 C CD2 . TYR D 440 ? 0.4551 0.4419 0.4176 0.0015  0.1248  0.0421  440 TYR D CD2 
15798 C CE1 . TYR D 440 ? 0.4829 0.4427 0.4338 0.0246  0.1041  0.0429  440 TYR D CE1 
15799 C CE2 . TYR D 440 ? 0.4791 0.4730 0.4594 0.0156  0.1320  0.0413  440 TYR D CE2 
15800 C CZ  . TYR D 440 ? 0.5011 0.4792 0.4735 0.0271  0.1214  0.0419  440 TYR D CZ  
15801 O OH  . TYR D 440 ? 0.5725 0.5524 0.5597 0.0409  0.1290  0.0409  440 TYR D OH  
15802 N N   . ILE D 441 ? 0.4063 0.3615 0.3116 -0.0333 0.0736  0.0471  441 ILE D N   
15803 C CA  . ILE D 441 ? 0.4072 0.3408 0.2887 -0.0364 0.0622  0.0467  441 ILE D CA  
15804 C C   . ILE D 441 ? 0.4366 0.3870 0.3340 -0.0302 0.0476  0.0488  441 ILE D C   
15805 O O   . ILE D 441 ? 0.4144 0.3473 0.2955 -0.0268 0.0384  0.0480  441 ILE D O   
15806 C CB  . ILE D 441 ? 0.4671 0.3930 0.3371 -0.0528 0.0672  0.0453  441 ILE D CB  
15807 C CG1 . ILE D 441 ? 0.4614 0.3515 0.2967 -0.0530 0.0589  0.0444  441 ILE D CG1 
15808 C CG2 . ILE D 441 ? 0.4444 0.4073 0.3466 -0.0621 0.0640  0.0455  441 ILE D CG2 
15809 C CD1 . ILE D 441 ? 0.5521 0.4039 0.3517 -0.0463 0.0617  0.0441  441 ILE D CD1 
15810 N N   . LEU D 442 ? 0.4519 0.4354 0.3804 -0.0278 0.0456  0.0517  442 LEU D N   
15811 C CA  . LEU D 442 ? 0.3969 0.3919 0.3350 -0.0212 0.0335  0.0549  442 LEU D CA  
15812 C C   . LEU D 442 ? 0.4170 0.4000 0.3523 -0.0083 0.0315  0.0559  442 LEU D C   
15813 O O   . LEU D 442 ? 0.3734 0.3495 0.3030 -0.0047 0.0238  0.0565  442 LEU D O   
15814 C CB  . LEU D 442 ? 0.3391 0.3699 0.3073 -0.0207 0.0303  0.0587  442 LEU D CB  
15815 C CG  . LEU D 442 ? 0.3566 0.4078 0.3362 -0.0348 0.0300  0.0566  442 LEU D CG  
15816 C CD1 . LEU D 442 ? 0.3540 0.4414 0.3631 -0.0306 0.0211  0.0609  442 LEU D CD1 
15817 C CD2 . LEU D 442 ? 0.3786 0.4120 0.3341 -0.0460 0.0241  0.0532  442 LEU D CD2 
15818 N N   . VAL D 443 ? 0.4107 0.3912 0.3510 -0.0020 0.0397  0.0554  443 VAL D N   
15819 C CA  . VAL D 443 ? 0.4291 0.3954 0.3658 0.0082  0.0381  0.0547  443 VAL D CA  
15820 C C   . VAL D 443 ? 0.4351 0.3757 0.3479 0.0074  0.0318  0.0504  443 VAL D C   
15821 O O   . VAL D 443 ? 0.4116 0.3481 0.3267 0.0121  0.0249  0.0501  443 VAL D O   
15822 C CB  . VAL D 443 ? 0.4046 0.3664 0.3441 0.0137  0.0493  0.0527  443 VAL D CB  
15823 C CG1 . VAL D 443 ? 0.3406 0.2842 0.2740 0.0222  0.0470  0.0502  443 VAL D CG1 
15824 C CG2 . VAL D 443 ? 0.3570 0.3482 0.3261 0.0170  0.0555  0.0568  443 VAL D CG2 
15825 N N   . ALA D 444 ? 0.4134 0.3361 0.3037 0.0016  0.0344  0.0472  444 ALA D N   
15826 C CA  . ALA D 444 ? 0.4466 0.3437 0.3130 0.0032  0.0268  0.0434  444 ALA D CA  
15827 C C   . ALA D 444 ? 0.4786 0.3784 0.3464 0.0018  0.0180  0.0439  444 ALA D C   
15828 O O   . ALA D 444 ? 0.4642 0.3487 0.3211 0.0063  0.0101  0.0407  444 ALA D O   
15829 C CB  . ALA D 444 ? 0.4818 0.3545 0.3188 -0.0017 0.0325  0.0414  444 ALA D CB  
15830 N N   . GLU D 445 ? 0.4807 0.3997 0.3617 -0.0035 0.0187  0.0471  445 GLU D N   
15831 C CA  . GLU D 445 ? 0.4729 0.3933 0.3534 -0.0042 0.0121  0.0468  445 GLU D CA  
15832 C C   . GLU D 445 ? 0.4686 0.4003 0.3658 0.0027  0.0087  0.0484  445 GLU D C   
15833 O O   . GLU D 445 ? 0.4795 0.4139 0.3772 0.0023  0.0058  0.0484  445 GLU D O   
15834 C CB  . GLU D 445 ? 0.4261 0.3592 0.3087 -0.0140 0.0132  0.0484  445 GLU D CB  
15835 C CG  . GLU D 445 ? 0.4694 0.3862 0.3331 -0.0236 0.0173  0.0459  445 GLU D CG  
15836 C CD  . GLU D 445 ? 0.5690 0.5048 0.4430 -0.0358 0.0208  0.0467  445 GLU D CD  
15837 O OE1 . GLU D 445 ? 0.5196 0.4817 0.4136 -0.0355 0.0168  0.0493  445 GLU D OE1 
15838 O OE2 . GLU D 445 ? 0.6260 0.5493 0.4873 -0.0461 0.0270  0.0447  445 GLU D OE2 
15839 N N   . GLY D 446 ? 0.3456 0.2812 0.2545 0.0082  0.0106  0.0496  446 GLY D N   
15840 C CA  . GLY D 446 ? 0.3289 0.2711 0.2521 0.0130  0.0094  0.0514  446 GLY D CA  
15841 C C   . GLY D 446 ? 0.3423 0.2743 0.2636 0.0155  0.0047  0.0460  446 GLY D C   
15842 O O   . GLY D 446 ? 0.3470 0.2651 0.2583 0.0174  0.0005  0.0407  446 GLY D O   
15843 N N   . SER D 447 ? 0.3093 0.2486 0.2404 0.0160  0.0056  0.0475  447 SER D N   
15844 C CA  . SER D 447 ? 0.3676 0.3027 0.3032 0.0184  0.0027  0.0417  447 SER D CA  
15845 C C   . SER D 447 ? 0.3742 0.3044 0.3197 0.0219  -0.0015 0.0361  447 SER D C   
15846 O O   . SER D 447 ? 0.3251 0.2504 0.2719 0.0252  -0.0082 0.0296  447 SER D O   
15847 C CB  . SER D 447 ? 0.3498 0.2939 0.2948 0.0173  0.0084  0.0444  447 SER D CB  
15848 O OG  . SER D 447 ? 0.3606 0.3088 0.3195 0.0176  0.0130  0.0479  447 SER D OG  
15849 N N   . ASP D 448 ? 0.3074 0.2379 0.2597 0.0218  0.0015  0.0381  448 ASP D N   
15850 C CA  . ASP D 448 ? 0.3201 0.2458 0.2833 0.0230  -0.0020 0.0319  448 ASP D CA  
15851 C C   . ASP D 448 ? 0.3573 0.2707 0.3074 0.0259  -0.0124 0.0244  448 ASP D C   
15852 O O   . ASP D 448 ? 0.3403 0.2532 0.3008 0.0274  -0.0206 0.0169  448 ASP D O   
15853 C CB  . ASP D 448 ? 0.2892 0.2115 0.2555 0.0228  0.0041  0.0353  448 ASP D CB  
15854 C CG  . ASP D 448 ? 0.3838 0.3145 0.3586 0.0220  0.0129  0.0445  448 ASP D CG  
15855 O OD1 . ASP D 448 ? 0.2968 0.2341 0.2638 0.0225  0.0149  0.0512  448 ASP D OD1 
15856 O OD2 . ASP D 448 ? 0.4279 0.3573 0.4162 0.0202  0.0173  0.0449  448 ASP D OD2 
15857 N N   . TRP D 449 ? 0.3679 0.2708 0.2950 0.0265  -0.0127 0.0263  449 TRP D N   
15858 C CA  . TRP D 449 ? 0.4415 0.3265 0.3480 0.0296  -0.0219 0.0206  449 TRP D CA  
15859 C C   . TRP D 449 ? 0.4703 0.3544 0.3786 0.0341  -0.0328 0.0162  449 TRP D C   
15860 O O   . TRP D 449 ? 0.4362 0.3137 0.3436 0.0384  -0.0450 0.0093  449 TRP D O   
15861 C CB  . TRP D 449 ? 0.4224 0.2947 0.3024 0.0278  -0.0165 0.0244  449 TRP D CB  
15862 C CG  . TRP D 449 ? 0.3379 0.2194 0.2242 0.0244  -0.0044 0.0298  449 TRP D CG  
15863 C CD1 . TRP D 449 ? 0.3694 0.2613 0.2570 0.0202  0.0033  0.0358  449 TRP D CD1 
15864 C CD2 . TRP D 449 ? 0.3572 0.2390 0.2515 0.0257  0.0009  0.0290  449 TRP D CD2 
15865 N NE1 . TRP D 449 ? 0.3529 0.2549 0.2517 0.0203  0.0118  0.0394  449 TRP D NE1 
15866 C CE2 . TRP D 449 ? 0.3507 0.2448 0.2527 0.0243  0.0115  0.0356  449 TRP D CE2 
15867 C CE3 . TRP D 449 ? 0.4090 0.2811 0.3049 0.0279  -0.0030 0.0227  449 TRP D CE3 
15868 C CZ2 . TRP D 449 ? 0.3728 0.2689 0.2841 0.0273  0.0193  0.0369  449 TRP D CZ2 
15869 C CZ3 . TRP D 449 ? 0.3960 0.2670 0.2984 0.0291  0.0059  0.0235  449 TRP D CZ3 
15870 C CH2 . TRP D 449 ? 0.4057 0.2879 0.3154 0.0299  0.0173  0.0309  449 TRP D CH2 
15871 N N   . PHE D 450 ? 0.5007 0.3918 0.4125 0.0337  -0.0291 0.0194  450 PHE D N   
15872 C CA  . PHE D 450 ? 0.4786 0.3691 0.3944 0.0398  -0.0371 0.0153  450 PHE D CA  
15873 C C   . PHE D 450 ? 0.4287 0.3380 0.3783 0.0416  -0.0396 0.0097  450 PHE D C   
15874 O O   . PHE D 450 ? 0.3627 0.2742 0.3223 0.0487  -0.0500 0.0035  450 PHE D O   
15875 C CB  . PHE D 450 ? 0.4594 0.3487 0.3665 0.0380  -0.0301 0.0194  450 PHE D CB  
15876 C CG  . PHE D 450 ? 0.4825 0.3574 0.3621 0.0326  -0.0253 0.0245  450 PHE D CG  
15877 C CD1 . PHE D 450 ? 0.4027 0.2879 0.2852 0.0249  -0.0157 0.0298  450 PHE D CD1 
15878 C CD2 . PHE D 450 ? 0.4711 0.3220 0.3230 0.0351  -0.0300 0.0241  450 PHE D CD2 
15879 C CE1 . PHE D 450 ? 0.3928 0.2695 0.2565 0.0187  -0.0105 0.0333  450 PHE D CE1 
15880 C CE2 . PHE D 450 ? 0.4716 0.3090 0.2999 0.0276  -0.0231 0.0283  450 PHE D CE2 
15881 C CZ  . PHE D 450 ? 0.4552 0.3083 0.2924 0.0188  -0.0130 0.0323  450 PHE D CZ  
15882 N N   . TRP D 451 ? 0.4097 0.3327 0.3784 0.0354  -0.0298 0.0120  451 TRP D N   
15883 C CA  . TRP D 451 ? 0.3988 0.3385 0.4007 0.0344  -0.0292 0.0067  451 TRP D CA  
15884 C C   . TRP D 451 ? 0.4211 0.3597 0.4324 0.0366  -0.0435 -0.0024 451 TRP D C   
15885 O O   . TRP D 451 ? 0.3375 0.2891 0.3734 0.0400  -0.0514 -0.0101 451 TRP D O   
15886 C CB  . TRP D 451 ? 0.3568 0.3037 0.3702 0.0268  -0.0153 0.0122  451 TRP D CB  
15887 C CG  . TRP D 451 ? 0.3746 0.3336 0.4197 0.0226  -0.0131 0.0065  451 TRP D CG  
15888 C CD1 . TRP D 451 ? 0.3762 0.3318 0.4308 0.0180  -0.0156 0.0024  451 TRP D CD1 
15889 C CD2 . TRP D 451 ? 0.4208 0.3964 0.4934 0.0213  -0.0066 0.0029  451 TRP D CD2 
15890 N NE1 . TRP D 451 ? 0.3849 0.3546 0.4725 0.0125  -0.0116 -0.0033 451 TRP D NE1 
15891 C CE2 . TRP D 451 ? 0.4156 0.3992 0.5162 0.0145  -0.0053 -0.0030 451 TRP D CE2 
15892 C CE3 . TRP D 451 ? 0.4952 0.4787 0.5715 0.0247  -0.0002 0.0034  451 TRP D CE3 
15893 C CZ2 . TRP D 451 ? 0.4967 0.4987 0.6317 0.0102  0.0032  -0.0080 451 TRP D CZ2 
15894 C CZ3 . TRP D 451 ? 0.5582 0.5590 0.6666 0.0223  0.0087  -0.0017 451 TRP D CZ3 
15895 C CH2 . TRP D 451 ? 0.5668 0.5781 0.7059 0.0146  0.0109  -0.0071 451 TRP D CH2 
15896 N N   . TRP D 452 ? 0.4250 0.3485 0.4170 0.0348  -0.0473 -0.0025 452 TRP D N   
15897 C CA  . TRP D 452 ? 0.4643 0.3836 0.4601 0.0354  -0.0615 -0.0120 452 TRP D CA  
15898 C C   . TRP D 452 ? 0.5365 0.4445 0.5133 0.0447  -0.0798 -0.0166 452 TRP D C   
15899 O O   . TRP D 452 ? 0.4855 0.3957 0.4716 0.0469  -0.0961 -0.0260 452 TRP D O   
15900 C CB  . TRP D 452 ? 0.4542 0.3576 0.4324 0.0307  -0.0571 -0.0112 452 TRP D CB  
15901 C CG  . TRP D 452 ? 0.4434 0.3549 0.4420 0.0232  -0.0421 -0.0077 452 TRP D CG  
15902 C CD1 . TRP D 452 ? 0.4621 0.3704 0.4522 0.0216  -0.0273 0.0022  452 TRP D CD1 
15903 C CD2 . TRP D 452 ? 0.4359 0.3591 0.4668 0.0165  -0.0406 -0.0134 452 TRP D CD2 
15904 N NE1 . TRP D 452 ? 0.4866 0.4001 0.4972 0.0160  -0.0173 0.0041  452 TRP D NE1 
15905 C CE2 . TRP D 452 ? 0.4488 0.3702 0.4841 0.0116  -0.0237 -0.0054 452 TRP D CE2 
15906 C CE3 . TRP D 452 ? 0.4477 0.3835 0.5058 0.0139  -0.0520 -0.0247 452 TRP D CE3 
15907 C CZ2 . TRP D 452 ? 0.4311 0.3577 0.4923 0.0033  -0.0158 -0.0075 452 TRP D CZ2 
15908 C CZ3 . TRP D 452 ? 0.4402 0.3858 0.5296 0.0040  -0.0438 -0.0281 452 TRP D CZ3 
15909 C CH2 . TRP D 452 ? 0.4413 0.3796 0.5296 -0.0016 -0.0249 -0.0192 452 TRP D CH2 
15910 N N   . GLN D 453 ? 0.5724 0.4668 0.5219 0.0500  -0.0786 -0.0103 453 GLN D N   
15911 C CA  . GLN D 453 ? 0.6228 0.4990 0.5468 0.0597  -0.0954 -0.0129 453 GLN D CA  
15912 C C   . GLN D 453 ? 0.6859 0.5798 0.6403 0.0680  -0.1109 -0.0209 453 GLN D C   
15913 O O   . GLN D 453 ? 0.6405 0.5534 0.6227 0.0698  -0.1041 -0.0206 453 GLN D O   
15914 C CB  . GLN D 453 ? 0.5974 0.4549 0.4899 0.0622  -0.0883 -0.0045 453 GLN D CB  
15915 C CG  . GLN D 453 ? 0.6365 0.4694 0.4983 0.0732  -0.1037 -0.0049 453 GLN D CG  
15916 C CD  . GLN D 453 ? 0.6471 0.4534 0.4715 0.0748  -0.1147 -0.0068 453 GLN D CD  
15917 O OE1 . GLN D 453 ? 0.6040 0.4130 0.4310 0.0687  -0.1141 -0.0107 453 GLN D OE1 
15918 N NE2 . GLN D 453 ? 0.6242 0.4006 0.4100 0.0833  -0.1244 -0.0039 453 GLN D NE2 
15919 N N   . GLY D 454 ? 0.8019 0.6901 0.7513 0.0732  -0.1318 -0.0287 454 GLY D N   
15920 C CA  . GLY D 454 ? 0.8858 0.7991 0.8757 0.0767  -0.1483 -0.0397 454 GLY D CA  
15921 C C   . GLY D 454 ? 0.9683 0.9086 0.9990 0.0840  -0.1478 -0.0421 454 GLY D C   
15922 O O   . GLY D 454 ? 1.0124 0.9419 1.0270 0.0931  -0.1445 -0.0361 454 GLY D O   
15923 N N   . GLU D 455 ? 1.0047 0.9788 1.0881 0.0800  -0.1488 -0.0510 455 GLU D N   
15924 C CA  . GLU D 455 ? 1.0306 1.0204 1.1420 0.0654  -0.1459 -0.0582 455 GLU D CA  
15925 C C   . GLU D 455 ? 1.0628 1.0461 1.1670 0.0637  -0.1695 -0.0683 455 GLU D C   
15926 O O   . GLU D 455 ? 1.0996 1.0515 1.1553 0.0660  -0.1777 -0.0657 455 GLU D O   
15927 C CB  . GLU D 455 ? 1.0103 0.9875 1.1047 0.0524  -0.1214 -0.0493 455 GLU D CB  
15928 C CG  . GLU D 455 ? 0.9978 0.9914 1.1156 0.0482  -0.0980 -0.0433 455 GLU D CG  
15929 C CD  . GLU D 455 ? 1.0103 1.0034 1.1337 0.0339  -0.0785 -0.0391 455 GLU D CD  
15930 O OE1 . GLU D 455 ? 1.0328 1.0242 1.1642 0.0256  -0.0829 -0.0452 455 GLU D OE1 
15931 O OE2 . GLU D 455 ? 0.9877 0.9802 1.1060 0.0314  -0.0594 -0.0299 455 GLU D OE2 
15932 N N   . GLU D 456 ? 1.0300 1.0437 1.1838 0.0585  -0.1792 -0.0807 456 GLU D N   
15933 C CA  . GLU D 456 ? 1.0178 1.0295 1.1725 0.0522  -0.2000 -0.0928 456 GLU D CA  
15934 C C   . GLU D 456 ? 1.0244 1.0028 1.1359 0.0416  -0.1894 -0.0890 456 GLU D C   
15935 O O   . GLU D 456 ? 1.0253 0.9977 1.1332 0.0336  -0.1632 -0.0801 456 GLU D O   
15936 C CB  . GLU D 456 ? 0.9755 1.0264 1.1964 0.0403  -0.2003 -0.1056 456 GLU D CB  
15937 N N   . LYS D 457 ? 1.0099 0.9662 1.0880 0.0428  -0.2105 -0.0960 457 LYS D N   
15938 C CA  . LYS D 457 ? 0.9920 0.9113 1.0203 0.0368  -0.2023 -0.0931 457 LYS D CA  
15939 C C   . LYS D 457 ? 0.9993 0.9204 1.0450 0.0219  -0.1753 -0.0903 457 LYS D C   
15940 O O   . LYS D 457 ? 1.0441 0.9573 1.0768 0.0224  -0.1524 -0.0774 457 LYS D O   
15941 C CB  . LYS D 457 ? 0.9947 0.8966 0.9980 0.0360  -0.2289 -0.1063 457 LYS D CB  
15942 N N   . ALA D 458 ? 0.9209 0.8520 0.9966 0.0085  -0.1783 -0.1023 458 ALA D N   
15943 C CA  . ALA D 458 ? 0.7972 0.7260 0.8897 -0.0061 -0.1544 -0.1007 458 ALA D CA  
15944 C C   . ALA D 458 ? 0.6956 0.5853 0.7392 -0.0076 -0.1445 -0.0973 458 ALA D C   
15945 O O   . ALA D 458 ? 0.6520 0.5215 0.6528 0.0027  -0.1420 -0.0887 458 ALA D O   
15946 C CB  . ALA D 458 ? 0.7548 0.7016 0.8727 -0.0063 -0.1294 -0.0877 458 ALA D CB  
15947 N N   . PRO D 459 ? 0.6845 0.5619 0.7339 -0.0204 -0.1374 -0.1045 459 PRO D N   
15948 C CA  . PRO D 459 ? 0.6968 0.5356 0.7002 -0.0205 -0.1293 -0.1042 459 PRO D CA  
15949 C C   . PRO D 459 ? 0.7348 0.5631 0.7162 -0.0123 -0.1057 -0.0868 459 PRO D C   
15950 O O   . PRO D 459 ? 0.6356 0.4792 0.6420 -0.0136 -0.0881 -0.0761 459 PRO D O   
15951 C CB  . PRO D 459 ? 0.7029 0.5342 0.7278 -0.0364 -0.1218 -0.1138 459 PRO D CB  
15952 C CG  . PRO D 459 ? 0.7051 0.5708 0.7829 -0.0462 -0.1355 -0.1244 459 PRO D CG  
15953 C CD  . PRO D 459 ? 0.6780 0.5747 0.7769 -0.0360 -0.1348 -0.1139 459 PRO D CD  
15954 N N   . PHE D 460 ? 0.7925 0.5949 0.7262 -0.0040 -0.1059 -0.0843 460 PHE D N   
15955 C CA  . PHE D 460 ? 0.7639 0.5538 0.6734 0.0031  -0.0848 -0.0706 460 PHE D CA  
15956 C C   . PHE D 460 ? 0.6694 0.4768 0.5807 0.0112  -0.0809 -0.0574 460 PHE D C   
15957 O O   . PHE D 460 ? 0.6467 0.4501 0.5465 0.0151  -0.0635 -0.0464 460 PHE D O   
15958 C CB  . PHE D 460 ? 0.7545 0.5413 0.6810 -0.0016 -0.0622 -0.0648 460 PHE D CB  
15959 C CG  . PHE D 460 ? 0.7665 0.5321 0.6923 -0.0107 -0.0624 -0.0773 460 PHE D CG  
15960 C CD1 . PHE D 460 ? 0.8555 0.5882 0.7412 -0.0086 -0.0626 -0.0852 460 PHE D CD1 
15961 C CD2 . PHE D 460 ? 0.7307 0.5065 0.6940 -0.0222 -0.0606 -0.0817 460 PHE D CD2 
15962 C CE1 . PHE D 460 ? 0.8782 0.5872 0.7602 -0.0174 -0.0625 -0.0982 460 PHE D CE1 
15963 C CE2 . PHE D 460 ? 0.7964 0.5492 0.7582 -0.0323 -0.0602 -0.0941 460 PHE D CE2 
15964 C CZ  . PHE D 460 ? 0.8556 0.5744 0.7763 -0.0297 -0.0619 -0.1027 460 PHE D CZ  
15965 N N   . VAL D 461 ? 0.6606 0.4866 0.5856 0.0143  -0.0967 -0.0588 461 VAL D N   
15966 C CA  . VAL D 461 ? 0.6609 0.4973 0.5825 0.0219  -0.0918 -0.0471 461 VAL D CA  
15967 C C   . VAL D 461 ? 0.6863 0.4978 0.5594 0.0290  -0.0929 -0.0432 461 VAL D C   
15968 O O   . VAL D 461 ? 0.7674 0.5803 0.6312 0.0325  -0.0816 -0.0324 461 VAL D O   
15969 C CB  . VAL D 461 ? 0.7502 0.6113 0.7003 0.0250  -0.1063 -0.0497 461 VAL D CB  
15970 C CG1 . VAL D 461 ? 0.7361 0.6231 0.7362 0.0163  -0.1005 -0.0530 461 VAL D CG1 
15971 C CG2 . VAL D 461 ? 0.8218 0.6731 0.7530 0.0308  -0.1330 -0.0598 461 VAL D CG2 
15972 N N   . GLU D 462 ? 0.6069 0.3940 0.4465 0.0304  -0.1063 -0.0522 462 GLU D N   
15973 C CA  . GLU D 462 ? 0.7266 0.4851 0.5153 0.0358  -0.1028 -0.0480 462 GLU D CA  
15974 C C   . GLU D 462 ? 0.6598 0.4122 0.4410 0.0337  -0.0761 -0.0399 462 GLU D C   
15975 O O   . GLU D 462 ? 0.7366 0.4772 0.4904 0.0367  -0.0661 -0.0324 462 GLU D O   
15976 C CB  . GLU D 462 ? 0.9146 0.6437 0.6637 0.0367  -0.1198 -0.0598 462 GLU D CB  
15977 C CG  . GLU D 462 ? 1.0911 0.8072 0.8383 0.0294  -0.1133 -0.0696 462 GLU D CG  
15978 C CD  . GLU D 462 ? 1.2000 0.9358 0.9895 0.0219  -0.1268 -0.0806 462 GLU D CD  
15979 O OE1 . GLU D 462 ? 1.2437 0.9703 1.0391 0.0144  -0.1189 -0.0878 462 GLU D OE1 
15980 O OE2 . GLU D 462 ? 1.2096 0.9697 1.0279 0.0234  -0.1441 -0.0824 462 GLU D OE2 
15981 N N   . VAL D 463 ? 0.5223 0.2829 0.3294 0.0287  -0.0641 -0.0411 463 VAL D N   
15982 C CA  . VAL D 463 ? 0.5878 0.3465 0.3938 0.0291  -0.0404 -0.0332 463 VAL D CA  
15983 C C   . VAL D 463 ? 0.5308 0.3118 0.3538 0.0308  -0.0310 -0.0202 463 VAL D C   
15984 O O   . VAL D 463 ? 0.4997 0.2777 0.3097 0.0325  -0.0165 -0.0133 463 VAL D O   
15985 C CB  . VAL D 463 ? 0.5919 0.3518 0.4217 0.0252  -0.0311 -0.0364 463 VAL D CB  
15986 C CG1 . VAL D 463 ? 0.5605 0.3222 0.3942 0.0288  -0.0083 -0.0269 463 VAL D CG1 
15987 C CG2 . VAL D 463 ? 0.5598 0.2931 0.3679 0.0223  -0.0395 -0.0508 463 VAL D CG2 
15988 N N   . PHE D 464 ? 0.5049 0.3091 0.3584 0.0295  -0.0383 -0.0176 464 PHE D N   
15989 C CA  . PHE D 464 ? 0.5014 0.3238 0.3665 0.0305  -0.0316 -0.0070 464 PHE D CA  
15990 C C   . PHE D 464 ? 0.5160 0.3257 0.3494 0.0335  -0.0347 -0.0043 464 PHE D C   
15991 O O   . PHE D 464 ? 0.4664 0.2806 0.2957 0.0328  -0.0232 0.0039  464 PHE D O   
15992 C CB  . PHE D 464 ? 0.4498 0.2949 0.3482 0.0290  -0.0385 -0.0067 464 PHE D CB  
15993 C CG  . PHE D 464 ? 0.4587 0.3158 0.3872 0.0246  -0.0297 -0.0055 464 PHE D CG  
15994 C CD1 . PHE D 464 ? 0.4388 0.3058 0.3771 0.0245  -0.0151 0.0049  464 PHE D CD1 
15995 C CD2 . PHE D 464 ? 0.5095 0.3658 0.4547 0.0201  -0.0364 -0.0146 464 PHE D CD2 
15996 C CE1 . PHE D 464 ? 0.3791 0.2513 0.3392 0.0214  -0.0066 0.0077  464 PHE D CE1 
15997 C CE2 . PHE D 464 ? 0.5019 0.3637 0.4712 0.0149  -0.0260 -0.0127 464 PHE D CE2 
15998 C CZ  . PHE D 464 ? 0.4383 0.3060 0.4128 0.0163  -0.0108 -0.0007 464 PHE D CZ  
15999 N N   . ASP D 465 ? 0.5206 0.3125 0.3300 0.0366  -0.0506 -0.0111 465 ASP D N   
16000 C CA  . ASP D 465 ? 0.5835 0.3551 0.3553 0.0397  -0.0527 -0.0077 465 ASP D CA  
16001 C C   . ASP D 465 ? 0.5605 0.3119 0.3013 0.0376  -0.0360 -0.0056 465 ASP D C   
16002 O O   . ASP D 465 ? 0.5760 0.3221 0.3013 0.0359  -0.0251 0.0014  465 ASP D O   
16003 C CB  . ASP D 465 ? 0.5438 0.2985 0.2938 0.0455  -0.0758 -0.0147 465 ASP D CB  
16004 C CG  . ASP D 465 ? 0.6074 0.3340 0.3121 0.0496  -0.0778 -0.0099 465 ASP D CG  
16005 O OD1 . ASP D 465 ? 0.5506 0.2825 0.2601 0.0519  -0.0784 -0.0037 465 ASP D OD1 
16006 O OD2 . ASP D 465 ? 0.6753 0.3713 0.3365 0.0502  -0.0775 -0.0124 465 ASP D OD2 
16007 N N   . LYS D 466 ? 0.5139 0.2534 0.2461 0.0369  -0.0326 -0.0124 466 LYS D N   
16008 C CA  . LYS D 466 ? 0.5674 0.2893 0.2736 0.0358  -0.0136 -0.0115 466 LYS D CA  
16009 C C   . LYS D 466 ? 0.5935 0.3388 0.3267 0.0334  0.0065  -0.0025 466 LYS D C   
16010 O O   . LYS D 466 ? 0.5746 0.3142 0.2915 0.0312  0.0207  0.0022  466 LYS D O   
16011 C CB  . LYS D 466 ? 0.6568 0.3634 0.3548 0.0362  -0.0124 -0.0215 466 LYS D CB  
16012 C CG  . LYS D 466 ? 0.7609 0.4486 0.4335 0.0365  0.0095  -0.0222 466 LYS D CG  
16013 C CD  . LYS D 466 ? 0.8776 0.5465 0.5403 0.0374  0.0109  -0.0334 466 LYS D CD  
16014 C CE  . LYS D 466 ? 1.0333 0.6694 0.6511 0.0375  -0.0079 -0.0442 466 LYS D CE  
16015 N NZ  . LYS D 466 ? 1.0832 0.7306 0.7251 0.0356  -0.0325 -0.0512 466 LYS D NZ  
16016 N N   . LEU D 467 ? 0.5344 0.3064 0.3091 0.0332  0.0075  0.0000  467 LEU D N   
16017 C CA  . LEU D 467 ? 0.4874 0.2836 0.2884 0.0321  0.0223  0.0087  467 LEU D CA  
16018 C C   . LEU D 467 ? 0.5172 0.3227 0.3162 0.0284  0.0224  0.0156  467 LEU D C   
16019 O O   . LEU D 467 ? 0.5773 0.3869 0.3730 0.0254  0.0362  0.0199  467 LEU D O   
16020 C CB  . LEU D 467 ? 0.4491 0.2664 0.2875 0.0331  0.0203  0.0109  467 LEU D CB  
16021 C CG  . LEU D 467 ? 0.4522 0.2596 0.2956 0.0360  0.0259  0.0058  467 LEU D CG  
16022 C CD1 . LEU D 467 ? 0.5125 0.3349 0.3880 0.0357  0.0225  0.0084  467 LEU D CD1 
16023 C CD2 . LEU D 467 ? 0.4344 0.2422 0.2770 0.0398  0.0445  0.0087  467 LEU D CD2 
16024 N N   . PHE D 468 ? 0.4825 0.2912 0.2845 0.0283  0.0078  0.0159  468 PHE D N   
16025 C CA  . PHE D 468 ? 0.5387 0.3523 0.3373 0.0249  0.0079  0.0216  468 PHE D CA  
16026 C C   . PHE D 468 ? 0.5777 0.3679 0.3402 0.0216  0.0161  0.0227  468 PHE D C   
16027 O O   . PHE D 468 ? 0.5227 0.3208 0.2880 0.0154  0.0278  0.0277  468 PHE D O   
16028 C CB  . PHE D 468 ? 0.4961 0.3093 0.2974 0.0279  -0.0090 0.0197  468 PHE D CB  
16029 C CG  . PHE D 468 ? 0.5344 0.3431 0.3243 0.0257  -0.0100 0.0240  468 PHE D CG  
16030 C CD1 . PHE D 468 ? 0.5101 0.3393 0.3201 0.0209  -0.0034 0.0290  468 PHE D CD1 
16031 C CD2 . PHE D 468 ? 0.5763 0.3575 0.3330 0.0291  -0.0188 0.0226  468 PHE D CD2 
16032 C CE1 . PHE D 468 ? 0.5367 0.3586 0.3347 0.0178  -0.0040 0.0316  468 PHE D CE1 
16033 C CE2 . PHE D 468 ? 0.5951 0.3671 0.3393 0.0274  -0.0189 0.0264  468 PHE D CE2 
16034 C CZ  . PHE D 468 ? 0.5540 0.3463 0.3195 0.0210  -0.0109 0.0303  468 PHE D CZ  
16035 N N   . ARG D 469 ? 0.5611 0.3215 0.2885 0.0249  0.0103  0.0177  469 ARG D N   
16036 C CA  . ARG D 469 ? 0.6089 0.3398 0.2939 0.0218  0.0186  0.0194  469 ARG D CA  
16037 C C   . ARG D 469 ? 0.5876 0.3214 0.2725 0.0168  0.0420  0.0204  469 ARG D C   
16038 O O   . ARG D 469 ? 0.5812 0.3076 0.2516 0.0097  0.0560  0.0244  469 ARG D O   
16039 C CB  . ARG D 469 ? 0.6601 0.3563 0.3035 0.0279  0.0041  0.0140  469 ARG D CB  
16040 C CG  . ARG D 469 ? 0.6919 0.3868 0.3372 0.0341  -0.0190 0.0135  469 ARG D CG  
16041 C CD  . ARG D 469 ? 0.7971 0.4601 0.4026 0.0415  -0.0370 0.0079  469 ARG D CD  
16042 N NE  . ARG D 469 ? 0.8381 0.4996 0.4453 0.0496  -0.0595 0.0077  469 ARG D NE  
16043 C CZ  . ARG D 469 ? 0.8059 0.4472 0.3889 0.0525  -0.0628 0.0132  469 ARG D CZ  
16044 N NH1 . ARG D 469 ? 0.7503 0.3767 0.3158 0.0446  -0.0431 0.0178  469 ARG D NH1 
16045 N NH2 . ARG D 469 ? 0.7950 0.4396 0.3886 0.0619  -0.0828 0.0113  469 ARG D NH2 
16046 N N   . SER D 470 ? 0.6305 0.3763 0.3348 0.0202  0.0476  0.0166  470 SER D N   
16047 C CA  . SER D 470 ? 0.5958 0.3487 0.3072 0.0178  0.0706  0.0170  470 SER D CA  
16048 C C   . SER D 470 ? 0.5655 0.3532 0.3142 0.0121  0.0801  0.0238  470 SER D C   
16049 O O   . SER D 470 ? 0.5592 0.3504 0.3066 0.0058  0.0983  0.0257  470 SER D O   
16050 C CB  . SER D 470 ? 0.6306 0.3869 0.3560 0.0247  0.0733  0.0115  470 SER D CB  
16051 O OG  . SER D 470 ? 0.7640 0.4870 0.4524 0.0281  0.0639  0.0035  470 SER D OG  
16052 N N   . PHE D 471 ? 0.4635 0.2774 0.2455 0.0135  0.0682  0.0271  471 PHE D N   
16053 C CA  . PHE D 471 ? 0.4791 0.3243 0.2921 0.0078  0.0732  0.0329  471 PHE D CA  
16054 C C   . PHE D 471 ? 0.5273 0.3616 0.3203 -0.0022 0.0754  0.0352  471 PHE D C   
16055 O O   . PHE D 471 ? 0.5134 0.3629 0.3188 -0.0108 0.0881  0.0374  471 PHE D O   
16056 C CB  . PHE D 471 ? 0.4953 0.3634 0.3378 0.0112  0.0593  0.0359  471 PHE D CB  
16057 C CG  . PHE D 471 ? 0.4391 0.3159 0.3020 0.0199  0.0584  0.0350  471 PHE D CG  
16058 C CD1 . PHE D 471 ? 0.4192 0.3077 0.2988 0.0240  0.0718  0.0356  471 PHE D CD1 
16059 C CD2 . PHE D 471 ? 0.3982 0.2711 0.2650 0.0239  0.0451  0.0335  471 PHE D CD2 
16060 C CE1 . PHE D 471 ? 0.4434 0.3344 0.3386 0.0327  0.0715  0.0352  471 PHE D CE1 
16061 C CE2 . PHE D 471 ? 0.3423 0.2184 0.2254 0.0301  0.0456  0.0327  471 PHE D CE2 
16062 C CZ  . PHE D 471 ? 0.3807 0.2639 0.2763 0.0349  0.0584  0.0341  471 PHE D CZ  
16063 N N   . VAL D 472 ? 0.5151 0.3221 0.2775 -0.0013 0.0629  0.0342  472 VAL D N   
16064 C CA  . VAL D 472 ? 0.5621 0.3502 0.2994 -0.0098 0.0649  0.0367  472 VAL D CA  
16065 C C   . VAL D 472 ? 0.6153 0.3815 0.3240 -0.0166 0.0843  0.0366  472 VAL D C   
16066 O O   . VAL D 472 ? 0.6296 0.3953 0.3355 -0.0285 0.0961  0.0392  472 VAL D O   
16067 C CB  . VAL D 472 ? 0.5545 0.3162 0.2652 -0.0036 0.0464  0.0359  472 VAL D CB  
16068 C CG1 . VAL D 472 ? 0.6578 0.3866 0.3302 -0.0099 0.0502  0.0387  472 VAL D CG1 
16069 C CG2 . VAL D 472 ? 0.5269 0.3129 0.2687 -0.0003 0.0326  0.0364  472 VAL D CG2 
16070 N N   . ARG D 473 ? 0.6423 0.3891 0.3287 -0.0106 0.0892  0.0329  473 ARG D N   
16071 C CA  . ARG D 473 ? 0.6756 0.4006 0.3330 -0.0173 0.1114  0.0324  473 ARG D CA  
16072 C C   . ARG D 473 ? 0.6588 0.4203 0.3572 -0.0243 0.1324  0.0328  473 ARG D C   
16073 O O   . ARG D 473 ? 0.6369 0.3978 0.3323 -0.0368 0.1497  0.0348  473 ARG D O   
16074 C CB  . ARG D 473 ? 0.6926 0.3873 0.3142 -0.0087 0.1117  0.0272  473 ARG D CB  
16075 C CG  . ARG D 473 ? 0.8225 0.5024 0.4263 -0.0138 0.1355  0.0244  473 ARG D CG  
16076 C CD  . ARG D 473 ? 0.9234 0.5699 0.4895 -0.0054 0.1316  0.0179  473 ARG D CD  
16077 N NE  . ARG D 473 ? 1.0730 0.7077 0.6271 -0.0096 0.1551  0.0147  473 ARG D NE  
16078 C CZ  . ARG D 473 ? 1.1175 0.7473 0.6670 -0.0038 0.1668  0.0086  473 ARG D CZ  
16079 N NH1 . ARG D 473 ? 1.0774 0.7111 0.6315 0.0060  0.1570  0.0043  473 ARG D NH1 
16080 N NH2 . ARG D 473 ? 1.1709 0.7901 0.7104 -0.0080 0.1889  0.0061  473 ARG D NH2 
16081 N N   . ARG D 474 ? 0.6206 0.4152 0.3602 -0.0163 0.1303  0.0312  474 ARG D N   
16082 C CA  . ARG D 474 ? 0.6211 0.4535 0.4038 -0.0191 0.1475  0.0314  474 ARG D CA  
16083 C C   . ARG D 474 ? 0.6331 0.4948 0.4453 -0.0313 0.1475  0.0353  474 ARG D C   
16084 O O   . ARG D 474 ? 0.5422 0.4271 0.3789 -0.0396 0.1655  0.0349  474 ARG D O   
16085 C CB  . ARG D 474 ? 0.5829 0.4405 0.4009 -0.0059 0.1409  0.0303  474 ARG D CB  
16086 C CG  . ARG D 474 ? 0.6146 0.5133 0.4806 -0.0046 0.1555  0.0311  474 ARG D CG  
16087 C CD  . ARG D 474 ? 0.7794 0.6692 0.6359 -0.0065 0.1831  0.0267  474 ARG D CD  
16088 N NE  . ARG D 474 ? 0.8909 0.8033 0.7813 0.0060  0.1939  0.0243  474 ARG D NE  
16089 C CZ  . ARG D 474 ? 0.9812 0.9382 0.9230 0.0071  0.2028  0.0259  474 ARG D CZ  
16090 N NH1 . ARG D 474 ? 0.9830 0.9682 0.9487 -0.0060 0.2019  0.0289  474 ARG D NH1 
16091 N NH2 . ARG D 474 ? 1.0193 0.9925 0.9894 0.0216  0.2119  0.0239  474 ARG D NH2 
16092 N N   . ALA D 475 ? 0.6068 0.4686 0.4181 -0.0330 0.1279  0.0380  475 ALA D N   
16093 C CA  . ALA D 475 ? 0.6293 0.5158 0.4647 -0.0450 0.1255  0.0404  475 ALA D CA  
16094 C C   . ALA D 475 ? 0.6731 0.5415 0.4873 -0.0620 0.1415  0.0403  475 ALA D C   
16095 O O   . ALA D 475 ? 0.6923 0.5867 0.5337 -0.0751 0.1461  0.0403  475 ALA D O   
16096 C CB  . ALA D 475 ? 0.6385 0.5222 0.4709 -0.0421 0.1030  0.0423  475 ALA D CB  
16097 N N   . GLN D 476 ? 0.6922 0.5153 0.4572 -0.0630 0.1499  0.0401  476 GLN D N   
16098 C CA  . GLN D 476 ? 0.7303 0.5309 0.4720 -0.0790 0.1654  0.0404  476 GLN D CA  
16099 C C   . GLN D 476 ? 0.8052 0.6143 0.5570 -0.0836 0.1895  0.0370  476 GLN D C   
16100 O O   . GLN D 476 ? 0.7692 0.5696 0.5155 -0.0965 0.2011  0.0355  476 GLN D O   
16101 C CB  . GLN D 476 ? 0.7518 0.5031 0.4437 -0.0734 0.1520  0.0401  476 GLN D CB  
16102 C CG  . GLN D 476 ? 0.7192 0.4626 0.4041 -0.0682 0.1291  0.0424  476 GLN D CG  
16103 C CD  . GLN D 476 ? 0.7848 0.4874 0.4290 -0.0559 0.1134  0.0413  476 GLN D CD  
16104 O OE1 . GLN D 476 ? 0.8309 0.5034 0.4488 -0.0591 0.1120  0.0408  476 GLN D OE1 
16105 N NE2 . GLN D 476 ? 0.8018 0.5032 0.4417 -0.0417 0.1010  0.0405  476 GLN D NE2 
16106 N N   . GLU D 477 ? 0.8548 0.6786 0.6208 -0.0728 0.1980  0.0351  477 GLU D N   
16107 C CA  . GLU D 477 ? 0.9310 0.7705 0.7160 -0.0752 0.2219  0.0311  477 GLU D CA  
16108 C C   . GLU D 477 ? 0.9011 0.7995 0.7508 -0.0787 0.2307  0.0311  477 GLU D C   
16109 O O   . GLU D 477 ? 0.8961 0.8214 0.7747 -0.0742 0.2092  0.0331  477 GLU D O   
16110 C CB  . GLU D 477 ? 0.9773 0.7951 0.7387 -0.0599 0.2265  0.0276  477 GLU D CB  
16111 C CG  . GLU D 477 ? 1.0423 0.8061 0.7437 -0.0541 0.2123  0.0271  477 GLU D CG  
16112 C CD  . GLU D 477 ? 1.0770 0.8217 0.7570 -0.0398 0.2131  0.0226  477 GLU D CD  
16113 O OE1 . GLU D 477 ? 1.1156 0.8177 0.7480 -0.0351 0.2021  0.0210  477 GLU D OE1 
16114 O OE2 . GLU D 477 ? 1.0637 0.8357 0.7756 -0.0326 0.2242  0.0203  477 GLU D OE2 
# 
