data_9JLR
# 
_entry.id   9JLR 
# 
_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   9JLR         pdb_00009jlr 10.2210/pdb9jlr/pdb 
WWPDB D_1300051231 ?            ?                   
# 
_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                        9JLR 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-19 
_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 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhu, Z.M.'   1 ? 
'Wang, W.W.'  2 ? 
'Li, M.J.'    3 ? 
'Xu, Q.'      4 ? 
'Zhou, H.'    5 ? 
'Huang, L.Q.' 6 ? 
'Wang, Q.S.'  7 ? 
'Yu, F.'      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            'Cryst.Growth Des.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1528-7505 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            24 
_citation.language                  ? 
_citation.page_first                10350 
_citation.page_last                 10357 
_citation.title                     
'High-Temperature Crystallization Method for the GH57 Family Hyperthermophilic Amylopullulanase from Aquifex aeolicus' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.cgd.4c01306 
_citation.pdbx_database_id_PubMed   ? 
_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 'Wang, W.'  2 ? 
primary 'Huang, L.' 3 ? 
primary 'Xu, Q.'    4 ? 
primary 'Zhou, H.'  5 ? 
primary 'Li, M.'    6 ? 
primary 'Yu, F.'    7 ? 
primary 'Wang, Q.'  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' 58323.418 4  ? E256Q ? ? 
2 branched man 
;alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
;
828.719   4  ? ?     ? ? 
3 water    nat water 18.015    51 ? ?     ? ? 
# 
_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
YFEIFGEHPVYMWPPQASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQELEH
HHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPQASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQELEH
HHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     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 GLN 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 ASP 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 
1 478 LEU n 
1 479 GLU n 
1 480 HIS n 
1 481 HIS n 
1 482 HIS n 
1 483 HIS n 
1 484 HIS n 
1 485 HIS 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                   485 
_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 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-ROH                                              'Glycam Condensed Sequence' GMML 
1.0   
2 2 'WURCS=2.0/1,5,4/[a2122h-1a_1-5]/1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1'                          WURCS                       
PDB2Glycan 1.1.0 
3 2 '[][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}}}}' LINUCS                      
PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 GLC C1 O1 1 GLC O4 HO4 sing ? 
2 2 3 GLC C1 O1 2 GLC O4 HO4 sing ? 
3 2 4 GLC C1 O1 3 GLC O4 HO4 sing ? 
4 2 5 GLC C1 O1 4 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 
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  
HIS 'L-peptide linking'           y HISTIDINE             ?                                     'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                   . WATER                 ?                                     'H2 O'           18.015  
ILE 'L-peptide linking'           y ISOLEUCINE            ?                                     'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE               ?                                     'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                ?                                     'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'           y METHIONINE            ?                                     'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking'           y PHENYLALANINE         ?                                     'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'           y PROLINE               ?                                     'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE                ?                                     'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE             ?                                     'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN            ?                                     'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE              ?                                     'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE                ?                                     'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_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   1   MET MET 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 GLN 256 256 256 GLN GLN 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 ASP 352 352 352 ASP ASP 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 
A 1 478 LEU 478 478 ?   ?   ?   A . n 
A 1 479 GLU 479 479 ?   ?   ?   A . n 
A 1 480 HIS 480 480 ?   ?   ?   A . n 
A 1 481 HIS 481 481 ?   ?   ?   A . n 
A 1 482 HIS 482 482 ?   ?   ?   A . n 
A 1 483 HIS 483 483 ?   ?   ?   A . n 
A 1 484 HIS 484 484 ?   ?   ?   A . n 
A 1 485 HIS 485 485 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET 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 GLN 256 256 256 GLN GLN 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 ASP 352 352 352 ASP ASP 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 
B 1 478 LEU 478 478 ?   ?   ?   B . n 
B 1 479 GLU 479 479 ?   ?   ?   B . n 
B 1 480 HIS 480 480 ?   ?   ?   B . n 
B 1 481 HIS 481 481 ?   ?   ?   B . n 
B 1 482 HIS 482 482 ?   ?   ?   B . n 
B 1 483 HIS 483 483 ?   ?   ?   B . n 
B 1 484 HIS 484 484 ?   ?   ?   B . n 
B 1 485 HIS 485 485 ?   ?   ?   B . n 
C 1 1   MET 1   1   1   MET MET 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 GLN 256 256 256 GLN GLN 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 ASP 352 352 352 ASP ASP 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 
C 1 478 LEU 478 478 478 LEU LEU C . n 
C 1 479 GLU 479 479 479 GLU GLU C . n 
C 1 480 HIS 480 480 480 HIS HIS C . n 
C 1 481 HIS 481 481 481 HIS HIS C . n 
C 1 482 HIS 482 482 482 HIS HIS C . n 
C 1 483 HIS 483 483 483 HIS HIS C . n 
C 1 484 HIS 484 484 484 HIS HIS C . n 
C 1 485 HIS 485 485 ?   ?   ?   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 GLN 256 256 256 GLN GLN 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 ASP 352 352 352 ASP ASP 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 
D 1 478 LEU 478 478 478 LEU LEU D . n 
D 1 479 GLU 479 479 479 GLU GLU D . n 
D 1 480 HIS 480 480 480 HIS HIS D . n 
D 1 481 HIS 481 481 481 HIS HIS D . n 
D 1 482 HIS 482 482 482 HIS HIS D . n 
D 1 483 HIS 483 483 483 HIS HIS D . n 
D 1 484 HIS 484 484 484 HIS HIS D . n 
D 1 485 HIS 485 485 485 HIS HIS 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 1 E GLC 1 n 
E 2 GLC 2 E GLC 2 E GLC 2 n 
E 2 GLC 3 E GLC 3 E GLC 3 n 
E 2 GLC 4 E GLC 4 E GLC 4 n 
E 2 GLC 5 E GLC 5 E GLC 5 n 
F 2 GLC 1 F GLC 1 F GLC 1 n 
F 2 GLC 2 F GLC 2 F GLC 2 n 
F 2 GLC 3 F GLC 3 F GLC 3 n 
F 2 GLC 4 F GLC 4 F GLC 4 n 
F 2 GLC 5 F GLC 5 F GLC 5 n 
G 2 GLC 1 G GLC 1 G GLC 1 n 
G 2 GLC 2 G GLC 2 G GLC 2 n 
G 2 GLC 3 G GLC 3 G GLC 3 n 
G 2 GLC 4 G GLC 4 G GLC 4 n 
G 2 GLC 5 G GLC 5 G GLC 5 n 
H 2 GLC 1 H GLC 1 H GLC 1 n 
H 2 GLC 2 H GLC 2 H GLC 2 n 
H 2 GLC 3 H GLC 3 H GLC 3 n 
H 2 GLC 4 H GLC 4 H GLC 4 n 
H 2 GLC 5 H GLC 5 H GLC 5 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 HOH 1  501 10 HOH HOH A . 
I 3 HOH 2  502 33 HOH HOH A . 
I 3 HOH 3  503 20 HOH HOH A . 
I 3 HOH 4  504 46 HOH HOH A . 
I 3 HOH 5  505 42 HOH HOH A . 
I 3 HOH 6  506 45 HOH HOH A . 
I 3 HOH 7  507 4  HOH HOH A . 
I 3 HOH 8  508 40 HOH HOH A . 
I 3 HOH 9  509 21 HOH HOH A . 
I 3 HOH 10 510 26 HOH HOH A . 
I 3 HOH 11 511 7  HOH HOH A . 
I 3 HOH 12 512 51 HOH HOH A . 
I 3 HOH 13 513 41 HOH HOH A . 
I 3 HOH 14 514 32 HOH HOH A . 
I 3 HOH 15 515 30 HOH HOH A . 
I 3 HOH 16 516 39 HOH HOH A . 
I 3 HOH 17 517 9  HOH HOH A . 
I 3 HOH 18 518 48 HOH HOH A . 
I 3 HOH 19 519 15 HOH HOH A . 
I 3 HOH 20 520 43 HOH HOH A . 
I 3 HOH 21 521 13 HOH HOH A . 
J 3 HOH 1  501 47 HOH HOH B . 
J 3 HOH 2  502 14 HOH HOH B . 
J 3 HOH 3  503 28 HOH HOH B . 
J 3 HOH 4  504 37 HOH HOH B . 
J 3 HOH 5  505 17 HOH HOH B . 
J 3 HOH 6  506 35 HOH HOH B . 
J 3 HOH 7  507 38 HOH HOH B . 
J 3 HOH 8  508 12 HOH HOH B . 
J 3 HOH 9  509 5  HOH HOH B . 
J 3 HOH 10 510 22 HOH HOH B . 
K 3 HOH 1  501 36 HOH HOH C . 
K 3 HOH 2  502 3  HOH HOH C . 
K 3 HOH 3  503 27 HOH HOH C . 
K 3 HOH 4  504 11 HOH HOH C . 
K 3 HOH 5  505 6  HOH HOH C . 
K 3 HOH 6  506 50 HOH HOH C . 
K 3 HOH 7  507 44 HOH HOH C . 
K 3 HOH 8  508 31 HOH HOH C . 
L 3 HOH 1  501 18 HOH HOH D . 
L 3 HOH 2  502 24 HOH HOH D . 
L 3 HOH 3  503 1  HOH HOH D . 
L 3 HOH 4  504 2  HOH HOH D . 
L 3 HOH 5  505 29 HOH HOH D . 
L 3 HOH 6  506 49 HOH HOH D . 
L 3 HOH 7  507 16 HOH HOH D . 
L 3 HOH 8  508 34 HOH HOH D . 
L 3 HOH 9  509 23 HOH HOH D . 
L 3 HOH 10 510 25 HOH HOH D . 
L 3 HOH 11 511 8  HOH HOH D . 
L 3 HOH 12 512 19 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.46 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JLR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.170 
_cell.length_a_esd                 ? 
_cell.length_b                     165.170 
_cell.length_b_esd                 ? 
_cell.length_c                     98.010 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JLR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JLR 
_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             2.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.41 
_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    '45% MPD, 5% PEG8000, 0.1 M MES 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-08-21 
_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   0.97914 
_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 BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97914 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JLR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.79 
_reflns.d_resolution_low                               62.92 
_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                                     52825 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.990 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.79 
_reflns_shell.d_res_low                                     2.86 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3869 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.816 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.391 
_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                                  1.687 
_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                                 9JLR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.79 
_refine.ls_d_res_low                             46.01 
_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                     52769 
_refine.ls_number_reflns_R_free                  2612 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.16 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1907 
_refine.ls_R_factor_R_free                       0.2446 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1880 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.95 
_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                            0.40 
_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.pdbx_number_atoms_protein        16352 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         224 
_refine_hist.number_atoms_solvent             51 
_refine_hist.number_atoms_total               16627 
_refine_hist.d_res_high                       2.79 
_refine_hist.d_res_low                        46.01 
# 
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' ? 0.005 ? 17039 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.799 ? 23051 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.150 ? 2259  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058 ? 2457  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 2880  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.79 2.84  . . 158 2596 99.00 . . . . 0.3232 . . . . . . . . . . . 0.3772 
'X-RAY DIFFRACTION' 2.84 2.90  . . 123 2638 97.00 . . . . 0.3080 . . . . . . . . . . . 0.3863 
'X-RAY DIFFRACTION' 2.90 2.95  . . 163 2612 99.00 . . . . 0.2861 . . . . . . . . . . . 0.3653 
'X-RAY DIFFRACTION' 2.95 3.02  . . 146 2576 97.00 . . . . 0.2605 . . . . . . . . . . . 0.3065 
'X-RAY DIFFRACTION' 3.02 3.09  . . 148 2622 99.00 . . . . 0.2492 . . . . . . . . . . . 0.2843 
'X-RAY DIFFRACTION' 3.09 3.17  . . 147 2631 98.00 . . . . 0.2365 . . . . . . . . . . . 0.3146 
'X-RAY DIFFRACTION' 3.17 3.25  . . 161 2626 99.00 . . . . 0.2265 . . . . . . . . . . . 0.2888 
'X-RAY DIFFRACTION' 3.25 3.35  . . 144 2609 98.00 . . . . 0.2282 . . . . . . . . . . . 0.3180 
'X-RAY DIFFRACTION' 3.35 3.46  . . 123 2667 98.00 . . . . 0.2075 . . . . . . . . . . . 0.3072 
'X-RAY DIFFRACTION' 3.46 3.58  . . 143 2622 99.00 . . . . 0.1956 . . . . . . . . . . . 0.2473 
'X-RAY DIFFRACTION' 3.58 3.72  . . 123 2674 98.00 . . . . 0.1837 . . . . . . . . . . . 0.2595 
'X-RAY DIFFRACTION' 3.72 3.89  . . 130 2635 99.00 . . . . 0.1837 . . . . . . . . . . . 0.2389 
'X-RAY DIFFRACTION' 3.89 4.10  . . 155 2627 98.00 . . . . 0.1790 . . . . . . . . . . . 0.2199 
'X-RAY DIFFRACTION' 4.10 4.35  . . 141 2650 99.00 . . . . 0.1632 . . . . . . . . . . . 0.2309 
'X-RAY DIFFRACTION' 4.35 4.69  . . 116 2682 98.00 . . . . 0.1523 . . . . . . . . . . . 0.1879 
'X-RAY DIFFRACTION' 4.69 5.16  . . 122 2683 98.00 . . . . 0.1651 . . . . . . . . . . . 0.2334 
'X-RAY DIFFRACTION' 5.16 5.90  . . 141 2658 99.00 . . . . 0.1744 . . . . . . . . . . . 0.2412 
'X-RAY DIFFRACTION' 5.91 7.43  . . 103 2673 98.00 . . . . 0.1945 . . . . . . . . . . . 0.2242 
'X-RAY DIFFRACTION' 7.44 46.01 . . 125 2676 97.00 . . . . 0.1365 . . . . . . . . . . . 0.1557 
# 
_struct.entry_id                     9JLR 
_struct.title                        
'Crystal structure of GH57 family amylopullulanase from Aquifex aeolicus mutant E256Q in complex with maltopentaose' 
_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        9JLR 
_struct_keywords.text            'GH57 family, amylopullulanase, Aquifex aeolicus, 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 3 ? 
# 
_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 9JLR A 1 ? 477 ? O66934 1 ? 477 ? 1 477 
2 1 9JLR B 1 ? 477 ? O66934 1 ? 477 ? 1 477 
3 1 9JLR C 1 ? 477 ? O66934 1 ? 477 ? 1 477 
4 1 9JLR 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 9JLR GLN A 256 ? UNP O66934 GLU 256 'engineered mutation' 256 1  
1 9JLR LEU A 478 ? UNP O66934 ?   ?   'expression tag'      478 2  
1 9JLR GLU A 479 ? UNP O66934 ?   ?   'expression tag'      479 3  
1 9JLR HIS A 480 ? UNP O66934 ?   ?   'expression tag'      480 4  
1 9JLR HIS A 481 ? UNP O66934 ?   ?   'expression tag'      481 5  
1 9JLR HIS A 482 ? UNP O66934 ?   ?   'expression tag'      482 6  
1 9JLR HIS A 483 ? UNP O66934 ?   ?   'expression tag'      483 7  
1 9JLR HIS A 484 ? UNP O66934 ?   ?   'expression tag'      484 8  
1 9JLR HIS A 485 ? UNP O66934 ?   ?   'expression tag'      485 9  
2 9JLR GLN B 256 ? UNP O66934 GLU 256 'engineered mutation' 256 10 
2 9JLR LEU B 478 ? UNP O66934 ?   ?   'expression tag'      478 11 
2 9JLR GLU B 479 ? UNP O66934 ?   ?   'expression tag'      479 12 
2 9JLR HIS B 480 ? UNP O66934 ?   ?   'expression tag'      480 13 
2 9JLR HIS B 481 ? UNP O66934 ?   ?   'expression tag'      481 14 
2 9JLR HIS B 482 ? UNP O66934 ?   ?   'expression tag'      482 15 
2 9JLR HIS B 483 ? UNP O66934 ?   ?   'expression tag'      483 16 
2 9JLR HIS B 484 ? UNP O66934 ?   ?   'expression tag'      484 17 
2 9JLR HIS B 485 ? UNP O66934 ?   ?   'expression tag'      485 18 
3 9JLR GLN C 256 ? UNP O66934 GLU 256 'engineered mutation' 256 19 
3 9JLR LEU C 478 ? UNP O66934 ?   ?   'expression tag'      478 20 
3 9JLR GLU C 479 ? UNP O66934 ?   ?   'expression tag'      479 21 
3 9JLR HIS C 480 ? UNP O66934 ?   ?   'expression tag'      480 22 
3 9JLR HIS C 481 ? UNP O66934 ?   ?   'expression tag'      481 23 
3 9JLR HIS C 482 ? UNP O66934 ?   ?   'expression tag'      482 24 
3 9JLR HIS C 483 ? UNP O66934 ?   ?   'expression tag'      483 25 
3 9JLR HIS C 484 ? UNP O66934 ?   ?   'expression tag'      484 26 
3 9JLR HIS C 485 ? UNP O66934 ?   ?   'expression tag'      485 27 
4 9JLR GLN D 256 ? UNP O66934 GLU 256 'engineered mutation' 256 28 
4 9JLR LEU D 478 ? UNP O66934 ?   ?   'expression tag'      478 29 
4 9JLR GLU D 479 ? UNP O66934 ?   ?   'expression tag'      479 30 
4 9JLR HIS D 480 ? UNP O66934 ?   ?   'expression tag'      480 31 
4 9JLR HIS D 481 ? UNP O66934 ?   ?   'expression tag'      481 32 
4 9JLR HIS D 482 ? UNP O66934 ?   ?   'expression tag'      482 33 
4 9JLR HIS D 483 ? UNP O66934 ?   ?   'expression tag'      483 34 
4 9JLR HIS D 484 ? UNP O66934 ?   ?   'expression tag'      484 35 
4 9JLR HIS D 485 ? UNP O66934 ?   ?   'expression tag'      485 36 
# 
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 
2 1 B,F,J 
3 1 C,G,K 
4 1 D,H,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 PRO A 28  ? VAL A 35  ? PRO A 28  VAL A 35  1 ? 8  
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 ? LYS A 119 ? PHE A 110 LYS A 119 1 ? 10 
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 ? GLU A 186 ? THR A 158 GLU A 186 1 ? 29 
HELX_P HELX_P14  AB5 LEU A 200 ? ASN A 206 ? LEU A 200 ASN A 206 1 ? 7  
HELX_P HELX_P15  AB6 PRO A 207 ? THR A 213 ? PRO A 207 THR A 213 5 ? 7  
HELX_P HELX_P16  AB7 PHE A 226 ? GLY A 246 ? PHE A 226 GLY A 246 1 ? 21 
HELX_P HELX_P17  AB8 PRO A 254 ? SER A 258 ? PRO A 254 SER A 258 5 ? 5  
HELX_P HELX_P18  AB9 SER A 260 ? LYS A 270 ? SER A 260 LYS A 270 1 ? 11 
HELX_P HELX_P19  AC1 ASP A 278 ? VAL A 286 ? ASP A 278 VAL A 286 1 ? 9  
HELX_P HELX_P20  AC2 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P21  AC3 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P22  AC4 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P23  AC5 GLY A 364 ? GLU A 378 ? GLY A 364 GLU A 378 1 ? 15 
HELX_P HELX_P24  AC6 THR A 385 ? LYS A 392 ? THR A 385 LYS A 392 1 ? 8  
HELX_P HELX_P25  AC7 ASN A 419 ? LYS A 434 ? ASN A 419 LYS A 434 1 ? 16 
HELX_P HELX_P26  AC8 ASP A 439 ? GLU A 445 ? ASP A 439 GLU A 445 1 ? 7  
HELX_P HELX_P27  AC9 GLY A 446 ? TRP A 452 ? GLY A 446 TRP A 452 1 ? 7  
HELX_P HELX_P28  AD1 PHE A 460 ? GLN A 476 ? PHE A 460 GLN A 476 1 ? 17 
HELX_P HELX_P29  AD2 PRO B 28  ? ASP B 37  ? PRO B 28  ASP B 37  1 ? 10 
HELX_P HELX_P30  AD3 TYR B 39  ? TYR B 44  ? TYR B 39  TYR B 44  1 ? 6  
HELX_P HELX_P31  AD4 LEU B 45  ? ASP B 47  ? LEU B 45  ASP B 47  5 ? 3  
HELX_P HELX_P32  AD5 THR B 57  ? GLN B 69  ? THR B 57  GLN B 69  1 ? 13 
HELX_P HELX_P33  AD6 ASP B 74  ? LYS B 82  ? ASP B 74  LYS B 82  1 ? 9  
HELX_P HELX_P34  AD7 ASP B 83  ? LEU B 87  ? ASP B 83  LEU B 87  5 ? 5  
HELX_P HELX_P35  AD8 GLU B 88  ? TYR B 103 ? GLU B 88  TYR B 103 1 ? 16 
HELX_P HELX_P36  AD9 LYS B 105 ? ARG B 109 ? LYS B 105 ARG B 109 5 ? 5  
HELX_P HELX_P37  AE1 PHE B 110 ? LYS B 119 ? PHE B 110 LYS B 119 1 ? 10 
HELX_P HELX_P38  AE2 ASN B 123 ? TRP B 138 ? ASN B 123 TRP B 138 1 ? 16 
HELX_P HELX_P39  AE3 GLY B 140 ? LEU B 147 ? GLY B 140 LEU B 147 1 ? 8  
HELX_P HELX_P40  AE4 LEU B 147 ? GLY B 154 ? LEU B 147 GLY B 154 1 ? 8  
HELX_P HELX_P41  AE5 THR B 158 ? LYS B 174 ? THR B 158 LYS B 174 1 ? 17 
HELX_P HELX_P42  AE6 LYS B 175 ? GLU B 186 ? LYS B 175 GLU B 186 1 ? 12 
HELX_P HELX_P43  AE7 LEU B 200 ? ASN B 206 ? LEU B 200 ASN B 206 1 ? 7  
HELX_P HELX_P44  AE8 CYS B 209 ? THR B 214 ? CYS B 209 THR B 214 1 ? 6  
HELX_P HELX_P45  AE9 PHE B 226 ? GLY B 246 ? PHE B 226 GLY B 246 1 ? 21 
HELX_P HELX_P46  AF1 PRO B 254 ? SER B 258 ? PRO B 254 SER B 258 5 ? 5  
HELX_P HELX_P47  AF2 SER B 260 ? LYS B 270 ? SER B 260 LYS B 270 1 ? 11 
HELX_P HELX_P48  AF3 ASP B 278 ? VAL B 286 ? ASP B 278 VAL B 286 1 ? 9  
HELX_P HELX_P49  AF4 ASP B 307 ? PHE B 316 ? ASP B 307 PHE B 316 1 ? 10 
HELX_P HELX_P50  AF5 SER B 317 ? ALA B 320 ? SER B 317 ALA B 320 5 ? 4  
HELX_P HELX_P51  AF6 ASN B 322 ? VAL B 341 ? ASN B 322 VAL B 341 1 ? 20 
HELX_P HELX_P52  AF7 CYS B 356 ? ASN B 363 ? CYS B 356 ASN B 363 5 ? 8  
HELX_P HELX_P53  AF8 GLY B 364 ? LYS B 377 ? GLY B 364 LYS B 377 1 ? 14 
HELX_P HELX_P54  AF9 THR B 385 ? LYS B 392 ? THR B 385 LYS B 392 1 ? 8  
HELX_P HELX_P55  AG1 ASN B 419 ? LYS B 435 ? ASN B 419 LYS B 435 1 ? 17 
HELX_P HELX_P56  AG2 ASP B 439 ? ALA B 444 ? ASP B 439 ALA B 444 1 ? 6  
HELX_P HELX_P57  AG3 GLY B 446 ? TRP B 452 ? GLY B 446 TRP B 452 1 ? 7  
HELX_P HELX_P58  AG4 PHE B 460 ? GLN B 476 ? PHE B 460 GLN B 476 1 ? 17 
HELX_P HELX_P59  AG5 PRO C 28  ? ASP C 37  ? PRO C 28  ASP C 37  1 ? 10 
HELX_P HELX_P60  AG6 TYR C 39  ? PHE C 48  ? TYR C 39  PHE C 48  1 ? 10 
HELX_P HELX_P61  AG7 THR C 57  ? GLN C 69  ? THR C 57  GLN C 69  1 ? 13 
HELX_P HELX_P62  AG8 VAL C 75  ? LYS C 82  ? VAL C 75  LYS C 82  1 ? 8  
HELX_P HELX_P63  AG9 ASP C 83  ? LEU C 87  ? ASP C 83  LEU C 87  5 ? 5  
HELX_P HELX_P64  AH1 GLU C 88  ? ASN C 102 ? GLU C 88  ASN C 102 1 ? 15 
HELX_P HELX_P65  AH2 LYS C 105 ? ARG C 109 ? LYS C 105 ARG C 109 5 ? 5  
HELX_P HELX_P66  AH3 PHE C 110 ? LYS C 119 ? PHE C 110 LYS C 119 1 ? 10 
HELX_P HELX_P67  AH4 ASN C 123 ? ALA C 137 ? ASN C 123 ALA C 137 1 ? 15 
HELX_P HELX_P68  AH5 GLY C 140 ? LEU C 147 ? GLY C 140 LEU C 147 1 ? 8  
HELX_P HELX_P69  AH6 LEU C 147 ? GLY C 154 ? LEU C 147 GLY C 154 1 ? 8  
HELX_P HELX_P70  AH7 THR C 158 ? GLU C 186 ? THR C 158 GLU C 186 1 ? 29 
HELX_P HELX_P71  AH8 LEU C 200 ? ASN C 206 ? LEU C 200 ASN C 206 1 ? 7  
HELX_P HELX_P72  AH9 PRO C 207 ? THR C 213 ? PRO C 207 THR C 213 5 ? 7  
HELX_P HELX_P73  AI1 PHE C 226 ? GLY C 246 ? PHE C 226 GLY C 246 1 ? 21 
HELX_P HELX_P74  AI2 PRO C 254 ? SER C 258 ? PRO C 254 SER C 258 5 ? 5  
HELX_P HELX_P75  AI3 SER C 260 ? LYS C 270 ? SER C 260 LYS C 270 1 ? 11 
HELX_P HELX_P76  AI4 ASP C 278 ? VAL C 286 ? ASP C 278 VAL C 286 1 ? 9  
HELX_P HELX_P77  AI5 ASP C 307 ? PHE C 316 ? ASP C 307 PHE C 316 1 ? 10 
HELX_P HELX_P78  AI6 SER C 317 ? ALA C 320 ? SER C 317 ALA C 320 5 ? 4  
HELX_P HELX_P79  AI7 ASN C 322 ? VAL C 341 ? ASN C 322 VAL C 341 1 ? 20 
HELX_P HELX_P80  AI8 ASN C 355 ? ASN C 363 ? ASN C 355 ASN C 363 5 ? 9  
HELX_P HELX_P81  AI9 GLY C 364 ? GLU C 378 ? GLY C 364 GLU C 378 1 ? 15 
HELX_P HELX_P82  AJ1 THR C 385 ? LYS C 392 ? THR C 385 LYS C 392 1 ? 8  
HELX_P HELX_P83  AJ2 ASN C 419 ? LYS C 435 ? ASN C 419 LYS C 435 1 ? 17 
HELX_P HELX_P84  AJ3 ASP C 439 ? GLU C 445 ? ASP C 439 GLU C 445 1 ? 7  
HELX_P HELX_P85  AJ4 GLY C 446 ? GLN C 453 ? GLY C 446 GLN C 453 1 ? 8  
HELX_P HELX_P86  AJ5 PHE C 460 ? GLN C 476 ? PHE C 460 GLN C 476 1 ? 17 
HELX_P HELX_P87  AJ6 PRO D 28  ? ASP D 37  ? PRO D 28  ASP D 37  1 ? 10 
HELX_P HELX_P88  AJ7 TYR D 39  ? PHE D 48  ? TYR D 39  PHE D 48  1 ? 10 
HELX_P HELX_P89  AJ8 THR D 57  ? GLN D 69  ? THR D 57  GLN D 69  1 ? 13 
HELX_P HELX_P90  AJ9 ASP D 74  ? LYS D 82  ? ASP D 74  LYS D 82  1 ? 9  
HELX_P HELX_P91  AK1 ASP D 83  ? LEU D 87  ? ASP D 83  LEU D 87  5 ? 5  
HELX_P HELX_P92  AK2 GLU D 88  ? ASN D 102 ? GLU D 88  ASN D 102 1 ? 15 
HELX_P HELX_P93  AK3 LYS D 105 ? ARG D 109 ? LYS D 105 ARG D 109 5 ? 5  
HELX_P HELX_P94  AK4 PHE D 110 ? LYS D 119 ? PHE D 110 LYS D 119 1 ? 10 
HELX_P HELX_P95  AK5 ASN D 123 ? TRP D 138 ? ASN D 123 TRP D 138 1 ? 16 
HELX_P HELX_P96  AK6 ARG D 141 ? LYS D 145 ? ARG D 141 LYS D 145 5 ? 5  
HELX_P HELX_P97  AK7 LEU D 147 ? GLY D 154 ? LEU D 147 GLY D 154 1 ? 8  
HELX_P HELX_P98  AK8 THR D 158 ? GLU D 186 ? THR D 158 GLU D 186 1 ? 29 
HELX_P HELX_P99  AK9 LEU D 200 ? ASN D 206 ? LEU D 200 ASN D 206 1 ? 7  
HELX_P HELX_P100 AL1 PRO D 207 ? GLU D 212 ? PRO D 207 GLU D 212 5 ? 6  
HELX_P HELX_P101 AL2 PHE D 226 ? GLY D 246 ? PHE D 226 GLY D 246 1 ? 21 
HELX_P HELX_P102 AL3 PRO D 254 ? SER D 258 ? PRO D 254 SER D 258 5 ? 5  
HELX_P HELX_P103 AL4 SER D 260 ? LYS D 270 ? SER D 260 LYS D 270 1 ? 11 
HELX_P HELX_P104 AL5 ASP D 278 ? VAL D 286 ? ASP D 278 VAL D 286 1 ? 9  
HELX_P HELX_P105 AL6 ASP D 307 ? SER D 317 ? ASP D 307 SER D 317 1 ? 11 
HELX_P HELX_P106 AL7 TYR D 318 ? TRP D 321 ? TYR D 318 TRP D 321 5 ? 4  
HELX_P HELX_P107 AL8 ASN D 322 ? VAL D 341 ? ASN D 322 VAL D 341 1 ? 20 
HELX_P HELX_P108 AL9 TYR D 360 ? ASN D 363 ? TYR D 360 ASN D 363 5 ? 4  
HELX_P HELX_P109 AM1 GLY D 364 ? GLU D 378 ? GLY D 364 GLU D 378 1 ? 15 
HELX_P HELX_P110 AM2 THR D 385 ? LYS D 392 ? THR D 385 LYS D 392 1 ? 8  
HELX_P HELX_P111 AM3 ASN D 419 ? LYS D 435 ? ASN D 419 LYS D 435 1 ? 17 
HELX_P HELX_P112 AM4 ASP D 439 ? GLU D 445 ? ASP D 439 GLU D 445 1 ? 7  
HELX_P HELX_P113 AM5 GLY D 446 ? GLN D 453 ? GLY D 446 GLN D 453 1 ? 8  
HELX_P HELX_P114 AM6 PHE D 460 ? ALA D 475 ? PHE D 460 ALA D 475 1 ? 16 
# 
_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 ? ? ? ? ? ? ? 1.412 ? ? 
covale2  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 2 E GLC 3 1_555 ? ? ? ? ? ? ? 1.469 ? ? 
covale3  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 3 E GLC 4 1_555 ? ? ? ? ? ? ? 1.454 ? ? 
covale4  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 4 E GLC 5 1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale5  covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 1 F GLC 2 1_555 ? ? ? ? ? ? ? 1.409 ? ? 
covale6  covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 2 F GLC 3 1_555 ? ? ? ? ? ? ? 1.468 ? ? 
covale7  covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 3 F GLC 4 1_555 ? ? ? ? ? ? ? 1.455 ? ? 
covale8  covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 4 F GLC 5 1_555 ? ? ? ? ? ? ? 1.431 ? ? 
covale9  covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 1 G GLC 2 1_555 ? ? ? ? ? ? ? 1.403 ? ? 
covale10 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 2 G GLC 3 1_555 ? ? ? ? ? ? ? 1.469 ? ? 
covale11 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 3 G GLC 4 1_555 ? ? ? ? ? ? ? 1.450 ? ? 
covale12 covale both ? G GLC . O4 ? ? ? 1_555 G GLC . C1 ? ? G GLC 4 G GLC 5 1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale13 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 1 H GLC 2 1_555 ? ? ? ? ? ? ? 1.422 ? ? 
covale14 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 2 H GLC 3 1_555 ? ? ? ? ? ? ? 1.471 ? ? 
covale15 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 3 H GLC 4 1_555 ? ? ? ? ? ? ? 1.461 ? ? 
covale16 covale both ? H GLC . O4 ? ? ? 1_555 H GLC . C1 ? ? H GLC 4 H GLC 5 1_555 ? ? ? ? ? ? ? 1.441 ? ? 
# 
_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 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 2 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? 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      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AB1 1 2 ? parallel      
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? parallel      
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? 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 ? THR A 193 ? VAL A 191 THR A 193 
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 ? ASP A 352 ? VAL A 346 ASP A 352 
AA2 1 VAL A 191 ? THR A 193 ? VAL A 191 THR A 193 
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 MET A 274 ? THR A 277 ? MET A 274 THR A 277 
AA4 2 ILE A 301 ? PHE A 305 ? ILE A 301 PHE A 305 
AA4 3 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 4 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 ? ASP B 352 ? VAL B 346 ASP 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 MET B 274 ? THR B 277 ? MET B 274 THR B 277 
AA7 2 ILE B 301 ? PHE B 305 ? ILE B 301 PHE B 305 
AA7 3 ARG B 294 ? PHE B 297 ? ARG B 294 PHE B 297 
AA7 4 THR B 397 ? ILE B 400 ? THR B 397 ILE B 400 
AA8 1 VAL C 191 ? SER C 192 ? VAL C 191 SER C 192 
AA8 2 ASN C 53  ? LEU C 56  ? ASN C 53  LEU C 56  
AA8 3 LEU C 4   ? MET C 12  ? LEU C 4   MET C 12  
AA8 4 VAL C 346 ? ASP C 352 ? VAL C 346 ASP C 352 
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 ILE C 381 ? THR C 383 ? ILE C 381 THR C 383 
AB1 1 GLU C 24  ? TYR C 25  ? GLU C 24  TYR C 25  
AB1 2 LYS C 73  ? ASP C 74  ? LYS C 73  ASP C 74  
AB2 1 MET C 274 ? THR C 277 ? MET C 274 THR C 277 
AB2 2 ILE C 301 ? PHE C 305 ? ILE C 301 PHE C 305 
AB2 3 ARG C 294 ? PHE C 297 ? ARG C 294 PHE C 297 
AB2 4 THR C 397 ? ILE C 400 ? THR C 397 ILE C 400 
AB3 1 VAL D 191 ? SER D 192 ? VAL D 191 SER D 192 
AB3 2 ASN D 53  ? LEU D 56  ? ASN D 53  LEU D 56  
AB3 3 LEU D 4   ? MET D 12  ? LEU D 4   MET D 12  
AB3 4 VAL D 346 ? ASP D 352 ? VAL D 346 ASP D 352 
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 ILE D 381 ? THR D 383 ? ILE D 381 THR D 383 
AB5 1 MET D 274 ? THR D 277 ? MET D 274 THR D 277 
AB5 2 ILE D 301 ? PHE D 305 ? ILE D 301 PHE D 305 
AB5 3 ARG D 294 ? PHE D 297 ? ARG D 294 PHE D 297 
AB5 4 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 55  ? O ASN A 55  N TRP A 10  ? N TRP A 10  
AA1 3 4 N PHE A 5   ? N PHE A 5   O VAL A 347 ? O VAL A 347 
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 55  ? O ASN A 55  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 THR A 277 ? N THR A 277 O PHE A 304 ? O PHE A 304 
AA4 2 3 O ILE A 301 ? O ILE A 301 N PHE A 297 ? N PHE A 297 
AA4 3 4 N TYR A 296 ? N TYR A 296 O GLU A 398 ? O GLU A 398 
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 55  ? O ASN B 55  N MET B 12  ? N MET B 12  
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 55  ? O ASN B 55  N MET B 12  ? N MET B 12  
AA6 3 4 N LEU B 4   ? N LEU B 4   O GLU B 382 ? O GLU B 382 
AA7 1 2 N THR B 277 ? N THR B 277 O PHE B 304 ? O PHE B 304 
AA7 2 3 O VAL B 303 ? O VAL B 303 N TYR B 295 ? N TYR B 295 
AA7 3 4 N ARG B 294 ? N ARG B 294 O GLU B 398 ? O GLU B 398 
AA8 1 2 O SER C 192 ? O SER C 192 N PHE C 54  ? N PHE C 54  
AA8 2 3 O ASN C 55  ? O ASN C 55  N MET C 12  ? N MET C 12  
AA8 3 4 N PHE C 5   ? N PHE C 5   O VAL C 347 ? O VAL C 347 
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 LEU C 4   ? N LEU C 4   O GLU C 382 ? O GLU C 382 
AB1 1 2 N TYR C 25  ? N TYR C 25  O LYS C 73  ? O LYS C 73  
AB2 1 2 N LEU C 275 ? N LEU C 275 O PHE C 304 ? O PHE C 304 
AB2 2 3 O ILE C 301 ? O ILE C 301 N PHE C 297 ? N PHE C 297 
AB2 3 4 N TYR C 296 ? N TYR C 296 O ILE C 400 ? O ILE C 400 
AB3 1 2 O SER D 192 ? O SER D 192 N LEU D 56  ? N LEU D 56  
AB3 2 3 O ASN D 55  ? O ASN D 55  N TRP D 10  ? N TRP D 10  
AB3 3 4 N VAL D 7   ? N VAL D 7   O VAL D 347 ? O VAL D 347 
AB4 1 2 O SER D 192 ? O SER D 192 N LEU D 56  ? N LEU D 56  
AB4 2 3 O ASN D 55  ? O ASN D 55  N TRP D 10  ? N TRP D 10  
AB4 3 4 N LEU D 6   ? N LEU D 6   O GLU D 382 ? O GLU D 382 
AB5 1 2 N LEU D 275 ? N LEU D 275 O PHE D 304 ? O PHE D 304 
AB5 2 3 O VAL D 303 ? O VAL D 303 N TYR D 295 ? N TYR D 295 
AB5 3 4 N TYR D 296 ? N TYR D 296 O GLU D 398 ? O GLU D 398 
# 
_pdbx_entry_details.entry_id                   9JLR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 OG1 A THR 383 ? ? O  A HOH 501 ? ? 1.97 
2  1 OG1 B THR 214 ? ? O  B HOH 501 ? ? 2.01 
3  1 O   B VAL 403 ? ? O  B HOH 502 ? ? 2.02 
4  1 OE1 B GLU 401 ? ? O  B HOH 503 ? ? 2.09 
5  1 OH  A TYR 372 ? ? O  A HOH 502 ? ? 2.10 
6  1 O   D SER 340 ? ? O  D HOH 501 ? ? 2.15 
7  1 OE1 A GLU 49  ? ? O  A HOH 503 ? ? 2.17 
8  1 OD1 A ASP 85  ? ? O  A HOH 504 ? ? 2.17 
9  1 O   C LEU 150 ? ? OH C TYR 157 ? ? 2.17 
10 1 ND2 B ASN 438 ? ? O  B ARG 474 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE2 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    GLU 
_pdbx_validate_symm_contact.auth_seq_id_1     393 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    ND1 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HIS 
_pdbx_validate_symm_contact.auth_seq_id_2     480 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_656 
_pdbx_validate_symm_contact.dist              2.16 
# 
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 ASP A 37  ? ? -132.14 -34.14  
2  1 TRP A 138 ? ? -97.22  34.57   
3  1 LEU A 147 ? ? -89.79  32.04   
4  1 ALA A 257 ? ? 57.78   19.89   
5  1 GLU A 287 ? ? -52.18  -78.24  
6  1 GLU A 299 ? ? 68.77   -8.10   
7  1 LYS B 73  ? ? -117.06 74.34   
8  1 LEU B 147 ? ? -101.21 41.73   
9  1 ALA B 257 ? ? 56.16   15.69   
10 1 GLU B 287 ? ? -52.85  -84.05  
11 1 GLU B 455 ? ? -67.05  -95.60  
12 1 ASP C 37  ? ? -132.42 -32.57  
13 1 GLU C 49  ? ? -104.41 72.43   
14 1 LYS C 73  ? ? -101.64 74.67   
15 1 GLU C 287 ? ? -47.98  -88.20  
16 1 GLU C 299 ? ? 65.60   -1.97   
17 1 LYS C 457 ? ? -38.43  111.86  
18 1 GLN C 476 ? ? -94.19  33.29   
19 1 HIS C 481 ? ? 70.50   123.39  
20 1 TYR D 108 ? ? -96.29  39.62   
21 1 ARG D 109 ? ? -105.34 78.22   
22 1 TYR D 197 ? ? -105.07 40.84   
23 1 ALA D 257 ? ? 59.91   16.00   
24 1 GLU D 287 ? ? -54.98  -88.39  
25 1 TYR D 292 ? ? -90.25  41.78   
26 1 ASN D 363 ? ? 35.85   30.11   
27 1 GLU D 455 ? ? -73.28  -135.04 
28 1 GLU D 456 ? ? -113.68 55.80   
# 
_pdbx_molecule_features.prd_id    PRD_900030 
_pdbx_molecule_features.name      alpha-maltopentaose 
_pdbx_molecule_features.type      Oligosaccharide 
_pdbx_molecule_features.class     'Substrate analog' 
_pdbx_molecule_features.details   oligosaccharide 
# 
loop_
_pdbx_molecule.instance_id 
_pdbx_molecule.prd_id 
_pdbx_molecule.asym_id 
1 PRD_900030 E 
2 PRD_900030 F 
3 PRD_900030 G 
4 PRD_900030 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 26.9449  0.5980   13.9122  0.4272 ? -0.0100 ? -0.0021 ? 0.4166 ? -0.0155 ? 0.4367 ? 2.6204 ? 
0.2513  ? 0.2940  ? 0.7516 ? 0.0004  ? 1.4244 ? -0.0507 ? -0.0617 ? 0.0238  ? 0.0818  ? 0.0626  ? -0.1803 ? 0.0908  ? 0.2771  ? 
0.0208  ? 
2  'X-RAY DIFFRACTION' ? refined 2.0700   -3.4250  0.1415   0.4486 ? -0.0419 ? 0.0404  ? 0.4330 ? 0.0071  ? 0.4795 ? 1.2723 ? 
0.4654  ? -0.0014 ? 1.2450 ? 0.4415  ? 2.0185 ? -0.0395 ? 0.2237  ? -0.1440 ? -0.2162 ? 0.1013  ? 0.0524  ? 0.0945  ? -0.1644 ? 
-0.0159 ? 
3  'X-RAY DIFFRACTION' ? refined 1.9820   8.1833   17.8993  0.4286 ? 0.0179  ? 0.0305  ? 0.4248 ? -0.0305 ? 0.4573 ? 4.1441 ? 
1.0730  ? 0.1854  ? 1.8857 ? -0.6696 ? 1.9527 ? -0.0395 ? -0.2351 ? 0.1901  ? -0.0185 ? -0.1658 ? -0.1586 ? -0.1509 ? -0.1515 ? 
0.2124  ? 
4  'X-RAY DIFFRACTION' ? refined 7.9050   -0.1223  -11.0222 0.5098 ? -0.0870 ? 0.0042  ? 0.4815 ? -0.0041 ? 0.5124 ? 2.2555 ? 
-1.4788 ? -0.4828 ? 2.5690 ? 0.9239  ? 2.3825 ? -0.0644 ? 0.4231  ? 0.2869  ? -0.5935 ? 0.1608  ? -0.3208 ? -0.4026 ? 0.0534  ? 
-0.0104 ? 
5  'X-RAY DIFFRACTION' ? refined 21.9859  -4.7670  -8.5039  0.4416 ? -0.0345 ? 0.0849  ? 0.5976 ? -0.0030 ? 0.5320 ? 7.3668 ? 
0.5379  ? 0.3629  ? 2.0393 ? 0.9058  ? 8.1431 ? -0.1385 ? 0.1619  ? 0.7298  ? -0.2097 ? 0.1084  ? -0.1261 ? -0.3552 ? -0.0689 ? 
0.0419  ? 
6  'X-RAY DIFFRACTION' ? refined -18.5832 43.0749  26.7779  0.3587 ? 0.0120  ? 0.0144  ? 0.4262 ? 0.0290  ? 0.4996 ? 4.4635 ? 
0.5930  ? -0.7103 ? 1.0029 ? 0.0062  ? 0.4130 ? -0.1861 ? -0.5123 ? 0.2594  ? 0.0673  ? 0.2212  ? 0.2148  ? -0.2394 ? -0.2829 ? 
-0.0562 ? 
7  'X-RAY DIFFRACTION' ? refined -34.5098 27.3173  27.5128  0.5500 ? 0.0118  ? 0.0043  ? 0.5951 ? 0.0718  ? 0.8480 ? 5.5827 ? 
0.3103  ? -0.1524 ? 1.0090 ? 0.4559  ? 0.8857 ? 0.1525  ? -0.4097 ? -1.3612 ? -0.1453 ? 0.0610  ? 0.2703  ? 0.1783  ? 0.0248  ? 
0.0061  ? 
8  'X-RAY DIFFRACTION' ? refined -24.3118 42.0626  34.1948  0.4785 ? 0.0152  ? 0.0049  ? 0.6166 ? -0.0199 ? 0.4975 ? 4.0026 ? 
0.5405  ? -0.0026 ? 0.7793 ? 0.1522  ? 0.6747 ? 0.0941  ? -0.7753 ? 0.1957  ? 0.1966  ? -0.0875 ? 0.1890  ? -0.1019 ? -0.1425 ? 
-0.0418 ? 
9  'X-RAY DIFFRACTION' ? refined 0.5078   37.6328  19.6247  0.3767 ? -0.0194 ? 0.0057  ? 0.3679 ? 0.0248  ? 0.4829 ? 2.6124 ? 
0.1847  ? 0.4360  ? 1.5840 ? 0.1784  ? 1.7416 ? 0.0200  ? -0.0252 ? -0.1348 ? -0.0689 ? 0.0898  ? 0.0260  ? -0.1108 ? 0.1070  ? 
-0.0305 ? 
10 'X-RAY DIFFRACTION' ? refined -2.4559  36.0886  21.6541  0.4869 ? -0.0059 ? 0.0151  ? 0.3187 ? -0.0107 ? 0.4592 ? 3.2675 ? 
-0.2591 ? -0.1222 ? 0.8138 ? -0.4558 ? 2.4206 ? -0.1287 ? -0.1658 ? -0.1586 ? -0.0827 ? -0.0587 ? 0.1223  ? 0.3248  ? 0.0360  ? 
0.0203  ? 
11 'X-RAY DIFFRACTION' ? refined -20.0079 40.9201  6.8785   0.5139 ? -0.0467 ? -0.0121 ? 0.6124 ? -0.0297 ? 0.3880 ? 6.4639 ? 
-1.3314 ? 0.3056  ? 3.7121 ? 0.0629  ? 6.4218 ? -0.2767 ? 0.0679  ? -0.2093 ? 0.0874  ? 0.2612  ? 0.4162  ? 0.1046  ? -0.4937 ? 
0.0128  ? 
12 'X-RAY DIFFRACTION' ? refined 3.6854   -9.7166  48.6283  0.6011 ? -0.0558 ? -0.0750 ? 0.8087 ? 0.0888  ? 0.5220 ? 2.6046 ? 
0.6120  ? 0.6696  ? 1.8251 ? -0.2516 ? 1.6849 ? -0.0403 ? 0.3205  ? -0.0466 ? -0.1537 ? 0.2233  ? 0.3187  ? 0.1677  ? -0.6553 ? 
-0.1210 ? 
13 'X-RAY DIFFRACTION' ? refined 24.8618  -0.1479  59.8987  0.5197 ? -0.0407 ? -0.0163 ? 0.4634 ? -0.0180 ? 0.4892 ? 2.0010 ? 
0.0457  ? 0.1280  ? 1.1923 ? -0.6766 ? 2.7519 ? 0.0389  ? 0.1375  ? 0.2017  ? -0.0142 ? 0.0393  ? -0.0854 ? -0.3786 ? 0.1164  ? 
-0.1274 ? 
14 'X-RAY DIFFRACTION' ? refined 11.7823  -18.8057 69.5056  0.5360 ? -0.0445 ? -0.0100 ? 0.6929 ? 0.0306  ? 0.4040 ? 2.8367 ? 
1.7130  ? 1.6969  ? 5.6380 ? -2.4279 ? 3.4815 ? -0.3187 ? -0.2156 ? 0.1227  ? -0.4446 ? 0.3230  ? -0.0303 ? -0.5310 ? -0.2594 ? 
0.0758  ? 
15 'X-RAY DIFFRACTION' ? refined 4.0941   46.8866  65.0183  0.6777 ? 0.0226  ? 0.0734  ? 0.6561 ? 0.0510  ? 0.4932 ? 3.2520 ? 
1.3304  ? -0.7708 ? 2.0048 ? 0.2738  ? 1.4612 ? -0.1795 ? 0.1235  ? 0.0575  ? -0.4153 ? 0.1890  ? -0.2219 ? 0.1586  ? 0.2542  ? 
-0.0575 ? 
16 'X-RAY DIFFRACTION' ? refined -16.8488 45.7471  73.3231  0.5679 ? -0.0014 ? 0.0014  ? 0.5517 ? 0.0312  ? 0.4785 ? 2.1786 ? 
0.1736  ? -0.3429 ? 1.0709 ? -0.1279 ? 1.3285 ? -0.2289 ? 0.3829  ? -0.0252 ? -0.2252 ? -0.0337 ? 0.0379  ? 0.0509  ? -0.2266 ? 
0.0986  ? 
17 'X-RAY DIFFRACTION' ? refined -13.4672 25.5524  69.2586  0.7918 ? -0.0464 ? 0.1044  ? 0.5958 ? -0.0031 ? 0.6219 ? 2.4962 ? 
-0.0342 ? -0.8045 ? 1.7687 ? 0.1719  ? 2.6677 ? -0.1132 ? 0.3416  ? -0.4321 ? -0.3144 ? -0.0029 ? -0.1957 ? 0.4762  ? -0.1734 ? 
0.1423  ? 
18 'X-RAY DIFFRACTION' ? refined -17.0953 34.4960  86.0272  0.6452 ? 0.0210  ? 0.0317  ? 0.5775 ? 0.0555  ? 0.3791 ? 2.6198 ? 
0.7970  ? 0.8826  ? 3.9534 ? -0.0305 ? 2.7300 ? 0.2260  ? -0.1503 ? -0.3161 ? 0.3106  ? 0.0914  ? 0.0427  ? 0.4631  ? -0.1229 ? 
-0.1373 ? 
19 'X-RAY DIFFRACTION' ? refined -12.4344 55.8659  89.5295  0.5752 ? 0.0238  ? -0.0044 ? 0.5209 ? -0.0402 ? 0.3905 ? 1.9988 ? 
-0.0682 ? 0.0250  ? 5.5053 ? -1.0581 ? 2.9273 ? -0.0303 ? -0.2230 ? 0.0249  ? 0.6568  ? 0.0248  ? -0.3924 ? -0.3311 ? 0.0783  ? 
0.0031  ? 
20 'X-RAY DIFFRACTION' ? refined -6.1722  58.4614  84.5471  0.4542 ? -0.0478 ? 0.1050  ? 0.6089 ? 0.0394  ? 0.6355 ? 2.4320 ? 
1.1578  ? -0.9291 ? 4.7793 ? 1.9378  ? 3.6159 ? 0.0395  ? -0.2848 ? 0.2626  ? -0.1723 ? 0.1688  ? -0.7857 ? 0.2745  ? 0.4219  ? 
-0.2543 ? 
# 
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 1 through 185 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 186 through 322 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 323 through 396 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 435 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 436 through 477 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1 through 88 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 89 through 123 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 124 through 200 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 201 through 360 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 361 through 434 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 435 through 477 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 1 through 185 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 186 through 444 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 445 through 484 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 1 through 158 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 159 through 278 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 279 through 396 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 397 through 419 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 420 through 444 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 445 through 485 )
;
# 
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 LEU 478 ? A LEU 478 
2  1 Y 1 A GLU 479 ? A GLU 479 
3  1 Y 1 A HIS 480 ? A HIS 480 
4  1 Y 1 A HIS 481 ? A HIS 481 
5  1 Y 1 A HIS 482 ? A HIS 482 
6  1 Y 1 A HIS 483 ? A HIS 483 
7  1 Y 1 A HIS 484 ? A HIS 484 
8  1 Y 1 A HIS 485 ? A HIS 485 
9  1 Y 1 B LEU 478 ? B LEU 478 
10 1 Y 1 B GLU 479 ? B GLU 479 
11 1 Y 1 B HIS 480 ? B HIS 480 
12 1 Y 1 B HIS 481 ? B HIS 481 
13 1 Y 1 B HIS 482 ? B HIS 482 
14 1 Y 1 B HIS 483 ? B HIS 483 
15 1 Y 1 B HIS 484 ? B HIS 484 
16 1 Y 1 B HIS 485 ? B HIS 485 
17 1 Y 1 C HIS 485 ? C HIS 485 
# 
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  
GLC C1   C N S 88  
GLC C2   C N R 89  
GLC C3   C N S 90  
GLC C4   C N S 91  
GLC C5   C N R 92  
GLC C6   C N N 93  
GLC O1   O N N 94  
GLC O2   O N N 95  
GLC O3   O N N 96  
GLC O4   O N N 97  
GLC O5   O N N 98  
GLC O6   O N N 99  
GLC H1   H N N 100 
GLC H2   H N N 101 
GLC H3   H N N 102 
GLC H4   H N N 103 
GLC H5   H N N 104 
GLC H61  H N N 105 
GLC H62  H N N 106 
GLC HO1  H N N 107 
GLC HO2  H N N 108 
GLC HO3  H N N 109 
GLC HO4  H N N 110 
GLC HO6  H N N 111 
GLN N    N N N 112 
GLN CA   C N S 113 
GLN C    C N N 114 
GLN O    O N N 115 
GLN CB   C N N 116 
GLN CG   C N N 117 
GLN CD   C N N 118 
GLN OE1  O N N 119 
GLN NE2  N N N 120 
GLN OXT  O N N 121 
GLN H    H N N 122 
GLN H2   H N N 123 
GLN HA   H N N 124 
GLN HB2  H N N 125 
GLN HB3  H N N 126 
GLN HG2  H N N 127 
GLN HG3  H N N 128 
GLN HE21 H N N 129 
GLN HE22 H N N 130 
GLN HXT  H N N 131 
GLU N    N N N 132 
GLU CA   C N S 133 
GLU C    C N N 134 
GLU O    O N N 135 
GLU CB   C N N 136 
GLU CG   C N N 137 
GLU CD   C N N 138 
GLU OE1  O N N 139 
GLU OE2  O N N 140 
GLU OXT  O N N 141 
GLU H    H N N 142 
GLU H2   H N N 143 
GLU HA   H N N 144 
GLU HB2  H N N 145 
GLU HB3  H N N 146 
GLU HG2  H N N 147 
GLU HG3  H N N 148 
GLU HE2  H N N 149 
GLU HXT  H N N 150 
GLY N    N N N 151 
GLY CA   C N N 152 
GLY C    C N N 153 
GLY O    O N N 154 
GLY OXT  O N N 155 
GLY H    H N N 156 
GLY H2   H N N 157 
GLY HA2  H N N 158 
GLY HA3  H N N 159 
GLY HXT  H N N 160 
HIS N    N N N 161 
HIS CA   C N S 162 
HIS C    C N N 163 
HIS O    O N N 164 
HIS CB   C N N 165 
HIS CG   C Y N 166 
HIS ND1  N Y N 167 
HIS CD2  C Y N 168 
HIS CE1  C Y N 169 
HIS NE2  N Y N 170 
HIS OXT  O N N 171 
HIS H    H N N 172 
HIS H2   H N N 173 
HIS HA   H N N 174 
HIS HB2  H N N 175 
HIS HB3  H N N 176 
HIS HD1  H N N 177 
HIS HD2  H N N 178 
HIS HE1  H N N 179 
HIS HE2  H N N 180 
HIS HXT  H N N 181 
HOH O    O N N 182 
HOH H1   H N N 183 
HOH H2   H N N 184 
ILE N    N N N 185 
ILE CA   C N S 186 
ILE C    C N N 187 
ILE O    O N N 188 
ILE CB   C N S 189 
ILE CG1  C N N 190 
ILE CG2  C N N 191 
ILE CD1  C N N 192 
ILE OXT  O N N 193 
ILE H    H N N 194 
ILE H2   H N N 195 
ILE HA   H N N 196 
ILE HB   H N N 197 
ILE HG12 H N N 198 
ILE HG13 H N N 199 
ILE HG21 H N N 200 
ILE HG22 H N N 201 
ILE HG23 H N N 202 
ILE HD11 H N N 203 
ILE HD12 H N N 204 
ILE HD13 H N N 205 
ILE HXT  H N N 206 
LEU N    N N N 207 
LEU CA   C N S 208 
LEU C    C N N 209 
LEU O    O N N 210 
LEU CB   C N N 211 
LEU CG   C N N 212 
LEU CD1  C N N 213 
LEU CD2  C N N 214 
LEU OXT  O N N 215 
LEU H    H N N 216 
LEU H2   H N N 217 
LEU HA   H N N 218 
LEU HB2  H N N 219 
LEU HB3  H N N 220 
LEU HG   H N N 221 
LEU HD11 H N N 222 
LEU HD12 H N N 223 
LEU HD13 H N N 224 
LEU HD21 H N N 225 
LEU HD22 H N N 226 
LEU HD23 H N N 227 
LEU HXT  H N N 228 
LYS N    N N N 229 
LYS CA   C N S 230 
LYS C    C N N 231 
LYS O    O N N 232 
LYS CB   C N N 233 
LYS CG   C N N 234 
LYS CD   C N N 235 
LYS CE   C N N 236 
LYS NZ   N N N 237 
LYS OXT  O N N 238 
LYS H    H N N 239 
LYS H2   H N N 240 
LYS HA   H N N 241 
LYS HB2  H N N 242 
LYS HB3  H N N 243 
LYS HG2  H N N 244 
LYS HG3  H N N 245 
LYS HD2  H N N 246 
LYS HD3  H N N 247 
LYS HE2  H N N 248 
LYS HE3  H N N 249 
LYS HZ1  H N N 250 
LYS HZ2  H N N 251 
LYS HZ3  H N N 252 
LYS HXT  H N N 253 
MET N    N N N 254 
MET CA   C N S 255 
MET C    C N N 256 
MET O    O N N 257 
MET CB   C N N 258 
MET CG   C N N 259 
MET SD   S N N 260 
MET CE   C N N 261 
MET OXT  O N N 262 
MET H    H N N 263 
MET H2   H N N 264 
MET HA   H N N 265 
MET HB2  H N N 266 
MET HB3  H N N 267 
MET HG2  H N N 268 
MET HG3  H N N 269 
MET HE1  H N N 270 
MET HE2  H N N 271 
MET HE3  H N N 272 
MET HXT  H N N 273 
PHE N    N N N 274 
PHE CA   C N S 275 
PHE C    C N N 276 
PHE O    O N N 277 
PHE CB   C N N 278 
PHE CG   C Y N 279 
PHE CD1  C Y N 280 
PHE CD2  C Y N 281 
PHE CE1  C Y N 282 
PHE CE2  C Y N 283 
PHE CZ   C Y N 284 
PHE OXT  O N N 285 
PHE H    H N N 286 
PHE H2   H N N 287 
PHE HA   H N N 288 
PHE HB2  H N N 289 
PHE HB3  H N N 290 
PHE HD1  H N N 291 
PHE HD2  H N N 292 
PHE HE1  H N N 293 
PHE HE2  H N N 294 
PHE HZ   H N N 295 
PHE HXT  H N N 296 
PRO N    N N N 297 
PRO CA   C N S 298 
PRO C    C N N 299 
PRO O    O N N 300 
PRO CB   C N N 301 
PRO CG   C N N 302 
PRO CD   C N N 303 
PRO OXT  O N N 304 
PRO H    H N N 305 
PRO HA   H N N 306 
PRO HB2  H N N 307 
PRO HB3  H N N 308 
PRO HG2  H N N 309 
PRO HG3  H N N 310 
PRO HD2  H N N 311 
PRO HD3  H N N 312 
PRO HXT  H N N 313 
SER N    N N N 314 
SER CA   C N S 315 
SER C    C N N 316 
SER O    O N N 317 
SER CB   C N N 318 
SER OG   O N N 319 
SER OXT  O N N 320 
SER H    H N N 321 
SER H2   H N N 322 
SER HA   H N N 323 
SER HB2  H N N 324 
SER HB3  H N N 325 
SER HG   H N N 326 
SER HXT  H N N 327 
THR N    N N N 328 
THR CA   C N S 329 
THR C    C N N 330 
THR O    O N N 331 
THR CB   C N R 332 
THR OG1  O N N 333 
THR CG2  C N N 334 
THR OXT  O N N 335 
THR H    H N N 336 
THR H2   H N N 337 
THR HA   H N N 338 
THR HB   H N N 339 
THR HG1  H N N 340 
THR HG21 H N N 341 
THR HG22 H N N 342 
THR HG23 H N N 343 
THR HXT  H N N 344 
TRP N    N N N 345 
TRP CA   C N S 346 
TRP C    C N N 347 
TRP O    O N N 348 
TRP CB   C N N 349 
TRP CG   C Y N 350 
TRP CD1  C Y N 351 
TRP CD2  C Y N 352 
TRP NE1  N Y N 353 
TRP CE2  C Y N 354 
TRP CE3  C Y N 355 
TRP CZ2  C Y N 356 
TRP CZ3  C Y N 357 
TRP CH2  C Y N 358 
TRP OXT  O N N 359 
TRP H    H N N 360 
TRP H2   H N N 361 
TRP HA   H N N 362 
TRP HB2  H N N 363 
TRP HB3  H N N 364 
TRP HD1  H N N 365 
TRP HE1  H N N 366 
TRP HE3  H N N 367 
TRP HZ2  H N N 368 
TRP HZ3  H N N 369 
TRP HH2  H N N 370 
TRP HXT  H N N 371 
TYR N    N N N 372 
TYR CA   C N S 373 
TYR C    C N N 374 
TYR O    O N N 375 
TYR CB   C N N 376 
TYR CG   C Y N 377 
TYR CD1  C Y N 378 
TYR CD2  C Y N 379 
TYR CE1  C Y N 380 
TYR CE2  C Y N 381 
TYR CZ   C Y N 382 
TYR OH   O N N 383 
TYR OXT  O N N 384 
TYR H    H N N 385 
TYR H2   H N N 386 
TYR HA   H N N 387 
TYR HB2  H N N 388 
TYR HB3  H N N 389 
TYR HD1  H N N 390 
TYR HD2  H N N 391 
TYR HE1  H N N 392 
TYR HE2  H N N 393 
TYR HH   H N N 394 
TYR HXT  H N N 395 
VAL N    N N N 396 
VAL CA   C N S 397 
VAL C    C N N 398 
VAL O    O N N 399 
VAL CB   C N N 400 
VAL CG1  C N N 401 
VAL CG2  C N N 402 
VAL OXT  O N N 403 
VAL H    H N N 404 
VAL H2   H N N 405 
VAL HA   H N N 406 
VAL HB   H N N 407 
VAL HG11 H N N 408 
VAL HG12 H N N 409 
VAL HG13 H N N 410 
VAL HG21 H N N 411 
VAL HG22 H N N 412 
VAL HG23 H N N 413 
VAL HXT  H N N 414 
# 
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  
GLC C1  C2   sing N N 83  
GLC C1  O1   sing N N 84  
GLC C1  O5   sing N N 85  
GLC C1  H1   sing N N 86  
GLC C2  C3   sing N N 87  
GLC C2  O2   sing N N 88  
GLC C2  H2   sing N N 89  
GLC C3  C4   sing N N 90  
GLC C3  O3   sing N N 91  
GLC C3  H3   sing N N 92  
GLC C4  C5   sing N N 93  
GLC C4  O4   sing N N 94  
GLC C4  H4   sing N N 95  
GLC C5  C6   sing N N 96  
GLC C5  O5   sing N N 97  
GLC C5  H5   sing N N 98  
GLC C6  O6   sing N N 99  
GLC C6  H61  sing N N 100 
GLC C6  H62  sing N N 101 
GLC O1  HO1  sing N N 102 
GLC O2  HO2  sing N N 103 
GLC O3  HO3  sing N N 104 
GLC O4  HO4  sing N N 105 
GLC O6  HO6  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
HOH O   H1   sing N N 174 
HOH O   H2   sing N N 175 
ILE N   CA   sing N N 176 
ILE N   H    sing N N 177 
ILE N   H2   sing N N 178 
ILE CA  C    sing N N 179 
ILE CA  CB   sing N N 180 
ILE CA  HA   sing N N 181 
ILE C   O    doub N N 182 
ILE C   OXT  sing N N 183 
ILE CB  CG1  sing N N 184 
ILE CB  CG2  sing N N 185 
ILE CB  HB   sing N N 186 
ILE CG1 CD1  sing N N 187 
ILE CG1 HG12 sing N N 188 
ILE CG1 HG13 sing N N 189 
ILE CG2 HG21 sing N N 190 
ILE CG2 HG22 sing N N 191 
ILE CG2 HG23 sing N N 192 
ILE CD1 HD11 sing N N 193 
ILE CD1 HD12 sing N N 194 
ILE CD1 HD13 sing N N 195 
ILE OXT HXT  sing N N 196 
LEU N   CA   sing N N 197 
LEU N   H    sing N N 198 
LEU N   H2   sing N N 199 
LEU CA  C    sing N N 200 
LEU CA  CB   sing N N 201 
LEU CA  HA   sing N N 202 
LEU C   O    doub N N 203 
LEU C   OXT  sing N N 204 
LEU CB  CG   sing N N 205 
LEU CB  HB2  sing N N 206 
LEU CB  HB3  sing N N 207 
LEU CG  CD1  sing N N 208 
LEU CG  CD2  sing N N 209 
LEU CG  HG   sing N N 210 
LEU CD1 HD11 sing N N 211 
LEU CD1 HD12 sing N N 212 
LEU CD1 HD13 sing N N 213 
LEU CD2 HD21 sing N N 214 
LEU CD2 HD22 sing N N 215 
LEU CD2 HD23 sing N N 216 
LEU OXT HXT  sing N N 217 
LYS N   CA   sing N N 218 
LYS N   H    sing N N 219 
LYS N   H2   sing N N 220 
LYS CA  C    sing N N 221 
LYS CA  CB   sing N N 222 
LYS CA  HA   sing N N 223 
LYS C   O    doub N N 224 
LYS C   OXT  sing N N 225 
LYS CB  CG   sing N N 226 
LYS CB  HB2  sing N N 227 
LYS CB  HB3  sing N N 228 
LYS CG  CD   sing N N 229 
LYS CG  HG2  sing N N 230 
LYS CG  HG3  sing N N 231 
LYS CD  CE   sing N N 232 
LYS CD  HD2  sing N N 233 
LYS CD  HD3  sing N N 234 
LYS CE  NZ   sing N N 235 
LYS CE  HE2  sing N N 236 
LYS CE  HE3  sing N N 237 
LYS NZ  HZ1  sing N N 238 
LYS NZ  HZ2  sing N N 239 
LYS NZ  HZ3  sing N N 240 
LYS OXT HXT  sing N N 241 
MET N   CA   sing N N 242 
MET N   H    sing N N 243 
MET N   H2   sing N N 244 
MET CA  C    sing N N 245 
MET CA  CB   sing N N 246 
MET CA  HA   sing N N 247 
MET C   O    doub N N 248 
MET C   OXT  sing N N 249 
MET CB  CG   sing N N 250 
MET CB  HB2  sing N N 251 
MET CB  HB3  sing N N 252 
MET CG  SD   sing N N 253 
MET CG  HG2  sing N N 254 
MET CG  HG3  sing N N 255 
MET SD  CE   sing N N 256 
MET CE  HE1  sing N N 257 
MET CE  HE2  sing N N 258 
MET CE  HE3  sing N N 259 
MET OXT HXT  sing N N 260 
PHE N   CA   sing N N 261 
PHE N   H    sing N N 262 
PHE N   H2   sing N N 263 
PHE CA  C    sing N N 264 
PHE CA  CB   sing N N 265 
PHE CA  HA   sing N N 266 
PHE C   O    doub N N 267 
PHE C   OXT  sing N N 268 
PHE CB  CG   sing N N 269 
PHE CB  HB2  sing N N 270 
PHE CB  HB3  sing N N 271 
PHE CG  CD1  doub Y N 272 
PHE CG  CD2  sing Y N 273 
PHE CD1 CE1  sing Y N 274 
PHE CD1 HD1  sing N N 275 
PHE CD2 CE2  doub Y N 276 
PHE CD2 HD2  sing N N 277 
PHE CE1 CZ   doub Y N 278 
PHE CE1 HE1  sing N N 279 
PHE CE2 CZ   sing Y N 280 
PHE CE2 HE2  sing N N 281 
PHE CZ  HZ   sing N N 282 
PHE OXT HXT  sing N N 283 
PRO N   CA   sing N N 284 
PRO N   CD   sing N N 285 
PRO N   H    sing N N 286 
PRO CA  C    sing N N 287 
PRO CA  CB   sing N N 288 
PRO CA  HA   sing N N 289 
PRO C   O    doub N N 290 
PRO C   OXT  sing N N 291 
PRO CB  CG   sing N N 292 
PRO CB  HB2  sing N N 293 
PRO CB  HB3  sing N N 294 
PRO CG  CD   sing N N 295 
PRO CG  HG2  sing N N 296 
PRO CG  HG3  sing N N 297 
PRO CD  HD2  sing N N 298 
PRO CD  HD3  sing N N 299 
PRO OXT HXT  sing N N 300 
SER N   CA   sing N N 301 
SER N   H    sing N N 302 
SER N   H2   sing N N 303 
SER CA  C    sing N N 304 
SER CA  CB   sing N N 305 
SER CA  HA   sing N N 306 
SER C   O    doub N N 307 
SER C   OXT  sing N N 308 
SER CB  OG   sing N N 309 
SER CB  HB2  sing N N 310 
SER CB  HB3  sing N N 311 
SER OG  HG   sing N N 312 
SER OXT HXT  sing N N 313 
THR N   CA   sing N N 314 
THR N   H    sing N N 315 
THR N   H2   sing N N 316 
THR CA  C    sing N N 317 
THR CA  CB   sing N N 318 
THR CA  HA   sing N N 319 
THR C   O    doub N N 320 
THR C   OXT  sing N N 321 
THR CB  OG1  sing N N 322 
THR CB  CG2  sing N N 323 
THR CB  HB   sing N N 324 
THR OG1 HG1  sing N N 325 
THR CG2 HG21 sing N N 326 
THR CG2 HG22 sing N N 327 
THR CG2 HG23 sing N N 328 
THR OXT HXT  sing N N 329 
TRP N   CA   sing N N 330 
TRP N   H    sing N N 331 
TRP N   H2   sing N N 332 
TRP CA  C    sing N N 333 
TRP CA  CB   sing N N 334 
TRP CA  HA   sing N N 335 
TRP C   O    doub N N 336 
TRP C   OXT  sing N N 337 
TRP CB  CG   sing N N 338 
TRP CB  HB2  sing N N 339 
TRP CB  HB3  sing N N 340 
TRP CG  CD1  doub Y N 341 
TRP CG  CD2  sing Y N 342 
TRP CD1 NE1  sing Y N 343 
TRP CD1 HD1  sing N N 344 
TRP CD2 CE2  doub Y N 345 
TRP CD2 CE3  sing Y N 346 
TRP NE1 CE2  sing Y N 347 
TRP NE1 HE1  sing N N 348 
TRP CE2 CZ2  sing Y N 349 
TRP CE3 CZ3  doub Y N 350 
TRP CE3 HE3  sing N N 351 
TRP CZ2 CH2  doub Y N 352 
TRP CZ2 HZ2  sing N N 353 
TRP CZ3 CH2  sing Y N 354 
TRP CZ3 HZ3  sing N N 355 
TRP CH2 HH2  sing N N 356 
TRP OXT HXT  sing N N 357 
TYR N   CA   sing N N 358 
TYR N   H    sing N N 359 
TYR N   H2   sing N N 360 
TYR CA  C    sing N N 361 
TYR CA  CB   sing N N 362 
TYR CA  HA   sing N N 363 
TYR C   O    doub N N 364 
TYR C   OXT  sing N N 365 
TYR CB  CG   sing N N 366 
TYR CB  HB2  sing N N 367 
TYR CB  HB3  sing N N 368 
TYR CG  CD1  doub Y N 369 
TYR CG  CD2  sing Y N 370 
TYR CD1 CE1  sing Y N 371 
TYR CD1 HD1  sing N N 372 
TYR CD2 CE2  doub Y N 373 
TYR CD2 HD2  sing N N 374 
TYR CE1 CZ   doub Y N 375 
TYR CE1 HE1  sing N N 376 
TYR CE2 CZ   sing Y N 377 
TYR CE2 HE2  sing N N 378 
TYR CZ  OH   sing N N 379 
TYR OH  HH   sing N N 380 
TYR OXT HXT  sing N N 381 
VAL N   CA   sing N N 382 
VAL N   H    sing N N 383 
VAL N   H2   sing N N 384 
VAL CA  C    sing N N 385 
VAL CA  CB   sing N N 386 
VAL CA  HA   sing N N 387 
VAL C   O    doub N N 388 
VAL C   OXT  sing N N 389 
VAL CB  CG1  sing N N 390 
VAL CB  CG2  sing N N 391 
VAL CB  HB   sing N N 392 
VAL CG1 HG11 sing N N 393 
VAL CG1 HG12 sing N N 394 
VAL CG1 HG13 sing N N 395 
VAL CG2 HG21 sing N N 396 
VAL CG2 HG22 sing N N 397 
VAL CG2 HG23 sing N N 398 
VAL OXT HXT  sing N N 399 
# 
_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 
# 
_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                    9JLR 
_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]   0.013856 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004896 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006054 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.010821 
_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   . MET A 1 1   ? -15.015 6.911   27.105  1.00 96.67  ? 1   MET A N   1 
ATOM   2     C CA  . MET A 1 1   ? -14.008 7.841   26.600  1.00 86.71  ? 1   MET A CA  1 
ATOM   3     C C   . MET A 1 1   ? -13.720 7.592   25.123  1.00 75.12  ? 1   MET A C   1 
ATOM   4     O O   . MET A 1 1   ? -13.312 6.491   24.748  1.00 91.92  ? 1   MET A O   1 
ATOM   5     C CB  . MET A 1 1   ? -12.710 7.722   27.409  1.00 66.76  ? 1   MET A CB  1 
ATOM   6     C CG  . MET A 1 1   ? -11.496 8.328   26.718  1.00 80.22  ? 1   MET A CG  1 
ATOM   7     S SD  . MET A 1 1   ? -9.919  7.685   27.307  1.00 93.02  ? 1   MET A SD  1 
ATOM   8     C CE  . MET A 1 1   ? -9.363  9.017   28.378  1.00 80.04  ? 1   MET A CE  1 
ATOM   9     N N   . LYS A 1 2   ? -13.942 8.604   24.283  1.00 72.82  ? 2   LYS A N   1 
ATOM   10    C CA  . LYS A 1 2   ? -13.496 8.521   22.896  1.00 65.79  ? 2   LYS A CA  1 
ATOM   11    C C   . LYS A 1 2   ? -11.981 8.472   22.854  1.00 61.21  ? 2   LYS A C   1 
ATOM   12    O O   . LYS A 1 2   ? -11.303 9.364   23.371  1.00 63.50  ? 2   LYS A O   1 
ATOM   13    C CB  . LYS A 1 2   ? -14.001 9.704   22.072  1.00 61.89  ? 2   LYS A CB  1 
ATOM   14    C CG  . LYS A 1 2   ? -13.861 9.502   20.564  1.00 52.44  ? 2   LYS A CG  1 
ATOM   15    C CD  . LYS A 1 2   ? -14.783 10.428  19.788  1.00 65.19  ? 2   LYS A CD  1 
ATOM   16    C CE  . LYS A 1 2   ? -14.274 11.869  19.797  1.00 71.02  ? 2   LYS A CE  1 
ATOM   17    N NZ  . LYS A 1 2   ? -14.737 12.688  20.968  1.00 76.33  ? 2   LYS A NZ  1 
ATOM   18    N N   . LYS A 1 3   ? -11.449 7.429   22.241  1.00 59.13  ? 3   LYS A N   1 
ATOM   19    C CA  . LYS A 1 3   ? -10.018 7.212   22.210  1.00 54.98  ? 3   LYS A CA  1 
ATOM   20    C C   . LYS A 1 3   ? -9.514  7.334   20.781  1.00 54.67  ? 3   LYS A C   1 
ATOM   21    O O   . LYS A 1 3   ? -10.275 7.221   19.815  1.00 50.90  ? 3   LYS A O   1 
ATOM   22    C CB  . LYS A 1 3   ? -9.667  5.840   22.793  1.00 52.56  ? 3   LYS A CB  1 
ATOM   23    C CG  . LYS A 1 3   ? -9.887  5.750   24.292  1.00 59.13  ? 3   LYS A CG  1 
ATOM   24    C CD  . LYS A 1 3   ? -9.523  4.378   24.817  1.00 59.15  ? 3   LYS A CD  1 
ATOM   25    C CE  . LYS A 1 3   ? -8.035  4.251   25.042  1.00 64.90  ? 3   LYS A CE  1 
ATOM   26    N NZ  . LYS A 1 3   ? -7.602  4.795   26.359  1.00 79.57  ? 3   LYS A NZ  1 
ATOM   27    N N   . LEU A 1 4   ? -8.218  7.602   20.667  1.00 53.73  ? 4   LEU A N   1 
ATOM   28    C CA  . LEU A 1 4   ? -7.495  7.546   19.406  1.00 50.52  ? 4   LEU A CA  1 
ATOM   29    C C   . LEU A 1 4   ? -6.548  6.360   19.468  1.00 43.55  ? 4   LEU A C   1 
ATOM   30    O O   . LEU A 1 4   ? -5.726  6.265   20.384  1.00 47.63  ? 4   LEU A O   1 
ATOM   31    C CB  . LEU A 1 4   ? -6.715  8.838   19.140  1.00 52.74  ? 4   LEU A CB  1 
ATOM   32    C CG  . LEU A 1 4   ? -6.040  8.981   17.760  1.00 53.85  ? 4   LEU A CG  1 
ATOM   33    C CD1 . LEU A 1 4   ? -5.894  10.447  17.372  1.00 54.35  ? 4   LEU A CD1 1 
ATOM   34    C CD2 . LEU A 1 4   ? -4.679  8.278   17.644  1.00 43.42  ? 4   LEU A CD2 1 
ATOM   35    N N   . PHE A 1 5   ? -6.657  5.472   18.490  1.00 47.05  ? 5   PHE A N   1 
ATOM   36    C CA  . PHE A 1 5   ? -5.842  4.267   18.432  1.00 49.32  ? 5   PHE A CA  1 
ATOM   37    C C   . PHE A 1 5   ? -4.644  4.518   17.525  1.00 48.46  ? 5   PHE A C   1 
ATOM   38    O O   . PHE A 1 5   ? -4.803  4.756   16.321  1.00 47.33  ? 5   PHE A O   1 
ATOM   39    C CB  . PHE A 1 5   ? -6.672  3.079   17.955  1.00 42.22  ? 5   PHE A CB  1 
ATOM   40    C CG  . PHE A 1 5   ? -7.837  2.762   18.854  1.00 47.49  ? 5   PHE A CG  1 
ATOM   41    C CD1 . PHE A 1 5   ? -7.629  2.309   20.147  1.00 48.92  ? 5   PHE A CD1 1 
ATOM   42    C CD2 . PHE A 1 5   ? -9.141  2.920   18.408  1.00 50.97  ? 5   PHE A CD2 1 
ATOM   43    C CE1 . PHE A 1 5   ? -8.697  2.017   20.977  1.00 44.54  ? 5   PHE A CE1 1 
ATOM   44    C CE2 . PHE A 1 5   ? -10.212 2.628   19.238  1.00 52.20  ? 5   PHE A CE2 1 
ATOM   45    C CZ  . PHE A 1 5   ? -9.985  2.176   20.521  1.00 45.40  ? 5   PHE A CZ  1 
ATOM   46    N N   . LEU A 1 6   ? -3.452  4.472   18.112  1.00 45.75  ? 6   LEU A N   1 
ATOM   47    C CA  . LEU A 1 6   ? -2.208  4.756   17.413  1.00 51.09  ? 6   LEU A CA  1 
ATOM   48    C C   . LEU A 1 6   ? -1.465  3.457   17.130  1.00 45.98  ? 6   LEU A C   1 
ATOM   49    O O   . LEU A 1 6   ? -1.246  2.649   18.040  1.00 50.20  ? 6   LEU A O   1 
ATOM   50    C CB  . LEU A 1 6   ? -1.333  5.698   18.243  1.00 44.74  ? 6   LEU A CB  1 
ATOM   51    C CG  . LEU A 1 6   ? -0.237  6.428   17.482  1.00 42.14  ? 6   LEU A CG  1 
ATOM   52    C CD1 . LEU A 1 6   ? -0.837  7.121   16.267  1.00 42.23  ? 6   LEU A CD1 1 
ATOM   53    C CD2 . LEU A 1 6   ? 0.450   7.418   18.410  1.00 44.37  ? 6   LEU A CD2 1 
ATOM   54    N N   . VAL A 1 7   ? -1.081  3.265   15.871  1.00 40.94  ? 7   VAL A N   1 
ATOM   55    C CA  . VAL A 1 7   ? -0.308  2.104   15.443  1.00 44.83  ? 7   VAL A CA  1 
ATOM   56    C C   . VAL A 1 7   ? 1.000   2.597   14.842  1.00 44.72  ? 7   VAL A C   1 
ATOM   57    O O   . VAL A 1 7   ? 0.996   3.342   13.852  1.00 41.39  ? 7   VAL A O   1 
ATOM   58    C CB  . VAL A 1 7   ? -1.076  1.238   14.434  1.00 42.54  ? 7   VAL A CB  1 
ATOM   59    C CG1 . VAL A 1 7   ? -0.155  0.186   13.823  1.00 41.97  ? 7   VAL A CG1 1 
ATOM   60    C CG2 . VAL A 1 7   ? -2.247  0.581   15.117  1.00 41.08  ? 7   VAL A CG2 1 
ATOM   61    N N   . PHE A 1 8   ? 2.112   2.176   15.437  1.00 42.42  ? 8   PHE A N   1 
ATOM   62    C CA  . PHE A 1 8   ? 3.442   2.455   14.918  1.00 44.45  ? 8   PHE A CA  1 
ATOM   63    C C   . PHE A 1 8   ? 3.947   1.215   14.197  1.00 42.38  ? 8   PHE A C   1 
ATOM   64    O O   . PHE A 1 8   ? 3.979   0.126   14.777  1.00 44.70  ? 8   PHE A O   1 
ATOM   65    C CB  . PHE A 1 8   ? 4.392   2.838   16.047  1.00 41.01  ? 8   PHE A CB  1 
ATOM   66    C CG  . PHE A 1 8   ? 4.251   4.262   16.503  1.00 40.11  ? 8   PHE A CG  1 
ATOM   67    C CD1 . PHE A 1 8   ? 4.626   5.305   15.674  1.00 40.15  ? 8   PHE A CD1 1 
ATOM   68    C CD2 . PHE A 1 8   ? 3.742   4.556   17.757  1.00 36.72  ? 8   PHE A CD2 1 
ATOM   69    C CE1 . PHE A 1 8   ? 4.497   6.617   16.087  1.00 41.68  ? 8   PHE A CE1 1 
ATOM   70    C CE2 . PHE A 1 8   ? 3.610   5.864   18.178  1.00 40.76  ? 8   PHE A CE2 1 
ATOM   71    C CZ  . PHE A 1 8   ? 3.988   6.899   17.342  1.00 44.91  ? 8   PHE A CZ  1 
ATOM   72    N N   . TRP A 1 9   ? 4.329   1.373   12.938  1.00 43.36  ? 9   TRP A N   1 
ATOM   73    C CA  . TRP A 1 9   ? 4.858   0.266   12.150  1.00 48.08  ? 9   TRP A CA  1 
ATOM   74    C C   . TRP A 1 9   ? 6.211   0.695   11.593  1.00 44.35  ? 9   TRP A C   1 
ATOM   75    O O   . TRP A 1 9   ? 6.271   1.510   10.667  1.00 51.34  ? 9   TRP A O   1 
ATOM   76    C CB  . TRP A 1 9   ? 3.877   -0.125  11.047  1.00 39.72  ? 9   TRP A CB  1 
ATOM   77    C CG  . TRP A 1 9   ? 4.030   -1.533  10.558  1.00 42.56  ? 9   TRP A CG  1 
ATOM   78    C CD1 . TRP A 1 9   ? 5.055   -2.386  10.830  1.00 43.92  ? 9   TRP A CD1 1 
ATOM   79    C CD2 . TRP A 1 9   ? 3.148   -2.237  9.671   1.00 45.21  ? 9   TRP A CD2 1 
ATOM   80    N NE1 . TRP A 1 9   ? 4.863   -3.583  10.179  1.00 37.20  ? 9   TRP A NE1 1 
ATOM   81    C CE2 . TRP A 1 9   ? 3.700   -3.515  9.461   1.00 38.44  ? 9   TRP A CE2 1 
ATOM   82    C CE3 . TRP A 1 9   ? 1.944   -1.910  9.039   1.00 41.57  ? 9   TRP A CE3 1 
ATOM   83    C CZ2 . TRP A 1 9   ? 3.090   -4.466  8.650   1.00 43.48  ? 9   TRP A CZ2 1 
ATOM   84    C CZ3 . TRP A 1 9   ? 1.342   -2.857  8.233   1.00 44.48  ? 9   TRP A CZ3 1 
ATOM   85    C CH2 . TRP A 1 9   ? 1.916   -4.119  8.044   1.00 44.22  ? 9   TRP A CH2 1 
ATOM   86    N N   . TRP A 1 10  ? 7.294   0.170   12.180  1.00 40.01  ? 10  TRP A N   1 
ATOM   87    C CA  . TRP A 1 10  ? 8.664   0.525   11.810  1.00 42.11  ? 10  TRP A CA  1 
ATOM   88    C C   . TRP A 1 10  ? 9.213   -0.496  10.821  1.00 43.11  ? 10  TRP A C   1 
ATOM   89    O O   . TRP A 1 10  ? 9.366   -1.675  11.164  1.00 45.80  ? 10  TRP A O   1 
ATOM   90    C CB  . TRP A 1 10  ? 9.581   0.576   13.033  1.00 43.89  ? 10  TRP A CB  1 
ATOM   91    C CG  . TRP A 1 10  ? 9.241   1.601   14.063  1.00 40.26  ? 10  TRP A CG  1 
ATOM   92    C CD1 . TRP A 1 10  ? 8.772   1.364   15.320  1.00 39.56  ? 10  TRP A CD1 1 
ATOM   93    C CD2 . TRP A 1 10  ? 9.374   3.024   13.945  1.00 40.52  ? 10  TRP A CD2 1 
ATOM   94    N NE1 . TRP A 1 10  ? 8.586   2.552   15.991  1.00 35.55  ? 10  TRP A NE1 1 
ATOM   95    C CE2 . TRP A 1 10  ? 8.947   3.586   15.168  1.00 38.43  ? 10  TRP A CE2 1 
ATOM   96    C CE3 . TRP A 1 10  ? 9.802   3.879   12.922  1.00 45.91  ? 10  TRP A CE3 1 
ATOM   97    C CZ2 . TRP A 1 10  ? 8.937   4.958   15.395  1.00 39.09  ? 10  TRP A CZ2 1 
ATOM   98    C CZ3 . TRP A 1 10  ? 9.792   5.249   13.152  1.00 39.33  ? 10  TRP A CZ3 1 
ATOM   99    C CH2 . TRP A 1 10  ? 9.362   5.771   14.377  1.00 42.07  ? 10  TRP A CH2 1 
ATOM   100   N N   . HIS A 1 11  ? 9.541   -0.041  9.615   1.00 41.73  ? 11  HIS A N   1 
ATOM   101   C CA  . HIS A 1 11  ? 10.029  -0.917  8.557   1.00 46.26  ? 11  HIS A CA  1 
ATOM   102   C C   . HIS A 1 11  ? 11.553  -0.948  8.552   1.00 41.68  ? 11  HIS A C   1 
ATOM   103   O O   . HIS A 1 11  ? 12.206  0.103   8.509   1.00 44.54  ? 11  HIS A O   1 
ATOM   104   C CB  . HIS A 1 11  ? 9.503   -0.469  7.190   1.00 41.45  ? 11  HIS A CB  1 
ATOM   105   C CG  . HIS A 1 11  ? 10.210  -1.103  6.029   1.00 41.40  ? 11  HIS A CG  1 
ATOM   106   N ND1 . HIS A 1 11  ? 10.168  -2.460  5.780   1.00 43.88  ? 11  HIS A ND1 1 
ATOM   107   C CD2 . HIS A 1 11  ? 10.960  -0.563  5.040   1.00 38.20  ? 11  HIS A CD2 1 
ATOM   108   C CE1 . HIS A 1 11  ? 10.868  -2.728  4.693   1.00 43.79  ? 11  HIS A CE1 1 
ATOM   109   N NE2 . HIS A 1 11  ? 11.355  -1.594  4.222   1.00 45.68  ? 11  HIS A NE2 1 
ATOM   110   N N   . MET A 1 12  ? 12.112  -2.154  8.584   1.00 35.75  ? 12  MET A N   1 
ATOM   111   C CA  . MET A 1 12  ? 13.555  -2.348  8.627   1.00 45.29  ? 12  MET A CA  1 
ATOM   112   C C   . MET A 1 12  ? 13.968  -3.186  7.432   1.00 40.31  ? 12  MET A C   1 
ATOM   113   O O   . MET A 1 12  ? 13.471  -4.302  7.247   1.00 37.12  ? 12  MET A O   1 
ATOM   114   C CB  . MET A 1 12  ? 13.988  -3.017  9.934   1.00 43.38  ? 12  MET A CB  1 
ATOM   115   C CG  . MET A 1 12  ? 13.223  -2.525  11.149  1.00 42.15  ? 12  MET A CG  1 
ATOM   116   S SD  . MET A 1 12  ? 13.788  -0.918  11.720  1.00 71.47  ? 12  MET A SD  1 
ATOM   117   C CE  . MET A 1 12  ? 13.908  -1.211  13.479  1.00 53.70  ? 12  MET A CE  1 
ATOM   118   N N   . HIS A 1 13  ? 14.883  -2.655  6.631   1.00 40.50  ? 13  HIS A N   1 
ATOM   119   C CA  . HIS A 1 13  ? 15.311  -3.383  5.454   1.00 40.66  ? 13  HIS A CA  1 
ATOM   120   C C   . HIS A 1 13  ? 16.722  -2.957  5.081   1.00 38.47  ? 13  HIS A C   1 
ATOM   121   O O   . HIS A 1 13  ? 17.066  -1.776  5.177   1.00 40.41  ? 13  HIS A O   1 
ATOM   122   C CB  . HIS A 1 13  ? 14.345  -3.140  4.293   1.00 39.05  ? 13  HIS A CB  1 
ATOM   123   C CG  . HIS A 1 13  ? 14.886  -3.566  2.972   1.00 36.58  ? 13  HIS A CG  1 
ATOM   124   N ND1 . HIS A 1 13  ? 15.275  -4.863  2.714   1.00 37.32  ? 13  HIS A ND1 1 
ATOM   125   C CD2 . HIS A 1 13  ? 15.125  -2.867  1.840   1.00 35.28  ? 13  HIS A CD2 1 
ATOM   126   C CE1 . HIS A 1 13  ? 15.724  -4.945  1.475   1.00 40.83  ? 13  HIS A CE1 1 
ATOM   127   N NE2 . HIS A 1 13  ? 15.642  -3.748  0.923   1.00 45.99  ? 13  HIS A NE2 1 
ATOM   128   N N   . GLN A 1 14  ? 17.543  -3.933  4.683   1.00 35.35  ? 14  GLN A N   1 
ATOM   129   C CA  . GLN A 1 14  ? 18.798  -3.647  3.999   1.00 40.10  ? 14  GLN A CA  1 
ATOM   130   C C   . GLN A 1 14  ? 18.943  -4.609  2.828   1.00 43.09  ? 14  GLN A C   1 
ATOM   131   O O   . GLN A 1 14  ? 18.886  -5.829  3.027   1.00 50.34  ? 14  GLN A O   1 
ATOM   132   C CB  . GLN A 1 14  ? 20.011  -3.776  4.933   1.00 46.20  ? 14  GLN A CB  1 
ATOM   133   C CG  . GLN A 1 14  ? 20.067  -2.741  6.056   1.00 41.37  ? 14  GLN A CG  1 
ATOM   134   C CD  . GLN A 1 14  ? 20.396  -1.332  5.580   1.00 42.44  ? 14  GLN A CD  1 
ATOM   135   O OE1 . GLN A 1 14  ? 20.923  -1.131  4.485   1.00 37.32  ? 14  GLN A OE1 1 
ATOM   136   N NE2 . GLN A 1 14  ? 20.082  -0.346  6.412   1.00 47.40  ? 14  GLN A NE2 1 
ATOM   137   N N   . PRO A 1 15  ? 19.121  -4.115  1.604   1.00 45.23  ? 15  PRO A N   1 
ATOM   138   C CA  . PRO A 1 15  ? 19.327  -5.017  0.468   1.00 39.28  ? 15  PRO A CA  1 
ATOM   139   C C   . PRO A 1 15  ? 20.592  -5.846  0.660   1.00 49.98  ? 15  PRO A C   1 
ATOM   140   O O   . PRO A 1 15  ? 21.459  -5.521  1.475   1.00 52.20  ? 15  PRO A O   1 
ATOM   141   C CB  . PRO A 1 15  ? 19.468  -4.054  -0.717  1.00 44.90  ? 15  PRO A CB  1 
ATOM   142   C CG  . PRO A 1 15  ? 19.969  -2.784  -0.089  1.00 45.58  ? 15  PRO A CG  1 
ATOM   143   C CD  . PRO A 1 15  ? 19.214  -2.702  1.200   1.00 46.14  ? 15  PRO A CD  1 
ATOM   144   N N   . LEU A 1 16  ? 20.693  -6.934  -0.101  1.00 49.47  ? 16  LEU A N   1 
ATOM   145   C CA  . LEU A 1 16  ? 21.836  -7.838  0.016   1.00 49.21  ? 16  LEU A CA  1 
ATOM   146   C C   . LEU A 1 16  ? 23.101  -7.149  -0.479  1.00 46.69  ? 16  LEU A C   1 
ATOM   147   O O   . LEU A 1 16  ? 23.319  -7.010  -1.684  1.00 48.50  ? 16  LEU A O   1 
ATOM   148   C CB  . LEU A 1 16  ? 21.592  -9.122  -0.767  1.00 47.97  ? 16  LEU A CB  1 
ATOM   149   C CG  . LEU A 1 16  ? 22.730  -10.134 -0.622  1.00 45.18  ? 16  LEU A CG  1 
ATOM   150   C CD1 . LEU A 1 16  ? 23.057  -10.329 0.853   1.00 46.23  ? 16  LEU A CD1 1 
ATOM   151   C CD2 . LEU A 1 16  ? 22.360  -11.449 -1.278  1.00 44.57  ? 16  LEU A CD2 1 
ATOM   152   N N   . TYR A 1 17  ? 23.952  -6.737  0.451   1.00 50.59  ? 17  TYR A N   1 
ATOM   153   C CA  . TYR A 1 17  ? 25.220  -6.100  0.124   1.00 52.30  ? 17  TYR A CA  1 
ATOM   154   C C   . TYR A 1 17  ? 26.347  -7.096  -0.126  1.00 49.56  ? 17  TYR A C   1 
ATOM   155   O O   . TYR A 1 17  ? 27.474  -6.675  -0.406  1.00 54.28  ? 17  TYR A O   1 
ATOM   156   C CB  . TYR A 1 17  ? 25.640  -5.158  1.250   1.00 49.86  ? 17  TYR A CB  1 
ATOM   157   C CG  . TYR A 1 17  ? 24.745  -3.967  1.483   1.00 41.55  ? 17  TYR A CG  1 
ATOM   158   C CD1 . TYR A 1 17  ? 24.558  -3.010  0.492   1.00 44.45  ? 17  TYR A CD1 1 
ATOM   159   C CD2 . TYR A 1 17  ? 24.135  -3.768  2.713   1.00 38.77  ? 17  TYR A CD2 1 
ATOM   160   C CE1 . TYR A 1 17  ? 23.763  -1.904  0.710   1.00 41.18  ? 17  TYR A CE1 1 
ATOM   161   C CE2 . TYR A 1 17  ? 23.338  -2.665  2.943   1.00 46.74  ? 17  TYR A CE2 1 
ATOM   162   C CZ  . TYR A 1 17  ? 23.155  -1.736  1.936   1.00 46.67  ? 17  TYR A CZ  1 
ATOM   163   O OH  . TYR A 1 17  ? 22.365  -0.633  2.153   1.00 44.06  ? 17  TYR A OH  1 
ATOM   164   N N   . ARG A 1 18  ? 26.079  -8.395  -0.024  1.00 51.27  ? 18  ARG A N   1 
ATOM   165   C CA  . ARG A 1 18  ? 27.121  -9.412  -0.116  1.00 57.24  ? 18  ARG A CA  1 
ATOM   166   C C   . ARG A 1 18  ? 27.362  -9.774  -1.577  1.00 54.73  ? 18  ARG A C   1 
ATOM   167   O O   . ARG A 1 18  ? 26.473  -10.327 -2.233  1.00 54.65  ? 18  ARG A O   1 
ATOM   168   C CB  . ARG A 1 18  ? 26.733  -10.657 0.683   1.00 56.04  ? 18  ARG A CB  1 
ATOM   169   C CG  . ARG A 1 18  ? 27.836  -11.704 0.737   1.00 62.36  ? 18  ARG A CG  1 
ATOM   170   C CD  . ARG A 1 18  ? 27.366  -13.028 1.343   1.00 67.02  ? 18  ARG A CD  1 
ATOM   171   N NE  . ARG A 1 18  ? 27.861  -14.180 0.589   1.00 69.42  ? 18  ARG A NE  1 
ATOM   172   C CZ  . ARG A 1 18  ? 27.474  -14.515 -0.635  1.00 66.11  ? 18  ARG A CZ  1 
ATOM   173   N NH1 . ARG A 1 18  ? 26.529  -13.841 -1.275  1.00 59.25  ? 18  ARG A NH1 1 
ATOM   174   N NH2 . ARG A 1 18  ? 28.048  -15.556 -1.232  1.00 61.58  ? 18  ARG A NH2 1 
ATOM   175   N N   . GLU A 1 19  ? 28.555  -9.469  -2.080  1.00 55.26  ? 19  GLU A N   1 
ATOM   176   C CA  . GLU A 1 19  ? 28.915  -9.850  -3.441  1.00 55.67  ? 19  GLU A CA  1 
ATOM   177   C C   . GLU A 1 19  ? 28.896  -11.374 -3.565  1.00 58.53  ? 19  GLU A C   1 
ATOM   178   O O   . GLU A 1 19  ? 29.492  -12.063 -2.726  1.00 63.46  ? 19  GLU A O   1 
ATOM   179   C CB  . GLU A 1 19  ? 30.303  -9.297  -3.790  1.00 58.64  ? 19  GLU A CB  1 
ATOM   180   C CG  . GLU A 1 19  ? 30.591  -9.166  -5.287  1.00 60.06  ? 19  GLU A CG  1 
ATOM   181   C CD  . GLU A 1 19  ? 31.322  -10.371 -5.853  1.00 65.08  ? 19  GLU A CD  1 
ATOM   182   O OE1 . GLU A 1 19  ? 31.565  -11.326 -5.087  1.00 65.12  ? 19  GLU A OE1 1 
ATOM   183   O OE2 . GLU A 1 19  ? 31.627  -10.380 -7.068  1.00 72.82  ? 19  GLU A OE2 1 
ATOM   184   N N   . PRO A 1 20  ? 28.236  -11.937 -4.585  1.00 58.73  ? 20  PRO A N   1 
ATOM   185   C CA  . PRO A 1 20  ? 28.116  -13.412 -4.646  1.00 64.97  ? 20  PRO A CA  1 
ATOM   186   C C   . PRO A 1 20  ? 29.447  -14.151 -4.726  1.00 67.57  ? 20  PRO A C   1 
ATOM   187   O O   . PRO A 1 20  ? 29.668  -15.089 -3.949  1.00 70.90  ? 20  PRO A O   1 
ATOM   188   C CB  . PRO A 1 20  ? 27.262  -13.635 -5.905  1.00 59.14  ? 20  PRO A CB  1 
ATOM   189   C CG  . PRO A 1 20  ? 27.468  -12.400 -6.726  1.00 60.28  ? 20  PRO A CG  1 
ATOM   190   C CD  . PRO A 1 20  ? 27.564  -11.285 -5.722  1.00 56.58  ? 20  PRO A CD  1 
ATOM   191   N N   . TYR A 1 21  ? 30.344  -13.754 -5.638  1.00 57.87  ? 21  TYR A N   1 
ATOM   192   C CA  . TYR A 1 21  ? 31.553  -14.538 -5.892  1.00 62.57  ? 21  TYR A CA  1 
ATOM   193   C C   . TYR A 1 21  ? 32.538  -14.453 -4.730  1.00 62.01  ? 21  TYR A C   1 
ATOM   194   O O   . TYR A 1 21  ? 33.023  -15.480 -4.240  1.00 53.70  ? 21  TYR A O   1 
ATOM   195   C CB  . TYR A 1 21  ? 32.208  -14.080 -7.194  1.00 55.97  ? 21  TYR A CB  1 
ATOM   196   C CG  . TYR A 1 21  ? 31.329  -14.314 -8.388  1.00 62.83  ? 21  TYR A CG  1 
ATOM   197   C CD1 . TYR A 1 21  ? 31.385  -15.511 -9.084  1.00 59.75  ? 21  TYR A CD1 1 
ATOM   198   C CD2 . TYR A 1 21  ? 30.420  -13.352 -8.806  1.00 68.50  ? 21  TYR A CD2 1 
ATOM   199   C CE1 . TYR A 1 21  ? 30.574  -15.745 -10.172 1.00 58.28  ? 21  TYR A CE1 1 
ATOM   200   C CE2 . TYR A 1 21  ? 29.598  -13.577 -9.901  1.00 69.52  ? 21  TYR A CE2 1 
ATOM   201   C CZ  . TYR A 1 21  ? 29.684  -14.780 -10.579 1.00 64.85  ? 21  TYR A CZ  1 
ATOM   202   O OH  . TYR A 1 21  ? 28.883  -15.037 -11.665 1.00 69.68  ? 21  TYR A OH  1 
ATOM   203   N N   . THR A 1 22  ? 32.852  -13.236 -4.280  1.00 61.61  ? 22  THR A N   1 
ATOM   204   C CA  . THR A 1 22  ? 33.817  -13.067 -3.201  1.00 62.88  ? 22  THR A CA  1 
ATOM   205   C C   . THR A 1 22  ? 33.205  -13.280 -1.821  1.00 67.02  ? 22  THR A C   1 
ATOM   206   O O   . THR A 1 22  ? 33.954  -13.444 -0.851  1.00 67.29  ? 22  THR A O   1 
ATOM   207   C CB  . THR A 1 22  ? 34.463  -11.675 -3.260  1.00 65.16  ? 22  THR A CB  1 
ATOM   208   O OG1 . THR A 1 22  ? 33.461  -10.657 -3.149  1.00 67.05  ? 22  THR A OG1 1 
ATOM   209   C CG2 . THR A 1 22  ? 35.214  -11.488 -4.569  1.00 63.04  ? 22  THR A CG2 1 
ATOM   210   N N   . GLY A 1 23  ? 31.875  -13.293 -1.712  1.00 64.30  ? 23  GLY A N   1 
ATOM   211   C CA  . GLY A 1 23  ? 31.231  -13.381 -0.409  1.00 64.63  ? 23  GLY A CA  1 
ATOM   212   C C   . GLY A 1 23  ? 31.594  -12.252 0.531   1.00 69.54  ? 23  GLY A C   1 
ATOM   213   O O   . GLY A 1 23  ? 31.633  -12.450 1.751   1.00 69.92  ? 23  GLY A O   1 
ATOM   214   N N   . GLU A 1 24  ? 31.865  -11.068 -0.006  1.00 67.18  ? 24  GLU A N   1 
ATOM   215   C CA  . GLU A 1 24  ? 32.334  -9.933  0.775   1.00 62.11  ? 24  GLU A CA  1 
ATOM   216   C C   . GLU A 1 24  ? 31.241  -8.882  0.819   1.00 59.14  ? 24  GLU A C   1 
ATOM   217   O O   . GLU A 1 24  ? 30.669  -8.531  -0.217  1.00 61.84  ? 24  GLU A O   1 
ATOM   218   C CB  . GLU A 1 24  ? 33.605  -9.339  0.167   1.00 69.98  ? 24  GLU A CB  1 
ATOM   219   C CG  . GLU A 1 24  ? 34.898  -9.967  0.652   1.00 74.76  ? 24  GLU A CG  1 
ATOM   220   C CD  . GLU A 1 24  ? 36.117  -9.192  0.190   1.00 86.44  ? 24  GLU A CD  1 
ATOM   221   O OE1 . GLU A 1 24  ? 35.963  -8.291  -0.663  1.00 105.07 ? 24  GLU A OE1 1 
ATOM   222   O OE2 . GLU A 1 24  ? 37.228  -9.480  0.683   1.00 108.55 ? 24  GLU A OE2 1 
ATOM   223   N N   . TYR A 1 25  ? 30.942  -8.390  2.012   1.00 52.79  ? 25  TYR A N   1 
ATOM   224   C CA  . TYR A 1 25  ? 29.975  -7.311  2.141   1.00 50.95  ? 25  TYR A CA  1 
ATOM   225   C C   . TYR A 1 25  ? 30.676  -6.021  1.745   1.00 52.46  ? 25  TYR A C   1 
ATOM   226   O O   . TYR A 1 25  ? 31.605  -5.573  2.424   1.00 59.03  ? 25  TYR A O   1 
ATOM   227   C CB  . TYR A 1 25  ? 29.427  -7.253  3.560   1.00 51.61  ? 25  TYR A CB  1 
ATOM   228   C CG  . TYR A 1 25  ? 28.433  -8.339  3.876   1.00 51.30  ? 25  TYR A CG  1 
ATOM   229   C CD1 . TYR A 1 25  ? 28.832  -9.663  3.987   1.00 58.76  ? 25  TYR A CD1 1 
ATOM   230   C CD2 . TYR A 1 25  ? 27.099  -8.038  4.079   1.00 52.78  ? 25  TYR A CD2 1 
ATOM   231   C CE1 . TYR A 1 25  ? 27.928  -10.652 4.286   1.00 58.03  ? 25  TYR A CE1 1 
ATOM   232   C CE2 . TYR A 1 25  ? 26.190  -9.017  4.379   1.00 49.23  ? 25  TYR A CE2 1 
ATOM   233   C CZ  . TYR A 1 25  ? 26.609  -10.321 4.481   1.00 50.39  ? 25  TYR A CZ  1 
ATOM   234   O OH  . TYR A 1 25  ? 25.707  -11.305 4.782   1.00 58.06  ? 25  TYR A OH  1 
ATOM   235   N N   . LEU A 1 26  ? 30.258  -5.445  0.622   1.00 45.18  ? 26  LEU A N   1 
ATOM   236   C CA  . LEU A 1 26  ? 30.913  -4.269  0.076   1.00 42.28  ? 26  LEU A CA  1 
ATOM   237   C C   . LEU A 1 26  ? 30.471  -2.970  0.742   1.00 43.08  ? 26  LEU A C   1 
ATOM   238   O O   . LEU A 1 26  ? 31.105  -1.939  0.514   1.00 43.07  ? 26  LEU A O   1 
ATOM   239   C CB  . LEU A 1 26  ? 30.658  -4.198  -1.432  1.00 49.96  ? 26  LEU A CB  1 
ATOM   240   C CG  . LEU A 1 26  ? 30.842  -5.504  -2.210  1.00 45.42  ? 26  LEU A CG  1 
ATOM   241   C CD1 . LEU A 1 26  ? 30.599  -5.268  -3.679  1.00 50.82  ? 26  LEU A CD1 1 
ATOM   242   C CD2 . LEU A 1 26  ? 32.225  -6.091  -2.001  1.00 45.49  ? 26  LEU A CD2 1 
ATOM   243   N N   . LEU A 1 27  ? 29.416  -2.985  1.547   1.00 51.58  ? 27  LEU A N   1 
ATOM   244   C CA  . LEU A 1 27  ? 29.032  -1.824  2.321   1.00 50.23  ? 27  LEU A CA  1 
ATOM   245   C C   . LEU A 1 27  ? 28.667  -2.250  3.731   1.00 52.62  ? 27  LEU A C   1 
ATOM   246   O O   . LEU A 1 27  ? 28.159  -3.360  3.931   1.00 56.81  ? 27  LEU A O   1 
ATOM   247   C CB  . LEU A 1 27  ? 27.840  -1.098  1.677   1.00 50.65  ? 27  LEU A CB  1 
ATOM   248   C CG  . LEU A 1 27  ? 28.163  -0.307  0.405   1.00 57.46  ? 27  LEU A CG  1 
ATOM   249   C CD1 . LEU A 1 27  ? 26.895  0.244   -0.203  1.00 54.83  ? 27  LEU A CD1 1 
ATOM   250   C CD2 . LEU A 1 27  ? 29.169  0.818   0.665   1.00 61.52  ? 27  LEU A CD2 1 
ATOM   251   N N   . PRO A 1 28  ? 28.911  -1.403  4.730   1.00 52.88  ? 28  PRO A N   1 
ATOM   252   C CA  . PRO A 1 28  ? 28.726  -1.860  6.119   1.00 52.27  ? 28  PRO A CA  1 
ATOM   253   C C   . PRO A 1 28  ? 27.415  -1.379  6.695   1.00 50.83  ? 28  PRO A C   1 
ATOM   254   O O   . PRO A 1 28  ? 27.287  -1.235  7.906   1.00 47.32  ? 28  PRO A O   1 
ATOM   255   C CB  . PRO A 1 28  ? 29.919  -1.219  6.863   1.00 54.61  ? 28  PRO A CB  1 
ATOM   256   C CG  . PRO A 1 28  ? 30.279  -0.014  6.005   1.00 58.92  ? 28  PRO A CG  1 
ATOM   257   C CD  . PRO A 1 28  ? 29.585  -0.102  4.663   1.00 46.77  ? 28  PRO A CD  1 
ATOM   258   N N   . TRP A 1 29  ? 26.456  -1.103  5.815   1.00 52.54  ? 29  TRP A N   1 
ATOM   259   C CA  . TRP A 1 29  ? 25.242  -0.425  6.265   1.00 47.71  ? 29  TRP A CA  1 
ATOM   260   C C   . TRP A 1 29  ? 24.391  -1.304  7.170   1.00 44.74  ? 29  TRP A C   1 
ATOM   261   O O   . TRP A 1 29  ? 23.665  -0.791  8.028   1.00 48.33  ? 29  TRP A O   1 
ATOM   262   C CB  . TRP A 1 29  ? 24.431  0.043   5.067   1.00 42.47  ? 29  TRP A CB  1 
ATOM   263   C CG  . TRP A 1 29  ? 25.030  1.175   4.322   1.00 41.26  ? 29  TRP A CG  1 
ATOM   264   C CD1 . TRP A 1 29  ? 25.243  1.239   2.980   1.00 49.18  ? 29  TRP A CD1 1 
ATOM   265   C CD2 . TRP A 1 29  ? 25.459  2.435   4.858   1.00 43.44  ? 29  TRP A CD2 1 
ATOM   266   N NE1 . TRP A 1 29  ? 25.782  2.456   2.640   1.00 51.59  ? 29  TRP A NE1 1 
ATOM   267   C CE2 . TRP A 1 29  ? 25.925  3.209   3.775   1.00 50.66  ? 29  TRP A CE2 1 
ATOM   268   C CE3 . TRP A 1 29  ? 25.497  2.985   6.142   1.00 48.39  ? 29  TRP A CE3 1 
ATOM   269   C CZ2 . TRP A 1 29  ? 26.423  4.498   3.940   1.00 48.98  ? 29  TRP A CZ2 1 
ATOM   270   C CZ3 . TRP A 1 29  ? 25.994  4.267   6.302   1.00 49.58  ? 29  TRP A CZ3 1 
ATOM   271   C CH2 . TRP A 1 29  ? 26.449  5.007   5.208   1.00 50.46  ? 29  TRP A CH2 1 
ATOM   272   N N   . THR A 1 30  ? 24.458  -2.625  6.984   1.00 48.05  ? 30  THR A N   1 
ATOM   273   C CA  . THR A 1 30  ? 23.750  -3.544  7.870   1.00 41.41  ? 30  THR A CA  1 
ATOM   274   C C   . THR A 1 30  ? 24.353  -3.533  9.270   1.00 48.75  ? 30  THR A C   1 
ATOM   275   O O   . THR A 1 30  ? 23.622  -3.507  10.267  1.00 51.51  ? 30  THR A O   1 
ATOM   276   C CB  . THR A 1 30  ? 23.781  -4.958  7.292   1.00 44.20  ? 30  THR A CB  1 
ATOM   277   O OG1 . THR A 1 30  ? 23.064  -4.989  6.051   1.00 51.83  ? 30  THR A OG1 1 
ATOM   278   C CG2 . THR A 1 30  ? 23.143  -5.938  8.252   1.00 45.56  ? 30  THR A CG2 1 
ATOM   279   N N   . PHE A 1 31  ? 25.685  -3.541  9.365   1.00 50.65  ? 31  PHE A N   1 
ATOM   280   C CA  . PHE A 1 31  ? 26.330  -3.554  10.674  1.00 51.47  ? 31  PHE A CA  1 
ATOM   281   C C   . PHE A 1 31  ? 26.028  -2.281  11.456  1.00 51.81  ? 31  PHE A C   1 
ATOM   282   O O   . PHE A 1 31  ? 25.740  -2.341  12.658  1.00 58.71  ? 31  PHE A O   1 
ATOM   283   C CB  . PHE A 1 31  ? 27.843  -3.746  10.510  1.00 53.71  ? 31  PHE A CB  1 
ATOM   284   C CG  . PHE A 1 31  ? 28.614  -3.671  11.806  1.00 50.48  ? 31  PHE A CG  1 
ATOM   285   C CD1 . PHE A 1 31  ? 28.764  -4.795  12.597  1.00 51.02  ? 31  PHE A CD1 1 
ATOM   286   C CD2 . PHE A 1 31  ? 29.194  -2.485  12.220  1.00 48.50  ? 31  PHE A CD2 1 
ATOM   287   C CE1 . PHE A 1 31  ? 29.468  -4.739  13.779  1.00 57.79  ? 31  PHE A CE1 1 
ATOM   288   C CE2 . PHE A 1 31  ? 29.899  -2.421  13.402  1.00 53.26  ? 31  PHE A CE2 1 
ATOM   289   C CZ  . PHE A 1 31  ? 30.039  -3.550  14.185  1.00 58.17  ? 31  PHE A CZ  1 
ATOM   290   N N   . PHE A 1 32  ? 26.072  -1.120  10.793  1.00 47.61  ? 32  PHE A N   1 
ATOM   291   C CA  . PHE A 1 32  ? 25.963  0.145   11.518  1.00 50.70  ? 32  PHE A CA  1 
ATOM   292   C C   . PHE A 1 32  ? 24.529  0.421   11.953  1.00 55.03  ? 32  PHE A C   1 
ATOM   293   O O   . PHE A 1 32  ? 24.297  1.015   13.016  1.00 53.55  ? 32  PHE A O   1 
ATOM   294   C CB  . PHE A 1 32  ? 26.491  1.298   10.666  1.00 51.40  ? 32  PHE A CB  1 
ATOM   295   C CG  . PHE A 1 32  ? 27.991  1.391   10.633  1.00 54.89  ? 32  PHE A CG  1 
ATOM   296   C CD1 . PHE A 1 32  ? 28.718  1.517   11.807  1.00 42.45  ? 32  PHE A CD1 1 
ATOM   297   C CD2 . PHE A 1 32  ? 28.673  1.366   9.424   1.00 51.58  ? 32  PHE A CD2 1 
ATOM   298   C CE1 . PHE A 1 32  ? 30.097  1.609   11.775  1.00 50.77  ? 32  PHE A CE1 1 
ATOM   299   C CE2 . PHE A 1 32  ? 30.053  1.460   9.389   1.00 50.19  ? 32  PHE A CE2 1 
ATOM   300   C CZ  . PHE A 1 32  ? 30.765  1.582   10.569  1.00 53.38  ? 32  PHE A CZ  1 
ATOM   301   N N   . HIS A 1 33  ? 23.556  0.008   11.143  1.00 53.00  ? 33  HIS A N   1 
ATOM   302   C CA  . HIS A 1 33  ? 22.158  0.194   11.499  1.00 49.82  ? 33  HIS A CA  1 
ATOM   303   C C   . HIS A 1 33  ? 21.669  -0.865  12.482  1.00 49.40  ? 33  HIS A C   1 
ATOM   304   O O   . HIS A 1 33  ? 20.706  -0.617  13.218  1.00 45.50  ? 33  HIS A O   1 
ATOM   305   C CB  . HIS A 1 33  ? 21.308  0.209   10.227  1.00 43.81  ? 33  HIS A CB  1 
ATOM   306   C CG  . HIS A 1 33  ? 21.282  1.540   9.544   1.00 43.01  ? 33  HIS A CG  1 
ATOM   307   N ND1 . HIS A 1 33  ? 20.682  2.650   10.104  1.00 51.21  ? 33  HIS A ND1 1 
ATOM   308   C CD2 . HIS A 1 33  ? 21.789  1.946   8.356   1.00 39.55  ? 33  HIS A CD2 1 
ATOM   309   C CE1 . HIS A 1 33  ? 20.816  3.680   9.288   1.00 48.17  ? 33  HIS A CE1 1 
ATOM   310   N NE2 . HIS A 1 33  ? 21.483  3.280   8.220   1.00 48.75  ? 33  HIS A NE2 1 
ATOM   311   N N   . ALA A 1 34  ? 22.332  -2.023  12.537  1.00 44.20  ? 34  ALA A N   1 
ATOM   312   C CA  . ALA A 1 34  ? 21.979  -3.021  13.541  1.00 50.21  ? 34  ALA A CA  1 
ATOM   313   C C   . ALA A 1 34  ? 22.486  -2.622  14.922  1.00 56.85  ? 34  ALA A C   1 
ATOM   314   O O   . ALA A 1 34  ? 21.762  -2.753  15.918  1.00 49.95  ? 34  ALA A O   1 
ATOM   315   C CB  . ALA A 1 34  ? 22.520  -4.396  13.139  1.00 42.62  ? 34  ALA A CB  1 
ATOM   316   N N   . VAL A 1 35  ? 23.720  -2.119  15.008  1.00 52.43  ? 35  VAL A N   1 
ATOM   317   C CA  . VAL A 1 35  ? 24.249  -1.716  16.306  1.00 53.23  ? 35  VAL A CA  1 
ATOM   318   C C   . VAL A 1 35  ? 23.621  -0.428  16.813  1.00 52.05  ? 35  VAL A C   1 
ATOM   319   O O   . VAL A 1 35  ? 23.939  0.008   17.924  1.00 57.85  ? 35  VAL A O   1 
ATOM   320   C CB  . VAL A 1 35  ? 25.780  -1.550  16.247  1.00 48.52  ? 35  VAL A CB  1 
ATOM   321   C CG1 . VAL A 1 35  ? 26.426  -2.885  15.990  1.00 50.69  ? 35  VAL A CG1 1 
ATOM   322   C CG2 . VAL A 1 35  ? 26.173  -0.538  15.192  1.00 47.94  ? 35  VAL A CG2 1 
ATOM   323   N N   . LYS A 1 36  ? 22.739  0.192   16.032  1.00 47.80  ? 36  LYS A N   1 
ATOM   324   C CA  . LYS A 1 36  ? 22.183  1.500   16.366  1.00 51.51  ? 36  LYS A CA  1 
ATOM   325   C C   . LYS A 1 36  ? 20.671  1.497   16.487  1.00 55.00  ? 36  LYS A C   1 
ATOM   326   O O   . LYS A 1 36  ? 20.128  2.190   17.355  1.00 58.51  ? 36  LYS A O   1 
ATOM   327   C CB  . LYS A 1 36  ? 22.609  2.546   15.313  1.00 49.51  ? 36  LYS A CB  1 
ATOM   328   C CG  . LYS A 1 36  ? 22.168  3.979   15.622  1.00 44.73  ? 36  LYS A CG  1 
ATOM   329   C CD  . LYS A 1 36  ? 22.713  5.014   14.621  1.00 49.16  ? 36  LYS A CD  1 
ATOM   330   C CE  . LYS A 1 36  ? 21.983  4.969   13.272  1.00 49.31  ? 36  LYS A CE  1 
ATOM   331   N NZ  . LYS A 1 36  ? 20.637  5.610   13.266  1.00 45.11  ? 36  LYS A NZ  1 
ATOM   332   N N   . ASP A 1 37  ? 19.971  0.734   15.645  1.00 58.11  ? 37  ASP A N   1 
ATOM   333   C CA  . ASP A 1 37  ? 18.516  0.808   15.614  1.00 50.87  ? 37  ASP A CA  1 
ATOM   334   C C   . ASP A 1 37  ? 17.836  -0.561  15.645  1.00 53.34  ? 37  ASP A C   1 
ATOM   335   O O   . ASP A 1 37  ? 16.766  -0.695  16.246  1.00 59.55  ? 37  ASP A O   1 
ATOM   336   C CB  . ASP A 1 37  ? 18.065  1.596   14.379  1.00 58.66  ? 37  ASP A CB  1 
ATOM   337   C CG  . ASP A 1 37  ? 18.950  2.813   14.093  1.00 57.04  ? 37  ASP A CG  1 
ATOM   338   O OD1 . ASP A 1 37  ? 18.799  3.844   14.790  1.00 59.23  ? 37  ASP A OD1 1 
ATOM   339   O OD2 . ASP A 1 37  ? 19.789  2.741   13.166  1.00 43.38  ? 37  ASP A OD2 1 
ATOM   340   N N   . TYR A 1 38  ? 18.434  -1.590  15.030  1.00 47.60  ? 38  TYR A N   1 
ATOM   341   C CA  . TYR A 1 38  ? 17.701  -2.843  14.838  1.00 42.47  ? 38  TYR A CA  1 
ATOM   342   C C   . TYR A 1 38  ? 17.419  -3.539  16.162  1.00 45.80  ? 38  TYR A C   1 
ATOM   343   O O   . TYR A 1 38  ? 16.322  -4.070  16.369  1.00 50.00  ? 38  TYR A O   1 
ATOM   344   C CB  . TYR A 1 38  ? 18.445  -3.775  13.880  1.00 44.91  ? 38  TYR A CB  1 
ATOM   345   C CG  . TYR A 1 38  ? 18.423  -3.277  12.442  1.00 47.62  ? 38  TYR A CG  1 
ATOM   346   C CD1 . TYR A 1 38  ? 17.419  -2.429  12.005  1.00 42.72  ? 38  TYR A CD1 1 
ATOM   347   C CD2 . TYR A 1 38  ? 19.408  -3.644  11.530  1.00 43.46  ? 38  TYR A CD2 1 
ATOM   348   C CE1 . TYR A 1 38  ? 17.398  -1.958  10.706  1.00 54.81  ? 38  TYR A CE1 1 
ATOM   349   C CE2 . TYR A 1 38  ? 19.395  -3.172  10.232  1.00 42.12  ? 38  TYR A CE2 1 
ATOM   350   C CZ  . TYR A 1 38  ? 18.386  -2.331  9.819   1.00 51.04  ? 38  TYR A CZ  1 
ATOM   351   O OH  . TYR A 1 38  ? 18.363  -1.862  8.518   1.00 50.49  ? 38  TYR A OH  1 
ATOM   352   N N   . TYR A 1 39  ? 18.379  -3.525  17.083  1.00 47.40  ? 39  TYR A N   1 
ATOM   353   C CA  . TYR A 1 39  ? 18.080  -4.012  18.425  1.00 46.62  ? 39  TYR A CA  1 
ATOM   354   C C   . TYR A 1 39  ? 17.424  -2.943  19.291  1.00 52.82  ? 39  TYR A C   1 
ATOM   355   O O   . TYR A 1 39  ? 16.615  -3.275  20.167  1.00 51.69  ? 39  TYR A O   1 
ATOM   356   C CB  . TYR A 1 39  ? 19.351  -4.518  19.103  1.00 45.96  ? 39  TYR A CB  1 
ATOM   357   C CG  . TYR A 1 39  ? 19.203  -4.868  20.573  1.00 51.65  ? 39  TYR A CG  1 
ATOM   358   C CD1 . TYR A 1 39  ? 19.395  -3.911  21.564  1.00 48.78  ? 39  TYR A CD1 1 
ATOM   359   C CD2 . TYR A 1 39  ? 18.897  -6.166  20.969  1.00 48.50  ? 39  TYR A CD2 1 
ATOM   360   C CE1 . TYR A 1 39  ? 19.269  -4.237  22.918  1.00 50.24  ? 39  TYR A CE1 1 
ATOM   361   C CE2 . TYR A 1 39  ? 18.774  -6.499  22.308  1.00 46.08  ? 39  TYR A CE2 1 
ATOM   362   C CZ  . TYR A 1 39  ? 18.960  -5.534  23.280  1.00 49.27  ? 39  TYR A CZ  1 
ATOM   363   O OH  . TYR A 1 39  ? 18.835  -5.871  24.611  1.00 50.39  ? 39  TYR A OH  1 
ATOM   364   N N   . ASP A 1 40  ? 17.749  -1.666  19.066  1.00 54.69  ? 40  ASP A N   1 
ATOM   365   C CA  . ASP A 1 40  ? 17.388  -0.629  20.030  1.00 56.04  ? 40  ASP A CA  1 
ATOM   366   C C   . ASP A 1 40  ? 15.947  -0.149  19.873  1.00 53.97  ? 40  ASP A C   1 
ATOM   367   O O   . ASP A 1 40  ? 15.320  0.236   20.868  1.00 47.85  ? 40  ASP A O   1 
ATOM   368   C CB  . ASP A 1 40  ? 18.370  0.546   19.928  1.00 54.09  ? 40  ASP A CB  1 
ATOM   369   C CG  . ASP A 1 40  ? 19.561  0.409   20.888  1.00 55.95  ? 40  ASP A CG  1 
ATOM   370   O OD1 . ASP A 1 40  ? 19.389  0.684   22.095  1.00 59.71  ? 40  ASP A OD1 1 
ATOM   371   O OD2 . ASP A 1 40  ? 20.669  0.029   20.440  1.00 54.05  ? 40  ASP A OD2 1 
ATOM   372   N N   . MET A 1 41  ? 15.403  -0.180  18.654  1.00 57.44  ? 41  MET A N   1 
ATOM   373   C CA  . MET A 1 41  ? 13.995  0.164   18.457  1.00 52.26  ? 41  MET A CA  1 
ATOM   374   C C   . MET A 1 41  ? 13.047  -0.738  19.241  1.00 49.90  ? 41  MET A C   1 
ATOM   375   O O   . MET A 1 41  ? 12.161  -0.204  19.931  1.00 50.26  ? 41  MET A O   1 
ATOM   376   C CB  . MET A 1 41  ? 13.672  0.164   16.959  1.00 48.75  ? 41  MET A CB  1 
ATOM   377   C CG  . MET A 1 41  ? 14.410  1.243   16.180  1.00 56.19  ? 41  MET A CG  1 
ATOM   378   S SD  . MET A 1 41  ? 14.035  2.927   16.719  1.00 71.24  ? 41  MET A SD  1 
ATOM   379   C CE  . MET A 1 41  ? 12.425  3.172   15.978  1.00 41.22  ? 41  MET A CE  1 
ATOM   380   N N   . PRO A 1 42  ? 13.155  -2.075  19.194  1.00 51.22  ? 42  PRO A N   1 
ATOM   381   C CA  . PRO A 1 42  ? 12.273  -2.891  20.044  1.00 49.12  ? 42  PRO A CA  1 
ATOM   382   C C   . PRO A 1 42  ? 12.647  -2.818  21.503  1.00 48.64  ? 42  PRO A C   1 
ATOM   383   O O   . PRO A 1 42  ? 11.773  -2.962  22.367  1.00 50.37  ? 42  PRO A O   1 
ATOM   384   C CB  . PRO A 1 42  ? 12.455  -4.318  19.503  1.00 48.13  ? 42  PRO A CB  1 
ATOM   385   C CG  . PRO A 1 42  ? 13.225  -4.176  18.238  1.00 52.73  ? 42  PRO A CG  1 
ATOM   386   C CD  . PRO A 1 42  ? 14.024  -2.926  18.365  1.00 54.18  ? 42  PRO A CD  1 
ATOM   387   N N   . ALA A 1 43  ? 13.926  -2.595  21.804  1.00 49.98  ? 43  ALA A N   1 
ATOM   388   C CA  . ALA A 1 43  ? 14.353  -2.498  23.192  1.00 51.29  ? 43  ALA A CA  1 
ATOM   389   C C   . ALA A 1 43  ? 13.652  -1.365  23.922  1.00 49.71  ? 43  ALA A C   1 
ATOM   390   O O   . ALA A 1 43  ? 13.677  -1.331  25.156  1.00 55.12  ? 43  ALA A O   1 
ATOM   391   C CB  . ALA A 1 43  ? 15.865  -2.312  23.260  1.00 46.04  ? 43  ALA A CB  1 
ATOM   392   N N   . TYR A 1 44  ? 13.036  -0.436  23.186  1.00 46.68  ? 44  TYR A N   1 
ATOM   393   C CA  . TYR A 1 44  ? 12.264  0.620   23.827  1.00 54.37  ? 44  TYR A CA  1 
ATOM   394   C C   . TYR A 1 44  ? 11.062  0.043   24.562  1.00 54.40  ? 44  TYR A C   1 
ATOM   395   O O   . TYR A 1 44  ? 10.675  0.538   25.628  1.00 52.40  ? 44  TYR A O   1 
ATOM   396   C CB  . TYR A 1 44  ? 11.812  1.644   22.789  1.00 53.52  ? 44  TYR A CB  1 
ATOM   397   C CG  . TYR A 1 44  ? 12.832  2.709   22.452  1.00 58.27  ? 44  TYR A CG  1 
ATOM   398   C CD1 . TYR A 1 44  ? 12.984  3.821   23.269  1.00 59.31  ? 44  TYR A CD1 1 
ATOM   399   C CD2 . TYR A 1 44  ? 13.628  2.618   21.313  1.00 54.01  ? 44  TYR A CD2 1 
ATOM   400   C CE1 . TYR A 1 44  ? 13.889  4.802   22.973  1.00 51.74  ? 44  TYR A CE1 1 
ATOM   401   C CE2 . TYR A 1 44  ? 14.548  3.608   21.007  1.00 46.49  ? 44  TYR A CE2 1 
ATOM   402   C CZ  . TYR A 1 44  ? 14.668  4.698   21.846  1.00 45.27  ? 44  TYR A CZ  1 
ATOM   403   O OH  . TYR A 1 44  ? 15.566  5.703   21.581  1.00 50.40  ? 44  TYR A OH  1 
ATOM   404   N N   . LEU A 1 45  ? 10.470  -1.021  24.013  1.00 50.96  ? 45  LEU A N   1 
ATOM   405   C CA  . LEU A 1 45  ? 9.284   -1.620  24.613  1.00 53.01  ? 45  LEU A CA  1 
ATOM   406   C C   . LEU A 1 45  ? 9.571   -2.231  25.977  1.00 53.01  ? 45  LEU A C   1 
ATOM   407   O O   . LEU A 1 45  ? 8.633   -2.485  26.742  1.00 62.02  ? 45  LEU A O   1 
ATOM   408   C CB  . LEU A 1 45  ? 8.697   -2.679  23.677  1.00 51.56  ? 45  LEU A CB  1 
ATOM   409   C CG  . LEU A 1 45  ? 8.193   -2.165  22.326  1.00 43.53  ? 45  LEU A CG  1 
ATOM   410   C CD1 . LEU A 1 45  ? 8.025   -3.325  21.374  1.00 42.96  ? 45  LEU A CD1 1 
ATOM   411   C CD2 . LEU A 1 45  ? 6.889   -1.413  22.485  1.00 46.84  ? 45  LEU A CD2 1 
ATOM   412   N N   . LYS A 1 46  ? 10.840  -2.470  26.303  1.00 53.80  ? 46  LYS A N   1 
ATOM   413   C CA  . LYS A 1 46  ? 11.183  -2.936  27.640  1.00 58.53  ? 46  LYS A CA  1 
ATOM   414   C C   . LYS A 1 46  ? 11.146  -1.820  28.672  1.00 54.79  ? 46  LYS A C   1 
ATOM   415   O O   . LYS A 1 46  ? 11.054  -2.107  29.870  1.00 61.42  ? 46  LYS A O   1 
ATOM   416   C CB  . LYS A 1 46  ? 12.569  -3.581  27.639  1.00 53.89  ? 46  LYS A CB  1 
ATOM   417   C CG  . LYS A 1 46  ? 12.782  -4.555  26.503  1.00 57.27  ? 46  LYS A CG  1 
ATOM   418   C CD  . LYS A 1 46  ? 13.575  -5.767  26.953  1.00 67.00  ? 46  LYS A CD  1 
ATOM   419   C CE  . LYS A 1 46  ? 15.004  -5.714  26.433  1.00 72.28  ? 46  LYS A CE  1 
ATOM   420   N NZ  . LYS A 1 46  ? 15.605  -7.075  26.317  1.00 77.81  ? 46  LYS A NZ  1 
ATOM   421   N N   . ASP A 1 47  ? 11.209  -0.562  28.241  1.00 57.34  ? 47  ASP A N   1 
ATOM   422   C CA  . ASP A 1 47  ? 11.253  0.568   29.158  1.00 63.56  ? 47  ASP A CA  1 
ATOM   423   C C   . ASP A 1 47  ? 10.058  1.499   29.020  1.00 59.21  ? 47  ASP A C   1 
ATOM   424   O O   . ASP A 1 47  ? 9.964   2.479   29.768  1.00 64.30  ? 47  ASP A O   1 
ATOM   425   C CB  . ASP A 1 47  ? 12.555  1.366   28.963  1.00 60.34  ? 47  ASP A CB  1 
ATOM   426   C CG  . ASP A 1 47  ? 13.790  0.586   29.390  1.00 65.20  ? 47  ASP A CG  1 
ATOM   427   O OD1 . ASP A 1 47  ? 13.730  -0.116  30.422  1.00 76.34  ? 47  ASP A OD1 1 
ATOM   428   O OD2 . ASP A 1 47  ? 14.818  0.667   28.685  1.00 65.22  ? 47  ASP A OD2 1 
ATOM   429   N N   . PHE A 1 48  ? 9.140   1.225   28.098  1.00 54.09  ? 48  PHE A N   1 
ATOM   430   C CA  . PHE A 1 48  ? 7.952   2.050   27.938  1.00 57.68  ? 48  PHE A CA  1 
ATOM   431   C C   . PHE A 1 48  ? 6.752   1.146   27.708  1.00 56.80  ? 48  PHE A C   1 
ATOM   432   O O   . PHE A 1 48  ? 6.798   0.253   26.857  1.00 60.63  ? 48  PHE A O   1 
ATOM   433   C CB  . PHE A 1 48  ? 8.121   3.045   26.781  1.00 60.70  ? 48  PHE A CB  1 
ATOM   434   C CG  . PHE A 1 48  ? 9.268   4.006   26.974  1.00 50.06  ? 48  PHE A CG  1 
ATOM   435   C CD1 . PHE A 1 48  ? 9.123   5.124   27.774  1.00 49.75  ? 48  PHE A CD1 1 
ATOM   436   C CD2 . PHE A 1 48  ? 10.487  3.785   26.358  1.00 52.55  ? 48  PHE A CD2 1 
ATOM   437   C CE1 . PHE A 1 48  ? 10.171  6.004   27.955  1.00 45.79  ? 48  PHE A CE1 1 
ATOM   438   C CE2 . PHE A 1 48  ? 11.539  4.664   26.537  1.00 54.46  ? 48  PHE A CE2 1 
ATOM   439   C CZ  . PHE A 1 48  ? 11.377  5.777   27.341  1.00 42.17  ? 48  PHE A CZ  1 
ATOM   440   N N   . GLU A 1 49  ? 5.686   1.378   28.476  1.00 62.56  ? 49  GLU A N   1 
ATOM   441   C CA  . GLU A 1 49  ? 4.486   0.539   28.439  1.00 59.57  ? 49  GLU A CA  1 
ATOM   442   C C   . GLU A 1 49  ? 3.577   0.944   27.276  1.00 48.63  ? 49  GLU A C   1 
ATOM   443   O O   . GLU A 1 49  ? 2.454   1.413   27.443  1.00 61.78  ? 49  GLU A O   1 
ATOM   444   C CB  . GLU A 1 49  ? 3.747   0.625   29.770  1.00 61.26  ? 49  GLU A CB  1 
ATOM   445   C CG  . GLU A 1 49  ? 4.091   -0.482  30.766  1.00 67.49  ? 49  GLU A CG  1 
ATOM   446   C CD  . GLU A 1 49  ? 5.585   -0.772  30.849  1.00 85.14  ? 49  GLU A CD  1 
ATOM   447   O OE1 . GLU A 1 49  ? 6.007   -1.879  30.446  1.00 88.96  ? 49  GLU A OE1 1 
ATOM   448   O OE2 . GLU A 1 49  ? 6.339   0.107   31.323  1.00 85.68  ? 49  GLU A OE2 1 
ATOM   449   N N   . ILE A 1 50  ? 4.091   0.751   26.069  1.00 50.64  ? 50  ILE A N   1 
ATOM   450   C CA  . ILE A 1 50  ? 3.375   1.093   24.851  1.00 49.13  ? 50  ILE A CA  1 
ATOM   451   C C   . ILE A 1 50  ? 3.484   -0.088  23.892  1.00 49.75  ? 50  ILE A C   1 
ATOM   452   O O   . ILE A 1 50  ? 4.144   -1.088  24.178  1.00 46.95  ? 50  ILE A O   1 
ATOM   453   C CB  . ILE A 1 50  ? 3.907   2.403   24.221  1.00 52.74  ? 50  ILE A CB  1 
ATOM   454   C CG1 . ILE A 1 50  ? 5.339   2.249   23.706  1.00 46.44  ? 50  ILE A CG1 1 
ATOM   455   C CG2 . ILE A 1 50  ? 3.799   3.600   25.172  1.00 55.92  ? 50  ILE A CG2 1 
ATOM   456   C CD1 . ILE A 1 50  ? 5.523   2.966   22.405  1.00 44.85  ? 50  ILE A CD1 1 
ATOM   457   N N   . LYS A 1 51  ? 2.796   0.017   22.757  1.00 50.03  ? 51  LYS A N   1 
ATOM   458   C CA  . LYS A 1 51  ? 2.810   -1.034  21.745  1.00 44.89  ? 51  LYS A CA  1 
ATOM   459   C C   . LYS A 1 51  ? 3.454   -0.493  20.481  1.00 47.84  ? 51  LYS A C   1 
ATOM   460   O O   . LYS A 1 51  ? 2.991   0.511   19.930  1.00 50.23  ? 51  LYS A O   1 
ATOM   461   C CB  . LYS A 1 51  ? 1.403   -1.550  21.446  1.00 37.85  ? 51  LYS A CB  1 
ATOM   462   C CG  . LYS A 1 51  ? 1.044   -2.791  22.254  1.00 40.28  ? 51  LYS A CG  1 
ATOM   463   C CD  . LYS A 1 51  ? 0.737   -2.447  23.692  1.00 47.28  ? 51  LYS A CD  1 
ATOM   464   C CE  . LYS A 1 51  ? -0.293  -3.386  24.292  1.00 53.60  ? 51  LYS A CE  1 
ATOM   465   N NZ  . LYS A 1 51  ? 0.158   -4.795  24.257  1.00 60.31  ? 51  LYS A NZ  1 
ATOM   466   N N   . LEU A 1 52  ? 4.511   -1.165  20.021  1.00 44.40  ? 52  LEU A N   1 
ATOM   467   C CA  . LEU A 1 52  ? 5.178   -0.848  18.765  1.00 48.23  ? 52  LEU A CA  1 
ATOM   468   C C   . LEU A 1 52  ? 5.220   -2.086  17.880  1.00 46.46  ? 52  LEU A C   1 
ATOM   469   O O   . LEU A 1 52  ? 5.362   -3.207  18.374  1.00 53.68  ? 52  LEU A O   1 
ATOM   470   C CB  . LEU A 1 52  ? 6.598   -0.347  19.004  1.00 44.39  ? 52  LEU A CB  1 
ATOM   471   C CG  . LEU A 1 52  ? 6.707   0.974   19.757  1.00 47.73  ? 52  LEU A CG  1 
ATOM   472   C CD1 . LEU A 1 52  ? 8.136   1.227   20.222  1.00 51.27  ? 52  LEU A CD1 1 
ATOM   473   C CD2 . LEU A 1 52  ? 6.225   2.101   18.880  1.00 47.89  ? 52  LEU A CD2 1 
ATOM   474   N N   . ASN A 1 53  ? 5.130   -1.878  16.571  1.00 40.96  ? 53  ASN A N   1 
ATOM   475   C CA  . ASN A 1 53  ? 5.143   -2.962  15.599  1.00 45.75  ? 53  ASN A CA  1 
ATOM   476   C C   . ASN A 1 53  ? 6.265   -2.765  14.593  1.00 50.32  ? 53  ASN A C   1 
ATOM   477   O O   . ASN A 1 53  ? 6.546   -1.639  14.165  1.00 51.79  ? 53  ASN A O   1 
ATOM   478   C CB  . ASN A 1 53  ? 3.819   -3.049  14.861  1.00 48.60  ? 53  ASN A CB  1 
ATOM   479   C CG  . ASN A 1 53  ? 2.653   -3.086  15.800  1.00 44.63  ? 53  ASN A CG  1 
ATOM   480   O OD1 . ASN A 1 53  ? 2.355   -4.122  16.389  1.00 49.05  ? 53  ASN A OD1 1 
ATOM   481   N ND2 . ASN A 1 53  ? 1.998   -1.946  15.974  1.00 44.57  ? 53  ASN A ND2 1 
ATOM   482   N N   . PHE A 1 54  ? 6.888   -3.870  14.198  1.00 47.64  ? 54  PHE A N   1 
ATOM   483   C CA  . PHE A 1 54  ? 8.081   -3.818  13.375  1.00 42.27  ? 54  PHE A CA  1 
ATOM   484   C C   . PHE A 1 54  ? 7.939   -4.733  12.178  1.00 39.93  ? 54  PHE A C   1 
ATOM   485   O O   . PHE A 1 54  ? 7.305   -5.788  12.251  1.00 44.93  ? 54  PHE A O   1 
ATOM   486   C CB  . PHE A 1 54  ? 9.317   -4.215  14.167  1.00 46.56  ? 54  PHE A CB  1 
ATOM   487   C CG  . PHE A 1 54  ? 9.539   -3.380  15.386  1.00 49.78  ? 54  PHE A CG  1 
ATOM   488   C CD1 . PHE A 1 54  ? 10.125  -2.132  15.281  1.00 49.35  ? 54  PHE A CD1 1 
ATOM   489   C CD2 . PHE A 1 54  ? 9.174   -3.845  16.633  1.00 40.54  ? 54  PHE A CD2 1 
ATOM   490   C CE1 . PHE A 1 54  ? 10.335  -1.358  16.396  1.00 49.23  ? 54  PHE A CE1 1 
ATOM   491   C CE2 . PHE A 1 54  ? 9.385   -3.076  17.754  1.00 51.31  ? 54  PHE A CE2 1 
ATOM   492   C CZ  . PHE A 1 54  ? 9.965   -1.828  17.637  1.00 47.76  ? 54  PHE A CZ  1 
ATOM   493   N N   . ASN A 1 55  ? 8.553   -4.318  11.076  1.00 43.74  ? 55  ASN A N   1 
ATOM   494   C CA  . ASN A 1 55  ? 8.628   -5.125  9.868   1.00 45.18  ? 55  ASN A CA  1 
ATOM   495   C C   . ASN A 1 55  ? 10.084  -5.436  9.583   1.00 39.68  ? 55  ASN A C   1 
ATOM   496   O O   . ASN A 1 55  ? 10.916  -4.527  9.524   1.00 45.51  ? 55  ASN A O   1 
ATOM   497   C CB  . ASN A 1 55  ? 8.014   -4.418  8.663   1.00 42.92  ? 55  ASN A CB  1 
ATOM   498   C CG  . ASN A 1 55  ? 8.133   -5.242  7.399   1.00 48.72  ? 55  ASN A CG  1 
ATOM   499   O OD1 . ASN A 1 55  ? 7.190   -5.930  7.014   1.00 49.79  ? 55  ASN A OD1 1 
ATOM   500   N ND2 . ASN A 1 55  ? 9.291   -5.176  6.740   1.00 45.58  ? 55  ASN A ND2 1 
ATOM   501   N N   . LEU A 1 56  ? 10.381  -6.712  9.381   1.00 42.54  ? 56  LEU A N   1 
ATOM   502   C CA  . LEU A 1 56  ? 11.727  -7.173  9.077   1.00 37.91  ? 56  LEU A CA  1 
ATOM   503   C C   . LEU A 1 56  ? 11.710  -7.861  7.721   1.00 40.67  ? 56  LEU A C   1 
ATOM   504   O O   . LEU A 1 56  ? 10.892  -8.757  7.488   1.00 40.17  ? 56  LEU A O   1 
ATOM   505   C CB  . LEU A 1 56  ? 12.218  -8.123  10.171  1.00 42.98  ? 56  LEU A CB  1 
ATOM   506   C CG  . LEU A 1 56  ? 12.137  -7.627  11.626  1.00 41.18  ? 56  LEU A CG  1 
ATOM   507   C CD1 . LEU A 1 56  ? 12.893  -8.563  12.546  1.00 42.00  ? 56  LEU A CD1 1 
ATOM   508   C CD2 . LEU A 1 56  ? 12.682  -6.205  11.793  1.00 38.90  ? 56  LEU A CD2 1 
ATOM   509   N N   . THR A 1 57  ? 12.591  -7.432  6.822   1.00 43.59  ? 57  THR A N   1 
ATOM   510   C CA  . THR A 1 57  ? 12.652  -8.160  5.566   1.00 42.19  ? 57  THR A CA  1 
ATOM   511   C C   . THR A 1 57  ? 13.491  -9.423  5.735   1.00 39.61  ? 57  THR A C   1 
ATOM   512   O O   . THR A 1 57  ? 14.376  -9.478  6.591   1.00 40.67  ? 57  THR A O   1 
ATOM   513   C CB  . THR A 1 57  ? 13.236  -7.297  4.448   1.00 45.74  ? 57  THR A CB  1 
ATOM   514   O OG1 . THR A 1 57  ? 14.597  -6.957  4.745   1.00 47.30  ? 57  THR A OG1 1 
ATOM   515   C CG2 . THR A 1 57  ? 12.407  -6.038  4.245   1.00 37.54  ? 57  THR A CG2 1 
ATOM   516   N N   . PRO A 1 58  ? 13.214  -10.457 4.940   1.00 48.37  ? 58  PRO A N   1 
ATOM   517   C CA  . PRO A 1 58  ? 14.032  -11.677 5.022   1.00 48.76  ? 58  PRO A CA  1 
ATOM   518   C C   . PRO A 1 58  ? 15.492  -11.452 4.680   1.00 46.17  ? 58  PRO A C   1 
ATOM   519   O O   . PRO A 1 58  ? 16.373  -12.026 5.333   1.00 50.12  ? 58  PRO A O   1 
ATOM   520   C CB  . PRO A 1 58  ? 13.346  -12.604 4.011   1.00 57.49  ? 58  PRO A CB  1 
ATOM   521   C CG  . PRO A 1 58  ? 11.918  -12.114 3.993   1.00 53.48  ? 58  PRO A CG  1 
ATOM   522   C CD  . PRO A 1 58  ? 12.062  -10.628 4.039   1.00 45.18  ? 58  PRO A CD  1 
ATOM   523   N N   . VAL A 1 59  ? 15.778  -10.625 3.673   1.00 41.27  ? 59  VAL A N   1 
ATOM   524   C CA  . VAL A 1 59  ? 17.169  -10.399 3.294   1.00 48.38  ? 59  VAL A CA  1 
ATOM   525   C C   . VAL A 1 59  ? 17.921  -9.678  4.408   1.00 44.03  ? 59  VAL A C   1 
ATOM   526   O O   . VAL A 1 59  ? 19.120  -9.907  4.605   1.00 42.55  ? 59  VAL A O   1 
ATOM   527   C CB  . VAL A 1 59  ? 17.235  -9.645  1.946   1.00 40.89  ? 59  VAL A CB  1 
ATOM   528   C CG1 . VAL A 1 59  ? 16.578  -8.286  2.054   1.00 46.63  ? 59  VAL A CG1 1 
ATOM   529   C CG2 . VAL A 1 59  ? 18.672  -9.512  1.486   1.00 46.02  ? 59  VAL A CG2 1 
ATOM   530   N N   . LEU A 1 60  ? 17.235  -8.816  5.169   1.00 41.27  ? 60  LEU A N   1 
ATOM   531   C CA  . LEU A 1 60  ? 17.853  -8.243  6.362   1.00 47.45  ? 60  LEU A CA  1 
ATOM   532   C C   . LEU A 1 60  ? 18.105  -9.313  7.417   1.00 47.03  ? 60  LEU A C   1 
ATOM   533   O O   . LEU A 1 60  ? 19.169  -9.333  8.050   1.00 45.32  ? 60  LEU A O   1 
ATOM   534   C CB  . LEU A 1 60  ? 16.986  -7.120  6.935   1.00 42.87  ? 60  LEU A CB  1 
ATOM   535   C CG  . LEU A 1 60  ? 17.560  -6.398  8.163   1.00 39.39  ? 60  LEU A CG  1 
ATOM   536   C CD1 . LEU A 1 60  ? 18.897  -5.727  7.859   1.00 43.16  ? 60  LEU A CD1 1 
ATOM   537   C CD2 . LEU A 1 60  ? 16.572  -5.368  8.678   1.00 39.40  ? 60  LEU A CD2 1 
ATOM   538   N N   . ILE A 1 61  ? 17.147  -10.225 7.600   1.00 39.52  ? 61  ILE A N   1 
ATOM   539   C CA  . ILE A 1 61  ? 17.322  -11.313 8.555   1.00 47.74  ? 61  ILE A CA  1 
ATOM   540   C C   . ILE A 1 61  ? 18.556  -12.134 8.209   1.00 51.40  ? 61  ILE A C   1 
ATOM   541   O O   . ILE A 1 61  ? 19.356  -12.479 9.088   1.00 53.73  ? 61  ILE A O   1 
ATOM   542   C CB  . ILE A 1 61  ? 16.055  -12.186 8.598   1.00 55.93  ? 61  ILE A CB  1 
ATOM   543   C CG1 . ILE A 1 61  ? 15.040  -11.589 9.573   1.00 51.41  ? 61  ILE A CG1 1 
ATOM   544   C CG2 . ILE A 1 61  ? 16.405  -13.612 8.980   1.00 50.22  ? 61  ILE A CG2 1 
ATOM   545   C CD1 . ILE A 1 61  ? 13.732  -12.328 9.614   1.00 46.34  ? 61  ILE A CD1 1 
ATOM   546   N N   . ASP A 1 62  ? 18.737  -12.445 6.922   1.00 50.41  ? 62  ASP A N   1 
ATOM   547   C CA  . ASP A 1 62  ? 19.879  -13.248 6.494   1.00 47.23  ? 62  ASP A CA  1 
ATOM   548   C C   . ASP A 1 62  ? 21.200  -12.565 6.819   1.00 54.49  ? 62  ASP A C   1 
ATOM   549   O O   . ASP A 1 62  ? 22.163  -13.226 7.228   1.00 57.08  ? 62  ASP A O   1 
ATOM   550   C CB  . ASP A 1 62  ? 19.795  -13.518 4.994   1.00 51.43  ? 62  ASP A CB  1 
ATOM   551   C CG  . ASP A 1 62  ? 18.616  -14.393 4.616   1.00 63.51  ? 62  ASP A CG  1 
ATOM   552   O OD1 . ASP A 1 62  ? 18.064  -15.093 5.496   1.00 70.30  ? 62  ASP A OD1 1 
ATOM   553   O OD2 . ASP A 1 62  ? 18.253  -14.390 3.421   1.00 64.57  ? 62  ASP A OD2 1 
ATOM   554   N N   . GLN A 1 63  ? 21.272  -11.244 6.628   1.00 46.39  ? 63  GLN A N   1 
ATOM   555   C CA  . GLN A 1 63  ? 22.537  -10.547 6.828   1.00 49.26  ? 63  GLN A CA  1 
ATOM   556   C C   . GLN A 1 63  ? 22.895  -10.457 8.306   1.00 51.50  ? 63  GLN A C   1 
ATOM   557   O O   . GLN A 1 63  ? 24.054  -10.671 8.680   1.00 48.03  ? 63  GLN A O   1 
ATOM   558   C CB  . GLN A 1 63  ? 22.477  -9.162  6.185   1.00 49.51  ? 63  GLN A CB  1 
ATOM   559   C CG  . GLN A 1 63  ? 22.396  -9.222  4.671   1.00 50.42  ? 63  GLN A CG  1 
ATOM   560   C CD  . GLN A 1 63  ? 22.232  -7.857  4.039   1.00 54.57  ? 63  GLN A CD  1 
ATOM   561   O OE1 . GLN A 1 63  ? 23.168  -7.056  4.009   1.00 56.91  ? 63  GLN A OE1 1 
ATOM   562   N NE2 . GLN A 1 63  ? 21.038  -7.582  3.530   1.00 50.33  ? 63  GLN A NE2 1 
ATOM   563   N N   . ILE A 1 64  ? 21.908  -10.162 9.158   1.00 48.80  ? 64  ILE A N   1 
ATOM   564   C CA  . ILE A 1 64  ? 22.147  -10.062 10.597  1.00 48.74  ? 64  ILE A CA  1 
ATOM   565   C C   . ILE A 1 64  ? 22.618  -11.395 11.161  1.00 49.74  ? 64  ILE A C   1 
ATOM   566   O O   . ILE A 1 64  ? 23.482  -11.440 12.045  1.00 50.64  ? 64  ILE A O   1 
ATOM   567   C CB  . ILE A 1 64  ? 20.877  -9.574  11.317  1.00 50.09  ? 64  ILE A CB  1 
ATOM   568   C CG1 . ILE A 1 64  ? 20.535  -8.157  10.875  1.00 53.39  ? 64  ILE A CG1 1 
ATOM   569   C CG2 . ILE A 1 64  ? 21.067  -9.604  12.820  1.00 49.07  ? 64  ILE A CG2 1 
ATOM   570   C CD1 . ILE A 1 64  ? 19.266  -7.624  11.492  1.00 44.63  ? 64  ILE A CD1 1 
ATOM   571   N N   . GLN A 1 65  ? 22.040  -12.499 10.684  1.00 48.80  ? 65  GLN A N   1 
ATOM   572   C CA  . GLN A 1 65  ? 22.460  -13.806 11.177  1.00 52.89  ? 65  GLN A CA  1 
ATOM   573   C C   . GLN A 1 65  ? 23.885  -14.118 10.754  1.00 56.09  ? 65  GLN A C   1 
ATOM   574   O O   . GLN A 1 65  ? 24.638  -14.739 11.513  1.00 59.65  ? 65  GLN A O   1 
ATOM   575   C CB  . GLN A 1 65  ? 21.520  -14.901 10.684  1.00 49.66  ? 65  GLN A CB  1 
ATOM   576   C CG  . GLN A 1 65  ? 20.107  -14.788 11.200  1.00 49.27  ? 65  GLN A CG  1 
ATOM   577   C CD  . GLN A 1 65  ? 19.161  -15.748 10.509  1.00 57.83  ? 65  GLN A CD  1 
ATOM   578   O OE1 . GLN A 1 65  ? 18.918  -15.649 9.303   1.00 61.03  ? 65  GLN A OE1 1 
ATOM   579   N NE2 . GLN A 1 65  ? 18.635  -16.700 11.270  1.00 56.24  ? 65  GLN A NE2 1 
ATOM   580   N N   . GLU A 1 66  ? 24.268  -13.709 9.541   1.00 54.27  ? 66  GLU A N   1 
ATOM   581   C CA  . GLU A 1 66  ? 25.646  -13.908 9.103   1.00 57.20  ? 66  GLU A CA  1 
ATOM   582   C C   . GLU A 1 66  ? 26.605  -13.070 9.932   1.00 54.11  ? 66  GLU A C   1 
ATOM   583   O O   . GLU A 1 66  ? 27.675  -13.547 10.327  1.00 55.51  ? 66  GLU A O   1 
ATOM   584   C CB  . GLU A 1 66  ? 25.792  -13.573 7.618   1.00 55.77  ? 66  GLU A CB  1 
ATOM   585   C CG  . GLU A 1 66  ? 27.222  -13.688 7.112   1.00 62.01  ? 66  GLU A CG  1 
ATOM   586   C CD  . GLU A 1 66  ? 27.318  -14.189 5.683   1.00 62.18  ? 66  GLU A CD  1 
ATOM   587   O OE1 . GLU A 1 66  ? 26.269  -14.295 5.022   1.00 65.76  ? 66  GLU A OE1 1 
ATOM   588   O OE2 . GLU A 1 66  ? 28.443  -14.479 5.220   1.00 68.60  ? 66  GLU A OE2 1 
ATOM   589   N N   . TYR A 1 67  ? 26.227  -11.823 10.217  1.00 46.00  ? 67  TYR A N   1 
ATOM   590   C CA  . TYR A 1 67  ? 27.039  -10.990 11.088  1.00 47.44  ? 67  TYR A CA  1 
ATOM   591   C C   . TYR A 1 67  ? 27.079  -11.544 12.507  1.00 52.10  ? 67  TYR A C   1 
ATOM   592   O O   . TYR A 1 67  ? 28.103  -11.431 13.186  1.00 58.23  ? 67  TYR A O   1 
ATOM   593   C CB  . TYR A 1 67  ? 26.504  -9.564  11.090  1.00 44.60  ? 67  TYR A CB  1 
ATOM   594   C CG  . TYR A 1 67  ? 27.050  -8.676  9.999   1.00 50.19  ? 67  TYR A CG  1 
ATOM   595   C CD1 . TYR A 1 67  ? 28.290  -8.055  10.127  1.00 47.38  ? 67  TYR A CD1 1 
ATOM   596   C CD2 . TYR A 1 67  ? 26.313  -8.429  8.854   1.00 49.98  ? 67  TYR A CD2 1 
ATOM   597   C CE1 . TYR A 1 67  ? 28.775  -7.228  9.135   1.00 46.75  ? 67  TYR A CE1 1 
ATOM   598   C CE2 . TYR A 1 67  ? 26.791  -7.607  7.860   1.00 49.36  ? 67  TYR A CE2 1 
ATOM   599   C CZ  . TYR A 1 67  ? 28.016  -7.008  8.000   1.00 51.28  ? 67  TYR A CZ  1 
ATOM   600   O OH  . TYR A 1 67  ? 28.460  -6.191  6.983   1.00 56.19  ? 67  TYR A OH  1 
ATOM   601   N N   . ALA A 1 68  ? 25.985  -12.149 12.970  1.00 60.02  ? 68  ALA A N   1 
ATOM   602   C CA  . ALA A 1 68  ? 25.954  -12.726 14.308  1.00 58.35  ? 68  ALA A CA  1 
ATOM   603   C C   . ALA A 1 68  ? 26.714  -14.041 14.391  1.00 58.66  ? 68  ALA A C   1 
ATOM   604   O O   . ALA A 1 68  ? 27.113  -14.439 15.490  1.00 60.61  ? 68  ALA A O   1 
ATOM   605   C CB  . ALA A 1 68  ? 24.506  -12.936 14.759  1.00 49.45  ? 68  ALA A CB  1 
ATOM   606   N N   . GLN A 1 69  ? 26.913  -14.716 13.257  1.00 62.39  ? 69  GLN A N   1 
ATOM   607   C CA  . GLN A 1 69  ? 27.674  -15.956 13.169  1.00 63.17  ? 69  GLN A CA  1 
ATOM   608   C C   . GLN A 1 69  ? 29.138  -15.718 12.821  1.00 70.82  ? 69  GLN A C   1 
ATOM   609   O O   . GLN A 1 69  ? 29.881  -16.685 12.623  1.00 73.92  ? 69  GLN A O   1 
ATOM   610   C CB  . GLN A 1 69  ? 27.046  -16.889 12.129  1.00 67.66  ? 69  GLN A CB  1 
ATOM   611   C CG  . GLN A 1 69  ? 25.826  -17.645 12.625  1.00 70.91  ? 69  GLN A CG  1 
ATOM   612   C CD  . GLN A 1 69  ? 24.915  -18.089 11.498  1.00 76.60  ? 69  GLN A CD  1 
ATOM   613   O OE1 . GLN A 1 69  ? 25.377  -18.546 10.452  1.00 74.90  ? 69  GLN A OE1 1 
ATOM   614   N NE2 . GLN A 1 69  ? 23.611  -17.944 11.703  1.00 75.73  ? 69  GLN A NE2 1 
ATOM   615   N N   . GLY A 1 70  ? 29.564  -14.459 12.727  1.00 70.35  ? 70  GLY A N   1 
ATOM   616   C CA  . GLY A 1 70  ? 30.949  -14.149 12.429  1.00 68.55  ? 70  GLY A CA  1 
ATOM   617   C C   . GLY A 1 70  ? 31.392  -14.497 11.030  1.00 69.36  ? 70  GLY A C   1 
ATOM   618   O O   . GLY A 1 70  ? 32.595  -14.605 10.780  1.00 78.40  ? 70  GLY A O   1 
ATOM   619   N N   . LYS A 1 71  ? 30.453  -14.669 10.102  1.00 72.52  ? 71  LYS A N   1 
ATOM   620   C CA  . LYS A 1 71  ? 30.785  -15.071 8.744   1.00 73.96  ? 71  LYS A CA  1 
ATOM   621   C C   . LYS A 1 71  ? 30.779  -13.916 7.751   1.00 62.27  ? 71  LYS A C   1 
ATOM   622   O O   . LYS A 1 71  ? 31.282  -14.081 6.635   1.00 70.54  ? 71  LYS A O   1 
ATOM   623   C CB  . LYS A 1 71  ? 29.815  -16.160 8.262   1.00 69.06  ? 71  LYS A CB  1 
ATOM   624   C CG  . LYS A 1 71  ? 29.484  -17.231 9.311   1.00 76.65  ? 71  LYS A CG  1 
ATOM   625   C CD  . LYS A 1 71  ? 30.522  -18.354 9.364   1.00 86.70  ? 71  LYS A CD  1 
ATOM   626   C CE  . LYS A 1 71  ? 31.604  -18.090 10.409  1.00 84.53  ? 71  LYS A CE  1 
ATOM   627   N NZ  . LYS A 1 71  ? 32.231  -19.348 10.906  1.00 84.33  ? 71  LYS A NZ  1 
ATOM   628   N N   . ALA A 1 72  ? 30.239  -12.759 8.119   1.00 63.37  ? 72  ALA A N   1 
ATOM   629   C CA  . ALA A 1 72  ? 30.172  -11.649 7.178   1.00 62.39  ? 72  ALA A CA  1 
ATOM   630   C C   . ALA A 1 72  ? 31.565  -11.068 6.976   1.00 61.99  ? 72  ALA A C   1 
ATOM   631   O O   . ALA A 1 72  ? 32.218  -10.653 7.939   1.00 66.33  ? 72  ALA A O   1 
ATOM   632   C CB  . ALA A 1 72  ? 29.201  -10.582 7.681   1.00 55.56  ? 72  ALA A CB  1 
ATOM   633   N N   . LYS A 1 73  ? 32.034  -11.063 5.730   1.00 62.36  ? 73  LYS A N   1 
ATOM   634   C CA  . LYS A 1 73  ? 33.350  -10.515 5.411   1.00 62.37  ? 73  LYS A CA  1 
ATOM   635   C C   . LYS A 1 73  ? 33.207  -9.052  4.992   1.00 65.05  ? 73  LYS A C   1 
ATOM   636   O O   . LYS A 1 73  ? 33.354  -8.684  3.826   1.00 70.19  ? 73  LYS A O   1 
ATOM   637   C CB  . LYS A 1 73  ? 34.029  -11.355 4.329   1.00 61.94  ? 73  LYS A CB  1 
ATOM   638   C CG  . LYS A 1 73  ? 34.311  -12.797 4.744   1.00 62.04  ? 73  LYS A CG  1 
ATOM   639   C CD  . LYS A 1 73  ? 34.103  -13.769 3.581   1.00 73.15  ? 73  LYS A CD  1 
ATOM   640   C CE  . LYS A 1 73  ? 33.603  -15.130 4.071   1.00 78.46  ? 73  LYS A CE  1 
ATOM   641   N NZ  . LYS A 1 73  ? 32.318  -15.555 3.433   1.00 72.67  ? 73  LYS A NZ  1 
ATOM   642   N N   . ASP A 1 74  ? 32.912  -8.213  5.984   1.00 57.34  ? 74  ASP A N   1 
ATOM   643   C CA  . ASP A 1 74  ? 32.762  -6.779  5.763   1.00 50.07  ? 74  ASP A CA  1 
ATOM   644   C C   . ASP A 1 74  ? 34.122  -6.129  5.530   1.00 53.93  ? 74  ASP A C   1 
ATOM   645   O O   . ASP A 1 74  ? 34.973  -6.129  6.423   1.00 62.41  ? 74  ASP A O   1 
ATOM   646   C CB  . ASP A 1 74  ? 32.071  -6.148  6.963   1.00 51.97  ? 74  ASP A CB  1 
ATOM   647   C CG  . ASP A 1 74  ? 31.653  -4.722  6.708   1.00 59.64  ? 74  ASP A CG  1 
ATOM   648   O OD1 . ASP A 1 74  ? 32.535  -3.854  6.516   1.00 56.43  ? 74  ASP A OD1 1 
ATOM   649   O OD2 . ASP A 1 74  ? 30.430  -4.472  6.685   1.00 60.84  ? 74  ASP A OD2 1 
ATOM   650   N N   . VAL A 1 75  ? 34.323  -5.551  4.343   1.00 59.54  ? 75  VAL A N   1 
ATOM   651   C CA  . VAL A 1 75  ? 35.631  -4.983  4.020   1.00 58.55  ? 75  VAL A CA  1 
ATOM   652   C C   . VAL A 1 75  ? 35.874  -3.702  4.805   1.00 51.95  ? 75  VAL A C   1 
ATOM   653   O O   . VAL A 1 75  ? 36.988  -3.453  5.277   1.00 60.82  ? 75  VAL A O   1 
ATOM   654   C CB  . VAL A 1 75  ? 35.772  -4.749  2.504   1.00 60.13  ? 75  VAL A CB  1 
ATOM   655   C CG1 . VAL A 1 75  ? 36.504  -5.914  1.859   1.00 62.71  ? 75  VAL A CG1 1 
ATOM   656   C CG2 . VAL A 1 75  ? 34.411  -4.543  1.852   1.00 54.41  ? 75  VAL A CG2 1 
ATOM   657   N N   . PHE A 1 76  ? 34.842  -2.871  4.958   1.00 52.65  ? 76  PHE A N   1 
ATOM   658   C CA  . PHE A 1 76  ? 34.993  -1.632  5.711   1.00 52.57  ? 76  PHE A CA  1 
ATOM   659   C C   . PHE A 1 76  ? 35.253  -1.909  7.186   1.00 55.37  ? 76  PHE A C   1 
ATOM   660   O O   . PHE A 1 76  ? 36.116  -1.271  7.801   1.00 59.12  ? 76  PHE A O   1 
ATOM   661   C CB  . PHE A 1 76  ? 33.750  -0.766  5.539   1.00 58.01  ? 76  PHE A CB  1 
ATOM   662   C CG  . PHE A 1 76  ? 33.923  0.628   6.038   1.00 55.67  ? 76  PHE A CG  1 
ATOM   663   C CD1 . PHE A 1 76  ? 34.552  1.583   5.258   1.00 60.81  ? 76  PHE A CD1 1 
ATOM   664   C CD2 . PHE A 1 76  ? 33.465  0.983   7.291   1.00 48.74  ? 76  PHE A CD2 1 
ATOM   665   C CE1 . PHE A 1 76  ? 34.714  2.871   5.721   1.00 66.82  ? 76  PHE A CE1 1 
ATOM   666   C CE2 . PHE A 1 76  ? 33.623  2.261   7.761   1.00 57.61  ? 76  PHE A CE2 1 
ATOM   667   C CZ  . PHE A 1 76  ? 34.250  3.209   6.977   1.00 68.05  ? 76  PHE A CZ  1 
ATOM   668   N N   . LEU A 1 77  ? 34.522  -2.862  7.771   1.00 56.35  ? 77  LEU A N   1 
ATOM   669   C CA  . LEU A 1 77  ? 34.735  -3.193  9.175   1.00 54.11  ? 77  LEU A CA  1 
ATOM   670   C C   . LEU A 1 77  ? 36.138  -3.726  9.421   1.00 61.52  ? 77  LEU A C   1 
ATOM   671   O O   . LEU A 1 77  ? 36.705  -3.507  10.500  1.00 63.17  ? 77  LEU A O   1 
ATOM   672   C CB  . LEU A 1 77  ? 33.695  -4.209  9.635   1.00 53.27  ? 77  LEU A CB  1 
ATOM   673   C CG  . LEU A 1 77  ? 32.670  -3.656  10.621  1.00 60.47  ? 77  LEU A CG  1 
ATOM   674   C CD1 . LEU A 1 77  ? 32.021  -4.818  11.331  1.00 62.03  ? 77  LEU A CD1 1 
ATOM   675   C CD2 . LEU A 1 77  ? 33.304  -2.680  11.622  1.00 53.79  ? 77  LEU A CD2 1 
ATOM   676   N N   . GLU A 1 78  ? 36.716  -4.425  8.439   1.00 59.67  ? 78  GLU A N   1 
ATOM   677   C CA  . GLU A 1 78  ? 38.093  -4.882  8.579   1.00 60.77  ? 78  GLU A CA  1 
ATOM   678   C C   . GLU A 1 78  ? 39.067  -3.711  8.623   1.00 60.43  ? 78  GLU A C   1 
ATOM   679   O O   . GLU A 1 78  ? 40.076  -3.777  9.336   1.00 59.20  ? 78  GLU A O   1 
ATOM   680   C CB  . GLU A 1 78  ? 38.448  -5.837  7.439   1.00 60.36  ? 78  GLU A CB  1 
ATOM   681   C CG  . GLU A 1 78  ? 39.669  -6.735  7.700   1.00 70.44  ? 78  GLU A CG  1 
ATOM   682   C CD  . GLU A 1 78  ? 39.751  -7.313  9.119   1.00 80.12  ? 78  GLU A CD  1 
ATOM   683   O OE1 . GLU A 1 78  ? 40.883  -7.426  9.641   1.00 66.03  ? 78  GLU A OE1 1 
ATOM   684   O OE2 . GLU A 1 78  ? 38.707  -7.700  9.695   1.00 84.20  ? 78  GLU A OE2 1 
ATOM   685   N N   . ALA A 1 79  ? 38.778  -2.633  7.884   1.00 53.62  ? 79  ALA A N   1 
ATOM   686   C CA  . ALA A 1 79  ? 39.589  -1.424  7.981   1.00 57.64  ? 79  ALA A CA  1 
ATOM   687   C C   . ALA A 1 79  ? 39.491  -0.806  9.368   1.00 63.12  ? 79  ALA A C   1 
ATOM   688   O O   . ALA A 1 79  ? 40.474  -0.258  9.880   1.00 62.66  ? 79  ALA A O   1 
ATOM   689   C CB  . ALA A 1 79  ? 39.158  -0.415  6.923   1.00 56.26  ? 79  ALA A CB  1 
ATOM   690   N N   . ILE A 1 80  ? 38.311  -0.874  9.989   1.00 54.37  ? 80  ILE A N   1 
ATOM   691   C CA  . ILE A 1 80  ? 38.176  -0.395  11.361  1.00 56.94  ? 80  ILE A CA  1 
ATOM   692   C C   . ILE A 1 80  ? 38.914  -1.320  12.324  1.00 58.34  ? 80  ILE A C   1 
ATOM   693   O O   . ILE A 1 80  ? 39.604  -0.860  13.241  1.00 58.29  ? 80  ILE A O   1 
ATOM   694   C CB  . ILE A 1 80  ? 36.689  -0.251  11.732  1.00 54.98  ? 80  ILE A CB  1 
ATOM   695   C CG1 . ILE A 1 80  ? 35.965  0.615   10.695  1.00 56.45  ? 80  ILE A CG1 1 
ATOM   696   C CG2 . ILE A 1 80  ? 36.534  0.330   13.129  1.00 57.42  ? 80  ILE A CG2 1 
ATOM   697   C CD1 . ILE A 1 80  ? 36.048  2.112   10.966  1.00 52.19  ? 80  ILE A CD1 1 
ATOM   698   N N   . ARG A 1 81  ? 38.810  -2.634  12.107  1.00 56.63  ? 81  ARG A N   1 
ATOM   699   C CA  . ARG A 1 81  ? 39.316  -3.605  13.073  1.00 56.21  ? 81  ARG A CA  1 
ATOM   700   C C   . ARG A 1 81  ? 40.840  -3.567  13.160  1.00 63.35  ? 81  ARG A C   1 
ATOM   701   O O   . ARG A 1 81  ? 41.406  -3.621  14.259  1.00 60.76  ? 81  ARG A O   1 
ATOM   702   C CB  . ARG A 1 81  ? 38.814  -5.005  12.695  1.00 60.11  ? 81  ARG A CB  1 
ATOM   703   C CG  . ARG A 1 81  ? 39.154  -6.132  13.677  1.00 67.08  ? 81  ARG A CG  1 
ATOM   704   C CD  . ARG A 1 81  ? 40.545  -6.702  13.344  1.00 79.82  ? 81  ARG A CD  1 
ATOM   705   N NE  . ARG A 1 81  ? 41.140  -7.676  14.260  1.00 92.43  ? 81  ARG A NE  1 
ATOM   706   C CZ  . ARG A 1 81  ? 41.213  -7.565  15.583  1.00 94.98  ? 81  ARG A CZ  1 
ATOM   707   N NH1 . ARG A 1 81  ? 40.539  -6.635  16.247  1.00 91.85  ? 81  ARG A NH1 1 
ATOM   708   N NH2 . ARG A 1 81  ? 42.006  -8.395  16.261  1.00 89.10  ? 81  ARG A NH2 1 
ATOM   709   N N   . LYS A 1 82  ? 41.515  -3.472  12.016  1.00 64.02  ? 82  LYS A N   1 
ATOM   710   C CA  . LYS A 1 82  ? 42.965  -3.610  11.963  1.00 54.43  ? 82  LYS A CA  1 
ATOM   711   C C   . LYS A 1 82  ? 43.673  -2.469  12.677  1.00 60.93  ? 82  LYS A C   1 
ATOM   712   O O   . LYS A 1 82  ? 43.172  -1.345  12.749  1.00 67.38  ? 82  LYS A O   1 
ATOM   713   C CB  . LYS A 1 82  ? 43.444  -3.634  10.518  1.00 58.36  ? 82  LYS A CB  1 
ATOM   714   C CG  . LYS A 1 82  ? 43.658  -5.010  9.948   1.00 71.44  ? 82  LYS A CG  1 
ATOM   715   C CD  . LYS A 1 82  ? 43.788  -4.963  8.432   1.00 67.01  ? 82  LYS A CD  1 
ATOM   716   C CE  . LYS A 1 82  ? 43.940  -3.538  7.915   1.00 57.45  ? 82  LYS A CE  1 
ATOM   717   N NZ  . LYS A 1 82  ? 44.402  -3.507  6.501   1.00 62.01  ? 82  LYS A NZ  1 
ATOM   718   N N   . ASP A 1 83  ? 44.865  -2.764  13.183  1.00 64.49  ? 83  ASP A N   1 
ATOM   719   C CA  . ASP A 1 83  ? 45.740  -1.703  13.647  1.00 60.13  ? 83  ASP A CA  1 
ATOM   720   C C   . ASP A 1 83  ? 46.031  -0.752  12.490  1.00 61.66  ? 83  ASP A C   1 
ATOM   721   O O   . ASP A 1 83  ? 46.254  -1.205  11.362  1.00 65.81  ? 83  ASP A O   1 
ATOM   722   C CB  . ASP A 1 83  ? 47.050  -2.277  14.185  1.00 62.34  ? 83  ASP A CB  1 
ATOM   723   C CG  . ASP A 1 83  ? 47.903  -1.228  14.855  1.00 64.97  ? 83  ASP A CG  1 
ATOM   724   O OD1 . ASP A 1 83  ? 48.707  -0.582  14.157  1.00 68.94  ? 83  ASP A OD1 1 
ATOM   725   O OD2 . ASP A 1 83  ? 47.758  -1.039  16.079  1.00 67.73  ? 83  ASP A OD2 1 
ATOM   726   N N   . PRO A 1 84  ? 46.034  0.563   12.727  1.00 62.32  ? 84  PRO A N   1 
ATOM   727   C CA  . PRO A 1 84  ? 46.298  1.507   11.629  1.00 61.78  ? 84  PRO A CA  1 
ATOM   728   C C   . PRO A 1 84  ? 47.665  1.341   10.984  1.00 61.96  ? 84  PRO A C   1 
ATOM   729   O O   . PRO A 1 84  ? 47.875  1.847   9.875   1.00 67.61  ? 84  PRO A O   1 
ATOM   730   C CB  . PRO A 1 84  ? 46.162  2.873   12.311  1.00 58.20  ? 84  PRO A CB  1 
ATOM   731   C CG  . PRO A 1 84  ? 45.268  2.609   13.488  1.00 56.77  ? 84  PRO A CG  1 
ATOM   732   C CD  . PRO A 1 84  ? 45.720  1.266   13.981  1.00 58.47  ? 84  PRO A CD  1 
ATOM   733   N N   . ASP A 1 85  ? 48.602  0.650   11.630  1.00 59.57  ? 85  ASP A N   1 
ATOM   734   C CA  . ASP A 1 85  ? 49.885  0.395   10.989  1.00 62.28  ? 85  ASP A CA  1 
ATOM   735   C C   . ASP A 1 85  ? 49.775  -0.639  9.879   1.00 62.71  ? 85  ASP A C   1 
ATOM   736   O O   . ASP A 1 85  ? 50.666  -0.711  9.028   1.00 68.44  ? 85  ASP A O   1 
ATOM   737   C CB  . ASP A 1 85  ? 50.912  -0.072  12.016  1.00 65.60  ? 85  ASP A CB  1 
ATOM   738   C CG  . ASP A 1 85  ? 51.497  1.069   12.824  1.00 67.04  ? 85  ASP A CG  1 
ATOM   739   O OD1 . ASP A 1 85  ? 51.566  2.211   12.315  1.00 63.14  ? 85  ASP A OD1 1 
ATOM   740   O OD2 . ASP A 1 85  ? 51.886  0.812   13.982  1.00 72.50  ? 85  ASP A OD2 1 
ATOM   741   N N   . ASP A 1 86  ? 48.719  -1.447  9.875   1.00 62.84  ? 86  ASP A N   1 
ATOM   742   C CA  . ASP A 1 86  ? 48.502  -2.438  8.830   1.00 65.76  ? 86  ASP A CA  1 
ATOM   743   C C   . ASP A 1 86  ? 47.575  -1.935  7.736   1.00 63.05  ? 86  ASP A C   1 
ATOM   744   O O   . ASP A 1 86  ? 47.107  -2.735  6.921   1.00 64.75  ? 86  ASP A O   1 
ATOM   745   C CB  . ASP A 1 86  ? 47.939  -3.729  9.434   1.00 65.50  ? 86  ASP A CB  1 
ATOM   746   C CG  . ASP A 1 86  ? 48.990  -4.533  10.177  1.00 69.33  ? 86  ASP A CG  1 
ATOM   747   O OD1 . ASP A 1 86  ? 49.965  -4.984  9.535   1.00 68.87  ? 86  ASP A OD1 1 
ATOM   748   O OD2 . ASP A 1 86  ? 48.842  -4.704  11.404  1.00 66.24  ? 86  ASP A OD2 1 
ATOM   749   N N   . LEU A 1 87  ? 47.317  -0.632  7.686   1.00 62.26  ? 87  LEU A N   1 
ATOM   750   C CA  . LEU A 1 87  ? 46.289  -0.067  6.824   1.00 64.55  ? 87  LEU A CA  1 
ATOM   751   C C   . LEU A 1 87  ? 46.908  0.460   5.533   1.00 68.66  ? 87  LEU A C   1 
ATOM   752   O O   . LEU A 1 87  ? 47.761  1.354   5.568   1.00 68.56  ? 87  LEU A O   1 
ATOM   753   C CB  . LEU A 1 87  ? 45.548  1.051   7.549   1.00 59.94  ? 87  LEU A CB  1 
ATOM   754   C CG  . LEU A 1 87  ? 44.304  0.638   8.316   1.00 57.25  ? 87  LEU A CG  1 
ATOM   755   C CD1 . LEU A 1 87  ? 43.740  1.853   9.001   1.00 57.36  ? 87  LEU A CD1 1 
ATOM   756   C CD2 . LEU A 1 87  ? 43.309  0.059   7.358   1.00 59.68  ? 87  LEU A CD2 1 
ATOM   757   N N   . GLU A 1 88  ? 46.460  -0.080  4.400   1.00 69.15  ? 88  GLU A N   1 
ATOM   758   C CA  . GLU A 1 88  ? 46.847  0.441   3.098   1.00 65.83  ? 88  GLU A CA  1 
ATOM   759   C C   . GLU A 1 88  ? 46.200  1.803   2.859   1.00 64.18  ? 88  GLU A C   1 
ATOM   760   O O   . GLU A 1 88  ? 45.222  2.177   3.512   1.00 70.72  ? 88  GLU A O   1 
ATOM   761   C CB  . GLU A 1 88  ? 46.442  -0.524  1.982   1.00 67.15  ? 88  GLU A CB  1 
ATOM   762   C CG  . GLU A 1 88  ? 47.011  -1.925  2.130   1.00 67.92  ? 88  GLU A CG  1 
ATOM   763   C CD  . GLU A 1 88  ? 48.430  -1.925  2.656   1.00 76.56  ? 88  GLU A CD  1 
ATOM   764   O OE1 . GLU A 1 88  ? 49.330  -1.390  1.968   1.00 80.65  ? 88  GLU A OE1 1 
ATOM   765   O OE2 . GLU A 1 88  ? 48.640  -2.457  3.769   1.00 75.69  ? 88  GLU A OE2 1 
ATOM   766   N N   . LYS A 1 89  ? 46.754  2.546   1.894   1.00 62.79  ? 89  LYS A N   1 
ATOM   767   C CA  . LYS A 1 89  ? 46.296  3.911   1.650   1.00 63.36  ? 89  LYS A CA  1 
ATOM   768   C C   . LYS A 1 89  ? 44.840  3.931   1.206   1.00 67.26  ? 89  LYS A C   1 
ATOM   769   O O   . LYS A 1 89  ? 44.089  4.852   1.544   1.00 68.57  ? 89  LYS A O   1 
ATOM   770   C CB  . LYS A 1 89  ? 47.179  4.595   0.603   1.00 59.21  ? 89  LYS A CB  1 
ATOM   771   C CG  . LYS A 1 89  ? 48.626  4.804   1.021   1.00 70.73  ? 89  LYS A CG  1 
ATOM   772   C CD  . LYS A 1 89  ? 49.120  6.186   0.616   1.00 73.59  ? 89  LYS A CD  1 
ATOM   773   C CE  . LYS A 1 89  ? 48.900  7.215   1.724   1.00 84.31  ? 89  LYS A CE  1 
ATOM   774   N NZ  . LYS A 1 89  ? 50.154  7.565   2.462   1.00 78.01  ? 89  LYS A NZ  1 
ATOM   775   N N   . GLU A 1 90  ? 44.424  2.926   0.435   1.00 65.00  ? 90  GLU A N   1 
ATOM   776   C CA  . GLU A 1 90  ? 43.055  2.902   -0.072  1.00 68.06  ? 90  GLU A CA  1 
ATOM   777   C C   . GLU A 1 90  ? 42.050  2.783   1.067   1.00 73.85  ? 90  GLU A C   1 
ATOM   778   O O   . GLU A 1 90  ? 40.996  3.434   1.054   1.00 67.06  ? 90  GLU A O   1 
ATOM   779   C CB  . GLU A 1 90  ? 42.891  1.746   -1.057  1.00 82.28  ? 90  GLU A CB  1 
ATOM   780   C CG  . GLU A 1 90  ? 43.685  0.506   -0.659  1.00 85.03  ? 90  GLU A CG  1 
ATOM   781   C CD  . GLU A 1 90  ? 44.909  0.273   -1.531  1.00 92.22  ? 90  GLU A CD  1 
ATOM   782   O OE1 . GLU A 1 90  ? 45.623  1.253   -1.838  1.00 82.48  ? 90  GLU A OE1 1 
ATOM   783   O OE2 . GLU A 1 90  ? 45.156  -0.895  -1.906  1.00 110.69 ? 90  GLU A OE2 1 
ATOM   784   N N   . GLU A 1 91  ? 42.368  1.963   2.070   1.00 69.05  ? 91  GLU A N   1 
ATOM   785   C CA  . GLU A 1 91  ? 41.479  1.810   3.213   1.00 63.18  ? 91  GLU A CA  1 
ATOM   786   C C   . GLU A 1 91  ? 41.404  3.098   4.020   1.00 57.57  ? 91  GLU A C   1 
ATOM   787   O O   . GLU A 1 91  ? 40.342  3.448   4.551   1.00 59.83  ? 91  GLU A O   1 
ATOM   788   C CB  . GLU A 1 91  ? 41.947  0.644   4.082   1.00 57.36  ? 91  GLU A CB  1 
ATOM   789   C CG  . GLU A 1 91  ? 42.504  -0.522  3.285   1.00 62.80  ? 91  GLU A CG  1 
ATOM   790   C CD  . GLU A 1 91  ? 42.965  -1.669  4.166   1.00 68.14  ? 91  GLU A CD  1 
ATOM   791   O OE1 . GLU A 1 91  ? 42.131  -2.530  4.518   1.00 60.87  ? 91  GLU A OE1 1 
ATOM   792   O OE2 . GLU A 1 91  ? 44.167  -1.709  4.509   1.00 68.12  ? 91  GLU A OE2 1 
ATOM   793   N N   . VAL A 1 92  ? 42.517  3.825   4.112   1.00 53.19  ? 92  VAL A N   1 
ATOM   794   C CA  . VAL A 1 92  ? 42.510  5.095   4.831   1.00 60.80  ? 92  VAL A CA  1 
ATOM   795   C C   . VAL A 1 92  ? 41.644  6.116   4.104   1.00 59.11  ? 92  VAL A C   1 
ATOM   796   O O   . VAL A 1 92  ? 40.856  6.834   4.728   1.00 65.37  ? 92  VAL A O   1 
ATOM   797   C CB  . VAL A 1 92  ? 43.944  5.613   5.029   1.00 56.20  ? 92  VAL A CB  1 
ATOM   798   C CG1 . VAL A 1 92  ? 43.910  7.008   5.631   1.00 52.03  ? 92  VAL A CG1 1 
ATOM   799   C CG2 . VAL A 1 92  ? 44.732  4.662   5.911   1.00 60.22  ? 92  VAL A CG2 1 
ATOM   800   N N   . GLU A 1 93  ? 41.776  6.200   2.777   1.00 55.20  ? 93  GLU A N   1 
ATOM   801   C CA  . GLU A 1 93  ? 40.890  7.065   2.007   1.00 61.99  ? 93  GLU A CA  1 
ATOM   802   C C   . GLU A 1 93  ? 39.437  6.623   2.141   1.00 62.52  ? 93  GLU A C   1 
ATOM   803   O O   . GLU A 1 93  ? 38.531  7.464   2.134   1.00 57.50  ? 93  GLU A O   1 
ATOM   804   C CB  . GLU A 1 93  ? 41.307  7.080   0.534   1.00 65.19  ? 93  GLU A CB  1 
ATOM   805   C CG  . GLU A 1 93  ? 41.293  8.469   -0.116  1.00 77.67  ? 93  GLU A CG  1 
ATOM   806   C CD  . GLU A 1 93  ? 39.886  8.927   -0.493  1.00 92.87  ? 93  GLU A CD  1 
ATOM   807   O OE1 . GLU A 1 93  ? 39.438  9.966   0.039   1.00 92.76  ? 93  GLU A OE1 1 
ATOM   808   O OE2 . GLU A 1 93  ? 39.234  8.261   -1.332  1.00 86.10  ? 93  GLU A OE2 1 
ATOM   809   N N   . LYS A 1 94  ? 39.198  5.314   2.268   1.00 61.03  ? 94  LYS A N   1 
ATOM   810   C CA  . LYS A 1 94  ? 37.843  4.816   2.478   1.00 54.55  ? 94  LYS A CA  1 
ATOM   811   C C   . LYS A 1 94  ? 37.285  5.291   3.810   1.00 58.49  ? 94  LYS A C   1 
ATOM   812   O O   . LYS A 1 94  ? 36.108  5.654   3.909   1.00 54.02  ? 94  LYS A O   1 
ATOM   813   C CB  . LYS A 1 94  ? 37.836  3.291   2.428   1.00 59.80  ? 94  LYS A CB  1 
ATOM   814   C CG  . LYS A 1 94  ? 37.704  2.709   1.038   1.00 68.11  ? 94  LYS A CG  1 
ATOM   815   C CD  . LYS A 1 94  ? 37.470  1.198   1.079   1.00 75.81  ? 94  LYS A CD  1 
ATOM   816   C CE  . LYS A 1 94  ? 37.191  0.690   2.493   1.00 69.58  ? 94  LYS A CE  1 
ATOM   817   N NZ  . LYS A 1 94  ? 37.188  -0.799  2.583   1.00 66.75  ? 94  LYS A NZ  1 
ATOM   818   N N   . LEU A 1 95  ? 38.114  5.270   4.853   1.00 59.86  ? 95  LEU A N   1 
ATOM   819   C CA  . LEU A 1 95  ? 37.676  5.746   6.157   1.00 54.50  ? 95  LEU A CA  1 
ATOM   820   C C   . LEU A 1 95  ? 37.350  7.233   6.119   1.00 55.51  ? 95  LEU A C   1 
ATOM   821   O O   . LEU A 1 95  ? 36.336  7.672   6.674   1.00 60.18  ? 95  LEU A O   1 
ATOM   822   C CB  . LEU A 1 95  ? 38.754  5.454   7.196   1.00 61.71  ? 95  LEU A CB  1 
ATOM   823   C CG  . LEU A 1 95  ? 38.380  4.375   8.207   1.00 73.56  ? 95  LEU A CG  1 
ATOM   824   C CD1 . LEU A 1 95  ? 38.360  2.987   7.567   1.00 67.95  ? 95  LEU A CD1 1 
ATOM   825   C CD2 . LEU A 1 95  ? 39.339  4.441   9.383   1.00 61.22  ? 95  LEU A CD2 1 
ATOM   826   N N   . ILE A 1 96  ? 38.186  8.021   5.445   1.00 53.62  ? 96  ILE A N   1 
ATOM   827   C CA  . ILE A 1 96  ? 37.989  9.468   5.423   1.00 57.45  ? 96  ILE A CA  1 
ATOM   828   C C   . ILE A 1 96  ? 36.758  9.845   4.600   1.00 55.49  ? 96  ILE A C   1 
ATOM   829   O O   . ILE A 1 96  ? 36.042  10.796  4.934   1.00 50.29  ? 96  ILE A O   1 
ATOM   830   C CB  . ILE A 1 96  ? 39.261  10.164  4.909   1.00 54.91  ? 96  ILE A CB  1 
ATOM   831   C CG1 . ILE A 1 96  ? 40.476  9.685   5.704   1.00 55.73  ? 96  ILE A CG1 1 
ATOM   832   C CG2 . ILE A 1 96  ? 39.125  11.666  5.035   1.00 55.39  ? 96  ILE A CG2 1 
ATOM   833   C CD1 . ILE A 1 96  ? 41.784  10.348  5.310   1.00 55.04  ? 96  ILE A CD1 1 
ATOM   834   N N   . GLU A 1 97  ? 36.481  9.106   3.523   1.00 54.83  ? 97  GLU A N   1 
ATOM   835   C CA  . GLU A 1 97  ? 35.287  9.403   2.737   1.00 58.15  ? 97  GLU A CA  1 
ATOM   836   C C   . GLU A 1 97  ? 34.022  8.991   3.475   1.00 66.61  ? 97  GLU A C   1 
ATOM   837   O O   . GLU A 1 97  ? 32.978  9.642   3.336   1.00 65.02  ? 97  GLU A O   1 
ATOM   838   C CB  . GLU A 1 97  ? 35.351  8.716   1.375   1.00 62.29  ? 97  GLU A CB  1 
ATOM   839   C CG  . GLU A 1 97  ? 36.476  9.216   0.476   1.00 83.73  ? 97  GLU A CG  1 
ATOM   840   C CD  . GLU A 1 97  ? 36.265  10.638  -0.037  1.00 97.78  ? 97  GLU A CD  1 
ATOM   841   O OE1 . GLU A 1 97  ? 36.555  11.596  0.714   1.00 97.83  ? 97  GLU A OE1 1 
ATOM   842   O OE2 . GLU A 1 97  ? 35.804  10.798  -1.189  1.00 102.43 ? 97  GLU A OE2 1 
ATOM   843   N N   . PHE A 1 98  ? 34.092  7.928   4.273   1.00 59.81  ? 98  PHE A N   1 
ATOM   844   C CA  . PHE A 1 98  ? 32.935  7.564   5.076   1.00 54.44  ? 98  PHE A CA  1 
ATOM   845   C C   . PHE A 1 98  ? 32.648  8.632   6.121   1.00 58.90  ? 98  PHE A C   1 
ATOM   846   O O   . PHE A 1 98  ? 31.486  8.965   6.381   1.00 65.31  ? 98  PHE A O   1 
ATOM   847   C CB  . PHE A 1 98  ? 33.165  6.212   5.733   1.00 51.77  ? 98  PHE A CB  1 
ATOM   848   C CG  . PHE A 1 98  ? 31.955  5.659   6.404   1.00 59.32  ? 98  PHE A CG  1 
ATOM   849   C CD1 . PHE A 1 98  ? 30.851  5.262   5.665   1.00 58.55  ? 98  PHE A CD1 1 
ATOM   850   C CD2 . PHE A 1 98  ? 31.925  5.517   7.779   1.00 61.06  ? 98  PHE A CD2 1 
ATOM   851   C CE1 . PHE A 1 98  ? 29.736  4.738   6.292   1.00 58.80  ? 98  PHE A CE1 1 
ATOM   852   C CE2 . PHE A 1 98  ? 30.821  4.998   8.413   1.00 56.62  ? 98  PHE A CE2 1 
ATOM   853   C CZ  . PHE A 1 98  ? 29.721  4.606   7.670   1.00 65.38  ? 98  PHE A CZ  1 
ATOM   854   N N   . THR A 1 99  ? 33.697  9.193   6.719   1.00 51.95  ? 99  THR A N   1 
ATOM   855   C CA  . THR A 1 99  ? 33.501  10.265  7.683   1.00 54.87  ? 99  THR A CA  1 
ATOM   856   C C   . THR A 1 99  ? 33.033  11.543  7.005   1.00 57.97  ? 99  THR A C   1 
ATOM   857   O O   . THR A 1 99  ? 32.278  12.323  7.600   1.00 62.84  ? 99  THR A O   1 
ATOM   858   C CB  . THR A 1 99  ? 34.795  10.520  8.447   1.00 58.80  ? 99  THR A CB  1 
ATOM   859   O OG1 . THR A 1 99  ? 35.283  9.278   8.962   1.00 58.52  ? 99  THR A OG1 1 
ATOM   860   C CG2 . THR A 1 99  ? 34.553  11.490  9.599   1.00 50.50  ? 99  THR A CG2 1 
ATOM   861   N N   . LYS A 1 100 ? 33.467  11.779  5.769   1.00 54.28  ? 100 LYS A N   1 
ATOM   862   C CA  . LYS A 1 100 ? 33.031  12.983  5.076   1.00 58.98  ? 100 LYS A CA  1 
ATOM   863   C C   . LYS A 1 100 ? 31.552  12.908  4.727   1.00 54.18  ? 100 LYS A C   1 
ATOM   864   O O   . LYS A 1 100 ? 30.860  13.932  4.745   1.00 56.28  ? 100 LYS A O   1 
ATOM   865   C CB  . LYS A 1 100 ? 33.883  13.201  3.821   1.00 75.09  ? 100 LYS A CB  1 
ATOM   866   C CG  . LYS A 1 100 ? 33.603  14.502  3.064   1.00 76.75  ? 100 LYS A CG  1 
ATOM   867   C CD  . LYS A 1 100 ? 32.857  14.234  1.757   1.00 71.68  ? 100 LYS A CD  1 
ATOM   868   C CE  . LYS A 1 100 ? 32.050  15.446  1.296   1.00 73.01  ? 100 LYS A CE  1 
ATOM   869   N NZ  . LYS A 1 100 ? 31.080  15.107  0.205   1.00 66.84  ? 100 LYS A NZ  1 
ATOM   870   N N   . LEU A 1 101 ? 31.048  11.706  4.439   1.00 56.90  ? 101 LEU A N   1 
ATOM   871   C CA  . LEU A 1 101 ? 29.638  11.544  4.102   1.00 53.87  ? 101 LEU A CA  1 
ATOM   872   C C   . LEU A 1 101 ? 28.738  11.797  5.302   1.00 60.66  ? 101 LEU A C   1 
ATOM   873   O O   . LEU A 1 101 ? 27.608  12.270  5.136   1.00 58.58  ? 101 LEU A O   1 
ATOM   874   C CB  . LEU A 1 101 ? 29.398  10.140  3.546   1.00 54.85  ? 101 LEU A CB  1 
ATOM   875   C CG  . LEU A 1 101 ? 27.965  9.723   3.208   1.00 71.08  ? 101 LEU A CG  1 
ATOM   876   C CD1 . LEU A 1 101 ? 27.409  10.502  2.022   1.00 68.74  ? 101 LEU A CD1 1 
ATOM   877   C CD2 . LEU A 1 101 ? 27.900  8.223   2.949   1.00 62.51  ? 101 LEU A CD2 1 
ATOM   878   N N   . ASN A 1 102 ? 29.216  11.494  6.509   1.00 61.02  ? 102 ASN A N   1 
ATOM   879   C CA  . ASN A 1 102 ? 28.432  11.631  7.727   1.00 52.06  ? 102 ASN A CA  1 
ATOM   880   C C   . ASN A 1 102 ? 28.889  12.792  8.597   1.00 52.20  ? 102 ASN A C   1 
ATOM   881   O O   . ASN A 1 102 ? 28.407  12.930  9.723   1.00 51.52  ? 102 ASN A O   1 
ATOM   882   C CB  . ASN A 1 102 ? 28.478  10.331  8.531   1.00 50.03  ? 102 ASN A CB  1 
ATOM   883   C CG  . ASN A 1 102 ? 28.357  9.090   7.656   1.00 59.37  ? 102 ASN A CG  1 
ATOM   884   O OD1 . ASN A 1 102 ? 27.652  9.091   6.646   1.00 61.10  ? 102 ASN A OD1 1 
ATOM   885   N ND2 . ASN A 1 102 ? 29.029  8.017   8.057   1.00 58.58  ? 102 ASN A ND2 1 
ATOM   886   N N   . TYR A 1 103 ? 29.795  13.637  8.092   1.00 58.54  ? 103 TYR A N   1 
ATOM   887   C CA  . TYR A 1 103 ? 30.418  14.664  8.924   1.00 54.65  ? 103 TYR A CA  1 
ATOM   888   C C   . TYR A 1 103 ? 29.386  15.605  9.524   1.00 52.56  ? 103 TYR A C   1 
ATOM   889   O O   . TYR A 1 103 ? 29.561  16.111  10.639  1.00 57.39  ? 103 TYR A O   1 
ATOM   890   C CB  . TYR A 1 103 ? 31.427  15.454  8.097   1.00 51.36  ? 103 TYR A CB  1 
ATOM   891   C CG  . TYR A 1 103 ? 32.281  16.425  8.881   1.00 56.66  ? 103 TYR A CG  1 
ATOM   892   C CD1 . TYR A 1 103 ? 33.438  16.006  9.529   1.00 64.45  ? 103 TYR A CD1 1 
ATOM   893   C CD2 . TYR A 1 103 ? 31.946  17.769  8.945   1.00 61.56  ? 103 TYR A CD2 1 
ATOM   894   C CE1 . TYR A 1 103 ? 34.233  16.906  10.227  1.00 60.93  ? 103 TYR A CE1 1 
ATOM   895   C CE2 . TYR A 1 103 ? 32.728  18.672  9.638   1.00 69.84  ? 103 TYR A CE2 1 
ATOM   896   C CZ  . TYR A 1 103 ? 33.867  18.241  10.274  1.00 62.98  ? 103 TYR A CZ  1 
ATOM   897   O OH  . TYR A 1 103 ? 34.618  19.168  10.952  1.00 67.83  ? 103 TYR A OH  1 
ATOM   898   N N   . GLU A 1 104 ? 28.311  15.864  8.795   1.00 51.64  ? 104 GLU A N   1 
ATOM   899   C CA  . GLU A 1 104 ? 27.330  16.842  9.228   1.00 56.91  ? 104 GLU A CA  1 
ATOM   900   C C   . GLU A 1 104 ? 26.104  16.211  9.866   1.00 55.01  ? 104 GLU A C   1 
ATOM   901   O O   . GLU A 1 104 ? 25.160  16.932  10.206  1.00 58.57  ? 104 GLU A O   1 
ATOM   902   C CB  . GLU A 1 104 ? 26.919  17.726  8.053   1.00 60.98  ? 104 GLU A CB  1 
ATOM   903   C CG  . GLU A 1 104 ? 27.808  18.941  7.893   1.00 66.38  ? 104 GLU A CG  1 
ATOM   904   C CD  . GLU A 1 104 ? 28.175  19.198  6.455   1.00 83.73  ? 104 GLU A CD  1 
ATOM   905   O OE1 . GLU A 1 104 ? 27.248  19.265  5.620   1.00 105.83 ? 104 GLU A OE1 1 
ATOM   906   O OE2 . GLU A 1 104 ? 29.380  19.350  6.159   1.00 89.86  ? 104 GLU A OE2 1 
ATOM   907   N N   . LYS A 1 105 ? 26.094  14.894  10.038  1.00 52.97  ? 105 LYS A N   1 
ATOM   908   C CA  . LYS A 1 105 ? 25.004  14.300  10.794  1.00 45.44  ? 105 LYS A CA  1 
ATOM   909   C C   . LYS A 1 105 ? 25.260  14.481  12.289  1.00 47.19  ? 105 LYS A C   1 
ATOM   910   O O   . LYS A 1 105 ? 26.404  14.380  12.736  1.00 52.02  ? 105 LYS A O   1 
ATOM   911   C CB  . LYS A 1 105 ? 24.853  12.816  10.459  1.00 47.53  ? 105 LYS A CB  1 
ATOM   912   C CG  . LYS A 1 105 ? 24.437  12.550  9.016   1.00 50.23  ? 105 LYS A CG  1 
ATOM   913   C CD  . LYS A 1 105 ? 24.785  11.126  8.595   1.00 55.04  ? 105 LYS A CD  1 
ATOM   914   C CE  . LYS A 1 105 ? 24.031  10.696  7.336   1.00 50.50  ? 105 LYS A CE  1 
ATOM   915   N NZ  . LYS A 1 105 ? 24.510  9.390   6.789   1.00 51.75  ? 105 LYS A NZ  1 
ATOM   916   N N   . PRO A 1 106 ? 24.222  14.770  13.076  1.00 45.40  ? 106 PRO A N   1 
ATOM   917   C CA  . PRO A 1 106 ? 24.439  15.036  14.506  1.00 48.40  ? 106 PRO A CA  1 
ATOM   918   C C   . PRO A 1 106 ? 25.078  13.890  15.265  1.00 43.98  ? 106 PRO A C   1 
ATOM   919   O O   . PRO A 1 106 ? 25.717  14.138  16.293  1.00 45.33  ? 106 PRO A O   1 
ATOM   920   C CB  . PRO A 1 106 ? 23.023  15.330  15.018  1.00 49.40  ? 106 PRO A CB  1 
ATOM   921   C CG  . PRO A 1 106 ? 22.315  15.848  13.821  1.00 43.39  ? 106 PRO A CG  1 
ATOM   922   C CD  . PRO A 1 106 ? 22.822  15.003  12.693  1.00 41.89  ? 106 PRO A CD  1 
ATOM   923   N N   . ILE A 1 107 ? 24.946  12.646  14.801  1.00 42.02  ? 107 ILE A N   1 
ATOM   924   C CA  . ILE A 1 107 ? 25.581  11.543  15.517  1.00 46.13  ? 107 ILE A CA  1 
ATOM   925   C C   . ILE A 1 107 ? 27.091  11.507  15.331  1.00 56.35  ? 107 ILE A C   1 
ATOM   926   O O   . ILE A 1 107 ? 27.771  10.748  16.037  1.00 52.00  ? 107 ILE A O   1 
ATOM   927   C CB  . ILE A 1 107 ? 24.972  10.196  15.092  1.00 39.18  ? 107 ILE A CB  1 
ATOM   928   C CG1 . ILE A 1 107 ? 25.040  10.043  13.580  1.00 45.68  ? 107 ILE A CG1 1 
ATOM   929   C CG2 . ILE A 1 107 ? 23.542  10.081  15.564  1.00 45.57  ? 107 ILE A CG2 1 
ATOM   930   C CD1 . ILE A 1 107 ? 25.206  8.622   13.148  1.00 40.14  ? 107 ILE A CD1 1 
ATOM   931   N N   . TYR A 1 108 ? 27.637  12.299  14.401  1.00 52.37  ? 108 TYR A N   1 
ATOM   932   C CA  . TYR A 1 108 ? 29.074  12.415  14.183  1.00 47.37  ? 108 TYR A CA  1 
ATOM   933   C C   . TYR A 1 108 ? 29.654  13.676  14.809  1.00 47.98  ? 108 TYR A C   1 
ATOM   934   O O   . TYR A 1 108 ? 30.754  14.094  14.439  1.00 62.06  ? 108 TYR A O   1 
ATOM   935   C CB  . TYR A 1 108 ? 29.392  12.387  12.684  1.00 41.95  ? 108 TYR A CB  1 
ATOM   936   C CG  . TYR A 1 108 ? 29.693  11.003  12.139  1.00 49.85  ? 108 TYR A CG  1 
ATOM   937   C CD1 . TYR A 1 108 ? 28.689  10.052  12.010  1.00 47.43  ? 108 TYR A CD1 1 
ATOM   938   C CD2 . TYR A 1 108 ? 30.980  10.648  11.752  1.00 52.68  ? 108 TYR A CD2 1 
ATOM   939   C CE1 . TYR A 1 108 ? 28.960  8.784   11.518  1.00 47.74  ? 108 TYR A CE1 1 
ATOM   940   C CE2 . TYR A 1 108 ? 31.258  9.379   11.257  1.00 52.50  ? 108 TYR A CE2 1 
ATOM   941   C CZ  . TYR A 1 108 ? 30.245  8.453   11.139  1.00 44.43  ? 108 TYR A CZ  1 
ATOM   942   O OH  . TYR A 1 108 ? 30.527  7.196   10.646  1.00 50.55  ? 108 TYR A OH  1 
ATOM   943   N N   . ARG A 1 109 ? 28.937  14.299  15.745  1.00 48.11  ? 109 ARG A N   1 
ATOM   944   C CA  . ARG A 1 109 ? 29.364  15.572  16.324  1.00 50.01  ? 109 ARG A CA  1 
ATOM   945   C C   . ARG A 1 109 ? 30.304  15.298  17.493  1.00 55.92  ? 109 ARG A C   1 
ATOM   946   O O   . ARG A 1 109 ? 29.974  15.475  18.667  1.00 52.33  ? 109 ARG A O   1 
ATOM   947   C CB  . ARG A 1 109 ? 28.166  16.403  16.759  1.00 59.17  ? 109 ARG A CB  1 
ATOM   948   C CG  . ARG A 1 109 ? 28.477  17.877  17.036  1.00 65.53  ? 109 ARG A CG  1 
ATOM   949   C CD  . ARG A 1 109 ? 27.475  18.790  16.336  1.00 70.94  ? 109 ARG A CD  1 
ATOM   950   N NE  . ARG A 1 109 ? 26.132  18.640  16.880  1.00 66.84  ? 109 ARG A NE  1 
ATOM   951   C CZ  . ARG A 1 109 ? 25.017  18.732  16.168  1.00 71.90  ? 109 ARG A CZ  1 
ATOM   952   N NH1 . ARG A 1 109 ? 25.041  19.006  14.872  1.00 70.00  ? 109 ARG A NH1 1 
ATOM   953   N NH2 . ARG A 1 109 ? 23.847  18.548  16.771  1.00 72.21  ? 109 ARG A NH2 1 
ATOM   954   N N   . PHE A 1 110 ? 31.497  14.842  17.143  1.00 63.10  ? 110 PHE A N   1 
ATOM   955   C CA  . PHE A 1 110 ? 32.570  14.649  18.101  1.00 56.07  ? 110 PHE A CA  1 
ATOM   956   C C   . PHE A 1 110 ? 33.667  15.643  17.767  1.00 58.65  ? 110 PHE A C   1 
ATOM   957   O O   . PHE A 1 110 ? 34.083  15.749  16.608  1.00 61.77  ? 110 PHE A O   1 
ATOM   958   C CB  . PHE A 1 110 ? 33.111  13.219  18.062  1.00 53.01  ? 110 PHE A CB  1 
ATOM   959   C CG  . PHE A 1 110 ? 32.140  12.171  18.547  1.00 52.36  ? 110 PHE A CG  1 
ATOM   960   C CD1 . PHE A 1 110 ? 31.237  11.577  17.675  1.00 50.06  ? 110 PHE A CD1 1 
ATOM   961   C CD2 . PHE A 1 110 ? 32.141  11.768  19.876  1.00 50.17  ? 110 PHE A CD2 1 
ATOM   962   C CE1 . PHE A 1 110 ? 30.362  10.602  18.118  1.00 47.67  ? 110 PHE A CE1 1 
ATOM   963   C CE2 . PHE A 1 110 ? 31.260  10.792  20.326  1.00 43.65  ? 110 PHE A CE2 1 
ATOM   964   C CZ  . PHE A 1 110 ? 30.371  10.210  19.445  1.00 43.39  ? 110 PHE A CZ  1 
ATOM   965   N N   . GLU A 1 111 ? 34.112  16.381  18.782  1.00 58.25  ? 111 GLU A N   1 
ATOM   966   C CA  . GLU A 1 111 ? 35.128  17.405  18.574  1.00 65.39  ? 111 GLU A CA  1 
ATOM   967   C C   . GLU A 1 111 ? 36.378  16.826  17.926  1.00 64.80  ? 111 GLU A C   1 
ATOM   968   O O   . GLU A 1 111 ? 37.026  17.487  17.105  1.00 72.06  ? 111 GLU A O   1 
ATOM   969   C CB  . GLU A 1 111 ? 35.465  18.064  19.908  1.00 71.37  ? 111 GLU A CB  1 
ATOM   970   C CG  . GLU A 1 111 ? 36.247  19.341  19.768  1.00 75.55  ? 111 GLU A CG  1 
ATOM   971   C CD  . GLU A 1 111 ? 35.455  20.420  19.070  1.00 89.32  ? 111 GLU A CD  1 
ATOM   972   O OE1 . GLU A 1 111 ? 34.269  20.634  19.421  1.00 96.10  ? 111 GLU A OE1 1 
ATOM   973   O OE2 . GLU A 1 111 ? 36.024  21.042  18.151  1.00 95.30  ? 111 GLU A OE2 1 
ATOM   974   N N   . ARG A 1 112 ? 36.736  15.593  18.289  1.00 53.58  ? 112 ARG A N   1 
ATOM   975   C CA  . ARG A 1 112 ? 37.910  14.963  17.698  1.00 60.43  ? 112 ARG A CA  1 
ATOM   976   C C   . ARG A 1 112 ? 37.761  14.821  16.188  1.00 62.67  ? 112 ARG A C   1 
ATOM   977   O O   . ARG A 1 112 ? 38.744  14.948  15.448  1.00 64.43  ? 112 ARG A O   1 
ATOM   978   C CB  . ARG A 1 112 ? 38.154  13.602  18.344  1.00 58.26  ? 112 ARG A CB  1 
ATOM   979   C CG  . ARG A 1 112 ? 39.526  13.009  18.062  1.00 54.75  ? 112 ARG A CG  1 
ATOM   980   C CD  . ARG A 1 112 ? 40.686  13.919  18.441  1.00 61.47  ? 112 ARG A CD  1 
ATOM   981   N NE  . ARG A 1 112 ? 41.912  13.147  18.620  1.00 69.85  ? 112 ARG A NE  1 
ATOM   982   C CZ  . ARG A 1 112 ? 43.088  13.473  18.101  1.00 72.48  ? 112 ARG A CZ  1 
ATOM   983   N NH1 . ARG A 1 112 ? 43.257  14.598  17.424  1.00 63.53  ? 112 ARG A NH1 1 
ATOM   984   N NH2 . ARG A 1 112 ? 44.126  12.661  18.286  1.00 69.64  ? 112 ARG A NH2 1 
ATOM   985   N N   . ILE A 1 113 ? 36.537  14.571  15.711  1.00 56.17  ? 113 ILE A N   1 
ATOM   986   C CA  . ILE A 1 113 ? 36.309  14.441  14.276  1.00 53.81  ? 113 ILE A CA  1 
ATOM   987   C C   . ILE A 1 113 ? 36.536  15.770  13.573  1.00 60.36  ? 113 ILE A C   1 
ATOM   988   O O   . ILE A 1 113 ? 37.027  15.808  12.439  1.00 69.00  ? 113 ILE A O   1 
ATOM   989   C CB  . ILE A 1 113 ? 34.896  13.910  13.997  1.00 56.37  ? 113 ILE A CB  1 
ATOM   990   C CG1 . ILE A 1 113 ? 34.739  12.486  14.533  1.00 59.87  ? 113 ILE A CG1 1 
ATOM   991   C CG2 . ILE A 1 113 ? 34.593  13.993  12.506  1.00 59.09  ? 113 ILE A CG2 1 
ATOM   992   C CD1 . ILE A 1 113 ? 35.005  11.398  13.508  1.00 52.72  ? 113 ILE A CD1 1 
ATOM   993   N N   . ARG A 1 114 ? 36.169  16.879  14.219  1.00 57.54  ? 114 ARG A N   1 
ATOM   994   C CA  . ARG A 1 114 ? 36.514  18.185  13.670  1.00 63.85  ? 114 ARG A CA  1 
ATOM   995   C C   . ARG A 1 114 ? 38.015  18.314  13.473  1.00 66.85  ? 114 ARG A C   1 
ATOM   996   O O   . ARG A 1 114 ? 38.473  18.701  12.392  1.00 68.11  ? 114 ARG A O   1 
ATOM   997   C CB  . ARG A 1 114 ? 36.008  19.309  14.567  1.00 68.85  ? 114 ARG A CB  1 
ATOM   998   C CG  . ARG A 1 114 ? 35.159  20.344  13.835  1.00 82.98  ? 114 ARG A CG  1 
ATOM   999   C CD  . ARG A 1 114 ? 34.829  21.504  14.748  1.00 80.26  ? 114 ARG A CD  1 
ATOM   1000  N NE  . ARG A 1 114 ? 36.022  21.967  15.446  1.00 94.30  ? 114 ARG A NE  1 
ATOM   1001  C CZ  . ARG A 1 114 ? 36.097  23.083  16.161  1.00 103.78 ? 114 ARG A CZ  1 
ATOM   1002  N NH1 . ARG A 1 114 ? 35.059  23.894  16.295  1.00 105.69 ? 114 ARG A NH1 1 
ATOM   1003  N NH2 . ARG A 1 114 ? 37.239  23.383  16.776  1.00 97.62  ? 114 ARG A NH2 1 
ATOM   1004  N N   . GLU A 1 115 ? 38.802  17.990  14.504  1.00 61.97  ? 115 GLU A N   1 
ATOM   1005  C CA  . GLU A 1 115 ? 40.251  18.134  14.395  1.00 65.64  ? 115 GLU A CA  1 
ATOM   1006  C C   . GLU A 1 115 ? 40.808  17.231  13.305  1.00 62.40  ? 115 GLU A C   1 
ATOM   1007  O O   . GLU A 1 115 ? 41.496  17.694  12.388  1.00 65.58  ? 115 GLU A O   1 
ATOM   1008  C CB  . GLU A 1 115 ? 40.927  17.828  15.732  1.00 65.55  ? 115 GLU A CB  1 
ATOM   1009  C CG  . GLU A 1 115 ? 40.096  18.131  16.957  1.00 65.49  ? 115 GLU A CG  1 
ATOM   1010  C CD  . GLU A 1 115 ? 40.895  17.989  18.239  1.00 71.28  ? 115 GLU A CD  1 
ATOM   1011  O OE1 . GLU A 1 115 ? 41.813  17.140  18.281  1.00 72.72  ? 115 GLU A OE1 1 
ATOM   1012  O OE2 . GLU A 1 115 ? 40.613  18.732  19.203  1.00 76.65  ? 115 GLU A OE2 1 
ATOM   1013  N N   . LEU A 1 116 ? 40.510  15.930  13.386  1.00 60.46  ? 116 LEU A N   1 
ATOM   1014  C CA  . LEU A 1 116 ? 41.150  14.973  12.491  1.00 59.19  ? 116 LEU A CA  1 
ATOM   1015  C C   . LEU A 1 116 ? 40.827  15.264  11.036  1.00 65.41  ? 116 LEU A C   1 
ATOM   1016  O O   . LEU A 1 116 ? 41.666  15.030  10.158  1.00 67.90  ? 116 LEU A O   1 
ATOM   1017  C CB  . LEU A 1 116 ? 40.748  13.543  12.853  1.00 47.47  ? 116 LEU A CB  1 
ATOM   1018  C CG  . LEU A 1 116 ? 41.019  13.119  14.301  1.00 64.21  ? 116 LEU A CG  1 
ATOM   1019  C CD1 . LEU A 1 116 ? 40.234  11.863  14.652  1.00 60.31  ? 116 LEU A CD1 1 
ATOM   1020  C CD2 . LEU A 1 116 ? 42.508  12.930  14.579  1.00 58.52  ? 116 LEU A CD2 1 
ATOM   1021  N N   . MET A 1 117 ? 39.632  15.791  10.761  1.00 62.21  ? 117 MET A N   1 
ATOM   1022  C CA  . MET A 1 117 ? 39.280  16.134  9.388   1.00 62.09  ? 117 MET A CA  1 
ATOM   1023  C C   . MET A 1 117 ? 39.998  17.397  8.929   1.00 66.42  ? 117 MET A C   1 
ATOM   1024  O O   . MET A 1 117 ? 40.385  17.506  7.761   1.00 68.54  ? 117 MET A O   1 
ATOM   1025  C CB  . MET A 1 117 ? 37.765  16.280  9.264   1.00 66.63  ? 117 MET A CB  1 
ATOM   1026  C CG  . MET A 1 117 ? 37.057  14.966  9.505   1.00 64.14  ? 117 MET A CG  1 
ATOM   1027  S SD  . MET A 1 117 ? 37.378  13.767  8.186   1.00 63.56  ? 117 MET A SD  1 
ATOM   1028  C CE  . MET A 1 117 ? 37.062  14.740  6.710   1.00 64.50  ? 117 MET A CE  1 
ATOM   1029  N N   . ASN A 1 118 ? 40.200  18.354  9.837   1.00 68.38  ? 118 ASN A N   1 
ATOM   1030  C CA  . ASN A 1 118 ? 41.016  19.520  9.531   1.00 67.50  ? 118 ASN A CA  1 
ATOM   1031  C C   . ASN A 1 118 ? 42.499  19.190  9.485   1.00 68.25  ? 118 ASN A C   1 
ATOM   1032  O O   . ASN A 1 118 ? 43.292  20.020  9.022   1.00 75.64  ? 118 ASN A O   1 
ATOM   1033  C CB  . ASN A 1 118 ? 40.757  20.626  10.556  1.00 66.95  ? 118 ASN A CB  1 
ATOM   1034  C CG  . ASN A 1 118 ? 39.305  21.048  10.592  1.00 80.49  ? 118 ASN A CG  1 
ATOM   1035  O OD1 . ASN A 1 118 ? 38.553  20.793  9.650   1.00 85.55  ? 118 ASN A OD1 1 
ATOM   1036  N ND2 . ASN A 1 118 ? 38.899  21.694  11.679  1.00 84.34  ? 118 ASN A ND2 1 
ATOM   1037  N N   . LYS A 1 119 ? 42.885  18.003  9.939   1.00 67.03  ? 119 LYS A N   1 
ATOM   1038  C CA  . LYS A 1 119 ? 44.283  17.607  9.937   1.00 70.45  ? 119 LYS A CA  1 
ATOM   1039  C C   . LYS A 1 119 ? 44.708  17.167  8.544   1.00 74.80  ? 119 LYS A C   1 
ATOM   1040  O O   . LYS A 1 119 ? 43.978  16.455  7.846   1.00 70.98  ? 119 LYS A O   1 
ATOM   1041  C CB  . LYS A 1 119 ? 44.521  16.488  10.950  1.00 67.38  ? 119 LYS A CB  1 
ATOM   1042  C CG  . LYS A 1 119 ? 45.393  16.909  12.133  1.00 70.34  ? 119 LYS A CG  1 
ATOM   1043  C CD  . LYS A 1 119 ? 45.186  16.004  13.344  1.00 74.88  ? 119 LYS A CD  1 
ATOM   1044  C CE  . LYS A 1 119 ? 45.692  16.650  14.636  1.00 83.71  ? 119 LYS A CE  1 
ATOM   1045  N NZ  . LYS A 1 119 ? 45.377  15.839  15.854  1.00 89.05  ? 119 LYS A NZ  1 
ATOM   1046  N N   . GLU A 1 120 ? 45.905  17.604  8.146   1.00 78.34  ? 120 GLU A N   1 
ATOM   1047  C CA  . GLU A 1 120 ? 46.402  17.370  6.793   1.00 81.22  ? 120 GLU A CA  1 
ATOM   1048  C C   . GLU A 1 120 ? 46.984  15.967  6.639   1.00 84.99  ? 120 GLU A C   1 
ATOM   1049  O O   . GLU A 1 120 ? 46.737  15.295  5.631   1.00 86.62  ? 120 GLU A O   1 
ATOM   1050  C CB  . GLU A 1 120 ? 47.450  18.423  6.425   1.00 77.91  ? 120 GLU A CB  1 
ATOM   1051  C CG  . GLU A 1 120 ? 48.509  18.698  7.510   1.00 93.18  ? 120 GLU A CG  1 
ATOM   1052  C CD  . GLU A 1 120 ? 47.984  19.487  8.703   1.00 94.60  ? 120 GLU A CD  1 
ATOM   1053  O OE1 . GLU A 1 120 ? 47.046  20.292  8.522   1.00 97.43  ? 120 GLU A OE1 1 
ATOM   1054  O OE2 . GLU A 1 120 ? 48.494  19.278  9.826   1.00 95.13  ? 120 GLU A OE2 1 
ATOM   1055  N N   . LYS A 1 121 ? 47.755  15.509  7.622   1.00 82.94  ? 121 LYS A N   1 
ATOM   1056  C CA  . LYS A 1 121 ? 48.285  14.154  7.653   1.00 80.08  ? 121 LYS A CA  1 
ATOM   1057  C C   . LYS A 1 121 ? 47.943  13.531  9.001   1.00 84.64  ? 121 LYS A C   1 
ATOM   1058  O O   . LYS A 1 121 ? 47.849  14.232  10.013  1.00 89.93  ? 121 LYS A O   1 
ATOM   1059  C CB  . LYS A 1 121 ? 49.805  14.152  7.409   1.00 84.04  ? 121 LYS A CB  1 
ATOM   1060  C CG  . LYS A 1 121 ? 50.526  12.871  7.799   1.00 90.10  ? 121 LYS A CG  1 
ATOM   1061  C CD  . LYS A 1 121 ? 51.357  12.339  6.642   1.00 94.49  ? 121 LYS A CD  1 
ATOM   1062  C CE  . LYS A 1 121 ? 51.706  10.872  6.837   1.00 93.98  ? 121 LYS A CE  1 
ATOM   1063  N NZ  . LYS A 1 121 ? 51.463  10.066  5.605   1.00 68.60  ? 121 LYS A NZ  1 
ATOM   1064  N N   . LEU A 1 122 ? 47.751  12.209  9.014   1.00 80.80  ? 122 LEU A N   1 
ATOM   1065  C CA  . LEU A 1 122 ? 47.269  11.504  10.199  1.00 70.55  ? 122 LEU A CA  1 
ATOM   1066  C C   . LEU A 1 122 ? 48.242  10.408  10.618  1.00 67.38  ? 122 LEU A C   1 
ATOM   1067  O O   . LEU A 1 122 ? 48.663  9.598   9.787   1.00 73.96  ? 122 LEU A O   1 
ATOM   1068  C CB  . LEU A 1 122 ? 45.884  10.904  9.934   1.00 68.43  ? 122 LEU A CB  1 
ATOM   1069  C CG  . LEU A 1 122 ? 44.803  11.957  9.695   1.00 67.00  ? 122 LEU A CG  1 
ATOM   1070  C CD1 . LEU A 1 122 ? 43.478  11.310  9.366   1.00 48.08  ? 122 LEU A CD1 1 
ATOM   1071  C CD2 . LEU A 1 122 ? 44.671  12.863  10.899  1.00 66.52  ? 122 LEU A CD2 1 
ATOM   1072  N N   . ASN A 1 123 ? 48.590  10.376  11.908  1.00 67.56  ? 123 ASN A N   1 
ATOM   1073  C CA  . ASN A 1 123 ? 49.418  9.315   12.467  1.00 60.79  ? 123 ASN A CA  1 
ATOM   1074  C C   . ASN A 1 123 ? 48.544  8.148   12.933  1.00 62.15  ? 123 ASN A C   1 
ATOM   1075  O O   . ASN A 1 123 ? 47.314  8.173   12.822  1.00 65.08  ? 123 ASN A O   1 
ATOM   1076  C CB  . ASN A 1 123 ? 50.297  9.849   13.603  1.00 57.57  ? 123 ASN A CB  1 
ATOM   1077  C CG  . ASN A 1 123 ? 49.495  10.350  14.796  1.00 69.12  ? 123 ASN A CG  1 
ATOM   1078  O OD1 . ASN A 1 123 ? 48.605  9.666   15.309  1.00 72.29  ? 123 ASN A OD1 1 
ATOM   1079  N ND2 . ASN A 1 123 ? 49.832  11.545  15.261  1.00 63.42  ? 123 ASN A ND2 1 
ATOM   1080  N N   . ARG A 1 124 ? 49.188  7.111   13.477  1.00 61.96  ? 124 ARG A N   1 
ATOM   1081  C CA  . ARG A 1 124 ? 48.461  5.899   13.853  1.00 60.16  ? 124 ARG A CA  1 
ATOM   1082  C C   . ARG A 1 124 ? 47.443  6.188   14.949  1.00 52.87  ? 124 ARG A C   1 
ATOM   1083  O O   . ARG A 1 124 ? 46.300  5.724   14.894  1.00 54.68  ? 124 ARG A O   1 
ATOM   1084  C CB  . ARG A 1 124 ? 49.440  4.812   14.303  1.00 57.82  ? 124 ARG A CB  1 
ATOM   1085  C CG  . ARG A 1 124 ? 48.779  3.630   15.011  1.00 60.67  ? 124 ARG A CG  1 
ATOM   1086  C CD  . ARG A 1 124 ? 49.779  2.895   15.900  1.00 62.40  ? 124 ARG A CD  1 
ATOM   1087  N NE  . ARG A 1 124 ? 49.207  1.704   16.522  1.00 68.63  ? 124 ARG A NE  1 
ATOM   1088  C CZ  . ARG A 1 124 ? 48.695  1.664   17.746  1.00 66.53  ? 124 ARG A CZ  1 
ATOM   1089  N NH1 . ARG A 1 124 ? 48.666  2.737   18.518  1.00 65.01  ? 124 ARG A NH1 1 
ATOM   1090  N NH2 . ARG A 1 124 ? 48.196  0.520   18.208  1.00 62.16  ? 124 ARG A NH2 1 
ATOM   1091  N N   . GLU A 1 125 ? 47.849  6.952   15.962  1.00 61.88  ? 125 GLU A N   1 
ATOM   1092  C CA  . GLU A 1 125 ? 46.962  7.220   17.089  1.00 63.21  ? 125 GLU A CA  1 
ATOM   1093  C C   . GLU A 1 125 ? 45.768  8.060   16.664  1.00 55.44  ? 125 GLU A C   1 
ATOM   1094  O O   . GLU A 1 125 ? 44.666  7.887   17.193  1.00 59.43  ? 125 GLU A O   1 
ATOM   1095  C CB  . GLU A 1 125 ? 47.737  7.907   18.212  1.00 63.65  ? 125 GLU A CB  1 
ATOM   1096  C CG  . GLU A 1 125 ? 48.660  6.976   18.991  1.00 69.84  ? 125 GLU A CG  1 
ATOM   1097  C CD  . GLU A 1 125 ? 49.674  6.271   18.109  1.00 75.04  ? 125 GLU A CD  1 
ATOM   1098  O OE1 . GLU A 1 125 ? 50.219  6.928   17.196  1.00 82.65  ? 125 GLU A OE1 1 
ATOM   1099  O OE2 . GLU A 1 125 ? 49.921  5.065   18.323  1.00 73.36  ? 125 GLU A OE2 1 
ATOM   1100  N N   . GLU A 1 126 ? 45.967  8.963   15.704  1.00 61.39  ? 126 GLU A N   1 
ATOM   1101  C CA  . GLU A 1 126 ? 44.846  9.697   15.132  1.00 59.46  ? 126 GLU A CA  1 
ATOM   1102  C C   . GLU A 1 126 ? 43.961  8.784   14.293  1.00 55.81  ? 126 GLU A C   1 
ATOM   1103  O O   . GLU A 1 126 ? 42.733  8.927   14.294  1.00 60.37  ? 126 GLU A O   1 
ATOM   1104  C CB  . GLU A 1 126 ? 45.369  10.863  14.302  1.00 62.26  ? 126 GLU A CB  1 
ATOM   1105  C CG  . GLU A 1 126 ? 46.061  11.923  15.139  1.00 65.24  ? 126 GLU A CG  1 
ATOM   1106  C CD  . GLU A 1 126 ? 46.984  12.785  14.319  1.00 71.73  ? 126 GLU A CD  1 
ATOM   1107  O OE1 . GLU A 1 126 ? 47.206  12.441  13.143  1.00 76.66  ? 126 GLU A OE1 1 
ATOM   1108  O OE2 . GLU A 1 126 ? 47.482  13.804  14.842  1.00 75.68  ? 126 GLU A OE2 1 
ATOM   1109  N N   . LEU A 1 127 ? 44.566  7.822   13.592  1.00 56.11  ? 127 LEU A N   1 
ATOM   1110  C CA  . LEU A 1 127 ? 43.798  6.875   12.791  1.00 51.24  ? 127 LEU A CA  1 
ATOM   1111  C C   . LEU A 1 127 ? 42.976  5.937   13.669  1.00 54.83  ? 127 LEU A C   1 
ATOM   1112  O O   . LEU A 1 127 ? 41.831  5.609   13.332  1.00 57.96  ? 127 LEU A O   1 
ATOM   1113  C CB  . LEU A 1 127 ? 44.742  6.085   11.895  1.00 53.92  ? 127 LEU A CB  1 
ATOM   1114  C CG  . LEU A 1 127 ? 45.310  6.821   10.684  1.00 58.18  ? 127 LEU A CG  1 
ATOM   1115  C CD1 . LEU A 1 127 ? 46.240  5.881   9.951   1.00 54.16  ? 127 LEU A CD1 1 
ATOM   1116  C CD2 . LEU A 1 127 ? 44.189  7.303   9.767   1.00 58.47  ? 127 LEU A CD2 1 
ATOM   1117  N N   . LEU A 1 128 ? 43.548  5.480   14.787  1.00 51.52  ? 128 LEU A N   1 
ATOM   1118  C CA  . LEU A 1 128 ? 42.772  4.719   15.762  1.00 56.50  ? 128 LEU A CA  1 
ATOM   1119  C C   . LEU A 1 128 ? 41.525  5.483   16.190  1.00 58.44  ? 128 LEU A C   1 
ATOM   1120  O O   . LEU A 1 128 ? 40.448  4.896   16.345  1.00 56.34  ? 128 LEU A O   1 
ATOM   1121  C CB  . LEU A 1 128 ? 43.639  4.390   16.978  1.00 54.98  ? 128 LEU A CB  1 
ATOM   1122  C CG  . LEU A 1 128 ? 43.974  2.919   17.252  1.00 54.70  ? 128 LEU A CG  1 
ATOM   1123  C CD1 . LEU A 1 128 ? 44.978  2.807   18.390  1.00 49.89  ? 128 LEU A CD1 1 
ATOM   1124  C CD2 . LEU A 1 128 ? 42.730  2.094   17.568  1.00 46.90  ? 128 LEU A CD2 1 
ATOM   1125  N N   . ASP A 1 129 ? 41.648  6.800   16.372  1.00 57.93  ? 129 ASP A N   1 
ATOM   1126  C CA  . ASP A 1 129 ? 40.501  7.594   16.795  1.00 50.77  ? 129 ASP A CA  1 
ATOM   1127  C C   . ASP A 1 129 ? 39.490  7.739   15.669  1.00 53.14  ? 129 ASP A C   1 
ATOM   1128  O O   . ASP A 1 129 ? 38.281  7.711   15.916  1.00 57.11  ? 129 ASP A O   1 
ATOM   1129  C CB  . ASP A 1 129 ? 40.966  8.959   17.290  1.00 57.98  ? 129 ASP A CB  1 
ATOM   1130  C CG  . ASP A 1 129 ? 41.779  8.863   18.575  1.00 65.72  ? 129 ASP A CG  1 
ATOM   1131  O OD1 . ASP A 1 129 ? 42.115  7.724   18.969  1.00 66.17  ? 129 ASP A OD1 1 
ATOM   1132  O OD2 . ASP A 1 129 ? 42.079  9.913   19.194  1.00 59.46  ? 129 ASP A OD2 1 
ATOM   1133  N N   . LEU A 1 130 ? 39.955  7.877   14.421  1.00 51.23  ? 130 LEU A N   1 
ATOM   1134  C CA  . LEU A 1 130 ? 39.011  7.924   13.305  1.00 49.60  ? 130 LEU A CA  1 
ATOM   1135  C C   . LEU A 1 130 ? 38.249  6.611   13.178  1.00 53.32  ? 130 LEU A C   1 
ATOM   1136  O O   . LEU A 1 130 ? 37.050  6.609   12.874  1.00 63.08  ? 130 LEU A O   1 
ATOM   1137  C CB  . LEU A 1 130 ? 39.722  8.258   11.994  1.00 55.89  ? 130 LEU A CB  1 
ATOM   1138  C CG  . LEU A 1 130 ? 38.745  8.763   10.916  1.00 48.12  ? 130 LEU A CG  1 
ATOM   1139  C CD1 . LEU A 1 130 ? 38.116  10.093  11.308  1.00 42.46  ? 130 LEU A CD1 1 
ATOM   1140  C CD2 . LEU A 1 130 ? 39.388  8.861   9.538   1.00 49.26  ? 130 LEU A CD2 1 
ATOM   1141  N N   . GLN A 1 131 ? 38.920  5.485   13.424  1.00 53.20  ? 131 GLN A N   1 
ATOM   1142  C CA  . GLN A 1 131 ? 38.229  4.198   13.451  1.00 52.92  ? 131 GLN A CA  1 
ATOM   1143  C C   . GLN A 1 131 ? 37.239  4.128   14.606  1.00 49.34  ? 131 GLN A C   1 
ATOM   1144  O O   . GLN A 1 131 ? 36.041  3.893   14.410  1.00 52.27  ? 131 GLN A O   1 
ATOM   1145  C CB  . GLN A 1 131 ? 39.238  3.062   13.577  1.00 61.70  ? 131 GLN A CB  1 
ATOM   1146  C CG  . GLN A 1 131 ? 40.201  2.925   12.431  1.00 57.01  ? 131 GLN A CG  1 
ATOM   1147  C CD  . GLN A 1 131 ? 41.304  1.956   12.758  1.00 53.00  ? 131 GLN A CD  1 
ATOM   1148  O OE1 . GLN A 1 131 ? 41.743  1.858   13.908  1.00 47.05  ? 131 GLN A OE1 1 
ATOM   1149  N NE2 . GLN A 1 131 ? 41.729  1.193   11.759  1.00 52.46  ? 131 GLN A NE2 1 
ATOM   1150  N N   . THR A 1 132 ? 37.734  4.328   15.829  1.00 53.73  ? 132 THR A N   1 
ATOM   1151  C CA  . THR A 1 132 ? 36.913  4.117   17.017  1.00 54.18  ? 132 THR A CA  1 
ATOM   1152  C C   . THR A 1 132 ? 35.750  5.093   17.083  1.00 47.84  ? 132 THR A C   1 
ATOM   1153  O O   . THR A 1 132 ? 34.616  4.696   17.378  1.00 51.70  ? 132 THR A O   1 
ATOM   1154  C CB  . THR A 1 132 ? 37.779  4.224   18.270  1.00 49.59  ? 132 THR A CB  1 
ATOM   1155  O OG1 . THR A 1 132 ? 39.064  3.642   18.011  1.00 49.51  ? 132 THR A OG1 1 
ATOM   1156  C CG2 . THR A 1 132 ? 37.116  3.510   19.417  1.00 52.90  ? 132 THR A CG2 1 
ATOM   1157  N N   . LEU A 1 133 ? 36.009  6.376   16.825  1.00 46.75  ? 133 LEU A N   1 
ATOM   1158  C CA  . LEU A 1 133 ? 34.915  7.338   16.806  1.00 55.12  ? 133 LEU A CA  1 
ATOM   1159  C C   . LEU A 1 133 ? 33.906  7.007   15.716  1.00 53.12  ? 133 LEU A C   1 
ATOM   1160  O O   . LEU A 1 133 ? 32.704  7.239   15.897  1.00 48.95  ? 133 LEU A O   1 
ATOM   1161  C CB  . LEU A 1 133 ? 35.453  8.755   16.616  1.00 57.30  ? 133 LEU A CB  1 
ATOM   1162  C CG  . LEU A 1 133 ? 36.208  9.338   17.812  1.00 52.86  ? 133 LEU A CG  1 
ATOM   1163  C CD1 . LEU A 1 133 ? 37.139  10.413  17.323  1.00 52.96  ? 133 LEU A CD1 1 
ATOM   1164  C CD2 . LEU A 1 133 ? 35.271  9.883   18.880  1.00 49.65  ? 133 LEU A CD2 1 
ATOM   1165  N N   . ASN A 1 134 ? 34.362  6.458   14.587  1.00 47.76  ? 134 ASN A N   1 
ATOM   1166  C CA  . ASN A 1 134 ? 33.416  6.057   13.556  1.00 50.31  ? 134 ASN A CA  1 
ATOM   1167  C C   . ASN A 1 134 ? 32.490  4.969   14.073  1.00 53.10  ? 134 ASN A C   1 
ATOM   1168  O O   . ASN A 1 134 ? 31.292  4.972   13.774  1.00 54.05  ? 134 ASN A O   1 
ATOM   1169  C CB  . ASN A 1 134 ? 34.156  5.600   12.301  1.00 50.75  ? 134 ASN A CB  1 
ATOM   1170  C CG  . ASN A 1 134 ? 34.083  6.626   11.176  1.00 56.71  ? 134 ASN A CG  1 
ATOM   1171  O OD1 . ASN A 1 134 ? 33.076  6.734   10.471  1.00 58.57  ? 134 ASN A OD1 1 
ATOM   1172  N ND2 . ASN A 1 134 ? 35.144  7.401   11.021  1.00 54.64  ? 134 ASN A ND2 1 
ATOM   1173  N N   . LEU A 1 135 ? 33.025  4.036   14.862  1.00 51.69  ? 135 LEU A N   1 
ATOM   1174  C CA  . LEU A 1 135 ? 32.181  3.021   15.485  1.00 44.39  ? 135 LEU A CA  1 
ATOM   1175  C C   . LEU A 1 135 ? 31.281  3.636   16.542  1.00 49.95  ? 135 LEU A C   1 
ATOM   1176  O O   . LEU A 1 135 ? 30.091  3.307   16.630  1.00 46.05  ? 135 LEU A O   1 
ATOM   1177  C CB  . LEU A 1 135 ? 33.045  1.946   16.126  1.00 47.93  ? 135 LEU A CB  1 
ATOM   1178  C CG  . LEU A 1 135 ? 33.636  0.889   15.216  1.00 51.36  ? 135 LEU A CG  1 
ATOM   1179  C CD1 . LEU A 1 135 ? 34.461  -0.021  16.078  1.00 49.21  ? 135 LEU A CD1 1 
ATOM   1180  C CD2 . LEU A 1 135 ? 32.543  0.125   14.506  1.00 55.02  ? 135 LEU A CD2 1 
ATOM   1181  N N   . LEU A 1 136 ? 31.841  4.528   17.359  1.00 46.34  ? 136 LEU A N   1 
ATOM   1182  C CA  . LEU A 1 136 ? 31.093  5.099   18.466  1.00 50.59  ? 136 LEU A CA  1 
ATOM   1183  C C   . LEU A 1 136 ? 30.009  6.065   18.005  1.00 45.62  ? 136 LEU A C   1 
ATOM   1184  O O   . LEU A 1 136 ? 29.059  6.300   18.757  1.00 51.44  ? 136 LEU A O   1 
ATOM   1185  C CB  . LEU A 1 136 ? 32.052  5.791   19.435  1.00 47.57  ? 136 LEU A CB  1 
ATOM   1186  C CG  . LEU A 1 136 ? 32.877  4.831   20.297  1.00 48.46  ? 136 LEU A CG  1 
ATOM   1187  C CD1 . LEU A 1 136 ? 33.779  5.613   21.237  1.00 45.05  ? 136 LEU A CD1 1 
ATOM   1188  C CD2 . LEU A 1 136 ? 31.987  3.862   21.069  1.00 46.38  ? 136 LEU A CD2 1 
ATOM   1189  N N   . ALA A 1 137 ? 30.113  6.625   16.796  1.00 45.07  ? 137 ALA A N   1 
ATOM   1190  C CA  . ALA A 1 137 ? 29.038  7.492   16.316  1.00 52.24  ? 137 ALA A CA  1 
ATOM   1191  C C   . ALA A 1 137 ? 27.750  6.713   16.095  1.00 50.03  ? 137 ALA A C   1 
ATOM   1192  O O   . ALA A 1 137 ? 26.655  7.268   16.235  1.00 50.62  ? 137 ALA A O   1 
ATOM   1193  C CB  . ALA A 1 137 ? 29.442  8.200   15.025  1.00 45.66  ? 137 ALA A CB  1 
ATOM   1194  N N   . TRP A 1 138 ? 27.863  5.432   15.759  1.00 47.52  ? 138 TRP A N   1 
ATOM   1195  C CA  . TRP A 1 138 ? 26.715  4.584   15.478  1.00 46.13  ? 138 TRP A CA  1 
ATOM   1196  C C   . TRP A 1 138 ? 26.315  3.759   16.690  1.00 46.51  ? 138 TRP A C   1 
ATOM   1197  O O   . TRP A 1 138 ? 25.884  2.611   16.551  1.00 47.13  ? 138 TRP A O   1 
ATOM   1198  C CB  . TRP A 1 138 ? 27.019  3.673   14.292  1.00 50.06  ? 138 TRP A CB  1 
ATOM   1199  C CG  . TRP A 1 138 ? 27.322  4.403   13.037  1.00 49.82  ? 138 TRP A CG  1 
ATOM   1200  C CD1 . TRP A 1 138 ? 28.531  4.904   12.649  1.00 48.13  ? 138 TRP A CD1 1 
ATOM   1201  C CD2 . TRP A 1 138 ? 26.401  4.713   11.981  1.00 53.80  ? 138 TRP A CD2 1 
ATOM   1202  N NE1 . TRP A 1 138 ? 28.419  5.513   11.417  1.00 49.95  ? 138 TRP A NE1 1 
ATOM   1203  C CE2 . TRP A 1 138 ? 27.122  5.406   10.986  1.00 52.94  ? 138 TRP A CE2 1 
ATOM   1204  C CE3 . TRP A 1 138 ? 25.039  4.470   11.780  1.00 50.81  ? 138 TRP A CE3 1 
ATOM   1205  C CZ2 . TRP A 1 138 ? 26.525  5.859   9.812   1.00 51.07  ? 138 TRP A CZ2 1 
ATOM   1206  C CZ3 . TRP A 1 138 ? 24.453  4.922   10.617  1.00 44.89  ? 138 TRP A CZ3 1 
ATOM   1207  C CH2 . TRP A 1 138 ? 25.192  5.607   9.649   1.00 45.51  ? 138 TRP A CH2 1 
ATOM   1208  N N   . CYS A 1 139 ? 26.468  4.319   17.882  1.00 50.32  ? 139 CYS A N   1 
ATOM   1209  C CA  . CYS A 1 139 ? 26.127  3.599   19.097  1.00 56.05  ? 139 CYS A CA  1 
ATOM   1210  C C   . CYS A 1 139 ? 24.646  3.768   19.427  1.00 53.39  ? 139 CYS A C   1 
ATOM   1211  O O   . CYS A 1 139 ? 24.140  4.892   19.495  1.00 42.42  ? 139 CYS A O   1 
ATOM   1212  C CB  . CYS A 1 139 ? 26.994  4.089   20.254  1.00 50.52  ? 139 CYS A CB  1 
ATOM   1213  S SG  . CYS A 1 139 ? 27.112  2.896   21.580  1.00 61.98  ? 139 CYS A SG  1 
ATOM   1214  N N   . GLY A 1 140 ? 23.957  2.650   19.634  1.00 54.39  ? 140 GLY A N   1 
ATOM   1215  C CA  . GLY A 1 140 ? 22.562  2.685   20.002  1.00 49.72  ? 140 GLY A CA  1 
ATOM   1216  C C   . GLY A 1 140 ? 22.347  3.081   21.454  1.00 57.79  ? 140 GLY A C   1 
ATOM   1217  O O   . GLY A 1 140 ? 23.283  3.262   22.236  1.00 52.11  ? 140 GLY A O   1 
ATOM   1218  N N   . ARG A 1 141 ? 21.062  3.192   21.812  1.00 52.84  ? 141 ARG A N   1 
ATOM   1219  C CA  . ARG A 1 141 ? 20.669  3.686   23.129  1.00 46.31  ? 141 ARG A CA  1 
ATOM   1220  C C   . ARG A 1 141 ? 21.163  2.773   24.244  1.00 51.89  ? 141 ARG A C   1 
ATOM   1221  O O   . ARG A 1 141 ? 21.541  3.245   25.325  1.00 49.08  ? 141 ARG A O   1 
ATOM   1222  C CB  . ARG A 1 141 ? 19.145  3.825   23.192  1.00 51.52  ? 141 ARG A CB  1 
ATOM   1223  C CG  . ARG A 1 141 ? 18.626  4.439   24.484  1.00 49.88  ? 141 ARG A CG  1 
ATOM   1224  C CD  . ARG A 1 141 ? 17.120  4.606   24.449  1.00 41.77  ? 141 ARG A CD  1 
ATOM   1225  N NE  . ARG A 1 141 ? 16.430  3.421   24.940  1.00 47.70  ? 141 ARG A NE  1 
ATOM   1226  C CZ  . ARG A 1 141 ? 15.726  3.376   26.064  1.00 49.26  ? 141 ARG A CZ  1 
ATOM   1227  N NH1 . ARG A 1 141 ? 15.594  4.438   26.839  1.00 50.06  ? 141 ARG A NH1 1 
ATOM   1228  N NH2 . ARG A 1 141 ? 15.140  2.234   26.421  1.00 52.59  ? 141 ARG A NH2 1 
ATOM   1229  N N   . THR A 1 142 ? 21.145  1.461   24.009  1.00 48.94  ? 142 THR A N   1 
ATOM   1230  C CA  . THR A 1 142 ? 21.524  0.516   25.052  1.00 48.94  ? 142 THR A CA  1 
ATOM   1231  C C   . THR A 1 142 ? 22.987  0.674   25.432  1.00 58.16  ? 142 THR A C   1 
ATOM   1232  O O   . THR A 1 142 ? 23.323  0.848   26.610  1.00 60.91  ? 142 THR A O   1 
ATOM   1233  C CB  . THR A 1 142 ? 21.252  -0.912  24.590  1.00 48.12  ? 142 THR A CB  1 
ATOM   1234  O OG1 . THR A 1 142 ? 20.062  -0.941  23.791  1.00 57.65  ? 142 THR A OG1 1 
ATOM   1235  C CG2 . THR A 1 142 ? 21.089  -1.823  25.790  1.00 60.96  ? 142 THR A CG2 1 
ATOM   1236  N N   . LEU A 1 143 ? 23.878  0.611   24.443  1.00 56.37  ? 143 LEU A N   1 
ATOM   1237  C CA  . LEU A 1 143 ? 25.302  0.666   24.731  1.00 51.11  ? 143 LEU A CA  1 
ATOM   1238  C C   . LEU A 1 143 ? 25.787  2.081   25.000  1.00 51.81  ? 143 LEU A C   1 
ATOM   1239  O O   . LEU A 1 143 ? 26.895  2.249   25.525  1.00 49.97  ? 143 LEU A O   1 
ATOM   1240  C CB  . LEU A 1 143 ? 26.100  0.063   23.576  1.00 48.19  ? 143 LEU A CB  1 
ATOM   1241  C CG  . LEU A 1 143 ? 26.093  -1.463  23.509  1.00 48.55  ? 143 LEU A CG  1 
ATOM   1242  C CD1 . LEU A 1 143 ? 26.908  -1.938  22.310  1.00 54.50  ? 143 LEU A CD1 1 
ATOM   1243  C CD2 . LEU A 1 143 ? 26.590  -2.081  24.815  1.00 53.84  ? 143 LEU A CD2 1 
ATOM   1244  N N   . ARG A 1 144 ? 24.994  3.097   24.635  1.00 53.69  ? 144 ARG A N   1 
ATOM   1245  C CA  . ARG A 1 144 ? 25.352  4.472   24.971  1.00 53.13  ? 144 ARG A CA  1 
ATOM   1246  C C   . ARG A 1 144 ? 25.370  4.682   26.474  1.00 49.06  ? 144 ARG A C   1 
ATOM   1247  O O   . ARG A 1 144 ? 26.114  5.531   26.973  1.00 49.60  ? 144 ARG A O   1 
ATOM   1248  C CB  . ARG A 1 144 ? 24.384  5.459   24.314  1.00 41.48  ? 144 ARG A CB  1 
ATOM   1249  C CG  . ARG A 1 144 ? 24.865  5.958   22.978  1.00 49.68  ? 144 ARG A CG  1 
ATOM   1250  C CD  . ARG A 1 144 ? 23.888  6.906   22.318  1.00 50.02  ? 144 ARG A CD  1 
ATOM   1251  N NE  . ARG A 1 144 ? 24.336  7.227   20.966  1.00 57.68  ? 144 ARG A NE  1 
ATOM   1252  C CZ  . ARG A 1 144 ? 24.150  8.396   20.368  1.00 59.73  ? 144 ARG A CZ  1 
ATOM   1253  N NH1 . ARG A 1 144 ? 23.516  9.387   20.974  1.00 68.70  ? 144 ARG A NH1 1 
ATOM   1254  N NH2 . ARG A 1 144 ? 24.622  8.578   19.137  1.00 50.98  ? 144 ARG A NH2 1 
ATOM   1255  N N   . LYS A 1 145 ? 24.552  3.927   27.205  1.00 46.79  ? 145 LYS A N   1 
ATOM   1256  C CA  . LYS A 1 145 ? 24.612  3.952   28.654  1.00 53.36  ? 145 LYS A CA  1 
ATOM   1257  C C   . LYS A 1 145 ? 25.788  3.148   29.182  1.00 58.94  ? 145 LYS A C   1 
ATOM   1258  O O   . LYS A 1 145 ? 26.349  3.496   30.227  1.00 62.47  ? 145 LYS A O   1 
ATOM   1259  C CB  . LYS A 1 145 ? 23.307  3.420   29.242  1.00 55.07  ? 145 LYS A CB  1 
ATOM   1260  C CG  . LYS A 1 145 ? 22.084  4.162   28.754  1.00 55.42  ? 145 LYS A CG  1 
ATOM   1261  C CD  . LYS A 1 145 ? 20.815  3.627   29.377  1.00 58.01  ? 145 LYS A CD  1 
ATOM   1262  C CE  . LYS A 1 145 ? 19.596  4.153   28.648  1.00 59.87  ? 145 LYS A CE  1 
ATOM   1263  N NZ  . LYS A 1 145 ? 18.652  3.046   28.344  1.00 57.44  ? 145 LYS A NZ  1 
ATOM   1264  N N   . ASP A 1 146 ? 26.182  2.087   28.477  1.00 55.06  ? 146 ASP A N   1 
ATOM   1265  C CA  . ASP A 1 146 ? 27.242  1.222   28.980  1.00 57.31  ? 146 ASP A CA  1 
ATOM   1266  C C   . ASP A 1 146 ? 28.625  1.809   28.713  1.00 62.19  ? 146 ASP A C   1 
ATOM   1267  O O   . ASP A 1 146 ? 29.470  1.856   29.615  1.00 70.23  ? 146 ASP A O   1 
ATOM   1268  C CB  . ASP A 1 146 ? 27.109  -0.179  28.377  1.00 55.27  ? 146 ASP A CB  1 
ATOM   1269  C CG  . ASP A 1 146 ? 26.028  -1.010  29.063  1.00 74.27  ? 146 ASP A CG  1 
ATOM   1270  O OD1 . ASP A 1 146 ? 25.408  -0.517  30.032  1.00 72.64  ? 146 ASP A OD1 1 
ATOM   1271  O OD2 . ASP A 1 146 ? 25.795  -2.160  28.630  1.00 82.61  ? 146 ASP A OD2 1 
ATOM   1272  N N   . LEU A 1 147 ? 28.881  2.258   27.482  1.00 59.76  ? 147 LEU A N   1 
ATOM   1273  C CA  . LEU A 1 147 ? 30.179  2.821   27.118  1.00 51.22  ? 147 LEU A CA  1 
ATOM   1274  C C   . LEU A 1 147 ? 30.244  4.324   27.352  1.00 55.31  ? 147 LEU A C   1 
ATOM   1275  O O   . LEU A 1 147 ? 30.935  5.037   26.611  1.00 55.20  ? 147 LEU A O   1 
ATOM   1276  C CB  . LEU A 1 147 ? 30.506  2.498   25.660  1.00 53.37  ? 147 LEU A CB  1 
ATOM   1277  C CG  . LEU A 1 147 ? 30.130  1.098   25.180  1.00 56.30  ? 147 LEU A CG  1 
ATOM   1278  C CD1 . LEU A 1 147 ? 30.370  0.929   23.672  1.00 46.93  ? 147 LEU A CD1 1 
ATOM   1279  C CD2 . LEU A 1 147 ? 30.905  0.072   25.989  1.00 42.09  ? 147 LEU A CD2 1 
ATOM   1280  N N   . LYS A 1 148 ? 29.530  4.820   28.366  1.00 55.43  ? 148 LYS A N   1 
ATOM   1281  C CA  . LYS A 1 148 ? 29.443  6.259   28.587  1.00 54.66  ? 148 LYS A CA  1 
ATOM   1282  C C   . LYS A 1 148 ? 30.819  6.884   28.755  1.00 58.76  ? 148 LYS A C   1 
ATOM   1283  O O   . LYS A 1 148 ? 31.073  7.983   28.251  1.00 64.54  ? 148 LYS A O   1 
ATOM   1284  C CB  . LYS A 1 148 ? 28.580  6.546   29.813  1.00 53.08  ? 148 LYS A CB  1 
ATOM   1285  C CG  . LYS A 1 148 ? 28.156  7.994   29.929  1.00 65.65  ? 148 LYS A CG  1 
ATOM   1286  C CD  . LYS A 1 148 ? 27.717  8.323   31.344  1.00 74.04  ? 148 LYS A CD  1 
ATOM   1287  C CE  . LYS A 1 148 ? 27.065  9.696   31.425  1.00 80.19  ? 148 LYS A CE  1 
ATOM   1288  N NZ  . LYS A 1 148 ? 26.839  10.326  30.092  1.00 76.81  ? 148 LYS A NZ  1 
ATOM   1289  N N   . ASP A 1 149 ? 31.727  6.192   29.450  1.00 60.96  ? 149 ASP A N   1 
ATOM   1290  C CA  . ASP A 1 149 ? 33.029  6.779   29.751  1.00 65.74  ? 149 ASP A CA  1 
ATOM   1291  C C   . ASP A 1 149 ? 33.927  6.803   28.515  1.00 59.01  ? 149 ASP A C   1 
ATOM   1292  O O   . ASP A 1 149 ? 34.557  7.827   28.223  1.00 55.30  ? 149 ASP A O   1 
ATOM   1293  C CB  . ASP A 1 149 ? 33.685  6.027   30.914  1.00 74.75  ? 149 ASP A CB  1 
ATOM   1294  C CG  . ASP A 1 149 ? 33.002  6.305   32.260  1.00 72.31  ? 149 ASP A CG  1 
ATOM   1295  O OD1 . ASP A 1 149 ? 32.232  7.284   32.367  1.00 59.88  ? 149 ASP A OD1 1 
ATOM   1296  O OD2 . ASP A 1 149 ? 33.236  5.534   33.216  1.00 81.56  ? 149 ASP A OD2 1 
ATOM   1297  N N   . LEU A 1 150 ? 33.995  5.692   27.773  1.00 53.43  ? 150 LEU A N   1 
ATOM   1298  C CA  . LEU A 1 150 ? 34.693  5.715   26.491  1.00 48.75  ? 150 LEU A CA  1 
ATOM   1299  C C   . LEU A 1 150 ? 34.149  6.823   25.597  1.00 59.06  ? 150 LEU A C   1 
ATOM   1300  O O   . LEU A 1 150 ? 34.918  7.549   24.954  1.00 62.02  ? 150 LEU A O   1 
ATOM   1301  C CB  . LEU A 1 150 ? 34.574  4.360   25.795  1.00 42.99  ? 150 LEU A CB  1 
ATOM   1302  C CG  . LEU A 1 150 ? 35.637  3.328   26.140  1.00 46.16  ? 150 LEU A CG  1 
ATOM   1303  C CD1 . LEU A 1 150 ? 35.245  1.984   25.558  1.00 50.51  ? 150 LEU A CD1 1 
ATOM   1304  C CD2 . LEU A 1 150 ? 36.989  3.777   25.624  1.00 60.67  ? 150 LEU A CD2 1 
ATOM   1305  N N   . LEU A 1 151 ? 32.820  6.983   25.561  1.00 53.69  ? 151 LEU A N   1 
ATOM   1306  C CA  . LEU A 1 151 ? 32.207  8.050   24.771  1.00 50.75  ? 151 LEU A CA  1 
ATOM   1307  C C   . LEU A 1 151 ? 32.537  9.431   25.320  1.00 62.51  ? 151 LEU A C   1 
ATOM   1308  O O   . LEU A 1 151 ? 32.599  10.402  24.556  1.00 56.26  ? 151 LEU A O   1 
ATOM   1309  C CB  . LEU A 1 151 ? 30.694  7.870   24.724  1.00 48.18  ? 151 LEU A CB  1 
ATOM   1310  C CG  . LEU A 1 151 ? 30.213  6.774   23.776  1.00 56.44  ? 151 LEU A CG  1 
ATOM   1311  C CD1 . LEU A 1 151 ? 28.854  6.260   24.220  1.00 55.53  ? 151 LEU A CD1 1 
ATOM   1312  C CD2 . LEU A 1 151 ? 30.178  7.252   22.318  1.00 43.82  ? 151 LEU A CD2 1 
ATOM   1313  N N   . ASN A 1 152 ? 32.733  9.544   26.637  1.00 67.55  ? 152 ASN A N   1 
ATOM   1314  C CA  . ASN A 1 152 ? 33.073  10.834  27.222  1.00 59.73  ? 152 ASN A CA  1 
ATOM   1315  C C   . ASN A 1 152 ? 34.524  11.197  26.964  1.00 58.13  ? 152 ASN A C   1 
ATOM   1316  O O   . ASN A 1 152 ? 34.855  12.386  26.882  1.00 70.95  ? 152 ASN A O   1 
ATOM   1317  C CB  . ASN A 1 152 ? 32.789  10.829  28.725  1.00 68.87  ? 152 ASN A CB  1 
ATOM   1318  C CG  . ASN A 1 152 ? 31.316  10.980  29.037  1.00 73.45  ? 152 ASN A CG  1 
ATOM   1319  O OD1 . ASN A 1 152 ? 30.767  10.269  29.882  1.00 72.95  ? 152 ASN A OD1 1 
ATOM   1320  N ND2 . ASN A 1 152 ? 30.660  11.900  28.340  1.00 78.07  ? 152 ASN A ND2 1 
ATOM   1321  N N   . LYS A 1 153 ? 35.399  10.197  26.845  1.00 59.68  ? 153 LYS A N   1 
ATOM   1322  C CA  . LYS A 1 153 ? 36.804  10.459  26.546  1.00 63.01  ? 153 LYS A CA  1 
ATOM   1323  C C   . LYS A 1 153 ? 36.936  11.307  25.288  1.00 59.63  ? 153 LYS A C   1 
ATOM   1324  O O   . LYS A 1 153 ? 37.543  12.384  25.302  1.00 51.97  ? 153 LYS A O   1 
ATOM   1325  C CB  . LYS A 1 153 ? 37.560  9.139   26.381  1.00 58.28  ? 153 LYS A CB  1 
ATOM   1326  C CG  . LYS A 1 153 ? 38.577  8.854   27.464  1.00 59.95  ? 153 LYS A CG  1 
ATOM   1327  C CD  . LYS A 1 153 ? 39.220  7.499   27.227  1.00 67.30  ? 153 LYS A CD  1 
ATOM   1328  C CE  . LYS A 1 153 ? 40.488  7.622   26.395  1.00 58.93  ? 153 LYS A CE  1 
ATOM   1329  N NZ  . LYS A 1 153 ? 41.216  6.330   26.324  1.00 63.81  ? 153 LYS A NZ  1 
ATOM   1330  N N   . GLY A 1 154 ? 36.350  10.833  24.188  1.00 50.37  ? 154 GLY A N   1 
ATOM   1331  C CA  . GLY A 1 154 ? 36.378  11.537  22.930  1.00 51.89  ? 154 GLY A CA  1 
ATOM   1332  C C   . GLY A 1 154 ? 37.659  11.405  22.136  1.00 55.83  ? 154 GLY A C   1 
ATOM   1333  O O   . GLY A 1 154 ? 37.665  11.751  20.948  1.00 56.64  ? 154 GLY A O   1 
ATOM   1334  N N   . ARG A 1 155 ? 38.741  10.916  22.735  1.00 54.55  ? 155 ARG A N   1 
ATOM   1335  C CA  . ARG A 1 155 ? 40.025  10.862  22.048  1.00 58.50  ? 155 ARG A CA  1 
ATOM   1336  C C   . ARG A 1 155 ? 40.924  9.861   22.763  1.00 58.41  ? 155 ARG A C   1 
ATOM   1337  O O   . ARG A 1 155 ? 40.533  9.242   23.755  1.00 58.06  ? 155 ARG A O   1 
ATOM   1338  C CB  . ARG A 1 155 ? 40.678  12.243  21.994  1.00 55.79  ? 155 ARG A CB  1 
ATOM   1339  C CG  . ARG A 1 155 ? 41.115  12.765  23.354  1.00 56.12  ? 155 ARG A CG  1 
ATOM   1340  C CD  . ARG A 1 155 ? 41.619  14.187  23.243  1.00 52.51  ? 155 ARG A CD  1 
ATOM   1341  N NE  . ARG A 1 155 ? 40.594  15.045  22.673  1.00 61.28  ? 155 ARG A NE  1 
ATOM   1342  C CZ  . ARG A 1 155 ? 40.763  15.813  21.606  1.00 65.88  ? 155 ARG A CZ  1 
ATOM   1343  N NH1 . ARG A 1 155 ? 41.933  15.896  20.993  1.00 67.79  ? 155 ARG A NH1 1 
ATOM   1344  N NH2 . ARG A 1 155 ? 39.730  16.511  21.139  1.00 67.47  ? 155 ARG A NH2 1 
ATOM   1345  N N   . ASN A 1 156 ? 42.143  9.709   22.242  1.00 62.33  ? 156 ASN A N   1 
ATOM   1346  C CA  . ASN A 1 156 ? 43.179  8.878   22.858  1.00 60.35  ? 156 ASN A CA  1 
ATOM   1347  C C   . ASN A 1 156 ? 42.703  7.442   23.076  1.00 59.03  ? 156 ASN A C   1 
ATOM   1348  O O   . ASN A 1 156 ? 43.001  6.819   24.098  1.00 55.70  ? 156 ASN A O   1 
ATOM   1349  C CB  . ASN A 1 156 ? 43.659  9.505   24.164  1.00 56.66  ? 156 ASN A CB  1 
ATOM   1350  C CG  . ASN A 1 156 ? 44.041  10.949  23.985  1.00 63.20  ? 156 ASN A CG  1 
ATOM   1351  O OD1 . ASN A 1 156 ? 44.187  11.421  22.857  1.00 60.35  ? 156 ASN A OD1 1 
ATOM   1352  N ND2 . ASN A 1 156 ? 44.192  11.668  25.090  1.00 70.98  ? 156 ASN A ND2 1 
ATOM   1353  N N   . TYR A 1 157 ? 41.970  6.909   22.101  1.00 49.38  ? 157 TYR A N   1 
ATOM   1354  C CA  . TYR A 1 157 ? 41.535  5.522   22.135  1.00 54.95  ? 157 TYR A CA  1 
ATOM   1355  C C   . TYR A 1 157 ? 42.690  4.582   21.779  1.00 57.66  ? 157 TYR A C   1 
ATOM   1356  O O   . TYR A 1 157 ? 43.642  4.954   21.087  1.00 53.73  ? 157 TYR A O   1 
ATOM   1357  C CB  . TYR A 1 157 ? 40.349  5.306   21.184  1.00 57.27  ? 157 TYR A CB  1 
ATOM   1358  C CG  . TYR A 1 157 ? 39.117  6.109   21.564  1.00 62.16  ? 157 TYR A CG  1 
ATOM   1359  C CD1 . TYR A 1 157 ? 38.358  5.772   22.681  1.00 49.81  ? 157 TYR A CD1 1 
ATOM   1360  C CD2 . TYR A 1 157 ? 38.712  7.204   20.806  1.00 57.47  ? 157 TYR A CD2 1 
ATOM   1361  C CE1 . TYR A 1 157 ? 37.242  6.507   23.038  1.00 47.01  ? 157 TYR A CE1 1 
ATOM   1362  C CE2 . TYR A 1 157 ? 37.590  7.944   21.157  1.00 48.28  ? 157 TYR A CE2 1 
ATOM   1363  C CZ  . TYR A 1 157 ? 36.860  7.591   22.271  1.00 53.98  ? 157 TYR A CZ  1 
ATOM   1364  O OH  . TYR A 1 157 ? 35.744  8.327   22.615  1.00 54.76  ? 157 TYR A OH  1 
ATOM   1365  N N   . THR A 1 158 ? 42.594  3.347   22.271  1.00 54.28  ? 158 THR A N   1 
ATOM   1366  C CA  . THR A 1 158 ? 43.580  2.304   22.032  1.00 50.85  ? 158 THR A CA  1 
ATOM   1367  C C   . THR A 1 158 ? 42.983  1.189   21.180  1.00 54.62  ? 158 THR A C   1 
ATOM   1368  O O   . THR A 1 158 ? 41.772  1.125   20.942  1.00 56.37  ? 158 THR A O   1 
ATOM   1369  C CB  . THR A 1 158 ? 44.106  1.731   23.358  1.00 59.54  ? 158 THR A CB  1 
ATOM   1370  O OG1 . THR A 1 158 ? 43.161  0.791   23.884  1.00 56.99  ? 158 THR A OG1 1 
ATOM   1371  C CG2 . THR A 1 158 ? 44.315  2.842   24.358  1.00 53.27  ? 158 THR A CG2 1 
ATOM   1372  N N   . GLN A 1 159 ? 43.867  0.297   20.720  1.00 50.63  ? 159 GLN A N   1 
ATOM   1373  C CA  . GLN A 1 159 ? 43.419  -0.864  19.957  1.00 56.40  ? 159 GLN A CA  1 
ATOM   1374  C C   . GLN A 1 159 ? 42.505  -1.746  20.796  1.00 63.33  ? 159 GLN A C   1 
ATOM   1375  O O   . GLN A 1 159 ? 41.473  -2.224  20.312  1.00 64.22  ? 159 GLN A O   1 
ATOM   1376  C CB  . GLN A 1 159 ? 44.624  -1.662  19.450  1.00 48.66  ? 159 GLN A CB  1 
ATOM   1377  C CG  . GLN A 1 159 ? 44.255  -2.843  18.568  1.00 61.67  ? 159 GLN A CG  1 
ATOM   1378  C CD  . GLN A 1 159 ? 43.743  -2.423  17.193  1.00 61.82  ? 159 GLN A CD  1 
ATOM   1379  O OE1 . GLN A 1 159 ? 44.065  -1.343  16.697  1.00 55.91  ? 159 GLN A OE1 1 
ATOM   1380  N NE2 . GLN A 1 159 ? 42.924  -3.273  16.583  1.00 58.19  ? 159 GLN A NE2 1 
ATOM   1381  N N   . GLU A 1 160 ? 42.855  -1.946  22.068  1.00 63.37  ? 160 GLU A N   1 
ATOM   1382  C CA  . GLU A 1 160 ? 42.056  -2.794  22.947  1.00 60.81  ? 160 GLU A CA  1 
ATOM   1383  C C   . GLU A 1 160 ? 40.695  -2.179  23.233  1.00 57.46  ? 160 GLU A C   1 
ATOM   1384  O O   . GLU A 1 160 ? 39.694  -2.896  23.332  1.00 59.92  ? 160 GLU A O   1 
ATOM   1385  C CB  . GLU A 1 160 ? 42.818  -3.038  24.250  1.00 65.32  ? 160 GLU A CB  1 
ATOM   1386  C CG  . GLU A 1 160 ? 43.952  -4.053  24.119  1.00 69.48  ? 160 GLU A CG  1 
ATOM   1387  C CD  . GLU A 1 160 ? 45.199  -3.485  23.450  1.00 76.42  ? 160 GLU A CD  1 
ATOM   1388  O OE1 . GLU A 1 160 ? 45.193  -2.298  23.048  1.00 66.00  ? 160 GLU A OE1 1 
ATOM   1389  O OE2 . GLU A 1 160 ? 46.183  -4.242  23.312  1.00 79.51  ? 160 GLU A OE2 1 
ATOM   1390  N N   . GLU A 1 161 ? 40.639  -0.854  23.379  1.00 55.98  ? 161 GLU A N   1 
ATOM   1391  C CA  . GLU A 1 161 ? 39.363  -0.192  23.632  1.00 55.87  ? 161 GLU A CA  1 
ATOM   1392  C C   . GLU A 1 161 ? 38.449  -0.285  22.416  1.00 60.73  ? 161 GLU A C   1 
ATOM   1393  O O   . GLU A 1 161 ? 37.235  -0.476  22.555  1.00 58.35  ? 161 GLU A O   1 
ATOM   1394  C CB  . GLU A 1 161 ? 39.599  1.268   24.028  1.00 53.68  ? 161 GLU A CB  1 
ATOM   1395  C CG  . GLU A 1 161 ? 40.221  1.452   25.413  1.00 56.39  ? 161 GLU A CG  1 
ATOM   1396  C CD  . GLU A 1 161 ? 40.641  2.893   25.697  1.00 64.34  ? 161 GLU A CD  1 
ATOM   1397  O OE1 . GLU A 1 161 ? 40.921  3.637   24.735  1.00 63.90  ? 161 GLU A OE1 1 
ATOM   1398  O OE2 . GLU A 1 161 ? 40.691  3.283   26.885  1.00 62.29  ? 161 GLU A OE2 1 
ATOM   1399  N N   . LYS A 1 162 ? 39.014  -0.161  21.213  1.00 61.48  ? 162 LYS A N   1 
ATOM   1400  C CA  . LYS A 1 162 ? 38.208  -0.306  20.006  1.00 56.25  ? 162 LYS A CA  1 
ATOM   1401  C C   . LYS A 1 162 ? 37.704  -1.736  19.853  1.00 54.20  ? 162 LYS A C   1 
ATOM   1402  O O   . LYS A 1 162 ? 36.570  -1.958  19.414  1.00 51.34  ? 162 LYS A O   1 
ATOM   1403  C CB  . LYS A 1 162 ? 39.026  0.118   18.785  1.00 55.90  ? 162 LYS A CB  1 
ATOM   1404  C CG  . LYS A 1 162 ? 38.357  -0.135  17.452  1.00 55.03  ? 162 LYS A CG  1 
ATOM   1405  C CD  . LYS A 1 162 ? 39.300  0.165   16.280  1.00 48.72  ? 162 LYS A CD  1 
ATOM   1406  C CE  . LYS A 1 162 ? 40.617  -0.629  16.369  1.00 57.82  ? 162 LYS A CE  1 
ATOM   1407  N NZ  . LYS A 1 162 ? 41.460  -0.585  15.125  1.00 43.78  ? 162 LYS A NZ  1 
ATOM   1408  N N   . GLU A 1 163 ? 38.526  -2.720  20.226  1.00 53.47  ? 163 GLU A N   1 
ATOM   1409  C CA  . GLU A 1 163 ? 38.102  -4.111  20.118  1.00 55.18  ? 163 GLU A CA  1 
ATOM   1410  C C   . GLU A 1 163 ? 37.063  -4.461  21.174  1.00 57.89  ? 163 GLU A C   1 
ATOM   1411  O O   . GLU A 1 163 ? 36.218  -5.337  20.950  1.00 58.63  ? 163 GLU A O   1 
ATOM   1412  C CB  . GLU A 1 163 ? 39.315  -5.033  20.223  1.00 57.92  ? 163 GLU A CB  1 
ATOM   1413  C CG  . GLU A 1 163 ? 40.150  -5.074  18.950  1.00 67.73  ? 163 GLU A CG  1 
ATOM   1414  C CD  . GLU A 1 163 ? 41.525  -5.691  19.153  1.00 75.78  ? 163 GLU A CD  1 
ATOM   1415  O OE1 . GLU A 1 163 ? 42.196  -5.341  20.147  1.00 83.64  ? 163 GLU A OE1 1 
ATOM   1416  O OE2 . GLU A 1 163 ? 41.940  -6.523  18.317  1.00 75.92  ? 163 GLU A OE2 1 
ATOM   1417  N N   . TYR A 1 164 ? 37.107  -3.792  22.327  1.00 52.65  ? 164 TYR A N   1 
ATOM   1418  C CA  . TYR A 1 164 ? 36.057  -3.973  23.320  1.00 52.83  ? 164 TYR A CA  1 
ATOM   1419  C C   . TYR A 1 164 ? 34.726  -3.462  22.788  1.00 57.36  ? 164 TYR A C   1 
ATOM   1420  O O   . TYR A 1 164 ? 33.695  -4.139  22.889  1.00 54.68  ? 164 TYR A O   1 
ATOM   1421  C CB  . TYR A 1 164 ? 36.432  -3.251  24.606  1.00 54.15  ? 164 TYR A CB  1 
ATOM   1422  C CG  . TYR A 1 164 ? 35.295  -3.144  25.579  1.00 58.04  ? 164 TYR A CG  1 
ATOM   1423  C CD1 . TYR A 1 164 ? 34.797  -4.270  26.220  1.00 58.39  ? 164 TYR A CD1 1 
ATOM   1424  C CD2 . TYR A 1 164 ? 34.707  -1.919  25.844  1.00 58.36  ? 164 TYR A CD2 1 
ATOM   1425  C CE1 . TYR A 1 164 ? 33.750  -4.174  27.116  1.00 70.27  ? 164 TYR A CE1 1 
ATOM   1426  C CE2 . TYR A 1 164 ? 33.661  -1.814  26.737  1.00 69.80  ? 164 TYR A CE2 1 
ATOM   1427  C CZ  . TYR A 1 164 ? 33.183  -2.943  27.370  1.00 70.00  ? 164 TYR A CZ  1 
ATOM   1428  O OH  . TYR A 1 164 ? 32.136  -2.840  28.259  1.00 79.88  ? 164 TYR A OH  1 
ATOM   1429  N N   . VAL A 1 165 ? 34.739  -2.264  22.205  1.00 55.15  ? 165 VAL A N   1 
ATOM   1430  C CA  . VAL A 1 165 ? 33.540  -1.721  21.580  1.00 46.57  ? 165 VAL A CA  1 
ATOM   1431  C C   . VAL A 1 165 ? 33.011  -2.691  20.533  1.00 48.08  ? 165 VAL A C   1 
ATOM   1432  O O   . VAL A 1 165 ? 31.808  -2.966  20.467  1.00 50.53  ? 165 VAL A O   1 
ATOM   1433  C CB  . VAL A 1 165 ? 33.843  -0.336  20.983  1.00 40.66  ? 165 VAL A CB  1 
ATOM   1434  C CG1 . VAL A 1 165 ? 32.892  -0.012  19.841  1.00 45.48  ? 165 VAL A CG1 1 
ATOM   1435  C CG2 . VAL A 1 165 ? 33.748  0.697   22.062  1.00 40.58  ? 165 VAL A CG2 1 
ATOM   1436  N N   . LEU A 1 166 ? 33.909  -3.260  19.732  1.00 51.67  ? 166 LEU A N   1 
ATOM   1437  C CA  . LEU A 1 166 ? 33.472  -4.115  18.636  1.00 50.72  ? 166 LEU A CA  1 
ATOM   1438  C C   . LEU A 1 166 ? 32.828  -5.394  19.151  1.00 52.57  ? 166 LEU A C   1 
ATOM   1439  O O   . LEU A 1 166 ? 31.858  -5.887  18.566  1.00 57.00  ? 166 LEU A O   1 
ATOM   1440  C CB  . LEU A 1 166 ? 34.650  -4.443  17.726  1.00 57.33  ? 166 LEU A CB  1 
ATOM   1441  C CG  . LEU A 1 166 ? 34.857  -3.450  16.593  1.00 53.78  ? 166 LEU A CG  1 
ATOM   1442  C CD1 . LEU A 1 166 ? 36.282  -3.539  16.061  1.00 57.39  ? 166 LEU A CD1 1 
ATOM   1443  C CD2 . LEU A 1 166 ? 33.829  -3.702  15.507  1.00 60.23  ? 166 LEU A CD2 1 
ATOM   1444  N N   . ASN A 1 167 ? 33.354  -5.957  20.239  1.00 50.54  ? 167 ASN A N   1 
ATOM   1445  C CA  . ASN A 1 167 ? 32.722  -7.146  20.798  1.00 53.52  ? 167 ASN A CA  1 
ATOM   1446  C C   . ASN A 1 167 ? 31.372  -6.805  21.411  1.00 57.70  ? 167 ASN A C   1 
ATOM   1447  O O   . ASN A 1 167 ? 30.390  -7.535  21.217  1.00 59.56  ? 167 ASN A O   1 
ATOM   1448  C CB  . ASN A 1 167 ? 33.638  -7.804  21.826  1.00 55.93  ? 167 ASN A CB  1 
ATOM   1449  C CG  . ASN A 1 167 ? 34.620  -8.762  21.189  1.00 72.67  ? 167 ASN A CG  1 
ATOM   1450  O OD1 . ASN A 1 167 ? 34.334  -9.363  20.151  1.00 82.75  ? 167 ASN A OD1 1 
ATOM   1451  N ND2 . ASN A 1 167 ? 35.791  -8.899  21.798  1.00 74.78  ? 167 ASN A ND2 1 
ATOM   1452  N N   . LYS A 1 168 ? 31.297  -5.687  22.136  1.00 54.96  ? 168 LYS A N   1 
ATOM   1453  C CA  . LYS A 1 168 ? 30.012  -5.221  22.637  1.00 49.90  ? 168 LYS A CA  1 
ATOM   1454  C C   . LYS A 1 168 ? 29.038  -4.988  21.493  1.00 50.58  ? 168 LYS A C   1 
ATOM   1455  O O   . LYS A 1 168 ? 27.841  -5.261  21.626  1.00 55.99  ? 168 LYS A O   1 
ATOM   1456  C CB  . LYS A 1 168 ? 30.200  -3.944  23.455  1.00 47.42  ? 168 LYS A CB  1 
ATOM   1457  C CG  . LYS A 1 168 ? 30.717  -4.181  24.869  1.00 60.62  ? 168 LYS A CG  1 
ATOM   1458  C CD  . LYS A 1 168 ? 29.785  -5.103  25.663  1.00 76.09  ? 168 LYS A CD  1 
ATOM   1459  C CE  . LYS A 1 168 ? 29.679  -4.685  27.138  1.00 79.54  ? 168 LYS A CE  1 
ATOM   1460  N NZ  . LYS A 1 168 ? 28.305  -4.857  27.718  1.00 67.75  ? 168 LYS A NZ  1 
ATOM   1461  N N   . TYR A 1 169 ? 29.537  -4.498  20.353  1.00 46.04  ? 169 TYR A N   1 
ATOM   1462  C CA  . TYR A 1 169 ? 28.670  -4.283  19.199  1.00 41.44  ? 169 TYR A CA  1 
ATOM   1463  C C   . TYR A 1 169 ? 28.161  -5.601  18.648  1.00 46.06  ? 169 TYR A C   1 
ATOM   1464  O O   . TYR A 1 169 ? 27.008  -5.700  18.217  1.00 51.24  ? 169 TYR A O   1 
ATOM   1465  C CB  . TYR A 1 169 ? 29.401  -3.511  18.103  1.00 39.18  ? 169 TYR A CB  1 
ATOM   1466  C CG  . TYR A 1 169 ? 29.374  -2.006  18.268  1.00 42.85  ? 169 TYR A CG  1 
ATOM   1467  C CD1 . TYR A 1 169 ? 29.163  -1.436  19.511  1.00 40.46  ? 169 TYR A CD1 1 
ATOM   1468  C CD2 . TYR A 1 169 ? 29.572  -1.154  17.180  1.00 44.82  ? 169 TYR A CD2 1 
ATOM   1469  C CE1 . TYR A 1 169 ? 29.146  -0.070  19.681  1.00 39.65  ? 169 TYR A CE1 1 
ATOM   1470  C CE2 . TYR A 1 169 ? 29.553  0.231   17.342  1.00 44.02  ? 169 TYR A CE2 1 
ATOM   1471  C CZ  . TYR A 1 169 ? 29.339  0.763   18.606  1.00 42.35  ? 169 TYR A CZ  1 
ATOM   1472  O OH  . TYR A 1 169 ? 29.307  2.124   18.826  1.00 38.51  ? 169 TYR A OH  1 
ATOM   1473  N N   . PHE A 1 170 ? 29.001  -6.629  18.652  1.00 45.46  ? 170 PHE A N   1 
ATOM   1474  C CA  . PHE A 1 170 ? 28.554  -7.906  18.117  1.00 57.18  ? 170 PHE A CA  1 
ATOM   1475  C C   . PHE A 1 170 ? 27.652  -8.650  19.087  1.00 49.90  ? 170 PHE A C   1 
ATOM   1476  O O   . PHE A 1 170 ? 26.821  -9.451  18.648  1.00 51.85  ? 170 PHE A O   1 
ATOM   1477  C CB  . PHE A 1 170 ? 29.751  -8.768  17.733  1.00 62.94  ? 170 PHE A CB  1 
ATOM   1478  C CG  . PHE A 1 170 ? 30.223  -8.553  16.324  1.00 67.03  ? 170 PHE A CG  1 
ATOM   1479  C CD1 . PHE A 1 170 ? 29.551  -9.131  15.258  1.00 75.30  ? 170 PHE A CD1 1 
ATOM   1480  C CD2 . PHE A 1 170 ? 31.331  -7.764  16.061  1.00 65.56  ? 170 PHE A CD2 1 
ATOM   1481  C CE1 . PHE A 1 170 ? 29.992  -8.937  13.949  1.00 72.92  ? 170 PHE A CE1 1 
ATOM   1482  C CE2 . PHE A 1 170 ? 31.771  -7.566  14.766  1.00 66.56  ? 170 PHE A CE2 1 
ATOM   1483  C CZ  . PHE A 1 170 ? 31.103  -8.153  13.709  1.00 67.09  ? 170 PHE A CZ  1 
ATOM   1484  N N   . GLU A 1 171 ? 27.777  -8.392  20.390  1.00 50.14  ? 171 GLU A N   1 
ATOM   1485  C CA  . GLU A 1 171 ? 26.826  -8.968  21.339  1.00 56.66  ? 171 GLU A CA  1 
ATOM   1486  C C   . GLU A 1 171 ? 25.414  -8.463  21.072  1.00 51.09  ? 171 GLU A C   1 
ATOM   1487  O O   . GLU A 1 171 ? 24.443  -9.223  21.172  1.00 51.12  ? 171 GLU A O   1 
ATOM   1488  C CB  . GLU A 1 171 ? 27.242  -8.645  22.772  1.00 53.09  ? 171 GLU A CB  1 
ATOM   1489  C CG  . GLU A 1 171 ? 28.396  -9.494  23.268  1.00 66.86  ? 171 GLU A CG  1 
ATOM   1490  C CD  . GLU A 1 171 ? 29.153  -8.837  24.398  1.00 78.50  ? 171 GLU A CD  1 
ATOM   1491  O OE1 . GLU A 1 171 ? 28.496  -8.231  25.269  1.00 88.01  ? 171 GLU A OE1 1 
ATOM   1492  O OE2 . GLU A 1 171 ? 30.401  -8.936  24.422  1.00 76.18  ? 171 GLU A OE2 1 
ATOM   1493  N N   . ILE A 1 172 ? 25.290  -7.183  20.722  1.00 48.53  ? 172 ILE A N   1 
ATOM   1494  C CA  . ILE A 1 172 ? 23.996  -6.604  20.378  1.00 50.33  ? 172 ILE A CA  1 
ATOM   1495  C C   . ILE A 1 172 ? 23.435  -7.255  19.115  1.00 47.96  ? 172 ILE A C   1 
ATOM   1496  O O   . ILE A 1 172 ? 22.224  -7.487  18.997  1.00 54.42  ? 172 ILE A O   1 
ATOM   1497  C CB  . ILE A 1 172 ? 24.134  -5.075  20.230  1.00 43.93  ? 172 ILE A CB  1 
ATOM   1498  C CG1 . ILE A 1 172 ? 23.935  -4.347  21.571  1.00 49.55  ? 172 ILE A CG1 1 
ATOM   1499  C CG2 . ILE A 1 172 ? 23.096  -4.547  19.270  1.00 46.84  ? 172 ILE A CG2 1 
ATOM   1500  C CD1 . ILE A 1 172 ? 24.612  -4.952  22.796  1.00 54.72  ? 172 ILE A CD1 1 
ATOM   1501  N N   . ILE A 1 173 ? 24.304  -7.576  18.159  1.00 47.82  ? 173 ILE A N   1 
ATOM   1502  C CA  . ILE A 1 173 ? 23.851  -8.212  16.928  1.00 54.31  ? 173 ILE A CA  1 
ATOM   1503  C C   . ILE A 1 173 ? 23.364  -9.629  17.205  1.00 56.13  ? 173 ILE A C   1 
ATOM   1504  O O   . ILE A 1 173 ? 22.352  -10.080 16.646  1.00 52.15  ? 173 ILE A O   1 
ATOM   1505  C CB  . ILE A 1 173 ? 24.984  -8.176  15.888  1.00 57.19  ? 173 ILE A CB  1 
ATOM   1506  C CG1 . ILE A 1 173 ? 25.191  -6.733  15.414  1.00 53.45  ? 173 ILE A CG1 1 
ATOM   1507  C CG2 . ILE A 1 173 ? 24.684  -9.132  14.746  1.00 55.16  ? 173 ILE A CG2 1 
ATOM   1508  C CD1 . ILE A 1 173 ? 26.301  -6.556  14.408  1.00 54.82  ? 173 ILE A CD1 1 
ATOM   1509  N N   . LYS A 1 174 ? 24.063  -10.346 18.089  1.00 51.70  ? 174 LYS A N   1 
ATOM   1510  C CA  . LYS A 1 174 ? 23.655  -11.696 18.460  1.00 49.66  ? 174 LYS A CA  1 
ATOM   1511  C C   . LYS A 1 174 ? 22.351  -11.710 19.243  1.00 50.54  ? 174 LYS A C   1 
ATOM   1512  O O   . LYS A 1 174 ? 21.662  -12.735 19.260  1.00 55.33  ? 174 LYS A O   1 
ATOM   1513  C CB  . LYS A 1 174 ? 24.752  -12.377 19.282  1.00 52.12  ? 174 LYS A CB  1 
ATOM   1514  C CG  . LYS A 1 174 ? 25.903  -12.926 18.451  1.00 54.88  ? 174 LYS A CG  1 
ATOM   1515  C CD  . LYS A 1 174 ? 27.214  -12.910 19.218  1.00 57.34  ? 174 LYS A CD  1 
ATOM   1516  C CE  . LYS A 1 174 ? 28.387  -12.835 18.251  1.00 67.69  ? 174 LYS A CE  1 
ATOM   1517  N NZ  . LYS A 1 174 ? 28.910  -14.181 17.892  1.00 75.48  ? 174 LYS A NZ  1 
ATOM   1518  N N   . LYS A 1 175 ? 21.999  -10.600 19.887  1.00 51.70  ? 175 LYS A N   1 
ATOM   1519  C CA  . LYS A 1 175 ? 20.781  -10.503 20.682  1.00 50.19  ? 175 LYS A CA  1 
ATOM   1520  C C   . LYS A 1 175 ? 19.623  -9.876  19.921  1.00 52.19  ? 175 LYS A C   1 
ATOM   1521  O O   . LYS A 1 175 ? 18.517  -9.798  20.467  1.00 54.27  ? 175 LYS A O   1 
ATOM   1522  C CB  . LYS A 1 175 ? 21.050  -9.696  21.959  1.00 51.13  ? 175 LYS A CB  1 
ATOM   1523  C CG  . LYS A 1 175 ? 21.948  -10.399 22.974  1.00 51.15  ? 175 LYS A CG  1 
ATOM   1524  C CD  . LYS A 1 175 ? 22.226  -9.546  24.211  1.00 50.90  ? 175 LYS A CD  1 
ATOM   1525  C CE  . LYS A 1 175 ? 21.755  -8.106  24.045  1.00 57.03  ? 175 LYS A CE  1 
ATOM   1526  N NZ  . LYS A 1 175 ? 22.333  -7.193  25.075  1.00 64.41  ? 175 LYS A NZ  1 
ATOM   1527  N N   . THR A 1 176 ? 19.847  -9.444  18.679  1.00 49.27  ? 176 THR A N   1 
ATOM   1528  C CA  . THR A 1 176 ? 18.856  -8.641  17.976  1.00 46.31  ? 176 THR A CA  1 
ATOM   1529  C C   . THR A 1 176 ? 17.593  -9.441  17.695  1.00 47.97  ? 176 THR A C   1 
ATOM   1530  O O   . THR A 1 176 ? 16.492  -9.039  18.090  1.00 47.66  ? 176 THR A O   1 
ATOM   1531  C CB  . THR A 1 176 ? 19.457  -8.093  16.679  1.00 53.97  ? 176 THR A CB  1 
ATOM   1532  O OG1 . THR A 1 176 ? 20.396  -7.054  16.998  1.00 47.65  ? 176 THR A OG1 1 
ATOM   1533  C CG2 . THR A 1 176 ? 18.367  -7.534  15.748  1.00 35.13  ? 176 THR A CG2 1 
ATOM   1534  N N   . LEU A 1 177 ? 17.727  -10.587 17.027  1.00 49.86  ? 177 LEU A N   1 
ATOM   1535  C CA  . LEU A 1 177 ? 16.529  -11.304 16.603  1.00 53.22  ? 177 LEU A CA  1 
ATOM   1536  C C   . LEU A 1 177 ? 15.765  -11.918 17.769  1.00 48.73  ? 177 LEU A C   1 
ATOM   1537  O O   . LEU A 1 177 ? 14.559  -12.150 17.640  1.00 53.53  ? 177 LEU A O   1 
ATOM   1538  C CB  . LEU A 1 177 ? 16.878  -12.388 15.585  1.00 49.21  ? 177 LEU A CB  1 
ATOM   1539  C CG  . LEU A 1 177 ? 17.507  -11.858 14.302  1.00 53.75  ? 177 LEU A CG  1 
ATOM   1540  C CD1 . LEU A 1 177 ? 19.026  -11.849 14.453  1.00 60.89  ? 177 LEU A CD1 1 
ATOM   1541  C CD2 . LEU A 1 177 ? 17.065  -12.689 13.108  1.00 54.58  ? 177 LEU A CD2 1 
ATOM   1542  N N   . SER A 1 178 ? 16.426  -12.172 18.904  1.00 47.17  ? 178 SER A N   1 
ATOM   1543  C CA  . SER A 1 178 ? 15.710  -12.698 20.066  1.00 51.87  ? 178 SER A CA  1 
ATOM   1544  C C   . SER A 1 178 ? 14.759  -11.668 20.658  1.00 51.29  ? 178 SER A C   1 
ATOM   1545  O O   . SER A 1 178 ? 13.716  -12.036 21.212  1.00 54.53  ? 178 SER A O   1 
ATOM   1546  C CB  . SER A 1 178 ? 16.689  -13.169 21.146  1.00 48.07  ? 178 SER A CB  1 
ATOM   1547  O OG  . SER A 1 178 ? 17.210  -14.456 20.855  1.00 50.88  ? 178 SER A OG  1 
ATOM   1548  N N   . ILE A 1 179 ? 15.101  -10.382 20.555  1.00 47.47  ? 179 ILE A N   1 
ATOM   1549  C CA  . ILE A 1 179 ? 14.233  -9.346  21.098  1.00 48.30  ? 179 ILE A CA  1 
ATOM   1550  C C   . ILE A 1 179 ? 12.976  -9.190  20.245  1.00 52.08  ? 179 ILE A C   1 
ATOM   1551  O O   . ILE A 1 179 ? 11.904  -8.860  20.768  1.00 51.10  ? 179 ILE A O   1 
ATOM   1552  C CB  . ILE A 1 179 ? 15.003  -8.020  21.240  1.00 39.89  ? 179 ILE A CB  1 
ATOM   1553  C CG1 . ILE A 1 179 ? 14.546  -7.283  22.502  1.00 51.89  ? 179 ILE A CG1 1 
ATOM   1554  C CG2 . ILE A 1 179 ? 14.811  -7.140  20.017  1.00 48.86  ? 179 ILE A CG2 1 
ATOM   1555  C CD1 . ILE A 1 179 ? 15.337  -6.037  22.810  1.00 51.34  ? 179 ILE A CD1 1 
ATOM   1556  N N   . TYR A 1 180 ? 13.072  -9.431  18.932  1.00 47.38  ? 180 TYR A N   1 
ATOM   1557  C CA  . TYR A 1 180 ? 11.874  -9.397  18.101  1.00 46.49  ? 180 TYR A CA  1 
ATOM   1558  C C   . TYR A 1 180 ? 10.975  -10.581 18.417  1.00 52.75  ? 180 TYR A C   1 
ATOM   1559  O O   . TYR A 1 180 ? 9.746   -10.447 18.456  1.00 52.26  ? 180 TYR A O   1 
ATOM   1560  C CB  . TYR A 1 180 ? 12.250  -9.388  16.621  1.00 49.92  ? 180 TYR A CB  1 
ATOM   1561  C CG  . TYR A 1 180 ? 12.735  -8.046  16.116  1.00 47.75  ? 180 TYR A CG  1 
ATOM   1562  C CD1 . TYR A 1 180 ? 11.842  -7.018  15.835  1.00 45.64  ? 180 TYR A CD1 1 
ATOM   1563  C CD2 . TYR A 1 180 ? 14.084  -7.815  15.903  1.00 39.19  ? 180 TYR A CD2 1 
ATOM   1564  C CE1 . TYR A 1 180 ? 12.285  -5.795  15.368  1.00 41.16  ? 180 TYR A CE1 1 
ATOM   1565  C CE2 . TYR A 1 180 ? 14.533  -6.600  15.437  1.00 41.89  ? 180 TYR A CE2 1 
ATOM   1566  C CZ  . TYR A 1 180 ? 13.636  -5.592  15.170  1.00 44.04  ? 180 TYR A CZ  1 
ATOM   1567  O OH  . TYR A 1 180 ? 14.108  -4.383  14.704  1.00 41.73  ? 180 TYR A OH  1 
ATOM   1568  N N   . ARG A 1 181 ? 11.582  -11.744 18.659  1.00 55.84  ? 181 ARG A N   1 
ATOM   1569  C CA  . ARG A 1 181 ? 10.844  -12.883 19.188  1.00 52.10  ? 181 ARG A CA  1 
ATOM   1570  C C   . ARG A 1 181 ? 10.231  -12.552 20.543  1.00 53.93  ? 181 ARG A C   1 
ATOM   1571  O O   . ARG A 1 181 ? 9.057   -12.849 20.796  1.00 54.51  ? 181 ARG A O   1 
ATOM   1572  C CB  . ARG A 1 181 ? 11.768  -14.088 19.308  1.00 50.67  ? 181 ARG A CB  1 
ATOM   1573  C CG  . ARG A 1 181 ? 11.708  -15.033 18.147  1.00 52.43  ? 181 ARG A CG  1 
ATOM   1574  C CD  . ARG A 1 181 ? 12.101  -16.397 18.647  1.00 58.85  ? 181 ARG A CD  1 
ATOM   1575  N NE  . ARG A 1 181 ? 10.929  -17.120 19.128  1.00 65.70  ? 181 ARG A NE  1 
ATOM   1576  C CZ  . ARG A 1 181 ? 10.355  -18.162 18.537  1.00 64.74  ? 181 ARG A CZ  1 
ATOM   1577  N NH1 . ARG A 1 181 ? 10.898  -18.754 17.488  1.00 57.27  ? 181 ARG A NH1 1 
ATOM   1578  N NH2 . ARG A 1 181 ? 9.223   -18.649 19.040  1.00 72.07  ? 181 ARG A NH2 1 
ATOM   1579  N N   . GLU A 1 182 ? 11.013  -11.916 21.424  1.00 52.71  ? 182 GLU A N   1 
ATOM   1580  C CA  . GLU A 1 182 ? 10.548  -11.640 22.780  1.00 57.99  ? 182 GLU A CA  1 
ATOM   1581  C C   . GLU A 1 182 ? 9.364   -10.677 22.784  1.00 60.52  ? 182 GLU A C   1 
ATOM   1582  O O   . GLU A 1 182 ? 8.378   -10.898 23.498  1.00 56.49  ? 182 GLU A O   1 
ATOM   1583  C CB  . GLU A 1 182 ? 11.691  -11.080 23.630  1.00 56.15  ? 182 GLU A CB  1 
ATOM   1584  C CG  . GLU A 1 182 ? 11.213  -10.331 24.859  1.00 65.50  ? 182 GLU A CG  1 
ATOM   1585  C CD  . GLU A 1 182 ? 12.337  -9.634  25.600  1.00 87.37  ? 182 GLU A CD  1 
ATOM   1586  O OE1 . GLU A 1 182 ? 13.481  -10.138 25.561  1.00 87.28  ? 182 GLU A OE1 1 
ATOM   1587  O OE2 . GLU A 1 182 ? 12.073  -8.593  26.239  1.00 98.75  ? 182 GLU A OE2 1 
ATOM   1588  N N   . ILE A 1 183 ? 9.432   -9.605  21.992  1.00 51.93  ? 183 ILE A N   1 
ATOM   1589  C CA  . ILE A 1 183 ? 8.332   -8.649  22.031  1.00 48.85  ? 183 ILE A CA  1 
ATOM   1590  C C   . ILE A 1 183 ? 7.092   -9.215  21.352  1.00 56.41  ? 183 ILE A C   1 
ATOM   1591  O O   . ILE A 1 183 ? 5.963   -8.851  21.714  1.00 53.44  ? 183 ILE A O   1 
ATOM   1592  C CB  . ILE A 1 183 ? 8.746   -7.296  21.425  1.00 43.20  ? 183 ILE A CB  1 
ATOM   1593  C CG1 . ILE A 1 183 ? 9.071   -7.424  19.932  1.00 44.94  ? 183 ILE A CG1 1 
ATOM   1594  C CG2 . ILE A 1 183 ? 9.870   -6.696  22.224  1.00 38.87  ? 183 ILE A CG2 1 
ATOM   1595  C CD1 . ILE A 1 183 ? 8.017   -6.841  19.020  1.00 37.97  ? 183 ILE A CD1 1 
ATOM   1596  N N   . LYS A 1 184 ? 7.264   -10.104 20.365  1.00 52.59  ? 184 LYS A N   1 
ATOM   1597  C CA  . LYS A 1 184 ? 6.104   -10.758 19.759  1.00 59.94  ? 184 LYS A CA  1 
ATOM   1598  C C   . LYS A 1 184 ? 5.422   -11.701 20.741  1.00 61.07  ? 184 LYS A C   1 
ATOM   1599  O O   . LYS A 1 184 ? 4.190   -11.707 20.850  1.00 57.09  ? 184 LYS A O   1 
ATOM   1600  C CB  . LYS A 1 184 ? 6.497   -11.516 18.490  1.00 52.45  ? 184 LYS A CB  1 
ATOM   1601  C CG  . LYS A 1 184 ? 5.451   -11.379 17.381  1.00 53.35  ? 184 LYS A CG  1 
ATOM   1602  C CD  . LYS A 1 184 ? 5.709   -12.284 16.178  1.00 51.52  ? 184 LYS A CD  1 
ATOM   1603  C CE  . LYS A 1 184 ? 5.340   -13.716 16.460  1.00 46.64  ? 184 LYS A CE  1 
ATOM   1604  N NZ  . LYS A 1 184 ? 3.961   -13.729 16.993  1.00 65.76  ? 184 LYS A NZ  1 
ATOM   1605  N N   . GLU A 1 185 ? 6.206   -12.517 21.453  1.00 59.26  ? 185 GLU A N   1 
ATOM   1606  C CA  . GLU A 1 185 ? 5.621   -13.455 22.403  1.00 55.26  ? 185 GLU A CA  1 
ATOM   1607  C C   . GLU A 1 185 ? 5.036   -12.742 23.608  1.00 47.20  ? 185 GLU A C   1 
ATOM   1608  O O   . GLU A 1 185 ? 4.091   -13.246 24.219  1.00 61.22  ? 185 GLU A O   1 
ATOM   1609  C CB  . GLU A 1 185 ? 6.664   -14.470 22.866  1.00 68.35  ? 185 GLU A CB  1 
ATOM   1610  C CG  . GLU A 1 185 ? 6.582   -15.823 22.167  1.00 79.61  ? 185 GLU A CG  1 
ATOM   1611  C CD  . GLU A 1 185 ? 7.940   -16.334 21.721  1.00 82.69  ? 185 GLU A CD  1 
ATOM   1612  O OE1 . GLU A 1 185 ? 8.966   -15.818 22.217  1.00 78.02  ? 185 GLU A OE1 1 
ATOM   1613  O OE2 . GLU A 1 185 ? 7.981   -17.252 20.875  1.00 103.91 ? 185 GLU A OE2 1 
ATOM   1614  N N   . GLU A 1 186 ? 5.586   -11.587 23.975  1.00 48.81  ? 186 GLU A N   1 
ATOM   1615  C CA  . GLU A 1 186 ? 5.113   -10.883 25.159  1.00 56.36  ? 186 GLU A CA  1 
ATOM   1616  C C   . GLU A 1 186 ? 3.894   -10.015 24.880  1.00 53.10  ? 186 GLU A C   1 
ATOM   1617  O O   . GLU A 1 186 ? 3.353   -9.412  25.811  1.00 46.60  ? 186 GLU A O   1 
ATOM   1618  C CB  . GLU A 1 186 ? 6.246   -10.038 25.755  1.00 56.57  ? 186 GLU A CB  1 
ATOM   1619  C CG  . GLU A 1 186 ? 6.858   -10.640 27.025  1.00 64.34  ? 186 GLU A CG  1 
ATOM   1620  C CD  . GLU A 1 186 ? 8.274   -10.151 27.304  1.00 76.19  ? 186 GLU A CD  1 
ATOM   1621  O OE1 . GLU A 1 186 ? 8.477   -8.927  27.457  1.00 77.36  ? 186 GLU A OE1 1 
ATOM   1622  O OE2 . GLU A 1 186 ? 9.188   -11.000 27.382  1.00 78.93  ? 186 GLU A OE2 1 
ATOM   1623  N N   . GLY A 1 187 ? 3.435   -9.955  23.634  1.00 56.86  ? 187 GLY A N   1 
ATOM   1624  C CA  . GLY A 1 187 ? 2.340   -9.081  23.280  1.00 54.21  ? 187 GLY A CA  1 
ATOM   1625  C C   . GLY A 1 187 ? 2.701   -7.618  23.178  1.00 51.75  ? 187 GLY A C   1 
ATOM   1626  O O   . GLY A 1 187 ? 1.813   -6.795  22.913  1.00 51.74  ? 187 GLY A O   1 
ATOM   1627  N N   . LYS A 1 188 ? 3.973   -7.264  23.372  1.00 48.65  ? 188 LYS A N   1 
ATOM   1628  C CA  . LYS A 1 188 ? 4.381   -5.868  23.335  1.00 44.38  ? 188 LYS A CA  1 
ATOM   1629  C C   . LYS A 1 188 ? 4.432   -5.324  21.918  1.00 40.84  ? 188 LYS A C   1 
ATOM   1630  O O   . LYS A 1 188 ? 4.643   -4.118  21.733  1.00 42.23  ? 188 LYS A O   1 
ATOM   1631  C CB  . LYS A 1 188 ? 5.734   -5.715  24.028  1.00 45.71  ? 188 LYS A CB  1 
ATOM   1632  C CG  . LYS A 1 188 ? 5.774   -6.363  25.403  1.00 46.14  ? 188 LYS A CG  1 
ATOM   1633  C CD  . LYS A 1 188 ? 7.041   -6.019  26.165  1.00 54.50  ? 188 LYS A CD  1 
ATOM   1634  C CE  . LYS A 1 188 ? 6.751   -5.813  27.643  1.00 62.86  ? 188 LYS A CE  1 
ATOM   1635  N NZ  . LYS A 1 188 ? 6.298   -7.059  28.320  1.00 66.94  ? 188 LYS A NZ  1 
ATOM   1636  N N   . GLY A 1 189 ? 4.238   -6.175  20.925  1.00 41.13  ? 189 GLY A N   1 
ATOM   1637  C CA  . GLY A 1 189 ? 4.144   -5.708  19.562  1.00 40.59  ? 189 GLY A CA  1 
ATOM   1638  C C   . GLY A 1 189 ? 4.055   -6.873  18.601  1.00 47.82  ? 189 GLY A C   1 
ATOM   1639  O O   . GLY A 1 189 ? 4.378   -8.021  18.937  1.00 48.92  ? 189 GLY A O   1 
ATOM   1640  N N   . SER A 1 190 ? 3.610   -6.550  17.396  1.00 46.30  ? 190 SER A N   1 
ATOM   1641  C CA  . SER A 1 190 ? 3.475   -7.511  16.313  1.00 45.78  ? 190 SER A CA  1 
ATOM   1642  C C   . SER A 1 190 ? 4.629   -7.340  15.335  1.00 51.95  ? 190 SER A C   1 
ATOM   1643  O O   . SER A 1 190 ? 5.075   -6.217  15.070  1.00 51.19  ? 190 SER A O   1 
ATOM   1644  C CB  . SER A 1 190 ? 2.138   -7.328  15.591  1.00 42.34  ? 190 SER A CB  1 
ATOM   1645  O OG  . SER A 1 190 ? 1.086   -7.915  16.330  1.00 45.63  ? 190 SER A OG  1 
ATOM   1646  N N   . VAL A 1 191 ? 5.120   -8.459  14.810  1.00 48.29  ? 191 VAL A N   1 
ATOM   1647  C CA  . VAL A 1 191 ? 6.192   -8.459  13.823  1.00 46.26  ? 191 VAL A CA  1 
ATOM   1648  C C   . VAL A 1 191 ? 5.639   -8.949  12.496  1.00 48.33  ? 191 VAL A C   1 
ATOM   1649  O O   . VAL A 1 191 ? 4.875   -9.920  12.440  1.00 53.72  ? 191 VAL A O   1 
ATOM   1650  C CB  . VAL A 1 191 ? 7.392   -9.321  14.252  1.00 51.96  ? 191 VAL A CB  1 
ATOM   1651  C CG1 . VAL A 1 191 ? 8.510   -9.176  13.236  1.00 43.66  ? 191 VAL A CG1 1 
ATOM   1652  C CG2 . VAL A 1 191 ? 7.873   -8.930  15.658  1.00 51.85  ? 191 VAL A CG2 1 
ATOM   1653  N N   . SER A 1 192 ? 6.039   -8.276  11.429  1.00 53.42  ? 192 SER A N   1 
ATOM   1654  C CA  . SER A 1 192 ? 5.609   -8.563  10.074  1.00 46.28  ? 192 SER A CA  1 
ATOM   1655  C C   . SER A 1 192 ? 6.843   -8.725  9.196   1.00 54.24  ? 192 SER A C   1 
ATOM   1656  O O   . SER A 1 192 ? 7.980   -8.521  9.634   1.00 50.58  ? 192 SER A O   1 
ATOM   1657  C CB  . SER A 1 192 ? 4.720   -7.437  9.544   1.00 47.70  ? 192 SER A CB  1 
ATOM   1658  O OG  . SER A 1 192 ? 5.534   -6.321  9.199   1.00 51.48  ? 192 SER A OG  1 
ATOM   1659  N N   . THR A 1 193 ? 6.613   -9.077  7.935   1.00 58.91  ? 193 THR A N   1 
ATOM   1660  C CA  . THR A 1 193 ? 7.690   -9.240  6.971   1.00 55.24  ? 193 THR A CA  1 
ATOM   1661  C C   . THR A 1 193 ? 7.244   -8.693  5.622   1.00 49.29  ? 193 THR A C   1 
ATOM   1662  O O   . THR A 1 193 ? 6.091   -8.301  5.432   1.00 43.57  ? 193 THR A O   1 
ATOM   1663  C CB  . THR A 1 193 ? 8.118   -10.708 6.846   1.00 58.38  ? 193 THR A CB  1 
ATOM   1664  O OG1 . THR A 1 193 ? 9.484   -10.765 6.417   1.00 56.63  ? 193 THR A OG1 1 
ATOM   1665  C CG2 . THR A 1 193 ? 7.220   -11.458 5.841   1.00 50.82  ? 193 THR A CG2 1 
ATOM   1666  N N   . SER A 1 194 ? 8.184   -8.644  4.692   1.00 49.99  ? 194 SER A N   1 
ATOM   1667  C CA  . SER A 1 194 ? 7.895   -8.235  3.328   1.00 49.55  ? 194 SER A CA  1 
ATOM   1668  C C   . SER A 1 194 ? 8.275   -9.385  2.406   1.00 53.10  ? 194 SER A C   1 
ATOM   1669  O O   . SER A 1 194 ? 8.928   -10.336 2.857   1.00 53.89  ? 194 SER A O   1 
ATOM   1670  C CB  . SER A 1 194 ? 8.671   -6.966  2.960   1.00 50.94  ? 194 SER A CB  1 
ATOM   1671  O OG  . SER A 1 194 ? 8.376   -5.887  3.831   1.00 53.02  ? 194 SER A OG  1 
ATOM   1672  N N   . PRO A 1 195 ? 7.882   -9.352  1.129   1.00 53.83  ? 195 PRO A N   1 
ATOM   1673  C CA  . PRO A 1 195 ? 8.466   -10.287 0.164   1.00 54.03  ? 195 PRO A CA  1 
ATOM   1674  C C   . PRO A 1 195 ? 9.988   -10.252 0.239   1.00 55.89  ? 195 PRO A C   1 
ATOM   1675  O O   . PRO A 1 195 ? 10.591  -9.201  0.486   1.00 44.95  ? 195 PRO A O   1 
ATOM   1676  C CB  . PRO A 1 195 ? 7.950   -9.769  -1.179  1.00 46.97  ? 195 PRO A CB  1 
ATOM   1677  C CG  . PRO A 1 195 ? 6.619   -9.189  -0.829  1.00 50.21  ? 195 PRO A CG  1 
ATOM   1678  C CD  . PRO A 1 195 ? 6.834   -8.521  0.506   1.00 44.01  ? 195 PRO A CD  1 
ATOM   1679  N N   . TYR A 1 196 ? 10.595  -11.414 -0.040  1.00 55.12  ? 196 TYR A N   1 
ATOM   1680  C CA  . TYR A 1 196 ? 11.943  -11.747 0.424   1.00 58.43  ? 196 TYR A CA  1 
ATOM   1681  C C   . TYR A 1 196 ? 12.951  -10.626 0.188   1.00 55.64  ? 196 TYR A C   1 
ATOM   1682  O O   . TYR A 1 196 ? 13.632  -10.175 1.118   1.00 46.16  ? 196 TYR A O   1 
ATOM   1683  C CB  . TYR A 1 196 ? 12.422  -13.044 -0.243  1.00 49.87  ? 196 TYR A CB  1 
ATOM   1684  C CG  . TYR A 1 196 ? 13.482  -13.742 0.569   1.00 53.00  ? 196 TYR A CG  1 
ATOM   1685  C CD1 . TYR A 1 196 ? 14.780  -13.255 0.613   1.00 60.73  ? 196 TYR A CD1 1 
ATOM   1686  C CD2 . TYR A 1 196 ? 13.187  -14.885 1.299   1.00 51.87  ? 196 TYR A CD2 1 
ATOM   1687  C CE1 . TYR A 1 196 ? 15.757  -13.886 1.357   1.00 54.92  ? 196 TYR A CE1 1 
ATOM   1688  C CE2 . TYR A 1 196 ? 14.157  -15.525 2.054   1.00 48.51  ? 196 TYR A CE2 1 
ATOM   1689  C CZ  . TYR A 1 196 ? 15.441  -15.019 2.077   1.00 57.57  ? 196 TYR A CZ  1 
ATOM   1690  O OH  . TYR A 1 196 ? 16.416  -15.641 2.821   1.00 74.78  ? 196 TYR A OH  1 
ATOM   1691  N N   . TYR A 1 197 ? 13.082  -10.184 -1.055  1.00 50.88  ? 197 TYR A N   1 
ATOM   1692  C CA  . TYR A 1 197 ? 14.147  -9.264  -1.433  1.00 51.88  ? 197 TYR A CA  1 
ATOM   1693  C C   . TYR A 1 197 ? 13.599  -7.881  -1.764  1.00 52.32  ? 197 TYR A C   1 
ATOM   1694  O O   . TYR A 1 197 ? 14.073  -7.209  -2.681  1.00 55.64  ? 197 TYR A O   1 
ATOM   1695  C CB  . TYR A 1 197 ? 14.950  -9.825  -2.604  1.00 55.82  ? 197 TYR A CB  1 
ATOM   1696  C CG  . TYR A 1 197 ? 15.833  -11.001 -2.239  1.00 53.74  ? 197 TYR A CG  1 
ATOM   1697  C CD1 . TYR A 1 197 ? 16.990  -10.826 -1.485  1.00 48.91  ? 197 TYR A CD1 1 
ATOM   1698  C CD2 . TYR A 1 197 ? 15.510  -12.285 -2.652  1.00 58.37  ? 197 TYR A CD2 1 
ATOM   1699  C CE1 . TYR A 1 197 ? 17.796  -11.899 -1.158  1.00 52.40  ? 197 TYR A CE1 1 
ATOM   1700  C CE2 . TYR A 1 197 ? 16.309  -13.364 -2.330  1.00 56.16  ? 197 TYR A CE2 1 
ATOM   1701  C CZ  . TYR A 1 197 ? 17.447  -13.168 -1.581  1.00 58.60  ? 197 TYR A CZ  1 
ATOM   1702  O OH  . TYR A 1 197 ? 18.231  -14.251 -1.266  1.00 65.07  ? 197 TYR A OH  1 
ATOM   1703  N N   . HIS A 1 198 ? 12.596  -7.444  -1.008  1.00 55.41  ? 198 HIS A N   1 
ATOM   1704  C CA  . HIS A 1 198 ? 11.998  -6.126  -1.164  1.00 49.73  ? 198 HIS A CA  1 
ATOM   1705  C C   . HIS A 1 198 ? 11.660  -5.780  -2.621  1.00 55.50  ? 198 HIS A C   1 
ATOM   1706  O O   . HIS A 1 198 ? 11.976  -4.688  -3.092  1.00 55.53  ? 198 HIS A O   1 
ATOM   1707  C CB  . HIS A 1 198 ? 12.918  -5.068  -0.573  1.00 42.37  ? 198 HIS A CB  1 
ATOM   1708  C CG  . HIS A 1 198 ? 12.191  -3.906  0.012   1.00 47.36  ? 198 HIS A CG  1 
ATOM   1709  N ND1 . HIS A 1 198 ? 12.095  -2.693  -0.635  1.00 49.35  ? 198 HIS A ND1 1 
ATOM   1710  C CD2 . HIS A 1 198 ? 11.512  -3.771  1.176   1.00 48.06  ? 198 HIS A CD2 1 
ATOM   1711  C CE1 . HIS A 1 198 ? 11.389  -1.859  0.107   1.00 53.50  ? 198 HIS A CE1 1 
ATOM   1712  N NE2 . HIS A 1 198 ? 11.024  -2.488  1.211   1.00 53.20  ? 198 HIS A NE2 1 
ATOM   1713  N N   . PRO A 1 199 ? 11.026  -6.691  -3.355  1.00 56.31  ? 199 PRO A N   1 
ATOM   1714  C CA  . PRO A 1 199 ? 10.736  -6.423  -4.764  1.00 53.52  ? 199 PRO A CA  1 
ATOM   1715  C C   . PRO A 1 199 ? 9.540   -5.488  -4.893  1.00 57.33  ? 199 PRO A C   1 
ATOM   1716  O O   . PRO A 1 199 ? 8.881   -5.138  -3.915  1.00 59.13  ? 199 PRO A O   1 
ATOM   1717  C CB  . PRO A 1 199 ? 10.422  -7.816  -5.306  1.00 53.36  ? 199 PRO A CB  1 
ATOM   1718  C CG  . PRO A 1 199 ? 9.725   -8.463  -4.157  1.00 52.19  ? 199 PRO A CG  1 
ATOM   1719  C CD  . PRO A 1 199 ? 10.425  -7.968  -2.922  1.00 50.08  ? 199 PRO A CD  1 
ATOM   1720  N N   . LEU A 1 200 ? 9.263   -5.082  -6.129  1.00 57.72  ? 200 LEU A N   1 
ATOM   1721  C CA  . LEU A 1 200 ? 8.065   -4.295  -6.429  1.00 56.19  ? 200 LEU A CA  1 
ATOM   1722  C C   . LEU A 1 200 ? 7.047   -5.243  -7.060  1.00 55.01  ? 200 LEU A C   1 
ATOM   1723  O O   . LEU A 1 200 ? 7.072   -5.497  -8.263  1.00 56.37  ? 200 LEU A O   1 
ATOM   1724  C CB  . LEU A 1 200 ? 8.402   -3.109  -7.327  1.00 53.87  ? 200 LEU A CB  1 
ATOM   1725  C CG  . LEU A 1 200 ? 8.886   -1.872  -6.560  1.00 52.44  ? 200 LEU A CG  1 
ATOM   1726  C CD1 . LEU A 1 200 ? 9.661   -0.934  -7.462  1.00 59.55  ? 200 LEU A CD1 1 
ATOM   1727  C CD2 . LEU A 1 200 ? 7.732   -1.132  -5.908  1.00 47.12  ? 200 LEU A CD2 1 
ATOM   1728  N N   . ILE A 1 201 ? 6.140   -5.768  -6.219  1.00 58.51  ? 201 ILE A N   1 
ATOM   1729  C CA  . ILE A 1 201 ? 5.229   -6.835  -6.667  1.00 53.66  ? 201 ILE A CA  1 
ATOM   1730  C C   . ILE A 1 201 ? 4.275   -6.391  -7.769  1.00 53.33  ? 201 ILE A C   1 
ATOM   1731  O O   . ILE A 1 201 ? 4.033   -7.180  -8.699  1.00 53.71  ? 201 ILE A O   1 
ATOM   1732  C CB  . ILE A 1 201 ? 4.500   -7.446  -5.461  1.00 44.99  ? 201 ILE A CB  1 
ATOM   1733  C CG1 . ILE A 1 201 ? 5.496   -8.131  -4.514  1.00 45.70  ? 201 ILE A CG1 1 
ATOM   1734  C CG2 . ILE A 1 201 ? 3.408   -8.405  -5.918  1.00 41.56  ? 201 ILE A CG2 1 
ATOM   1735  C CD1 . ILE A 1 201 ? 5.913   -9.533  -4.954  1.00 46.38  ? 201 ILE A CD1 1 
ATOM   1736  N N   . PRO A 1 202 ? 3.673   -5.192  -7.734  1.00 48.07  ? 202 PRO A N   1 
ATOM   1737  C CA  . PRO A 1 202 ? 2.800   -4.792  -8.855  1.00 48.71  ? 202 PRO A CA  1 
ATOM   1738  C C   . PRO A 1 202 ? 3.474   -4.873  -10.216 1.00 52.06  ? 202 PRO A C   1 
ATOM   1739  O O   . PRO A 1 202 ? 2.831   -5.261  -11.199 1.00 55.52  ? 202 PRO A O   1 
ATOM   1740  C CB  . PRO A 1 202 ? 2.418   -3.351  -8.495  1.00 43.44  ? 202 PRO A CB  1 
ATOM   1741  C CG  . PRO A 1 202 ? 2.498   -3.312  -7.009  1.00 46.39  ? 202 PRO A CG  1 
ATOM   1742  C CD  . PRO A 1 202 ? 3.646   -4.199  -6.643  1.00 46.74  ? 202 PRO A CD  1 
ATOM   1743  N N   . ILE A 1 203 ? 4.763   -4.532  -10.293 1.00 52.65  ? 203 ILE A N   1 
ATOM   1744  C CA  . ILE A 1 203 ? 5.473   -4.561  -11.569 1.00 55.43  ? 203 ILE A CA  1 
ATOM   1745  C C   . ILE A 1 203 ? 5.743   -5.997  -12.003 1.00 53.46  ? 203 ILE A C   1 
ATOM   1746  O O   . ILE A 1 203 ? 5.557   -6.350  -13.174 1.00 57.14  ? 203 ILE A O   1 
ATOM   1747  C CB  . ILE A 1 203 ? 6.768   -3.732  -11.472 1.00 55.50  ? 203 ILE A CB  1 
ATOM   1748  C CG1 . ILE A 1 203 ? 6.420   -2.262  -11.228 1.00 52.64  ? 203 ILE A CG1 1 
ATOM   1749  C CG2 . ILE A 1 203 ? 7.617   -3.887  -12.726 1.00 48.77  ? 203 ILE A CG2 1 
ATOM   1750  C CD1 . ILE A 1 203 ? 7.550   -1.312  -11.517 1.00 53.65  ? 203 ILE A CD1 1 
ATOM   1751  N N   . LEU A 1 204 ? 6.182   -6.850  -11.074 1.00 51.26  ? 204 LEU A N   1 
ATOM   1752  C CA  . LEU A 1 204 ? 6.453   -8.242  -11.421 1.00 53.72  ? 204 LEU A CA  1 
ATOM   1753  C C   . LEU A 1 204 ? 5.199   -8.950  -11.926 1.00 57.23  ? 204 LEU A C   1 
ATOM   1754  O O   . LEU A 1 204 ? 5.265   -9.739  -12.877 1.00 63.16  ? 204 LEU A O   1 
ATOM   1755  C CB  . LEU A 1 204 ? 7.026   -8.980  -10.215 1.00 52.85  ? 204 LEU A CB  1 
ATOM   1756  C CG  . LEU A 1 204 ? 8.336   -8.413  -9.681  1.00 55.18  ? 204 LEU A CG  1 
ATOM   1757  C CD1 . LEU A 1 204 ? 8.887   -9.284  -8.553  1.00 57.12  ? 204 LEU A CD1 1 
ATOM   1758  C CD2 . LEU A 1 204 ? 9.335   -8.272  -10.817 1.00 49.64  ? 204 LEU A CD2 1 
ATOM   1759  N N   . LEU A 1 205 ? 4.049   -8.684  -11.299 1.00 56.91  ? 205 LEU A N   1 
ATOM   1760  C CA  . LEU A 1 205 ? 2.805   -9.333  -11.700 1.00 58.16  ? 205 LEU A CA  1 
ATOM   1761  C C   . LEU A 1 205 ? 2.306   -8.798  -13.035 1.00 49.87  ? 205 LEU A C   1 
ATOM   1762  O O   . LEU A 1 205 ? 2.088   -9.560  -13.982 1.00 49.08  ? 205 LEU A O   1 
ATOM   1763  C CB  . LEU A 1 205 ? 1.737   -9.139  -10.623 1.00 57.59  ? 205 LEU A CB  1 
ATOM   1764  C CG  . LEU A 1 205 ? 2.019   -9.844  -9.300  1.00 53.82  ? 205 LEU A CG  1 
ATOM   1765  C CD1 . LEU A 1 205 ? 0.845   -9.681  -8.336  1.00 51.41  ? 205 LEU A CD1 1 
ATOM   1766  C CD2 . LEU A 1 205 ? 2.334   -11.315 -9.560  1.00 46.59  ? 205 LEU A CD2 1 
ATOM   1767  N N   . ASN A 1 206 ? 2.091   -7.498  -13.120 1.00 48.52  ? 206 ASN A N   1 
ATOM   1768  C CA  . ASN A 1 206 ? 1.733   -6.893  -14.390 1.00 50.70  ? 206 ASN A CA  1 
ATOM   1769  C C   . ASN A 1 206 ? 2.433   -5.549  -14.536 1.00 56.61  ? 206 ASN A C   1 
ATOM   1770  O O   . ASN A 1 206 ? 2.123   -4.604  -13.796 1.00 54.94  ? 206 ASN A O   1 
ATOM   1771  C CB  . ASN A 1 206 ? 0.216   -6.730  -14.511 1.00 61.38  ? 206 ASN A CB  1 
ATOM   1772  C CG  . ASN A 1 206 ? -0.177  -5.835  -15.669 1.00 66.44  ? 206 ASN A CG  1 
ATOM   1773  O OD1 . ASN A 1 206 ? -0.655  -4.726  -15.460 1.00 78.37  ? 206 ASN A OD1 1 
ATOM   1774  N ND2 . ASN A 1 206 ? 0.037   -6.306  -16.896 1.00 70.90  ? 206 ASN A ND2 1 
ATOM   1775  N N   . PRO A 1 207 ? 3.384   -5.422  -15.468 1.00 57.06  ? 207 PRO A N   1 
ATOM   1776  C CA  . PRO A 1 207 ? 4.092   -4.140  -15.636 1.00 50.99  ? 207 PRO A CA  1 
ATOM   1777  C C   . PRO A 1 207 ? 3.209   -2.999  -16.095 1.00 56.19  ? 207 PRO A C   1 
ATOM   1778  O O   . PRO A 1 207 ? 3.599   -1.834  -15.926 1.00 51.27  ? 207 PRO A O   1 
ATOM   1779  C CB  . PRO A 1 207 ? 5.157   -4.483  -16.685 1.00 55.36  ? 207 PRO A CB  1 
ATOM   1780  C CG  . PRO A 1 207 ? 5.393   -5.932  -16.474 1.00 51.14  ? 207 PRO A CG  1 
ATOM   1781  C CD  . PRO A 1 207 ? 4.007   -6.474  -16.282 1.00 55.04  ? 207 PRO A CD  1 
ATOM   1782  N N   . ASN A 1 208 ? 2.030   -3.291  -16.662 1.00 69.18  ? 208 ASN A N   1 
ATOM   1783  C CA  . ASN A 1 208 ? 1.066   -2.265  -17.042 1.00 58.96  ? 208 ASN A CA  1 
ATOM   1784  C C   . ASN A 1 208 ? 0.535   -1.466  -15.860 1.00 59.80  ? 208 ASN A C   1 
ATOM   1785  O O   . ASN A 1 208 ? -0.290  -0.571  -16.078 1.00 60.44  ? 208 ASN A O   1 
ATOM   1786  C CB  . ASN A 1 208 ? -0.097  -2.897  -17.790 1.00 53.98  ? 208 ASN A CB  1 
ATOM   1787  C CG  . ASN A 1 208 ? 0.298   -3.333  -19.162 1.00 63.79  ? 208 ASN A CG  1 
ATOM   1788  O OD1 . ASN A 1 208 ? 0.378   -4.520  -19.456 1.00 74.65  ? 208 ASN A OD1 1 
ATOM   1789  N ND2 . ASN A 1 208 ? 0.618   -2.363  -20.006 1.00 63.16  ? 208 ASN A ND2 1 
ATOM   1790  N N   . CYS A 1 209 ? 0.957   -1.763  -14.627 1.00 57.95  ? 209 CYS A N   1 
ATOM   1791  C CA  . CYS A 1 209 ? 0.527   -0.973  -13.474 1.00 60.82  ? 209 CYS A CA  1 
ATOM   1792  C C   . CYS A 1 209 ? 1.132   0.422   -13.462 1.00 60.42  ? 209 CYS A C   1 
ATOM   1793  O O   . CYS A 1 209 ? 0.652   1.282   -12.715 1.00 67.09  ? 209 CYS A O   1 
ATOM   1794  C CB  . CYS A 1 209 ? 0.883   -1.694  -12.175 1.00 50.18  ? 209 CYS A CB  1 
ATOM   1795  S SG  . CYS A 1 209 ? 2.648   -2.058  -11.983 1.00 64.86  ? 209 CYS A SG  1 
ATOM   1796  N N   . VAL A 1 210 ? 2.181   0.667   -14.252 1.00 50.74  ? 210 VAL A N   1 
ATOM   1797  C CA  . VAL A 1 210 ? 2.803   1.986   -14.215 1.00 61.39  ? 210 VAL A CA  1 
ATOM   1798  C C   . VAL A 1 210 ? 1.926   3.013   -14.911 1.00 55.81  ? 210 VAL A C   1 
ATOM   1799  O O   . VAL A 1 210 ? 1.980   4.203   -14.587 1.00 59.54  ? 210 VAL A O   1 
ATOM   1800  C CB  . VAL A 1 210 ? 4.214   1.940   -14.827 1.00 60.48  ? 210 VAL A CB  1 
ATOM   1801  C CG1 . VAL A 1 210 ? 4.966   0.720   -14.326 1.00 55.96  ? 210 VAL A CG1 1 
ATOM   1802  C CG2 . VAL A 1 210 ? 4.131   1.953   -16.351 1.00 52.39  ? 210 VAL A CG2 1 
ATOM   1803  N N   . TYR A 1 211 ? 1.097   2.583   -15.855 1.00 57.16  ? 211 TYR A N   1 
ATOM   1804  C CA  . TYR A 1 211 ? 0.289   3.532   -16.605 1.00 60.83  ? 211 TYR A CA  1 
ATOM   1805  C C   . TYR A 1 211 ? -0.965  3.968   -15.863 1.00 59.34  ? 211 TYR A C   1 
ATOM   1806  O O   . TYR A 1 211 ? -1.654  4.878   -16.339 1.00 56.07  ? 211 TYR A O   1 
ATOM   1807  C CB  . TYR A 1 211 ? -0.102  2.937   -17.950 1.00 54.10  ? 211 TYR A CB  1 
ATOM   1808  C CG  . TYR A 1 211 ? 1.040   2.371   -18.754 1.00 54.18  ? 211 TYR A CG  1 
ATOM   1809  C CD1 . TYR A 1 211 ? 1.992   3.202   -19.320 1.00 52.88  ? 211 TYR A CD1 1 
ATOM   1810  C CD2 . TYR A 1 211 ? 1.151   1.004   -18.967 1.00 53.51  ? 211 TYR A CD2 1 
ATOM   1811  C CE1 . TYR A 1 211 ? 3.025   2.693   -20.075 1.00 52.55  ? 211 TYR A CE1 1 
ATOM   1812  C CE2 . TYR A 1 211 ? 2.178   0.483   -19.718 1.00 51.88  ? 211 TYR A CE2 1 
ATOM   1813  C CZ  . TYR A 1 211 ? 3.115   1.331   -20.271 1.00 56.74  ? 211 TYR A CZ  1 
ATOM   1814  O OH  . TYR A 1 211 ? 4.147   0.822   -21.026 1.00 65.69  ? 211 TYR A OH  1 
ATOM   1815  N N   . GLU A 1 212 ? -1.277  3.347   -14.722 1.00 56.71  ? 212 GLU A N   1 
ATOM   1816  C CA  . GLU A 1 212 ? -2.445  3.758   -13.950 1.00 54.24  ? 212 GLU A CA  1 
ATOM   1817  C C   . GLU A 1 212 ? -2.273  5.159   -13.381 1.00 56.78  ? 212 GLU A C   1 
ATOM   1818  O O   . GLU A 1 212 ? -3.244  5.917   -13.292 1.00 59.12  ? 212 GLU A O   1 
ATOM   1819  C CB  . GLU A 1 212 ? -2.708  2.761   -12.823 1.00 49.57  ? 212 GLU A CB  1 
ATOM   1820  C CG  . GLU A 1 212 ? -2.821  1.320   -13.297 1.00 57.98  ? 212 GLU A CG  1 
ATOM   1821  C CD  . GLU A 1 212 ? -3.720  0.476   -12.412 1.00 75.02  ? 212 GLU A CD  1 
ATOM   1822  O OE1 . GLU A 1 212 ? -4.766  0.985   -11.958 1.00 79.17  ? 212 GLU A OE1 1 
ATOM   1823  O OE2 . GLU A 1 212 ? -3.387  -0.705  -12.182 1.00 84.86  ? 212 GLU A OE2 1 
ATOM   1824  N N   . THR A 1 213 ? -1.052  5.520   -12.999 1.00 61.90  ? 213 THR A N   1 
ATOM   1825  C CA  . THR A 1 213 ? -0.759  6.847   -12.491 1.00 59.46  ? 213 THR A CA  1 
ATOM   1826  C C   . THR A 1 213 ? 0.189   7.641   -13.379 1.00 63.28  ? 213 THR A C   1 
ATOM   1827  O O   . THR A 1 213 ? 0.343   8.845   -13.156 1.00 64.17  ? 213 THR A O   1 
ATOM   1828  C CB  . THR A 1 213 ? -0.167  6.749   -11.077 1.00 58.21  ? 213 THR A CB  1 
ATOM   1829  O OG1 . THR A 1 213 ? 0.958   5.861   -11.082 1.00 63.53  ? 213 THR A OG1 1 
ATOM   1830  C CG2 . THR A 1 213 ? -1.207  6.206   -10.119 1.00 55.23  ? 213 THR A CG2 1 
ATOM   1831  N N   . THR A 1 214 ? 0.801   7.016   -14.385 1.00 61.66  ? 214 THR A N   1 
ATOM   1832  C CA  . THR A 1 214 ? 1.790   7.669   -15.245 1.00 58.92  ? 214 THR A CA  1 
ATOM   1833  C C   . THR A 1 214 ? 1.589   7.174   -16.669 1.00 59.75  ? 214 THR A C   1 
ATOM   1834  O O   . THR A 1 214 ? 2.298   6.279   -17.144 1.00 54.60  ? 214 THR A O   1 
ATOM   1835  C CB  . THR A 1 214 ? 3.208   7.391   -14.752 1.00 62.51  ? 214 THR A CB  1 
ATOM   1836  O OG1 . THR A 1 214 ? 3.270   6.066   -14.206 1.00 68.07  ? 214 THR A OG1 1 
ATOM   1837  C CG2 . THR A 1 214 ? 3.589   8.393   -13.672 1.00 58.13  ? 214 THR A CG2 1 
ATOM   1838  N N   . PRO A 1 215 ? 0.635   7.768   -17.395 1.00 66.27  ? 215 PRO A N   1 
ATOM   1839  C CA  . PRO A 1 215 ? 0.135   7.134   -18.625 1.00 58.67  ? 215 PRO A CA  1 
ATOM   1840  C C   . PRO A 1 215 ? 1.072   7.220   -19.816 1.00 65.36  ? 215 PRO A C   1 
ATOM   1841  O O   . PRO A 1 215 ? 0.987   6.360   -20.701 1.00 74.79  ? 215 PRO A O   1 
ATOM   1842  C CB  . PRO A 1 215 ? -1.175  7.892   -18.892 1.00 58.61  ? 215 PRO A CB  1 
ATOM   1843  C CG  . PRO A 1 215 ? -1.535  8.482   -17.547 1.00 65.79  ? 215 PRO A CG  1 
ATOM   1844  C CD  . PRO A 1 215 ? -0.224  8.880   -16.973 1.00 61.57  ? 215 PRO A CD  1 
ATOM   1845  N N   . ASN A 1 216 ? 1.939   8.225   -19.899 1.00 64.75  ? 216 ASN A N   1 
ATOM   1846  C CA  . ASN A 1 216 ? 2.776   8.389   -21.082 1.00 65.37  ? 216 ASN A CA  1 
ATOM   1847  C C   . ASN A 1 216 ? 4.222   7.968   -20.862 1.00 67.05  ? 216 ASN A C   1 
ATOM   1848  O O   . ASN A 1 216 ? 5.073   8.270   -21.706 1.00 66.93  ? 216 ASN A O   1 
ATOM   1849  C CB  . ASN A 1 216 ? 2.720   9.834   -21.579 1.00 67.42  ? 216 ASN A CB  1 
ATOM   1850  C CG  . ASN A 1 216 ? 1.332   10.417  -21.498 1.00 76.26  ? 216 ASN A CG  1 
ATOM   1851  O OD1 . ASN A 1 216 ? 0.977   11.072  -20.520 1.00 81.33  ? 216 ASN A OD1 1 
ATOM   1852  N ND2 . ASN A 1 216 ? 0.530   10.171  -22.527 1.00 75.91  ? 216 ASN A ND2 1 
ATOM   1853  N N   . VAL A 1 217 ? 4.523   7.254   -19.774 1.00 58.65  ? 217 VAL A N   1 
ATOM   1854  C CA  . VAL A 1 217 ? 5.897   6.820   -19.570 1.00 58.06  ? 217 VAL A CA  1 
ATOM   1855  C C   . VAL A 1 217 ? 6.280   5.788   -20.622 1.00 65.91  ? 217 VAL A C   1 
ATOM   1856  O O   . VAL A 1 217 ? 5.441   5.213   -21.327 1.00 60.46  ? 217 VAL A O   1 
ATOM   1857  C CB  . VAL A 1 217 ? 6.106   6.255   -18.160 1.00 50.91  ? 217 VAL A CB  1 
ATOM   1858  C CG1 . VAL A 1 217 ? 5.871   7.331   -17.145 1.00 59.50  ? 217 VAL A CG1 1 
ATOM   1859  C CG2 . VAL A 1 217 ? 5.182   5.074   -17.937 1.00 57.06  ? 217 VAL A CG2 1 
ATOM   1860  N N   . LYS A 1 218 ? 7.575   5.533   -20.702 1.00 74.48  ? 218 LYS A N   1 
ATOM   1861  C CA  . LYS A 1 218 ? 8.136   4.541   -21.601 1.00 68.85  ? 218 LYS A CA  1 
ATOM   1862  C C   . LYS A 1 218 ? 8.793   3.475   -20.734 1.00 62.44  ? 218 LYS A C   1 
ATOM   1863  O O   . LYS A 1 218 ? 9.739   3.775   -19.999 1.00 57.22  ? 218 LYS A O   1 
ATOM   1864  C CB  . LYS A 1 218 ? 9.147   5.189   -22.549 1.00 58.43  ? 218 LYS A CB  1 
ATOM   1865  C CG  . LYS A 1 218 ? 8.567   5.671   -23.874 1.00 64.91  ? 218 LYS A CG  1 
ATOM   1866  C CD  . LYS A 1 218 ? 8.701   4.585   -24.936 1.00 74.65  ? 218 LYS A CD  1 
ATOM   1867  C CE  . LYS A 1 218 ? 9.292   5.095   -26.234 1.00 67.73  ? 218 LYS A CE  1 
ATOM   1868  N NZ  . LYS A 1 218 ? 9.815   3.975   -27.038 1.00 71.16  ? 218 LYS A NZ  1 
ATOM   1869  N N   . ILE A 1 219 ? 8.272   2.252   -20.785 1.00 64.53  ? 219 ILE A N   1 
ATOM   1870  C CA  . ILE A 1 219 ? 8.832   1.155   -19.997 1.00 66.34  ? 219 ILE A CA  1 
ATOM   1871  C C   . ILE A 1 219 ? 9.372   0.099   -20.957 1.00 67.97  ? 219 ILE A C   1 
ATOM   1872  O O   . ILE A 1 219 ? 8.900   -0.001  -22.101 1.00 69.49  ? 219 ILE A O   1 
ATOM   1873  C CB  . ILE A 1 219 ? 7.791   0.579   -19.017 1.00 58.90  ? 219 ILE A CB  1 
ATOM   1874  C CG1 . ILE A 1 219 ? 6.777   -0.302  -19.737 1.00 63.94  ? 219 ILE A CG1 1 
ATOM   1875  C CG2 . ILE A 1 219 ? 7.059   1.683   -18.321 1.00 49.87  ? 219 ILE A CG2 1 
ATOM   1876  C CD1 . ILE A 1 219 ? 6.190   -1.381  -18.849 1.00 53.06  ? 219 ILE A CD1 1 
ATOM   1877  N N   . PRO A 1 220 ? 10.356  -0.698  -20.546 1.00 70.25  ? 220 PRO A N   1 
ATOM   1878  C CA  . PRO A 1 220 ? 10.914  -1.705  -21.449 1.00 65.80  ? 220 PRO A CA  1 
ATOM   1879  C C   . PRO A 1 220 ? 9.899   -2.791  -21.763 1.00 73.60  ? 220 PRO A C   1 
ATOM   1880  O O   . PRO A 1 220 ? 9.019   -3.109  -20.958 1.00 71.15  ? 220 PRO A O   1 
ATOM   1881  C CB  . PRO A 1 220 ? 12.094  -2.266  -20.652 1.00 64.90  ? 220 PRO A CB  1 
ATOM   1882  C CG  . PRO A 1 220 ? 11.644  -2.106  -19.229 1.00 68.22  ? 220 PRO A CG  1 
ATOM   1883  C CD  . PRO A 1 220 ? 10.976  -0.768  -19.211 1.00 67.63  ? 220 PRO A CD  1 
ATOM   1884  N N   . ASP A 1 221 ? 10.029  -3.356  -22.958 1.00 77.59  ? 221 ASP A N   1 
ATOM   1885  C CA  . ASP A 1 221 ? 9.182   -4.468  -23.374 1.00 79.14  ? 221 ASP A CA  1 
ATOM   1886  C C   . ASP A 1 221 ? 9.484   -5.680  -22.502 1.00 78.39  ? 221 ASP A C   1 
ATOM   1887  O O   . ASP A 1 221 ? 10.571  -6.261  -22.590 1.00 77.39  ? 221 ASP A O   1 
ATOM   1888  C CB  . ASP A 1 221 ? 9.417   -4.780  -24.848 1.00 77.52  ? 221 ASP A CB  1 
ATOM   1889  C CG  . ASP A 1 221 ? 8.149   -5.180  -25.564 1.00 94.42  ? 221 ASP A CG  1 
ATOM   1890  O OD1 . ASP A 1 221 ? 7.231   -4.338  -25.670 1.00 98.70  ? 221 ASP A OD1 1 
ATOM   1891  O OD2 . ASP A 1 221 ? 8.070   -6.340  -26.020 1.00 101.06 ? 221 ASP A OD2 1 
ATOM   1892  N N   . PHE A 1 222 ? 8.534   -6.056  -21.647 1.00 70.79  ? 222 PHE A N   1 
ATOM   1893  C CA  . PHE A 1 222 ? 8.717   -7.186  -20.736 1.00 64.71  ? 222 PHE A CA  1 
ATOM   1894  C C   . PHE A 1 222 ? 8.433   -8.468  -21.512 1.00 71.99  ? 222 PHE A C   1 
ATOM   1895  O O   . PHE A 1 222 ? 7.300   -8.950  -21.580 1.00 72.04  ? 222 PHE A O   1 
ATOM   1896  C CB  . PHE A 1 222 ? 7.820   -7.045  -19.513 1.00 58.93  ? 222 PHE A CB  1 
ATOM   1897  C CG  . PHE A 1 222 ? 8.449   -6.277  -18.378 1.00 63.27  ? 222 PHE A CG  1 
ATOM   1898  C CD1 . PHE A 1 222 ? 8.372   -4.891  -18.331 1.00 70.48  ? 222 PHE A CD1 1 
ATOM   1899  C CD2 . PHE A 1 222 ? 9.109   -6.938  -17.350 1.00 62.10  ? 222 PHE A CD2 1 
ATOM   1900  C CE1 . PHE A 1 222 ? 8.947   -4.178  -17.283 1.00 63.14  ? 222 PHE A CE1 1 
ATOM   1901  C CE2 . PHE A 1 222 ? 9.686   -6.229  -16.302 1.00 51.34  ? 222 PHE A CE2 1 
ATOM   1902  C CZ  . PHE A 1 222 ? 9.602   -4.850  -16.270 1.00 49.76  ? 222 PHE A CZ  1 
ATOM   1903  N N   . ALA A 1 223 ? 9.485   -9.023  -22.113 1.00 73.42  ? 223 ALA A N   1 
ATOM   1904  C CA  . ALA A 1 223 ? 9.391   -10.233 -22.919 1.00 61.94  ? 223 ALA A CA  1 
ATOM   1905  C C   . ALA A 1 223 ? 9.371   -11.507 -22.085 1.00 63.48  ? 223 ALA A C   1 
ATOM   1906  O O   . ALA A 1 223 ? 9.289   -12.599 -22.656 1.00 58.69  ? 223 ALA A O   1 
ATOM   1907  C CB  . ALA A 1 223 ? 10.554  -10.286 -23.911 1.00 66.86  ? 223 ALA A CB  1 
ATOM   1908  N N   . VAL A 1 224 ? 9.453   -11.400 -20.759 1.00 66.12  ? 224 VAL A N   1 
ATOM   1909  C CA  . VAL A 1 224 ? 9.406   -12.546 -19.862 1.00 68.90  ? 224 VAL A CA  1 
ATOM   1910  C C   . VAL A 1 224 ? 8.392   -12.245 -18.764 1.00 65.64  ? 224 VAL A C   1 
ATOM   1911  O O   . VAL A 1 224 ? 8.042   -11.090 -18.507 1.00 66.95  ? 224 VAL A O   1 
ATOM   1912  C CB  . VAL A 1 224 ? 10.799  -12.871 -19.262 1.00 69.37  ? 224 VAL A CB  1 
ATOM   1913  C CG1 . VAL A 1 224 ? 11.098  -11.976 -18.064 1.00 66.51  ? 224 VAL A CG1 1 
ATOM   1914  C CG2 . VAL A 1 224 ? 10.900  -14.352 -18.883 1.00 72.34  ? 224 VAL A CG2 1 
ATOM   1915  N N   . SER A 1 225 ? 7.907   -13.300 -18.118 1.00 57.31  ? 225 SER A N   1 
ATOM   1916  C CA  . SER A 1 225 ? 6.946   -13.153 -17.033 1.00 64.82  ? 225 SER A CA  1 
ATOM   1917  C C   . SER A 1 225 ? 7.651   -13.280 -15.691 1.00 65.79  ? 225 SER A C   1 
ATOM   1918  O O   . SER A 1 225 ? 8.463   -14.191 -15.491 1.00 64.39  ? 225 SER A O   1 
ATOM   1919  C CB  . SER A 1 225 ? 5.825   -14.185 -17.137 1.00 68.32  ? 225 SER A CB  1 
ATOM   1920  O OG  . SER A 1 225 ? 4.714   -13.781 -16.355 1.00 67.12  ? 225 SER A OG  1 
ATOM   1921  N N   . PHE A 1 226 ? 7.344   -12.355 -14.781 1.00 60.21  ? 226 PHE A N   1 
ATOM   1922  C CA  . PHE A 1 226 ? 7.893   -12.366 -13.433 1.00 60.85  ? 226 PHE A CA  1 
ATOM   1923  C C   . PHE A 1 226 ? 6.857   -12.782 -12.395 1.00 65.88  ? 226 PHE A C   1 
ATOM   1924  O O   . PHE A 1 226 ? 7.122   -12.683 -11.191 1.00 61.67  ? 226 PHE A O   1 
ATOM   1925  C CB  . PHE A 1 226 ? 8.464   -10.988 -13.080 1.00 58.39  ? 226 PHE A CB  1 
ATOM   1926  C CG  . PHE A 1 226 ? 9.750   -10.649 -13.795 1.00 61.76  ? 226 PHE A CG  1 
ATOM   1927  C CD1 . PHE A 1 226 ? 10.971  -11.105 -13.318 1.00 58.67  ? 226 PHE A CD1 1 
ATOM   1928  C CD2 . PHE A 1 226 ? 9.738   -9.864  -14.940 1.00 60.73  ? 226 PHE A CD2 1 
ATOM   1929  C CE1 . PHE A 1 226 ? 12.152  -10.792 -13.974 1.00 58.28  ? 226 PHE A CE1 1 
ATOM   1930  C CE2 . PHE A 1 226 ? 10.913  -9.547  -15.598 1.00 55.47  ? 226 PHE A CE2 1 
ATOM   1931  C CZ  . PHE A 1 226 ? 12.123  -10.013 -15.114 1.00 61.22  ? 226 PHE A CZ  1 
ATOM   1932  N N   . ARG A 1 227 ? 5.686   -13.254 -12.831 1.00 62.39  ? 227 ARG A N   1 
ATOM   1933  C CA  . ARG A 1 227 ? 4.608   -13.528 -11.887 1.00 59.57  ? 227 ARG A CA  1 
ATOM   1934  C C   . ARG A 1 227 ? 4.948   -14.694 -10.973 1.00 59.57  ? 227 ARG A C   1 
ATOM   1935  O O   . ARG A 1 227 ? 4.577   -14.691 -9.794  1.00 60.54  ? 227 ARG A O   1 
ATOM   1936  C CB  . ARG A 1 227 ? 3.311   -13.799 -12.644 1.00 58.71  ? 227 ARG A CB  1 
ATOM   1937  C CG  . ARG A 1 227 ? 3.087   -12.816 -13.768 1.00 60.59  ? 227 ARG A CG  1 
ATOM   1938  C CD  . ARG A 1 227 ? 1.742   -12.984 -14.441 1.00 54.39  ? 227 ARG A CD  1 
ATOM   1939  N NE  . ARG A 1 227 ? 0.714   -13.530 -13.559 1.00 61.91  ? 227 ARG A NE  1 
ATOM   1940  C CZ  . ARG A 1 227 ? -0.219  -12.810 -12.950 1.00 49.34  ? 227 ARG A CZ  1 
ATOM   1941  N NH1 . ARG A 1 227 ? -0.234  -11.488 -13.024 1.00 50.28  ? 227 ARG A NH1 1 
ATOM   1942  N NH2 . ARG A 1 227 ? -1.163  -13.431 -12.250 1.00 50.69  ? 227 ARG A NH2 1 
ATOM   1943  N N   . GLU A 1 228 ? 5.643   -15.704 -11.498 1.00 60.83  ? 228 GLU A N   1 
ATOM   1944  C CA  . GLU A 1 228 ? 6.032   -16.832 -10.659 1.00 61.65  ? 228 GLU A CA  1 
ATOM   1945  C C   . GLU A 1 228 ? 7.061   -16.400 -9.625  1.00 65.37  ? 228 GLU A C   1 
ATOM   1946  O O   . GLU A 1 228 ? 6.954   -16.749 -8.443  1.00 70.40  ? 228 GLU A O   1 
ATOM   1947  C CB  . GLU A 1 228 ? 6.573   -17.976 -11.517 1.00 68.12  ? 228 GLU A CB  1 
ATOM   1948  C CG  . GLU A 1 228 ? 7.590   -18.873 -10.805 1.00 73.34  ? 228 GLU A CG  1 
ATOM   1949  C CD  . GLU A 1 228 ? 6.940   -19.961 -9.966  1.00 79.41  ? 228 GLU A CD  1 
ATOM   1950  O OE1 . GLU A 1 228 ? 5.717   -20.167 -10.105 1.00 83.12  ? 228 GLU A OE1 1 
ATOM   1951  O OE2 . GLU A 1 228 ? 7.651   -20.612 -9.168  1.00 84.68  ? 228 GLU A OE2 1 
ATOM   1952  N N   . ASP A 1 229 ? 8.064   -15.628 -10.052 1.00 63.81  ? 229 ASP A N   1 
ATOM   1953  C CA  . ASP A 1 229 ? 9.056   -15.138 -9.103  1.00 64.62  ? 229 ASP A CA  1 
ATOM   1954  C C   . ASP A 1 229 ? 8.422   -14.228 -8.056  1.00 61.81  ? 229 ASP A C   1 
ATOM   1955  O O   . ASP A 1 229 ? 8.909   -14.151 -6.922  1.00 66.89  ? 229 ASP A O   1 
ATOM   1956  C CB  . ASP A 1 229 ? 10.189  -14.417 -9.840  1.00 62.51  ? 229 ASP A CB  1 
ATOM   1957  C CG  . ASP A 1 229 ? 11.202  -15.383 -10.457 1.00 75.49  ? 229 ASP A CG  1 
ATOM   1958  O OD1 . ASP A 1 229 ? 11.058  -16.616 -10.286 1.00 75.98  ? 229 ASP A OD1 1 
ATOM   1959  O OD2 . ASP A 1 229 ? 12.149  -14.904 -11.117 1.00 73.78  ? 229 ASP A OD2 1 
ATOM   1960  N N   . ALA A 1 230 ? 7.330   -13.543 -8.405  1.00 58.87  ? 230 ALA A N   1 
ATOM   1961  C CA  . ALA A 1 230 ? 6.653   -12.700 -7.425  1.00 57.54  ? 230 ALA A CA  1 
ATOM   1962  C C   . ALA A 1 230 ? 6.088   -13.545 -6.294  1.00 63.98  ? 230 ALA A C   1 
ATOM   1963  O O   . ALA A 1 230 ? 6.230   -13.210 -5.109  1.00 66.44  ? 230 ALA A O   1 
ATOM   1964  C CB  . ALA A 1 230 ? 5.546   -11.888 -8.093  1.00 53.76  ? 230 ALA A CB  1 
ATOM   1965  N N   . SER A 1 231 ? 5.462   -14.666 -6.646  1.00 61.19  ? 231 SER A N   1 
ATOM   1966  C CA  . SER A 1 231 ? 4.943   -15.571 -5.632  1.00 61.82  ? 231 SER A CA  1 
ATOM   1967  C C   . SER A 1 231 ? 6.069   -16.138 -4.777  1.00 63.18  ? 231 SER A C   1 
ATOM   1968  O O   . SER A 1 231 ? 5.908   -16.311 -3.563  1.00 59.08  ? 231 SER A O   1 
ATOM   1969  C CB  . SER A 1 231 ? 4.155   -16.687 -6.306  1.00 58.94  ? 231 SER A CB  1 
ATOM   1970  O OG  . SER A 1 231 ? 3.117   -16.126 -7.084  1.00 60.11  ? 231 SER A OG  1 
ATOM   1971  N N   . LYS A 1 232 ? 7.224   -16.421 -5.390  1.00 57.90  ? 232 LYS A N   1 
ATOM   1972  C CA  . LYS A 1 232 ? 8.343   -16.967 -4.626  1.00 58.10  ? 232 LYS A CA  1 
ATOM   1973  C C   . LYS A 1 232 ? 8.804   -15.994 -3.555  1.00 53.83  ? 232 LYS A C   1 
ATOM   1974  O O   . LYS A 1 232 ? 9.170   -16.406 -2.451  1.00 50.22  ? 232 LYS A O   1 
ATOM   1975  C CB  . LYS A 1 232 ? 9.505   -17.324 -5.550  1.00 53.19  ? 232 LYS A CB  1 
ATOM   1976  C CG  . LYS A 1 232 ? 9.149   -18.340 -6.614  1.00 63.92  ? 232 LYS A CG  1 
ATOM   1977  C CD  . LYS A 1 232 ? 10.238  -19.392 -6.762  1.00 63.56  ? 232 LYS A CD  1 
ATOM   1978  C CE  . LYS A 1 232 ? 10.774  -19.443 -8.187  1.00 71.06  ? 232 LYS A CE  1 
ATOM   1979  N NZ  . LYS A 1 232 ? 12.187  -19.922 -8.268  1.00 76.57  ? 232 LYS A NZ  1 
ATOM   1980  N N   . HIS A 1 233 ? 8.782   -14.696 -3.856  1.00 53.36  ? 233 HIS A N   1 
ATOM   1981  C CA  . HIS A 1 233 ? 9.160   -13.710 -2.851  1.00 55.63  ? 233 HIS A CA  1 
ATOM   1982  C C   . HIS A 1 233 ? 8.256   -13.812 -1.633  1.00 53.49  ? 233 HIS A C   1 
ATOM   1983  O O   . HIS A 1 233 ? 8.732   -13.921 -0.497  1.00 54.08  ? 233 HIS A O   1 
ATOM   1984  C CB  . HIS A 1 233 ? 9.109   -12.308 -3.448  1.00 56.67  ? 233 HIS A CB  1 
ATOM   1985  C CG  . HIS A 1 233 ? 10.378  -11.892 -4.127  1.00 58.26  ? 233 HIS A CG  1 
ATOM   1986  N ND1 . HIS A 1 233 ? 10.422  -11.503 -5.450  1.00 50.84  ? 233 HIS A ND1 1 
ATOM   1987  C CD2 . HIS A 1 233 ? 11.647  -11.792 -3.663  1.00 54.88  ? 233 HIS A CD2 1 
ATOM   1988  C CE1 . HIS A 1 233 ? 11.662  -11.179 -5.771  1.00 52.52  ? 233 HIS A CE1 1 
ATOM   1989  N NE2 . HIS A 1 233 ? 12.425  -11.349 -4.706  1.00 56.03  ? 233 HIS A NE2 1 
ATOM   1990  N N   . VAL A 1 234 ? 6.944   -13.809 -1.855  1.00 53.45  ? 234 VAL A N   1 
ATOM   1991  C CA  . VAL A 1 234 ? 6.004   -13.956 -0.751  1.00 50.81  ? 234 VAL A CA  1 
ATOM   1992  C C   . VAL A 1 234 ? 6.203   -15.299 -0.060  1.00 50.89  ? 234 VAL A C   1 
ATOM   1993  O O   . VAL A 1 234 ? 6.298   -15.379 1.170   1.00 50.75  ? 234 VAL A O   1 
ATOM   1994  C CB  . VAL A 1 234 ? 4.568   -13.781 -1.266  1.00 55.51  ? 234 VAL A CB  1 
ATOM   1995  C CG1 . VAL A 1 234 ? 3.583   -13.732 -0.103  1.00 62.11  ? 234 VAL A CG1 1 
ATOM   1996  C CG2 . VAL A 1 234 ? 4.486   -12.528 -2.126  1.00 48.65  ? 234 VAL A CG2 1 
ATOM   1997  N N   . GLU A 1 235 ? 6.317   -16.370 -0.844  1.00 51.75  ? 235 GLU A N   1 
ATOM   1998  C CA  . GLU A 1 235 ? 6.338   -17.707 -0.263  1.00 52.13  ? 235 GLU A CA  1 
ATOM   1999  C C   . GLU A 1 235 ? 7.613   -17.962 0.532   1.00 60.32  ? 235 GLU A C   1 
ATOM   2000  O O   . GLU A 1 235 ? 7.553   -18.516 1.635   1.00 63.72  ? 235 GLU A O   1 
ATOM   2001  C CB  . GLU A 1 235 ? 6.146   -18.750 -1.364  1.00 61.67  ? 235 GLU A CB  1 
ATOM   2002  C CG  . GLU A 1 235 ? 4.742   -18.729 -1.966  1.00 64.92  ? 235 GLU A CG  1 
ATOM   2003  C CD  . GLU A 1 235 ? 4.580   -19.668 -3.149  1.00 79.96  ? 235 GLU A CD  1 
ATOM   2004  O OE1 . GLU A 1 235 ? 4.850   -20.881 -3.010  1.00 85.51  ? 235 GLU A OE1 1 
ATOM   2005  O OE2 . GLU A 1 235 ? 4.173   -19.184 -4.226  1.00 80.05  ? 235 GLU A OE2 1 
ATOM   2006  N N   . LEU A 1 236 ? 8.776   -17.553 0.005   1.00 57.57  ? 236 LEU A N   1 
ATOM   2007  C CA  . LEU A 1 236 ? 10.031  -17.767 0.728   1.00 51.28  ? 236 LEU A CA  1 
ATOM   2008  C C   . LEU A 1 236 ? 10.116  -16.910 1.989   1.00 54.92  ? 236 LEU A C   1 
ATOM   2009  O O   . LEU A 1 236 ? 10.684  -17.346 2.999   1.00 54.48  ? 236 LEU A O   1 
ATOM   2010  C CB  . LEU A 1 236 ? 11.225  -17.489 -0.187  1.00 59.98  ? 236 LEU A CB  1 
ATOM   2011  C CG  . LEU A 1 236 ? 11.348  -18.354 -1.446  1.00 57.61  ? 236 LEU A CG  1 
ATOM   2012  C CD1 . LEU A 1 236 ? 12.568  -17.967 -2.267  1.00 47.36  ? 236 LEU A CD1 1 
ATOM   2013  C CD2 . LEU A 1 236 ? 11.372  -19.836 -1.095  1.00 60.20  ? 236 LEU A CD2 1 
ATOM   2014  N N   . ALA A 1 237 ? 9.539   -15.706 1.960   1.00 53.87  ? 237 ALA A N   1 
ATOM   2015  C CA  . ALA A 1 237 ? 9.506   -14.864 3.154   1.00 54.95  ? 237 ALA A CA  1 
ATOM   2016  C C   . ALA A 1 237 ? 8.720   -15.518 4.290   1.00 60.08  ? 237 ALA A C   1 
ATOM   2017  O O   . ALA A 1 237 ? 9.086   -15.384 5.465   1.00 56.16  ? 237 ALA A O   1 
ATOM   2018  C CB  . ALA A 1 237 ? 8.911   -13.500 2.809   1.00 56.78  ? 237 ALA A CB  1 
ATOM   2019  N N   . LYS A 1 238 ? 7.630   -16.220 3.967   1.00 57.91  ? 238 LYS A N   1 
ATOM   2020  C CA  . LYS A 1 238 ? 6.868   -16.903 5.012   1.00 59.25  ? 238 LYS A CA  1 
ATOM   2021  C C   . LYS A 1 238 ? 7.704   -17.983 5.685   1.00 57.80  ? 238 LYS A C   1 
ATOM   2022  O O   . LYS A 1 238 ? 7.565   -18.227 6.889   1.00 64.32  ? 238 LYS A O   1 
ATOM   2023  C CB  . LYS A 1 238 ? 5.585   -17.499 4.429   1.00 52.06  ? 238 LYS A CB  1 
ATOM   2024  C CG  . LYS A 1 238 ? 4.629   -16.441 3.898   1.00 52.23  ? 238 LYS A CG  1 
ATOM   2025  C CD  . LYS A 1 238 ? 3.311   -17.022 3.403   1.00 57.05  ? 238 LYS A CD  1 
ATOM   2026  C CE  . LYS A 1 238 ? 2.637   -17.880 4.456   1.00 64.62  ? 238 LYS A CE  1 
ATOM   2027  N NZ  . LYS A 1 238 ? 1.574   -18.750 3.879   1.00 61.43  ? 238 LYS A NZ  1 
ATOM   2028  N N   . GLU A 1 239 ? 8.582   -18.641 4.925   1.00 51.14  ? 239 GLU A N   1 
ATOM   2029  C CA  . GLU A 1 239 ? 9.422   -19.673 5.519   1.00 60.88  ? 239 GLU A CA  1 
ATOM   2030  C C   . GLU A 1 239 ? 10.502  -19.057 6.396   1.00 56.28  ? 239 GLU A C   1 
ATOM   2031  O O   . GLU A 1 239 ? 10.793  -19.568 7.484   1.00 55.69  ? 239 GLU A O   1 
ATOM   2032  C CB  . GLU A 1 239 ? 10.038  -20.546 4.426   1.00 62.98  ? 239 GLU A CB  1 
ATOM   2033  C CG  . GLU A 1 239 ? 9.123   -20.745 3.226   1.00 63.70  ? 239 GLU A CG  1 
ATOM   2034  C CD  . GLU A 1 239 ? 9.778   -21.513 2.082   1.00 79.25  ? 239 GLU A CD  1 
ATOM   2035  O OE1 . GLU A 1 239 ? 9.049   -22.045 1.215   1.00 85.13  ? 239 GLU A OE1 1 
ATOM   2036  O OE2 . GLU A 1 239 ? 11.024  -21.577 2.040   1.00 83.71  ? 239 GLU A OE2 1 
ATOM   2037  N N   . LYS A 1 240 ? 11.102  -17.954 5.947   1.00 50.06  ? 240 LYS A N   1 
ATOM   2038  C CA  . LYS A 1 240 ? 12.064  -17.269 6.796   1.00 55.49  ? 240 LYS A CA  1 
ATOM   2039  C C   . LYS A 1 240 ? 11.398  -16.790 8.082   1.00 53.28  ? 240 LYS A C   1 
ATOM   2040  O O   . LYS A 1 240 ? 11.972  -16.908 9.170   1.00 55.24  ? 240 LYS A O   1 
ATOM   2041  C CB  . LYS A 1 240 ? 12.709  -16.114 6.028   1.00 52.99  ? 240 LYS A CB  1 
ATOM   2042  C CG  . LYS A 1 240 ? 14.028  -15.644 6.624   1.00 55.80  ? 240 LYS A CG  1 
ATOM   2043  C CD  . LYS A 1 240 ? 15.181  -16.616 6.375   1.00 52.69  ? 240 LYS A CD  1 
ATOM   2044  C CE  . LYS A 1 240 ? 16.031  -16.785 7.634   1.00 55.12  ? 240 LYS A CE  1 
ATOM   2045  N NZ  . LYS A 1 240 ? 17.451  -17.136 7.345   1.00 58.43  ? 240 LYS A NZ  1 
ATOM   2046  N N   . TYR A 1 241 ? 10.165  -16.293 7.984   1.00 56.50  ? 241 TYR A N   1 
ATOM   2047  C CA  . TYR A 1 241 ? 9.421   -15.921 9.182   1.00 54.00  ? 241 TYR A CA  1 
ATOM   2048  C C   . TYR A 1 241 ? 9.194   -17.135 10.073  1.00 53.69  ? 241 TYR A C   1 
ATOM   2049  O O   . TYR A 1 241 ? 9.396   -17.075 11.292  1.00 55.62  ? 241 TYR A O   1 
ATOM   2050  C CB  . TYR A 1 241 ? 8.098   -15.276 8.777   1.00 52.67  ? 241 TYR A CB  1 
ATOM   2051  C CG  . TYR A 1 241 ? 7.364   -14.514 9.859   1.00 51.77  ? 241 TYR A CG  1 
ATOM   2052  C CD1 . TYR A 1 241 ? 6.630   -15.180 10.829  1.00 47.91  ? 241 TYR A CD1 1 
ATOM   2053  C CD2 . TYR A 1 241 ? 7.379   -13.127 9.886   1.00 49.19  ? 241 TYR A CD2 1 
ATOM   2054  C CE1 . TYR A 1 241 ? 5.940   -14.494 11.796  1.00 40.87  ? 241 TYR A CE1 1 
ATOM   2055  C CE2 . TYR A 1 241 ? 6.689   -12.427 10.859  1.00 46.69  ? 241 TYR A CE2 1 
ATOM   2056  C CZ  . TYR A 1 241 ? 5.971   -13.119 11.811  1.00 39.19  ? 241 TYR A CZ  1 
ATOM   2057  O OH  . TYR A 1 241 ? 5.275   -12.448 12.788  1.00 43.04  ? 241 TYR A OH  1 
ATOM   2058  N N   . PHE A 1 242 ? 8.796   -18.260 9.471   1.00 53.93  ? 242 PHE A N   1 
ATOM   2059  C CA  . PHE A 1 242 ? 8.589   -19.483 10.239  1.00 56.54  ? 242 PHE A CA  1 
ATOM   2060  C C   . PHE A 1 242 ? 9.881   -19.949 10.894  1.00 59.67  ? 242 PHE A C   1 
ATOM   2061  O O   . PHE A 1 242 ? 9.865   -20.455 12.022  1.00 58.05  ? 242 PHE A O   1 
ATOM   2062  C CB  . PHE A 1 242 ? 8.016   -20.584 9.345   1.00 55.61  ? 242 PHE A CB  1 
ATOM   2063  C CG  . PHE A 1 242 ? 7.556   -21.794 10.108  1.00 55.88  ? 242 PHE A CG  1 
ATOM   2064  C CD1 . PHE A 1 242 ? 8.458   -22.759 10.529  1.00 53.55  ? 242 PHE A CD1 1 
ATOM   2065  C CD2 . PHE A 1 242 ? 6.216   -21.969 10.397  1.00 58.13  ? 242 PHE A CD2 1 
ATOM   2066  C CE1 . PHE A 1 242 ? 8.033   -23.867 11.237  1.00 63.59  ? 242 PHE A CE1 1 
ATOM   2067  C CE2 . PHE A 1 242 ? 5.781   -23.073 11.105  1.00 57.83  ? 242 PHE A CE2 1 
ATOM   2068  C CZ  . PHE A 1 242 ? 6.691   -24.026 11.525  1.00 60.58  ? 242 PHE A CZ  1 
ATOM   2069  N N   . GLU A 1 243 ? 11.009  -19.799 10.198  1.00 57.07  ? 243 GLU A N   1 
ATOM   2070  C CA  . GLU A 1 243 ? 12.292  -20.153 10.793  1.00 49.84  ? 243 GLU A CA  1 
ATOM   2071  C C   . GLU A 1 243 ? 12.539  -19.357 12.067  1.00 53.06  ? 243 GLU A C   1 
ATOM   2072  O O   . GLU A 1 243 ? 12.866  -19.927 13.114  1.00 57.29  ? 243 GLU A O   1 
ATOM   2073  C CB  . GLU A 1 243 ? 13.420  -19.920 9.790   1.00 55.52  ? 243 GLU A CB  1 
ATOM   2074  C CG  . GLU A 1 243 ? 14.713  -20.646 10.151  1.00 71.22  ? 243 GLU A CG  1 
ATOM   2075  C CD  . GLU A 1 243 ? 15.961  -19.902 9.704   1.00 80.01  ? 243 GLU A CD  1 
ATOM   2076  O OE1 . GLU A 1 243 ? 16.227  -19.848 8.483   1.00 79.04  ? 243 GLU A OE1 1 
ATOM   2077  O OE2 . GLU A 1 243 ? 16.680  -19.372 10.579  1.00 82.65  ? 243 GLU A OE2 1 
ATOM   2078  N N   . ILE A 1 244 ? 12.357  -18.036 12.006  1.00 51.89  ? 244 ILE A N   1 
ATOM   2079  C CA  . ILE A 1 244 ? 12.708  -17.185 13.142  1.00 53.36  ? 244 ILE A CA  1 
ATOM   2080  C C   . ILE A 1 244 ? 11.661  -17.278 14.241  1.00 56.63  ? 244 ILE A C   1 
ATOM   2081  O O   . ILE A 1 244 ? 11.996  -17.335 15.431  1.00 56.97  ? 244 ILE A O   1 
ATOM   2082  C CB  . ILE A 1 244 ? 12.898  -15.727 12.695  1.00 54.11  ? 244 ILE A CB  1 
ATOM   2083  C CG1 . ILE A 1 244 ? 13.689  -15.674 11.386  1.00 57.27  ? 244 ILE A CG1 1 
ATOM   2084  C CG2 . ILE A 1 244 ? 13.533  -14.917 13.825  1.00 62.56  ? 244 ILE A CG2 1 
ATOM   2085  C CD1 . ILE A 1 244 ? 15.177  -15.826 11.595  1.00 58.98  ? 244 ILE A CD1 1 
ATOM   2086  N N   . PHE A 1 245 ? 10.379  -17.257 13.867  1.00 51.82  ? 245 PHE A N   1 
ATOM   2087  C CA  . PHE A 1 245 ? 9.305   -17.121 14.839  1.00 49.85  ? 245 PHE A CA  1 
ATOM   2088  C C   . PHE A 1 245 ? 8.449   -18.366 15.020  1.00 58.16  ? 245 PHE A C   1 
ATOM   2089  O O   . PHE A 1 245 ? 7.681   -18.421 15.986  1.00 66.44  ? 245 PHE A O   1 
ATOM   2090  C CB  . PHE A 1 245 ? 8.399   -15.941 14.464  1.00 52.80  ? 245 PHE A CB  1 
ATOM   2091  C CG  . PHE A 1 245 ? 9.114   -14.631 14.418  1.00 51.68  ? 245 PHE A CG  1 
ATOM   2092  C CD1 . PHE A 1 245 ? 9.327   -13.902 15.574  1.00 51.09  ? 245 PHE A CD1 1 
ATOM   2093  C CD2 . PHE A 1 245 ? 9.588   -14.135 13.217  1.00 56.46  ? 245 PHE A CD2 1 
ATOM   2094  C CE1 . PHE A 1 245 ? 9.996   -12.697 15.534  1.00 61.34  ? 245 PHE A CE1 1 
ATOM   2095  C CE2 . PHE A 1 245 ? 10.259  -12.930 13.168  1.00 53.46  ? 245 PHE A CE2 1 
ATOM   2096  C CZ  . PHE A 1 245 ? 10.464  -12.209 14.325  1.00 57.09  ? 245 PHE A CZ  1 
ATOM   2097  N N   . GLY A 1 246 ? 8.545   -19.356 14.137  1.00 54.26  ? 246 GLY A N   1 
ATOM   2098  C CA  . GLY A 1 246 ? 7.831   -20.602 14.349  1.00 55.04  ? 246 GLY A CA  1 
ATOM   2099  C C   . GLY A 1 246 ? 6.394   -20.618 13.884  1.00 58.41  ? 246 GLY A C   1 
ATOM   2100  O O   . GLY A 1 246 ? 5.688   -21.605 14.130  1.00 56.83  ? 246 GLY A O   1 
ATOM   2101  N N   . GLU A 1 247 ? 5.941   -19.558 13.222  1.00 56.64  ? 247 GLU A N   1 
ATOM   2102  C CA  . GLU A 1 247 ? 4.578   -19.438 12.736  1.00 54.77  ? 247 GLU A CA  1 
ATOM   2103  C C   . GLU A 1 247 ? 4.633   -18.720 11.398  1.00 59.63  ? 247 GLU A C   1 
ATOM   2104  O O   . GLU A 1 247 ? 5.620   -18.053 11.075  1.00 64.54  ? 247 GLU A O   1 
ATOM   2105  C CB  . GLU A 1 247 ? 3.689   -18.682 13.744  1.00 63.36  ? 247 GLU A CB  1 
ATOM   2106  C CG  . GLU A 1 247 ? 2.203   -18.606 13.382  1.00 73.74  ? 247 GLU A CG  1 
ATOM   2107  C CD  . GLU A 1 247 ? 1.651   -19.929 12.856  1.00 81.80  ? 247 GLU A CD  1 
ATOM   2108  O OE1 . GLU A 1 247 ? 1.196   -20.760 13.673  1.00 78.12  ? 247 GLU A OE1 1 
ATOM   2109  O OE2 . GLU A 1 247 ? 1.658   -20.135 11.620  1.00 73.90  ? 247 GLU A OE2 1 
ATOM   2110  N N   . HIS A 1 248 ? 3.581   -18.884 10.600  1.00 57.99  ? 248 HIS A N   1 
ATOM   2111  C CA  . HIS A 1 248 ? 3.585   -18.191 9.321   1.00 53.14  ? 248 HIS A CA  1 
ATOM   2112  C C   . HIS A 1 248 ? 3.098   -16.756 9.507   1.00 49.21  ? 248 HIS A C   1 
ATOM   2113  O O   . HIS A 1 248 ? 2.234   -16.497 10.345  1.00 54.70  ? 248 HIS A O   1 
ATOM   2114  C CB  . HIS A 1 248 ? 2.715   -18.928 8.300   1.00 51.52  ? 248 HIS A CB  1 
ATOM   2115  C CG  . HIS A 1 248 ? 3.483   -19.900 7.455   1.00 62.84  ? 248 HIS A CG  1 
ATOM   2116  N ND1 . HIS A 1 248 ? 2.877   -20.880 6.699   1.00 67.10  ? 248 HIS A ND1 1 
ATOM   2117  C CD2 . HIS A 1 248 ? 4.816   -20.038 7.248   1.00 67.50  ? 248 HIS A CD2 1 
ATOM   2118  C CE1 . HIS A 1 248 ? 3.801   -21.582 6.066   1.00 73.28  ? 248 HIS A CE1 1 
ATOM   2119  N NE2 . HIS A 1 248 ? 4.986   -21.091 6.380   1.00 73.89  ? 248 HIS A NE2 1 
ATOM   2120  N N   . PRO A 1 249 ? 3.663   -15.803 8.772   1.00 46.37  ? 249 PRO A N   1 
ATOM   2121  C CA  . PRO A 1 249 ? 3.255   -14.409 8.948   1.00 48.17  ? 249 PRO A CA  1 
ATOM   2122  C C   . PRO A 1 249 ? 1.859   -14.179 8.398   1.00 53.09  ? 249 PRO A C   1 
ATOM   2123  O O   . PRO A 1 249 ? 1.502   -14.669 7.324   1.00 50.80  ? 249 PRO A O   1 
ATOM   2124  C CB  . PRO A 1 249 ? 4.308   -13.630 8.155   1.00 42.47  ? 249 PRO A CB  1 
ATOM   2125  C CG  . PRO A 1 249 ? 4.732   -14.585 7.104   1.00 53.60  ? 249 PRO A CG  1 
ATOM   2126  C CD  . PRO A 1 249 ? 4.730   -15.934 7.770   1.00 47.60  ? 249 PRO A CD  1 
ATOM   2127  N N   . VAL A 1 250 ? 1.062   -13.437 9.158   1.00 49.69  ? 250 VAL A N   1 
ATOM   2128  C CA  . VAL A 1 250 ? -0.257  -13.036 8.691   1.00 50.77  ? 250 VAL A CA  1 
ATOM   2129  C C   . VAL A 1 250 ? -0.294  -11.571 8.275   1.00 50.30  ? 250 VAL A C   1 
ATOM   2130  O O   . VAL A 1 250 ? -1.256  -11.153 7.611   1.00 45.57  ? 250 VAL A O   1 
ATOM   2131  C CB  . VAL A 1 250 ? -1.325  -13.302 9.771   1.00 48.69  ? 250 VAL A CB  1 
ATOM   2132  C CG1 . VAL A 1 250 ? -1.511  -14.791 9.967   1.00 41.23  ? 250 VAL A CG1 1 
ATOM   2133  C CG2 . VAL A 1 250 ? -0.922  -12.617 11.070  1.00 41.19  ? 250 VAL A CG2 1 
ATOM   2134  N N   . TYR A 1 251 ? 0.701   -10.778 8.659   1.00 49.41  ? 251 TYR A N   1 
ATOM   2135  C CA  . TYR A 1 251 ? 0.732   -9.352  8.371   1.00 51.18  ? 251 TYR A CA  1 
ATOM   2136  C C   . TYR A 1 251 ? 1.978   -9.061  7.552   1.00 47.39  ? 251 TYR A C   1 
ATOM   2137  O O   . TYR A 1 251 ? 3.074   -9.501  7.911   1.00 53.98  ? 251 TYR A O   1 
ATOM   2138  C CB  . TYR A 1 251 ? 0.730   -8.524  9.666   1.00 46.39  ? 251 TYR A CB  1 
ATOM   2139  C CG  . TYR A 1 251 ? -0.358  -8.903  10.648  1.00 47.81  ? 251 TYR A CG  1 
ATOM   2140  C CD1 . TYR A 1 251 ? -1.657  -9.086  10.218  1.00 50.28  ? 251 TYR A CD1 1 
ATOM   2141  C CD2 . TYR A 1 251 ? -0.077  -9.106  11.999  1.00 44.59  ? 251 TYR A CD2 1 
ATOM   2142  C CE1 . TYR A 1 251 ? -2.653  -9.435  11.093  1.00 55.49  ? 251 TYR A CE1 1 
ATOM   2143  C CE2 . TYR A 1 251 ? -1.070  -9.462  12.883  1.00 46.41  ? 251 TYR A CE2 1 
ATOM   2144  C CZ  . TYR A 1 251 ? -2.364  -9.625  12.416  1.00 52.25  ? 251 TYR A CZ  1 
ATOM   2145  O OH  . TYR A 1 251 ? -3.406  -9.983  13.243  1.00 59.18  ? 251 TYR A OH  1 
ATOM   2146  N N   . MET A 1 252 ? 1.818   -8.333  6.452   1.00 47.65  ? 252 MET A N   1 
ATOM   2147  C CA  . MET A 1 252 ? 2.967   -8.019  5.617   1.00 51.20  ? 252 MET A CA  1 
ATOM   2148  C C   . MET A 1 252 ? 2.898   -6.579  5.140   1.00 46.75  ? 252 MET A C   1 
ATOM   2149  O O   . MET A 1 252 ? 1.825   -6.071  4.806   1.00 45.21  ? 252 MET A O   1 
ATOM   2150  C CB  . MET A 1 252 ? 3.077   -8.973  4.418   1.00 48.27  ? 252 MET A CB  1 
ATOM   2151  C CG  . MET A 1 252 ? 3.818   -10.264 4.767   1.00 60.29  ? 252 MET A CG  1 
ATOM   2152  S SD  . MET A 1 252 ? 4.157   -11.378 3.389   1.00 56.77  ? 252 MET A SD  1 
ATOM   2153  C CE  . MET A 1 252 ? 4.040   -10.228 2.047   1.00 58.13  ? 252 MET A CE  1 
ATOM   2154  N N   . TRP A 1 253 ? 4.055   -5.924  5.122   1.00 49.88  ? 253 TRP A N   1 
ATOM   2155  C CA  . TRP A 1 253 ? 4.170   -4.581  4.581   1.00 47.83  ? 253 TRP A CA  1 
ATOM   2156  C C   . TRP A 1 253 ? 4.611   -4.666  3.129   1.00 45.95  ? 253 TRP A C   1 
ATOM   2157  O O   . TRP A 1 253 ? 5.697   -5.202  2.862   1.00 47.79  ? 253 TRP A O   1 
ATOM   2158  C CB  . TRP A 1 253 ? 5.177   -3.775  5.391   1.00 44.71  ? 253 TRP A CB  1 
ATOM   2159  C CG  . TRP A 1 253 ? 5.683   -2.568  4.679   1.00 47.42  ? 253 TRP A CG  1 
ATOM   2160  C CD1 . TRP A 1 253 ? 6.886   -2.434  4.046   1.00 44.49  ? 253 TRP A CD1 1 
ATOM   2161  C CD2 . TRP A 1 253 ? 5.012   -1.311  4.537   1.00 42.33  ? 253 TRP A CD2 1 
ATOM   2162  N NE1 . TRP A 1 253 ? 7.001   -1.172  3.506   1.00 47.88  ? 253 TRP A NE1 1 
ATOM   2163  C CE2 . TRP A 1 253 ? 5.864   -0.464  3.794   1.00 47.09  ? 253 TRP A CE2 1 
ATOM   2164  C CE3 . TRP A 1 253 ? 3.775   -0.819  4.959   1.00 41.45  ? 253 TRP A CE3 1 
ATOM   2165  C CZ2 . TRP A 1 253 ? 5.514   0.844   3.467   1.00 53.02  ? 253 TRP A CZ2 1 
ATOM   2166  C CZ3 . TRP A 1 253 ? 3.430   0.485   4.629   1.00 42.81  ? 253 TRP A CZ3 1 
ATOM   2167  C CH2 . TRP A 1 253 ? 4.296   1.299   3.894   1.00 44.01  ? 253 TRP A CH2 1 
ATOM   2168  N N   . PRO A 1 254 ? 3.826   -4.183  2.169   1.00 42.94  ? 254 PRO A N   1 
ATOM   2169  C CA  . PRO A 1 254 ? 4.279   -4.179  0.766   1.00 40.27  ? 254 PRO A CA  1 
ATOM   2170  C C   . PRO A 1 254 ? 5.484   -3.273  0.599   1.00 43.93  ? 254 PRO A C   1 
ATOM   2171  O O   . PRO A 1 254 ? 5.471   -2.124  1.067   1.00 48.88  ? 254 PRO A O   1 
ATOM   2172  C CB  . PRO A 1 254 ? 3.067   -3.626  0.001   1.00 42.14  ? 254 PRO A CB  1 
ATOM   2173  C CG  . PRO A 1 254 ? 2.282   -2.886  1.018   1.00 44.61  ? 254 PRO A CG  1 
ATOM   2174  C CD  . PRO A 1 254 ? 2.467   -3.639  2.307   1.00 42.24  ? 254 PRO A CD  1 
ATOM   2175  N N   . PRO A 1 255 ? 6.543   -3.747  -0.054  1.00 38.22  ? 255 PRO A N   1 
ATOM   2176  C CA  . PRO A 1 255 ? 7.748   -2.921  -0.220  1.00 44.16  ? 255 PRO A CA  1 
ATOM   2177  C C   . PRO A 1 255 ? 7.434   -1.593  -0.902  1.00 43.32  ? 255 PRO A C   1 
ATOM   2178  O O   . PRO A 1 255 ? 6.779   -1.547  -1.945  1.00 41.22  ? 255 PRO A O   1 
ATOM   2179  C CB  . PRO A 1 255 ? 8.660   -3.810  -1.074  1.00 43.29  ? 255 PRO A CB  1 
ATOM   2180  C CG  . PRO A 1 255 ? 8.184   -5.214  -0.760  1.00 45.22  ? 255 PRO A CG  1 
ATOM   2181  C CD  . PRO A 1 255 ? 6.703   -5.081  -0.650  1.00 45.30  ? 255 PRO A CD  1 
ATOM   2182  N N   . GLN A 1 256 ? 7.901   -0.502  -0.288  1.00 42.67  ? 256 GLN A N   1 
ATOM   2183  C CA  . GLN A 1 256 ? 7.615   0.863   -0.743  1.00 46.15  ? 256 GLN A CA  1 
ATOM   2184  C C   . GLN A 1 256 ? 6.109   1.132   -0.835  1.00 49.07  ? 256 GLN A C   1 
ATOM   2185  O O   . GLN A 1 256 ? 5.666   1.941   -1.657  1.00 51.30  ? 256 GLN A O   1 
ATOM   2186  C CB  . GLN A 1 256 ? 8.294   1.171   -2.084  1.00 41.29  ? 256 GLN A CB  1 
ATOM   2187  C CG  . GLN A 1 256 ? 9.734   0.665   -2.203  1.00 47.44  ? 256 GLN A CG  1 
ATOM   2188  C CD  . GLN A 1 256 ? 10.757  1.700   -1.786  1.00 48.31  ? 256 GLN A CD  1 
ATOM   2189  O OE1 . GLN A 1 256 ? 10.404  2.815   -1.408  1.00 49.61  ? 256 GLN A OE1 1 
ATOM   2190  N NE2 . GLN A 1 256 ? 12.032  1.329   -1.829  1.00 51.68  ? 256 GLN A NE2 1 
ATOM   2191  N N   . ALA A 1 257 ? 5.314   0.454   0.005   1.00 47.28  ? 257 ALA A N   1 
ATOM   2192  C CA  . ALA A 1 257 ? 3.855   0.604   0.082   1.00 42.12  ? 257 ALA A CA  1 
ATOM   2193  C C   . ALA A 1 257 ? 3.161   0.322   -1.250  1.00 51.35  ? 257 ALA A C   1 
ATOM   2194  O O   . ALA A 1 257 ? 2.008   0.731   -1.452  1.00 46.88  ? 257 ALA A O   1 
ATOM   2195  C CB  . ALA A 1 257 ? 3.455   1.992   0.596   1.00 35.84  ? 257 ALA A CB  1 
ATOM   2196  N N   . SER A 1 258 ? 3.839   -0.390  -2.152  1.00 50.00  ? 258 SER A N   1 
ATOM   2197  C CA  . SER A 1 258 ? 3.326   -0.624  -3.498  1.00 48.98  ? 258 SER A CA  1 
ATOM   2198  C C   . SER A 1 258 ? 2.170   -1.620  -3.462  1.00 42.47  ? 258 SER A C   1 
ATOM   2199  O O   . SER A 1 258 ? 2.342   -2.766  -3.033  1.00 39.48  ? 258 SER A O   1 
ATOM   2200  C CB  . SER A 1 258 ? 4.447   -1.120  -4.412  1.00 47.14  ? 258 SER A CB  1 
ATOM   2201  O OG  . SER A 1 258 ? 5.098   -2.268  -3.881  1.00 60.80  ? 258 SER A OG  1 
ATOM   2202  N N   . VAL A 1 259 ? 0.988   -1.177  -3.912  1.00 49.34  ? 259 VAL A N   1 
ATOM   2203  C CA  . VAL A 1 259 ? -0.223  -1.992  -3.948  1.00 38.47  ? 259 VAL A CA  1 
ATOM   2204  C C   . VAL A 1 259 ? -0.816  -1.951  -5.353  1.00 48.05  ? 259 VAL A C   1 
ATOM   2205  O O   . VAL A 1 259 ? -0.733  -0.946  -6.067  1.00 48.49  ? 259 VAL A O   1 
ATOM   2206  C CB  . VAL A 1 259 ? -1.296  -1.542  -2.910  1.00 40.59  ? 259 VAL A CB  1 
ATOM   2207  C CG1 . VAL A 1 259 ? -0.908  -1.938  -1.484  1.00 42.73  ? 259 VAL A CG1 1 
ATOM   2208  C CG2 . VAL A 1 259 ? -1.602  -0.039  -3.015  1.00 38.11  ? 259 VAL A CG2 1 
ATOM   2209  N N   . SER A 1 260 ? -1.416  -3.067  -5.750  1.00 48.41  ? 260 SER A N   1 
ATOM   2210  C CA  . SER A 1 260 ? -2.234  -3.118  -6.950  1.00 46.31  ? 260 SER A CA  1 
ATOM   2211  C C   . SER A 1 260 ? -3.362  -4.095  -6.675  1.00 51.53  ? 260 SER A C   1 
ATOM   2212  O O   . SER A 1 260 ? -3.279  -4.910  -5.753  1.00 56.63  ? 260 SER A O   1 
ATOM   2213  C CB  . SER A 1 260 ? -1.432  -3.552  -8.182  1.00 42.15  ? 260 SER A CB  1 
ATOM   2214  O OG  . SER A 1 260 ? -1.288  -4.964  -8.212  1.00 52.82  ? 260 SER A OG  1 
ATOM   2215  N N   . ASN A 1 261 ? -4.426  -4.005  -7.478  1.00 46.79  ? 261 ASN A N   1 
ATOM   2216  C CA  . ASN A 1 261 ? -5.486  -5.007  -7.387  1.00 54.54  ? 261 ASN A CA  1 
ATOM   2217  C C   . ASN A 1 261 ? -4.942  -6.420  -7.564  1.00 56.86  ? 261 ASN A C   1 
ATOM   2218  O O   . ASN A 1 261 ? -5.496  -7.373  -7.005  1.00 56.88  ? 261 ASN A O   1 
ATOM   2219  C CB  . ASN A 1 261 ? -6.574  -4.739  -8.429  1.00 55.59  ? 261 ASN A CB  1 
ATOM   2220  C CG  . ASN A 1 261 ? -7.208  -3.378  -8.273  1.00 54.52  ? 261 ASN A CG  1 
ATOM   2221  O OD1 . ASN A 1 261 ? -7.780  -3.071  -7.231  1.00 58.88  ? 261 ASN A OD1 1 
ATOM   2222  N ND2 . ASN A 1 261 ? -7.141  -2.566  -9.318  1.00 55.81  ? 261 ASN A ND2 1 
ATOM   2223  N N   . GLU A 1 262 ? -3.858  -6.571  -8.331  1.00 60.62  ? 262 GLU A N   1 
ATOM   2224  C CA  . GLU A 1 262 ? -3.250  -7.880  -8.557  1.00 60.49  ? 262 GLU A CA  1 
ATOM   2225  C C   . GLU A 1 262 ? -2.406  -8.325  -7.367  1.00 51.47  ? 262 GLU A C   1 
ATOM   2226  O O   . GLU A 1 262 ? -2.499  -9.482  -6.934  1.00 49.64  ? 262 GLU A O   1 
ATOM   2227  C CB  . GLU A 1 262 ? -2.402  -7.841  -9.827  1.00 59.61  ? 262 GLU A CB  1 
ATOM   2228  C CG  . GLU A 1 262 ? -3.150  -7.301  -11.033 1.00 65.47  ? 262 GLU A CG  1 
ATOM   2229  C CD  . GLU A 1 262 ? -3.532  -8.388  -12.012 1.00 77.64  ? 262 GLU A CD  1 
ATOM   2230  O OE1 . GLU A 1 262 ? -4.097  -9.411  -11.572 1.00 86.47  ? 262 GLU A OE1 1 
ATOM   2231  O OE2 . GLU A 1 262 ? -3.270  -8.219  -13.221 1.00 76.75  ? 262 GLU A OE2 1 
ATOM   2232  N N   . ALA A 1 263 ? -1.573  -7.429  -6.834  1.00 44.40  ? 263 ALA A N   1 
ATOM   2233  C CA  . ALA A 1 263 ? -0.785  -7.764  -5.651  1.00 46.35  ? 263 ALA A CA  1 
ATOM   2234  C C   . ALA A 1 263 ? -1.681  -8.136  -4.478  1.00 44.96  ? 263 ALA A C   1 
ATOM   2235  O O   . ALA A 1 263 ? -1.398  -9.091  -3.746  1.00 42.38  ? 263 ALA A O   1 
ATOM   2236  C CB  . ALA A 1 263 ? 0.124   -6.595  -5.276  1.00 46.50  ? 263 ALA A CB  1 
ATOM   2237  N N   . LEU A 1 264 ? -2.782  -7.404  -4.296  1.00 48.16  ? 264 LEU A N   1 
ATOM   2238  C CA  . LEU A 1 264 ? -3.698  -7.691  -3.195  1.00 47.21  ? 264 LEU A CA  1 
ATOM   2239  C C   . LEU A 1 264 ? -4.314  -9.077  -3.333  1.00 47.65  ? 264 LEU A C   1 
ATOM   2240  O O   . LEU A 1 264 ? -4.521  -9.777  -2.334  1.00 49.05  ? 264 LEU A O   1 
ATOM   2241  C CB  . LEU A 1 264 ? -4.784  -6.622  -3.140  1.00 47.67  ? 264 LEU A CB  1 
ATOM   2242  C CG  . LEU A 1 264 ? -4.305  -5.230  -2.745  1.00 46.96  ? 264 LEU A CG  1 
ATOM   2243  C CD1 . LEU A 1 264 ? -5.234  -4.194  -3.333  1.00 56.79  ? 264 LEU A CD1 1 
ATOM   2244  C CD2 . LEU A 1 264 ? -4.261  -5.102  -1.238  1.00 46.56  ? 264 LEU A CD2 1 
ATOM   2245  N N   . GLU A 1 265 ? -4.622  -9.486  -4.566  1.00 55.93  ? 265 GLU A N   1 
ATOM   2246  C CA  . GLU A 1 265 ? -5.060  -10.855 -4.809  1.00 53.31  ? 265 GLU A CA  1 
ATOM   2247  C C   . GLU A 1 265 ? -3.975  -11.850 -4.422  1.00 55.07  ? 265 GLU A C   1 
ATOM   2248  O O   . GLU A 1 265 ? -4.242  -12.824 -3.712  1.00 55.19  ? 265 GLU A O   1 
ATOM   2249  C CB  . GLU A 1 265 ? -5.452  -11.033 -6.277  1.00 61.65  ? 265 GLU A CB  1 
ATOM   2250  C CG  . GLU A 1 265 ? -6.713  -10.291 -6.682  1.00 54.63  ? 265 GLU A CG  1 
ATOM   2251  C CD  . GLU A 1 265 ? -6.749  -9.975  -8.166  1.00 64.98  ? 265 GLU A CD  1 
ATOM   2252  O OE1 . GLU A 1 265 ? -5.885  -10.489 -8.909  1.00 66.18  ? 265 GLU A OE1 1 
ATOM   2253  O OE2 . GLU A 1 265 ? -7.641  -9.209  -8.590  1.00 66.60  ? 265 GLU A OE2 1 
ATOM   2254  N N   . LEU A 1 266 ? -2.734  -11.609 -4.870  1.00 50.16  ? 266 LEU A N   1 
ATOM   2255  C CA  . LEU A 1 266 ? -1.625  -12.504 -4.541  1.00 47.30  ? 266 LEU A CA  1 
ATOM   2256  C C   . LEU A 1 266 ? -1.421  -12.601 -3.034  1.00 44.96  ? 266 LEU A C   1 
ATOM   2257  O O   . LEU A 1 266 ? -1.257  -13.696 -2.487  1.00 46.03  ? 266 LEU A O   1 
ATOM   2258  C CB  . LEU A 1 266 ? -0.336  -12.031 -5.223  1.00 51.93  ? 266 LEU A CB  1 
ATOM   2259  C CG  . LEU A 1 266 ? 0.983   -12.646 -4.727  1.00 45.73  ? 266 LEU A CG  1 
ATOM   2260  C CD1 . LEU A 1 266 ? 1.112   -14.100 -5.146  1.00 45.23  ? 266 LEU A CD1 1 
ATOM   2261  C CD2 . LEU A 1 266 ? 2.171   -11.852 -5.223  1.00 51.13  ? 266 LEU A CD2 1 
ATOM   2262  N N   . TYR A 1 267 ? -1.430  -11.462 -2.342  1.00 41.08  ? 267 TYR A N   1 
ATOM   2263  C CA  . TYR A 1 267 ? -1.263  -11.492 -0.893  1.00 48.41  ? 267 TYR A CA  1 
ATOM   2264  C C   . TYR A 1 267 ? -2.385  -12.272 -0.214  1.00 53.36  ? 267 TYR A C   1 
ATOM   2265  O O   . TYR A 1 267 ? -2.172  -12.880 0.843   1.00 50.94  ? 267 TYR A O   1 
ATOM   2266  C CB  . TYR A 1 267 ? -1.193  -10.068 -0.343  1.00 45.75  ? 267 TYR A CB  1 
ATOM   2267  C CG  . TYR A 1 267 ? 0.091   -9.344  -0.655  1.00 49.72  ? 267 TYR A CG  1 
ATOM   2268  C CD1 . TYR A 1 267 ? 1.322   -9.939  -0.410  1.00 55.94  ? 267 TYR A CD1 1 
ATOM   2269  C CD2 . TYR A 1 267 ? 0.079   -8.061  -1.197  1.00 55.86  ? 267 TYR A CD2 1 
ATOM   2270  C CE1 . TYR A 1 267 ? 2.509   -9.278  -0.698  1.00 53.64  ? 267 TYR A CE1 1 
ATOM   2271  C CE2 . TYR A 1 267 ? 1.267   -7.390  -1.486  1.00 53.02  ? 267 TYR A CE2 1 
ATOM   2272  C CZ  . TYR A 1 267 ? 2.482   -8.010  -1.226  1.00 52.29  ? 267 TYR A CZ  1 
ATOM   2273  O OH  . TYR A 1 267 ? 3.686   -7.392  -1.489  1.00 53.82  ? 267 TYR A OH  1 
ATOM   2274  N N   . TYR A 1 268 ? -3.579  -12.278 -0.813  1.00 45.16  ? 268 TYR A N   1 
ATOM   2275  C CA  . TYR A 1 268 ? -4.683  -13.068 -0.276  1.00 48.78  ? 268 TYR A CA  1 
ATOM   2276  C C   . TYR A 1 268 ? -4.474  -14.563 -0.520  1.00 52.09  ? 268 TYR A C   1 
ATOM   2277  O O   . TYR A 1 268 ? -4.775  -15.381 0.356   1.00 60.68  ? 268 TYR A O   1 
ATOM   2278  C CB  . TYR A 1 268 ? -6.006  -12.576 -0.876  1.00 51.76  ? 268 TYR A CB  1 
ATOM   2279  C CG  . TYR A 1 268 ? -7.112  -13.609 -0.972  1.00 54.80  ? 268 TYR A CG  1 
ATOM   2280  C CD1 . TYR A 1 268 ? -7.736  -14.097 0.169   1.00 57.01  ? 268 TYR A CD1 1 
ATOM   2281  C CD2 . TYR A 1 268 ? -7.547  -14.080 -2.208  1.00 50.31  ? 268 TYR A CD2 1 
ATOM   2282  C CE1 . TYR A 1 268 ? -8.754  -15.039 0.083   1.00 60.26  ? 268 TYR A CE1 1 
ATOM   2283  C CE2 . TYR A 1 268 ? -8.560  -15.020 -2.301  1.00 50.23  ? 268 TYR A CE2 1 
ATOM   2284  C CZ  . TYR A 1 268 ? -9.162  -15.496 -1.151  1.00 59.61  ? 268 TYR A CZ  1 
ATOM   2285  O OH  . TYR A 1 268 ? -10.175 -16.432 -1.222  1.00 71.21  ? 268 TYR A OH  1 
ATOM   2286  N N   . GLU A 1 269 ? -3.937  -14.943 -1.687  1.00 48.87  ? 269 GLU A N   1 
ATOM   2287  C CA  . GLU A 1 269 ? -3.769  -16.363 -1.994  1.00 49.95  ? 269 GLU A CA  1 
ATOM   2288  C C   . GLU A 1 269 ? -2.594  -16.988 -1.257  1.00 51.19  ? 269 GLU A C   1 
ATOM   2289  O O   . GLU A 1 269 ? -2.523  -18.219 -1.162  1.00 52.09  ? 269 GLU A O   1 
ATOM   2290  C CB  . GLU A 1 269 ? -3.597  -16.575 -3.500  1.00 52.93  ? 269 GLU A CB  1 
ATOM   2291  C CG  . GLU A 1 269 ? -4.506  -15.699 -4.335  1.00 58.36  ? 269 GLU A CG  1 
ATOM   2292  C CD  . GLU A 1 269 ? -4.911  -16.323 -5.656  1.00 81.00  ? 269 GLU A CD  1 
ATOM   2293  O OE1 . GLU A 1 269 ? -4.132  -16.206 -6.626  1.00 89.27  ? 269 GLU A OE1 1 
ATOM   2294  O OE2 . GLU A 1 269 ? -6.014  -16.908 -5.731  1.00 77.11  ? 269 GLU A OE2 1 
ATOM   2295  N N   . LYS A 1 270 ? -1.673  -16.180 -0.741  1.00 48.47  ? 270 LYS A N   1 
ATOM   2296  C CA  . LYS A 1 270 ? -0.566  -16.703 0.044   1.00 53.40  ? 270 LYS A CA  1 
ATOM   2297  C C   . LYS A 1 270 ? -0.798  -16.570 1.543   1.00 51.74  ? 270 LYS A C   1 
ATOM   2298  O O   . LYS A 1 270 ? 0.095   -16.905 2.327   1.00 58.99  ? 270 LYS A O   1 
ATOM   2299  C CB  . LYS A 1 270 ? 0.745   -16.011 -0.358  1.00 57.55  ? 270 LYS A CB  1 
ATOM   2300  C CG  . LYS A 1 270 ? 0.866   -15.691 -1.856  1.00 55.83  ? 270 LYS A CG  1 
ATOM   2301  C CD  . LYS A 1 270 ? 1.704   -16.700 -2.631  1.00 56.46  ? 270 LYS A CD  1 
ATOM   2302  C CE  . LYS A 1 270 ? 1.068   -18.077 -2.672  1.00 66.92  ? 270 LYS A CE  1 
ATOM   2303  N NZ  . LYS A 1 270 ? 1.484   -18.844 -3.877  1.00 79.07  ? 270 LYS A NZ  1 
ATOM   2304  N N   . GLY A 1 271 ? -1.971  -16.105 1.961   1.00 43.19  ? 271 GLY A N   1 
ATOM   2305  C CA  . GLY A 1 271 ? -2.354  -16.154 3.356   1.00 46.88  ? 271 GLY A CA  1 
ATOM   2306  C C   . GLY A 1 271 ? -2.185  -14.884 4.160   1.00 52.19  ? 271 GLY A C   1 
ATOM   2307  O O   . GLY A 1 271 ? -2.307  -14.933 5.389   1.00 54.22  ? 271 GLY A O   1 
ATOM   2308  N N   . ILE A 1 272 ? -1.919  -13.752 3.521   1.00 51.20  ? 272 ILE A N   1 
ATOM   2309  C CA  . ILE A 1 272 ? -1.745  -12.500 4.248   1.00 48.47  ? 272 ILE A CA  1 
ATOM   2310  C C   . ILE A 1 272 ? -3.122  -11.950 4.616   1.00 57.50  ? 272 ILE A C   1 
ATOM   2311  O O   . ILE A 1 272 ? -3.974  -11.743 3.744   1.00 58.87  ? 272 ILE A O   1 
ATOM   2312  C CB  . ILE A 1 272 ? -0.936  -11.493 3.418   1.00 50.42  ? 272 ILE A CB  1 
ATOM   2313  C CG1 . ILE A 1 272 ? 0.471   -12.040 3.149   1.00 50.05  ? 272 ILE A CG1 1 
ATOM   2314  C CG2 . ILE A 1 272 ? -0.841  -10.152 4.122   1.00 47.56  ? 272 ILE A CG2 1 
ATOM   2315  C CD1 . ILE A 1 272 ? 1.067   -12.847 4.304   1.00 48.29  ? 272 ILE A CD1 1 
ATOM   2316  N N   . ASN A 1 273 ? -3.353  -11.740 5.919   1.00 56.37  ? 273 ASN A N   1 
ATOM   2317  C CA  . ASN A 1 273 ? -4.629  -11.202 6.387   1.00 48.71  ? 273 ASN A CA  1 
ATOM   2318  C C   . ASN A 1 273 ? -4.713  -9.690  6.237   1.00 51.40  ? 273 ASN A C   1 
ATOM   2319  O O   . ASN A 1 273 ? -5.807  -9.157  6.030   1.00 55.75  ? 273 ASN A O   1 
ATOM   2320  C CB  . ASN A 1 273 ? -4.863  -11.564 7.853   1.00 52.18  ? 273 ASN A CB  1 
ATOM   2321  C CG  . ASN A 1 273 ? -5.071  -13.039 8.052   1.00 54.88  ? 273 ASN A CG  1 
ATOM   2322  O OD1 . ASN A 1 273 ? -5.087  -13.801 7.089   1.00 57.06  ? 273 ASN A OD1 1 
ATOM   2323  N ND2 . ASN A 1 273 ? -5.250  -13.455 9.301   1.00 54.82  ? 273 ASN A ND2 1 
ATOM   2324  N N   . MET A 1 274 ? -3.589  -8.986  6.339   1.00 52.93  ? 274 MET A N   1 
ATOM   2325  C CA  . MET A 1 274 ? -3.615  -7.532  6.316   1.00 48.86  ? 274 MET A CA  1 
ATOM   2326  C C   . MET A 1 274 ? -2.305  -6.986  5.763   1.00 51.65  ? 274 MET A C   1 
ATOM   2327  O O   . MET A 1 274 ? -1.238  -7.580  5.940   1.00 49.72  ? 274 MET A O   1 
ATOM   2328  C CB  . MET A 1 274 ? -3.869  -6.958  7.717   1.00 53.94  ? 274 MET A CB  1 
ATOM   2329  C CG  . MET A 1 274 ? -3.810  -5.436  7.792   1.00 49.61  ? 274 MET A CG  1 
ATOM   2330  S SD  . MET A 1 274 ? -2.176  -4.831  8.285   1.00 72.49  ? 274 MET A SD  1 
ATOM   2331  C CE  . MET A 1 274 ? -2.060  -5.433  9.966   1.00 52.66  ? 274 MET A CE  1 
ATOM   2332  N N   . LEU A 1 275 ? -2.405  -5.834  5.101   1.00 50.37  ? 275 LEU A N   1 
ATOM   2333  C CA  . LEU A 1 275 ? -1.261  -5.078  4.621   1.00 42.86  ? 275 LEU A CA  1 
ATOM   2334  C C   . LEU A 1 275 ? -1.568  -3.596  4.793   1.00 50.96  ? 275 LEU A C   1 
ATOM   2335  O O   . LEU A 1 275 ? -2.654  -3.212  5.243   1.00 51.95  ? 275 LEU A O   1 
ATOM   2336  C CB  . LEU A 1 275 ? -0.936  -5.416  3.165   1.00 48.77  ? 275 LEU A CB  1 
ATOM   2337  C CG  . LEU A 1 275 ? -1.880  -4.979  2.039   1.00 55.64  ? 275 LEU A CG  1 
ATOM   2338  C CD1 . LEU A 1 275 ? -1.314  -5.482  0.716   1.00 55.57  ? 275 LEU A CD1 1 
ATOM   2339  C CD2 . LEU A 1 275 ? -3.337  -5.438  2.229   1.00 54.30  ? 275 LEU A CD2 1 
ATOM   2340  N N   . ALA A 1 276 ? -0.607  -2.751  4.430   1.00 48.06  ? 276 ALA A N   1 
ATOM   2341  C CA  . ALA A 1 276 ? -0.751  -1.318  4.624   1.00 46.17  ? 276 ALA A CA  1 
ATOM   2342  C C   . ALA A 1 276 ? -0.120  -0.581  3.459   1.00 43.93  ? 276 ALA A C   1 
ATOM   2343  O O   . ALA A 1 276 ? 0.896   -1.014  2.914   1.00 36.98  ? 276 ALA A O   1 
ATOM   2344  C CB  . ALA A 1 276 ? -0.104  -0.844  5.930   1.00 42.15  ? 276 ALA A CB  1 
ATOM   2345  N N   . THR A 1 277 ? -0.717  0.549   3.092   1.00 38.34  ? 277 THR A N   1 
ATOM   2346  C CA  . THR A 1 277 ? -0.159  1.370   2.030   1.00 35.78  ? 277 THR A CA  1 
ATOM   2347  C C   . THR A 1 277 ? -0.370  2.840   2.369   1.00 35.59  ? 277 THR A C   1 
ATOM   2348  O O   . THR A 1 277 ? -0.915  3.181   3.420   1.00 46.47  ? 277 THR A O   1 
ATOM   2349  C CB  . THR A 1 277 ? -0.763  1.008   0.674   1.00 39.75  ? 277 THR A CB  1 
ATOM   2350  O OG1 . THR A 1 277 ? -0.241  1.898   -0.316  1.00 51.56  ? 277 THR A OG1 1 
ATOM   2351  C CG2 . THR A 1 277 ? -2.286  1.109   0.704   1.00 43.64  ? 277 THR A CG2 1 
ATOM   2352  N N   . ASP A 1 278 ? 0.068   3.713   1.464   1.00 38.73  ? 278 ASP A N   1 
ATOM   2353  C CA  . ASP A 1 278 ? 0.164   5.137   1.752   1.00 45.19  ? 278 ASP A CA  1 
ATOM   2354  C C   . ASP A 1 278 ? -1.143  5.866   1.457   1.00 52.01  ? 278 ASP A C   1 
ATOM   2355  O O   . ASP A 1 278 ? -1.963  5.442   0.635   1.00 46.96  ? 278 ASP A O   1 
ATOM   2356  C CB  . ASP A 1 278 ? 1.301   5.782   0.949   1.00 46.37  ? 278 ASP A CB  1 
ATOM   2357  C CG  . ASP A 1 278 ? 1.605   7.222   1.395   1.00 56.11  ? 278 ASP A CG  1 
ATOM   2358  O OD1 . ASP A 1 278 ? 1.753   7.479   2.613   1.00 53.01  ? 278 ASP A OD1 1 
ATOM   2359  O OD2 . ASP A 1 278 ? 1.683   8.110   0.518   1.00 61.01  ? 278 ASP A OD2 1 
ATOM   2360  N N   . GLU A 1 279 ? -1.302  7.008   2.138   1.00 50.87  ? 279 GLU A N   1 
ATOM   2361  C CA  . GLU A 1 279 ? -2.493  7.838   1.993   1.00 53.47  ? 279 GLU A CA  1 
ATOM   2362  C C   . GLU A 1 279 ? -2.704  8.304   0.553   1.00 56.17  ? 279 GLU A C   1 
ATOM   2363  O O   . GLU A 1 279 ? -3.851  8.473   0.122   1.00 59.45  ? 279 GLU A O   1 
ATOM   2364  C CB  . GLU A 1 279 ? -2.394  9.043   2.931   1.00 50.74  ? 279 GLU A CB  1 
ATOM   2365  C CG  . GLU A 1 279 ? -3.715  9.461   3.557   1.00 67.21  ? 279 GLU A CG  1 
ATOM   2366  C CD  . GLU A 1 279 ? -3.596  10.733  4.386   1.00 74.18  ? 279 GLU A CD  1 
ATOM   2367  O OE1 . GLU A 1 279 ? -2.493  11.000  4.919   1.00 61.74  ? 279 GLU A OE1 1 
ATOM   2368  O OE2 . GLU A 1 279 ? -4.607  11.460  4.514   1.00 72.23  ? 279 GLU A OE2 1 
ATOM   2369  N N   . VAL A 1 280 ? -1.620  8.528   -0.198  1.00 49.78  ? 280 VAL A N   1 
ATOM   2370  C CA  . VAL A 1 280 ? -1.736  8.973   -1.588  1.00 54.24  ? 280 VAL A CA  1 
ATOM   2371  C C   . VAL A 1 280 ? -2.549  7.978   -2.408  1.00 59.75  ? 280 VAL A C   1 
ATOM   2372  O O   . VAL A 1 280 ? -3.419  8.365   -3.200  1.00 51.94  ? 280 VAL A O   1 
ATOM   2373  C CB  . VAL A 1 280 ? -0.338  9.185   -2.196  1.00 55.61  ? 280 VAL A CB  1 
ATOM   2374  C CG1 . VAL A 1 280 ? -0.448  9.464   -3.684  1.00 48.76  ? 280 VAL A CG1 1 
ATOM   2375  C CG2 . VAL A 1 280 ? 0.388   10.319  -1.484  1.00 56.06  ? 280 VAL A CG2 1 
ATOM   2376  N N   . ILE A 1 281 ? -2.269  6.682   -2.241  1.00 58.38  ? 281 ILE A N   1 
ATOM   2377  C CA  . ILE A 1 281 ? -3.015  5.652   -2.962  1.00 55.77  ? 281 ILE A CA  1 
ATOM   2378  C C   . ILE A 1 281 ? -4.487  5.703   -2.583  1.00 55.81  ? 281 ILE A C   1 
ATOM   2379  O O   . ILE A 1 281 ? -5.370  5.570   -3.439  1.00 52.47  ? 281 ILE A O   1 
ATOM   2380  C CB  . ILE A 1 281 ? -2.404  4.265   -2.692  1.00 55.29  ? 281 ILE A CB  1 
ATOM   2381  C CG1 . ILE A 1 281 ? -0.883  4.316   -2.855  1.00 53.98  ? 281 ILE A CG1 1 
ATOM   2382  C CG2 . ILE A 1 281 ? -3.029  3.209   -3.599  1.00 50.54  ? 281 ILE A CG2 1 
ATOM   2383  C CD1 . ILE A 1 281 ? -0.419  4.524   -4.271  1.00 47.92  ? 281 ILE A CD1 1 
ATOM   2384  N N   . LEU A 1 282 ? -4.777  5.909   -1.298  1.00 56.31  ? 282 LEU A N   1 
ATOM   2385  C CA  . LEU A 1 282 ? -6.164  6.071   -0.881  1.00 58.15  ? 282 LEU A CA  1 
ATOM   2386  C C   . LEU A 1 282 ? -6.822  7.221   -1.631  1.00 56.64  ? 282 LEU A C   1 
ATOM   2387  O O   . LEU A 1 282 ? -7.912  7.069   -2.196  1.00 60.80  ? 282 LEU A O   1 
ATOM   2388  C CB  . LEU A 1 282 ? -6.239  6.303   0.626   1.00 53.35  ? 282 LEU A CB  1 
ATOM   2389  C CG  . LEU A 1 282 ? -7.672  6.412   1.129   1.00 54.07  ? 282 LEU A CG  1 
ATOM   2390  C CD1 . LEU A 1 282 ? -8.419  5.094   0.886   1.00 56.92  ? 282 LEU A CD1 1 
ATOM   2391  C CD2 . LEU A 1 282 ? -7.676  6.818   2.593   1.00 52.60  ? 282 LEU A CD2 1 
ATOM   2392  N N   . LYS A 1 283 ? -6.153  8.375   -1.673  1.00 51.60  ? 283 LYS A N   1 
ATOM   2393  C CA  . LYS A 1 283 ? -6.737  9.542   -2.326  1.00 55.35  ? 283 LYS A CA  1 
ATOM   2394  C C   . LYS A 1 283 ? -6.858  9.351   -3.833  1.00 47.44  ? 283 LYS A C   1 
ATOM   2395  O O   . LYS A 1 283 ? -7.762  9.914   -4.454  1.00 56.59  ? 283 LYS A O   1 
ATOM   2396  C CB  . LYS A 1 283 ? -5.912  10.785  -2.000  1.00 55.07  ? 283 LYS A CB  1 
ATOM   2397  C CG  . LYS A 1 283 ? -5.913  11.153  -0.515  1.00 60.81  ? 283 LYS A CG  1 
ATOM   2398  C CD  . LYS A 1 283 ? -7.303  11.025  0.127   1.00 62.84  ? 283 LYS A CD  1 
ATOM   2399  C CE  . LYS A 1 283 ? -7.234  10.358  1.502   1.00 63.25  ? 283 LYS A CE  1 
ATOM   2400  N NZ  . LYS A 1 283 ? -6.849  11.307  2.591   1.00 55.43  ? 283 LYS A NZ  1 
ATOM   2401  N N   . ASN A 1 284 ? -5.976  8.560   -4.438  1.00 52.31  ? 284 ASN A N   1 
ATOM   2402  C CA  . ASN A 1 284 ? -6.117  8.282   -5.863  1.00 52.67  ? 284 ASN A CA  1 
ATOM   2403  C C   . ASN A 1 284 ? -7.202  7.249   -6.113  1.00 60.73  ? 284 ASN A C   1 
ATOM   2404  O O   . ASN A 1 284 ? -7.870  7.284   -7.152  1.00 67.88  ? 284 ASN A O   1 
ATOM   2405  C CB  . ASN A 1 284 ? -4.801  7.784   -6.451  1.00 60.81  ? 284 ASN A CB  1 
ATOM   2406  C CG  . ASN A 1 284 ? -3.652  8.740   -6.224  1.00 61.04  ? 284 ASN A CG  1 
ATOM   2407  O OD1 . ASN A 1 284 ? -2.515  8.314   -6.027  1.00 66.27  ? 284 ASN A OD1 1 
ATOM   2408  N ND2 . ASN A 1 284 ? -3.935  10.037  -6.266  1.00 60.17  ? 284 ASN A ND2 1 
ATOM   2409  N N   . SER A 1 285 ? -7.396  6.324   -5.173  1.00 60.15  ? 285 SER A N   1 
ATOM   2410  C CA  . SER A 1 285 ? -8.234  5.161   -5.436  1.00 55.94  ? 285 SER A CA  1 
ATOM   2411  C C   . SER A 1 285 ? -9.690  5.375   -5.054  1.00 61.17  ? 285 SER A C   1 
ATOM   2412  O O   . SER A 1 285 ? -10.588 4.922   -5.773  1.00 64.97  ? 285 SER A O   1 
ATOM   2413  C CB  . SER A 1 285 ? -7.685  3.945   -4.697  1.00 52.42  ? 285 SER A CB  1 
ATOM   2414  O OG  . SER A 1 285 ? -6.313  3.793   -4.983  1.00 54.97  ? 285 SER A OG  1 
ATOM   2415  N N   . VAL A 1 286 ? -9.956  6.043   -3.941  1.00 55.92  ? 286 VAL A N   1 
ATOM   2416  C CA  . VAL A 1 286 ? -11.324 6.153   -3.456  1.00 59.06  ? 286 VAL A CA  1 
ATOM   2417  C C   . VAL A 1 286 ? -11.691 7.627   -3.370  1.00 65.32  ? 286 VAL A C   1 
ATOM   2418  O O   . VAL A 1 286 ? -10.841 8.476   -3.084  1.00 65.96  ? 286 VAL A O   1 
ATOM   2419  C CB  . VAL A 1 286 ? -11.501 5.450   -2.093  1.00 59.00  ? 286 VAL A CB  1 
ATOM   2420  C CG1 . VAL A 1 286 ? -12.671 6.025   -1.335  1.00 70.21  ? 286 VAL A CG1 1 
ATOM   2421  C CG2 . VAL A 1 286 ? -11.660 3.957   -2.288  1.00 54.17  ? 286 VAL A CG2 1 
ATOM   2422  N N   . GLU A 1 287 ? -12.972 7.923   -3.612  1.00 67.33  ? 287 GLU A N   1 
ATOM   2423  C CA  . GLU A 1 287 ? -13.485 9.280   -3.771  1.00 72.77  ? 287 GLU A CA  1 
ATOM   2424  C C   . GLU A 1 287 ? -13.107 10.222  -2.629  1.00 81.56  ? 287 GLU A C   1 
ATOM   2425  O O   . GLU A 1 287 ? -12.208 11.055  -2.786  1.00 94.25  ? 287 GLU A O   1 
ATOM   2426  C CB  . GLU A 1 287 ? -15.004 9.239   -3.936  1.00 84.32  ? 287 GLU A CB  1 
ATOM   2427  C CG  . GLU A 1 287 ? -15.575 10.459  -4.653  1.00 93.75  ? 287 GLU A CG  1 
ATOM   2428  C CD  . GLU A 1 287 ? -17.058 10.669  -4.386  1.00 97.98  ? 287 GLU A CD  1 
ATOM   2429  O OE1 . GLU A 1 287 ? -17.755 9.688   -4.045  1.00 96.26  ? 287 GLU A OE1 1 
ATOM   2430  O OE2 . GLU A 1 287 ? -17.526 11.819  -4.515  1.00 90.43  ? 287 GLU A OE2 1 
ATOM   2431  N N   . ARG A 1 288 ? -13.795 10.134  -1.485  1.00 73.29  ? 288 ARG A N   1 
ATOM   2432  C CA  . ARG A 1 288 ? -13.491 10.976  -0.323  1.00 72.38  ? 288 ARG A CA  1 
ATOM   2433  C C   . ARG A 1 288 ? -13.340 10.076  0.904   1.00 73.64  ? 288 ARG A C   1 
ATOM   2434  O O   . ARG A 1 288 ? -14.182 10.083  1.803   1.00 71.42  ? 288 ARG A O   1 
ATOM   2435  C CB  . ARG A 1 288 ? -14.565 12.052  -0.102  1.00 76.21  ? 288 ARG A CB  1 
ATOM   2436  C CG  . ARG A 1 288 ? -15.426 12.346  -1.329  1.00 91.80  ? 288 ARG A CG  1 
ATOM   2437  C CD  . ARG A 1 288 ? -16.722 13.078  -0.985  1.00 89.59  ? 288 ARG A CD  1 
ATOM   2438  N NE  . ARG A 1 288 ? -17.471 12.424  0.082   1.00 99.43  ? 288 ARG A NE  1 
ATOM   2439  C CZ  . ARG A 1 288 ? -18.190 11.320  -0.073  1.00 97.15  ? 288 ARG A CZ  1 
ATOM   2440  N NH1 . ARG A 1 288 ? -18.254 10.695  -1.237  1.00 100.18 ? 288 ARG A NH1 1 
ATOM   2441  N NH2 . ARG A 1 288 ? -18.859 10.828  0.968   1.00 100.13 ? 288 ARG A NH2 1 
ATOM   2442  N N   . ALA A 1 289 ? -12.252 9.312   0.940   1.00 65.27  ? 289 ALA A N   1 
ATOM   2443  C CA  . ALA A 1 289 ? -11.989 8.406   2.044   1.00 60.26  ? 289 ALA A CA  1 
ATOM   2444  C C   . ALA A 1 289 ? -11.199 9.089   3.152   1.00 59.78  ? 289 ALA A C   1 
ATOM   2445  O O   . ALA A 1 289 ? -10.572 10.132  2.962   1.00 60.30  ? 289 ALA A O   1 
ATOM   2446  C CB  . ALA A 1 289 ? -11.226 7.174   1.562   1.00 55.06  ? 289 ALA A CB  1 
ATOM   2447  N N   . SER A 1 290 ? -11.242 8.482   4.313   1.00 57.51  ? 290 SER A N   1 
ATOM   2448  C CA  . SER A 1 290 ? -10.385 8.853   5.418   1.00 55.83  ? 290 SER A CA  1 
ATOM   2449  C C   . SER A 1 290 ? -9.387  7.738   5.703   1.00 56.44  ? 290 SER A C   1 
ATOM   2450  O O   . SER A 1 290 ? -9.727  6.555   5.637   1.00 46.63  ? 290 SER A O   1 
ATOM   2451  C CB  . SER A 1 290 ? -11.200 9.125   6.681   1.00 59.40  ? 290 SER A CB  1 
ATOM   2452  O OG  . SER A 1 290 ? -10.393 8.978   7.836   1.00 58.71  ? 290 SER A OG  1 
ATOM   2453  N N   . PRO A 1 291 ? -8.146  8.089   6.022   1.00 58.19  ? 291 PRO A N   1 
ATOM   2454  C CA  . PRO A 1 291 ? -7.143  7.087   6.399   1.00 53.50  ? 291 PRO A CA  1 
ATOM   2455  C C   . PRO A 1 291 ? -7.255  6.587   7.833   1.00 56.15  ? 291 PRO A C   1 
ATOM   2456  O O   . PRO A 1 291 ? -6.324  5.929   8.304   1.00 58.74  ? 291 PRO A O   1 
ATOM   2457  C CB  . PRO A 1 291 ? -5.846  7.873   6.207   1.00 55.26  ? 291 PRO A CB  1 
ATOM   2458  C CG  . PRO A 1 291 ? -6.208  9.254   6.666   1.00 53.56  ? 291 PRO A CG  1 
ATOM   2459  C CD  . PRO A 1 291 ? -7.622  9.460   6.168   1.00 58.38  ? 291 PRO A CD  1 
ATOM   2460  N N   . TYR A 1 292 ? -8.366  6.872   8.524   1.00 52.26  ? 292 TYR A N   1 
ATOM   2461  C CA  . TYR A 1 292 ? -8.546  6.546   9.936   1.00 55.24  ? 292 TYR A CA  1 
ATOM   2462  C C   . TYR A 1 292 ? -9.552  5.419   10.128  1.00 55.21  ? 292 TYR A C   1 
ATOM   2463  O O   . TYR A 1 292 ? -10.301 5.399   11.108  1.00 52.09  ? 292 TYR A O   1 
ATOM   2464  C CB  . TYR A 1 292 ? -8.963  7.792   10.725  1.00 52.85  ? 292 TYR A CB  1 
ATOM   2465  C CG  . TYR A 1 292 ? -8.056  8.974   10.447  1.00 53.88  ? 292 TYR A CG  1 
ATOM   2466  C CD1 . TYR A 1 292 ? -6.675  8.832   10.518  1.00 54.38  ? 292 TYR A CD1 1 
ATOM   2467  C CD2 . TYR A 1 292 ? -8.568  10.211  10.073  1.00 52.13  ? 292 TYR A CD2 1 
ATOM   2468  C CE1 . TYR A 1 292 ? -5.827  9.886   10.243  1.00 52.91  ? 292 TYR A CE1 1 
ATOM   2469  C CE2 . TYR A 1 292 ? -7.715  11.286  9.792   1.00 58.43  ? 292 TYR A CE2 1 
ATOM   2470  C CZ  . TYR A 1 292 ? -6.343  11.109  9.881   1.00 53.36  ? 292 TYR A CZ  1 
ATOM   2471  O OH  . TYR A 1 292 ? -5.471  12.141  9.613   1.00 46.50  ? 292 TYR A OH  1 
ATOM   2472  N N   . LEU A 1 293 ? -9.558  4.469   9.195   1.00 57.67  ? 293 LEU A N   1 
ATOM   2473  C CA  . LEU A 1 293 ? -10.541 3.400   9.134   1.00 53.24  ? 293 LEU A CA  1 
ATOM   2474  C C   . LEU A 1 293 ? -9.858  2.121   8.688   1.00 47.59  ? 293 LEU A C   1 
ATOM   2475  O O   . LEU A 1 293 ? -8.930  2.149   7.876   1.00 52.71  ? 293 LEU A O   1 
ATOM   2476  C CB  . LEU A 1 293 ? -11.677 3.713   8.139   1.00 50.06  ? 293 LEU A CB  1 
ATOM   2477  C CG  . LEU A 1 293 ? -12.842 4.616   8.546   1.00 49.90  ? 293 LEU A CG  1 
ATOM   2478  C CD1 . LEU A 1 293 ? -12.436 6.055   8.425   1.00 58.93  ? 293 LEU A CD1 1 
ATOM   2479  C CD2 . LEU A 1 293 ? -14.071 4.367   7.699   1.00 54.46  ? 293 LEU A CD2 1 
ATOM   2480  N N   . ARG A 1 294 ? -10.333 0.998   9.211   1.00 39.98  ? 294 ARG A N   1 
ATOM   2481  C CA  . ARG A 1 294 ? -9.983  -0.283  8.621   1.00 43.07  ? 294 ARG A CA  1 
ATOM   2482  C C   . ARG A 1 294 ? -10.738 -0.463  7.312   1.00 50.76  ? 294 ARG A C   1 
ATOM   2483  O O   . ARG A 1 294 ? -11.932 -0.165  7.221   1.00 44.90  ? 294 ARG A O   1 
ATOM   2484  C CB  . ARG A 1 294 ? -10.318 -1.427  9.573   1.00 40.12  ? 294 ARG A CB  1 
ATOM   2485  C CG  . ARG A 1 294 ? -9.991  -2.788  8.992   1.00 40.98  ? 294 ARG A CG  1 
ATOM   2486  C CD  . ARG A 1 294 ? -10.657 -3.910  9.760   1.00 50.76  ? 294 ARG A CD  1 
ATOM   2487  N NE  . ARG A 1 294 ? -10.181 -4.003  11.134  1.00 52.34  ? 294 ARG A NE  1 
ATOM   2488  C CZ  . ARG A 1 294 ? -10.875 -3.586  12.182  1.00 58.38  ? 294 ARG A CZ  1 
ATOM   2489  N NH1 . ARG A 1 294 ? -12.066 -3.029  12.038  1.00 61.21  ? 294 ARG A NH1 1 
ATOM   2490  N NH2 . ARG A 1 294 ? -10.361 -3.727  13.402  1.00 54.41  ? 294 ARG A NH2 1 
ATOM   2491  N N   . TYR A 1 295 ? -10.042 -0.948  6.291   1.00 48.52  ? 295 TYR A N   1 
ATOM   2492  C CA  . TYR A 1 295 ? -10.645 -1.168  4.988   1.00 42.76  ? 295 TYR A CA  1 
ATOM   2493  C C   . TYR A 1 295 ? -10.581 -2.644  4.627   1.00 41.75  ? 295 TYR A C   1 
ATOM   2494  O O   . TYR A 1 295 ? -9.531  -3.277  4.766   1.00 46.20  ? 295 TYR A O   1 
ATOM   2495  C CB  . TYR A 1 295 ? -9.952  -0.326  3.918   1.00 44.27  ? 295 TYR A CB  1 
ATOM   2496  C CG  . TYR A 1 295 ? -10.283 1.151   3.971   1.00 44.41  ? 295 TYR A CG  1 
ATOM   2497  C CD1 . TYR A 1 295 ? -9.545  2.022   4.757   1.00 45.88  ? 295 TYR A CD1 1 
ATOM   2498  C CD2 . TYR A 1 295 ? -11.330 1.675   3.225   1.00 48.99  ? 295 TYR A CD2 1 
ATOM   2499  C CE1 . TYR A 1 295 ? -9.838  3.380   4.799   1.00 49.55  ? 295 TYR A CE1 1 
ATOM   2500  C CE2 . TYR A 1 295 ? -11.631 3.029   3.260   1.00 52.09  ? 295 TYR A CE2 1 
ATOM   2501  C CZ  . TYR A 1 295 ? -10.880 3.877   4.050   1.00 45.49  ? 295 TYR A CZ  1 
ATOM   2502  O OH  . TYR A 1 295 ? -11.168 5.224   4.094   1.00 42.85  ? 295 TYR A OH  1 
ATOM   2503  N N   . TYR A 1 296 ? -11.704 -3.189  4.175   1.00 50.56  ? 296 TYR A N   1 
ATOM   2504  C CA  . TYR A 1 296 ? -11.735 -4.517  3.579   1.00 49.91  ? 296 TYR A CA  1 
ATOM   2505  C C   . TYR A 1 296 ? -11.621 -4.370  2.066   1.00 52.58  ? 296 TYR A C   1 
ATOM   2506  O O   . TYR A 1 296 ? -12.383 -3.613  1.451   1.00 46.71  ? 296 TYR A O   1 
ATOM   2507  C CB  . TYR A 1 296 ? -13.028 -5.257  3.927   1.00 52.44  ? 296 TYR A CB  1 
ATOM   2508  C CG  . TYR A 1 296 ? -13.142 -5.792  5.342   1.00 51.74  ? 296 TYR A CG  1 
ATOM   2509  C CD1 . TYR A 1 296 ? -12.025 -6.212  6.064   1.00 54.67  ? 296 TYR A CD1 1 
ATOM   2510  C CD2 . TYR A 1 296 ? -14.385 -5.905  5.944   1.00 53.42  ? 296 TYR A CD2 1 
ATOM   2511  C CE1 . TYR A 1 296 ? -12.156 -6.708  7.365   1.00 44.66  ? 296 TYR A CE1 1 
ATOM   2512  C CE2 . TYR A 1 296 ? -14.523 -6.398  7.226   1.00 60.94  ? 296 TYR A CE2 1 
ATOM   2513  C CZ  . TYR A 1 296 ? -13.415 -6.797  7.934   1.00 55.41  ? 296 TYR A CZ  1 
ATOM   2514  O OH  . TYR A 1 296 ? -13.591 -7.284  9.209   1.00 54.32  ? 296 TYR A OH  1 
ATOM   2515  N N   . PHE A 1 297 ? -10.666 -5.075  1.470   1.00 53.76  ? 297 PHE A N   1 
ATOM   2516  C CA  . PHE A 1 297 ? -10.536 -5.094  0.017   1.00 48.12  ? 297 PHE A CA  1 
ATOM   2517  C C   . PHE A 1 297 ? -11.310 -6.297  -0.502  1.00 47.99  ? 297 PHE A C   1 
ATOM   2518  O O   . PHE A 1 297 ? -10.874 -7.443  -0.359  1.00 52.03  ? 297 PHE A O   1 
ATOM   2519  C CB  . PHE A 1 297 ? -9.074  -5.139  -0.411  1.00 56.51  ? 297 PHE A CB  1 
ATOM   2520  C CG  . PHE A 1 297 ? -8.890  -4.998  -1.891  1.00 58.59  ? 297 PHE A CG  1 
ATOM   2521  C CD1 . PHE A 1 297 ? -8.970  -3.753  -2.495  1.00 55.39  ? 297 PHE A CD1 1 
ATOM   2522  C CD2 . PHE A 1 297 ? -8.695  -6.114  -2.688  1.00 52.86  ? 297 PHE A CD2 1 
ATOM   2523  C CE1 . PHE A 1 297 ? -8.830  -3.622  -3.863  1.00 50.87  ? 297 PHE A CE1 1 
ATOM   2524  C CE2 . PHE A 1 297 ? -8.557  -5.990  -4.053  1.00 48.51  ? 297 PHE A CE2 1 
ATOM   2525  C CZ  . PHE A 1 297 ? -8.622  -4.743  -4.642  1.00 55.01  ? 297 PHE A CZ  1 
ATOM   2526  N N   . ARG A 1 298 ? -12.486 -6.029  -1.079  1.00 54.96  ? 298 ARG A N   1 
ATOM   2527  C CA  . ARG A 1 298 ? -13.327 -7.055  -1.703  1.00 56.52  ? 298 ARG A CA  1 
ATOM   2528  C C   . ARG A 1 298 ? -13.586 -8.224  -0.756  1.00 63.54  ? 298 ARG A C   1 
ATOM   2529  O O   . ARG A 1 298 ? -13.711 -9.373  -1.190  1.00 68.86  ? 298 ARG A O   1 
ATOM   2530  C CB  . ARG A 1 298 ? -12.702 -7.536  -3.014  1.00 51.58  ? 298 ARG A CB  1 
ATOM   2531  C CG  . ARG A 1 298 ? -12.116 -6.395  -3.829  1.00 50.42  ? 298 ARG A CG  1 
ATOM   2532  C CD  . ARG A 1 298 ? -12.335 -6.550  -5.309  1.00 47.41  ? 298 ARG A CD  1 
ATOM   2533  N NE  . ARG A 1 298 ? -11.218 -7.224  -5.961  1.00 48.65  ? 298 ARG A NE  1 
ATOM   2534  C CZ  . ARG A 1 298 ? -10.437 -6.650  -6.865  1.00 50.96  ? 298 ARG A CZ  1 
ATOM   2535  N NH1 . ARG A 1 298 ? -10.599 -5.381  -7.209  1.00 46.85  ? 298 ARG A NH1 1 
ATOM   2536  N NH2 . ARG A 1 298 ? -9.471  -7.363  -7.436  1.00 54.89  ? 298 ARG A NH2 1 
ATOM   2537  N N   . GLU A 1 299 ? -13.625 -7.926  0.547   1.00 63.71  ? 299 GLU A N   1 
ATOM   2538  C CA  . GLU A 1 299 ? -13.858 -8.892  1.619   1.00 65.44  ? 299 GLU A CA  1 
ATOM   2539  C C   . GLU A 1 299 ? -12.701 -9.871  1.797   1.00 66.67  ? 299 GLU A C   1 
ATOM   2540  O O   . GLU A 1 299 ? -12.684 -10.642 2.761   1.00 71.27  ? 299 GLU A O   1 
ATOM   2541  C CB  . GLU A 1 299 ? -15.156 -9.661  1.375   1.00 62.08  ? 299 GLU A CB  1 
ATOM   2542  C CG  . GLU A 1 299 ? -16.369 -8.754  1.296   1.00 75.97  ? 299 GLU A CG  1 
ATOM   2543  C CD  . GLU A 1 299 ? -17.677 -9.514  1.295   1.00 85.62  ? 299 GLU A CD  1 
ATOM   2544  O OE1 . GLU A 1 299 ? -17.640 -10.763 1.300   1.00 93.21  ? 299 GLU A OE1 1 
ATOM   2545  O OE2 . GLU A 1 299 ? -18.741 -8.861  1.279   1.00 89.32  ? 299 GLU A OE2 1 
ATOM   2546  N N   . LEU A 1 300 ? -11.724 -9.853  0.889   1.00 60.44  ? 300 LEU A N   1 
ATOM   2547  C CA  . LEU A 1 300 ? -10.659 -10.848 0.955   1.00 58.51  ? 300 LEU A CA  1 
ATOM   2548  C C   . LEU A 1 300 ? -9.616  -10.476 2.002   1.00 60.67  ? 300 LEU A C   1 
ATOM   2549  O O   . LEU A 1 300 ? -9.217  -11.312 2.823   1.00 59.13  ? 300 LEU A O   1 
ATOM   2550  C CB  . LEU A 1 300 ? -10.012 -11.021 -0.419  1.00 61.28  ? 300 LEU A CB  1 
ATOM   2551  C CG  . LEU A 1 300 ? -10.961 -11.100 -1.618  1.00 64.87  ? 300 LEU A CG  1 
ATOM   2552  C CD1 . LEU A 1 300 ? -10.304 -10.559 -2.881  1.00 54.13  ? 300 LEU A CD1 1 
ATOM   2553  C CD2 . LEU A 1 300 ? -11.419 -12.530 -1.833  1.00 64.22  ? 300 LEU A CD2 1 
ATOM   2554  N N   . ILE A 1 301 ? -9.172  -9.222  2.003   1.00 61.80  ? 301 ILE A N   1 
ATOM   2555  C CA  . ILE A 1 301 ? -8.032  -8.807  2.808   1.00 55.73  ? 301 ILE A CA  1 
ATOM   2556  C C   . ILE A 1 301 ? -8.334  -7.469  3.467   1.00 51.98  ? 301 ILE A C   1 
ATOM   2557  O O   . ILE A 1 301 ? -9.197  -6.707  3.024   1.00 50.53  ? 301 ILE A O   1 
ATOM   2558  C CB  . ILE A 1 301 ? -6.750  -8.716  1.953   1.00 57.83  ? 301 ILE A CB  1 
ATOM   2559  C CG1 . ILE A 1 301 ? -5.510  -8.947  2.814   1.00 61.01  ? 301 ILE A CG1 1 
ATOM   2560  C CG2 . ILE A 1 301 ? -6.678  -7.379  1.239   1.00 56.94  ? 301 ILE A CG2 1 
ATOM   2561  C CD1 . ILE A 1 301 ? -4.224  -8.949  2.021   1.00 63.16  ? 301 ILE A CD1 1 
ATOM   2562  N N   . SER A 1 302 ? -7.604  -7.187  4.540   1.00 47.57  ? 302 SER A N   1 
ATOM   2563  C CA  . SER A 1 302 ? -7.749  -5.937  5.270   1.00 46.65  ? 302 SER A CA  1 
ATOM   2564  C C   . SER A 1 302 ? -6.602  -5.003  4.919   1.00 44.73  ? 302 SER A C   1 
ATOM   2565  O O   . SER A 1 302 ? -5.432  -5.393  4.977   1.00 47.28  ? 302 SER A O   1 
ATOM   2566  C CB  . SER A 1 302 ? -7.781  -6.188  6.775   1.00 45.60  ? 302 SER A CB  1 
ATOM   2567  O OG  . SER A 1 302 ? -9.085  -6.543  7.182   1.00 52.45  ? 302 SER A OG  1 
ATOM   2568  N N   . VAL A 1 303 ? -6.939  -3.770  4.566   1.00 42.10  ? 303 VAL A N   1 
ATOM   2569  C CA  . VAL A 1 303 ? -5.959  -2.763  4.191   1.00 48.47  ? 303 VAL A CA  1 
ATOM   2570  C C   . VAL A 1 303 ? -6.070  -1.592  5.157   1.00 46.76  ? 303 VAL A C   1 
ATOM   2571  O O   . VAL A 1 303 ? -7.171  -1.087  5.409   1.00 46.65  ? 303 VAL A O   1 
ATOM   2572  C CB  . VAL A 1 303 ? -6.162  -2.304  2.734   1.00 40.07  ? 303 VAL A CB  1 
ATOM   2573  C CG1 . VAL A 1 303 ? -4.998  -1.438  2.284   1.00 40.72  ? 303 VAL A CG1 1 
ATOM   2574  C CG2 . VAL A 1 303 ? -6.331  -3.513  1.823   1.00 38.74  ? 303 VAL A CG2 1 
ATOM   2575  N N   . PHE A 1 304 ? -4.934  -1.166  5.697   1.00 42.95  ? 304 PHE A N   1 
ATOM   2576  C CA  . PHE A 1 304 ? -4.845  0.062   6.471   1.00 41.84  ? 304 PHE A CA  1 
ATOM   2577  C C   . PHE A 1 304 ? -4.010  1.074   5.697   1.00 49.70  ? 304 PHE A C   1 
ATOM   2578  O O   . PHE A 1 304 ? -3.043  0.705   5.024   1.00 55.10  ? 304 PHE A O   1 
ATOM   2579  C CB  . PHE A 1 304 ? -4.226  -0.198  7.846   1.00 38.91  ? 304 PHE A CB  1 
ATOM   2580  C CG  . PHE A 1 304 ? -5.189  -0.765  8.840   1.00 41.66  ? 304 PHE A CG  1 
ATOM   2581  C CD1 . PHE A 1 304 ? -6.134  0.046   9.445   1.00 46.17  ? 304 PHE A CD1 1 
ATOM   2582  C CD2 . PHE A 1 304 ? -5.170  -2.113  9.155   1.00 41.53  ? 304 PHE A CD2 1 
ATOM   2583  C CE1 . PHE A 1 304 ? -7.030  -0.475  10.360  1.00 42.15  ? 304 PHE A CE1 1 
ATOM   2584  C CE2 . PHE A 1 304 ? -6.067  -2.641  10.068  1.00 46.81  ? 304 PHE A CE2 1 
ATOM   2585  C CZ  . PHE A 1 304 ? -6.996  -1.821  10.671  1.00 42.94  ? 304 PHE A CZ  1 
ATOM   2586  N N   . PHE A 1 305 ? -4.382  2.346   5.784   1.00 53.41  ? 305 PHE A N   1 
ATOM   2587  C CA  . PHE A 1 305 ? -3.679  3.413   5.081   1.00 44.64  ? 305 PHE A CA  1 
ATOM   2588  C C   . PHE A 1 305 ? -2.988  4.324   6.086   1.00 54.66  ? 305 PHE A C   1 
ATOM   2589  O O   . PHE A 1 305 ? -3.626  4.818   7.023   1.00 57.59  ? 305 PHE A O   1 
ATOM   2590  C CB  . PHE A 1 305 ? -4.640  4.218   4.209   1.00 49.39  ? 305 PHE A CB  1 
ATOM   2591  C CG  . PHE A 1 305 ? -5.308  3.405   3.147   1.00 53.09  ? 305 PHE A CG  1 
ATOM   2592  C CD1 . PHE A 1 305 ? -6.438  2.663   3.435   1.00 48.74  ? 305 PHE A CD1 1 
ATOM   2593  C CD2 . PHE A 1 305 ? -4.798  3.366   1.862   1.00 51.88  ? 305 PHE A CD2 1 
ATOM   2594  C CE1 . PHE A 1 305 ? -7.050  1.903   2.459   1.00 50.26  ? 305 PHE A CE1 1 
ATOM   2595  C CE2 . PHE A 1 305 ? -5.410  2.611   0.882   1.00 50.60  ? 305 PHE A CE2 1 
ATOM   2596  C CZ  . PHE A 1 305 ? -6.536  1.878   1.182   1.00 49.47  ? 305 PHE A CZ  1 
ATOM   2597  N N   . ARG A 1 306 ? -1.693  4.554   5.883   1.00 50.61  ? 306 ARG A N   1 
ATOM   2598  C CA  . ARG A 1 306 ? -0.915  5.358   6.811   1.00 45.06  ? 306 ARG A CA  1 
ATOM   2599  C C   . ARG A 1 306 ? -1.230  6.846   6.648   1.00 57.43  ? 306 ARG A C   1 
ATOM   2600  O O   . ARG A 1 306 ? -1.724  7.302   5.609   1.00 51.89  ? 306 ARG A O   1 
ATOM   2601  C CB  . ARG A 1 306 ? 0.579   5.116   6.602   1.00 46.33  ? 306 ARG A CB  1 
ATOM   2602  C CG  . ARG A 1 306 ? 1.258   6.200   5.767   1.00 54.25  ? 306 ARG A CG  1 
ATOM   2603  C CD  . ARG A 1 306 ? 2.748   5.959   5.559   1.00 46.03  ? 306 ARG A CD  1 
ATOM   2604  N NE  . ARG A 1 306 ? 3.233   6.678   4.386   1.00 47.27  ? 306 ARG A NE  1 
ATOM   2605  C CZ  . ARG A 1 306 ? 4.453   7.187   4.268   1.00 51.00  ? 306 ARG A CZ  1 
ATOM   2606  N NH1 . ARG A 1 306 ? 5.361   7.031   5.218   1.00 49.23  ? 306 ARG A NH1 1 
ATOM   2607  N NH2 . ARG A 1 306 ? 4.770   7.870   3.168   1.00 46.52  ? 306 ARG A NH2 1 
ATOM   2608  N N   . ASP A 1 307 ? -0.942  7.604   7.709   1.00 60.60  ? 307 ASP A N   1 
ATOM   2609  C CA  . ASP A 1 307 ? -1.036  9.061   7.697   1.00 57.72  ? 307 ASP A CA  1 
ATOM   2610  C C   . ASP A 1 307 ? 0.269   9.603   7.128   1.00 53.34  ? 307 ASP A C   1 
ATOM   2611  O O   . ASP A 1 307 ? 1.319   9.521   7.774   1.00 51.07  ? 307 ASP A O   1 
ATOM   2612  C CB  . ASP A 1 307 ? -1.295  9.599   9.104   1.00 48.02  ? 307 ASP A CB  1 
ATOM   2613  C CG  . ASP A 1 307 ? -1.764  11.049  9.106   1.00 58.40  ? 307 ASP A CG  1 
ATOM   2614  O OD1 . ASP A 1 307 ? -0.931  11.955  8.884   1.00 58.23  ? 307 ASP A OD1 1 
ATOM   2615  O OD2 . ASP A 1 307 ? -2.970  11.285  9.344   1.00 61.55  ? 307 ASP A OD2 1 
ATOM   2616  N N   . LYS A 1 308 ? 0.206   10.142  5.910   1.00 57.67  ? 308 LYS A N   1 
ATOM   2617  C CA  . LYS A 1 308 ? 1.416   10.624  5.252   1.00 51.49  ? 308 LYS A CA  1 
ATOM   2618  C C   . LYS A 1 308 ? 2.042   11.773  6.030   1.00 49.00  ? 308 LYS A C   1 
ATOM   2619  O O   . LYS A 1 308 ? 3.271   11.864  6.134   1.00 48.86  ? 308 LYS A O   1 
ATOM   2620  C CB  . LYS A 1 308 ? 1.096   11.050  3.815   1.00 51.39  ? 308 LYS A CB  1 
ATOM   2621  C CG  . LYS A 1 308 ? 2.295   11.613  3.074   1.00 59.96  ? 308 LYS A CG  1 
ATOM   2622  C CD  . LYS A 1 308 ? 1.938   12.283  1.762   1.00 52.91  ? 308 LYS A CD  1 
ATOM   2623  C CE  . LYS A 1 308 ? 3.041   12.119  0.722   1.00 56.10  ? 308 LYS A CE  1 
ATOM   2624  N NZ  . LYS A 1 308 ? 3.769   10.820  0.821   1.00 62.18  ? 308 LYS A NZ  1 
ATOM   2625  N N   . THR A 1 309 ? 1.207   12.641  6.610   1.00 46.45  ? 309 THR A N   1 
ATOM   2626  C CA  . THR A 1 309 ? 1.696   13.837  7.292   1.00 50.25  ? 309 THR A CA  1 
ATOM   2627  C C   . THR A 1 309 ? 2.495   13.484  8.541   1.00 50.14  ? 309 THR A C   1 
ATOM   2628  O O   . THR A 1 309 ? 3.654   13.892  8.688   1.00 47.69  ? 309 THR A O   1 
ATOM   2629  C CB  . THR A 1 309 ? 0.522   14.750  7.646   1.00 47.26  ? 309 THR A CB  1 
ATOM   2630  O OG1 . THR A 1 309 ? -0.274  14.973  6.475   1.00 48.76  ? 309 THR A OG1 1 
ATOM   2631  C CG2 . THR A 1 309 ? 1.024   16.084  8.187   1.00 46.50  ? 309 THR A CG2 1 
ATOM   2632  N N   . LEU A 1 310 ? 1.888   12.732  9.461   1.00 47.03  ? 310 LEU A N   1 
ATOM   2633  C CA  . LEU A 1 310 ? 2.563   12.433  10.721  1.00 45.19  ? 310 LEU A CA  1 
ATOM   2634  C C   . LEU A 1 310 ? 3.802   11.584  10.489  1.00 47.61  ? 310 LEU A C   1 
ATOM   2635  O O   . LEU A 1 310 ? 4.831   11.768  11.152  1.00 44.92  ? 310 LEU A O   1 
ATOM   2636  C CB  . LEU A 1 310 ? 1.609   11.722  11.678  1.00 50.18  ? 310 LEU A CB  1 
ATOM   2637  C CG  . LEU A 1 310 ? 0.340   12.476  12.059  1.00 47.93  ? 310 LEU A CG  1 
ATOM   2638  C CD1 . LEU A 1 310 ? -0.569  11.545  12.821  1.00 46.34  ? 310 LEU A CD1 1 
ATOM   2639  C CD2 . LEU A 1 310 ? 0.662   13.715  12.880  1.00 45.40  ? 310 LEU A CD2 1 
ATOM   2640  N N   . SER A 1 311 ? 3.717   10.646  9.547   1.00 54.00  ? 311 SER A N   1 
ATOM   2641  C CA  . SER A 1 311 ? 4.849   9.773   9.268   1.00 53.11  ? 311 SER A CA  1 
ATOM   2642  C C   . SER A 1 311 ? 6.016   10.556  8.675   1.00 49.01  ? 311 SER A C   1 
ATOM   2643  O O   . SER A 1 311 ? 7.165   10.389  9.103   1.00 48.16  ? 311 SER A O   1 
ATOM   2644  C CB  . SER A 1 311 ? 4.406   8.640   8.340   1.00 49.23  ? 311 SER A CB  1 
ATOM   2645  O OG  . SER A 1 311 ? 3.272   7.969   8.885   1.00 49.70  ? 311 SER A OG  1 
ATOM   2646  N N   . ASP A 1 312 ? 5.744   11.439  7.712   1.00 49.14  ? 312 ASP A N   1 
ATOM   2647  C CA  . ASP A 1 312 ? 6.836   12.195  7.110   1.00 45.65  ? 312 ASP A CA  1 
ATOM   2648  C C   . ASP A 1 312 ? 7.412   13.222  8.077   1.00 45.00  ? 312 ASP A C   1 
ATOM   2649  O O   . ASP A 1 312 ? 8.595   13.564  7.974   1.00 49.86  ? 312 ASP A O   1 
ATOM   2650  C CB  . ASP A 1 312 ? 6.366   12.877  5.828   1.00 40.31  ? 312 ASP A CB  1 
ATOM   2651  C CG  . ASP A 1 312 ? 5.995   11.888  4.734   1.00 55.52  ? 312 ASP A CG  1 
ATOM   2652  O OD1 . ASP A 1 312 ? 6.548   10.762  4.694   1.00 60.25  ? 312 ASP A OD1 1 
ATOM   2653  O OD2 . ASP A 1 312 ? 5.135   12.248  3.907   1.00 54.14  ? 312 ASP A OD2 1 
ATOM   2654  N N   . LEU A 1 313 ? 6.604   13.718  9.017   1.00 43.13  ? 313 LEU A N   1 
ATOM   2655  C CA  . LEU A 1 313 ? 7.114   14.648  10.024  1.00 48.28  ? 313 LEU A CA  1 
ATOM   2656  C C   . LEU A 1 313 ? 8.258   14.019  10.815  1.00 50.34  ? 313 LEU A C   1 
ATOM   2657  O O   . LEU A 1 313 ? 9.301   14.647  11.032  1.00 46.96  ? 313 LEU A O   1 
ATOM   2658  C CB  . LEU A 1 313 ? 5.985   15.081  10.966  1.00 49.97  ? 313 LEU A CB  1 
ATOM   2659  C CG  . LEU A 1 313 ? 5.159   16.295  10.530  1.00 53.31  ? 313 LEU A CG  1 
ATOM   2660  C CD1 . LEU A 1 313 ? 3.837   16.356  11.279  1.00 48.71  ? 313 LEU A CD1 1 
ATOM   2661  C CD2 . LEU A 1 313 ? 5.938   17.589  10.697  1.00 53.42  ? 313 LEU A CD2 1 
ATOM   2662  N N   . ILE A 1 314 ? 8.070   12.774  11.264  1.00 46.96  ? 314 ILE A N   1 
ATOM   2663  C CA  . ILE A 1 314 ? 9.134   12.051  11.952  1.00 42.70  ? 314 ILE A CA  1 
ATOM   2664  C C   . ILE A 1 314 ? 10.252  11.713  10.977  1.00 46.20  ? 314 ILE A C   1 
ATOM   2665  O O   . ILE A 1 314 ? 11.438  11.906  11.279  1.00 50.06  ? 314 ILE A O   1 
ATOM   2666  C CB  . ILE A 1 314 ? 8.562   10.790  12.634  1.00 42.75  ? 314 ILE A CB  1 
ATOM   2667  C CG1 . ILE A 1 314 ? 7.778   11.173  13.881  1.00 44.26  ? 314 ILE A CG1 1 
ATOM   2668  C CG2 . ILE A 1 314 ? 9.646   9.795   13.005  1.00 33.86  ? 314 ILE A CG2 1 
ATOM   2669  C CD1 . ILE A 1 314 ? 6.526   10.368  14.047  1.00 39.37  ? 314 ILE A CD1 1 
ATOM   2670  N N   . GLY A 1 315 ? 9.895   11.240  9.781   1.00 41.35  ? 315 GLY A N   1 
ATOM   2671  C CA  . GLY A 1 315 ? 10.907  10.813  8.829   1.00 45.94  ? 315 GLY A CA  1 
ATOM   2672  C C   . GLY A 1 315 ? 11.789  11.937  8.313   1.00 44.42  ? 315 GLY A C   1 
ATOM   2673  O O   . GLY A 1 315 ? 12.946  11.697  7.950   1.00 43.48  ? 315 GLY A O   1 
ATOM   2674  N N   . PHE A 1 316 ? 11.269  13.180  8.285   1.00 41.75  ? 316 PHE A N   1 
ATOM   2675  C CA  . PHE A 1 316 ? 11.982  14.272  7.626   1.00 47.95  ? 316 PHE A CA  1 
ATOM   2676  C C   . PHE A 1 316 ? 11.956  15.606  8.364   1.00 49.44  ? 316 PHE A C   1 
ATOM   2677  O O   . PHE A 1 316 ? 12.878  16.405  8.165   1.00 52.21  ? 316 PHE A O   1 
ATOM   2678  C CB  . PHE A 1 316 ? 11.433  14.492  6.200   1.00 42.62  ? 316 PHE A CB  1 
ATOM   2679  C CG  . PHE A 1 316 ? 11.395  13.242  5.361   1.00 39.40  ? 316 PHE A CG  1 
ATOM   2680  C CD1 . PHE A 1 316 ? 12.546  12.762  4.753   1.00 39.06  ? 316 PHE A CD1 1 
ATOM   2681  C CD2 . PHE A 1 316 ? 10.207  12.546  5.178   1.00 41.78  ? 316 PHE A CD2 1 
ATOM   2682  C CE1 . PHE A 1 316 ? 12.514  11.606  3.978   1.00 38.55  ? 316 PHE A CE1 1 
ATOM   2683  C CE2 . PHE A 1 316 ? 10.168  11.391  4.409   1.00 38.29  ? 316 PHE A CE2 1 
ATOM   2684  C CZ  . PHE A 1 316 ? 11.326  10.921  3.809   1.00 44.01  ? 316 PHE A CZ  1 
ATOM   2685  N N   . SER A 1 317 ? 10.951  15.908  9.180   1.00 43.98  ? 317 SER A N   1 
ATOM   2686  C CA  . SER A 1 317 ? 10.847  17.261  9.720   1.00 42.33  ? 317 SER A CA  1 
ATOM   2687  C C   . SER A 1 317 ? 11.350  17.395  11.143  1.00 53.91  ? 317 SER A C   1 
ATOM   2688  O O   . SER A 1 317 ? 12.049  18.365  11.458  1.00 52.89  ? 317 SER A O   1 
ATOM   2689  C CB  . SER A 1 317 ? 9.402   17.746  9.676   1.00 51.73  ? 317 SER A CB  1 
ATOM   2690  O OG  . SER A 1 317 ? 8.961   17.828  8.345   1.00 61.70  ? 317 SER A OG  1 
ATOM   2691  N N   . TYR A 1 318 ? 10.987  16.456  12.012  1.00 51.53  ? 318 TYR A N   1 
ATOM   2692  C CA  . TYR A 1 318 ? 11.212  16.632  13.437  1.00 46.68  ? 318 TYR A CA  1 
ATOM   2693  C C   . TYR A 1 318 ? 12.681  16.628  13.828  1.00 53.58  ? 318 TYR A C   1 
ATOM   2694  O O   . TYR A 1 318 ? 12.989  17.044  14.950  1.00 45.99  ? 318 TYR A O   1 
ATOM   2695  C CB  . TYR A 1 318 ? 10.477  15.549  14.221  1.00 47.13  ? 318 TYR A CB  1 
ATOM   2696  C CG  . TYR A 1 318 ? 9.000   15.795  14.390  1.00 52.28  ? 318 TYR A CG  1 
ATOM   2697  C CD1 . TYR A 1 318 ? 8.444   17.029  14.087  1.00 52.44  ? 318 TYR A CD1 1 
ATOM   2698  C CD2 . TYR A 1 318 ? 8.164   14.804  14.891  1.00 50.53  ? 318 TYR A CD2 1 
ATOM   2699  C CE1 . TYR A 1 318 ? 7.100   17.268  14.256  1.00 49.17  ? 318 TYR A CE1 1 
ATOM   2700  C CE2 . TYR A 1 318 ? 6.807   15.035  15.067  1.00 46.76  ? 318 TYR A CE2 1 
ATOM   2701  C CZ  . TYR A 1 318 ? 6.284   16.275  14.744  1.00 48.75  ? 318 TYR A CZ  1 
ATOM   2702  O OH  . TYR A 1 318 ? 4.946   16.551  14.898  1.00 47.52  ? 318 TYR A OH  1 
ATOM   2703  N N   . HIS A 1 319 ? 13.588  16.175  12.951  1.00 53.91  ? 319 HIS A N   1 
ATOM   2704  C CA  . HIS A 1 319 ? 14.996  16.125  13.337  1.00 44.52  ? 319 HIS A CA  1 
ATOM   2705  C C   . HIS A 1 319 ? 15.541  17.512  13.628  1.00 44.20  ? 319 HIS A C   1 
ATOM   2706  O O   . HIS A 1 319 ? 16.450  17.657  14.449  1.00 48.37  ? 319 HIS A O   1 
ATOM   2707  C CB  . HIS A 1 319 ? 15.843  15.442  12.259  1.00 49.55  ? 319 HIS A CB  1 
ATOM   2708  C CG  . HIS A 1 319 ? 16.048  16.265  11.022  1.00 53.33  ? 319 HIS A CG  1 
ATOM   2709  N ND1 . HIS A 1 319 ? 15.029  16.547  10.139  1.00 54.03  ? 319 HIS A ND1 1 
ATOM   2710  C CD2 . HIS A 1 319 ? 17.157  16.857  10.516  1.00 57.84  ? 319 HIS A CD2 1 
ATOM   2711  C CE1 . HIS A 1 319 ? 15.499  17.276  9.143   1.00 48.58  ? 319 HIS A CE1 1 
ATOM   2712  N NE2 . HIS A 1 319 ? 16.787  17.483  9.349   1.00 53.61  ? 319 HIS A NE2 1 
ATOM   2713  N N   . ALA A 1 320 ? 14.989  18.541  12.986  1.00 43.03  ? 320 ALA A N   1 
ATOM   2714  C CA  . ALA A 1 320 ? 15.497  19.893  13.186  1.00 50.05  ? 320 ALA A CA  1 
ATOM   2715  C C   . ALA A 1 320 ? 14.984  20.526  14.474  1.00 52.87  ? 320 ALA A C   1 
ATOM   2716  O O   . ALA A 1 320 ? 15.665  21.381  15.051  1.00 57.62  ? 320 ALA A O   1 
ATOM   2717  C CB  . ALA A 1 320 ? 15.129  20.774  11.994  1.00 45.18  ? 320 ALA A CB  1 
ATOM   2718  N N   . TRP A 1 321 ? 13.804  20.127  14.937  1.00 51.86  ? 321 TRP A N   1 
ATOM   2719  C CA  . TRP A 1 321 ? 13.187  20.766  16.087  1.00 53.04  ? 321 TRP A CA  1 
ATOM   2720  C C   . TRP A 1 321 ? 13.773  20.216  17.386  1.00 57.52  ? 321 TRP A C   1 
ATOM   2721  O O   . TRP A 1 321 ? 14.403  19.158  17.418  1.00 57.62  ? 321 TRP A O   1 
ATOM   2722  C CB  . TRP A 1 321 ? 11.669  20.554  16.093  1.00 47.86  ? 321 TRP A CB  1 
ATOM   2723  C CG  . TRP A 1 321 ? 10.931  20.749  14.788  1.00 47.92  ? 321 TRP A CG  1 
ATOM   2724  C CD1 . TRP A 1 321 ? 11.457  20.807  13.525  1.00 53.59  ? 321 TRP A CD1 1 
ATOM   2725  C CD2 . TRP A 1 321 ? 9.518   20.937  14.637  1.00 57.31  ? 321 TRP A CD2 1 
ATOM   2726  N NE1 . TRP A 1 321 ? 10.457  21.004  12.600  1.00 58.14  ? 321 TRP A NE1 1 
ATOM   2727  C CE2 . TRP A 1 321 ? 9.258   21.091  13.258  1.00 58.12  ? 321 TRP A CE2 1 
ATOM   2728  C CE3 . TRP A 1 321 ? 8.446   20.985  15.536  1.00 52.14  ? 321 TRP A CE3 1 
ATOM   2729  C CZ2 . TRP A 1 321 ? 7.971   21.288  12.760  1.00 56.59  ? 321 TRP A CZ2 1 
ATOM   2730  C CZ3 . TRP A 1 321 ? 7.173   21.180  15.038  1.00 55.28  ? 321 TRP A CZ3 1 
ATOM   2731  C CH2 . TRP A 1 321 ? 6.945   21.328  13.665  1.00 60.60  ? 321 TRP A CH2 1 
ATOM   2732  N N   . ASN A 1 322 ? 13.545  20.943  18.474  1.00 59.08  ? 322 ASN A N   1 
ATOM   2733  C CA  . ASN A 1 322 ? 13.812  20.382  19.787  1.00 60.63  ? 322 ASN A CA  1 
ATOM   2734  C C   . ASN A 1 322 ? 12.856  19.233  20.066  1.00 61.59  ? 322 ASN A C   1 
ATOM   2735  O O   . ASN A 1 322 ? 11.765  19.149  19.494  1.00 60.49  ? 322 ASN A O   1 
ATOM   2736  C CB  . ASN A 1 322 ? 13.674  21.448  20.863  1.00 58.23  ? 322 ASN A CB  1 
ATOM   2737  C CG  . ASN A 1 322 ? 14.512  22.648  20.566  1.00 67.94  ? 322 ASN A CG  1 
ATOM   2738  O OD1 . ASN A 1 322 ? 15.734  22.552  20.480  1.00 68.50  ? 322 ASN A OD1 1 
ATOM   2739  N ND2 . ASN A 1 322 ? 13.866  23.789  20.382  1.00 68.87  ? 322 ASN A ND2 1 
ATOM   2740  N N   . ALA A 1 323 ? 13.277  18.339  20.961  1.00 62.27  ? 323 ALA A N   1 
ATOM   2741  C CA  . ALA A 1 323 ? 12.496  17.133  21.211  1.00 51.68  ? 323 ALA A CA  1 
ATOM   2742  C C   . ALA A 1 323 ? 11.140  17.466  21.822  1.00 58.77  ? 323 ALA A C   1 
ATOM   2743  O O   . ALA A 1 323 ? 10.116  16.891  21.431  1.00 60.52  ? 323 ALA A O   1 
ATOM   2744  C CB  . ALA A 1 323 ? 13.281  16.178  22.109  1.00 46.93  ? 323 ALA A CB  1 
ATOM   2745  N N   . GLU A 1 324 ? 11.108  18.406  22.771  1.00 60.00  ? 324 GLU A N   1 
ATOM   2746  C CA  . GLU A 1 324 ? 9.846   18.762  23.410  1.00 60.99  ? 324 GLU A CA  1 
ATOM   2747  C C   . GLU A 1 324 ? 8.862   19.351  22.407  1.00 63.24  ? 324 GLU A C   1 
ATOM   2748  O O   . GLU A 1 324 ? 7.656   19.088  22.478  1.00 61.94  ? 324 GLU A O   1 
ATOM   2749  C CB  . GLU A 1 324 ? 10.096  19.741  24.557  1.00 66.65  ? 324 GLU A CB  1 
ATOM   2750  C CG  . GLU A 1 324 ? 9.059   19.655  25.663  1.00 68.47  ? 324 GLU A CG  1 
ATOM   2751  C CD  . GLU A 1 324 ? 8.540   21.015  26.087  1.00 84.59  ? 324 GLU A CD  1 
ATOM   2752  O OE1 . GLU A 1 324 ? 7.560   21.060  26.860  1.00 93.69  ? 324 GLU A OE1 1 
ATOM   2753  O OE2 . GLU A 1 324 ? 9.111   22.041  25.654  1.00 89.80  ? 324 GLU A OE2 1 
ATOM   2754  N N   . ASP A 1 325 ? 9.358   20.139  21.453  1.00 61.66  ? 325 ASP A N   1 
ATOM   2755  C CA  . ASP A 1 325 ? 8.476   20.760  20.470  1.00 59.11  ? 325 ASP A CA  1 
ATOM   2756  C C   . ASP A 1 325 ? 7.860   19.714  19.546  1.00 59.51  ? 325 ASP A C   1 
ATOM   2757  O O   . ASP A 1 325 ? 6.646   19.723  19.300  1.00 55.31  ? 325 ASP A O   1 
ATOM   2758  C CB  . ASP A 1 325 ? 9.258   21.803  19.677  1.00 60.00  ? 325 ASP A CB  1 
ATOM   2759  C CG  . ASP A 1 325 ? 9.655   23.007  20.527  1.00 66.36  ? 325 ASP A CG  1 
ATOM   2760  O OD1 . ASP A 1 325 ? 9.690   22.873  21.770  1.00 69.03  ? 325 ASP A OD1 1 
ATOM   2761  O OD2 . ASP A 1 325 ? 9.913   24.091  19.962  1.00 71.52  ? 325 ASP A OD2 1 
ATOM   2762  N N   . ALA A 1 326 ? 8.683   18.786  19.048  1.00 55.30  ? 326 ALA A N   1 
ATOM   2763  C CA  . ALA A 1 326 ? 8.203   17.796  18.089  1.00 48.93  ? 326 ALA A CA  1 
ATOM   2764  C C   . ALA A 1 326 ? 7.123   16.919  18.700  1.00 48.59  ? 326 ALA A C   1 
ATOM   2765  O O   . ALA A 1 326 ? 6.082   16.670  18.081  1.00 54.87  ? 326 ALA A O   1 
ATOM   2766  C CB  . ALA A 1 326 ? 9.366   16.942  17.593  1.00 51.32  ? 326 ALA A CB  1 
ATOM   2767  N N   . VAL A 1 327 ? 7.352   16.442  19.922  1.00 52.96  ? 327 VAL A N   1 
ATOM   2768  C CA  . VAL A 1 327 ? 6.339   15.638  20.596  1.00 55.20  ? 327 VAL A CA  1 
ATOM   2769  C C   . VAL A 1 327 ? 5.048   16.433  20.759  1.00 49.38  ? 327 VAL A C   1 
ATOM   2770  O O   . VAL A 1 327 ? 3.955   15.926  20.485  1.00 55.83  ? 327 VAL A O   1 
ATOM   2771  C CB  . VAL A 1 327 ? 6.877   15.130  21.946  1.00 52.84  ? 327 VAL A CB  1 
ATOM   2772  C CG1 . VAL A 1 327 ? 5.766   14.473  22.731  1.00 47.42  ? 327 VAL A CG1 1 
ATOM   2773  C CG2 . VAL A 1 327 ? 8.059   14.172  21.730  1.00 47.27  ? 327 VAL A CG2 1 
ATOM   2774  N N   . ARG A 1 328 ? 5.151   17.698  21.174  1.00 48.15  ? 328 ARG A N   1 
ATOM   2775  C CA  . ARG A 1 328 ? 3.952   18.509  21.360  1.00 52.03  ? 328 ARG A CA  1 
ATOM   2776  C C   . ARG A 1 328 ? 3.235   18.744  20.036  1.00 55.12  ? 328 ARG A C   1 
ATOM   2777  O O   . ARG A 1 328 ? 2.000   18.720  19.979  1.00 53.08  ? 328 ARG A O   1 
ATOM   2778  C CB  . ARG A 1 328 ? 4.312   19.835  22.027  1.00 50.57  ? 328 ARG A CB  1 
ATOM   2779  C CG  . ARG A 1 328 ? 4.692   19.678  23.477  1.00 51.68  ? 328 ARG A CG  1 
ATOM   2780  C CD  . ARG A 1 328 ? 4.515   20.953  24.274  1.00 62.96  ? 328 ARG A CD  1 
ATOM   2781  N NE  . ARG A 1 328 ? 5.778   21.670  24.388  1.00 73.16  ? 328 ARG A NE  1 
ATOM   2782  C CZ  . ARG A 1 328 ? 6.132   22.705  23.637  1.00 77.48  ? 328 ARG A CZ  1 
ATOM   2783  N NH1 . ARG A 1 328 ? 5.306   23.231  22.747  1.00 78.04  ? 328 ARG A NH1 1 
ATOM   2784  N NH2 . ARG A 1 328 ? 7.341   23.234  23.794  1.00 77.76  ? 328 ARG A NH2 1 
ATOM   2785  N N   . ASP A 1 329 ? 3.991   18.980  18.962  1.00 54.96  ? 329 ASP A N   1 
ATOM   2786  C CA  . ASP A 1 329 ? 3.384   19.070  17.639  1.00 50.53  ? 329 ASP A CA  1 
ATOM   2787  C C   . ASP A 1 329 ? 2.643   17.781  17.310  1.00 51.55  ? 329 ASP A C   1 
ATOM   2788  O O   . ASP A 1 329 ? 1.488   17.807  16.871  1.00 49.52  ? 329 ASP A O   1 
ATOM   2789  C CB  . ASP A 1 329 ? 4.468   19.369  16.596  1.00 50.48  ? 329 ASP A CB  1 
ATOM   2790  C CG  . ASP A 1 329 ? 3.908   19.566  15.192  1.00 60.71  ? 329 ASP A CG  1 
ATOM   2791  O OD1 . ASP A 1 329 ? 3.367   20.658  14.904  1.00 59.17  ? 329 ASP A OD1 1 
ATOM   2792  O OD2 . ASP A 1 329 ? 4.010   18.625  14.375  1.00 57.83  ? 329 ASP A OD2 1 
ATOM   2793  N N   . PHE A 1 330 ? 3.285   16.638  17.568  1.00 50.74  ? 330 PHE A N   1 
ATOM   2794  C CA  . PHE A 1 330 ? 2.705   15.344  17.220  1.00 47.76  ? 330 PHE A CA  1 
ATOM   2795  C C   . PHE A 1 330 ? 1.403   15.100  17.975  1.00 51.24  ? 330 PHE A C   1 
ATOM   2796  O O   . PHE A 1 330 ? 0.387   14.716  17.382  1.00 50.58  ? 330 PHE A O   1 
ATOM   2797  C CB  . PHE A 1 330 ? 3.729   14.243  17.502  1.00 44.20  ? 330 PHE A CB  1 
ATOM   2798  C CG  . PHE A 1 330 ? 3.281   12.864  17.107  1.00 48.15  ? 330 PHE A CG  1 
ATOM   2799  C CD1 . PHE A 1 330 ? 3.319   12.455  15.781  1.00 51.69  ? 330 PHE A CD1 1 
ATOM   2800  C CD2 . PHE A 1 330 ? 2.853   11.966  18.067  1.00 44.90  ? 330 PHE A CD2 1 
ATOM   2801  C CE1 . PHE A 1 330 ? 2.919   11.180  15.423  1.00 63.36  ? 330 PHE A CE1 1 
ATOM   2802  C CE2 . PHE A 1 330 ? 2.454   10.691  17.720  1.00 49.30  ? 330 PHE A CE2 1 
ATOM   2803  C CZ  . PHE A 1 330 ? 2.484   10.295  16.398  1.00 62.22  ? 330 PHE A CZ  1 
ATOM   2804  N N   . ILE A 1 331 ? 1.404   15.339  19.287  1.00 48.95  ? 331 ILE A N   1 
ATOM   2805  C CA  . ILE A 1 331 ? 0.176   15.165  20.052  1.00 50.83  ? 331 ILE A CA  1 
ATOM   2806  C C   . ILE A 1 331 ? -0.866  16.189  19.622  1.00 55.72  ? 331 ILE A C   1 
ATOM   2807  O O   . ILE A 1 331 ? -2.073  15.905  19.635  1.00 59.48  ? 331 ILE A O   1 
ATOM   2808  C CB  . ILE A 1 331 ? 0.478   15.240  21.559  1.00 48.74  ? 331 ILE A CB  1 
ATOM   2809  C CG1 . ILE A 1 331 ? 1.588   14.248  21.928  1.00 46.12  ? 331 ILE A CG1 1 
ATOM   2810  C CG2 . ILE A 1 331 ? -0.778  14.964  22.380  1.00 42.55  ? 331 ILE A CG2 1 
ATOM   2811  C CD1 . ILE A 1 331 ? 1.351   12.825  21.465  1.00 44.36  ? 331 ILE A CD1 1 
ATOM   2812  N N   . GLY A 1 332 ? -0.425  17.382  19.213  1.00 52.86  ? 332 GLY A N   1 
ATOM   2813  C CA  . GLY A 1 332 ? -1.366  18.385  18.745  1.00 44.00  ? 332 GLY A CA  1 
ATOM   2814  C C   . GLY A 1 332 ? -2.104  17.939  17.500  1.00 50.72  ? 332 GLY A C   1 
ATOM   2815  O O   . GLY A 1 332 ? -3.317  18.122  17.379  1.00 53.04  ? 332 GLY A O   1 
ATOM   2816  N N   . ARG A 1 333 ? -1.383  17.338  16.555  1.00 49.34  ? 333 ARG A N   1 
ATOM   2817  C CA  . ARG A 1 333 ? -2.060  16.870  15.353  1.00 54.34  ? 333 ARG A CA  1 
ATOM   2818  C C   . ARG A 1 333 ? -2.929  15.661  15.650  1.00 51.78  ? 333 ARG A C   1 
ATOM   2819  O O   . ARG A 1 333 ? -3.962  15.463  14.996  1.00 52.26  ? 333 ARG A O   1 
ATOM   2820  C CB  . ARG A 1 333 ? -1.051  16.549  14.260  1.00 48.76  ? 333 ARG A CB  1 
ATOM   2821  C CG  . ARG A 1 333 ? 0.031   17.577  14.114  1.00 41.78  ? 333 ARG A CG  1 
ATOM   2822  C CD  . ARG A 1 333 ? 0.530   17.599  12.697  1.00 50.44  ? 333 ARG A CD  1 
ATOM   2823  N NE  . ARG A 1 333 ? 1.604   18.565  12.529  1.00 57.23  ? 333 ARG A NE  1 
ATOM   2824  C CZ  . ARG A 1 333 ? 1.773   19.313  11.449  1.00 54.94  ? 333 ARG A CZ  1 
ATOM   2825  N NH1 . ARG A 1 333 ? 0.957   19.224  10.412  1.00 61.77  ? 333 ARG A NH1 1 
ATOM   2826  N NH2 . ARG A 1 333 ? 2.781   20.177  11.412  1.00 62.01  ? 333 ARG A NH2 1 
ATOM   2827  N N   . LEU A 1 334 ? -2.544  14.856  16.641  1.00 47.07  ? 334 LEU A N   1 
ATOM   2828  C CA  . LEU A 1 334 ? -3.406  13.761  17.061  1.00 52.29  ? 334 LEU A CA  1 
ATOM   2829  C C   . LEU A 1 334 ? -4.669  14.290  17.727  1.00 57.22  ? 334 LEU A C   1 
ATOM   2830  O O   . LEU A 1 334 ? -5.758  13.734  17.534  1.00 58.39  ? 334 LEU A O   1 
ATOM   2831  C CB  . LEU A 1 334 ? -2.650  12.816  17.997  1.00 53.85  ? 334 LEU A CB  1 
ATOM   2832  C CG  . LEU A 1 334 ? -1.613  11.901  17.332  1.00 49.92  ? 334 LEU A CG  1 
ATOM   2833  C CD1 . LEU A 1 334 ? -1.199  10.814  18.286  1.00 48.09  ? 334 LEU A CD1 1 
ATOM   2834  C CD2 . LEU A 1 334 ? -2.126  11.282  16.045  1.00 47.50  ? 334 LEU A CD2 1 
ATOM   2835  N N   . LYS A 1 335 ? -4.555  15.374  18.501  1.00 55.23  ? 335 LYS A N   1 
ATOM   2836  C CA  . LYS A 1 335 ? -5.746  15.927  19.131  1.00 53.34  ? 335 LYS A CA  1 
ATOM   2837  C C   . LYS A 1 335 ? -6.707  16.486  18.091  1.00 52.87  ? 335 LYS A C   1 
ATOM   2838  O O   . LYS A 1 335 ? -7.921  16.485  18.311  1.00 60.83  ? 335 LYS A O   1 
ATOM   2839  C CB  . LYS A 1 335 ? -5.363  17.000  20.157  1.00 57.63  ? 335 LYS A CB  1 
ATOM   2840  C CG  . LYS A 1 335 ? -5.358  18.418  19.601  1.00 66.98  ? 335 LYS A CG  1 
ATOM   2841  C CD  . LYS A 1 335 ? -4.902  19.477  20.610  1.00 72.40  ? 335 LYS A CD  1 
ATOM   2842  C CE  . LYS A 1 335 ? -6.072  20.341  21.096  1.00 77.72  ? 335 LYS A CE  1 
ATOM   2843  N NZ  . LYS A 1 335 ? -5.659  21.604  21.792  1.00 59.06  ? 335 LYS A NZ  1 
ATOM   2844  N N   . LYS A 1 336 ? -6.190  16.933  16.944  1.00 53.62  ? 336 LYS A N   1 
ATOM   2845  C CA  . LYS A 1 336 ? -7.059  17.456  15.895  1.00 57.58  ? 336 LYS A CA  1 
ATOM   2846  C C   . LYS A 1 336 ? -7.732  16.334  15.119  1.00 59.44  ? 336 LYS A C   1 
ATOM   2847  O O   . LYS A 1 336 ? -8.882  16.480  14.687  1.00 61.82  ? 336 LYS A O   1 
ATOM   2848  C CB  . LYS A 1 336 ? -6.263  18.353  14.946  1.00 58.61  ? 336 LYS A CB  1 
ATOM   2849  C CG  . LYS A 1 336 ? -7.083  19.475  14.327  1.00 65.52  ? 336 LYS A CG  1 
ATOM   2850  C CD  . LYS A 1 336 ? -6.266  20.305  13.343  1.00 68.53  ? 336 LYS A CD  1 
ATOM   2851  C CE  . LYS A 1 336 ? -4.785  20.266  13.649  1.00 59.35  ? 336 LYS A CE  1 
ATOM   2852  N NZ  . LYS A 1 336 ? -4.095  21.325  12.875  1.00 64.09  ? 336 LYS A NZ  1 
ATOM   2853  N N   . ILE A 1 337 ? -7.033  15.214  14.924  1.00 50.82  ? 337 ILE A N   1 
ATOM   2854  C CA  . ILE A 1 337 ? -7.662  14.045  14.318  1.00 49.46  ? 337 ILE A CA  1 
ATOM   2855  C C   . ILE A 1 337 ? -8.805  13.543  15.195  1.00 51.16  ? 337 ILE A C   1 
ATOM   2856  O O   . ILE A 1 337 ? -9.883  13.195  14.699  1.00 55.71  ? 337 ILE A O   1 
ATOM   2857  C CB  . ILE A 1 337 ? -6.607  12.954  14.073  1.00 54.31  ? 337 ILE A CB  1 
ATOM   2858  C CG1 . ILE A 1 337 ? -5.813  13.272  12.810  1.00 52.36  ? 337 ILE A CG1 1 
ATOM   2859  C CG2 . ILE A 1 337 ? -7.272  11.613  13.940  1.00 57.04  ? 337 ILE A CG2 1 
ATOM   2860  C CD1 . ILE A 1 337 ? -4.529  12.498  12.694  1.00 50.45  ? 337 ILE A CD1 1 
ATOM   2861  N N   . HIS A 1 338 ? -8.591  13.527  16.513  1.00 52.52  ? 338 HIS A N   1 
ATOM   2862  C CA  . HIS A 1 338 ? -9.617  13.083  17.458  1.00 58.46  ? 338 HIS A CA  1 
ATOM   2863  C C   . HIS A 1 338 ? -10.912 13.876  17.309  1.00 57.39  ? 338 HIS A C   1 
ATOM   2864  O O   . HIS A 1 338 ? -12.008 13.304  17.339  1.00 60.07  ? 338 HIS A O   1 
ATOM   2865  C CB  . HIS A 1 338 ? -9.067  13.208  18.880  1.00 60.64  ? 338 HIS A CB  1 
ATOM   2866  C CG  . HIS A 1 338 ? -9.848  12.458  19.913  1.00 52.37  ? 338 HIS A CG  1 
ATOM   2867  N ND1 . HIS A 1 338 ? -10.875 13.032  20.630  1.00 62.55  ? 338 HIS A ND1 1 
ATOM   2868  C CD2 . HIS A 1 338 ? -9.737  11.187  20.365  1.00 52.63  ? 338 HIS A CD2 1 
ATOM   2869  C CE1 . HIS A 1 338 ? -11.366 12.146  21.478  1.00 65.75  ? 338 HIS A CE1 1 
ATOM   2870  N NE2 . HIS A 1 338 ? -10.694 11.018  21.336  1.00 61.76  ? 338 HIS A NE2 1 
ATOM   2871  N N   . GLU A 1 339 ? -10.805 15.197  17.153  1.00 57.10  ? 339 GLU A N   1 
ATOM   2872  C CA  . GLU A 1 339 ? -11.968 16.059  16.981  1.00 57.87  ? 339 GLU A CA  1 
ATOM   2873  C C   . GLU A 1 339 ? -12.442 16.133  15.535  1.00 59.75  ? 339 GLU A C   1 
ATOM   2874  O O   . GLU A 1 339 ? -13.563 16.594  15.290  1.00 66.48  ? 339 GLU A O   1 
ATOM   2875  C CB  . GLU A 1 339 ? -11.648 17.467  17.489  1.00 62.47  ? 339 GLU A CB  1 
ATOM   2876  C CG  . GLU A 1 339 ? -11.386 17.525  18.990  1.00 77.48  ? 339 GLU A CG  1 
ATOM   2877  C CD  . GLU A 1 339 ? -10.224 18.438  19.354  1.00 81.25  ? 339 GLU A CD  1 
ATOM   2878  O OE1 . GLU A 1 339 ? -9.814  19.262  18.507  1.00 82.33  ? 339 GLU A OE1 1 
ATOM   2879  O OE2 . GLU A 1 339 ? -9.702  18.311  20.482  1.00 79.48  ? 339 GLU A OE2 1 
ATOM   2880  N N   . SER A 1 340 ? -11.621 15.698  14.575  1.00 57.30  ? 340 SER A N   1 
ATOM   2881  C CA  . SER A 1 340 ? -12.028 15.748  13.175  1.00 55.49  ? 340 SER A CA  1 
ATOM   2882  C C   . SER A 1 340 ? -13.089 14.704  12.858  1.00 50.31  ? 340 SER A C   1 
ATOM   2883  O O   . SER A 1 340 ? -13.924 14.922  11.975  1.00 51.11  ? 340 SER A O   1 
ATOM   2884  C CB  . SER A 1 340 ? -10.798 15.574  12.273  1.00 55.69  ? 340 SER A CB  1 
ATOM   2885  O OG  . SER A 1 340 ? -10.802 14.333  11.576  1.00 55.34  ? 340 SER A OG  1 
ATOM   2886  N N   . VAL A 1 341 ? -13.086 13.582  13.563  1.00 52.63  ? 341 VAL A N   1 
ATOM   2887  C CA  . VAL A 1 341 ? -13.966 12.472  13.237  1.00 51.95  ? 341 VAL A CA  1 
ATOM   2888  C C   . VAL A 1 341 ? -14.933 12.245  14.388  1.00 60.24  ? 341 VAL A C   1 
ATOM   2889  O O   . VAL A 1 341 ? -14.642 12.549  15.552  1.00 54.22  ? 341 VAL A O   1 
ATOM   2890  C CB  . VAL A 1 341 ? -13.175 11.183  12.910  1.00 53.93  ? 341 VAL A CB  1 
ATOM   2891  C CG1 . VAL A 1 341 ? -12.225 11.428  11.753  1.00 53.67  ? 341 VAL A CG1 1 
ATOM   2892  C CG2 . VAL A 1 341 ? -12.408 10.674  14.120  1.00 48.23  ? 341 VAL A CG2 1 
ATOM   2893  N N   . ASP A 1 342 ? -16.107 11.716  14.043  1.00 67.61  ? 342 ASP A N   1 
ATOM   2894  C CA  . ASP A 1 342 ? -17.133 11.364  15.012  1.00 60.81  ? 342 ASP A CA  1 
ATOM   2895  C C   . ASP A 1 342 ? -17.127 9.879   15.351  1.00 64.90  ? 342 ASP A C   1 
ATOM   2896  O O   . ASP A 1 342 ? -18.091 9.384   15.944  1.00 72.60  ? 342 ASP A O   1 
ATOM   2897  C CB  . ASP A 1 342 ? -18.506 11.781  14.498  1.00 56.20  ? 342 ASP A CB  1 
ATOM   2898  C CG  . ASP A 1 342 ? -18.729 13.268  14.608  1.00 73.05  ? 342 ASP A CG  1 
ATOM   2899  O OD1 . ASP A 1 342 ? -18.117 13.882  15.512  1.00 81.23  ? 342 ASP A OD1 1 
ATOM   2900  O OD2 . ASP A 1 342 ? -19.524 13.812  13.810  1.00 71.17  ? 342 ASP A OD2 1 
ATOM   2901  N N   . PHE A 1 343 ? -16.073 9.159   14.977  1.00 65.64  ? 343 PHE A N   1 
ATOM   2902  C CA  . PHE A 1 343 ? -15.857 7.775   15.383  1.00 59.85  ? 343 PHE A CA  1 
ATOM   2903  C C   . PHE A 1 343 ? -14.583 7.696   16.217  1.00 50.18  ? 343 PHE A C   1 
ATOM   2904  O O   . PHE A 1 343 ? -14.001 8.715   16.588  1.00 55.78  ? 343 PHE A O   1 
ATOM   2905  C CB  . PHE A 1 343 ? -15.817 6.845   14.161  1.00 50.36  ? 343 PHE A CB  1 
ATOM   2906  C CG  . PHE A 1 343 ? -14.856 7.271   13.086  1.00 52.49  ? 343 PHE A CG  1 
ATOM   2907  C CD1 . PHE A 1 343 ? -13.496 7.029   13.209  1.00 55.41  ? 343 PHE A CD1 1 
ATOM   2908  C CD2 . PHE A 1 343 ? -15.316 7.908   11.942  1.00 52.01  ? 343 PHE A CD2 1 
ATOM   2909  C CE1 . PHE A 1 343 ? -12.614 7.420   12.215  1.00 56.61  ? 343 PHE A CE1 1 
ATOM   2910  C CE2 . PHE A 1 343 ? -14.438 8.300   10.945  1.00 52.06  ? 343 PHE A CE2 1 
ATOM   2911  C CZ  . PHE A 1 343 ? -13.088 8.058   11.084  1.00 53.59  ? 343 PHE A CZ  1 
ATOM   2912  N N   . GLN A 1 344 ? -14.155 6.470   16.537  1.00 46.88  ? 344 GLN A N   1 
ATOM   2913  C CA  . GLN A 1 344 ? -12.884 6.298   17.235  1.00 50.02  ? 344 GLN A CA  1 
ATOM   2914  C C   . GLN A 1 344 ? -11.798 5.993   16.203  1.00 49.95  ? 344 GLN A C   1 
ATOM   2915  O O   . GLN A 1 344 ? -11.735 4.873   15.681  1.00 51.25  ? 344 GLN A O   1 
ATOM   2916  C CB  . GLN A 1 344 ? -12.996 5.195   18.291  1.00 55.47  ? 344 GLN A CB  1 
ATOM   2917  C CG  . GLN A 1 344 ? -13.287 5.731   19.703  1.00 54.61  ? 344 GLN A CG  1 
ATOM   2918  C CD  . GLN A 1 344 ? -13.316 4.644   20.758  1.00 59.26  ? 344 GLN A CD  1 
ATOM   2919  O OE1 . GLN A 1 344 ? -13.512 3.472   20.448  1.00 55.82  ? 344 GLN A OE1 1 
ATOM   2920  N NE2 . GLN A 1 344 ? -13.117 5.029   22.015  1.00 59.63  ? 344 GLN A NE2 1 
ATOM   2921  N N   . PRO A 1 345 ? -10.935 6.958   15.880  1.00 54.19  ? 345 PRO A N   1 
ATOM   2922  C CA  . PRO A 1 345 ? -10.033 6.805   14.729  1.00 52.18  ? 345 PRO A CA  1 
ATOM   2923  C C   . PRO A 1 345 ? -8.827  5.916   14.997  1.00 49.49  ? 345 PRO A C   1 
ATOM   2924  O O   . PRO A 1 345 ? -8.310  5.836   16.114  1.00 45.00  ? 345 PRO A O   1 
ATOM   2925  C CB  . PRO A 1 345 ? -9.584  8.246   14.456  1.00 51.37  ? 345 PRO A CB  1 
ATOM   2926  C CG  . PRO A 1 345 ? -9.578  8.863   15.824  1.00 50.46  ? 345 PRO A CG  1 
ATOM   2927  C CD  . PRO A 1 345 ? -10.797 8.286   16.510  1.00 50.02  ? 345 PRO A CD  1 
ATOM   2928  N N   . VAL A 1 346 ? -8.380  5.245   13.937  1.00 48.89  ? 346 VAL A N   1 
ATOM   2929  C CA  . VAL A 1 346 ? -7.144  4.467   13.944  1.00 55.30  ? 346 VAL A CA  1 
ATOM   2930  C C   . VAL A 1 346 ? -6.118  5.230   13.115  1.00 51.11  ? 346 VAL A C   1 
ATOM   2931  O O   . VAL A 1 346 ? -6.360  5.530   11.939  1.00 55.87  ? 346 VAL A O   1 
ATOM   2932  C CB  . VAL A 1 346 ? -7.353  3.044   13.397  1.00 58.00  ? 346 VAL A CB  1 
ATOM   2933  C CG1 . VAL A 1 346 ? -8.077  3.060   12.047  1.00 52.23  ? 346 VAL A CG1 1 
ATOM   2934  C CG2 . VAL A 1 346 ? -6.025  2.337   13.271  1.00 45.14  ? 346 VAL A CG2 1 
ATOM   2935  N N   . VAL A 1 347 ? -4.977  5.553   13.717  1.00 47.04  ? 347 VAL A N   1 
ATOM   2936  C CA  . VAL A 1 347 ? -3.948  6.348   13.049  1.00 53.13  ? 347 VAL A CA  1 
ATOM   2937  C C   . VAL A 1 347 ? -2.711  5.484   12.847  1.00 38.81  ? 347 VAL A C   1 
ATOM   2938  O O   . VAL A 1 347 ? -1.982  5.197   13.805  1.00 43.03  ? 347 VAL A O   1 
ATOM   2939  C CB  . VAL A 1 347 ? -3.603  7.617   13.836  1.00 52.22  ? 347 VAL A CB  1 
ATOM   2940  C CG1 . VAL A 1 347 ? -2.528  8.395   13.097  1.00 43.09  ? 347 VAL A CG1 1 
ATOM   2941  C CG2 . VAL A 1 347 ? -4.854  8.472   14.057  1.00 48.95  ? 347 VAL A CG2 1 
ATOM   2942  N N   . PHE A 1 348 ? -2.451  5.101   11.598  1.00 38.92  ? 348 PHE A N   1 
ATOM   2943  C CA  . PHE A 1 348 ? -1.307  4.262   11.251  1.00 43.90  ? 348 PHE A CA  1 
ATOM   2944  C C   . PHE A 1 348 ? -0.119  5.137   10.879  1.00 45.69  ? 348 PHE A C   1 
ATOM   2945  O O   . PHE A 1 348 ? -0.210  5.960   9.960   1.00 48.68  ? 348 PHE A O   1 
ATOM   2946  C CB  . PHE A 1 348 ? -1.647  3.327   10.092  1.00 50.95  ? 348 PHE A CB  1 
ATOM   2947  C CG  . PHE A 1 348 ? -1.977  1.921   10.519  1.00 52.06  ? 348 PHE A CG  1 
ATOM   2948  C CD1 . PHE A 1 348 ? -3.139  1.661   11.232  1.00 39.17  ? 348 PHE A CD1 1 
ATOM   2949  C CD2 . PHE A 1 348 ? -1.148  0.856   10.181  1.00 40.53  ? 348 PHE A CD2 1 
ATOM   2950  C CE1 . PHE A 1 348 ? -3.457  0.382   11.623  1.00 36.25  ? 348 PHE A CE1 1 
ATOM   2951  C CE2 . PHE A 1 348 ? -1.471  -0.441  10.572  1.00 41.69  ? 348 PHE A CE2 1 
ATOM   2952  C CZ  . PHE A 1 348 ? -2.629  -0.671  11.294  1.00 37.77  ? 348 PHE A CZ  1 
ATOM   2953  N N   . VAL A 1 349 ? 0.994   4.948   11.583  1.00 44.51  ? 349 VAL A N   1 
ATOM   2954  C CA  . VAL A 1 349 ? 2.226   5.693   11.349  1.00 46.13  ? 349 VAL A CA  1 
ATOM   2955  C C   . VAL A 1 349 ? 3.278   4.701   10.866  1.00 47.54  ? 349 VAL A C   1 
ATOM   2956  O O   . VAL A 1 349 ? 3.829   3.927   11.663  1.00 45.73  ? 349 VAL A O   1 
ATOM   2957  C CB  . VAL A 1 349 ? 2.695   6.425   12.613  1.00 39.41  ? 349 VAL A CB  1 
ATOM   2958  C CG1 . VAL A 1 349 ? 4.048   7.068   12.379  1.00 40.26  ? 349 VAL A CG1 1 
ATOM   2959  C CG2 . VAL A 1 349 ? 1.670   7.460   13.031  1.00 37.00  ? 349 VAL A CG2 1 
ATOM   2960  N N   . VAL A 1 350 ? 3.565   4.717   9.567   1.00 42.27  ? 350 VAL A N   1 
ATOM   2961  C CA  . VAL A 1 350 ? 4.512   3.778   8.975   1.00 50.18  ? 350 VAL A CA  1 
ATOM   2962  C C   . VAL A 1 350 ? 5.607   4.551   8.251   1.00 49.16  ? 350 VAL A C   1 
ATOM   2963  O O   . VAL A 1 350 ? 5.315   5.420   7.420   1.00 47.88  ? 350 VAL A O   1 
ATOM   2964  C CB  . VAL A 1 350 ? 3.825   2.802   8.008   1.00 49.82  ? 350 VAL A CB  1 
ATOM   2965  C CG1 . VAL A 1 350 ? 4.791   1.693   7.634   1.00 45.94  ? 350 VAL A CG1 1 
ATOM   2966  C CG2 . VAL A 1 350 ? 2.560   2.238   8.635   1.00 41.51  ? 350 VAL A CG2 1 
ATOM   2967  N N   . LEU A 1 351 ? 6.862   4.215   8.548   1.00 49.28  ? 351 LEU A N   1 
ATOM   2968  C CA  . LEU A 1 351 ? 8.014   4.821   7.893   1.00 47.28  ? 351 LEU A CA  1 
ATOM   2969  C C   . LEU A 1 351 ? 9.215   3.913   8.109   1.00 44.63  ? 351 LEU A C   1 
ATOM   2970  O O   . LEU A 1 351 ? 9.170   2.976   8.910   1.00 44.39  ? 351 LEU A O   1 
ATOM   2971  C CB  . LEU A 1 351 ? 8.292   6.230   8.430   1.00 45.21  ? 351 LEU A CB  1 
ATOM   2972  C CG  . LEU A 1 351 ? 8.538   6.377   9.939   1.00 51.29  ? 351 LEU A CG  1 
ATOM   2973  C CD1 . LEU A 1 351 ? 9.406   7.597   10.198  1.00 54.43  ? 351 LEU A CD1 1 
ATOM   2974  C CD2 . LEU A 1 351 ? 7.250   6.466   10.762  1.00 37.25  ? 351 LEU A CD2 1 
ATOM   2975  N N   . ASP A 1 352 ? 10.299  4.201   7.387   1.00 51.31  ? 352 ASP A N   1 
ATOM   2976  C CA  . ASP A 1 352 ? 11.552  3.494   7.641   1.00 56.25  ? 352 ASP A CA  1 
ATOM   2977  C C   . ASP A 1 352 ? 11.964  3.702   9.089   1.00 52.64  ? 352 ASP A C   1 
ATOM   2978  O O   . ASP A 1 352 ? 11.926  4.826   9.598   1.00 51.73  ? 352 ASP A O   1 
ATOM   2979  C CB  . ASP A 1 352 ? 12.658  3.982   6.708   1.00 48.40  ? 352 ASP A CB  1 
ATOM   2980  C CG  . ASP A 1 352 ? 12.265  3.898   5.259   1.00 52.60  ? 352 ASP A CG  1 
ATOM   2981  O OD1 . ASP A 1 352 ? 11.208  3.299   4.976   1.00 56.64  ? 352 ASP A OD1 1 
ATOM   2982  O OD2 . ASP A 1 352 ? 13.012  4.429   4.405   1.00 56.17  ? 352 ASP A OD2 1 
ATOM   2983  N N   . GLY A 1 353 ? 12.335  2.618   9.760   1.00 46.47  ? 353 GLY A N   1 
ATOM   2984  C CA  . GLY A 1 353 ? 12.639  2.696   11.170  1.00 48.26  ? 353 GLY A CA  1 
ATOM   2985  C C   . GLY A 1 353 ? 14.087  2.926   11.548  1.00 52.90  ? 353 GLY A C   1 
ATOM   2986  O O   . GLY A 1 353 ? 14.410  2.856   12.739  1.00 54.33  ? 353 GLY A O   1 
ATOM   2987  N N   . GLU A 1 354 ? 14.977  3.209   10.597  1.00 46.13  ? 354 GLU A N   1 
ATOM   2988  C CA  . GLU A 1 354 ? 16.386  3.327   10.948  1.00 50.52  ? 354 GLU A CA  1 
ATOM   2989  C C   . GLU A 1 354 ? 17.047  4.566   10.348  1.00 54.42  ? 354 GLU A C   1 
ATOM   2990  O O   . GLU A 1 354 ? 18.036  5.069   10.892  1.00 59.74  ? 354 GLU A O   1 
ATOM   2991  C CB  . GLU A 1 354 ? 17.136  2.057   10.518  1.00 52.51  ? 354 GLU A CB  1 
ATOM   2992  C CG  . GLU A 1 354 ? 17.332  1.893   9.004   1.00 55.99  ? 354 GLU A CG  1 
ATOM   2993  C CD  . GLU A 1 354 ? 16.186  1.150   8.309   1.00 60.04  ? 354 GLU A CD  1 
ATOM   2994  O OE1 . GLU A 1 354 ? 15.159  1.793   7.995   1.00 54.23  ? 354 GLU A OE1 1 
ATOM   2995  O OE2 . GLU A 1 354 ? 16.328  -0.066  8.039   1.00 53.18  ? 354 GLU A OE2 1 
ATOM   2996  N N   . ASN A 1 355 ? 16.510  5.082   9.244   1.00 56.80  ? 355 ASN A N   1 
ATOM   2997  C CA  . ASN A 1 355 ? 17.262  6.060   8.462   1.00 50.66  ? 355 ASN A CA  1 
ATOM   2998  C C   . ASN A 1 355 ? 17.083  7.485   8.953   1.00 50.20  ? 355 ASN A C   1 
ATOM   2999  O O   . ASN A 1 355 ? 17.909  8.349   8.639   1.00 54.81  ? 355 ASN A O   1 
ATOM   3000  C CB  . ASN A 1 355 ? 16.861  5.970   6.996   1.00 46.10  ? 355 ASN A CB  1 
ATOM   3001  C CG  . ASN A 1 355 ? 17.040  4.580   6.441   1.00 48.89  ? 355 ASN A CG  1 
ATOM   3002  O OD1 . ASN A 1 355 ? 18.059  3.933   6.675   1.00 54.19  ? 355 ASN A OD1 1 
ATOM   3003  N ND2 . ASN A 1 355 ? 16.036  4.097   5.723   1.00 50.52  ? 355 ASN A ND2 1 
ATOM   3004  N N   . CYS A 1 356 ? 16.023  7.764   9.702   1.00 45.14  ? 356 CYS A N   1 
ATOM   3005  C CA  . CYS A 1 356 ? 15.798  9.149   10.085  1.00 51.16  ? 356 CYS A CA  1 
ATOM   3006  C C   . CYS A 1 356 ? 16.615  9.533   11.306  1.00 53.01  ? 356 CYS A C   1 
ATOM   3007  O O   . CYS A 1 356 ? 16.965  10.707  11.466  1.00 59.81  ? 356 CYS A O   1 
ATOM   3008  C CB  . CYS A 1 356 ? 14.308  9.410   10.342  1.00 49.99  ? 356 CYS A CB  1 
ATOM   3009  S SG  . CYS A 1 356 ? 13.522  8.320   11.535  1.00 63.85  ? 356 CYS A SG  1 
ATOM   3010  N N   . TRP A 1 357 ? 16.968  8.557   12.146  1.00 48.76  ? 357 TRP A N   1 
ATOM   3011  C CA  . TRP A 1 357 ? 17.496  8.878   13.467  1.00 49.56  ? 357 TRP A CA  1 
ATOM   3012  C C   . TRP A 1 357 ? 18.883  9.499   13.408  1.00 51.15  ? 357 TRP A C   1 
ATOM   3013  O O   . TRP A 1 357 ? 19.235  10.295  14.288  1.00 52.59  ? 357 TRP A O   1 
ATOM   3014  C CB  . TRP A 1 357 ? 17.503  7.627   14.339  1.00 49.30  ? 357 TRP A CB  1 
ATOM   3015  C CG  . TRP A 1 357 ? 16.178  6.936   14.337  1.00 43.82  ? 357 TRP A CG  1 
ATOM   3016  C CD1 . TRP A 1 357 ? 15.942  5.624   14.060  1.00 49.23  ? 357 TRP A CD1 1 
ATOM   3017  C CD2 . TRP A 1 357 ? 14.903  7.520   14.634  1.00 41.91  ? 357 TRP A CD2 1 
ATOM   3018  N NE1 . TRP A 1 357 ? 14.599  5.352   14.159  1.00 45.85  ? 357 TRP A NE1 1 
ATOM   3019  C CE2 . TRP A 1 357 ? 13.940  6.500   14.512  1.00 46.73  ? 357 TRP A CE2 1 
ATOM   3020  C CE3 . TRP A 1 357 ? 14.481  8.806   14.991  1.00 48.60  ? 357 TRP A CE3 1 
ATOM   3021  C CZ2 . TRP A 1 357 ? 12.580  6.724   14.733  1.00 51.01  ? 357 TRP A CZ2 1 
ATOM   3022  C CZ3 . TRP A 1 357 ? 13.124  9.029   15.209  1.00 47.73  ? 357 TRP A CZ3 1 
ATOM   3023  C CH2 . TRP A 1 357 ? 12.193  7.993   15.079  1.00 45.32  ? 357 TRP A CH2 1 
ATOM   3024  N N   . GLU A 1 358 ? 19.674  9.168   12.381  1.00 51.70  ? 358 GLU A N   1 
ATOM   3025  C CA  . GLU A 1 358 ? 21.034  9.693   12.305  1.00 52.09  ? 358 GLU A CA  1 
ATOM   3026  C C   . GLU A 1 358 ? 21.044  11.208  12.163  1.00 51.60  ? 358 GLU A C   1 
ATOM   3027  O O   . GLU A 1 358 ? 22.000  11.864  12.591  1.00 49.10  ? 358 GLU A O   1 
ATOM   3028  C CB  . GLU A 1 358 ? 21.795  9.047   11.142  1.00 58.24  ? 358 GLU A CB  1 
ATOM   3029  C CG  . GLU A 1 358 ? 21.114  9.189   9.781   1.00 60.36  ? 358 GLU A CG  1 
ATOM   3030  C CD  . GLU A 1 358 ? 21.623  8.179   8.759   1.00 61.43  ? 358 GLU A CD  1 
ATOM   3031  O OE1 . GLU A 1 358 ? 22.823  7.843   8.794   1.00 57.63  ? 358 GLU A OE1 1 
ATOM   3032  O OE2 . GLU A 1 358 ? 20.821  7.708   7.926   1.00 70.63  ? 358 GLU A OE2 1 
ATOM   3033  N N   . TYR A 1 359 ? 19.994  11.781  11.572  1.00 52.24  ? 359 TYR A N   1 
ATOM   3034  C CA  . TYR A 1 359 ? 19.915  13.227  11.412  1.00 51.53  ? 359 TYR A CA  1 
ATOM   3035  C C   . TYR A 1 359 ? 19.341  13.918  12.640  1.00 47.37  ? 359 TYR A C   1 
ATOM   3036  O O   . TYR A 1 359 ? 19.346  15.154  12.696  1.00 46.52  ? 359 TYR A O   1 
ATOM   3037  C CB  . TYR A 1 359 ? 19.087  13.567  10.172  1.00 46.43  ? 359 TYR A CB  1 
ATOM   3038  C CG  . TYR A 1 359 ? 19.622  12.908  8.923   1.00 58.28  ? 359 TYR A CG  1 
ATOM   3039  C CD1 . TYR A 1 359 ? 20.696  13.453  8.224   1.00 51.52  ? 359 TYR A CD1 1 
ATOM   3040  C CD2 . TYR A 1 359 ? 19.072  11.721  8.457   1.00 65.60  ? 359 TYR A CD2 1 
ATOM   3041  C CE1 . TYR A 1 359 ? 21.189  12.842  7.083   1.00 56.20  ? 359 TYR A CE1 1 
ATOM   3042  C CE2 . TYR A 1 359 ? 19.560  11.101  7.321   1.00 60.71  ? 359 TYR A CE2 1 
ATOM   3043  C CZ  . TYR A 1 359 ? 20.616  11.662  6.639   1.00 64.86  ? 359 TYR A CZ  1 
ATOM   3044  O OH  . TYR A 1 359 ? 21.083  11.029  5.512   1.00 73.80  ? 359 TYR A OH  1 
ATOM   3045  N N   . TYR A 1 360 ? 18.865  13.151  13.617  1.00 44.72  ? 360 TYR A N   1 
ATOM   3046  C CA  . TYR A 1 360 ? 18.382  13.685  14.880  1.00 46.56  ? 360 TYR A CA  1 
ATOM   3047  C C   . TYR A 1 360 ? 19.532  13.850  15.861  1.00 50.36  ? 360 TYR A C   1 
ATOM   3048  O O   . TYR A 1 360 ? 20.557  13.169  15.778  1.00 47.20  ? 360 TYR A O   1 
ATOM   3049  C CB  . TYR A 1 360 ? 17.355  12.761  15.517  1.00 46.25  ? 360 TYR A CB  1 
ATOM   3050  C CG  . TYR A 1 360 ? 15.936  12.839  15.010  1.00 47.61  ? 360 TYR A CG  1 
ATOM   3051  C CD1 . TYR A 1 360 ? 15.600  12.360  13.752  1.00 41.51  ? 360 TYR A CD1 1 
ATOM   3052  C CD2 . TYR A 1 360 ? 14.914  13.286  15.832  1.00 49.71  ? 360 TYR A CD2 1 
ATOM   3053  C CE1 . TYR A 1 360 ? 14.310  12.387  13.303  1.00 45.54  ? 360 TYR A CE1 1 
ATOM   3054  C CE2 . TYR A 1 360 ? 13.608  13.314  15.393  1.00 44.59  ? 360 TYR A CE2 1 
ATOM   3055  C CZ  . TYR A 1 360 ? 13.311  12.863  14.126  1.00 48.86  ? 360 TYR A CZ  1 
ATOM   3056  O OH  . TYR A 1 360 ? 12.010  12.887  13.680  1.00 44.87  ? 360 TYR A OH  1 
ATOM   3057  N N   . GLU A 1 361 ? 19.327  14.736  16.829  1.00 51.74  ? 361 GLU A N   1 
ATOM   3058  C CA  . GLU A 1 361 ? 20.287  14.891  17.910  1.00 52.31  ? 361 GLU A CA  1 
ATOM   3059  C C   . GLU A 1 361 ? 20.309  13.636  18.772  1.00 56.09  ? 361 GLU A C   1 
ATOM   3060  O O   . GLU A 1 361 ? 19.255  13.102  19.134  1.00 56.90  ? 361 GLU A O   1 
ATOM   3061  C CB  . GLU A 1 361 ? 19.938  16.109  18.757  1.00 56.04  ? 361 GLU A CB  1 
ATOM   3062  C CG  . GLU A 1 361 ? 20.996  16.477  19.763  1.00 68.88  ? 361 GLU A CG  1 
ATOM   3063  C CD  . GLU A 1 361 ? 22.207  17.116  19.121  1.00 84.70  ? 361 GLU A CD  1 
ATOM   3064  O OE1 . GLU A 1 361 ? 23.336  16.598  19.299  1.00 75.14  ? 361 GLU A OE1 1 
ATOM   3065  O OE2 . GLU A 1 361 ? 22.018  18.128  18.416  1.00 88.66  ? 361 GLU A OE2 1 
ATOM   3066  N N   . GLU A 1 362 ? 21.519  13.167  19.086  1.00 56.62  ? 362 GLU A N   1 
ATOM   3067  C CA  . GLU A 1 362 ? 21.729  11.969  19.902  1.00 53.15  ? 362 GLU A CA  1 
ATOM   3068  C C   . GLU A 1 362 ? 20.960  10.775  19.347  1.00 51.02  ? 362 GLU A C   1 
ATOM   3069  O O   . GLU A 1 362 ? 20.349  10.002  20.089  1.00 54.29  ? 362 GLU A O   1 
ATOM   3070  C CB  . GLU A 1 362 ? 21.361  12.231  21.362  1.00 62.05  ? 362 GLU A CB  1 
ATOM   3071  C CG  . GLU A 1 362 ? 22.307  13.206  22.045  1.00 72.39  ? 362 GLU A CG  1 
ATOM   3072  C CD  . GLU A 1 362 ? 21.844  13.631  23.426  1.00 91.71  ? 362 GLU A CD  1 
ATOM   3073  O OE1 . GLU A 1 362 ? 21.624  12.752  24.289  1.00 94.22  ? 362 GLU A OE1 1 
ATOM   3074  O OE2 . GLU A 1 362 ? 21.703  14.852  23.647  1.00 108.64 ? 362 GLU A OE2 1 
ATOM   3075  N N   . ASN A 1 363 ? 20.984  10.635  18.020  1.00 53.07  ? 363 ASN A N   1 
ATOM   3076  C CA  . ASN A 1 363 ? 20.315  9.535   17.318  1.00 58.13  ? 363 ASN A CA  1 
ATOM   3077  C C   . ASN A 1 363 ? 18.820  9.452   17.637  1.00 53.30  ? 363 ASN A C   1 
ATOM   3078  O O   . ASN A 1 363 ? 18.226  8.371   17.620  1.00 52.78  ? 363 ASN A O   1 
ATOM   3079  C CB  . ASN A 1 363 ? 20.999  8.195   17.608  1.00 50.94  ? 363 ASN A CB  1 
ATOM   3080  C CG  . ASN A 1 363 ? 20.565  7.118   16.650  1.00 51.75  ? 363 ASN A CG  1 
ATOM   3081  O OD1 . ASN A 1 363 ? 20.551  7.325   15.438  1.00 55.64  ? 363 ASN A OD1 1 
ATOM   3082  N ND2 . ASN A 1 363 ? 20.200  5.962   17.186  1.00 50.27  ? 363 ASN A ND2 1 
ATOM   3083  N N   . GLY A 1 364 ? 18.186  10.583  17.927  1.00 49.78  ? 364 GLY A N   1 
ATOM   3084  C CA  . GLY A 1 364 ? 16.760  10.582  18.173  1.00 50.13  ? 364 GLY A CA  1 
ATOM   3085  C C   . GLY A 1 364 ? 16.313  9.957   19.473  1.00 48.39  ? 364 GLY A C   1 
ATOM   3086  O O   . GLY A 1 364 ? 15.103  9.830   19.686  1.00 49.75  ? 364 GLY A O   1 
ATOM   3087  N N   . ILE A 1 365 ? 17.236  9.560   20.353  1.00 49.48  ? 365 ILE A N   1 
ATOM   3088  C CA  . ILE A 1 365 ? 16.833  8.984   21.638  1.00 49.35  ? 365 ILE A CA  1 
ATOM   3089  C C   . ILE A 1 365 ? 15.977  9.952   22.453  1.00 51.74  ? 365 ILE A C   1 
ATOM   3090  O O   . ILE A 1 365 ? 14.936  9.527   22.979  1.00 50.69  ? 365 ILE A O   1 
ATOM   3091  C CB  . ILE A 1 365 ? 18.065  8.485   22.407  1.00 52.85  ? 365 ILE A CB  1 
ATOM   3092  C CG1 . ILE A 1 365 ? 18.602  7.191   21.772  1.00 49.41  ? 365 ILE A CG1 1 
ATOM   3093  C CG2 . ILE A 1 365 ? 17.723  8.286   23.891  1.00 50.52  ? 365 ILE A CG2 1 
ATOM   3094  C CD1 . ILE A 1 365 ? 20.128  7.096   21.661  1.00 46.31  ? 365 ILE A CD1 1 
ATOM   3095  N N   . PRO A 1 366 ? 16.328  11.243  22.587  1.00 55.51  ? 366 PRO A N   1 
ATOM   3096  C CA  . PRO A 1 366 ? 15.424  12.158  23.317  1.00 52.87  ? 366 PRO A CA  1 
ATOM   3097  C C   . PRO A 1 366 ? 14.029  12.235  22.723  1.00 47.97  ? 366 PRO A C   1 
ATOM   3098  O O   . PRO A 1 366 ? 13.050  12.055  23.457  1.00 53.26  ? 366 PRO A O   1 
ATOM   3099  C CB  . PRO A 1 366 ? 16.162  13.501  23.244  1.00 53.27  ? 366 PRO A CB  1 
ATOM   3100  C CG  . PRO A 1 366 ? 17.598  13.121  23.085  1.00 51.32  ? 366 PRO A CG  1 
ATOM   3101  C CD  . PRO A 1 366 ? 17.576  11.924  22.196  1.00 51.87  ? 366 PRO A CD  1 
ATOM   3102  N N   . PHE A 1 367 ? 13.906  12.494  21.416  1.00 41.66  ? 367 PHE A N   1 
ATOM   3103  C CA  . PHE A 1 367 ? 12.588  12.537  20.787  1.00 40.55  ? 367 PHE A CA  1 
ATOM   3104  C C   . PHE A 1 367 ? 11.789  11.274  21.086  1.00 47.38  ? 367 PHE A C   1 
ATOM   3105  O O   . PHE A 1 367 ? 10.633  11.345  21.520  1.00 49.73  ? 367 PHE A O   1 
ATOM   3106  C CB  . PHE A 1 367 ? 12.708  12.713  19.276  1.00 40.08  ? 367 PHE A CB  1 
ATOM   3107  C CG  . PHE A 1 367 ? 11.385  12.585  18.546  1.00 44.36  ? 367 PHE A CG  1 
ATOM   3108  C CD1 . PHE A 1 367 ? 10.380  13.522  18.737  1.00 41.47  ? 367 PHE A CD1 1 
ATOM   3109  C CD2 . PHE A 1 367 ? 11.138  11.516  17.697  1.00 44.27  ? 367 PHE A CD2 1 
ATOM   3110  C CE1 . PHE A 1 367 ? 9.168   13.410  18.080  1.00 45.37  ? 367 PHE A CE1 1 
ATOM   3111  C CE2 . PHE A 1 367 ? 9.922   11.396  17.034  1.00 40.77  ? 367 PHE A CE2 1 
ATOM   3112  C CZ  . PHE A 1 367 ? 8.936   12.343  17.226  1.00 44.61  ? 367 PHE A CZ  1 
ATOM   3113  N N   . LEU A 1 368 ? 12.395  10.103  20.864  1.00 39.32  ? 368 LEU A N   1 
ATOM   3114  C CA  . LEU A 1 368 ? 11.671  8.850   21.060  1.00 44.53  ? 368 LEU A CA  1 
ATOM   3115  C C   . LEU A 1 368 ? 11.309  8.636   22.524  1.00 47.95  ? 368 LEU A C   1 
ATOM   3116  O O   . LEU A 1 368 ? 10.217  8.143   22.834  1.00 47.88  ? 368 LEU A O   1 
ATOM   3117  C CB  . LEU A 1 368 ? 12.495  7.675   20.533  1.00 41.92  ? 368 LEU A CB  1 
ATOM   3118  C CG  . LEU A 1 368 ? 12.539  7.566   19.005  1.00 45.30  ? 368 LEU A CG  1 
ATOM   3119  C CD1 . LEU A 1 368 ? 13.419  6.411   18.568  1.00 47.79  ? 368 LEU A CD1 1 
ATOM   3120  C CD2 . LEU A 1 368 ? 11.146  7.407   18.423  1.00 45.22  ? 368 LEU A CD2 1 
ATOM   3121  N N   . GLU A 1 369 ? 12.207  9.007   23.440  1.00 48.76  ? 369 GLU A N   1 
ATOM   3122  C CA  . GLU A 1 369 ? 11.930  8.812   24.858  1.00 49.28  ? 369 GLU A CA  1 
ATOM   3123  C C   . GLU A 1 369 ? 10.853  9.758   25.372  1.00 50.10  ? 369 GLU A C   1 
ATOM   3124  O O   . GLU A 1 369 ? 10.119  9.397   26.298  1.00 42.41  ? 369 GLU A O   1 
ATOM   3125  C CB  . GLU A 1 369 ? 13.202  8.982   25.680  1.00 49.42  ? 369 GLU A CB  1 
ATOM   3126  C CG  . GLU A 1 369 ? 14.135  7.799   25.626  1.00 51.65  ? 369 GLU A CG  1 
ATOM   3127  C CD  . GLU A 1 369 ? 15.275  7.930   26.616  1.00 59.13  ? 369 GLU A CD  1 
ATOM   3128  O OE1 . GLU A 1 369 ? 15.553  9.066   27.061  1.00 63.82  ? 369 GLU A OE1 1 
ATOM   3129  O OE2 . GLU A 1 369 ? 15.886  6.895   26.955  1.00 53.28  ? 369 GLU A OE2 1 
ATOM   3130  N N   . LYS A 1 370 ? 10.758  10.974  24.815  1.00 48.75  ? 370 LYS A N   1 
ATOM   3131  C CA  . LYS A 1 370 ? 9.684   11.878  25.219  1.00 51.74  ? 370 LYS A CA  1 
ATOM   3132  C C   . LYS A 1 370 ? 8.369   11.513  24.547  1.00 51.80  ? 370 LYS A C   1 
ATOM   3133  O O   . LYS A 1 370 ? 7.304   11.647  25.161  1.00 50.07  ? 370 LYS A O   1 
ATOM   3134  C CB  . LYS A 1 370 ? 10.042  13.339  24.916  1.00 52.39  ? 370 LYS A CB  1 
ATOM   3135  C CG  . LYS A 1 370 ? 10.971  13.970  25.950  1.00 67.05  ? 370 LYS A CG  1 
ATOM   3136  C CD  . LYS A 1 370 ? 12.364  14.244  25.389  1.00 67.83  ? 370 LYS A CD  1 
ATOM   3137  C CE  . LYS A 1 370 ? 13.410  14.357  26.498  1.00 74.22  ? 370 LYS A CE  1 
ATOM   3138  N NZ  . LYS A 1 370 ? 13.725  13.013  27.089  1.00 70.37  ? 370 LYS A NZ  1 
ATOM   3139  N N   . LEU A 1 371 ? 8.424   11.037  23.303  1.00 51.05  ? 371 LEU A N   1 
ATOM   3140  C CA  . LEU A 1 371 ? 7.213   10.589  22.628  1.00 46.33  ? 371 LEU A CA  1 
ATOM   3141  C C   . LEU A 1 371 ? 6.619   9.367   23.312  1.00 49.08  ? 371 LEU A C   1 
ATOM   3142  O O   . LEU A 1 371 ? 5.400   9.281   23.495  1.00 51.80  ? 371 LEU A O   1 
ATOM   3143  C CB  . LEU A 1 371 ? 7.522   10.284  21.168  1.00 44.34  ? 371 LEU A CB  1 
ATOM   3144  C CG  . LEU A 1 371 ? 6.336   9.802   20.353  1.00 41.53  ? 371 LEU A CG  1 
ATOM   3145  C CD1 . LEU A 1 371 ? 5.269   10.875  20.371  1.00 52.27  ? 371 LEU A CD1 1 
ATOM   3146  C CD2 . LEU A 1 371 ? 6.776   9.472   18.937  1.00 40.70  ? 371 LEU A CD2 1 
ATOM   3147  N N   . TYR A 1 372 ? 7.465   8.416   23.709  1.00 45.84  ? 372 TYR A N   1 
ATOM   3148  C CA  . TYR A 1 372 ? 6.955   7.208   24.344  1.00 42.70  ? 372 TYR A CA  1 
ATOM   3149  C C   . TYR A 1 372 ? 6.490   7.477   25.762  1.00 48.35  ? 372 TYR A C   1 
ATOM   3150  O O   . TYR A 1 372 ? 5.527   6.854   26.221  1.00 53.84  ? 372 TYR A O   1 
ATOM   3151  C CB  . TYR A 1 372 ? 8.017   6.121   24.334  1.00 45.88  ? 372 TYR A CB  1 
ATOM   3152  C CG  . TYR A 1 372 ? 8.357   5.636   22.953  1.00 45.84  ? 372 TYR A CG  1 
ATOM   3153  C CD1 . TYR A 1 372 ? 7.526   5.909   21.870  1.00 46.55  ? 372 TYR A CD1 1 
ATOM   3154  C CD2 . TYR A 1 372 ? 9.514   4.913   22.725  1.00 46.95  ? 372 TYR A CD2 1 
ATOM   3155  C CE1 . TYR A 1 372 ? 7.842   5.464   20.597  1.00 46.94  ? 372 TYR A CE1 1 
ATOM   3156  C CE2 . TYR A 1 372 ? 9.837   4.467   21.463  1.00 53.92  ? 372 TYR A CE2 1 
ATOM   3157  C CZ  . TYR A 1 372 ? 9.004   4.741   20.400  1.00 48.29  ? 372 TYR A CZ  1 
ATOM   3158  O OH  . TYR A 1 372 ? 9.358   4.281   19.149  1.00 39.43  ? 372 TYR A OH  1 
ATOM   3159  N N   . SER A 1 373 ? 7.151   8.394   26.474  1.00 45.26  ? 373 SER A N   1 
ATOM   3160  C CA  . SER A 1 373 ? 6.673   8.725   27.812  1.00 56.14  ? 373 SER A CA  1 
ATOM   3161  C C   . SER A 1 373 ? 5.392   9.541   27.737  1.00 54.25  ? 373 SER A C   1 
ATOM   3162  O O   . SER A 1 373 ? 4.471   9.326   28.533  1.00 53.25  ? 373 SER A O   1 
ATOM   3163  C CB  . SER A 1 373 ? 7.740   9.474   28.608  1.00 49.04  ? 373 SER A CB  1 
ATOM   3164  O OG  . SER A 1 373 ? 8.472   10.349  27.777  1.00 64.49  ? 373 SER A OG  1 
ATOM   3165  N N   . THR A 1 374 ? 5.313   10.479  26.786  1.00 50.29  ? 374 THR A N   1 
ATOM   3166  C CA  . THR A 1 374 ? 4.080   11.237  26.602  1.00 52.92  ? 374 THR A CA  1 
ATOM   3167  C C   . THR A 1 374 ? 2.928   10.304  26.265  1.00 52.62  ? 374 THR A C   1 
ATOM   3168  O O   . THR A 1 374 ? 1.849   10.387  26.862  1.00 51.19  ? 374 THR A O   1 
ATOM   3169  C CB  . THR A 1 374 ? 4.241   12.289  25.499  1.00 51.26  ? 374 THR A CB  1 
ATOM   3170  O OG1 . THR A 1 374 ? 5.313   13.184  25.823  1.00 43.35  ? 374 THR A OG1 1 
ATOM   3171  C CG2 . THR A 1 374 ? 2.950   13.096  25.347  1.00 53.68  ? 374 THR A CG2 1 
ATOM   3172  N N   . LEU A 1 375 ? 3.152   9.393   25.312  1.00 54.04  ? 375 LEU A N   1 
ATOM   3173  C CA  . LEU A 1 375 ? 2.105   8.469   24.893  1.00 54.92  ? 375 LEU A CA  1 
ATOM   3174  C C   . LEU A 1 375 ? 1.696   7.535   26.022  1.00 53.37  ? 375 LEU A C   1 
ATOM   3175  O O   . LEU A 1 375 ? 0.557   7.051   26.047  1.00 58.65  ? 375 LEU A O   1 
ATOM   3176  C CB  . LEU A 1 375 ? 2.569   7.665   23.682  1.00 48.11  ? 375 LEU A CB  1 
ATOM   3177  C CG  . LEU A 1 375 ? 2.629   8.431   22.362  1.00 50.26  ? 375 LEU A CG  1 
ATOM   3178  C CD1 . LEU A 1 375 ? 3.414   7.625   21.342  1.00 49.93  ? 375 LEU A CD1 1 
ATOM   3179  C CD2 . LEU A 1 375 ? 1.230   8.761   21.852  1.00 59.97  ? 375 LEU A CD2 1 
ATOM   3180  N N   . GLU A 1 376 ? 2.606   7.273   26.961  1.00 56.28  ? 376 GLU A N   1 
ATOM   3181  C CA  . GLU A 1 376 ? 2.258   6.478   28.134  1.00 65.72  ? 376 GLU A CA  1 
ATOM   3182  C C   . GLU A 1 376 ? 1.198   7.172   28.990  1.00 64.30  ? 376 GLU A C   1 
ATOM   3183  O O   . GLU A 1 376 ? 0.251   6.525   29.453  1.00 71.45  ? 376 GLU A O   1 
ATOM   3184  C CB  . GLU A 1 376 ? 3.508   6.193   28.970  1.00 57.88  ? 376 GLU A CB  1 
ATOM   3185  C CG  . GLU A 1 376 ? 4.112   4.814   28.770  1.00 52.29  ? 376 GLU A CG  1 
ATOM   3186  C CD  . GLU A 1 376 ? 5.167   4.498   29.817  1.00 72.44  ? 376 GLU A CD  1 
ATOM   3187  O OE1 . GLU A 1 376 ? 4.798   4.309   30.997  1.00 75.08  ? 376 GLU A OE1 1 
ATOM   3188  O OE2 . GLU A 1 376 ? 6.366   4.453   29.470  1.00 75.01  ? 376 GLU A OE2 1 
ATOM   3189  N N   . LYS A 1 377 ? 1.333   8.488   29.209  1.00 60.50  ? 377 LYS A N   1 
ATOM   3190  C CA  . LYS A 1 377 ? 0.423   9.199   30.107  1.00 60.85  ? 377 LYS A CA  1 
ATOM   3191  C C   . LYS A 1 377 ? -0.862  9.647   29.422  1.00 58.30  ? 377 LYS A C   1 
ATOM   3192  O O   . LYS A 1 377 ? -1.906  9.708   30.077  1.00 72.77  ? 377 LYS A O   1 
ATOM   3193  C CB  . LYS A 1 377 ? 1.120   10.416  30.723  1.00 55.34  ? 377 LYS A CB  1 
ATOM   3194  C CG  . LYS A 1 377 ? 2.601   10.226  30.941  1.00 59.56  ? 377 LYS A CG  1 
ATOM   3195  C CD  . LYS A 1 377 ? 3.298   11.510  31.388  1.00 71.92  ? 377 LYS A CD  1 
ATOM   3196  C CE  . LYS A 1 377 ? 4.610   11.734  30.620  1.00 71.46  ? 377 LYS A CE  1 
ATOM   3197  N NZ  . LYS A 1 377 ? 5.668   12.401  31.443  1.00 67.35  ? 377 LYS A NZ  1 
ATOM   3198  N N   . GLU A 1 378 ? -0.816  9.986   28.134  1.00 56.43  ? 378 GLU A N   1 
ATOM   3199  C CA  . GLU A 1 378 ? -2.020  10.432  27.429  1.00 58.74  ? 378 GLU A CA  1 
ATOM   3200  C C   . GLU A 1 378 ? -2.983  9.262   27.285  1.00 64.38  ? 378 GLU A C   1 
ATOM   3201  O O   . GLU A 1 378 ? -2.749  8.355   26.478  1.00 59.43  ? 378 GLU A O   1 
ATOM   3202  C CB  . GLU A 1 378 ? -1.676  11.009  26.059  1.00 49.83  ? 378 GLU A CB  1 
ATOM   3203  C CG  . GLU A 1 378 ? -0.825  12.264  26.113  1.00 58.29  ? 378 GLU A CG  1 
ATOM   3204  C CD  . GLU A 1 378 ? -1.394  13.326  27.037  1.00 67.95  ? 378 GLU A CD  1 
ATOM   3205  O OE1 . GLU A 1 378 ? -2.450  13.910  26.714  1.00 78.42  ? 378 GLU A OE1 1 
ATOM   3206  O OE2 . GLU A 1 378 ? -0.791  13.559  28.107  1.00 63.17  ? 378 GLU A OE2 1 
ATOM   3207  N N   . GLU A 1 379 ? -4.078  9.290   28.053  1.00 67.41  ? 379 GLU A N   1 
ATOM   3208  C CA  . GLU A 1 379 ? -5.019  8.180   28.078  1.00 72.33  ? 379 GLU A CA  1 
ATOM   3209  C C   . GLU A 1 379 ? -6.057  8.220   26.956  1.00 62.40  ? 379 GLU A C   1 
ATOM   3210  O O   . GLU A 1 379 ? -6.683  7.191   26.688  1.00 65.49  ? 379 GLU A O   1 
ATOM   3211  C CB  . GLU A 1 379 ? -5.731  8.107   29.434  1.00 73.19  ? 379 GLU A CB  1 
ATOM   3212  C CG  . GLU A 1 379 ? -5.329  6.890   30.302  1.00 71.74  ? 379 GLU A CG  1 
ATOM   3213  C CD  . GLU A 1 379 ? -5.565  5.504   29.657  1.00 93.51  ? 379 GLU A CD  1 
ATOM   3214  O OE1 . GLU A 1 379 ? -6.141  5.390   28.548  1.00 91.81  ? 379 GLU A OE1 1 
ATOM   3215  O OE2 . GLU A 1 379 ? -5.146  4.504   30.280  1.00 94.90  ? 379 GLU A OE2 1 
ATOM   3216  N N   . TRP A 1 380 ? -6.251  9.349   26.274  1.00 58.72  ? 380 TRP A N   1 
ATOM   3217  C CA  . TRP A 1 380 ? -7.092  9.327   25.081  1.00 61.57  ? 380 TRP A CA  1 
ATOM   3218  C C   . TRP A 1 380 ? -6.409  8.659   23.890  1.00 58.05  ? 380 TRP A C   1 
ATOM   3219  O O   . TRP A 1 380 ? -7.049  8.479   22.851  1.00 51.66  ? 380 TRP A O   1 
ATOM   3220  C CB  . TRP A 1 380 ? -7.529  10.744  24.700  1.00 58.72  ? 380 TRP A CB  1 
ATOM   3221  C CG  . TRP A 1 380 ? -6.396  11.675  24.434  1.00 52.66  ? 380 TRP A CG  1 
ATOM   3222  C CD1 . TRP A 1 380 ? -5.589  12.278  25.354  1.00 50.41  ? 380 TRP A CD1 1 
ATOM   3223  C CD2 . TRP A 1 380 ? -5.944  12.114  23.153  1.00 58.97  ? 380 TRP A CD2 1 
ATOM   3224  N NE1 . TRP A 1 380 ? -4.656  13.065  24.722  1.00 54.75  ? 380 TRP A NE1 1 
ATOM   3225  C CE2 . TRP A 1 380 ? -4.853  12.981  23.369  1.00 60.08  ? 380 TRP A CE2 1 
ATOM   3226  C CE3 . TRP A 1 380 ? -6.354  11.855  21.843  1.00 57.38  ? 380 TRP A CE3 1 
ATOM   3227  C CZ2 . TRP A 1 380 ? -4.169  13.591  22.320  1.00 56.86  ? 380 TRP A CZ2 1 
ATOM   3228  C CZ3 . TRP A 1 380 ? -5.675  12.459  20.806  1.00 61.43  ? 380 TRP A CZ3 1 
ATOM   3229  C CH2 . TRP A 1 380 ? -4.593  13.315  21.049  1.00 60.26  ? 380 TRP A CH2 1 
ATOM   3230  N N   . ILE A 1 381 ? -5.134  8.293   24.008  1.00 58.62  ? 381 ILE A N   1 
ATOM   3231  C CA  . ILE A 1 381 ? -4.414  7.559   22.972  1.00 55.91  ? 381 ILE A CA  1 
ATOM   3232  C C   . ILE A 1 381 ? -4.108  6.165   23.498  1.00 51.60  ? 381 ILE A C   1 
ATOM   3233  O O   . ILE A 1 381 ? -3.521  6.019   24.575  1.00 56.86  ? 381 ILE A O   1 
ATOM   3234  C CB  . ILE A 1 381 ? -3.119  8.275   22.541  1.00 54.55  ? 381 ILE A CB  1 
ATOM   3235  C CG1 . ILE A 1 381 ? -3.331  9.782   22.385  1.00 59.32  ? 381 ILE A CG1 1 
ATOM   3236  C CG2 . ILE A 1 381 ? -2.593  7.696   21.245  1.00 53.01  ? 381 ILE A CG2 1 
ATOM   3237  C CD1 . ILE A 1 381 ? -2.029  10.578  22.372  1.00 52.56  ? 381 ILE A CD1 1 
ATOM   3238  N N   . GLU A 1 382 ? -4.508  5.145   22.744  1.00 45.32  ? 382 GLU A N   1 
ATOM   3239  C CA  . GLU A 1 382 ? -4.156  3.763   23.040  1.00 49.40  ? 382 GLU A CA  1 
ATOM   3240  C C   . GLU A 1 382 ? -3.297  3.252   21.888  1.00 51.26  ? 382 GLU A C   1 
ATOM   3241  O O   . GLU A 1 382 ? -3.773  3.157   20.750  1.00 49.31  ? 382 GLU A O   1 
ATOM   3242  C CB  . GLU A 1 382 ? -5.406  2.901   23.236  1.00 51.42  ? 382 GLU A CB  1 
ATOM   3243  C CG  . GLU A 1 382 ? -5.124  1.434   23.541  1.00 54.17  ? 382 GLU A CG  1 
ATOM   3244  C CD  . GLU A 1 382 ? -6.378  0.650   23.899  1.00 72.29  ? 382 GLU A CD  1 
ATOM   3245  O OE1 . GLU A 1 382 ? -7.456  1.264   24.060  1.00 79.22  ? 382 GLU A OE1 1 
ATOM   3246  O OE2 . GLU A 1 382 ? -6.287  -0.592  24.005  1.00 81.94  ? 382 GLU A OE2 1 
ATOM   3247  N N   . THR A 1 383 ? -2.026  2.961   22.174  1.00 43.87  ? 383 THR A N   1 
ATOM   3248  C CA  . THR A 1 383 ? -1.170  2.296   21.200  1.00 44.30  ? 383 THR A CA  1 
ATOM   3249  C C   . THR A 1 383 ? -1.600  0.846   21.038  1.00 46.99  ? 383 THR A C   1 
ATOM   3250  O O   . THR A 1 383 ? -1.939  0.170   22.014  1.00 53.88  ? 383 THR A O   1 
ATOM   3251  C CB  . THR A 1 383 ? 0.302   2.346   21.626  1.00 53.44  ? 383 THR A CB  1 
ATOM   3252  O OG1 . THR A 1 383 ? 0.434   1.946   22.998  1.00 52.26  ? 383 THR A OG1 1 
ATOM   3253  C CG2 . THR A 1 383 ? 0.872   3.743   21.436  1.00 50.61  ? 383 THR A CG2 1 
ATOM   3254  N N   . LEU A 1 384 ? -1.568  0.359   19.801  1.00 42.17  ? 384 LEU A N   1 
ATOM   3255  C CA  . LEU A 1 384 ? -2.046  -0.979  19.498  1.00 44.45  ? 384 LEU A CA  1 
ATOM   3256  C C   . LEU A 1 384 ? -0.991  -1.759  18.719  1.00 47.41  ? 384 LEU A C   1 
ATOM   3257  O O   . LEU A 1 384 ? -0.132  -1.176  18.052  1.00 46.19  ? 384 LEU A O   1 
ATOM   3258  C CB  . LEU A 1 384 ? -3.346  -0.915  18.689  1.00 44.04  ? 384 LEU A CB  1 
ATOM   3259  C CG  . LEU A 1 384 ? -4.633  -0.561  19.439  1.00 46.37  ? 384 LEU A CG  1 
ATOM   3260  C CD1 . LEU A 1 384 ? -5.722  -0.272  18.442  1.00 42.14  ? 384 LEU A CD1 1 
ATOM   3261  C CD2 . LEU A 1 384 ? -5.084  -1.642  20.397  1.00 56.28  ? 384 LEU A CD2 1 
ATOM   3262  N N   . THR A 1 385 ? -1.050  -3.087  18.828  1.00 44.20  ? 385 THR A N   1 
ATOM   3263  C CA  . THR A 1 385 ? -0.336  -3.942  17.896  1.00 37.55  ? 385 THR A CA  1 
ATOM   3264  C C   . THR A 1 385 ? -1.186  -4.160  16.649  1.00 44.18  ? 385 THR A C   1 
ATOM   3265  O O   . THR A 1 385 ? -2.404  -3.956  16.647  1.00 44.70  ? 385 THR A O   1 
ATOM   3266  C CB  . THR A 1 385 ? 0.003   -5.312  18.500  1.00 38.87  ? 385 THR A CB  1 
ATOM   3267  O OG1 . THR A 1 385 ? -1.147  -6.163  18.444  1.00 43.20  ? 385 THR A OG1 1 
ATOM   3268  C CG2 . THR A 1 385 ? 0.442   -5.188  19.927  1.00 39.08  ? 385 THR A CG2 1 
ATOM   3269  N N   . LEU A 1 386 ? -0.522  -4.603  15.581  1.00 48.74  ? 386 LEU A N   1 
ATOM   3270  C CA  . LEU A 1 386 ? -1.230  -4.951  14.357  1.00 44.53  ? 386 LEU A CA  1 
ATOM   3271  C C   . LEU A 1 386 ? -2.293  -6.012  14.610  1.00 51.81  ? 386 LEU A C   1 
ATOM   3272  O O   . LEU A 1 386 ? -3.342  -6.008  13.954  1.00 57.45  ? 386 LEU A O   1 
ATOM   3273  C CB  . LEU A 1 386 ? -0.233  -5.425  13.299  1.00 46.92  ? 386 LEU A CB  1 
ATOM   3274  C CG  . LEU A 1 386 ? 0.944   -4.476  13.047  1.00 43.89  ? 386 LEU A CG  1 
ATOM   3275  C CD1 . LEU A 1 386 ? 1.995   -5.171  12.219  1.00 48.87  ? 386 LEU A CD1 1 
ATOM   3276  C CD2 . LEU A 1 386 ? 0.501   -3.192  12.359  1.00 38.51  ? 386 LEU A CD2 1 
ATOM   3277  N N   . GLU A 1 387 ? -2.052  -6.922  15.556  1.00 46.01  ? 387 GLU A N   1 
ATOM   3278  C CA  . GLU A 1 387 ? -3.066  -7.918  15.877  1.00 42.89  ? 387 GLU A CA  1 
ATOM   3279  C C   . GLU A 1 387 ? -4.229  -7.288  16.634  1.00 50.47  ? 387 GLU A C   1 
ATOM   3280  O O   . GLU A 1 387 ? -5.398  -7.539  16.314  1.00 54.74  ? 387 GLU A O   1 
ATOM   3281  C CB  . GLU A 1 387 ? -2.442  -9.057  16.676  1.00 43.41  ? 387 GLU A CB  1 
ATOM   3282  C CG  . GLU A 1 387 ? -3.434  -9.825  17.504  1.00 57.47  ? 387 GLU A CG  1 
ATOM   3283  C CD  . GLU A 1 387 ? -3.253  -11.315 17.380  1.00 73.42  ? 387 GLU A CD  1 
ATOM   3284  O OE1 . GLU A 1 387 ? -4.275  -12.033 17.378  1.00 88.51  ? 387 GLU A OE1 1 
ATOM   3285  O OE2 . GLU A 1 387 ? -2.091  -11.766 17.285  1.00 64.54  ? 387 GLU A OE2 1 
ATOM   3286  N N   . GLU A 1 388 ? -3.929  -6.451  17.634  1.00 50.07  ? 388 GLU A N   1 
ATOM   3287  C CA  . GLU A 1 388 ? -4.991  -5.749  18.352  1.00 46.81  ? 388 GLU A CA  1 
ATOM   3288  C C   . GLU A 1 388 ? -5.804  -4.864  17.414  1.00 42.76  ? 388 GLU A C   1 
ATOM   3289  O O   . GLU A 1 388 ? -7.029  -4.774  17.544  1.00 44.68  ? 388 GLU A O   1 
ATOM   3290  C CB  . GLU A 1 388 ? -4.403  -4.918  19.492  1.00 39.62  ? 388 GLU A CB  1 
ATOM   3291  C CG  . GLU A 1 388 ? -3.719  -5.731  20.556  1.00 45.94  ? 388 GLU A CG  1 
ATOM   3292  C CD  . GLU A 1 388 ? -3.045  -4.868  21.607  1.00 52.82  ? 388 GLU A CD  1 
ATOM   3293  O OE1 . GLU A 1 388 ? -2.641  -3.730  21.284  1.00 46.43  ? 388 GLU A OE1 1 
ATOM   3294  O OE2 . GLU A 1 388 ? -2.912  -5.332  22.758  1.00 61.51  ? 388 GLU A OE2 1 
ATOM   3295  N N   . ALA A 1 389 ? -5.143  -4.185  16.473  1.00 47.52  ? 389 ALA A N   1 
ATOM   3296  C CA  . ALA A 1 389 ? -5.893  -3.377  15.516  1.00 49.69  ? 389 ALA A CA  1 
ATOM   3297  C C   . ALA A 1 389 ? -6.763  -4.244  14.625  1.00 48.02  ? 389 ALA A C   1 
ATOM   3298  O O   . ALA A 1 389 ? -7.808  -3.790  14.148  1.00 52.39  ? 389 ALA A O   1 
ATOM   3299  C CB  . ALA A 1 389 ? -4.953  -2.527  14.661  1.00 40.37  ? 389 ALA A CB  1 
ATOM   3300  N N   . MET A 1 390 ? -6.355  -5.489  14.390  1.00 49.04  ? 390 MET A N   1 
ATOM   3301  C CA  . MET A 1 390 ? -7.159  -6.370  13.557  1.00 46.86  ? 390 MET A CA  1 
ATOM   3302  C C   . MET A 1 390 ? -8.427  -6.796  14.274  1.00 52.53  ? 390 MET A C   1 
ATOM   3303  O O   . MET A 1 390 ? -9.509  -6.809  13.676  1.00 60.33  ? 390 MET A O   1 
ATOM   3304  C CB  . MET A 1 390 ? -6.342  -7.583  13.138  1.00 54.29  ? 390 MET A CB  1 
ATOM   3305  C CG  . MET A 1 390 ? -5.468  -7.310  11.933  1.00 62.66  ? 390 MET A CG  1 
ATOM   3306  S SD  . MET A 1 390 ? -6.444  -6.808  10.495  1.00 65.99  ? 390 MET A SD  1 
ATOM   3307  C CE  . MET A 1 390 ? -6.900  -8.425  9.852   1.00 58.32  ? 390 MET A CE  1 
ATOM   3308  N N   . ARG A 1 391 ? -8.322  -7.125  15.560  1.00 52.86  ? 391 ARG A N   1 
ATOM   3309  C CA  . ARG A 1 391 ? -9.463  -7.632  16.309  1.00 53.44  ? 391 ARG A CA  1 
ATOM   3310  C C   . ARG A 1 391 ? -10.323 -6.532  16.918  1.00 52.15  ? 391 ARG A C   1 
ATOM   3311  O O   . ARG A 1 391 ? -11.415 -6.832  17.406  1.00 62.26  ? 391 ARG A O   1 
ATOM   3312  C CB  . ARG A 1 391 ? -8.992  -8.572  17.427  1.00 50.28  ? 391 ARG A CB  1 
ATOM   3313  C CG  . ARG A 1 391 ? -8.028  -9.658  16.985  1.00 51.79  ? 391 ARG A CG  1 
ATOM   3314  C CD  . ARG A 1 391 ? -8.678  -10.602 16.000  1.00 52.64  ? 391 ARG A CD  1 
ATOM   3315  N NE  . ARG A 1 391 ? -7.778  -10.942 14.901  1.00 58.14  ? 391 ARG A NE  1 
ATOM   3316  C CZ  . ARG A 1 391 ? -8.005  -10.643 13.628  1.00 54.66  ? 391 ARG A CZ  1 
ATOM   3317  N NH1 . ARG A 1 391 ? -9.082  -9.971  13.258  1.00 53.75  ? 391 ARG A NH1 1 
ATOM   3318  N NH2 . ARG A 1 391 ? -7.129  -11.025 12.702  1.00 56.88  ? 391 ARG A NH2 1 
ATOM   3319  N N   . LYS A 1 392 ? -9.864  -5.279  16.910  1.00 48.16  ? 392 LYS A N   1 
ATOM   3320  C CA  . LYS A 1 392 ? -10.597 -4.203  17.567  1.00 49.01  ? 392 LYS A CA  1 
ATOM   3321  C C   . LYS A 1 392 ? -11.931 -3.941  16.878  1.00 66.95  ? 392 LYS A C   1 
ATOM   3322  O O   . LYS A 1 392 ? -11.983 -3.750  15.658  1.00 66.82  ? 392 LYS A O   1 
ATOM   3323  C CB  . LYS A 1 392 ? -9.769  -2.922  17.584  1.00 50.10  ? 392 LYS A CB  1 
ATOM   3324  C CG  . LYS A 1 392 ? -10.094 -2.005  18.762  1.00 57.75  ? 392 LYS A CG  1 
ATOM   3325  C CD  . LYS A 1 392 ? -9.022  -2.091  19.844  1.00 54.19  ? 392 LYS A CD  1 
ATOM   3326  C CE  . LYS A 1 392 ? -9.584  -1.806  21.234  1.00 58.92  ? 392 LYS A CE  1 
ATOM   3327  N NZ  . LYS A 1 392 ? -8.565  -2.040  22.307  1.00 63.79  ? 392 LYS A NZ  1 
ATOM   3328  N N   . GLU A 1 393 ? -13.012 -3.918  17.665  1.00 56.44  ? 393 GLU A N   1 
ATOM   3329  C CA  . GLU A 1 393 ? -14.336 -3.620  17.137  1.00 53.40  ? 393 GLU A CA  1 
ATOM   3330  C C   . GLU A 1 393 ? -14.741 -2.164  17.324  1.00 55.13  ? 393 GLU A C   1 
ATOM   3331  O O   . GLU A 1 393 ? -15.859 -1.791  16.957  1.00 65.01  ? 393 GLU A O   1 
ATOM   3332  C CB  . GLU A 1 393 ? -15.393 -4.534  17.769  1.00 61.43  ? 393 GLU A CB  1 
ATOM   3333  C CG  . GLU A 1 393 ? -16.032 -5.528  16.785  1.00 74.66  ? 393 GLU A CG  1 
ATOM   3334  C CD  . GLU A 1 393 ? -16.795 -4.854  15.641  1.00 71.46  ? 393 GLU A CD  1 
ATOM   3335  O OE1 . GLU A 1 393 ? -17.320 -3.736  15.830  1.00 81.24  ? 393 GLU A OE1 1 
ATOM   3336  O OE2 . GLU A 1 393 ? -16.862 -5.442  14.543  1.00 57.00  ? 393 GLU A OE2 1 
ATOM   3337  N N   . ASP A 1 394 ? -13.867 -1.330  17.872  1.00 53.36  ? 394 ASP A N   1 
ATOM   3338  C CA  . ASP A 1 394 ? -14.139 0.091   18.008  1.00 49.92  ? 394 ASP A CA  1 
ATOM   3339  C C   . ASP A 1 394 ? -13.585 0.903   16.841  1.00 56.02  ? 394 ASP A C   1 
ATOM   3340  O O   . ASP A 1 394 ? -13.603 2.137   16.894  1.00 54.87  ? 394 ASP A O   1 
ATOM   3341  C CB  . ASP A 1 394 ? -13.552 0.611   19.323  1.00 63.97  ? 394 ASP A CB  1 
ATOM   3342  C CG  . ASP A 1 394 ? -13.685 -0.384  20.462  1.00 69.06  ? 394 ASP A CG  1 
ATOM   3343  O OD1 . ASP A 1 394 ? -13.010 -1.437  20.425  1.00 70.52  ? 394 ASP A OD1 1 
ATOM   3344  O OD2 . ASP A 1 394 ? -14.454 -0.102  21.405  1.00 67.50  ? 394 ASP A OD2 1 
ATOM   3345  N N   . VAL A 1 395 ? -13.087 0.237   15.801  1.00 58.03  ? 395 VAL A N   1 
ATOM   3346  C CA  . VAL A 1 395 ? -12.507 0.883   14.626  1.00 60.45  ? 395 VAL A CA  1 
ATOM   3347  C C   . VAL A 1 395 ? -13.472 0.667   13.467  1.00 48.84  ? 395 VAL A C   1 
ATOM   3348  O O   . VAL A 1 395 ? -13.822 -0.476  13.148  1.00 49.95  ? 395 VAL A O   1 
ATOM   3349  C CB  . VAL A 1 395 ? -11.107 0.325   14.304  1.00 57.83  ? 395 VAL A CB  1 
ATOM   3350  C CG1 . VAL A 1 395 ? -10.742 0.564   12.839  1.00 50.08  ? 395 VAL A CG1 1 
ATOM   3351  C CG2 . VAL A 1 395 ? -10.052 0.937   15.225  1.00 55.24  ? 395 VAL A CG2 1 
ATOM   3352  N N   . LYS A 1 396 ? -13.911 1.759   12.847  1.00 45.09  ? 396 LYS A N   1 
ATOM   3353  C CA  . LYS A 1 396 ? -14.885 1.658   11.768  1.00 49.06  ? 396 LYS A CA  1 
ATOM   3354  C C   . LYS A 1 396 ? -14.261 0.992   10.548  1.00 49.32  ? 396 LYS A C   1 
ATOM   3355  O O   . LYS A 1 396 ? -13.102 1.243   10.209  1.00 58.60  ? 396 LYS A O   1 
ATOM   3356  C CB  . LYS A 1 396 ? -15.415 3.043   11.395  1.00 49.02  ? 396 LYS A CB  1 
ATOM   3357  C CG  . LYS A 1 396 ? -16.233 3.736   12.472  1.00 46.55  ? 396 LYS A CG  1 
ATOM   3358  C CD  . LYS A 1 396 ? -16.895 2.757   13.412  1.00 49.79  ? 396 LYS A CD  1 
ATOM   3359  C CE  . LYS A 1 396 ? -17.883 3.457   14.316  1.00 44.38  ? 396 LYS A CE  1 
ATOM   3360  N NZ  . LYS A 1 396 ? -18.330 2.459   15.308  1.00 44.68  ? 396 LYS A NZ  1 
ATOM   3361  N N   . THR A 1 397 ? -15.031 0.134   9.890   1.00 48.18  ? 397 THR A N   1 
ATOM   3362  C CA  . THR A 1 397 ? -14.555 -0.624  8.743   1.00 47.47  ? 397 THR A CA  1 
ATOM   3363  C C   . THR A 1 397 ? -15.422 -0.326  7.525   1.00 60.79  ? 397 THR A C   1 
ATOM   3364  O O   . THR A 1 397 ? -16.654 -0.256  7.618   1.00 56.75  ? 397 THR A O   1 
ATOM   3365  C CB  . THR A 1 397 ? -14.552 -2.133  9.029   1.00 49.44  ? 397 THR A CB  1 
ATOM   3366  O OG1 . THR A 1 397 ? -13.956 -2.382  10.309  1.00 53.40  ? 397 THR A OG1 1 
ATOM   3367  C CG2 . THR A 1 397 ? -13.760 -2.874  7.966   1.00 45.15  ? 397 THR A CG2 1 
ATOM   3368  N N   . GLU A 1 398 ? -14.766 -0.137  6.388   1.00 56.47  ? 398 GLU A N   1 
ATOM   3369  C CA  . GLU A 1 398 ? -15.434 0.067   5.117   1.00 52.73  ? 398 GLU A CA  1 
ATOM   3370  C C   . GLU A 1 398 ? -14.842 -0.902  4.113   1.00 55.65  ? 398 GLU A C   1 
ATOM   3371  O O   . GLU A 1 398 ? -13.679 -1.296  4.222   1.00 53.21  ? 398 GLU A O   1 
ATOM   3372  C CB  . GLU A 1 398 ? -15.279 1.510   4.629   1.00 58.69  ? 398 GLU A CB  1 
ATOM   3373  C CG  . GLU A 1 398 ? -16.465 2.390   4.983   1.00 72.12  ? 398 GLU A CG  1 
ATOM   3374  C CD  . GLU A 1 398 ? -16.437 3.733   4.278   1.00 81.57  ? 398 GLU A CD  1 
ATOM   3375  O OE1 . GLU A 1 398 ? -17.103 4.675   4.760   1.00 88.21  ? 398 GLU A OE1 1 
ATOM   3376  O OE2 . GLU A 1 398 ? -15.742 3.849   3.246   1.00 83.21  ? 398 GLU A OE2 1 
ATOM   3377  N N   . VAL A 1 399 ? -15.638 -1.304  3.134   1.00 58.03  ? 399 VAL A N   1 
ATOM   3378  C CA  . VAL A 1 399 ? -15.149 -2.201  2.097   1.00 54.89  ? 399 VAL A CA  1 
ATOM   3379  C C   . VAL A 1 399 ? -14.972 -1.402  0.817   1.00 54.92  ? 399 VAL A C   1 
ATOM   3380  O O   . VAL A 1 399 ? -15.857 -0.629  0.431   1.00 48.23  ? 399 VAL A O   1 
ATOM   3381  C CB  . VAL A 1 399 ? -16.079 -3.406  1.897   1.00 52.50  ? 399 VAL A CB  1 
ATOM   3382  C CG1 . VAL A 1 399 ? -17.516 -2.960  1.811   1.00 64.09  ? 399 VAL A CG1 1 
ATOM   3383  C CG2 . VAL A 1 399 ? -15.658 -4.180  0.670   1.00 58.00  ? 399 VAL A CG2 1 
ATOM   3384  N N   . ILE A 1 400 ? -13.802 -1.553  0.192   1.00 56.61  ? 400 ILE A N   1 
ATOM   3385  C CA  . ILE A 1 400 ? -13.480 -0.926  -1.082  1.00 51.12  ? 400 ILE A CA  1 
ATOM   3386  C C   . ILE A 1 400 ? -13.198 -2.019  -2.103  1.00 51.29  ? 400 ILE A C   1 
ATOM   3387  O O   . ILE A 1 400 ? -12.858 -3.152  -1.749  1.00 51.36  ? 400 ILE A O   1 
ATOM   3388  C CB  . ILE A 1 400 ? -12.286 0.041   -0.960  1.00 45.69  ? 400 ILE A CB  1 
ATOM   3389  C CG1 . ILE A 1 400 ? -11.007 -0.724  -0.631  1.00 50.37  ? 400 ILE A CG1 1 
ATOM   3390  C CG2 . ILE A 1 400 ? -12.567 1.099   0.081   1.00 47.16  ? 400 ILE A CG2 1 
ATOM   3391  C CD1 . ILE A 1 400 ? -9.922  0.144   -0.033  1.00 48.89  ? 400 ILE A CD1 1 
ATOM   3392  N N   . GLU A 1 401 ? -13.339 -1.670  -3.381  1.00 44.21  ? 401 GLU A N   1 
ATOM   3393  C CA  . GLU A 1 401 ? -13.264 -2.652  -4.451  1.00 50.38  ? 401 GLU A CA  1 
ATOM   3394  C C   . GLU A 1 401 ? -12.026 -2.520  -5.321  1.00 54.35  ? 401 GLU A C   1 
ATOM   3395  O O   . GLU A 1 401 ? -11.648 -3.495  -5.979  1.00 48.70  ? 401 GLU A O   1 
ATOM   3396  C CB  . GLU A 1 401 ? -14.519 -2.563  -5.340  1.00 62.28  ? 401 GLU A CB  1 
ATOM   3397  C CG  . GLU A 1 401 ? -15.147 -3.923  -5.696  1.00 65.01  ? 401 GLU A CG  1 
ATOM   3398  C CD  . GLU A 1 401 ? -15.923 -4.532  -4.538  1.00 67.00  ? 401 GLU A CD  1 
ATOM   3399  O OE1 . GLU A 1 401 ? -16.583 -3.758  -3.815  1.00 64.38  ? 401 GLU A OE1 1 
ATOM   3400  O OE2 . GLU A 1 401 ? -15.867 -5.770  -4.343  1.00 68.91  ? 401 GLU A OE2 1 
ATOM   3401  N N   . SER A 1 402 ? -11.375 -1.359  -5.328  1.00 62.75  ? 402 SER A N   1 
ATOM   3402  C CA  . SER A 1 402 ? -10.249 -1.145  -6.225  1.00 57.62  ? 402 SER A CA  1 
ATOM   3403  C C   . SER A 1 402 ? -9.190  -0.275  -5.562  1.00 52.06  ? 402 SER A C   1 
ATOM   3404  O O   . SER A 1 402 ? -9.420  0.362   -4.531  1.00 48.46  ? 402 SER A O   1 
ATOM   3405  C CB  . SER A 1 402 ? -10.708 -0.512  -7.544  1.00 49.90  ? 402 SER A CB  1 
ATOM   3406  O OG  . SER A 1 402 ? -10.759 0.901   -7.447  1.00 56.90  ? 402 SER A OG  1 
ATOM   3407  N N   . VAL A 1 403 ? -8.009  -0.287  -6.173  1.00 53.53  ? 403 VAL A N   1 
ATOM   3408  C CA  . VAL A 1 403 ? -6.932  0.639   -5.869  1.00 50.36  ? 403 VAL A CA  1 
ATOM   3409  C C   . VAL A 1 403 ? -6.290  1.033   -7.192  1.00 56.35  ? 403 VAL A C   1 
ATOM   3410  O O   . VAL A 1 403 ? -6.446  0.355   -8.210  1.00 56.87  ? 403 VAL A O   1 
ATOM   3411  C CB  . VAL A 1 403 ? -5.878  0.034   -4.916  1.00 54.19  ? 403 VAL A CB  1 
ATOM   3412  C CG1 . VAL A 1 403 ? -6.445  -0.109  -3.524  1.00 46.67  ? 403 VAL A CG1 1 
ATOM   3413  C CG2 . VAL A 1 403 ? -5.395  -1.306  -5.446  1.00 58.00  ? 403 VAL A CG2 1 
ATOM   3414  N N   . LYS A 1 404 ? -5.582  2.159   -7.170  1.00 58.90  ? 404 LYS A N   1 
ATOM   3415  C CA  . LYS A 1 404 ? -4.758  2.606   -8.286  1.00 51.90  ? 404 LYS A CA  1 
ATOM   3416  C C   . LYS A 1 404 ? -3.306  2.338   -7.933  1.00 58.41  ? 404 LYS A C   1 
ATOM   3417  O O   . LYS A 1 404 ? -2.817  2.812   -6.900  1.00 56.32  ? 404 LYS A O   1 
ATOM   3418  C CB  . LYS A 1 404 ? -4.972  4.087   -8.581  1.00 53.04  ? 404 LYS A CB  1 
ATOM   3419  C CG  . LYS A 1 404 ? -6.144  4.358   -9.483  1.00 56.67  ? 404 LYS A CG  1 
ATOM   3420  C CD  . LYS A 1 404 ? -6.101  3.471   -10.714 1.00 64.66  ? 404 LYS A CD  1 
ATOM   3421  C CE  . LYS A 1 404 ? -7.146  3.891   -11.731 1.00 70.70  ? 404 LYS A CE  1 
ATOM   3422  N NZ  . LYS A 1 404 ? -7.052  5.337   -12.064 1.00 68.68  ? 404 LYS A NZ  1 
ATOM   3423  N N   . ALA A 1 405 ? -2.621  1.593   -8.794  1.00 57.73  ? 405 ALA A N   1 
ATOM   3424  C CA  . ALA A 1 405 ? -1.283  1.116   -8.473  1.00 57.86  ? 405 ALA A CA  1 
ATOM   3425  C C   . ALA A 1 405 ? -0.313  2.277   -8.267  1.00 56.92  ? 405 ALA A C   1 
ATOM   3426  O O   . ALA A 1 405 ? -0.284  3.224   -9.059  1.00 71.27  ? 405 ALA A O   1 
ATOM   3427  C CB  . ALA A 1 405 ? -0.791  0.193   -9.589  1.00 57.06  ? 405 ALA A CB  1 
ATOM   3428  N N   . GLY A 1 406 ? 0.467   2.209   -7.196  1.00 50.98  ? 406 GLY A N   1 
ATOM   3429  C CA  . GLY A 1 406 ? 1.479   3.217   -6.951  1.00 54.64  ? 406 GLY A CA  1 
ATOM   3430  C C   . GLY A 1 406 ? 2.371   2.870   -5.775  1.00 57.19  ? 406 GLY A C   1 
ATOM   3431  O O   . GLY A 1 406 ? 2.469   1.712   -5.369  1.00 58.29  ? 406 GLY A O   1 
ATOM   3432  N N   . THR A 1 407 ? 3.035   3.896   -5.237  1.00 49.93  ? 407 THR A N   1 
ATOM   3433  C CA  . THR A 1 407 ? 3.950   3.740   -4.116  1.00 49.53  ? 407 THR A CA  1 
ATOM   3434  C C   . THR A 1 407 ? 3.780   4.929   -3.185  1.00 49.77  ? 407 THR A C   1 
ATOM   3435  O O   . THR A 1 407 ? 2.985   5.836   -3.444  1.00 49.00  ? 407 THR A O   1 
ATOM   3436  C CB  . THR A 1 407 ? 5.411   3.638   -4.579  1.00 52.32  ? 407 THR A CB  1 
ATOM   3437  O OG1 . THR A 1 407 ? 5.711   4.726   -5.461  1.00 52.63  ? 407 THR A OG1 1 
ATOM   3438  C CG2 . THR A 1 407 ? 5.664   2.321   -5.288  1.00 48.01  ? 407 THR A CG2 1 
ATOM   3439  N N   . TRP A 1 408 ? 4.540   4.937   -2.092  1.00 46.55  ? 408 TRP A N   1 
ATOM   3440  C CA  . TRP A 1 408 ? 4.467   6.095   -1.218  1.00 48.67  ? 408 TRP A CA  1 
ATOM   3441  C C   . TRP A 1 408 ? 5.318   7.252   -1.734  1.00 48.30  ? 408 TRP A C   1 
ATOM   3442  O O   . TRP A 1 408 ? 5.353   8.316   -1.106  1.00 49.02  ? 408 TRP A O   1 
ATOM   3443  C CB  . TRP A 1 408 ? 4.828   5.697   0.225   1.00 45.39  ? 408 TRP A CB  1 
ATOM   3444  C CG  . TRP A 1 408 ? 6.158   5.016   0.452   1.00 45.61  ? 408 TRP A CG  1 
ATOM   3445  C CD1 . TRP A 1 408 ? 7.121   4.747   -0.476  1.00 52.86  ? 408 TRP A CD1 1 
ATOM   3446  C CD2 . TRP A 1 408 ? 6.674   4.544   1.709   1.00 43.87  ? 408 TRP A CD2 1 
ATOM   3447  N NE1 . TRP A 1 408 ? 8.203   4.132   0.120   1.00 40.77  ? 408 TRP A NE1 1 
ATOM   3448  C CE2 . TRP A 1 408 ? 7.951   3.998   1.460   1.00 48.10  ? 408 TRP A CE2 1 
ATOM   3449  C CE3 . TRP A 1 408 ? 6.178   4.529   3.019   1.00 43.21  ? 408 TRP A CE3 1 
ATOM   3450  C CZ2 . TRP A 1 408 ? 8.740   3.444   2.474   1.00 55.18  ? 408 TRP A CZ2 1 
ATOM   3451  C CZ3 . TRP A 1 408 ? 6.967   3.978   4.025   1.00 49.64  ? 408 TRP A CZ3 1 
ATOM   3452  C CH2 . TRP A 1 408 ? 8.229   3.443   3.746   1.00 48.35  ? 408 TRP A CH2 1 
ATOM   3453  N N   . PHE A 1 409 ? 5.955   7.076   -2.886  1.00 51.00  ? 409 PHE A N   1 
ATOM   3454  C CA  . PHE A 1 409 ? 6.757   8.096   -3.557  1.00 56.84  ? 409 PHE A CA  1 
ATOM   3455  C C   . PHE A 1 409 ? 5.918   8.609   -4.731  1.00 61.27  ? 409 PHE A C   1 
ATOM   3456  O O   . PHE A 1 409 ? 5.962   8.062   -5.837  1.00 53.83  ? 409 PHE A O   1 
ATOM   3457  C CB  . PHE A 1 409 ? 8.097   7.504   -4.004  1.00 47.98  ? 409 PHE A CB  1 
ATOM   3458  C CG  . PHE A 1 409 ? 9.139   8.528   -4.376  1.00 53.96  ? 409 PHE A CG  1 
ATOM   3459  C CD1 . PHE A 1 409 ? 8.870   9.527   -5.294  1.00 62.39  ? 409 PHE A CD1 1 
ATOM   3460  C CD2 . PHE A 1 409 ? 10.411  8.465   -3.823  1.00 65.23  ? 409 PHE A CD2 1 
ATOM   3461  C CE1 . PHE A 1 409 ? 9.836   10.456  -5.639  1.00 61.14  ? 409 PHE A CE1 1 
ATOM   3462  C CE2 . PHE A 1 409 ? 11.380  9.385   -4.162  1.00 65.85  ? 409 PHE A CE2 1 
ATOM   3463  C CZ  . PHE A 1 409 ? 11.089  10.386  -5.075  1.00 68.78  ? 409 PHE A CZ  1 
ATOM   3464  N N   . ASP A 1 410 ? 5.133   9.654   -4.467  1.00 62.38  ? 410 ASP A N   1 
ATOM   3465  C CA  . ASP A 1 410 ? 4.272   10.336  -5.433  1.00 57.47  ? 410 ASP A CA  1 
ATOM   3466  C C   . ASP A 1 410 ? 3.172   9.458   -6.009  1.00 57.29  ? 410 ASP A C   1 
ATOM   3467  O O   . ASP A 1 410 ? 2.564   9.836   -7.015  1.00 60.40  ? 410 ASP A O   1 
ATOM   3468  C CB  . ASP A 1 410 ? 5.071   10.924  -6.595  1.00 59.24  ? 410 ASP A CB  1 
ATOM   3469  C CG  . ASP A 1 410 ? 6.090   11.926  -6.142  1.00 71.87  ? 410 ASP A CG  1 
ATOM   3470  O OD1 . ASP A 1 410 ? 5.789   12.690  -5.197  1.00 74.61  ? 410 ASP A OD1 1 
ATOM   3471  O OD2 . ASP A 1 410 ? 7.190   11.946  -6.731  1.00 77.74  ? 410 ASP A OD2 1 
ATOM   3472  N N   . GLY A 1 411 ? 2.895   8.300   -5.416  1.00 57.92  ? 411 GLY A N   1 
ATOM   3473  C CA  . GLY A 1 411 ? 1.850   7.448   -5.951  1.00 56.38  ? 411 GLY A CA  1 
ATOM   3474  C C   . GLY A 1 411 ? 2.175   6.803   -7.278  1.00 59.16  ? 411 GLY A C   1 
ATOM   3475  O O   . GLY A 1 411 ? 1.289   6.202   -7.893  1.00 58.70  ? 411 GLY A O   1 
ATOM   3476  N N   . ASN A 1 412 ? 3.416   6.913   -7.744  1.00 53.88  ? 412 ASN A N   1 
ATOM   3477  C CA  . ASN A 1 412 ? 3.834   6.313   -8.997  1.00 49.61  ? 412 ASN A CA  1 
ATOM   3478  C C   . ASN A 1 412 ? 5.124   5.542   -8.769  1.00 49.66  ? 412 ASN A C   1 
ATOM   3479  O O   . ASN A 1 412 ? 5.752   5.639   -7.709  1.00 52.07  ? 412 ASN A O   1 
ATOM   3480  C CB  . ASN A 1 412 ? 4.002   7.379   -10.093 1.00 55.94  ? 412 ASN A CB  1 
ATOM   3481  C CG  . ASN A 1 412 ? 4.982   8.472   -9.710  1.00 49.45  ? 412 ASN A CG  1 
ATOM   3482  O OD1 . ASN A 1 412 ? 6.160   8.209   -9.476  1.00 61.26  ? 412 ASN A OD1 1 
ATOM   3483  N ND2 . ASN A 1 412 ? 4.503   9.707   -9.659  1.00 46.46  ? 412 ASN A ND2 1 
ATOM   3484  N N   . PHE A 1 413 ? 5.509   4.760   -9.781  1.00 51.24  ? 413 PHE A N   1 
ATOM   3485  C CA  . PHE A 1 413 ? 6.719   3.948   -9.755  1.00 50.01  ? 413 PHE A CA  1 
ATOM   3486  C C   . PHE A 1 413 ? 7.894   4.638   -10.447 1.00 50.22  ? 413 PHE A C   1 
ATOM   3487  O O   . PHE A 1 413 ? 8.843   3.962   -10.862 1.00 49.49  ? 413 PHE A O   1 
ATOM   3488  C CB  . PHE A 1 413 ? 6.460   2.590   -10.415 1.00 49.41  ? 413 PHE A CB  1 
ATOM   3489  C CG  . PHE A 1 413 ? 5.304   1.825   -9.825  1.00 54.85  ? 413 PHE A CG  1 
ATOM   3490  C CD1 . PHE A 1 413 ? 4.009   2.023   -10.293 1.00 54.23  ? 413 PHE A CD1 1 
ATOM   3491  C CD2 . PHE A 1 413 ? 5.510   0.894   -8.817  1.00 48.26  ? 413 PHE A CD2 1 
ATOM   3492  C CE1 . PHE A 1 413 ? 2.942   1.319   -9.756  1.00 45.73  ? 413 PHE A CE1 1 
ATOM   3493  C CE2 . PHE A 1 413 ? 4.445   0.185   -8.277  1.00 49.12  ? 413 PHE A CE2 1 
ATOM   3494  C CZ  . PHE A 1 413 ? 3.158   0.400   -8.750  1.00 52.75  ? 413 PHE A CZ  1 
ATOM   3495  N N   . LEU A 1 414 ? 7.846   5.967   -10.591 1.00 48.81  ? 414 LEU A N   1 
ATOM   3496  C CA  . LEU A 1 414 ? 8.851   6.657   -11.396 1.00 56.06  ? 414 LEU A CA  1 
ATOM   3497  C C   . LEU A 1 414 ? 10.235  6.637   -10.760 1.00 57.01  ? 414 LEU A C   1 
ATOM   3498  O O   . LEU A 1 414 ? 11.228  6.883   -11.456 1.00 59.55  ? 414 LEU A O   1 
ATOM   3499  C CB  . LEU A 1 414 ? 8.426   8.101   -11.657 1.00 49.66  ? 414 LEU A CB  1 
ATOM   3500  C CG  . LEU A 1 414 ? 7.249   8.287   -12.607 1.00 48.98  ? 414 LEU A CG  1 
ATOM   3501  C CD1 . LEU A 1 414 ? 6.760   9.719   -12.555 1.00 52.39  ? 414 LEU A CD1 1 
ATOM   3502  C CD2 . LEU A 1 414 ? 7.662   7.909   -14.007 1.00 50.43  ? 414 LEU A CD2 1 
ATOM   3503  N N   . LYS A 1 415 ? 10.325  6.352   -9.462  1.00 57.29  ? 415 LYS A N   1 
ATOM   3504  C CA  . LYS A 1 415 ? 11.623  6.254   -8.809  1.00 56.20  ? 415 LYS A CA  1 
ATOM   3505  C C   . LYS A 1 415 ? 12.396  5.016   -9.256  1.00 61.88  ? 415 LYS A C   1 
ATOM   3506  O O   . LYS A 1 415 ? 13.621  4.967   -9.084  1.00 66.82  ? 415 LYS A O   1 
ATOM   3507  C CB  . LYS A 1 415 ? 11.427  6.253   -7.289  1.00 56.84  ? 415 LYS A CB  1 
ATOM   3508  C CG  . LYS A 1 415 ? 12.701  6.389   -6.486  1.00 60.98  ? 415 LYS A CG  1 
ATOM   3509  C CD  . LYS A 1 415 ? 13.454  7.658   -6.825  1.00 64.93  ? 415 LYS A CD  1 
ATOM   3510  C CE  . LYS A 1 415 ? 14.362  8.083   -5.681  1.00 66.69  ? 415 LYS A CE  1 
ATOM   3511  N NZ  . LYS A 1 415 ? 15.809  7.818   -5.953  1.00 76.36  ? 415 LYS A NZ  1 
ATOM   3512  N N   . TRP A 1 416 ? 11.710  4.023   -9.840  1.00 59.39  ? 416 TRP A N   1 
ATOM   3513  C CA  . TRP A 1 416 ? 12.321  2.760   -10.239 1.00 55.71  ? 416 TRP A CA  1 
ATOM   3514  C C   . TRP A 1 416 ? 12.205  2.447   -11.722 1.00 51.96  ? 416 TRP A C   1 
ATOM   3515  O O   . TRP A 1 416 ? 12.962  1.605   -12.213 1.00 56.83  ? 416 TRP A O   1 
ATOM   3516  C CB  . TRP A 1 416 ? 11.711  1.589   -9.443  1.00 54.85  ? 416 TRP A CB  1 
ATOM   3517  C CG  . TRP A 1 416 ? 11.666  1.858   -7.981  1.00 47.88  ? 416 TRP A CG  1 
ATOM   3518  C CD1 . TRP A 1 416 ? 12.582  1.474   -7.046  1.00 54.35  ? 416 TRP A CD1 1 
ATOM   3519  C CD2 . TRP A 1 416 ? 10.653  2.578   -7.278  1.00 54.59  ? 416 TRP A CD2 1 
ATOM   3520  N NE1 . TRP A 1 416 ? 12.207  1.921   -5.800  1.00 58.19  ? 416 TRP A NE1 1 
ATOM   3521  C CE2 . TRP A 1 416 ? 11.022  2.600   -5.915  1.00 55.05  ? 416 TRP A CE2 1 
ATOM   3522  C CE3 . TRP A 1 416 ? 9.466   3.207   -7.666  1.00 47.01  ? 416 TRP A CE3 1 
ATOM   3523  C CZ2 . TRP A 1 416 ? 10.248  3.227   -4.945  1.00 44.25  ? 416 TRP A CZ2 1 
ATOM   3524  C CZ3 . TRP A 1 416 ? 8.702   3.828   -6.705  1.00 46.39  ? 416 TRP A CZ3 1 
ATOM   3525  C CH2 . TRP A 1 416 ? 9.093   3.834   -5.359  1.00 52.86  ? 416 TRP A CH2 1 
ATOM   3526  N N   . ILE A 1 417 ? 11.301  3.099   -12.450 1.00 54.81  ? 417 ILE A N   1 
ATOM   3527  C CA  . ILE A 1 417 ? 11.100  2.823   -13.867 1.00 48.85  ? 417 ILE A CA  1 
ATOM   3528  C C   . ILE A 1 417 ? 10.645  4.107   -14.539 1.00 52.34  ? 417 ILE A C   1 
ATOM   3529  O O   . ILE A 1 417 ? 10.133  5.017   -13.883 1.00 58.27  ? 417 ILE A O   1 
ATOM   3530  C CB  . ILE A 1 417 ? 10.084  1.676   -14.059 1.00 48.50  ? 417 ILE A CB  1 
ATOM   3531  C CG1 . ILE A 1 417 ? 10.221  1.047   -15.445 1.00 49.92  ? 417 ILE A CG1 1 
ATOM   3532  C CG2 . ILE A 1 417 ? 8.667   2.163   -13.760 1.00 52.95  ? 417 ILE A CG2 1 
ATOM   3533  C CD1 . ILE A 1 417 ? 9.744   -0.379  -15.498 1.00 46.81  ? 417 ILE A CD1 1 
ATOM   3534  N N   . GLY A 1 418 ? 10.851  4.199   -15.850 1.00 50.28  ? 418 GLY A N   1 
ATOM   3535  C CA  . GLY A 1 418 ? 10.349  5.368   -16.545 1.00 52.25  ? 418 GLY A CA  1 
ATOM   3536  C C   . GLY A 1 418 ? 11.353  6.126   -17.384 1.00 61.69  ? 418 GLY A C   1 
ATOM   3537  O O   . GLY A 1 418 ? 10.996  6.603   -18.465 1.00 72.82  ? 418 GLY A O   1 
ATOM   3538  N N   . ASN A 1 419 ? 12.594  6.263   -16.915 1.00 72.51  ? 419 ASN A N   1 
ATOM   3539  C CA  . ASN A 1 419 ? 13.652  6.916   -17.679 1.00 75.43  ? 419 ASN A CA  1 
ATOM   3540  C C   . ASN A 1 419 ? 14.642  5.893   -18.228 1.00 77.20  ? 419 ASN A C   1 
ATOM   3541  O O   . ASN A 1 419 ? 14.690  4.740   -17.784 1.00 70.78  ? 419 ASN A O   1 
ATOM   3542  C CB  . ASN A 1 419 ? 14.356  8.012   -16.844 1.00 70.16  ? 419 ASN A CB  1 
ATOM   3543  C CG  . ASN A 1 419 ? 15.388  7.477   -15.827 1.00 81.92  ? 419 ASN A CG  1 
ATOM   3544  O OD1 . ASN A 1 419 ? 15.909  6.360   -15.919 1.00 81.69  ? 419 ASN A OD1 1 
ATOM   3545  N ND2 . ASN A 1 419 ? 15.680  8.311   -14.836 1.00 86.63  ? 419 ASN A ND2 1 
ATOM   3546  N N   . LYS A 1 420 ? 15.435  6.338   -19.210 1.00 71.71  ? 420 LYS A N   1 
ATOM   3547  C CA  . LYS A 1 420 ? 16.371  5.438   -19.882 1.00 73.79  ? 420 LYS A CA  1 
ATOM   3548  C C   . LYS A 1 420 ? 17.280  4.730   -18.888 1.00 76.04  ? 420 LYS A C   1 
ATOM   3549  O O   . LYS A 1 420 ? 17.482  3.512   -18.975 1.00 75.43  ? 420 LYS A O   1 
ATOM   3550  C CB  . LYS A 1 420 ? 17.205  6.212   -20.908 1.00 73.10  ? 420 LYS A CB  1 
ATOM   3551  C CG  . LYS A 1 420 ? 16.607  6.198   -22.311 1.00 79.85  ? 420 LYS A CG  1 
ATOM   3552  C CD  . LYS A 1 420 ? 17.589  5.699   -23.374 1.00 76.89  ? 420 LYS A CD  1 
ATOM   3553  C CE  . LYS A 1 420 ? 19.039  5.761   -22.905 1.00 84.67  ? 420 LYS A CE  1 
ATOM   3554  N NZ  . LYS A 1 420 ? 20.031  5.563   -24.007 1.00 74.54  ? 420 LYS A NZ  1 
ATOM   3555  N N   . GLU A 1 421 ? 17.809  5.476   -17.916 1.00 75.09  ? 421 GLU A N   1 
ATOM   3556  C CA  . GLU A 1 421 ? 18.692  4.900   -16.906 1.00 75.20  ? 421 GLU A CA  1 
ATOM   3557  C C   . GLU A 1 421 ? 17.992  3.799   -16.118 1.00 80.84  ? 421 GLU A C   1 
ATOM   3558  O O   . GLU A 1 421 ? 18.489  2.670   -16.033 1.00 79.20  ? 421 GLU A O   1 
ATOM   3559  C CB  . GLU A 1 421 ? 19.180  6.008   -15.974 1.00 79.06  ? 421 GLU A CB  1 
ATOM   3560  C CG  . GLU A 1 421 ? 19.733  7.226   -16.710 1.00 87.83  ? 421 GLU A CG  1 
ATOM   3561  C CD  . GLU A 1 421 ? 18.684  8.304   -16.947 1.00 89.95  ? 421 GLU A CD  1 
ATOM   3562  O OE1 . GLU A 1 421 ? 17.949  8.215   -17.955 1.00 85.62  ? 421 GLU A OE1 1 
ATOM   3563  O OE2 . GLU A 1 421 ? 18.597  9.244   -16.127 1.00 93.23  ? 421 GLU A OE2 1 
ATOM   3564  N N   . LYS A 1 422 ? 16.832  4.112   -15.530 1.00 79.71  ? 422 LYS A N   1 
ATOM   3565  C CA  . LYS A 1 422 ? 16.067  3.088   -14.825 1.00 79.20  ? 422 LYS A CA  1 
ATOM   3566  C C   . LYS A 1 422 ? 15.680  1.950   -15.761 1.00 72.70  ? 422 LYS A C   1 
ATOM   3567  O O   . LYS A 1 422 ? 15.747  0.776   -15.380 1.00 70.22  ? 422 LYS A O   1 
ATOM   3568  C CB  . LYS A 1 422 ? 14.822  3.705   -14.186 1.00 70.67  ? 422 LYS A CB  1 
ATOM   3569  C CG  . LYS A 1 422 ? 15.090  4.425   -12.879 1.00 67.93  ? 422 LYS A CG  1 
ATOM   3570  C CD  . LYS A 1 422 ? 14.597  5.858   -12.946 1.00 66.43  ? 422 LYS A CD  1 
ATOM   3571  C CE  . LYS A 1 422 ? 14.667  6.543   -11.592 1.00 69.93  ? 422 LYS A CE  1 
ATOM   3572  N NZ  . LYS A 1 422 ? 15.937  6.264   -10.879 1.00 71.26  ? 422 LYS A NZ  1 
ATOM   3573  N N   . ASN A 1 423 ? 15.284  2.275   -16.996 1.00 66.33  ? 423 ASN A N   1 
ATOM   3574  C CA  . ASN A 1 423 ? 14.884  1.233   -17.935 1.00 64.31  ? 423 ASN A CA  1 
ATOM   3575  C C   . ASN A 1 423 ? 16.052  0.348   -18.355 1.00 63.83  ? 423 ASN A C   1 
ATOM   3576  O O   . ASN A 1 423 ? 15.828  -0.791  -18.779 1.00 62.40  ? 423 ASN A O   1 
ATOM   3577  C CB  . ASN A 1 423 ? 14.222  1.858   -19.166 1.00 67.62  ? 423 ASN A CB  1 
ATOM   3578  C CG  . ASN A 1 423 ? 12.882  2.511   -18.849 1.00 65.17  ? 423 ASN A CG  1 
ATOM   3579  O OD1 . ASN A 1 423 ? 12.154  2.080   -17.950 1.00 63.09  ? 423 ASN A OD1 1 
ATOM   3580  N ND2 . ASN A 1 423 ? 12.555  3.562   -19.589 1.00 66.13  ? 423 ASN A ND2 1 
ATOM   3581  N N   . GLU A 1 424 ? 17.289  0.838   -18.246 1.00 67.80  ? 424 GLU A N   1 
ATOM   3582  C CA  . GLU A 1 424 ? 18.447  -0.013  -18.502 1.00 70.40  ? 424 GLU A CA  1 
ATOM   3583  C C   . GLU A 1 424 ? 18.461  -1.214  -17.564 1.00 63.82  ? 424 GLU A C   1 
ATOM   3584  O O   . GLU A 1 424 ? 18.666  -2.356  -17.992 1.00 64.04  ? 424 GLU A O   1 
ATOM   3585  C CB  . GLU A 1 424 ? 19.736  0.791   -18.350 1.00 70.24  ? 424 GLU A CB  1 
ATOM   3586  C CG  . GLU A 1 424 ? 20.810  0.420   -19.355 1.00 81.93  ? 424 GLU A CG  1 
ATOM   3587  C CD  . GLU A 1 424 ? 22.205  0.671   -18.824 1.00 92.07  ? 424 GLU A CD  1 
ATOM   3588  O OE1 . GLU A 1 424 ? 22.366  1.569   -17.969 1.00 102.53 ? 424 GLU A OE1 1 
ATOM   3589  O OE2 . GLU A 1 424 ? 23.143  -0.023  -19.267 1.00 93.39  ? 424 GLU A OE2 1 
ATOM   3590  N N   . TYR A 1 425 ? 18.226  -0.972  -16.274 1.00 66.31  ? 425 TYR A N   1 
ATOM   3591  C CA  . TYR A 1 425 ? 18.261  -2.053  -15.294 1.00 66.84  ? 425 TYR A CA  1 
ATOM   3592  C C   . TYR A 1 425 ? 17.171  -3.090  -15.547 1.00 56.28  ? 425 TYR A C   1 
ATOM   3593  O O   . TYR A 1 425 ? 17.369  -4.281  -15.273 1.00 52.71  ? 425 TYR A O   1 
ATOM   3594  C CB  . TYR A 1 425 ? 18.128  -1.475  -13.889 1.00 63.55  ? 425 TYR A CB  1 
ATOM   3595  C CG  . TYR A 1 425 ? 19.432  -1.284  -13.148 1.00 61.73  ? 425 TYR A CG  1 
ATOM   3596  C CD1 . TYR A 1 425 ? 20.595  -0.897  -13.811 1.00 60.42  ? 425 TYR A CD1 1 
ATOM   3597  C CD2 . TYR A 1 425 ? 19.492  -1.476  -11.776 1.00 58.65  ? 425 TYR A CD2 1 
ATOM   3598  C CE1 . TYR A 1 425 ? 21.783  -0.720  -13.116 1.00 64.50  ? 425 TYR A CE1 1 
ATOM   3599  C CE2 . TYR A 1 425 ? 20.665  -1.304  -11.078 1.00 62.79  ? 425 TYR A CE2 1 
ATOM   3600  C CZ  . TYR A 1 425 ? 21.808  -0.928  -11.746 1.00 70.35  ? 425 TYR A CZ  1 
ATOM   3601  O OH  . TYR A 1 425 ? 22.967  -0.751  -11.026 1.00 68.52  ? 425 TYR A OH  1 
ATOM   3602  N N   . TRP A 1 426 ? 16.015  -2.666  -16.062 1.00 56.76  ? 426 TRP A N   1 
ATOM   3603  C CA  . TRP A 1 426 ? 14.952  -3.629  -16.338 1.00 59.11  ? 426 TRP A CA  1 
ATOM   3604  C C   . TRP A 1 426 ? 15.275  -4.461  -17.576 1.00 54.44  ? 426 TRP A C   1 
ATOM   3605  O O   . TRP A 1 426 ? 15.077  -5.684  -17.579 1.00 50.99  ? 426 TRP A O   1 
ATOM   3606  C CB  . TRP A 1 426 ? 13.607  -2.907  -16.484 1.00 54.10  ? 426 TRP A CB  1 
ATOM   3607  C CG  . TRP A 1 426 ? 13.087  -2.301  -15.186 1.00 52.01  ? 426 TRP A CG  1 
ATOM   3608  C CD1 . TRP A 1 426 ? 13.075  -0.977  -14.850 1.00 52.81  ? 426 TRP A CD1 1 
ATOM   3609  C CD2 . TRP A 1 426 ? 12.500  -2.997  -14.076 1.00 53.26  ? 426 TRP A CD2 1 
ATOM   3610  N NE1 . TRP A 1 426 ? 12.527  -0.806  -13.602 1.00 49.97  ? 426 TRP A NE1 1 
ATOM   3611  C CE2 . TRP A 1 426 ? 12.166  -2.030  -13.105 1.00 52.75  ? 426 TRP A CE2 1 
ATOM   3612  C CE3 . TRP A 1 426 ? 12.226  -4.344  -13.808 1.00 53.37  ? 426 TRP A CE3 1 
ATOM   3613  C CZ2 . TRP A 1 426 ? 11.574  -2.366  -11.887 1.00 55.40  ? 426 TRP A CZ2 1 
ATOM   3614  C CZ3 . TRP A 1 426 ? 11.636  -4.677  -12.598 1.00 46.82  ? 426 TRP A CZ3 1 
ATOM   3615  C CH2 . TRP A 1 426 ? 11.317  -3.692  -11.654 1.00 53.30  ? 426 TRP A CH2 1 
ATOM   3616  N N   . LYS A 1 427 ? 15.813  -3.827  -18.622 1.00 54.23  ? 427 LYS A N   1 
ATOM   3617  C CA  . LYS A 1 427 ? 16.207  -4.582  -19.808 1.00 58.27  ? 427 LYS A CA  1 
ATOM   3618  C C   . LYS A 1 427 ? 17.247  -5.639  -19.467 1.00 57.28  ? 427 LYS A C   1 
ATOM   3619  O O   . LYS A 1 427 ? 17.209  -6.748  -20.015 1.00 54.28  ? 427 LYS A O   1 
ATOM   3620  C CB  . LYS A 1 427 ? 16.741  -3.646  -20.890 1.00 58.93  ? 427 LYS A CB  1 
ATOM   3621  C CG  . LYS A 1 427 ? 15.668  -3.131  -21.827 1.00 67.15  ? 427 LYS A CG  1 
ATOM   3622  C CD  . LYS A 1 427 ? 16.086  -1.818  -22.461 1.00 64.07  ? 427 LYS A CD  1 
ATOM   3623  C CE  . LYS A 1 427 ? 14.897  -0.897  -22.677 1.00 62.98  ? 427 LYS A CE  1 
ATOM   3624  N NZ  . LYS A 1 427 ? 15.259  0.540   -22.516 1.00 68.61  ? 427 LYS A NZ  1 
ATOM   3625  N N   . ILE A 1 428 ? 18.183  -5.311  -18.565 1.00 52.84  ? 428 ILE A N   1 
ATOM   3626  C CA  . ILE A 1 428 ? 19.173  -6.287  -18.108 1.00 51.65  ? 428 ILE A CA  1 
ATOM   3627  C C   . ILE A 1 428 ? 18.492  -7.424  -17.363 1.00 51.61  ? 428 ILE A C   1 
ATOM   3628  O O   . ILE A 1 428 ? 18.815  -8.602  -17.560 1.00 49.55  ? 428 ILE A O   1 
ATOM   3629  C CB  . ILE A 1 428 ? 20.236  -5.602  -17.226 1.00 57.01  ? 428 ILE A CB  1 
ATOM   3630  C CG1 . ILE A 1 428 ? 21.216  -4.792  -18.078 1.00 54.86  ? 428 ILE A CG1 1 
ATOM   3631  C CG2 . ILE A 1 428 ? 20.986  -6.630  -16.381 1.00 53.82  ? 428 ILE A CG2 1 
ATOM   3632  C CD1 . ILE A 1 428 ? 21.693  -3.505  -17.429 1.00 56.67  ? 428 ILE A CD1 1 
ATOM   3633  N N   . LEU A 1 429 ? 17.538  -7.084  -16.493 1.00 55.38  ? 429 LEU A N   1 
ATOM   3634  C CA  . LEU A 1 429 ? 16.846  -8.094  -15.705 1.00 49.52  ? 429 LEU A CA  1 
ATOM   3635  C C   . LEU A 1 429 ? 16.012  -9.003  -16.595 1.00 50.11  ? 429 LEU A C   1 
ATOM   3636  O O   . LEU A 1 429 ? 16.035  -10.229 -16.436 1.00 52.35  ? 429 LEU A O   1 
ATOM   3637  C CB  . LEU A 1 429 ? 15.979  -7.414  -14.644 1.00 51.08  ? 429 LEU A CB  1 
ATOM   3638  C CG  . LEU A 1 429 ? 15.476  -8.299  -13.501 1.00 54.57  ? 429 LEU A CG  1 
ATOM   3639  C CD1 . LEU A 1 429 ? 16.645  -9.012  -12.848 1.00 54.77  ? 429 LEU A CD1 1 
ATOM   3640  C CD2 . LEU A 1 429 ? 14.669  -7.513  -12.462 1.00 54.36  ? 429 LEU A CD2 1 
ATOM   3641  N N   . ILE A 1 430 ? 15.276  -8.421  -17.548 1.00 51.93  ? 430 ILE A N   1 
ATOM   3642  C CA  . ILE A 1 430 ? 14.395  -9.222  -18.397 1.00 58.03  ? 430 ILE A CA  1 
ATOM   3643  C C   . ILE A 1 430 ? 15.211  -10.215 -19.211 1.00 60.74  ? 430 ILE A C   1 
ATOM   3644  O O   . ILE A 1 430 ? 14.899  -11.411 -19.263 1.00 64.38  ? 430 ILE A O   1 
ATOM   3645  C CB  . ILE A 1 430 ? 13.544  -8.316  -19.306 1.00 60.75  ? 430 ILE A CB  1 
ATOM   3646  C CG1 . ILE A 1 430 ? 12.519  -7.542  -18.482 1.00 54.79  ? 430 ILE A CG1 1 
ATOM   3647  C CG2 . ILE A 1 430 ? 12.832  -9.130  -20.378 1.00 59.27  ? 430 ILE A CG2 1 
ATOM   3648  C CD1 . ILE A 1 430 ? 12.087  -6.255  -19.137 1.00 65.06  ? 430 ILE A CD1 1 
ATOM   3649  N N   . GLU A 1 431 ? 16.279  -9.729  -19.846 1.00 61.39  ? 431 GLU A N   1 
ATOM   3650  C CA  . GLU A 1 431 ? 17.125  -10.596 -20.656 1.00 59.28  ? 431 GLU A CA  1 
ATOM   3651  C C   . GLU A 1 431 ? 17.798  -11.659 -19.804 1.00 58.55  ? 431 GLU A C   1 
ATOM   3652  O O   . GLU A 1 431 ? 18.007  -12.789 -20.257 1.00 68.86  ? 431 GLU A O   1 
ATOM   3653  C CB  . GLU A 1 431 ? 18.169  -9.762  -21.394 1.00 57.01  ? 431 GLU A CB  1 
ATOM   3654  C CG  . GLU A 1 431 ? 17.635  -9.104  -22.643 1.00 59.72  ? 431 GLU A CG  1 
ATOM   3655  C CD  . GLU A 1 431 ? 17.421  -10.099 -23.769 1.00 72.28  ? 431 GLU A CD  1 
ATOM   3656  O OE1 . GLU A 1 431 ? 18.077  -11.162 -23.758 1.00 69.99  ? 431 GLU A OE1 1 
ATOM   3657  O OE2 . GLU A 1 431 ? 16.608  -9.815  -24.673 1.00 77.93  ? 431 GLU A OE2 1 
ATOM   3658  N N   . ALA A 1 432 ? 18.145  -11.319 -18.566 1.00 49.51  ? 432 ALA A N   1 
ATOM   3659  C CA  . ALA A 1 432 ? 18.765  -12.315 -17.707 1.00 53.52  ? 432 ALA A CA  1 
ATOM   3660  C C   . ALA A 1 432 ? 17.748  -13.353 -17.246 1.00 67.12  ? 432 ALA A C   1 
ATOM   3661  O O   . ALA A 1 432 ? 18.044  -14.553 -17.246 1.00 75.18  ? 432 ALA A O   1 
ATOM   3662  C CB  . ALA A 1 432 ? 19.438  -11.641 -16.519 1.00 52.44  ? 432 ALA A CB  1 
ATOM   3663  N N   . LYS A 1 433 ? 16.537  -12.917 -16.873 1.00 58.99  ? 433 LYS A N   1 
ATOM   3664  C CA  . LYS A 1 433 ? 15.514  -13.865 -16.438 1.00 57.30  ? 433 LYS A CA  1 
ATOM   3665  C C   . LYS A 1 433 ? 15.223  -14.901 -17.516 1.00 60.04  ? 433 LYS A C   1 
ATOM   3666  O O   . LYS A 1 433 ? 14.914  -16.056 -17.199 1.00 64.52  ? 433 LYS A O   1 
ATOM   3667  C CB  . LYS A 1 433 ? 14.237  -13.120 -16.042 1.00 65.82  ? 433 LYS A CB  1 
ATOM   3668  C CG  . LYS A 1 433 ? 13.131  -14.000 -15.453 1.00 59.98  ? 433 LYS A CG  1 
ATOM   3669  C CD  . LYS A 1 433 ? 13.649  -14.854 -14.311 1.00 55.85  ? 433 LYS A CD  1 
ATOM   3670  C CE  . LYS A 1 433 ? 12.894  -16.174 -14.212 1.00 65.31  ? 433 LYS A CE  1 
ATOM   3671  N NZ  . LYS A 1 433 ? 11.415  -15.997 -14.254 1.00 62.23  ? 433 LYS A NZ  1 
ATOM   3672  N N   . LYS A 1 434 ? 15.341  -14.516 -18.792 1.00 63.58  ? 434 LYS A N   1 
ATOM   3673  C CA  . LYS A 1 434 ? 15.230  -15.487 -19.878 1.00 65.42  ? 434 LYS A CA  1 
ATOM   3674  C C   . LYS A 1 434 ? 16.294  -16.566 -19.778 1.00 64.92  ? 434 LYS A C   1 
ATOM   3675  O O   . LYS A 1 434 ? 16.106  -17.676 -20.288 1.00 68.97  ? 434 LYS A O   1 
ATOM   3676  C CB  . LYS A 1 434 ? 15.348  -14.796 -21.232 1.00 54.09  ? 434 LYS A CB  1 
ATOM   3677  C CG  . LYS A 1 434 ? 14.246  -13.818 -21.523 1.00 52.42  ? 434 LYS A CG  1 
ATOM   3678  C CD  . LYS A 1 434 ? 14.127  -13.584 -23.013 1.00 61.74  ? 434 LYS A CD  1 
ATOM   3679  C CE  . LYS A 1 434 ? 14.494  -12.155 -23.352 1.00 65.04  ? 434 LYS A CE  1 
ATOM   3680  N NZ  . LYS A 1 434 ? 14.051  -11.245 -22.266 1.00 65.80  ? 434 LYS A NZ  1 
ATOM   3681  N N   . LYS A 1 435 ? 17.419  -16.259 -19.142 1.00 60.67  ? 435 LYS A N   1 
ATOM   3682  C CA  . LYS A 1 435 ? 18.520  -17.197 -19.020 1.00 59.92  ? 435 LYS A CA  1 
ATOM   3683  C C   . LYS A 1 435 ? 18.790  -17.584 -17.574 1.00 59.09  ? 435 LYS A C   1 
ATOM   3684  O O   . LYS A 1 435 ? 19.807  -18.222 -17.296 1.00 66.41  ? 435 LYS A O   1 
ATOM   3685  C CB  . LYS A 1 435 ? 19.773  -16.598 -19.660 1.00 66.55  ? 435 LYS A CB  1 
ATOM   3686  C CG  . LYS A 1 435 ? 19.509  -15.895 -20.996 1.00 67.90  ? 435 LYS A CG  1 
ATOM   3687  C CD  . LYS A 1 435 ? 20.745  -15.146 -21.481 1.00 63.83  ? 435 LYS A CD  1 
ATOM   3688  C CE  . LYS A 1 435 ? 20.891  -15.214 -22.990 1.00 57.83  ? 435 LYS A CE  1 
ATOM   3689  N NZ  . LYS A 1 435 ? 20.471  -16.540 -23.508 1.00 61.59  ? 435 LYS A NZ  1 
ATOM   3690  N N   . ALA A 1 436 ? 17.905  -17.225 -16.648 1.00 65.74  ? 436 ALA A N   1 
ATOM   3691  C CA  . ALA A 1 436 ? 18.221  -17.369 -15.230 1.00 66.64  ? 436 ALA A CA  1 
ATOM   3692  C C   . ALA A 1 436 ? 18.116  -18.829 -14.809 1.00 64.42  ? 436 ALA A C   1 
ATOM   3693  O O   . ALA A 1 436 ? 17.055  -19.447 -14.938 1.00 70.59  ? 436 ALA A O   1 
ATOM   3694  C CB  . ALA A 1 436 ? 17.303  -16.492 -14.381 1.00 58.54  ? 436 ALA A CB  1 
ATOM   3695  N N   . LYS A 1 437 ? 19.218  -19.380 -14.308 1.00 69.03  ? 437 LYS A N   1 
ATOM   3696  C CA  . LYS A 1 437 ? 19.268  -20.776 -13.914 1.00 68.76  ? 437 LYS A CA  1 
ATOM   3697  C C   . LYS A 1 437 ? 19.280  -20.977 -12.406 1.00 63.71  ? 437 LYS A C   1 
ATOM   3698  O O   . LYS A 1 437 ? 19.205  -22.125 -11.954 1.00 62.73  ? 437 LYS A O   1 
ATOM   3699  C CB  . LYS A 1 437 ? 20.497  -21.458 -14.537 1.00 70.50  ? 437 LYS A CB  1 
ATOM   3700  C CG  . LYS A 1 437 ? 20.393  -21.686 -16.052 1.00 73.37  ? 437 LYS A CG  1 
ATOM   3701  C CD  . LYS A 1 437 ? 19.978  -23.124 -16.405 1.00 77.19  ? 437 LYS A CD  1 
ATOM   3702  C CE  . LYS A 1 437 ? 18.498  -23.395 -16.122 1.00 87.03  ? 437 LYS A CE  1 
ATOM   3703  N NZ  . LYS A 1 437 ? 18.168  -24.844 -15.927 1.00 85.33  ? 437 LYS A NZ  1 
ATOM   3704  N N   . ASN A 1 438 ? 19.368  -19.901 -11.620 1.00 62.14  ? 438 ASN A N   1 
ATOM   3705  C CA  . ASN A 1 438 ? 19.318  -19.974 -10.163 1.00 70.05  ? 438 ASN A CA  1 
ATOM   3706  C C   . ASN A 1 438 ? 18.480  -18.813 -9.637  1.00 68.88  ? 438 ASN A C   1 
ATOM   3707  O O   . ASN A 1 438 ? 17.988  -17.977 -10.400 1.00 65.63  ? 438 ASN A O   1 
ATOM   3708  C CB  . ASN A 1 438 ? 20.722  -19.967 -9.545  1.00 65.83  ? 438 ASN A CB  1 
ATOM   3709  C CG  . ASN A 1 438 ? 21.570  -18.812 -10.030 1.00 70.12  ? 438 ASN A CG  1 
ATOM   3710  O OD1 . ASN A 1 438 ? 21.563  -17.735 -9.436  1.00 70.37  ? 438 ASN A OD1 1 
ATOM   3711  N ND2 . ASN A 1 438 ? 22.323  -19.035 -11.102 1.00 71.31  ? 438 ASN A ND2 1 
ATOM   3712  N N   . ASP A 1 439 ? 18.315  -18.760 -8.319  1.00 69.73  ? 439 ASP A N   1 
ATOM   3713  C CA  . ASP A 1 439 ? 17.429  -17.773 -7.714  1.00 72.51  ? 439 ASP A CA  1 
ATOM   3714  C C   . ASP A 1 439 ? 18.131  -16.471 -7.360  1.00 66.31  ? 439 ASP A C   1 
ATOM   3715  O O   . ASP A 1 439 ? 17.521  -15.617 -6.707  1.00 65.72  ? 439 ASP A O   1 
ATOM   3716  C CB  . ASP A 1 439 ? 16.750  -18.344 -6.465  1.00 73.65  ? 439 ASP A CB  1 
ATOM   3717  C CG  . ASP A 1 439 ? 16.193  -19.728 -6.688  1.00 86.42  ? 439 ASP A CG  1 
ATOM   3718  O OD1 . ASP A 1 439 ? 16.962  -20.608 -7.131  1.00 104.92 ? 439 ASP A OD1 1 
ATOM   3719  O OD2 . ASP A 1 439 ? 14.991  -19.939 -6.414  1.00 101.54 ? 439 ASP A OD2 1 
ATOM   3720  N N   . TYR A 1 440 ? 19.386  -16.286 -7.785  1.00 66.40  ? 440 TYR A N   1 
ATOM   3721  C CA  . TYR A 1 440 ? 19.987  -14.962 -7.688  1.00 62.04  ? 440 TYR A CA  1 
ATOM   3722  C C   . TYR A 1 440 ? 19.243  -13.950 -8.544  1.00 62.11  ? 440 TYR A C   1 
ATOM   3723  O O   . TYR A 1 440 ? 19.474  -12.746 -8.394  1.00 67.67  ? 440 TYR A O   1 
ATOM   3724  C CB  . TYR A 1 440 ? 21.477  -14.985 -8.076  1.00 58.70  ? 440 TYR A CB  1 
ATOM   3725  C CG  . TYR A 1 440 ? 22.390  -15.168 -6.879  1.00 63.89  ? 440 TYR A CG  1 
ATOM   3726  C CD1 . TYR A 1 440 ? 22.687  -14.105 -6.027  1.00 63.66  ? 440 TYR A CD1 1 
ATOM   3727  C CD2 . TYR A 1 440 ? 22.931  -16.411 -6.582  1.00 59.94  ? 440 TYR A CD2 1 
ATOM   3728  C CE1 . TYR A 1 440 ? 23.508  -14.281 -4.915  1.00 50.05  ? 440 TYR A CE1 1 
ATOM   3729  C CE2 . TYR A 1 440 ? 23.753  -16.594 -5.482  1.00 63.85  ? 440 TYR A CE2 1 
ATOM   3730  C CZ  . TYR A 1 440 ? 24.037  -15.532 -4.650  1.00 57.87  ? 440 TYR A CZ  1 
ATOM   3731  O OH  . TYR A 1 440 ? 24.855  -15.737 -3.561  1.00 58.38  ? 440 TYR A OH  1 
ATOM   3732  N N   . ILE A 1 441 ? 18.346  -14.407 -9.420  1.00 56.82  ? 441 ILE A N   1 
ATOM   3733  C CA  . ILE A 1 441 ? 17.487  -13.475 -10.138 1.00 62.63  ? 441 ILE A CA  1 
ATOM   3734  C C   . ILE A 1 441 ? 16.608  -12.704 -9.159  1.00 59.32  ? 441 ILE A C   1 
ATOM   3735  O O   . ILE A 1 441 ? 16.323  -11.520 -9.375  1.00 54.42  ? 441 ILE A O   1 
ATOM   3736  C CB  . ILE A 1 441 ? 16.655  -14.226 -11.206 1.00 50.56  ? 441 ILE A CB  1 
ATOM   3737  C CG1 . ILE A 1 441 ? 16.153  -13.265 -12.284 1.00 52.89  ? 441 ILE A CG1 1 
ATOM   3738  C CG2 . ILE A 1 441 ? 15.497  -14.972 -10.586 1.00 57.04  ? 441 ILE A CG2 1 
ATOM   3739  C CD1 . ILE A 1 441 ? 17.252  -12.662 -13.122 1.00 47.12  ? 441 ILE A CD1 1 
ATOM   3740  N N   . LEU A 1 442 ? 16.202  -13.341 -8.051  1.00 54.90  ? 442 LEU A N   1 
ATOM   3741  C CA  . LEU A 1 442 ? 15.328  -12.685 -7.083  1.00 58.48  ? 442 LEU A CA  1 
ATOM   3742  C C   . LEU A 1 442 ? 16.039  -11.552 -6.353  1.00 60.44  ? 442 LEU A C   1 
ATOM   3743  O O   . LEU A 1 442 ? 15.414  -10.535 -6.032  1.00 61.97  ? 442 LEU A O   1 
ATOM   3744  C CB  . LEU A 1 442 ? 14.788  -13.706 -6.076  1.00 63.26  ? 442 LEU A CB  1 
ATOM   3745  C CG  . LEU A 1 442 ? 14.123  -14.964 -6.645  1.00 62.22  ? 442 LEU A CG  1 
ATOM   3746  C CD1 . LEU A 1 442 ? 13.564  -15.857 -5.546  1.00 50.40  ? 442 LEU A CD1 1 
ATOM   3747  C CD2 . LEU A 1 442 ? 13.036  -14.589 -7.624  1.00 58.85  ? 442 LEU A CD2 1 
ATOM   3748  N N   . VAL A 1 443 ? 17.334  -11.708 -6.070  1.00 58.12  ? 443 VAL A N   1 
ATOM   3749  C CA  . VAL A 1 443 ? 18.108  -10.603 -5.512  1.00 53.43  ? 443 VAL A CA  1 
ATOM   3750  C C   . VAL A 1 443 ? 18.094  -9.410  -6.458  1.00 53.48  ? 443 VAL A C   1 
ATOM   3751  O O   . VAL A 1 443 ? 17.911  -8.265  -6.030  1.00 59.04  ? 443 VAL A O   1 
ATOM   3752  C CB  . VAL A 1 443 ? 19.539  -11.070 -5.201  1.00 55.28  ? 443 VAL A CB  1 
ATOM   3753  C CG1 . VAL A 1 443 ? 20.236  -10.102 -4.239  1.00 42.24  ? 443 VAL A CG1 1 
ATOM   3754  C CG2 . VAL A 1 443 ? 19.486  -12.475 -4.629  1.00 60.21  ? 443 VAL A CG2 1 
ATOM   3755  N N   . ALA A 1 444 ? 18.258  -9.657  -7.760  1.00 53.09  ? 444 ALA A N   1 
ATOM   3756  C CA  . ALA A 1 444 ? 18.328  -8.569  -8.732  1.00 55.37  ? 444 ALA A CA  1 
ATOM   3757  C C   . ALA A 1 444 ? 16.989  -7.879  -8.969  1.00 55.95  ? 444 ALA A C   1 
ATOM   3758  O O   . ALA A 1 444 ? 16.979  -6.780  -9.537  1.00 49.66  ? 444 ALA A O   1 
ATOM   3759  C CB  . ALA A 1 444 ? 18.879  -9.086  -10.061 1.00 55.79  ? 444 ALA A CB  1 
ATOM   3760  N N   . GLU A 1 445 ? 15.870  -8.486  -8.565  1.00 57.86  ? 445 GLU A N   1 
ATOM   3761  C CA  . GLU A 1 445 ? 14.563  -7.845  -8.648  1.00 52.83  ? 445 GLU A CA  1 
ATOM   3762  C C   . GLU A 1 445 ? 14.268  -6.967  -7.434  1.00 52.94  ? 445 GLU A C   1 
ATOM   3763  O O   . GLU A 1 445 ? 13.124  -6.534  -7.258  1.00 57.86  ? 445 GLU A O   1 
ATOM   3764  C CB  . GLU A 1 445 ? 13.454  -8.898  -8.819  1.00 52.69  ? 445 GLU A CB  1 
ATOM   3765  C CG  . GLU A 1 445 ? 13.687  -9.918  -9.935  1.00 55.43  ? 445 GLU A CG  1 
ATOM   3766  C CD  . GLU A 1 445 ? 12.809  -11.157 -9.792  1.00 63.85  ? 445 GLU A CD  1 
ATOM   3767  O OE1 . GLU A 1 445 ? 11.595  -11.006 -9.551  1.00 69.54  ? 445 GLU A OE1 1 
ATOM   3768  O OE2 . GLU A 1 445 ? 13.332  -12.286 -9.918  1.00 70.13  ? 445 GLU A OE2 1 
ATOM   3769  N N   . GLY A 1 446 ? 15.272  -6.694  -6.603  1.00 49.49  ? 446 GLY A N   1 
ATOM   3770  C CA  . GLY A 1 446 ? 15.062  -5.855  -5.441  1.00 49.69  ? 446 GLY A CA  1 
ATOM   3771  C C   . GLY A 1 446 ? 14.904  -4.394  -5.815  1.00 53.81  ? 446 GLY A C   1 
ATOM   3772  O O   . GLY A 1 446 ? 15.442  -3.918  -6.815  1.00 58.37  ? 446 GLY A O   1 
ATOM   3773  N N   . SER A 1 447 ? 14.151  -3.670  -4.987  1.00 54.68  ? 447 SER A N   1 
ATOM   3774  C CA  . SER A 1 447 ? 13.810  -2.294  -5.332  1.00 60.01  ? 447 SER A CA  1 
ATOM   3775  C C   . SER A 1 447 ? 15.018  -1.367  -5.243  1.00 59.41  ? 447 SER A C   1 
ATOM   3776  O O   . SER A 1 447 ? 15.104  -0.392  -6.000  1.00 60.30  ? 447 SER A O   1 
ATOM   3777  C CB  . SER A 1 447 ? 12.659  -1.803  -4.443  1.00 52.15  ? 447 SER A CB  1 
ATOM   3778  O OG  . SER A 1 447 ? 13.115  -1.314  -3.190  1.00 57.67  ? 447 SER A OG  1 
ATOM   3779  N N   . ASP A 1 448 ? 15.973  -1.669  -4.359  1.00 49.24  ? 448 ASP A N   1 
ATOM   3780  C CA  . ASP A 1 448 ? 17.048  -0.720  -4.081  1.00 50.27  ? 448 ASP A CA  1 
ATOM   3781  C C   . ASP A 1 448 ? 17.927  -0.490  -5.304  1.00 57.04  ? 448 ASP A C   1 
ATOM   3782  O O   . ASP A 1 448 ? 18.336  0.645   -5.573  1.00 59.33  ? 448 ASP A O   1 
ATOM   3783  C CB  . ASP A 1 448 ? 17.874  -1.210  -2.891  1.00 53.88  ? 448 ASP A CB  1 
ATOM   3784  C CG  . ASP A 1 448 ? 17.003  -1.667  -1.734  1.00 61.97  ? 448 ASP A CG  1 
ATOM   3785  O OD1 . ASP A 1 448 ? 16.446  -2.785  -1.810  1.00 66.27  ? 448 ASP A OD1 1 
ATOM   3786  O OD2 . ASP A 1 448 ? 16.860  -0.903  -0.753  1.00 60.21  ? 448 ASP A OD2 1 
ATOM   3787  N N   . TRP A 1 449 ? 18.208  -1.547  -6.071  1.00 53.36  ? 449 TRP A N   1 
ATOM   3788  C CA  . TRP A 1 449 ? 19.052  -1.402  -7.253  1.00 46.40  ? 449 TRP A CA  1 
ATOM   3789  C C   . TRP A 1 449 ? 18.483  -0.358  -8.206  1.00 50.20  ? 449 TRP A C   1 
ATOM   3790  O O   . TRP A 1 449 ? 19.216  0.475   -8.749  1.00 67.15  ? 449 TRP A O   1 
ATOM   3791  C CB  . TRP A 1 449 ? 19.204  -2.749  -7.963  1.00 52.14  ? 449 TRP A CB  1 
ATOM   3792  C CG  . TRP A 1 449 ? 19.428  -3.920  -7.044  1.00 53.40  ? 449 TRP A CG  1 
ATOM   3793  C CD1 . TRP A 1 449 ? 18.675  -5.061  -6.974  1.00 47.13  ? 449 TRP A CD1 1 
ATOM   3794  C CD2 . TRP A 1 449 ? 20.475  -4.072  -6.067  1.00 51.64  ? 449 TRP A CD2 1 
ATOM   3795  N NE1 . TRP A 1 449 ? 19.185  -5.905  -6.014  1.00 45.82  ? 449 TRP A NE1 1 
ATOM   3796  C CE2 . TRP A 1 449 ? 20.286  -5.324  -5.442  1.00 47.18  ? 449 TRP A CE2 1 
ATOM   3797  C CE3 . TRP A 1 449 ? 21.546  -3.271  -5.659  1.00 43.46  ? 449 TRP A CE3 1 
ATOM   3798  C CZ2 . TRP A 1 449 ? 21.128  -5.791  -4.432  1.00 44.46  ? 449 TRP A CZ2 1 
ATOM   3799  C CZ3 . TRP A 1 449 ? 22.378  -3.738  -4.660  1.00 46.54  ? 449 TRP A CZ3 1 
ATOM   3800  C CH2 . TRP A 1 449 ? 22.166  -4.987  -4.059  1.00 46.79  ? 449 TRP A CH2 1 
ATOM   3801  N N   . PHE A 1 450 ? 17.172  -0.379  -8.416  1.00 49.91  ? 450 PHE A N   1 
ATOM   3802  C CA  . PHE A 1 450 ? 16.585  0.541   -9.381  1.00 56.42  ? 450 PHE A CA  1 
ATOM   3803  C C   . PHE A 1 450 ? 16.481  1.949   -8.812  1.00 56.29  ? 450 PHE A C   1 
ATOM   3804  O O   . PHE A 1 450 ? 16.448  2.928   -9.569  1.00 59.50  ? 450 PHE A O   1 
ATOM   3805  C CB  . PHE A 1 450 ? 15.213  0.026   -9.822  1.00 60.38  ? 450 PHE A CB  1 
ATOM   3806  C CG  . PHE A 1 450 ? 15.235  -1.384  -10.366 1.00 64.29  ? 450 PHE A CG  1 
ATOM   3807  C CD1 . PHE A 1 450 ? 15.605  -1.636  -11.678 1.00 68.28  ? 450 PHE A CD1 1 
ATOM   3808  C CD2 . PHE A 1 450 ? 14.910  -2.462  -9.552  1.00 66.48  ? 450 PHE A CD2 1 
ATOM   3809  C CE1 . PHE A 1 450 ? 15.623  -2.940  -12.179 1.00 68.81  ? 450 PHE A CE1 1 
ATOM   3810  C CE2 . PHE A 1 450 ? 14.931  -3.766  -10.048 1.00 67.08  ? 450 PHE A CE2 1 
ATOM   3811  C CZ  . PHE A 1 450 ? 15.289  -3.999  -11.366 1.00 61.49  ? 450 PHE A CZ  1 
ATOM   3812  N N   . TRP A 1 451 ? 16.450  2.067   -7.484  1.00 56.17  ? 451 TRP A N   1 
ATOM   3813  C CA  . TRP A 1 451 ? 16.266  3.366   -6.848  1.00 59.96  ? 451 TRP A CA  1 
ATOM   3814  C C   . TRP A 1 451 ? 17.456  4.274   -7.124  1.00 61.85  ? 451 TRP A C   1 
ATOM   3815  O O   . TRP A 1 451 ? 17.289  5.444   -7.491  1.00 66.07  ? 451 TRP A O   1 
ATOM   3816  C CB  . TRP A 1 451 ? 16.043  3.163   -5.342  1.00 59.47  ? 451 TRP A CB  1 
ATOM   3817  C CG  . TRP A 1 451 ? 16.028  4.400   -4.477  1.00 63.45  ? 451 TRP A CG  1 
ATOM   3818  C CD1 . TRP A 1 451 ? 17.082  5.223   -4.205  1.00 65.27  ? 451 TRP A CD1 1 
ATOM   3819  C CD2 . TRP A 1 451 ? 14.914  4.924   -3.739  1.00 66.60  ? 451 TRP A CD2 1 
ATOM   3820  N NE1 . TRP A 1 451 ? 16.693  6.232   -3.362  1.00 69.44  ? 451 TRP A NE1 1 
ATOM   3821  C CE2 . TRP A 1 451 ? 15.367  6.071   -3.058  1.00 70.34  ? 451 TRP A CE2 1 
ATOM   3822  C CE3 . TRP A 1 451 ? 13.576  4.538   -3.593  1.00 68.66  ? 451 TRP A CE3 1 
ATOM   3823  C CZ2 . TRP A 1 451 ? 14.531  6.839   -2.246  1.00 74.60  ? 451 TRP A CZ2 1 
ATOM   3824  C CZ3 . TRP A 1 451 ? 12.745  5.304   -2.781  1.00 71.28  ? 451 TRP A CZ3 1 
ATOM   3825  C CH2 . TRP A 1 451 ? 13.228  6.440   -2.121  1.00 74.97  ? 451 TRP A CH2 1 
ATOM   3826  N N   . TRP A 1 452 ? 18.668  3.737   -6.990  1.00 59.29  ? 452 TRP A N   1 
ATOM   3827  C CA  . TRP A 1 452 ? 19.880  4.540   -7.057  1.00 61.31  ? 452 TRP A CA  1 
ATOM   3828  C C   . TRP A 1 452 ? 20.302  4.886   -8.473  1.00 64.37  ? 452 TRP A C   1 
ATOM   3829  O O   . TRP A 1 452 ? 21.265  5.641   -8.641  1.00 69.85  ? 452 TRP A O   1 
ATOM   3830  C CB  . TRP A 1 452 ? 21.029  3.815   -6.358  1.00 58.52  ? 452 TRP A CB  1 
ATOM   3831  C CG  . TRP A 1 452 ? 20.767  3.558   -4.915  1.00 60.06  ? 452 TRP A CG  1 
ATOM   3832  C CD1 . TRP A 1 452 ? 20.512  2.353   -4.329  1.00 56.20  ? 452 TRP A CD1 1 
ATOM   3833  C CD2 . TRP A 1 452 ? 20.732  4.532   -3.864  1.00 60.98  ? 452 TRP A CD2 1 
ATOM   3834  N NE1 . TRP A 1 452 ? 20.320  2.516   -2.981  1.00 55.34  ? 452 TRP A NE1 1 
ATOM   3835  C CE2 . TRP A 1 452 ? 20.450  3.844   -2.669  1.00 59.28  ? 452 TRP A CE2 1 
ATOM   3836  C CE3 . TRP A 1 452 ? 20.913  5.919   -3.817  1.00 65.70  ? 452 TRP A CE3 1 
ATOM   3837  C CZ2 . TRP A 1 452 ? 20.343  4.493   -1.441  1.00 61.98  ? 452 TRP A CZ2 1 
ATOM   3838  C CZ3 . TRP A 1 452 ? 20.808  6.564   -2.595  1.00 68.46  ? 452 TRP A CZ3 1 
ATOM   3839  C CH2 . TRP A 1 452 ? 20.527  5.850   -1.425  1.00 66.51  ? 452 TRP A CH2 1 
ATOM   3840  N N   . GLN A 1 453 ? 19.612  4.375   -9.485  1.00 64.21  ? 453 GLN A N   1 
ATOM   3841  C CA  . GLN A 1 453 ? 20.105  4.433   -10.854 1.00 68.61  ? 453 GLN A CA  1 
ATOM   3842  C C   . GLN A 1 453 ? 19.660  5.724   -11.526 1.00 76.55  ? 453 GLN A C   1 
ATOM   3843  O O   . GLN A 1 453 ? 18.466  5.942   -11.749 1.00 87.54  ? 453 GLN A O   1 
ATOM   3844  C CB  . GLN A 1 453 ? 19.635  3.217   -11.640 1.00 68.46  ? 453 GLN A CB  1 
ATOM   3845  C CG  . GLN A 1 453 ? 20.562  2.046   -11.469 1.00 75.64  ? 453 GLN A CG  1 
ATOM   3846  C CD  . GLN A 1 453 ? 22.014  2.388   -11.782 1.00 82.80  ? 453 GLN A CD  1 
ATOM   3847  O OE1 . GLN A 1 453 ? 22.369  2.633   -12.935 1.00 90.14  ? 453 GLN A OE1 1 
ATOM   3848  N NE2 . GLN A 1 453 ? 22.861  2.391   -10.754 1.00 79.13  ? 453 GLN A NE2 1 
ATOM   3849  N N   . GLY A 1 454 ? 20.630  6.574   -11.854 1.00 79.47  ? 454 GLY A N   1 
ATOM   3850  C CA  . GLY A 1 454 ? 20.411  7.694   -12.734 1.00 76.89  ? 454 GLY A CA  1 
ATOM   3851  C C   . GLY A 1 454 ? 19.707  8.886   -12.134 1.00 95.27  ? 454 GLY A C   1 
ATOM   3852  O O   . GLY A 1 454 ? 19.613  9.919   -12.807 1.00 106.30 ? 454 GLY A O   1 
ATOM   3853  N N   . GLU A 1 455 ? 19.212  8.795   -10.900 1.00 103.05 ? 455 GLU A N   1 
ATOM   3854  C CA  . GLU A 1 455 ? 18.459  9.906   -10.327 1.00 112.34 ? 455 GLU A CA  1 
ATOM   3855  C C   . GLU A 1 455 ? 19.333  11.148  -10.182 1.00 122.26 ? 455 GLU A C   1 
ATOM   3856  O O   . GLU A 1 455 ? 19.068  12.173  -10.819 1.00 125.45 ? 455 GLU A O   1 
ATOM   3857  C CB  . GLU A 1 455 ? 17.843  9.503   -8.984  1.00 107.06 ? 455 GLU A CB  1 
ATOM   3858  C CG  . GLU A 1 455 ? 16.621  10.334  -8.569  1.00 114.22 ? 455 GLU A CG  1 
ATOM   3859  C CD  . GLU A 1 455 ? 15.396  10.136  -9.463  1.00 117.78 ? 455 GLU A CD  1 
ATOM   3860  O OE1 . GLU A 1 455 ? 15.479  10.390  -10.685 1.00 125.60 ? 455 GLU A OE1 1 
ATOM   3861  O OE2 . GLU A 1 455 ? 14.332  9.753   -8.933  1.00 103.65 ? 455 GLU A OE2 1 
ATOM   3862  N N   . GLU A 1 456 ? 20.375  11.070  -9.357  1.00 124.46 ? 456 GLU A N   1 
ATOM   3863  C CA  . GLU A 1 456 ? 21.352  12.145  -9.233  1.00 128.74 ? 456 GLU A CA  1 
ATOM   3864  C C   . GLU A 1 456 ? 22.666  11.538  -8.761  1.00 132.66 ? 456 GLU A C   1 
ATOM   3865  O O   . GLU A 1 456 ? 22.755  10.334  -8.491  1.00 126.08 ? 456 GLU A O   1 
ATOM   3866  C CB  . GLU A 1 456 ? 20.858  13.252  -8.284  1.00 122.95 ? 456 GLU A CB  1 
ATOM   3867  C CG  . GLU A 1 456 ? 20.636  12.809  -6.838  1.00 121.58 ? 456 GLU A CG  1 
ATOM   3868  C CD  . GLU A 1 456 ? 19.289  12.149  -6.622  1.00 126.63 ? 456 GLU A CD  1 
ATOM   3869  O OE1 . GLU A 1 456 ? 18.253  12.822  -6.820  1.00 128.83 ? 456 GLU A OE1 1 
ATOM   3870  O OE2 . GLU A 1 456 ? 19.271  10.952  -6.263  1.00 121.30 ? 456 GLU A OE2 1 
ATOM   3871  N N   . LYS A 1 457 ? 23.697  12.383  -8.681  1.00 128.63 ? 457 LYS A N   1 
ATOM   3872  C CA  . LYS A 1 457 ? 24.975  11.961  -8.120  1.00 122.50 ? 457 LYS A CA  1 
ATOM   3873  C C   . LYS A 1 457 ? 24.801  11.760  -6.619  1.00 121.70 ? 457 LYS A C   1 
ATOM   3874  O O   . LYS A 1 457 ? 24.400  12.682  -5.894  1.00 125.07 ? 457 LYS A O   1 
ATOM   3875  C CB  . LYS A 1 457 ? 26.070  12.989  -8.428  1.00 126.64 ? 457 LYS A CB  1 
ATOM   3876  C CG  . LYS A 1 457 ? 27.500  12.560  -8.073  1.00 114.36 ? 457 LYS A CG  1 
ATOM   3877  C CD  . LYS A 1 457 ? 27.638  11.046  -7.973  1.00 116.72 ? 457 LYS A CD  1 
ATOM   3878  C CE  . LYS A 1 457 ? 29.074  10.598  -7.768  1.00 117.55 ? 457 LYS A CE  1 
ATOM   3879  N NZ  . LYS A 1 457 ? 29.129  9.108   -7.658  1.00 101.03 ? 457 LYS A NZ  1 
ATOM   3880  N N   . ALA A 1 458 ? 25.108  10.554  -6.164  1.00 115.60 ? 458 ALA A N   1 
ATOM   3881  C CA  . ALA A 1 458 ? 24.718  10.096  -4.841  1.00 112.46 ? 458 ALA A CA  1 
ATOM   3882  C C   . ALA A 1 458 ? 25.835  9.205   -4.315  1.00 109.51 ? 458 ALA A C   1 
ATOM   3883  O O   . ALA A 1 458 ? 26.765  8.854   -5.055  1.00 107.40 ? 458 ALA A O   1 
ATOM   3884  C CB  . ALA A 1 458 ? 23.375  9.350   -4.908  1.00 106.07 ? 458 ALA A CB  1 
ATOM   3885  N N   . PRO A 1 459 ? 25.777  8.810   -3.037  1.00 107.41 ? 459 PRO A N   1 
ATOM   3886  C CA  . PRO A 1 459 ? 26.916  8.096   -2.438  1.00 99.80  ? 459 PRO A CA  1 
ATOM   3887  C C   . PRO A 1 459 ? 26.901  6.612   -2.789  1.00 90.58  ? 459 PRO A C   1 
ATOM   3888  O O   . PRO A 1 459 ? 25.856  5.950   -2.744  1.00 88.75  ? 459 PRO A O   1 
ATOM   3889  C CB  . PRO A 1 459 ? 26.719  8.320   -0.925  1.00 95.62  ? 459 PRO A CB  1 
ATOM   3890  C CG  . PRO A 1 459 ? 25.647  9.386   -0.843  1.00 94.49  ? 459 PRO A CG  1 
ATOM   3891  C CD  . PRO A 1 459 ? 24.788  9.140   -2.001  1.00 94.13  ? 459 PRO A CD  1 
ATOM   3892  N N   . PHE A 1 460 ? 28.074  6.108   -3.172  1.00 88.16  ? 460 PHE A N   1 
ATOM   3893  C CA  . PHE A 1 460 ? 28.348  4.688   -3.349  1.00 75.70  ? 460 PHE A CA  1 
ATOM   3894  C C   . PHE A 1 460 ? 27.381  4.013   -4.299  1.00 66.75  ? 460 PHE A C   1 
ATOM   3895  O O   . PHE A 1 460 ? 27.166  2.802   -4.197  1.00 67.80  ? 460 PHE A O   1 
ATOM   3896  C CB  . PHE A 1 460 ? 28.348  3.954   -2.009  1.00 74.43  ? 460 PHE A CB  1 
ATOM   3897  C CG  . PHE A 1 460 ? 29.212  4.598   -0.974  1.00 79.62  ? 460 PHE A CG  1 
ATOM   3898  C CD1 . PHE A 1 460 ? 30.511  4.972   -1.272  1.00 71.31  ? 460 PHE A CD1 1 
ATOM   3899  C CD2 . PHE A 1 460 ? 28.724  4.833   0.297   1.00 78.55  ? 460 PHE A CD2 1 
ATOM   3900  C CE1 . PHE A 1 460 ? 31.305  5.562   -0.318  1.00 86.33  ? 460 PHE A CE1 1 
ATOM   3901  C CE2 . PHE A 1 460 ? 29.513  5.426   1.257   1.00 77.17  ? 460 PHE A CE2 1 
ATOM   3902  C CZ  . PHE A 1 460 ? 30.806  5.792   0.951   1.00 85.26  ? 460 PHE A CZ  1 
ATOM   3903  N N   . VAL A 1 461 ? 26.785  4.776   -5.217  1.00 73.19  ? 461 VAL A N   1 
ATOM   3904  C CA  . VAL A 1 461 ? 25.979  4.176   -6.275  1.00 74.56  ? 461 VAL A CA  1 
ATOM   3905  C C   . VAL A 1 461 ? 26.821  3.223   -7.104  1.00 70.90  ? 461 VAL A C   1 
ATOM   3906  O O   . VAL A 1 461 ? 26.294  2.291   -7.726  1.00 71.78  ? 461 VAL A O   1 
ATOM   3907  C CB  . VAL A 1 461 ? 25.344  5.268   -7.157  1.00 78.66  ? 461 VAL A CB  1 
ATOM   3908  C CG1 . VAL A 1 461 ? 24.432  6.147   -6.324  1.00 82.67  ? 461 VAL A CG1 1 
ATOM   3909  C CG2 . VAL A 1 461 ? 26.433  6.107   -7.829  1.00 80.22  ? 461 VAL A CG2 1 
ATOM   3910  N N   . GLU A 1 462 ? 28.136  3.447   -7.137  1.00 62.66  ? 462 GLU A N   1 
ATOM   3911  C CA  . GLU A 1 462 ? 29.045  2.492   -7.751  1.00 63.06  ? 462 GLU A CA  1 
ATOM   3912  C C   . GLU A 1 462 ? 28.855  1.106   -7.151  1.00 56.34  ? 462 GLU A C   1 
ATOM   3913  O O   . GLU A 1 462 ? 28.737  0.113   -7.876  1.00 62.32  ? 462 GLU A O   1 
ATOM   3914  C CB  . GLU A 1 462 ? 30.490  2.963   -7.567  1.00 70.09  ? 462 GLU A CB  1 
ATOM   3915  C CG  . GLU A 1 462 ? 30.663  4.477   -7.567  1.00 76.78  ? 462 GLU A CG  1 
ATOM   3916  C CD  . GLU A 1 462 ? 30.466  5.088   -8.944  1.00 90.04  ? 462 GLU A CD  1 
ATOM   3917  O OE1 . GLU A 1 462 ? 30.559  4.341   -9.941  1.00 97.00  ? 462 GLU A OE1 1 
ATOM   3918  O OE2 . GLU A 1 462 ? 30.229  6.314   -9.030  1.00 84.76  ? 462 GLU A OE2 1 
ATOM   3919  N N   . VAL A 1 463 ? 28.812  1.027   -5.819  1.00 56.16  ? 463 VAL A N   1 
ATOM   3920  C CA  . VAL A 1 463 ? 28.739  -0.264  -5.141  1.00 57.32  ? 463 VAL A CA  1 
ATOM   3921  C C   . VAL A 1 463 ? 27.433  -0.968  -5.469  1.00 52.85  ? 463 VAL A C   1 
ATOM   3922  O O   . VAL A 1 463 ? 27.391  -2.198  -5.601  1.00 51.69  ? 463 VAL A O   1 
ATOM   3923  C CB  . VAL A 1 463 ? 28.905  -0.085  -3.620  1.00 63.84  ? 463 VAL A CB  1 
ATOM   3924  C CG1 . VAL A 1 463 ? 29.219  -1.416  -2.969  1.00 57.96  ? 463 VAL A CG1 1 
ATOM   3925  C CG2 . VAL A 1 463 ? 29.996  0.922   -3.319  1.00 57.59  ? 463 VAL A CG2 1 
ATOM   3926  N N   . PHE A 1 464 ? 26.347  -0.203  -5.595  1.00 53.83  ? 464 PHE A N   1 
ATOM   3927  C CA  . PHE A 1 464 ? 25.053  -0.797  -5.910  1.00 53.73  ? 464 PHE A CA  1 
ATOM   3928  C C   . PHE A 1 464 ? 25.032  -1.350  -7.325  1.00 50.62  ? 464 PHE A C   1 
ATOM   3929  O O   . PHE A 1 464 ? 24.457  -2.416  -7.572  1.00 54.37  ? 464 PHE A O   1 
ATOM   3930  C CB  . PHE A 1 464 ? 23.941  0.231   -5.716  1.00 50.78  ? 464 PHE A CB  1 
ATOM   3931  C CG  . PHE A 1 464 ? 23.689  0.569   -4.283  1.00 49.99  ? 464 PHE A CG  1 
ATOM   3932  C CD1 . PHE A 1 464 ? 22.791  -0.172  -3.532  1.00 53.01  ? 464 PHE A CD1 1 
ATOM   3933  C CD2 . PHE A 1 464 ? 24.360  1.614   -3.678  1.00 52.83  ? 464 PHE A CD2 1 
ATOM   3934  C CE1 . PHE A 1 464 ? 22.561  0.132   -2.199  1.00 51.80  ? 464 PHE A CE1 1 
ATOM   3935  C CE2 . PHE A 1 464 ? 24.138  1.926   -2.350  1.00 55.99  ? 464 PHE A CE2 1 
ATOM   3936  C CZ  . PHE A 1 464 ? 23.236  1.182   -1.607  1.00 52.40  ? 464 PHE A CZ  1 
ATOM   3937  N N   . ASP A 1 465 ? 25.655  -0.639  -8.266  1.00 56.19  ? 465 ASP A N   1 
ATOM   3938  C CA  . ASP A 1 465 ? 25.715  -1.115  -9.644  1.00 53.51  ? 465 ASP A CA  1 
ATOM   3939  C C   . ASP A 1 465 ? 26.588  -2.357  -9.754  1.00 57.99  ? 465 ASP A C   1 
ATOM   3940  O O   . ASP A 1 465 ? 26.287  -3.267  -10.537 1.00 58.57  ? 465 ASP A O   1 
ATOM   3941  C CB  . ASP A 1 465 ? 26.224  0.007   -10.550 1.00 58.38  ? 465 ASP A CB  1 
ATOM   3942  C CG  . ASP A 1 465 ? 26.183  -0.354  -12.025 1.00 63.35  ? 465 ASP A CG  1 
ATOM   3943  O OD1 . ASP A 1 465 ? 25.084  -0.340  -12.621 1.00 59.94  ? 465 ASP A OD1 1 
ATOM   3944  O OD2 . ASP A 1 465 ? 27.263  -0.614  -12.598 1.00 65.97  ? 465 ASP A OD2 1 
ATOM   3945  N N   . LYS A 1 466 ? 27.669  -2.417  -8.967  1.00 55.82  ? 466 LYS A N   1 
ATOM   3946  C CA  . LYS A 1 466 ? 28.524  -3.601  -8.975  1.00 54.16  ? 466 LYS A CA  1 
ATOM   3947  C C   . LYS A 1 466 ? 27.766  -4.820  -8.469  1.00 52.80  ? 466 LYS A C   1 
ATOM   3948  O O   . LYS A 1 466 ? 27.885  -5.916  -9.030  1.00 54.08  ? 466 LYS A O   1 
ATOM   3949  C CB  . LYS A 1 466 ? 29.777  -3.361  -8.126  1.00 57.47  ? 466 LYS A CB  1 
ATOM   3950  C CG  . LYS A 1 466 ? 30.859  -4.450  -8.229  1.00 55.00  ? 466 LYS A CG  1 
ATOM   3951  C CD  . LYS A 1 466 ? 32.231  -3.877  -7.887  1.00 51.98  ? 466 LYS A CD  1 
ATOM   3952  C CE  . LYS A 1 466 ? 33.040  -4.823  -7.008  1.00 72.94  ? 466 LYS A CE  1 
ATOM   3953  N NZ  . LYS A 1 466 ? 34.452  -4.951  -7.466  1.00 68.92  ? 466 LYS A NZ  1 
ATOM   3954  N N   . LEU A 1 467 ? 26.974  -4.654  -7.412  1.00 54.67  ? 467 LEU A N   1 
ATOM   3955  C CA  . LEU A 1 467 ? 26.271  -5.808  -6.867  1.00 51.28  ? 467 LEU A CA  1 
ATOM   3956  C C   . LEU A 1 467 ? 25.178  -6.269  -7.814  1.00 52.44  ? 467 LEU A C   1 
ATOM   3957  O O   . LEU A 1 467 ? 25.089  -7.461  -8.130  1.00 54.92  ? 467 LEU A O   1 
ATOM   3958  C CB  . LEU A 1 467 ? 25.706  -5.492  -5.488  1.00 54.26  ? 467 LEU A CB  1 
ATOM   3959  C CG  . LEU A 1 467 ? 26.775  -5.307  -4.413  1.00 51.10  ? 467 LEU A CG  1 
ATOM   3960  C CD1 . LEU A 1 467 ? 26.254  -4.429  -3.295  1.00 49.18  ? 467 LEU A CD1 1 
ATOM   3961  C CD2 . LEU A 1 467 ? 27.199  -6.657  -3.882  1.00 45.31  ? 467 LEU A CD2 1 
ATOM   3962  N N   . PHE A 1 468 ? 24.344  -5.336  -8.285  1.00 56.67  ? 468 PHE A N   1 
ATOM   3963  C CA  . PHE A 1 468 ? 23.330  -5.665  -9.281  1.00 58.35  ? 468 PHE A CA  1 
ATOM   3964  C C   . PHE A 1 468 ? 23.929  -6.512  -10.398 1.00 61.08  ? 468 PHE A C   1 
ATOM   3965  O O   . PHE A 1 468 ? 23.549  -7.675  -10.591 1.00 57.76  ? 468 PHE A O   1 
ATOM   3966  C CB  . PHE A 1 468 ? 22.710  -4.379  -9.844  1.00 54.57  ? 468 PHE A CB  1 
ATOM   3967  C CG  . PHE A 1 468 ? 21.608  -4.621  -10.841 1.00 53.76  ? 468 PHE A CG  1 
ATOM   3968  C CD1 . PHE A 1 468 ? 20.372  -5.081  -10.420 1.00 49.13  ? 468 PHE A CD1 1 
ATOM   3969  C CD2 . PHE A 1 468 ? 21.798  -4.380  -12.193 1.00 56.48  ? 468 PHE A CD2 1 
ATOM   3970  C CE1 . PHE A 1 468 ? 19.350  -5.318  -11.325 1.00 51.69  ? 468 PHE A CE1 1 
ATOM   3971  C CE2 . PHE A 1 468 ? 20.774  -4.610  -13.110 1.00 59.88  ? 468 PHE A CE2 1 
ATOM   3972  C CZ  . PHE A 1 468 ? 19.547  -5.082  -12.670 1.00 54.39  ? 468 PHE A CZ  1 
ATOM   3973  N N   . ARG A 1 469 ? 24.925  -5.956  -11.099 1.00 60.12  ? 469 ARG A N   1 
ATOM   3974  C CA  . ARG A 1 469 ? 25.542  -6.659  -12.219 1.00 51.82  ? 469 ARG A CA  1 
ATOM   3975  C C   . ARG A 1 469 ? 26.174  -7.972  -11.784 1.00 58.60  ? 469 ARG A C   1 
ATOM   3976  O O   . ARG A 1 469 ? 26.254  -8.913  -12.582 1.00 64.06  ? 469 ARG A O   1 
ATOM   3977  C CB  . ARG A 1 469 ? 26.571  -5.761  -12.897 1.00 49.74  ? 469 ARG A CB  1 
ATOM   3978  C CG  . ARG A 1 469 ? 25.963  -4.469  -13.411 1.00 57.86  ? 469 ARG A CG  1 
ATOM   3979  C CD  . ARG A 1 469 ? 26.960  -3.588  -14.139 1.00 56.76  ? 469 ARG A CD  1 
ATOM   3980  N NE  . ARG A 1 469 ? 26.312  -2.401  -14.691 1.00 63.86  ? 469 ARG A NE  1 
ATOM   3981  C CZ  . ARG A 1 469 ? 25.610  -2.372  -15.817 1.00 61.65  ? 469 ARG A CZ  1 
ATOM   3982  N NH1 . ARG A 1 469 ? 25.469  -3.449  -16.572 1.00 65.42  ? 469 ARG A NH1 1 
ATOM   3983  N NH2 . ARG A 1 469 ? 25.038  -1.231  -16.198 1.00 58.10  ? 469 ARG A NH2 1 
ATOM   3984  N N   . SER A 1 470 ? 26.616  -8.060  -10.526 1.00 64.40  ? 470 SER A N   1 
ATOM   3985  C CA  . SER A 1 470 ? 27.146  -9.314  -10.001 1.00 58.75  ? 470 SER A CA  1 
ATOM   3986  C C   . SER A 1 470 ? 26.032  -10.325 -9.767  1.00 59.68  ? 470 SER A C   1 
ATOM   3987  O O   . SER A 1 470 ? 26.154  -11.499 -10.139 1.00 62.66  ? 470 SER A O   1 
ATOM   3988  C CB  . SER A 1 470 ? 27.905  -9.056  -8.702  1.00 56.42  ? 470 SER A CB  1 
ATOM   3989  O OG  . SER A 1 470 ? 28.916  -10.023 -8.506  1.00 69.08  ? 470 SER A OG  1 
ATOM   3990  N N   . PHE A 1 471 ? 24.942  -9.887  -9.133  1.00 55.86  ? 471 PHE A N   1 
ATOM   3991  C CA  . PHE A 1 471 ? 23.809  -10.777 -8.902  1.00 55.15  ? 471 PHE A CA  1 
ATOM   3992  C C   . PHE A 1 471 ? 23.196  -11.248 -10.212 1.00 58.67  ? 471 PHE A C   1 
ATOM   3993  O O   . PHE A 1 471 ? 22.802  -12.414 -10.331 1.00 63.55  ? 471 PHE A O   1 
ATOM   3994  C CB  . PHE A 1 471 ? 22.749  -10.079 -8.056  1.00 47.63  ? 471 PHE A CB  1 
ATOM   3995  C CG  . PHE A 1 471 ? 23.179  -9.813  -6.650  1.00 46.36  ? 471 PHE A CG  1 
ATOM   3996  C CD1 . PHE A 1 471 ? 23.710  -10.826 -5.872  1.00 54.01  ? 471 PHE A CD1 1 
ATOM   3997  C CD2 . PHE A 1 471 ? 23.047  -8.549  -6.101  1.00 42.80  ? 471 PHE A CD2 1 
ATOM   3998  C CE1 . PHE A 1 471 ? 24.105  -10.585 -4.572  1.00 47.21  ? 471 PHE A CE1 1 
ATOM   3999  C CE2 . PHE A 1 471 ? 23.442  -8.300  -4.802  1.00 41.93  ? 471 PHE A CE2 1 
ATOM   4000  C CZ  . PHE A 1 471 ? 23.972  -9.321  -4.037  1.00 43.99  ? 471 PHE A CZ  1 
ATOM   4001  N N   . VAL A 1 472 ? 23.081  -10.350 -11.198 1.00 56.49  ? 472 VAL A N   1 
ATOM   4002  C CA  . VAL A 1 472 ? 22.568  -10.736 -12.513 1.00 59.21  ? 472 VAL A CA  1 
ATOM   4003  C C   . VAL A 1 472 ? 23.444  -11.808 -13.141 1.00 64.05  ? 472 VAL A C   1 
ATOM   4004  O O   . VAL A 1 472 ? 22.945  -12.801 -13.685 1.00 67.65  ? 472 VAL A O   1 
ATOM   4005  C CB  . VAL A 1 472 ? 22.439  -9.510  -13.434 1.00 62.57  ? 472 VAL A CB  1 
ATOM   4006  C CG1 . VAL A 1 472 ? 21.673  -9.902  -14.670 1.00 67.97  ? 472 VAL A CG1 1 
ATOM   4007  C CG2 . VAL A 1 472 ? 21.651  -8.410  -12.733 1.00 56.19  ? 472 VAL A CG2 1 
ATOM   4008  N N   . ARG A 1 473 ? 24.761  -11.622 -13.079 1.00 61.06  ? 473 ARG A N   1 
ATOM   4009  C CA  . ARG A 1 473 ? 25.671  -12.562 -13.724 1.00 63.13  ? 473 ARG A CA  1 
ATOM   4010  C C   . ARG A 1 473 ? 25.603  -13.928 -13.051 1.00 67.65  ? 473 ARG A C   1 
ATOM   4011  O O   . ARG A 1 473 ? 25.457  -14.956 -13.723 1.00 67.40  ? 473 ARG A O   1 
ATOM   4012  C CB  . ARG A 1 473 ? 27.093  -11.997 -13.704 1.00 63.98  ? 473 ARG A CB  1 
ATOM   4013  C CG  . ARG A 1 473 ? 28.175  -13.037 -13.870 1.00 74.13  ? 473 ARG A CG  1 
ATOM   4014  C CD  . ARG A 1 473 ? 29.569  -12.503 -13.520 1.00 86.94  ? 473 ARG A CD  1 
ATOM   4015  N NE  . ARG A 1 473 ? 29.619  -11.045 -13.492 1.00 94.07  ? 473 ARG A NE  1 
ATOM   4016  C CZ  . ARG A 1 473 ? 30.239  -10.323 -12.564 1.00 90.25  ? 473 ARG A CZ  1 
ATOM   4017  N NH1 . ARG A 1 473 ? 30.836  -10.890 -11.527 1.00 93.46  ? 473 ARG A NH1 1 
ATOM   4018  N NH2 . ARG A 1 473 ? 30.242  -8.994  -12.667 1.00 82.12  ? 473 ARG A NH2 1 
ATOM   4019  N N   . ARG A 1 474 ? 25.671  -13.950 -11.712 1.00 70.74  ? 474 ARG A N   1 
ATOM   4020  C CA  . ARG A 1 474 ? 25.576  -15.200 -10.960 1.00 67.56  ? 474 ARG A CA  1 
ATOM   4021  C C   . ARG A 1 474 ? 24.218  -15.868 -11.136 1.00 64.34  ? 474 ARG A C   1 
ATOM   4022  O O   . ARG A 1 474 ? 24.111  -17.090 -10.981 1.00 63.69  ? 474 ARG A O   1 
ATOM   4023  C CB  . ARG A 1 474 ? 25.880  -14.932 -9.475  1.00 61.04  ? 474 ARG A CB  1 
ATOM   4024  C CG  . ARG A 1 474 ? 25.684  -16.104 -8.535  1.00 64.13  ? 474 ARG A CG  1 
ATOM   4025  C CD  . ARG A 1 474 ? 26.882  -17.010 -8.618  1.00 64.50  ? 474 ARG A CD  1 
ATOM   4026  N NE  . ARG A 1 474 ? 26.628  -18.093 -9.558  1.00 76.48  ? 474 ARG A NE  1 
ATOM   4027  C CZ  . ARG A 1 474 ? 25.894  -19.168 -9.301  1.00 73.86  ? 474 ARG A CZ  1 
ATOM   4028  N NH1 . ARG A 1 474 ? 25.430  -19.416 -8.087  1.00 70.22  ? 474 ARG A NH1 1 
ATOM   4029  N NH2 . ARG A 1 474 ? 25.614  -20.010 -10.292 1.00 70.24  ? 474 ARG A NH2 1 
ATOM   4030  N N   . ALA A 1 475 ? 23.191  -15.099 -11.508 1.00 65.05  ? 475 ALA A N   1 
ATOM   4031  C CA  . ALA A 1 475 ? 21.868  -15.657 -11.761 1.00 64.91  ? 475 ALA A CA  1 
ATOM   4032  C C   . ALA A 1 475 ? 21.801  -16.455 -13.057 1.00 65.06  ? 475 ALA A C   1 
ATOM   4033  O O   . ALA A 1 475 ? 20.869  -17.245 -13.232 1.00 68.34  ? 475 ALA A O   1 
ATOM   4034  C CB  . ALA A 1 475 ? 20.826  -14.540 -11.794 1.00 55.14  ? 475 ALA A CB  1 
ATOM   4035  N N   . GLN A 1 476 ? 22.750  -16.268 -13.971 1.00 65.11  ? 476 GLN A N   1 
ATOM   4036  C CA  . GLN A 1 476 ? 22.757  -16.977 -15.244 1.00 70.13  ? 476 GLN A CA  1 
ATOM   4037  C C   . GLN A 1 476 ? 23.853  -18.041 -15.296 1.00 76.57  ? 476 GLN A C   1 
ATOM   4038  O O   . GLN A 1 476 ? 24.389  -18.338 -16.368 1.00 71.10  ? 476 GLN A O   1 
ATOM   4039  C CB  . GLN A 1 476 ? 22.901  -15.988 -16.402 1.00 69.74  ? 476 GLN A CB  1 
ATOM   4040  C CG  . GLN A 1 476 ? 22.329  -14.612 -16.108 1.00 67.66  ? 476 GLN A CG  1 
ATOM   4041  C CD  . GLN A 1 476 ? 22.698  -13.573 -17.149 1.00 71.48  ? 476 GLN A CD  1 
ATOM   4042  O OE1 . GLN A 1 476 ? 22.493  -13.769 -18.346 1.00 67.84  ? 476 GLN A OE1 1 
ATOM   4043  N NE2 . GLN A 1 476 ? 23.258  -12.457 -16.692 1.00 72.03  ? 476 GLN A NE2 1 
ATOM   4044  N N   . GLU A 1 477 ? 24.189  -18.626 -14.147 1.00 66.36  ? 477 GLU A N   1 
ATOM   4045  C CA  . GLU A 1 477 ? 25.180  -19.696 -14.092 1.00 64.18  ? 477 GLU A CA  1 
ATOM   4046  C C   . GLU A 1 477 ? 24.724  -20.845 -13.189 1.00 62.00  ? 477 GLU A C   1 
ATOM   4047  O O   . GLU A 1 477 ? 25.490  -21.768 -12.894 1.00 64.00  ? 477 GLU A O   1 
ATOM   4048  C CB  . GLU A 1 477 ? 26.527  -19.149 -13.618 1.00 69.62  ? 477 GLU A CB  1 
ATOM   4049  C CG  . GLU A 1 477 ? 27.059  -17.980 -14.454 1.00 78.14  ? 477 GLU A CG  1 
ATOM   4050  C CD  . GLU A 1 477 ? 28.214  -17.259 -13.785 1.00 85.04  ? 477 GLU A CD  1 
ATOM   4051  O OE1 . GLU A 1 477 ? 28.717  -17.778 -12.769 1.00 87.67  ? 477 GLU A OE1 1 
ATOM   4052  O OE2 . GLU A 1 477 ? 28.635  -16.191 -14.283 1.00 86.46  ? 477 GLU A OE2 1 
ATOM   4053  N N   . MET B 1 1   ? 17.012  35.182  44.663  1.00 100.61 ? 1   MET B N   1 
ATOM   4054  C CA  . MET B 1 1   ? 16.085  34.146  44.215  1.00 97.34  ? 1   MET B CA  1 
ATOM   4055  C C   . MET B 1 1   ? 15.684  34.359  42.761  1.00 83.96  ? 1   MET B C   1 
ATOM   4056  O O   . MET B 1 1   ? 15.021  35.346  42.430  1.00 85.51  ? 1   MET B O   1 
ATOM   4057  C CB  . MET B 1 1   ? 14.831  34.119  45.098  1.00 101.67 ? 1   MET B CB  1 
ATOM   4058  C CG  . MET B 1 1   ? 15.075  34.467  46.558  1.00 111.86 ? 1   MET B CG  1 
ATOM   4059  S SD  . MET B 1 1   ? 14.899  36.238  46.864  1.00 127.35 ? 1   MET B SD  1 
ATOM   4060  C CE  . MET B 1 1   ? 13.117  36.426  46.895  1.00 107.18 ? 1   MET B CE  1 
ATOM   4061  N N   . LYS B 1 2   ? 16.100  33.433  41.898  1.00 74.44  ? 2   LYS B N   1 
ATOM   4062  C CA  . LYS B 1 2   ? 15.655  33.440  40.512  1.00 65.06  ? 2   LYS B CA  1 
ATOM   4063  C C   . LYS B 1 2   ? 14.135  33.445  40.459  1.00 68.89  ? 2   LYS B C   1 
ATOM   4064  O O   . LYS B 1 2   ? 13.478  32.590  41.062  1.00 72.62  ? 2   LYS B O   1 
ATOM   4065  C CB  . LYS B 1 2   ? 16.211  32.221  39.785  1.00 63.33  ? 2   LYS B CB  1 
ATOM   4066  C CG  . LYS B 1 2   ? 15.646  32.013  38.399  1.00 66.68  ? 2   LYS B CG  1 
ATOM   4067  C CD  . LYS B 1 2   ? 16.626  31.245  37.531  1.00 67.95  ? 2   LYS B CD  1 
ATOM   4068  C CE  . LYS B 1 2   ? 16.040  29.929  37.065  1.00 61.94  ? 2   LYS B CE  1 
ATOM   4069  N NZ  . LYS B 1 2   ? 15.170  30.143  35.876  1.00 67.89  ? 2   LYS B NZ  1 
ATOM   4070  N N   . LYS B 1 3   ? 13.574  34.420  39.752  1.00 62.99  ? 3   LYS B N   1 
ATOM   4071  C CA  . LYS B 1 3   ? 12.131  34.615  39.714  1.00 67.20  ? 3   LYS B CA  1 
ATOM   4072  C C   . LYS B 1 3   ? 11.613  34.385  38.299  1.00 66.13  ? 3   LYS B C   1 
ATOM   4073  O O   . LYS B 1 3   ? 12.185  34.903  37.332  1.00 65.61  ? 3   LYS B O   1 
ATOM   4074  C CB  . LYS B 1 3   ? 11.766  36.023  40.207  1.00 63.65  ? 3   LYS B CB  1 
ATOM   4075  C CG  . LYS B 1 3   ? 11.380  36.071  41.679  1.00 72.68  ? 3   LYS B CG  1 
ATOM   4076  C CD  . LYS B 1 3   ? 11.191  37.498  42.180  1.00 71.34  ? 3   LYS B CD  1 
ATOM   4077  C CE  . LYS B 1 3   ? 11.372  37.589  43.694  1.00 80.54  ? 3   LYS B CE  1 
ATOM   4078  N NZ  . LYS B 1 3   ? 10.578  38.708  44.279  1.00 100.45 ? 3   LYS B NZ  1 
ATOM   4079  N N   . LEU B 1 4   ? 10.554  33.586  38.181  1.00 63.54  ? 4   LEU B N   1 
ATOM   4080  C CA  . LEU B 1 4   ? 9.801   33.482  36.937  1.00 61.96  ? 4   LEU B CA  1 
ATOM   4081  C C   . LEU B 1 4   ? 8.923   34.713  36.767  1.00 59.94  ? 4   LEU B C   1 
ATOM   4082  O O   . LEU B 1 4   ? 8.273   35.161  37.716  1.00 57.27  ? 4   LEU B O   1 
ATOM   4083  C CB  . LEU B 1 4   ? 8.924   32.226  36.929  1.00 60.40  ? 4   LEU B CB  1 
ATOM   4084  C CG  . LEU B 1 4   ? 7.950   32.033  35.750  1.00 59.02  ? 4   LEU B CG  1 
ATOM   4085  C CD1 . LEU B 1 4   ? 7.894   30.572  35.354  1.00 58.88  ? 4   LEU B CD1 1 
ATOM   4086  C CD2 . LEU B 1 4   ? 6.533   32.556  36.007  1.00 51.54  ? 4   LEU B CD2 1 
ATOM   4087  N N   . PHE B 1 5   ? 8.884   35.243  35.545  1.00 60.46  ? 5   PHE B N   1 
ATOM   4088  C CA  . PHE B 1 5   ? 8.067   36.406  35.210  1.00 56.51  ? 5   PHE B CA  1 
ATOM   4089  C C   . PHE B 1 5   ? 6.852   35.956  34.401  1.00 55.41  ? 5   PHE B C   1 
ATOM   4090  O O   . PHE B 1 5   ? 6.995   35.459  33.277  1.00 54.26  ? 5   PHE B O   1 
ATOM   4091  C CB  . PHE B 1 5   ? 8.889   37.447  34.447  1.00 44.21  ? 5   PHE B CB  1 
ATOM   4092  C CG  . PHE B 1 5   ? 10.010  38.041  35.260  1.00 54.08  ? 5   PHE B CG  1 
ATOM   4093  C CD1 . PHE B 1 5   ? 9.755   38.627  36.489  1.00 63.04  ? 5   PHE B CD1 1 
ATOM   4094  C CD2 . PHE B 1 5   ? 11.315  38.019  34.797  1.00 56.38  ? 5   PHE B CD2 1 
ATOM   4095  C CE1 . PHE B 1 5   ? 10.780  39.174  37.244  1.00 57.43  ? 5   PHE B CE1 1 
ATOM   4096  C CE2 . PHE B 1 5   ? 12.342  38.566  35.546  1.00 59.25  ? 5   PHE B CE2 1 
ATOM   4097  C CZ  . PHE B 1 5   ? 12.071  39.145  36.773  1.00 56.77  ? 5   PHE B CZ  1 
ATOM   4098  N N   . LEU B 1 6   ? 5.664   36.135  34.978  1.00 55.28  ? 6   LEU B N   1 
ATOM   4099  C CA  . LEU B 1 6   ? 4.400   35.730  34.374  1.00 53.42  ? 6   LEU B CA  1 
ATOM   4100  C C   . LEU B 1 6   ? 3.635   36.964  33.921  1.00 49.06  ? 6   LEU B C   1 
ATOM   4101  O O   . LEU B 1 6   ? 3.448   37.906  34.698  1.00 51.29  ? 6   LEU B O   1 
ATOM   4102  C CB  . LEU B 1 6   ? 3.558   34.925  35.370  1.00 50.12  ? 6   LEU B CB  1 
ATOM   4103  C CG  . LEU B 1 6   ? 2.284   34.255  34.864  1.00 43.76  ? 6   LEU B CG  1 
ATOM   4104  C CD1 . LEU B 1 6   ? 2.575   33.367  33.669  1.00 48.71  ? 6   LEU B CD1 1 
ATOM   4105  C CD2 . LEU B 1 6   ? 1.691   33.433  35.987  1.00 49.61  ? 6   LEU B CD2 1 
ATOM   4106  N N   . VAL B 1 7   ? 3.191   36.954  32.670  1.00 46.27  ? 7   VAL B N   1 
ATOM   4107  C CA  . VAL B 1 7   ? 2.469   38.073  32.085  1.00 52.25  ? 7   VAL B CA  1 
ATOM   4108  C C   . VAL B 1 7   ? 1.151   37.543  31.536  1.00 46.51  ? 7   VAL B C   1 
ATOM   4109  O O   . VAL B 1 7   ? 1.141   36.653  30.673  1.00 43.37  ? 7   VAL B O   1 
ATOM   4110  C CB  . VAL B 1 7   ? 3.283   38.774  30.984  1.00 49.57  ? 7   VAL B CB  1 
ATOM   4111  C CG1 . VAL B 1 7   ? 2.378   39.711  30.190  1.00 46.03  ? 7   VAL B CG1 1 
ATOM   4112  C CG2 . VAL B 1 7   ? 4.468   39.527  31.576  1.00 38.51  ? 7   VAL B CG2 1 
ATOM   4113  N N   . PHE B 1 8   ? 0.049   38.091  32.040  1.00 50.47  ? 8   PHE B N   1 
ATOM   4114  C CA  . PHE B 1 8   ? -1.299  37.747  31.609  1.00 43.93  ? 8   PHE B CA  1 
ATOM   4115  C C   . PHE B 1 8   ? -1.803  38.864  30.709  1.00 47.96  ? 8   PHE B C   1 
ATOM   4116  O O   . PHE B 1 8   ? -1.818  40.033  31.111  1.00 50.46  ? 8   PHE B O   1 
ATOM   4117  C CB  . PHE B 1 8   ? -2.227  37.586  32.811  1.00 42.95  ? 8   PHE B CB  1 
ATOM   4118  C CG  . PHE B 1 8   ? -2.196  36.225  33.444  1.00 43.14  ? 8   PHE B CG  1 
ATOM   4119  C CD1 . PHE B 1 8   ? -2.735  35.126  32.791  1.00 38.17  ? 8   PHE B CD1 1 
ATOM   4120  C CD2 . PHE B 1 8   ? -1.652  36.049  34.712  1.00 44.82  ? 8   PHE B CD2 1 
ATOM   4121  C CE1 . PHE B 1 8   ? -2.722  33.873  33.386  1.00 53.94  ? 8   PHE B CE1 1 
ATOM   4122  C CE2 . PHE B 1 8   ? -1.635  34.797  35.313  1.00 46.25  ? 8   PHE B CE2 1 
ATOM   4123  C CZ  . PHE B 1 8   ? -2.168  33.709  34.652  1.00 51.54  ? 8   PHE B CZ  1 
ATOM   4124  N N   . TRP B 1 9   ? -2.202  38.511  29.496  1.00 47.90  ? 9   TRP B N   1 
ATOM   4125  C CA  . TRP B 1 9   ? -2.734  39.460  28.527  1.00 40.46  ? 9   TRP B CA  1 
ATOM   4126  C C   . TRP B 1 9   ? -4.056  38.887  28.058  1.00 45.46  ? 9   TRP B C   1 
ATOM   4127  O O   . TRP B 1 9   ? -4.079  37.916  27.295  1.00 53.62  ? 9   TRP B O   1 
ATOM   4128  C CB  . TRP B 1 9   ? -1.773  39.669  27.358  1.00 40.32  ? 9   TRP B CB  1 
ATOM   4129  C CG  . TRP B 1 9   ? -1.977  40.953  26.591  1.00 39.69  ? 9   TRP B CG  1 
ATOM   4130  C CD1 . TRP B 1 9   ? -3.071  41.768  26.630  1.00 47.27  ? 9   TRP B CD1 1 
ATOM   4131  C CD2 . TRP B 1 9   ? -1.064  41.555  25.662  1.00 35.47  ? 9   TRP B CD2 1 
ATOM   4132  N NE1 . TRP B 1 9   ? -2.893  42.843  25.791  1.00 44.21  ? 9   TRP B NE1 1 
ATOM   4133  C CE2 . TRP B 1 9   ? -1.669  42.734  25.185  1.00 39.37  ? 9   TRP B CE2 1 
ATOM   4134  C CE3 . TRP B 1 9   ? 0.209   41.215  25.195  1.00 44.66  ? 9   TRP B CE3 1 
ATOM   4135  C CZ2 . TRP B 1 9   ? -1.045  43.576  24.263  1.00 51.19  ? 9   TRP B CZ2 1 
ATOM   4136  C CZ3 . TRP B 1 9   ? 0.829   42.056  24.280  1.00 52.84  ? 9   TRP B CZ3 1 
ATOM   4137  C CH2 . TRP B 1 9   ? 0.201   43.218  23.823  1.00 51.36  ? 9   TRP B CH2 1 
ATOM   4138  N N   . TRP B 1 10  ? -5.149  39.457  28.552  1.00 46.08  ? 10  TRP B N   1 
ATOM   4139  C CA  . TRP B 1 10  ? -6.489  39.009  28.205  1.00 41.16  ? 10  TRP B CA  1 
ATOM   4140  C C   . TRP B 1 10  ? -7.008  39.843  27.044  1.00 43.24  ? 10  TRP B C   1 
ATOM   4141  O O   . TRP B 1 10  ? -6.994  41.075  27.112  1.00 49.72  ? 10  TRP B O   1 
ATOM   4142  C CB  . TRP B 1 10  ? -7.431  39.148  29.395  1.00 42.97  ? 10  TRP B CB  1 
ATOM   4143  C CG  . TRP B 1 10  ? -7.076  38.354  30.602  1.00 38.88  ? 10  TRP B CG  1 
ATOM   4144  C CD1 . TRP B 1 10  ? -6.652  38.844  31.802  1.00 42.21  ? 10  TRP B CD1 1 
ATOM   4145  C CD2 . TRP B 1 10  ? -7.155  36.931  30.755  1.00 42.05  ? 10  TRP B CD2 1 
ATOM   4146  N NE1 . TRP B 1 10  ? -6.447  37.813  32.693  1.00 44.44  ? 10  TRP B NE1 1 
ATOM   4147  C CE2 . TRP B 1 10  ? -6.749  36.629  32.073  1.00 44.88  ? 10  TRP B CE2 1 
ATOM   4148  C CE3 . TRP B 1 10  ? -7.524  35.882  29.907  1.00 43.25  ? 10  TRP B CE3 1 
ATOM   4149  C CZ2 . TRP B 1 10  ? -6.700  35.324  32.558  1.00 39.63  ? 10  TRP B CZ2 1 
ATOM   4150  C CZ3 . TRP B 1 10  ? -7.474  34.586  30.395  1.00 36.86  ? 10  TRP B CZ3 1 
ATOM   4151  C CH2 . TRP B 1 10  ? -7.063  34.320  31.703  1.00 36.31  ? 10  TRP B CH2 1 
ATOM   4152  N N   . HIS B 1 11  ? -7.468  39.172  25.988  1.00 49.86  ? 11  HIS B N   1 
ATOM   4153  C CA  . HIS B 1 11  ? -7.962  39.833  24.783  1.00 47.21  ? 11  HIS B CA  1 
ATOM   4154  C C   . HIS B 1 11  ? -9.479  39.909  24.836  1.00 44.55  ? 11  HIS B C   1 
ATOM   4155  O O   . HIS B 1 11  ? -10.151 38.881  24.969  1.00 46.55  ? 11  HIS B O   1 
ATOM   4156  C CB  . HIS B 1 11  ? -7.518  39.093  23.522  1.00 45.08  ? 11  HIS B CB  1 
ATOM   4157  C CG  . HIS B 1 11  ? -8.131  39.621  22.261  1.00 44.87  ? 11  HIS B CG  1 
ATOM   4158  N ND1 . HIS B 1 11  ? -8.117  40.961  21.931  1.00 47.32  ? 11  HIS B ND1 1 
ATOM   4159  C CD2 . HIS B 1 11  ? -8.746  38.988  21.233  1.00 44.33  ? 11  HIS B CD2 1 
ATOM   4160  C CE1 . HIS B 1 11  ? -8.714  41.131  20.764  1.00 48.12  ? 11  HIS B CE1 1 
ATOM   4161  N NE2 . HIS B 1 11  ? -9.103  39.949  20.318  1.00 45.73  ? 11  HIS B NE2 1 
ATOM   4162  N N   . MET B 1 12  ? -10.011 41.119  24.709  1.00 42.71  ? 12  MET B N   1 
ATOM   4163  C CA  . MET B 1 12  ? -11.447 41.360  24.764  1.00 43.08  ? 12  MET B CA  1 
ATOM   4164  C C   . MET B 1 12  ? -11.871 42.025  23.463  1.00 47.41  ? 12  MET B C   1 
ATOM   4165  O O   . MET B 1 12  ? -11.450 43.150  23.173  1.00 46.53  ? 12  MET B O   1 
ATOM   4166  C CB  . MET B 1 12  ? -11.801 42.224  25.968  1.00 43.40  ? 12  MET B CB  1 
ATOM   4167  C CG  . MET B 1 12  ? -11.096 41.808  27.249  1.00 40.62  ? 12  MET B CG  1 
ATOM   4168  S SD  . MET B 1 12  ? -11.646 40.189  27.804  1.00 62.33  ? 12  MET B SD  1 
ATOM   4169  C CE  . MET B 1 12  ? -11.670 40.405  29.585  1.00 52.86  ? 12  MET B CE  1 
ATOM   4170  N N   . HIS B 1 13  ? -12.696 41.333  22.677  1.00 48.59  ? 13  HIS B N   1 
ATOM   4171  C CA  . HIS B 1 13  ? -13.134 41.854  21.388  1.00 45.37  ? 13  HIS B CA  1 
ATOM   4172  C C   . HIS B 1 13  ? -14.543 41.370  21.087  1.00 46.79  ? 13  HIS B C   1 
ATOM   4173  O O   . HIS B 1 13  ? -14.914 40.245  21.440  1.00 42.65  ? 13  HIS B O   1 
ATOM   4174  C CB  . HIS B 1 13  ? -12.191 41.426  20.255  1.00 40.87  ? 13  HIS B CB  1 
ATOM   4175  C CG  . HIS B 1 13  ? -12.758 41.591  18.874  1.00 40.44  ? 13  HIS B CG  1 
ATOM   4176  N ND1 . HIS B 1 13  ? -13.036 42.824  18.321  1.00 44.36  ? 13  HIS B ND1 1 
ATOM   4177  C CD2 . HIS B 1 13  ? -13.039 40.680  17.911  1.00 42.39  ? 13  HIS B CD2 1 
ATOM   4178  C CE1 . HIS B 1 13  ? -13.490 42.664  17.090  1.00 45.98  ? 13  HIS B CE1 1 
ATOM   4179  N NE2 . HIS B 1 13  ? -13.501 41.372  16.816  1.00 45.73  ? 13  HIS B NE2 1 
ATOM   4180  N N   . GLN B 1 14  ? -15.319 42.229  20.425  1.00 47.24  ? 14  GLN B N   1 
ATOM   4181  C CA  . GLN B 1 14  ? -16.584 41.828  19.817  1.00 44.42  ? 14  GLN B CA  1 
ATOM   4182  C C   . GLN B 1 14  ? -16.772 42.560  18.488  1.00 48.51  ? 14  GLN B C   1 
ATOM   4183  O O   . GLN B 1 14  ? -16.626 43.787  18.434  1.00 55.15  ? 14  GLN B O   1 
ATOM   4184  C CB  . GLN B 1 14  ? -17.747 42.117  20.768  1.00 47.55  ? 14  GLN B CB  1 
ATOM   4185  C CG  . GLN B 1 14  ? -17.763 41.247  22.031  1.00 44.76  ? 14  GLN B CG  1 
ATOM   4186  C CD  . GLN B 1 14  ? -18.118 39.803  21.748  1.00 48.95  ? 14  GLN B CD  1 
ATOM   4187  O OE1 . GLN B 1 14  ? -18.560 39.469  20.649  1.00 46.69  ? 14  GLN B OE1 1 
ATOM   4188  N NE2 . GLN B 1 14  ? -17.977 38.946  22.755  1.00 51.53  ? 14  GLN B NE2 1 
ATOM   4189  N N   . PRO B 1 15  ? -17.078 41.858  17.396  1.00 46.26  ? 15  PRO B N   1 
ATOM   4190  C CA  . PRO B 1 15  ? -17.357 42.540  16.127  1.00 41.98  ? 15  PRO B CA  1 
ATOM   4191  C C   . PRO B 1 15  ? -18.567 43.454  16.222  1.00 49.16  ? 15  PRO B C   1 
ATOM   4192  O O   . PRO B 1 15  ? -19.337 43.428  17.186  1.00 54.71  ? 15  PRO B O   1 
ATOM   4193  C CB  . PRO B 1 15  ? -17.622 41.385  15.154  1.00 42.55  ? 15  PRO B CB  1 
ATOM   4194  C CG  . PRO B 1 15  ? -17.985 40.225  16.016  1.00 40.23  ? 15  PRO B CG  1 
ATOM   4195  C CD  . PRO B 1 15  ? -17.131 40.395  17.244  1.00 51.26  ? 15  PRO B CD  1 
ATOM   4196  N N   . LEU B 1 16  ? -18.737 44.270  15.181  1.00 51.10  ? 16  LEU B N   1 
ATOM   4197  C CA  . LEU B 1 16  ? -19.876 45.182  15.088  1.00 47.08  ? 16  LEU B CA  1 
ATOM   4198  C C   . LEU B 1 16  ? -21.126 44.394  14.718  1.00 49.99  ? 16  LEU B C   1 
ATOM   4199  O O   . LEU B 1 16  ? -21.276 43.959  13.570  1.00 48.69  ? 16  LEU B O   1 
ATOM   4200  C CB  . LEU B 1 16  ? -19.610 46.281  14.064  1.00 41.28  ? 16  LEU B CB  1 
ATOM   4201  C CG  . LEU B 1 16  ? -20.584 47.461  14.072  1.00 49.48  ? 16  LEU B CG  1 
ATOM   4202  C CD1 . LEU B 1 16  ? -20.969 47.861  15.494  1.00 55.44  ? 16  LEU B CD1 1 
ATOM   4203  C CD2 . LEU B 1 16  ? -19.983 48.639  13.333  1.00 39.30  ? 16  LEU B CD2 1 
ATOM   4204  N N   . TYR B 1 17  ? -22.020 44.212  15.694  1.00 53.51  ? 17  TYR B N   1 
ATOM   4205  C CA  . TYR B 1 17  ? -23.281 43.504  15.516  1.00 48.79  ? 17  TYR B CA  1 
ATOM   4206  C C   . TYR B 1 17  ? -24.426 44.418  15.106  1.00 49.40  ? 17  TYR B C   1 
ATOM   4207  O O   . TYR B 1 17  ? -25.561 43.945  14.988  1.00 56.54  ? 17  TYR B O   1 
ATOM   4208  C CB  . TYR B 1 17  ? -23.673 42.777  16.807  1.00 49.62  ? 17  TYR B CB  1 
ATOM   4209  C CG  . TYR B 1 17  ? -22.742 41.655  17.206  1.00 44.81  ? 17  TYR B CG  1 
ATOM   4210  C CD1 . TYR B 1 17  ? -22.418 40.635  16.316  1.00 43.57  ? 17  TYR B CD1 1 
ATOM   4211  C CD2 . TYR B 1 17  ? -22.209 41.603  18.480  1.00 48.77  ? 17  TYR B CD2 1 
ATOM   4212  C CE1 . TYR B 1 17  ? -21.570 39.608  16.686  1.00 46.80  ? 17  TYR B CE1 1 
ATOM   4213  C CE2 . TYR B 1 17  ? -21.360 40.584  18.863  1.00 53.78  ? 17  TYR B CE2 1 
ATOM   4214  C CZ  . TYR B 1 17  ? -21.042 39.591  17.969  1.00 54.86  ? 17  TYR B CZ  1 
ATOM   4215  O OH  . TYR B 1 17  ? -20.192 38.595  18.392  1.00 49.07  ? 17  TYR B OH  1 
ATOM   4216  N N   . ARG B 1 18  ? -24.172 45.707  14.901  1.00 49.69  ? 18  ARG B N   1 
ATOM   4217  C CA  . ARG B 1 18  ? -25.229 46.689  14.669  1.00 58.47  ? 18  ARG B CA  1 
ATOM   4218  C C   . ARG B 1 18  ? -25.412 46.891  13.165  1.00 59.52  ? 18  ARG B C   1 
ATOM   4219  O O   . ARG B 1 18  ? -24.513 47.398  12.487  1.00 56.65  ? 18  ARG B O   1 
ATOM   4220  C CB  . ARG B 1 18  ? -24.887 47.996  15.384  1.00 56.69  ? 18  ARG B CB  1 
ATOM   4221  C CG  . ARG B 1 18  ? -25.604 49.233  14.878  1.00 60.51  ? 18  ARG B CG  1 
ATOM   4222  C CD  . ARG B 1 18  ? -24.872 50.471  15.360  1.00 54.70  ? 18  ARG B CD  1 
ATOM   4223  N NE  . ARG B 1 18  ? -25.763 51.586  15.650  1.00 52.07  ? 18  ARG B NE  1 
ATOM   4224  C CZ  . ARG B 1 18  ? -26.167 52.467  14.747  1.00 59.89  ? 18  ARG B CZ  1 
ATOM   4225  N NH1 . ARG B 1 18  ? -25.819 52.359  13.476  1.00 67.49  ? 18  ARG B NH1 1 
ATOM   4226  N NH2 . ARG B 1 18  ? -26.937 53.482  15.130  1.00 60.95  ? 18  ARG B NH2 1 
ATOM   4227  N N   . GLU B 1 19  ? -26.574 46.497  12.647  1.00 57.97  ? 19  GLU B N   1 
ATOM   4228  C CA  . GLU B 1 19  ? -26.831 46.633  11.218  1.00 64.60  ? 19  GLU B CA  1 
ATOM   4229  C C   . GLU B 1 19  ? -26.921 48.112  10.838  1.00 63.54  ? 19  GLU B C   1 
ATOM   4230  O O   . GLU B 1 19  ? -27.540 48.899  11.560  1.00 64.96  ? 19  GLU B O   1 
ATOM   4231  C CB  . GLU B 1 19  ? -28.122 45.902  10.841  1.00 57.15  ? 19  GLU B CB  1 
ATOM   4232  C CG  . GLU B 1 19  ? -28.145 45.314  9.436   1.00 57.99  ? 19  GLU B CG  1 
ATOM   4233  C CD  . GLU B 1 19  ? -28.964 46.150  8.468   1.00 66.85  ? 19  GLU B CD  1 
ATOM   4234  O OE1 . GLU B 1 19  ? -29.317 47.295  8.822   1.00 67.49  ? 19  GLU B OE1 1 
ATOM   4235  O OE2 . GLU B 1 19  ? -29.257 45.664  7.353   1.00 64.56  ? 19  GLU B OE2 1 
ATOM   4236  N N   . PRO B 1 20  ? -26.316 48.520  9.715   1.00 62.99  ? 20  PRO B N   1 
ATOM   4237  C CA  . PRO B 1 20  ? -26.212 49.965  9.422   1.00 59.74  ? 20  PRO B CA  1 
ATOM   4238  C C   . PRO B 1 20  ? -27.535 50.654  9.123   1.00 72.59  ? 20  PRO B C   1 
ATOM   4239  O O   . PRO B 1 20  ? -27.745 51.779  9.592   1.00 81.16  ? 20  PRO B O   1 
ATOM   4240  C CB  . PRO B 1 20  ? -25.280 49.996  8.203   1.00 67.01  ? 20  PRO B CB  1 
ATOM   4241  C CG  . PRO B 1 20  ? -25.443 48.645  7.579   1.00 67.96  ? 20  PRO B CG  1 
ATOM   4242  C CD  . PRO B 1 20  ? -25.549 47.719  8.751   1.00 60.85  ? 20  PRO B CD  1 
ATOM   4243  N N   . TYR B 1 21  ? -28.427 50.035  8.341   1.00 65.70  ? 21  TYR B N   1 
ATOM   4244  C CA  . TYR B 1 21  ? -29.674 50.705  7.977   1.00 65.68  ? 21  TYR B CA  1 
ATOM   4245  C C   . TYR B 1 21  ? -30.655 50.748  9.141   1.00 68.85  ? 21  TYR B C   1 
ATOM   4246  O O   . TYR B 1 21  ? -31.137 51.824  9.513   1.00 69.40  ? 21  TYR B O   1 
ATOM   4247  C CB  . TYR B 1 21  ? -30.319 50.018  6.770   1.00 73.14  ? 21  TYR B CB  1 
ATOM   4248  C CG  . TYR B 1 21  ? -29.422 49.959  5.562   1.00 73.91  ? 21  TYR B CG  1 
ATOM   4249  C CD1 . TYR B 1 21  ? -28.998 51.120  4.934   1.00 71.47  ? 21  TYR B CD1 1 
ATOM   4250  C CD2 . TYR B 1 21  ? -28.990 48.742  5.054   1.00 74.29  ? 21  TYR B CD2 1 
ATOM   4251  C CE1 . TYR B 1 21  ? -28.170 51.073  3.835   1.00 75.45  ? 21  TYR B CE1 1 
ATOM   4252  C CE2 . TYR B 1 21  ? -28.162 48.685  3.954   1.00 71.22  ? 21  TYR B CE2 1 
ATOM   4253  C CZ  . TYR B 1 21  ? -27.755 49.854  3.348   1.00 73.37  ? 21  TYR B CZ  1 
ATOM   4254  O OH  . TYR B 1 21  ? -26.929 49.806  2.251   1.00 77.11  ? 21  TYR B OH  1 
ATOM   4255  N N   . THR B 1 22  ? -30.969 49.588  9.725   1.00 67.52  ? 22  THR B N   1 
ATOM   4256  C CA  . THR B 1 22  ? -31.925 49.548  10.826  1.00 67.48  ? 22  THR B CA  1 
ATOM   4257  C C   . THR B 1 22  ? -31.361 50.146  12.109  1.00 66.54  ? 22  THR B C   1 
ATOM   4258  O O   . THR B 1 22  ? -32.135 50.603  12.956  1.00 71.75  ? 22  THR B O   1 
ATOM   4259  C CB  . THR B 1 22  ? -32.382 48.108  11.084  1.00 69.84  ? 22  THR B CB  1 
ATOM   4260  O OG1 . THR B 1 22  ? -33.354 48.090  12.136  1.00 84.41  ? 22  THR B OG1 1 
ATOM   4261  C CG2 . THR B 1 22  ? -31.223 47.250  11.494  1.00 60.30  ? 22  THR B CG2 1 
ATOM   4262  N N   . GLY B 1 23  ? -30.041 50.175  12.270  1.00 68.03  ? 23  GLY B N   1 
ATOM   4263  C CA  . GLY B 1 23  ? -29.465 50.683  13.501  1.00 70.26  ? 23  GLY B CA  1 
ATOM   4264  C C   . GLY B 1 23  ? -29.663 49.778  14.695  1.00 69.60  ? 23  GLY B C   1 
ATOM   4265  O O   . GLY B 1 23  ? -29.652 50.252  15.835  1.00 74.78  ? 23  GLY B O   1 
ATOM   4266  N N   . GLU B 1 24  ? -29.831 48.479  14.466  1.00 69.60  ? 24  GLU B N   1 
ATOM   4267  C CA  . GLU B 1 24  ? -30.193 47.537  15.515  1.00 67.27  ? 24  GLU B CA  1 
ATOM   4268  C C   . GLU B 1 24  ? -29.139 46.448  15.635  1.00 59.42  ? 24  GLU B C   1 
ATOM   4269  O O   . GLU B 1 24  ? -28.628 45.953  14.627  1.00 63.19  ? 24  GLU B O   1 
ATOM   4270  C CB  . GLU B 1 24  ? -31.564 46.917  15.232  1.00 64.37  ? 24  GLU B CB  1 
ATOM   4271  C CG  . GLU B 1 24  ? -32.685 47.544  16.028  1.00 59.61  ? 24  GLU B CG  1 
ATOM   4272  C CD  . GLU B 1 24  ? -34.017 47.453  15.329  1.00 92.09  ? 24  GLU B CD  1 
ATOM   4273  O OE1 . GLU B 1 24  ? -34.086 46.769  14.288  1.00 98.80  ? 24  GLU B OE1 1 
ATOM   4274  O OE2 . GLU B 1 24  ? -34.997 48.058  15.820  1.00 113.72 ? 24  GLU B OE2 1 
ATOM   4275  N N   . TYR B 1 25  ? -28.817 46.079  16.874  1.00 56.02  ? 25  TYR B N   1 
ATOM   4276  C CA  . TYR B 1 25  ? -27.877 44.994  17.140  1.00 52.82  ? 25  TYR B CA  1 
ATOM   4277  C C   . TYR B 1 25  ? -28.579 43.659  16.932  1.00 54.28  ? 25  TYR B C   1 
ATOM   4278  O O   . TYR B 1 25  ? -29.533 43.333  17.649  1.00 58.57  ? 25  TYR B O   1 
ATOM   4279  C CB  . TYR B 1 25  ? -27.333 45.091  18.563  1.00 58.17  ? 25  TYR B CB  1 
ATOM   4280  C CG  . TYR B 1 25  ? -26.287 46.160  18.745  1.00 55.53  ? 25  TYR B CG  1 
ATOM   4281  C CD1 . TYR B 1 25  ? -26.654 47.454  19.066  1.00 55.06  ? 25  TYR B CD1 1 
ATOM   4282  C CD2 . TYR B 1 25  ? -24.936 45.880  18.577  1.00 57.87  ? 25  TYR B CD2 1 
ATOM   4283  C CE1 . TYR B 1 25  ? -25.718 48.436  19.227  1.00 58.75  ? 25  TYR B CE1 1 
ATOM   4284  C CE2 . TYR B 1 25  ? -23.981 46.866  18.742  1.00 58.26  ? 25  TYR B CE2 1 
ATOM   4285  C CZ  . TYR B 1 25  ? -24.384 48.147  19.067  1.00 59.01  ? 25  TYR B CZ  1 
ATOM   4286  O OH  . TYR B 1 25  ? -23.469 49.161  19.238  1.00 62.20  ? 25  TYR B OH  1 
ATOM   4287  N N   . LEU B 1 26  ? -28.110 42.889  15.955  1.00 48.68  ? 26  LEU B N   1 
ATOM   4288  C CA  . LEU B 1 26  ? -28.772 41.651  15.574  1.00 47.79  ? 26  LEU B CA  1 
ATOM   4289  C C   . LEU B 1 26  ? -28.396 40.476  16.462  1.00 52.19  ? 26  LEU B C   1 
ATOM   4290  O O   . LEU B 1 26  ? -28.913 39.371  16.251  1.00 44.12  ? 26  LEU B O   1 
ATOM   4291  C CB  . LEU B 1 26  ? -28.452 41.321  14.114  1.00 50.77  ? 26  LEU B CB  1 
ATOM   4292  C CG  . LEU B 1 26  ? -28.660 42.455  13.108  1.00 53.56  ? 26  LEU B CG  1 
ATOM   4293  C CD1 . LEU B 1 26  ? -28.497 41.959  11.679  1.00 61.41  ? 26  LEU B CD1 1 
ATOM   4294  C CD2 . LEU B 1 26  ? -30.034 43.079  13.293  1.00 43.08  ? 26  LEU B CD2 1 
ATOM   4295  N N   . LEU B 1 27  ? -27.507 40.684  17.428  1.00 58.14  ? 27  LEU B N   1 
ATOM   4296  C CA  . LEU B 1 27  ? -27.036 39.653  18.337  1.00 52.93  ? 27  LEU B CA  1 
ATOM   4297  C C   . LEU B 1 27  ? -26.715 40.281  19.684  1.00 57.49  ? 27  LEU B C   1 
ATOM   4298  O O   . LEU B 1 27  ? -26.240 41.424  19.743  1.00 52.95  ? 27  LEU B O   1 
ATOM   4299  C CB  . LEU B 1 27  ? -25.787 38.941  17.795  1.00 51.68  ? 27  LEU B CB  1 
ATOM   4300  C CG  . LEU B 1 27  ? -26.028 37.868  16.733  1.00 52.04  ? 27  LEU B CG  1 
ATOM   4301  C CD1 . LEU B 1 27  ? -24.885 37.811  15.736  1.00 44.12  ? 27  LEU B CD1 1 
ATOM   4302  C CD2 . LEU B 1 27  ? -26.254 36.514  17.371  1.00 58.16  ? 27  LEU B CD2 1 
ATOM   4303  N N   . PRO B 1 28  ? -26.950 39.557  20.777  1.00 59.75  ? 28  PRO B N   1 
ATOM   4304  C CA  . PRO B 1 28  ? -26.763 40.120  22.121  1.00 58.31  ? 28  PRO B CA  1 
ATOM   4305  C C   . PRO B 1 28  ? -25.402 39.865  22.751  1.00 53.69  ? 28  PRO B C   1 
ATOM   4306  O O   . PRO B 1 28  ? -25.240 40.129  23.949  1.00 52.24  ? 28  PRO B O   1 
ATOM   4307  C CB  . PRO B 1 28  ? -27.855 39.398  22.916  1.00 57.03  ? 28  PRO B CB  1 
ATOM   4308  C CG  . PRO B 1 28  ? -27.933 38.043  22.269  1.00 52.87  ? 28  PRO B CG  1 
ATOM   4309  C CD  . PRO B 1 28  ? -27.514 38.196  20.824  1.00 56.49  ? 28  PRO B CD  1 
ATOM   4310  N N   . TRP B 1 29  ? -24.425 39.388  21.979  1.00 56.10  ? 29  TRP B N   1 
ATOM   4311  C CA  . TRP B 1 29  ? -23.191 38.883  22.571  1.00 51.12  ? 29  TRP B CA  1 
ATOM   4312  C C   . TRP B 1 29  ? -22.404 39.982  23.273  1.00 47.84  ? 29  TRP B C   1 
ATOM   4313  O O   . TRP B 1 29  ? -21.836 39.758  24.347  1.00 50.54  ? 29  TRP B O   1 
ATOM   4314  C CB  . TRP B 1 29  ? -22.350 38.220  21.495  1.00 45.85  ? 29  TRP B CB  1 
ATOM   4315  C CG  . TRP B 1 29  ? -23.016 37.047  20.891  1.00 48.87  ? 29  TRP B CG  1 
ATOM   4316  C CD1 . TRP B 1 29  ? -23.285 36.859  19.571  1.00 51.79  ? 29  TRP B CD1 1 
ATOM   4317  C CD2 . TRP B 1 29  ? -23.485 35.872  21.570  1.00 50.55  ? 29  TRP B CD2 1 
ATOM   4318  N NE1 . TRP B 1 29  ? -23.889 35.641  19.380  1.00 54.39  ? 29  TRP B NE1 1 
ATOM   4319  C CE2 . TRP B 1 29  ? -24.025 35.015  20.592  1.00 52.16  ? 29  TRP B CE2 1 
ATOM   4320  C CE3 . TRP B 1 29  ? -23.500 35.461  22.908  1.00 50.73  ? 29  TRP B CE3 1 
ATOM   4321  C CZ2 . TRP B 1 29  ? -24.575 33.773  20.905  1.00 55.98  ? 29  TRP B CZ2 1 
ATOM   4322  C CZ3 . TRP B 1 29  ? -24.048 34.225  23.217  1.00 54.91  ? 29  TRP B CZ3 1 
ATOM   4323  C CH2 . TRP B 1 29  ? -24.577 33.397  22.219  1.00 55.80  ? 29  TRP B CH2 1 
ATOM   4324  N N   . THR B 1 30  ? -22.354 41.174  22.686  1.00 45.86  ? 30  THR B N   1 
ATOM   4325  C CA  . THR B 1 30  ? -21.631 42.261  23.333  1.00 49.38  ? 30  THR B CA  1 
ATOM   4326  C C   . THR B 1 30  ? -22.174 42.532  24.732  1.00 42.55  ? 30  THR B C   1 
ATOM   4327  O O   . THR B 1 30  ? -21.404 42.713  25.679  1.00 44.00  ? 30  THR B O   1 
ATOM   4328  C CB  . THR B 1 30  ? -21.700 43.512  22.466  1.00 50.25  ? 30  THR B CB  1 
ATOM   4329  O OG1 . THR B 1 30  ? -21.199 43.202  21.163  1.00 48.09  ? 30  THR B OG1 1 
ATOM   4330  C CG2 . THR B 1 30  ? -20.853 44.605  23.066  1.00 44.21  ? 30  THR B CG2 1 
ATOM   4331  N N   . PHE B 1 31  ? -23.498 42.512  24.893  1.00 53.19  ? 31  PHE B N   1 
ATOM   4332  C CA  . PHE B 1 31  ? -24.095 42.855  26.182  1.00 49.12  ? 31  PHE B CA  1 
ATOM   4333  C C   . PHE B 1 31  ? -23.798 41.785  27.226  1.00 53.14  ? 31  PHE B C   1 
ATOM   4334  O O   . PHE B 1 31  ? -23.391 42.096  28.354  1.00 51.49  ? 31  PHE B O   1 
ATOM   4335  C CB  . PHE B 1 31  ? -25.603 43.061  26.011  1.00 50.27  ? 31  PHE B CB  1 
ATOM   4336  C CG  . PHE B 1 31  ? -26.367 43.176  27.307  1.00 54.36  ? 31  PHE B CG  1 
ATOM   4337  C CD1 . PHE B 1 31  ? -26.519 44.402  27.941  1.00 52.48  ? 31  PHE B CD1 1 
ATOM   4338  C CD2 . PHE B 1 31  ? -26.946 42.055  27.886  1.00 55.31  ? 31  PHE B CD2 1 
ATOM   4339  C CE1 . PHE B 1 31  ? -27.230 44.506  29.130  1.00 52.10  ? 31  PHE B CE1 1 
ATOM   4340  C CE2 . PHE B 1 31  ? -27.655 42.152  29.076  1.00 54.57  ? 31  PHE B CE2 1 
ATOM   4341  C CZ  . PHE B 1 31  ? -27.798 43.376  29.697  1.00 53.30  ? 31  PHE B CZ  1 
ATOM   4342  N N   . PHE B 1 32  ? -23.973 40.514  26.858  1.00 52.16  ? 32  PHE B N   1 
ATOM   4343  C CA  . PHE B 1 32  ? -23.811 39.432  27.826  1.00 55.43  ? 32  PHE B CA  1 
ATOM   4344  C C   . PHE B 1 32  ? -22.373 39.311  28.305  1.00 48.29  ? 32  PHE B C   1 
ATOM   4345  O O   . PHE B 1 32  ? -22.125 38.984  29.470  1.00 50.47  ? 32  PHE B O   1 
ATOM   4346  C CB  . PHE B 1 32  ? -24.279 38.112  27.220  1.00 56.22  ? 32  PHE B CB  1 
ATOM   4347  C CG  . PHE B 1 32  ? -25.767 37.963  27.180  1.00 53.62  ? 32  PHE B CG  1 
ATOM   4348  C CD1 . PHE B 1 32  ? -26.524 38.142  28.325  1.00 51.73  ? 32  PHE B CD1 1 
ATOM   4349  C CD2 . PHE B 1 32  ? -26.411 37.646  25.997  1.00 55.88  ? 32  PHE B CD2 1 
ATOM   4350  C CE1 . PHE B 1 32  ? -27.896 38.005  28.293  1.00 59.07  ? 32  PHE B CE1 1 
ATOM   4351  C CE2 . PHE B 1 32  ? -27.786 37.508  25.956  1.00 58.66  ? 32  PHE B CE2 1 
ATOM   4352  C CZ  . PHE B 1 32  ? -28.531 37.687  27.107  1.00 61.13  ? 32  PHE B CZ  1 
ATOM   4353  N N   . HIS B 1 33  ? -21.408 39.558  27.424  1.00 52.54  ? 33  HIS B N   1 
ATOM   4354  C CA  . HIS B 1 33  ? -20.021 39.466  27.850  1.00 51.60  ? 33  HIS B CA  1 
ATOM   4355  C C   . HIS B 1 33  ? -19.574 40.713  28.594  1.00 51.92  ? 33  HIS B C   1 
ATOM   4356  O O   . HIS B 1 33  ? -18.574 40.669  29.319  1.00 52.22  ? 33  HIS B O   1 
ATOM   4357  C CB  . HIS B 1 33  ? -19.128 39.179  26.649  1.00 42.84  ? 33  HIS B CB  1 
ATOM   4358  C CG  . HIS B 1 33  ? -19.133 37.739  26.249  1.00 45.89  ? 33  HIS B CG  1 
ATOM   4359  N ND1 . HIS B 1 33  ? -18.894 36.719  27.148  1.00 44.79  ? 33  HIS B ND1 1 
ATOM   4360  C CD2 . HIS B 1 33  ? -19.388 37.142  25.061  1.00 49.79  ? 33  HIS B CD2 1 
ATOM   4361  C CE1 . HIS B 1 33  ? -18.983 35.557  26.525  1.00 46.32  ? 33  HIS B CE1 1 
ATOM   4362  N NE2 . HIS B 1 33  ? -19.281 35.785  25.258  1.00 48.39  ? 33  HIS B NE2 1 
ATOM   4363  N N   . ALA B 1 34  ? -20.314 41.812  28.459  1.00 49.66  ? 34  ALA B N   1 
ATOM   4364  C CA  . ALA B 1 34  ? -20.043 42.981  29.285  1.00 53.07  ? 34  ALA B CA  1 
ATOM   4365  C C   . ALA B 1 34  ? -20.426 42.722  30.736  1.00 56.92  ? 34  ALA B C   1 
ATOM   4366  O O   . ALA B 1 34  ? -19.682 43.076  31.660  1.00 63.61  ? 34  ALA B O   1 
ATOM   4367  C CB  . ALA B 1 34  ? -20.782 44.201  28.736  1.00 37.73  ? 34  ALA B CB  1 
ATOM   4368  N N   . VAL B 1 35  ? -21.579 42.089  30.960  1.00 47.62  ? 35  VAL B N   1 
ATOM   4369  C CA  . VAL B 1 35  ? -22.018 41.886  32.334  1.00 50.39  ? 35  VAL B CA  1 
ATOM   4370  C C   . VAL B 1 35  ? -21.219 40.769  32.995  1.00 49.49  ? 35  VAL B C   1 
ATOM   4371  O O   . VAL B 1 35  ? -20.943 40.825  34.196  1.00 56.62  ? 35  VAL B O   1 
ATOM   4372  C CB  . VAL B 1 35  ? -23.536 41.617  32.376  1.00 53.48  ? 35  VAL B CB  1 
ATOM   4373  C CG1 . VAL B 1 35  ? -24.308 42.832  31.863  1.00 46.71  ? 35  VAL B CG1 1 
ATOM   4374  C CG2 . VAL B 1 35  ? -23.878 40.416  31.551  1.00 52.56  ? 35  VAL B CG2 1 
ATOM   4375  N N   . LYS B 1 36  ? -20.800 39.762  32.232  1.00 47.03  ? 36  LYS B N   1 
ATOM   4376  C CA  . LYS B 1 36  ? -20.134 38.622  32.845  1.00 50.30  ? 36  LYS B CA  1 
ATOM   4377  C C   . LYS B 1 36  ? -18.629 38.810  32.998  1.00 54.66  ? 36  LYS B C   1 
ATOM   4378  O O   . LYS B 1 36  ? -18.073 38.438  34.034  1.00 64.05  ? 36  LYS B O   1 
ATOM   4379  C CB  . LYS B 1 36  ? -20.398 37.351  32.040  1.00 56.11  ? 36  LYS B CB  1 
ATOM   4380  C CG  . LYS B 1 36  ? -20.408 36.094  32.897  1.00 57.72  ? 36  LYS B CG  1 
ATOM   4381  C CD  . LYS B 1 36  ? -20.777 34.855  32.103  1.00 48.47  ? 36  LYS B CD  1 
ATOM   4382  C CE  . LYS B 1 36  ? -20.014 34.775  30.783  1.00 54.77  ? 36  LYS B CE  1 
ATOM   4383  N NZ  . LYS B 1 36  ? -18.574 34.417  30.898  1.00 56.07  ? 36  LYS B NZ  1 
ATOM   4384  N N   . ASP B 1 37  ? -17.956 39.377  31.999  1.00 52.73  ? 37  ASP B N   1 
ATOM   4385  C CA  . ASP B 1 37  ? -16.499 39.328  31.917  1.00 46.42  ? 37  ASP B CA  1 
ATOM   4386  C C   . ASP B 1 37  ? -15.807 40.684  31.759  1.00 50.22  ? 37  ASP B C   1 
ATOM   4387  O O   . ASP B 1 37  ? -14.739 40.873  32.340  1.00 54.18  ? 37  ASP B O   1 
ATOM   4388  C CB  . ASP B 1 37  ? -16.076 38.419  30.744  1.00 52.82  ? 37  ASP B CB  1 
ATOM   4389  C CG  . ASP B 1 37  ? -16.910 37.128  30.653  1.00 56.70  ? 37  ASP B CG  1 
ATOM   4390  O OD1 . ASP B 1 37  ? -16.773 36.253  31.542  1.00 49.28  ? 37  ASP B OD1 1 
ATOM   4391  O OD2 . ASP B 1 37  ? -17.696 36.982  29.681  1.00 48.79  ? 37  ASP B OD2 1 
ATOM   4392  N N   . TYR B 1 38  ? -16.386 41.644  31.024  1.00 53.22  ? 38  TYR B N   1 
ATOM   4393  C CA  . TYR B 1 38  ? -15.624 42.834  30.633  1.00 48.13  ? 38  TYR B CA  1 
ATOM   4394  C C   . TYR B 1 38  ? -15.399 43.804  31.786  1.00 48.04  ? 38  TYR B C   1 
ATOM   4395  O O   . TYR B 1 38  ? -14.458 44.602  31.734  1.00 39.10  ? 38  TYR B O   1 
ATOM   4396  C CB  . TYR B 1 38  ? -16.313 43.549  29.473  1.00 46.20  ? 38  TYR B CB  1 
ATOM   4397  C CG  . TYR B 1 38  ? -16.282 42.746  28.199  1.00 54.26  ? 38  TYR B CG  1 
ATOM   4398  C CD1 . TYR B 1 38  ? -15.253 41.850  27.955  1.00 47.73  ? 38  TYR B CD1 1 
ATOM   4399  C CD2 . TYR B 1 38  ? -17.289 42.867  27.242  1.00 51.57  ? 38  TYR B CD2 1 
ATOM   4400  C CE1 . TYR B 1 38  ? -15.218 41.095  26.796  1.00 50.24  ? 38  TYR B CE1 1 
ATOM   4401  C CE2 . TYR B 1 38  ? -17.262 42.116  26.079  1.00 46.42  ? 38  TYR B CE2 1 
ATOM   4402  C CZ  . TYR B 1 38  ? -16.222 41.230  25.861  1.00 50.60  ? 38  TYR B CZ  1 
ATOM   4403  O OH  . TYR B 1 38  ? -16.176 40.472  24.712  1.00 47.70  ? 38  TYR B OH  1 
ATOM   4404  N N   . TYR B 1 39  ? -16.243 43.775  32.815  1.00 49.80  ? 39  TYR B N   1 
ATOM   4405  C CA  . TYR B 1 39  ? -15.931 44.502  34.041  1.00 52.49  ? 39  TYR B CA  1 
ATOM   4406  C C   . TYR B 1 39  ? -15.262 43.619  35.082  1.00 53.93  ? 39  TYR B C   1 
ATOM   4407  O O   . TYR B 1 39  ? -14.341 44.068  35.769  1.00 54.17  ? 39  TYR B O   1 
ATOM   4408  C CB  . TYR B 1 39  ? -17.196 45.122  34.650  1.00 53.10  ? 39  TYR B CB  1 
ATOM   4409  C CG  . TYR B 1 39  ? -16.991 45.820  35.993  1.00 53.88  ? 39  TYR B CG  1 
ATOM   4410  C CD1 . TYR B 1 39  ? -17.089 45.119  37.190  1.00 55.59  ? 39  TYR B CD1 1 
ATOM   4411  C CD2 . TYR B 1 39  ? -16.714 47.181  36.057  1.00 52.74  ? 39  TYR B CD2 1 
ATOM   4412  C CE1 . TYR B 1 39  ? -16.899 45.750  38.415  1.00 59.91  ? 39  TYR B CE1 1 
ATOM   4413  C CE2 . TYR B 1 39  ? -16.529 47.822  37.280  1.00 61.97  ? 39  TYR B CE2 1 
ATOM   4414  C CZ  . TYR B 1 39  ? -16.622 47.101  38.456  1.00 67.19  ? 39  TYR B CZ  1 
ATOM   4415  O OH  . TYR B 1 39  ? -16.437 47.728  39.673  1.00 62.62  ? 39  TYR B OH  1 
ATOM   4416  N N   . ASP B 1 40  ? -15.693 42.363  35.200  1.00 57.09  ? 40  ASP B N   1 
ATOM   4417  C CA  . ASP B 1 40  ? -15.263 41.544  36.326  1.00 55.01  ? 40  ASP B CA  1 
ATOM   4418  C C   . ASP B 1 40  ? -13.822 41.096  36.171  1.00 53.25  ? 40  ASP B C   1 
ATOM   4419  O O   . ASP B 1 40  ? -13.088 41.024  37.161  1.00 55.24  ? 40  ASP B O   1 
ATOM   4420  C CB  . ASP B 1 40  ? -16.188 40.341  36.484  1.00 54.02  ? 40  ASP B CB  1 
ATOM   4421  C CG  . ASP B 1 40  ? -17.508 40.713  37.125  1.00 63.12  ? 40  ASP B CG  1 
ATOM   4422  O OD1 . ASP B 1 40  ? -17.523 40.976  38.346  1.00 67.38  ? 40  ASP B OD1 1 
ATOM   4423  O OD2 . ASP B 1 40  ? -18.525 40.777  36.403  1.00 67.15  ? 40  ASP B OD2 1 
ATOM   4424  N N   . MET B 1 41  ? -13.396 40.797  34.941  1.00 55.50  ? 41  MET B N   1 
ATOM   4425  C CA  . MET B 1 41  ? -12.022 40.340  34.732  1.00 57.06  ? 41  MET B CA  1 
ATOM   4426  C C   . MET B 1 41  ? -10.984 41.366  35.168  1.00 51.71  ? 41  MET B C   1 
ATOM   4427  O O   . MET B 1 41  ? -10.071 40.994  35.925  1.00 54.31  ? 41  MET B O   1 
ATOM   4428  C CB  . MET B 1 41  ? -11.809 39.924  33.272  1.00 45.08  ? 41  MET B CB  1 
ATOM   4429  C CG  . MET B 1 41  ? -12.274 38.515  32.948  1.00 42.73  ? 41  MET B CG  1 
ATOM   4430  S SD  . MET B 1 41  ? -11.213 37.165  33.510  1.00 57.02  ? 41  MET B SD  1 
ATOM   4431  C CE  . MET B 1 41  ? -9.658  37.985  33.900  1.00 54.98  ? 41  MET B CE  1 
ATOM   4432  N N   . PRO B 1 42  ? -11.047 42.640  34.761  1.00 48.22  ? 42  PRO B N   1 
ATOM   4433  C CA  . PRO B 1 42  ? -10.171 43.631  35.401  1.00 50.38  ? 42  PRO B CA  1 
ATOM   4434  C C   . PRO B 1 42  ? -10.478 43.850  36.870  1.00 46.38  ? 42  PRO B C   1 
ATOM   4435  O O   . PRO B 1 42  ? -9.591  44.301  37.600  1.00 45.18  ? 42  PRO B O   1 
ATOM   4436  C CB  . PRO B 1 42  ? -10.415 44.908  34.580  1.00 44.66  ? 42  PRO B CB  1 
ATOM   4437  C CG  . PRO B 1 42  ? -11.715 44.709  33.939  1.00 38.57  ? 42  PRO B CG  1 
ATOM   4438  C CD  . PRO B 1 42  ? -11.798 43.244  33.647  1.00 41.50  ? 42  PRO B CD  1 
ATOM   4439  N N   . ALA B 1 43  ? -11.693 43.538  37.329  1.00 53.95  ? 43  ALA B N   1 
ATOM   4440  C CA  . ALA B 1 43  ? -12.091 43.818  38.704  1.00 52.47  ? 43  ALA B CA  1 
ATOM   4441  C C   . ALA B 1 43  ? -11.452 42.878  39.710  1.00 52.55  ? 43  ALA B C   1 
ATOM   4442  O O   . ALA B 1 43  ? -11.459 43.190  40.906  1.00 58.06  ? 43  ALA B O   1 
ATOM   4443  C CB  . ALA B 1 43  ? -13.613 43.737  38.850  1.00 56.50  ? 43  ALA B CB  1 
ATOM   4444  N N   . TYR B 1 44  ? -10.937 41.727  39.263  1.00 52.56  ? 44  TYR B N   1 
ATOM   4445  C CA  . TYR B 1 44  ? -10.166 40.872  40.158  1.00 57.56  ? 44  TYR B CA  1 
ATOM   4446  C C   . TYR B 1 44  ? -8.992  41.640  40.760  1.00 59.21  ? 44  TYR B C   1 
ATOM   4447  O O   . TYR B 1 44  ? -8.635  41.416  41.924  1.00 57.93  ? 44  TYR B O   1 
ATOM   4448  C CB  . TYR B 1 44  ? -9.668  39.620  39.415  1.00 50.81  ? 44  TYR B CB  1 
ATOM   4449  C CG  . TYR B 1 44  ? -10.717 38.556  39.127  1.00 51.91  ? 44  TYR B CG  1 
ATOM   4450  C CD1 . TYR B 1 44  ? -11.615 38.698  38.076  1.00 60.97  ? 44  TYR B CD1 1 
ATOM   4451  C CD2 . TYR B 1 44  ? -10.796 37.395  39.888  1.00 54.07  ? 44  TYR B CD2 1 
ATOM   4452  C CE1 . TYR B 1 44  ? -12.579 37.726  37.801  1.00 55.16  ? 44  TYR B CE1 1 
ATOM   4453  C CE2 . TYR B 1 44  ? -11.756 36.410  39.621  1.00 54.11  ? 44  TYR B CE2 1 
ATOM   4454  C CZ  . TYR B 1 44  ? -12.644 36.582  38.575  1.00 61.32  ? 44  TYR B CZ  1 
ATOM   4455  O OH  . TYR B 1 44  ? -13.593 35.616  38.304  1.00 57.91  ? 44  TYR B OH  1 
ATOM   4456  N N   . LEU B 1 45  ? -8.410  42.572  39.990  1.00 49.60  ? 45  LEU B N   1 
ATOM   4457  C CA  . LEU B 1 45  ? -7.238  43.320  40.436  1.00 56.13  ? 45  LEU B CA  1 
ATOM   4458  C C   . LEU B 1 45  ? -7.523  44.140  41.686  1.00 60.53  ? 45  LEU B C   1 
ATOM   4459  O O   . LEU B 1 45  ? -6.618  44.370  42.496  1.00 56.88  ? 45  LEU B O   1 
ATOM   4460  C CB  . LEU B 1 45  ? -6.739  44.237  39.315  1.00 52.23  ? 45  LEU B CB  1 
ATOM   4461  C CG  . LEU B 1 45  ? -6.064  43.546  38.126  1.00 55.25  ? 45  LEU B CG  1 
ATOM   4462  C CD1 . LEU B 1 45  ? -6.203  44.354  36.829  1.00 47.19  ? 45  LEU B CD1 1 
ATOM   4463  C CD2 . LEU B 1 45  ? -4.600  43.225  38.424  1.00 49.58  ? 45  LEU B CD2 1 
ATOM   4464  N N   . LYS B 1 46  ? -8.761  44.603  41.857  1.00 58.64  ? 46  LYS B N   1 
ATOM   4465  C CA  . LYS B 1 46  ? -9.105  45.310  43.083  1.00 56.56  ? 46  LYS B CA  1 
ATOM   4466  C C   . LYS B 1 46  ? -9.075  44.389  44.292  1.00 58.90  ? 46  LYS B C   1 
ATOM   4467  O O   . LYS B 1 46  ? -8.928  44.871  45.419  1.00 61.53  ? 46  LYS B O   1 
ATOM   4468  C CB  . LYS B 1 46  ? -10.479 45.957  42.946  1.00 53.82  ? 46  LYS B CB  1 
ATOM   4469  C CG  . LYS B 1 46  ? -10.677 46.645  41.614  1.00 64.25  ? 46  LYS B CG  1 
ATOM   4470  C CD  . LYS B 1 46  ? -12.148 46.802  41.272  1.00 73.66  ? 46  LYS B CD  1 
ATOM   4471  C CE  . LYS B 1 46  ? -12.910 47.532  42.371  1.00 72.65  ? 46  LYS B CE  1 
ATOM   4472  N NZ  . LYS B 1 46  ? -14.100 48.256  41.842  1.00 69.26  ? 46  LYS B NZ  1 
ATOM   4473  N N   . ASP B 1 47  ? -9.188  43.079  44.082  1.00 57.17  ? 47  ASP B N   1 
ATOM   4474  C CA  . ASP B 1 47  ? -9.226  42.123  45.177  1.00 63.20  ? 47  ASP B CA  1 
ATOM   4475  C C   . ASP B 1 47  ? -7.950  41.304  45.318  1.00 62.85  ? 47  ASP B C   1 
ATOM   4476  O O   . ASP B 1 47  ? -7.848  40.512  46.262  1.00 70.56  ? 47  ASP B O   1 
ATOM   4477  C CB  . ASP B 1 47  ? -10.421 41.168  45.007  1.00 65.64  ? 47  ASP B CB  1 
ATOM   4478  C CG  . ASP B 1 47  ? -11.763 41.856  45.218  1.00 75.11  ? 47  ASP B CG  1 
ATOM   4479  O OD1 . ASP B 1 47  ? -11.789 43.103  45.279  1.00 90.44  ? 47  ASP B OD1 1 
ATOM   4480  O OD2 . ASP B 1 47  ? -12.794 41.153  45.316  1.00 80.43  ? 47  ASP B OD2 1 
ATOM   4481  N N   . PHE B 1 48  ? -6.979  41.465  44.418  1.00 58.18  ? 48  PHE B N   1 
ATOM   4482  C CA  . PHE B 1 48  ? -5.793  40.622  44.412  1.00 59.17  ? 48  PHE B CA  1 
ATOM   4483  C C   . PHE B 1 48  ? -4.578  41.445  44.020  1.00 68.49  ? 48  PHE B C   1 
ATOM   4484  O O   . PHE B 1 48  ? -4.611  42.196  43.039  1.00 71.78  ? 48  PHE B O   1 
ATOM   4485  C CB  . PHE B 1 48  ? -5.930  39.424  43.450  1.00 59.67  ? 48  PHE B CB  1 
ATOM   4486  C CG  . PHE B 1 48  ? -7.014  38.445  43.835  1.00 67.23  ? 48  PHE B CG  1 
ATOM   4487  C CD1 . PHE B 1 48  ? -6.748  37.392  44.697  1.00 66.19  ? 48  PHE B CD1 1 
ATOM   4488  C CD2 . PHE B 1 48  ? -8.304  38.585  43.339  1.00 61.23  ? 48  PHE B CD2 1 
ATOM   4489  C CE1 . PHE B 1 48  ? -7.750  36.494  45.052  1.00 56.17  ? 48  PHE B CE1 1 
ATOM   4490  C CE2 . PHE B 1 48  ? -9.296  37.694  43.683  1.00 58.96  ? 48  PHE B CE2 1 
ATOM   4491  C CZ  . PHE B 1 48  ? -9.016  36.646  44.545  1.00 59.23  ? 48  PHE B CZ  1 
ATOM   4492  N N   . GLU B 1 49  ? -3.503  41.284  44.794  1.00 73.82  ? 49  GLU B N   1 
ATOM   4493  C CA  . GLU B 1 49  ? -2.253  42.016  44.590  1.00 68.16  ? 49  GLU B CA  1 
ATOM   4494  C C   . GLU B 1 49  ? -1.392  41.289  43.557  1.00 65.00  ? 49  GLU B C   1 
ATOM   4495  O O   . GLU B 1 49  ? -0.337  40.728  43.854  1.00 68.66  ? 49  GLU B O   1 
ATOM   4496  C CB  . GLU B 1 49  ? -1.512  42.179  45.912  1.00 63.59  ? 49  GLU B CB  1 
ATOM   4497  C CG  . GLU B 1 49  ? -1.782  43.491  46.630  1.00 79.74  ? 49  GLU B CG  1 
ATOM   4498  C CD  . GLU B 1 49  ? -2.789  43.352  47.761  1.00 93.69  ? 49  GLU B CD  1 
ATOM   4499  O OE1 . GLU B 1 49  ? -3.178  42.208  48.081  1.00 88.30  ? 49  GLU B OE1 1 
ATOM   4500  O OE2 . GLU B 1 49  ? -3.193  44.389  48.330  1.00 94.05  ? 49  GLU B OE2 1 
ATOM   4501  N N   . ILE B 1 50  ? -1.884  41.287  42.323  1.00 61.40  ? 50  ILE B N   1 
ATOM   4502  C CA  . ILE B 1 50  ? -1.147  40.794  41.166  1.00 61.97  ? 50  ILE B CA  1 
ATOM   4503  C C   . ILE B 1 50  ? -1.324  41.792  40.027  1.00 58.89  ? 50  ILE B C   1 
ATOM   4504  O O   . ILE B 1 50  ? -2.020  42.802  40.161  1.00 58.43  ? 50  ILE B O   1 
ATOM   4505  C CB  . ILE B 1 50  ? -1.607  39.388  40.734  1.00 54.85  ? 50  ILE B CB  1 
ATOM   4506  C CG1 . ILE B 1 50  ? -3.108  39.409  40.439  1.00 65.07  ? 50  ILE B CG1 1 
ATOM   4507  C CG2 . ILE B 1 50  ? -1.250  38.361  41.782  1.00 50.14  ? 50  ILE B CG2 1 
ATOM   4508  C CD1 . ILE B 1 50  ? -3.606  38.176  39.745  1.00 60.17  ? 50  ILE B CD1 1 
ATOM   4509  N N   . LYS B 1 51  ? -0.687  41.503  38.896  1.00 54.68  ? 51  LYS B N   1 
ATOM   4510  C CA  . LYS B 1 51  ? -0.749  42.350  37.713  1.00 51.80  ? 51  LYS B CA  1 
ATOM   4511  C C   . LYS B 1 51  ? -1.459  41.602  36.595  1.00 55.65  ? 51  LYS B C   1 
ATOM   4512  O O   . LYS B 1 51  ? -1.150  40.434  36.327  1.00 55.03  ? 51  LYS B O   1 
ATOM   4513  C CB  . LYS B 1 51  ? 0.652   42.767  37.258  1.00 51.65  ? 51  LYS B CB  1 
ATOM   4514  C CG  . LYS B 1 51  ? 1.417   43.590  38.277  1.00 48.41  ? 51  LYS B CG  1 
ATOM   4515  C CD  . LYS B 1 51  ? 0.726   44.908  38.581  1.00 48.44  ? 51  LYS B CD  1 
ATOM   4516  C CE  . LYS B 1 51  ? 1.673   45.900  39.241  1.00 51.44  ? 51  LYS B CE  1 
ATOM   4517  N NZ  . LYS B 1 51  ? 0.942   46.938  40.025  1.00 62.50  ? 51  LYS B NZ  1 
ATOM   4518  N N   . LEU B 1 52  ? -2.400  42.279  35.941  1.00 55.36  ? 52  LEU B N   1 
ATOM   4519  C CA  . LEU B 1 52  ? -3.147  41.720  34.822  1.00 48.75  ? 52  LEU B CA  1 
ATOM   4520  C C   . LEU B 1 52  ? -3.228  42.755  33.710  1.00 49.57  ? 52  LEU B C   1 
ATOM   4521  O O   . LEU B 1 52  ? -3.470  43.935  33.970  1.00 52.86  ? 52  LEU B O   1 
ATOM   4522  C CB  . LEU B 1 52  ? -4.560  41.299  35.250  1.00 45.57  ? 52  LEU B CB  1 
ATOM   4523  C CG  . LEU B 1 52  ? -4.686  40.141  36.243  1.00 50.03  ? 52  LEU B CG  1 
ATOM   4524  C CD1 . LEU B 1 52  ? -6.126  39.951  36.691  1.00 45.07  ? 52  LEU B CD1 1 
ATOM   4525  C CD2 . LEU B 1 52  ? -4.167  38.865  35.627  1.00 54.67  ? 52  LEU B CD2 1 
ATOM   4526  N N   . ASN B 1 53  ? -3.028  42.312  32.474  1.00 52.97  ? 53  ASN B N   1 
ATOM   4527  C CA  . ASN B 1 53  ? -3.086  43.190  31.315  1.00 48.16  ? 53  ASN B CA  1 
ATOM   4528  C C   . ASN B 1 53  ? -4.256  42.795  30.429  1.00 43.76  ? 53  ASN B C   1 
ATOM   4529  O O   . ASN B 1 53  ? -4.643  41.624  30.371  1.00 47.05  ? 53  ASN B O   1 
ATOM   4530  C CB  . ASN B 1 53  ? -1.787  43.138  30.518  1.00 42.28  ? 53  ASN B CB  1 
ATOM   4531  C CG  . ASN B 1 53  ? -0.595  43.472  31.361  1.00 44.63  ? 53  ASN B CG  1 
ATOM   4532  O OD1 . ASN B 1 53  ? -0.277  44.643  31.565  1.00 45.99  ? 53  ASN B OD1 1 
ATOM   4533  N ND2 . ASN B 1 53  ? 0.075   42.444  31.870  1.00 43.09  ? 53  ASN B ND2 1 
ATOM   4534  N N   . PHE B 1 54  ? -4.812  43.781  29.730  1.00 44.47  ? 54  PHE B N   1 
ATOM   4535  C CA  . PHE B 1 54  ? -6.012  43.573  28.937  1.00 39.60  ? 54  PHE B CA  1 
ATOM   4536  C C   . PHE B 1 54  ? -5.881  44.268  27.594  1.00 46.49  ? 54  PHE B C   1 
ATOM   4537  O O   . PHE B 1 54  ? -5.198  45.289  27.461  1.00 49.15  ? 54  PHE B O   1 
ATOM   4538  C CB  . PHE B 1 54  ? -7.253  44.090  29.668  1.00 42.86  ? 54  PHE B CB  1 
ATOM   4539  C CG  . PHE B 1 54  ? -7.443  43.471  31.011  1.00 47.23  ? 54  PHE B CG  1 
ATOM   4540  C CD1 . PHE B 1 54  ? -6.871  44.039  32.139  1.00 40.27  ? 54  PHE B CD1 1 
ATOM   4541  C CD2 . PHE B 1 54  ? -8.143  42.288  31.140  1.00 41.04  ? 54  PHE B CD2 1 
ATOM   4542  C CE1 . PHE B 1 54  ? -7.025  43.451  33.371  1.00 44.83  ? 54  PHE B CE1 1 
ATOM   4543  C CE2 . PHE B 1 54  ? -8.299  41.697  32.373  1.00 45.51  ? 54  PHE B CE2 1 
ATOM   4544  C CZ  . PHE B 1 54  ? -7.739  42.275  33.487  1.00 45.77  ? 54  PHE B CZ  1 
ATOM   4545  N N   . ASN B 1 55  ? -6.547  43.696  26.597  1.00 48.43  ? 55  ASN B N   1 
ATOM   4546  C CA  . ASN B 1 55  ? -6.667  44.293  25.277  1.00 47.56  ? 55  ASN B CA  1 
ATOM   4547  C C   . ASN B 1 55  ? -8.141  44.517  24.972  1.00 48.68  ? 55  ASN B C   1 
ATOM   4548  O O   . ASN B 1 55  ? -8.954  43.597  25.112  1.00 49.48  ? 55  ASN B O   1 
ATOM   4549  C CB  . ASN B 1 55  ? -6.029  43.404  24.210  1.00 47.47  ? 55  ASN B CB  1 
ATOM   4550  C CG  . ASN B 1 55  ? -6.278  43.915  22.809  1.00 50.86  ? 55  ASN B CG  1 
ATOM   4551  O OD1 . ASN B 1 55  ? -7.296  43.598  22.185  1.00 45.73  ? 55  ASN B OD1 1 
ATOM   4552  N ND2 . ASN B 1 55  ? -5.359  44.734  22.314  1.00 44.20  ? 55  ASN B ND2 1 
ATOM   4553  N N   . LEU B 1 56  ? -8.485  45.735  24.567  1.00 43.03  ? 56  LEU B N   1 
ATOM   4554  C CA  . LEU B 1 56  ? -9.855  46.087  24.220  1.00 42.16  ? 56  LEU B CA  1 
ATOM   4555  C C   . LEU B 1 56  ? -9.852  46.655  22.811  1.00 42.01  ? 56  LEU B C   1 
ATOM   4556  O O   . LEU B 1 56  ? -9.113  47.602  22.525  1.00 46.58  ? 56  LEU B O   1 
ATOM   4557  C CB  . LEU B 1 56  ? -10.432 47.091  25.216  1.00 49.93  ? 56  LEU B CB  1 
ATOM   4558  C CG  . LEU B 1 56  ? -10.669 46.559  26.633  1.00 51.26  ? 56  LEU B CG  1 
ATOM   4559  C CD1 . LEU B 1 56  ? -9.754  47.287  27.577  1.00 54.70  ? 56  LEU B CD1 1 
ATOM   4560  C CD2 . LEU B 1 56  ? -12.109 46.747  27.074  1.00 56.15  ? 56  LEU B CD2 1 
ATOM   4561  N N   . THR B 1 57  ? -10.652 46.061  21.935  1.00 44.48  ? 57  THR B N   1 
ATOM   4562  C CA  . THR B 1 57  ? -10.733 46.517  20.556  1.00 40.87  ? 57  THR B CA  1 
ATOM   4563  C C   . THR B 1 57  ? -11.658 47.724  20.460  1.00 43.84  ? 57  THR B C   1 
ATOM   4564  O O   . THR B 1 57  ? -12.682 47.781  21.151  1.00 46.89  ? 57  THR B O   1 
ATOM   4565  C CB  . THR B 1 57  ? -11.242 45.411  19.643  1.00 38.28  ? 57  THR B CB  1 
ATOM   4566  O OG1 . THR B 1 57  ? -12.378 44.786  20.245  1.00 48.42  ? 57  THR B OG1 1 
ATOM   4567  C CG2 . THR B 1 57  ? -10.165 44.385  19.416  1.00 41.78  ? 57  THR B CG2 1 
ATOM   4568  N N   . PRO B 1 58  ? -11.321 48.691  19.606  1.00 43.62  ? 58  PRO B N   1 
ATOM   4569  C CA  . PRO B 1 58  ? -12.156 49.895  19.502  1.00 48.55  ? 58  PRO B CA  1 
ATOM   4570  C C   . PRO B 1 58  ? -13.601 49.603  19.147  1.00 47.36  ? 58  PRO B C   1 
ATOM   4571  O O   . PRO B 1 58  ? -14.508 50.257  19.678  1.00 49.62  ? 58  PRO B O   1 
ATOM   4572  C CB  . PRO B 1 58  ? -11.439 50.701  18.416  1.00 43.88  ? 58  PRO B CB  1 
ATOM   4573  C CG  . PRO B 1 58  ? -10.003 50.272  18.565  1.00 42.46  ? 58  PRO B CG  1 
ATOM   4574  C CD  . PRO B 1 58  ? -10.101 48.799  18.791  1.00 40.78  ? 58  PRO B CD  1 
ATOM   4575  N N   . VAL B 1 59  ? -13.849 48.625  18.276  1.00 38.39  ? 59  VAL B N   1 
ATOM   4576  C CA  . VAL B 1 59  ? -15.229 48.326  17.909  1.00 49.64  ? 59  VAL B CA  1 
ATOM   4577  C C   . VAL B 1 59  ? -16.006 47.844  19.130  1.00 49.86  ? 59  VAL B C   1 
ATOM   4578  O O   . VAL B 1 59  ? -17.188 48.164  19.297  1.00 46.31  ? 59  VAL B O   1 
ATOM   4579  C CB  . VAL B 1 59  ? -15.266 47.310  16.752  1.00 42.55  ? 59  VAL B CB  1 
ATOM   4580  C CG1 . VAL B 1 59  ? -14.241 46.220  16.976  1.00 45.52  ? 59  VAL B CG1 1 
ATOM   4581  C CG2 . VAL B 1 59  ? -16.646 46.724  16.620  1.00 45.56  ? 59  VAL B CG2 1 
ATOM   4582  N N   . LEU B 1 60  ? -15.350 47.086  20.015  1.00 48.80  ? 60  LEU B N   1 
ATOM   4583  C CA  . LEU B 1 60  ? -15.999 46.698  21.262  1.00 48.65  ? 60  LEU B CA  1 
ATOM   4584  C C   . LEU B 1 60  ? -16.250 47.916  22.138  1.00 47.45  ? 60  LEU B C   1 
ATOM   4585  O O   . LEU B 1 60  ? -17.332 48.069  22.717  1.00 48.85  ? 60  LEU B O   1 
ATOM   4586  C CB  . LEU B 1 60  ? -15.151 45.666  22.007  1.00 48.53  ? 60  LEU B CB  1 
ATOM   4587  C CG  . LEU B 1 60  ? -15.656 45.372  23.428  1.00 51.71  ? 60  LEU B CG  1 
ATOM   4588  C CD1 . LEU B 1 60  ? -16.997 44.654  23.380  1.00 44.30  ? 60  LEU B CD1 1 
ATOM   4589  C CD2 . LEU B 1 60  ? -14.647 44.583  24.260  1.00 44.33  ? 60  LEU B CD2 1 
ATOM   4590  N N   . ILE B 1 61  ? -15.266 48.809  22.224  1.00 49.37  ? 61  ILE B N   1 
ATOM   4591  C CA  . ILE B 1 61  ? -15.415 49.997  23.054  1.00 51.45  ? 61  ILE B CA  1 
ATOM   4592  C C   . ILE B 1 61  ? -16.546 50.875  22.533  1.00 48.91  ? 61  ILE B C   1 
ATOM   4593  O O   . ILE B 1 61  ? -17.315 51.450  23.314  1.00 52.88  ? 61  ILE B O   1 
ATOM   4594  C CB  . ILE B 1 61  ? -14.076 50.750  23.125  1.00 47.59  ? 61  ILE B CB  1 
ATOM   4595  C CG1 . ILE B 1 61  ? -13.004 49.822  23.687  1.00 44.80  ? 61  ILE B CG1 1 
ATOM   4596  C CG2 . ILE B 1 61  ? -14.207 51.988  23.985  1.00 55.25  ? 61  ILE B CG2 1 
ATOM   4597  C CD1 . ILE B 1 61  ? -11.855 50.546  24.321  1.00 56.76  ? 61  ILE B CD1 1 
ATOM   4598  N N   . ASP B 1 62  ? -16.683 50.976  21.208  1.00 49.51  ? 62  ASP B N   1 
ATOM   4599  C CA  . ASP B 1 62  ? -17.797 51.728  20.631  1.00 53.20  ? 62  ASP B CA  1 
ATOM   4600  C C   . ASP B 1 62  ? -19.132 51.157  21.092  1.00 55.84  ? 62  ASP B C   1 
ATOM   4601  O O   . ASP B 1 62  ? -20.036 51.897  21.503  1.00 57.14  ? 62  ASP B O   1 
ATOM   4602  C CB  . ASP B 1 62  ? -17.725 51.706  19.103  1.00 46.20  ? 62  ASP B CB  1 
ATOM   4603  C CG  . ASP B 1 62  ? -16.714 52.690  18.535  1.00 58.15  ? 62  ASP B CG  1 
ATOM   4604  O OD1 . ASP B 1 62  ? -16.405 53.714  19.188  1.00 61.91  ? 62  ASP B OD1 1 
ATOM   4605  O OD2 . ASP B 1 62  ? -16.227 52.431  17.414  1.00 58.55  ? 62  ASP B OD2 1 
ATOM   4606  N N   . GLN B 1 63  ? -19.267 49.831  21.032  1.00 60.01  ? 63  GLN B N   1 
ATOM   4607  C CA  . GLN B 1 63  ? -20.512 49.191  21.436  1.00 54.34  ? 63  GLN B CA  1 
ATOM   4608  C C   . GLN B 1 63  ? -20.788 49.399  22.917  1.00 55.02  ? 63  GLN B C   1 
ATOM   4609  O O   . GLN B 1 63  ? -21.915 49.733  23.299  1.00 56.56  ? 63  GLN B O   1 
ATOM   4610  C CB  . GLN B 1 63  ? -20.463 47.707  21.090  1.00 45.68  ? 63  GLN B CB  1 
ATOM   4611  C CG  . GLN B 1 63  ? -20.264 47.476  19.607  1.00 49.59  ? 63  GLN B CG  1 
ATOM   4612  C CD  . GLN B 1 63  ? -20.097 46.020  19.271  1.00 55.13  ? 63  GLN B CD  1 
ATOM   4613  O OE1 . GLN B 1 63  ? -21.032 45.232  19.408  1.00 57.55  ? 63  GLN B OE1 1 
ATOM   4614  N NE2 . GLN B 1 63  ? -18.905 45.648  18.825  1.00 49.88  ? 63  GLN B NE2 1 
ATOM   4615  N N   . ILE B 1 64  ? -19.772 49.213  23.767  1.00 51.03  ? 64  ILE B N   1 
ATOM   4616  C CA  . ILE B 1 64  ? -19.966 49.426  25.200  1.00 52.62  ? 64  ILE B CA  1 
ATOM   4617  C C   . ILE B 1 64  ? -20.460 50.838  25.463  1.00 53.79  ? 64  ILE B C   1 
ATOM   4618  O O   . ILE B 1 64  ? -21.336 51.057  26.309  1.00 57.70  ? 64  ILE B O   1 
ATOM   4619  C CB  . ILE B 1 64  ? -18.671 49.140  25.981  1.00 56.92  ? 64  ILE B CB  1 
ATOM   4620  C CG1 . ILE B 1 64  ? -18.182 47.715  25.732  1.00 48.22  ? 64  ILE B CG1 1 
ATOM   4621  C CG2 . ILE B 1 64  ? -18.899 49.381  27.471  1.00 52.74  ? 64  ILE B CG2 1 
ATOM   4622  C CD1 . ILE B 1 64  ? -16.893 47.387  26.455  1.00 41.50  ? 64  ILE B CD1 1 
ATOM   4623  N N   . GLN B 1 65  ? -19.910 51.818  24.745  1.00 52.43  ? 65  GLN B N   1 
ATOM   4624  C CA  . GLN B 1 65  ? -20.397 53.183  24.899  1.00 59.28  ? 65  GLN B CA  1 
ATOM   4625  C C   . GLN B 1 65  ? -21.851 53.296  24.467  1.00 55.52  ? 65  GLN B C   1 
ATOM   4626  O O   . GLN B 1 65  ? -22.649 53.966  25.131  1.00 57.88  ? 65  GLN B O   1 
ATOM   4627  C CB  . GLN B 1 65  ? -19.515 54.157  24.118  1.00 58.76  ? 65  GLN B CB  1 
ATOM   4628  C CG  . GLN B 1 65  ? -18.117 54.310  24.714  1.00 60.37  ? 65  GLN B CG  1 
ATOM   4629  C CD  . GLN B 1 65  ? -17.173 55.105  23.832  1.00 65.50  ? 65  GLN B CD  1 
ATOM   4630  O OE1 . GLN B 1 65  ? -17.076 54.867  22.628  1.00 64.80  ? 65  GLN B OE1 1 
ATOM   4631  N NE2 . GLN B 1 65  ? -16.461 56.053  24.434  1.00 62.82  ? 65  GLN B NE2 1 
ATOM   4632  N N   . GLU B 1 66  ? -22.227 52.620  23.376  1.00 55.86  ? 66  GLU B N   1 
ATOM   4633  C CA  . GLU B 1 66  ? -23.614 52.689  22.926  1.00 53.81  ? 66  GLU B CA  1 
ATOM   4634  C C   . GLU B 1 66  ? -24.546 51.974  23.899  1.00 51.63  ? 66  GLU B C   1 
ATOM   4635  O O   . GLU B 1 66  ? -25.662 52.442  24.151  1.00 55.78  ? 66  GLU B O   1 
ATOM   4636  C CB  . GLU B 1 66  ? -23.754 52.109  21.518  1.00 52.71  ? 66  GLU B CB  1 
ATOM   4637  C CG  . GLU B 1 66  ? -25.100 52.425  20.870  1.00 67.14  ? 66  GLU B CG  1 
ATOM   4638  C CD  . GLU B 1 66  ? -25.113 52.231  19.359  1.00 68.13  ? 66  GLU B CD  1 
ATOM   4639  O OE1 . GLU B 1 66  ? -24.590 51.204  18.879  1.00 60.23  ? 66  GLU B OE1 1 
ATOM   4640  O OE2 . GLU B 1 66  ? -25.664 53.102  18.649  1.00 69.54  ? 66  GLU B OE2 1 
ATOM   4641  N N   . TYR B 1 67  ? -24.100 50.853  24.474  1.00 49.91  ? 67  TYR B N   1 
ATOM   4642  C CA  . TYR B 1 67  ? -24.919 50.154  25.460  1.00 51.54  ? 67  TYR B CA  1 
ATOM   4643  C C   . TYR B 1 67  ? -25.000 50.922  26.770  1.00 59.15  ? 67  TYR B C   1 
ATOM   4644  O O   . TYR B 1 67  ? -26.013 50.838  27.475  1.00 66.37  ? 67  TYR B O   1 
ATOM   4645  C CB  . TYR B 1 67  ? -24.370 48.754  25.732  1.00 50.71  ? 67  TYR B CB  1 
ATOM   4646  C CG  . TYR B 1 67  ? -24.912 47.686  24.816  1.00 58.30  ? 67  TYR B CG  1 
ATOM   4647  C CD1 . TYR B 1 67  ? -26.075 46.993  25.132  1.00 51.20  ? 67  TYR B CD1 1 
ATOM   4648  C CD2 . TYR B 1 67  ? -24.249 47.357  23.638  1.00 55.93  ? 67  TYR B CD2 1 
ATOM   4649  C CE1 . TYR B 1 67  ? -26.572 46.008  24.291  1.00 53.11  ? 67  TYR B CE1 1 
ATOM   4650  C CE2 . TYR B 1 67  ? -24.738 46.375  22.794  1.00 58.51  ? 67  TYR B CE2 1 
ATOM   4651  C CZ  . TYR B 1 67  ? -25.897 45.702  23.123  1.00 55.12  ? 67  TYR B CZ  1 
ATOM   4652  O OH  . TYR B 1 67  ? -26.374 44.725  22.274  1.00 62.05  ? 67  TYR B OH  1 
ATOM   4653  N N   . ALA B 1 68  ? -23.952 51.672  27.113  1.00 49.77  ? 68  ALA B N   1 
ATOM   4654  C CA  . ALA B 1 68  ? -23.953 52.395  28.377  1.00 54.38  ? 68  ALA B CA  1 
ATOM   4655  C C   . ALA B 1 68  ? -24.793 53.662  28.325  1.00 53.82  ? 68  ALA B C   1 
ATOM   4656  O O   . ALA B 1 68  ? -25.285 54.105  29.365  1.00 64.60  ? 68  ALA B O   1 
ATOM   4657  C CB  . ALA B 1 68  ? -22.524 52.744  28.789  1.00 61.62  ? 68  ALA B CB  1 
ATOM   4658  N N   . GLN B 1 69  ? -24.960 54.266  27.149  1.00 56.99  ? 69  GLN B N   1 
ATOM   4659  C CA  . GLN B 1 69  ? -25.728 55.497  27.002  1.00 62.34  ? 69  GLN B CA  1 
ATOM   4660  C C   . GLN B 1 69  ? -27.151 55.239  26.505  1.00 61.05  ? 69  GLN B C   1 
ATOM   4661  O O   . GLN B 1 69  ? -27.820 56.172  26.052  1.00 59.23  ? 69  GLN B O   1 
ATOM   4662  C CB  . GLN B 1 69  ? -24.978 56.470  26.077  1.00 61.39  ? 69  GLN B CB  1 
ATOM   4663  C CG  . GLN B 1 69  ? -23.481 56.525  26.394  1.00 69.03  ? 69  GLN B CG  1 
ATOM   4664  C CD  . GLN B 1 69  ? -22.617 57.156  25.306  1.00 85.07  ? 69  GLN B CD  1 
ATOM   4665  O OE1 . GLN B 1 69  ? -23.115 57.676  24.310  1.00 89.80  ? 69  GLN B OE1 1 
ATOM   4666  N NE2 . GLN B 1 69  ? -21.298 57.052  25.475  1.00 77.20  ? 69  GLN B NE2 1 
ATOM   4667  N N   . GLY B 1 70  ? -27.625 53.993  26.597  1.00 61.13  ? 70  GLY B N   1 
ATOM   4668  C CA  . GLY B 1 70  ? -28.994 53.636  26.292  1.00 56.87  ? 70  GLY B CA  1 
ATOM   4669  C C   . GLY B 1 70  ? -29.375 53.636  24.827  1.00 62.86  ? 70  GLY B C   1 
ATOM   4670  O O   . GLY B 1 70  ? -30.539 53.352  24.513  1.00 64.24  ? 70  GLY B O   1 
ATOM   4671  N N   . LYS B 1 71  ? -28.444 53.929  23.918  1.00 60.31  ? 71  LYS B N   1 
ATOM   4672  C CA  . LYS B 1 71  ? -28.793 54.062  22.509  1.00 60.42  ? 71  LYS B CA  1 
ATOM   4673  C C   . LYS B 1 71  ? -28.824 52.740  21.759  1.00 57.05  ? 71  LYS B C   1 
ATOM   4674  O O   . LYS B 1 71  ? -29.317 52.702  20.627  1.00 71.64  ? 71  LYS B O   1 
ATOM   4675  C CB  . LYS B 1 71  ? -27.822 55.008  21.809  1.00 63.90  ? 71  LYS B CB  1 
ATOM   4676  C CG  . LYS B 1 71  ? -27.540 56.276  22.571  1.00 71.90  ? 71  LYS B CG  1 
ATOM   4677  C CD  . LYS B 1 71  ? -26.624 57.156  21.752  1.00 83.03  ? 71  LYS B CD  1 
ATOM   4678  C CE  . LYS B 1 71  ? -25.635 57.888  22.631  1.00 73.25  ? 71  LYS B CE  1 
ATOM   4679  N NZ  . LYS B 1 71  ? -24.259 57.380  22.395  1.00 71.90  ? 71  LYS B NZ  1 
ATOM   4680  N N   . ALA B 1 72  ? -28.332 51.660  22.351  1.00 50.73  ? 72  ALA B N   1 
ATOM   4681  C CA  . ALA B 1 72  ? -28.313 50.387  21.646  1.00 59.90  ? 72  ALA B CA  1 
ATOM   4682  C C   . ALA B 1 72  ? -29.718 49.800  21.551  1.00 54.90  ? 72  ALA B C   1 
ATOM   4683  O O   . ALA B 1 72  ? -30.522 49.909  22.478  1.00 54.07  ? 72  ALA B O   1 
ATOM   4684  C CB  . ALA B 1 72  ? -27.376 49.401  22.348  1.00 56.95  ? 72  ALA B CB  1 
ATOM   4685  N N   . LYS B 1 73  ? -30.008 49.168  20.426  1.00 59.79  ? 73  LYS B N   1 
ATOM   4686  C CA  . LYS B 1 73  ? -31.283 48.504  20.197  1.00 54.29  ? 73  LYS B CA  1 
ATOM   4687  C C   . LYS B 1 73  ? -31.022 47.010  20.010  1.00 55.99  ? 73  LYS B C   1 
ATOM   4688  O O   . LYS B 1 73  ? -31.077 46.499  18.889  1.00 55.38  ? 73  LYS B O   1 
ATOM   4689  C CB  . LYS B 1 73  ? -31.981 49.099  18.974  1.00 58.73  ? 73  LYS B CB  1 
ATOM   4690  C CG  . LYS B 1 73  ? -32.033 50.613  18.923  1.00 64.35  ? 73  LYS B CG  1 
ATOM   4691  C CD  . LYS B 1 73  ? -32.461 51.093  17.535  1.00 64.87  ? 73  LYS B CD  1 
ATOM   4692  C CE  . LYS B 1 73  ? -32.281 52.597  17.388  1.00 66.63  ? 73  LYS B CE  1 
ATOM   4693  N NZ  . LYS B 1 73  ? -31.763 52.979  16.047  1.00 76.21  ? 73  LYS B NZ  1 
ATOM   4694  N N   . ASP B 1 74  ? -30.724 46.313  21.101  1.00 57.91  ? 74  ASP B N   1 
ATOM   4695  C CA  . ASP B 1 74  ? -30.521 44.870  21.024  1.00 62.84  ? 74  ASP B CA  1 
ATOM   4696  C C   . ASP B 1 74  ? -31.877 44.183  20.920  1.00 58.33  ? 74  ASP B C   1 
ATOM   4697  O O   . ASP B 1 74  ? -32.711 44.301  21.823  1.00 57.35  ? 74  ASP B O   1 
ATOM   4698  C CB  . ASP B 1 74  ? -29.749 44.382  22.248  1.00 66.51  ? 74  ASP B CB  1 
ATOM   4699  C CG  . ASP B 1 74  ? -29.242 42.951  22.104  1.00 68.17  ? 74  ASP B CG  1 
ATOM   4700  O OD1 . ASP B 1 74  ? -29.268 42.385  20.984  1.00 69.11  ? 74  ASP B OD1 1 
ATOM   4701  O OD2 . ASP B 1 74  ? -28.821 42.386  23.135  1.00 65.54  ? 74  ASP B OD2 1 
ATOM   4702  N N   . VAL B 1 75  ? -32.111 43.491  19.802  1.00 63.00  ? 75  VAL B N   1 
ATOM   4703  C CA  . VAL B 1 75  ? -33.429 42.915  19.560  1.00 63.67  ? 75  VAL B CA  1 
ATOM   4704  C C   . VAL B 1 75  ? -33.704 41.788  20.542  1.00 62.34  ? 75  VAL B C   1 
ATOM   4705  O O   . VAL B 1 75  ? -34.830 41.626  21.030  1.00 61.08  ? 75  VAL B O   1 
ATOM   4706  C CB  . VAL B 1 75  ? -33.537 42.442  18.101  1.00 62.30  ? 75  VAL B CB  1 
ATOM   4707  C CG1 . VAL B 1 75  ? -33.707 43.634  17.198  1.00 61.01  ? 75  VAL B CG1 1 
ATOM   4708  C CG2 . VAL B 1 75  ? -32.300 41.655  17.710  1.00 61.78  ? 75  VAL B CG2 1 
ATOM   4709  N N   . PHE B 1 76  ? -32.681 40.999  20.858  1.00 59.48  ? 76  PHE B N   1 
ATOM   4710  C CA  . PHE B 1 76  ? -32.870 39.928  21.824  1.00 62.67  ? 76  PHE B CA  1 
ATOM   4711  C C   . PHE B 1 76  ? -33.137 40.489  23.212  1.00 60.22  ? 76  PHE B C   1 
ATOM   4712  O O   . PHE B 1 76  ? -33.925 39.922  23.975  1.00 62.45  ? 76  PHE B O   1 
ATOM   4713  C CB  . PHE B 1 76  ? -31.653 39.006  21.837  1.00 57.12  ? 76  PHE B CB  1 
ATOM   4714  C CG  . PHE B 1 76  ? -31.824 37.801  22.705  1.00 57.32  ? 76  PHE B CG  1 
ATOM   4715  C CD1 . PHE B 1 76  ? -32.542 36.706  22.255  1.00 61.03  ? 76  PHE B CD1 1 
ATOM   4716  C CD2 . PHE B 1 76  ? -31.270 37.760  23.976  1.00 60.02  ? 76  PHE B CD2 1 
ATOM   4717  C CE1 . PHE B 1 76  ? -32.703 35.587  23.058  1.00 67.87  ? 76  PHE B CE1 1 
ATOM   4718  C CE2 . PHE B 1 76  ? -31.425 36.646  24.782  1.00 59.20  ? 76  PHE B CE2 1 
ATOM   4719  C CZ  . PHE B 1 76  ? -32.144 35.557  24.323  1.00 63.53  ? 76  PHE B CZ  1 
ATOM   4720  N N   . LEU B 1 77  ? -32.499 41.609  23.555  1.00 59.56  ? 77  LEU B N   1 
ATOM   4721  C CA  . LEU B 1 77  ? -32.694 42.177  24.883  1.00 58.08  ? 77  LEU B CA  1 
ATOM   4722  C C   . LEU B 1 77  ? -34.123 42.659  25.074  1.00 55.04  ? 77  LEU B C   1 
ATOM   4723  O O   . LEU B 1 77  ? -34.708 42.475  26.147  1.00 61.18  ? 77  LEU B O   1 
ATOM   4724  C CB  . LEU B 1 77  ? -31.711 43.318  25.116  1.00 61.96  ? 77  LEU B CB  1 
ATOM   4725  C CG  . LEU B 1 77  ? -30.964 43.255  26.442  1.00 68.63  ? 77  LEU B CG  1 
ATOM   4726  C CD1 . LEU B 1 77  ? -30.145 41.967  26.519  1.00 64.45  ? 77  LEU B CD1 1 
ATOM   4727  C CD2 . LEU B 1 77  ? -30.084 44.490  26.578  1.00 58.71  ? 77  LEU B CD2 1 
ATOM   4728  N N   . GLU B 1 78  ? -34.708 43.267  24.040  1.00 52.26  ? 78  GLU B N   1 
ATOM   4729  C CA  . GLU B 1 78  ? -36.088 43.728  24.153  1.00 68.41  ? 78  GLU B CA  1 
ATOM   4730  C C   . GLU B 1 78  ? -37.042 42.571  24.424  1.00 60.88  ? 78  GLU B C   1 
ATOM   4731  O O   . GLU B 1 78  ? -38.050 42.748  25.118  1.00 59.72  ? 78  GLU B O   1 
ATOM   4732  C CB  . GLU B 1 78  ? -36.500 44.475  22.883  1.00 78.72  ? 78  GLU B CB  1 
ATOM   4733  C CG  . GLU B 1 78  ? -36.705 45.969  23.092  1.00 79.30  ? 78  GLU B CG  1 
ATOM   4734  C CD  . GLU B 1 78  ? -37.968 46.271  23.879  1.00 85.41  ? 78  GLU B CD  1 
ATOM   4735  O OE1 . GLU B 1 78  ? -39.077 46.007  23.362  1.00 89.94  ? 78  GLU B OE1 1 
ATOM   4736  O OE2 . GLU B 1 78  ? -37.853 46.776  25.017  1.00 79.96  ? 78  GLU B OE2 1 
ATOM   4737  N N   . ALA B 1 79  ? -36.733 41.383  23.891  1.00 58.58  ? 79  ALA B N   1 
ATOM   4738  C CA  . ALA B 1 79  ? -37.510 40.188  24.202  1.00 55.09  ? 79  ALA B CA  1 
ATOM   4739  C C   . ALA B 1 79  ? -37.439 39.862  25.683  1.00 58.66  ? 79  ALA B C   1 
ATOM   4740  O O   . ALA B 1 79  ? -38.456 39.538  26.309  1.00 63.29  ? 79  ALA B O   1 
ATOM   4741  C CB  . ALA B 1 79  ? -37.002 39.006  23.380  1.00 51.02  ? 79  ALA B CB  1 
ATOM   4742  N N   . ILE B 1 80  ? -36.242 39.939  26.257  1.00 52.19  ? 80  ILE B N   1 
ATOM   4743  C CA  . ILE B 1 80  ? -36.077 39.701  27.684  1.00 47.65  ? 80  ILE B CA  1 
ATOM   4744  C C   . ILE B 1 80  ? -36.825 40.755  28.488  1.00 56.83  ? 80  ILE B C   1 
ATOM   4745  O O   . ILE B 1 80  ? -37.575 40.431  29.415  1.00 67.23  ? 80  ILE B O   1 
ATOM   4746  C CB  . ILE B 1 80  ? -34.584 39.688  28.047  1.00 65.64  ? 80  ILE B CB  1 
ATOM   4747  C CG1 . ILE B 1 80  ? -33.802 38.762  27.104  1.00 56.56  ? 80  ILE B CG1 1 
ATOM   4748  C CG2 . ILE B 1 80  ? -34.419 39.318  29.518  1.00 68.60  ? 80  ILE B CG2 1 
ATOM   4749  C CD1 . ILE B 1 80  ? -33.613 37.357  27.600  1.00 50.67  ? 80  ILE B CD1 1 
ATOM   4750  N N   . ARG B 1 81  ? -36.635 42.033  28.139  1.00 54.32  ? 81  ARG B N   1 
ATOM   4751  C CA  . ARG B 1 81  ? -37.212 43.123  28.922  1.00 53.32  ? 81  ARG B CA  1 
ATOM   4752  C C   . ARG B 1 81  ? -38.738 43.097  28.885  1.00 61.47  ? 81  ARG B C   1 
ATOM   4753  O O   . ARG B 1 81  ? -39.392 43.345  29.907  1.00 62.64  ? 81  ARG B O   1 
ATOM   4754  C CB  . ARG B 1 81  ? -36.687 44.469  28.413  1.00 49.65  ? 81  ARG B CB  1 
ATOM   4755  C CG  . ARG B 1 81  ? -36.639 45.582  29.455  1.00 51.40  ? 81  ARG B CG  1 
ATOM   4756  C CD  . ARG B 1 81  ? -37.034 46.898  28.819  1.00 50.09  ? 81  ARG B CD  1 
ATOM   4757  N NE  . ARG B 1 81  ? -38.225 46.742  27.985  1.00 71.62  ? 81  ARG B NE  1 
ATOM   4758  C CZ  . ARG B 1 81  ? -39.481 46.904  28.393  1.00 75.66  ? 81  ARG B CZ  1 
ATOM   4759  N NH1 . ARG B 1 81  ? -39.767 47.266  29.635  1.00 65.50  ? 81  ARG B NH1 1 
ATOM   4760  N NH2 . ARG B 1 81  ? -40.475 46.706  27.529  1.00 64.62  ? 81  ARG B NH2 1 
ATOM   4761  N N   . LYS B 1 82  ? -39.320 42.801  27.724  1.00 59.09  ? 82  LYS B N   1 
ATOM   4762  C CA  . LYS B 1 82  ? -40.767 42.872  27.560  1.00 56.62  ? 82  LYS B CA  1 
ATOM   4763  C C   . LYS B 1 82  ? -41.475 41.940  28.537  1.00 56.36  ? 82  LYS B C   1 
ATOM   4764  O O   . LYS B 1 82  ? -40.964 40.876  28.895  1.00 66.58  ? 82  LYS B O   1 
ATOM   4765  C CB  . LYS B 1 82  ? -41.159 42.491  26.132  1.00 59.29  ? 82  LYS B CB  1 
ATOM   4766  C CG  . LYS B 1 82  ? -41.379 43.650  25.177  1.00 63.86  ? 82  LYS B CG  1 
ATOM   4767  C CD  . LYS B 1 82  ? -41.028 43.242  23.745  1.00 65.95  ? 82  LYS B CD  1 
ATOM   4768  C CE  . LYS B 1 82  ? -42.232 42.665  23.009  1.00 69.59  ? 82  LYS B CE  1 
ATOM   4769  N NZ  . LYS B 1 82  ? -42.390 43.223  21.634  1.00 65.64  ? 82  LYS B NZ  1 
ATOM   4770  N N   . ASP B 1 83  ? -42.655 42.357  28.983  1.00 53.39  ? 83  ASP B N   1 
ATOM   4771  C CA  . ASP B 1 83  ? -43.536 41.429  29.669  1.00 58.42  ? 83  ASP B CA  1 
ATOM   4772  C C   . ASP B 1 83  ? -43.833 40.268  28.723  1.00 62.42  ? 83  ASP B C   1 
ATOM   4773  O O   . ASP B 1 83  ? -44.018 40.490  27.520  1.00 64.97  ? 83  ASP B O   1 
ATOM   4774  C CB  . ASP B 1 83  ? -44.830 42.134  30.093  1.00 66.00  ? 83  ASP B CB  1 
ATOM   4775  C CG  . ASP B 1 83  ? -45.759 41.243  30.906  1.00 69.90  ? 83  ASP B CG  1 
ATOM   4776  O OD1 . ASP B 1 83  ? -46.280 40.247  30.364  1.00 69.72  ? 83  ASP B OD1 1 
ATOM   4777  O OD2 . ASP B 1 83  ? -45.973 41.548  32.099  1.00 71.39  ? 83  ASP B OD2 1 
ATOM   4778  N N   . PRO B 1 84  ? -43.845 39.024  29.210  1.00 59.13  ? 84  PRO B N   1 
ATOM   4779  C CA  . PRO B 1 84  ? -44.034 37.886  28.297  1.00 59.23  ? 84  PRO B CA  1 
ATOM   4780  C C   . PRO B 1 84  ? -45.352 37.924  27.548  1.00 63.76  ? 84  PRO B C   1 
ATOM   4781  O O   . PRO B 1 84  ? -45.472 37.268  26.506  1.00 67.31  ? 84  PRO B O   1 
ATOM   4782  C CB  . PRO B 1 84  ? -43.954 36.674  29.233  1.00 59.47  ? 84  PRO B CB  1 
ATOM   4783  C CG  . PRO B 1 84  ? -43.150 37.162  30.392  1.00 58.17  ? 84  PRO B CG  1 
ATOM   4784  C CD  . PRO B 1 84  ? -43.621 38.572  30.591  1.00 59.09  ? 84  PRO B CD  1 
ATOM   4785  N N   . ASP B 1 85  ? -46.337 38.684  28.028  1.00 63.03  ? 85  ASP B N   1 
ATOM   4786  C CA  . ASP B 1 85  ? -47.613 38.757  27.332  1.00 61.75  ? 85  ASP B CA  1 
ATOM   4787  C C   . ASP B 1 85  ? -47.523 39.551  26.037  1.00 60.21  ? 85  ASP B C   1 
ATOM   4788  O O   . ASP B 1 85  ? -48.338 39.332  25.137  1.00 58.03  ? 85  ASP B O   1 
ATOM   4789  C CB  . ASP B 1 85  ? -48.666 39.365  28.250  1.00 63.71  ? 85  ASP B CB  1 
ATOM   4790  C CG  . ASP B 1 85  ? -49.076 38.419  29.347  1.00 70.20  ? 85  ASP B CG  1 
ATOM   4791  O OD1 . ASP B 1 85  ? -48.910 37.194  29.163  1.00 70.76  ? 85  ASP B OD1 1 
ATOM   4792  O OD2 . ASP B 1 85  ? -49.562 38.898  30.391  1.00 78.00  ? 85  ASP B OD2 1 
ATOM   4793  N N   . ASP B 1 86  ? -46.555 40.456  25.917  1.00 69.51  ? 86  ASP B N   1 
ATOM   4794  C CA  . ASP B 1 86  ? -46.373 41.237  24.700  1.00 70.48  ? 86  ASP B CA  1 
ATOM   4795  C C   . ASP B 1 86  ? -45.408 40.589  23.717  1.00 64.87  ? 86  ASP B C   1 
ATOM   4796  O O   . ASP B 1 86  ? -45.188 41.141  22.635  1.00 66.26  ? 86  ASP B O   1 
ATOM   4797  C CB  . ASP B 1 86  ? -45.880 42.649  25.037  1.00 69.40  ? 86  ASP B CB  1 
ATOM   4798  C CG  . ASP B 1 86  ? -46.869 43.423  25.878  1.00 74.51  ? 86  ASP B CG  1 
ATOM   4799  O OD1 . ASP B 1 86  ? -46.893 43.193  27.104  1.00 79.79  ? 86  ASP B OD1 1 
ATOM   4800  O OD2 . ASP B 1 86  ? -47.622 44.251  25.319  1.00 73.57  ? 86  ASP B OD2 1 
ATOM   4801  N N   . LEU B 1 87  ? -44.841 39.434  24.058  1.00 66.69  ? 87  LEU B N   1 
ATOM   4802  C CA  . LEU B 1 87  ? -43.877 38.767  23.192  1.00 69.71  ? 87  LEU B CA  1 
ATOM   4803  C C   . LEU B 1 87  ? -44.584 38.138  22.003  1.00 68.98  ? 87  LEU B C   1 
ATOM   4804  O O   . LEU B 1 87  ? -45.606 37.468  22.166  1.00 63.13  ? 87  LEU B O   1 
ATOM   4805  C CB  . LEU B 1 87  ? -43.131 37.685  23.964  1.00 59.67  ? 87  LEU B CB  1 
ATOM   4806  C CG  . LEU B 1 87  ? -42.145 38.176  25.008  1.00 61.69  ? 87  LEU B CG  1 
ATOM   4807  C CD1 . LEU B 1 87  ? -41.431 36.993  25.630  1.00 61.07  ? 87  LEU B CD1 1 
ATOM   4808  C CD2 . LEU B 1 87  ? -41.167 39.130  24.359  1.00 65.81  ? 87  LEU B CD2 1 
ATOM   4809  N N   . GLU B 1 88  ? -44.032 38.336  20.811  1.00 71.67  ? 88  GLU B N   1 
ATOM   4810  C CA  . GLU B 1 88  ? -44.569 37.677  19.633  1.00 73.18  ? 88  GLU B CA  1 
ATOM   4811  C C   . GLU B 1 88  ? -43.918 36.309  19.464  1.00 67.76  ? 88  GLU B C   1 
ATOM   4812  O O   . GLU B 1 88  ? -42.934 35.972  20.128  1.00 62.92  ? 88  GLU B O   1 
ATOM   4813  C CB  . GLU B 1 88  ? -44.369 38.535  18.379  1.00 66.95  ? 88  GLU B CB  1 
ATOM   4814  C CG  . GLU B 1 88  ? -45.003 39.922  18.447  1.00 63.88  ? 88  GLU B CG  1 
ATOM   4815  C CD  . GLU B 1 88  ? -46.448 39.902  18.924  1.00 74.84  ? 88  GLU B CD  1 
ATOM   4816  O OE1 . GLU B 1 88  ? -47.188 38.953  18.579  1.00 74.45  ? 88  GLU B OE1 1 
ATOM   4817  O OE2 . GLU B 1 88  ? -46.845 40.847  19.642  1.00 76.50  ? 88  GLU B OE2 1 
ATOM   4818  N N   . LYS B 1 89  ? -44.488 35.514  18.555  1.00 69.22  ? 89  LYS B N   1 
ATOM   4819  C CA  . LYS B 1 89  ? -44.057 34.128  18.408  1.00 68.10  ? 89  LYS B CA  1 
ATOM   4820  C C   . LYS B 1 89  ? -42.590 34.038  18.016  1.00 66.27  ? 89  LYS B C   1 
ATOM   4821  O O   . LYS B 1 89  ? -41.848 33.212  18.557  1.00 67.77  ? 89  LYS B O   1 
ATOM   4822  C CB  . LYS B 1 89  ? -44.927 33.415  17.377  1.00 68.61  ? 89  LYS B CB  1 
ATOM   4823  C CG  . LYS B 1 89  ? -46.425 33.432  17.691  1.00 81.97  ? 89  LYS B CG  1 
ATOM   4824  C CD  . LYS B 1 89  ? -46.722 33.181  19.165  1.00 72.54  ? 89  LYS B CD  1 
ATOM   4825  C CE  . LYS B 1 89  ? -47.677 32.009  19.342  1.00 79.38  ? 89  LYS B CE  1 
ATOM   4826  N NZ  . LYS B 1 89  ? -49.090 32.367  19.030  1.00 91.77  ? 89  LYS B NZ  1 
ATOM   4827  N N   . GLU B 1 90  ? -42.149 34.886  17.084  1.00 66.54  ? 90  GLU B N   1 
ATOM   4828  C CA  . GLU B 1 90  ? -40.757 34.838  16.650  1.00 65.32  ? 90  GLU B CA  1 
ATOM   4829  C C   . GLU B 1 90  ? -39.813 35.188  17.793  1.00 67.23  ? 90  GLU B C   1 
ATOM   4830  O O   . GLU B 1 90  ? -38.741 34.588  17.926  1.00 64.95  ? 90  GLU B O   1 
ATOM   4831  C CB  . GLU B 1 90  ? -40.553 35.773  15.459  1.00 67.95  ? 90  GLU B CB  1 
ATOM   4832  C CG  . GLU B 1 90  ? -40.905 37.217  15.753  1.00 81.61  ? 90  GLU B CG  1 
ATOM   4833  C CD  . GLU B 1 90  ? -42.171 37.665  15.052  1.00 99.21  ? 90  GLU B CD  1 
ATOM   4834  O OE1 . GLU B 1 90  ? -42.284 38.866  14.728  1.00 110.84 ? 90  GLU B OE1 1 
ATOM   4835  O OE2 . GLU B 1 90  ? -43.055 36.812  14.826  1.00 105.50 ? 90  GLU B OE2 1 
ATOM   4836  N N   . GLU B 1 91  ? -40.207 36.136  18.650  1.00 63.62  ? 91  GLU B N   1 
ATOM   4837  C CA  . GLU B 1 91  ? -39.380 36.471  19.804  1.00 59.81  ? 91  GLU B CA  1 
ATOM   4838  C C   . GLU B 1 91  ? -39.307 35.303  20.775  1.00 64.15  ? 91  GLU B C   1 
ATOM   4839  O O   . GLU B 1 91  ? -38.236 34.991  21.312  1.00 64.87  ? 91  GLU B O   1 
ATOM   4840  C CB  . GLU B 1 91  ? -39.932 37.702  20.511  1.00 59.20  ? 91  GLU B CB  1 
ATOM   4841  C CG  . GLU B 1 91  ? -39.927 38.960  19.689  1.00 55.00  ? 91  GLU B CG  1 
ATOM   4842  C CD  . GLU B 1 91  ? -40.588 40.099  20.426  1.00 75.04  ? 91  GLU B CD  1 
ATOM   4843  O OE1 . GLU B 1 91  ? -41.811 40.018  20.683  1.00 79.62  ? 91  GLU B OE1 1 
ATOM   4844  O OE2 . GLU B 1 91  ? -39.873 41.059  20.785  1.00 76.59  ? 91  GLU B OE2 1 
ATOM   4845  N N   . VAL B 1 92  ? -40.444 34.645  21.007  1.00 61.41  ? 92  VAL B N   1 
ATOM   4846  C CA  . VAL B 1 92  ? -40.480 33.495  21.902  1.00 62.33  ? 92  VAL B CA  1 
ATOM   4847  C C   . VAL B 1 92  ? -39.630 32.358  21.345  1.00 58.92  ? 92  VAL B C   1 
ATOM   4848  O O   . VAL B 1 92  ? -38.890 31.700  22.087  1.00 59.69  ? 92  VAL B O   1 
ATOM   4849  C CB  . VAL B 1 92  ? -41.941 33.068  22.140  1.00 57.00  ? 92  VAL B CB  1 
ATOM   4850  C CG1 . VAL B 1 92  ? -42.001 31.788  22.931  1.00 55.66  ? 92  VAL B CG1 1 
ATOM   4851  C CG2 . VAL B 1 92  ? -42.687 34.161  22.866  1.00 52.53  ? 92  VAL B CG2 1 
ATOM   4852  N N   . GLU B 1 93  ? -39.708 32.115  20.031  1.00 57.60  ? 93  GLU B N   1 
ATOM   4853  C CA  . GLU B 1 93  ? -38.886 31.069  19.426  1.00 63.19  ? 93  GLU B CA  1 
ATOM   4854  C C   . GLU B 1 93  ? -37.406 31.355  19.621  1.00 58.40  ? 93  GLU B C   1 
ATOM   4855  O O   . GLU B 1 93  ? -36.617 30.439  19.876  1.00 57.20  ? 93  GLU B O   1 
ATOM   4856  C CB  . GLU B 1 93  ? -39.210 30.929  17.937  1.00 56.79  ? 93  GLU B CB  1 
ATOM   4857  C CG  . GLU B 1 93  ? -40.514 30.177  17.682  1.00 83.65  ? 93  GLU B CG  1 
ATOM   4858  C CD  . GLU B 1 93  ? -40.668 29.685  16.250  1.00 97.87  ? 93  GLU B CD  1 
ATOM   4859  O OE1 . GLU B 1 93  ? -40.306 30.433  15.316  1.00 97.21  ? 93  GLU B OE1 1 
ATOM   4860  O OE2 . GLU B 1 93  ? -41.169 28.554  16.059  1.00 97.40  ? 93  GLU B OE2 1 
ATOM   4861  N N   . LYS B 1 94  ? -37.017 32.627  19.524  1.00 59.09  ? 94  LYS B N   1 
ATOM   4862  C CA  . LYS B 1 94  ? -35.610 32.987  19.583  1.00 53.95  ? 94  LYS B CA  1 
ATOM   4863  C C   . LYS B 1 94  ? -35.066 32.915  21.001  1.00 63.33  ? 94  LYS B C   1 
ATOM   4864  O O   . LYS B 1 94  ? -33.867 32.672  21.192  1.00 64.11  ? 94  LYS B O   1 
ATOM   4865  C CB  . LYS B 1 94  ? -35.408 34.382  18.988  1.00 60.14  ? 94  LYS B CB  1 
ATOM   4866  C CG  . LYS B 1 94  ? -35.545 34.428  17.469  1.00 58.78  ? 94  LYS B CG  1 
ATOM   4867  C CD  . LYS B 1 94  ? -35.976 35.800  16.947  1.00 67.97  ? 94  LYS B CD  1 
ATOM   4868  C CE  . LYS B 1 94  ? -35.760 36.910  17.965  1.00 68.17  ? 94  LYS B CE  1 
ATOM   4869  N NZ  . LYS B 1 94  ? -35.531 38.232  17.314  1.00 75.28  ? 94  LYS B NZ  1 
ATOM   4870  N N   . LEU B 1 95  ? -35.923 33.115  22.001  1.00 58.31  ? 95  LEU B N   1 
ATOM   4871  C CA  . LEU B 1 95  ? -35.502 32.894  23.378  1.00 55.11  ? 95  LEU B CA  1 
ATOM   4872  C C   . LEU B 1 95  ? -35.183 31.426  23.611  1.00 52.98  ? 95  LEU B C   1 
ATOM   4873  O O   . LEU B 1 95  ? -34.175 31.090  24.240  1.00 64.34  ? 95  LEU B O   1 
ATOM   4874  C CB  . LEU B 1 95  ? -36.601 33.356  24.330  1.00 62.37  ? 95  LEU B CB  1 
ATOM   4875  C CG  . LEU B 1 95  ? -36.194 33.923  25.685  1.00 64.47  ? 95  LEU B CG  1 
ATOM   4876  C CD1 . LEU B 1 95  ? -37.439 34.394  26.396  1.00 54.21  ? 95  LEU B CD1 1 
ATOM   4877  C CD2 . LEU B 1 95  ? -35.431 32.923  26.532  1.00 71.47  ? 95  LEU B CD2 1 
ATOM   4878  N N   . ILE B 1 96  ? -36.034 30.536  23.107  1.00 56.66  ? 96  ILE B N   1 
ATOM   4879  C CA  . ILE B 1 96  ? -35.788 29.109  23.254  1.00 61.32  ? 96  ILE B CA  1 
ATOM   4880  C C   . ILE B 1 96  ? -34.539 28.701  22.491  1.00 55.76  ? 96  ILE B C   1 
ATOM   4881  O O   . ILE B 1 96  ? -33.721 27.921  22.989  1.00 54.05  ? 96  ILE B O   1 
ATOM   4882  C CB  . ILE B 1 96  ? -37.023 28.318  22.796  1.00 55.90  ? 96  ILE B CB  1 
ATOM   4883  C CG1 . ILE B 1 96  ? -38.200 28.630  23.709  1.00 51.66  ? 96  ILE B CG1 1 
ATOM   4884  C CG2 . ILE B 1 96  ? -36.735 26.839  22.788  1.00 56.98  ? 96  ILE B CG2 1 
ATOM   4885  C CD1 . ILE B 1 96  ? -39.501 28.244  23.113  1.00 54.72  ? 96  ILE B CD1 1 
ATOM   4886  N N   . GLU B 1 97  ? -34.370 29.226  21.275  1.00 59.79  ? 97  GLU B N   1 
ATOM   4887  C CA  . GLU B 1 97  ? -33.194 28.904  20.477  1.00 60.96  ? 97  GLU B CA  1 
ATOM   4888  C C   . GLU B 1 97  ? -31.922 29.366  21.175  1.00 61.88  ? 97  GLU B C   1 
ATOM   4889  O O   . GLU B 1 97  ? -30.899 28.669  21.146  1.00 64.54  ? 97  GLU B O   1 
ATOM   4890  C CB  . GLU B 1 97  ? -33.315 29.546  19.095  1.00 67.15  ? 97  GLU B CB  1 
ATOM   4891  C CG  . GLU B 1 97  ? -32.808 28.688  17.940  1.00 80.78  ? 97  GLU B CG  1 
ATOM   4892  C CD  . GLU B 1 97  ? -32.317 29.526  16.765  1.00 92.07  ? 97  GLU B CD  1 
ATOM   4893  O OE1 . GLU B 1 97  ? -32.549 30.755  16.765  1.00 91.22  ? 97  GLU B OE1 1 
ATOM   4894  O OE2 . GLU B 1 97  ? -31.687 28.958  15.847  1.00 93.47  ? 97  GLU B OE2 1 
ATOM   4895  N N   . PHE B 1 98  ? -31.966 30.544  21.804  1.00 56.33  ? 98  PHE B N   1 
ATOM   4896  C CA  . PHE B 1 98  ? -30.827 31.007  22.590  1.00 63.19  ? 98  PHE B CA  1 
ATOM   4897  C C   . PHE B 1 98  ? -30.561 30.069  23.760  1.00 58.55  ? 98  PHE B C   1 
ATOM   4898  O O   . PHE B 1 98  ? -29.422 29.639  23.980  1.00 60.04  ? 98  PHE B O   1 
ATOM   4899  C CB  . PHE B 1 98  ? -31.072 32.434  23.082  1.00 58.67  ? 98  PHE B CB  1 
ATOM   4900  C CG  . PHE B 1 98  ? -29.839 33.112  23.620  1.00 59.63  ? 98  PHE B CG  1 
ATOM   4901  C CD1 . PHE B 1 98  ? -28.895 33.650  22.763  1.00 54.31  ? 98  PHE B CD1 1 
ATOM   4902  C CD2 . PHE B 1 98  ? -29.629 33.211  24.985  1.00 61.16  ? 98  PHE B CD2 1 
ATOM   4903  C CE1 . PHE B 1 98  ? -27.766 34.278  23.259  1.00 60.24  ? 98  PHE B CE1 1 
ATOM   4904  C CE2 . PHE B 1 98  ? -28.503 33.836  25.488  1.00 57.04  ? 98  PHE B CE2 1 
ATOM   4905  C CZ  . PHE B 1 98  ? -27.569 34.370  24.623  1.00 65.86  ? 98  PHE B CZ  1 
ATOM   4906  N N   . THR B 1 99  ? -31.610 29.731  24.513  1.00 55.08  ? 99  THR B N   1 
ATOM   4907  C CA  . THR B 1 99  ? -31.479 28.767  25.602  1.00 56.57  ? 99  THR B CA  1 
ATOM   4908  C C   . THR B 1 99  ? -30.848 27.471  25.111  1.00 55.72  ? 99  THR B C   1 
ATOM   4909  O O   . THR B 1 99  ? -29.911 26.953  25.728  1.00 54.80  ? 99  THR B O   1 
ATOM   4910  C CB  . THR B 1 99  ? -32.850 28.492  26.228  1.00 60.44  ? 99  THR B CB  1 
ATOM   4911  O OG1 . THR B 1 99  ? -33.629 29.696  26.232  1.00 62.69  ? 99  THR B OG1 1 
ATOM   4912  C CG2 . THR B 1 99  ? -32.700 27.998  27.660  1.00 51.33  ? 99  THR B CG2 1 
ATOM   4913  N N   . LYS B 1 100 ? -31.337 26.946  23.982  1.00 67.29  ? 100 LYS B N   1 
ATOM   4914  C CA  . LYS B 1 100 ? -30.853 25.661  23.487  1.00 57.53  ? 100 LYS B CA  1 
ATOM   4915  C C   . LYS B 1 100 ? -29.358 25.698  23.223  1.00 56.44  ? 100 LYS B C   1 
ATOM   4916  O O   . LYS B 1 100 ? -28.657 24.715  23.487  1.00 66.96  ? 100 LYS B O   1 
ATOM   4917  C CB  . LYS B 1 100 ? -31.612 25.262  22.222  1.00 56.51  ? 100 LYS B CB  1 
ATOM   4918  C CG  . LYS B 1 100 ? -32.863 24.409  22.476  1.00 68.69  ? 100 LYS B CG  1 
ATOM   4919  C CD  . LYS B 1 100 ? -32.553 22.911  22.396  1.00 80.22  ? 100 LYS B CD  1 
ATOM   4920  C CE  . LYS B 1 100 ? -33.055 22.140  23.621  1.00 77.92  ? 100 LYS B CE  1 
ATOM   4921  N NZ  . LYS B 1 100 ? -32.898 20.656  23.467  1.00 63.58  ? 100 LYS B NZ  1 
ATOM   4922  N N   . LEU B 1 101 ? -28.843 26.824  22.711  1.00 60.00  ? 101 LEU B N   1 
ATOM   4923  C CA  . LEU B 1 101 ? -27.403 26.903  22.474  1.00 60.55  ? 101 LEU B CA  1 
ATOM   4924  C C   . LEU B 1 101 ? -26.624 26.763  23.771  1.00 62.94  ? 101 LEU B C   1 
ATOM   4925  O O   . LEU B 1 101 ? -25.558 26.142  23.787  1.00 64.74  ? 101 LEU B O   1 
ATOM   4926  C CB  . LEU B 1 101 ? -26.999 28.222  21.810  1.00 58.72  ? 101 LEU B CB  1 
ATOM   4927  C CG  . LEU B 1 101 ? -25.828 28.160  20.812  1.00 71.59  ? 101 LEU B CG  1 
ATOM   4928  C CD1 . LEU B 1 101 ? -25.543 29.532  20.209  1.00 70.36  ? 101 LEU B CD1 1 
ATOM   4929  C CD2 . LEU B 1 101 ? -24.557 27.521  21.387  1.00 70.32  ? 101 LEU B CD2 1 
ATOM   4930  N N   . ASN B 1 102 ? -27.127 27.326  24.866  1.00 55.52  ? 102 ASN B N   1 
ATOM   4931  C CA  . ASN B 1 102 ? -26.361 27.397  26.100  1.00 51.46  ? 102 ASN B CA  1 
ATOM   4932  C C   . ASN B 1 102 ? -26.827 26.400  27.156  1.00 63.73  ? 102 ASN B C   1 
ATOM   4933  O O   . ASN B 1 102 ? -26.377 26.477  28.302  1.00 65.52  ? 102 ASN B O   1 
ATOM   4934  C CB  . ASN B 1 102 ? -26.402 28.827  26.632  1.00 52.06  ? 102 ASN B CB  1 
ATOM   4935  C CG  . ASN B 1 102 ? -26.264 29.857  25.517  1.00 59.04  ? 102 ASN B CG  1 
ATOM   4936  O OD1 . ASN B 1 102 ? -25.205 29.987  24.903  1.00 62.34  ? 102 ASN B OD1 1 
ATOM   4937  N ND2 . ASN B 1 102 ? -27.345 30.572  25.232  1.00 65.74  ? 102 ASN B ND2 1 
ATOM   4938  N N   . TYR B 1 103 ? -27.681 25.439  26.784  1.00 65.22  ? 103 TYR B N   1 
ATOM   4939  C CA  . TYR B 1 103 ? -28.206 24.470  27.749  1.00 64.47  ? 103 TYR B CA  1 
ATOM   4940  C C   . TYR B 1 103 ? -27.081 23.698  28.430  1.00 67.38  ? 103 TYR B C   1 
ATOM   4941  O O   . TYR B 1 103 ? -27.117 23.467  29.646  1.00 62.58  ? 103 TYR B O   1 
ATOM   4942  C CB  . TYR B 1 103 ? -29.170 23.519  27.031  1.00 64.80  ? 103 TYR B CB  1 
ATOM   4943  C CG  . TYR B 1 103 ? -30.158 22.776  27.906  1.00 69.84  ? 103 TYR B CG  1 
ATOM   4944  C CD1 . TYR B 1 103 ? -31.018 23.453  28.765  1.00 67.35  ? 103 TYR B CD1 1 
ATOM   4945  C CD2 . TYR B 1 103 ? -30.255 21.391  27.841  1.00 70.03  ? 103 TYR B CD2 1 
ATOM   4946  C CE1 . TYR B 1 103 ? -31.932 22.760  29.555  1.00 78.34  ? 103 TYR B CE1 1 
ATOM   4947  C CE2 . TYR B 1 103 ? -31.159 20.696  28.620  1.00 74.89  ? 103 TYR B CE2 1 
ATOM   4948  C CZ  . TYR B 1 103 ? -31.995 21.379  29.475  1.00 81.04  ? 103 TYR B CZ  1 
ATOM   4949  O OH  . TYR B 1 103 ? -32.890 20.662  30.239  1.00 85.89  ? 103 TYR B OH  1 
ATOM   4950  N N   . GLU B 1 104 ? -26.052 23.334  27.659  1.00 73.61  ? 104 GLU B N   1 
ATOM   4951  C CA  . GLU B 1 104 ? -24.936 22.509  28.110  1.00 66.71  ? 104 GLU B CA  1 
ATOM   4952  C C   . GLU B 1 104 ? -23.926 23.282  28.948  1.00 60.82  ? 104 GLU B C   1 
ATOM   4953  O O   . GLU B 1 104 ? -23.133 22.666  29.669  1.00 68.71  ? 104 GLU B O   1 
ATOM   4954  C CB  . GLU B 1 104 ? -24.218 21.903  26.898  1.00 65.67  ? 104 GLU B CB  1 
ATOM   4955  C CG  . GLU B 1 104 ? -24.088 22.847  25.674  1.00 77.78  ? 104 GLU B CG  1 
ATOM   4956  C CD  . GLU B 1 104 ? -25.350 22.919  24.809  1.00 89.49  ? 104 GLU B CD  1 
ATOM   4957  O OE1 . GLU B 1 104 ? -25.257 22.659  23.585  1.00 90.12  ? 104 GLU B OE1 1 
ATOM   4958  O OE2 . GLU B 1 104 ? -26.428 23.259  25.347  1.00 95.46  ? 104 GLU B OE2 1 
ATOM   4959  N N   . LYS B 1 105 ? -23.929 24.604  28.870  1.00 57.86  ? 105 LYS B N   1 
ATOM   4960  C CA  . LYS B 1 105 ? -22.919 25.383  29.565  1.00 55.73  ? 105 LYS B CA  1 
ATOM   4961  C C   . LYS B 1 105 ? -23.151 25.330  31.071  1.00 56.67  ? 105 LYS B C   1 
ATOM   4962  O O   . LYS B 1 105 ? -24.295 25.424  31.525  1.00 60.38  ? 105 LYS B O   1 
ATOM   4963  C CB  . LYS B 1 105 ? -22.944 26.827  29.085  1.00 55.98  ? 105 LYS B CB  1 
ATOM   4964  C CG  . LYS B 1 105 ? -23.133 26.959  27.586  1.00 61.34  ? 105 LYS B CG  1 
ATOM   4965  C CD  . LYS B 1 105 ? -22.246 28.033  26.990  1.00 60.81  ? 105 LYS B CD  1 
ATOM   4966  C CE  . LYS B 1 105 ? -22.102 27.869  25.480  1.00 58.77  ? 105 LYS B CE  1 
ATOM   4967  N NZ  . LYS B 1 105 ? -22.042 29.181  24.763  1.00 57.10  ? 105 LYS B NZ  1 
ATOM   4968  N N   . PRO B 1 106 ? -22.084 25.183  31.863  1.00 57.64  ? 106 PRO B N   1 
ATOM   4969  C CA  . PRO B 1 106 ? -22.233 25.162  33.332  1.00 58.87  ? 106 PRO B CA  1 
ATOM   4970  C C   . PRO B 1 106 ? -22.969 26.367  33.906  1.00 57.26  ? 106 PRO B C   1 
ATOM   4971  O O   . PRO B 1 106 ? -23.763 26.205  34.840  1.00 58.35  ? 106 PRO B O   1 
ATOM   4972  C CB  . PRO B 1 106 ? -20.777 25.115  33.817  1.00 65.39  ? 106 PRO B CB  1 
ATOM   4973  C CG  . PRO B 1 106 ? -20.015 24.493  32.670  1.00 60.09  ? 106 PRO B CG  1 
ATOM   4974  C CD  . PRO B 1 106 ? -20.695 24.969  31.426  1.00 57.97  ? 106 PRO B CD  1 
ATOM   4975  N N   . ILE B 1 107 ? -22.737 27.570  33.371  1.00 54.93  ? 107 ILE B N   1 
ATOM   4976  C CA  . ILE B 1 107 ? -23.411 28.767  33.855  1.00 53.57  ? 107 ILE B CA  1 
ATOM   4977  C C   . ILE B 1 107 ? -24.922 28.716  33.660  1.00 61.55  ? 107 ILE B C   1 
ATOM   4978  O O   . ILE B 1 107 ? -25.644 29.536  34.240  1.00 55.74  ? 107 ILE B O   1 
ATOM   4979  C CB  . ILE B 1 107 ? -22.821 30.020  33.169  1.00 51.64  ? 107 ILE B CB  1 
ATOM   4980  C CG1 . ILE B 1 107 ? -22.734 29.817  31.656  1.00 56.39  ? 107 ILE B CG1 1 
ATOM   4981  C CG2 . ILE B 1 107 ? -21.448 30.319  33.702  1.00 58.60  ? 107 ILE B CG2 1 
ATOM   4982  C CD1 . ILE B 1 107 ? -22.915 31.090  30.859  1.00 48.91  ? 107 ILE B CD1 1 
ATOM   4983  N N   . TYR B 1 108 ? -25.420 27.776  32.855  1.00 64.46  ? 108 TYR B N   1 
ATOM   4984  C CA  . TYR B 1 108 ? -26.846 27.612  32.612  1.00 62.78  ? 108 TYR B CA  1 
ATOM   4985  C C   . TYR B 1 108 ? -27.437 26.429  33.370  1.00 67.24  ? 108 TYR B C   1 
ATOM   4986  O O   . TYR B 1 108 ? -28.503 25.934  32.990  1.00 77.35  ? 108 TYR B O   1 
ATOM   4987  C CB  . TYR B 1 108 ? -27.111 27.436  31.118  1.00 56.47  ? 108 TYR B CB  1 
ATOM   4988  C CG  . TYR B 1 108 ? -27.459 28.702  30.383  1.00 58.42  ? 108 TYR B CG  1 
ATOM   4989  C CD1 . TYR B 1 108 ? -26.502 29.679  30.142  1.00 57.60  ? 108 TYR B CD1 1 
ATOM   4990  C CD2 . TYR B 1 108 ? -28.743 28.913  29.912  1.00 63.96  ? 108 TYR B CD2 1 
ATOM   4991  C CE1 . TYR B 1 108 ? -26.825 30.837  29.458  1.00 58.09  ? 108 TYR B CE1 1 
ATOM   4992  C CE2 . TYR B 1 108 ? -29.076 30.063  29.231  1.00 63.46  ? 108 TYR B CE2 1 
ATOM   4993  C CZ  . TYR B 1 108 ? -28.119 31.021  29.003  1.00 60.85  ? 108 TYR B CZ  1 
ATOM   4994  O OH  . TYR B 1 108 ? -28.483 32.159  28.320  1.00 65.27  ? 108 TYR B OH  1 
ATOM   4995  N N   . ARG B 1 109 ? -26.765 25.952  34.419  1.00 63.08  ? 109 ARG B N   1 
ATOM   4996  C CA  . ARG B 1 109 ? -27.250 24.787  35.159  1.00 64.13  ? 109 ARG B CA  1 
ATOM   4997  C C   . ARG B 1 109 ? -28.224 25.241  36.243  1.00 74.34  ? 109 ARG B C   1 
ATOM   4998  O O   . ARG B 1 109 ? -27.961 25.194  37.447  1.00 77.98  ? 109 ARG B O   1 
ATOM   4999  C CB  . ARG B 1 109 ? -26.094 23.989  35.737  1.00 63.60  ? 109 ARG B CB  1 
ATOM   5000  C CG  . ARG B 1 109 ? -26.054 22.574  35.209  1.00 75.15  ? 109 ARG B CG  1 
ATOM   5001  C CD  . ARG B 1 109 ? -24.921 21.781  35.809  1.00 83.88  ? 109 ARG B CD  1 
ATOM   5002  N NE  . ARG B 1 109 ? -23.753 21.736  34.937  1.00 76.90  ? 109 ARG B NE  1 
ATOM   5003  C CZ  . ARG B 1 109 ? -22.507 21.939  35.339  1.00 75.35  ? 109 ARG B CZ  1 
ATOM   5004  N NH1 . ARG B 1 109 ? -22.221 22.193  36.606  1.00 79.69  ? 109 ARG B NH1 1 
ATOM   5005  N NH2 . ARG B 1 109 ? -21.522 21.868  34.449  1.00 81.63  ? 109 ARG B NH2 1 
ATOM   5006  N N   . PHE B 1 110 ? -29.370 25.713  35.767  1.00 73.84  ? 110 PHE B N   1 
ATOM   5007  C CA  . PHE B 1 110 ? -30.521 26.007  36.599  1.00 73.20  ? 110 PHE B CA  1 
ATOM   5008  C C   . PHE B 1 110 ? -31.567 24.928  36.360  1.00 78.71  ? 110 PHE B C   1 
ATOM   5009  O O   . PHE B 1 110 ? -31.834 24.554  35.211  1.00 76.87  ? 110 PHE B O   1 
ATOM   5010  C CB  . PHE B 1 110 ? -31.120 27.376  36.271  1.00 74.63  ? 110 PHE B CB  1 
ATOM   5011  C CG  . PHE B 1 110 ? -30.199 28.531  36.525  1.00 76.08  ? 110 PHE B CG  1 
ATOM   5012  C CD1 . PHE B 1 110 ? -30.104 29.110  37.782  1.00 71.51  ? 110 PHE B CD1 1 
ATOM   5013  C CD2 . PHE B 1 110 ? -29.441 29.054  35.492  1.00 72.65  ? 110 PHE B CD2 1 
ATOM   5014  C CE1 . PHE B 1 110 ? -29.248 30.193  37.998  1.00 66.93  ? 110 PHE B CE1 1 
ATOM   5015  C CE2 . PHE B 1 110 ? -28.597 30.126  35.705  1.00 67.07  ? 110 PHE B CE2 1 
ATOM   5016  C CZ  . PHE B 1 110 ? -28.503 30.694  36.960  1.00 65.49  ? 110 PHE B CZ  1 
ATOM   5017  N N   . GLU B 1 111 ? -32.162 24.439  37.453  1.00 78.45  ? 111 GLU B N   1 
ATOM   5018  C CA  . GLU B 1 111 ? -33.152 23.373  37.347  1.00 80.09  ? 111 GLU B CA  1 
ATOM   5019  C C   . GLU B 1 111 ? -34.403 23.833  36.615  1.00 79.45  ? 111 GLU B C   1 
ATOM   5020  O O   . GLU B 1 111 ? -35.009 23.045  35.880  1.00 73.13  ? 111 GLU B O   1 
ATOM   5021  C CB  . GLU B 1 111 ? -33.542 22.832  38.731  1.00 88.43  ? 111 GLU B CB  1 
ATOM   5022  C CG  . GLU B 1 111 ? -32.431 22.643  39.779  1.00 102.97 ? 111 GLU B CG  1 
ATOM   5023  C CD  . GLU B 1 111 ? -31.712 23.937  40.207  1.00 110.09 ? 111 GLU B CD  1 
ATOM   5024  O OE1 . GLU B 1 111 ? -30.573 23.835  40.701  1.00 126.32 ? 111 GLU B OE1 1 
ATOM   5025  O OE2 . GLU B 1 111 ? -32.302 25.019  40.039  1.00 113.77 ? 111 GLU B OE2 1 
ATOM   5026  N N   . ARG B 1 112 ? -34.805 25.092  36.802  1.00 73.38  ? 112 ARG B N   1 
ATOM   5027  C CA  . ARG B 1 112 ? -35.982 25.599  36.107  1.00 75.33  ? 112 ARG B CA  1 
ATOM   5028  C C   . ARG B 1 112 ? -35.777 25.586  34.599  1.00 72.72  ? 112 ARG B C   1 
ATOM   5029  O O   . ARG B 1 112 ? -36.709 25.289  33.843  1.00 78.76  ? 112 ARG B O   1 
ATOM   5030  C CB  . ARG B 1 112 ? -36.311 27.012  36.584  1.00 78.35  ? 112 ARG B CB  1 
ATOM   5031  C CG  . ARG B 1 112 ? -37.683 27.177  37.215  1.00 76.47  ? 112 ARG B CG  1 
ATOM   5032  C CD  . ARG B 1 112 ? -38.781 26.855  36.214  1.00 74.61  ? 112 ARG B CD  1 
ATOM   5033  N NE  . ARG B 1 112 ? -40.053 27.446  36.613  1.00 74.87  ? 112 ARG B NE  1 
ATOM   5034  C CZ  . ARG B 1 112 ? -41.224 27.161  36.062  1.00 78.93  ? 112 ARG B CZ  1 
ATOM   5035  N NH1 . ARG B 1 112 ? -41.339 26.237  35.125  1.00 91.40  ? 112 ARG B NH1 1 
ATOM   5036  N NH2 . ARG B 1 112 ? -42.312 27.806  36.479  1.00 79.25  ? 112 ARG B NH2 1 
ATOM   5037  N N   . ILE B 1 113 ? -34.561 25.905  34.145  1.00 69.52  ? 113 ILE B N   1 
ATOM   5038  C CA  . ILE B 1 113 ? -34.246 25.837  32.721  1.00 67.34  ? 113 ILE B CA  1 
ATOM   5039  C C   . ILE B 1 113 ? -34.513 24.438  32.184  1.00 70.31  ? 113 ILE B C   1 
ATOM   5040  O O   . ILE B 1 113 ? -35.008 24.273  31.063  1.00 81.46  ? 113 ILE B O   1 
ATOM   5041  C CB  . ILE B 1 113 ? -32.788 26.270  32.476  1.00 75.77  ? 113 ILE B CB  1 
ATOM   5042  C CG1 . ILE B 1 113 ? -32.656 27.783  32.514  1.00 74.26  ? 113 ILE B CG1 1 
ATOM   5043  C CG2 . ILE B 1 113 ? -32.300 25.809  31.132  1.00 70.28  ? 113 ILE B CG2 1 
ATOM   5044  C CD1 . ILE B 1 113 ? -31.248 28.230  32.249  1.00 66.50  ? 113 ILE B CD1 1 
ATOM   5045  N N   . ARG B 1 114 ? -34.206 23.409  32.978  1.00 77.44  ? 114 ARG B N   1 
ATOM   5046  C CA  . ARG B 1 114 ? -34.493 22.037  32.567  1.00 78.51  ? 114 ARG B CA  1 
ATOM   5047  C C   . ARG B 1 114 ? -35.990 21.802  32.395  1.00 83.76  ? 114 ARG B C   1 
ATOM   5048  O O   . ARG B 1 114 ? -36.420 21.175  31.417  1.00 84.53  ? 114 ARG B O   1 
ATOM   5049  C CB  . ARG B 1 114 ? -33.905 21.052  33.580  1.00 80.91  ? 114 ARG B CB  1 
ATOM   5050  C CG  . ARG B 1 114 ? -32.428 20.750  33.343  1.00 86.29  ? 114 ARG B CG  1 
ATOM   5051  C CD  . ARG B 1 114 ? -31.520 21.417  34.371  1.00 89.71  ? 114 ARG B CD  1 
ATOM   5052  N NE  . ARG B 1 114 ? -30.116 21.062  34.180  1.00 90.85  ? 114 ARG B NE  1 
ATOM   5053  C CZ  . ARG B 1 114 ? -29.330 21.557  33.233  1.00 83.00  ? 114 ARG B CZ  1 
ATOM   5054  N NH1 . ARG B 1 114 ? -29.759 22.484  32.388  1.00 72.40  ? 114 ARG B NH1 1 
ATOM   5055  N NH2 . ARG B 1 114 ? -28.079 21.113  33.135  1.00 83.97  ? 114 ARG B NH2 1 
ATOM   5056  N N   . GLU B 1 115 ? -36.802 22.295  33.334  1.00 76.71  ? 115 GLU B N   1 
ATOM   5057  C CA  . GLU B 1 115 ? -38.244 22.072  33.255  1.00 75.27  ? 115 GLU B CA  1 
ATOM   5058  C C   . GLU B 1 115 ? -38.845 22.811  32.067  1.00 85.14  ? 115 GLU B C   1 
ATOM   5059  O O   . GLU B 1 115 ? -39.627 22.239  31.297  1.00 86.78  ? 115 GLU B O   1 
ATOM   5060  C CB  . GLU B 1 115 ? -38.924 22.517  34.551  1.00 85.03  ? 115 GLU B CB  1 
ATOM   5061  C CG  . GLU B 1 115 ? -38.003 22.553  35.757  1.00 92.10  ? 115 GLU B CG  1 
ATOM   5062  C CD  . GLU B 1 115 ? -38.709 22.961  37.041  1.00 92.87  ? 115 GLU B CD  1 
ATOM   5063  O OE1 . GLU B 1 115 ? -39.854 23.459  36.963  1.00 87.87  ? 115 GLU B OE1 1 
ATOM   5064  O OE2 . GLU B 1 115 ? -38.112 22.803  38.128  1.00 89.07  ? 115 GLU B OE2 1 
ATOM   5065  N N   . LEU B 1 116 ? -38.502 24.096  31.916  1.00 78.96  ? 116 LEU B N   1 
ATOM   5066  C CA  . LEU B 1 116 ? -39.034 24.886  30.813  1.00 72.89  ? 116 LEU B CA  1 
ATOM   5067  C C   . LEU B 1 116 ? -38.706 24.250  29.473  1.00 69.60  ? 116 LEU B C   1 
ATOM   5068  O O   . LEU B 1 116 ? -39.561 24.184  28.583  1.00 69.46  ? 116 LEU B O   1 
ATOM   5069  C CB  . LEU B 1 116 ? -38.486 26.313  30.888  1.00 70.65  ? 116 LEU B CB  1 
ATOM   5070  C CG  . LEU B 1 116 ? -38.886 27.108  32.128  1.00 72.45  ? 116 LEU B CG  1 
ATOM   5071  C CD1 . LEU B 1 116 ? -37.959 28.279  32.319  1.00 70.25  ? 116 LEU B CD1 1 
ATOM   5072  C CD2 . LEU B 1 116 ? -40.291 27.605  31.964  1.00 71.56  ? 116 LEU B CD2 1 
ATOM   5073  N N   . MET B 1 117 ? -37.479 23.746  29.323  1.00 67.11  ? 117 MET B N   1 
ATOM   5074  C CA  . MET B 1 117 ? -37.057 23.197  28.036  1.00 77.71  ? 117 MET B CA  1 
ATOM   5075  C C   . MET B 1 117 ? -37.777 21.888  27.720  1.00 80.73  ? 117 MET B C   1 
ATOM   5076  O O   . MET B 1 117 ? -38.153 21.636  26.566  1.00 74.65  ? 117 MET B O   1 
ATOM   5077  C CB  . MET B 1 117 ? -35.540 23.001  28.019  1.00 74.90  ? 117 MET B CB  1 
ATOM   5078  C CG  . MET B 1 117 ? -34.758 24.306  27.929  1.00 71.45  ? 117 MET B CG  1 
ATOM   5079  S SD  . MET B 1 117 ? -34.671 24.973  26.253  1.00 91.78  ? 117 MET B SD  1 
ATOM   5080  C CE  . MET B 1 117 ? -35.997 26.183  26.287  1.00 71.33  ? 117 MET B CE  1 
ATOM   5081  N N   . ASN B 1 118 ? -37.996 21.050  28.732  1.00 78.88  ? 118 ASN B N   1 
ATOM   5082  C CA  . ASN B 1 118 ? -38.766 19.829  28.544  1.00 83.80  ? 118 ASN B CA  1 
ATOM   5083  C C   . ASN B 1 118 ? -40.272 20.077  28.492  1.00 74.62  ? 118 ASN B C   1 
ATOM   5084  O O   . ASN B 1 118 ? -41.019 19.163  28.133  1.00 82.09  ? 118 ASN B O   1 
ATOM   5085  C CB  . ASN B 1 118 ? -38.432 18.839  29.661  1.00 86.63  ? 118 ASN B CB  1 
ATOM   5086  C CG  . ASN B 1 118 ? -37.022 18.297  29.549  1.00 84.70  ? 118 ASN B CG  1 
ATOM   5087  O OD1 . ASN B 1 118 ? -36.730 17.447  28.710  1.00 82.50  ? 118 ASN B OD1 1 
ATOM   5088  N ND2 . ASN B 1 118 ? -36.126 18.824  30.373  1.00 88.33  ? 118 ASN B ND2 1 
ATOM   5089  N N   . LYS B 1 119 ? -40.737 21.280  28.828  1.00 70.57  ? 119 LYS B N   1 
ATOM   5090  C CA  . LYS B 1 119 ? -42.151 21.612  28.694  1.00 78.86  ? 119 LYS B CA  1 
ATOM   5091  C C   . LYS B 1 119 ? -42.471 22.010  27.258  1.00 79.99  ? 119 LYS B C   1 
ATOM   5092  O O   . LYS B 1 119 ? -41.671 22.667  26.586  1.00 75.31  ? 119 LYS B O   1 
ATOM   5093  C CB  . LYS B 1 119 ? -42.533 22.743  29.649  1.00 79.33  ? 119 LYS B CB  1 
ATOM   5094  C CG  . LYS B 1 119 ? -43.099 22.271  30.976  1.00 87.87  ? 119 LYS B CG  1 
ATOM   5095  C CD  . LYS B 1 119 ? -43.249 23.424  31.948  1.00 84.16  ? 119 LYS B CD  1 
ATOM   5096  C CE  . LYS B 1 119 ? -43.116 22.967  33.398  1.00 92.57  ? 119 LYS B CE  1 
ATOM   5097  N NZ  . LYS B 1 119 ? -43.313 21.499  33.593  1.00 90.73  ? 119 LYS B NZ  1 
ATOM   5098  N N   . GLU B 1 120 ? -43.664 21.626  26.802  1.00 80.14  ? 120 GLU B N   1 
ATOM   5099  C CA  . GLU B 1 120 ? -44.031 21.772  25.396  1.00 76.74  ? 120 GLU B CA  1 
ATOM   5100  C C   . GLU B 1 120 ? -44.606 23.151  25.101  1.00 73.56  ? 120 GLU B C   1 
ATOM   5101  O O   . GLU B 1 120 ? -44.312 23.738  24.053  1.00 72.06  ? 120 GLU B O   1 
ATOM   5102  C CB  . GLU B 1 120 ? -45.033 20.681  24.998  1.00 74.33  ? 120 GLU B CB  1 
ATOM   5103  C CG  . GLU B 1 120 ? -44.748 19.263  25.539  1.00 97.31  ? 120 GLU B CG  1 
ATOM   5104  C CD  . GLU B 1 120 ? -44.865 19.125  27.058  1.00 105.73 ? 120 GLU B CD  1 
ATOM   5105  O OE1 . GLU B 1 120 ? -44.545 18.033  27.578  1.00 109.72 ? 120 GLU B OE1 1 
ATOM   5106  O OE2 . GLU B 1 120 ? -45.263 20.106  27.730  1.00 100.03 ? 120 GLU B OE2 1 
ATOM   5107  N N   . LYS B 1 121 ? -45.425 23.672  26.011  1.00 69.12  ? 121 LYS B N   1 
ATOM   5108  C CA  . LYS B 1 121 ? -45.965 25.020  25.934  1.00 63.48  ? 121 LYS B CA  1 
ATOM   5109  C C   . LYS B 1 121 ? -45.788 25.701  27.285  1.00 66.71  ? 121 LYS B C   1 
ATOM   5110  O O   . LYS B 1 121 ? -45.881 25.058  28.335  1.00 77.14  ? 121 LYS B O   1 
ATOM   5111  C CB  . LYS B 1 121 ? -47.445 25.009  25.543  1.00 66.34  ? 121 LYS B CB  1 
ATOM   5112  C CG  . LYS B 1 121 ? -47.975 26.349  25.076  1.00 71.80  ? 121 LYS B CG  1 
ATOM   5113  C CD  . LYS B 1 121 ? -47.598 26.626  23.628  1.00 73.03  ? 121 LYS B CD  1 
ATOM   5114  C CE  . LYS B 1 121 ? -48.301 27.876  23.105  1.00 85.52  ? 121 LYS B CE  1 
ATOM   5115  N NZ  . LYS B 1 121 ? -49.064 27.627  21.840  1.00 86.57  ? 121 LYS B NZ  1 
ATOM   5116  N N   . LEU B 1 122 ? -45.554 27.014  27.256  1.00 67.07  ? 122 LEU B N   1 
ATOM   5117  C CA  . LEU B 1 122 ? -45.125 27.771  28.429  1.00 69.50  ? 122 LEU B CA  1 
ATOM   5118  C C   . LEU B 1 122 ? -46.057 28.948  28.675  1.00 63.17  ? 122 LEU B C   1 
ATOM   5119  O O   . LEU B 1 122 ? -46.363 29.694  27.743  1.00 64.29  ? 122 LEU B O   1 
ATOM   5120  C CB  . LEU B 1 122 ? -43.691 28.284  28.239  1.00 68.32  ? 122 LEU B CB  1 
ATOM   5121  C CG  . LEU B 1 122 ? -42.640 27.192  28.043  1.00 69.61  ? 122 LEU B CG  1 
ATOM   5122  C CD1 . LEU B 1 122 ? -41.305 27.783  27.602  1.00 56.77  ? 122 LEU B CD1 1 
ATOM   5123  C CD2 . LEU B 1 122 ? -42.491 26.331  29.290  1.00 68.67  ? 122 LEU B CD2 1 
ATOM   5124  N N   . ASN B 1 123 ? -46.485 29.132  29.924  1.00 66.03  ? 123 ASN B N   1 
ATOM   5125  C CA  . ASN B 1 123 ? -47.337 30.268  30.253  1.00 68.73  ? 123 ASN B CA  1 
ATOM   5126  C C   . ASN B 1 123 ? -46.487 31.510  30.501  1.00 63.44  ? 123 ASN B C   1 
ATOM   5127  O O   . ASN B 1 123 ? -45.261 31.501  30.356  1.00 63.85  ? 123 ASN B O   1 
ATOM   5128  C CB  . ASN B 1 123 ? -48.217 29.975  31.467  1.00 72.82  ? 123 ASN B CB  1 
ATOM   5129  C CG  . ASN B 1 123 ? -47.516 29.131  32.509  1.00 79.67  ? 123 ASN B CG  1 
ATOM   5130  O OD1 . ASN B 1 123 ? -47.152 27.989  32.250  1.00 84.84  ? 123 ASN B OD1 1 
ATOM   5131  N ND2 . ASN B 1 123 ? -47.295 29.703  33.689  1.00 78.42  ? 123 ASN B ND2 1 
ATOM   5132  N N   . ARG B 1 124 ? -47.157 32.599  30.883  1.00 61.34  ? 124 ARG B N   1 
ATOM   5133  C CA  . ARG B 1 124 ? -46.456 33.860  31.100  1.00 64.14  ? 124 ARG B CA  1 
ATOM   5134  C C   . ARG B 1 124 ? -45.419 33.729  32.209  1.00 68.98  ? 124 ARG B C   1 
ATOM   5135  O O   . ARG B 1 124 ? -44.278 34.182  32.066  1.00 59.61  ? 124 ARG B O   1 
ATOM   5136  C CB  . ARG B 1 124 ? -47.459 34.967  31.428  1.00 61.64  ? 124 ARG B CB  1 
ATOM   5137  C CG  . ARG B 1 124 ? -46.844 36.137  32.192  1.00 59.31  ? 124 ARG B CG  1 
ATOM   5138  C CD  . ARG B 1 124 ? -47.876 37.173  32.624  1.00 56.38  ? 124 ARG B CD  1 
ATOM   5139  N NE  . ARG B 1 124 ? -47.258 38.451  32.965  1.00 64.27  ? 124 ARG B NE  1 
ATOM   5140  C CZ  . ARG B 1 124 ? -46.645 38.721  34.114  1.00 65.99  ? 124 ARG B CZ  1 
ATOM   5141  N NH1 . ARG B 1 124 ? -46.569 37.825  35.087  1.00 54.00  ? 124 ARG B NH1 1 
ATOM   5142  N NH2 . ARG B 1 124 ? -46.100 39.923  34.294  1.00 53.36  ? 124 ARG B NH2 1 
ATOM   5143  N N   . GLU B 1 125 ? -45.795 33.096  33.321  1.00 66.30  ? 125 GLU B N   1 
ATOM   5144  C CA  . GLU B 1 125 ? -44.886 32.994  34.456  1.00 56.27  ? 125 GLU B CA  1 
ATOM   5145  C C   . GLU B 1 125 ? -43.675 32.137  34.117  1.00 63.75  ? 125 GLU B C   1 
ATOM   5146  O O   . GLU B 1 125 ? -42.549 32.439  34.535  1.00 66.72  ? 125 GLU B O   1 
ATOM   5147  C CB  . GLU B 1 125 ? -45.636 32.429  35.655  1.00 58.84  ? 125 GLU B CB  1 
ATOM   5148  C CG  . GLU B 1 125 ? -46.555 33.445  36.323  1.00 67.47  ? 125 GLU B CG  1 
ATOM   5149  C CD  . GLU B 1 125 ? -47.805 33.783  35.502  1.00 74.38  ? 125 GLU B CD  1 
ATOM   5150  O OE1 . GLU B 1 125 ? -48.507 32.864  35.016  1.00 70.63  ? 125 GLU B OE1 1 
ATOM   5151  O OE2 . GLU B 1 125 ? -48.087 34.989  35.350  1.00 74.31  ? 125 GLU B OE2 1 
ATOM   5152  N N   . GLU B 1 126 ? -43.888 31.062  33.360  1.00 68.51  ? 126 GLU B N   1 
ATOM   5153  C CA  . GLU B 1 126 ? -42.775 30.231  32.927  1.00 63.30  ? 126 GLU B CA  1 
ATOM   5154  C C   . GLU B 1 126 ? -41.868 30.994  31.975  1.00 57.24  ? 126 GLU B C   1 
ATOM   5155  O O   . GLU B 1 126 ? -40.643 30.982  32.128  1.00 65.25  ? 126 GLU B O   1 
ATOM   5156  C CB  . GLU B 1 126 ? -43.309 28.956  32.283  1.00 70.08  ? 126 GLU B CB  1 
ATOM   5157  C CG  . GLU B 1 126 ? -44.072 28.074  33.257  1.00 73.32  ? 126 GLU B CG  1 
ATOM   5158  C CD  . GLU B 1 126 ? -44.577 26.797  32.622  1.00 80.72  ? 126 GLU B CD  1 
ATOM   5159  O OE1 . GLU B 1 126 ? -44.863 26.813  31.407  1.00 78.10  ? 126 GLU B OE1 1 
ATOM   5160  O OE2 . GLU B 1 126 ? -44.728 25.790  33.346  1.00 85.11  ? 126 GLU B OE2 1 
ATOM   5161  N N   . LEU B 1 127 ? -42.458 31.687  30.998  1.00 59.02  ? 127 LEU B N   1 
ATOM   5162  C CA  . LEU B 1 127 ? -41.666 32.513  30.094  1.00 55.71  ? 127 LEU B CA  1 
ATOM   5163  C C   . LEU B 1 127 ? -40.864 33.555  30.861  1.00 52.16  ? 127 LEU B C   1 
ATOM   5164  O O   . LEU B 1 127 ? -39.721 33.857  30.501  1.00 61.46  ? 127 LEU B O   1 
ATOM   5165  C CB  . LEU B 1 127 ? -42.572 33.192  29.070  1.00 52.82  ? 127 LEU B CB  1 
ATOM   5166  C CG  . LEU B 1 127 ? -42.807 32.430  27.769  1.00 47.02  ? 127 LEU B CG  1 
ATOM   5167  C CD1 . LEU B 1 127 ? -43.847 33.137  26.943  1.00 46.74  ? 127 LEU B CD1 1 
ATOM   5168  C CD2 . LEU B 1 127 ? -41.530 32.326  26.990  1.00 51.91  ? 127 LEU B CD2 1 
ATOM   5169  N N   . LEU B 1 128 ? -41.446 34.117  31.923  1.00 48.85  ? 128 LEU B N   1 
ATOM   5170  C CA  . LEU B 1 128 ? -40.703 35.065  32.742  1.00 51.62  ? 128 LEU B CA  1 
ATOM   5171  C C   . LEU B 1 128 ? -39.487 34.396  33.361  1.00 62.03  ? 128 LEU B C   1 
ATOM   5172  O O   . LEU B 1 128 ? -38.419 35.015  33.474  1.00 61.35  ? 128 LEU B O   1 
ATOM   5173  C CB  . LEU B 1 128 ? -41.609 35.657  33.824  1.00 56.41  ? 128 LEU B CB  1 
ATOM   5174  C CG  . LEU B 1 128 ? -41.305 37.068  34.349  1.00 58.04  ? 128 LEU B CG  1 
ATOM   5175  C CD1 . LEU B 1 128 ? -41.070 38.052  33.218  1.00 55.62  ? 128 LEU B CD1 1 
ATOM   5176  C CD2 . LEU B 1 128 ? -42.440 37.566  35.225  1.00 54.42  ? 128 LEU B CD2 1 
ATOM   5177  N N   . ASP B 1 129 ? -39.618 33.120  33.728  1.00 59.53  ? 129 ASP B N   1 
ATOM   5178  C CA  . ASP B 1 129 ? -38.486 32.409  34.311  1.00 62.64  ? 129 ASP B CA  1 
ATOM   5179  C C   . ASP B 1 129 ? -37.402 32.151  33.272  1.00 59.65  ? 129 ASP B C   1 
ATOM   5180  O O   . ASP B 1 129 ? -36.207 32.216  33.584  1.00 66.45  ? 129 ASP B O   1 
ATOM   5181  C CB  . ASP B 1 129 ? -38.963 31.110  34.960  1.00 60.67  ? 129 ASP B CB  1 
ATOM   5182  C CG  . ASP B 1 129 ? -39.554 31.337  36.344  1.00 67.06  ? 129 ASP B CG  1 
ATOM   5183  O OD1 . ASP B 1 129 ? -39.706 32.512  36.744  1.00 63.70  ? 129 ASP B OD1 1 
ATOM   5184  O OD2 . ASP B 1 129 ? -39.870 30.342  37.032  1.00 77.65  ? 129 ASP B OD2 1 
ATOM   5185  N N   . LEU B 1 130 ? -37.792 31.885  32.026  1.00 50.96  ? 130 LEU B N   1 
ATOM   5186  C CA  . LEU B 1 130 ? -36.794 31.733  30.975  1.00 53.99  ? 130 LEU B CA  1 
ATOM   5187  C C   . LEU B 1 130 ? -36.045 33.040  30.746  1.00 59.53  ? 130 LEU B C   1 
ATOM   5188  O O   . LEU B 1 130 ? -34.813 33.046  30.627  1.00 62.61  ? 130 LEU B O   1 
ATOM   5189  C CB  . LEU B 1 130 ? -37.458 31.254  29.686  1.00 60.52  ? 130 LEU B CB  1 
ATOM   5190  C CG  . LEU B 1 130 ? -36.595 30.392  28.763  1.00 58.25  ? 130 LEU B CG  1 
ATOM   5191  C CD1 . LEU B 1 130 ? -35.938 29.240  29.521  1.00 54.50  ? 130 LEU B CD1 1 
ATOM   5192  C CD2 . LEU B 1 130 ? -37.440 29.876  27.613  1.00 59.23  ? 130 LEU B CD2 1 
ATOM   5193  N N   . GLN B 1 131 ? -36.770 34.161  30.708  1.00 58.04  ? 131 GLN B N   1 
ATOM   5194  C CA  . GLN B 1 131 ? -36.132 35.456  30.496  1.00 57.18  ? 131 GLN B CA  1 
ATOM   5195  C C   . GLN B 1 131 ? -35.166 35.781  31.623  1.00 53.09  ? 131 GLN B C   1 
ATOM   5196  O O   . GLN B 1 131 ? -33.992 36.080  31.383  1.00 58.56  ? 131 GLN B O   1 
ATOM   5197  C CB  . GLN B 1 131 ? -37.186 36.553  30.386  1.00 60.82  ? 131 GLN B CB  1 
ATOM   5198  C CG  . GLN B 1 131 ? -38.068 36.481  29.152  1.00 58.11  ? 131 GLN B CG  1 
ATOM   5199  C CD  . GLN B 1 131 ? -39.200 37.482  29.213  1.00 53.48  ? 131 GLN B CD  1 
ATOM   5200  O OE1 . GLN B 1 131 ? -39.800 37.693  30.268  1.00 52.34  ? 131 GLN B OE1 1 
ATOM   5201  N NE2 . GLN B 1 131 ? -39.476 38.131  28.093  1.00 52.82  ? 131 GLN B NE2 1 
ATOM   5202  N N   . THR B 1 132 ? -35.642 35.710  32.865  1.00 52.92  ? 132 THR B N   1 
ATOM   5203  C CA  . THR B 1 132 ? -34.809 36.103  33.996  1.00 55.12  ? 132 THR B CA  1 
ATOM   5204  C C   . THR B 1 132 ? -33.629 35.157  34.188  1.00 55.25  ? 132 THR B C   1 
ATOM   5205  O O   . THR B 1 132 ? -32.543 35.586  34.589  1.00 62.13  ? 132 THR B O   1 
ATOM   5206  C CB  . THR B 1 132 ? -35.646 36.164  35.268  1.00 56.94  ? 132 THR B CB  1 
ATOM   5207  O OG1 . THR B 1 132 ? -36.808 36.964  35.031  1.00 57.66  ? 132 THR B OG1 1 
ATOM   5208  C CG2 . THR B 1 132 ? -34.838 36.789  36.385  1.00 56.93  ? 132 THR B CG2 1 
ATOM   5209  N N   . LEU B 1 133 ? -33.815 33.866  33.913  1.00 54.23  ? 133 LEU B N   1 
ATOM   5210  C CA  . LEU B 1 133 ? -32.721 32.930  34.142  1.00 55.62  ? 133 LEU B CA  1 
ATOM   5211  C C   . LEU B 1 133 ? -31.674 33.020  33.043  1.00 54.19  ? 133 LEU B C   1 
ATOM   5212  O O   . LEU B 1 133 ? -30.484 32.818  33.308  1.00 59.01  ? 133 LEU B O   1 
ATOM   5213  C CB  . LEU B 1 133 ? -33.255 31.506  34.266  1.00 62.11  ? 133 LEU B CB  1 
ATOM   5214  C CG  . LEU B 1 133 ? -33.912 31.179  35.608  1.00 62.22  ? 133 LEU B CG  1 
ATOM   5215  C CD1 . LEU B 1 133 ? -34.211 29.709  35.703  1.00 68.68  ? 133 LEU B CD1 1 
ATOM   5216  C CD2 . LEU B 1 133 ? -32.999 31.576  36.735  1.00 62.56  ? 133 LEU B CD2 1 
ATOM   5217  N N   . ASN B 1 134 ? -32.094 33.312  31.811  1.00 57.70  ? 134 ASN B N   1 
ATOM   5218  C CA  . ASN B 1 134 ? -31.129 33.657  30.776  1.00 54.76  ? 134 ASN B CA  1 
ATOM   5219  C C   . ASN B 1 134 ? -30.279 34.836  31.215  1.00 52.19  ? 134 ASN B C   1 
ATOM   5220  O O   . ASN B 1 134 ? -29.067 34.865  30.977  1.00 59.56  ? 134 ASN B O   1 
ATOM   5221  C CB  . ASN B 1 134 ? -31.846 33.980  29.467  1.00 55.77  ? 134 ASN B CB  1 
ATOM   5222  C CG  . ASN B 1 134 ? -31.986 32.775  28.574  1.00 58.71  ? 134 ASN B CG  1 
ATOM   5223  O OD1 . ASN B 1 134 ? -31.081 32.450  27.805  1.00 57.17  ? 134 ASN B OD1 1 
ATOM   5224  N ND2 . ASN B 1 134 ? -33.122 32.097  28.670  1.00 54.97  ? 134 ASN B ND2 1 
ATOM   5225  N N   . LEU B 1 135 ? -30.895 35.808  31.881  1.00 50.62  ? 135 LEU B N   1 
ATOM   5226  C CA  . LEU B 1 135 ? -30.141 36.942  32.393  1.00 55.73  ? 135 LEU B CA  1 
ATOM   5227  C C   . LEU B 1 135 ? -29.210 36.514  33.517  1.00 55.87  ? 135 LEU B C   1 
ATOM   5228  O O   . LEU B 1 135 ? -28.010 36.810  33.496  1.00 62.44  ? 135 LEU B O   1 
ATOM   5229  C CB  . LEU B 1 135 ? -31.101 38.016  32.883  1.00 49.32  ? 135 LEU B CB  1 
ATOM   5230  C CG  . LEU B 1 135 ? -31.539 39.018  31.830  1.00 49.21  ? 135 LEU B CG  1 
ATOM   5231  C CD1 . LEU B 1 135 ? -32.381 40.005  32.541  1.00 57.13  ? 135 LEU B CD1 1 
ATOM   5232  C CD2 . LEU B 1 135 ? -30.365 39.719  31.191  1.00 61.95  ? 135 LEU B CD2 1 
ATOM   5233  N N   . LEU B 1 136 ? -29.747 35.809  34.510  1.00 52.59  ? 136 LEU B N   1 
ATOM   5234  C CA  . LEU B 1 136 ? -28.956 35.512  35.696  1.00 57.00  ? 136 LEU B CA  1 
ATOM   5235  C C   . LEU B 1 136 ? -27.835 34.525  35.394  1.00 62.33  ? 136 LEU B C   1 
ATOM   5236  O O   . LEU B 1 136 ? -26.832 34.493  36.114  1.00 64.62  ? 136 LEU B O   1 
ATOM   5237  C CB  . LEU B 1 136 ? -29.858 34.986  36.807  1.00 59.19  ? 136 LEU B CB  1 
ATOM   5238  C CG  . LEU B 1 136 ? -30.839 36.009  37.370  1.00 59.14  ? 136 LEU B CG  1 
ATOM   5239  C CD1 . LEU B 1 136 ? -31.637 35.404  38.514  1.00 61.79  ? 136 LEU B CD1 1 
ATOM   5240  C CD2 . LEU B 1 136 ? -30.091 37.244  37.827  1.00 64.22  ? 136 LEU B CD2 1 
ATOM   5241  N N   . ALA B 1 137 ? -27.978 33.717  34.341  1.00 59.39  ? 137 ALA B N   1 
ATOM   5242  C CA  . ALA B 1 137 ? -26.887 32.823  33.959  1.00 58.36  ? 137 ALA B CA  1 
ATOM   5243  C C   . ALA B 1 137 ? -25.644 33.614  33.577  1.00 58.43  ? 137 ALA B C   1 
ATOM   5244  O O   . ALA B 1 137 ? -24.518 33.237  33.925  1.00 62.91  ? 137 ALA B O   1 
ATOM   5245  C CB  . ALA B 1 137 ? -27.316 31.923  32.801  1.00 54.83  ? 137 ALA B CB  1 
ATOM   5246  N N   . TRP B 1 138 ? -25.836 34.725  32.872  1.00 61.54  ? 138 TRP B N   1 
ATOM   5247  C CA  . TRP B 1 138 ? -24.746 35.603  32.457  1.00 55.98  ? 138 TRP B CA  1 
ATOM   5248  C C   . TRP B 1 138 ? -24.478 36.663  33.525  1.00 54.25  ? 138 TRP B C   1 
ATOM   5249  O O   . TRP B 1 138 ? -24.558 37.862  33.282  1.00 59.93  ? 138 TRP B O   1 
ATOM   5250  C CB  . TRP B 1 138 ? -25.080 36.253  31.119  1.00 52.96  ? 138 TRP B CB  1 
ATOM   5251  C CG  . TRP B 1 138 ? -25.230 35.295  29.993  1.00 54.99  ? 138 TRP B CG  1 
ATOM   5252  C CD1 . TRP B 1 138 ? -26.380 34.703  29.569  1.00 56.68  ? 138 TRP B CD1 1 
ATOM   5253  C CD2 . TRP B 1 138 ? -24.189 34.817  29.130  1.00 62.13  ? 138 TRP B CD2 1 
ATOM   5254  N NE1 . TRP B 1 138 ? -26.121 33.881  28.494  1.00 60.71  ? 138 TRP B NE1 1 
ATOM   5255  C CE2 . TRP B 1 138 ? -24.783 33.934  28.207  1.00 54.35  ? 138 TRP B CE2 1 
ATOM   5256  C CE3 . TRP B 1 138 ? -22.811 35.052  29.048  1.00 56.38  ? 138 TRP B CE3 1 
ATOM   5257  C CZ2 . TRP B 1 138 ? -24.050 33.284  27.220  1.00 55.16  ? 138 TRP B CZ2 1 
ATOM   5258  C CZ3 . TRP B 1 138 ? -22.084 34.404  28.068  1.00 49.72  ? 138 TRP B CZ3 1 
ATOM   5259  C CH2 . TRP B 1 138 ? -22.704 33.531  27.167  1.00 59.36  ? 138 TRP B CH2 1 
ATOM   5260  N N   . CYS B 1 139 ? -24.157 36.204  34.727  1.00 60.07  ? 139 CYS B N   1 
ATOM   5261  C CA  . CYS B 1 139 ? -23.890 37.093  35.850  1.00 61.80  ? 139 CYS B CA  1 
ATOM   5262  C C   . CYS B 1 139 ? -22.410 37.032  36.206  1.00 63.74  ? 139 CYS B C   1 
ATOM   5263  O O   . CYS B 1 139 ? -21.835 35.941  36.315  1.00 58.35  ? 139 CYS B O   1 
ATOM   5264  C CB  . CYS B 1 139 ? -24.748 36.724  37.064  1.00 56.67  ? 139 CYS B CB  1 
ATOM   5265  S SG  . CYS B 1 139 ? -24.876 38.019  38.314  1.00 57.70  ? 139 CYS B SG  1 
ATOM   5266  N N   . GLY B 1 140 ? -21.795 38.215  36.385  1.00 64.35  ? 140 GLY B N   1 
ATOM   5267  C CA  . GLY B 1 140 ? -20.397 38.295  36.749  1.00 61.15  ? 140 GLY B CA  1 
ATOM   5268  C C   . GLY B 1 140 ? -20.157 38.192  38.248  1.00 60.35  ? 140 GLY B C   1 
ATOM   5269  O O   . GLY B 1 140 ? -21.089 38.276  39.048  1.00 61.81  ? 140 GLY B O   1 
ATOM   5270  N N   . ARG B 1 141 ? -18.872 38.030  38.596  1.00 57.71  ? 141 ARG B N   1 
ATOM   5271  C CA  . ARG B 1 141 ? -18.466 37.775  39.980  1.00 54.32  ? 141 ARG B CA  1 
ATOM   5272  C C   . ARG B 1 141 ? -18.930 38.879  40.925  1.00 57.12  ? 141 ARG B C   1 
ATOM   5273  O O   . ARG B 1 141 ? -19.334 38.604  42.062  1.00 58.70  ? 141 ARG B O   1 
ATOM   5274  C CB  . ARG B 1 141 ? -16.945 37.608  40.048  1.00 53.33  ? 141 ARG B CB  1 
ATOM   5275  C CG  . ARG B 1 141 ? -16.334 37.709  41.438  1.00 60.10  ? 141 ARG B CG  1 
ATOM   5276  C CD  . ARG B 1 141 ? -14.817 37.511  41.379  1.00 65.19  ? 141 ARG B CD  1 
ATOM   5277  N NE  . ARG B 1 141 ? -14.119 38.784  41.512  1.00 56.83  ? 141 ARG B NE  1 
ATOM   5278  C CZ  . ARG B 1 141 ? -13.534 39.217  42.617  1.00 50.08  ? 141 ARG B CZ  1 
ATOM   5279  N NH1 . ARG B 1 141 ? -13.448 38.460  43.699  1.00 56.46  ? 141 ARG B NH1 1 
ATOM   5280  N NH2 . ARG B 1 141 ? -13.030 40.446  42.640  1.00 53.41  ? 141 ARG B NH2 1 
ATOM   5281  N N   . THR B 1 142 ? -18.885 40.133  40.475  1.00 56.88  ? 142 THR B N   1 
ATOM   5282  C CA  . THR B 1 142 ? -19.319 41.239  41.324  1.00 59.48  ? 142 THR B CA  1 
ATOM   5283  C C   . THR B 1 142 ? -20.791 41.123  41.692  1.00 59.75  ? 142 THR B C   1 
ATOM   5284  O O   . THR B 1 142 ? -21.150 41.164  42.873  1.00 58.76  ? 142 THR B O   1 
ATOM   5285  C CB  . THR B 1 142 ? -19.062 42.574  40.629  1.00 59.09  ? 142 THR B CB  1 
ATOM   5286  O OG1 . THR B 1 142 ? -17.651 42.762  40.454  1.00 68.81  ? 142 THR B OG1 1 
ATOM   5287  C CG2 . THR B 1 142 ? -19.666 43.719  41.442  1.00 52.93  ? 142 THR B CG2 1 
ATOM   5288  N N   . LEU B 1 143 ? -21.662 41.000  40.684  1.00 57.70  ? 143 LEU B N   1 
ATOM   5289  C CA  . LEU B 1 143 ? -23.102 41.030  40.905  1.00 56.44  ? 143 LEU B CA  1 
ATOM   5290  C C   . LEU B 1 143 ? -23.651 39.725  41.466  1.00 59.68  ? 143 LEU B C   1 
ATOM   5291  O O   . LEU B 1 143 ? -24.757 39.727  42.021  1.00 63.50  ? 143 LEU B O   1 
ATOM   5292  C CB  . LEU B 1 143 ? -23.818 41.374  39.599  1.00 58.94  ? 143 LEU B CB  1 
ATOM   5293  C CG  . LEU B 1 143 ? -23.775 42.852  39.202  1.00 58.20  ? 143 LEU B CG  1 
ATOM   5294  C CD1 . LEU B 1 143 ? -24.977 43.229  38.335  1.00 56.20  ? 143 LEU B CD1 1 
ATOM   5295  C CD2 . LEU B 1 143 ? -23.681 43.747  40.444  1.00 49.34  ? 143 LEU B CD2 1 
ATOM   5296  N N   . ARG B 1 144 ? -22.919 38.613  41.328  1.00 59.79  ? 144 ARG B N   1 
ATOM   5297  C CA  . ARG B 1 144 ? -23.329 37.373  41.985  1.00 65.46  ? 144 ARG B CA  1 
ATOM   5298  C C   . ARG B 1 144 ? -23.461 37.555  43.489  1.00 68.19  ? 144 ARG B C   1 
ATOM   5299  O O   . ARG B 1 144 ? -24.261 36.864  44.132  1.00 67.30  ? 144 ARG B O   1 
ATOM   5300  C CB  . ARG B 1 144 ? -22.335 36.253  41.677  1.00 55.66  ? 144 ARG B CB  1 
ATOM   5301  C CG  . ARG B 1 144 ? -22.387 35.816  40.237  1.00 57.07  ? 144 ARG B CG  1 
ATOM   5302  C CD  . ARG B 1 144 ? -21.955 34.386  40.016  1.00 50.91  ? 144 ARG B CD  1 
ATOM   5303  N NE  . ARG B 1 144 ? -21.648 34.196  38.603  1.00 58.43  ? 144 ARG B NE  1 
ATOM   5304  C CZ  . ARG B 1 144 ? -21.561 33.020  37.998  1.00 64.45  ? 144 ARG B CZ  1 
ATOM   5305  N NH1 . ARG B 1 144 ? -21.719 31.887  38.661  1.00 68.10  ? 144 ARG B NH1 1 
ATOM   5306  N NH2 . ARG B 1 144 ? -21.327 32.980  36.691  1.00 65.45  ? 144 ARG B NH2 1 
ATOM   5307  N N   . LYS B 1 145 ? -22.678 38.474  44.063  1.00 66.75  ? 145 LYS B N   1 
ATOM   5308  C CA  . LYS B 1 145 ? -22.807 38.830  45.470  1.00 66.39  ? 145 LYS B CA  1 
ATOM   5309  C C   . LYS B 1 145 ? -24.013 39.736  45.713  1.00 74.70  ? 145 LYS B C   1 
ATOM   5310  O O   . LYS B 1 145 ? -24.688 39.613  46.743  1.00 71.97  ? 145 LYS B O   1 
ATOM   5311  C CB  . LYS B 1 145 ? -21.523 39.508  45.943  1.00 68.89  ? 145 LYS B CB  1 
ATOM   5312  C CG  . LYS B 1 145 ? -20.248 38.769  45.538  1.00 64.69  ? 145 LYS B CG  1 
ATOM   5313  C CD  . LYS B 1 145 ? -19.022 39.672  45.598  1.00 62.74  ? 145 LYS B CD  1 
ATOM   5314  C CE  . LYS B 1 145 ? -17.735 38.867  45.483  1.00 68.43  ? 145 LYS B CE  1 
ATOM   5315  N NZ  . LYS B 1 145 ? -17.561 37.907  46.609  1.00 81.83  ? 145 LYS B NZ  1 
ATOM   5316  N N   . ASP B 1 146 ? -24.304 40.644  44.774  1.00 73.32  ? 146 ASP B N   1 
ATOM   5317  C CA  . ASP B 1 146 ? -25.439 41.550  44.936  1.00 71.16  ? 146 ASP B CA  1 
ATOM   5318  C C   . ASP B 1 146 ? -26.766 40.828  44.740  1.00 68.13  ? 146 ASP B C   1 
ATOM   5319  O O   . ASP B 1 146 ? -27.730 41.082  45.472  1.00 83.21  ? 146 ASP B O   1 
ATOM   5320  C CB  . ASP B 1 146 ? -25.322 42.720  43.956  1.00 74.20  ? 146 ASP B CB  1 
ATOM   5321  C CG  . ASP B 1 146 ? -25.807 44.039  44.548  1.00 87.21  ? 146 ASP B CG  1 
ATOM   5322  O OD1 . ASP B 1 146 ? -26.800 44.025  45.310  1.00 93.44  ? 146 ASP B OD1 1 
ATOM   5323  O OD2 . ASP B 1 146 ? -25.206 45.095  44.241  1.00 82.99  ? 146 ASP B OD2 1 
ATOM   5324  N N   . LEU B 1 147 ? -26.840 39.936  43.755  1.00 62.29  ? 147 LEU B N   1 
ATOM   5325  C CA  . LEU B 1 147 ? -28.076 39.243  43.396  1.00 64.07  ? 147 LEU B CA  1 
ATOM   5326  C C   . LEU B 1 147 ? -28.114 37.829  43.951  1.00 71.61  ? 147 LEU B C   1 
ATOM   5327  O O   . LEU B 1 147 ? -28.551 36.896  43.267  1.00 64.58  ? 147 LEU B O   1 
ATOM   5328  C CB  . LEU B 1 147 ? -28.252 39.221  41.884  1.00 61.96  ? 147 LEU B CB  1 
ATOM   5329  C CG  . LEU B 1 147 ? -27.908 40.519  41.163  1.00 69.31  ? 147 LEU B CG  1 
ATOM   5330  C CD1 . LEU B 1 147 ? -27.500 40.223  39.724  1.00 63.13  ? 147 LEU B CD1 1 
ATOM   5331  C CD2 . LEU B 1 147 ? -29.088 41.489  41.231  1.00 61.79  ? 147 LEU B CD2 1 
ATOM   5332  N N   . LYS B 1 148 ? -27.673 37.651  45.198  1.00 72.63  ? 148 LYS B N   1 
ATOM   5333  C CA  . LYS B 1 148 ? -27.553 36.310  45.759  1.00 72.37  ? 148 LYS B CA  1 
ATOM   5334  C C   . LYS B 1 148 ? -28.915 35.644  45.917  1.00 74.05  ? 148 LYS B C   1 
ATOM   5335  O O   . LYS B 1 148 ? -29.128 34.530  45.426  1.00 76.87  ? 148 LYS B O   1 
ATOM   5336  C CB  . LYS B 1 148 ? -26.819 36.364  47.097  1.00 77.55  ? 148 LYS B CB  1 
ATOM   5337  C CG  . LYS B 1 148 ? -26.275 35.024  47.556  1.00 78.78  ? 148 LYS B CG  1 
ATOM   5338  C CD  . LYS B 1 148 ? -25.135 35.196  48.540  1.00 73.98  ? 148 LYS B CD  1 
ATOM   5339  C CE  . LYS B 1 148 ? -25.296 36.437  49.414  1.00 82.03  ? 148 LYS B CE  1 
ATOM   5340  N NZ  . LYS B 1 148 ? -26.561 36.448  50.207  1.00 83.06  ? 148 LYS B NZ  1 
ATOM   5341  N N   . ASP B 1 149 ? -29.855 36.304  46.599  1.00 71.70  ? 149 ASP B N   1 
ATOM   5342  C CA  . ASP B 1 149 ? -31.150 35.670  46.834  1.00 78.00  ? 149 ASP B CA  1 
ATOM   5343  C C   . ASP B 1 149 ? -31.867 35.384  45.521  1.00 78.96  ? 149 ASP B C   1 
ATOM   5344  O O   . ASP B 1 149 ? -32.397 34.285  45.322  1.00 83.42  ? 149 ASP B O   1 
ATOM   5345  C CB  . ASP B 1 149 ? -32.029 36.531  47.740  1.00 80.85  ? 149 ASP B CB  1 
ATOM   5346  C CG  . ASP B 1 149 ? -33.515 36.233  47.555  1.00 102.45 ? 149 ASP B CG  1 
ATOM   5347  O OD1 . ASP B 1 149 ? -33.998 35.217  48.106  1.00 104.47 ? 149 ASP B OD1 1 
ATOM   5348  O OD2 . ASP B 1 149 ? -34.201 37.016  46.861  1.00 94.18  ? 149 ASP B OD2 1 
ATOM   5349  N N   . LEU B 1 150 ? -31.895 36.362  44.607  1.00 72.81  ? 150 LEU B N   1 
ATOM   5350  C CA  . LEU B 1 150 ? -32.500 36.118  43.301  1.00 64.48  ? 150 LEU B CA  1 
ATOM   5351  C C   . LEU B 1 150 ? -31.879 34.895  42.640  1.00 67.26  ? 150 LEU B C   1 
ATOM   5352  O O   . LEU B 1 150 ? -32.590 34.054  42.077  1.00 63.98  ? 150 LEU B O   1 
ATOM   5353  C CB  . LEU B 1 150 ? -32.351 37.349  42.402  1.00 60.06  ? 150 LEU B CB  1 
ATOM   5354  C CG  . LEU B 1 150 ? -33.166 38.588  42.777  1.00 64.43  ? 150 LEU B CG  1 
ATOM   5355  C CD1 . LEU B 1 150 ? -32.497 39.843  42.253  1.00 65.85  ? 150 LEU B CD1 1 
ATOM   5356  C CD2 . LEU B 1 150 ? -34.579 38.486  42.242  1.00 65.90  ? 150 LEU B CD2 1 
ATOM   5357  N N   . LEU B 1 151 ? -30.553 34.760  42.737  1.00 73.30  ? 151 LEU B N   1 
ATOM   5358  C CA  . LEU B 1 151 ? -29.869 33.599  42.174  1.00 73.29  ? 151 LEU B CA  1 
ATOM   5359  C C   . LEU B 1 151 ? -30.259 32.316  42.902  1.00 74.70  ? 151 LEU B C   1 
ATOM   5360  O O   . LEU B 1 151 ? -30.373 31.253  42.279  1.00 73.78  ? 151 LEU B O   1 
ATOM   5361  C CB  . LEU B 1 151 ? -28.355 33.808  42.226  1.00 62.26  ? 151 LEU B CB  1 
ATOM   5362  C CG  . LEU B 1 151 ? -27.756 34.722  41.148  1.00 75.80  ? 151 LEU B CG  1 
ATOM   5363  C CD1 . LEU B 1 151 ? -26.347 35.173  41.527  1.00 75.06  ? 151 LEU B CD1 1 
ATOM   5364  C CD2 . LEU B 1 151 ? -27.765 34.056  39.768  1.00 72.00  ? 151 LEU B CD2 1 
ATOM   5365  N N   . ASN B 1 152 ? -30.474 32.397  44.218  1.00 71.75  ? 152 ASN B N   1 
ATOM   5366  C CA  . ASN B 1 152 ? -30.845 31.228  45.009  1.00 76.22  ? 152 ASN B CA  1 
ATOM   5367  C C   . ASN B 1 152 ? -32.330 30.880  44.903  1.00 75.99  ? 152 ASN B C   1 
ATOM   5368  O O   . ASN B 1 152 ? -32.696 29.724  45.138  1.00 76.80  ? 152 ASN B O   1 
ATOM   5369  C CB  . ASN B 1 152 ? -30.476 31.447  46.482  1.00 77.80  ? 152 ASN B CB  1 
ATOM   5370  C CG  . ASN B 1 152 ? -28.976 31.598  46.703  1.00 85.39  ? 152 ASN B CG  1 
ATOM   5371  O OD1 . ASN B 1 152 ? -28.164 30.969  46.024  1.00 88.50  ? 152 ASN B OD1 1 
ATOM   5372  N ND2 . ASN B 1 152 ? -28.604 32.434  47.670  1.00 77.38  ? 152 ASN B ND2 1 
ATOM   5373  N N   . LYS B 1 153 ? -33.192 31.845  44.567  1.00 70.38  ? 153 LYS B N   1 
ATOM   5374  C CA  . LYS B 1 153 ? -34.607 31.537  44.368  1.00 67.39  ? 153 LYS B CA  1 
ATOM   5375  C C   . LYS B 1 153 ? -34.783 30.460  43.303  1.00 74.77  ? 153 LYS B C   1 
ATOM   5376  O O   . LYS B 1 153 ? -35.455 29.447  43.533  1.00 76.51  ? 153 LYS B O   1 
ATOM   5377  C CB  . LYS B 1 153 ? -35.371 32.808  43.987  1.00 73.31  ? 153 LYS B CB  1 
ATOM   5378  C CG  . LYS B 1 153 ? -36.894 32.705  44.080  1.00 82.54  ? 153 LYS B CG  1 
ATOM   5379  C CD  . LYS B 1 153 ? -37.537 34.074  44.328  1.00 84.90  ? 153 LYS B CD  1 
ATOM   5380  C CE  . LYS B 1 153 ? -38.191 34.628  43.061  1.00 77.21  ? 153 LYS B CE  1 
ATOM   5381  N NZ  . LYS B 1 153 ? -39.265 35.633  43.319  1.00 59.74  ? 153 LYS B NZ  1 
ATOM   5382  N N   . GLY B 1 154 ? -34.185 30.666  42.127  1.00 72.01  ? 154 GLY B N   1 
ATOM   5383  C CA  . GLY B 1 154 ? -34.200 29.692  41.057  1.00 64.27  ? 154 GLY B CA  1 
ATOM   5384  C C   . GLY B 1 154 ? -35.448 29.665  40.199  1.00 72.51  ? 154 GLY B C   1 
ATOM   5385  O O   . GLY B 1 154 ? -35.441 28.994  39.158  1.00 81.27  ? 154 GLY B O   1 
ATOM   5386  N N   . ARG B 1 155 ? -36.510 30.374  40.580  1.00 68.95  ? 155 ARG B N   1 
ATOM   5387  C CA  . ARG B 1 155 ? -37.795 30.237  39.900  1.00 73.45  ? 155 ARG B CA  1 
ATOM   5388  C C   . ARG B 1 155 ? -38.749 31.325  40.375  1.00 76.16  ? 155 ARG B C   1 
ATOM   5389  O O   . ARG B 1 155 ? -38.459 32.066  41.319  1.00 73.24  ? 155 ARG B O   1 
ATOM   5390  C CB  . ARG B 1 155 ? -38.409 28.863  40.159  1.00 76.81  ? 155 ARG B CB  1 
ATOM   5391  C CG  . ARG B 1 155 ? -38.423 28.477  41.624  1.00 66.95  ? 155 ARG B CG  1 
ATOM   5392  C CD  . ARG B 1 155 ? -38.457 26.978  41.784  1.00 69.48  ? 155 ARG B CD  1 
ATOM   5393  N NE  . ARG B 1 155 ? -39.375 26.349  40.842  1.00 76.41  ? 155 ARG B NE  1 
ATOM   5394  C CZ  . ARG B 1 155 ? -39.024 25.417  39.970  1.00 79.65  ? 155 ARG B CZ  1 
ATOM   5395  N NH1 . ARG B 1 155 ? -37.777 24.980  39.889  1.00 73.84  ? 155 ARG B NH1 1 
ATOM   5396  N NH2 . ARG B 1 155 ? -39.947 24.903  39.164  1.00 86.05  ? 155 ARG B NH2 1 
ATOM   5397  N N   . ASN B 1 156 ? -39.912 31.385  39.714  1.00 64.09  ? 156 ASN B N   1 
ATOM   5398  C CA  . ASN B 1 156 ? -41.011 32.277  40.083  1.00 65.15  ? 156 ASN B CA  1 
ATOM   5399  C C   . ASN B 1 156 ? -40.552 33.732  40.167  1.00 69.41  ? 156 ASN B C   1 
ATOM   5400  O O   . ASN B 1 156 ? -40.798 34.432  41.150  1.00 70.50  ? 156 ASN B O   1 
ATOM   5401  C CB  . ASN B 1 156 ? -41.662 31.827  41.392  1.00 67.96  ? 156 ASN B CB  1 
ATOM   5402  C CG  . ASN B 1 156 ? -41.739 30.321  41.509  1.00 73.52  ? 156 ASN B CG  1 
ATOM   5403  O OD1 . ASN B 1 156 ? -41.141 29.723  42.402  1.00 81.41  ? 156 ASN B OD1 1 
ATOM   5404  N ND2 . ASN B 1 156 ? -42.459 29.695  40.585  1.00 71.43  ? 156 ASN B ND2 1 
ATOM   5405  N N   . TYR B 1 157 ? -39.888 34.193  39.114  1.00 70.31  ? 157 TYR B N   1 
ATOM   5406  C CA  . TYR B 1 157 ? -39.476 35.584  39.084  1.00 67.61  ? 157 TYR B CA  1 
ATOM   5407  C C   . TYR B 1 157 ? -40.637 36.468  38.643  1.00 66.65  ? 157 TYR B C   1 
ATOM   5408  O O   . TYR B 1 157 ? -41.597 36.015  38.016  1.00 73.58  ? 157 TYR B O   1 
ATOM   5409  C CB  . TYR B 1 157 ? -38.270 35.768  38.164  1.00 61.08  ? 157 TYR B CB  1 
ATOM   5410  C CG  . TYR B 1 157 ? -37.038 35.057  38.674  1.00 64.58  ? 157 TYR B CG  1 
ATOM   5411  C CD1 . TYR B 1 157 ? -36.360 35.520  39.794  1.00 63.43  ? 157 TYR B CD1 1 
ATOM   5412  C CD2 . TYR B 1 157 ? -36.559 33.916  38.042  1.00 60.79  ? 157 TYR B CD2 1 
ATOM   5413  C CE1 . TYR B 1 157 ? -35.238 34.870  40.269  1.00 65.86  ? 157 TYR B CE1 1 
ATOM   5414  C CE2 . TYR B 1 157 ? -35.439 33.258  38.510  1.00 68.23  ? 157 TYR B CE2 1 
ATOM   5415  C CZ  . TYR B 1 157 ? -34.780 33.741  39.624  1.00 71.95  ? 157 TYR B CZ  1 
ATOM   5416  O OH  . TYR B 1 157 ? -33.659 33.099  40.104  1.00 71.42  ? 157 TYR B OH  1 
ATOM   5417  N N   . THR B 1 158 ? -40.548 37.740  39.001  1.00 62.00  ? 158 THR B N   1 
ATOM   5418  C CA  . THR B 1 158 ? -41.531 38.736  38.621  1.00 54.36  ? 158 THR B CA  1 
ATOM   5419  C C   . THR B 1 158 ? -40.911 39.715  37.638  1.00 62.94  ? 158 THR B C   1 
ATOM   5420  O O   . THR B 1 158 ? -39.691 39.759  37.445  1.00 60.53  ? 158 THR B O   1 
ATOM   5421  C CB  . THR B 1 158 ? -42.054 39.484  39.849  1.00 61.23  ? 158 THR B CB  1 
ATOM   5422  O OG1 . THR B 1 158 ? -41.224 40.626  40.108  1.00 64.22  ? 158 THR B OG1 1 
ATOM   5423  C CG2 . THR B 1 158 ? -42.030 38.577  41.050  1.00 59.98  ? 158 THR B CG2 1 
ATOM   5424  N N   . GLN B 1 159 ? -41.782 40.510  37.013  1.00 62.24  ? 159 GLN B N   1 
ATOM   5425  C CA  . GLN B 1 159 ? -41.302 41.505  36.065  1.00 57.00  ? 159 GLN B CA  1 
ATOM   5426  C C   . GLN B 1 159 ? -40.419 42.535  36.758  1.00 56.98  ? 159 GLN B C   1 
ATOM   5427  O O   . GLN B 1 159 ? -39.354 42.890  36.243  1.00 62.35  ? 159 GLN B O   1 
ATOM   5428  C CB  . GLN B 1 159 ? -42.481 42.166  35.354  1.00 52.43  ? 159 GLN B CB  1 
ATOM   5429  C CG  . GLN B 1 159 ? -42.059 43.263  34.415  1.00 51.76  ? 159 GLN B CG  1 
ATOM   5430  C CD  . GLN B 1 159 ? -41.604 42.722  33.071  1.00 53.35  ? 159 GLN B CD  1 
ATOM   5431  O OE1 . GLN B 1 159 ? -41.531 41.510  32.869  1.00 53.12  ? 159 GLN B OE1 1 
ATOM   5432  N NE2 . GLN B 1 159 ? -41.292 43.621  32.147  1.00 53.63  ? 159 GLN B NE2 1 
ATOM   5433  N N   . GLU B 1 160 ? -40.814 42.986  37.950  1.00 54.41  ? 160 GLU B N   1 
ATOM   5434  C CA  . GLU B 1 160 ? -40.008 43.971  38.666  1.00 64.87  ? 160 GLU B CA  1 
ATOM   5435  C C   . GLU B 1 160 ? -38.619 43.425  38.999  1.00 65.63  ? 160 GLU B C   1 
ATOM   5436  O O   . GLU B 1 160 ? -37.618 44.143  38.889  1.00 57.66  ? 160 GLU B O   1 
ATOM   5437  C CB  . GLU B 1 160 ? -40.740 44.416  39.931  1.00 58.02  ? 160 GLU B CB  1 
ATOM   5438  C CG  . GLU B 1 160 ? -41.965 45.264  39.648  1.00 70.47  ? 160 GLU B CG  1 
ATOM   5439  C CD  . GLU B 1 160 ? -43.259 44.460  39.647  1.00 86.08  ? 160 GLU B CD  1 
ATOM   5440  O OE1 . GLU B 1 160 ? -43.276 43.326  39.117  1.00 86.16  ? 160 GLU B OE1 1 
ATOM   5441  O OE2 . GLU B 1 160 ? -44.265 44.969  40.184  1.00 96.53  ? 160 GLU B OE2 1 
ATOM   5442  N N   . GLU B 1 161 ? -38.537 42.151  39.396  1.00 64.57  ? 161 GLU B N   1 
ATOM   5443  C CA  . GLU B 1 161 ? -37.243 41.544  39.700  1.00 58.28  ? 161 GLU B CA  1 
ATOM   5444  C C   . GLU B 1 161 ? -36.349 41.523  38.467  1.00 56.90  ? 161 GLU B C   1 
ATOM   5445  O O   . GLU B 1 161 ? -35.161 41.862  38.538  1.00 53.70  ? 161 GLU B O   1 
ATOM   5446  C CB  . GLU B 1 161 ? -37.447 40.128  40.244  1.00 54.15  ? 161 GLU B CB  1 
ATOM   5447  C CG  . GLU B 1 161 ? -38.086 40.097  41.629  1.00 64.45  ? 161 GLU B CG  1 
ATOM   5448  C CD  . GLU B 1 161 ? -38.515 38.703  42.075  1.00 71.15  ? 161 GLU B CD  1 
ATOM   5449  O OE1 . GLU B 1 161 ? -38.668 37.806  41.220  1.00 70.31  ? 161 GLU B OE1 1 
ATOM   5450  O OE2 . GLU B 1 161 ? -38.708 38.504  43.290  1.00 72.50  ? 161 GLU B OE2 1 
ATOM   5451  N N   . LYS B 1 162 ? -36.914 41.136  37.323  1.00 55.36  ? 162 LYS B N   1 
ATOM   5452  C CA  . LYS B 1 162 ? -36.142 41.099  36.086  1.00 60.25  ? 162 LYS B CA  1 
ATOM   5453  C C   . LYS B 1 162 ? -35.649 42.489  35.693  1.00 55.30  ? 162 LYS B C   1 
ATOM   5454  O O   . LYS B 1 162 ? -34.527 42.642  35.196  1.00 51.59  ? 162 LYS B O   1 
ATOM   5455  C CB  . LYS B 1 162 ? -36.991 40.496  34.969  1.00 63.67  ? 162 LYS B CB  1 
ATOM   5456  C CG  . LYS B 1 162 ? -36.341 40.557  33.609  1.00 60.53  ? 162 LYS B CG  1 
ATOM   5457  C CD  . LYS B 1 162 ? -37.274 40.026  32.540  1.00 57.80  ? 162 LYS B CD  1 
ATOM   5458  C CE  . LYS B 1 162 ? -38.657 40.647  32.653  1.00 61.38  ? 162 LYS B CE  1 
ATOM   5459  N NZ  . LYS B 1 162 ? -39.515 40.464  31.436  1.00 56.49  ? 162 LYS B NZ  1 
ATOM   5460  N N   . GLU B 1 163 ? -36.477 43.516  35.906  1.00 58.03  ? 163 GLU B N   1 
ATOM   5461  C CA  . GLU B 1 163 ? -36.056 44.880  35.602  1.00 57.96  ? 163 GLU B CA  1 
ATOM   5462  C C   . GLU B 1 163 ? -35.043 45.390  36.619  1.00 55.12  ? 163 GLU B C   1 
ATOM   5463  O O   . GLU B 1 163 ? -34.279 46.316  36.321  1.00 61.33  ? 163 GLU B O   1 
ATOM   5464  C CB  . GLU B 1 163 ? -37.281 45.793  35.540  1.00 58.99  ? 163 GLU B CB  1 
ATOM   5465  C CG  . GLU B 1 163 ? -38.233 45.464  34.388  1.00 64.09  ? 163 GLU B CG  1 
ATOM   5466  C CD  . GLU B 1 163 ? -39.590 46.148  34.513  1.00 72.67  ? 163 GLU B CD  1 
ATOM   5467  O OE1 . GLU B 1 163 ? -39.889 46.703  35.593  1.00 73.14  ? 163 GLU B OE1 1 
ATOM   5468  O OE2 . GLU B 1 163 ? -40.363 46.123  33.530  1.00 69.95  ? 163 GLU B OE2 1 
ATOM   5469  N N   . TYR B 1 164 ? -35.028 44.809  37.823  1.00 51.52  ? 164 TYR B N   1 
ATOM   5470  C CA  . TYR B 1 164 ? -33.983 45.130  38.791  1.00 52.79  ? 164 TYR B CA  1 
ATOM   5471  C C   . TYR B 1 164 ? -32.652 44.533  38.353  1.00 58.66  ? 164 TYR B C   1 
ATOM   5472  O O   . TYR B 1 164 ? -31.612 45.203  38.386  1.00 52.89  ? 164 TYR B O   1 
ATOM   5473  C CB  . TYR B 1 164 ? -34.380 44.621  40.180  1.00 54.01  ? 164 TYR B CB  1 
ATOM   5474  C CG  . TYR B 1 164 ? -33.285 44.728  41.219  1.00 56.79  ? 164 TYR B CG  1 
ATOM   5475  C CD1 . TYR B 1 164 ? -32.944 45.955  41.777  1.00 61.33  ? 164 TYR B CD1 1 
ATOM   5476  C CD2 . TYR B 1 164 ? -32.591 43.602  41.643  1.00 54.60  ? 164 TYR B CD2 1 
ATOM   5477  C CE1 . TYR B 1 164 ? -31.940 46.056  42.727  1.00 69.24  ? 164 TYR B CE1 1 
ATOM   5478  C CE2 . TYR B 1 164 ? -31.585 43.694  42.596  1.00 63.31  ? 164 TYR B CE2 1 
ATOM   5479  C CZ  . TYR B 1 164 ? -31.262 44.924  43.134  1.00 69.90  ? 164 TYR B CZ  1 
ATOM   5480  O OH  . TYR B 1 164 ? -30.261 45.026  44.078  1.00 70.39  ? 164 TYR B OH  1 
ATOM   5481  N N   . VAL B 1 165 ? -32.679 43.274  37.917  1.00 58.85  ? 165 VAL B N   1 
ATOM   5482  C CA  . VAL B 1 165 ? -31.482 42.606  37.415  1.00 50.49  ? 165 VAL B CA  1 
ATOM   5483  C C   . VAL B 1 165 ? -30.912 43.357  36.222  1.00 53.35  ? 165 VAL B C   1 
ATOM   5484  O O   . VAL B 1 165 ? -29.695 43.546  36.104  1.00 54.72  ? 165 VAL B O   1 
ATOM   5485  C CB  . VAL B 1 165 ? -31.814 41.152  37.049  1.00 50.54  ? 165 VAL B CB  1 
ATOM   5486  C CG1 . VAL B 1 165 ? -30.666 40.525  36.274  1.00 58.44  ? 165 VAL B CG1 1 
ATOM   5487  C CG2 . VAL B 1 165 ? -32.130 40.371  38.297  1.00 58.68  ? 165 VAL B CG2 1 
ATOM   5488  N N   . LEU B 1 166 ? -31.785 43.780  35.309  1.00 55.66  ? 166 LEU B N   1 
ATOM   5489  C CA  . LEU B 1 166 ? -31.327 44.508  34.134  1.00 61.33  ? 166 LEU B CA  1 
ATOM   5490  C C   . LEU B 1 166 ? -30.774 45.871  34.505  1.00 62.55  ? 166 LEU B C   1 
ATOM   5491  O O   . LEU B 1 166 ? -29.820 46.344  33.876  1.00 62.96  ? 166 LEU B O   1 
ATOM   5492  C CB  . LEU B 1 166 ? -32.468 44.666  33.132  1.00 61.87  ? 166 LEU B CB  1 
ATOM   5493  C CG  . LEU B 1 166 ? -32.679 43.473  32.206  1.00 62.08  ? 166 LEU B CG  1 
ATOM   5494  C CD1 . LEU B 1 166 ? -34.089 43.482  31.611  1.00 59.14  ? 166 LEU B CD1 1 
ATOM   5495  C CD2 . LEU B 1 166 ? -31.594 43.421  31.126  1.00 60.11  ? 166 LEU B CD2 1 
ATOM   5496  N N   . ASN B 1 167 ? -31.360 46.522  35.509  1.00 57.26  ? 167 ASN B N   1 
ATOM   5497  C CA  . ASN B 1 167 ? -30.850 47.822  35.917  1.00 65.13  ? 167 ASN B CA  1 
ATOM   5498  C C   . ASN B 1 167 ? -29.407 47.716  36.393  1.00 67.24  ? 167 ASN B C   1 
ATOM   5499  O O   . ASN B 1 167 ? -28.563 48.545  36.034  1.00 69.00  ? 167 ASN B O   1 
ATOM   5500  C CB  . ASN B 1 167 ? -31.733 48.410  37.009  1.00 65.86  ? 167 ASN B CB  1 
ATOM   5501  C CG  . ASN B 1 167 ? -31.961 49.886  36.821  1.00 88.55  ? 167 ASN B CG  1 
ATOM   5502  O OD1 . ASN B 1 167 ? -32.782 50.297  35.998  1.00 88.98  ? 167 ASN B OD1 1 
ATOM   5503  N ND2 . ASN B 1 167 ? -31.219 50.698  37.567  1.00 81.51  ? 167 ASN B ND2 1 
ATOM   5504  N N   . LYS B 1 168 ? -29.104 46.689  37.188  1.00 60.68  ? 168 LYS B N   1 
ATOM   5505  C CA  . LYS B 1 168 ? -27.752 46.531  37.706  1.00 61.84  ? 168 LYS B CA  1 
ATOM   5506  C C   . LYS B 1 168 ? -26.789 46.113  36.605  1.00 63.43  ? 168 LYS B C   1 
ATOM   5507  O O   . LYS B 1 168 ? -25.613 46.499  36.620  1.00 57.56  ? 168 LYS B O   1 
ATOM   5508  C CB  . LYS B 1 168 ? -27.739 45.516  38.847  1.00 58.91  ? 168 LYS B CB  1 
ATOM   5509  C CG  . LYS B 1 168 ? -28.855 45.695  39.845  1.00 66.20  ? 168 LYS B CG  1 
ATOM   5510  C CD  . LYS B 1 168 ? -28.615 46.901  40.737  1.00 69.62  ? 168 LYS B CD  1 
ATOM   5511  C CE  . LYS B 1 168 ? -27.469 46.660  41.703  1.00 60.78  ? 168 LYS B CE  1 
ATOM   5512  N NZ  . LYS B 1 168 ? -27.596 47.543  42.897  1.00 80.29  ? 168 LYS B NZ  1 
ATOM   5513  N N   . TYR B 1 169 ? -27.263 45.305  35.654  1.00 57.97  ? 169 TYR B N   1 
ATOM   5514  C CA  . TYR B 1 169 ? -26.412 44.895  34.545  1.00 50.44  ? 169 TYR B CA  1 
ATOM   5515  C C   . TYR B 1 169 ? -25.936 46.104  33.754  1.00 57.86  ? 169 TYR B C   1 
ATOM   5516  O O   . TYR B 1 169 ? -24.788 46.147  33.289  1.00 59.67  ? 169 TYR B O   1 
ATOM   5517  C CB  . TYR B 1 169 ? -27.166 43.927  33.636  1.00 54.34  ? 169 TYR B CB  1 
ATOM   5518  C CG  . TYR B 1 169 ? -27.112 42.481  34.077  1.00 52.43  ? 169 TYR B CG  1 
ATOM   5519  C CD1 . TYR B 1 169 ? -26.828 42.139  35.392  1.00 45.74  ? 169 TYR B CD1 1 
ATOM   5520  C CD2 . TYR B 1 169 ? -27.363 41.455  33.174  1.00 54.77  ? 169 TYR B CD2 1 
ATOM   5521  C CE1 . TYR B 1 169 ? -26.788 40.808  35.792  1.00 49.91  ? 169 TYR B CE1 1 
ATOM   5522  C CE2 . TYR B 1 169 ? -27.324 40.127  33.564  1.00 52.58  ? 169 TYR B CE2 1 
ATOM   5523  C CZ  . TYR B 1 169 ? -27.037 39.805  34.872  1.00 49.58  ? 169 TYR B CZ  1 
ATOM   5524  O OH  . TYR B 1 169 ? -26.999 38.478  35.257  1.00 47.01  ? 169 TYR B OH  1 
ATOM   5525  N N   . PHE B 1 170 ? -26.802 47.103  33.599  1.00 55.12  ? 170 PHE B N   1 
ATOM   5526  C CA  . PHE B 1 170 ? -26.381 48.319  32.922  1.00 57.11  ? 170 PHE B CA  1 
ATOM   5527  C C   . PHE B 1 170 ? -25.511 49.176  33.822  1.00 59.95  ? 170 PHE B C   1 
ATOM   5528  O O   . PHE B 1 170 ? -24.663 49.927  33.326  1.00 66.54  ? 170 PHE B O   1 
ATOM   5529  C CB  . PHE B 1 170 ? -27.597 49.105  32.441  1.00 64.30  ? 170 PHE B CB  1 
ATOM   5530  C CG  . PHE B 1 170 ? -28.133 48.634  31.122  1.00 66.04  ? 170 PHE B CG  1 
ATOM   5531  C CD1 . PHE B 1 170 ? -27.430 48.872  29.948  1.00 64.50  ? 170 PHE B CD1 1 
ATOM   5532  C CD2 . PHE B 1 170 ? -29.335 47.950  31.052  1.00 70.09  ? 170 PHE B CD2 1 
ATOM   5533  C CE1 . PHE B 1 170 ? -27.921 48.441  28.728  1.00 64.60  ? 170 PHE B CE1 1 
ATOM   5534  C CE2 . PHE B 1 170 ? -29.834 47.515  29.834  1.00 63.81  ? 170 PHE B CE2 1 
ATOM   5535  C CZ  . PHE B 1 170 ? -29.127 47.761  28.672  1.00 63.85  ? 170 PHE B CZ  1 
ATOM   5536  N N   . GLU B 1 171 ? -25.698 49.073  35.141  1.00 59.47  ? 171 GLU B N   1 
ATOM   5537  C CA  . GLU B 1 171 ? -24.789 49.736  36.070  1.00 60.67  ? 171 GLU B CA  1 
ATOM   5538  C C   . GLU B 1 171 ? -23.361 49.241  35.903  1.00 58.20  ? 171 GLU B C   1 
ATOM   5539  O O   . GLU B 1 171 ? -22.412 50.016  36.063  1.00 65.42  ? 171 GLU B O   1 
ATOM   5540  C CB  . GLU B 1 171 ? -25.245 49.524  37.514  1.00 57.31  ? 171 GLU B CB  1 
ATOM   5541  C CG  . GLU B 1 171 ? -26.108 50.642  38.071  1.00 65.21  ? 171 GLU B CG  1 
ATOM   5542  C CD  . GLU B 1 171 ? -25.761 52.022  37.509  1.00 84.02  ? 171 GLU B CD  1 
ATOM   5543  O OE1 . GLU B 1 171 ? -24.569 52.412  37.480  1.00 81.99  ? 171 GLU B OE1 1 
ATOM   5544  O OE2 . GLU B 1 171 ? -26.701 52.728  37.087  1.00 101.10 ? 171 GLU B OE2 1 
ATOM   5545  N N   . ILE B 1 172 ? -23.192 47.956  35.590  1.00 51.29  ? 172 ILE B N   1 
ATOM   5546  C CA  . ILE B 1 172 ? -21.865 47.414  35.323  1.00 52.53  ? 172 ILE B CA  1 
ATOM   5547  C C   . ILE B 1 172 ? -21.309 47.974  34.020  1.00 53.24  ? 172 ILE B C   1 
ATOM   5548  O O   . ILE B 1 172 ? -20.130 48.341  33.939  1.00 49.69  ? 172 ILE B O   1 
ATOM   5549  C CB  . ILE B 1 172 ? -21.930 45.877  35.303  1.00 51.40  ? 172 ILE B CB  1 
ATOM   5550  C CG1 . ILE B 1 172 ? -22.325 45.353  36.682  1.00 48.98  ? 172 ILE B CG1 1 
ATOM   5551  C CG2 . ILE B 1 172 ? -20.612 45.290  34.868  1.00 49.94  ? 172 ILE B CG2 1 
ATOM   5552  C CD1 . ILE B 1 172 ? -21.547 45.989  37.811  1.00 46.41  ? 172 ILE B CD1 1 
ATOM   5553  N N   . ILE B 1 173 ? -22.152 48.065  32.988  1.00 54.70  ? 173 ILE B N   1 
ATOM   5554  C CA  . ILE B 1 173 ? -21.686 48.485  31.668  1.00 52.56  ? 173 ILE B CA  1 
ATOM   5555  C C   . ILE B 1 173 ? -21.246 49.941  31.689  1.00 52.33  ? 173 ILE B C   1 
ATOM   5556  O O   . ILE B 1 173 ? -20.266 50.322  31.037  1.00 49.97  ? 173 ILE B O   1 
ATOM   5557  C CB  . ILE B 1 173 ? -22.786 48.245  30.623  1.00 53.35  ? 173 ILE B CB  1 
ATOM   5558  C CG1 . ILE B 1 173 ? -22.936 46.749  30.367  1.00 43.75  ? 173 ILE B CG1 1 
ATOM   5559  C CG2 . ILE B 1 173 ? -22.487 49.024  29.343  1.00 53.54  ? 173 ILE B CG2 1 
ATOM   5560  C CD1 . ILE B 1 173 ? -23.621 46.432  29.079  1.00 50.48  ? 173 ILE B CD1 1 
ATOM   5561  N N   . LYS B 1 174 ? -21.962 50.780  32.436  1.00 54.33  ? 174 LYS B N   1 
ATOM   5562  C CA  . LYS B 1 174 ? -21.581 52.181  32.536  1.00 56.73  ? 174 LYS B CA  1 
ATOM   5563  C C   . LYS B 1 174 ? -20.312 52.387  33.355  1.00 56.93  ? 174 LYS B C   1 
ATOM   5564  O O   . LYS B 1 174 ? -19.729 53.474  33.294  1.00 64.33  ? 174 LYS B O   1 
ATOM   5565  C CB  . LYS B 1 174 ? -22.721 52.995  33.139  1.00 65.28  ? 174 LYS B CB  1 
ATOM   5566  C CG  . LYS B 1 174 ? -24.019 52.885  32.358  1.00 64.59  ? 174 LYS B CG  1 
ATOM   5567  C CD  . LYS B 1 174 ? -24.967 54.030  32.677  1.00 70.83  ? 174 LYS B CD  1 
ATOM   5568  C CE  . LYS B 1 174 ? -26.000 53.640  33.724  1.00 69.50  ? 174 LYS B CE  1 
ATOM   5569  N NZ  . LYS B 1 174 ? -25.474 53.814  35.105  1.00 75.40  ? 174 LYS B NZ  1 
ATOM   5570  N N   . LYS B 1 175 ? -19.870 51.382  34.112  1.00 52.62  ? 175 LYS B N   1 
ATOM   5571  C CA  . LYS B 1 175 ? -18.633 51.475  34.882  1.00 66.02  ? 175 LYS B CA  1 
ATOM   5572  C C   . LYS B 1 175 ? -17.508 50.640  34.286  1.00 63.41  ? 175 LYS B C   1 
ATOM   5573  O O   . LYS B 1 175 ? -16.421 50.573  34.873  1.00 55.25  ? 175 LYS B O   1 
ATOM   5574  C CB  . LYS B 1 175 ? -18.876 51.052  36.337  1.00 59.27  ? 175 LYS B CB  1 
ATOM   5575  C CG  . LYS B 1 175 ? -19.852 51.944  37.089  1.00 64.15  ? 175 LYS B CG  1 
ATOM   5576  C CD  . LYS B 1 175 ? -19.770 51.759  38.608  1.00 75.07  ? 175 LYS B CD  1 
ATOM   5577  C CE  . LYS B 1 175 ? -19.954 50.293  39.019  1.00 72.44  ? 175 LYS B CE  1 
ATOM   5578  N NZ  . LYS B 1 175 ? -19.721 50.026  40.479  1.00 72.02  ? 175 LYS B NZ  1 
ATOM   5579  N N   . THR B 1 176 ? -17.744 50.005  33.138  1.00 53.64  ? 176 THR B N   1 
ATOM   5580  C CA  . THR B 1 176 ? -16.753 49.099  32.573  1.00 55.59  ? 176 THR B CA  1 
ATOM   5581  C C   . THR B 1 176 ? -15.502 49.850  32.138  1.00 59.64  ? 176 THR B C   1 
ATOM   5582  O O   . THR B 1 176 ? -14.395 49.548  32.594  1.00 56.92  ? 176 THR B O   1 
ATOM   5583  C CB  . THR B 1 176 ? -17.365 48.327  31.405  1.00 51.48  ? 176 THR B CB  1 
ATOM   5584  O OG1 . THR B 1 176 ? -18.291 47.364  31.923  1.00 56.41  ? 176 THR B OG1 1 
ATOM   5585  C CG2 . THR B 1 176 ? -16.284 47.611  30.605  1.00 46.24  ? 176 THR B CG2 1 
ATOM   5586  N N   . LEU B 1 177 ? -15.660 50.844  31.261  1.00 55.92  ? 177 LEU B N   1 
ATOM   5587  C CA  . LEU B 1 177 ? -14.493 51.557  30.752  1.00 52.25  ? 177 LEU B CA  1 
ATOM   5588  C C   . LEU B 1 177 ? -13.722 52.253  31.868  1.00 53.46  ? 177 LEU B C   1 
ATOM   5589  O O   . LEU B 1 177 ? -12.499 52.401  31.773  1.00 58.27  ? 177 LEU B O   1 
ATOM   5590  C CB  . LEU B 1 177 ? -14.918 52.562  29.685  1.00 50.06  ? 177 LEU B CB  1 
ATOM   5591  C CG  . LEU B 1 177 ? -15.397 51.908  28.384  1.00 57.21  ? 177 LEU B CG  1 
ATOM   5592  C CD1 . LEU B 1 177 ? -15.708 52.953  27.312  1.00 50.02  ? 177 LEU B CD1 1 
ATOM   5593  C CD2 . LEU B 1 177 ? -14.395 50.862  27.865  1.00 51.83  ? 177 LEU B CD2 1 
ATOM   5594  N N   . SER B 1 178 ? -14.408 52.663  32.940  1.00 58.30  ? 178 SER B N   1 
ATOM   5595  C CA  . SER B 1 178 ? -13.720 53.354  34.028  1.00 61.78  ? 178 SER B CA  1 
ATOM   5596  C C   . SER B 1 178 ? -12.785 52.419  34.781  1.00 55.16  ? 178 SER B C   1 
ATOM   5597  O O   . SER B 1 178 ? -11.710 52.837  35.222  1.00 56.11  ? 178 SER B O   1 
ATOM   5598  C CB  . SER B 1 178 ? -14.731 53.980  34.988  1.00 59.78  ? 178 SER B CB  1 
ATOM   5599  O OG  . SER B 1 178 ? -14.957 55.344  34.670  1.00 71.82  ? 178 SER B OG  1 
ATOM   5600  N N   . ILE B 1 179 ? -13.172 51.151  34.934  1.00 51.42  ? 179 ILE B N   1 
ATOM   5601  C CA  . ILE B 1 179 ? -12.323 50.203  35.644  1.00 51.91  ? 179 ILE B CA  1 
ATOM   5602  C C   . ILE B 1 179 ? -11.033 49.957  34.871  1.00 56.14  ? 179 ILE B C   1 
ATOM   5603  O O   . ILE B 1 179 ? -9.989  49.661  35.466  1.00 55.71  ? 179 ILE B O   1 
ATOM   5604  C CB  . ILE B 1 179 ? -13.094 48.896  35.918  1.00 50.35  ? 179 ILE B CB  1 
ATOM   5605  C CG1 . ILE B 1 179 ? -12.675 48.279  37.254  1.00 58.66  ? 179 ILE B CG1 1 
ATOM   5606  C CG2 . ILE B 1 179 ? -12.839 47.894  34.828  1.00 52.44  ? 179 ILE B CG2 1 
ATOM   5607  C CD1 . ILE B 1 179 ? -13.019 49.103  38.466  1.00 68.20  ? 179 ILE B CD1 1 
ATOM   5608  N N   . TYR B 1 180 ? -11.067 50.105  33.545  1.00 52.84  ? 180 TYR B N   1 
ATOM   5609  C CA  . TYR B 1 180 ? -9.853  49.933  32.755  1.00 53.82  ? 180 TYR B CA  1 
ATOM   5610  C C   . TYR B 1 180 ? -8.940  51.148  32.869  1.00 53.45  ? 180 TYR B C   1 
ATOM   5611  O O   . TYR B 1 180 ? -7.712  51.002  32.917  1.00 46.87  ? 180 TYR B O   1 
ATOM   5612  C CB  . TYR B 1 180 ? -10.211 49.666  31.296  1.00 51.87  ? 180 TYR B CB  1 
ATOM   5613  C CG  . TYR B 1 180 ? -10.775 48.286  31.048  1.00 52.26  ? 180 TYR B CG  1 
ATOM   5614  C CD1 . TYR B 1 180 ? -9.944  47.175  30.968  1.00 47.08  ? 180 TYR B CD1 1 
ATOM   5615  C CD2 . TYR B 1 180 ? -12.142 48.093  30.890  1.00 48.73  ? 180 TYR B CD2 1 
ATOM   5616  C CE1 . TYR B 1 180 ? -10.457 45.909  30.732  1.00 42.57  ? 180 TYR B CE1 1 
ATOM   5617  C CE2 . TYR B 1 180 ? -12.665 46.830  30.655  1.00 48.50  ? 180 TYR B CE2 1 
ATOM   5618  C CZ  . TYR B 1 180 ? -11.819 45.740  30.577  1.00 50.34  ? 180 TYR B CZ  1 
ATOM   5619  O OH  . TYR B 1 180 ? -12.328 44.478  30.346  1.00 46.97  ? 180 TYR B OH  1 
ATOM   5620  N N   . ARG B 1 181 ? -9.516  52.355  32.916  1.00 54.85  ? 181 ARG B N   1 
ATOM   5621  C CA  . ARG B 1 181 ? -8.712  53.532  33.232  1.00 61.19  ? 181 ARG B CA  1 
ATOM   5622  C C   . ARG B 1 181 ? -8.096  53.412  34.618  1.00 61.81  ? 181 ARG B C   1 
ATOM   5623  O O   . ARG B 1 181 ? -6.917  53.731  34.812  1.00 66.58  ? 181 ARG B O   1 
ATOM   5624  C CB  . ARG B 1 181 ? -9.550  54.808  33.152  1.00 53.70  ? 181 ARG B CB  1 
ATOM   5625  C CG  . ARG B 1 181 ? -9.911  55.255  31.760  1.00 62.42  ? 181 ARG B CG  1 
ATOM   5626  C CD  . ARG B 1 181 ? -10.760 56.506  31.833  1.00 68.50  ? 181 ARG B CD  1 
ATOM   5627  N NE  . ARG B 1 181 ? -11.774 56.563  30.782  1.00 72.27  ? 181 ARG B NE  1 
ATOM   5628  C CZ  . ARG B 1 181 ? -13.069 56.750  31.006  1.00 72.83  ? 181 ARG B CZ  1 
ATOM   5629  N NH1 . ARG B 1 181 ? -13.544 56.884  32.233  1.00 73.11  ? 181 ARG B NH1 1 
ATOM   5630  N NH2 . ARG B 1 181 ? -13.908 56.813  29.973  1.00 68.65  ? 181 ARG B NH2 1 
ATOM   5631  N N   . GLU B 1 182 ? -8.875  52.936  35.593  1.00 52.15  ? 182 GLU B N   1 
ATOM   5632  C CA  . GLU B 1 182 ? -8.404  52.929  36.974  1.00 62.39  ? 182 GLU B CA  1 
ATOM   5633  C C   . GLU B 1 182 ? -7.212  51.989  37.162  1.00 63.96  ? 182 GLU B C   1 
ATOM   5634  O O   . GLU B 1 182 ? -6.244  52.346  37.841  1.00 59.23  ? 182 GLU B O   1 
ATOM   5635  C CB  . GLU B 1 182 ? -9.555  52.565  37.913  1.00 54.79  ? 182 GLU B CB  1 
ATOM   5636  C CG  . GLU B 1 182 ? -9.147  52.324  39.352  1.00 65.73  ? 182 GLU B CG  1 
ATOM   5637  C CD  . GLU B 1 182 ? -10.335 51.957  40.224  1.00 82.16  ? 182 GLU B CD  1 
ATOM   5638  O OE1 . GLU B 1 182 ? -11.477 51.981  39.710  1.00 63.56  ? 182 GLU B OE1 1 
ATOM   5639  O OE2 . GLU B 1 182 ? -10.127 51.654  41.420  1.00 76.14  ? 182 GLU B OE2 1 
ATOM   5640  N N   . ILE B 1 183 ? -7.244  50.795  36.562  1.00 57.43  ? 183 ILE B N   1 
ATOM   5641  C CA  . ILE B 1 183 ? -6.108  49.891  36.741  1.00 53.40  ? 183 ILE B CA  1 
ATOM   5642  C C   . ILE B 1 183 ? -4.890  50.388  35.977  1.00 57.48  ? 183 ILE B C   1 
ATOM   5643  O O   . ILE B 1 183 ? -3.746  50.114  36.370  1.00 57.35  ? 183 ILE B O   1 
ATOM   5644  C CB  . ILE B 1 183 ? -6.463  48.452  36.333  1.00 51.89  ? 183 ILE B CB  1 
ATOM   5645  C CG1 . ILE B 1 183 ? -6.414  48.307  34.807  1.00 56.73  ? 183 ILE B CG1 1 
ATOM   5646  C CG2 . ILE B 1 183 ? -7.798  48.058  36.923  1.00 58.74  ? 183 ILE B CG2 1 
ATOM   5647  C CD1 . ILE B 1 183 ? -6.160  46.908  34.316  1.00 54.79  ? 183 ILE B CD1 1 
ATOM   5648  N N   . LYS B 1 184 ? -5.099  51.121  34.884  1.00 57.78  ? 184 LYS B N   1 
ATOM   5649  C CA  . LYS B 1 184 ? -3.967  51.699  34.172  1.00 56.87  ? 184 LYS B CA  1 
ATOM   5650  C C   . LYS B 1 184 ? -3.299  52.778  35.013  1.00 56.81  ? 184 LYS B C   1 
ATOM   5651  O O   . LYS B 1 184 ? -2.081  52.754  35.217  1.00 65.89  ? 184 LYS B O   1 
ATOM   5652  C CB  . LYS B 1 184 ? -4.424  52.258  32.826  1.00 51.40  ? 184 LYS B CB  1 
ATOM   5653  C CG  . LYS B 1 184 ? -3.284  52.486  31.864  1.00 57.96  ? 184 LYS B CG  1 
ATOM   5654  C CD  . LYS B 1 184 ? -3.779  52.862  30.482  1.00 59.78  ? 184 LYS B CD  1 
ATOM   5655  C CE  . LYS B 1 184 ? -3.114  54.132  29.990  1.00 52.92  ? 184 LYS B CE  1 
ATOM   5656  N NZ  . LYS B 1 184 ? -3.560  55.302  30.794  1.00 65.24  ? 184 LYS B NZ  1 
ATOM   5657  N N   . GLU B 1 185 ? -4.091  53.719  35.537  1.00 61.13  ? 185 GLU B N   1 
ATOM   5658  C CA  . GLU B 1 185 ? -3.533  54.802  36.341  1.00 62.03  ? 185 GLU B CA  1 
ATOM   5659  C C   . GLU B 1 185 ? -2.941  54.281  37.645  1.00 59.73  ? 185 GLU B C   1 
ATOM   5660  O O   . GLU B 1 185 ? -1.854  54.707  38.052  1.00 54.31  ? 185 GLU B O   1 
ATOM   5661  C CB  . GLU B 1 185 ? -4.611  55.848  36.626  1.00 63.86  ? 185 GLU B CB  1 
ATOM   5662  C CG  . GLU B 1 185 ? -5.338  56.323  35.385  1.00 73.55  ? 185 GLU B CG  1 
ATOM   5663  C CD  . GLU B 1 185 ? -5.505  57.827  35.338  1.00 85.69  ? 185 GLU B CD  1 
ATOM   5664  O OE1 . GLU B 1 185 ? -6.460  58.297  34.684  1.00 79.57  ? 185 GLU B OE1 1 
ATOM   5665  O OE2 . GLU B 1 185 ? -4.682  58.541  35.949  1.00 90.92  ? 185 GLU B OE2 1 
ATOM   5666  N N   . GLU B 1 186 ? -3.644  53.371  38.321  1.00 67.73  ? 186 GLU B N   1 
ATOM   5667  C CA  . GLU B 1 186 ? -3.160  52.801  39.572  1.00 66.20  ? 186 GLU B CA  1 
ATOM   5668  C C   . GLU B 1 186 ? -2.068  51.760  39.356  1.00 67.62  ? 186 GLU B C   1 
ATOM   5669  O O   . GLU B 1 186 ? -1.559  51.204  40.337  1.00 66.90  ? 186 GLU B O   1 
ATOM   5670  C CB  . GLU B 1 186 ? -4.328  52.204  40.369  1.00 56.61  ? 186 GLU B CB  1 
ATOM   5671  C CG  . GLU B 1 186 ? -5.248  53.280  40.965  1.00 77.62  ? 186 GLU B CG  1 
ATOM   5672  C CD  . GLU B 1 186 ? -6.330  52.727  41.884  1.00 85.28  ? 186 GLU B CD  1 
ATOM   5673  O OE1 . GLU B 1 186 ? -6.440  51.490  42.008  1.00 78.88  ? 186 GLU B OE1 1 
ATOM   5674  O OE2 . GLU B 1 186 ? -7.065  53.535  42.494  1.00 87.71  ? 186 GLU B OE2 1 
ATOM   5675  N N   . GLY B 1 187 ? -1.687  51.500  38.105  1.00 54.91  ? 187 GLY B N   1 
ATOM   5676  C CA  . GLY B 1 187 ? -0.549  50.655  37.826  1.00 54.08  ? 187 GLY B CA  1 
ATOM   5677  C C   . GLY B 1 187 ? -0.799  49.172  37.946  1.00 62.91  ? 187 GLY B C   1 
ATOM   5678  O O   . GLY B 1 187 ? 0.147   48.388  37.798  1.00 64.07  ? 187 GLY B O   1 
ATOM   5679  N N   . LYS B 1 188 ? -2.042  48.757  38.204  1.00 52.75  ? 188 LYS B N   1 
ATOM   5680  C CA  . LYS B 1 188 ? -2.327  47.339  38.373  1.00 46.88  ? 188 LYS B CA  1 
ATOM   5681  C C   . LYS B 1 188 ? -2.230  46.573  37.064  1.00 48.47  ? 188 LYS B C   1 
ATOM   5682  O O   . LYS B 1 188 ? -2.076  45.348  37.087  1.00 46.96  ? 188 LYS B O   1 
ATOM   5683  C CB  . LYS B 1 188 ? -3.717  47.143  38.979  1.00 57.95  ? 188 LYS B CB  1 
ATOM   5684  C CG  . LYS B 1 188 ? -4.104  48.183  40.007  1.00 56.86  ? 188 LYS B CG  1 
ATOM   5685  C CD  . LYS B 1 188 ? -4.969  47.577  41.090  1.00 57.71  ? 188 LYS B CD  1 
ATOM   5686  C CE  . LYS B 1 188 ? -5.233  48.589  42.178  1.00 62.25  ? 188 LYS B CE  1 
ATOM   5687  N NZ  . LYS B 1 188 ? -6.673  48.924  42.271  1.00 67.61  ? 188 LYS B NZ  1 
ATOM   5688  N N   . GLY B 1 189 ? -2.319  47.257  35.929  1.00 51.29  ? 189 GLY B N   1 
ATOM   5689  C CA  . GLY B 1 189 ? -2.191  46.569  34.662  1.00 54.03  ? 189 GLY B CA  1 
ATOM   5690  C C   . GLY B 1 189 ? -2.213  47.476  33.453  1.00 49.67  ? 189 GLY B C   1 
ATOM   5691  O O   . GLY B 1 189 ? -2.915  48.489  33.436  1.00 57.09  ? 189 GLY B O   1 
ATOM   5692  N N   . SER B 1 190 ? -1.443  47.115  32.433  1.00 48.65  ? 190 SER B N   1 
ATOM   5693  C CA  . SER B 1 190 ? -1.408  47.882  31.199  1.00 48.48  ? 190 SER B CA  1 
ATOM   5694  C C   . SER B 1 190 ? -2.616  47.531  30.335  1.00 47.73  ? 190 SER B C   1 
ATOM   5695  O O   . SER B 1 190 ? -3.092  46.393  30.343  1.00 42.90  ? 190 SER B O   1 
ATOM   5696  C CB  . SER B 1 190 ? -0.110  47.596  30.441  1.00 47.49  ? 190 SER B CB  1 
ATOM   5697  O OG  . SER B 1 190 ? 0.899   48.531  30.786  1.00 60.36  ? 190 SER B OG  1 
ATOM   5698  N N   . VAL B 1 191 ? -3.120  48.517  29.598  1.00 48.04  ? 191 VAL B N   1 
ATOM   5699  C CA  . VAL B 1 191 ? -4.217  48.316  28.658  1.00 51.40  ? 191 VAL B CA  1 
ATOM   5700  C C   . VAL B 1 191 ? -3.695  48.592  27.255  1.00 39.92  ? 191 VAL B C   1 
ATOM   5701  O O   . VAL B 1 191 ? -3.029  49.606  27.021  1.00 45.43  ? 191 VAL B O   1 
ATOM   5702  C CB  . VAL B 1 191 ? -5.428  49.211  28.987  1.00 50.65  ? 191 VAL B CB  1 
ATOM   5703  C CG1 . VAL B 1 191 ? -6.609  48.840  28.107  1.00 45.22  ? 191 VAL B CG1 1 
ATOM   5704  C CG2 . VAL B 1 191 ? -5.810  49.081  30.445  1.00 43.93  ? 191 VAL B CG2 1 
ATOM   5705  N N   . SER B 1 192 ? -3.983  47.690  26.330  1.00 40.71  ? 192 SER B N   1 
ATOM   5706  C CA  . SER B 1 192 ? -3.600  47.841  24.935  1.00 47.33  ? 192 SER B CA  1 
ATOM   5707  C C   . SER B 1 192 ? -4.844  47.825  24.060  1.00 48.86  ? 192 SER B C   1 
ATOM   5708  O O   . SER B 1 192 ? -5.965  47.611  24.530  1.00 54.68  ? 192 SER B O   1 
ATOM   5709  C CB  . SER B 1 192 ? -2.644  46.731  24.505  1.00 45.73  ? 192 SER B CB  1 
ATOM   5710  O OG  . SER B 1 192 ? -3.384  45.581  24.128  1.00 46.75  ? 192 SER B OG  1 
ATOM   5711  N N   . THR B 1 193 ? -4.638  48.043  22.768  1.00 45.99  ? 193 THR B N   1 
ATOM   5712  C CA  . THR B 1 193 ? -5.723  47.965  21.808  1.00 53.07  ? 193 THR B CA  1 
ATOM   5713  C C   . THR B 1 193 ? -5.248  47.191  20.585  1.00 50.24  ? 193 THR B C   1 
ATOM   5714  O O   . THR B 1 193 ? -4.109  46.718  20.518  1.00 43.45  ? 193 THR B O   1 
ATOM   5715  C CB  . THR B 1 193 ? -6.228  49.358  21.433  1.00 51.59  ? 193 THR B CB  1 
ATOM   5716  O OG1 . THR B 1 193 ? -7.468  49.239  20.718  1.00 48.57  ? 193 THR B OG1 1 
ATOM   5717  C CG2 . THR B 1 193 ? -5.191  50.075  20.584  1.00 52.64  ? 193 THR B CG2 1 
ATOM   5718  N N   . SER B 1 194 ? -6.147  47.034  19.631  1.00 42.68  ? 194 SER B N   1 
ATOM   5719  C CA  . SER B 1 194 ? -5.881  46.376  18.363  1.00 42.54  ? 194 SER B CA  1 
ATOM   5720  C C   . SER B 1 194 ? -6.307  47.325  17.263  1.00 47.60  ? 194 SER B C   1 
ATOM   5721  O O   . SER B 1 194 ? -7.015  48.305  17.520  1.00 48.61  ? 194 SER B O   1 
ATOM   5722  C CB  . SER B 1 194 ? -6.650  45.048  18.255  1.00 46.06  ? 194 SER B CB  1 
ATOM   5723  O OG  . SER B 1 194 ? -6.354  44.177  19.334  1.00 49.68  ? 194 SER B OG  1 
ATOM   5724  N N   . PRO B 1 195 ? -5.859  47.090  16.025  1.00 50.87  ? 195 PRO B N   1 
ATOM   5725  C CA  . PRO B 1 195 ? -6.435  47.815  14.885  1.00 50.07  ? 195 PRO B CA  1 
ATOM   5726  C C   . PRO B 1 195 ? -7.959  47.753  14.908  1.00 48.59  ? 195 PRO B C   1 
ATOM   5727  O O   . PRO B 1 195 ? -8.542  46.705  15.193  1.00 54.84  ? 195 PRO B O   1 
ATOM   5728  C CB  . PRO B 1 195 ? -5.855  47.073  13.681  1.00 50.72  ? 195 PRO B CB  1 
ATOM   5729  C CG  . PRO B 1 195 ? -4.510  46.631  14.175  1.00 49.31  ? 195 PRO B CG  1 
ATOM   5730  C CD  . PRO B 1 195 ? -4.720  46.246  15.616  1.00 41.00  ? 195 PRO B CD  1 
ATOM   5731  N N   . TYR B 1 196 ? -8.591  48.884  14.566  1.00 49.30  ? 196 TYR B N   1 
ATOM   5732  C CA  . TYR B 1 196 ? -9.975  49.195  14.929  1.00 50.85  ? 196 TYR B CA  1 
ATOM   5733  C C   . TYR B 1 196 ? -10.945 48.014  14.845  1.00 46.27  ? 196 TYR B C   1 
ATOM   5734  O O   . TYR B 1 196 ? -11.522 47.597  15.856  1.00 39.33  ? 196 TYR B O   1 
ATOM   5735  C CB  . TYR B 1 196 ? -10.493 50.345  14.052  1.00 43.10  ? 196 TYR B CB  1 
ATOM   5736  C CG  . TYR B 1 196 ? -11.471 51.241  14.765  1.00 42.12  ? 196 TYR B CG  1 
ATOM   5737  C CD1 . TYR B 1 196 ? -12.781 50.835  14.983  1.00 51.71  ? 196 TYR B CD1 1 
ATOM   5738  C CD2 . TYR B 1 196 ? -11.091 52.495  15.219  1.00 46.48  ? 196 TYR B CD2 1 
ATOM   5739  C CE1 . TYR B 1 196 ? -13.687 51.651  15.634  1.00 44.88  ? 196 TYR B CE1 1 
ATOM   5740  C CE2 . TYR B 1 196 ? -11.991 53.325  15.870  1.00 50.20  ? 196 TYR B CE2 1 
ATOM   5741  C CZ  . TYR B 1 196 ? -13.286 52.896  16.075  1.00 48.96  ? 196 TYR B CZ  1 
ATOM   5742  O OH  . TYR B 1 196 ? -14.177 53.718  16.722  1.00 58.57  ? 196 TYR B OH  1 
ATOM   5743  N N   . TYR B 1 197 ? -11.144 47.473  13.644  1.00 49.86  ? 197 TYR B N   1 
ATOM   5744  C CA  . TYR B 1 197 ? -12.198 46.492  13.389  1.00 48.85  ? 197 TYR B CA  1 
ATOM   5745  C C   . TYR B 1 197 ? -11.658 45.060  13.349  1.00 49.14  ? 197 TYR B C   1 
ATOM   5746  O O   . TYR B 1 197 ? -12.088 44.241  12.531  1.00 51.09  ? 197 TYR B O   1 
ATOM   5747  C CB  . TYR B 1 197 ? -12.936 46.860  12.098  1.00 50.13  ? 197 TYR B CB  1 
ATOM   5748  C CG  . TYR B 1 197 ? -13.827 48.061  12.268  1.00 51.80  ? 197 TYR B CG  1 
ATOM   5749  C CD1 . TYR B 1 197 ? -15.000 47.962  13.004  1.00 53.28  ? 197 TYR B CD1 1 
ATOM   5750  C CD2 . TYR B 1 197 ? -13.488 49.303  11.739  1.00 48.74  ? 197 TYR B CD2 1 
ATOM   5751  C CE1 . TYR B 1 197 ? -15.824 49.053  13.200  1.00 48.50  ? 197 TYR B CE1 1 
ATOM   5752  C CE2 . TYR B 1 197 ? -14.317 50.417  11.932  1.00 48.18  ? 197 TYR B CE2 1 
ATOM   5753  C CZ  . TYR B 1 197 ? -15.486 50.277  12.668  1.00 52.75  ? 197 TYR B CZ  1 
ATOM   5754  O OH  . TYR B 1 197 ? -16.336 51.342  12.885  1.00 51.99  ? 197 TYR B OH  1 
ATOM   5755  N N   . HIS B 1 198 ? -10.709 44.739  14.220  1.00 45.44  ? 198 HIS B N   1 
ATOM   5756  C CA  . HIS B 1 198 ? -10.037 43.441  14.248  1.00 48.19  ? 198 HIS B CA  1 
ATOM   5757  C C   . HIS B 1 198 ? -9.654  42.902  12.867  1.00 52.11  ? 198 HIS B C   1 
ATOM   5758  O O   . HIS B 1 198 ? -9.934  41.730  12.584  1.00 57.18  ? 198 HIS B O   1 
ATOM   5759  C CB  . HIS B 1 198 ? -10.930 42.423  14.963  1.00 45.90  ? 198 HIS B CB  1 
ATOM   5760  C CG  . HIS B 1 198 ? -10.174 41.385  15.735  1.00 45.67  ? 198 HIS B CG  1 
ATOM   5761  N ND1 . HIS B 1 198 ? -10.085 40.071  15.328  1.00 41.72  ? 198 HIS B ND1 1 
ATOM   5762  C CD2 . HIS B 1 198 ? -9.469  41.471  16.888  1.00 45.76  ? 198 HIS B CD2 1 
ATOM   5763  C CE1 . HIS B 1 198 ? -9.361  39.391  16.200  1.00 44.12  ? 198 HIS B CE1 1 
ATOM   5764  N NE2 . HIS B 1 198 ? -8.974  40.217  17.155  1.00 46.97  ? 198 HIS B NE2 1 
ATOM   5765  N N   . PRO B 1 199 ? -9.017  43.686  11.990  1.00 55.31  ? 199 PRO B N   1 
ATOM   5766  C CA  . PRO B 1 199 ? -8.666  43.175  10.660  1.00 49.92  ? 199 PRO B CA  1 
ATOM   5767  C C   . PRO B 1 199 ? -7.406  42.328  10.659  1.00 51.59  ? 199 PRO B C   1 
ATOM   5768  O O   . PRO B 1 199 ? -6.571  42.388  11.559  1.00 63.88  ? 199 PRO B O   1 
ATOM   5769  C CB  . PRO B 1 199 ? -8.423  44.447  9.851   1.00 54.22  ? 199 PRO B CB  1 
ATOM   5770  C CG  . PRO B 1 199 ? -7.870  45.376  10.840  1.00 47.96  ? 199 PRO B CG  1 
ATOM   5771  C CD  . PRO B 1 199 ? -8.569  45.085  12.148  1.00 52.22  ? 199 PRO B CD  1 
ATOM   5772  N N   . LEU B 1 200 ? -7.250  41.573  9.580   1.00 56.21  ? 200 LEU B N   1 
ATOM   5773  C CA  . LEU B 1 200 ? -6.006  40.846  9.338   1.00 58.28  ? 200 LEU B CA  1 
ATOM   5774  C C   . LEU B 1 200 ? -5.053  41.786  8.620   1.00 49.23  ? 200 LEU B C   1 
ATOM   5775  O O   . LEU B 1 200 ? -5.003  41.821  7.390   1.00 49.99  ? 200 LEU B O   1 
ATOM   5776  C CB  . LEU B 1 200 ? -6.275  39.574  8.538   1.00 60.65  ? 200 LEU B CB  1 
ATOM   5777  C CG  . LEU B 1 200 ? -7.022  38.492  9.318   1.00 58.13  ? 200 LEU B CG  1 
ATOM   5778  C CD1 . LEU B 1 200 ? -7.607  37.451  8.385   1.00 58.88  ? 200 LEU B CD1 1 
ATOM   5779  C CD2 . LEU B 1 200 ? -6.154  37.826  10.384  1.00 45.62  ? 200 LEU B CD2 1 
ATOM   5780  N N   . ILE B 1 201 ? -4.298  42.565  9.412   1.00 53.77  ? 201 ILE B N   1 
ATOM   5781  C CA  . ILE B 1 201 ? -3.381  43.547  8.833   1.00 48.25  ? 201 ILE B CA  1 
ATOM   5782  C C   . ILE B 1 201 ? -2.446  42.921  7.813   1.00 53.49  ? 201 ILE B C   1 
ATOM   5783  O O   . ILE B 1 201 ? -2.252  43.520  6.745   1.00 53.93  ? 201 ILE B O   1 
ATOM   5784  C CB  . ILE B 1 201 ? -2.645  44.312  9.942   1.00 42.92  ? 201 ILE B CB  1 
ATOM   5785  C CG1 . ILE B 1 201 ? -3.418  45.598  10.267  1.00 46.54  ? 201 ILE B CG1 1 
ATOM   5786  C CG2 . ILE B 1 201 ? -1.273  44.706  9.530   1.00 49.40  ? 201 ILE B CG2 1 
ATOM   5787  C CD1 . ILE B 1 201 ? -4.653  45.300  10.958  1.00 54.26  ? 201 ILE B CD1 1 
ATOM   5788  N N   . PRO B 1 202 ? -1.864  41.736  8.031   1.00 51.12  ? 202 PRO B N   1 
ATOM   5789  C CA  . PRO B 1 202 ? -0.969  41.176  7.000   1.00 48.30  ? 202 PRO B CA  1 
ATOM   5790  C C   . PRO B 1 202 ? -1.601  41.041  5.624   1.00 48.41  ? 202 PRO B C   1 
ATOM   5791  O O   . PRO B 1 202 ? -0.987  41.449  4.634   1.00 59.59  ? 202 PRO B O   1 
ATOM   5792  C CB  . PRO B 1 202 ? -0.575  39.817  7.600   1.00 51.14  ? 202 PRO B CB  1 
ATOM   5793  C CG  . PRO B 1 202 ? -0.574  40.075  9.067   1.00 51.85  ? 202 PRO B CG  1 
ATOM   5794  C CD  . PRO B 1 202 ? -1.781  40.958  9.280   1.00 52.98  ? 202 PRO B CD  1 
ATOM   5795  N N   . ILE B 1 203 ? -2.825  40.517  5.533   1.00 49.72  ? 203 ILE B N   1 
ATOM   5796  C CA  . ILE B 1 203 ? -3.466  40.377  4.229   1.00 51.03  ? 203 ILE B CA  1 
ATOM   5797  C C   . ILE B 1 203 ? -3.775  41.740  3.620   1.00 51.81  ? 203 ILE B C   1 
ATOM   5798  O O   . ILE B 1 203 ? -3.676  41.925  2.401   1.00 49.54  ? 203 ILE B O   1 
ATOM   5799  C CB  . ILE B 1 203 ? -4.729  39.516  4.348   1.00 47.87  ? 203 ILE B CB  1 
ATOM   5800  C CG1 . ILE B 1 203 ? -4.349  38.099  4.750   1.00 50.32  ? 203 ILE B CG1 1 
ATOM   5801  C CG2 . ILE B 1 203 ? -5.439  39.478  3.023   1.00 49.69  ? 203 ILE B CG2 1 
ATOM   5802  C CD1 . ILE B 1 203 ? -5.477  37.128  4.605   1.00 45.85  ? 203 ILE B CD1 1 
ATOM   5803  N N   . LEU B 1 204 ? -4.159  42.714  4.452   1.00 50.20  ? 204 LEU B N   1 
ATOM   5804  C CA  . LEU B 1 204 ? -4.447  44.054  3.942   1.00 51.92  ? 204 LEU B CA  1 
ATOM   5805  C C   . LEU B 1 204 ? -3.216  44.703  3.320   1.00 51.53  ? 204 LEU B C   1 
ATOM   5806  O O   . LEU B 1 204 ? -3.316  45.375  2.288   1.00 56.04  ? 204 LEU B O   1 
ATOM   5807  C CB  . LEU B 1 204 ? -4.989  44.939  5.057   1.00 54.82  ? 204 LEU B CB  1 
ATOM   5808  C CG  . LEU B 1 204 ? -6.313  44.490  5.653   1.00 55.36  ? 204 LEU B CG  1 
ATOM   5809  C CD1 . LEU B 1 204 ? -6.693  45.413  6.804   1.00 56.67  ? 204 LEU B CD1 1 
ATOM   5810  C CD2 . LEU B 1 204 ? -7.397  44.443  4.573   1.00 51.05  ? 204 LEU B CD2 1 
ATOM   5811  N N   . LEU B 1 205 ? -2.049  44.536  3.944   1.00 51.43  ? 205 LEU B N   1 
ATOM   5812  C CA  . LEU B 1 205 ? -0.830  45.094  3.371   1.00 54.65  ? 205 LEU B CA  1 
ATOM   5813  C C   . LEU B 1 205 ? -0.415  44.318  2.129   1.00 54.28  ? 205 LEU B C   1 
ATOM   5814  O O   . LEU B 1 205 ? -0.355  44.873  1.028   1.00 54.93  ? 205 LEU B O   1 
ATOM   5815  C CB  . LEU B 1 205 ? 0.287   45.097  4.414   1.00 57.81  ? 205 LEU B CB  1 
ATOM   5816  C CG  . LEU B 1 205 ? -0.024  45.922  5.664   1.00 54.04  ? 205 LEU B CG  1 
ATOM   5817  C CD1 . LEU B 1 205 ? 1.040   45.714  6.722   1.00 50.80  ? 205 LEU B CD1 1 
ATOM   5818  C CD2 . LEU B 1 205 ? -0.138  47.394  5.299   1.00 49.42  ? 205 LEU B CD2 1 
ATOM   5819  N N   . ASN B 1 206 ? -0.129  43.025  2.290   1.00 52.78  ? 206 ASN B N   1 
ATOM   5820  C CA  . ASN B 1 206 ? 0.243   42.183  1.164   1.00 58.98  ? 206 ASN B CA  1 
ATOM   5821  C C   . ASN B 1 206 ? -0.467  40.843  1.251   1.00 54.67  ? 206 ASN B C   1 
ATOM   5822  O O   . ASN B 1 206 ? -0.166  40.036  2.140   1.00 52.84  ? 206 ASN B O   1 
ATOM   5823  C CB  . ASN B 1 206 ? 1.761   41.969  1.097   1.00 61.39  ? 206 ASN B CB  1 
ATOM   5824  C CG  . ASN B 1 206 ? 2.225   41.545  -0.285  1.00 66.66  ? 206 ASN B CG  1 
ATOM   5825  O OD1 . ASN B 1 206 ? 1.697   42.009  -1.299  1.00 68.51  ? 206 ASN B OD1 1 
ATOM   5826  N ND2 . ASN B 1 206 ? 3.223   40.668  -0.335  1.00 66.65  ? 206 ASN B ND2 1 
ATOM   5827  N N   . PRO B 1 207 ? -1.407  40.568  0.344   1.00 62.16  ? 207 PRO B N   1 
ATOM   5828  C CA  . PRO B 1 207 ? -2.081  39.258  0.347   1.00 57.96  ? 207 PRO B CA  1 
ATOM   5829  C C   . PRO B 1 207 ? -1.152  38.081  0.107   1.00 64.35  ? 207 PRO B C   1 
ATOM   5830  O O   . PRO B 1 207 ? -1.522  36.956  0.463   1.00 57.53  ? 207 PRO B O   1 
ATOM   5831  C CB  . PRO B 1 207 ? -3.101  39.399  -0.794  1.00 48.54  ? 207 PRO B CB  1 
ATOM   5832  C CG  . PRO B 1 207 ? -3.301  40.879  -0.936  1.00 47.44  ? 207 PRO B CG  1 
ATOM   5833  C CD  . PRO B 1 207 ? -1.940  41.447  -0.708  1.00 49.51  ? 207 PRO B CD  1 
ATOM   5834  N N   . ASN B 1 208 ? 0.039   38.293  -0.480  1.00 62.11  ? 208 ASN B N   1 
ATOM   5835  C CA  . ASN B 1 208 ? 0.962   37.189  -0.740  1.00 56.57  ? 208 ASN B CA  1 
ATOM   5836  C C   . ASN B 1 208 ? 1.621   36.648  0.515   1.00 61.60  ? 208 ASN B C   1 
ATOM   5837  O O   . ASN B 1 208 ? 2.412   35.703  0.408   1.00 64.40  ? 208 ASN B O   1 
ATOM   5838  C CB  . ASN B 1 208 ? 2.061   37.603  -1.719  1.00 56.59  ? 208 ASN B CB  1 
ATOM   5839  C CG  . ASN B 1 208 ? 1.531   38.339  -2.909  1.00 61.78  ? 208 ASN B CG  1 
ATOM   5840  O OD1 . ASN B 1 208 ? 1.829   39.515  -3.106  1.00 70.78  ? 208 ASN B OD1 1 
ATOM   5841  N ND2 . ASN B 1 208 ? 0.749   37.649  -3.728  1.00 65.04  ? 208 ASN B ND2 1 
ATOM   5842  N N   . CYS B 1 209 ? 1.350   37.224  1.687   1.00 61.58  ? 209 CYS B N   1 
ATOM   5843  C CA  . CYS B 1 209 ? 1.858   36.642  2.923   1.00 60.74  ? 209 CYS B CA  1 
ATOM   5844  C C   . CYS B 1 209 ? 1.241   35.281  3.213   1.00 64.47  ? 209 CYS B C   1 
ATOM   5845  O O   . CYS B 1 209 ? 1.745   34.566  4.086   1.00 60.48  ? 209 CYS B O   1 
ATOM   5846  C CB  . CYS B 1 209 ? 1.604   37.588  4.097   1.00 56.19  ? 209 CYS B CB  1 
ATOM   5847  S SG  . CYS B 1 209 ? -0.141  37.883  4.473   1.00 94.29  ? 209 CYS B SG  1 
ATOM   5848  N N   . VAL B 1 210 ? 0.168   34.915  2.502   1.00 64.62  ? 210 VAL B N   1 
ATOM   5849  C CA  . VAL B 1 210 ? -0.461  33.612  2.680   1.00 55.80  ? 210 VAL B CA  1 
ATOM   5850  C C   . VAL B 1 210 ? 0.423   32.502  2.134   1.00 53.68  ? 210 VAL B C   1 
ATOM   5851  O O   . VAL B 1 210 ? 0.355   31.362  2.605   1.00 61.45  ? 210 VAL B O   1 
ATOM   5852  C CB  . VAL B 1 210 ? -1.848  33.597  2.008   1.00 55.03  ? 210 VAL B CB  1 
ATOM   5853  C CG1 . VAL B 1 210 ? -2.704  34.742  2.512   1.00 55.05  ? 210 VAL B CG1 1 
ATOM   5854  C CG2 . VAL B 1 210 ? -1.712  33.670  0.504   1.00 54.01  ? 210 VAL B CG2 1 
ATOM   5855  N N   . TYR B 1 211 ? 1.261   32.804  1.138   1.00 58.88  ? 211 TYR B N   1 
ATOM   5856  C CA  . TYR B 1 211 ? 2.047   31.769  0.474   1.00 61.78  ? 211 TYR B CA  1 
ATOM   5857  C C   . TYR B 1 211 ? 3.311   31.402  1.240   1.00 63.55  ? 211 TYR B C   1 
ATOM   5858  O O   . TYR B 1 211 ? 3.889   30.342  0.974   1.00 64.31  ? 211 TYR B O   1 
ATOM   5859  C CB  . TYR B 1 211 ? 2.408   32.206  -0.950  1.00 57.32  ? 211 TYR B CB  1 
ATOM   5860  C CG  . TYR B 1 211 ? 1.201   32.505  -1.810  1.00 58.17  ? 211 TYR B CG  1 
ATOM   5861  C CD1 . TYR B 1 211 ? 0.368   31.484  -2.242  1.00 61.30  ? 211 TYR B CD1 1 
ATOM   5862  C CD2 . TYR B 1 211 ? 0.888   33.807  -2.185  1.00 57.36  ? 211 TYR B CD2 1 
ATOM   5863  C CE1 . TYR B 1 211 ? -0.742  31.744  -3.023  1.00 64.27  ? 211 TYR B CE1 1 
ATOM   5864  C CE2 . TYR B 1 211 ? -0.226  34.077  -2.969  1.00 59.61  ? 211 TYR B CE2 1 
ATOM   5865  C CZ  . TYR B 1 211 ? -1.037  33.038  -3.385  1.00 62.24  ? 211 TYR B CZ  1 
ATOM   5866  O OH  . TYR B 1 211 ? -2.150  33.278  -4.165  1.00 66.70  ? 211 TYR B OH  1 
ATOM   5867  N N   . GLU B 1 212 ? 3.750   32.247  2.177   1.00 61.53  ? 212 GLU B N   1 
ATOM   5868  C CA  . GLU B 1 212 ? 4.880   31.886  3.028   1.00 61.38  ? 212 GLU B CA  1 
ATOM   5869  C C   . GLU B 1 212 ? 4.575   30.621  3.819   1.00 64.72  ? 212 GLU B C   1 
ATOM   5870  O O   . GLU B 1 212 ? 5.405   29.709  3.910   1.00 71.46  ? 212 GLU B O   1 
ATOM   5871  C CB  . GLU B 1 212 ? 5.222   33.037  3.977   1.00 63.85  ? 212 GLU B CB  1 
ATOM   5872  C CG  . GLU B 1 212 ? 5.227   34.430  3.348   1.00 71.83  ? 212 GLU B CG  1 
ATOM   5873  C CD  . GLU B 1 212 ? 5.857   35.475  4.261   1.00 68.65  ? 212 GLU B CD  1 
ATOM   5874  O OE1 . GLU B 1 212 ? 6.847   35.143  4.946   1.00 64.90  ? 212 GLU B OE1 1 
ATOM   5875  O OE2 . GLU B 1 212 ? 5.366   36.626  4.296   1.00 73.69  ? 212 GLU B OE2 1 
ATOM   5876  N N   . THR B 1 213 ? 3.376   30.546  4.386   1.00 63.34  ? 213 THR B N   1 
ATOM   5877  C CA  . THR B 1 213 ? 3.014   29.388  5.183   1.00 62.46  ? 213 THR B CA  1 
ATOM   5878  C C   . THR B 1 213 ? 2.231   28.337  4.404   1.00 61.25  ? 213 THR B C   1 
ATOM   5879  O O   . THR B 1 213 ? 2.459   27.145  4.581   1.00 54.84  ? 213 THR B O   1 
ATOM   5880  C CB  . THR B 1 213 ? 2.233   29.828  6.411   1.00 63.27  ? 213 THR B CB  1 
ATOM   5881  O OG1 . THR B 1 213 ? 1.640   31.104  6.142   1.00 66.28  ? 213 THR B OG1 1 
ATOM   5882  C CG2 . THR B 1 213 ? 3.164   29.952  7.592   1.00 55.67  ? 213 THR B CG2 1 
ATOM   5883  N N   . THR B 1 214 ? 1.341   28.750  3.518   1.00 64.17  ? 214 THR B N   1 
ATOM   5884  C CA  . THR B 1 214 ? 0.632   27.849  2.639   1.00 63.46  ? 214 THR B CA  1 
ATOM   5885  C C   . THR B 1 214 ? 0.873   28.236  1.210   1.00 62.18  ? 214 THR B C   1 
ATOM   5886  O O   . THR B 1 214 ? 0.140   29.060  0.625   1.00 62.37  ? 214 THR B O   1 
ATOM   5887  C CB  . THR B 1 214 ? -0.835  27.837  2.940   1.00 57.25  ? 214 THR B CB  1 
ATOM   5888  O OG1 . THR B 1 214 ? -1.396  29.183  2.926   1.00 64.59  ? 214 THR B OG1 1 
ATOM   5889  C CG2 . THR B 1 214 ? -1.105  27.277  4.360   1.00 56.68  ? 214 THR B CG2 1 
ATOM   5890  N N   . PRO B 1 215 ? 1.907   27.688  0.601   1.00 60.46  ? 215 PRO B N   1 
ATOM   5891  C CA  . PRO B 1 215 ? 2.238   28.180  -0.815  1.00 58.91  ? 215 PRO B CA  1 
ATOM   5892  C C   . PRO B 1 215 ? 1.279   27.698  -1.875  1.00 63.80  ? 215 PRO B C   1 
ATOM   5893  O O   . PRO B 1 215 ? 1.002   28.449  -2.787  1.00 67.34  ? 215 PRO B O   1 
ATOM   5894  C CB  . PRO B 1 215 ? 3.680   27.574  -1.131  1.00 59.53  ? 215 PRO B CB  1 
ATOM   5895  C CG  . PRO B 1 215 ? 3.943   26.706  0.055   1.00 68.78  ? 215 PRO B CG  1 
ATOM   5896  C CD  . PRO B 1 215 ? 3.042   26.870  1.173   1.00 63.02  ? 215 PRO B CD  1 
ATOM   5897  N N   . ASN B 1 216 ? 0.674   26.513  -1.683  1.00 59.68  ? 216 ASN B N   1 
ATOM   5898  C CA  . ASN B 1 216 ? -0.218  25.977  -2.723  1.00 62.47  ? 216 ASN B CA  1 
ATOM   5899  C C   . ASN B 1 216 ? -1.666  26.462  -2.608  1.00 69.18  ? 216 ASN B C   1 
ATOM   5900  O O   . ASN B 1 216 ? -2.536  26.000  -3.362  1.00 69.39  ? 216 ASN B O   1 
ATOM   5901  C CB  . ASN B 1 216 ? -0.184  24.438  -2.689  1.00 65.67  ? 216 ASN B CB  1 
ATOM   5902  C CG  . ASN B 1 216 ? 1.194   23.892  -2.938  1.00 66.57  ? 216 ASN B CG  1 
ATOM   5903  O OD1 . ASN B 1 216 ? 1.927   24.407  -3.782  1.00 70.84  ? 216 ASN B OD1 1 
ATOM   5904  N ND2 . ASN B 1 216 ? 1.583   22.882  -2.167  1.00 65.94  ? 216 ASN B ND2 1 
ATOM   5905  N N   . VAL B 1 217 ? -1.933  27.388  -1.687  1.00 60.11  ? 217 VAL B N   1 
ATOM   5906  C CA  . VAL B 1 217 ? -3.285  27.876  -1.496  1.00 59.79  ? 217 VAL B CA  1 
ATOM   5907  C C   . VAL B 1 217 ? -3.745  28.639  -2.743  1.00 66.37  ? 217 VAL B C   1 
ATOM   5908  O O   . VAL B 1 217 ? -2.941  29.129  -3.549  1.00 64.77  ? 217 VAL B O   1 
ATOM   5909  C CB  . VAL B 1 217 ? -3.354  28.759  -0.238  1.00 58.93  ? 217 VAL B CB  1 
ATOM   5910  C CG1 . VAL B 1 217 ? -2.732  30.111  -0.505  1.00 63.76  ? 217 VAL B CG1 1 
ATOM   5911  C CG2 . VAL B 1 217 ? -4.794  28.928  0.251   1.00 53.14  ? 217 VAL B CG2 1 
ATOM   5912  N N   . LYS B 1 218 ? -5.058  28.725  -2.907  1.00 61.50  ? 218 LYS B N   1 
ATOM   5913  C CA  . LYS B 1 218 ? -5.652  29.497  -3.987  1.00 66.92  ? 218 LYS B CA  1 
ATOM   5914  C C   . LYS B 1 218 ? -6.442  30.643  -3.374  1.00 68.14  ? 218 LYS B C   1 
ATOM   5915  O O   . LYS B 1 218 ? -7.378  30.414  -2.600  1.00 64.92  ? 218 LYS B O   1 
ATOM   5916  C CB  . LYS B 1 218 ? -6.539  28.624  -4.873  1.00 71.05  ? 218 LYS B CB  1 
ATOM   5917  C CG  . LYS B 1 218 ? -6.643  29.115  -6.310  1.00 73.47  ? 218 LYS B CG  1 
ATOM   5918  C CD  . LYS B 1 218 ? -7.677  30.245  -6.456  1.00 77.70  ? 218 LYS B CD  1 
ATOM   5919  C CE  . LYS B 1 218 ? -9.057  29.877  -5.884  1.00 78.52  ? 218 LYS B CE  1 
ATOM   5920  N NZ  . LYS B 1 218 ? -10.054 31.010  -5.874  1.00 68.98  ? 218 LYS B NZ  1 
ATOM   5921  N N   . ILE B 1 219 ? -6.038  31.863  -3.694  1.00 69.98  ? 219 ILE B N   1 
ATOM   5922  C CA  . ILE B 1 219 ? -6.715  33.068  -3.224  1.00 62.91  ? 219 ILE B CA  1 
ATOM   5923  C C   . ILE B 1 219 ? -7.121  33.863  -4.455  1.00 66.34  ? 219 ILE B C   1 
ATOM   5924  O O   . ILE B 1 219 ? -6.560  33.674  -5.549  1.00 66.97  ? 219 ILE B O   1 
ATOM   5925  C CB  . ILE B 1 219 ? -5.825  33.890  -2.262  1.00 61.55  ? 219 ILE B CB  1 
ATOM   5926  C CG1 . ILE B 1 219 ? -4.821  34.736  -3.042  1.00 57.53  ? 219 ILE B CG1 1 
ATOM   5927  C CG2 . ILE B 1 219 ? -5.115  32.991  -1.259  1.00 58.65  ? 219 ILE B CG2 1 
ATOM   5928  C CD1 . ILE B 1 219 ? -4.187  35.815  -2.214  1.00 56.70  ? 219 ILE B CD1 1 
ATOM   5929  N N   . PRO B 1 220 ? -8.111  34.743  -4.329  1.00 72.32  ? 220 PRO B N   1 
ATOM   5930  C CA  . PRO B 1 220 ? -8.522  35.554  -5.480  1.00 76.26  ? 220 PRO B CA  1 
ATOM   5931  C C   . PRO B 1 220 ? -7.448  36.570  -5.837  1.00 70.74  ? 220 PRO B C   1 
ATOM   5932  O O   . PRO B 1 220 ? -6.491  36.799  -5.096  1.00 72.87  ? 220 PRO B O   1 
ATOM   5933  C CB  . PRO B 1 220 ? -9.810  36.231  -4.995  1.00 69.47  ? 220 PRO B CB  1 
ATOM   5934  C CG  . PRO B 1 220 ? -9.672  36.261  -3.500  1.00 65.46  ? 220 PRO B CG  1 
ATOM   5935  C CD  . PRO B 1 220 ? -8.955  34.994  -3.145  1.00 64.29  ? 220 PRO B CD  1 
ATOM   5936  N N   . ASP B 1 221 ? -7.610  37.178  -7.007  1.00 71.52  ? 221 ASP B N   1 
ATOM   5937  C CA  . ASP B 1 221 ? -6.723  38.259  -7.417  1.00 75.56  ? 221 ASP B CA  1 
ATOM   5938  C C   . ASP B 1 221 ? -7.154  39.547  -6.727  1.00 69.09  ? 221 ASP B C   1 
ATOM   5939  O O   . ASP B 1 221 ? -8.288  40.002  -6.904  1.00 77.12  ? 221 ASP B O   1 
ATOM   5940  C CB  . ASP B 1 221 ? -6.740  38.430  -8.933  1.00 76.04  ? 221 ASP B CB  1 
ATOM   5941  C CG  . ASP B 1 221 ? -5.698  39.416  -9.415  1.00 82.18  ? 221 ASP B CG  1 
ATOM   5942  O OD1 . ASP B 1 221 ? -4.490  39.165  -9.210  1.00 89.50  ? 221 ASP B OD1 1 
ATOM   5943  O OD2 . ASP B 1 221 ? -6.092  40.452  -9.991  1.00 87.31  ? 221 ASP B OD2 1 
ATOM   5944  N N   . PHE B 1 222 ? -6.259  40.129  -5.937  1.00 62.89  ? 222 PHE B N   1 
ATOM   5945  C CA  . PHE B 1 222 ? -6.560  41.352  -5.195  1.00 62.24  ? 222 PHE B CA  1 
ATOM   5946  C C   . PHE B 1 222 ? -6.181  42.537  -6.075  1.00 62.29  ? 222 PHE B C   1 
ATOM   5947  O O   . PHE B 1 222 ? -5.043  43.003  -6.068  1.00 67.24  ? 222 PHE B O   1 
ATOM   5948  C CB  . PHE B 1 222 ? -5.805  41.376  -3.872  1.00 61.42  ? 222 PHE B CB  1 
ATOM   5949  C CG  . PHE B 1 222 ? -6.407  40.511  -2.802  1.00 61.47  ? 222 PHE B CG  1 
ATOM   5950  C CD1 . PHE B 1 222 ? -6.397  39.130  -2.920  1.00 62.30  ? 222 PHE B CD1 1 
ATOM   5951  C CD2 . PHE B 1 222 ? -6.945  41.079  -1.658  1.00 58.73  ? 222 PHE B CD2 1 
ATOM   5952  C CE1 . PHE B 1 222 ? -6.936  38.332  -1.931  1.00 67.29  ? 222 PHE B CE1 1 
ATOM   5953  C CE2 . PHE B 1 222 ? -7.485  40.287  -0.662  1.00 57.04  ? 222 PHE B CE2 1 
ATOM   5954  C CZ  . PHE B 1 222 ? -7.480  38.911  -0.798  1.00 64.27  ? 222 PHE B CZ  1 
ATOM   5955  N N   . ALA B 1 223 ? -7.148  43.039  -6.845  1.00 68.42  ? 223 ALA B N   1 
ATOM   5956  C CA  . ALA B 1 223 ? -6.862  44.160  -7.737  1.00 74.40  ? 223 ALA B CA  1 
ATOM   5957  C C   . ALA B 1 223 ? -6.622  45.443  -6.949  1.00 72.52  ? 223 ALA B C   1 
ATOM   5958  O O   . ALA B 1 223 ? -5.650  46.165  -7.198  1.00 88.53  ? 223 ALA B O   1 
ATOM   5959  C CB  . ALA B 1 223 ? -8.001  44.346  -8.738  1.00 76.19  ? 223 ALA B CB  1 
ATOM   5960  N N   . VAL B 1 224 ? -7.492  45.740  -5.989  1.00 63.29  ? 224 VAL B N   1 
ATOM   5961  C CA  . VAL B 1 224 ? -7.373  46.954  -5.186  1.00 70.35  ? 224 VAL B CA  1 
ATOM   5962  C C   . VAL B 1 224 ? -6.202  46.844  -4.216  1.00 70.66  ? 224 VAL B C   1 
ATOM   5963  O O   . VAL B 1 224 ? -5.576  45.785  -4.100  1.00 69.91  ? 224 VAL B O   1 
ATOM   5964  C CB  . VAL B 1 224 ? -8.683  47.221  -4.429  1.00 74.19  ? 224 VAL B CB  1 
ATOM   5965  C CG1 . VAL B 1 224 ? -9.862  46.991  -5.349  1.00 73.38  ? 224 VAL B CG1 1 
ATOM   5966  C CG2 . VAL B 1 224 ? -8.771  46.313  -3.209  1.00 68.67  ? 224 VAL B CG2 1 
ATOM   5967  N N   . SER B 1 225 ? -5.894  47.938  -3.516  1.00 70.91  ? 225 SER B N   1 
ATOM   5968  C CA  . SER B 1 225 ? -4.935  47.931  -2.417  1.00 71.08  ? 225 SER B CA  1 
ATOM   5969  C C   . SER B 1 225 ? -5.652  48.244  -1.111  1.00 69.73  ? 225 SER B C   1 
ATOM   5970  O O   . SER B 1 225 ? -6.525  49.119  -1.058  1.00 62.56  ? 225 SER B O   1 
ATOM   5971  C CB  . SER B 1 225 ? -3.798  48.941  -2.638  1.00 65.53  ? 225 SER B CB  1 
ATOM   5972  O OG  . SER B 1 225 ? -3.300  49.463  -1.410  1.00 53.24  ? 225 SER B OG  1 
ATOM   5973  N N   . PHE B 1 226 ? -5.288  47.509  -0.065  1.00 67.03  ? 226 PHE B N   1 
ATOM   5974  C CA  . PHE B 1 226 ? -5.771  47.767  1.280   1.00 65.77  ? 226 PHE B CA  1 
ATOM   5975  C C   . PHE B 1 226 ? -4.675  48.336  2.173   1.00 59.53  ? 226 PHE B C   1 
ATOM   5976  O O   . PHE B 1 226 ? -4.829  48.352  3.398   1.00 61.82  ? 226 PHE B O   1 
ATOM   5977  C CB  . PHE B 1 226 ? -6.338  46.482  1.886   1.00 67.37  ? 226 PHE B CB  1 
ATOM   5978  C CG  . PHE B 1 226 ? -7.510  45.902  1.130   1.00 70.82  ? 226 PHE B CG  1 
ATOM   5979  C CD1 . PHE B 1 226 ? -8.779  46.451  1.253   1.00 67.81  ? 226 PHE B CD1 1 
ATOM   5980  C CD2 . PHE B 1 226 ? -7.346  44.790  0.317   1.00 73.45  ? 226 PHE B CD2 1 
ATOM   5981  C CE1 . PHE B 1 226 ? -9.856  45.907  0.571   1.00 65.98  ? 226 PHE B CE1 1 
ATOM   5982  C CE2 . PHE B 1 226 ? -8.422  44.242  -0.370  1.00 66.46  ? 226 PHE B CE2 1 
ATOM   5983  C CZ  . PHE B 1 226 ? -9.677  44.801  -0.240  1.00 63.07  ? 226 PHE B CZ  1 
ATOM   5984  N N   . ARG B 1 227 ? -3.571  48.805  1.586   1.00 60.51  ? 227 ARG B N   1 
ATOM   5985  C CA  . ARG B 1 227 ? -2.455  49.275  2.398   1.00 60.30  ? 227 ARG B CA  1 
ATOM   5986  C C   . ARG B 1 227 ? -2.825  50.523  3.182   1.00 60.04  ? 227 ARG B C   1 
ATOM   5987  O O   . ARG B 1 227 ? -2.382  50.698  4.322   1.00 66.48  ? 227 ARG B O   1 
ATOM   5988  C CB  . ARG B 1 227 ? -1.239  49.538  1.520   1.00 52.34  ? 227 ARG B CB  1 
ATOM   5989  C CG  . ARG B 1 227 ? -0.826  48.343  0.696   1.00 61.96  ? 227 ARG B CG  1 
ATOM   5990  C CD  . ARG B 1 227 ? 0.558   48.557  0.107   1.00 77.33  ? 227 ARG B CD  1 
ATOM   5991  N NE  . ARG B 1 227 ? 1.534   48.852  1.148   1.00 83.78  ? 227 ARG B NE  1 
ATOM   5992  C CZ  . ARG B 1 227 ? 2.715   48.261  1.266   1.00 84.91  ? 227 ARG B CZ  1 
ATOM   5993  N NH1 . ARG B 1 227 ? 3.140   47.378  0.376   1.00 91.05  ? 227 ARG B NH1 1 
ATOM   5994  N NH2 . ARG B 1 227 ? 3.488   48.564  2.304   1.00 79.56  ? 227 ARG B NH2 1 
ATOM   5995  N N   . GLU B 1 228 ? -3.630  51.405  2.596   1.00 60.38  ? 228 GLU B N   1 
ATOM   5996  C CA  . GLU B 1 228 ? -4.024  52.594  3.336   1.00 63.20  ? 228 GLU B CA  1 
ATOM   5997  C C   . GLU B 1 228 ? -5.068  52.267  4.390   1.00 63.84  ? 228 GLU B C   1 
ATOM   5998  O O   . GLU B 1 228 ? -5.097  52.903  5.451   1.00 67.78  ? 228 GLU B O   1 
ATOM   5999  C CB  . GLU B 1 228 ? -4.536  53.668  2.385   1.00 52.79  ? 228 GLU B CB  1 
ATOM   6000  C CG  . GLU B 1 228 ? -3.636  54.877  2.350   1.00 68.01  ? 228 GLU B CG  1 
ATOM   6001  C CD  . GLU B 1 228 ? -3.736  55.698  3.618   1.00 76.11  ? 228 GLU B CD  1 
ATOM   6002  O OE1 . GLU B 1 228 ? -2.771  55.698  4.410   1.00 74.38  ? 228 GLU B OE1 1 
ATOM   6003  O OE2 . GLU B 1 228 ? -4.789  56.337  3.827   1.00 87.14  ? 228 GLU B OE2 1 
ATOM   6004  N N   . ASP B 1 229 ? -5.915  51.270  4.129   1.00 60.71  ? 229 ASP B N   1 
ATOM   6005  C CA  . ASP B 1 229 ? -6.908  50.876  5.120   1.00 62.40  ? 229 ASP B CA  1 
ATOM   6006  C C   . ASP B 1 229 ? -6.246  50.297  6.364   1.00 57.18  ? 229 ASP B C   1 
ATOM   6007  O O   . ASP B 1 229 ? -6.736  50.505  7.481   1.00 55.04  ? 229 ASP B O   1 
ATOM   6008  C CB  . ASP B 1 229 ? -7.894  49.882  4.502   1.00 59.30  ? 229 ASP B CB  1 
ATOM   6009  C CG  . ASP B 1 229 ? -8.929  50.565  3.614   1.00 68.86  ? 229 ASP B CG  1 
ATOM   6010  O OD1 . ASP B 1 229 ? -8.672  51.704  3.159   1.00 68.62  ? 229 ASP B OD1 1 
ATOM   6011  O OD2 . ASP B 1 229 ? -9.990  49.960  3.354   1.00 68.27  ? 229 ASP B OD2 1 
ATOM   6012  N N   . ALA B 1 230 ? -5.123  49.595  6.198   1.00 51.54  ? 230 ALA B N   1 
ATOM   6013  C CA  . ALA B 1 230 ? -4.402  49.084  7.358   1.00 54.84  ? 230 ALA B CA  1 
ATOM   6014  C C   . ALA B 1 230 ? -3.866  50.224  8.216   1.00 54.48  ? 230 ALA B C   1 
ATOM   6015  O O   . ALA B 1 230 ? -3.936  50.167  9.451   1.00 56.44  ? 230 ALA B O   1 
ATOM   6016  C CB  . ALA B 1 230 ? -3.266  48.168  6.911   1.00 56.08  ? 230 ALA B CB  1 
ATOM   6017  N N   . SER B 1 231 ? -3.337  51.272  7.581   1.00 50.63  ? 231 SER B N   1 
ATOM   6018  C CA  . SER B 1 231 ? -2.910  52.447  8.331   1.00 56.61  ? 231 SER B CA  1 
ATOM   6019  C C   . SER B 1 231 ? -4.081  53.116  9.034   1.00 56.99  ? 231 SER B C   1 
ATOM   6020  O O   . SER B 1 231 ? -3.914  53.669  10.127  1.00 54.16  ? 231 SER B O   1 
ATOM   6021  C CB  . SER B 1 231 ? -2.219  53.441  7.403   1.00 60.97  ? 231 SER B CB  1 
ATOM   6022  O OG  . SER B 1 231 ? -1.123  52.824  6.759   1.00 71.68  ? 231 SER B OG  1 
ATOM   6023  N N   . LYS B 1 232 ? -5.270  53.079  8.425   1.00 57.87  ? 232 LYS B N   1 
ATOM   6024  C CA  . LYS B 1 232 ? -6.434  53.691  9.057   1.00 56.90  ? 232 LYS B CA  1 
ATOM   6025  C C   . LYS B 1 232 ? -6.836  52.932  10.312  1.00 49.32  ? 232 LYS B C   1 
ATOM   6026  O O   . LYS B 1 232 ? -7.116  53.543  11.349  1.00 45.75  ? 232 LYS B O   1 
ATOM   6027  C CB  . LYS B 1 232 ? -7.597  53.764  8.064   1.00 50.48  ? 232 LYS B CB  1 
ATOM   6028  C CG  . LYS B 1 232 ? -7.395  54.808  6.982   1.00 54.47  ? 232 LYS B CG  1 
ATOM   6029  C CD  . LYS B 1 232 ? -8.644  55.038  6.140   1.00 64.19  ? 232 LYS B CD  1 
ATOM   6030  C CE  . LYS B 1 232 ? -8.299  55.062  4.651   1.00 66.63  ? 232 LYS B CE  1 
ATOM   6031  N NZ  . LYS B 1 232 ? -8.776  56.297  3.963   1.00 70.18  ? 232 LYS B NZ  1 
ATOM   6032  N N   . HIS B 1 233 ? -6.867  51.599  10.234  1.00 47.04  ? 233 HIS B N   1 
ATOM   6033  C CA  . HIS B 1 233 ? -7.236  50.797  11.394  1.00 48.16  ? 233 HIS B CA  1 
ATOM   6034  C C   . HIS B 1 233 ? -6.381  51.151  12.598  1.00 55.62  ? 233 HIS B C   1 
ATOM   6035  O O   . HIS B 1 233 ? -6.894  51.308  13.712  1.00 53.89  ? 233 HIS B O   1 
ATOM   6036  C CB  . HIS B 1 233 ? -7.102  49.311  11.072  1.00 50.93  ? 233 HIS B CB  1 
ATOM   6037  C CG  . HIS B 1 233 ? -8.209  48.772  10.223  1.00 54.44  ? 233 HIS B CG  1 
ATOM   6038  N ND1 . HIS B 1 233 ? -9.468  48.510  10.721  1.00 53.61  ? 233 HIS B ND1 1 
ATOM   6039  C CD2 . HIS B 1 233 ? -8.242  48.430  8.914   1.00 46.85  ? 233 HIS B CD2 1 
ATOM   6040  C CE1 . HIS B 1 233 ? -10.231 48.040  9.751   1.00 54.67  ? 233 HIS B CE1 1 
ATOM   6041  N NE2 . HIS B 1 233 ? -9.511  47.980  8.645   1.00 55.10  ? 233 HIS B NE2 1 
ATOM   6042  N N   . VAL B 1 234 ? -5.075  51.309  12.386  1.00 55.59  ? 234 VAL B N   1 
ATOM   6043  C CA  . VAL B 1 234 ? -4.176  51.580  13.499  1.00 48.11  ? 234 VAL B CA  1 
ATOM   6044  C C   . VAL B 1 234 ? -4.356  53.005  13.991  1.00 50.35  ? 234 VAL B C   1 
ATOM   6045  O O   . VAL B 1 234 ? -4.538  53.246  15.189  1.00 58.43  ? 234 VAL B O   1 
ATOM   6046  C CB  . VAL B 1 234 ? -2.722  51.311  13.088  1.00 50.24  ? 234 VAL B CB  1 
ATOM   6047  C CG1 . VAL B 1 234 ? -1.828  51.428  14.304  1.00 49.57  ? 234 VAL B CG1 1 
ATOM   6048  C CG2 . VAL B 1 234 ? -2.611  49.942  12.460  1.00 41.91  ? 234 VAL B CG2 1 
ATOM   6049  N N   . GLU B 1 235 ? -4.308  53.973  13.073  1.00 53.55  ? 235 GLU B N   1 
ATOM   6050  C CA  . GLU B 1 235 ? -4.415  55.374  13.472  1.00 58.05  ? 235 GLU B CA  1 
ATOM   6051  C C   . GLU B 1 235 ? -5.755  55.662  14.145  1.00 54.50  ? 235 GLU B C   1 
ATOM   6052  O O   . GLU B 1 235 ? -5.814  56.400  15.134  1.00 55.67  ? 235 GLU B O   1 
ATOM   6053  C CB  . GLU B 1 235 ? -4.208  56.289  12.261  1.00 59.58  ? 235 GLU B CB  1 
ATOM   6054  C CG  . GLU B 1 235 ? -2.837  56.148  11.597  1.00 66.93  ? 235 GLU B CG  1 
ATOM   6055  C CD  . GLU B 1 235 ? -2.183  57.483  11.265  1.00 81.98  ? 235 GLU B CD  1 
ATOM   6056  O OE1 . GLU B 1 235 ? -1.597  58.105  12.177  1.00 75.75  ? 235 GLU B OE1 1 
ATOM   6057  O OE2 . GLU B 1 235 ? -2.252  57.911  10.090  1.00 87.51  ? 235 GLU B OE2 1 
ATOM   6058  N N   . LEU B 1 236 ? -6.843  55.078  13.634  1.00 55.27  ? 236 LEU B N   1 
ATOM   6059  C CA  . LEU B 1 236 ? -8.146  55.295  14.258  1.00 52.51  ? 236 LEU B CA  1 
ATOM   6060  C C   . LEU B 1 236 ? -8.242  54.588  15.599  1.00 50.00  ? 236 LEU B C   1 
ATOM   6061  O O   . LEU B 1 236 ? -8.936  55.063  16.506  1.00 55.94  ? 236 LEU B O   1 
ATOM   6062  C CB  . LEU B 1 236 ? -9.265  54.823  13.333  1.00 48.71  ? 236 LEU B CB  1 
ATOM   6063  C CG  . LEU B 1 236 ? -9.413  55.640  12.049  1.00 47.74  ? 236 LEU B CG  1 
ATOM   6064  C CD1 . LEU B 1 236 ? -10.225 54.876  11.018  1.00 47.74  ? 236 LEU B CD1 1 
ATOM   6065  C CD2 . LEU B 1 236 ? -10.036 56.992  12.346  1.00 49.69  ? 236 LEU B CD2 1 
ATOM   6066  N N   . ALA B 1 237 ? -7.563  53.451  15.740  1.00 49.35  ? 237 ALA B N   1 
ATOM   6067  C CA  . ALA B 1 237 ? -7.496  52.800  17.040  1.00 48.66  ? 237 ALA B CA  1 
ATOM   6068  C C   . ALA B 1 237 ? -6.741  53.660  18.042  1.00 49.54  ? 237 ALA B C   1 
ATOM   6069  O O   . ALA B 1 237 ? -7.103  53.709  19.222  1.00 55.63  ? 237 ALA B O   1 
ATOM   6070  C CB  . ALA B 1 237 ? -6.840  51.427  16.910  1.00 45.89  ? 237 ALA B CB  1 
ATOM   6071  N N   . LYS B 1 238 ? -5.694  54.354  17.595  1.00 52.57  ? 238 LYS B N   1 
ATOM   6072  C CA  . LYS B 1 238 ? -4.950  55.199  18.519  1.00 55.13  ? 238 LYS B CA  1 
ATOM   6073  C C   . LYS B 1 238 ? -5.784  56.392  18.960  1.00 60.99  ? 238 LYS B C   1 
ATOM   6074  O O   . LYS B 1 238 ? -5.623  56.882  20.084  1.00 64.12  ? 238 LYS B O   1 
ATOM   6075  C CB  . LYS B 1 238 ? -3.640  55.649  17.874  1.00 57.09  ? 238 LYS B CB  1 
ATOM   6076  C CG  . LYS B 1 238 ? -2.769  54.487  17.414  1.00 56.62  ? 238 LYS B CG  1 
ATOM   6077  C CD  . LYS B 1 238 ? -1.509  54.949  16.693  1.00 57.59  ? 238 LYS B CD  1 
ATOM   6078  C CE  . LYS B 1 238 ? -0.989  56.267  17.244  1.00 55.70  ? 238 LYS B CE  1 
ATOM   6079  N NZ  . LYS B 1 238 ? 0.151   56.792  16.442  1.00 60.41  ? 238 LYS B NZ  1 
ATOM   6080  N N   . GLU B 1 239 ? -6.693  56.859  18.102  1.00 60.72  ? 239 GLU B N   1 
ATOM   6081  C CA  . GLU B 1 239 ? -7.584  57.943  18.499  1.00 64.98  ? 239 GLU B CA  1 
ATOM   6082  C C   . GLU B 1 239 ? -8.623  57.461  19.501  1.00 63.60  ? 239 GLU B C   1 
ATOM   6083  O O   . GLU B 1 239 ? -8.897  58.142  20.495  1.00 59.93  ? 239 GLU B O   1 
ATOM   6084  C CB  . GLU B 1 239 ? -8.262  58.547  17.273  1.00 63.55  ? 239 GLU B CB  1 
ATOM   6085  C CG  . GLU B 1 239 ? -7.374  59.511  16.510  1.00 80.79  ? 239 GLU B CG  1 
ATOM   6086  C CD  . GLU B 1 239 ? -6.878  60.666  17.370  1.00 94.76  ? 239 GLU B CD  1 
ATOM   6087  O OE1 . GLU B 1 239 ? -7.609  61.672  17.501  1.00 100.79 ? 239 GLU B OE1 1 
ATOM   6088  O OE2 . GLU B 1 239 ? -5.752  60.573  17.909  1.00 88.62  ? 239 GLU B OE2 1 
ATOM   6089  N N   . LYS B 1 240 ? -9.208  56.285  19.259  1.00 59.39  ? 240 LYS B N   1 
ATOM   6090  C CA  . LYS B 1 240 ? -10.170 55.743  20.209  1.00 61.53  ? 240 LYS B CA  1 
ATOM   6091  C C   . LYS B 1 240 ? -9.518  55.499  21.563  1.00 64.47  ? 240 LYS B C   1 
ATOM   6092  O O   . LYS B 1 240 ? -10.093 55.837  22.606  1.00 73.39  ? 240 LYS B O   1 
ATOM   6093  C CB  . LYS B 1 240 ? -10.782 54.456  19.662  1.00 50.93  ? 240 LYS B CB  1 
ATOM   6094  C CG  . LYS B 1 240 ? -12.038 54.008  20.394  1.00 55.58  ? 240 LYS B CG  1 
ATOM   6095  C CD  . LYS B 1 240 ? -13.269 54.755  19.913  1.00 55.02  ? 240 LYS B CD  1 
ATOM   6096  C CE  . LYS B 1 240 ? -14.162 55.159  21.077  1.00 66.16  ? 240 LYS B CE  1 
ATOM   6097  N NZ  . LYS B 1 240 ? -15.328 55.977  20.629  1.00 67.58  ? 240 LYS B NZ  1 
ATOM   6098  N N   . TYR B 1 241 ? -8.312  54.921  21.565  1.00 54.71  ? 241 TYR B N   1 
ATOM   6099  C CA  . TYR B 1 241 ? -7.595  54.713  22.820  1.00 58.21  ? 241 TYR B CA  1 
ATOM   6100  C C   . TYR B 1 241 ? -7.338  56.042  23.520  1.00 59.62  ? 241 TYR B C   1 
ATOM   6101  O O   . TYR B 1 241 ? -7.526  56.155  24.737  1.00 56.77  ? 241 TYR B O   1 
ATOM   6102  C CB  . TYR B 1 241 ? -6.284  53.956  22.564  1.00 53.82  ? 241 TYR B CB  1 
ATOM   6103  C CG  . TYR B 1 241 ? -5.548  53.519  23.824  1.00 51.27  ? 241 TYR B CG  1 
ATOM   6104  C CD1 . TYR B 1 241 ? -4.678  54.380  24.479  1.00 51.50  ? 241 TYR B CD1 1 
ATOM   6105  C CD2 . TYR B 1 241 ? -5.720  52.245  24.353  1.00 52.00  ? 241 TYR B CD2 1 
ATOM   6106  C CE1 . TYR B 1 241 ? -4.003  53.992  25.627  1.00 56.21  ? 241 TYR B CE1 1 
ATOM   6107  C CE2 . TYR B 1 241 ? -5.047  51.843  25.508  1.00 51.94  ? 241 TYR B CE2 1 
ATOM   6108  C CZ  . TYR B 1 241 ? -4.188  52.723  26.140  1.00 57.40  ? 241 TYR B CZ  1 
ATOM   6109  O OH  . TYR B 1 241 ? -3.510  52.345  27.285  1.00 52.57  ? 241 TYR B OH  1 
ATOM   6110  N N   . PHE B 1 242 ? -6.927  57.066  22.763  1.00 60.62  ? 242 PHE B N   1 
ATOM   6111  C CA  . PHE B 1 242 ? -6.706  58.384  23.352  1.00 61.15  ? 242 PHE B CA  1 
ATOM   6112  C C   . PHE B 1 242 ? -7.982  58.913  23.988  1.00 61.02  ? 242 PHE B C   1 
ATOM   6113  O O   . PHE B 1 242 ? -7.955  59.456  25.098  1.00 63.23  ? 242 PHE B O   1 
ATOM   6114  C CB  . PHE B 1 242 ? -6.186  59.361  22.294  1.00 62.43  ? 242 PHE B CB  1 
ATOM   6115  C CG  . PHE B 1 242 ? -5.988  60.770  22.805  1.00 65.88  ? 242 PHE B CG  1 
ATOM   6116  C CD1 . PHE B 1 242 ? -7.057  61.648  22.917  1.00 70.54  ? 242 PHE B CD1 1 
ATOM   6117  C CD2 . PHE B 1 242 ? -4.723  61.223  23.144  1.00 66.42  ? 242 PHE B CD2 1 
ATOM   6118  C CE1 . PHE B 1 242 ? -6.873  62.938  23.382  1.00 77.20  ? 242 PHE B CE1 1 
ATOM   6119  C CE2 . PHE B 1 242 ? -4.531  62.510  23.609  1.00 59.05  ? 242 PHE B CE2 1 
ATOM   6120  C CZ  . PHE B 1 242 ? -5.606  63.370  23.727  1.00 70.07  ? 242 PHE B CZ  1 
ATOM   6121  N N   . GLU B 1 243 ? -9.111  58.768  23.287  1.00 65.44  ? 243 GLU B N   1 
ATOM   6122  C CA  . GLU B 1 243 ? -10.382 59.265  23.807  1.00 65.75  ? 243 GLU B CA  1 
ATOM   6123  C C   . GLU B 1 243 ? -10.697 58.655  25.162  1.00 61.13  ? 243 GLU B C   1 
ATOM   6124  O O   . GLU B 1 243 ? -11.180 59.345  26.067  1.00 65.15  ? 243 GLU B O   1 
ATOM   6125  C CB  . GLU B 1 243 ? -11.511 58.970  22.820  1.00 70.30  ? 243 GLU B CB  1 
ATOM   6126  C CG  . GLU B 1 243 ? -11.356 59.643  21.465  1.00 77.46  ? 243 GLU B CG  1 
ATOM   6127  C CD  . GLU B 1 243 ? -11.752 61.107  21.485  1.00 87.86  ? 243 GLU B CD  1 
ATOM   6128  O OE1 . GLU B 1 243 ? -10.898 61.950  21.831  1.00 94.80  ? 243 GLU B OE1 1 
ATOM   6129  O OE2 . GLU B 1 243 ? -12.916 61.418  21.152  1.00 100.38 ? 243 GLU B OE2 1 
ATOM   6130  N N   . ILE B 1 244 ? -10.396 57.370  25.329  1.00 61.10  ? 244 ILE B N   1 
ATOM   6131  C CA  . ILE B 1 244 ? -10.717 56.683  26.573  1.00 64.49  ? 244 ILE B CA  1 
ATOM   6132  C C   . ILE B 1 244 ? -9.684  56.984  27.650  1.00 60.07  ? 244 ILE B C   1 
ATOM   6133  O O   . ILE B 1 244 ? -10.040 57.308  28.789  1.00 61.53  ? 244 ILE B O   1 
ATOM   6134  C CB  . ILE B 1 244 ? -10.844 55.171  26.329  1.00 62.41  ? 244 ILE B CB  1 
ATOM   6135  C CG1 . ILE B 1 244 ? -11.767 54.896  25.138  1.00 55.17  ? 244 ILE B CG1 1 
ATOM   6136  C CG2 . ILE B 1 244 ? -11.308 54.479  27.602  1.00 64.29  ? 244 ILE B CG2 1 
ATOM   6137  C CD1 . ILE B 1 244 ? -13.162 55.436  25.310  1.00 55.15  ? 244 ILE B CD1 1 
ATOM   6138  N N   . PHE B 1 245 ? -8.395  56.878  27.318  1.00 61.67  ? 245 PHE B N   1 
ATOM   6139  C CA  . PHE B 1 245 ? -7.339  56.889  28.328  1.00 65.15  ? 245 PHE B CA  1 
ATOM   6140  C C   . PHE B 1 245 ? -6.534  58.181  28.382  1.00 62.96  ? 245 PHE B C   1 
ATOM   6141  O O   . PHE B 1 245 ? -5.721  58.337  29.298  1.00 63.60  ? 245 PHE B O   1 
ATOM   6142  C CB  . PHE B 1 245 ? -6.377  55.715  28.104  1.00 64.59  ? 245 PHE B CB  1 
ATOM   6143  C CG  . PHE B 1 245 ? -7.045  54.377  28.149  1.00 59.27  ? 245 PHE B CG  1 
ATOM   6144  C CD1 . PHE B 1 245 ? -7.183  53.700  29.349  1.00 57.03  ? 245 PHE B CD1 1 
ATOM   6145  C CD2 . PHE B 1 245 ? -7.557  53.806  26.996  1.00 55.12  ? 245 PHE B CD2 1 
ATOM   6146  C CE1 . PHE B 1 245 ? -7.810  52.470  29.397  1.00 65.26  ? 245 PHE B CE1 1 
ATOM   6147  C CE2 . PHE B 1 245 ? -8.184  52.576  27.039  1.00 55.30  ? 245 PHE B CE2 1 
ATOM   6148  C CZ  . PHE B 1 245 ? -8.313  51.908  28.238  1.00 57.23  ? 245 PHE B CZ  1 
ATOM   6149  N N   . GLY B 1 246 ? -6.724  59.096  27.430  1.00 63.72  ? 246 GLY B N   1 
ATOM   6150  C CA  . GLY B 1 246 ? -6.029  60.363  27.435  1.00 59.74  ? 246 GLY B CA  1 
ATOM   6151  C C   . GLY B 1 246 ? -4.659  60.356  26.797  1.00 65.62  ? 246 GLY B C   1 
ATOM   6152  O O   . GLY B 1 246 ? -4.056  61.428  26.655  1.00 75.20  ? 246 GLY B O   1 
ATOM   6153  N N   . GLU B 1 247 ? -4.141  59.193  26.415  1.00 62.67  ? 247 GLU B N   1 
ATOM   6154  C CA  . GLU B 1 247 ? -2.820  59.086  25.816  1.00 59.13  ? 247 GLU B CA  1 
ATOM   6155  C C   . GLU B 1 247 ? -2.897  58.127  24.642  1.00 60.82  ? 247 GLU B C   1 
ATOM   6156  O O   . GLU B 1 247 ? -3.848  57.352  24.509  1.00 61.57  ? 247 GLU B O   1 
ATOM   6157  C CB  . GLU B 1 247 ? -1.772  58.597  26.828  1.00 70.30  ? 247 GLU B CB  1 
ATOM   6158  C CG  . GLU B 1 247 ? -2.275  57.494  27.759  1.00 73.35  ? 247 GLU B CG  1 
ATOM   6159  C CD  . GLU B 1 247 ? -1.354  57.252  28.947  1.00 76.47  ? 247 GLU B CD  1 
ATOM   6160  O OE1 . GLU B 1 247 ? -0.126  57.142  28.736  1.00 74.38  ? 247 GLU B OE1 1 
ATOM   6161  O OE2 . GLU B 1 247 ? -1.859  57.174  30.089  1.00 67.94  ? 247 GLU B OE2 1 
ATOM   6162  N N   . HIS B 1 248 ? -1.891  58.188  23.787  1.00 62.86  ? 248 HIS B N   1 
ATOM   6163  C CA  . HIS B 1 248 ? -1.856  57.243  22.685  1.00 54.44  ? 248 HIS B CA  1 
ATOM   6164  C C   . HIS B 1 248 ? -1.274  55.918  23.166  1.00 50.19  ? 248 HIS B C   1 
ATOM   6165  O O   . HIS B 1 248 ? -0.544  55.877  24.158  1.00 51.72  ? 248 HIS B O   1 
ATOM   6166  C CB  . HIS B 1 248 ? -1.035  57.801  21.531  1.00 51.20  ? 248 HIS B CB  1 
ATOM   6167  C CG  . HIS B 1 248 ? -1.826  58.668  20.602  1.00 62.27  ? 248 HIS B CG  1 
ATOM   6168  N ND1 . HIS B 1 248 ? -1.315  59.162  19.421  1.00 67.42  ? 248 HIS B ND1 1 
ATOM   6169  C CD2 . HIS B 1 248 ? -3.101  59.120  20.679  1.00 70.56  ? 248 HIS B CD2 1 
ATOM   6170  C CE1 . HIS B 1 248 ? -2.238  59.890  18.816  1.00 76.26  ? 248 HIS B CE1 1 
ATOM   6171  N NE2 . HIS B 1 248 ? -3.331  59.879  19.558  1.00 76.71  ? 248 HIS B NE2 1 
ATOM   6172  N N   . PRO B 1 249 ? -1.614  54.815  22.508  1.00 48.94  ? 249 PRO B N   1 
ATOM   6173  C CA  . PRO B 1 249 ? -1.134  53.514  22.973  1.00 40.92  ? 249 PRO B CA  1 
ATOM   6174  C C   . PRO B 1 249 ? 0.261   53.216  22.456  1.00 46.25  ? 249 PRO B C   1 
ATOM   6175  O O   . PRO B 1 249 ? 0.629   53.592  21.340  1.00 53.41  ? 249 PRO B O   1 
ATOM   6176  C CB  . PRO B 1 249 ? -2.159  52.541  22.388  1.00 44.08  ? 249 PRO B CB  1 
ATOM   6177  C CG  . PRO B 1 249 ? -2.558  53.193  21.108  1.00 50.12  ? 249 PRO B CG  1 
ATOM   6178  C CD  . PRO B 1 249 ? -2.574  54.677  21.397  1.00 55.29  ? 249 PRO B CD  1 
ATOM   6179  N N   . VAL B 1 250 ? 1.043   52.535  23.290  1.00 46.38  ? 250 VAL B N   1 
ATOM   6180  C CA  . VAL B 1 250 ? 2.353   52.043  22.890  1.00 49.34  ? 250 VAL B CA  1 
ATOM   6181  C C   . VAL B 1 250 ? 2.381   50.527  22.703  1.00 50.51  ? 250 VAL B C   1 
ATOM   6182  O O   . VAL B 1 250 ? 3.340   50.016  22.104  1.00 48.62  ? 250 VAL B O   1 
ATOM   6183  C CB  . VAL B 1 250 ? 3.440   52.476  23.895  1.00 48.83  ? 250 VAL B CB  1 
ATOM   6184  C CG1 . VAL B 1 250 ? 3.750   53.942  23.707  1.00 41.71  ? 250 VAL B CG1 1 
ATOM   6185  C CG2 . VAL B 1 250 ? 2.987   52.194  25.326  1.00 40.54  ? 250 VAL B CG2 1 
ATOM   6186  N N   . TYR B 1 251 ? 1.371   49.797  23.192  1.00 52.23  ? 251 TYR B N   1 
ATOM   6187  C CA  . TYR B 1 251 ? 1.282   48.345  23.073  1.00 45.08  ? 251 TYR B CA  1 
ATOM   6188  C C   . TYR B 1 251 ? 0.027   47.986  22.292  1.00 49.48  ? 251 TYR B C   1 
ATOM   6189  O O   . TYR B 1 251 ? -1.033  48.594  22.480  1.00 51.65  ? 251 TYR B O   1 
ATOM   6190  C CB  . TYR B 1 251 ? 1.263   47.649  24.458  1.00 45.62  ? 251 TYR B CB  1 
ATOM   6191  C CG  . TYR B 1 251 ? 2.286   48.218  25.412  1.00 51.98  ? 251 TYR B CG  1 
ATOM   6192  C CD1 . TYR B 1 251 ? 3.639   48.181  25.102  1.00 61.84  ? 251 TYR B CD1 1 
ATOM   6193  C CD2 . TYR B 1 251 ? 1.903   48.824  26.604  1.00 49.79  ? 251 TYR B CD2 1 
ATOM   6194  C CE1 . TYR B 1 251 ? 4.586   48.722  25.955  1.00 62.36  ? 251 TYR B CE1 1 
ATOM   6195  C CE2 . TYR B 1 251 ? 2.849   49.372  27.468  1.00 56.42  ? 251 TYR B CE2 1 
ATOM   6196  C CZ  . TYR B 1 251 ? 4.188   49.317  27.136  1.00 63.50  ? 251 TYR B CZ  1 
ATOM   6197  O OH  . TYR B 1 251 ? 5.140   49.854  27.975  1.00 74.01  ? 251 TYR B OH  1 
ATOM   6198  N N   . MET B 1 252 ? 0.154   46.998  21.414  1.00 49.87  ? 252 MET B N   1 
ATOM   6199  C CA  . MET B 1 252 ? -0.923  46.614  20.519  1.00 49.14  ? 252 MET B CA  1 
ATOM   6200  C C   . MET B 1 252 ? -0.936  45.100  20.406  1.00 49.74  ? 252 MET B C   1 
ATOM   6201  O O   . MET B 1 252 ? 0.122   44.480  20.267  1.00 49.07  ? 252 MET B O   1 
ATOM   6202  C CB  . MET B 1 252 ? -0.746  47.250  19.131  1.00 48.88  ? 252 MET B CB  1 
ATOM   6203  C CG  . MET B 1 252 ? -2.057  47.546  18.420  1.00 51.28  ? 252 MET B CG  1 
ATOM   6204  S SD  . MET B 1 252 ? -1.973  48.812  17.148  1.00 64.19  ? 252 MET B SD  1 
ATOM   6205  C CE  . MET B 1 252 ? -2.841  50.182  17.903  1.00 43.96  ? 252 MET B CE  1 
ATOM   6206  N N   . TRP B 1 253 ? -2.129  44.503  20.495  1.00 51.57  ? 253 TRP B N   1 
ATOM   6207  C CA  . TRP B 1 253 ? -2.276  43.069  20.269  1.00 52.94  ? 253 TRP B CA  1 
ATOM   6208  C C   . TRP B 1 253 ? -2.677  42.841  18.823  1.00 46.91  ? 253 TRP B C   1 
ATOM   6209  O O   . TRP B 1 253 ? -3.773  43.267  18.429  1.00 46.47  ? 253 TRP B O   1 
ATOM   6210  C CB  . TRP B 1 253 ? -3.321  42.454  21.198  1.00 43.80  ? 253 TRP B CB  1 
ATOM   6211  C CG  . TRP B 1 253 ? -3.815  41.113  20.689  1.00 47.85  ? 253 TRP B CG  1 
ATOM   6212  C CD1 . TRP B 1 253 ? -5.029  40.847  20.116  1.00 44.85  ? 253 TRP B CD1 1 
ATOM   6213  C CD2 . TRP B 1 253 ? -3.093  39.875  20.682  1.00 43.22  ? 253 TRP B CD2 1 
ATOM   6214  N NE1 . TRP B 1 253 ? -5.107  39.520  19.761  1.00 39.53  ? 253 TRP B NE1 1 
ATOM   6215  C CE2 . TRP B 1 253 ? -3.932  38.901  20.098  1.00 42.40  ? 253 TRP B CE2 1 
ATOM   6216  C CE3 . TRP B 1 253 ? -1.820  39.493  21.117  1.00 43.33  ? 253 TRP B CE3 1 
ATOM   6217  C CZ2 . TRP B 1 253 ? -3.538  37.573  19.938  1.00 47.38  ? 253 TRP B CZ2 1 
ATOM   6218  C CZ3 . TRP B 1 253 ? -1.431  38.171  20.961  1.00 47.92  ? 253 TRP B CZ3 1 
ATOM   6219  C CH2 . TRP B 1 253 ? -2.286  37.228  20.376  1.00 51.99  ? 253 TRP B CH2 1 
ATOM   6220  N N   . PRO B 1 254 ? -1.848  42.205  18.001  1.00 48.00  ? 254 PRO B N   1 
ATOM   6221  C CA  . PRO B 1 254 ? -2.244  41.942  16.616  1.00 44.24  ? 254 PRO B CA  1 
ATOM   6222  C C   . PRO B 1 254 ? -3.407  40.969  16.578  1.00 39.90  ? 254 PRO B C   1 
ATOM   6223  O O   . PRO B 1 254 ? -3.387  39.939  17.268  1.00 42.92  ? 254 PRO B O   1 
ATOM   6224  C CB  . PRO B 1 254 ? -0.979  41.337  15.987  1.00 48.26  ? 254 PRO B CB  1 
ATOM   6225  C CG  . PRO B 1 254 ? -0.182  40.838  17.136  1.00 47.86  ? 254 PRO B CG  1 
ATOM   6226  C CD  . PRO B 1 254 ? -0.465  41.778  18.270  1.00 47.71  ? 254 PRO B CD  1 
ATOM   6227  N N   . PRO B 1 255 ? -4.453  41.280  15.815  1.00 38.92  ? 255 PRO B N   1 
ATOM   6228  C CA  . PRO B 1 255 ? -5.641  40.418  15.789  1.00 37.97  ? 255 PRO B CA  1 
ATOM   6229  C C   . PRO B 1 255 ? -5.308  39.026  15.278  1.00 36.95  ? 255 PRO B C   1 
ATOM   6230  O O   . PRO B 1 255 ? -4.683  38.866  14.231  1.00 45.83  ? 255 PRO B O   1 
ATOM   6231  C CB  . PRO B 1 255 ? -6.586  41.165  14.842  1.00 45.82  ? 255 PRO B CB  1 
ATOM   6232  C CG  . PRO B 1 255 ? -6.116  42.592  14.912  1.00 44.53  ? 255 PRO B CG  1 
ATOM   6233  C CD  . PRO B 1 255 ? -4.632  42.465  14.964  1.00 42.09  ? 255 PRO B CD  1 
ATOM   6234  N N   . GLN B 1 256 ? -5.741  38.014  16.028  1.00 42.57  ? 256 GLN B N   1 
ATOM   6235  C CA  . GLN B 1 256 ? -5.451  36.605  15.745  1.00 45.25  ? 256 GLN B CA  1 
ATOM   6236  C C   . GLN B 1 256 ? -3.956  36.304  15.783  1.00 44.87  ? 256 GLN B C   1 
ATOM   6237  O O   . GLN B 1 256 ? -3.504  35.343  15.155  1.00 48.23  ? 256 GLN B O   1 
ATOM   6238  C CB  . GLN B 1 256 ? -6.036  36.155  14.399  1.00 43.06  ? 256 GLN B CB  1 
ATOM   6239  C CG  . GLN B 1 256 ? -7.443  36.651  14.125  1.00 41.08  ? 256 GLN B CG  1 
ATOM   6240  C CD  . GLN B 1 256 ? -8.491  35.821  14.836  1.00 54.01  ? 256 GLN B CD  1 
ATOM   6241  O OE1 . GLN B 1 256 ? -8.186  34.770  15.411  1.00 53.62  ? 256 GLN B OE1 1 
ATOM   6242  N NE2 . GLN B 1 256 ? -9.729  36.302  14.831  1.00 53.78  ? 256 GLN B NE2 1 
ATOM   6243  N N   . ALA B 1 257 ? -3.187  37.116  16.515  1.00 45.39  ? 257 ALA B N   1 
ATOM   6244  C CA  . ALA B 1 257 ? -1.726  37.083  16.582  1.00 48.32  ? 257 ALA B CA  1 
ATOM   6245  C C   . ALA B 1 257 ? -1.063  37.220  15.213  1.00 52.88  ? 257 ALA B C   1 
ATOM   6246  O O   . ALA B 1 257 ? 0.143   36.950  15.081  1.00 55.20  ? 257 ALA B O   1 
ATOM   6247  C CB  . ALA B 1 257 ? -1.216  35.815  17.282  1.00 47.12  ? 257 ALA B CB  1 
ATOM   6248  N N   . SER B 1 258 ? -1.808  37.664  14.199  1.00 45.87  ? 258 SER B N   1 
ATOM   6249  C CA  . SER B 1 258 ? -1.318  37.637  12.827  1.00 52.16  ? 258 SER B CA  1 
ATOM   6250  C C   . SER B 1 258 ? -0.232  38.684  12.619  1.00 48.92  ? 258 SER B C   1 
ATOM   6251  O O   . SER B 1 258 ? -0.431  39.868  12.905  1.00 49.29  ? 258 SER B O   1 
ATOM   6252  C CB  . SER B 1 258 ? -2.474  37.853  11.849  1.00 55.37  ? 258 SER B CB  1 
ATOM   6253  O OG  . SER B 1 258 ? -3.447  38.732  12.392  1.00 64.19  ? 258 SER B OG  1 
ATOM   6254  N N   . VAL B 1 259 ? 0.923   38.243  12.121  1.00 53.87  ? 259 VAL B N   1 
ATOM   6255  C CA  . VAL B 1 259 ? 2.085   39.108  11.968  1.00 54.05  ? 259 VAL B CA  1 
ATOM   6256  C C   . VAL B 1 259 ? 2.762   38.820  10.636  1.00 52.24  ? 259 VAL B C   1 
ATOM   6257  O O   . VAL B 1 259 ? 2.666   37.720  10.085  1.00 49.67  ? 259 VAL B O   1 
ATOM   6258  C CB  . VAL B 1 259 ? 3.099   38.929  13.114  1.00 43.39  ? 259 VAL B CB  1 
ATOM   6259  C CG1 . VAL B 1 259 ? 2.668   39.725  14.326  1.00 50.91  ? 259 VAL B CG1 1 
ATOM   6260  C CG2 . VAL B 1 259 ? 3.251   37.462  13.451  1.00 50.05  ? 259 VAL B CG2 1 
ATOM   6261  N N   . SER B 1 260 ? 3.449   39.833  10.127  1.00 49.65  ? 260 SER B N   1 
ATOM   6262  C CA  . SER B 1 260 ? 4.275   39.721  8.942   1.00 49.70  ? 260 SER B CA  1 
ATOM   6263  C C   . SER B 1 260 ? 5.399   40.722  9.122   1.00 50.17  ? 260 SER B C   1 
ATOM   6264  O O   . SER B 1 260 ? 5.363   41.568  10.021  1.00 50.19  ? 260 SER B O   1 
ATOM   6265  C CB  . SER B 1 260 ? 3.476   39.986  7.652   1.00 49.92  ? 260 SER B CB  1 
ATOM   6266  O OG  . SER B 1 260 ? 3.163   41.363  7.490   1.00 51.69  ? 260 SER B OG  1 
ATOM   6267  N N   . ASN B 1 261 ? 6.418   40.612  8.275   1.00 40.62  ? 261 ASN B N   1 
ATOM   6268  C CA  . ASN B 1 261 ? 7.462   41.631  8.290   1.00 51.80  ? 261 ASN B CA  1 
ATOM   6269  C C   . ASN B 1 261 ? 6.884   43.014  8.016   1.00 55.71  ? 261 ASN B C   1 
ATOM   6270  O O   . ASN B 1 261 ? 7.321   44.009  8.609   1.00 57.17  ? 261 ASN B O   1 
ATOM   6271  C CB  . ASN B 1 261 ? 8.548   41.290  7.275   1.00 59.16  ? 261 ASN B CB  1 
ATOM   6272  C CG  . ASN B 1 261 ? 9.275   40.020  7.621   1.00 62.40  ? 261 ASN B CG  1 
ATOM   6273  O OD1 . ASN B 1 261 ? 9.768   39.861  8.740   1.00 58.20  ? 261 ASN B OD1 1 
ATOM   6274  N ND2 . ASN B 1 261 ? 9.366   39.107  6.657   1.00 58.26  ? 261 ASN B ND2 1 
ATOM   6275  N N   . GLU B 1 262 ? 5.878   43.087  7.141   1.00 57.65  ? 262 GLU B N   1 
ATOM   6276  C CA  . GLU B 1 262 ? 5.275   44.364  6.785   1.00 56.51  ? 262 GLU B CA  1 
ATOM   6277  C C   . GLU B 1 262 ? 4.373   44.882  7.900   1.00 61.18  ? 262 GLU B C   1 
ATOM   6278  O O   . GLU B 1 262 ? 4.395   46.077  8.232   1.00 65.98  ? 262 GLU B O   1 
ATOM   6279  C CB  . GLU B 1 262 ? 4.485   44.205  5.488   1.00 58.46  ? 262 GLU B CB  1 
ATOM   6280  C CG  . GLU B 1 262 ? 5.277   43.705  4.231   1.00 65.37  ? 262 GLU B CG  1 
ATOM   6281  C CD  . GLU B 1 262 ? 5.749   42.235  4.222   1.00 71.08  ? 262 GLU B CD  1 
ATOM   6282  O OE1 . GLU B 1 262 ? 5.973   41.719  3.087   1.00 79.14  ? 262 GLU B OE1 1 
ATOM   6283  O OE2 . GLU B 1 262 ? 5.884   41.618  5.313   1.00 73.75  ? 262 GLU B OE2 1 
ATOM   6284  N N   . ALA B 1 263 ? 3.528   44.005  8.446   1.00 54.98  ? 263 ALA B N   1 
ATOM   6285  C CA  . ALA B 1 263 ? 2.701   44.373  9.588   1.00 51.13  ? 263 ALA B CA  1 
ATOM   6286  C C   . ALA B 1 263 ? 3.556   44.961  10.705  1.00 54.85  ? 263 ALA B C   1 
ATOM   6287  O O   . ALA B 1 263 ? 3.260   46.039  11.234  1.00 54.56  ? 263 ALA B O   1 
ATOM   6288  C CB  . ALA B 1 263 ? 1.919   43.149  10.069  1.00 51.47  ? 263 ALA B CB  1 
ATOM   6289  N N   . LEU B 1 264 ? 4.659   44.291  11.038  1.00 51.45  ? 264 LEU B N   1 
ATOM   6290  C CA  . LEU B 1 264 ? 5.533   44.802  12.088  1.00 54.68  ? 264 LEU B CA  1 
ATOM   6291  C C   . LEU B 1 264 ? 6.080   46.177  11.726  1.00 60.28  ? 264 LEU B C   1 
ATOM   6292  O O   . LEU B 1 264 ? 6.284   47.026  12.604  1.00 61.33  ? 264 LEU B O   1 
ATOM   6293  C CB  . LEU B 1 264 ? 6.669   43.814  12.346  1.00 51.15  ? 264 LEU B CB  1 
ATOM   6294  C CG  . LEU B 1 264 ? 6.231   42.563  13.104  1.00 45.42  ? 264 LEU B CG  1 
ATOM   6295  C CD1 . LEU B 1 264 ? 7.181   41.425  12.826  1.00 36.55  ? 264 LEU B CD1 1 
ATOM   6296  C CD2 . LEU B 1 264 ? 6.163   42.857  14.586  1.00 47.78  ? 264 LEU B CD2 1 
ATOM   6297  N N   . GLU B 1 265 ? 6.303   46.425  10.431  1.00 56.17  ? 265 GLU B N   1 
ATOM   6298  C CA  . GLU B 1 265 ? 6.793   47.732  10.008  1.00 54.59  ? 265 GLU B CA  1 
ATOM   6299  C C   . GLU B 1 265 ? 5.728   48.805  10.194  1.00 57.15  ? 265 GLU B C   1 
ATOM   6300  O O   . GLU B 1 265 ? 6.046   49.951  10.535  1.00 57.14  ? 265 GLU B O   1 
ATOM   6301  C CB  . GLU B 1 265 ? 7.256   47.673  8.555   1.00 51.97  ? 265 GLU B CB  1 
ATOM   6302  C CG  . GLU B 1 265 ? 8.495   46.822  8.351   1.00 57.21  ? 265 GLU B CG  1 
ATOM   6303  C CD  . GLU B 1 265 ? 8.892   46.704  6.892   1.00 65.10  ? 265 GLU B CD  1 
ATOM   6304  O OE1 . GLU B 1 265 ? 9.024   45.561  6.409   1.00 61.40  ? 265 GLU B OE1 1 
ATOM   6305  O OE2 . GLU B 1 265 ? 9.078   47.746  6.227   1.00 73.19  ? 265 GLU B OE2 1 
ATOM   6306  N N   . LEU B 1 266 ? 4.457   48.453  9.988   1.00 55.17  ? 266 LEU B N   1 
ATOM   6307  C CA  . LEU B 1 266 ? 3.396   49.446  10.118  1.00 56.30  ? 266 LEU B CA  1 
ATOM   6308  C C   . LEU B 1 266 ? 3.184   49.829  11.576  1.00 51.19  ? 266 LEU B C   1 
ATOM   6309  O O   . LEU B 1 266 ? 3.004   51.009  11.896  1.00 51.93  ? 266 LEU B O   1 
ATOM   6310  C CB  . LEU B 1 266 ? 2.107   48.915  9.488   1.00 52.90  ? 266 LEU B CB  1 
ATOM   6311  C CG  . LEU B 1 266 ? 1.042   49.911  9.009   1.00 52.84  ? 266 LEU B CG  1 
ATOM   6312  C CD1 . LEU B 1 266 ? 0.285   50.529  10.165  1.00 52.11  ? 266 LEU B CD1 1 
ATOM   6313  C CD2 . LEU B 1 266 ? 1.668   51.008  8.162   1.00 60.64  ? 266 LEU B CD2 1 
ATOM   6314  N N   . TYR B 1 267 ? 3.211   48.849  12.475  1.00 52.44  ? 267 TYR B N   1 
ATOM   6315  C CA  . TYR B 1 267 ? 3.078   49.160  13.891  1.00 59.98  ? 267 TYR B CA  1 
ATOM   6316  C C   . TYR B 1 267 ? 4.216   50.056  14.367  1.00 55.20  ? 267 TYR B C   1 
ATOM   6317  O O   . TYR B 1 267 ? 3.998   50.977  15.164  1.00 54.32  ? 267 TYR B O   1 
ATOM   6318  C CB  . TYR B 1 267 ? 3.034   47.875  14.707  1.00 56.60  ? 267 TYR B CB  1 
ATOM   6319  C CG  . TYR B 1 267 ? 1.833   47.003  14.442  1.00 57.13  ? 267 TYR B CG  1 
ATOM   6320  C CD1 . TYR B 1 267 ? 0.550   47.436  14.752  1.00 54.24  ? 267 TYR B CD1 1 
ATOM   6321  C CD2 . TYR B 1 267 ? 1.983   45.730  13.912  1.00 53.34  ? 267 TYR B CD2 1 
ATOM   6322  C CE1 . TYR B 1 267 ? -0.556  46.619  14.527  1.00 52.45  ? 267 TYR B CE1 1 
ATOM   6323  C CE2 . TYR B 1 267 ? 0.896   44.913  13.686  1.00 50.34  ? 267 TYR B CE2 1 
ATOM   6324  C CZ  . TYR B 1 267 ? -0.373  45.354  13.993  1.00 53.81  ? 267 TYR B CZ  1 
ATOM   6325  O OH  . TYR B 1 267 ? -1.443  44.514  13.755  1.00 50.80  ? 267 TYR B OH  1 
ATOM   6326  N N   . TYR B 1 268 ? 5.436   49.806  13.879  1.00 52.97  ? 268 TYR B N   1 
ATOM   6327  C CA  . TYR B 1 268 ? 6.564   50.656  14.249  1.00 60.12  ? 268 TYR B CA  1 
ATOM   6328  C C   . TYR B 1 268 ? 6.351   52.082  13.760  1.00 56.42  ? 268 TYR B C   1 
ATOM   6329  O O   . TYR B 1 268 ? 6.572   53.040  14.509  1.00 58.94  ? 268 TYR B O   1 
ATOM   6330  C CB  . TYR B 1 268 ? 7.873   50.080  13.694  1.00 57.99  ? 268 TYR B CB  1 
ATOM   6331  C CG  . TYR B 1 268 ? 9.047   51.052  13.646  1.00 58.35  ? 268 TYR B CG  1 
ATOM   6332  C CD1 . TYR B 1 268 ? 9.776   51.366  14.793  1.00 60.54  ? 268 TYR B CD1 1 
ATOM   6333  C CD2 . TYR B 1 268 ? 9.445   51.633  12.447  1.00 55.68  ? 268 TYR B CD2 1 
ATOM   6334  C CE1 . TYR B 1 268 ? 10.867  52.251  14.745  1.00 55.32  ? 268 TYR B CE1 1 
ATOM   6335  C CE2 . TYR B 1 268 ? 10.530  52.517  12.388  1.00 60.77  ? 268 TYR B CE2 1 
ATOM   6336  C CZ  . TYR B 1 268 ? 11.238  52.823  13.536  1.00 63.78  ? 268 TYR B CZ  1 
ATOM   6337  O OH  . TYR B 1 268 ? 12.309  53.699  13.459  1.00 62.05  ? 268 TYR B OH  1 
ATOM   6338  N N   . GLU B 1 269 ? 5.898   52.242  12.511  1.00 52.57  ? 269 GLU B N   1 
ATOM   6339  C CA  . GLU B 1 269 ? 5.724   53.573  11.942  1.00 51.13  ? 269 GLU B CA  1 
ATOM   6340  C C   . GLU B 1 269 ? 4.566   54.324  12.577  1.00 50.64  ? 269 GLU B C   1 
ATOM   6341  O O   . GLU B 1 269 ? 4.482   55.549  12.438  1.00 51.06  ? 269 GLU B O   1 
ATOM   6342  C CB  . GLU B 1 269 ? 5.519   53.478  10.429  1.00 60.59  ? 269 GLU B CB  1 
ATOM   6343  C CG  . GLU B 1 269 ? 6.755   53.013  9.669   1.00 71.40  ? 269 GLU B CG  1 
ATOM   6344  C CD  . GLU B 1 269 ? 6.430   52.447  8.298   1.00 83.73  ? 269 GLU B CD  1 
ATOM   6345  O OE1 . GLU B 1 269 ? 7.207   51.598  7.810   1.00 85.08  ? 269 GLU B OE1 1 
ATOM   6346  O OE2 . GLU B 1 269 ? 5.401   52.844  7.709   1.00 86.36  ? 269 GLU B OE2 1 
ATOM   6347  N N   . LYS B 1 270 ? 3.675   53.629  13.277  1.00 52.91  ? 270 LYS B N   1 
ATOM   6348  C CA  . LYS B 1 270 ? 2.566   54.283  13.949  1.00 51.83  ? 270 LYS B CA  1 
ATOM   6349  C C   . LYS B 1 270 ? 2.774   54.368  15.455  1.00 50.47  ? 270 LYS B C   1 
ATOM   6350  O O   . LYS B 1 270 ? 1.824   54.644  16.194  1.00 51.85  ? 270 LYS B O   1 
ATOM   6351  C CB  . LYS B 1 270 ? 1.259   53.578  13.605  1.00 47.43  ? 270 LYS B CB  1 
ATOM   6352  C CG  . LYS B 1 270 ? 1.041   53.462  12.111  1.00 52.06  ? 270 LYS B CG  1 
ATOM   6353  C CD  . LYS B 1 270 ? 0.425   54.721  11.529  1.00 53.87  ? 270 LYS B CD  1 
ATOM   6354  C CE  . LYS B 1 270 ? 0.148   54.540  10.048  1.00 59.04  ? 270 LYS B CE  1 
ATOM   6355  N NZ  . LYS B 1 270 ? 0.924   55.481  9.199   1.00 64.75  ? 270 LYS B NZ  1 
ATOM   6356  N N   . GLY B 1 271 ? 4.000   54.154  15.919  1.00 45.28  ? 271 GLY B N   1 
ATOM   6357  C CA  . GLY B 1 271 ? 4.368   54.476  17.278  1.00 49.96  ? 271 GLY B CA  1 
ATOM   6358  C C   . GLY B 1 271 ? 4.353   53.325  18.254  1.00 53.02  ? 271 GLY B C   1 
ATOM   6359  O O   . GLY B 1 271 ? 4.650   53.543  19.434  1.00 62.76  ? 271 GLY B O   1 
ATOM   6360  N N   . ILE B 1 272 ? 4.038   52.113  17.810  1.00 49.93  ? 272 ILE B N   1 
ATOM   6361  C CA  . ILE B 1 272 ? 3.870   50.991  18.729  1.00 55.14  ? 272 ILE B CA  1 
ATOM   6362  C C   . ILE B 1 272 ? 5.229   50.380  19.040  1.00 54.37  ? 272 ILE B C   1 
ATOM   6363  O O   . ILE B 1 272 ? 5.953   49.964  18.130  1.00 56.84  ? 272 ILE B O   1 
ATOM   6364  C CB  . ILE B 1 272 ? 2.912   49.938  18.153  1.00 55.41  ? 272 ILE B CB  1 
ATOM   6365  C CG1 . ILE B 1 272 ? 1.637   50.616  17.644  1.00 54.73  ? 272 ILE B CG1 1 
ATOM   6366  C CG2 . ILE B 1 272 ? 2.604   48.876  19.205  1.00 42.79  ? 272 ILE B CG2 1 
ATOM   6367  C CD1 . ILE B 1 272 ? 0.748   51.148  18.749  1.00 45.37  ? 272 ILE B CD1 1 
ATOM   6368  N N   . ASN B 1 273 ? 5.565   50.305  20.331  1.00 50.55  ? 273 ASN B N   1 
ATOM   6369  C CA  . ASN B 1 273 ? 6.832   49.725  20.754  1.00 47.37  ? 273 ASN B CA  1 
ATOM   6370  C C   . ASN B 1 273 ? 6.778   48.218  20.971  1.00 51.10  ? 273 ASN B C   1 
ATOM   6371  O O   . ASN B 1 273 ? 7.825   47.571  20.916  1.00 62.21  ? 273 ASN B O   1 
ATOM   6372  C CB  . ASN B 1 273 ? 7.334   50.368  22.056  1.00 55.77  ? 273 ASN B CB  1 
ATOM   6373  C CG  . ASN B 1 273 ? 7.250   51.887  22.050  1.00 61.20  ? 273 ASN B CG  1 
ATOM   6374  O OD1 . ASN B 1 273 ? 7.020   52.505  23.092  1.00 62.24  ? 273 ASN B OD1 1 
ATOM   6375  N ND2 . ASN B 1 273 ? 7.438   52.494  20.881  1.00 52.30  ? 273 ASN B ND2 1 
ATOM   6376  N N   . MET B 1 274 ? 5.609   47.637  21.231  1.00 56.69  ? 274 MET B N   1 
ATOM   6377  C CA  . MET B 1 274 ? 5.564   46.229  21.603  1.00 50.99  ? 274 MET B CA  1 
ATOM   6378  C C   . MET B 1 274 ? 4.260   45.603  21.130  1.00 49.21  ? 274 MET B C   1 
ATOM   6379  O O   . MET B 1 274 ? 3.196   46.222  21.212  1.00 49.97  ? 274 MET B O   1 
ATOM   6380  C CB  . MET B 1 274 ? 5.702   46.051  23.120  1.00 54.36  ? 274 MET B CB  1 
ATOM   6381  C CG  . MET B 1 274 ? 5.880   44.604  23.573  1.00 57.21  ? 274 MET B CG  1 
ATOM   6382  S SD  . MET B 1 274 ? 4.320   43.853  24.065  1.00 60.75  ? 274 MET B SD  1 
ATOM   6383  C CE  . MET B 1 274 ? 4.379   44.033  25.851  1.00 52.97  ? 274 MET B CE  1 
ATOM   6384  N N   . LEU B 1 275 ? 4.359   44.377  20.627  1.00 42.02  ? 275 LEU B N   1 
ATOM   6385  C CA  . LEU B 1 275 ? 3.208   43.553  20.314  1.00 42.91  ? 275 LEU B CA  1 
ATOM   6386  C C   . LEU B 1 275 ? 3.551   42.123  20.696  1.00 54.47  ? 275 LEU B C   1 
ATOM   6387  O O   . LEU B 1 275 ? 4.640   41.841  21.211  1.00 47.78  ? 275 LEU B O   1 
ATOM   6388  C CB  . LEU B 1 275 ? 2.803   43.669  18.840  1.00 43.31  ? 275 LEU B CB  1 
ATOM   6389  C CG  . LEU B 1 275 ? 3.822   43.351  17.752  1.00 57.29  ? 275 LEU B CG  1 
ATOM   6390  C CD1 . LEU B 1 275 ? 3.910   41.848  17.453  1.00 57.62  ? 275 LEU B CD1 1 
ATOM   6391  C CD2 . LEU B 1 275 ? 3.435   44.129  16.512  1.00 55.93  ? 275 LEU B CD2 1 
ATOM   6392  N N   . ALA B 1 276 ? 2.619   41.211  20.423  1.00 52.14  ? 276 ALA B N   1 
ATOM   6393  C CA  . ALA B 1 276 ? 2.741   39.838  20.891  1.00 54.44  ? 276 ALA B CA  1 
ATOM   6394  C C   . ALA B 1 276 ? 2.094   38.901  19.889  1.00 43.83  ? 276 ALA B C   1 
ATOM   6395  O O   . ALA B 1 276 ? 1.035   39.215  19.349  1.00 49.35  ? 276 ALA B O   1 
ATOM   6396  C CB  . ALA B 1 276 ? 2.080   39.650  22.262  1.00 47.44  ? 276 ALA B CB  1 
ATOM   6397  N N   . THR B 1 277 ? 2.701   37.736  19.677  1.00 38.52  ? 277 THR B N   1 
ATOM   6398  C CA  . THR B 1 277 ? 2.134   36.754  18.768  1.00 48.11  ? 277 THR B CA  1 
ATOM   6399  C C   . THR B 1 277 ? 2.315   35.357  19.362  1.00 40.71  ? 277 THR B C   1 
ATOM   6400  O O   . THR B 1 277 ? 2.761   35.201  20.502  1.00 39.49  ? 277 THR B O   1 
ATOM   6401  C CB  . THR B 1 277 ? 2.756   36.920  17.376  1.00 44.80  ? 277 THR B CB  1 
ATOM   6402  O OG1 . THR B 1 277 ? 2.147   36.011  16.451  1.00 51.25  ? 277 THR B OG1 1 
ATOM   6403  C CG2 . THR B 1 277 ? 4.238   36.688  17.438  1.00 42.04  ? 277 THR B CG2 1 
ATOM   6404  N N   . ASP B 1 278 ? 1.941   34.335  18.589  1.00 46.31  ? 278 ASP B N   1 
ATOM   6405  C CA  . ASP B 1 278 ? 1.961   32.954  19.055  1.00 52.69  ? 278 ASP B CA  1 
ATOM   6406  C C   . ASP B 1 278 ? 3.337   32.327  18.855  1.00 54.45  ? 278 ASP B C   1 
ATOM   6407  O O   . ASP B 1 278 ? 4.147   32.788  18.045  1.00 46.76  ? 278 ASP B O   1 
ATOM   6408  C CB  . ASP B 1 278 ? 0.905   32.116  18.331  1.00 49.95  ? 278 ASP B CB  1 
ATOM   6409  C CG  . ASP B 1 278 ? 0.714   30.761  18.972  1.00 55.22  ? 278 ASP B CG  1 
ATOM   6410  O OD1 . ASP B 1 278 ? 0.810   30.711  20.214  1.00 60.10  ? 278 ASP B OD1 1 
ATOM   6411  O OD2 . ASP B 1 278 ? 0.459   29.763  18.262  1.00 54.38  ? 278 ASP B OD2 1 
ATOM   6412  N N   . GLU B 1 279 ? 3.602   31.251  19.611  1.00 50.17  ? 279 GLU B N   1 
ATOM   6413  C CA  . GLU B 1 279 ? 4.902   30.602  19.483  1.00 57.59  ? 279 GLU B CA  1 
ATOM   6414  C C   . GLU B 1 279 ? 4.990   29.753  18.227  1.00 57.18  ? 279 GLU B C   1 
ATOM   6415  O O   . GLU B 1 279 ? 6.096   29.385  17.822  1.00 56.40  ? 279 GLU B O   1 
ATOM   6416  C CB  . GLU B 1 279 ? 5.239   29.761  20.723  1.00 56.84  ? 279 GLU B CB  1 
ATOM   6417  C CG  . GLU B 1 279 ? 4.204   28.740  21.161  1.00 58.00  ? 279 GLU B CG  1 
ATOM   6418  C CD  . GLU B 1 279 ? 4.719   27.852  22.292  1.00 68.19  ? 279 GLU B CD  1 
ATOM   6419  O OE1 . GLU B 1 279 ? 5.912   27.478  22.260  1.00 72.60  ? 279 GLU B OE1 1 
ATOM   6420  O OE2 . GLU B 1 279 ? 3.937   27.528  23.214  1.00 66.34  ? 279 GLU B OE2 1 
ATOM   6421  N N   . VAL B 1 280 ? 3.857   29.458  17.586  1.00 51.07  ? 280 VAL B N   1 
ATOM   6422  C CA  . VAL B 1 280 ? 3.915   28.775  16.299  1.00 55.73  ? 280 VAL B CA  1 
ATOM   6423  C C   . VAL B 1 280 ? 4.629   29.636  15.266  1.00 56.67  ? 280 VAL B C   1 
ATOM   6424  O O   . VAL B 1 280 ? 5.298   29.115  14.366  1.00 59.63  ? 280 VAL B O   1 
ATOM   6425  C CB  . VAL B 1 280 ? 2.502   28.396  15.829  1.00 57.09  ? 280 VAL B CB  1 
ATOM   6426  C CG1 . VAL B 1 280 ? 1.740   29.638  15.389  1.00 50.91  ? 280 VAL B CG1 1 
ATOM   6427  C CG2 . VAL B 1 280 ? 2.598   27.393  14.705  1.00 57.08  ? 280 VAL B CG2 1 
ATOM   6428  N N   . ILE B 1 281 ? 4.505   30.962  15.378  1.00 55.08  ? 281 ILE B N   1 
ATOM   6429  C CA  . ILE B 1 281 ? 5.214   31.867  14.480  1.00 51.42  ? 281 ILE B CA  1 
ATOM   6430  C C   . ILE B 1 281 ? 6.699   31.870  14.809  1.00 59.82  ? 281 ILE B C   1 
ATOM   6431  O O   . ILE B 1 281 ? 7.553   31.865  13.912  1.00 62.81  ? 281 ILE B O   1 
ATOM   6432  C CB  . ILE B 1 281 ? 4.605   33.280  14.565  1.00 42.02  ? 281 ILE B CB  1 
ATOM   6433  C CG1 . ILE B 1 281 ? 3.140   33.230  14.154  1.00 54.34  ? 281 ILE B CG1 1 
ATOM   6434  C CG2 . ILE B 1 281 ? 5.332   34.245  13.660  1.00 46.20  ? 281 ILE B CG2 1 
ATOM   6435  C CD1 . ILE B 1 281 ? 2.886   32.307  12.974  1.00 57.59  ? 281 ILE B CD1 1 
ATOM   6436  N N   . LEU B 1 282 ? 7.029   31.857  16.103  1.00 49.90  ? 282 LEU B N   1 
ATOM   6437  C CA  . LEU B 1 282 ? 8.426   31.866  16.512  1.00 51.63  ? 282 LEU B CA  1 
ATOM   6438  C C   . LEU B 1 282 ? 9.135   30.593  16.071  1.00 55.91  ? 282 LEU B C   1 
ATOM   6439  O O   . LEU B 1 282 ? 10.261  30.646  15.559  1.00 59.30  ? 282 LEU B O   1 
ATOM   6440  C CB  . LEU B 1 282 ? 8.516   32.044  18.026  1.00 49.44  ? 282 LEU B CB  1 
ATOM   6441  C CG  . LEU B 1 282 ? 9.900   31.915  18.641  1.00 47.25  ? 282 LEU B CG  1 
ATOM   6442  C CD1 . LEU B 1 282 ? 10.695  33.166  18.325  1.00 45.47  ? 282 LEU B CD1 1 
ATOM   6443  C CD2 . LEU B 1 282 ? 9.788   31.678  20.146  1.00 45.88  ? 282 LEU B CD2 1 
ATOM   6444  N N   . LYS B 1 283 ? 8.490   29.435  16.251  1.00 50.37  ? 283 LYS B N   1 
ATOM   6445  C CA  . LYS B 1 283 ? 9.113   28.185  15.826  1.00 56.91  ? 283 LYS B CA  1 
ATOM   6446  C C   . LYS B 1 283 ? 9.267   28.124  14.312  1.00 54.26  ? 283 LYS B C   1 
ATOM   6447  O O   . LYS B 1 283 ? 10.230  27.533  13.812  1.00 47.99  ? 283 LYS B O   1 
ATOM   6448  C CB  . LYS B 1 283 ? 8.309   26.983  16.330  1.00 53.46  ? 283 LYS B CB  1 
ATOM   6449  C CG  . LYS B 1 283 ? 7.965   27.048  17.800  1.00 54.95  ? 283 LYS B CG  1 
ATOM   6450  C CD  . LYS B 1 283 ? 9.105   26.577  18.660  1.00 51.85  ? 283 LYS B CD  1 
ATOM   6451  C CE  . LYS B 1 283 ? 9.073   27.233  20.031  1.00 56.44  ? 283 LYS B CE  1 
ATOM   6452  N NZ  . LYS B 1 283 ? 9.963   26.524  20.987  1.00 61.38  ? 283 LYS B NZ  1 
ATOM   6453  N N   . ASN B 1 284 ? 8.344   28.745  13.575  1.00 56.83  ? 284 ASN B N   1 
ATOM   6454  C CA  . ASN B 1 284 ? 8.416   28.768  12.120  1.00 53.58  ? 284 ASN B CA  1 
ATOM   6455  C C   . ASN B 1 284 ? 9.470   29.743  11.615  1.00 58.18  ? 284 ASN B C   1 
ATOM   6456  O O   . ASN B 1 284 ? 10.107  29.495  10.586  1.00 54.64  ? 284 ASN B O   1 
ATOM   6457  C CB  . ASN B 1 284 ? 7.056   29.135  11.544  1.00 48.59  ? 284 ASN B CB  1 
ATOM   6458  C CG  . ASN B 1 284 ? 6.108   27.991  11.574  1.00 60.17  ? 284 ASN B CG  1 
ATOM   6459  O OD1 . ASN B 1 284 ? 6.414   26.947  12.150  1.00 69.86  ? 284 ASN B OD1 1 
ATOM   6460  N ND2 . ASN B 1 284 ? 4.942   28.166  10.964  1.00 54.92  ? 284 ASN B ND2 1 
ATOM   6461  N N   . SER B 1 285 ? 9.650   30.864  12.304  1.00 55.51  ? 285 SER B N   1 
ATOM   6462  C CA  . SER B 1 285 ? 10.562  31.891  11.826  1.00 55.67  ? 285 SER B CA  1 
ATOM   6463  C C   . SER B 1 285 ? 11.973  31.739  12.386  1.00 56.50  ? 285 SER B C   1 
ATOM   6464  O O   . SER B 1 285 ? 12.940  32.063  11.689  1.00 58.17  ? 285 SER B O   1 
ATOM   6465  C CB  . SER B 1 285 ? 10.018  33.283  12.170  1.00 60.68  ? 285 SER B CB  1 
ATOM   6466  O OG  . SER B 1 285 ? 8.607   33.343  12.045  1.00 52.10  ? 285 SER B OG  1 
ATOM   6467  N N   . VAL B 1 286 ? 12.122  31.249  13.618  1.00 59.04  ? 286 VAL B N   1 
ATOM   6468  C CA  . VAL B 1 286 ? 13.421  31.102  14.271  1.00 58.84  ? 286 VAL B CA  1 
ATOM   6469  C C   . VAL B 1 286 ? 13.668  29.631  14.569  1.00 58.74  ? 286 VAL B C   1 
ATOM   6470  O O   . VAL B 1 286 ? 12.741  28.899  14.927  1.00 61.22  ? 286 VAL B O   1 
ATOM   6471  C CB  . VAL B 1 286 ? 13.514  31.931  15.567  1.00 56.48  ? 286 VAL B CB  1 
ATOM   6472  C CG1 . VAL B 1 286 ? 14.957  32.032  16.030  1.00 53.07  ? 286 VAL B CG1 1 
ATOM   6473  C CG2 . VAL B 1 286 ? 12.944  33.309  15.342  1.00 53.83  ? 286 VAL B CG2 1 
ATOM   6474  N N   . GLU B 1 287 ? 14.935  29.215  14.461  1.00 68.11  ? 287 GLU B N   1 
ATOM   6475  C CA  . GLU B 1 287 ? 15.330  27.807  14.457  1.00 72.36  ? 287 GLU B CA  1 
ATOM   6476  C C   . GLU B 1 287 ? 14.787  27.022  15.646  1.00 72.98  ? 287 GLU B C   1 
ATOM   6477  O O   . GLU B 1 287 ? 13.760  26.343  15.534  1.00 84.08  ? 287 GLU B O   1 
ATOM   6478  C CB  . GLU B 1 287 ? 16.856  27.685  14.418  1.00 71.35  ? 287 GLU B CB  1 
ATOM   6479  C CG  . GLU B 1 287 ? 17.585  28.694  15.300  1.00 84.74  ? 287 GLU B CG  1 
ATOM   6480  C CD  . GLU B 1 287 ? 18.973  28.234  15.728  1.00 106.46 ? 287 GLU B CD  1 
ATOM   6481  O OE1 . GLU B 1 287 ? 19.121  27.069  16.163  1.00 102.28 ? 287 GLU B OE1 1 
ATOM   6482  O OE2 . GLU B 1 287 ? 19.918  29.046  15.637  1.00 108.40 ? 287 GLU B OE2 1 
ATOM   6483  N N   . ARG B 1 288 ? 15.478  27.078  16.779  1.00 67.61  ? 288 ARG B N   1 
ATOM   6484  C CA  . ARG B 1 288 ? 15.058  26.379  17.988  1.00 71.18  ? 288 ARG B CA  1 
ATOM   6485  C C   . ARG B 1 288 ? 14.960  27.395  19.125  1.00 73.07  ? 288 ARG B C   1 
ATOM   6486  O O   . ARG B 1 288 ? 15.647  27.309  20.141  1.00 66.55  ? 288 ARG B O   1 
ATOM   6487  C CB  . ARG B 1 288 ? 16.023  25.238  18.305  1.00 66.81  ? 288 ARG B CB  1 
ATOM   6488  C CG  . ARG B 1 288 ? 16.197  24.237  17.162  1.00 73.12  ? 288 ARG B CG  1 
ATOM   6489  C CD  . ARG B 1 288 ? 17.488  23.424  17.297  1.00 69.89  ? 288 ARG B CD  1 
ATOM   6490  N NE  . ARG B 1 288 ? 17.329  22.251  18.147  1.00 71.69  ? 288 ARG B NE  1 
ATOM   6491  C CZ  . ARG B 1 288 ? 17.666  21.021  17.779  1.00 68.12  ? 288 ARG B CZ  1 
ATOM   6492  N NH1 . ARG B 1 288 ? 18.188  20.781  16.589  1.00 63.76  ? 288 ARG B NH1 1 
ATOM   6493  N NH2 . ARG B 1 288 ? 17.452  20.005  18.614  1.00 65.17  ? 288 ARG B NH2 1 
ATOM   6494  N N   . ALA B 1 289 ? 14.098  28.391  18.927  1.00 73.21  ? 289 ALA B N   1 
ATOM   6495  C CA  . ALA B 1 289 ? 13.974  29.497  19.862  1.00 68.77  ? 289 ALA B CA  1 
ATOM   6496  C C   . ALA B 1 289 ? 13.056  29.133  21.024  1.00 65.16  ? 289 ALA B C   1 
ATOM   6497  O O   . ALA B 1 289 ? 12.219  28.229  20.940  1.00 56.92  ? 289 ALA B O   1 
ATOM   6498  C CB  . ALA B 1 289 ? 13.449  30.746  19.151  1.00 53.01  ? 289 ALA B CB  1 
ATOM   6499  N N   . SER B 1 290 ? 13.233  29.852  22.125  1.00 60.28  ? 290 SER B N   1 
ATOM   6500  C CA  . SER B 1 290 ? 12.349  29.697  23.263  1.00 56.22  ? 290 SER B CA  1 
ATOM   6501  C C   . SER B 1 290 ? 11.457  30.918  23.395  1.00 55.80  ? 290 SER B C   1 
ATOM   6502  O O   . SER B 1 290 ? 11.916  32.046  23.210  1.00 55.61  ? 290 SER B O   1 
ATOM   6503  C CB  . SER B 1 290 ? 13.132  29.514  24.569  1.00 56.31  ? 290 SER B CB  1 
ATOM   6504  O OG  . SER B 1 290 ? 12.365  29.972  25.669  1.00 62.76  ? 290 SER B OG  1 
ATOM   6505  N N   . PRO B 1 291 ? 10.177  30.732  23.707  1.00 47.20  ? 291 PRO B N   1 
ATOM   6506  C CA  . PRO B 1 291 ? 9.288   31.870  23.929  1.00 50.71  ? 291 PRO B CA  1 
ATOM   6507  C C   . PRO B 1 291 ? 9.438   32.519  25.295  1.00 53.57  ? 291 PRO B C   1 
ATOM   6508  O O   . PRO B 1 291 ? 8.582   33.320  25.675  1.00 60.60  ? 291 PRO B O   1 
ATOM   6509  C CB  . PRO B 1 291 ? 7.907   31.220  23.777  1.00 51.13  ? 291 PRO B CB  1 
ATOM   6510  C CG  . PRO B 1 291 ? 8.098   29.876  24.380  1.00 57.09  ? 291 PRO B CG  1 
ATOM   6511  C CD  . PRO B 1 291 ? 9.475   29.451  23.896  1.00 50.71  ? 291 PRO B CD  1 
ATOM   6512  N N   . TYR B 1 292 ? 10.497  32.205  26.038  1.00 46.51  ? 292 TYR B N   1 
ATOM   6513  C CA  . TYR B 1 292 ? 10.694  32.742  27.378  1.00 51.47  ? 292 TYR B CA  1 
ATOM   6514  C C   . TYR B 1 292 ? 11.708  33.880  27.399  1.00 55.17  ? 292 TYR B C   1 
ATOM   6515  O O   . TYR B 1 292 ? 12.367  34.110  28.420  1.00 55.49  ? 292 TYR B O   1 
ATOM   6516  C CB  . TYR B 1 292 ? 11.104  31.624  28.336  1.00 50.26  ? 292 TYR B CB  1 
ATOM   6517  C CG  . TYR B 1 292 ? 10.136  30.472  28.332  1.00 47.65  ? 292 TYR B CG  1 
ATOM   6518  C CD1 . TYR B 1 292 ? 8.771   30.693  28.443  1.00 50.35  ? 292 TYR B CD1 1 
ATOM   6519  C CD2 . TYR B 1 292 ? 10.581  29.165  28.206  1.00 53.87  ? 292 TYR B CD2 1 
ATOM   6520  C CE1 . TYR B 1 292 ? 7.872   29.640  28.431  1.00 53.94  ? 292 TYR B CE1 1 
ATOM   6521  C CE2 . TYR B 1 292 ? 9.692   28.104  28.194  1.00 59.13  ? 292 TYR B CE2 1 
ATOM   6522  C CZ  . TYR B 1 292 ? 8.339   28.349  28.306  1.00 55.85  ? 292 TYR B CZ  1 
ATOM   6523  O OH  . TYR B 1 292 ? 7.455   27.297  28.296  1.00 61.78  ? 292 TYR B OH  1 
ATOM   6524  N N   . LEU B 1 293 ? 11.819  34.604  26.285  1.00 53.95  ? 293 LEU B N   1 
ATOM   6525  C CA  . LEU B 1 293 ? 12.752  35.706  26.109  1.00 49.33  ? 293 LEU B CA  1 
ATOM   6526  C C   . LEU B 1 293 ? 12.039  36.855  25.420  1.00 49.36  ? 293 LEU B C   1 
ATOM   6527  O O   . LEU B 1 293 ? 11.084  36.648  24.669  1.00 57.51  ? 293 LEU B O   1 
ATOM   6528  C CB  . LEU B 1 293 ? 13.963  35.297  25.257  1.00 51.20  ? 293 LEU B CB  1 
ATOM   6529  C CG  . LEU B 1 293 ? 14.813  34.142  25.777  1.00 50.67  ? 293 LEU B CG  1 
ATOM   6530  C CD1 . LEU B 1 293 ? 14.474  32.865  25.040  1.00 56.45  ? 293 LEU B CD1 1 
ATOM   6531  C CD2 . LEU B 1 293 ? 16.295  34.452  25.638  1.00 57.09  ? 293 LEU B CD2 1 
ATOM   6532  N N   . ARG B 1 294 ? 12.521  38.065  25.667  1.00 51.56  ? 294 ARG B N   1 
ATOM   6533  C CA  . ARG B 1 294 ? 12.057  39.223  24.917  1.00 53.26  ? 294 ARG B CA  1 
ATOM   6534  C C   . ARG B 1 294 ? 12.792  39.294  23.580  1.00 52.46  ? 294 ARG B C   1 
ATOM   6535  O O   . ARG B 1 294 ? 14.021  39.184  23.535  1.00 52.65  ? 294 ARG B O   1 
ATOM   6536  C CB  . ARG B 1 294 ? 12.282  40.502  25.722  1.00 53.48  ? 294 ARG B CB  1 
ATOM   6537  C CG  . ARG B 1 294 ? 11.960  41.753  24.931  1.00 54.13  ? 294 ARG B CG  1 
ATOM   6538  C CD  . ARG B 1 294 ? 12.593  43.006  25.521  1.00 68.22  ? 294 ARG B CD  1 
ATOM   6539  N NE  . ARG B 1 294 ? 12.293  43.214  26.935  1.00 68.48  ? 294 ARG B NE  1 
ATOM   6540  C CZ  . ARG B 1 294 ? 13.211  43.373  27.880  1.00 60.65  ? 294 ARG B CZ  1 
ATOM   6541  N NH1 . ARG B 1 294 ? 14.498  43.224  27.625  1.00 67.51  ? 294 ARG B NH1 1 
ATOM   6542  N NH2 . ARG B 1 294 ? 12.826  43.672  29.117  1.00 63.85  ? 294 ARG B NH2 1 
ATOM   6543  N N   . TYR B 1 295 ? 12.043  39.450  22.492  1.00 47.08  ? 295 TYR B N   1 
ATOM   6544  C CA  . TYR B 1 295 ? 12.611  39.559  21.156  1.00 46.75  ? 295 TYR B CA  1 
ATOM   6545  C C   . TYR B 1 295 ? 12.477  40.990  20.646  1.00 47.60  ? 295 TYR B C   1 
ATOM   6546  O O   . TYR B 1 295 ? 11.445  41.638  20.848  1.00 47.78  ? 295 TYR B O   1 
ATOM   6547  C CB  . TYR B 1 295 ? 11.938  38.573  20.186  1.00 43.12  ? 295 TYR B CB  1 
ATOM   6548  C CG  . TYR B 1 295 ? 12.321  37.131  20.452  1.00 48.49  ? 295 TYR B CG  1 
ATOM   6549  C CD1 . TYR B 1 295 ? 11.718  36.410  21.475  1.00 49.41  ? 295 TYR B CD1 1 
ATOM   6550  C CD2 . TYR B 1 295 ? 13.315  36.501  19.710  1.00 46.34  ? 295 TYR B CD2 1 
ATOM   6551  C CE1 . TYR B 1 295 ? 12.077  35.091  21.738  1.00 49.39  ? 295 TYR B CE1 1 
ATOM   6552  C CE2 . TYR B 1 295 ? 13.681  35.186  19.967  1.00 54.67  ? 295 TYR B CE2 1 
ATOM   6553  C CZ  . TYR B 1 295 ? 13.058  34.484  20.983  1.00 53.74  ? 295 TYR B CZ  1 
ATOM   6554  O OH  . TYR B 1 295 ? 13.419  33.178  21.246  1.00 52.55  ? 295 TYR B OH  1 
ATOM   6555  N N   . TYR B 1 296 ? 13.540  41.486  20.009  1.00 49.87  ? 296 TYR B N   1 
ATOM   6556  C CA  . TYR B 1 296 ? 13.547  42.785  19.337  1.00 52.24  ? 296 TYR B CA  1 
ATOM   6557  C C   . TYR B 1 296 ? 13.623  42.547  17.833  1.00 57.05  ? 296 TYR B C   1 
ATOM   6558  O O   . TYR B 1 296 ? 14.655  42.094  17.328  1.00 62.78  ? 296 TYR B O   1 
ATOM   6559  C CB  . TYR B 1 296 ? 14.721  43.653  19.787  1.00 50.68  ? 296 TYR B CB  1 
ATOM   6560  C CG  . TYR B 1 296 ? 14.481  44.399  21.069  1.00 59.60  ? 296 TYR B CG  1 
ATOM   6561  C CD1 . TYR B 1 296 ? 13.311  45.108  21.272  1.00 62.33  ? 296 TYR B CD1 1 
ATOM   6562  C CD2 . TYR B 1 296 ? 15.435  44.406  22.076  1.00 70.51  ? 296 TYR B CD2 1 
ATOM   6563  C CE1 . TYR B 1 296 ? 13.087  45.793  22.443  1.00 64.71  ? 296 TYR B CE1 1 
ATOM   6564  C CE2 . TYR B 1 296 ? 15.218  45.088  23.260  1.00 66.95  ? 296 TYR B CE2 1 
ATOM   6565  C CZ  . TYR B 1 296 ? 14.039  45.780  23.433  1.00 70.65  ? 296 TYR B CZ  1 
ATOM   6566  O OH  . TYR B 1 296 ? 13.798  46.471  24.594  1.00 81.34  ? 296 TYR B OH  1 
ATOM   6567  N N   . PHE B 1 297 ? 12.544  42.874  17.121  1.00 45.59  ? 297 PHE B N   1 
ATOM   6568  C CA  . PHE B 1 297 ? 12.492  42.762  15.664  1.00 44.23  ? 297 PHE B CA  1 
ATOM   6569  C C   . PHE B 1 297 ? 13.288  43.903  15.039  1.00 49.33  ? 297 PHE B C   1 
ATOM   6570  O O   . PHE B 1 297 ? 12.896  45.069  15.144  1.00 53.00  ? 297 PHE B O   1 
ATOM   6571  C CB  . PHE B 1 297 ? 11.039  42.788  15.198  1.00 48.02  ? 297 PHE B CB  1 
ATOM   6572  C CG  . PHE B 1 297 ? 10.839  42.561  13.714  1.00 45.79  ? 297 PHE B CG  1 
ATOM   6573  C CD1 . PHE B 1 297 ? 10.917  41.285  13.175  1.00 48.50  ? 297 PHE B CD1 1 
ATOM   6574  C CD2 . PHE B 1 297 ? 10.522  43.617  12.868  1.00 43.67  ? 297 PHE B CD2 1 
ATOM   6575  C CE1 . PHE B 1 297 ? 10.708  41.066  11.814  1.00 54.38  ? 297 PHE B CE1 1 
ATOM   6576  C CE2 . PHE B 1 297 ? 10.311  43.405  11.505  1.00 48.33  ? 297 PHE B CE2 1 
ATOM   6577  C CZ  . PHE B 1 297 ? 10.403  42.129  10.978  1.00 47.79  ? 297 PHE B CZ  1 
ATOM   6578  N N   . ARG B 1 298 ? 14.408  43.562  14.390  1.00 51.78  ? 298 ARG B N   1 
ATOM   6579  C CA  . ARG B 1 298 ? 15.236  44.510  13.627  1.00 48.03  ? 298 ARG B CA  1 
ATOM   6580  C C   . ARG B 1 298 ? 15.581  45.746  14.440  1.00 52.91  ? 298 ARG B C   1 
ATOM   6581  O O   . ARG B 1 298 ? 15.765  46.833  13.886  1.00 63.31  ? 298 ARG B O   1 
ATOM   6582  C CB  . ARG B 1 298 ? 14.562  44.911  12.316  1.00 42.97  ? 298 ARG B CB  1 
ATOM   6583  C CG  . ARG B 1 298 ? 14.163  43.735  11.445  1.00 48.50  ? 298 ARG B CG  1 
ATOM   6584  C CD  . ARG B 1 298 ? 13.786  44.156  10.035  1.00 43.63  ? 298 ARG B CD  1 
ATOM   6585  N NE  . ARG B 1 298 ? 13.320  43.010  9.268   1.00 52.86  ? 298 ARG B NE  1 
ATOM   6586  C CZ  . ARG B 1 298 ? 12.419  43.075  8.296   1.00 60.27  ? 298 ARG B CZ  1 
ATOM   6587  N NH1 . ARG B 1 298 ? 11.928  44.233  7.886   1.00 48.33  ? 298 ARG B NH1 1 
ATOM   6588  N NH2 . ARG B 1 298 ? 11.979  41.947  7.739   1.00 62.88  ? 298 ARG B NH2 1 
ATOM   6589  N N   . GLU B 1 299 ? 15.658  45.585  15.763  1.00 48.30  ? 299 GLU B N   1 
ATOM   6590  C CA  . GLU B 1 299 ? 15.984  46.676  16.675  1.00 59.56  ? 299 GLU B CA  1 
ATOM   6591  C C   . GLU B 1 299 ? 14.914  47.761  16.650  1.00 58.92  ? 299 GLU B C   1 
ATOM   6592  O O   . GLU B 1 299 ? 15.076  48.806  17.290  1.00 63.98  ? 299 GLU B O   1 
ATOM   6593  C CB  . GLU B 1 299 ? 17.346  47.284  16.341  1.00 69.48  ? 299 GLU B CB  1 
ATOM   6594  C CG  . GLU B 1 299 ? 18.424  46.286  15.902  1.00 79.80  ? 299 GLU B CG  1 
ATOM   6595  C CD  . GLU B 1 299 ? 19.522  46.108  16.932  1.00 82.74  ? 299 GLU B CD  1 
ATOM   6596  O OE1 . GLU B 1 299 ? 19.504  46.844  17.939  1.00 80.65  ? 299 GLU B OE1 1 
ATOM   6597  O OE2 . GLU B 1 299 ? 20.435  45.280  16.703  1.00 78.42  ? 299 GLU B OE2 1 
ATOM   6598  N N   . LEU B 1 300 ? 13.819  47.530  15.920  1.00 58.82  ? 300 LEU B N   1 
ATOM   6599  C CA  . LEU B 1 300 ? 12.779  48.545  15.780  1.00 60.07  ? 300 LEU B CA  1 
ATOM   6600  C C   . LEU B 1 300 ? 11.621  48.355  16.750  1.00 52.85  ? 300 LEU B C   1 
ATOM   6601  O O   . LEU B 1 300 ? 11.053  49.343  17.229  1.00 52.73  ? 300 LEU B O   1 
ATOM   6602  C CB  . LEU B 1 300 ? 12.252  48.567  14.342  1.00 54.39  ? 300 LEU B CB  1 
ATOM   6603  C CG  . LEU B 1 300 ? 13.237  49.123  13.308  1.00 53.44  ? 300 LEU B CG  1 
ATOM   6604  C CD1 . LEU B 1 300 ? 12.502  49.595  12.065  1.00 56.17  ? 300 LEU B CD1 1 
ATOM   6605  C CD2 . LEU B 1 300 ? 14.078  50.255  13.895  1.00 50.86  ? 300 LEU B CD2 1 
ATOM   6606  N N   . ILE B 1 301 ? 11.260  47.112  17.058  1.00 52.31  ? 301 ILE B N   1 
ATOM   6607  C CA  . ILE B 1 301 ? 10.092  46.820  17.876  1.00 53.48  ? 301 ILE B CA  1 
ATOM   6608  C C   . ILE B 1 301 ? 10.415  45.635  18.769  1.00 51.43  ? 301 ILE B C   1 
ATOM   6609  O O   . ILE B 1 301 ? 11.375  44.898  18.542  1.00 60.39  ? 301 ILE B O   1 
ATOM   6610  C CB  . ILE B 1 301 ? 8.831   46.529  17.022  1.00 49.76  ? 301 ILE B CB  1 
ATOM   6611  C CG1 . ILE B 1 301 ? 7.550   46.898  17.774  1.00 56.47  ? 301 ILE B CG1 1 
ATOM   6612  C CG2 . ILE B 1 301 ? 8.774   45.073  16.609  1.00 48.96  ? 301 ILE B CG2 1 
ATOM   6613  C CD1 . ILE B 1 301 ? 6.301   46.794  16.917  1.00 56.58  ? 301 ILE B CD1 1 
ATOM   6614  N N   . SER B 1 302 ? 9.595   45.458  19.793  1.00 45.96  ? 302 SER B N   1 
ATOM   6615  C CA  . SER B 1 302 ? 9.742   44.366  20.737  1.00 48.44  ? 302 SER B CA  1 
ATOM   6616  C C   . SER B 1 302 ? 8.579   43.403  20.576  1.00 49.33  ? 302 SER B C   1 
ATOM   6617  O O   . SER B 1 302 ? 7.417   43.819  20.611  1.00 48.41  ? 302 SER B O   1 
ATOM   6618  C CB  . SER B 1 302 ? 9.794   44.891  22.168  1.00 48.92  ? 302 SER B CB  1 
ATOM   6619  O OG  . SER B 1 302 ? 9.807   43.811  23.080  1.00 55.17  ? 302 SER B OG  1 
ATOM   6620  N N   . VAL B 1 303 ? 8.889   42.122  20.398  1.00 45.54  ? 303 VAL B N   1 
ATOM   6621  C CA  . VAL B 1 303 ? 7.873   41.099  20.184  1.00 53.74  ? 303 VAL B CA  1 
ATOM   6622  C C   . VAL B 1 303 ? 7.998   40.043  21.268  1.00 50.85  ? 303 VAL B C   1 
ATOM   6623  O O   . VAL B 1 303 ? 9.074   39.467  21.458  1.00 54.52  ? 303 VAL B O   1 
ATOM   6624  C CB  . VAL B 1 303 ? 7.990   40.443  18.797  1.00 50.95  ? 303 VAL B CB  1 
ATOM   6625  C CG1 . VAL B 1 303 ? 6.909   39.394  18.654  1.00 46.20  ? 303 VAL B CG1 1 
ATOM   6626  C CG2 . VAL B 1 303 ? 7.907   41.485  17.676  1.00 45.41  ? 303 VAL B CG2 1 
ATOM   6627  N N   . PHE B 1 304 ? 6.893   39.771  21.954  1.00 53.17  ? 304 PHE B N   1 
ATOM   6628  C CA  . PHE B 1 304 ? 6.812   38.671  22.904  1.00 52.17  ? 304 PHE B CA  1 
ATOM   6629  C C   . PHE B 1 304 ? 5.986   37.549  22.284  1.00 47.54  ? 304 PHE B C   1 
ATOM   6630  O O   . PHE B 1 304 ? 4.912   37.796  21.728  1.00 42.28  ? 304 PHE B O   1 
ATOM   6631  C CB  . PHE B 1 304 ? 6.190   39.134  24.225  1.00 48.83  ? 304 PHE B CB  1 
ATOM   6632  C CG  . PHE B 1 304 ? 7.174   39.776  25.172  1.00 47.23  ? 304 PHE B CG  1 
ATOM   6633  C CD1 . PHE B 1 304 ? 8.080   39.003  25.885  1.00 50.07  ? 304 PHE B CD1 1 
ATOM   6634  C CD2 . PHE B 1 304 ? 7.200   41.153  25.344  1.00 42.56  ? 304 PHE B CD2 1 
ATOM   6635  C CE1 . PHE B 1 304 ? 8.992   39.595  26.758  1.00 45.47  ? 304 PHE B CE1 1 
ATOM   6636  C CE2 . PHE B 1 304 ? 8.108   41.747  26.212  1.00 46.39  ? 304 PHE B CE2 1 
ATOM   6637  C CZ  . PHE B 1 304 ? 9.003   40.970  26.919  1.00 42.03  ? 304 PHE B CZ  1 
ATOM   6638  N N   . PHE B 1 305 ? 6.492   36.327  22.360  1.00 47.79  ? 305 PHE B N   1 
ATOM   6639  C CA  . PHE B 1 305 ? 5.804   35.167  21.810  1.00 48.87  ? 305 PHE B CA  1 
ATOM   6640  C C   . PHE B 1 305 ? 5.138   34.390  22.938  1.00 51.86  ? 305 PHE B C   1 
ATOM   6641  O O   . PHE B 1 305 ? 5.801   33.992  23.901  1.00 56.32  ? 305 PHE B O   1 
ATOM   6642  C CB  . PHE B 1 305 ? 6.780   34.280  21.042  1.00 52.57  ? 305 PHE B CB  1 
ATOM   6643  C CG  . PHE B 1 305 ? 7.458   34.980  19.908  1.00 43.96  ? 305 PHE B CG  1 
ATOM   6644  C CD1 . PHE B 1 305 ? 8.644   35.664  20.105  1.00 47.18  ? 305 PHE B CD1 1 
ATOM   6645  C CD2 . PHE B 1 305 ? 6.899   34.971  18.649  1.00 45.01  ? 305 PHE B CD2 1 
ATOM   6646  C CE1 . PHE B 1 305 ? 9.265   36.318  19.057  1.00 51.28  ? 305 PHE B CE1 1 
ATOM   6647  C CE2 . PHE B 1 305 ? 7.517   35.619  17.594  1.00 48.38  ? 305 PHE B CE2 1 
ATOM   6648  C CZ  . PHE B 1 305 ? 8.698   36.293  17.798  1.00 45.53  ? 305 PHE B CZ  1 
ATOM   6649  N N   . ARG B 1 306 ? 3.835   34.166  22.806  1.00 47.96  ? 306 ARG B N   1 
ATOM   6650  C CA  . ARG B 1 306 ? 3.047   33.587  23.884  1.00 46.62  ? 306 ARG B CA  1 
ATOM   6651  C C   . ARG B 1 306 ? 3.368   32.105  24.085  1.00 47.17  ? 306 ARG B C   1 
ATOM   6652  O O   . ARG B 1 306 ? 3.879   31.419  23.196  1.00 50.69  ? 306 ARG B O   1 
ATOM   6653  C CB  . ARG B 1 306 ? 1.563   33.756  23.593  1.00 46.36  ? 306 ARG B CB  1 
ATOM   6654  C CG  . ARG B 1 306 ? 0.952   32.559  22.913  1.00 50.56  ? 306 ARG B CG  1 
ATOM   6655  C CD  . ARG B 1 306 ? -0.544  32.685  22.793  1.00 48.20  ? 306 ARG B CD  1 
ATOM   6656  N NE  . ARG B 1 306 ? -1.059  31.752  21.801  1.00 44.47  ? 306 ARG B NE  1 
ATOM   6657  C CZ  . ARG B 1 306 ? -2.208  31.105  21.913  1.00 54.68  ? 306 ARG B CZ  1 
ATOM   6658  N NH1 . ARG B 1 306 ? -3.006  31.291  22.956  1.00 52.65  ? 306 ARG B NH1 1 
ATOM   6659  N NH2 . ARG B 1 306 ? -2.571  30.260  20.950  1.00 61.55  ? 306 ARG B NH2 1 
ATOM   6660  N N   . ASP B 1 307 ? 3.056   31.614  25.284  1.00 50.12  ? 307 ASP B N   1 
ATOM   6661  C CA  . ASP B 1 307 ? 3.178   30.194  25.612  1.00 54.43  ? 307 ASP B CA  1 
ATOM   6662  C C   . ASP B 1 307 ? 1.879   29.502  25.226  1.00 63.09  ? 307 ASP B C   1 
ATOM   6663  O O   . ASP B 1 307 ? 0.906   29.519  25.985  1.00 64.57  ? 307 ASP B O   1 
ATOM   6664  C CB  . ASP B 1 307 ? 3.482   30.004  27.092  1.00 45.21  ? 307 ASP B CB  1 
ATOM   6665  C CG  . ASP B 1 307 ? 3.905   28.587  27.416  1.00 64.33  ? 307 ASP B CG  1 
ATOM   6666  O OD1 . ASP B 1 307 ? 3.262   27.636  26.917  1.00 64.22  ? 307 ASP B OD1 1 
ATOM   6667  O OD2 . ASP B 1 307 ? 4.907   28.422  28.146  1.00 67.44  ? 307 ASP B OD2 1 
ATOM   6668  N N   . LYS B 1 308 ? 1.868   28.879  24.043  1.00 56.07  ? 308 LYS B N   1 
ATOM   6669  C CA  . LYS B 1 308 ? 0.647   28.251  23.549  1.00 53.62  ? 308 LYS B CA  1 
ATOM   6670  C C   . LYS B 1 308 ? 0.118   27.216  24.535  1.00 54.93  ? 308 LYS B C   1 
ATOM   6671  O O   . LYS B 1 308 ? -1.092  27.135  24.767  1.00 53.72  ? 308 LYS B O   1 
ATOM   6672  C CB  . LYS B 1 308 ? 0.902   27.611  22.181  1.00 52.05  ? 308 LYS B CB  1 
ATOM   6673  C CG  . LYS B 1 308 ? -0.344  27.426  21.321  1.00 59.28  ? 308 LYS B CG  1 
ATOM   6674  C CD  . LYS B 1 308 ? -0.080  26.499  20.130  1.00 57.55  ? 308 LYS B CD  1 
ATOM   6675  C CE  . LYS B 1 308 ? -1.158  26.640  19.061  1.00 70.87  ? 308 LYS B CE  1 
ATOM   6676  N NZ  . LYS B 1 308 ? -2.361  25.790  19.321  1.00 66.91  ? 308 LYS B NZ  1 
ATOM   6677  N N   . THR B 1 309 ? 1.010   26.428  25.139  1.00 54.79  ? 309 THR B N   1 
ATOM   6678  C CA  . THR B 1 309 ? 0.562   25.303  25.955  1.00 52.95  ? 309 THR B CA  1 
ATOM   6679  C C   . THR B 1 309 ? -0.148  25.784  27.211  1.00 54.69  ? 309 THR B C   1 
ATOM   6680  O O   . THR B 1 309 ? -1.205  25.260  27.582  1.00 57.72  ? 309 THR B O   1 
ATOM   6681  C CB  . THR B 1 309 ? 1.743   24.406  26.319  1.00 57.09  ? 309 THR B CB  1 
ATOM   6682  O OG1 . THR B 1 309 ? 2.520   24.137  25.143  1.00 66.21  ? 309 THR B OG1 1 
ATOM   6683  C CG2 . THR B 1 309 ? 1.236   23.093  26.914  1.00 54.29  ? 309 THR B CG2 1 
ATOM   6684  N N   . LEU B 1 310 ? 0.419   26.785  27.881  1.00 51.43  ? 310 LEU B N   1 
ATOM   6685  C CA  . LEU B 1 310 ? -0.217  27.308  29.085  1.00 52.93  ? 310 LEU B CA  1 
ATOM   6686  C C   . LEU B 1 310 ? -1.507  28.046  28.752  1.00 51.13  ? 310 LEU B C   1 
ATOM   6687  O O   . LEU B 1 310 ? -2.520  27.885  29.445  1.00 54.35  ? 310 LEU B O   1 
ATOM   6688  C CB  . LEU B 1 310 ? 0.746   28.227  29.829  1.00 54.54  ? 310 LEU B CB  1 
ATOM   6689  C CG  . LEU B 1 310 ? 1.906   27.556  30.553  1.00 55.69  ? 310 LEU B CG  1 
ATOM   6690  C CD1 . LEU B 1 310 ? 2.916   28.620  30.886  1.00 51.12  ? 310 LEU B CD1 1 
ATOM   6691  C CD2 . LEU B 1 310 ? 1.438   26.824  31.813  1.00 61.94  ? 310 LEU B CD2 1 
ATOM   6692  N N   . SER B 1 311 ? -1.488  28.853  27.689  1.00 46.36  ? 311 SER B N   1 
ATOM   6693  C CA  . SER B 1 311 ? -2.678  29.590  27.278  1.00 48.06  ? 311 SER B CA  1 
ATOM   6694  C C   . SER B 1 311 ? -3.820  28.653  26.894  1.00 53.78  ? 311 SER B C   1 
ATOM   6695  O O   . SER B 1 311 ? -4.968  28.869  27.305  1.00 51.04  ? 311 SER B O   1 
ATOM   6696  C CB  . SER B 1 311 ? -2.338  30.516  26.113  1.00 50.25  ? 311 SER B CB  1 
ATOM   6697  O OG  . SER B 1 311 ? -1.446  31.538  26.520  1.00 55.51  ? 311 SER B OG  1 
ATOM   6698  N N   . ASP B 1 312 ? -3.531  27.612  26.104  1.00 49.51  ? 312 ASP B N   1 
ATOM   6699  C CA  . ASP B 1 312 ? -4.584  26.707  25.647  1.00 54.94  ? 312 ASP B CA  1 
ATOM   6700  C C   . ASP B 1 312 ? -5.097  25.803  26.758  1.00 52.24  ? 312 ASP B C   1 
ATOM   6701  O O   . ASP B 1 312 ? -6.233  25.319  26.674  1.00 54.23  ? 312 ASP B O   1 
ATOM   6702  C CB  . ASP B 1 312 ? -4.090  25.860  24.474  1.00 49.54  ? 312 ASP B CB  1 
ATOM   6703  C CG  . ASP B 1 312 ? -3.873  26.679  23.218  1.00 58.02  ? 312 ASP B CG  1 
ATOM   6704  O OD1 . ASP B 1 312 ? -4.245  27.875  23.210  1.00 51.74  ? 312 ASP B OD1 1 
ATOM   6705  O OD2 . ASP B 1 312 ? -3.328  26.127  22.238  1.00 65.80  ? 312 ASP B OD2 1 
ATOM   6706  N N   . LEU B 1 313 ? -4.288  25.556  27.787  1.00 51.62  ? 313 LEU B N   1 
ATOM   6707  C CA  . LEU B 1 313 ? -4.796  24.869  28.971  1.00 56.82  ? 313 LEU B CA  1 
ATOM   6708  C C   . LEU B 1 313 ? -5.929  25.659  29.619  1.00 56.60  ? 313 LEU B C   1 
ATOM   6709  O O   . LEU B 1 313 ? -6.988  25.100  29.933  1.00 50.33  ? 313 LEU B O   1 
ATOM   6710  C CB  . LEU B 1 313 ? -3.663  24.634  29.972  1.00 50.03  ? 313 LEU B CB  1 
ATOM   6711  C CG  . LEU B 1 313 ? -2.814  23.390  29.712  1.00 51.46  ? 313 LEU B CG  1 
ATOM   6712  C CD1 . LEU B 1 313 ? -1.413  23.585  30.258  1.00 54.42  ? 313 LEU B CD1 1 
ATOM   6713  C CD2 . LEU B 1 313 ? -3.462  22.147  30.311  1.00 48.77  ? 313 LEU B CD2 1 
ATOM   6714  N N   . ILE B 1 314 ? -5.718  26.962  29.838  1.00 55.35  ? 314 ILE B N   1 
ATOM   6715  C CA  . ILE B 1 314 ? -6.758  27.801  30.434  1.00 52.96  ? 314 ILE B CA  1 
ATOM   6716  C C   . ILE B 1 314 ? -7.960  27.878  29.509  1.00 49.26  ? 314 ILE B C   1 
ATOM   6717  O O   . ILE B 1 314 ? -9.107  27.686  29.928  1.00 59.95  ? 314 ILE B O   1 
ATOM   6718  C CB  . ILE B 1 314 ? -6.213  29.209  30.743  1.00 61.35  ? 314 ILE B CB  1 
ATOM   6719  C CG1 . ILE B 1 314 ? -5.044  29.144  31.730  1.00 62.22  ? 314 ILE B CG1 1 
ATOM   6720  C CG2 . ILE B 1 314 ? -7.332  30.123  31.252  1.00 49.01  ? 314 ILE B CG2 1 
ATOM   6721  C CD1 . ILE B 1 314 ? -4.341  30.475  31.926  1.00 52.45  ? 314 ILE B CD1 1 
ATOM   6722  N N   . GLY B 1 315 ? -7.706  28.143  28.227  1.00 50.45  ? 315 GLY B N   1 
ATOM   6723  C CA  . GLY B 1 315 ? -8.791  28.400  27.297  1.00 54.68  ? 315 GLY B CA  1 
ATOM   6724  C C   . GLY B 1 315 ? -9.679  27.196  27.047  1.00 51.47  ? 315 GLY B C   1 
ATOM   6725  O O   . GLY B 1 315 ? -10.901 27.332  26.957  1.00 60.40  ? 315 GLY B O   1 
ATOM   6726  N N   . PHE B 1 316 ? -9.085  26.004  26.937  1.00 50.70  ? 316 PHE B N   1 
ATOM   6727  C CA  . PHE B 1 316 ? -9.812  24.819  26.485  1.00 54.64  ? 316 PHE B CA  1 
ATOM   6728  C C   . PHE B 1 316 ? -9.751  23.655  27.462  1.00 59.92  ? 316 PHE B C   1 
ATOM   6729  O O   . PHE B 1 316 ? -10.781 23.016  27.720  1.00 65.78  ? 316 PHE B O   1 
ATOM   6730  C CB  . PHE B 1 316 ? -9.283  24.376  25.106  1.00 51.83  ? 316 PHE B CB  1 
ATOM   6731  C CG  . PHE B 1 316 ? -9.019  25.517  24.175  1.00 53.08  ? 316 PHE B CG  1 
ATOM   6732  C CD1 . PHE B 1 316 ? -10.047 26.067  23.431  1.00 44.89  ? 316 PHE B CD1 1 
ATOM   6733  C CD2 . PHE B 1 316 ? -7.744  26.055  24.053  1.00 48.29  ? 316 PHE B CD2 1 
ATOM   6734  C CE1 . PHE B 1 316 ? -9.814  27.133  22.575  1.00 43.45  ? 316 PHE B CE1 1 
ATOM   6735  C CE2 . PHE B 1 316 ? -7.506  27.121  23.199  1.00 45.96  ? 316 PHE B CE2 1 
ATOM   6736  C CZ  . PHE B 1 316 ? -8.545  27.657  22.459  1.00 45.33  ? 316 PHE B CZ  1 
ATOM   6737  N N   . SER B 1 317 ? -8.575  23.346  28.006  1.00 54.52  ? 317 SER B N   1 
ATOM   6738  C CA  . SER B 1 317 ? -8.421  22.099  28.747  1.00 51.74  ? 317 SER B CA  1 
ATOM   6739  C C   . SER B 1 317 ? -9.060  22.164  30.126  1.00 56.48  ? 317 SER B C   1 
ATOM   6740  O O   . SER B 1 317 ? -9.781  21.241  30.523  1.00 58.72  ? 317 SER B O   1 
ATOM   6741  C CB  . SER B 1 317 ? -6.937  21.748  28.864  1.00 55.25  ? 317 SER B CB  1 
ATOM   6742  O OG  . SER B 1 317 ? -6.473  21.129  27.681  1.00 55.45  ? 317 SER B OG  1 
ATOM   6743  N N   . TYR B 1 318 ? -8.823  23.246  30.859  1.00 60.94  ? 318 TYR B N   1 
ATOM   6744  C CA  . TYR B 1 318 ? -9.130  23.269  32.285  1.00 59.67  ? 318 TYR B CA  1 
ATOM   6745  C C   . TYR B 1 318 ? -10.618 23.335  32.605  1.00 54.80  ? 318 TYR B C   1 
ATOM   6746  O O   . TYR B 1 318 ? -10.953 23.344  33.792  1.00 61.64  ? 318 TYR B O   1 
ATOM   6747  C CB  . TYR B 1 318 ? -8.424  24.451  32.953  1.00 59.51  ? 318 TYR B CB  1 
ATOM   6748  C CG  . TYR B 1 318 ? -6.956  24.235  33.249  1.00 51.63  ? 318 TYR B CG  1 
ATOM   6749  C CD1 . TYR B 1 318 ? -6.431  22.958  33.384  1.00 56.64  ? 318 TYR B CD1 1 
ATOM   6750  C CD2 . TYR B 1 318 ? -6.101  25.315  33.408  1.00 57.02  ? 318 TYR B CD2 1 
ATOM   6751  C CE1 . TYR B 1 318 ? -5.083  22.763  33.663  1.00 61.37  ? 318 TYR B CE1 1 
ATOM   6752  C CE2 . TYR B 1 318 ? -4.754  25.132  33.686  1.00 55.93  ? 318 TYR B CE2 1 
ATOM   6753  C CZ  . TYR B 1 318 ? -4.251  23.855  33.812  1.00 58.68  ? 318 TYR B CZ  1 
ATOM   6754  O OH  . TYR B 1 318 ? -2.914  23.672  34.086  1.00 59.35  ? 318 TYR B OH  1 
ATOM   6755  N N   . HIS B 1 319 ? -11.518 23.388  31.618  1.00 57.96  ? 319 HIS B N   1 
ATOM   6756  C CA  . HIS B 1 319 ? -12.934 23.457  31.970  1.00 52.36  ? 319 HIS B CA  1 
ATOM   6757  C C   . HIS B 1 319 ? -13.420 22.146  32.575  1.00 60.70  ? 319 HIS B C   1 
ATOM   6758  O O   . HIS B 1 319 ? -14.341 22.153  33.401  1.00 65.98  ? 319 HIS B O   1 
ATOM   6759  C CB  . HIS B 1 319 ? -13.771 23.850  30.752  1.00 48.30  ? 319 HIS B CB  1 
ATOM   6760  C CG  . HIS B 1 319 ? -13.956 22.749  29.758  1.00 54.46  ? 319 HIS B CG  1 
ATOM   6761  N ND1 . HIS B 1 319 ? -13.197 22.655  28.611  1.00 57.43  ? 319 HIS B ND1 1 
ATOM   6762  C CD2 . HIS B 1 319 ? -14.825 21.711  29.721  1.00 65.05  ? 319 HIS B CD2 1 
ATOM   6763  C CE1 . HIS B 1 319 ? -13.581 21.599  27.917  1.00 60.88  ? 319 HIS B CE1 1 
ATOM   6764  N NE2 . HIS B 1 319 ? -14.567 21.008  28.568  1.00 66.62  ? 319 HIS B NE2 1 
ATOM   6765  N N   . ALA B 1 320 ? -12.804 21.019  32.201  1.00 54.54  ? 320 ALA B N   1 
ATOM   6766  C CA  . ALA B 1 320 ? -13.155 19.735  32.794  1.00 63.14  ? 320 ALA B CA  1 
ATOM   6767  C C   . ALA B 1 320 ? -12.534 19.525  34.171  1.00 59.47  ? 320 ALA B C   1 
ATOM   6768  O O   . ALA B 1 320 ? -13.030 18.694  34.940  1.00 57.92  ? 320 ALA B O   1 
ATOM   6769  C CB  . ALA B 1 320 ? -12.720 18.593  31.872  1.00 66.33  ? 320 ALA B CB  1 
ATOM   6770  N N   . TRP B 1 321 ? -11.467 20.248  34.495  1.00 59.23  ? 321 TRP B N   1 
ATOM   6771  C CA  . TRP B 1 321 ? -10.742 20.013  35.733  1.00 65.23  ? 321 TRP B CA  1 
ATOM   6772  C C   . TRP B 1 321 ? -11.410 20.725  36.901  1.00 62.74  ? 321 TRP B C   1 
ATOM   6773  O O   . TRP B 1 321 ? -12.055 21.762  36.730  1.00 62.25  ? 321 TRP B O   1 
ATOM   6774  C CB  . TRP B 1 321 ? -9.297  20.508  35.621  1.00 65.53  ? 321 TRP B CB  1 
ATOM   6775  C CG  . TRP B 1 321 ? -8.471  19.925  34.507  1.00 60.74  ? 321 TRP B CG  1 
ATOM   6776  C CD1 . TRP B 1 321 ? -8.823  19.783  33.194  1.00 61.57  ? 321 TRP B CD1 1 
ATOM   6777  C CD2 . TRP B 1 321 ? -7.134  19.430  34.618  1.00 66.72  ? 321 TRP B CD2 1 
ATOM   6778  N NE1 . TRP B 1 321 ? -7.789  19.219  32.485  1.00 61.80  ? 321 TRP B NE1 1 
ATOM   6779  C CE2 . TRP B 1 321 ? -6.741  18.992  33.338  1.00 61.31  ? 321 TRP B CE2 1 
ATOM   6780  C CE3 . TRP B 1 321 ? -6.232  19.310  35.681  1.00 61.59  ? 321 TRP B CE3 1 
ATOM   6781  C CZ2 . TRP B 1 321 ? -5.487  18.443  33.093  1.00 67.16  ? 321 TRP B CZ2 1 
ATOM   6782  C CZ3 . TRP B 1 321 ? -4.994  18.766  35.437  1.00 59.04  ? 321 TRP B CZ3 1 
ATOM   6783  C CH2 . TRP B 1 321 ? -4.629  18.339  34.154  1.00 70.42  ? 321 TRP B CH2 1 
ATOM   6784  N N   . ASN B 1 322 ? -11.219 20.174  38.103  1.00 65.28  ? 322 ASN B N   1 
ATOM   6785  C CA  . ASN B 1 322 ? -11.498 20.930  39.319  1.00 70.20  ? 322 ASN B CA  1 
ATOM   6786  C C   . ASN B 1 322 ? -10.461 22.030  39.499  1.00 69.28  ? 322 ASN B C   1 
ATOM   6787  O O   . ASN B 1 322 ? -9.277  21.843  39.197  1.00 66.98  ? 322 ASN B O   1 
ATOM   6788  C CB  . ASN B 1 322 ? -11.498 20.028  40.555  1.00 74.55  ? 322 ASN B CB  1 
ATOM   6789  C CG  . ASN B 1 322 ? -11.917 18.615  40.246  1.00 89.50  ? 322 ASN B CG  1 
ATOM   6790  O OD1 . ASN B 1 322 ? -13.053 18.370  39.838  1.00 90.95  ? 322 ASN B OD1 1 
ATOM   6791  N ND2 . ASN B 1 322 ? -11.013 17.666  40.465  1.00 86.34  ? 322 ASN B ND2 1 
ATOM   6792  N N   . ALA B 1 323 ? -10.912 23.176  40.015  1.00 60.04  ? 323 ALA B N   1 
ATOM   6793  C CA  . ALA B 1 323 ? -10.071 24.369  40.029  1.00 68.06  ? 323 ALA B CA  1 
ATOM   6794  C C   . ALA B 1 323 ? -8.753  24.124  40.757  1.00 71.26  ? 323 ALA B C   1 
ATOM   6795  O O   . ALA B 1 323 ? -7.680  24.457  40.237  1.00 62.60  ? 323 ALA B O   1 
ATOM   6796  C CB  . ALA B 1 323 ? -10.839 25.533  40.658  1.00 68.12  ? 323 ALA B CB  1 
ATOM   6797  N N   . GLU B 1 324 ? -8.810  23.514  41.946  1.00 69.85  ? 324 GLU B N   1 
ATOM   6798  C CA  . GLU B 1 324 ? -7.591  23.275  42.712  1.00 70.72  ? 324 GLU B CA  1 
ATOM   6799  C C   . GLU B 1 324 ? -6.624  22.360  41.972  1.00 73.94  ? 324 GLU B C   1 
ATOM   6800  O O   . GLU B 1 324 ? -5.405  22.550  42.060  1.00 78.69  ? 324 GLU B O   1 
ATOM   6801  C CB  . GLU B 1 324 ? -7.933  22.690  44.081  1.00 70.88  ? 324 GLU B CB  1 
ATOM   6802  C CG  . GLU B 1 324 ? -7.973  23.742  45.176  1.00 80.67  ? 324 GLU B CG  1 
ATOM   6803  C CD  . GLU B 1 324 ? -7.470  23.242  46.517  1.00 95.97  ? 324 GLU B CD  1 
ATOM   6804  O OE1 . GLU B 1 324 ? -6.338  22.712  46.580  1.00 91.11  ? 324 GLU B OE1 1 
ATOM   6805  O OE2 . GLU B 1 324 ? -8.215  23.379  47.510  1.00 106.32 ? 324 GLU B OE2 1 
ATOM   6806  N N   . ASP B 1 325 ? -7.137  21.378  41.228  1.00 67.24  ? 325 ASP B N   1 
ATOM   6807  C CA  . ASP B 1 325 ? -6.256  20.543  40.419  1.00 67.77  ? 325 ASP B CA  1 
ATOM   6808  C C   . ASP B 1 325 ? -5.680  21.326  39.247  1.00 67.00  ? 325 ASP B C   1 
ATOM   6809  O O   . ASP B 1 325 ? -4.521  21.125  38.867  1.00 65.56  ? 325 ASP B O   1 
ATOM   6810  C CB  . ASP B 1 325 ? -7.009  19.311  39.931  1.00 72.13  ? 325 ASP B CB  1 
ATOM   6811  C CG  . ASP B 1 325 ? -7.617  18.523  41.071  1.00 79.02  ? 325 ASP B CG  1 
ATOM   6812  O OD1 . ASP B 1 325 ? -6.857  18.119  41.976  1.00 70.03  ? 325 ASP B OD1 1 
ATOM   6813  O OD2 . ASP B 1 325 ? -8.852  18.324  41.074  1.00 85.10  ? 325 ASP B OD2 1 
ATOM   6814  N N   . ALA B 1 326 ? -6.468  22.232  38.667  1.00 67.36  ? 326 ALA B N   1 
ATOM   6815  C CA  . ALA B 1 326 ? -5.961  23.023  37.553  1.00 65.15  ? 326 ALA B CA  1 
ATOM   6816  C C   . ALA B 1 326 ? -4.894  24.010  38.013  1.00 62.96  ? 326 ALA B C   1 
ATOM   6817  O O   . ALA B 1 326 ? -3.868  24.174  37.342  1.00 63.63  ? 326 ALA B O   1 
ATOM   6818  C CB  . ALA B 1 326 ? -7.107  23.750  36.855  1.00 61.96  ? 326 ALA B CB  1 
ATOM   6819  N N   . VAL B 1 327 ? -5.112  24.678  39.150  1.00 63.20  ? 327 VAL B N   1 
ATOM   6820  C CA  . VAL B 1 327 ? -4.108  25.611  39.660  1.00 61.35  ? 327 VAL B CA  1 
ATOM   6821  C C   . VAL B 1 327 ? -2.805  24.879  39.944  1.00 58.76  ? 327 VAL B C   1 
ATOM   6822  O O   . VAL B 1 327 ? -1.714  25.359  39.610  1.00 54.02  ? 327 VAL B O   1 
ATOM   6823  C CB  . VAL B 1 327 ? -4.625  26.350  40.908  1.00 62.48  ? 327 VAL B CB  1 
ATOM   6824  C CG1 . VAL B 1 327 ? -3.631  27.414  41.315  1.00 61.10  ? 327 VAL B CG1 1 
ATOM   6825  C CG2 . VAL B 1 327 ? -5.956  27.014  40.614  1.00 63.66  ? 327 VAL B CG2 1 
ATOM   6826  N N   . ARG B 1 328 ? -2.899  23.692  40.548  1.00 61.19  ? 328 ARG B N   1 
ATOM   6827  C CA  . ARG B 1 328 ? -1.689  22.938  40.857  1.00 64.98  ? 328 ARG B CA  1 
ATOM   6828  C C   . ARG B 1 328 ? -0.984  22.477  39.589  1.00 55.63  ? 328 ARG B C   1 
ATOM   6829  O O   . ARG B 1 328 ? 0.249   22.459  39.531  1.00 56.02  ? 328 ARG B O   1 
ATOM   6830  C CB  . ARG B 1 328 ? -2.015  21.745  41.756  1.00 66.21  ? 328 ARG B CB  1 
ATOM   6831  C CG  . ARG B 1 328 ? -1.886  22.048  43.236  1.00 70.47  ? 328 ARG B CG  1 
ATOM   6832  C CD  . ARG B 1 328 ? -2.929  21.312  44.035  1.00 72.92  ? 328 ARG B CD  1 
ATOM   6833  N NE  . ARG B 1 328 ? -2.995  19.905  43.661  1.00 77.28  ? 328 ARG B NE  1 
ATOM   6834  C CZ  . ARG B 1 328 ? -3.996  19.095  43.976  1.00 83.21  ? 328 ARG B CZ  1 
ATOM   6835  N NH1 . ARG B 1 328 ? -5.032  19.520  44.680  1.00 82.28  ? 328 ARG B NH1 1 
ATOM   6836  N NH2 . ARG B 1 328 ? -3.956  17.827  43.578  1.00 82.11  ? 328 ARG B NH2 1 
ATOM   6837  N N   . ASP B 1 329 ? -1.746  22.109  38.560  1.00 63.06  ? 329 ASP B N   1 
ATOM   6838  C CA  . ASP B 1 329 ? -1.133  21.819  37.271  1.00 60.06  ? 329 ASP B CA  1 
ATOM   6839  C C   . ASP B 1 329 ? -0.442  23.056  36.718  1.00 55.83  ? 329 ASP B C   1 
ATOM   6840  O O   . ASP B 1 329 ? 0.734   23.010  36.347  1.00 60.79  ? 329 ASP B O   1 
ATOM   6841  C CB  . ASP B 1 329 ? -2.186  21.306  36.296  1.00 65.53  ? 329 ASP B CB  1 
ATOM   6842  C CG  . ASP B 1 329 ? -1.583  20.814  35.002  1.00 61.29  ? 329 ASP B CG  1 
ATOM   6843  O OD1 . ASP B 1 329 ? -1.063  19.678  34.986  1.00 55.57  ? 329 ASP B OD1 1 
ATOM   6844  O OD2 . ASP B 1 329 ? -1.631  21.565  34.006  1.00 59.07  ? 329 ASP B OD2 1 
ATOM   6845  N N   . PHE B 1 330 ? -1.156  24.186  36.695  1.00 59.04  ? 330 PHE B N   1 
ATOM   6846  C CA  . PHE B 1 330 ? -0.599  25.425  36.158  1.00 56.75  ? 330 PHE B CA  1 
ATOM   6847  C C   . PHE B 1 330 ? 0.689   25.815  36.877  1.00 56.28  ? 330 PHE B C   1 
ATOM   6848  O O   . PHE B 1 330 ? 1.714   26.076  36.237  1.00 59.68  ? 330 PHE B O   1 
ATOM   6849  C CB  . PHE B 1 330 ? -1.638  26.543  36.256  1.00 51.48  ? 330 PHE B CB  1 
ATOM   6850  C CG  . PHE B 1 330 ? -1.414  27.662  35.286  1.00 56.04  ? 330 PHE B CG  1 
ATOM   6851  C CD1 . PHE B 1 330 ? -1.690  27.495  33.939  1.00 58.22  ? 330 PHE B CD1 1 
ATOM   6852  C CD2 . PHE B 1 330 ? -0.919  28.880  35.720  1.00 57.29  ? 330 PHE B CD2 1 
ATOM   6853  C CE1 . PHE B 1 330 ? -1.481  28.528  33.043  1.00 61.06  ? 330 PHE B CE1 1 
ATOM   6854  C CE2 . PHE B 1 330 ? -0.707  29.914  34.833  1.00 57.22  ? 330 PHE B CE2 1 
ATOM   6855  C CZ  . PHE B 1 330 ? -0.988  29.739  33.491  1.00 64.10  ? 330 PHE B CZ  1 
ATOM   6856  N N   . ILE B 1 331 ? 0.660   25.848  38.214  1.00 56.07  ? 331 ILE B N   1 
ATOM   6857  C CA  . ILE B 1 331 ? 1.863   26.190  38.974  1.00 57.63  ? 331 ILE B CA  1 
ATOM   6858  C C   . ILE B 1 331 ? 2.965   25.169  38.704  1.00 58.98  ? 331 ILE B C   1 
ATOM   6859  O O   . ILE B 1 331 ? 4.133   25.531  38.509  1.00 56.97  ? 331 ILE B O   1 
ATOM   6860  C CB  . ILE B 1 331 ? 1.539   26.308  40.479  1.00 51.49  ? 331 ILE B CB  1 
ATOM   6861  C CG1 . ILE B 1 331 ? 0.448   27.349  40.719  1.00 52.37  ? 331 ILE B CG1 1 
ATOM   6862  C CG2 . ILE B 1 331 ? 2.760   26.718  41.277  1.00 56.39  ? 331 ILE B CG2 1 
ATOM   6863  C CD1 . ILE B 1 331 ? 0.620   28.597  39.912  1.00 51.70  ? 331 ILE B CD1 1 
ATOM   6864  N N   . GLY B 1 332 ? 2.602   23.884  38.650  1.00 53.73  ? 332 GLY B N   1 
ATOM   6865  C CA  . GLY B 1 332 ? 3.585   22.852  38.361  1.00 52.32  ? 332 GLY B CA  1 
ATOM   6866  C C   . GLY B 1 332 ? 4.316   23.090  37.054  1.00 53.53  ? 332 GLY B C   1 
ATOM   6867  O O   . GLY B 1 332 ? 5.544   22.981  36.986  1.00 51.96  ? 332 GLY B O   1 
ATOM   6868  N N   . ARG B 1 333 ? 3.572   23.429  35.997  1.00 48.94  ? 333 ARG B N   1 
ATOM   6869  C CA  . ARG B 1 333 ? 4.215   23.717  34.718  1.00 56.48  ? 333 ARG B CA  1 
ATOM   6870  C C   . ARG B 1 333 ? 5.097   24.955  34.806  1.00 55.03  ? 333 ARG B C   1 
ATOM   6871  O O   . ARG B 1 333 ? 6.100   25.060  34.089  1.00 48.45  ? 333 ARG B O   1 
ATOM   6872  C CB  . ARG B 1 333 ? 3.166   23.891  33.618  1.00 53.87  ? 333 ARG B CB  1 
ATOM   6873  C CG  . ARG B 1 333 ? 2.069   22.859  33.637  1.00 50.39  ? 333 ARG B CG  1 
ATOM   6874  C CD  . ARG B 1 333 ? 1.581   22.546  32.248  1.00 50.90  ? 333 ARG B CD  1 
ATOM   6875  N NE  . ARG B 1 333 ? 0.621   21.451  32.255  1.00 49.98  ? 333 ARG B NE  1 
ATOM   6876  C CZ  . ARG B 1 333 ? 0.410   20.635  31.232  1.00 57.22  ? 333 ARG B CZ  1 
ATOM   6877  N NH1 . ARG B 1 333 ? 1.079   20.764  30.095  1.00 46.42  ? 333 ARG B NH1 1 
ATOM   6878  N NH2 . ARG B 1 333 ? -0.493  19.663  31.352  1.00 56.43  ? 333 ARG B NH2 1 
ATOM   6879  N N   . LEU B 1 334 ? 4.742   25.900  35.678  1.00 52.71  ? 334 LEU B N   1 
ATOM   6880  C CA  . LEU B 1 334 ? 5.566   27.089  35.846  1.00 55.12  ? 334 LEU B CA  1 
ATOM   6881  C C   . LEU B 1 334 ? 6.841   26.781  36.621  1.00 56.72  ? 334 LEU B C   1 
ATOM   6882  O O   . LEU B 1 334 ? 7.877   27.410  36.376  1.00 57.94  ? 334 LEU B O   1 
ATOM   6883  C CB  . LEU B 1 334 ? 4.759   28.186  36.536  1.00 59.33  ? 334 LEU B CB  1 
ATOM   6884  C CG  . LEU B 1 334 ? 3.599   28.701  35.683  1.00 60.10  ? 334 LEU B CG  1 
ATOM   6885  C CD1 . LEU B 1 334 ? 2.768   29.749  36.419  1.00 55.99  ? 334 LEU B CD1 1 
ATOM   6886  C CD2 . LEU B 1 334 ? 4.132   29.241  34.363  1.00 58.89  ? 334 LEU B CD2 1 
ATOM   6887  N N   . LYS B 1 335 ? 6.788   25.826  37.557  1.00 53.31  ? 335 LYS B N   1 
ATOM   6888  C CA  . LYS B 1 335 ? 8.012   25.376  38.214  1.00 57.30  ? 335 LYS B CA  1 
ATOM   6889  C C   . LYS B 1 335 ? 8.946   24.712  37.219  1.00 56.21  ? 335 LYS B C   1 
ATOM   6890  O O   . LYS B 1 335 ? 10.166  24.897  37.281  1.00 51.42  ? 335 LYS B O   1 
ATOM   6891  C CB  . LYS B 1 335 ? 7.696   24.400  39.349  1.00 59.16  ? 335 LYS B CB  1 
ATOM   6892  C CG  . LYS B 1 335 ? 7.001   25.020  40.543  1.00 59.36  ? 335 LYS B CG  1 
ATOM   6893  C CD  . LYS B 1 335 ? 6.125   24.010  41.269  1.00 61.57  ? 335 LYS B CD  1 
ATOM   6894  C CE  . LYS B 1 335 ? 5.760   24.496  42.667  1.00 64.08  ? 335 LYS B CE  1 
ATOM   6895  N NZ  . LYS B 1 335 ? 4.930   23.497  43.396  1.00 58.91  ? 335 LYS B NZ  1 
ATOM   6896  N N   . LYS B 1 336 ? 8.386   23.924  36.298  1.00 54.49  ? 336 LYS B N   1 
ATOM   6897  C CA  . LYS B 1 336 ? 9.206   23.236  35.310  1.00 57.64  ? 336 LYS B CA  1 
ATOM   6898  C C   . LYS B 1 336 ? 9.850   24.229  34.356  1.00 58.71  ? 336 LYS B C   1 
ATOM   6899  O O   . LYS B 1 336 ? 11.018  24.078  33.979  1.00 60.01  ? 336 LYS B O   1 
ATOM   6900  C CB  . LYS B 1 336 ? 8.355   22.222  34.547  1.00 61.66  ? 336 LYS B CB  1 
ATOM   6901  C CG  . LYS B 1 336 ? 8.395   20.820  35.134  1.00 62.23  ? 336 LYS B CG  1 
ATOM   6902  C CD  . LYS B 1 336 ? 7.642   19.831  34.262  1.00 59.25  ? 336 LYS B CD  1 
ATOM   6903  C CE  . LYS B 1 336 ? 8.051   18.399  34.574  1.00 62.85  ? 336 LYS B CE  1 
ATOM   6904  N NZ  . LYS B 1 336 ? 7.409   17.420  33.651  1.00 76.27  ? 336 LYS B NZ  1 
ATOM   6905  N N   . ILE B 1 337 ? 9.100   25.258  33.960  1.00 56.82  ? 337 ILE B N   1 
ATOM   6906  C CA  . ILE B 1 337 ? 9.675   26.324  33.152  1.00 56.14  ? 337 ILE B CA  1 
ATOM   6907  C C   . ILE B 1 337 ? 10.809  26.996  33.915  1.00 56.64  ? 337 ILE B C   1 
ATOM   6908  O O   . ILE B 1 337 ? 11.882  27.260  33.361  1.00 66.72  ? 337 ILE B O   1 
ATOM   6909  C CB  . ILE B 1 337 ? 8.578   27.327  32.744  1.00 59.16  ? 337 ILE B CB  1 
ATOM   6910  C CG1 . ILE B 1 337 ? 7.781   26.795  31.544  1.00 55.43  ? 337 ILE B CG1 1 
ATOM   6911  C CG2 . ILE B 1 337 ? 9.193   28.670  32.408  1.00 53.37  ? 337 ILE B CG2 1 
ATOM   6912  C CD1 . ILE B 1 337 ? 6.300   27.177  31.549  1.00 44.00  ? 337 ILE B CD1 1 
ATOM   6913  N N   . HIS B 1 338 ? 10.601  27.246  35.207  1.00 52.15  ? 338 HIS B N   1 
ATOM   6914  C CA  . HIS B 1 338 ? 11.632  27.874  36.026  1.00 58.52  ? 338 HIS B CA  1 
ATOM   6915  C C   . HIS B 1 338 ? 12.907  27.038  36.058  1.00 61.14  ? 338 HIS B C   1 
ATOM   6916  O O   . HIS B 1 338 ? 14.018  27.579  36.017  1.00 62.56  ? 338 HIS B O   1 
ATOM   6917  C CB  . HIS B 1 338 ? 11.082  28.091  37.432  1.00 57.00  ? 338 HIS B CB  1 
ATOM   6918  C CG  . HIS B 1 338 ? 11.906  29.000  38.283  1.00 54.96  ? 338 HIS B CG  1 
ATOM   6919  N ND1 . HIS B 1 338 ? 12.927  28.538  39.086  1.00 56.78  ? 338 HIS B ND1 1 
ATOM   6920  C CD2 . HIS B 1 338 ? 11.840  30.336  38.486  1.00 59.25  ? 338 HIS B CD2 1 
ATOM   6921  C CE1 . HIS B 1 338 ? 13.465  29.553  39.736  1.00 62.17  ? 338 HIS B CE1 1 
ATOM   6922  N NE2 . HIS B 1 338 ? 12.824  30.655  39.391  1.00 67.25  ? 338 HIS B NE2 1 
ATOM   6923  N N   . GLU B 1 339 ? 12.768  25.716  36.106  1.00 63.81  ? 339 GLU B N   1 
ATOM   6924  C CA  . GLU B 1 339 ? 13.926  24.837  36.199  1.00 68.30  ? 339 GLU B CA  1 
ATOM   6925  C C   . GLU B 1 339 ? 14.603  24.611  34.852  1.00 60.94  ? 339 GLU B C   1 
ATOM   6926  O O   . GLU B 1 339 ? 15.801  24.318  34.817  1.00 69.18  ? 339 GLU B O   1 
ATOM   6927  C CB  . GLU B 1 339 ? 13.492  23.508  36.830  1.00 70.03  ? 339 GLU B CB  1 
ATOM   6928  C CG  . GLU B 1 339 ? 14.138  22.255  36.274  1.00 90.58  ? 339 GLU B CG  1 
ATOM   6929  C CD  . GLU B 1 339 ? 13.374  20.986  36.658  1.00 105.00 ? 339 GLU B CD  1 
ATOM   6930  O OE1 . GLU B 1 339 ? 12.994  20.223  35.745  1.00 111.81 ? 339 GLU B OE1 1 
ATOM   6931  O OE2 . GLU B 1 339 ? 13.154  20.747  37.866  1.00 115.72 ? 339 GLU B OE2 1 
ATOM   6932  N N   . SER B 1 340 ? 13.886  24.795  33.748  1.00 58.89  ? 340 SER B N   1 
ATOM   6933  C CA  . SER B 1 340 ? 14.426  24.447  32.442  1.00 62.01  ? 340 SER B CA  1 
ATOM   6934  C C   . SER B 1 340 ? 15.407  25.477  31.896  1.00 68.68  ? 340 SER B C   1 
ATOM   6935  O O   . SER B 1 340 ? 16.166  25.156  30.973  1.00 65.15  ? 340 SER B O   1 
ATOM   6936  C CB  . SER B 1 340 ? 13.286  24.259  31.441  1.00 57.16  ? 340 SER B CB  1 
ATOM   6937  O OG  . SER B 1 340 ? 12.954  25.497  30.835  1.00 67.35  ? 340 SER B OG  1 
ATOM   6938  N N   . VAL B 1 341 ? 15.420  26.696  32.431  1.00 66.40  ? 341 VAL B N   1 
ATOM   6939  C CA  . VAL B 1 341 ? 16.231  27.773  31.877  1.00 67.43  ? 341 VAL B CA  1 
ATOM   6940  C C   . VAL B 1 341 ? 17.179  28.295  32.946  1.00 69.28  ? 341 VAL B C   1 
ATOM   6941  O O   . VAL B 1 341 ? 16.809  28.419  34.119  1.00 72.22  ? 341 VAL B O   1 
ATOM   6942  C CB  . VAL B 1 341 ? 15.357  28.910  31.306  1.00 58.25  ? 341 VAL B CB  1 
ATOM   6943  C CG1 . VAL B 1 341 ? 14.540  28.394  30.129  1.00 60.28  ? 341 VAL B CG1 1 
ATOM   6944  C CG2 . VAL B 1 341 ? 14.446  29.497  32.391  1.00 62.56  ? 341 VAL B CG2 1 
ATOM   6945  N N   . ASP B 1 342 ? 18.412  28.589  32.536  1.00 66.81  ? 342 ASP B N   1 
ATOM   6946  C CA  . ASP B 1 342 ? 19.369  29.187  33.459  1.00 73.44  ? 342 ASP B CA  1 
ATOM   6947  C C   . ASP B 1 342 ? 19.002  30.635  33.764  1.00 71.28  ? 342 ASP B C   1 
ATOM   6948  O O   . ASP B 1 342 ? 19.143  31.092  34.905  1.00 61.27  ? 342 ASP B O   1 
ATOM   6949  C CB  . ASP B 1 342 ? 20.770  29.085  32.870  1.00 72.26  ? 342 ASP B CB  1 
ATOM   6950  C CG  . ASP B 1 342 ? 20.970  27.804  32.085  1.00 90.85  ? 342 ASP B CG  1 
ATOM   6951  O OD1 . ASP B 1 342 ? 21.167  26.738  32.710  1.00 99.98  ? 342 ASP B OD1 1 
ATOM   6952  O OD2 . ASP B 1 342 ? 20.927  27.866  30.838  1.00 93.85  ? 342 ASP B OD2 1 
ATOM   6953  N N   . PHE B 1 343 ? 18.499  31.360  32.769  1.00 55.86  ? 343 PHE B N   1 
ATOM   6954  C CA  . PHE B 1 343 ? 18.145  32.762  32.941  1.00 58.66  ? 343 PHE B CA  1 
ATOM   6955  C C   . PHE B 1 343 ? 16.823  32.882  33.702  1.00 65.37  ? 343 PHE B C   1 
ATOM   6956  O O   . PHE B 1 343 ? 16.292  31.905  34.239  1.00 63.47  ? 343 PHE B O   1 
ATOM   6957  C CB  . PHE B 1 343 ? 18.090  33.456  31.583  1.00 61.80  ? 343 PHE B CB  1 
ATOM   6958  C CG  . PHE B 1 343 ? 17.239  32.744  30.564  1.00 61.96  ? 343 PHE B CG  1 
ATOM   6959  C CD1 . PHE B 1 343 ? 17.757  31.711  29.795  1.00 52.02  ? 343 PHE B CD1 1 
ATOM   6960  C CD2 . PHE B 1 343 ? 15.924  33.125  30.363  1.00 59.89  ? 343 PHE B CD2 1 
ATOM   6961  C CE1 . PHE B 1 343 ? 16.973  31.066  28.861  1.00 49.29  ? 343 PHE B CE1 1 
ATOM   6962  C CE2 . PHE B 1 343 ? 15.136  32.484  29.428  1.00 53.75  ? 343 PHE B CE2 1 
ATOM   6963  C CZ  . PHE B 1 343 ? 15.658  31.454  28.677  1.00 51.09  ? 343 PHE B CZ  1 
ATOM   6964  N N   . GLN B 1 344 ? 16.279  34.101  33.771  1.00 57.57  ? 344 GLN B N   1 
ATOM   6965  C CA  . GLN B 1 344 ? 14.965  34.316  34.367  1.00 62.56  ? 344 GLN B CA  1 
ATOM   6966  C C   . GLN B 1 344 ? 13.925  34.418  33.264  1.00 60.68  ? 344 GLN B C   1 
ATOM   6967  O O   . GLN B 1 344 ? 13.968  35.365  32.461  1.00 53.57  ? 344 GLN B O   1 
ATOM   6968  C CB  . GLN B 1 344 ? 14.953  35.572  35.231  1.00 56.19  ? 344 GLN B CB  1 
ATOM   6969  C CG  . GLN B 1 344 ? 15.387  35.288  36.652  1.00 59.03  ? 344 GLN B CG  1 
ATOM   6970  C CD  . GLN B 1 344 ? 15.380  36.506  37.544  1.00 63.87  ? 344 GLN B CD  1 
ATOM   6971  O OE1 . GLN B 1 344 ? 14.727  36.524  38.590  1.00 67.97  ? 344 GLN B OE1 1 
ATOM   6972  N NE2 . GLN B 1 344 ? 16.107  37.536  37.138  1.00 55.44  ? 344 GLN B NE2 1 
ATOM   6973  N N   . PRO B 1 345 ? 12.987  33.485  33.182  1.00 61.26  ? 345 PRO B N   1 
ATOM   6974  C CA  . PRO B 1 345 ? 12.072  33.460  32.043  1.00 57.46  ? 345 PRO B CA  1 
ATOM   6975  C C   . PRO B 1 345 ? 10.963  34.494  32.176  1.00 56.05  ? 345 PRO B C   1 
ATOM   6976  O O   . PRO B 1 345 ? 10.571  34.899  33.276  1.00 56.56  ? 345 PRO B O   1 
ATOM   6977  C CB  . PRO B 1 345 ? 11.514  32.032  32.097  1.00 51.94  ? 345 PRO B CB  1 
ATOM   6978  C CG  . PRO B 1 345 ? 11.446  31.762  33.574  1.00 58.30  ? 345 PRO B CG  1 
ATOM   6979  C CD  . PRO B 1 345 ? 12.701  32.400  34.141  1.00 64.10  ? 345 PRO B CD  1 
ATOM   6980  N N   . VAL B 1 346 ? 10.480  34.942  31.021  1.00 49.49  ? 346 VAL B N   1 
ATOM   6981  C CA  . VAL B 1 346 ? 9.242   35.703  30.913  1.00 56.48  ? 346 VAL B CA  1 
ATOM   6982  C C   . VAL B 1 346 ? 8.223   34.799  30.227  1.00 52.59  ? 346 VAL B C   1 
ATOM   6983  O O   . VAL B 1 346 ? 8.473   34.284  29.129  1.00 49.58  ? 346 VAL B O   1 
ATOM   6984  C CB  . VAL B 1 346 ? 9.444   37.035  30.167  1.00 52.77  ? 346 VAL B CB  1 
ATOM   6985  C CG1 . VAL B 1 346 ? 10.111  36.825  28.803  1.00 50.74  ? 346 VAL B CG1 1 
ATOM   6986  C CG2 . VAL B 1 346 ? 8.112   37.763  30.020  1.00 39.18  ? 346 VAL B CG2 1 
ATOM   6987  N N   . VAL B 1 347 ? 7.099   34.560  30.896  1.00 49.58  ? 347 VAL B N   1 
ATOM   6988  C CA  . VAL B 1 347 ? 6.072   33.647  30.412  1.00 48.65  ? 347 VAL B CA  1 
ATOM   6989  C C   . VAL B 1 347 ? 4.845   34.477  30.065  1.00 51.46  ? 347 VAL B C   1 
ATOM   6990  O O   . VAL B 1 347 ? 4.206   35.061  30.951  1.00 50.84  ? 347 VAL B O   1 
ATOM   6991  C CB  . VAL B 1 347 ? 5.735   32.564  31.445  1.00 49.50  ? 347 VAL B CB  1 
ATOM   6992  C CG1 . VAL B 1 347 ? 4.510   31.785  31.007  1.00 47.74  ? 347 VAL B CG1 1 
ATOM   6993  C CG2 . VAL B 1 347 ? 6.918   31.632  31.635  1.00 53.01  ? 347 VAL B CG2 1 
ATOM   6994  N N   . PHE B 1 348 ? 4.514   34.530  28.775  1.00 46.81  ? 348 PHE B N   1 
ATOM   6995  C CA  . PHE B 1 348 ? 3.372   35.296  28.289  1.00 44.82  ? 348 PHE B CA  1 
ATOM   6996  C C   . PHE B 1 348 ? 2.199   34.351  28.071  1.00 46.56  ? 348 PHE B C   1 
ATOM   6997  O O   . PHE B 1 348 ? 2.287   33.423  27.258  1.00 46.78  ? 348 PHE B O   1 
ATOM   6998  C CB  . PHE B 1 348 ? 3.706   36.029  26.993  1.00 41.59  ? 348 PHE B CB  1 
ATOM   6999  C CG  . PHE B 1 348 ? 3.976   37.500  27.173  1.00 42.23  ? 348 PHE B CG  1 
ATOM   7000  C CD1 . PHE B 1 348 ? 5.146   37.935  27.774  1.00 46.19  ? 348 PHE B CD1 1 
ATOM   7001  C CD2 . PHE B 1 348 ? 3.064   38.448  26.734  1.00 42.80  ? 348 PHE B CD2 1 
ATOM   7002  C CE1 . PHE B 1 348 ? 5.404   39.283  27.936  1.00 43.63  ? 348 PHE B CE1 1 
ATOM   7003  C CE2 . PHE B 1 348 ? 3.317   39.805  26.890  1.00 44.46  ? 348 PHE B CE2 1 
ATOM   7004  C CZ  . PHE B 1 348 ? 4.492   40.220  27.495  1.00 46.67  ? 348 PHE B CZ  1 
ATOM   7005  N N   . VAL B 1 349 ? 1.108   34.594  28.794  1.00 48.07  ? 349 VAL B N   1 
ATOM   7006  C CA  . VAL B 1 349 ? -0.122  33.813  28.693  1.00 47.34  ? 349 VAL B CA  1 
ATOM   7007  C C   . VAL B 1 349 ? -1.183  34.737  28.113  1.00 47.02  ? 349 VAL B C   1 
ATOM   7008  O O   . VAL B 1 349 ? -1.756  35.570  28.828  1.00 44.95  ? 349 VAL B O   1 
ATOM   7009  C CB  . VAL B 1 349 ? -0.567  33.245  30.045  1.00 49.48  ? 349 VAL B CB  1 
ATOM   7010  C CG1 . VAL B 1 349 ? -1.805  32.387  29.858  1.00 43.69  ? 349 VAL B CG1 1 
ATOM   7011  C CG2 . VAL B 1 349 ? 0.562   32.462  30.723  1.00 40.30  ? 349 VAL B CG2 1 
ATOM   7012  N N   . VAL B 1 350 ? -1.454  34.580  26.818  1.00 48.27  ? 350 VAL B N   1 
ATOM   7013  C CA  . VAL B 1 350 ? -2.335  35.466  26.068  1.00 45.08  ? 350 VAL B CA  1 
ATOM   7014  C C   . VAL B 1 350 ? -3.445  34.629  25.455  1.00 45.58  ? 350 VAL B C   1 
ATOM   7015  O O   . VAL B 1 350 ? -3.176  33.609  24.807  1.00 48.30  ? 350 VAL B O   1 
ATOM   7016  C CB  . VAL B 1 350 ? -1.573  36.229  24.970  1.00 45.59  ? 350 VAL B CB  1 
ATOM   7017  C CG1 . VAL B 1 350 ? -2.498  37.199  24.270  1.00 49.53  ? 350 VAL B CG1 1 
ATOM   7018  C CG2 . VAL B 1 350 ? -0.374  36.943  25.548  1.00 41.45  ? 350 VAL B CG2 1 
ATOM   7019  N N   . LEU B 1 351 ? -4.684  35.074  25.642  1.00 49.67  ? 351 LEU B N   1 
ATOM   7020  C CA  . LEU B 1 351 ? -5.863  34.368  25.159  1.00 49.67  ? 351 LEU B CA  1 
ATOM   7021  C C   . LEU B 1 351 ? -7.058  35.296  25.294  1.00 52.96  ? 351 LEU B C   1 
ATOM   7022  O O   . LEU B 1 351 ? -7.025  36.274  26.052  1.00 48.87  ? 351 LEU B O   1 
ATOM   7023  C CB  . LEU B 1 351 ? -6.111  33.071  25.935  1.00 42.36  ? 351 LEU B CB  1 
ATOM   7024  C CG  . LEU B 1 351 ? -6.344  33.182  27.440  1.00 37.21  ? 351 LEU B CG  1 
ATOM   7025  C CD1 . LEU B 1 351 ? -7.215  32.044  27.922  1.00 46.59  ? 351 LEU B CD1 1 
ATOM   7026  C CD2 . LEU B 1 351 ? -5.031  33.164  28.181  1.00 52.47  ? 351 LEU B CD2 1 
ATOM   7027  N N   . ASP B 1 352 ? -8.112  34.977  24.544  1.00 46.74  ? 352 ASP B N   1 
ATOM   7028  C CA  . ASP B 1 352 ? -9.353  35.726  24.650  1.00 44.57  ? 352 ASP B CA  1 
ATOM   7029  C C   . ASP B 1 352 ? -9.867  35.665  26.081  1.00 48.56  ? 352 ASP B C   1 
ATOM   7030  O O   . ASP B 1 352 ? -9.981  34.584  26.667  1.00 47.50  ? 352 ASP B O   1 
ATOM   7031  C CB  . ASP B 1 352 ? -10.396 35.166  23.682  1.00 49.77  ? 352 ASP B CB  1 
ATOM   7032  C CG  . ASP B 1 352 ? -9.838  34.936  22.289  1.00 57.41  ? 352 ASP B CG  1 
ATOM   7033  O OD1 . ASP B 1 352 ? -8.949  35.704  21.858  1.00 60.66  ? 352 ASP B OD1 1 
ATOM   7034  O OD2 . ASP B 1 352 ? -10.306 33.995  21.614  1.00 64.62  ? 352 ASP B OD2 1 
ATOM   7035  N N   . GLY B 1 353 ? -10.164 36.833  26.644  1.00 48.50  ? 353 GLY B N   1 
ATOM   7036  C CA  . GLY B 1 353 ? -10.544 36.924  28.034  1.00 46.90  ? 353 GLY B CA  1 
ATOM   7037  C C   . GLY B 1 353 ? -12.009 36.738  28.357  1.00 48.36  ? 353 GLY B C   1 
ATOM   7038  O O   . GLY B 1 353 ? -12.363 36.837  29.534  1.00 52.25  ? 353 GLY B O   1 
ATOM   7039  N N   . GLU B 1 354 ? -12.874 36.459  27.375  1.00 48.66  ? 354 GLU B N   1 
ATOM   7040  C CA  . GLU B 1 354 ? -14.311 36.349  27.616  1.00 45.70  ? 354 GLU B CA  1 
ATOM   7041  C C   . GLU B 1 354 ? -14.920 34.996  27.255  1.00 49.02  ? 354 GLU B C   1 
ATOM   7042  O O   . GLU B 1 354 ? -15.963 34.643  27.811  1.00 53.40  ? 354 GLU B O   1 
ATOM   7043  C CB  . GLU B 1 354 ? -15.069 37.447  26.845  1.00 47.50  ? 354 GLU B CB  1 
ATOM   7044  C CG  . GLU B 1 354 ? -14.972 37.359  25.323  1.00 47.44  ? 354 GLU B CG  1 
ATOM   7045  C CD  . GLU B 1 354 ? -13.707 38.008  24.778  1.00 52.11  ? 354 GLU B CD  1 
ATOM   7046  O OE1 . GLU B 1 354 ? -13.753 39.202  24.407  1.00 45.49  ? 354 GLU B OE1 1 
ATOM   7047  O OE2 . GLU B 1 354 ? -12.664 37.319  24.715  1.00 48.08  ? 354 GLU B OE2 1 
ATOM   7048  N N   . ASN B 1 355 ? -14.309 34.224  26.360  1.00 44.77  ? 355 ASN B N   1 
ATOM   7049  C CA  . ASN B 1 355 ? -15.000 33.070  25.799  1.00 42.39  ? 355 ASN B CA  1 
ATOM   7050  C C   . ASN B 1 355 ? -14.801 31.777  26.581  1.00 44.36  ? 355 ASN B C   1 
ATOM   7051  O O   . ASN B 1 355 ? -15.605 30.856  26.427  1.00 53.59  ? 355 ASN B O   1 
ATOM   7052  C CB  . ASN B 1 355 ? -14.560 32.858  24.349  1.00 45.43  ? 355 ASN B CB  1 
ATOM   7053  C CG  . ASN B 1 355 ? -14.738 34.108  23.497  1.00 54.22  ? 355 ASN B CG  1 
ATOM   7054  O OD1 . ASN B 1 355 ? -15.782 34.765  23.536  1.00 46.75  ? 355 ASN B OD1 1 
ATOM   7055  N ND2 . ASN B 1 355 ? -13.703 34.452  22.733  1.00 52.10  ? 355 ASN B ND2 1 
ATOM   7056  N N   . CYS B 1 356 ? -13.776 31.666  27.419  1.00 47.64  ? 356 CYS B N   1 
ATOM   7057  C CA  . CYS B 1 356 ? -13.528 30.360  28.021  1.00 47.77  ? 356 CYS B CA  1 
ATOM   7058  C C   . CYS B 1 356 ? -14.276 30.145  29.328  1.00 48.99  ? 356 CYS B C   1 
ATOM   7059  O O   . CYS B 1 356 ? -14.425 28.995  29.758  1.00 51.20  ? 356 CYS B O   1 
ATOM   7060  C CB  . CYS B 1 356 ? -12.032 30.148  28.246  1.00 46.67  ? 356 CYS B CB  1 
ATOM   7061  S SG  . CYS B 1 356 ? -11.282 31.304  29.397  1.00 59.84  ? 356 CYS B SG  1 
ATOM   7062  N N   . TRP B 1 357 ? -14.776 31.211  29.954  1.00 49.93  ? 357 TRP B N   1 
ATOM   7063  C CA  . TRP B 1 357 ? -15.299 31.081  31.309  1.00 52.27  ? 357 TRP B CA  1 
ATOM   7064  C C   . TRP B 1 357 ? -16.689 30.461  31.346  1.00 48.33  ? 357 TRP B C   1 
ATOM   7065  O O   . TRP B 1 357 ? -17.047 29.811  32.335  1.00 49.24  ? 357 TRP B O   1 
ATOM   7066  C CB  . TRP B 1 357 ? -15.289 32.446  31.997  1.00 54.88  ? 357 TRP B CB  1 
ATOM   7067  C CG  . TRP B 1 357 ? -13.953 33.146  31.867  1.00 50.48  ? 357 TRP B CG  1 
ATOM   7068  C CD1 . TRP B 1 357 ? -13.731 34.404  31.388  1.00 48.70  ? 357 TRP B CD1 1 
ATOM   7069  C CD2 . TRP B 1 357 ? -12.664 32.624  32.229  1.00 49.29  ? 357 TRP B CD2 1 
ATOM   7070  N NE1 . TRP B 1 357 ? -12.388 34.697  31.425  1.00 51.74  ? 357 TRP B NE1 1 
ATOM   7071  C CE2 . TRP B 1 357 ? -11.712 33.621  31.937  1.00 53.33  ? 357 TRP B CE2 1 
ATOM   7072  C CE3 . TRP B 1 357 ? -12.223 31.411  32.768  1.00 52.06  ? 357 TRP B CE3 1 
ATOM   7073  C CZ2 . TRP B 1 357 ? -10.345 33.442  32.167  1.00 46.35  ? 357 TRP B CZ2 1 
ATOM   7074  C CZ3 . TRP B 1 357 ? -10.864 31.235  32.994  1.00 52.71  ? 357 TRP B CZ3 1 
ATOM   7075  C CH2 . TRP B 1 357 ? -9.944  32.245  32.694  1.00 43.48  ? 357 TRP B CH2 1 
ATOM   7076  N N   . GLU B 1 358 ? -17.473 30.620  30.285  1.00 52.27  ? 358 GLU B N   1 
ATOM   7077  C CA  . GLU B 1 358 ? -18.815 30.053  30.291  1.00 52.44  ? 358 GLU B CA  1 
ATOM   7078  C C   . GLU B 1 358 ? -18.801 28.539  30.456  1.00 52.73  ? 358 GLU B C   1 
ATOM   7079  O O   . GLU B 1 358 ? -19.807 27.964  30.889  1.00 53.13  ? 358 GLU B O   1 
ATOM   7080  C CB  . GLU B 1 358 ? -19.542 30.423  29.008  1.00 53.58  ? 358 GLU B CB  1 
ATOM   7081  C CG  . GLU B 1 358 ? -18.615 30.584  27.831  1.00 56.73  ? 358 GLU B CG  1 
ATOM   7082  C CD  . GLU B 1 358 ? -19.331 31.135  26.626  1.00 64.75  ? 358 GLU B CD  1 
ATOM   7083  O OE1 . GLU B 1 358 ? -20.085 30.370  25.991  1.00 65.45  ? 358 GLU B OE1 1 
ATOM   7084  O OE2 . GLU B 1 358 ? -19.142 32.331  26.312  1.00 58.51  ? 358 GLU B OE2 1 
ATOM   7085  N N   . TYR B 1 359 ? -17.684 27.884  30.149  1.00 54.58  ? 359 TYR B N   1 
ATOM   7086  C CA  . TYR B 1 359 ? -17.603 26.432  30.236  1.00 53.70  ? 359 TYR B CA  1 
ATOM   7087  C C   . TYR B 1 359 ? -16.997 25.945  31.546  1.00 52.02  ? 359 TYR B C   1 
ATOM   7088  O O   . TYR B 1 359 ? -16.944 24.733  31.773  1.00 53.33  ? 359 TYR B O   1 
ATOM   7089  C CB  . TYR B 1 359 ? -16.807 25.883  29.054  1.00 47.56  ? 359 TYR B CB  1 
ATOM   7090  C CG  . TYR B 1 359 ? -17.355 26.307  27.711  1.00 46.76  ? 359 TYR B CG  1 
ATOM   7091  C CD1 . TYR B 1 359 ? -18.405 25.623  27.124  1.00 52.03  ? 359 TYR B CD1 1 
ATOM   7092  C CD2 . TYR B 1 359 ? -16.835 27.410  27.043  1.00 45.05  ? 359 TYR B CD2 1 
ATOM   7093  C CE1 . TYR B 1 359 ? -18.912 26.006  25.896  1.00 55.96  ? 359 TYR B CE1 1 
ATOM   7094  C CE2 . TYR B 1 359 ? -17.332 27.803  25.820  1.00 50.46  ? 359 TYR B CE2 1 
ATOM   7095  C CZ  . TYR B 1 359 ? -18.375 27.095  25.248  1.00 64.32  ? 359 TYR B CZ  1 
ATOM   7096  O OH  . TYR B 1 359 ? -18.894 27.464  24.026  1.00 73.44  ? 359 TYR B OH  1 
ATOM   7097  N N   . TYR B 1 360 ? -16.552 26.853  32.408  1.00 49.45  ? 360 TYR B N   1 
ATOM   7098  C CA  . TYR B 1 360 ? -16.110 26.487  33.744  1.00 52.48  ? 360 TYR B CA  1 
ATOM   7099  C C   . TYR B 1 360 ? -17.292 26.511  34.704  1.00 58.42  ? 360 TYR B C   1 
ATOM   7100  O O   . TYR B 1 360 ? -18.294 27.192  34.475  1.00 55.37  ? 360 TYR B O   1 
ATOM   7101  C CB  . TYR B 1 360 ? -15.041 27.448  34.256  1.00 52.22  ? 360 TYR B CB  1 
ATOM   7102  C CG  . TYR B 1 360 ? -13.663 27.315  33.642  1.00 54.22  ? 360 TYR B CG  1 
ATOM   7103  C CD1 . TYR B 1 360 ? -13.488 27.294  32.264  1.00 53.63  ? 360 TYR B CD1 1 
ATOM   7104  C CD2 . TYR B 1 360 ? -12.532 27.241  34.447  1.00 51.26  ? 360 TYR B CD2 1 
ATOM   7105  C CE1 . TYR B 1 360 ? -12.231 27.188  31.703  1.00 57.69  ? 360 TYR B CE1 1 
ATOM   7106  C CE2 . TYR B 1 360 ? -11.267 27.133  33.893  1.00 58.64  ? 360 TYR B CE2 1 
ATOM   7107  C CZ  . TYR B 1 360 ? -11.124 27.108  32.521  1.00 60.22  ? 360 TYR B CZ  1 
ATOM   7108  O OH  . TYR B 1 360 ? -9.873  27.003  31.961  1.00 56.98  ? 360 TYR B OH  1 
ATOM   7109  N N   . GLU B 1 361 ? -17.162 25.767  35.798  1.00 56.63  ? 361 GLU B N   1 
ATOM   7110  C CA  . GLU B 1 361 ? -18.153 25.863  36.859  1.00 66.81  ? 361 GLU B CA  1 
ATOM   7111  C C   . GLU B 1 361 ? -18.102 27.251  37.481  1.00 70.22  ? 361 GLU B C   1 
ATOM   7112  O O   . GLU B 1 361 ? -17.022 27.762  37.793  1.00 74.01  ? 361 GLU B O   1 
ATOM   7113  C CB  . GLU B 1 361 ? -17.911 24.795  37.920  1.00 61.23  ? 361 GLU B CB  1 
ATOM   7114  C CG  . GLU B 1 361 ? -18.066 23.389  37.397  1.00 71.63  ? 361 GLU B CG  1 
ATOM   7115  C CD  . GLU B 1 361 ? -19.348 22.740  37.860  1.00 84.45  ? 361 GLU B CD  1 
ATOM   7116  O OE1 . GLU B 1 361 ? -19.963 23.259  38.815  1.00 101.89 ? 361 GLU B OE1 1 
ATOM   7117  O OE2 . GLU B 1 361 ? -19.732 21.701  37.281  1.00 98.96  ? 361 GLU B OE2 1 
ATOM   7118  N N   . GLU B 1 362 ? -19.277 27.866  37.635  1.00 67.94  ? 362 GLU B N   1 
ATOM   7119  C CA  . GLU B 1 362 ? -19.401 29.205  38.209  1.00 70.74  ? 362 GLU B CA  1 
ATOM   7120  C C   . GLU B 1 362 ? -18.562 30.221  37.432  1.00 65.42  ? 362 GLU B C   1 
ATOM   7121  O O   . GLU B 1 362 ? -17.859 31.045  38.020  1.00 63.51  ? 362 GLU B O   1 
ATOM   7122  C CB  . GLU B 1 362 ? -19.023 29.202  39.691  1.00 75.61  ? 362 GLU B CB  1 
ATOM   7123  C CG  . GLU B 1 362 ? -19.562 28.010  40.466  1.00 81.43  ? 362 GLU B CG  1 
ATOM   7124  C CD  . GLU B 1 362 ? -20.086 28.391  41.832  1.00 89.96  ? 362 GLU B CD  1 
ATOM   7125  O OE1 . GLU B 1 362 ? -20.181 29.605  42.117  1.00 92.01  ? 362 GLU B OE1 1 
ATOM   7126  O OE2 . GLU B 1 362 ? -20.399 27.476  42.622  1.00 91.66  ? 362 GLU B OE2 1 
ATOM   7127  N N   . ASN B 1 363 ? -18.613 30.131  36.097  1.00 62.74  ? 363 ASN B N   1 
ATOM   7128  C CA  . ASN B 1 363 ? -17.961 31.088  35.187  1.00 60.40  ? 363 ASN B CA  1 
ATOM   7129  C C   . ASN B 1 363 ? -16.467 31.263  35.479  1.00 55.79  ? 363 ASN B C   1 
ATOM   7130  O O   . ASN B 1 363 ? -15.930 32.364  35.389  1.00 61.06  ? 363 ASN B O   1 
ATOM   7131  C CB  . ASN B 1 363 ? -18.664 32.450  35.225  1.00 53.28  ? 363 ASN B CB  1 
ATOM   7132  C CG  . ASN B 1 363 ? -18.359 33.304  34.014  1.00 57.44  ? 363 ASN B CG  1 
ATOM   7133  O OD1 . ASN B 1 363 ? -18.455 32.841  32.878  1.00 60.27  ? 363 ASN B OD1 1 
ATOM   7134  N ND2 . ASN B 1 363 ? -17.990 34.558  34.249  1.00 58.20  ? 363 ASN B ND2 1 
ATOM   7135  N N   . GLY B 1 364 ? -15.770 30.191  35.841  1.00 55.78  ? 364 GLY B N   1 
ATOM   7136  C CA  . GLY B 1 364 ? -14.373 30.316  36.222  1.00 60.79  ? 364 GLY B CA  1 
ATOM   7137  C C   . GLY B 1 364 ? -14.086 31.158  37.451  1.00 55.42  ? 364 GLY B C   1 
ATOM   7138  O O   . GLY B 1 364 ? -12.909 31.299  37.798  1.00 61.84  ? 364 GLY B O   1 
ATOM   7139  N N   . ILE B 1 365 ? -15.105 31.719  38.122  1.00 54.57  ? 365 ILE B N   1 
ATOM   7140  C CA  . ILE B 1 365 ? -14.855 32.473  39.341  1.00 59.14  ? 365 ILE B CA  1 
ATOM   7141  C C   . ILE B 1 365 ? -14.079 31.648  40.352  1.00 63.70  ? 365 ILE B C   1 
ATOM   7142  O O   . ILE B 1 365 ? -13.110 32.169  40.921  1.00 64.08  ? 365 ILE B O   1 
ATOM   7143  C CB  . ILE B 1 365 ? -16.171 33.029  39.900  1.00 62.16  ? 365 ILE B CB  1 
ATOM   7144  C CG1 . ILE B 1 365 ? -16.731 34.091  38.940  1.00 54.93  ? 365 ILE B CG1 1 
ATOM   7145  C CG2 . ILE B 1 365 ? -15.918 33.639  41.279  1.00 64.91  ? 365 ILE B CG2 1 
ATOM   7146  C CD1 . ILE B 1 365 ? -18.201 34.295  39.052  1.00 52.49  ? 365 ILE B CD1 1 
ATOM   7147  N N   . PRO B 1 366 ? -14.401 30.376  40.611  1.00 64.44  ? 366 PRO B N   1 
ATOM   7148  C CA  . PRO B 1 366 ? -13.563 29.617  41.557  1.00 65.64  ? 366 PRO B CA  1 
ATOM   7149  C C   . PRO B 1 366 ? -12.166 29.338  41.032  1.00 60.21  ? 366 PRO B C   1 
ATOM   7150  O O   . PRO B 1 366 ? -11.204 29.385  41.806  1.00 64.35  ? 366 PRO B O   1 
ATOM   7151  C CB  . PRO B 1 366 ? -14.358 28.312  41.766  1.00 63.37  ? 366 PRO B CB  1 
ATOM   7152  C CG  . PRO B 1 366 ? -15.754 28.634  41.353  1.00 62.75  ? 366 PRO B CG  1 
ATOM   7153  C CD  . PRO B 1 366 ? -15.571 29.585  40.202  1.00 66.04  ? 366 PRO B CD  1 
ATOM   7154  N N   . PHE B 1 367 ? -12.026 29.041  39.737  1.00 54.71  ? 367 PHE B N   1 
ATOM   7155  C CA  . PHE B 1 367 ? -10.700 28.791  39.181  1.00 56.34  ? 367 PHE B CA  1 
ATOM   7156  C C   . PHE B 1 367 ? -9.825  30.031  39.282  1.00 59.25  ? 367 PHE B C   1 
ATOM   7157  O O   . PHE B 1 367 ? -8.692  29.968  39.774  1.00 56.31  ? 367 PHE B O   1 
ATOM   7158  C CB  . PHE B 1 367 ? -10.808 28.336  37.723  1.00 59.93  ? 367 PHE B CB  1 
ATOM   7159  C CG  . PHE B 1 367 ? -9.483  28.298  37.000  1.00 54.31  ? 367 PHE B CG  1 
ATOM   7160  C CD1 . PHE B 1 367 ? -8.573  27.273  37.230  1.00 55.93  ? 367 PHE B CD1 1 
ATOM   7161  C CD2 . PHE B 1 367 ? -9.139  29.298  36.105  1.00 56.66  ? 367 PHE B CD2 1 
ATOM   7162  C CE1 . PHE B 1 367 ? -7.349  27.241  36.570  1.00 53.69  ? 367 PHE B CE1 1 
ATOM   7163  C CE2 . PHE B 1 367 ? -7.910  29.272  35.442  1.00 65.89  ? 367 PHE B CE2 1 
ATOM   7164  C CZ  . PHE B 1 367 ? -7.017  28.242  35.676  1.00 53.35  ? 367 PHE B CZ  1 
ATOM   7165  N N   . LEU B 1 368 ? -10.338 31.175  38.820  1.00 51.40  ? 368 LEU B N   1 
ATOM   7166  C CA  . LEU B 1 368 ? -9.515  32.379  38.761  1.00 51.79  ? 368 LEU B CA  1 
ATOM   7167  C C   . LEU B 1 368 ? -9.144  32.871  40.153  1.00 50.93  ? 368 LEU B C   1 
ATOM   7168  O O   . LEU B 1 368 ? -8.034  33.369  40.371  1.00 52.28  ? 368 LEU B O   1 
ATOM   7169  C CB  . LEU B 1 368 ? -10.242 33.471  37.982  1.00 48.96  ? 368 LEU B CB  1 
ATOM   7170  C CG  . LEU B 1 368 ? -10.157 33.256  36.474  1.00 53.28  ? 368 LEU B CG  1 
ATOM   7171  C CD1 . LEU B 1 368 ? -10.762 34.418  35.707  1.00 57.16  ? 368 LEU B CD1 1 
ATOM   7172  C CD2 . LEU B 1 368 ? -8.711  33.060  36.079  1.00 56.54  ? 368 LEU B CD2 1 
ATOM   7173  N N   . GLU B 1 369 ? -10.052 32.729  41.114  1.00 56.13  ? 369 GLU B N   1 
ATOM   7174  C CA  . GLU B 1 369 ? -9.750  33.206  42.454  1.00 54.92  ? 369 GLU B CA  1 
ATOM   7175  C C   . GLU B 1 369 ? -8.703  32.333  43.130  1.00 54.40  ? 369 GLU B C   1 
ATOM   7176  O O   . GLU B 1 369 ? -7.928  32.829  43.955  1.00 53.71  ? 369 GLU B O   1 
ATOM   7177  C CB  . GLU B 1 369 ? -11.033 33.284  43.281  1.00 53.73  ? 369 GLU B CB  1 
ATOM   7178  C CG  . GLU B 1 369 ? -11.923 34.446  42.865  1.00 56.15  ? 369 GLU B CG  1 
ATOM   7179  C CD  . GLU B 1 369 ? -13.092 34.671  43.800  1.00 66.83  ? 369 GLU B CD  1 
ATOM   7180  O OE1 . GLU B 1 369 ? -13.552 33.697  44.430  1.00 73.52  ? 369 GLU B OE1 1 
ATOM   7181  O OE2 . GLU B 1 369 ? -13.556 35.827  43.901  1.00 70.91  ? 369 GLU B OE2 1 
ATOM   7182  N N   . LYS B 1 370 ? -8.648  31.044  42.785  1.00 53.49  ? 370 LYS B N   1 
ATOM   7183  C CA  . LYS B 1 370 ? -7.599  30.187  43.330  1.00 55.13  ? 370 LYS B CA  1 
ATOM   7184  C C   . LYS B 1 370 ? -6.264  30.459  42.651  1.00 61.05  ? 370 LYS B C   1 
ATOM   7185  O O   . LYS B 1 370 ? -5.218  30.491  43.311  1.00 65.99  ? 370 LYS B O   1 
ATOM   7186  C CB  . LYS B 1 370 ? -7.984  28.715  43.181  1.00 55.85  ? 370 LYS B CB  1 
ATOM   7187  C CG  . LYS B 1 370 ? -7.918  27.919  44.474  1.00 58.53  ? 370 LYS B CG  1 
ATOM   7188  C CD  . LYS B 1 370 ? -6.484  27.615  44.873  1.00 60.82  ? 370 LYS B CD  1 
ATOM   7189  C CE  . LYS B 1 370 ? -6.427  26.777  46.146  1.00 72.37  ? 370 LYS B CE  1 
ATOM   7190  N NZ  . LYS B 1 370 ? -5.104  26.848  46.840  1.00 76.84  ? 370 LYS B NZ  1 
ATOM   7191  N N   . LEU B 1 371 ? -6.283  30.657  41.332  1.00 56.12  ? 371 LEU B N   1 
ATOM   7192  C CA  . LEU B 1 371 ? -5.054  30.948  40.605  1.00 56.74  ? 371 LEU B CA  1 
ATOM   7193  C C   . LEU B 1 371 ? -4.446  32.260  41.079  1.00 58.77  ? 371 LEU B C   1 
ATOM   7194  O O   . LEU B 1 371 ? -3.280  32.308  41.488  1.00 58.94  ? 371 LEU B O   1 
ATOM   7195  C CB  . LEU B 1 371 ? -5.343  30.995  39.106  1.00 58.98  ? 371 LEU B CB  1 
ATOM   7196  C CG  . LEU B 1 371 ? -4.216  31.503  38.217  1.00 51.45  ? 371 LEU B CG  1 
ATOM   7197  C CD1 . LEU B 1 371 ? -3.145  30.440  38.100  1.00 46.74  ? 371 LEU B CD1 1 
ATOM   7198  C CD2 . LEU B 1 371 ? -4.766  31.876  36.860  1.00 51.05  ? 371 LEU B CD2 1 
ATOM   7199  N N   . TYR B 1 372 ? -5.242  33.332  41.058  1.00 53.98  ? 372 TYR B N   1 
ATOM   7200  C CA  . TYR B 1 372 ? -4.761  34.639  41.493  1.00 58.15  ? 372 TYR B CA  1 
ATOM   7201  C C   . TYR B 1 372 ? -4.337  34.645  42.960  1.00 56.60  ? 372 TYR B C   1 
ATOM   7202  O O   . TYR B 1 372 ? -3.408  35.372  43.332  1.00 54.53  ? 372 TYR B O   1 
ATOM   7203  C CB  . TYR B 1 372 ? -5.842  35.691  41.250  1.00 49.44  ? 372 TYR B CB  1 
ATOM   7204  C CG  . TYR B 1 372 ? -6.189  35.874  39.798  1.00 51.87  ? 372 TYR B CG  1 
ATOM   7205  C CD1 . TYR B 1 372 ? -5.324  35.452  38.797  1.00 56.82  ? 372 TYR B CD1 1 
ATOM   7206  C CD2 . TYR B 1 372 ? -7.377  36.490  39.421  1.00 56.22  ? 372 TYR B CD2 1 
ATOM   7207  C CE1 . TYR B 1 372 ? -5.634  35.634  37.454  1.00 59.95  ? 372 TYR B CE1 1 
ATOM   7208  C CE2 . TYR B 1 372 ? -7.696  36.672  38.083  1.00 55.21  ? 372 TYR B CE2 1 
ATOM   7209  C CZ  . TYR B 1 372 ? -6.822  36.243  37.105  1.00 53.18  ? 372 TYR B CZ  1 
ATOM   7210  O OH  . TYR B 1 372 ? -7.135  36.425  35.777  1.00 56.66  ? 372 TYR B OH  1 
ATOM   7211  N N   . SER B 1 373 ? -5.003  33.862  43.813  1.00 53.57  ? 373 SER B N   1 
ATOM   7212  C CA  . SER B 1 373 ? -4.600  33.817  45.217  1.00 59.67  ? 373 SER B CA  1 
ATOM   7213  C C   . SER B 1 373 ? -3.294  33.052  45.390  1.00 65.61  ? 373 SER B C   1 
ATOM   7214  O O   . SER B 1 373 ? -2.398  33.495  46.119  1.00 65.39  ? 373 SER B O   1 
ATOM   7215  C CB  . SER B 1 373 ? -5.712  33.207  46.073  1.00 56.22  ? 373 SER B CB  1 
ATOM   7216  O OG  . SER B 1 373 ? -5.654  31.792  46.072  1.00 58.57  ? 373 SER B OG  1 
ATOM   7217  N N   . THR B 1 374 ? -3.161  31.909  44.717  1.00 60.26  ? 374 THR B N   1 
ATOM   7218  C CA  . THR B 1 374 ? -1.942  31.121  44.847  1.00 61.22  ? 374 THR B CA  1 
ATOM   7219  C C   . THR B 1 374 ? -0.730  31.890  44.331  1.00 64.81  ? 374 THR B C   1 
ATOM   7220  O O   . THR B 1 374 ? 0.328   31.891  44.968  1.00 73.23  ? 374 THR B O   1 
ATOM   7221  C CB  . THR B 1 374 ? -2.111  29.796  44.112  1.00 62.17  ? 374 THR B CB  1 
ATOM   7222  O OG1 . THR B 1 374 ? -3.130  29.032  44.766  1.00 63.49  ? 374 THR B OG1 1 
ATOM   7223  C CG2 . THR B 1 374 ? -0.813  29.019  44.125  1.00 67.07  ? 374 THR B CG2 1 
ATOM   7224  N N   . LEU B 1 375 ? -0.874  32.568  43.188  1.00 66.42  ? 375 LEU B N   1 
ATOM   7225  C CA  . LEU B 1 375 ? 0.206   33.398  42.659  1.00 63.59  ? 375 LEU B CA  1 
ATOM   7226  C C   . LEU B 1 375 ? 0.604   34.497  43.635  1.00 61.87  ? 375 LEU B C   1 
ATOM   7227  O O   . LEU B 1 375 ? 1.788   34.843  43.739  1.00 68.58  ? 375 LEU B O   1 
ATOM   7228  C CB  . LEU B 1 375 ? -0.221  34.010  41.324  1.00 54.15  ? 375 LEU B CB  1 
ATOM   7229  C CG  . LEU B 1 375 ? -0.457  32.989  40.214  1.00 54.64  ? 375 LEU B CG  1 
ATOM   7230  C CD1 . LEU B 1 375 ? -0.577  33.662  38.868  1.00 54.07  ? 375 LEU B CD1 1 
ATOM   7231  C CD2 . LEU B 1 375 ? 0.695   32.014  40.203  1.00 58.65  ? 375 LEU B CD2 1 
ATOM   7232  N N   . GLU B 1 376 ? -0.371  35.047  44.360  1.00 58.12  ? 376 GLU B N   1 
ATOM   7233  C CA  . GLU B 1 376 ? -0.104  36.118  45.311  1.00 66.78  ? 376 GLU B CA  1 
ATOM   7234  C C   . GLU B 1 376 ? 0.840   35.676  46.423  1.00 69.30  ? 376 GLU B C   1 
ATOM   7235  O O   . GLU B 1 376 ? 1.504   36.515  47.044  1.00 63.06  ? 376 GLU B O   1 
ATOM   7236  C CB  . GLU B 1 376 ? -1.422  36.595  45.915  1.00 64.14  ? 376 GLU B CB  1 
ATOM   7237  C CG  . GLU B 1 376 ? -1.635  38.078  45.897  1.00 61.38  ? 376 GLU B CG  1 
ATOM   7238  C CD  . GLU B 1 376 ? -2.864  38.454  46.684  1.00 73.06  ? 376 GLU B CD  1 
ATOM   7239  O OE1 . GLU B 1 376 ? -3.753  37.589  46.833  1.00 73.70  ? 376 GLU B OE1 1 
ATOM   7240  O OE2 . GLU B 1 376 ? -2.934  39.598  47.174  1.00 79.23  ? 376 GLU B OE2 1 
ATOM   7241  N N   . LYS B 1 377 ? 0.905   34.373  46.701  1.00 68.54  ? 377 LYS B N   1 
ATOM   7242  C CA  . LYS B 1 377 ? 1.696   33.849  47.806  1.00 70.25  ? 377 LYS B CA  1 
ATOM   7243  C C   . LYS B 1 377 ? 2.889   33.022  47.334  1.00 71.16  ? 377 LYS B C   1 
ATOM   7244  O O   . LYS B 1 377 ? 3.505   32.318  48.142  1.00 83.34  ? 377 LYS B O   1 
ATOM   7245  C CB  . LYS B 1 377 ? 0.812   33.025  48.746  1.00 71.48  ? 377 LYS B CB  1 
ATOM   7246  C CG  . LYS B 1 377 ? -0.323  33.815  49.398  1.00 70.61  ? 377 LYS B CG  1 
ATOM   7247  C CD  . LYS B 1 377 ? 0.181   35.093  50.066  1.00 72.18  ? 377 LYS B CD  1 
ATOM   7248  C CE  . LYS B 1 377 ? -0.852  35.661  51.038  1.00 76.65  ? 377 LYS B CE  1 
ATOM   7249  N NZ  . LYS B 1 377 ? -0.649  37.112  51.322  1.00 70.58  ? 377 LYS B NZ  1 
ATOM   7250  N N   . GLU B 1 378 ? 3.235   33.099  46.047  1.00 73.08  ? 378 GLU B N   1 
ATOM   7251  C CA  . GLU B 1 378 ? 4.422   32.442  45.502  1.00 78.87  ? 378 GLU B CA  1 
ATOM   7252  C C   . GLU B 1 378 ? 5.434   33.517  45.126  1.00 76.74  ? 378 GLU B C   1 
ATOM   7253  O O   . GLU B 1 378 ? 5.235   34.257  44.158  1.00 75.64  ? 378 GLU B O   1 
ATOM   7254  C CB  . GLU B 1 378 ? 4.082   31.574  44.289  1.00 71.96  ? 378 GLU B CB  1 
ATOM   7255  C CG  . GLU B 1 378 ? 3.011   30.492  44.504  1.00 83.14  ? 378 GLU B CG  1 
ATOM   7256  C CD  . GLU B 1 378 ? 3.292   29.529  45.661  1.00 95.37  ? 378 GLU B CD  1 
ATOM   7257  O OE1 . GLU B 1 378 ? 3.410   29.968  46.830  1.00 93.42  ? 378 GLU B OE1 1 
ATOM   7258  O OE2 . GLU B 1 378 ? 3.387   28.311  45.389  1.00 103.17 ? 378 GLU B OE2 1 
ATOM   7259  N N   . GLU B 1 379 ? 6.529   33.583  45.875  1.00 74.47  ? 379 GLU B N   1 
ATOM   7260  C CA  . GLU B 1 379 ? 7.531   34.613  45.651  1.00 76.48  ? 379 GLU B CA  1 
ATOM   7261  C C   . GLU B 1 379 ? 8.395   34.324  44.434  1.00 78.64  ? 379 GLU B C   1 
ATOM   7262  O O   . GLU B 1 379 ? 9.018   35.246  43.893  1.00 79.04  ? 379 GLU B O   1 
ATOM   7263  C CB  . GLU B 1 379 ? 8.376   34.713  46.895  1.00 73.80  ? 379 GLU B CB  1 
ATOM   7264  C CG  . GLU B 1 379 ? 7.553   34.254  48.057  1.00 88.46  ? 379 GLU B CG  1 
ATOM   7265  C CD  . GLU B 1 379 ? 8.137   34.663  49.383  1.00 104.04 ? 379 GLU B CD  1 
ATOM   7266  O OE1 . GLU B 1 379 ? 7.499   35.435  50.114  1.00 102.96 ? 379 GLU B OE1 1 
ATOM   7267  O OE2 . GLU B 1 379 ? 9.246   34.213  49.714  1.00 104.88 ? 379 GLU B OE2 1 
ATOM   7268  N N   . TRP B 1 380 ? 8.444   33.072  43.990  1.00 69.71  ? 380 TRP B N   1 
ATOM   7269  C CA  . TRP B 1 380 ? 9.214   32.738  42.804  1.00 64.93  ? 380 TRP B CA  1 
ATOM   7270  C C   . TRP B 1 380 ? 8.497   33.092  41.507  1.00 62.47  ? 380 TRP B C   1 
ATOM   7271  O O   . TRP B 1 380 ? 9.058   32.856  40.437  1.00 62.68  ? 380 TRP B O   1 
ATOM   7272  C CB  . TRP B 1 380 ? 9.581   31.253  42.827  1.00 61.85  ? 380 TRP B CB  1 
ATOM   7273  C CG  . TRP B 1 380 ? 8.425   30.334  42.658  1.00 64.43  ? 380 TRP B CG  1 
ATOM   7274  C CD1 . TRP B 1 380 ? 7.600   29.864  43.634  1.00 65.21  ? 380 TRP B CD1 1 
ATOM   7275  C CD2 . TRP B 1 380 ? 7.963   29.766  41.431  1.00 63.34  ? 380 TRP B CD2 1 
ATOM   7276  N NE1 . TRP B 1 380 ? 6.648   29.035  43.090  1.00 74.02  ? 380 TRP B NE1 1 
ATOM   7277  C CE2 . TRP B 1 380 ? 6.850   28.959  41.738  1.00 62.66  ? 380 TRP B CE2 1 
ATOM   7278  C CE3 . TRP B 1 380 ? 8.384   29.861  40.101  1.00 61.71  ? 380 TRP B CE3 1 
ATOM   7279  C CZ2 . TRP B 1 380 ? 6.154   28.255  40.765  1.00 61.95  ? 380 TRP B CZ2 1 
ATOM   7280  C CZ3 . TRP B 1 380 ? 7.691   29.162  39.136  1.00 60.95  ? 380 TRP B CZ3 1 
ATOM   7281  C CH2 . TRP B 1 380 ? 6.589   28.369  39.473  1.00 67.53  ? 380 TRP B CH2 1 
ATOM   7282  N N   . ILE B 1 381 ? 7.283   33.645  41.567  1.00 69.22  ? 381 ILE B N   1 
ATOM   7283  C CA  . ILE B 1 381 ? 6.579   34.161  40.395  1.00 68.47  ? 381 ILE B CA  1 
ATOM   7284  C C   . ILE B 1 381 ? 6.316   35.643  40.622  1.00 66.86  ? 381 ILE B C   1 
ATOM   7285  O O   . ILE B 1 381 ? 5.931   36.053  41.722  1.00 66.69  ? 381 ILE B O   1 
ATOM   7286  C CB  . ILE B 1 381 ? 5.250   33.423  40.114  1.00 67.33  ? 381 ILE B CB  1 
ATOM   7287  C CG1 . ILE B 1 381 ? 5.450   31.912  40.010  1.00 68.98  ? 381 ILE B CG1 1 
ATOM   7288  C CG2 . ILE B 1 381 ? 4.588   33.946  38.832  1.00 53.28  ? 381 ILE B CG2 1 
ATOM   7289  C CD1 . ILE B 1 381 ? 4.240   31.121  40.476  1.00 65.11  ? 381 ILE B CD1 1 
ATOM   7290  N N   . GLU B 1 382 ? 6.523   36.441  39.578  1.00 56.08  ? 382 GLU B N   1 
ATOM   7291  C CA  . GLU B 1 382 ? 6.337   37.888  39.632  1.00 58.52  ? 382 GLU B CA  1 
ATOM   7292  C C   . GLU B 1 382 ? 5.479   38.280  38.436  1.00 56.39  ? 382 GLU B C   1 
ATOM   7293  O O   . GLU B 1 382 ? 5.994   38.416  37.323  1.00 58.17  ? 382 GLU B O   1 
ATOM   7294  C CB  . GLU B 1 382 ? 7.676   38.626  39.621  1.00 58.26  ? 382 GLU B CB  1 
ATOM   7295  C CG  . GLU B 1 382 ? 7.577   40.120  39.950  1.00 67.33  ? 382 GLU B CG  1 
ATOM   7296  C CD  . GLU B 1 382 ? 8.863   40.700  40.534  1.00 85.32  ? 382 GLU B CD  1 
ATOM   7297  O OE1 . GLU B 1 382 ? 9.521   40.009  41.343  1.00 83.83  ? 382 GLU B OE1 1 
ATOM   7298  O OE2 . GLU B 1 382 ? 9.210   41.854  40.191  1.00 84.60  ? 382 GLU B OE2 1 
ATOM   7299  N N   . THR B 1 383 ? 4.177   38.449  38.659  1.00 60.77  ? 383 THR B N   1 
ATOM   7300  C CA  . THR B 1 383 ? 3.309   38.949  37.603  1.00 57.83  ? 383 THR B CA  1 
ATOM   7301  C C   . THR B 1 383 ? 3.684   40.388  37.285  1.00 58.14  ? 383 THR B C   1 
ATOM   7302  O O   . THR B 1 383 ? 4.030   41.169  38.178  1.00 52.75  ? 383 THR B O   1 
ATOM   7303  C CB  . THR B 1 383 ? 1.835   38.850  38.002  1.00 51.08  ? 383 THR B CB  1 
ATOM   7304  O OG1 . THR B 1 383 ? 1.545   39.773  39.060  1.00 55.66  ? 383 THR B OG1 1 
ATOM   7305  C CG2 . THR B 1 383 ? 1.507   37.441  38.466  1.00 48.79  ? 383 THR B CG2 1 
ATOM   7306  N N   . LEU B 1 384 ? 3.638   40.730  35.999  1.00 50.83  ? 384 LEU B N   1 
ATOM   7307  C CA  . LEU B 1 384 ? 4.129   42.020  35.545  1.00 49.49  ? 384 LEU B CA  1 
ATOM   7308  C C   . LEU B 1 384 ? 3.169   42.641  34.544  1.00 47.46  ? 384 LEU B C   1 
ATOM   7309  O O   . LEU B 1 384 ? 2.435   41.948  33.834  1.00 49.80  ? 384 LEU B O   1 
ATOM   7310  C CB  . LEU B 1 384 ? 5.507   41.894  34.900  1.00 46.70  ? 384 LEU B CB  1 
ATOM   7311  C CG  . LEU B 1 384 ? 6.627   41.448  35.824  1.00 49.95  ? 384 LEU B CG  1 
ATOM   7312  C CD1 . LEU B 1 384 ? 7.689   40.821  34.962  1.00 59.33  ? 384 LEU B CD1 1 
ATOM   7313  C CD2 . LEU B 1 384 ? 7.174   42.617  36.626  1.00 57.37  ? 384 LEU B CD2 1 
ATOM   7314  N N   . THR B 1 385 ? 3.200   43.968  34.492  1.00 47.66  ? 385 THR B N   1 
ATOM   7315  C CA  . THR B 1 385 ? 2.503   44.711  33.462  1.00 41.66  ? 385 THR B CA  1 
ATOM   7316  C C   . THR B 1 385 ? 3.300   44.673  32.170  1.00 47.07  ? 385 THR B C   1 
ATOM   7317  O O   . THR B 1 385 ? 4.495   44.363  32.155  1.00 49.69  ? 385 THR B O   1 
ATOM   7318  C CB  . THR B 1 385 ? 2.306   46.164  33.873  1.00 40.68  ? 385 THR B CB  1 
ATOM   7319  O OG1 . THR B 1 385 ? 3.514   46.887  33.624  1.00 48.01  ? 385 THR B OG1 1 
ATOM   7320  C CG2 . THR B 1 385 ? 2.006   46.241  35.353  1.00 52.34  ? 385 THR B CG2 1 
ATOM   7321  N N   . LEU B 1 386 ? 2.620   45.010  31.073  1.00 49.22  ? 386 LEU B N   1 
ATOM   7322  C CA  . LEU B 1 386 ? 3.297   45.093  29.785  1.00 49.19  ? 386 LEU B CA  1 
ATOM   7323  C C   . LEU B 1 386 ? 4.414   46.131  29.821  1.00 56.30  ? 386 LEU B C   1 
ATOM   7324  O O   . LEU B 1 386 ? 5.457   45.955  29.179  1.00 55.77  ? 386 LEU B O   1 
ATOM   7325  C CB  . LEU B 1 386 ? 2.285   45.415  28.687  1.00 49.51  ? 386 LEU B CB  1 
ATOM   7326  C CG  . LEU B 1 386 ? 1.117   44.438  28.535  1.00 49.50  ? 386 LEU B CG  1 
ATOM   7327  C CD1 . LEU B 1 386 ? 0.191   44.888  27.411  1.00 46.03  ? 386 LEU B CD1 1 
ATOM   7328  C CD2 . LEU B 1 386 ? 1.617   43.021  28.277  1.00 35.85  ? 386 LEU B CD2 1 
ATOM   7329  N N   . GLU B 1 387 ? 4.219   47.213  30.582  1.00 57.57  ? 387 GLU B N   1 
ATOM   7330  C CA  . GLU B 1 387 ? 5.273   48.209  30.745  1.00 53.50  ? 387 GLU B CA  1 
ATOM   7331  C C   . GLU B 1 387 ? 6.435   47.638  31.545  1.00 55.12  ? 387 GLU B C   1 
ATOM   7332  O O   . GLU B 1 387 ? 7.603   47.792  31.162  1.00 55.89  ? 387 GLU B O   1 
ATOM   7333  C CB  . GLU B 1 387 ? 4.716   49.466  31.416  1.00 52.26  ? 387 GLU B CB  1 
ATOM   7334  C CG  . GLU B 1 387 ? 5.266   50.766  30.842  1.00 69.26  ? 387 GLU B CG  1 
ATOM   7335  C CD  . GLU B 1 387 ? 5.070   51.957  31.761  1.00 94.47  ? 387 GLU B CD  1 
ATOM   7336  O OE1 . GLU B 1 387 ? 5.026   51.760  32.994  1.00 100.31 ? 387 GLU B OE1 1 
ATOM   7337  O OE2 . GLU B 1 387 ? 4.971   53.094  31.249  1.00 97.92  ? 387 GLU B OE2 1 
ATOM   7338  N N   . GLU B 1 388 ? 6.131   46.962  32.658  1.00 49.15  ? 388 GLU B N   1 
ATOM   7339  C CA  . GLU B 1 388 ? 7.186   46.393  33.493  1.00 54.21  ? 388 GLU B CA  1 
ATOM   7340  C C   . GLU B 1 388 ? 7.971   45.326  32.740  1.00 53.98  ? 388 GLU B C   1 
ATOM   7341  O O   . GLU B 1 388 ? 9.186   45.193  32.923  1.00 52.86  ? 388 GLU B O   1 
ATOM   7342  C CB  . GLU B 1 388 ? 6.593   45.818  34.782  1.00 48.18  ? 388 GLU B CB  1 
ATOM   7343  C CG  . GLU B 1 388 ? 6.383   46.851  35.885  1.00 44.59  ? 388 GLU B CG  1 
ATOM   7344  C CD  . GLU B 1 388 ? 5.314   46.439  36.880  1.00 60.73  ? 388 GLU B CD  1 
ATOM   7345  O OE1 . GLU B 1 388 ? 4.958   45.239  36.919  1.00 59.73  ? 388 GLU B OE1 1 
ATOM   7346  O OE2 . GLU B 1 388 ? 4.829   47.314  37.628  1.00 67.99  ? 388 GLU B OE2 1 
ATOM   7347  N N   . ALA B 1 389 ? 7.295   44.557  31.885  1.00 51.71  ? 389 ALA B N   1 
ATOM   7348  C CA  . ALA B 1 389 ? 8.009   43.609  31.038  1.00 43.78  ? 389 ALA B CA  1 
ATOM   7349  C C   . ALA B 1 389 ? 8.822   44.324  29.972  1.00 51.93  ? 389 ALA B C   1 
ATOM   7350  O O   . ALA B 1 389 ? 9.808   43.774  29.470  1.00 62.82  ? 389 ALA B O   1 
ATOM   7351  C CB  . ALA B 1 389 ? 7.039   42.631  30.386  1.00 46.62  ? 389 ALA B CB  1 
ATOM   7352  N N   . MET B 1 390 ? 8.429   45.541  29.612  1.00 49.38  ? 390 MET B N   1 
ATOM   7353  C CA  . MET B 1 390 ? 9.175   46.294  28.618  1.00 51.85  ? 390 MET B CA  1 
ATOM   7354  C C   . MET B 1 390 ? 10.394  46.984  29.213  1.00 60.03  ? 390 MET B C   1 
ATOM   7355  O O   . MET B 1 390 ? 11.348  47.272  28.482  1.00 54.45  ? 390 MET B O   1 
ATOM   7356  C CB  . MET B 1 390 ? 8.267   47.329  27.958  1.00 56.96  ? 390 MET B CB  1 
ATOM   7357  C CG  . MET B 1 390 ? 7.712   46.926  26.594  1.00 64.01  ? 390 MET B CG  1 
ATOM   7358  S SD  . MET B 1 390 ? 8.904   46.124  25.517  1.00 82.15  ? 390 MET B SD  1 
ATOM   7359  C CE  . MET B 1 390 ? 9.367   47.505  24.465  1.00 66.31  ? 390 MET B CE  1 
ATOM   7360  N N   . ARG B 1 391 ? 10.388  47.248  30.519  1.00 62.63  ? 391 ARG B N   1 
ATOM   7361  C CA  . ARG B 1 391 ? 11.510  47.894  31.186  1.00 57.28  ? 391 ARG B CA  1 
ATOM   7362  C C   . ARG B 1 391 ? 12.378  46.920  31.973  1.00 57.08  ? 391 ARG B C   1 
ATOM   7363  O O   . ARG B 1 391 ? 13.391  47.339  32.537  1.00 61.54  ? 391 ARG B O   1 
ATOM   7364  C CB  . ARG B 1 391 ? 11.011  49.004  32.121  1.00 53.89  ? 391 ARG B CB  1 
ATOM   7365  C CG  . ARG B 1 391 ? 9.826   49.797  31.599  1.00 57.97  ? 391 ARG B CG  1 
ATOM   7366  C CD  . ARG B 1 391 ? 10.268  51.127  31.018  1.00 61.83  ? 391 ARG B CD  1 
ATOM   7367  N NE  . ARG B 1 391 ? 10.994  50.949  29.766  1.00 63.62  ? 391 ARG B NE  1 
ATOM   7368  C CZ  . ARG B 1 391 ? 10.444  50.603  28.610  1.00 56.29  ? 391 ARG B CZ  1 
ATOM   7369  N NH1 . ARG B 1 391 ? 9.136   50.448  28.484  1.00 62.39  ? 391 ARG B NH1 1 
ATOM   7370  N NH2 . ARG B 1 391 ? 11.226  50.406  27.553  1.00 56.29  ? 391 ARG B NH2 1 
ATOM   7371  N N   . LYS B 1 392 ? 12.024  45.636  32.006  1.00 58.33  ? 392 LYS B N   1 
ATOM   7372  C CA  . LYS B 1 392 ? 12.718  44.692  32.871  1.00 62.35  ? 392 LYS B CA  1 
ATOM   7373  C C   . LYS B 1 392 ? 14.107  44.365  32.330  1.00 70.57  ? 392 LYS B C   1 
ATOM   7374  O O   . LYS B 1 392 ? 14.269  44.010  31.158  1.00 64.96  ? 392 LYS B O   1 
ATOM   7375  C CB  . LYS B 1 392 ? 11.899  43.415  33.029  1.00 58.93  ? 392 LYS B CB  1 
ATOM   7376  C CG  . LYS B 1 392 ? 12.079  42.724  34.379  1.00 63.36  ? 392 LYS B CG  1 
ATOM   7377  C CD  . LYS B 1 392 ? 11.438  43.518  35.504  1.00 55.63  ? 392 LYS B CD  1 
ATOM   7378  C CE  . LYS B 1 392 ? 11.031  42.607  36.646  1.00 56.99  ? 392 LYS B CE  1 
ATOM   7379  N NZ  . LYS B 1 392 ? 10.611  43.380  37.846  1.00 66.13  ? 392 LYS B NZ  1 
ATOM   7380  N N   . GLU B 1 393 ? 15.107  44.478  33.205  1.00 73.53  ? 393 GLU B N   1 
ATOM   7381  C CA  . GLU B 1 393 ? 16.493  44.179  32.868  1.00 77.43  ? 393 GLU B CA  1 
ATOM   7382  C C   . GLU B 1 393 ? 16.898  42.744  33.172  1.00 81.32  ? 393 GLU B C   1 
ATOM   7383  O O   . GLU B 1 393 ? 17.897  42.267  32.615  1.00 83.02  ? 393 GLU B O   1 
ATOM   7384  C CB  . GLU B 1 393 ? 17.443  45.124  33.613  1.00 83.08  ? 393 GLU B CB  1 
ATOM   7385  C CG  . GLU B 1 393 ? 17.868  46.366  32.822  1.00 90.74  ? 393 GLU B CG  1 
ATOM   7386  C CD  . GLU B 1 393 ? 17.805  46.170  31.312  1.00 95.72  ? 393 GLU B CD  1 
ATOM   7387  O OE1 . GLU B 1 393 ? 18.604  45.368  30.769  1.00 88.60  ? 393 GLU B OE1 1 
ATOM   7388  O OE2 . GLU B 1 393 ? 16.953  46.830  30.674  1.00 90.60  ? 393 GLU B OE2 1 
ATOM   7389  N N   . ASP B 1 394 ? 16.149  42.047  34.031  1.00 76.77  ? 394 ASP B N   1 
ATOM   7390  C CA  . ASP B 1 394 ? 16.473  40.670  34.385  1.00 73.88  ? 394 ASP B CA  1 
ATOM   7391  C C   . ASP B 1 394 ? 16.223  39.692  33.244  1.00 67.82  ? 394 ASP B C   1 
ATOM   7392  O O   . ASP B 1 394 ? 16.726  38.564  33.289  1.00 71.96  ? 394 ASP B O   1 
ATOM   7393  C CB  . ASP B 1 394 ? 15.653  40.225  35.605  1.00 76.12  ? 394 ASP B CB  1 
ATOM   7394  C CG  . ASP B 1 394 ? 15.602  41.275  36.706  1.00 83.74  ? 394 ASP B CG  1 
ATOM   7395  O OD1 . ASP B 1 394 ? 16.374  42.255  36.643  1.00 98.28  ? 394 ASP B OD1 1 
ATOM   7396  O OD2 . ASP B 1 394 ? 14.783  41.121  37.638  1.00 92.92  ? 394 ASP B OD2 1 
ATOM   7397  N N   . VAL B 1 395 ? 15.455  40.077  32.241  1.00 69.29  ? 395 VAL B N   1 
ATOM   7398  C CA  . VAL B 1 395 ? 15.028  39.142  31.205  1.00 68.89  ? 395 VAL B CA  1 
ATOM   7399  C C   . VAL B 1 395 ? 16.040  39.141  30.070  1.00 56.74  ? 395 VAL B C   1 
ATOM   7400  O O   . VAL B 1 395 ? 16.656  40.162  29.741  1.00 58.67  ? 395 VAL B O   1 
ATOM   7401  C CB  . VAL B 1 395 ? 13.606  39.471  30.697  1.00 64.74  ? 395 VAL B CB  1 
ATOM   7402  C CG1 . VAL B 1 395 ? 12.677  39.808  31.864  1.00 50.69  ? 395 VAL B CG1 1 
ATOM   7403  C CG2 . VAL B 1 395 ? 13.644  40.601  29.694  1.00 63.53  ? 395 VAL B CG2 1 
ATOM   7404  N N   . LYS B 1 396 ? 16.224  37.967  29.477  1.00 54.16  ? 396 LYS B N   1 
ATOM   7405  C CA  . LYS B 1 396 ? 17.165  37.813  28.379  1.00 55.77  ? 396 LYS B CA  1 
ATOM   7406  C C   . LYS B 1 396 ? 16.520  38.286  27.084  1.00 54.39  ? 396 LYS B C   1 
ATOM   7407  O O   . LYS B 1 396 ? 15.314  38.128  26.884  1.00 52.62  ? 396 LYS B O   1 
ATOM   7408  C CB  . LYS B 1 396 ? 17.621  36.357  28.268  1.00 55.22  ? 396 LYS B CB  1 
ATOM   7409  C CG  . LYS B 1 396 ? 18.809  36.000  29.170  1.00 65.87  ? 396 LYS B CG  1 
ATOM   7410  C CD  . LYS B 1 396 ? 19.565  34.769  28.659  1.00 69.64  ? 396 LYS B CD  1 
ATOM   7411  C CE  . LYS B 1 396 ? 20.060  34.952  27.227  1.00 74.03  ? 396 LYS B CE  1 
ATOM   7412  N NZ  . LYS B 1 396 ? 21.209  35.891  27.131  1.00 60.42  ? 396 LYS B NZ  1 
ATOM   7413  N N   . THR B 1 397 ? 17.321  38.898  26.214  1.00 58.54  ? 397 THR B N   1 
ATOM   7414  C CA  . THR B 1 397 ? 16.800  39.541  25.013  1.00 56.00  ? 397 THR B CA  1 
ATOM   7415  C C   . THR B 1 397 ? 17.605  39.120  23.793  1.00 57.33  ? 397 THR B C   1 
ATOM   7416  O O   . THR B 1 397 ? 18.840  39.190  23.802  1.00 66.69  ? 397 THR B O   1 
ATOM   7417  C CB  . THR B 1 397 ? 16.814  41.068  25.147  1.00 59.77  ? 397 THR B CB  1 
ATOM   7418  O OG1 . THR B 1 397 ? 15.884  41.479  26.159  1.00 57.77  ? 397 THR B OG1 1 
ATOM   7419  C CG2 . THR B 1 397 ? 16.430  41.701  23.835  1.00 57.49  ? 397 THR B CG2 1 
ATOM   7420  N N   . GLU B 1 398 ? 16.902  38.693  22.743  1.00 52.50  ? 398 GLU B N   1 
ATOM   7421  C CA  . GLU B 1 398 ? 17.511  38.308  21.478  1.00 52.71  ? 398 GLU B CA  1 
ATOM   7422  C C   . GLU B 1 398 ? 16.913  39.143  20.357  1.00 48.96  ? 398 GLU B C   1 
ATOM   7423  O O   . GLU B 1 398 ? 15.722  39.464  20.380  1.00 54.83  ? 398 GLU B O   1 
ATOM   7424  C CB  . GLU B 1 398 ? 17.310  36.810  21.187  1.00 55.34  ? 398 GLU B CB  1 
ATOM   7425  C CG  . GLU B 1 398 ? 17.760  36.364  19.789  1.00 60.61  ? 398 GLU B CG  1 
ATOM   7426  C CD  . GLU B 1 398 ? 18.207  34.909  19.741  1.00 67.66  ? 398 GLU B CD  1 
ATOM   7427  O OE1 . GLU B 1 398 ? 18.265  34.277  20.814  1.00 66.25  ? 398 GLU B OE1 1 
ATOM   7428  O OE2 . GLU B 1 398 ? 18.516  34.402  18.637  1.00 77.80  ? 398 GLU B OE2 1 
ATOM   7429  N N   . VAL B 1 399 ? 17.743  39.498  19.376  1.00 57.31  ? 399 VAL B N   1 
ATOM   7430  C CA  . VAL B 1 399 ? 17.304  40.264  18.212  1.00 57.99  ? 399 VAL B CA  1 
ATOM   7431  C C   . VAL B 1 399 ? 17.100  39.321  17.038  1.00 52.43  ? 399 VAL B C   1 
ATOM   7432  O O   . VAL B 1 399 ? 17.991  38.532  16.699  1.00 57.92  ? 399 VAL B O   1 
ATOM   7433  C CB  . VAL B 1 399 ? 18.312  41.358  17.833  1.00 56.04  ? 399 VAL B CB  1 
ATOM   7434  C CG1 . VAL B 1 399 ? 17.799  42.098  16.601  1.00 46.04  ? 399 VAL B CG1 1 
ATOM   7435  C CG2 . VAL B 1 399 ? 18.552  42.304  18.994  1.00 59.27  ? 399 VAL B CG2 1 
ATOM   7436  N N   . ILE B 1 400 ? 15.942  39.424  16.402  1.00 47.54  ? 400 ILE B N   1 
ATOM   7437  C CA  . ILE B 1 400 ? 15.621  38.657  15.208  1.00 47.35  ? 400 ILE B CA  1 
ATOM   7438  C C   . ILE B 1 400 ? 15.254  39.640  14.105  1.00 44.91  ? 400 ILE B C   1 
ATOM   7439  O O   . ILE B 1 400 ? 14.799  40.757  14.367  1.00 45.90  ? 400 ILE B O   1 
ATOM   7440  C CB  . ILE B 1 400 ? 14.475  37.653  15.455  1.00 46.64  ? 400 ILE B CB  1 
ATOM   7441  C CG1 . ILE B 1 400 ? 13.171  38.379  15.795  1.00 43.64  ? 400 ILE B CG1 1 
ATOM   7442  C CG2 . ILE B 1 400 ? 14.842  36.673  16.563  1.00 49.04  ? 400 ILE B CG2 1 
ATOM   7443  C CD1 . ILE B 1 400 ? 11.975  37.465  15.730  1.00 37.57  ? 400 ILE B CD1 1 
ATOM   7444  N N   . GLU B 1 401 ? 15.444  39.217  12.860  1.00 46.03  ? 401 GLU B N   1 
ATOM   7445  C CA  . GLU B 1 401 ? 15.309  40.134  11.739  1.00 50.97  ? 401 GLU B CA  1 
ATOM   7446  C C   . GLU B 1 401 ? 14.194  39.777  10.759  1.00 53.14  ? 401 GLU B C   1 
ATOM   7447  O O   . GLU B 1 401 ? 14.053  40.463  9.741   1.00 51.23  ? 401 GLU B O   1 
ATOM   7448  C CB  . GLU B 1 401 ? 16.646  40.245  10.987  1.00 54.57  ? 401 GLU B CB  1 
ATOM   7449  C CG  . GLU B 1 401 ? 17.804  40.820  11.831  1.00 56.79  ? 401 GLU B CG  1 
ATOM   7450  C CD  . GLU B 1 401 ? 18.004  42.318  11.636  1.00 59.33  ? 401 GLU B CD  1 
ATOM   7451  O OE1 . GLU B 1 401 ? 17.665  42.828  10.547  1.00 56.98  ? 401 GLU B OE1 1 
ATOM   7452  O OE2 . GLU B 1 401 ? 18.511  42.986  12.567  1.00 60.26  ? 401 GLU B OE2 1 
ATOM   7453  N N   . SER B 1 402 ? 13.385  38.752  11.035  1.00 56.71  ? 402 SER B N   1 
ATOM   7454  C CA  . SER B 1 402 ? 12.326  38.357  10.109  1.00 55.27  ? 402 SER B CA  1 
ATOM   7455  C C   . SER B 1 402 ? 11.335  37.437  10.814  1.00 52.27  ? 402 SER B C   1 
ATOM   7456  O O   . SER B 1 402 ? 11.675  36.760  11.789  1.00 47.47  ? 402 SER B O   1 
ATOM   7457  C CB  . SER B 1 402 ? 12.900  37.665  8.864   1.00 41.54  ? 402 SER B CB  1 
ATOM   7458  O OG  . SER B 1 402 ? 13.447  36.399  9.195   1.00 49.22  ? 402 SER B OG  1 
ATOM   7459  N N   . VAL B 1 403 ? 10.104  37.419  10.306  1.00 45.01  ? 403 VAL B N   1 
ATOM   7460  C CA  . VAL B 1 403 ? 9.079   36.487  10.762  1.00 53.66  ? 403 VAL B CA  1 
ATOM   7461  C C   . VAL B 1 403 ? 8.368   35.934  9.541   1.00 54.27  ? 403 VAL B C   1 
ATOM   7462  O O   . VAL B 1 403 ? 8.229   36.613  8.520   1.00 59.71  ? 403 VAL B O   1 
ATOM   7463  C CB  . VAL B 1 403 ? 8.046   37.140  11.706  1.00 54.41  ? 403 VAL B CB  1 
ATOM   7464  C CG1 . VAL B 1 403 ? 8.648   37.409  13.064  1.00 43.60  ? 403 VAL B CG1 1 
ATOM   7465  C CG2 . VAL B 1 403 ? 7.535   38.420  11.090  1.00 51.38  ? 403 VAL B CG2 1 
ATOM   7466  N N   . LYS B 1 404 ? 7.907   34.697  9.648   1.00 52.90  ? 404 LYS B N   1 
ATOM   7467  C CA  . LYS B 1 404 ? 7.055   34.128  8.617   1.00 48.15  ? 404 LYS B CA  1 
ATOM   7468  C C   . LYS B 1 404 ? 5.605   34.432  8.964   1.00 57.01  ? 404 LYS B C   1 
ATOM   7469  O O   . LYS B 1 404 ? 5.160   34.170  10.087  1.00 55.50  ? 404 LYS B O   1 
ATOM   7470  C CB  . LYS B 1 404 ? 7.285   32.627  8.483   1.00 44.76  ? 404 LYS B CB  1 
ATOM   7471  C CG  . LYS B 1 404 ? 8.074   32.249  7.243   1.00 56.56  ? 404 LYS B CG  1 
ATOM   7472  C CD  . LYS B 1 404 ? 8.137   30.738  7.082   1.00 65.32  ? 404 LYS B CD  1 
ATOM   7473  C CE  . LYS B 1 404 ? 9.500   30.289  6.568   1.00 70.16  ? 404 LYS B CE  1 
ATOM   7474  N NZ  . LYS B 1 404 ? 9.680   28.806  6.599   1.00 62.26  ? 404 LYS B NZ  1 
ATOM   7475  N N   . ALA B 1 405 ? 4.881   34.993  7.997   1.00 57.89  ? 405 ALA B N   1 
ATOM   7476  C CA  . ALA B 1 405 ? 3.522   35.459  8.232   1.00 49.35  ? 405 ALA B CA  1 
ATOM   7477  C C   . ALA B 1 405 ? 2.601   34.309  8.613   1.00 49.98  ? 405 ALA B C   1 
ATOM   7478  O O   . ALA B 1 405 ? 2.546   33.285  7.930   1.00 56.98  ? 405 ALA B O   1 
ATOM   7479  C CB  . ALA B 1 405 ? 2.991   36.168  6.992   1.00 50.18  ? 405 ALA B CB  1 
ATOM   7480  N N   . GLY B 1 406 ? 1.871   34.492  9.704   1.00 45.71  ? 406 GLY B N   1 
ATOM   7481  C CA  . GLY B 1 406 ? 0.944   33.478  10.158  1.00 51.00  ? 406 GLY B CA  1 
ATOM   7482  C C   . GLY B 1 406 ? 0.023   34.036  11.217  1.00 50.65  ? 406 GLY B C   1 
ATOM   7483  O O   . GLY B 1 406 ? 0.001   35.240  11.471  1.00 53.38  ? 406 GLY B O   1 
ATOM   7484  N N   . THR B 1 407 ? -0.745  33.136  11.835  1.00 55.22  ? 407 THR B N   1 
ATOM   7485  C CA  . THR B 1 407 ? -1.698  33.464  12.897  1.00 53.27  ? 407 THR B CA  1 
ATOM   7486  C C   . THR B 1 407 ? -1.542  32.457  14.031  1.00 47.01  ? 407 THR B C   1 
ATOM   7487  O O   . THR B 1 407 ? -0.760  31.508  13.938  1.00 51.89  ? 407 THR B O   1 
ATOM   7488  C CB  . THR B 1 407 ? -3.148  33.440  12.395  1.00 48.36  ? 407 THR B CB  1 
ATOM   7489  O OG1 . THR B 1 407 ? -3.522  32.088  12.099  1.00 50.40  ? 407 THR B OG1 1 
ATOM   7490  C CG2 . THR B 1 407 ? -3.308  34.287  11.148  1.00 46.35  ? 407 THR B CG2 1 
ATOM   7491  N N   . TRP B 1 408 ? -2.307  32.641  15.108  1.00 45.78  ? 408 TRP B N   1 
ATOM   7492  C CA  . TRP B 1 408 ? -2.282  31.632  16.163  1.00 48.32  ? 408 TRP B CA  1 
ATOM   7493  C C   . TRP B 1 408 ? -3.150  30.421  15.846  1.00 50.99  ? 408 TRP B C   1 
ATOM   7494  O O   . TRP B 1 408 ? -3.203  29.492  16.660  1.00 52.65  ? 408 TRP B O   1 
ATOM   7495  C CB  . TRP B 1 408 ? -2.677  32.233  17.519  1.00 40.19  ? 408 TRP B CB  1 
ATOM   7496  C CG  . TRP B 1 408 ? -4.004  32.911  17.618  1.00 47.82  ? 408 TRP B CG  1 
ATOM   7497  C CD1 . TRP B 1 408 ? -4.958  33.041  16.646  1.00 51.46  ? 408 TRP B CD1 1 
ATOM   7498  C CD2 . TRP B 1 408 ? -4.519  33.572  18.777  1.00 45.95  ? 408 TRP B CD2 1 
ATOM   7499  N NE1 . TRP B 1 408 ? -6.038  33.743  17.136  1.00 41.03  ? 408 TRP B NE1 1 
ATOM   7500  C CE2 . TRP B 1 408 ? -5.789  34.080  18.442  1.00 45.45  ? 408 TRP B CE2 1 
ATOM   7501  C CE3 . TRP B 1 408 ? -4.026  33.782  20.068  1.00 36.78  ? 408 TRP B CE3 1 
ATOM   7502  C CZ2 . TRP B 1 408 ? -6.570  34.786  19.354  1.00 52.50  ? 408 TRP B CZ2 1 
ATOM   7503  C CZ3 . TRP B 1 408 ? -4.797  34.477  20.965  1.00 43.16  ? 408 TRP B CZ3 1 
ATOM   7504  C CH2 . TRP B 1 408 ? -6.054  34.974  20.609  1.00 48.84  ? 408 TRP B CH2 1 
ATOM   7505  N N   . PHE B 1 409 ? -3.789  30.393  14.678  1.00 51.41  ? 409 PHE B N   1 
ATOM   7506  C CA  . PHE B 1 409 ? -4.592  29.260  14.217  1.00 57.20  ? 409 PHE B CA  1 
ATOM   7507  C C   . PHE B 1 409 ? -3.796  28.488  13.160  1.00 54.04  ? 409 PHE B C   1 
ATOM   7508  O O   . PHE B 1 409 ? -3.915  28.747  11.960  1.00 59.26  ? 409 PHE B O   1 
ATOM   7509  C CB  . PHE B 1 409 ? -5.932  29.743  13.664  1.00 61.44  ? 409 PHE B CB  1 
ATOM   7510  C CG  . PHE B 1 409 ? -7.040  28.749  13.817  1.00 62.21  ? 409 PHE B CG  1 
ATOM   7511  C CD1 . PHE B 1 409 ? -7.013  27.547  13.123  1.00 69.87  ? 409 PHE B CD1 1 
ATOM   7512  C CD2 . PHE B 1 409 ? -8.108  29.009  14.659  1.00 59.62  ? 409 PHE B CD2 1 
ATOM   7513  C CE1 . PHE B 1 409 ? -8.031  26.621  13.265  1.00 64.56  ? 409 PHE B CE1 1 
ATOM   7514  C CE2 . PHE B 1 409 ? -9.134  28.082  14.806  1.00 64.32  ? 409 PHE B CE2 1 
ATOM   7515  C CZ  . PHE B 1 409 ? -9.093  26.890  14.108  1.00 61.29  ? 409 PHE B CZ  1 
ATOM   7516  N N   . ASP B 1 410 ? -2.989  27.529  13.623  1.00 55.66  ? 410 ASP B N   1 
ATOM   7517  C CA  . ASP B 1 410 ? -2.178  26.628  12.797  1.00 57.61  ? 410 ASP B CA  1 
ATOM   7518  C C   . ASP B 1 410 ? -1.046  27.348  12.071  1.00 56.32  ? 410 ASP B C   1 
ATOM   7519  O O   . ASP B 1 410 ? -0.469  26.805  11.124  1.00 55.34  ? 410 ASP B O   1 
ATOM   7520  C CB  . ASP B 1 410 ? -3.039  25.846  11.796  1.00 49.53  ? 410 ASP B CB  1 
ATOM   7521  C CG  . ASP B 1 410 ? -4.076  24.959  12.474  1.00 60.51  ? 410 ASP B CG  1 
ATOM   7522  O OD1 . ASP B 1 410 ? -4.423  25.211  13.653  1.00 63.58  ? 410 ASP B OD1 1 
ATOM   7523  O OD2 . ASP B 1 410 ? -4.547  24.004  11.823  1.00 67.87  ? 410 ASP B OD2 1 
ATOM   7524  N N   . GLY B 1 411 ? -0.705  28.559  12.497  1.00 61.67  ? 411 GLY B N   1 
ATOM   7525  C CA  . GLY B 1 411 ? 0.346   29.311  11.848  1.00 47.55  ? 411 GLY B CA  1 
ATOM   7526  C C   . GLY B 1 411 ? 0.034   29.782  10.448  1.00 56.21  ? 411 GLY B C   1 
ATOM   7527  O O   . GLY B 1 411 ? 0.932   30.296  9.782   1.00 55.74  ? 411 GLY B O   1 
ATOM   7528  N N   . ASN B 1 412 ? -1.210  29.639  9.979   1.00 60.92  ? 412 ASN B N   1 
ATOM   7529  C CA  . ASN B 1 412 ? -1.575  30.001  8.611   1.00 59.24  ? 412 ASN B CA  1 
ATOM   7530  C C   . ASN B 1 412 ? -2.840  30.853  8.602   1.00 54.96  ? 412 ASN B C   1 
ATOM   7531  O O   . ASN B 1 412 ? -3.445  31.130  9.643   1.00 56.94  ? 412 ASN B O   1 
ATOM   7532  C CB  . ASN B 1 412 ? -1.762  28.754  7.738   1.00 56.80  ? 412 ASN B CB  1 
ATOM   7533  C CG  . ASN B 1 412 ? -2.847  27.831  8.258   1.00 61.32  ? 412 ASN B CG  1 
ATOM   7534  O OD1 . ASN B 1 412 ? -4.022  28.203  8.345   1.00 69.68  ? 412 ASN B OD1 1 
ATOM   7535  N ND2 . ASN B 1 412 ? -2.457  26.613  8.606   1.00 56.90  ? 412 ASN B ND2 1 
ATOM   7536  N N   . PHE B 1 413 ? -3.244  31.261  7.398   1.00 51.49  ? 413 PHE B N   1 
ATOM   7537  C CA  . PHE B 1 413 ? -4.434  32.074  7.196   1.00 55.33  ? 413 PHE B CA  1 
ATOM   7538  C C   . PHE B 1 413 ? -5.601  31.278  6.623   1.00 60.48  ? 413 PHE B C   1 
ATOM   7539  O O   . PHE B 1 413 ? -6.561  31.879  6.124   1.00 64.41  ? 413 PHE B O   1 
ATOM   7540  C CB  . PHE B 1 413 ? -4.128  33.257  6.278   1.00 50.12  ? 413 PHE B CB  1 
ATOM   7541  C CG  . PHE B 1 413 ? -3.205  34.267  6.876   1.00 48.27  ? 413 PHE B CG  1 
ATOM   7542  C CD1 . PHE B 1 413 ? -3.683  35.229  7.752   1.00 49.90  ? 413 PHE B CD1 1 
ATOM   7543  C CD2 . PHE B 1 413 ? -1.865  34.277  6.542   1.00 53.41  ? 413 PHE B CD2 1 
ATOM   7544  C CE1 . PHE B 1 413 ? -2.840  36.172  8.293   1.00 56.05  ? 413 PHE B CE1 1 
ATOM   7545  C CE2 . PHE B 1 413 ? -1.012  35.217  7.082   1.00 54.28  ? 413 PHE B CE2 1 
ATOM   7546  C CZ  . PHE B 1 413 ? -1.498  36.165  7.959   1.00 58.56  ? 413 PHE B CZ  1 
ATOM   7547  N N   . LEU B 1 414 ? -5.543  29.945  6.685   1.00 58.03  ? 414 LEU B N   1 
ATOM   7548  C CA  . LEU B 1 414 ? -6.592  29.133  6.076   1.00 57.92  ? 414 LEU B CA  1 
ATOM   7549  C C   . LEU B 1 414 ? -7.915  29.216  6.828   1.00 56.85  ? 414 LEU B C   1 
ATOM   7550  O O   . LEU B 1 414 ? -8.953  28.830  6.279   1.00 54.85  ? 414 LEU B O   1 
ATOM   7551  C CB  . LEU B 1 414 ? -6.146  27.678  5.979   1.00 58.58  ? 414 LEU B CB  1 
ATOM   7552  C CG  . LEU B 1 414 ? -4.784  27.471  5.332   1.00 55.16  ? 414 LEU B CG  1 
ATOM   7553  C CD1 . LEU B 1 414 ? -4.425  26.000  5.395   1.00 51.42  ? 414 LEU B CD1 1 
ATOM   7554  C CD2 . LEU B 1 414 ? -4.795  27.988  3.910   1.00 59.27  ? 414 LEU B CD2 1 
ATOM   7555  N N   . LYS B 1 415 ? -7.908  29.709  8.065   1.00 52.94  ? 415 LYS B N   1 
ATOM   7556  C CA  . LYS B 1 415 ? -9.163  29.915  8.774   1.00 59.31  ? 415 LYS B CA  1 
ATOM   7557  C C   . LYS B 1 415 ? -9.983  31.050  8.169   1.00 62.27  ? 415 LYS B C   1 
ATOM   7558  O O   . LYS B 1 415 ? -11.200 31.106  8.385   1.00 59.59  ? 415 LYS B O   1 
ATOM   7559  C CB  . LYS B 1 415 ? -8.887  30.193  10.253  1.00 60.54  ? 415 LYS B CB  1 
ATOM   7560  C CG  . LYS B 1 415 ? -10.121 30.201  11.145  1.00 61.75  ? 415 LYS B CG  1 
ATOM   7561  C CD  . LYS B 1 415 ? -10.791 28.837  11.191  1.00 70.21  ? 415 LYS B CD  1 
ATOM   7562  C CE  . LYS B 1 415 ? -12.276 28.960  11.511  1.00 70.84  ? 415 LYS B CE  1 
ATOM   7563  N NZ  . LYS B 1 415 ? -12.642 28.302  12.798  1.00 74.68  ? 415 LYS B NZ  1 
ATOM   7564  N N   . TRP B 1 416 ? -9.352  31.951  7.412   1.00 59.66  ? 416 TRP B N   1 
ATOM   7565  C CA  . TRP B 1 416 ? -10.056 33.083  6.829   1.00 55.32  ? 416 TRP B CA  1 
ATOM   7566  C C   . TRP B 1 416 ? -10.003 33.145  5.313   1.00 53.37  ? 416 TRP B C   1 
ATOM   7567  O O   . TRP B 1 416 ? -10.824 33.849  4.718   1.00 59.03  ? 416 TRP B O   1 
ATOM   7568  C CB  . TRP B 1 416 ? -9.509  34.404  7.385   1.00 51.10  ? 416 TRP B CB  1 
ATOM   7569  C CG  . TRP B 1 416 ? -9.487  34.454  8.865   1.00 54.28  ? 416 TRP B CG  1 
ATOM   7570  C CD1 . TRP B 1 416 ? -10.448 34.971  9.685   1.00 55.17  ? 416 TRP B CD1 1 
ATOM   7571  C CD2 . TRP B 1 416 ? -8.450  33.965  9.716   1.00 56.95  ? 416 TRP B CD2 1 
ATOM   7572  N NE1 . TRP B 1 416 ? -10.070 34.833  11.002  1.00 56.10  ? 416 TRP B NE1 1 
ATOM   7573  C CE2 . TRP B 1 416 ? -8.846  34.217  11.046  1.00 56.33  ? 416 TRP B CE2 1 
ATOM   7574  C CE3 . TRP B 1 416 ? -7.225  33.338  9.485   1.00 52.25  ? 416 TRP B CE3 1 
ATOM   7575  C CZ2 . TRP B 1 416 ? -8.060  33.861  12.136  1.00 47.27  ? 416 TRP B CZ2 1 
ATOM   7576  C CZ3 . TRP B 1 416 ? -6.450  32.987  10.563  1.00 49.90  ? 416 TRP B CZ3 1 
ATOM   7577  C CH2 . TRP B 1 416 ? -6.867  33.250  11.873  1.00 51.93  ? 416 TRP B CH2 1 
ATOM   7578  N N   . ILE B 1 417 ? -9.076  32.434  4.672   1.00 53.86  ? 417 ILE B N   1 
ATOM   7579  C CA  . ILE B 1 417 ? -8.942  32.438  3.222   1.00 58.31  ? 417 ILE B CA  1 
ATOM   7580  C C   . ILE B 1 417 ? -8.506  31.047  2.785   1.00 56.57  ? 417 ILE B C   1 
ATOM   7581  O O   . ILE B 1 417 ? -8.014  30.248  3.584   1.00 51.35  ? 417 ILE B O   1 
ATOM   7582  C CB  . ILE B 1 417 ? -7.932  33.512  2.738   1.00 61.15  ? 417 ILE B CB  1 
ATOM   7583  C CG1 . ILE B 1 417 ? -8.266  33.995  1.314   1.00 61.18  ? 417 ILE B CG1 1 
ATOM   7584  C CG2 . ILE B 1 417 ? -6.506  32.987  2.862   1.00 60.88  ? 417 ILE B CG2 1 
ATOM   7585  C CD1 . ILE B 1 417 ? -7.484  35.237  0.853   1.00 54.18  ? 417 ILE B CD1 1 
ATOM   7586  N N   . GLY B 1 418 ? -8.725  30.743  1.505   1.00 56.39  ? 418 GLY B N   1 
ATOM   7587  C CA  . GLY B 1 418 ? -8.200  29.539  0.898   1.00 56.01  ? 418 GLY B CA  1 
ATOM   7588  C C   . GLY B 1 418 ? -9.232  28.520  0.457   1.00 60.79  ? 418 GLY B C   1 
ATOM   7589  O O   . GLY B 1 418 ? -8.890  27.620  -0.323  1.00 70.21  ? 418 GLY B O   1 
ATOM   7590  N N   . ASN B 1 419 ? -10.464 28.597  0.946   1.00 66.56  ? 419 ASN B N   1 
ATOM   7591  C CA  . ASN B 1 419 ? -11.532 27.748  0.437   1.00 72.43  ? 419 ASN B CA  1 
ATOM   7592  C C   . ASN B 1 419 ? -12.507 28.594  -0.366  1.00 69.77  ? 419 ASN B C   1 
ATOM   7593  O O   . ASN B 1 419 ? -12.517 29.824  -0.271  1.00 70.21  ? 419 ASN B O   1 
ATOM   7594  C CB  . ASN B 1 419 ? -12.211 26.956  1.576   1.00 71.51  ? 419 ASN B CB  1 
ATOM   7595  C CG  . ASN B 1 419 ? -13.307 27.728  2.326   1.00 78.94  ? 419 ASN B CG  1 
ATOM   7596  O OD1 . ASN B 1 419 ? -13.994 28.605  1.800   1.00 78.85  ? 419 ASN B OD1 1 
ATOM   7597  N ND2 . ASN B 1 419 ? -13.454 27.388  3.597   1.00 84.93  ? 419 ASN B ND2 1 
ATOM   7598  N N   . LYS B 1 420 ? -13.322 27.917  -1.175  1.00 71.88  ? 420 LYS B N   1 
ATOM   7599  C CA  . LYS B 1 420 ? -14.204 28.641  -2.084  1.00 70.71  ? 420 LYS B CA  1 
ATOM   7600  C C   . LYS B 1 420 ? -15.150 29.563  -1.325  1.00 72.08  ? 420 LYS B C   1 
ATOM   7601  O O   . LYS B 1 420 ? -15.352 30.713  -1.725  1.00 65.27  ? 420 LYS B O   1 
ATOM   7602  C CB  . LYS B 1 420 ? -14.980 27.659  -2.961  1.00 65.84  ? 420 LYS B CB  1 
ATOM   7603  C CG  . LYS B 1 420 ? -15.988 26.817  -2.216  1.00 72.57  ? 420 LYS B CG  1 
ATOM   7604  C CD  . LYS B 1 420 ? -16.852 26.032  -3.174  1.00 75.67  ? 420 LYS B CD  1 
ATOM   7605  C CE  . LYS B 1 420 ? -17.793 26.948  -3.940  1.00 77.73  ? 420 LYS B CE  1 
ATOM   7606  N NZ  . LYS B 1 420 ? -18.388 26.268  -5.124  1.00 74.72  ? 420 LYS B NZ  1 
ATOM   7607  N N   . GLU B 1 421 ? -15.703 29.094  -0.201  1.00 70.77  ? 421 GLU B N   1 
ATOM   7608  C CA  . GLU B 1 421 ? -16.684 29.889  0.532   1.00 67.91  ? 421 GLU B CA  1 
ATOM   7609  C C   . GLU B 1 421 ? -16.038 31.104  1.184   1.00 65.20  ? 421 GLU B C   1 
ATOM   7610  O O   . GLU B 1 421 ? -16.577 32.215  1.111   1.00 64.58  ? 421 GLU B O   1 
ATOM   7611  C CB  . GLU B 1 421 ? -17.383 29.016  1.570   1.00 76.57  ? 421 GLU B CB  1 
ATOM   7612  C CG  . GLU B 1 421 ? -18.128 27.855  0.945   1.00 86.38  ? 421 GLU B CG  1 
ATOM   7613  C CD  . GLU B 1 421 ? -17.827 26.531  1.617   1.00 101.03 ? 421 GLU B CD  1 
ATOM   7614  O OE1 . GLU B 1 421 ? -17.017 25.762  1.057   1.00 104.08 ? 421 GLU B OE1 1 
ATOM   7615  O OE2 . GLU B 1 421 ? -18.407 26.249  2.687   1.00 96.52  ? 421 GLU B OE2 1 
ATOM   7616  N N   . LYS B 1 422 ? -14.879 30.916  1.819   1.00 64.43  ? 422 LYS B N   1 
ATOM   7617  C CA  . LYS B 1 422 ? -14.142 32.056  2.352   1.00 69.76  ? 422 LYS B CA  1 
ATOM   7618  C C   . LYS B 1 422 ? -13.652 32.987  1.245   1.00 63.92  ? 422 LYS B C   1 
ATOM   7619  O O   . LYS B 1 422 ? -13.582 34.203  1.451   1.00 64.95  ? 422 LYS B O   1 
ATOM   7620  C CB  . LYS B 1 422 ? -12.961 31.578  3.204   1.00 69.44  ? 422 LYS B CB  1 
ATOM   7621  C CG  . LYS B 1 422 ? -13.314 31.304  4.659   1.00 64.16  ? 422 LYS B CG  1 
ATOM   7622  C CD  . LYS B 1 422 ? -12.297 30.399  5.327   1.00 59.93  ? 422 LYS B CD  1 
ATOM   7623  C CE  . LYS B 1 422 ? -12.986 29.345  6.184   1.00 68.01  ? 422 LYS B CE  1 
ATOM   7624  N NZ  . LYS B 1 422 ? -13.640 29.895  7.405   1.00 67.61  ? 422 LYS B NZ  1 
ATOM   7625  N N   . ASN B 1 423 ? -13.313 32.448  0.069   1.00 63.19  ? 423 ASN B N   1 
ATOM   7626  C CA  . ASN B 1 423 ? -12.799 33.298  -1.002  1.00 64.56  ? 423 ASN B CA  1 
ATOM   7627  C C   . ASN B 1 423 ? -13.900 34.147  -1.632  1.00 61.99  ? 423 ASN B C   1 
ATOM   7628  O O   . ASN B 1 423 ? -13.609 35.211  -2.188  1.00 57.95  ? 423 ASN B O   1 
ATOM   7629  C CB  . ASN B 1 423 ? -12.091 32.455  -2.071  1.00 64.45  ? 423 ASN B CB  1 
ATOM   7630  C CG  . ASN B 1 423 ? -10.732 31.926  -1.609  1.00 62.14  ? 423 ASN B CG  1 
ATOM   7631  O OD1 . ASN B 1 423 ? -10.189 32.358  -0.592  1.00 66.92  ? 423 ASN B OD1 1 
ATOM   7632  N ND2 . ASN B 1 423 ? -10.196 30.960  -2.347  1.00 62.98  ? 423 ASN B ND2 1 
ATOM   7633  N N   . GLU B 1 424 ? -15.163 33.706  -1.552  1.00 65.22  ? 424 GLU B N   1 
ATOM   7634  C CA  . GLU B 1 424 ? -16.267 34.528  -2.051  1.00 66.05  ? 424 GLU B CA  1 
ATOM   7635  C C   . GLU B 1 424 ? -16.388 35.831  -1.267  1.00 61.90  ? 424 GLU B C   1 
ATOM   7636  O O   . GLU B 1 424 ? -16.618 36.897  -1.854  1.00 56.04  ? 424 GLU B O   1 
ATOM   7637  C CB  . GLU B 1 424 ? -17.594 33.759  -1.999  1.00 73.32  ? 424 GLU B CB  1 
ATOM   7638  C CG  . GLU B 1 424 ? -17.625 32.431  -2.763  1.00 88.24  ? 424 GLU B CG  1 
ATOM   7639  C CD  . GLU B 1 424 ? -18.876 31.596  -2.477  1.00 91.94  ? 424 GLU B CD  1 
ATOM   7640  O OE1 . GLU B 1 424 ? -18.867 30.831  -1.491  1.00 87.96  ? 424 GLU B OE1 1 
ATOM   7641  O OE2 . GLU B 1 424 ? -19.861 31.683  -3.244  1.00 89.34  ? 424 GLU B OE2 1 
ATOM   7642  N N   . TYR B 1 425 ? -16.232 35.770  0.061   1.00 63.72  ? 425 TYR B N   1 
ATOM   7643  C CA  . TYR B 1 425 ? -16.282 36.985  0.875   1.00 62.86  ? 425 TYR B CA  1 
ATOM   7644  C C   . TYR B 1 425 ? -15.172 37.957  0.497   1.00 57.66  ? 425 TYR B C   1 
ATOM   7645  O O   . TYR B 1 425 ? -15.366 39.179  0.530   1.00 58.94  ? 425 TYR B O   1 
ATOM   7646  C CB  . TYR B 1 425 ? -16.182 36.630  2.357   1.00 63.11  ? 425 TYR B CB  1 
ATOM   7647  C CG  . TYR B 1 425 ? -17.504 36.531  3.070   1.00 61.62  ? 425 TYR B CG  1 
ATOM   7648  C CD1 . TYR B 1 425 ? -18.676 36.273  2.368   1.00 59.68  ? 425 TYR B CD1 1 
ATOM   7649  C CD2 . TYR B 1 425 ? -17.571 36.646  4.452   1.00 64.05  ? 425 TYR B CD2 1 
ATOM   7650  C CE1 . TYR B 1 425 ? -19.880 36.166  3.018   1.00 61.23  ? 425 TYR B CE1 1 
ATOM   7651  C CE2 . TYR B 1 425 ? -18.771 36.540  5.114   1.00 61.08  ? 425 TYR B CE2 1 
ATOM   7652  C CZ  . TYR B 1 425 ? -19.921 36.305  4.391   1.00 69.87  ? 425 TYR B CZ  1 
ATOM   7653  O OH  . TYR B 1 425 ? -21.121 36.193  5.038   1.00 77.07  ? 425 TYR B OH  1 
ATOM   7654  N N   . TRP B 1 426 ? -13.992 37.433  0.154   1.00 64.23  ? 426 TRP B N   1 
ATOM   7655  C CA  . TRP B 1 426 ? -12.892 38.299  -0.259  1.00 68.94  ? 426 TRP B CA  1 
ATOM   7656  C C   . TRP B 1 426 ? -13.172 38.928  -1.614  1.00 61.94  ? 426 TRP B C   1 
ATOM   7657  O O   . TRP B 1 426 ? -12.905 40.118  -1.816  1.00 61.27  ? 426 TRP B O   1 
ATOM   7658  C CB  . TRP B 1 426 ? -11.576 37.519  -0.290  1.00 62.79  ? 426 TRP B CB  1 
ATOM   7659  C CG  . TRP B 1 426 ? -11.025 37.244  1.078   1.00 61.79  ? 426 TRP B CG  1 
ATOM   7660  C CD1 . TRP B 1 426 ? -11.063 36.057  1.750   1.00 60.97  ? 426 TRP B CD1 1 
ATOM   7661  C CD2 . TRP B 1 426 ? -10.358 38.175  1.944   1.00 58.43  ? 426 TRP B CD2 1 
ATOM   7662  N NE1 . TRP B 1 426 ? -10.464 36.190  2.982   1.00 57.86  ? 426 TRP B NE1 1 
ATOM   7663  C CE2 . TRP B 1 426 ? -10.022 37.479  3.125   1.00 54.98  ? 426 TRP B CE2 1 
ATOM   7664  C CE3 . TRP B 1 426 ? -10.013 39.526  1.837   1.00 57.35  ? 426 TRP B CE3 1 
ATOM   7665  C CZ2 . TRP B 1 426 ? -9.359  38.089  4.189   1.00 52.66  ? 426 TRP B CZ2 1 
ATOM   7666  C CZ3 . TRP B 1 426 ? -9.352  40.131  2.898   1.00 50.45  ? 426 TRP B CZ3 1 
ATOM   7667  C CH2 . TRP B 1 426 ? -9.032  39.411  4.056   1.00 53.87  ? 426 TRP B CH2 1 
ATOM   7668  N N   . LYS B 1 427 ? -13.711 38.147  -2.553  1.00 60.42  ? 427 LYS B N   1 
ATOM   7669  C CA  . LYS B 1 427 ? -14.068 38.714  -3.848  1.00 56.19  ? 427 LYS B CA  1 
ATOM   7670  C C   . LYS B 1 427 ? -15.080 39.838  -3.687  1.00 62.40  ? 427 LYS B C   1 
ATOM   7671  O O   . LYS B 1 427 ? -14.961 40.876  -4.345  1.00 69.63  ? 427 LYS B O   1 
ATOM   7672  C CB  . LYS B 1 427 ? -14.600 37.628  -4.780  1.00 58.60  ? 427 LYS B CB  1 
ATOM   7673  C CG  . LYS B 1 427 ? -13.689 36.419  -4.908  1.00 59.01  ? 427 LYS B CG  1 
ATOM   7674  C CD  . LYS B 1 427 ? -14.259 35.371  -5.858  1.00 61.66  ? 427 LYS B CD  1 
ATOM   7675  C CE  . LYS B 1 427 ? -14.168 33.967  -5.262  1.00 68.00  ? 427 LYS B CE  1 
ATOM   7676  N NZ  . LYS B 1 427 ? -15.222 33.038  -5.775  1.00 71.85  ? 427 LYS B NZ  1 
ATOM   7677  N N   . ILE B 1 428 ? -16.056 39.671  -2.786  1.00 55.64  ? 428 ILE B N   1 
ATOM   7678  C CA  . ILE B 1 428 ? -17.037 40.731  -2.547  1.00 55.78  ? 428 ILE B CA  1 
ATOM   7679  C C   . ILE B 1 428 ? -16.356 41.983  -2.017  1.00 56.34  ? 428 ILE B C   1 
ATOM   7680  O O   . ILE B 1 428 ? -16.633 43.102  -2.468  1.00 57.48  ? 428 ILE B O   1 
ATOM   7681  C CB  . ILE B 1 428 ? -18.139 40.246  -1.587  1.00 56.46  ? 428 ILE B CB  1 
ATOM   7682  C CG1 . ILE B 1 428 ? -19.021 39.210  -2.267  1.00 57.69  ? 428 ILE B CG1 1 
ATOM   7683  C CG2 . ILE B 1 428 ? -18.992 41.407  -1.104  1.00 55.32  ? 428 ILE B CG2 1 
ATOM   7684  C CD1 . ILE B 1 428 ? -19.552 38.190  -1.322  1.00 57.28  ? 428 ILE B CD1 1 
ATOM   7685  N N   . LEU B 1 429 ? -15.455 41.815  -1.049  1.00 58.75  ? 429 LEU B N   1 
ATOM   7686  C CA  . LEU B 1 429 ? -14.768 42.966  -0.478  1.00 62.98  ? 429 LEU B CA  1 
ATOM   7687  C C   . LEU B 1 429 ? -13.869 43.639  -1.508  1.00 65.97  ? 429 LEU B C   1 
ATOM   7688  O O   . LEU B 1 429 ? -13.758 44.871  -1.527  1.00 75.79  ? 429 LEU B O   1 
ATOM   7689  C CB  . LEU B 1 429 ? -13.968 42.538  0.753   1.00 55.47  ? 429 LEU B CB  1 
ATOM   7690  C CG  . LEU B 1 429 ? -13.289 43.654  1.549   1.00 59.21  ? 429 LEU B CG  1 
ATOM   7691  C CD1 . LEU B 1 429 ? -14.254 44.302  2.523   1.00 64.20  ? 429 LEU B CD1 1 
ATOM   7692  C CD2 . LEU B 1 429 ? -12.085 43.113  2.286   1.00 65.33  ? 429 LEU B CD2 1 
ATOM   7693  N N   . ILE B 1 430 ? -13.227 42.856  -2.381  1.00 59.02  ? 430 ILE B N   1 
ATOM   7694  C CA  . ILE B 1 430 ? -12.387 43.446  -3.419  1.00 59.43  ? 430 ILE B CA  1 
ATOM   7695  C C   . ILE B 1 430 ? -13.222 44.338  -4.329  1.00 67.99  ? 430 ILE B C   1 
ATOM   7696  O O   . ILE B 1 430 ? -12.846 45.479  -4.622  1.00 71.21  ? 430 ILE B O   1 
ATOM   7697  C CB  . ILE B 1 430 ? -11.653 42.346  -4.206  1.00 71.00  ? 430 ILE B CB  1 
ATOM   7698  C CG1 . ILE B 1 430 ? -10.609 41.677  -3.309  1.00 66.57  ? 430 ILE B CG1 1 
ATOM   7699  C CG2 . ILE B 1 430 ? -10.985 42.923  -5.458  1.00 73.82  ? 430 ILE B CG2 1 
ATOM   7700  C CD1 . ILE B 1 430 ? -10.166 40.323  -3.796  1.00 66.64  ? 430 ILE B CD1 1 
ATOM   7701  N N   . GLU B 1 431 ? -14.385 43.843  -4.764  1.00 67.25  ? 431 GLU B N   1 
ATOM   7702  C CA  . GLU B 1 431 ? -15.268 44.657  -5.599  1.00 72.10  ? 431 GLU B CA  1 
ATOM   7703  C C   . GLU B 1 431 ? -15.810 45.858  -4.834  1.00 75.87  ? 431 GLU B C   1 
ATOM   7704  O O   . GLU B 1 431 ? -15.973 46.943  -5.404  1.00 79.75  ? 431 GLU B O   1 
ATOM   7705  C CB  . GLU B 1 431 ? -16.436 43.824  -6.129  1.00 72.54  ? 431 GLU B CB  1 
ATOM   7706  C CG  . GLU B 1 431 ? -16.101 42.404  -6.551  1.00 78.89  ? 431 GLU B CG  1 
ATOM   7707  C CD  . GLU B 1 431 ? -15.476 42.312  -7.926  1.00 97.63  ? 431 GLU B CD  1 
ATOM   7708  O OE1 . GLU B 1 431 ? -15.067 43.358  -8.470  1.00 96.39  ? 431 GLU B OE1 1 
ATOM   7709  O OE2 . GLU B 1 431 ? -15.404 41.186  -8.466  1.00 108.69 ? 431 GLU B OE2 1 
ATOM   7710  N N   . ALA B 1 432 ? -16.121 45.675  -3.547  1.00 68.93  ? 432 ALA B N   1 
ATOM   7711  C CA  . ALA B 1 432 ? -16.657 46.777  -2.755  1.00 63.85  ? 432 ALA B CA  1 
ATOM   7712  C C   . ALA B 1 432 ? -15.615 47.866  -2.551  1.00 65.60  ? 432 ALA B C   1 
ATOM   7713  O O   . ALA B 1 432 ? -15.932 49.056  -2.649  1.00 68.25  ? 432 ALA B O   1 
ATOM   7714  C CB  . ALA B 1 432 ? -17.165 46.268  -1.410  1.00 60.82  ? 432 ALA B CB  1 
ATOM   7715  N N   . LYS B 1 433 ? -14.368 47.474  -2.265  1.00 69.38  ? 433 LYS B N   1 
ATOM   7716  C CA  . LYS B 1 433 ? -13.284 48.440  -2.131  1.00 60.29  ? 433 LYS B CA  1 
ATOM   7717  C C   . LYS B 1 433 ? -13.162 49.313  -3.366  1.00 65.76  ? 433 LYS B C   1 
ATOM   7718  O O   . LYS B 1 433 ? -12.827 50.498  -3.256  1.00 61.47  ? 433 LYS B O   1 
ATOM   7719  C CB  . LYS B 1 433 ? -11.960 47.715  -1.883  1.00 59.18  ? 433 LYS B CB  1 
ATOM   7720  C CG  . LYS B 1 433 ? -10.795 48.629  -1.468  1.00 66.80  ? 433 LYS B CG  1 
ATOM   7721  C CD  . LYS B 1 433 ? -10.964 49.177  -0.054  1.00 65.99  ? 433 LYS B CD  1 
ATOM   7722  C CE  . LYS B 1 433 ? -10.189 50.477  0.141   1.00 63.02  ? 433 LYS B CE  1 
ATOM   7723  N NZ  . LYS B 1 433 ? -10.969 51.492  0.910   1.00 57.01  ? 433 LYS B NZ  1 
ATOM   7724  N N   . LYS B 1 434 ? -13.433 48.747  -4.546  1.00 66.91  ? 434 LYS B N   1 
ATOM   7725  C CA  . LYS B 1 434 ? -13.347 49.511  -5.784  1.00 62.41  ? 434 LYS B CA  1 
ATOM   7726  C C   . LYS B 1 434 ? -14.292 50.700  -5.771  1.00 68.61  ? 434 LYS B C   1 
ATOM   7727  O O   . LYS B 1 434 ? -13.913 51.803  -6.179  1.00 73.14  ? 434 LYS B O   1 
ATOM   7728  C CB  . LYS B 1 434 ? -13.644 48.603  -6.977  1.00 63.61  ? 434 LYS B CB  1 
ATOM   7729  C CG  . LYS B 1 434 ? -12.424 47.849  -7.493  1.00 69.74  ? 434 LYS B CG  1 
ATOM   7730  C CD  . LYS B 1 434 ? -12.739 46.386  -7.765  1.00 75.07  ? 434 LYS B CD  1 
ATOM   7731  C CE  . LYS B 1 434 ? -11.619 45.699  -8.536  1.00 64.26  ? 434 LYS B CE  1 
ATOM   7732  N NZ  . LYS B 1 434 ? -11.699 44.213  -8.420  1.00 68.18  ? 434 LYS B NZ  1 
ATOM   7733  N N   . LYS B 1 435 ? -15.524 50.504  -5.298  1.00 68.75  ? 435 LYS B N   1 
ATOM   7734  C CA  . LYS B 1 435 ? -16.542 51.546  -5.334  1.00 75.48  ? 435 LYS B CA  1 
ATOM   7735  C C   . LYS B 1 435 ? -16.956 52.006  -3.939  1.00 66.86  ? 435 LYS B C   1 
ATOM   7736  O O   . LYS B 1 435 ? -18.046 52.560  -3.773  1.00 74.21  ? 435 LYS B O   1 
ATOM   7737  C CB  . LYS B 1 435 ? -17.761 51.059  -6.120  1.00 72.62  ? 435 LYS B CB  1 
ATOM   7738  C CG  . LYS B 1 435 ? -17.437 50.630  -7.534  1.00 72.86  ? 435 LYS B CG  1 
ATOM   7739  C CD  . LYS B 1 435 ? -17.343 49.113  -7.657  1.00 71.68  ? 435 LYS B CD  1 
ATOM   7740  C CE  . LYS B 1 435 ? -18.718 48.459  -7.664  1.00 76.36  ? 435 LYS B CE  1 
ATOM   7741  N NZ  . LYS B 1 435 ? -18.615 46.970  -7.710  1.00 79.09  ? 435 LYS B NZ  1 
ATOM   7742  N N   . ALA B 1 436 ? -16.114 51.791  -2.934  1.00 65.37  ? 436 ALA B N   1 
ATOM   7743  C CA  . ALA B 1 436 ? -16.470 52.158  -1.571  1.00 61.19  ? 436 ALA B CA  1 
ATOM   7744  C C   . ALA B 1 436 ? -16.268 53.652  -1.361  1.00 65.27  ? 436 ALA B C   1 
ATOM   7745  O O   . ALA B 1 436 ? -15.213 54.200  -1.696  1.00 68.13  ? 436 ALA B O   1 
ATOM   7746  C CB  . ALA B 1 436 ? -15.643 51.360  -0.565  1.00 55.37  ? 436 ALA B CB  1 
ATOM   7747  N N   . LYS B 1 437 ? -17.287 54.312  -0.807  1.00 68.85  ? 437 LYS B N   1 
ATOM   7748  C CA  . LYS B 1 437 ? -17.240 55.750  -0.577  1.00 69.18  ? 437 LYS B CA  1 
ATOM   7749  C C   . LYS B 1 437 ? -17.354 56.137  0.891   1.00 67.33  ? 437 LYS B C   1 
ATOM   7750  O O   . LYS B 1 437 ? -17.365 57.333  1.199   1.00 70.13  ? 437 LYS B O   1 
ATOM   7751  C CB  . LYS B 1 437 ? -18.342 56.461  -1.377  1.00 66.47  ? 437 LYS B CB  1 
ATOM   7752  C CG  . LYS B 1 437 ? -18.588 55.876  -2.757  1.00 69.96  ? 437 LYS B CG  1 
ATOM   7753  C CD  . LYS B 1 437 ? -18.752 56.965  -3.811  1.00 74.61  ? 437 LYS B CD  1 
ATOM   7754  C CE  . LYS B 1 437 ? -17.408 57.449  -4.350  1.00 82.39  ? 437 LYS B CE  1 
ATOM   7755  N NZ  . LYS B 1 437 ? -16.656 56.382  -5.070  1.00 81.41  ? 437 LYS B NZ  1 
ATOM   7756  N N   . ASN B 1 438 ? -17.442 55.179  1.804   1.00 62.76  ? 438 ASN B N   1 
ATOM   7757  C CA  . ASN B 1 438 ? -17.441 55.482  3.226   1.00 68.39  ? 438 ASN B CA  1 
ATOM   7758  C C   . ASN B 1 438 ? -16.549 54.483  3.953   1.00 66.57  ? 438 ASN B C   1 
ATOM   7759  O O   . ASN B 1 438 ? -15.953 53.589  3.344   1.00 65.26  ? 438 ASN B O   1 
ATOM   7760  C CB  . ASN B 1 438 ? -18.866 55.486  3.798   1.00 62.17  ? 438 ASN B CB  1 
ATOM   7761  C CG  . ASN B 1 438 ? -19.490 54.108  3.828   1.00 66.85  ? 438 ASN B CG  1 
ATOM   7762  O OD1 . ASN B 1 438 ? -18.942 53.175  4.406   1.00 71.86  ? 438 ASN B OD1 1 
ATOM   7763  N ND2 . ASN B 1 438 ? -20.652 53.979  3.212   1.00 72.72  ? 438 ASN B ND2 1 
ATOM   7764  N N   . ASP B 1 439 ? -16.483 54.625  5.272   1.00 59.04  ? 439 ASP B N   1 
ATOM   7765  C CA  . ASP B 1 439 ? -15.577 53.830  6.089   1.00 60.52  ? 439 ASP B CA  1 
ATOM   7766  C C   . ASP B 1 439 ? -16.213 52.549  6.621   1.00 64.10  ? 439 ASP B C   1 
ATOM   7767  O O   . ASP B 1 439 ? -15.564 51.830  7.386   1.00 69.24  ? 439 ASP B O   1 
ATOM   7768  C CB  . ASP B 1 439 ? -15.045 54.672  7.256   1.00 61.36  ? 439 ASP B CB  1 
ATOM   7769  C CG  . ASP B 1 439 ? -13.652 55.238  6.989   1.00 76.48  ? 439 ASP B CG  1 
ATOM   7770  O OD1 . ASP B 1 439 ? -12.970 54.762  6.052   1.00 77.03  ? 439 ASP B OD1 1 
ATOM   7771  O OD2 . ASP B 1 439 ? -13.240 56.168  7.718   1.00 77.05  ? 439 ASP B OD2 1 
ATOM   7772  N N   . TYR B 1 440 ? -17.456 52.239  6.244   1.00 58.24  ? 440 TYR B N   1 
ATOM   7773  C CA  . TYR B 1 440 ? -17.994 50.917  6.546   1.00 51.94  ? 440 TYR B CA  1 
ATOM   7774  C C   . TYR B 1 440 ? -17.259 49.827  5.786   1.00 53.34  ? 440 TYR B C   1 
ATOM   7775  O O   . TYR B 1 440 ? -17.451 48.640  6.077   1.00 51.68  ? 440 TYR B O   1 
ATOM   7776  C CB  . TYR B 1 440 ? -19.483 50.845  6.208   1.00 61.95  ? 440 TYR B CB  1 
ATOM   7777  C CG  . TYR B 1 440 ? -20.430 51.239  7.323   1.00 59.89  ? 440 TYR B CG  1 
ATOM   7778  C CD1 . TYR B 1 440 ? -20.833 50.318  8.274   1.00 60.34  ? 440 TYR B CD1 1 
ATOM   7779  C CD2 . TYR B 1 440 ? -20.944 52.527  7.404   1.00 62.25  ? 440 TYR B CD2 1 
ATOM   7780  C CE1 . TYR B 1 440 ? -21.714 50.668  9.288   1.00 61.91  ? 440 TYR B CE1 1 
ATOM   7781  C CE2 . TYR B 1 440 ? -21.822 52.889  8.411   1.00 63.84  ? 440 TYR B CE2 1 
ATOM   7782  C CZ  . TYR B 1 440 ? -22.205 51.954  9.353   1.00 64.27  ? 440 TYR B CZ  1 
ATOM   7783  O OH  . TYR B 1 440 ? -23.078 52.295  10.364  1.00 63.39  ? 440 TYR B OH  1 
ATOM   7784  N N   . ILE B 1 441 ? -16.438 50.204  4.805   1.00 57.29  ? 441 ILE B N   1 
ATOM   7785  C CA  . ILE B 1 441 ? -15.562 49.232  4.168   1.00 61.36  ? 441 ILE B CA  1 
ATOM   7786  C C   . ILE B 1 441 ? -14.602 48.642  5.197   1.00 51.89  ? 441 ILE B C   1 
ATOM   7787  O O   . ILE B 1 441 ? -14.259 47.456  5.130   1.00 49.32  ? 441 ILE B O   1 
ATOM   7788  C CB  . ILE B 1 441 ? -14.835 49.894  2.971   1.00 54.11  ? 441 ILE B CB  1 
ATOM   7789  C CG1 . ILE B 1 441 ? -14.020 48.876  2.178   1.00 54.74  ? 441 ILE B CG1 1 
ATOM   7790  C CG2 . ILE B 1 441 ? -13.937 51.014  3.431   1.00 53.86  ? 441 ILE B CG2 1 
ATOM   7791  C CD1 . ILE B 1 441 ? -14.855 47.839  1.506   1.00 43.85  ? 441 ILE B CD1 1 
ATOM   7792  N N   . LEU B 1 442 ? -14.193 49.441  6.190   1.00 49.49  ? 442 LEU B N   1 
ATOM   7793  C CA  . LEU B 1 442 ? -13.311 48.940  7.241   1.00 55.79  ? 442 LEU B CA  1 
ATOM   7794  C C   . LEU B 1 442 ? -14.032 47.967  8.162   1.00 55.14  ? 442 LEU B C   1 
ATOM   7795  O O   . LEU B 1 442 ? -13.413 47.041  8.694   1.00 56.90  ? 442 LEU B O   1 
ATOM   7796  C CB  . LEU B 1 442 ? -12.740 50.104  8.051   1.00 55.49  ? 442 LEU B CB  1 
ATOM   7797  C CG  . LEU B 1 442 ? -12.246 51.333  7.283   1.00 58.44  ? 442 LEU B CG  1 
ATOM   7798  C CD1 . LEU B 1 442 ? -11.546 52.311  8.216   1.00 59.61  ? 442 LEU B CD1 1 
ATOM   7799  C CD2 . LEU B 1 442 ? -11.312 50.930  6.150   1.00 59.02  ? 442 LEU B CD2 1 
ATOM   7800  N N   . VAL B 1 443 ? -15.331 48.166  8.370   1.00 53.65  ? 443 VAL B N   1 
ATOM   7801  C CA  . VAL B 1 443 ? -16.099 47.221  9.168   1.00 46.58  ? 443 VAL B CA  1 
ATOM   7802  C C   . VAL B 1 443 ? -16.195 45.880  8.461   1.00 47.16  ? 443 VAL B C   1 
ATOM   7803  O O   . VAL B 1 443 ? -16.158 44.821  9.100   1.00 52.49  ? 443 VAL B O   1 
ATOM   7804  C CB  . VAL B 1 443 ? -17.485 47.803  9.475   1.00 46.76  ? 443 VAL B CB  1 
ATOM   7805  C CG1 . VAL B 1 443 ? -18.069 47.103  10.677  1.00 52.10  ? 443 VAL B CG1 1 
ATOM   7806  C CG2 . VAL B 1 443 ? -17.373 49.306  9.713   1.00 44.41  ? 443 VAL B CG2 1 
ATOM   7807  N N   . ALA B 1 444 ? -16.317 45.897  7.135   1.00 56.19  ? 444 ALA B N   1 
ATOM   7808  C CA  . ALA B 1 444 ? -16.376 44.652  6.382   1.00 58.91  ? 444 ALA B CA  1 
ATOM   7809  C C   . ALA B 1 444 ? -15.023 43.962  6.285   1.00 57.63  ? 444 ALA B C   1 
ATOM   7810  O O   . ALA B 1 444 ? -14.971 42.811  5.835   1.00 66.04  ? 444 ALA B O   1 
ATOM   7811  C CB  . ALA B 1 444 ? -16.934 44.911  4.981   1.00 44.66  ? 444 ALA B CB  1 
ATOM   7812  N N   . GLU B 1 445 ? -13.938 44.636  6.683   1.00 49.60  ? 445 GLU B N   1 
ATOM   7813  C CA  . GLU B 1 445 ? -12.621 44.009  6.737   1.00 55.06  ? 445 GLU B CA  1 
ATOM   7814  C C   . GLU B 1 445 ? -12.420 43.189  8.008   1.00 55.24  ? 445 GLU B C   1 
ATOM   7815  O O   . GLU B 1 445 ? -11.298 42.766  8.296   1.00 52.86  ? 445 GLU B O   1 
ATOM   7816  C CB  . GLU B 1 445 ? -11.534 45.084  6.492   1.00 58.63  ? 445 GLU B CB  1 
ATOM   7817  C CG  . GLU B 1 445 ? -11.452 45.465  5.022   1.00 63.90  ? 445 GLU B CG  1 
ATOM   7818  C CD  . GLU B 1 445 ? -10.942 46.898  4.819   1.00 61.82  ? 445 GLU B CD  1 
ATOM   7819  O OE1 . GLU B 1 445 ? -10.720 47.640  5.817   1.00 56.99  ? 445 GLU B OE1 1 
ATOM   7820  O OE2 . GLU B 1 445 ? -10.744 47.295  3.653   1.00 65.48  ? 445 GLU B OE2 1 
ATOM   7821  N N   . GLY B 1 446 ? -13.480 42.890  8.737   1.00 59.63  ? 446 GLY B N   1 
ATOM   7822  C CA  . GLY B 1 446 ? -13.290 42.245  10.014  1.00 55.68  ? 446 GLY B CA  1 
ATOM   7823  C C   . GLY B 1 446 ? -12.885 40.799  9.817   1.00 56.34  ? 446 GLY B C   1 
ATOM   7824  O O   . GLY B 1 446 ? -13.340 40.125  8.882   1.00 59.98  ? 446 GLY B O   1 
ATOM   7825  N N   . SER B 1 447 ? -12.114 40.287  10.771  1.00 46.07  ? 447 SER B N   1 
ATOM   7826  C CA  . SER B 1 447 ? -11.734 38.896  10.700  1.00 51.06  ? 447 SER B CA  1 
ATOM   7827  C C   . SER B 1 447 ? -12.901 38.003  11.030  1.00 49.80  ? 447 SER B C   1 
ATOM   7828  O O   . SER B 1 447 ? -12.910 36.851  10.602  1.00 56.09  ? 447 SER B O   1 
ATOM   7829  C CB  . SER B 1 447 ? -10.559 38.611  11.647  1.00 54.79  ? 447 SER B CB  1 
ATOM   7830  O OG  . SER B 1 447 ? -10.954 38.491  13.001  1.00 53.74  ? 447 SER B OG  1 
ATOM   7831  N N   . ASP B 1 448 ? -13.895 38.515  11.750  1.00 42.10  ? 448 ASP B N   1 
ATOM   7832  C CA  . ASP B 1 448 ? -14.965 37.643  12.210  1.00 52.76  ? 448 ASP B CA  1 
ATOM   7833  C C   . ASP B 1 448 ? -15.883 37.204  11.068  1.00 50.41  ? 448 ASP B C   1 
ATOM   7834  O O   . ASP B 1 448 ? -16.430 36.099  11.114  1.00 49.50  ? 448 ASP B O   1 
ATOM   7835  C CB  . ASP B 1 448 ? -15.734 38.332  13.333  1.00 48.64  ? 448 ASP B CB  1 
ATOM   7836  C CG  . ASP B 1 448 ? -14.814 38.754  14.485  1.00 54.23  ? 448 ASP B CG  1 
ATOM   7837  O OD1 . ASP B 1 448 ? -14.382 37.870  15.259  1.00 55.30  ? 448 ASP B OD1 1 
ATOM   7838  O OD2 . ASP B 1 448 ? -14.530 39.967  14.627  1.00 47.99  ? 448 ASP B OD2 1 
ATOM   7839  N N   . TRP B 1 449 ? -16.029 38.019  10.019  1.00 51.69  ? 449 TRP B N   1 
ATOM   7840  C CA  . TRP B 1 449 ? -16.912 37.641  8.914   1.00 53.14  ? 449 TRP B CA  1 
ATOM   7841  C C   . TRP B 1 449 ? -16.378 36.424  8.170   1.00 54.57  ? 449 TRP B C   1 
ATOM   7842  O O   . TRP B 1 449 ? -17.146 35.542  7.766   1.00 63.15  ? 449 TRP B O   1 
ATOM   7843  C CB  . TRP B 1 449 ? -17.094 38.819  7.954   1.00 53.61  ? 449 TRP B CB  1 
ATOM   7844  C CG  . TRP B 1 449 ? -17.344 40.129  8.656   1.00 50.93  ? 449 TRP B CG  1 
ATOM   7845  C CD1 . TRP B 1 449 ? -16.661 41.298  8.475   1.00 47.79  ? 449 TRP B CD1 1 
ATOM   7846  C CD2 . TRP B 1 449 ? -18.354 40.403  9.640   1.00 49.50  ? 449 TRP B CD2 1 
ATOM   7847  N NE1 . TRP B 1 449 ? -17.172 42.277  9.292   1.00 46.47  ? 449 TRP B NE1 1 
ATOM   7848  C CE2 . TRP B 1 449 ? -18.212 41.755  10.016  1.00 49.53  ? 449 TRP B CE2 1 
ATOM   7849  C CE3 . TRP B 1 449 ? -19.360 39.636  10.242  1.00 49.89  ? 449 TRP B CE3 1 
ATOM   7850  C CZ2 . TRP B 1 449 ? -19.038 42.357  10.970  1.00 49.19  ? 449 TRP B CZ2 1 
ATOM   7851  C CZ3 . TRP B 1 449 ? -20.182 40.236  11.191  1.00 50.26  ? 449 TRP B CZ3 1 
ATOM   7852  C CH2 . TRP B 1 449 ? -20.015 41.582  11.545  1.00 52.45  ? 449 TRP B CH2 1 
ATOM   7853  N N   . PHE B 1 450 ? -15.061 36.346  8.002   1.00 49.42  ? 450 PHE B N   1 
ATOM   7854  C CA  . PHE B 1 450 ? -14.472 35.253  7.243   1.00 52.97  ? 450 PHE B CA  1 
ATOM   7855  C C   . PHE B 1 450 ? -14.343 33.988  8.078   1.00 58.18  ? 450 PHE B C   1 
ATOM   7856  O O   . PHE B 1 450 ? -14.355 32.881  7.529   1.00 58.12  ? 450 PHE B O   1 
ATOM   7857  C CB  . PHE B 1 450 ? -13.110 35.688  6.704   1.00 51.29  ? 450 PHE B CB  1 
ATOM   7858  C CG  . PHE B 1 450 ? -13.161 36.967  5.914   1.00 55.61  ? 450 PHE B CG  1 
ATOM   7859  C CD1 . PHE B 1 450 ? -13.121 38.198  6.551   1.00 49.92  ? 450 PHE B CD1 1 
ATOM   7860  C CD2 . PHE B 1 450 ? -13.260 36.938  4.535   1.00 56.19  ? 450 PHE B CD2 1 
ATOM   7861  C CE1 . PHE B 1 450 ? -13.176 39.373  5.826   1.00 47.12  ? 450 PHE B CE1 1 
ATOM   7862  C CE2 . PHE B 1 450 ? -13.312 38.111  3.806   1.00 53.25  ? 450 PHE B CE2 1 
ATOM   7863  C CZ  . PHE B 1 450 ? -13.271 39.328  4.454   1.00 49.40  ? 450 PHE B CZ  1 
ATOM   7864  N N   . TRP B 1 451 ? -14.239 34.135  9.400   1.00 59.83  ? 451 TRP B N   1 
ATOM   7865  C CA  . TRP B 1 451 ? -14.090 32.978  10.275  1.00 56.41  ? 451 TRP B CA  1 
ATOM   7866  C C   . TRP B 1 451 ? -15.346 32.111  10.253  1.00 56.62  ? 451 TRP B C   1 
ATOM   7867  O O   . TRP B 1 451 ? -15.261 30.881  10.156  1.00 58.19  ? 451 TRP B O   1 
ATOM   7868  C CB  . TRP B 1 451 ? -13.750 33.462  11.689  1.00 50.35  ? 451 TRP B CB  1 
ATOM   7869  C CG  . TRP B 1 451 ? -13.843 32.460  12.811  1.00 57.88  ? 451 TRP B CG  1 
ATOM   7870  C CD1 . TRP B 1 451 ? -14.959 31.792  13.239  1.00 60.50  ? 451 TRP B CD1 1 
ATOM   7871  C CD2 . TRP B 1 451 ? -12.781 32.061  13.690  1.00 57.20  ? 451 TRP B CD2 1 
ATOM   7872  N NE1 . TRP B 1 451 ? -14.648 30.986  14.306  1.00 61.61  ? 451 TRP B NE1 1 
ATOM   7873  C CE2 . TRP B 1 451 ? -13.319 31.135  14.605  1.00 61.91  ? 451 TRP B CE2 1 
ATOM   7874  C CE3 . TRP B 1 451 ? -11.426 32.390  13.783  1.00 58.70  ? 451 TRP B CE3 1 
ATOM   7875  C CZ2 . TRP B 1 451 ? -12.549 30.534  15.599  1.00 61.86  ? 451 TRP B CZ2 1 
ATOM   7876  C CZ3 . TRP B 1 451 ? -10.663 31.792  14.770  1.00 59.03  ? 451 TRP B CZ3 1 
ATOM   7877  C CH2 . TRP B 1 451 ? -11.227 30.874  15.664  1.00 60.89  ? 451 TRP B CH2 1 
ATOM   7878  N N   . TRP B 1 452 ? -16.524 32.739  10.328  1.00 59.92  ? 452 TRP B N   1 
ATOM   7879  C CA  . TRP B 1 452 ? -17.795 32.026  10.424  1.00 58.52  ? 452 TRP B CA  1 
ATOM   7880  C C   . TRP B 1 452 ? -18.345 31.588  9.077   1.00 62.99  ? 452 TRP B C   1 
ATOM   7881  O O   . TRP B 1 452 ? -19.370 30.897  9.038   1.00 62.45  ? 452 TRP B O   1 
ATOM   7882  C CB  . TRP B 1 452 ? -18.846 32.896  11.115  1.00 55.74  ? 452 TRP B CB  1 
ATOM   7883  C CG  . TRP B 1 452 ? -18.498 33.306  12.506  1.00 54.17  ? 452 TRP B CG  1 
ATOM   7884  C CD1 . TRP B 1 452 ? -18.259 34.575  12.952  1.00 52.79  ? 452 TRP B CD1 1 
ATOM   7885  C CD2 . TRP B 1 452 ? -18.374 32.450  13.646  1.00 52.13  ? 452 TRP B CD2 1 
ATOM   7886  N NE1 . TRP B 1 452 ? -17.983 34.558  14.297  1.00 49.85  ? 452 TRP B NE1 1 
ATOM   7887  C CE2 . TRP B 1 452 ? -18.048 33.266  14.747  1.00 51.65  ? 452 TRP B CE2 1 
ATOM   7888  C CE3 . TRP B 1 452 ? -18.503 31.073  13.842  1.00 55.42  ? 452 TRP B CE3 1 
ATOM   7889  C CZ2 . TRP B 1 452 ? -17.849 32.750  16.025  1.00 54.27  ? 452 TRP B CZ2 1 
ATOM   7890  C CZ3 . TRP B 1 452 ? -18.305 30.563  15.108  1.00 58.05  ? 452 TRP B CZ3 1 
ATOM   7891  C CH2 . TRP B 1 452 ? -17.982 31.399  16.184  1.00 57.42  ? 452 TRP B CH2 1 
ATOM   7892  N N   . GLN B 1 453 ? -17.713 31.979  7.981   1.00 64.40  ? 453 GLN B N   1 
ATOM   7893  C CA  . GLN B 1 453 ? -18.249 31.732  6.652   1.00 67.32  ? 453 GLN B CA  1 
ATOM   7894  C C   . GLN B 1 453 ? -17.673 30.433  6.105   1.00 71.58  ? 453 GLN B C   1 
ATOM   7895  O O   . GLN B 1 453 ? -16.452 30.256  6.067   1.00 74.39  ? 453 GLN B O   1 
ATOM   7896  C CB  . GLN B 1 453 ? -17.945 32.901  5.715   1.00 64.03  ? 453 GLN B CB  1 
ATOM   7897  C CG  . GLN B 1 453 ? -18.129 32.526  4.263   1.00 67.56  ? 453 GLN B CG  1 
ATOM   7898  C CD  . GLN B 1 453 ? -19.501 32.882  3.736   1.00 76.75  ? 453 GLN B CD  1 
ATOM   7899  O OE1 . GLN B 1 453 ? -20.472 32.948  4.491   1.00 82.19  ? 453 GLN B OE1 1 
ATOM   7900  N NE2 . GLN B 1 453 ? -19.601 33.055  2.422   1.00 75.17  ? 453 GLN B NE2 1 
ATOM   7901  N N   . GLY B 1 454 ? -18.550 29.521  5.701   1.00 77.99  ? 454 GLY B N   1 
ATOM   7902  C CA  . GLY B 1 454 ? -18.114 28.312  5.041   1.00 84.37  ? 454 GLY B CA  1 
ATOM   7903  C C   . GLY B 1 454 ? -17.477 27.266  5.926   1.00 84.25  ? 454 GLY B C   1 
ATOM   7904  O O   . GLY B 1 454 ? -17.045 26.230  5.409   1.00 99.34  ? 454 GLY B O   1 
ATOM   7905  N N   . GLU B 1 455 ? -17.405 27.490  7.236   1.00 81.18  ? 455 GLU B N   1 
ATOM   7906  C CA  . GLU B 1 455 ? -16.869 26.482  8.143   1.00 92.22  ? 455 GLU B CA  1 
ATOM   7907  C C   . GLU B 1 455 ? -17.785 25.260  8.204   1.00 100.43 ? 455 GLU B C   1 
ATOM   7908  O O   . GLU B 1 455 ? -17.690 24.359  7.363   1.00 99.23  ? 455 GLU B O   1 
ATOM   7909  C CB  . GLU B 1 455 ? -16.671 27.074  9.540   1.00 85.34  ? 455 GLU B CB  1 
ATOM   7910  C CG  . GLU B 1 455 ? -15.261 27.599  9.804   1.00 84.70  ? 455 GLU B CG  1 
ATOM   7911  C CD  . GLU B 1 455 ? -14.186 26.545  9.591   1.00 92.97  ? 455 GLU B CD  1 
ATOM   7912  O OE1 . GLU B 1 455 ? -14.311 25.443  10.168  1.00 95.85  ? 455 GLU B OE1 1 
ATOM   7913  O OE2 . GLU B 1 455 ? -13.210 26.819  8.859   1.00 86.71  ? 455 GLU B OE2 1 
ATOM   7914  N N   . GLU B 1 456 ? -18.668 25.219  9.200   1.00 99.87  ? 456 GLU B N   1 
ATOM   7915  C CA  . GLU B 1 456 ? -19.618 24.129  9.366   1.00 98.81  ? 456 GLU B CA  1 
ATOM   7916  C C   . GLU B 1 456 ? -20.942 24.712  9.832   1.00 98.55  ? 456 GLU B C   1 
ATOM   7917  O O   . GLU B 1 456 ? -20.976 25.705  10.565  1.00 97.66  ? 456 GLU B O   1 
ATOM   7918  C CB  . GLU B 1 456 ? -19.109 23.079  10.368  1.00 99.93  ? 456 GLU B CB  1 
ATOM   7919  C CG  . GLU B 1 456 ? -18.060 22.129  9.799   1.00 97.96  ? 456 GLU B CG  1 
ATOM   7920  C CD  . GLU B 1 456 ? -18.592 20.724  9.596   1.00 108.41 ? 456 GLU B CD  1 
ATOM   7921  O OE1 . GLU B 1 456 ? -19.493 20.316  10.361  1.00 115.51 ? 456 GLU B OE1 1 
ATOM   7922  O OE2 . GLU B 1 456 ? -18.109 20.028  8.676   1.00 102.79 ? 456 GLU B OE2 1 
ATOM   7923  N N   . LYS B 1 457 ? -22.035 24.086  9.402   1.00 100.50 ? 457 LYS B N   1 
ATOM   7924  C CA  . LYS B 1 457 ? -23.371 24.621  9.648   1.00 104.22 ? 457 LYS B CA  1 
ATOM   7925  C C   . LYS B 1 457 ? -23.681 24.582  11.141  1.00 106.77 ? 457 LYS B C   1 
ATOM   7926  O O   . LYS B 1 457 ? -23.839 23.506  11.728  1.00 113.53 ? 457 LYS B O   1 
ATOM   7927  C CB  . LYS B 1 457 ? -24.403 23.835  8.844   1.00 101.73 ? 457 LYS B CB  1 
ATOM   7928  C CG  . LYS B 1 457 ? -25.732 24.549  8.672   1.00 104.02 ? 457 LYS B CG  1 
ATOM   7929  C CD  . LYS B 1 457 ? -26.812 23.935  9.551   1.00 106.03 ? 457 LYS B CD  1 
ATOM   7930  C CE  . LYS B 1 457 ? -28.186 24.122  8.932   1.00 105.02 ? 457 LYS B CE  1 
ATOM   7931  N NZ  . LYS B 1 457 ? -29.237 23.370  9.668   1.00 117.18 ? 457 LYS B NZ  1 
ATOM   7932  N N   . ALA B 1 458 ? -23.751 25.757  11.752  1.00 104.29 ? 458 ALA B N   1 
ATOM   7933  C CA  . ALA B 1 458 ? -24.063 25.940  13.160  1.00 99.07  ? 458 ALA B CA  1 
ATOM   7934  C C   . ALA B 1 458 ? -24.983 27.144  13.275  1.00 97.15  ? 458 ALA B C   1 
ATOM   7935  O O   . ALA B 1 458 ? -25.009 27.996  12.379  1.00 100.20 ? 458 ALA B O   1 
ATOM   7936  C CB  . ALA B 1 458 ? -22.790 26.150  13.992  1.00 102.81 ? 458 ALA B CB  1 
ATOM   7937  N N   . PRO B 1 459 ? -25.744 27.251  14.362  1.00 90.45  ? 459 PRO B N   1 
ATOM   7938  C CA  . PRO B 1 459 ? -26.737 28.324  14.447  1.00 91.76  ? 459 PRO B CA  1 
ATOM   7939  C C   . PRO B 1 459 ? -26.094 29.698  14.572  1.00 92.21  ? 459 PRO B C   1 
ATOM   7940  O O   . PRO B 1 459 ? -24.906 29.851  14.871  1.00 95.34  ? 459 PRO B O   1 
ATOM   7941  C CB  . PRO B 1 459 ? -27.538 27.966  15.704  1.00 92.09  ? 459 PRO B CB  1 
ATOM   7942  C CG  . PRO B 1 459 ? -26.565 27.237  16.546  1.00 98.18  ? 459 PRO B CG  1 
ATOM   7943  C CD  . PRO B 1 459 ? -25.760 26.412  15.574  1.00 100.57 ? 459 PRO B CD  1 
ATOM   7944  N N   . PHE B 1 460 ? -26.919 30.709  14.300  1.00 87.19  ? 460 PHE B N   1 
ATOM   7945  C CA  . PHE B 1 460 ? -26.626 32.133  14.394  1.00 76.15  ? 460 PHE B CA  1 
ATOM   7946  C C   . PHE B 1 460 ? -25.547 32.577  13.421  1.00 73.33  ? 460 PHE B C   1 
ATOM   7947  O O   . PHE B 1 460 ? -25.186 33.758  13.420  1.00 78.40  ? 460 PHE B O   1 
ATOM   7948  C CB  . PHE B 1 460 ? -26.237 32.542  15.821  1.00 77.99  ? 460 PHE B CB  1 
ATOM   7949  C CG  . PHE B 1 460 ? -27.296 32.232  16.836  1.00 78.97  ? 460 PHE B CG  1 
ATOM   7950  C CD1 . PHE B 1 460 ? -28.587 32.749  16.672  1.00 87.65  ? 460 PHE B CD1 1 
ATOM   7951  C CD2 . PHE B 1 460 ? -27.017 31.403  17.915  1.00 80.40  ? 460 PHE B CD2 1 
ATOM   7952  C CE1 . PHE B 1 460 ? -29.579 32.480  17.567  1.00 95.77  ? 460 PHE B CE1 1 
ATOM   7953  C CE2 . PHE B 1 460 ? -28.004 31.106  18.840  1.00 85.57  ? 460 PHE B CE2 1 
ATOM   7954  C CZ  . PHE B 1 460 ? -29.288 31.639  18.677  1.00 88.50  ? 460 PHE B CZ  1 
ATOM   7955  N N   . VAL B 1 461 ? -25.029 31.682  12.582  1.00 73.45  ? 461 VAL B N   1 
ATOM   7956  C CA  . VAL B 1 461 ? -24.009 32.069  11.616  1.00 72.53  ? 461 VAL B CA  1 
ATOM   7957  C C   . VAL B 1 461 ? -24.607 32.949  10.523  1.00 65.50  ? 461 VAL B C   1 
ATOM   7958  O O   . VAL B 1 461 ? -23.930 33.836  9.984   1.00 60.28  ? 461 VAL B O   1 
ATOM   7959  C CB  . VAL B 1 461 ? -23.340 30.801  11.050  1.00 81.13  ? 461 VAL B CB  1 
ATOM   7960  C CG1 . VAL B 1 461 ? -22.692 31.060  9.693   1.00 80.06  ? 461 VAL B CG1 1 
ATOM   7961  C CG2 . VAL B 1 461 ? -22.336 30.239  12.059  1.00 80.51  ? 461 VAL B CG2 1 
ATOM   7962  N N   . GLU B 1 462 ? -25.888 32.749  10.204  1.00 72.71  ? 462 GLU B N   1 
ATOM   7963  C CA  . GLU B 1 462 ? -26.510 33.501  9.120   1.00 65.60  ? 462 GLU B CA  1 
ATOM   7964  C C   . GLU B 1 462 ? -26.532 34.992  9.408   1.00 64.29  ? 462 GLU B C   1 
ATOM   7965  O O   . GLU B 1 462 ? -26.476 35.804  8.478   1.00 61.63  ? 462 GLU B O   1 
ATOM   7966  C CB  . GLU B 1 462 ? -27.930 33.001  8.871   1.00 67.75  ? 462 GLU B CB  1 
ATOM   7967  C CG  . GLU B 1 462 ? -28.795 32.877  10.125  1.00 80.18  ? 462 GLU B CG  1 
ATOM   7968  C CD  . GLU B 1 462 ? -28.580 31.567  10.872  1.00 93.57  ? 462 GLU B CD  1 
ATOM   7969  O OE1 . GLU B 1 462 ? -28.577 31.582  12.125  1.00 91.36  ? 462 GLU B OE1 1 
ATOM   7970  O OE2 . GLU B 1 462 ? -28.410 30.523  10.204  1.00 98.34  ? 462 GLU B OE2 1 
ATOM   7971  N N   . VAL B 1 463 ? -26.603 35.374  10.683  1.00 60.99  ? 463 VAL B N   1 
ATOM   7972  C CA  . VAL B 1 463 ? -26.628 36.792  11.017  1.00 61.01  ? 463 VAL B CA  1 
ATOM   7973  C C   . VAL B 1 463 ? -25.327 37.459  10.611  1.00 56.36  ? 463 VAL B C   1 
ATOM   7974  O O   . VAL B 1 463 ? -25.320 38.603  10.140  1.00 57.44  ? 463 VAL B O   1 
ATOM   7975  C CB  . VAL B 1 463 ? -26.899 36.992  12.513  1.00 59.91  ? 463 VAL B CB  1 
ATOM   7976  C CG1 . VAL B 1 463 ? -26.923 38.470  12.808  1.00 54.40  ? 463 VAL B CG1 1 
ATOM   7977  C CG2 . VAL B 1 463 ? -28.207 36.334  12.900  1.00 59.80  ? 463 VAL B CG2 1 
ATOM   7978  N N   . PHE B 1 464 ? -24.204 36.768  10.805  1.00 56.23  ? 464 PHE B N   1 
ATOM   7979  C CA  . PHE B 1 464 ? -22.920 37.352  10.435  1.00 55.95  ? 464 PHE B CA  1 
ATOM   7980  C C   . PHE B 1 464 ? -22.874 37.650  8.948   1.00 53.63  ? 464 PHE B C   1 
ATOM   7981  O O   . PHE B 1 464 ? -22.339 38.682  8.524   1.00 54.51  ? 464 PHE B O   1 
ATOM   7982  C CB  . PHE B 1 464 ? -21.780 36.416  10.828  1.00 53.54  ? 464 PHE B CB  1 
ATOM   7983  C CG  . PHE B 1 464 ? -21.554 36.322  12.304  1.00 49.54  ? 464 PHE B CG  1 
ATOM   7984  C CD1 . PHE B 1 464 ? -20.728 37.223  12.949  1.00 51.99  ? 464 PHE B CD1 1 
ATOM   7985  C CD2 . PHE B 1 464 ? -22.165 35.329  13.050  1.00 54.98  ? 464 PHE B CD2 1 
ATOM   7986  C CE1 . PHE B 1 464 ? -20.514 37.136  14.309  1.00 48.81  ? 464 PHE B CE1 1 
ATOM   7987  C CE2 . PHE B 1 464 ? -21.954 35.235  14.411  1.00 51.88  ? 464 PHE B CE2 1 
ATOM   7988  C CZ  . PHE B 1 464 ? -21.127 36.141  15.041  1.00 50.41  ? 464 PHE B CZ  1 
ATOM   7989  N N   . ASP B 1 465 ? -23.454 36.768  8.140   1.00 55.58  ? 465 ASP B N   1 
ATOM   7990  C CA  . ASP B 1 465 ? -23.537 37.042  6.717   1.00 60.76  ? 465 ASP B CA  1 
ATOM   7991  C C   . ASP B 1 465 ? -24.404 38.266  6.447   1.00 64.51  ? 465 ASP B C   1 
ATOM   7992  O O   . ASP B 1 465 ? -24.015 39.156  5.680   1.00 61.42  ? 465 ASP B O   1 
ATOM   7993  C CB  . ASP B 1 465 ? -24.071 35.821  5.982   1.00 63.96  ? 465 ASP B CB  1 
ATOM   7994  C CG  . ASP B 1 465 ? -24.143 36.047  4.506   1.00 67.98  ? 465 ASP B CG  1 
ATOM   7995  O OD1 . ASP B 1 465 ? -23.091 35.879  3.853   1.00 57.99  ? 465 ASP B OD1 1 
ATOM   7996  O OD2 . ASP B 1 465 ? -25.236 36.388  4.004   1.00 73.05  ? 465 ASP B OD2 1 
ATOM   7997  N N   . LYS B 1 466 ? -25.576 38.339  7.093   1.00 52.03  ? 466 LYS B N   1 
ATOM   7998  C CA  . LYS B 1 466 ? -26.453 39.497  6.913   1.00 60.14  ? 466 LYS B CA  1 
ATOM   7999  C C   . LYS B 1 466 ? -25.758 40.788  7.337   1.00 54.77  ? 466 LYS B C   1 
ATOM   8000  O O   . LYS B 1 466 ? -25.924 41.835  6.697   1.00 48.41  ? 466 LYS B O   1 
ATOM   8001  C CB  . LYS B 1 466 ? -27.757 39.303  7.694   1.00 57.49  ? 466 LYS B CB  1 
ATOM   8002  C CG  . LYS B 1 466 ? -28.442 37.967  7.431   1.00 71.76  ? 466 LYS B CG  1 
ATOM   8003  C CD  . LYS B 1 466 ? -28.921 37.845  5.983   1.00 73.42  ? 466 LYS B CD  1 
ATOM   8004  C CE  . LYS B 1 466 ? -30.410 37.501  5.901   1.00 87.13  ? 466 LYS B CE  1 
ATOM   8005  N NZ  . LYS B 1 466 ? -31.012 37.771  4.554   1.00 86.98  ? 466 LYS B NZ  1 
ATOM   8006  N N   . LEU B 1 467 ? -24.964 40.734  8.407   1.00 55.99  ? 467 LEU B N   1 
ATOM   8007  C CA  . LEU B 1 467 ? -24.237 41.922  8.833   1.00 57.18  ? 467 LEU B CA  1 
ATOM   8008  C C   . LEU B 1 467 ? -23.113 42.257  7.860   1.00 61.89  ? 467 LEU B C   1 
ATOM   8009  O O   . LEU B 1 467 ? -22.962 43.414  7.449   1.00 59.72  ? 467 LEU B O   1 
ATOM   8010  C CB  . LEU B 1 467 ? -23.687 41.732  10.242  1.00 53.22  ? 467 LEU B CB  1 
ATOM   8011  C CG  . LEU B 1 467 ? -24.720 41.981  11.335  1.00 54.99  ? 467 LEU B CG  1 
ATOM   8012  C CD1 . LEU B 1 467 ? -24.274 41.288  12.610  1.00 55.07  ? 467 LEU B CD1 1 
ATOM   8013  C CD2 . LEU B 1 467 ? -24.943 43.472  11.560  1.00 53.00  ? 467 LEU B CD2 1 
ATOM   8014  N N   . PHE B 1 468 ? -22.314 41.255  7.474   1.00 54.30  ? 468 PHE B N   1 
ATOM   8015  C CA  . PHE B 1 468 ? -21.231 41.510  6.529   1.00 52.83  ? 468 PHE B CA  1 
ATOM   8016  C C   . PHE B 1 468 ? -21.775 42.034  5.208   1.00 55.19  ? 468 PHE B C   1 
ATOM   8017  O O   . PHE B 1 468 ? -21.199 42.949  4.608   1.00 52.81  ? 468 PHE B O   1 
ATOM   8018  C CB  . PHE B 1 468 ? -20.404 40.242  6.305   1.00 55.62  ? 468 PHE B CB  1 
ATOM   8019  C CG  . PHE B 1 468 ? -19.386 40.364  5.197   1.00 51.06  ? 468 PHE B CG  1 
ATOM   8020  C CD1 . PHE B 1 468 ? -18.214 41.078  5.389   1.00 54.28  ? 468 PHE B CD1 1 
ATOM   8021  C CD2 . PHE B 1 468 ? -19.605 39.766  3.968   1.00 52.77  ? 468 PHE B CD2 1 
ATOM   8022  C CE1 . PHE B 1 468 ? -17.273 41.189  4.373   1.00 57.07  ? 468 PHE B CE1 1 
ATOM   8023  C CE2 . PHE B 1 468 ? -18.669 39.873  2.945   1.00 59.50  ? 468 PHE B CE2 1 
ATOM   8024  C CZ  . PHE B 1 468 ? -17.500 40.586  3.147   1.00 50.83  ? 468 PHE B CZ  1 
ATOM   8025  N N   . ARG B 1 469 ? -22.895 41.477  4.743   1.00 50.73  ? 469 ARG B N   1 
ATOM   8026  C CA  . ARG B 1 469 ? -23.465 41.948  3.487   1.00 57.45  ? 469 ARG B CA  1 
ATOM   8027  C C   . ARG B 1 469 ? -24.111 43.316  3.631   1.00 57.52  ? 469 ARG B C   1 
ATOM   8028  O O   . ARG B 1 469 ? -24.224 44.047  2.640   1.00 59.54  ? 469 ARG B O   1 
ATOM   8029  C CB  . ARG B 1 469 ? -24.473 40.933  2.950   1.00 48.23  ? 469 ARG B CB  1 
ATOM   8030  C CG  . ARG B 1 469 ? -23.820 39.596  2.655   1.00 60.45  ? 469 ARG B CG  1 
ATOM   8031  C CD  . ARG B 1 469 ? -24.560 38.775  1.616   1.00 69.27  ? 469 ARG B CD  1 
ATOM   8032  N NE  . ARG B 1 469 ? -23.867 37.520  1.345   1.00 60.71  ? 469 ARG B NE  1 
ATOM   8033  C CZ  . ARG B 1 469 ? -23.257 37.219  0.206   1.00 66.60  ? 469 ARG B CZ  1 
ATOM   8034  N NH1 . ARG B 1 469 ? -23.255 38.057  -0.821  1.00 69.59  ? 469 ARG B NH1 1 
ATOM   8035  N NH2 . ARG B 1 469 ? -22.646 36.041  0.089   1.00 58.13  ? 469 ARG B NH2 1 
ATOM   8036  N N   . SER B 1 470 ? -24.527 43.682  4.840   1.00 57.23  ? 470 SER B N   1 
ATOM   8037  C CA  . SER B 1 470 ? -25.059 45.020  5.037   1.00 57.07  ? 470 SER B CA  1 
ATOM   8038  C C   . SER B 1 470 ? -23.943 46.050  4.980   1.00 58.19  ? 470 SER B C   1 
ATOM   8039  O O   . SER B 1 470 ? -24.072 47.079  4.308   1.00 59.88  ? 470 SER B O   1 
ATOM   8040  C CB  . SER B 1 470 ? -25.810 45.089  6.364   1.00 52.47  ? 470 SER B CB  1 
ATOM   8041  O OG  . SER B 1 470 ? -26.845 46.050  6.303   1.00 57.51  ? 470 SER B OG  1 
ATOM   8042  N N   . PHE B 1 471 ? -22.831 45.784  5.667   1.00 51.11  ? 471 PHE B N   1 
ATOM   8043  C CA  . PHE B 1 471 ? -21.733 46.739  5.661   1.00 53.83  ? 471 PHE B CA  1 
ATOM   8044  C C   . PHE B 1 471 ? -21.176 46.941  4.254   1.00 55.69  ? 471 PHE B C   1 
ATOM   8045  O O   . PHE B 1 471 ? -20.849 48.069  3.865   1.00 57.47  ? 471 PHE B O   1 
ATOM   8046  C CB  . PHE B 1 471 ? -20.635 46.285  6.621   1.00 52.71  ? 471 PHE B CB  1 
ATOM   8047  C CG  . PHE B 1 471 ? -21.077 46.180  8.041   1.00 43.90  ? 471 PHE B CG  1 
ATOM   8048  C CD1 . PHE B 1 471 ? -21.752 47.218  8.656   1.00 55.97  ? 471 PHE B CD1 1 
ATOM   8049  C CD2 . PHE B 1 471 ? -20.829 45.031  8.762   1.00 50.30  ? 471 PHE B CD2 1 
ATOM   8050  C CE1 . PHE B 1 471 ? -22.159 47.117  9.979   1.00 56.22  ? 471 PHE B CE1 1 
ATOM   8051  C CE2 . PHE B 1 471 ? -21.239 44.916  10.078  1.00 51.34  ? 471 PHE B CE2 1 
ATOM   8052  C CZ  . PHE B 1 471 ? -21.901 45.961  10.688  1.00 51.84  ? 471 PHE B CZ  1 
ATOM   8053  N N   . VAL B 1 472 ? -21.067 45.874  3.464   1.00 55.76  ? 472 VAL B N   1 
ATOM   8054  C CA  . VAL B 1 472 ? -20.486 46.050  2.136   1.00 58.67  ? 472 VAL B CA  1 
ATOM   8055  C C   . VAL B 1 472 ? -21.407 46.884  1.254   1.00 61.59  ? 472 VAL B C   1 
ATOM   8056  O O   . VAL B 1 472 ? -20.939 47.692  0.444   1.00 69.47  ? 472 VAL B O   1 
ATOM   8057  C CB  . VAL B 1 472 ? -20.153 44.695  1.491   1.00 52.21  ? 472 VAL B CB  1 
ATOM   8058  C CG1 . VAL B 1 472 ? -19.218 43.916  2.378   1.00 59.33  ? 472 VAL B CG1 1 
ATOM   8059  C CG2 . VAL B 1 472 ? -21.400 43.912  1.242   1.00 55.84  ? 472 VAL B CG2 1 
ATOM   8060  N N   . ARG B 1 473 ? -22.727 46.719  1.400   1.00 59.95  ? 473 ARG B N   1 
ATOM   8061  C CA  . ARG B 1 473 ? -23.648 47.526  0.603   1.00 66.45  ? 473 ARG B CA  1 
ATOM   8062  C C   . ARG B 1 473 ? -23.612 48.982  1.043   1.00 69.85  ? 473 ARG B C   1 
ATOM   8063  O O   . ARG B 1 473 ? -23.641 49.893  0.206   1.00 72.29  ? 473 ARG B O   1 
ATOM   8064  C CB  . ARG B 1 473 ? -25.077 46.979  0.691   1.00 64.74  ? 473 ARG B CB  1 
ATOM   8065  C CG  . ARG B 1 473 ? -26.079 47.849  -0.068  1.00 65.28  ? 473 ARG B CG  1 
ATOM   8066  C CD  . ARG B 1 473 ? -27.353 47.115  -0.500  1.00 77.60  ? 473 ARG B CD  1 
ATOM   8067  N NE  . ARG B 1 473 ? -28.351 46.979  0.560   1.00 91.73  ? 473 ARG B NE  1 
ATOM   8068  C CZ  . ARG B 1 473 ? -29.365 47.815  0.754   1.00 84.14  ? 473 ARG B CZ  1 
ATOM   8069  N NH1 . ARG B 1 473 ? -29.528 48.890  0.000   1.00 92.25  ? 473 ARG B NH1 1 
ATOM   8070  N NH2 . ARG B 1 473 ? -30.238 47.567  1.731   1.00 66.06  ? 473 ARG B NH2 1 
ATOM   8071  N N   . ARG B 1 474 ? -23.531 49.215  2.353   1.00 64.11  ? 474 ARG B N   1 
ATOM   8072  C CA  . ARG B 1 474 ? -23.454 50.565  2.892   1.00 64.13  ? 474 ARG B CA  1 
ATOM   8073  C C   . ARG B 1 474 ? -22.149 51.262  2.522   1.00 65.16  ? 474 ARG B C   1 
ATOM   8074  O O   . ARG B 1 474 ? -22.096 52.496  2.519   1.00 71.71  ? 474 ARG B O   1 
ATOM   8075  C CB  . ARG B 1 474 ? -23.630 50.501  4.410   1.00 62.19  ? 474 ARG B CB  1 
ATOM   8076  C CG  . ARG B 1 474 ? -23.835 51.824  5.126   1.00 70.59  ? 474 ARG B CG  1 
ATOM   8077  C CD  . ARG B 1 474 ? -24.888 52.735  4.501   1.00 76.61  ? 474 ARG B CD  1 
ATOM   8078  N NE  . ARG B 1 474 ? -24.960 53.963  5.287   1.00 89.90  ? 474 ARG B NE  1 
ATOM   8079  C CZ  . ARG B 1 474 ? -25.621 54.096  6.431   1.00 93.55  ? 474 ARG B CZ  1 
ATOM   8080  N NH1 . ARG B 1 474 ? -26.431 53.148  6.881   1.00 89.34  ? 474 ARG B NH1 1 
ATOM   8081  N NH2 . ARG B 1 474 ? -25.459 55.207  7.148   1.00 91.99  ? 474 ARG B NH2 1 
ATOM   8082  N N   . ALA B 1 475 ? -21.104 50.503  2.185   1.00 59.88  ? 475 ALA B N   1 
ATOM   8083  C CA  . ALA B 1 475 ? -19.829 51.116  1.825   1.00 67.75  ? 475 ALA B CA  1 
ATOM   8084  C C   . ALA B 1 475 ? -19.896 51.813  0.467   1.00 67.64  ? 475 ALA B C   1 
ATOM   8085  O O   . ALA B 1 475 ? -19.254 52.853  0.269   1.00 63.68  ? 475 ALA B O   1 
ATOM   8086  C CB  . ALA B 1 475 ? -18.721 50.061  1.833   1.00 62.30  ? 475 ALA B CB  1 
ATOM   8087  N N   . GLN B 1 476 ? -20.672 51.268  -0.473  1.00 61.75  ? 476 GLN B N   1 
ATOM   8088  C CA  . GLN B 1 476 ? -20.716 51.756  -1.849  1.00 62.93  ? 476 GLN B CA  1 
ATOM   8089  C C   . GLN B 1 476 ? -21.762 52.843  -2.083  1.00 66.69  ? 476 GLN B C   1 
ATOM   8090  O O   . GLN B 1 476 ? -22.007 53.210  -3.236  1.00 76.39  ? 476 GLN B O   1 
ATOM   8091  C CB  . GLN B 1 476 ? -20.961 50.586  -2.806  1.00 67.04  ? 476 GLN B CB  1 
ATOM   8092  C CG  . GLN B 1 476 ? -20.555 49.249  -2.226  1.00 61.32  ? 476 GLN B CG  1 
ATOM   8093  C CD  . GLN B 1 476 ? -20.452 48.160  -3.268  1.00 62.86  ? 476 GLN B CD  1 
ATOM   8094  O OE1 . GLN B 1 476 ? -19.917 48.369  -4.358  1.00 68.29  ? 476 GLN B OE1 1 
ATOM   8095  N NE2 . GLN B 1 476 ? -20.958 46.980  -2.934  1.00 65.61  ? 476 GLN B NE2 1 
ATOM   8096  N N   . GLU B 1 477 ? -22.378 53.372  -1.031  1.00 66.95  ? 477 GLU B N   1 
ATOM   8097  C CA  . GLU B 1 477 ? -23.340 54.459  -1.187  1.00 71.27  ? 477 GLU B CA  1 
ATOM   8098  C C   . GLU B 1 477 ? -22.824 55.759  -0.575  1.00 84.81  ? 477 GLU B C   1 
ATOM   8099  O O   . GLU B 1 477 ? -23.520 56.408  0.209   1.00 94.91  ? 477 GLU B O   1 
ATOM   8100  C CB  . GLU B 1 477 ? -24.678 54.077  -0.558  1.00 71.35  ? 477 GLU B CB  1 
ATOM   8101  C CG  . GLU B 1 477 ? -25.000 52.598  -0.666  1.00 70.40  ? 477 GLU B CG  1 
ATOM   8102  C CD  . GLU B 1 477 ? -26.242 52.214  0.107   1.00 72.30  ? 477 GLU B CD  1 
ATOM   8103  O OE1 . GLU B 1 477 ? -26.788 53.079  0.823   1.00 83.12  ? 477 GLU B OE1 1 
ATOM   8104  O OE2 . GLU B 1 477 ? -26.684 51.053  -0.018  1.00 69.90  ? 477 GLU B OE2 1 
ATOM   8105  N N   . MET C 1 1   ? 34.783  21.005  39.444  1.00 91.45  ? 1   MET C N   1 
ATOM   8106  C CA  . MET C 1 1   ? 33.614  20.610  40.217  1.00 80.44  ? 1   MET C CA  1 
ATOM   8107  C C   . MET C 1 1   ? 33.907  19.654  41.345  1.00 76.06  ? 1   MET C C   1 
ATOM   8108  O O   . MET C 1 1   ? 34.241  18.489  41.114  1.00 72.28  ? 1   MET C O   1 
ATOM   8109  C CB  . MET C 1 1   ? 32.600  19.953  39.316  1.00 85.81  ? 1   MET C CB  1 
ATOM   8110  C CG  . MET C 1 1   ? 31.211  19.928  39.883  1.00 93.57  ? 1   MET C CG  1 
ATOM   8111  S SD  . MET C 1 1   ? 30.064  19.928  38.522  1.00 120.35 ? 1   MET C SD  1 
ATOM   8112  C CE  . MET C 1 1   ? 31.117  19.255  37.227  1.00 97.12  ? 1   MET C CE  1 
ATOM   8113  N N   . LYS C 1 2   ? 33.748  20.143  42.569  1.00 79.27  ? 2   LYS C N   1 
ATOM   8114  C CA  . LYS C 1 2   ? 33.793  19.259  43.719  1.00 74.78  ? 2   LYS C CA  1 
ATOM   8115  C C   . LYS C 1 2   ? 32.591  18.332  43.665  1.00 81.69  ? 2   LYS C C   1 
ATOM   8116  O O   . LYS C 1 2   ? 31.472  18.760  43.367  1.00 85.00  ? 2   LYS C O   1 
ATOM   8117  C CB  . LYS C 1 2   ? 33.797  20.061  45.015  1.00 68.45  ? 2   LYS C CB  1 
ATOM   8118  C CG  . LYS C 1 2   ? 33.720  19.201  46.261  1.00 81.26  ? 2   LYS C CG  1 
ATOM   8119  C CD  . LYS C 1 2   ? 34.253  19.946  47.467  1.00 83.38  ? 2   LYS C CD  1 
ATOM   8120  C CE  . LYS C 1 2   ? 33.140  20.647  48.211  1.00 81.78  ? 2   LYS C CE  1 
ATOM   8121  N NZ  . LYS C 1 2   ? 33.547  22.010  48.637  1.00 74.87  ? 2   LYS C NZ  1 
ATOM   8122  N N   . LYS C 1 3   ? 32.824  17.055  43.929  1.00 80.64  ? 3   LYS C N   1 
ATOM   8123  C CA  . LYS C 1 3   ? 31.804  16.028  43.760  1.00 79.93  ? 3   LYS C CA  1 
ATOM   8124  C C   . LYS C 1 3   ? 31.445  15.456  45.122  1.00 75.74  ? 3   LYS C C   1 
ATOM   8125  O O   . LYS C 1 3   ? 32.277  14.813  45.770  1.00 74.39  ? 3   LYS C O   1 
ATOM   8126  C CB  . LYS C 1 3   ? 32.292  14.928  42.820  1.00 81.80  ? 3   LYS C CB  1 
ATOM   8127  C CG  . LYS C 1 3   ? 33.212  15.420  41.715  1.00 88.95  ? 3   LYS C CG  1 
ATOM   8128  C CD  . LYS C 1 3   ? 33.400  14.363  40.636  1.00 93.90  ? 3   LYS C CD  1 
ATOM   8129  C CE  . LYS C 1 3   ? 34.880  14.121  40.354  1.00 96.28  ? 3   LYS C CE  1 
ATOM   8130  N NZ  . LYS C 1 3   ? 35.113  12.840  39.626  1.00 95.75  ? 3   LYS C NZ  1 
ATOM   8131  N N   . LEU C 1 4   ? 30.209  15.689  45.552  1.00 79.73  ? 4   LEU C N   1 
ATOM   8132  C CA  . LEU C 1 4   ? 29.680  14.962  46.697  1.00 77.14  ? 4   LEU C CA  1 
ATOM   8133  C C   . LEU C 1 4   ? 29.465  13.505  46.300  1.00 68.97  ? 4   LEU C C   1 
ATOM   8134  O O   . LEU C 1 4   ? 28.918  13.217  45.229  1.00 65.50  ? 4   LEU C O   1 
ATOM   8135  C CB  . LEU C 1 4   ? 28.374  15.600  47.182  1.00 72.27  ? 4   LEU C CB  1 
ATOM   8136  C CG  . LEU C 1 4   ? 27.531  14.816  48.196  1.00 71.98  ? 4   LEU C CG  1 
ATOM   8137  C CD1 . LEU C 1 4   ? 26.940  15.758  49.242  1.00 71.23  ? 4   LEU C CD1 1 
ATOM   8138  C CD2 . LEU C 1 4   ? 26.426  14.004  47.518  1.00 70.37  ? 4   LEU C CD2 1 
ATOM   8139  N N   . PHE C 1 5   ? 29.925  12.587  47.145  1.00 65.80  ? 5   PHE C N   1 
ATOM   8140  C CA  . PHE C 1 5   ? 29.836  11.157  46.876  1.00 68.80  ? 5   PHE C CA  1 
ATOM   8141  C C   . PHE C 1 5   ? 28.705  10.592  47.721  1.00 63.92  ? 5   PHE C C   1 
ATOM   8142  O O   . PHE C 1 5   ? 28.800  10.547  48.951  1.00 67.57  ? 5   PHE C O   1 
ATOM   8143  C CB  . PHE C 1 5   ? 31.162  10.458  47.164  1.00 58.75  ? 5   PHE C CB  1 
ATOM   8144  C CG  . PHE C 1 5   ? 32.289  10.930  46.290  1.00 67.00  ? 5   PHE C CG  1 
ATOM   8145  C CD1 . PHE C 1 5   ? 32.173  10.893  44.912  1.00 66.12  ? 5   PHE C CD1 1 
ATOM   8146  C CD2 . PHE C 1 5   ? 33.461  11.420  46.845  1.00 72.02  ? 5   PHE C CD2 1 
ATOM   8147  C CE1 . PHE C 1 5   ? 33.202  11.335  44.104  1.00 69.05  ? 5   PHE C CE1 1 
ATOM   8148  C CE2 . PHE C 1 5   ? 34.494  11.862  46.043  1.00 73.30  ? 5   PHE C CE2 1 
ATOM   8149  C CZ  . PHE C 1 5   ? 34.364  11.818  44.668  1.00 79.74  ? 5   PHE C CZ  1 
ATOM   8150  N N   . LEU C 1 6   ? 27.633  10.180  47.058  1.00 64.40  ? 6   LEU C N   1 
ATOM   8151  C CA  . LEU C 1 6   ? 26.455  9.636   47.717  1.00 67.56  ? 6   LEU C CA  1 
ATOM   8152  C C   . LEU C 1 6   ? 26.450  8.124   47.556  1.00 64.54  ? 6   LEU C C   1 
ATOM   8153  O O   . LEU C 1 6   ? 26.506  7.615   46.430  1.00 64.11  ? 6   LEU C O   1 
ATOM   8154  C CB  . LEU C 1 6   ? 25.182  10.243  47.130  1.00 70.76  ? 6   LEU C CB  1 
ATOM   8155  C CG  . LEU C 1 6   ? 23.879  9.967   47.873  1.00 63.19  ? 6   LEU C CG  1 
ATOM   8156  C CD1 . LEU C 1 6   ? 23.877  10.679  49.215  1.00 63.22  ? 6   LEU C CD1 1 
ATOM   8157  C CD2 . LEU C 1 6   ? 22.697  10.401  47.015  1.00 65.97  ? 6   LEU C CD2 1 
ATOM   8158  N N   . VAL C 1 7   ? 26.387  7.415   48.679  1.00 65.05  ? 7   VAL C N   1 
ATOM   8159  C CA  . VAL C 1 7   ? 26.360  5.957   48.710  1.00 62.92  ? 7   VAL C CA  1 
ATOM   8160  C C   . VAL C 1 7   ? 25.037  5.524   49.331  1.00 63.90  ? 7   VAL C C   1 
ATOM   8161  O O   . VAL C 1 7   ? 24.796  5.750   50.524  1.00 68.70  ? 7   VAL C O   1 
ATOM   8162  C CB  . VAL C 1 7   ? 27.551  5.385   49.490  1.00 56.65  ? 7   VAL C CB  1 
ATOM   8163  C CG1 . VAL C 1 7   ? 27.533  3.868   49.439  1.00 58.68  ? 7   VAL C CG1 1 
ATOM   8164  C CG2 . VAL C 1 7   ? 28.864  5.931   48.933  1.00 55.62  ? 7   VAL C CG2 1 
ATOM   8165  N N   . PHE C 1 8   ? 24.179  4.900   48.524  1.00 56.75  ? 8   PHE C N   1 
ATOM   8166  C CA  . PHE C 1 8   ? 22.923  4.330   48.995  1.00 49.68  ? 8   PHE C CA  1 
ATOM   8167  C C   . PHE C 1 8   ? 23.137  2.872   49.375  1.00 45.58  ? 8   PHE C C   1 
ATOM   8168  O O   . PHE C 1 8   ? 23.653  2.090   48.572  1.00 54.80  ? 8   PHE C O   1 
ATOM   8169  C CB  . PHE C 1 8   ? 21.854  4.422   47.906  1.00 57.86  ? 8   PHE C CB  1 
ATOM   8170  C CG  . PHE C 1 8   ? 21.157  5.751   47.838  1.00 58.89  ? 8   PHE C CG  1 
ATOM   8171  C CD1 . PHE C 1 8   ? 20.479  6.254   48.938  1.00 60.26  ? 8   PHE C CD1 1 
ATOM   8172  C CD2 . PHE C 1 8   ? 21.174  6.491   46.671  1.00 48.09  ? 8   PHE C CD2 1 
ATOM   8173  C CE1 . PHE C 1 8   ? 19.840  7.472   48.876  1.00 59.03  ? 8   PHE C CE1 1 
ATOM   8174  C CE2 . PHE C 1 8   ? 20.534  7.709   46.602  1.00 65.35  ? 8   PHE C CE2 1 
ATOM   8175  C CZ  . PHE C 1 8   ? 19.866  8.203   47.703  1.00 59.04  ? 8   PHE C CZ  1 
ATOM   8176  N N   . TRP C 1 9   ? 22.726  2.501   50.586  1.00 51.97  ? 9   TRP C N   1 
ATOM   8177  C CA  . TRP C 1 9   ? 22.917  1.140   51.104  1.00 53.18  ? 9   TRP C CA  1 
ATOM   8178  C C   . TRP C 1 9   ? 21.598  0.679   51.725  1.00 55.15  ? 9   TRP C C   1 
ATOM   8179  O O   . TRP C 1 9   ? 21.306  0.995   52.882  1.00 53.61  ? 9   TRP C O   1 
ATOM   8180  C CB  . TRP C 1 9   ? 24.078  1.106   52.116  1.00 52.90  ? 9   TRP C CB  1 
ATOM   8181  C CG  . TRP C 1 9   ? 24.676  -0.259  52.385  1.00 53.96  ? 9   TRP C CG  1 
ATOM   8182  C CD1 . TRP C 1 9   ? 24.227  -1.467  51.919  1.00 52.79  ? 9   TRP C CD1 1 
ATOM   8183  C CD2 . TRP C 1 9   ? 25.841  -0.547  53.180  1.00 54.27  ? 9   TRP C CD2 1 
ATOM   8184  N NE1 . TRP C 1 9   ? 25.035  -2.484  52.381  1.00 45.71  ? 9   TRP C NE1 1 
ATOM   8185  C CE2 . TRP C 1 9   ? 26.031  -1.946  53.156  1.00 53.04  ? 9   TRP C CE2 1 
ATOM   8186  C CE3 . TRP C 1 9   ? 26.738  0.241   53.911  1.00 52.40  ? 9   TRP C CE3 1 
ATOM   8187  C CZ2 . TRP C 1 9   ? 27.082  -2.570  53.833  1.00 55.33  ? 9   TRP C CZ2 1 
ATOM   8188  C CZ3 . TRP C 1 9   ? 27.778  -0.383  54.580  1.00 51.20  ? 9   TRP C CZ3 1 
ATOM   8189  C CH2 . TRP C 1 9   ? 27.940  -1.773  54.537  1.00 54.52  ? 9   TRP C CH2 1 
ATOM   8190  N N   . TRP C 1 10  ? 20.798  -0.056  50.952  1.00 53.88  ? 10  TRP C N   1 
ATOM   8191  C CA  . TRP C 1 10  ? 19.515  -0.561  51.432  1.00 49.52  ? 10  TRP C CA  1 
ATOM   8192  C C   . TRP C 1 10  ? 19.703  -1.893  52.144  1.00 48.55  ? 10  TRP C C   1 
ATOM   8193  O O   . TRP C 1 10  ? 20.287  -2.824  51.584  1.00 47.95  ? 10  TRP C O   1 
ATOM   8194  C CB  . TRP C 1 10  ? 18.540  -0.737  50.271  1.00 54.32  ? 10  TRP C CB  1 
ATOM   8195  C CG  . TRP C 1 10  ? 18.332  0.486   49.436  1.00 56.16  ? 10  TRP C CG  1 
ATOM   8196  C CD1 . TRP C 1 10  ? 18.821  0.715   48.182  1.00 45.15  ? 10  TRP C CD1 1 
ATOM   8197  C CD2 . TRP C 1 10  ? 17.556  1.640   49.782  1.00 61.99  ? 10  TRP C CD2 1 
ATOM   8198  N NE1 . TRP C 1 10  ? 18.408  1.948   47.731  1.00 50.91  ? 10  TRP C NE1 1 
ATOM   8199  C CE2 . TRP C 1 10  ? 17.630  2.535   48.695  1.00 60.84  ? 10  TRP C CE2 1 
ATOM   8200  C CE3 . TRP C 1 10  ? 16.811  2.006   50.909  1.00 54.33  ? 10  TRP C CE3 1 
ATOM   8201  C CZ2 . TRP C 1 10  ? 16.986  3.770   48.701  1.00 61.82  ? 10  TRP C CZ2 1 
ATOM   8202  C CZ3 . TRP C 1 10  ? 16.173  3.231   50.912  1.00 50.03  ? 10  TRP C CZ3 1 
ATOM   8203  C CH2 . TRP C 1 10  ? 16.265  4.099   49.818  1.00 59.87  ? 10  TRP C CH2 1 
ATOM   8204  N N   . HIS C 1 11  ? 19.197  -1.990  53.370  1.00 48.23  ? 11  HIS C N   1 
ATOM   8205  C CA  . HIS C 1 11  ? 19.392  -3.170  54.207  1.00 44.34  ? 11  HIS C CA  1 
ATOM   8206  C C   . HIS C 1 11  ? 18.124  -4.020  54.208  1.00 43.94  ? 11  HIS C C   1 
ATOM   8207  O O   . HIS C 1 11  ? 17.042  -3.529  54.555  1.00 41.66  ? 11  HIS C O   1 
ATOM   8208  C CB  . HIS C 1 11  ? 19.771  -2.765  55.631  1.00 45.64  ? 11  HIS C CB  1 
ATOM   8209  C CG  . HIS C 1 11  ? 19.488  -3.825  56.645  1.00 42.06  ? 11  HIS C CG  1 
ATOM   8210  N ND1 . HIS C 1 11  ? 20.118  -5.051  56.633  1.00 41.24  ? 11  HIS C ND1 1 
ATOM   8211  C CD2 . HIS C 1 11  ? 18.609  -3.863  57.673  1.00 44.94  ? 11  HIS C CD2 1 
ATOM   8212  C CE1 . HIS C 1 11  ? 19.653  -5.792  57.622  1.00 46.43  ? 11  HIS C CE1 1 
ATOM   8213  N NE2 . HIS C 1 11  ? 18.735  -5.095  58.267  1.00 49.47  ? 11  HIS C NE2 1 
ATOM   8214  N N   . MET C 1 12  ? 18.259  -5.294  53.835  1.00 40.92  ? 12  MET C N   1 
ATOM   8215  C CA  . MET C 1 12  ? 17.117  -6.194  53.689  1.00 54.45  ? 12  MET C CA  1 
ATOM   8216  C C   . MET C 1 12  ? 17.274  -7.375  54.636  1.00 46.37  ? 12  MET C C   1 
ATOM   8217  O O   . MET C 1 12  ? 18.284  -8.084  54.587  1.00 47.61  ? 12  MET C O   1 
ATOM   8218  C CB  . MET C 1 12  ? 16.978  -6.682  52.242  1.00 51.88  ? 12  MET C CB  1 
ATOM   8219  C CG  . MET C 1 12  ? 17.293  -5.619  51.202  1.00 52.95  ? 12  MET C CG  1 
ATOM   8220  S SD  . MET C 1 12  ? 16.011  -4.357  51.051  1.00 75.02  ? 12  MET C SD  1 
ATOM   8221  C CE  . MET C 1 12  ? 15.864  -4.239  49.270  1.00 68.70  ? 12  MET C CE  1 
ATOM   8222  N N   . HIS C 1 13  ? 16.269  -7.593  55.482  1.00 44.61  ? 13  HIS C N   1 
ATOM   8223  C CA  . HIS C 1 13  ? 16.351  -8.645  56.481  1.00 50.30  ? 13  HIS C CA  1 
ATOM   8224  C C   . HIS C 1 13  ? 14.957  -9.045  56.954  1.00 54.84  ? 13  HIS C C   1 
ATOM   8225  O O   . HIS C 1 13  ? 14.065  -8.199  57.081  1.00 54.89  ? 13  HIS C O   1 
ATOM   8226  C CB  . HIS C 1 13  ? 17.206  -8.209  57.675  1.00 48.22  ? 13  HIS C CB  1 
ATOM   8227  C CG  . HIS C 1 13  ? 16.944  -9.007  58.908  1.00 46.09  ? 13  HIS C CG  1 
ATOM   8228  N ND1 . HIS C 1 13  ? 17.203  -10.359 58.984  1.00 45.47  ? 13  HIS C ND1 1 
ATOM   8229  C CD2 . HIS C 1 13  ? 16.428  -8.652  60.107  1.00 47.12  ? 13  HIS C CD2 1 
ATOM   8230  C CE1 . HIS C 1 13  ? 16.857  -10.803 60.178  1.00 45.91  ? 13  HIS C CE1 1 
ATOM   8231  N NE2 . HIS C 1 13  ? 16.387  -9.787  60.880  1.00 51.46  ? 13  HIS C NE2 1 
ATOM   8232  N N   . GLN C 1 14  ? 14.784  -10.343 57.212  1.00 49.39  ? 14  GLN C N   1 
ATOM   8233  C CA  . GLN C 1 14  ? 13.566  -10.904 57.771  1.00 55.20  ? 14  GLN C CA  1 
ATOM   8234  C C   . GLN C 1 14  ? 13.975  -11.992 58.749  1.00 52.87  ? 14  GLN C C   1 
ATOM   8235  O O   . GLN C 1 14  ? 14.882  -12.783 58.448  1.00 52.65  ? 14  GLN C O   1 
ATOM   8236  C CB  . GLN C 1 14  ? 12.646  -11.517 56.709  1.00 55.31  ? 14  GLN C CB  1 
ATOM   8237  C CG  . GLN C 1 14  ? 11.825  -10.527 55.928  1.00 52.19  ? 14  GLN C CG  1 
ATOM   8238  C CD  . GLN C 1 14  ? 10.968  -9.650  56.805  1.00 53.84  ? 14  GLN C CD  1 
ATOM   8239  O OE1 . GLN C 1 14  ? 10.449  -10.089 57.828  1.00 53.12  ? 14  GLN C OE1 1 
ATOM   8240  N NE2 . GLN C 1 14  ? 10.784  -8.405  56.387  1.00 61.27  ? 14  GLN C NE2 1 
ATOM   8241  N N   . PRO C 1 15  ? 13.320  -12.079 59.899  1.00 49.94  ? 15  PRO C N   1 
ATOM   8242  C CA  . PRO C 1 15  ? 13.640  -13.148 60.847  1.00 50.45  ? 15  PRO C CA  1 
ATOM   8243  C C   . PRO C 1 15  ? 13.203  -14.492 60.291  1.00 49.52  ? 15  PRO C C   1 
ATOM   8244  O O   . PRO C 1 15  ? 12.561  -14.585 59.245  1.00 56.01  ? 15  PRO C O   1 
ATOM   8245  C CB  . PRO C 1 15  ? 12.851  -12.770 62.106  1.00 49.43  ? 15  PRO C CB  1 
ATOM   8246  C CG  . PRO C 1 15  ? 12.430  -11.342 61.894  1.00 58.74  ? 15  PRO C CG  1 
ATOM   8247  C CD  . PRO C 1 15  ? 12.278  -11.186 60.418  1.00 54.64  ? 15  PRO C CD  1 
ATOM   8248  N N   . LEU C 1 16  ? 13.560  -15.544 61.009  1.00 58.18  ? 16  LEU C N   1 
ATOM   8249  C CA  . LEU C 1 16  ? 13.208  -16.895 60.585  1.00 54.18  ? 16  LEU C CA  1 
ATOM   8250  C C   . LEU C 1 16  ? 11.792  -17.169 61.057  1.00 54.80  ? 16  LEU C C   1 
ATOM   8251  O O   . LEU C 1 16  ? 11.565  -17.501 62.221  1.00 56.01  ? 16  LEU C O   1 
ATOM   8252  C CB  . LEU C 1 16  ? 14.194  -17.915 61.138  1.00 55.29  ? 16  LEU C CB  1 
ATOM   8253  C CG  . LEU C 1 16  ? 14.016  -19.318 60.541  1.00 53.79  ? 16  LEU C CG  1 
ATOM   8254  C CD1 . LEU C 1 16  ? 13.903  -19.225 59.037  1.00 57.75  ? 16  LEU C CD1 1 
ATOM   8255  C CD2 . LEU C 1 16  ? 15.122  -20.279 60.932  1.00 49.84  ? 16  LEU C CD2 1 
ATOM   8256  N N   . TYR C 1 17  ? 10.827  -16.986 60.153  1.00 59.87  ? 17  TYR C N   1 
ATOM   8257  C CA  . TYR C 1 17  ? 9.418   -17.183 60.466  1.00 56.95  ? 17  TYR C CA  1 
ATOM   8258  C C   . TYR C 1 17  ? 8.986   -18.643 60.410  1.00 60.12  ? 17  TYR C C   1 
ATOM   8259  O O   . TYR C 1 17  ? 7.813   -18.926 60.669  1.00 58.91  ? 17  TYR C O   1 
ATOM   8260  C CB  . TYR C 1 17  ? 8.552   -16.371 59.507  1.00 50.69  ? 17  TYR C CB  1 
ATOM   8261  C CG  . TYR C 1 17  ? 8.693   -14.877 59.638  1.00 53.16  ? 17  TYR C CG  1 
ATOM   8262  C CD1 . TYR C 1 17  ? 8.358   -14.232 60.819  1.00 56.99  ? 17  TYR C CD1 1 
ATOM   8263  C CD2 . TYR C 1 17  ? 9.109   -14.103 58.564  1.00 54.38  ? 17  TYR C CD2 1 
ATOM   8264  C CE1 . TYR C 1 17  ? 8.463   -12.866 60.938  1.00 60.18  ? 17  TYR C CE1 1 
ATOM   8265  C CE2 . TYR C 1 17  ? 9.212   -12.736 58.670  1.00 55.61  ? 17  TYR C CE2 1 
ATOM   8266  C CZ  . TYR C 1 17  ? 8.888   -12.120 59.861  1.00 58.60  ? 17  TYR C CZ  1 
ATOM   8267  O OH  . TYR C 1 17  ? 8.988   -10.754 59.981  1.00 58.90  ? 17  TYR C OH  1 
ATOM   8268  N N   . ARG C 1 18  ? 9.888   -19.566 60.076  1.00 60.24  ? 18  ARG C N   1 
ATOM   8269  C CA  . ARG C 1 18  ? 9.548   -20.976 59.897  1.00 58.69  ? 18  ARG C CA  1 
ATOM   8270  C C   . ARG C 1 18  ? 9.706   -21.708 61.227  1.00 65.48  ? 18  ARG C C   1 
ATOM   8271  O O   . ARG C 1 18  ? 10.826  -21.855 61.731  1.00 60.95  ? 18  ARG C O   1 
ATOM   8272  C CB  . ARG C 1 18  ? 10.434  -21.595 58.817  1.00 56.74  ? 18  ARG C CB  1 
ATOM   8273  C CG  . ARG C 1 18  ? 10.178  -23.065 58.512  1.00 65.42  ? 18  ARG C CG  1 
ATOM   8274  C CD  . ARG C 1 18  ? 11.454  -23.723 57.994  1.00 66.00  ? 18  ARG C CD  1 
ATOM   8275  N NE  . ARG C 1 18  ? 11.292  -25.133 57.653  1.00 64.75  ? 18  ARG C NE  1 
ATOM   8276  C CZ  . ARG C 1 18  ? 11.335  -26.131 58.527  1.00 68.37  ? 18  ARG C CZ  1 
ATOM   8277  N NH1 . ARG C 1 18  ? 11.480  -25.911 59.823  1.00 71.38  ? 18  ARG C NH1 1 
ATOM   8278  N NH2 . ARG C 1 18  ? 11.230  -27.383 58.088  1.00 68.47  ? 18  ARG C NH2 1 
ATOM   8279  N N   . GLU C 1 19  ? 8.591   -22.175 61.788  1.00 67.59  ? 19  GLU C N   1 
ATOM   8280  C CA  . GLU C 1 19  ? 8.636   -22.936 63.031  1.00 67.69  ? 19  GLU C CA  1 
ATOM   8281  C C   . GLU C 1 19  ? 9.487   -24.192 62.839  1.00 69.69  ? 19  GLU C C   1 
ATOM   8282  O O   . GLU C 1 19  ? 9.406   -24.840 61.789  1.00 73.39  ? 19  GLU C O   1 
ATOM   8283  C CB  . GLU C 1 19  ? 7.215   -23.309 63.474  1.00 68.33  ? 19  GLU C CB  1 
ATOM   8284  C CG  . GLU C 1 19  ? 7.027   -23.466 64.985  1.00 63.55  ? 19  GLU C CG  1 
ATOM   8285  C CD  . GLU C 1 19  ? 7.242   -24.893 65.443  1.00 74.51  ? 19  GLU C CD  1 
ATOM   8286  O OE1 . GLU C 1 19  ? 7.485   -25.750 64.568  1.00 79.97  ? 19  GLU C OE1 1 
ATOM   8287  O OE2 . GLU C 1 19  ? 7.189   -25.159 66.665  1.00 75.74  ? 19  GLU C OE2 1 
ATOM   8288  N N   . PRO C 1 20  ? 10.329  -24.560 63.820  1.00 68.40  ? 20  PRO C N   1 
ATOM   8289  C CA  . PRO C 1 20  ? 11.216  -25.721 63.633  1.00 65.68  ? 20  PRO C CA  1 
ATOM   8290  C C   . PRO C 1 20  ? 10.509  -27.073 63.606  1.00 70.53  ? 20  PRO C C   1 
ATOM   8291  O O   . PRO C 1 20  ? 10.826  -27.912 62.758  1.00 74.54  ? 20  PRO C O   1 
ATOM   8292  C CB  . PRO C 1 20  ? 12.172  -25.618 64.828  1.00 72.41  ? 20  PRO C CB  1 
ATOM   8293  C CG  . PRO C 1 20  ? 11.407  -24.861 65.860  1.00 69.56  ? 20  PRO C CG  1 
ATOM   8294  C CD  . PRO C 1 20  ? 10.591  -23.864 65.092  1.00 63.58  ? 20  PRO C CD  1 
ATOM   8295  N N   . TYR C 1 21  ? 9.564   -27.304 64.519  1.00 75.55  ? 21  TYR C N   1 
ATOM   8296  C CA  . TYR C 1 21  ? 8.900   -28.605 64.598  1.00 73.24  ? 21  TYR C CA  1 
ATOM   8297  C C   . TYR C 1 21  ? 7.883   -28.785 63.471  1.00 70.97  ? 21  TYR C C   1 
ATOM   8298  O O   . TYR C 1 21  ? 8.015   -29.691 62.638  1.00 72.40  ? 21  TYR C O   1 
ATOM   8299  C CB  . TYR C 1 21  ? 8.232   -28.768 65.965  1.00 71.03  ? 21  TYR C CB  1 
ATOM   8300  C CG  . TYR C 1 21  ? 9.209   -28.836 67.120  1.00 77.07  ? 21  TYR C CG  1 
ATOM   8301  C CD1 . TYR C 1 21  ? 10.186  -29.821 67.172  1.00 81.89  ? 21  TYR C CD1 1 
ATOM   8302  C CD2 . TYR C 1 21  ? 9.160   -27.910 68.154  1.00 80.01  ? 21  TYR C CD2 1 
ATOM   8303  C CE1 . TYR C 1 21  ? 11.080  -29.887 68.225  1.00 73.95  ? 21  TYR C CE1 1 
ATOM   8304  C CE2 . TYR C 1 21  ? 10.049  -27.966 69.207  1.00 74.70  ? 21  TYR C CE2 1 
ATOM   8305  C CZ  . TYR C 1 21  ? 11.004  -28.953 69.239  1.00 73.35  ? 21  TYR C CZ  1 
ATOM   8306  O OH  . TYR C 1 21  ? 11.881  -28.997 70.293  1.00 72.59  ? 21  TYR C OH  1 
ATOM   8307  N N   . THR C 1 22  ? 6.857   -27.924 63.427  1.00 75.13  ? 22  THR C N   1 
ATOM   8308  C CA  . THR C 1 22  ? 5.805   -28.059 62.415  1.00 74.96  ? 22  THR C CA  1 
ATOM   8309  C C   . THR C 1 22  ? 6.344   -27.810 61.008  1.00 70.78  ? 22  THR C C   1 
ATOM   8310  O O   . THR C 1 22  ? 5.961   -28.503 60.059  1.00 67.73  ? 22  THR C O   1 
ATOM   8311  C CB  . THR C 1 22  ? 4.632   -27.110 62.716  1.00 70.97  ? 22  THR C CB  1 
ATOM   8312  O OG1 . THR C 1 22  ? 4.908   -25.797 62.210  1.00 73.75  ? 22  THR C OG1 1 
ATOM   8313  C CG2 . THR C 1 22  ? 4.372   -27.020 64.212  1.00 67.49  ? 22  THR C CG2 1 
ATOM   8314  N N   . GLY C 1 23  ? 7.241   -26.841 60.851  1.00 72.02  ? 23  GLY C N   1 
ATOM   8315  C CA  . GLY C 1 23  ? 7.720   -26.461 59.543  1.00 73.17  ? 23  GLY C CA  1 
ATOM   8316  C C   . GLY C 1 23  ? 6.936   -25.349 58.878  1.00 71.99  ? 23  GLY C C   1 
ATOM   8317  O O   . GLY C 1 23  ? 7.364   -24.853 57.828  1.00 73.11  ? 23  GLY C O   1 
ATOM   8318  N N   . GLU C 1 24  ? 5.814   -24.935 59.456  1.00 71.21  ? 24  GLU C N   1 
ATOM   8319  C CA  . GLU C 1 24  ? 5.007   -23.884 58.853  1.00 70.56  ? 24  GLU C CA  1 
ATOM   8320  C C   . GLU C 1 24  ? 5.674   -22.521 59.017  1.00 71.70  ? 24  GLU C C   1 
ATOM   8321  O O   . GLU C 1 24  ? 6.463   -22.294 59.938  1.00 69.27  ? 24  GLU C O   1 
ATOM   8322  C CB  . GLU C 1 24  ? 3.609   -23.863 59.479  1.00 70.30  ? 24  GLU C CB  1 
ATOM   8323  C CG  . GLU C 1 24  ? 2.949   -25.236 59.569  1.00 83.88  ? 24  GLU C CG  1 
ATOM   8324  C CD  . GLU C 1 24  ? 1.738   -25.269 60.496  1.00 94.00  ? 24  GLU C CD  1 
ATOM   8325  O OE1 . GLU C 1 24  ? 1.683   -24.459 61.449  1.00 90.33  ? 24  GLU C OE1 1 
ATOM   8326  O OE2 . GLU C 1 24  ? 0.847   -26.120 60.280  1.00 95.80  ? 24  GLU C OE2 1 
ATOM   8327  N N   . TYR C 1 25  ? 5.349   -21.611 58.097  1.00 72.25  ? 25  TYR C N   1 
ATOM   8328  C CA  . TYR C 1 25  ? 5.721   -20.201 58.186  1.00 64.44  ? 25  TYR C CA  1 
ATOM   8329  C C   . TYR C 1 25  ? 4.551   -19.466 58.833  1.00 69.65  ? 25  TYR C C   1 
ATOM   8330  O O   . TYR C 1 25  ? 3.540   -19.185 58.180  1.00 61.03  ? 25  TYR C O   1 
ATOM   8331  C CB  . TYR C 1 25  ? 6.035   -19.635 56.807  1.00 62.73  ? 25  TYR C CB  1 
ATOM   8332  C CG  . TYR C 1 25  ? 7.425   -19.933 56.315  1.00 63.28  ? 25  TYR C CG  1 
ATOM   8333  C CD1 . TYR C 1 25  ? 7.774   -21.208 55.895  1.00 69.14  ? 25  TYR C CD1 1 
ATOM   8334  C CD2 . TYR C 1 25  ? 8.388   -18.935 56.255  1.00 66.22  ? 25  TYR C CD2 1 
ATOM   8335  C CE1 . TYR C 1 25  ? 9.049   -21.484 55.438  1.00 69.87  ? 25  TYR C CE1 1 
ATOM   8336  C CE2 . TYR C 1 25  ? 9.660   -19.199 55.799  1.00 62.38  ? 25  TYR C CE2 1 
ATOM   8337  C CZ  . TYR C 1 25  ? 9.987   -20.473 55.392  1.00 70.90  ? 25  TYR C CZ  1 
ATOM   8338  O OH  . TYR C 1 25  ? 11.260  -20.728 54.939  1.00 79.32  ? 25  TYR C OH  1 
ATOM   8339  N N   . LEU C 1 26  ? 4.694   -19.150 60.124  1.00 64.25  ? 26  LEU C N   1 
ATOM   8340  C CA  . LEU C 1 26  ? 3.603   -18.546 60.882  1.00 63.67  ? 26  LEU C CA  1 
ATOM   8341  C C   . LEU C 1 26  ? 3.353   -17.087 60.525  1.00 60.79  ? 26  LEU C C   1 
ATOM   8342  O O   . LEU C 1 26  ? 2.342   -16.531 60.967  1.00 63.23  ? 26  LEU C O   1 
ATOM   8343  C CB  . LEU C 1 26  ? 3.874   -18.662 62.382  1.00 58.54  ? 26  LEU C CB  1 
ATOM   8344  C CG  . LEU C 1 26  ? 4.484   -19.976 62.855  1.00 56.72  ? 26  LEU C CG  1 
ATOM   8345  C CD1 . LEU C 1 26  ? 4.729   -19.928 64.357  1.00 57.22  ? 26  LEU C CD1 1 
ATOM   8346  C CD2 . LEU C 1 26  ? 3.578   -21.138 62.476  1.00 57.82  ? 26  LEU C CD2 1 
ATOM   8347  N N   . LEU C 1 27  ? 4.234   -16.456 59.752  1.00 57.42  ? 27  LEU C N   1 
ATOM   8348  C CA  . LEU C 1 27  ? 4.007   -15.097 59.292  1.00 53.93  ? 27  LEU C CA  1 
ATOM   8349  C C   . LEU C 1 27  ? 4.380   -14.996 57.820  1.00 58.21  ? 27  LEU C C   1 
ATOM   8350  O O   . LEU C 1 27  ? 5.332   -15.652 57.375  1.00 66.38  ? 27  LEU C O   1 
ATOM   8351  C CB  . LEU C 1 27  ? 4.822   -14.093 60.108  1.00 53.28  ? 27  LEU C CB  1 
ATOM   8352  C CG  . LEU C 1 27  ? 4.209   -13.738 61.463  1.00 60.37  ? 27  LEU C CG  1 
ATOM   8353  C CD1 . LEU C 1 27  ? 5.019   -12.633 62.101  1.00 61.67  ? 27  LEU C CD1 1 
ATOM   8354  C CD2 . LEU C 1 27  ? 2.739   -13.334 61.347  1.00 56.41  ? 27  LEU C CD2 1 
ATOM   8355  N N   . PRO C 1 28  ? 3.652   -14.195 57.041  1.00 61.73  ? 28  PRO C N   1 
ATOM   8356  C CA  . PRO C 1 28  ? 3.913   -14.107 55.592  1.00 60.74  ? 28  PRO C CA  1 
ATOM   8357  C C   . PRO C 1 28  ? 4.818   -12.957 55.158  1.00 59.54  ? 28  PRO C C   1 
ATOM   8358  O O   . PRO C 1 28  ? 4.897   -12.698 53.954  1.00 59.37  ? 28  PRO C O   1 
ATOM   8359  C CB  . PRO C 1 28  ? 2.501   -13.909 55.035  1.00 60.04  ? 28  PRO C CB  1 
ATOM   8360  C CG  . PRO C 1 28  ? 1.844   -13.036 56.078  1.00 64.71  ? 28  PRO C CG  1 
ATOM   8361  C CD  . PRO C 1 28  ? 2.438   -13.441 57.421  1.00 63.02  ? 28  PRO C CD  1 
ATOM   8362  N N   . TRP C 1 29  ? 5.505   -12.293 56.093  1.00 60.61  ? 29  TRP C N   1 
ATOM   8363  C CA  . TRP C 1 29  ? 6.202   -11.049 55.768  1.00 62.14  ? 29  TRP C CA  1 
ATOM   8364  C C   . TRP C 1 29  ? 7.312   -11.261 54.750  1.00 58.53  ? 29  TRP C C   1 
ATOM   8365  O O   . TRP C 1 29  ? 7.603   -10.361 53.953  1.00 52.43  ? 29  TRP C O   1 
ATOM   8366  C CB  . TRP C 1 29  ? 6.763   -10.418 57.043  1.00 60.55  ? 29  TRP C CB  1 
ATOM   8367  C CG  . TRP C 1 29  ? 5.711   -9.985  58.022  1.00 61.94  ? 29  TRP C CG  1 
ATOM   8368  C CD1 . TRP C 1 29  ? 5.634   -10.323 59.343  1.00 69.42  ? 29  TRP C CD1 1 
ATOM   8369  C CD2 . TRP C 1 29  ? 4.591   -9.127  57.764  1.00 64.81  ? 29  TRP C CD2 1 
ATOM   8370  N NE1 . TRP C 1 29  ? 4.536   -9.733  59.925  1.00 64.21  ? 29  TRP C NE1 1 
ATOM   8371  C CE2 . TRP C 1 29  ? 3.880   -8.992  58.977  1.00 70.99  ? 29  TRP C CE2 1 
ATOM   8372  C CE3 . TRP C 1 29  ? 4.122   -8.455  56.630  1.00 64.52  ? 29  TRP C CE3 1 
ATOM   8373  C CZ2 . TRP C 1 29  ? 2.725   -8.216  59.083  1.00 69.27  ? 29  TRP C CZ2 1 
ATOM   8374  C CZ3 . TRP C 1 29  ? 2.975   -7.688  56.739  1.00 64.52  ? 29  TRP C CZ3 1 
ATOM   8375  C CH2 . TRP C 1 29  ? 2.291   -7.575  57.955  1.00 64.66  ? 29  TRP C CH2 1 
ATOM   8376  N N   . THR C 1 30  ? 7.947   -12.433 54.769  1.00 61.77  ? 30  THR C N   1 
ATOM   8377  C CA  . THR C 1 30  ? 8.970   -12.734 53.777  1.00 53.30  ? 30  THR C CA  1 
ATOM   8378  C C   . THR C 1 30  ? 8.379   -12.758 52.373  1.00 57.74  ? 30  THR C C   1 
ATOM   8379  O O   . THR C 1 30  ? 8.957   -12.186 51.443  1.00 62.16  ? 30  THR C O   1 
ATOM   8380  C CB  . THR C 1 30  ? 9.640   -14.068 54.101  1.00 59.58  ? 30  THR C CB  1 
ATOM   8381  O OG1 . THR C 1 30  ? 10.043  -14.080 55.479  1.00 58.97  ? 30  THR C OG1 1 
ATOM   8382  C CG2 . THR C 1 30  ? 10.866  -14.267 53.215  1.00 59.24  ? 30  THR C CG2 1 
ATOM   8383  N N   . PHE C 1 31  ? 7.217   -13.397 52.203  1.00 54.68  ? 31  PHE C N   1 
ATOM   8384  C CA  . PHE C 1 31  ? 6.598   -13.455 50.881  1.00 54.38  ? 31  PHE C CA  1 
ATOM   8385  C C   . PHE C 1 31  ? 6.207   -12.060 50.399  1.00 57.54  ? 31  PHE C C   1 
ATOM   8386  O O   . PHE C 1 31  ? 6.560   -11.659 49.284  1.00 55.82  ? 31  PHE C O   1 
ATOM   8387  C CB  . PHE C 1 31  ? 5.391   -14.405 50.899  1.00 54.41  ? 31  PHE C CB  1 
ATOM   8388  C CG  . PHE C 1 31  ? 4.440   -14.222 49.743  1.00 62.06  ? 31  PHE C CG  1 
ATOM   8389  C CD1 . PHE C 1 31  ? 3.500   -13.192 49.735  1.00 62.49  ? 31  PHE C CD1 1 
ATOM   8390  C CD2 . PHE C 1 31  ? 4.457   -15.127 48.677  1.00 62.16  ? 31  PHE C CD2 1 
ATOM   8391  C CE1 . PHE C 1 31  ? 2.620   -13.047 48.677  1.00 64.15  ? 31  PHE C CE1 1 
ATOM   8392  C CE2 . PHE C 1 31  ? 3.593   -14.995 47.608  1.00 58.19  ? 31  PHE C CE2 1 
ATOM   8393  C CZ  . PHE C 1 31  ? 2.663   -13.946 47.605  1.00 57.87  ? 31  PHE C CZ  1 
ATOM   8394  N N   . PHE C 1 32  ? 5.501   -11.293 51.239  1.00 56.02  ? 32  PHE C N   1 
ATOM   8395  C CA  . PHE C 1 32  ? 4.943   -10.007 50.814  1.00 52.92  ? 32  PHE C CA  1 
ATOM   8396  C C   . PHE C 1 32  ? 6.033   -8.985  50.520  1.00 57.36  ? 32  PHE C C   1 
ATOM   8397  O O   . PHE C 1 32  ? 5.976   -8.285  49.502  1.00 60.37  ? 32  PHE C O   1 
ATOM   8398  C CB  . PHE C 1 32  ? 3.984   -9.482  51.885  1.00 65.63  ? 32  PHE C CB  1 
ATOM   8399  C CG  . PHE C 1 32  ? 2.660   -10.201 51.915  1.00 62.18  ? 32  PHE C CG  1 
ATOM   8400  C CD1 . PHE C 1 32  ? 1.974   -10.459 50.742  1.00 51.88  ? 32  PHE C CD1 1 
ATOM   8401  C CD2 . PHE C 1 32  ? 2.139   -10.675 53.116  1.00 62.36  ? 32  PHE C CD2 1 
ATOM   8402  C CE1 . PHE C 1 32  ? 0.768   -11.135 50.763  1.00 59.08  ? 32  PHE C CE1 1 
ATOM   8403  C CE2 . PHE C 1 32  ? 0.937   -11.358 53.148  1.00 66.47  ? 32  PHE C CE2 1 
ATOM   8404  C CZ  . PHE C 1 32  ? 0.245   -11.590 51.970  1.00 65.19  ? 32  PHE C CZ  1 
ATOM   8405  N N   . HIS C 1 33  ? 7.032   -8.873  51.398  1.00 57.41  ? 33  HIS C N   1 
ATOM   8406  C CA  . HIS C 1 33  ? 8.107   -7.923  51.149  1.00 52.55  ? 33  HIS C CA  1 
ATOM   8407  C C   . HIS C 1 33  ? 8.999   -8.370  49.999  1.00 61.02  ? 33  HIS C C   1 
ATOM   8408  O O   . HIS C 1 33  ? 9.658   -7.529  49.378  1.00 63.59  ? 33  HIS C O   1 
ATOM   8409  C CB  . HIS C 1 33  ? 8.932   -7.711  52.415  1.00 57.87  ? 33  HIS C CB  1 
ATOM   8410  C CG  . HIS C 1 33  ? 8.381   -6.653  53.319  1.00 58.53  ? 33  HIS C CG  1 
ATOM   8411  N ND1 . HIS C 1 33  ? 8.186   -5.352  52.907  1.00 60.04  ? 33  HIS C ND1 1 
ATOM   8412  C CD2 . HIS C 1 33  ? 8.008   -6.696  54.620  1.00 54.49  ? 33  HIS C CD2 1 
ATOM   8413  C CE1 . HIS C 1 33  ? 7.702   -4.642  53.911  1.00 62.00  ? 33  HIS C CE1 1 
ATOM   8414  N NE2 . HIS C 1 33  ? 7.587   -5.433  54.962  1.00 59.09  ? 33  HIS C NE2 1 
ATOM   8415  N N   . ALA C 1 34  ? 9.022   -9.669  49.688  1.00 58.09  ? 34  ALA C N   1 
ATOM   8416  C CA  . ALA C 1 34  ? 9.744   -10.123 48.503  1.00 59.51  ? 34  ALA C CA  1 
ATOM   8417  C C   . ALA C 1 34  ? 9.039   -9.694  47.223  1.00 65.23  ? 34  ALA C C   1 
ATOM   8418  O O   . ALA C 1 34  ? 9.686   -9.215  46.283  1.00 67.55  ? 34  ALA C O   1 
ATOM   8419  C CB  . ALA C 1 34  ? 9.921   -11.640 48.530  1.00 62.85  ? 34  ALA C CB  1 
ATOM   8420  N N   . VAL C 1 35  ? 7.712   -9.854  47.166  1.00 60.55  ? 35  VAL C N   1 
ATOM   8421  C CA  . VAL C 1 35  ? 6.988   -9.477  45.956  1.00 58.34  ? 35  VAL C CA  1 
ATOM   8422  C C   . VAL C 1 35  ? 6.916   -7.962  45.815  1.00 64.26  ? 35  VAL C C   1 
ATOM   8423  O O   . VAL C 1 35  ? 6.771   -7.444  44.702  1.00 70.81  ? 35  VAL C O   1 
ATOM   8424  C CB  . VAL C 1 35  ? 5.581   -10.105 45.938  1.00 63.55  ? 35  VAL C CB  1 
ATOM   8425  C CG1 . VAL C 1 35  ? 5.658   -11.608 46.168  1.00 57.07  ? 35  VAL C CG1 1 
ATOM   8426  C CG2 . VAL C 1 35  ? 4.677   -9.432  46.956  1.00 64.70  ? 35  VAL C CG2 1 
ATOM   8427  N N   . LYS C 1 36  ? 7.029   -7.224  46.920  1.00 62.13  ? 36  LYS C N   1 
ATOM   8428  C CA  . LYS C 1 36  ? 6.891   -5.775  46.861  1.00 61.03  ? 36  LYS C CA  1 
ATOM   8429  C C   . LYS C 1 36  ? 8.227   -5.057  46.685  1.00 67.25  ? 36  LYS C C   1 
ATOM   8430  O O   . LYS C 1 36  ? 8.306   -4.081  45.931  1.00 68.06  ? 36  LYS C O   1 
ATOM   8431  C CB  . LYS C 1 36  ? 6.201   -5.269  48.126  1.00 59.07  ? 36  LYS C CB  1 
ATOM   8432  C CG  . LYS C 1 36  ? 5.544   -3.912  47.992  1.00 62.19  ? 36  LYS C CG  1 
ATOM   8433  C CD  . LYS C 1 36  ? 4.732   -3.595  49.245  1.00 63.30  ? 36  LYS C CD  1 
ATOM   8434  C CE  . LYS C 1 36  ? 5.603   -3.535  50.511  1.00 69.80  ? 36  LYS C CE  1 
ATOM   8435  N NZ  . LYS C 1 36  ? 6.347   -2.257  50.739  1.00 54.17  ? 36  LYS C NZ  1 
ATOM   8436  N N   . ASP C 1 37  ? 9.289   -5.506  47.358  1.00 67.11  ? 37  ASP C N   1 
ATOM   8437  C CA  . ASP C 1 37  ? 10.497  -4.689  47.422  1.00 65.54  ? 37  ASP C CA  1 
ATOM   8438  C C   . ASP C 1 37  ? 11.790  -5.442  47.117  1.00 64.09  ? 37  ASP C C   1 
ATOM   8439  O O   . ASP C 1 37  ? 12.725  -4.856  46.564  1.00 65.89  ? 37  ASP C O   1 
ATOM   8440  C CB  . ASP C 1 37  ? 10.626  -4.025  48.801  1.00 64.92  ? 37  ASP C CB  1 
ATOM   8441  C CG  . ASP C 1 37  ? 9.304   -3.484  49.326  1.00 66.35  ? 37  ASP C CG  1 
ATOM   8442  O OD1 . ASP C 1 37  ? 8.942   -2.343  48.965  1.00 65.67  ? 37  ASP C OD1 1 
ATOM   8443  O OD2 . ASP C 1 37  ? 8.649   -4.182  50.131  1.00 61.50  ? 37  ASP C OD2 1 
ATOM   8444  N N   . TYR C 1 38  ? 11.871  -6.728  47.466  1.00 59.86  ? 38  TYR C N   1 
ATOM   8445  C CA  . TYR C 1 38  ? 13.157  -7.419  47.373  1.00 58.98  ? 38  TYR C CA  1 
ATOM   8446  C C   . TYR C 1 38  ? 13.625  -7.567  45.928  1.00 56.55  ? 38  TYR C C   1 
ATOM   8447  O O   . TYR C 1 38  ? 14.827  -7.487  45.653  1.00 54.55  ? 38  TYR C O   1 
ATOM   8448  C CB  . TYR C 1 38  ? 13.086  -8.779  48.067  1.00 59.41  ? 38  TYR C CB  1 
ATOM   8449  C CG  . TYR C 1 38  ? 12.999  -8.657  49.573  1.00 55.93  ? 38  TYR C CG  1 
ATOM   8450  C CD1 . TYR C 1 38  ? 13.489  -7.530  50.222  1.00 47.95  ? 38  TYR C CD1 1 
ATOM   8451  C CD2 . TYR C 1 38  ? 12.431  -9.667  50.346  1.00 54.73  ? 38  TYR C CD2 1 
ATOM   8452  C CE1 . TYR C 1 38  ? 13.406  -7.405  51.594  1.00 56.99  ? 38  TYR C CE1 1 
ATOM   8453  C CE2 . TYR C 1 38  ? 12.337  -9.550  51.716  1.00 53.76  ? 38  TYR C CE2 1 
ATOM   8454  C CZ  . TYR C 1 38  ? 12.830  -8.419  52.340  1.00 62.84  ? 38  TYR C CZ  1 
ATOM   8455  O OH  . TYR C 1 38  ? 12.751  -8.295  53.714  1.00 62.34  ? 38  TYR C OH  1 
ATOM   8456  N N   . TYR C 1 39  ? 12.703  -7.765  44.988  1.00 58.39  ? 39  TYR C N   1 
ATOM   8457  C CA  . TYR C 1 39  ? 13.126  -7.785  43.593  1.00 51.78  ? 39  TYR C CA  1 
ATOM   8458  C C   . TYR C 1 39  ? 13.154  -6.385  42.996  1.00 51.95  ? 39  TYR C C   1 
ATOM   8459  O O   . TYR C 1 39  ? 14.062  -6.054  42.227  1.00 52.41  ? 39  TYR C O   1 
ATOM   8460  C CB  . TYR C 1 39  ? 12.209  -8.686  42.773  1.00 55.93  ? 39  TYR C CB  1 
ATOM   8461  C CG  . TYR C 1 39  ? 12.449  -8.652  41.278  1.00 55.98  ? 39  TYR C CG  1 
ATOM   8462  C CD1 . TYR C 1 39  ? 11.806  -7.716  40.477  1.00 57.14  ? 39  TYR C CD1 1 
ATOM   8463  C CD2 . TYR C 1 39  ? 13.274  -9.582  40.662  1.00 62.05  ? 39  TYR C CD2 1 
ATOM   8464  C CE1 . TYR C 1 39  ? 12.001  -7.684  39.119  1.00 61.71  ? 39  TYR C CE1 1 
ATOM   8465  C CE2 . TYR C 1 39  ? 13.472  -9.562  39.293  1.00 60.78  ? 39  TYR C CE2 1 
ATOM   8466  C CZ  . TYR C 1 39  ? 12.831  -8.608  38.527  1.00 63.60  ? 39  TYR C CZ  1 
ATOM   8467  O OH  . TYR C 1 39  ? 13.014  -8.570  37.163  1.00 64.60  ? 39  TYR C OH  1 
ATOM   8468  N N   . ASP C 1 40  ? 12.179  -5.549  43.345  1.00 57.77  ? 40  ASP C N   1 
ATOM   8469  C CA  . ASP C 1 40  ? 11.991  -4.301  42.613  1.00 62.36  ? 40  ASP C CA  1 
ATOM   8470  C C   . ASP C 1 40  ? 13.008  -3.242  43.013  1.00 60.49  ? 40  ASP C C   1 
ATOM   8471  O O   . ASP C 1 40  ? 13.444  -2.454  42.166  1.00 57.39  ? 40  ASP C O   1 
ATOM   8472  C CB  . ASP C 1 40  ? 10.574  -3.775  42.823  1.00 66.93  ? 40  ASP C CB  1 
ATOM   8473  C CG  . ASP C 1 40  ? 9.521   -4.803  42.495  1.00 72.94  ? 40  ASP C CG  1 
ATOM   8474  O OD1 . ASP C 1 40  ? 9.529   -5.895  43.107  1.00 74.49  ? 40  ASP C OD1 1 
ATOM   8475  O OD2 . ASP C 1 40  ? 8.672   -4.507  41.631  1.00 77.37  ? 40  ASP C OD2 1 
ATOM   8476  N N   . MET C 1 41  ? 13.393  -3.206  44.289  1.00 58.29  ? 41  MET C N   1 
ATOM   8477  C CA  . MET C 1 41  ? 14.357  -2.204  44.743  1.00 62.39  ? 41  MET C CA  1 
ATOM   8478  C C   . MET C 1 41  ? 15.681  -2.279  43.989  1.00 63.97  ? 41  MET C C   1 
ATOM   8479  O O   . MET C 1 41  ? 16.182  -1.222  43.562  1.00 62.30  ? 41  MET C O   1 
ATOM   8480  C CB  . MET C 1 41  ? 14.553  -2.327  46.257  1.00 49.61  ? 41  MET C CB  1 
ATOM   8481  C CG  . MET C 1 41  ? 13.502  -1.583  47.044  1.00 51.40  ? 41  MET C CG  1 
ATOM   8482  S SD  . MET C 1 41  ? 13.533  0.175   46.675  1.00 70.45  ? 41  MET C SD  1 
ATOM   8483  C CE  . MET C 1 41  ? 15.059  0.670   47.472  1.00 61.32  ? 41  MET C CE  1 
ATOM   8484  N N   . PRO C 1 42  ? 16.300  -3.449  43.785  1.00 61.69  ? 42  PRO C N   1 
ATOM   8485  C CA  . PRO C 1 42  ? 17.461  -3.495  42.884  1.00 57.85  ? 42  PRO C CA  1 
ATOM   8486  C C   . PRO C 1 42  ? 17.088  -3.398  41.415  1.00 58.77  ? 42  PRO C C   1 
ATOM   8487  O O   . PRO C 1 42  ? 17.946  -3.041  40.601  1.00 60.28  ? 42  PRO C O   1 
ATOM   8488  C CB  . PRO C 1 42  ? 18.108  -4.846  43.213  1.00 54.85  ? 42  PRO C CB  1 
ATOM   8489  C CG  . PRO C 1 42  ? 16.990  -5.677  43.712  1.00 52.45  ? 42  PRO C CG  1 
ATOM   8490  C CD  . PRO C 1 42  ? 16.105  -4.738  44.477  1.00 58.64  ? 42  PRO C CD  1 
ATOM   8491  N N   . ALA C 1 43  ? 15.837  -3.682  41.050  1.00 57.62  ? 43  ALA C N   1 
ATOM   8492  C CA  . ALA C 1 43  ? 15.442  -3.592  39.650  1.00 61.49  ? 43  ALA C CA  1 
ATOM   8493  C C   . ALA C 1 43  ? 15.437  -2.157  39.135  1.00 71.45  ? 43  ALA C C   1 
ATOM   8494  O O   . ALA C 1 43  ? 15.491  -1.951  37.916  1.00 67.49  ? 43  ALA C O   1 
ATOM   8495  C CB  . ALA C 1 43  ? 14.064  -4.221  39.444  1.00 57.77  ? 43  ALA C CB  1 
ATOM   8496  N N   . TYR C 1 44  ? 15.371  -1.162  40.028  1.00 72.91  ? 44  TYR C N   1 
ATOM   8497  C CA  . TYR C 1 44  ? 15.474  0.225   39.584  1.00 69.24  ? 44  TYR C CA  1 
ATOM   8498  C C   . TYR C 1 44  ? 16.771  0.465   38.825  1.00 64.81  ? 44  TYR C C   1 
ATOM   8499  O O   . TYR C 1 44  ? 16.835  1.346   37.960  1.00 66.40  ? 44  TYR C O   1 
ATOM   8500  C CB  . TYR C 1 44  ? 15.400  1.177   40.775  1.00 67.64  ? 44  TYR C CB  1 
ATOM   8501  C CG  . TYR C 1 44  ? 14.019  1.466   41.316  1.00 60.96  ? 44  TYR C CG  1 
ATOM   8502  C CD1 . TYR C 1 44  ? 13.373  0.560   42.142  1.00 63.42  ? 44  TYR C CD1 1 
ATOM   8503  C CD2 . TYR C 1 44  ? 13.391  2.675   41.051  1.00 57.35  ? 44  TYR C CD2 1 
ATOM   8504  C CE1 . TYR C 1 44  ? 12.128  0.833   42.664  1.00 63.42  ? 44  TYR C CE1 1 
ATOM   8505  C CE2 . TYR C 1 44  ? 12.150  2.955   41.568  1.00 55.67  ? 44  TYR C CE2 1 
ATOM   8506  C CZ  . TYR C 1 44  ? 11.522  2.032   42.376  1.00 61.15  ? 44  TYR C CZ  1 
ATOM   8507  O OH  . TYR C 1 44  ? 10.280  2.305   42.900  1.00 66.91  ? 44  TYR C OH  1 
ATOM   8508  N N   . LEU C 1 45  ? 17.814  -0.314  39.138  1.00 61.90  ? 45  LEU C N   1 
ATOM   8509  C CA  . LEU C 1 45  ? 19.128  -0.118  38.532  1.00 65.25  ? 45  LEU C CA  1 
ATOM   8510  C C   . LEU C 1 45  ? 19.117  -0.376  37.027  1.00 70.47  ? 45  LEU C C   1 
ATOM   8511  O O   . LEU C 1 45  ? 19.953  0.172   36.297  1.00 71.38  ? 45  LEU C O   1 
ATOM   8512  C CB  . LEU C 1 45  ? 20.150  -1.022  39.219  1.00 59.60  ? 45  LEU C CB  1 
ATOM   8513  C CG  . LEU C 1 45  ? 20.784  -0.424  40.479  1.00 61.40  ? 45  LEU C CG  1 
ATOM   8514  C CD1 . LEU C 1 45  ? 21.697  -1.426  41.174  1.00 55.91  ? 45  LEU C CD1 1 
ATOM   8515  C CD2 . LEU C 1 45  ? 21.534  0.857   40.141  1.00 59.96  ? 45  LEU C CD2 1 
ATOM   8516  N N   . LYS C 1 46  ? 18.184  -1.195  36.541  1.00 66.02  ? 46  LYS C N   1 
ATOM   8517  C CA  . LYS C 1 46  ? 18.059  -1.402  35.106  1.00 68.55  ? 46  LYS C CA  1 
ATOM   8518  C C   . LYS C 1 46  ? 17.412  -0.222  34.395  1.00 69.73  ? 46  LYS C C   1 
ATOM   8519  O O   . LYS C 1 46  ? 17.635  -0.051  33.192  1.00 65.62  ? 46  LYS C O   1 
ATOM   8520  C CB  . LYS C 1 46  ? 17.254  -2.671  34.825  1.00 79.79  ? 46  LYS C CB  1 
ATOM   8521  C CG  . LYS C 1 46  ? 18.046  -3.744  34.099  1.00 90.65  ? 46  LYS C CG  1 
ATOM   8522  C CD  . LYS C 1 46  ? 17.869  -5.102  34.757  1.00 90.21  ? 46  LYS C CD  1 
ATOM   8523  C CE  . LYS C 1 46  ? 16.514  -5.721  34.449  1.00 93.75  ? 46  LYS C CE  1 
ATOM   8524  N NZ  . LYS C 1 46  ? 16.325  -7.019  35.162  1.00 82.97  ? 46  LYS C NZ  1 
ATOM   8525  N N   . ASP C 1 47  ? 16.626  0.591   35.108  1.00 76.34  ? 47  ASP C N   1 
ATOM   8526  C CA  . ASP C 1 47  ? 15.852  1.673   34.509  1.00 75.50  ? 47  ASP C CA  1 
ATOM   8527  C C   . ASP C 1 47  ? 16.403  3.062   34.818  1.00 76.39  ? 47  ASP C C   1 
ATOM   8528  O O   . ASP C 1 47  ? 15.891  4.048   34.275  1.00 82.03  ? 47  ASP C O   1 
ATOM   8529  C CB  . ASP C 1 47  ? 14.380  1.600   34.967  1.00 78.55  ? 47  ASP C CB  1 
ATOM   8530  C CG  . ASP C 1 47  ? 13.780  0.195   34.844  1.00 81.02  ? 47  ASP C CG  1 
ATOM   8531  O OD1 . ASP C 1 47  ? 14.436  -0.783  35.262  1.00 81.50  ? 47  ASP C OD1 1 
ATOM   8532  O OD2 . ASP C 1 47  ? 12.646  0.071   34.326  1.00 97.86  ? 47  ASP C OD2 1 
ATOM   8533  N N   . PHE C 1 48  ? 17.417  3.168   35.675  1.00 74.75  ? 48  PHE C N   1 
ATOM   8534  C CA  . PHE C 1 48  ? 18.060  4.435   35.988  1.00 75.26  ? 48  PHE C CA  1 
ATOM   8535  C C   . PHE C 1 48  ? 19.567  4.213   36.011  1.00 76.50  ? 48  PHE C C   1 
ATOM   8536  O O   . PHE C 1 48  ? 20.046  3.117   36.314  1.00 72.42  ? 48  PHE C O   1 
ATOM   8537  C CB  . PHE C 1 48  ? 17.578  5.013   37.337  1.00 70.06  ? 48  PHE C CB  1 
ATOM   8538  C CG  . PHE C 1 48  ? 16.090  5.247   37.405  1.00 66.69  ? 48  PHE C CG  1 
ATOM   8539  C CD1 . PHE C 1 48  ? 15.212  4.195   37.632  1.00 68.81  ? 48  PHE C CD1 1 
ATOM   8540  C CD2 . PHE C 1 48  ? 15.568  6.519   37.228  1.00 68.34  ? 48  PHE C CD2 1 
ATOM   8541  C CE1 . PHE C 1 48  ? 13.845  4.408   37.685  1.00 64.61  ? 48  PHE C CE1 1 
ATOM   8542  C CE2 . PHE C 1 48  ? 14.196  6.737   37.281  1.00 63.23  ? 48  PHE C CE2 1 
ATOM   8543  C CZ  . PHE C 1 48  ? 13.338  5.680   37.509  1.00 58.95  ? 48  PHE C CZ  1 
ATOM   8544  N N   . GLU C 1 49  ? 20.315  5.259   35.681  1.00 74.95  ? 49  GLU C N   1 
ATOM   8545  C CA  . GLU C 1 49  ? 21.768  5.143   35.560  1.00 72.30  ? 49  GLU C CA  1 
ATOM   8546  C C   . GLU C 1 49  ? 22.446  5.774   36.777  1.00 65.40  ? 49  GLU C C   1 
ATOM   8547  O O   . GLU C 1 49  ? 23.035  6.851   36.718  1.00 62.24  ? 49  GLU C O   1 
ATOM   8548  C CB  . GLU C 1 49  ? 22.237  5.776   34.256  1.00 69.70  ? 49  GLU C CB  1 
ATOM   8549  C CG  . GLU C 1 49  ? 21.836  4.998   33.007  1.00 75.34  ? 49  GLU C CG  1 
ATOM   8550  C CD  . GLU C 1 49  ? 22.624  3.711   32.834  1.00 74.25  ? 49  GLU C CD  1 
ATOM   8551  O OE1 . GLU C 1 49  ? 22.144  2.798   32.127  1.00 77.57  ? 49  GLU C OE1 1 
ATOM   8552  O OE2 . GLU C 1 49  ? 23.721  3.609   33.418  1.00 93.81  ? 49  GLU C OE2 1 
ATOM   8553  N N   . ILE C 1 50  ? 22.331  5.075   37.906  1.00 65.65  ? 50  ILE C N   1 
ATOM   8554  C CA  . ILE C 1 50  ? 22.976  5.442   39.162  1.00 56.38  ? 50  ILE C CA  1 
ATOM   8555  C C   . ILE C 1 50  ? 23.561  4.178   39.784  1.00 56.00  ? 50  ILE C C   1 
ATOM   8556  O O   . ILE C 1 50  ? 23.498  3.089   39.209  1.00 53.56  ? 50  ILE C O   1 
ATOM   8557  C CB  . ILE C 1 50  ? 22.004  6.129   40.146  1.00 54.71  ? 50  ILE C CB  1 
ATOM   8558  C CG1 . ILE C 1 50  ? 20.652  5.414   40.162  1.00 61.24  ? 50  ILE C CG1 1 
ATOM   8559  C CG2 . ILE C 1 50  ? 21.817  7.588   39.801  1.00 55.40  ? 50  ILE C CG2 1 
ATOM   8560  C CD1 . ILE C 1 50  ? 19.954  5.469   41.499  1.00 52.47  ? 50  ILE C CD1 1 
ATOM   8561  N N   . LYS C 1 51  ? 24.128  4.325   40.975  1.00 60.41  ? 51  LYS C N   1 
ATOM   8562  C CA  . LYS C 1 51  ? 24.655  3.199   41.732  1.00 50.88  ? 51  LYS C CA  1 
ATOM   8563  C C   . LYS C 1 51  ? 23.820  3.016   42.989  1.00 51.61  ? 51  LYS C C   1 
ATOM   8564  O O   . LYS C 1 51  ? 23.484  3.994   43.665  1.00 54.62  ? 51  LYS C O   1 
ATOM   8565  C CB  . LYS C 1 51  ? 26.126  3.420   42.078  1.00 51.00  ? 51  LYS C CB  1 
ATOM   8566  C CG  . LYS C 1 51  ? 26.993  3.652   40.857  1.00 61.33  ? 51  LYS C CG  1 
ATOM   8567  C CD  . LYS C 1 51  ? 26.976  2.461   39.912  1.00 57.99  ? 51  LYS C CD  1 
ATOM   8568  C CE  . LYS C 1 51  ? 28.300  2.340   39.176  1.00 56.41  ? 51  LYS C CE  1 
ATOM   8569  N NZ  . LYS C 1 51  ? 28.095  2.231   37.700  1.00 67.32  ? 51  LYS C NZ  1 
ATOM   8570  N N   . LEU C 1 52  ? 23.465  1.772   43.285  1.00 48.43  ? 52  LEU C N   1 
ATOM   8571  C CA  . LEU C 1 52  ? 22.761  1.451   44.517  1.00 50.31  ? 52  LEU C CA  1 
ATOM   8572  C C   . LEU C 1 52  ? 23.364  0.181   45.085  1.00 49.16  ? 52  LEU C C   1 
ATOM   8573  O O   . LEU C 1 52  ? 23.587  -0.780  44.343  1.00 53.21  ? 52  LEU C O   1 
ATOM   8574  C CB  . LEU C 1 52  ? 21.257  1.261   44.275  1.00 54.74  ? 52  LEU C CB  1 
ATOM   8575  C CG  . LEU C 1 52  ? 20.467  2.464   43.757  1.00 51.22  ? 52  LEU C CG  1 
ATOM   8576  C CD1 . LEU C 1 52  ? 19.075  2.055   43.278  1.00 48.38  ? 52  LEU C CD1 1 
ATOM   8577  C CD2 . LEU C 1 52  ? 20.375  3.529   44.832  1.00 47.65  ? 52  LEU C CD2 1 
ATOM   8578  N N   . ASN C 1 53  ? 23.609  0.167   46.390  1.00 45.21  ? 53  ASN C N   1 
ATOM   8579  C CA  . ASN C 1 53  ? 24.168  -0.993  47.067  1.00 45.96  ? 53  ASN C CA  1 
ATOM   8580  C C   . ASN C 1 53  ? 23.144  -1.612  48.010  1.00 48.97  ? 53  ASN C C   1 
ATOM   8581  O O   . ASN C 1 53  ? 22.247  -0.929  48.514  1.00 43.32  ? 53  ASN C O   1 
ATOM   8582  C CB  . ASN C 1 53  ? 25.424  -0.607  47.836  1.00 48.48  ? 53  ASN C CB  1 
ATOM   8583  C CG  . ASN C 1 53  ? 26.417  0.102   46.965  1.00 52.08  ? 53  ASN C CG  1 
ATOM   8584  O OD1 . ASN C 1 53  ? 27.204  -0.535  46.266  1.00 55.92  ? 53  ASN C OD1 1 
ATOM   8585  N ND2 . ASN C 1 53  ? 26.360  1.428   46.958  1.00 48.11  ? 53  ASN C ND2 1 
ATOM   8586  N N   . PHE C 1 54  ? 23.290  -2.914  48.257  1.00 48.58  ? 54  PHE C N   1 
ATOM   8587  C CA  . PHE C 1 54  ? 22.279  -3.664  48.988  1.00 45.40  ? 54  PHE C CA  1 
ATOM   8588  C C   . PHE C 1 54  ? 22.917  -4.607  49.997  1.00 48.19  ? 54  PHE C C   1 
ATOM   8589  O O   . PHE C 1 54  ? 24.025  -5.109  49.798  1.00 51.77  ? 54  PHE C O   1 
ATOM   8590  C CB  . PHE C 1 54  ? 21.392  -4.450  48.023  1.00 43.82  ? 54  PHE C CB  1 
ATOM   8591  C CG  . PHE C 1 54  ? 20.562  -3.571  47.136  1.00 55.26  ? 54  PHE C CG  1 
ATOM   8592  C CD1 . PHE C 1 54  ? 21.055  -3.132  45.916  1.00 44.74  ? 54  PHE C CD1 1 
ATOM   8593  C CD2 . PHE C 1 54  ? 19.299  -3.155  47.538  1.00 54.33  ? 54  PHE C CD2 1 
ATOM   8594  C CE1 . PHE C 1 54  ? 20.301  -2.308  45.107  1.00 49.78  ? 54  PHE C CE1 1 
ATOM   8595  C CE2 . PHE C 1 54  ? 18.538  -2.331  46.733  1.00 50.80  ? 54  PHE C CE2 1 
ATOM   8596  C CZ  . PHE C 1 54  ? 19.042  -1.906  45.513  1.00 61.09  ? 54  PHE C CZ  1 
ATOM   8597  N N   . ASN C 1 55  ? 22.194  -4.846  51.086  1.00 49.85  ? 55  ASN C N   1 
ATOM   8598  C CA  . ASN C 1 55  ? 22.595  -5.803  52.105  1.00 46.92  ? 55  ASN C CA  1 
ATOM   8599  C C   . ASN C 1 55  ? 21.508  -6.858  52.245  1.00 49.32  ? 55  ASN C C   1 
ATOM   8600  O O   . ASN C 1 55  ? 20.330  -6.521  52.420  1.00 46.86  ? 55  ASN C O   1 
ATOM   8601  C CB  . ASN C 1 55  ? 22.849  -5.110  53.443  1.00 44.21  ? 55  ASN C CB  1 
ATOM   8602  C CG  . ASN C 1 55  ? 23.322  -6.067  54.505  1.00 49.17  ? 55  ASN C CG  1 
ATOM   8603  O OD1 . ASN C 1 55  ? 24.506  -6.394  54.573  1.00 55.11  ? 55  ASN C OD1 1 
ATOM   8604  N ND2 . ASN C 1 55  ? 22.401  -6.526  55.346  1.00 43.58  ? 55  ASN C ND2 1 
ATOM   8605  N N   . LEU C 1 56  ? 21.905  -8.128  52.155  1.00 52.38  ? 56  LEU C N   1 
ATOM   8606  C CA  . LEU C 1 56  ? 20.992  -9.261  52.277  1.00 47.56  ? 56  LEU C CA  1 
ATOM   8607  C C   . LEU C 1 56  ? 21.426  -10.121 53.456  1.00 53.36  ? 56  LEU C C   1 
ATOM   8608  O O   . LEU C 1 56  ? 22.557  -10.623 53.481  1.00 55.31  ? 56  LEU C O   1 
ATOM   8609  C CB  . LEU C 1 56  ? 20.976  -10.090 50.992  1.00 45.51  ? 56  LEU C CB  1 
ATOM   8610  C CG  . LEU C 1 56  ? 20.397  -9.341  49.787  1.00 57.78  ? 56  LEU C CG  1 
ATOM   8611  C CD1 . LEU C 1 56  ? 20.495  -10.153 48.495  1.00 59.18  ? 56  LEU C CD1 1 
ATOM   8612  C CD2 . LEU C 1 56  ? 18.953  -8.916  50.053  1.00 56.62  ? 56  LEU C CD2 1 
ATOM   8613  N N   . THR C 1 57  ? 20.534  -10.296 54.427  1.00 50.88  ? 57  THR C N   1 
ATOM   8614  C CA  . THR C 1 57  ? 20.884  -11.175 55.533  1.00 49.30  ? 57  THR C CA  1 
ATOM   8615  C C   . THR C 1 57  ? 20.770  -12.634 55.098  1.00 47.94  ? 57  THR C C   1 
ATOM   8616  O O   . THR C 1 57  ? 19.873  -12.981 54.325  1.00 52.44  ? 57  THR C O   1 
ATOM   8617  C CB  . THR C 1 57  ? 19.981  -10.919 56.734  1.00 45.02  ? 57  THR C CB  1 
ATOM   8618  O OG1 . THR C 1 57  ? 18.608  -10.972 56.332  1.00 54.12  ? 57  THR C OG1 1 
ATOM   8619  C CG2 . THR C 1 57  ? 20.285  -9.563  57.302  1.00 41.92  ? 57  THR C CG2 1 
ATOM   8620  N N   . PRO C 1 58  ? 21.667  -13.503 55.574  1.00 54.47  ? 58  PRO C N   1 
ATOM   8621  C CA  . PRO C 1 58  ? 21.600  -14.914 55.155  1.00 51.52  ? 58  PRO C CA  1 
ATOM   8622  C C   . PRO C 1 58  ? 20.278  -15.585 55.482  1.00 56.51  ? 58  PRO C C   1 
ATOM   8623  O O   . PRO C 1 58  ? 19.803  -16.410 54.691  1.00 61.61  ? 58  PRO C O   1 
ATOM   8624  C CB  . PRO C 1 58  ? 22.772  -15.548 55.918  1.00 50.62  ? 58  PRO C CB  1 
ATOM   8625  C CG  . PRO C 1 58  ? 23.725  -14.405 56.143  1.00 45.41  ? 58  PRO C CG  1 
ATOM   8626  C CD  . PRO C 1 58  ? 22.824  -13.249 56.454  1.00 46.44  ? 58  PRO C CD  1 
ATOM   8627  N N   . VAL C 1 59  ? 19.660  -15.251 56.619  1.00 51.95  ? 59  VAL C N   1 
ATOM   8628  C CA  . VAL C 1 59  ? 18.380  -15.862 56.968  1.00 55.21  ? 59  VAL C CA  1 
ATOM   8629  C C   . VAL C 1 59  ? 17.320  -15.515 55.930  1.00 57.27  ? 59  VAL C C   1 
ATOM   8630  O O   . VAL C 1 59  ? 16.490  -16.356 55.564  1.00 60.87  ? 59  VAL C O   1 
ATOM   8631  C CB  . VAL C 1 59  ? 17.949  -15.439 58.384  1.00 57.23  ? 59  VAL C CB  1 
ATOM   8632  C CG1 . VAL C 1 59  ? 18.123  -13.935 58.569  1.00 56.38  ? 59  VAL C CG1 1 
ATOM   8633  C CG2 . VAL C 1 59  ? 16.507  -15.857 58.636  1.00 54.61  ? 59  VAL C CG2 1 
ATOM   8634  N N   . LEU C 1 60  ? 17.333  -14.275 55.434  1.00 56.87  ? 60  LEU C N   1 
ATOM   8635  C CA  . LEU C 1 60  ? 16.381  -13.890 54.398  1.00 59.67  ? 60  LEU C CA  1 
ATOM   8636  C C   . LEU C 1 60  ? 16.655  -14.643 53.104  1.00 56.86  ? 60  LEU C C   1 
ATOM   8637  O O   . LEU C 1 60  ? 15.720  -15.037 52.396  1.00 60.80  ? 60  LEU C O   1 
ATOM   8638  C CB  . LEU C 1 60  ? 16.435  -12.379 54.167  1.00 52.82  ? 60  LEU C CB  1 
ATOM   8639  C CG  . LEU C 1 60  ? 15.615  -11.888 52.975  1.00 51.38  ? 60  LEU C CG  1 
ATOM   8640  C CD1 . LEU C 1 60  ? 14.138  -12.119 53.242  1.00 57.01  ? 60  LEU C CD1 1 
ATOM   8641  C CD2 . LEU C 1 60  ? 15.891  -10.419 52.684  1.00 48.80  ? 60  LEU C CD2 1 
ATOM   8642  N N   . ILE C 1 61  ? 17.933  -14.872 52.797  1.00 53.97  ? 61  ILE C N   1 
ATOM   8643  C CA  . ILE C 1 61  ? 18.311  -15.597 51.587  1.00 54.02  ? 61  ILE C CA  1 
ATOM   8644  C C   . ILE C 1 61  ? 17.800  -17.033 51.642  1.00 59.78  ? 61  ILE C C   1 
ATOM   8645  O O   . ILE C 1 61  ? 17.380  -17.600 50.626  1.00 64.69  ? 61  ILE C O   1 
ATOM   8646  C CB  . ILE C 1 61  ? 19.839  -15.537 51.408  1.00 47.44  ? 61  ILE C CB  1 
ATOM   8647  C CG1 . ILE C 1 61  ? 20.228  -14.218 50.752  1.00 50.54  ? 61  ILE C CG1 1 
ATOM   8648  C CG2 . ILE C 1 61  ? 20.356  -16.718 50.597  1.00 52.17  ? 61  ILE C CG2 1 
ATOM   8649  C CD1 . ILE C 1 61  ? 21.708  -13.962 50.768  1.00 54.90  ? 61  ILE C CD1 1 
ATOM   8650  N N   . ASP C 1 62  ? 17.817  -17.638 52.831  1.00 60.44  ? 62  ASP C N   1 
ATOM   8651  C CA  . ASP C 1 62  ? 17.306  -18.998 52.984  1.00 57.31  ? 62  ASP C CA  1 
ATOM   8652  C C   . ASP C 1 62  ? 15.820  -19.067 52.675  1.00 60.21  ? 62  ASP C C   1 
ATOM   8653  O O   . ASP C 1 62  ? 15.362  -19.974 51.970  1.00 61.57  ? 62  ASP C O   1 
ATOM   8654  C CB  . ASP C 1 62  ? 17.571  -19.498 54.400  1.00 52.67  ? 62  ASP C CB  1 
ATOM   8655  C CG  . ASP C 1 62  ? 19.007  -19.857 54.610  1.00 61.05  ? 62  ASP C CG  1 
ATOM   8656  O OD1 . ASP C 1 62  ? 19.672  -20.122 53.592  1.00 67.29  ? 62  ASP C OD1 1 
ATOM   8657  O OD2 . ASP C 1 62  ? 19.471  -19.871 55.771  1.00 66.72  ? 62  ASP C OD2 1 
ATOM   8658  N N   . GLN C 1 63  ? 15.050  -18.113 53.202  1.00 53.84  ? 63  GLN C N   1 
ATOM   8659  C CA  . GLN C 1 63  ? 13.600  -18.193 53.090  1.00 57.14  ? 63  GLN C CA  1 
ATOM   8660  C C   . GLN C 1 63  ? 13.142  -17.962 51.657  1.00 59.70  ? 63  GLN C C   1 
ATOM   8661  O O   . GLN C 1 63  ? 12.219  -18.631 51.182  1.00 55.12  ? 63  GLN C O   1 
ATOM   8662  C CB  . GLN C 1 63  ? 12.949  -17.190 54.039  1.00 62.18  ? 63  GLN C CB  1 
ATOM   8663  C CG  . GLN C 1 63  ? 13.383  -17.313 55.494  1.00 60.23  ? 63  GLN C CG  1 
ATOM   8664  C CD  . GLN C 1 63  ? 12.642  -16.340 56.393  1.00 62.15  ? 63  GLN C CD  1 
ATOM   8665  O OE1 . GLN C 1 63  ? 11.695  -16.715 57.087  1.00 60.34  ? 63  GLN C OE1 1 
ATOM   8666  N NE2 . GLN C 1 63  ? 13.068  -15.080 56.380  1.00 58.86  ? 63  GLN C NE2 1 
ATOM   8667  N N   . ILE C 1 64  ? 13.776  -17.018 50.954  1.00 59.81  ? 64  ILE C N   1 
ATOM   8668  C CA  . ILE C 1 64  ? 13.462  -16.809 49.543  1.00 58.73  ? 64  ILE C CA  1 
ATOM   8669  C C   . ILE C 1 64  ? 13.768  -18.064 48.743  1.00 58.29  ? 64  ILE C C   1 
ATOM   8670  O O   . ILE C 1 64  ? 13.018  -18.441 47.835  1.00 55.03  ? 64  ILE C O   1 
ATOM   8671  C CB  . ILE C 1 64  ? 14.233  -15.593 48.997  1.00 59.47  ? 64  ILE C CB  1 
ATOM   8672  C CG1 . ILE C 1 64  ? 13.847  -14.331 49.763  1.00 54.54  ? 64  ILE C CG1 1 
ATOM   8673  C CG2 . ILE C 1 64  ? 13.986  -15.432 47.504  1.00 50.27  ? 64  ILE C CG2 1 
ATOM   8674  C CD1 . ILE C 1 64  ? 14.723  -13.154 49.447  1.00 51.25  ? 64  ILE C CD1 1 
ATOM   8675  N N   . GLN C 1 65  ? 14.878  -18.732 49.069  1.00 58.35  ? 65  GLN C N   1 
ATOM   8676  C CA  . GLN C 1 65  ? 15.242  -19.962 48.375  1.00 59.79  ? 65  GLN C CA  1 
ATOM   8677  C C   . GLN C 1 65  ? 14.211  -21.053 48.622  1.00 65.72  ? 65  GLN C C   1 
ATOM   8678  O O   . GLN C 1 65  ? 13.810  -21.763 47.693  1.00 66.09  ? 65  GLN C O   1 
ATOM   8679  C CB  . GLN C 1 65  ? 16.628  -20.417 48.822  1.00 53.44  ? 65  GLN C CB  1 
ATOM   8680  C CG  . GLN C 1 65  ? 17.757  -19.702 48.118  1.00 53.08  ? 65  GLN C CG  1 
ATOM   8681  C CD  . GLN C 1 65  ? 19.109  -20.300 48.428  1.00 65.12  ? 65  GLN C CD  1 
ATOM   8682  O OE1 . GLN C 1 65  ? 19.373  -20.723 49.554  1.00 67.33  ? 65  GLN C OE1 1 
ATOM   8683  N NE2 . GLN C 1 65  ? 19.978  -20.340 47.426  1.00 68.23  ? 65  GLN C NE2 1 
ATOM   8684  N N   . GLU C 1 66  ? 13.763  -21.194 49.872  1.00 64.63  ? 66  GLU C N   1 
ATOM   8685  C CA  . GLU C 1 66  ? 12.698  -22.147 50.167  1.00 67.34  ? 66  GLU C CA  1 
ATOM   8686  C C   . GLU C 1 66  ? 11.384  -21.725 49.520  1.00 62.82  ? 66  GLU C C   1 
ATOM   8687  O O   . GLU C 1 66  ? 10.664  -22.563 48.967  1.00 64.74  ? 66  GLU C O   1 
ATOM   8688  C CB  . GLU C 1 66  ? 12.527  -22.304 51.677  1.00 59.49  ? 66  GLU C CB  1 
ATOM   8689  C CG  . GLU C 1 66  ? 11.784  -23.567 52.068  1.00 66.38  ? 66  GLU C CG  1 
ATOM   8690  C CD  . GLU C 1 66  ? 11.661  -23.717 53.567  1.00 77.77  ? 66  GLU C CD  1 
ATOM   8691  O OE1 . GLU C 1 66  ? 11.999  -22.751 54.280  1.00 75.14  ? 66  GLU C OE1 1 
ATOM   8692  O OE2 . GLU C 1 66  ? 11.239  -24.799 54.032  1.00 80.12  ? 66  GLU C OE2 1 
ATOM   8693  N N   . TYR C 1 67  ? 11.055  -20.432 49.578  1.00 54.52  ? 67  TYR C N   1 
ATOM   8694  C CA  . TYR C 1 67  ? 9.837   -19.951 48.936  1.00 57.52  ? 67  TYR C CA  1 
ATOM   8695  C C   . TYR C 1 67  ? 9.872   -20.198 47.433  1.00 64.31  ? 67  TYR C C   1 
ATOM   8696  O O   . TYR C 1 67  ? 8.859   -20.582 46.835  1.00 64.05  ? 67  TYR C O   1 
ATOM   8697  C CB  . TYR C 1 67  ? 9.642   -18.462 49.223  1.00 59.39  ? 67  TYR C CB  1 
ATOM   8698  C CG  . TYR C 1 67  ? 8.762   -18.144 50.415  1.00 58.75  ? 67  TYR C CG  1 
ATOM   8699  C CD1 . TYR C 1 67  ? 7.379   -18.062 50.287  1.00 54.17  ? 67  TYR C CD1 1 
ATOM   8700  C CD2 . TYR C 1 67  ? 9.319   -17.900 51.659  1.00 63.17  ? 67  TYR C CD2 1 
ATOM   8701  C CE1 . TYR C 1 67  ? 6.586   -17.763 51.370  1.00 56.60  ? 67  TYR C CE1 1 
ATOM   8702  C CE2 . TYR C 1 67  ? 8.533   -17.602 52.749  1.00 60.01  ? 67  TYR C CE2 1 
ATOM   8703  C CZ  . TYR C 1 67  ? 7.171   -17.533 52.601  1.00 56.81  ? 67  TYR C CZ  1 
ATOM   8704  O OH  . TYR C 1 67  ? 6.396   -17.232 53.695  1.00 59.34  ? 67  TYR C OH  1 
ATOM   8705  N N   . ALA C 1 68  ? 11.034  -19.985 46.803  1.00 63.93  ? 68  ALA C N   1 
ATOM   8706  C CA  . ALA C 1 68  ? 11.160  -20.179 45.361  1.00 62.40  ? 68  ALA C CA  1 
ATOM   8707  C C   . ALA C 1 68  ? 11.249  -21.649 44.981  1.00 66.77  ? 68  ALA C C   1 
ATOM   8708  O O   . ALA C 1 68  ? 10.892  -22.011 43.853  1.00 70.18  ? 68  ALA C O   1 
ATOM   8709  C CB  . ALA C 1 68  ? 12.386  -19.437 44.831  1.00 60.22  ? 68  ALA C CB  1 
ATOM   8710  N N   . GLN C 1 69  ? 11.711  -22.496 45.895  1.00 64.13  ? 69  GLN C N   1 
ATOM   8711  C CA  . GLN C 1 69  ? 11.765  -23.935 45.687  1.00 65.48  ? 69  GLN C CA  1 
ATOM   8712  C C   . GLN C 1 69  ? 10.439  -24.633 45.981  1.00 64.09  ? 69  GLN C C   1 
ATOM   8713  O O   . GLN C 1 69  ? 10.365  -25.858 45.855  1.00 74.26  ? 69  GLN C O   1 
ATOM   8714  C CB  . GLN C 1 69  ? 12.863  -24.544 46.562  1.00 75.56  ? 69  GLN C CB  1 
ATOM   8715  C CG  . GLN C 1 69  ? 14.267  -24.411 46.004  1.00 81.85  ? 69  GLN C CG  1 
ATOM   8716  C CD  . GLN C 1 69  ? 15.309  -24.909 46.979  1.00 75.77  ? 69  GLN C CD  1 
ATOM   8717  O OE1 . GLN C 1 69  ? 15.015  -25.118 48.152  1.00 77.35  ? 69  GLN C OE1 1 
ATOM   8718  N NE2 . GLN C 1 69  ? 16.539  -25.080 46.505  1.00 73.30  ? 69  GLN C NE2 1 
ATOM   8719  N N   . GLY C 1 70  ? 9.401   -23.898 46.381  1.00 63.42  ? 70  GLY C N   1 
ATOM   8720  C CA  . GLY C 1 70  ? 8.099   -24.491 46.630  1.00 79.31  ? 70  GLY C CA  1 
ATOM   8721  C C   . GLY C 1 70  ? 7.960   -25.240 47.938  1.00 74.62  ? 70  GLY C C   1 
ATOM   8722  O O   . GLY C 1 70  ? 6.892   -25.814 48.196  1.00 70.30  ? 70  GLY C O   1 
ATOM   8723  N N   . LYS C 1 71  ? 8.993   -25.239 48.780  1.00 72.75  ? 71  LYS C N   1 
ATOM   8724  C CA  . LYS C 1 71  ? 9.011   -26.005 50.017  1.00 72.38  ? 71  LYS C CA  1 
ATOM   8725  C C   . LYS C 1 71  ? 8.657   -25.162 51.243  1.00 75.55  ? 71  LYS C C   1 
ATOM   8726  O O   . LYS C 1 71  ? 8.973   -25.559 52.369  1.00 83.55  ? 71  LYS C O   1 
ATOM   8727  C CB  . LYS C 1 71  ? 10.385  -26.654 50.197  1.00 74.25  ? 71  LYS C CB  1 
ATOM   8728  C CG  . LYS C 1 71  ? 11.171  -26.816 48.899  1.00 73.59  ? 71  LYS C CG  1 
ATOM   8729  C CD  . LYS C 1 71  ? 12.643  -27.098 49.155  1.00 75.98  ? 71  LYS C CD  1 
ATOM   8730  C CE  . LYS C 1 71  ? 12.887  -28.571 49.421  1.00 74.49  ? 71  LYS C CE  1 
ATOM   8731  N NZ  . LYS C 1 71  ? 14.322  -28.900 49.229  1.00 91.30  ? 71  LYS C NZ  1 
ATOM   8732  N N   . ALA C 1 72  ? 8.008   -24.014 51.052  1.00 73.53  ? 72  ALA C N   1 
ATOM   8733  C CA  . ALA C 1 72  ? 7.641   -23.122 52.150  1.00 75.54  ? 72  ALA C CA  1 
ATOM   8734  C C   . ALA C 1 72  ? 6.150   -23.258 52.434  1.00 81.53  ? 72  ALA C C   1 
ATOM   8735  O O   . ALA C 1 72  ? 5.322   -23.060 51.538  1.00 82.95  ? 72  ALA C O   1 
ATOM   8736  C CB  . ALA C 1 72  ? 7.996   -21.671 51.823  1.00 64.77  ? 72  ALA C CB  1 
ATOM   8737  N N   . LYS C 1 73  ? 5.811   -23.578 53.683  1.00 77.14  ? 73  LYS C N   1 
ATOM   8738  C CA  . LYS C 1 73  ? 4.424   -23.833 54.070  1.00 76.56  ? 73  LYS C CA  1 
ATOM   8739  C C   . LYS C 1 73  ? 3.851   -22.611 54.784  1.00 73.79  ? 73  LYS C C   1 
ATOM   8740  O O   . LYS C 1 73  ? 3.681   -22.585 56.003  1.00 74.52  ? 73  LYS C O   1 
ATOM   8741  C CB  . LYS C 1 73  ? 4.339   -25.078 54.945  1.00 74.90  ? 73  LYS C CB  1 
ATOM   8742  C CG  . LYS C 1 73  ? 5.411   -26.113 54.660  1.00 75.72  ? 73  LYS C CG  1 
ATOM   8743  C CD  . LYS C 1 73  ? 5.475   -27.131 55.787  1.00 79.77  ? 73  LYS C CD  1 
ATOM   8744  C CE  . LYS C 1 73  ? 6.432   -28.271 55.470  1.00 73.67  ? 73  LYS C CE  1 
ATOM   8745  N NZ  . LYS C 1 73  ? 5.825   -29.609 55.737  1.00 74.82  ? 73  LYS C NZ  1 
ATOM   8746  N N   . ASP C 1 74  ? 3.555   -21.583 53.993  1.00 69.66  ? 74  ASP C N   1 
ATOM   8747  C CA  . ASP C 1 74  ? 2.987   -20.354 54.530  1.00 65.36  ? 74  ASP C CA  1 
ATOM   8748  C C   . ASP C 1 74  ? 1.511   -20.580 54.840  1.00 66.00  ? 74  ASP C C   1 
ATOM   8749  O O   . ASP C 1 74  ? 0.719   -20.865 53.936  1.00 77.53  ? 74  ASP C O   1 
ATOM   8750  C CB  . ASP C 1 74  ? 3.181   -19.208 53.540  1.00 61.03  ? 74  ASP C CB  1 
ATOM   8751  C CG  . ASP C 1 74  ? 2.950   -17.845 54.165  1.00 68.19  ? 74  ASP C CG  1 
ATOM   8752  O OD1 . ASP C 1 74  ? 1.900   -17.650 54.815  1.00 85.08  ? 74  ASP C OD1 1 
ATOM   8753  O OD2 . ASP C 1 74  ? 3.817   -16.962 54.003  1.00 58.43  ? 74  ASP C OD2 1 
ATOM   8754  N N   . VAL C 1 75  ? 1.145   -20.452 56.118  1.00 63.68  ? 75  VAL C N   1 
ATOM   8755  C CA  . VAL C 1 75  ? -0.222  -20.743 56.545  1.00 61.84  ? 75  VAL C CA  1 
ATOM   8756  C C   . VAL C 1 75  ? -1.192  -19.717 55.975  1.00 71.54  ? 75  VAL C C   1 
ATOM   8757  O O   . VAL C 1 75  ? -2.262  -20.065 55.459  1.00 72.15  ? 75  VAL C O   1 
ATOM   8758  C CB  . VAL C 1 75  ? -0.302  -20.798 58.082  1.00 70.13  ? 75  VAL C CB  1 
ATOM   8759  C CG1 . VAL C 1 75  ? 0.276   -22.108 58.588  1.00 72.88  ? 75  VAL C CG1 1 
ATOM   8760  C CG2 . VAL C 1 75  ? 0.417   -19.604 58.712  1.00 73.48  ? 75  VAL C CG2 1 
ATOM   8761  N N   . PHE C 1 76  ? -0.830  -18.434 56.057  1.00 72.05  ? 76  PHE C N   1 
ATOM   8762  C CA  . PHE C 1 76  ? -1.712  -17.373 55.586  1.00 74.09  ? 76  PHE C CA  1 
ATOM   8763  C C   . PHE C 1 76  ? -1.831  -17.378 54.063  1.00 76.40  ? 76  PHE C C   1 
ATOM   8764  O O   . PHE C 1 76  ? -2.883  -17.013 53.522  1.00 74.38  ? 76  PHE C O   1 
ATOM   8765  C CB  . PHE C 1 76  ? -1.200  -16.028 56.112  1.00 66.26  ? 76  PHE C CB  1 
ATOM   8766  C CG  . PHE C 1 76  ? -2.121  -14.880 55.846  1.00 69.31  ? 76  PHE C CG  1 
ATOM   8767  C CD1 . PHE C 1 76  ? -3.110  -14.556 56.752  1.00 63.56  ? 76  PHE C CD1 1 
ATOM   8768  C CD2 . PHE C 1 76  ? -2.004  -14.132 54.681  1.00 74.86  ? 76  PHE C CD2 1 
ATOM   8769  C CE1 . PHE C 1 76  ? -3.963  -13.503 56.512  1.00 78.03  ? 76  PHE C CE1 1 
ATOM   8770  C CE2 . PHE C 1 76  ? -2.852  -13.076 54.435  1.00 67.36  ? 76  PHE C CE2 1 
ATOM   8771  C CZ  . PHE C 1 76  ? -3.836  -12.763 55.350  1.00 76.35  ? 76  PHE C CZ  1 
ATOM   8772  N N   . LEU C 1 77  ? -0.781  -17.815 53.362  1.00 71.67  ? 77  LEU C N   1 
ATOM   8773  C CA  . LEU C 1 77  ? -0.833  -17.881 51.904  1.00 71.95  ? 77  LEU C CA  1 
ATOM   8774  C C   . LEU C 1 77  ? -1.815  -18.939 51.425  1.00 72.38  ? 77  LEU C C   1 
ATOM   8775  O O   . LEU C 1 77  ? -2.505  -18.742 50.418  1.00 72.06  ? 77  LEU C O   1 
ATOM   8776  C CB  . LEU C 1 77  ? 0.551   -18.174 51.346  1.00 77.54  ? 77  LEU C CB  1 
ATOM   8777  C CG  . LEU C 1 77  ? 1.071   -17.259 50.248  1.00 70.84  ? 77  LEU C CG  1 
ATOM   8778  C CD1 . LEU C 1 77  ? 0.886   -15.779 50.600  1.00 66.50  ? 77  LEU C CD1 1 
ATOM   8779  C CD2 . LEU C 1 77  ? 2.526   -17.617 50.050  1.00 63.48  ? 77  LEU C CD2 1 
ATOM   8780  N N   . GLU C 1 78  ? -1.867  -20.085 52.109  1.00 74.15  ? 78  GLU C N   1 
ATOM   8781  C CA  . GLU C 1 78  ? -2.876  -21.080 51.769  1.00 80.56  ? 78  GLU C CA  1 
ATOM   8782  C C   . GLU C 1 78  ? -4.284  -20.544 52.000  1.00 77.64  ? 78  GLU C C   1 
ATOM   8783  O O   . GLU C 1 78  ? -5.209  -20.893 51.258  1.00 77.83  ? 78  GLU C O   1 
ATOM   8784  C CB  . GLU C 1 78  ? -2.655  -22.359 52.574  1.00 83.09  ? 78  GLU C CB  1 
ATOM   8785  C CG  . GLU C 1 78  ? -3.606  -23.478 52.181  1.00 99.13  ? 78  GLU C CG  1 
ATOM   8786  C CD  . GLU C 1 78  ? -2.892  -24.783 51.916  1.00 106.15 ? 78  GLU C CD  1 
ATOM   8787  O OE1 . GLU C 1 78  ? -3.227  -25.792 52.574  1.00 103.55 ? 78  GLU C OE1 1 
ATOM   8788  O OE2 . GLU C 1 78  ? -1.994  -24.798 51.047  1.00 100.30 ? 78  GLU C OE2 1 
ATOM   8789  N N   . ALA C 1 79  ? -4.461  -19.689 53.011  1.00 71.92  ? 79  ALA C N   1 
ATOM   8790  C CA  . ALA C 1 79  ? -5.756  -19.052 53.220  1.00 74.40  ? 79  ALA C CA  1 
ATOM   8791  C C   . ALA C 1 79  ? -6.098  -18.123 52.063  1.00 73.42  ? 79  ALA C C   1 
ATOM   8792  O O   . ALA C 1 79  ? -7.268  -17.998 51.681  1.00 82.84  ? 79  ALA C O   1 
ATOM   8793  C CB  . ALA C 1 79  ? -5.759  -18.293 54.544  1.00 75.34  ? 79  ALA C CB  1 
ATOM   8794  N N   . ILE C 1 80  ? -5.090  -17.460 51.495  1.00 67.69  ? 80  ILE C N   1 
ATOM   8795  C CA  . ILE C 1 80  ? -5.306  -16.707 50.265  1.00 73.02  ? 80  ILE C CA  1 
ATOM   8796  C C   . ILE C 1 80  ? -5.555  -17.655 49.101  1.00 77.35  ? 80  ILE C C   1 
ATOM   8797  O O   . ILE C 1 80  ? -6.461  -17.439 48.285  1.00 72.54  ? 80  ILE C O   1 
ATOM   8798  C CB  . ILE C 1 80  ? -4.108  -15.786 49.971  1.00 71.03  ? 80  ILE C CB  1 
ATOM   8799  C CG1 . ILE C 1 80  ? -4.192  -14.486 50.755  1.00 72.81  ? 80  ILE C CG1 1 
ATOM   8800  C CG2 . ILE C 1 80  ? -4.003  -15.473 48.493  1.00 69.38  ? 80  ILE C CG2 1 
ATOM   8801  C CD1 . ILE C 1 80  ? -2.838  -14.003 51.178  1.00 70.38  ? 80  ILE C CD1 1 
ATOM   8802  N N   . ARG C 1 81  ? -4.753  -18.718 49.004  1.00 74.10  ? 81  ARG C N   1 
ATOM   8803  C CA  . ARG C 1 81  ? -4.792  -19.584 47.832  1.00 74.86  ? 81  ARG C CA  1 
ATOM   8804  C C   . ARG C 1 81  ? -6.135  -20.295 47.700  1.00 77.61  ? 81  ARG C C   1 
ATOM   8805  O O   . ARG C 1 81  ? -6.744  -20.300 46.623  1.00 71.98  ? 81  ARG C O   1 
ATOM   8806  C CB  . ARG C 1 81  ? -3.651  -20.604 47.898  1.00 77.21  ? 81  ARG C CB  1 
ATOM   8807  C CG  . ARG C 1 81  ? -3.749  -21.650 46.790  1.00 90.05  ? 81  ARG C CG  1 
ATOM   8808  C CD  . ARG C 1 81  ? -2.771  -22.818 46.936  1.00 93.11  ? 81  ARG C CD  1 
ATOM   8809  N NE  . ARG C 1 81  ? -3.251  -23.871 47.826  1.00 97.74  ? 81  ARG C NE  1 
ATOM   8810  C CZ  . ARG C 1 81  ? -4.213  -24.731 47.508  1.00 90.96  ? 81  ARG C CZ  1 
ATOM   8811  N NH1 . ARG C 1 81  ? -4.874  -24.637 46.361  1.00 82.61  ? 81  ARG C NH1 1 
ATOM   8812  N NH2 . ARG C 1 81  ? -4.516  -25.712 48.354  1.00 81.91  ? 81  ARG C NH2 1 
ATOM   8813  N N   . LYS C 1 82  ? -6.608  -20.902 48.785  1.00 77.13  ? 82  LYS C N   1 
ATOM   8814  C CA  . LYS C 1 82  ? -7.766  -21.778 48.712  1.00 77.16  ? 82  LYS C CA  1 
ATOM   8815  C C   . LYS C 1 82  ? -9.028  -21.004 48.353  1.00 76.63  ? 82  LYS C C   1 
ATOM   8816  O O   . LYS C 1 82  ? -9.191  -19.830 48.702  1.00 75.49  ? 82  LYS C O   1 
ATOM   8817  C CB  . LYS C 1 82  ? -7.972  -22.501 50.044  1.00 80.66  ? 82  LYS C CB  1 
ATOM   8818  C CG  . LYS C 1 82  ? -7.634  -23.988 50.028  1.00 84.85  ? 82  LYS C CG  1 
ATOM   8819  C CD  . LYS C 1 82  ? -8.101  -24.676 51.310  1.00 87.26  ? 82  LYS C CD  1 
ATOM   8820  C CE  . LYS C 1 82  ? -7.780  -23.843 52.542  1.00 90.12  ? 82  LYS C CE  1 
ATOM   8821  N NZ  . LYS C 1 82  ? -7.745  -24.676 53.774  1.00 93.70  ? 82  LYS C NZ  1 
ATOM   8822  N N   . ASP C 1 83  ? -9.922  -21.682 47.640  1.00 74.28  ? 83  ASP C N   1 
ATOM   8823  C CA  . ASP C 1 83  ? -11.261 -21.156 47.427  1.00 79.54  ? 83  ASP C CA  1 
ATOM   8824  C C   . ASP C 1 83  ? -11.959 -20.976 48.775  1.00 81.21  ? 83  ASP C C   1 
ATOM   8825  O O   . ASP C 1 83  ? -11.862 -21.855 49.635  1.00 81.18  ? 83  ASP C O   1 
ATOM   8826  C CB  . ASP C 1 83  ? -12.061 -22.110 46.539  1.00 78.53  ? 83  ASP C CB  1 
ATOM   8827  C CG  . ASP C 1 83  ? -13.420 -21.561 46.166  1.00 84.33  ? 83  ASP C CG  1 
ATOM   8828  O OD1 . ASP C 1 83  ? -14.287 -21.414 47.054  1.00 92.60  ? 83  ASP C OD1 1 
ATOM   8829  O OD2 . ASP C 1 83  ? -13.618 -21.265 44.970  1.00 93.20  ? 83  ASP C OD2 1 
ATOM   8830  N N   . PRO C 1 84  ? -12.676 -19.867 48.991  1.00 83.56  ? 84  PRO C N   1 
ATOM   8831  C CA  . PRO C 1 84  ? -13.228 -19.601 50.331  1.00 77.80  ? 84  PRO C CA  1 
ATOM   8832  C C   . PRO C 1 84  ? -14.234 -20.638 50.789  1.00 79.89  ? 84  PRO C C   1 
ATOM   8833  O O   . PRO C 1 84  ? -14.530 -20.710 51.989  1.00 80.28  ? 84  PRO C O   1 
ATOM   8834  C CB  . PRO C 1 84  ? -13.891 -18.231 50.167  1.00 79.73  ? 84  PRO C CB  1 
ATOM   8835  C CG  . PRO C 1 84  ? -13.248 -17.628 48.939  1.00 76.92  ? 84  PRO C CG  1 
ATOM   8836  C CD  . PRO C 1 84  ? -13.024 -18.800 48.040  1.00 81.60  ? 84  PRO C CD  1 
ATOM   8837  N N   . ASP C 1 85  ? -14.784 -21.432 49.871  1.00 84.80  ? 85  ASP C N   1 
ATOM   8838  C CA  . ASP C 1 85  ? -15.692 -22.495 50.278  1.00 91.29  ? 85  ASP C CA  1 
ATOM   8839  C C   . ASP C 1 85  ? -14.955 -23.589 51.039  1.00 83.62  ? 85  ASP C C   1 
ATOM   8840  O O   . ASP C 1 85  ? -15.554 -24.275 51.875  1.00 85.32  ? 85  ASP C O   1 
ATOM   8841  C CB  . ASP C 1 85  ? -16.416 -23.056 49.055  1.00 89.12  ? 85  ASP C CB  1 
ATOM   8842  C CG  . ASP C 1 85  ? -17.658 -22.257 48.709  1.00 103.44 ? 85  ASP C CG  1 
ATOM   8843  O OD1 . ASP C 1 85  ? -17.999 -21.330 49.477  1.00 114.28 ? 85  ASP C OD1 1 
ATOM   8844  O OD2 . ASP C 1 85  ? -18.285 -22.544 47.669  1.00 113.66 ? 85  ASP C OD2 1 
ATOM   8845  N N   . ASP C 1 86  ? -13.660 -23.753 50.776  1.00 84.62  ? 86  ASP C N   1 
ATOM   8846  C CA  . ASP C 1 86  ? -12.817 -24.700 51.490  1.00 84.19  ? 86  ASP C CA  1 
ATOM   8847  C C   . ASP C 1 86  ? -12.081 -24.058 52.663  1.00 82.99  ? 86  ASP C C   1 
ATOM   8848  O O   . ASP C 1 86  ? -11.231 -24.710 53.281  1.00 89.73  ? 86  ASP C O   1 
ATOM   8849  C CB  . ASP C 1 86  ? -11.807 -25.324 50.525  1.00 81.22  ? 86  ASP C CB  1 
ATOM   8850  C CG  . ASP C 1 86  ? -12.474 -26.063 49.382  1.00 94.51  ? 86  ASP C CG  1 
ATOM   8851  O OD1 . ASP C 1 86  ? -13.714 -26.244 49.421  1.00 100.47 ? 86  ASP C OD1 1 
ATOM   8852  O OD2 . ASP C 1 86  ? -11.752 -26.476 48.451  1.00 88.61  ? 86  ASP C OD2 1 
ATOM   8853  N N   . LEU C 1 87  ? -12.388 -22.800 52.977  1.00 79.37  ? 87  LEU C N   1 
ATOM   8854  C CA  . LEU C 1 87  ? -11.670 -22.047 53.997  1.00 79.86  ? 87  LEU C CA  1 
ATOM   8855  C C   . LEU C 1 87  ? -12.236 -22.335 55.381  1.00 84.40  ? 87  LEU C C   1 
ATOM   8856  O O   . LEU C 1 87  ? -13.449 -22.259 55.594  1.00 87.68  ? 87  LEU C O   1 
ATOM   8857  C CB  . LEU C 1 87  ? -11.745 -20.546 53.712  1.00 78.30  ? 87  LEU C CB  1 
ATOM   8858  C CG  . LEU C 1 87  ? -10.697 -19.914 52.796  1.00 84.82  ? 87  LEU C CG  1 
ATOM   8859  C CD1 . LEU C 1 87  ? -10.866 -18.404 52.819  1.00 79.04  ? 87  LEU C CD1 1 
ATOM   8860  C CD2 . LEU C 1 87  ? -9.272  -20.312 53.184  1.00 80.76  ? 87  LEU C CD2 1 
ATOM   8861  N N   . GLU C 1 88  ? -11.354 -22.646 56.323  1.00 86.81  ? 88  GLU C N   1 
ATOM   8862  C CA  . GLU C 1 88  ? -11.782 -22.788 57.704  1.00 90.12  ? 88  GLU C CA  1 
ATOM   8863  C C   . GLU C 1 88  ? -12.048 -21.416 58.315  1.00 89.23  ? 88  GLU C C   1 
ATOM   8864  O O   . GLU C 1 88  ? -11.492 -20.401 57.884  1.00 88.58  ? 88  GLU C O   1 
ATOM   8865  C CB  . GLU C 1 88  ? -10.735 -23.539 58.520  1.00 92.57  ? 88  GLU C CB  1 
ATOM   8866  C CG  . GLU C 1 88  ? -10.341 -24.918 57.961  1.00 97.18  ? 88  GLU C CG  1 
ATOM   8867  C CD  . GLU C 1 88  ? -11.490 -25.770 57.381  1.00 108.97 ? 88  GLU C CD  1 
ATOM   8868  O OE1 . GLU C 1 88  ? -11.185 -26.581 56.478  1.00 104.92 ? 88  GLU C OE1 1 
ATOM   8869  O OE2 . GLU C 1 88  ? -12.652 -25.708 57.866  1.00 107.96 ? 88  GLU C OE2 1 
ATOM   8870  N N   . LYS C 1 89  ? -12.934 -21.390 59.317  1.00 85.94  ? 89  LYS C N   1 
ATOM   8871  C CA  . LYS C 1 89  ? -13.311 -20.125 59.941  1.00 87.25  ? 89  LYS C CA  1 
ATOM   8872  C C   . LYS C 1 89  ? -12.095 -19.418 60.536  1.00 88.51  ? 89  LYS C C   1 
ATOM   8873  O O   . LYS C 1 89  ? -11.995 -18.186 60.473  1.00 87.88  ? 89  LYS C O   1 
ATOM   8874  C CB  . LYS C 1 89  ? -14.389 -20.364 61.006  1.00 91.19  ? 89  LYS C CB  1 
ATOM   8875  C CG  . LYS C 1 89  ? -14.500 -19.267 62.064  1.00 94.10  ? 89  LYS C CG  1 
ATOM   8876  C CD  . LYS C 1 89  ? -15.098 -17.986 61.484  1.00 89.50  ? 89  LYS C CD  1 
ATOM   8877  C CE  . LYS C 1 89  ? -14.563 -16.746 62.200  1.00 96.01  ? 89  LYS C CE  1 
ATOM   8878  N NZ  . LYS C 1 89  ? -15.143 -15.470 61.688  1.00 91.37  ? 89  LYS C NZ  1 
ATOM   8879  N N   . GLU C 1 90  ? -11.152 -20.180 61.101  1.00 86.18  ? 90  GLU C N   1 
ATOM   8880  C CA  . GLU C 1 90  ? -9.899  -19.587 61.563  1.00 90.45  ? 90  GLU C CA  1 
ATOM   8881  C C   . GLU C 1 90  ? -9.187  -18.853 60.435  1.00 79.35  ? 90  GLU C C   1 
ATOM   8882  O O   . GLU C 1 90  ? -8.668  -17.751 60.638  1.00 83.76  ? 90  GLU C O   1 
ATOM   8883  C CB  . GLU C 1 90  ? -8.982  -20.660 62.152  1.00 92.30  ? 90  GLU C CB  1 
ATOM   8884  C CG  . GLU C 1 90  ? -9.025  -21.987 61.420  1.00 92.83  ? 90  GLU C CG  1 
ATOM   8885  C CD  . GLU C 1 90  ? -10.038 -22.937 62.020  1.00 94.12  ? 90  GLU C CD  1 
ATOM   8886  O OE1 . GLU C 1 90  ? -11.153 -22.477 62.352  1.00 93.80  ? 90  GLU C OE1 1 
ATOM   8887  O OE2 . GLU C 1 90  ? -9.720  -24.136 62.166  1.00 92.15  ? 90  GLU C OE2 1 
ATOM   8888  N N   . GLU C 1 91  ? -9.157  -19.446 59.238  1.00 82.43  ? 91  GLU C N   1 
ATOM   8889  C CA  . GLU C 1 91  ? -8.528  -18.793 58.092  1.00 76.75  ? 91  GLU C CA  1 
ATOM   8890  C C   . GLU C 1 91  ? -9.235  -17.491 57.744  1.00 78.03  ? 91  GLU C C   1 
ATOM   8891  O O   . GLU C 1 91  ? -8.589  -16.509 57.359  1.00 75.87  ? 91  GLU C O   1 
ATOM   8892  C CB  . GLU C 1 91  ? -8.528  -19.736 56.891  1.00 82.00  ? 91  GLU C CB  1 
ATOM   8893  C CG  . GLU C 1 91  ? -8.201  -21.176 57.250  1.00 82.54  ? 91  GLU C CG  1 
ATOM   8894  C CD  . GLU C 1 91  ? -7.852  -22.030 56.047  1.00 83.58  ? 91  GLU C CD  1 
ATOM   8895  O OE1 . GLU C 1 91  ? -6.682  -21.992 55.614  1.00 85.75  ? 91  GLU C OE1 1 
ATOM   8896  O OE2 . GLU C 1 91  ? -8.735  -22.761 55.553  1.00 85.70  ? 91  GLU C OE2 1 
ATOM   8897  N N   . VAL C 1 92  ? -10.566 -17.468 57.867  1.00 78.77  ? 92  VAL C N   1 
ATOM   8898  C CA  . VAL C 1 92  ? -11.324 -16.240 57.640  1.00 73.72  ? 92  VAL C CA  1 
ATOM   8899  C C   . VAL C 1 92  ? -10.849 -15.144 58.585  1.00 81.13  ? 92  VAL C C   1 
ATOM   8900  O O   . VAL C 1 92  ? -10.547 -14.025 58.159  1.00 87.23  ? 92  VAL C O   1 
ATOM   8901  C CB  . VAL C 1 92  ? -12.834 -16.498 57.797  1.00 80.75  ? 92  VAL C CB  1 
ATOM   8902  C CG1 . VAL C 1 92  ? -13.618 -15.202 57.642  1.00 83.18  ? 92  VAL C CG1 1 
ATOM   8903  C CG2 . VAL C 1 92  ? -13.306 -17.526 56.783  1.00 86.58  ? 92  VAL C CG2 1 
ATOM   8904  N N   . GLU C 1 93  ? -10.754 -15.456 59.882  1.00 81.76  ? 93  GLU C N   1 
ATOM   8905  C CA  . GLU C 1 93  ? -10.358 -14.450 60.866  1.00 78.38  ? 93  GLU C CA  1 
ATOM   8906  C C   . GLU C 1 93  ? -8.938  -13.944 60.623  1.00 82.84  ? 93  GLU C C   1 
ATOM   8907  O O   . GLU C 1 93  ? -8.649  -12.760 60.842  1.00 82.24  ? 93  GLU C O   1 
ATOM   8908  C CB  . GLU C 1 93  ? -10.488 -15.017 62.278  1.00 84.99  ? 93  GLU C CB  1 
ATOM   8909  C CG  . GLU C 1 93  ? -10.098 -14.038 63.376  1.00 94.16  ? 93  GLU C CG  1 
ATOM   8910  C CD  . GLU C 1 93  ? -11.100 -12.916 63.545  1.00 95.49  ? 93  GLU C CD  1 
ATOM   8911  O OE1 . GLU C 1 93  ? -12.022 -13.065 64.374  1.00 88.21  ? 93  GLU C OE1 1 
ATOM   8912  O OE2 . GLU C 1 93  ? -10.964 -11.884 62.850  1.00 94.59  ? 93  GLU C OE2 1 
ATOM   8913  N N   . LYS C 1 94  ? -8.032  -14.826 60.186  1.00 83.44  ? 94  LYS C N   1 
ATOM   8914  C CA  . LYS C 1 94  ? -6.696  -14.378 59.795  1.00 77.29  ? 94  LYS C CA  1 
ATOM   8915  C C   . LYS C 1 94  ? -6.773  -13.354 58.672  1.00 74.08  ? 94  LYS C C   1 
ATOM   8916  O O   . LYS C 1 94  ? -6.072  -12.335 58.702  1.00 68.44  ? 94  LYS C O   1 
ATOM   8917  C CB  . LYS C 1 94  ? -5.838  -15.569 59.362  1.00 67.84  ? 94  LYS C CB  1 
ATOM   8918  C CG  . LYS C 1 94  ? -5.828  -16.724 60.348  1.00 71.06  ? 94  LYS C CG  1 
ATOM   8919  C CD  . LYS C 1 94  ? -4.462  -17.379 60.455  1.00 70.27  ? 94  LYS C CD  1 
ATOM   8920  C CE  . LYS C 1 94  ? -4.460  -18.423 61.565  1.00 70.48  ? 94  LYS C CE  1 
ATOM   8921  N NZ  . LYS C 1 94  ? -3.568  -18.054 62.707  1.00 67.78  ? 94  LYS C NZ  1 
ATOM   8922  N N   . LEU C 1 95  ? -7.636  -13.606 57.680  1.00 77.33  ? 95  LEU C N   1 
ATOM   8923  C CA  . LEU C 1 95  ? -7.761  -12.717 56.527  1.00 74.72  ? 95  LEU C CA  1 
ATOM   8924  C C   . LEU C 1 95  ? -8.311  -11.354 56.928  1.00 80.86  ? 95  LEU C C   1 
ATOM   8925  O O   . LEU C 1 95  ? -7.830  -10.321 56.443  1.00 77.15  ? 95  LEU C O   1 
ATOM   8926  C CB  . LEU C 1 95  ? -8.656  -13.359 55.464  1.00 68.07  ? 95  LEU C CB  1 
ATOM   8927  C CG  . LEU C 1 95  ? -8.026  -14.324 54.454  1.00 73.48  ? 95  LEU C CG  1 
ATOM   8928  C CD1 . LEU C 1 95  ? -6.917  -15.142 55.077  1.00 77.41  ? 95  LEU C CD1 1 
ATOM   8929  C CD2 . LEU C 1 95  ? -9.073  -15.239 53.840  1.00 67.58  ? 95  LEU C CD2 1 
ATOM   8930  N N   . ILE C 1 96  ? -9.333  -11.339 57.793  1.00 78.74  ? 96  ILE C N   1 
ATOM   8931  C CA  . ILE C 1 96  ? -9.898  -10.087 58.298  1.00 79.75  ? 96  ILE C CA  1 
ATOM   8932  C C   . ILE C 1 96  ? -8.873  -9.340  59.143  1.00 84.32  ? 96  ILE C C   1 
ATOM   8933  O O   . ILE C 1 96  ? -8.680  -8.129  58.985  1.00 85.46  ? 96  ILE C O   1 
ATOM   8934  C CB  . ILE C 1 96  ? -11.191 -10.365 59.093  1.00 78.05  ? 96  ILE C CB  1 
ATOM   8935  C CG1 . ILE C 1 96  ? -12.021 -11.448 58.407  1.00 75.91  ? 96  ILE C CG1 1 
ATOM   8936  C CG2 . ILE C 1 96  ? -12.013 -9.096  59.284  1.00 74.16  ? 96  ILE C CG2 1 
ATOM   8937  C CD1 . ILE C 1 96  ? -12.822 -10.940 57.236  1.00 73.74  ? 96  ILE C CD1 1 
ATOM   8938  N N   . GLU C 1 97  ? -8.197  -10.053 60.052  1.00 79.30  ? 97  GLU C N   1 
ATOM   8939  C CA  . GLU C 1 97  ? -7.249  -9.399  60.950  1.00 77.24  ? 97  GLU C CA  1 
ATOM   8940  C C   . GLU C 1 97  ? -6.069  -8.818  60.184  1.00 75.69  ? 97  GLU C C   1 
ATOM   8941  O O   . GLU C 1 97  ? -5.575  -7.737  60.524  1.00 74.87  ? 97  GLU C O   1 
ATOM   8942  C CB  . GLU C 1 97  ? -6.765  -10.383 62.014  1.00 84.48  ? 97  GLU C CB  1 
ATOM   8943  C CG  . GLU C 1 97  ? -7.589  -10.366 63.299  1.00 93.06  ? 97  GLU C CG  1 
ATOM   8944  C CD  . GLU C 1 97  ? -7.964  -8.962  63.747  1.00 95.70  ? 97  GLU C CD  1 
ATOM   8945  O OE1 . GLU C 1 97  ? -7.086  -8.071  63.733  1.00 99.70  ? 97  GLU C OE1 1 
ATOM   8946  O OE2 . GLU C 1 97  ? -9.142  -8.747  64.108  1.00 95.97  ? 97  GLU C OE2 1 
ATOM   8947  N N   . PHE C 1 98  ? -5.601  -9.523  59.151  1.00 71.10  ? 98  PHE C N   1 
ATOM   8948  C CA  . PHE C 1 98  ? -4.506  -9.003  58.337  1.00 70.25  ? 98  PHE C CA  1 
ATOM   8949  C C   . PHE C 1 98  ? -4.918  -7.729  57.620  1.00 76.01  ? 98  PHE C C   1 
ATOM   8950  O O   . PHE C 1 98  ? -4.103  -6.815  57.432  1.00 68.71  ? 98  PHE C O   1 
ATOM   8951  C CB  . PHE C 1 98  ? -4.062  -10.054 57.324  1.00 63.75  ? 98  PHE C CB  1 
ATOM   8952  C CG  . PHE C 1 98  ? -2.641  -9.900  56.873  1.00 69.67  ? 98  PHE C CG  1 
ATOM   8953  C CD1 . PHE C 1 98  ? -1.595  -10.019 57.773  1.00 73.94  ? 98  PHE C CD1 1 
ATOM   8954  C CD2 . PHE C 1 98  ? -2.349  -9.630  55.544  1.00 69.03  ? 98  PHE C CD2 1 
ATOM   8955  C CE1 . PHE C 1 98  ? -0.282  -9.877  57.356  1.00 71.26  ? 98  PHE C CE1 1 
ATOM   8956  C CE2 . PHE C 1 98  ? -1.040  -9.485  55.121  1.00 65.16  ? 98  PHE C CE2 1 
ATOM   8957  C CZ  . PHE C 1 98  ? -0.006  -9.610  56.028  1.00 70.42  ? 98  PHE C CZ  1 
ATOM   8958  N N   . THR C 1 99  ? -6.184  -7.654  57.206  1.00 78.94  ? 99  THR C N   1 
ATOM   8959  C CA  . THR C 1 99  ? -6.669  -6.464  56.521  1.00 78.07  ? 99  THR C CA  1 
ATOM   8960  C C   . THR C 1 99  ? -6.810  -5.293  57.483  1.00 75.35  ? 99  THR C C   1 
ATOM   8961  O O   . THR C 1 99  ? -6.551  -4.145  57.110  1.00 77.89  ? 99  THR C O   1 
ATOM   8962  C CB  . THR C 1 99  ? -8.000  -6.756  55.833  1.00 77.17  ? 99  THR C CB  1 
ATOM   8963  O OG1 . THR C 1 99  ? -7.936  -8.031  55.181  1.00 69.92  ? 99  THR C OG1 1 
ATOM   8964  C CG2 . THR C 1 99  ? -8.300  -5.683  54.808  1.00 76.46  ? 99  THR C CG2 1 
ATOM   8965  N N   . LYS C 1 100 ? -7.211  -5.561  58.726  1.00 75.98  ? 100 LYS C N   1 
ATOM   8966  C CA  . LYS C 1 100 ? -7.310  -4.479  59.699  1.00 77.76  ? 100 LYS C CA  1 
ATOM   8967  C C   . LYS C 1 100 ? -5.941  -3.927  60.065  1.00 66.13  ? 100 LYS C C   1 
ATOM   8968  O O   . LYS C 1 100 ? -5.809  -2.724  60.315  1.00 68.26  ? 100 LYS C O   1 
ATOM   8969  C CB  . LYS C 1 100 ? -8.043  -4.951  60.955  1.00 75.41  ? 100 LYS C CB  1 
ATOM   8970  C CG  . LYS C 1 100 ? -8.780  -3.836  61.665  1.00 78.02  ? 100 LYS C CG  1 
ATOM   8971  C CD  . LYS C 1 100 ? -9.726  -4.364  62.725  1.00 83.59  ? 100 LYS C CD  1 
ATOM   8972  C CE  . LYS C 1 100 ? -10.530 -5.546  62.221  1.00 81.78  ? 100 LYS C CE  1 
ATOM   8973  N NZ  . LYS C 1 100 ? -11.138 -6.284  63.358  1.00 90.43  ? 100 LYS C NZ  1 
ATOM   8974  N N   . LEU C 1 101 ? -4.917  -4.784  60.100  1.00 70.44  ? 101 LEU C N   1 
ATOM   8975  C CA  . LEU C 1 101 ? -3.563  -4.327  60.409  1.00 72.15  ? 101 LEU C CA  1 
ATOM   8976  C C   . LEU C 1 101 ? -3.041  -3.371  59.341  1.00 70.83  ? 101 LEU C C   1 
ATOM   8977  O O   . LEU C 1 101 ? -2.496  -2.307  59.658  1.00 64.85  ? 101 LEU C O   1 
ATOM   8978  C CB  . LEU C 1 101 ? -2.625  -5.523  60.546  1.00 62.64  ? 101 LEU C CB  1 
ATOM   8979  C CG  . LEU C 1 101 ? -1.149  -5.135  60.643  1.00 76.88  ? 101 LEU C CG  1 
ATOM   8980  C CD1 . LEU C 1 101 ? -0.868  -4.394  61.944  1.00 83.11  ? 101 LEU C CD1 1 
ATOM   8981  C CD2 . LEU C 1 101 ? -0.260  -6.347  60.522  1.00 82.03  ? 101 LEU C CD2 1 
ATOM   8982  N N   . ASN C 1 102 ? -3.199  -3.735  58.068  1.00 70.05  ? 102 ASN C N   1 
ATOM   8983  C CA  . ASN C 1 102 ? -2.698  -2.948  56.951  1.00 68.02  ? 102 ASN C CA  1 
ATOM   8984  C C   . ASN C 1 102 ? -3.760  -2.039  56.344  1.00 71.71  ? 102 ASN C C   1 
ATOM   8985  O O   . ASN C 1 102 ? -3.560  -1.527  55.237  1.00 74.09  ? 102 ASN C O   1 
ATOM   8986  C CB  . ASN C 1 102 ? -2.128  -3.874  55.873  1.00 73.87  ? 102 ASN C CB  1 
ATOM   8987  C CG  . ASN C 1 102 ? -1.291  -5.000  56.446  1.00 69.46  ? 102 ASN C CG  1 
ATOM   8988  O OD1 . ASN C 1 102 ? -0.248  -4.768  57.051  1.00 70.03  ? 102 ASN C OD1 1 
ATOM   8989  N ND2 . ASN C 1 102 ? -1.751  -6.230  56.260  1.00 72.28  ? 102 ASN C ND2 1 
ATOM   8990  N N   . TYR C 1 103 ? -4.867  -1.807  57.054  1.00 77.51  ? 103 TYR C N   1 
ATOM   8991  C CA  . TYR C 1 103 ? -6.010  -1.095  56.485  1.00 73.99  ? 103 TYR C CA  1 
ATOM   8992  C C   . TYR C 1 103 ? -5.653  0.344   56.134  1.00 75.00  ? 103 TYR C C   1 
ATOM   8993  O O   . TYR C 1 103 ? -5.808  0.776   54.984  1.00 81.44  ? 103 TYR C O   1 
ATOM   8994  C CB  . TYR C 1 103 ? -7.186  -1.144  57.467  1.00 75.83  ? 103 TYR C CB  1 
ATOM   8995  C CG  . TYR C 1 103 ? -8.408  -0.358  57.036  1.00 87.09  ? 103 TYR C CG  1 
ATOM   8996  C CD1 . TYR C 1 103 ? -9.363  -0.921  56.199  1.00 85.74  ? 103 TYR C CD1 1 
ATOM   8997  C CD2 . TYR C 1 103 ? -8.617  0.942   57.485  1.00 86.23  ? 103 TYR C CD2 1 
ATOM   8998  C CE1 . TYR C 1 103 ? -10.483 -0.208  55.808  1.00 92.27  ? 103 TYR C CE1 1 
ATOM   8999  C CE2 . TYR C 1 103 ? -9.734  1.662   57.097  1.00 92.81  ? 103 TYR C CE2 1 
ATOM   9000  C CZ  . TYR C 1 103 ? -10.666 1.083   56.259  1.00 96.94  ? 103 TYR C CZ  1 
ATOM   9001  O OH  . TYR C 1 103 ? -11.785 1.789   55.868  1.00 95.42  ? 103 TYR C OH  1 
ATOM   9002  N N   . GLU C 1 104 ? -5.169  1.103   57.115  1.00 68.36  ? 104 GLU C N   1 
ATOM   9003  C CA  . GLU C 1 104 ? -4.875  2.519   56.932  1.00 75.20  ? 104 GLU C CA  1 
ATOM   9004  C C   . GLU C 1 104 ? -3.579  2.774   56.176  1.00 81.69  ? 104 GLU C C   1 
ATOM   9005  O O   . GLU C 1 104 ? -3.132  3.926   56.124  1.00 82.54  ? 104 GLU C O   1 
ATOM   9006  C CB  . GLU C 1 104 ? -4.827  3.219   58.287  1.00 72.71  ? 104 GLU C CB  1 
ATOM   9007  C CG  . GLU C 1 104 ? -5.952  2.794   59.195  1.00 83.02  ? 104 GLU C CG  1 
ATOM   9008  C CD  . GLU C 1 104 ? -6.153  3.746   60.344  1.00 92.69  ? 104 GLU C CD  1 
ATOM   9009  O OE1 . GLU C 1 104 ? -7.318  4.111   60.609  1.00 95.54  ? 104 GLU C OE1 1 
ATOM   9010  O OE2 . GLU C 1 104 ? -5.147  4.128   60.980  1.00 80.18  ? 104 GLU C OE2 1 
ATOM   9011  N N   . LYS C 1 105 ? -2.980  1.744   55.586  1.00 80.00  ? 105 LYS C N   1 
ATOM   9012  C CA  . LYS C 1 105 ? -1.766  1.933   54.815  1.00 74.74  ? 105 LYS C CA  1 
ATOM   9013  C C   . LYS C 1 105 ? -2.137  2.358   53.400  1.00 74.75  ? 105 LYS C C   1 
ATOM   9014  O O   . LYS C 1 105 ? -3.124  1.863   52.850  1.00 77.18  ? 105 LYS C O   1 
ATOM   9015  C CB  . LYS C 1 105 ? -0.971  0.647   54.773  1.00 75.06  ? 105 LYS C CB  1 
ATOM   9016  C CG  . LYS C 1 105 ? -0.568  0.209   56.150  1.00 79.99  ? 105 LYS C CG  1 
ATOM   9017  C CD  . LYS C 1 105 ? 0.222   -1.076  56.108  1.00 74.72  ? 105 LYS C CD  1 
ATOM   9018  C CE  . LYS C 1 105 ? 0.654   -1.482  57.510  1.00 74.17  ? 105 LYS C CE  1 
ATOM   9019  N NZ  . LYS C 1 105 ? 1.331   -2.793  57.556  1.00 77.37  ? 105 LYS C NZ  1 
ATOM   9020  N N   . PRO C 1 106 ? -1.377  3.277   52.803  1.00 77.03  ? 106 PRO C N   1 
ATOM   9021  C CA  . PRO C 1 106 ? -1.745  3.800   51.478  1.00 75.24  ? 106 PRO C CA  1 
ATOM   9022  C C   . PRO C 1 106 ? -1.817  2.739   50.398  1.00 75.96  ? 106 PRO C C   1 
ATOM   9023  O O   . PRO C 1 106 ? -2.602  2.886   49.453  1.00 71.51  ? 106 PRO C O   1 
ATOM   9024  C CB  . PRO C 1 106 ? -0.632  4.815   51.200  1.00 77.45  ? 106 PRO C CB  1 
ATOM   9025  C CG  . PRO C 1 106 ? -0.221  5.258   52.573  1.00 76.04  ? 106 PRO C CG  1 
ATOM   9026  C CD  . PRO C 1 106 ? -0.233  4.001   53.376  1.00 77.12  ? 106 PRO C CD  1 
ATOM   9027  N N   . ILE C 1 107 ? -1.026  1.669   50.513  1.00 75.18  ? 107 ILE C N   1 
ATOM   9028  C CA  . ILE C 1 107 ? -1.059  0.597   49.525  1.00 77.52  ? 107 ILE C CA  1 
ATOM   9029  C C   . ILE C 1 107 ? -2.348  -0.212  49.573  1.00 74.77  ? 107 ILE C C   1 
ATOM   9030  O O   . ILE C 1 107 ? -2.631  -0.956  48.628  1.00 71.14  ? 107 ILE C O   1 
ATOM   9031  C CB  . ILE C 1 107 ? 0.163   -0.329  49.707  1.00 75.62  ? 107 ILE C CB  1 
ATOM   9032  C CG1 . ILE C 1 107 ? 0.015   -1.162  50.988  1.00 74.78  ? 107 ILE C CG1 1 
ATOM   9033  C CG2 . ILE C 1 107 ? 1.454   0.491   49.716  1.00 72.26  ? 107 ILE C CG2 1 
ATOM   9034  C CD1 . ILE C 1 107 ? 1.231   -2.008  51.346  1.00 73.18  ? 107 ILE C CD1 1 
ATOM   9035  N N   . TYR C 1 108 ? -3.135  -0.089  50.646  1.00 73.05  ? 108 TYR C N   1 
ATOM   9036  C CA  . TYR C 1 108 ? -4.410  -0.786  50.795  1.00 69.27  ? 108 TYR C CA  1 
ATOM   9037  C C   . TYR C 1 108 ? -5.595  0.124   50.494  1.00 76.45  ? 108 TYR C C   1 
ATOM   9038  O O   . TYR C 1 108 ? -6.699  -0.096  51.006  1.00 83.37  ? 108 TYR C O   1 
ATOM   9039  C CB  . TYR C 1 108 ? -4.543  -1.370  52.204  1.00 71.89  ? 108 TYR C CB  1 
ATOM   9040  C CG  . TYR C 1 108 ? -4.092  -2.813  52.337  1.00 71.97  ? 108 TYR C CG  1 
ATOM   9041  C CD1 . TYR C 1 108 ? -2.747  -3.124  52.485  1.00 72.44  ? 108 TYR C CD1 1 
ATOM   9042  C CD2 . TYR C 1 108 ? -5.006  -3.860  52.319  1.00 70.74  ? 108 TYR C CD2 1 
ATOM   9043  C CE1 . TYR C 1 108 ? -2.322  -4.431  52.601  1.00 68.51  ? 108 TYR C CE1 1 
ATOM   9044  C CE2 . TYR C 1 108 ? -4.586  -5.179  52.441  1.00 68.26  ? 108 TYR C CE2 1 
ATOM   9045  C CZ  . TYR C 1 108 ? -3.240  -5.456  52.586  1.00 63.83  ? 108 TYR C CZ  1 
ATOM   9046  O OH  . TYR C 1 108 ? -2.799  -6.756  52.705  1.00 60.84  ? 108 TYR C OH  1 
ATOM   9047  N N   . ARG C 1 109 ? -5.384  1.150   49.673  1.00 79.29  ? 109 ARG C N   1 
ATOM   9048  C CA  . ARG C 1 109 ? -6.445  2.097   49.332  1.00 78.05  ? 109 ARG C CA  1 
ATOM   9049  C C   . ARG C 1 109 ? -7.262  1.588   48.145  1.00 74.59  ? 109 ARG C C   1 
ATOM   9050  O O   . ARG C 1 109 ? -7.329  2.203   47.082  1.00 76.75  ? 109 ARG C O   1 
ATOM   9051  C CB  . ARG C 1 109 ? -5.861  3.478   49.046  1.00 77.50  ? 109 ARG C CB  1 
ATOM   9052  C CG  . ARG C 1 109 ? -6.489  4.579   49.892  1.00 80.48  ? 109 ARG C CG  1 
ATOM   9053  C CD  . ARG C 1 109 ? -6.129  5.978   49.404  1.00 80.14  ? 109 ARG C CD  1 
ATOM   9054  N NE  . ARG C 1 109 ? -4.694  6.216   49.293  1.00 78.49  ? 109 ARG C NE  1 
ATOM   9055  C CZ  . ARG C 1 109 ? -3.951  6.760   50.248  1.00 79.85  ? 109 ARG C CZ  1 
ATOM   9056  N NH1 . ARG C 1 109 ? -4.462  7.065   51.431  1.00 82.85  ? 109 ARG C NH1 1 
ATOM   9057  N NH2 . ARG C 1 109 ? -2.666  7.008   50.010  1.00 81.25  ? 109 ARG C NH2 1 
ATOM   9058  N N   . PHE C 1 110 ? -7.897  0.438   48.349  1.00 72.94  ? 110 PHE C N   1 
ATOM   9059  C CA  . PHE C 1 110 ? -8.841  -0.120  47.390  1.00 77.23  ? 110 PHE C CA  1 
ATOM   9060  C C   . PHE C 1 110 ? -10.253 0.045   47.937  1.00 79.58  ? 110 PHE C C   1 
ATOM   9061  O O   . PHE C 1 110 ? -10.519 -0.292  49.097  1.00 77.98  ? 110 PHE C O   1 
ATOM   9062  C CB  . PHE C 1 110 ? -8.533  -1.591  47.108  1.00 72.15  ? 110 PHE C CB  1 
ATOM   9063  C CG  . PHE C 1 110 ? -7.230  -1.804  46.415  1.00 77.17  ? 110 PHE C CG  1 
ATOM   9064  C CD1 . PHE C 1 110 ? -6.887  -1.043  45.309  1.00 82.01  ? 110 PHE C CD1 1 
ATOM   9065  C CD2 . PHE C 1 110 ? -6.337  -2.762  46.870  1.00 79.46  ? 110 PHE C CD2 1 
ATOM   9066  C CE1 . PHE C 1 110 ? -5.670  -1.234  44.669  1.00 82.43  ? 110 PHE C CE1 1 
ATOM   9067  C CE2 . PHE C 1 110 ? -5.123  -2.955  46.238  1.00 63.63  ? 110 PHE C CE2 1 
ATOM   9068  C CZ  . PHE C 1 110 ? -4.791  -2.191  45.136  1.00 70.23  ? 110 PHE C CZ  1 
ATOM   9069  N N   . GLU C 1 111 ? -11.150 0.578   47.101  1.00 85.30  ? 111 GLU C N   1 
ATOM   9070  C CA  . GLU C 1 111 ? -12.510 0.855   47.554  1.00 84.37  ? 111 GLU C CA  1 
ATOM   9071  C C   . GLU C 1 111 ? -13.225 -0.425  47.962  1.00 86.58  ? 111 GLU C C   1 
ATOM   9072  O O   . GLU C 1 111 ? -13.933 -0.449  48.974  1.00 87.61  ? 111 GLU C O   1 
ATOM   9073  C CB  . GLU C 1 111 ? -13.298 1.585   46.466  1.00 78.82  ? 111 GLU C CB  1 
ATOM   9074  C CG  . GLU C 1 111 ? -14.336 2.585   46.998  1.00 89.26  ? 111 GLU C CG  1 
ATOM   9075  C CD  . GLU C 1 111 ? -15.597 1.916   47.554  1.00 101.93 ? 111 GLU C CD  1 
ATOM   9076  O OE1 . GLU C 1 111 ? -15.858 0.744   47.208  1.00 103.09 ? 111 GLU C OE1 1 
ATOM   9077  O OE2 . GLU C 1 111 ? -16.342 2.569   48.320  1.00 91.19  ? 111 GLU C OE2 1 
ATOM   9078  N N   . ARG C 1 112 ? -13.050 -1.499  47.186  1.00 84.03  ? 112 ARG C N   1 
ATOM   9079  C CA  . ARG C 1 112 ? -13.656 -2.780  47.537  1.00 83.04  ? 112 ARG C CA  1 
ATOM   9080  C C   . ARG C 1 112 ? -13.244 -3.227  48.937  1.00 80.05  ? 112 ARG C C   1 
ATOM   9081  O O   . ARG C 1 112 ? -14.070 -3.736  49.701  1.00 84.62  ? 112 ARG C O   1 
ATOM   9082  C CB  . ARG C 1 112 ? -13.279 -3.835  46.497  1.00 80.69  ? 112 ARG C CB  1 
ATOM   9083  C CG  . ARG C 1 112 ? -13.821 -5.224  46.790  1.00 86.20  ? 112 ARG C CG  1 
ATOM   9084  C CD  . ARG C 1 112 ? -15.338 -5.272  46.682  1.00 90.95  ? 112 ARG C CD  1 
ATOM   9085  N NE  . ARG C 1 112 ? -15.792 -6.533  46.108  1.00 92.38  ? 112 ARG C NE  1 
ATOM   9086  C CZ  . ARG C 1 112 ? -17.036 -6.985  46.176  1.00 87.01  ? 112 ARG C CZ  1 
ATOM   9087  N NH1 . ARG C 1 112 ? -17.993 -6.286  46.762  1.00 89.40  ? 112 ARG C NH1 1 
ATOM   9088  N NH2 . ARG C 1 112 ? -17.329 -8.161  45.629  1.00 87.01  ? 112 ARG C NH2 1 
ATOM   9089  N N   . ILE C 1 113 ? -11.973 -3.037  49.295  1.00 81.51  ? 113 ILE C N   1 
ATOM   9090  C CA  . ILE C 1 113 ? -11.526 -3.394  50.640  1.00 79.07  ? 113 ILE C CA  1 
ATOM   9091  C C   . ILE C 1 113 ? -12.278 -2.580  51.681  1.00 81.99  ? 113 ILE C C   1 
ATOM   9092  O O   . ILE C 1 113 ? -12.675 -3.100  52.732  1.00 89.95  ? 113 ILE C O   1 
ATOM   9093  C CB  . ILE C 1 113 ? -10.006 -3.204  50.773  1.00 74.95  ? 113 ILE C CB  1 
ATOM   9094  C CG1 . ILE C 1 113 ? -9.258  -4.405  50.191  1.00 81.82  ? 113 ILE C CG1 1 
ATOM   9095  C CG2 . ILE C 1 113 ? -9.633  -2.990  52.227  1.00 75.63  ? 113 ILE C CG2 1 
ATOM   9096  C CD1 . ILE C 1 113 ? -7.877  -4.075  49.666  1.00 73.67  ? 113 ILE C CD1 1 
ATOM   9097  N N   . ARG C 1 114 ? -12.475 -1.288  51.411  1.00 78.27  ? 114 ARG C N   1 
ATOM   9098  C CA  . ARG C 1 114 ? -13.278 -0.442  52.290  1.00 88.73  ? 114 ARG C CA  1 
ATOM   9099  C C   . ARG C 1 114 ? -14.680 -1.017  52.474  1.00 90.46  ? 114 ARG C C   1 
ATOM   9100  O O   . ARG C 1 114 ? -15.143 -1.228  53.600  1.00 80.88  ? 114 ARG C O   1 
ATOM   9101  C CB  . ARG C 1 114 ? -13.352 0.978   51.715  1.00 86.44  ? 114 ARG C CB  1 
ATOM   9102  C CG  . ARG C 1 114 ? -12.816 2.082   52.619  1.00 90.31  ? 114 ARG C CG  1 
ATOM   9103  C CD  . ARG C 1 114 ? -11.287 2.068   52.716  1.00 100.90 ? 114 ARG C CD  1 
ATOM   9104  N NE  . ARG C 1 114 ? -10.795 3.031   53.700  1.00 100.92 ? 114 ARG C NE  1 
ATOM   9105  C CZ  . ARG C 1 114 ? -9.575  3.555   53.703  1.00 101.04 ? 114 ARG C CZ  1 
ATOM   9106  N NH1 . ARG C 1 114 ? -8.673  3.214   52.796  1.00 99.52  ? 114 ARG C NH1 1 
ATOM   9107  N NH2 . ARG C 1 114 ? -9.253  4.449   54.635  1.00 98.22  ? 114 ARG C NH2 1 
ATOM   9108  N N   . GLU C 1 115 ? -15.372 -1.273  51.360  1.00 93.29  ? 115 GLU C N   1 
ATOM   9109  C CA  . GLU C 1 115 ? -16.741 -1.778  51.431  1.00 91.47  ? 115 GLU C CA  1 
ATOM   9110  C C   . GLU C 1 115 ? -16.784 -3.167  52.057  1.00 92.83  ? 115 GLU C C   1 
ATOM   9111  O O   . GLU C 1 115 ? -17.677 -3.469  52.859  1.00 94.07  ? 115 GLU C O   1 
ATOM   9112  C CB  . GLU C 1 115 ? -17.363 -1.795  50.032  1.00 91.63  ? 115 GLU C CB  1 
ATOM   9113  C CG  . GLU C 1 115 ? -18.322 -2.953  49.786  1.00 106.17 ? 115 GLU C CG  1 
ATOM   9114  C CD  . GLU C 1 115 ? -18.636 -3.160  48.314  1.00 109.22 ? 115 GLU C CD  1 
ATOM   9115  O OE1 . GLU C 1 115 ? -19.440 -4.063  48.004  1.00 110.87 ? 115 GLU C OE1 1 
ATOM   9116  O OE2 . GLU C 1 115 ? -18.072 -2.433  47.466  1.00 99.25  ? 115 GLU C OE2 1 
ATOM   9117  N N   . LEU C 1 116 ? -15.820 -4.022  51.712  1.00 88.62  ? 116 LEU C N   1 
ATOM   9118  C CA  . LEU C 1 116 ? -15.836 -5.390  52.215  1.00 88.43  ? 116 LEU C CA  1 
ATOM   9119  C C   . LEU C 1 116 ? -15.732 -5.421  53.735  1.00 91.07  ? 116 LEU C C   1 
ATOM   9120  O O   . LEU C 1 116 ? -16.376 -6.247  54.393  1.00 84.86  ? 116 LEU C O   1 
ATOM   9121  C CB  . LEU C 1 116 ? -14.701 -6.192  51.580  1.00 84.36  ? 116 LEU C CB  1 
ATOM   9122  C CG  . LEU C 1 116 ? -14.969 -6.699  50.163  1.00 83.62  ? 116 LEU C CG  1 
ATOM   9123  C CD1 . LEU C 1 116 ? -14.169 -7.945  49.901  1.00 79.70  ? 116 LEU C CD1 1 
ATOM   9124  C CD2 . LEU C 1 116 ? -16.441 -6.946  49.937  1.00 89.80  ? 116 LEU C CD2 1 
ATOM   9125  N N   . MET C 1 117 ? -14.941 -4.514  54.312  1.00 89.78  ? 117 MET C N   1 
ATOM   9126  C CA  . MET C 1 117 ? -14.756 -4.495  55.757  1.00 85.51  ? 117 MET C CA  1 
ATOM   9127  C C   . MET C 1 117 ? -16.036 -4.102  56.483  1.00 92.29  ? 117 MET C C   1 
ATOM   9128  O O   . MET C 1 117 ? -16.273 -4.561  57.606  1.00 98.15  ? 117 MET C O   1 
ATOM   9129  C CB  . MET C 1 117 ? -13.631 -3.531  56.118  1.00 88.23  ? 117 MET C CB  1 
ATOM   9130  C CG  . MET C 1 117 ? -12.227 -4.034  55.809  1.00 88.56  ? 117 MET C CG  1 
ATOM   9131  S SD  . MET C 1 117 ? -12.040 -5.824  55.759  1.00 89.01  ? 117 MET C SD  1 
ATOM   9132  C CE  . MET C 1 117 ? -11.428 -6.117  57.415  1.00 71.53  ? 117 MET C CE  1 
ATOM   9133  N N   . ASN C 1 118 ? -16.869 -3.257  55.862  1.00 96.22  ? 118 ASN C N   1 
ATOM   9134  C CA  . ASN C 1 118 ? -18.112 -2.817  56.489  1.00 97.60  ? 118 ASN C CA  1 
ATOM   9135  C C   . ASN C 1 118 ? -19.189 -3.890  56.475  1.00 90.94  ? 118 ASN C C   1 
ATOM   9136  O O   . ASN C 1 118 ? -20.137 -3.805  57.262  1.00 101.19 ? 118 ASN C O   1 
ATOM   9137  C CB  . ASN C 1 118 ? -18.639 -1.554  55.806  1.00 95.55  ? 118 ASN C CB  1 
ATOM   9138  C CG  . ASN C 1 118 ? -17.648 -0.417  55.854  1.00 102.67 ? 118 ASN C CG  1 
ATOM   9139  O OD1 . ASN C 1 118 ? -16.438 -0.633  55.942  1.00 100.97 ? 118 ASN C OD1 1 
ATOM   9140  N ND2 . ASN C 1 118 ? -18.156 0.809   55.808  1.00 98.77  ? 118 ASN C ND2 1 
ATOM   9141  N N   . LYS C 1 119 ? -19.066 -4.892  55.610  1.00 89.51  ? 119 LYS C N   1 
ATOM   9142  C CA  . LYS C 1 119 ? -20.051 -5.962  55.568  1.00 102.55 ? 119 LYS C CA  1 
ATOM   9143  C C   . LYS C 1 119 ? -19.866 -6.887  56.767  1.00 102.20 ? 119 LYS C C   1 
ATOM   9144  O O   . LYS C 1 119 ? -18.763 -7.385  57.017  1.00 97.38  ? 119 LYS C O   1 
ATOM   9145  C CB  . LYS C 1 119 ? -19.924 -6.747  54.263  1.00 93.70  ? 119 LYS C CB  1 
ATOM   9146  C CG  . LYS C 1 119 ? -21.150 -6.705  53.359  1.00 91.28  ? 119 LYS C CG  1 
ATOM   9147  C CD  . LYS C 1 119 ? -22.222 -7.649  53.874  1.00 104.81 ? 119 LYS C CD  1 
ATOM   9148  C CE  . LYS C 1 119 ? -23.196 -8.067  52.789  1.00 99.38  ? 119 LYS C CE  1 
ATOM   9149  N NZ  . LYS C 1 119 ? -24.317 -8.862  53.354  1.00 98.23  ? 119 LYS C NZ  1 
ATOM   9150  N N   . GLU C 1 120 ? -20.955 -7.119  57.508  1.00 109.34 ? 120 GLU C N   1 
ATOM   9151  C CA  . GLU C 1 120 ? -20.888 -7.994  58.675  1.00 110.97 ? 120 GLU C CA  1 
ATOM   9152  C C   . GLU C 1 120 ? -20.603 -9.434  58.264  1.00 114.64 ? 120 GLU C C   1 
ATOM   9153  O O   . GLU C 1 120 ? -19.874 -10.152 58.961  1.00 112.39 ? 120 GLU C O   1 
ATOM   9154  C CB  . GLU C 1 120 ? -22.190 -7.890  59.479  1.00 122.61 ? 120 GLU C CB  1 
ATOM   9155  C CG  . GLU C 1 120 ? -22.224 -8.688  60.794  1.00 127.99 ? 120 GLU C CG  1 
ATOM   9156  C CD  . GLU C 1 120 ? -22.595 -10.151 60.623  1.00 128.70 ? 120 GLU C CD  1 
ATOM   9157  O OE1 . GLU C 1 120 ? -22.461 -10.908 61.614  1.00 116.92 ? 120 GLU C OE1 1 
ATOM   9158  O OE2 . GLU C 1 120 ? -23.038 -10.528 59.513  1.00 132.95 ? 120 GLU C OE2 1 
ATOM   9159  N N   . LYS C 1 121 ? -21.162 -9.868  57.134  1.00 114.07 ? 121 LYS C N   1 
ATOM   9160  C CA  . LYS C 1 121 ? -20.960 -11.211 56.611  1.00 111.88 ? 121 LYS C CA  1 
ATOM   9161  C C   . LYS C 1 121 ? -20.430 -11.128 55.185  1.00 103.07 ? 121 LYS C C   1 
ATOM   9162  O O   . LYS C 1 121 ? -20.738 -10.190 54.447  1.00 104.85 ? 121 LYS C O   1 
ATOM   9163  C CB  . LYS C 1 121 ? -22.263 -12.021 56.652  1.00 102.63 ? 121 LYS C CB  1 
ATOM   9164  C CG  . LYS C 1 121 ? -22.088 -13.463 57.097  1.00 101.45 ? 121 LYS C CG  1 
ATOM   9165  C CD  . LYS C 1 121 ? -23.212 -14.342 56.572  1.00 105.11 ? 121 LYS C CD  1 
ATOM   9166  C CE  . LYS C 1 121 ? -24.477 -14.197 57.417  1.00 108.52 ? 121 LYS C CE  1 
ATOM   9167  N NZ  . LYS C 1 121 ? -25.152 -15.503 57.673  1.00 102.26 ? 121 LYS C NZ  1 
ATOM   9168  N N   . LEU C 1 122 ? -19.619 -12.113 54.799  1.00 91.44  ? 122 LEU C N   1 
ATOM   9169  C CA  . LEU C 1 122 ? -18.936 -12.093 53.512  1.00 97.59  ? 122 LEU C CA  1 
ATOM   9170  C C   . LEU C 1 122 ? -19.169 -13.408 52.782  1.00 92.68  ? 122 LEU C C   1 
ATOM   9171  O O   . LEU C 1 122 ? -18.929 -14.484 53.340  1.00 95.09  ? 122 LEU C O   1 
ATOM   9172  C CB  . LEU C 1 122 ? -17.430 -11.837 53.687  1.00 92.85  ? 122 LEU C CB  1 
ATOM   9173  C CG  . LEU C 1 122 ? -16.945 -10.449 54.141  1.00 93.64  ? 122 LEU C CG  1 
ATOM   9174  C CD1 . LEU C 1 122 ? -17.502 -9.353  53.225  1.00 87.81  ? 122 LEU C CD1 1 
ATOM   9175  C CD2 . LEU C 1 122 ? -17.206 -10.140 55.624  1.00 100.10 ? 122 LEU C CD2 1 
ATOM   9176  N N   . ASN C 1 123 ? -19.631 -13.321 51.537  1.00 87.06  ? 123 ASN C N   1 
ATOM   9177  C CA  . ASN C 1 123 ? -19.904 -14.514 50.753  1.00 87.97  ? 123 ASN C CA  1 
ATOM   9178  C C   . ASN C 1 123 ? -18.621 -15.009 50.092  1.00 88.11  ? 123 ASN C C   1 
ATOM   9179  O O   . ASN C 1 123 ? -17.528 -14.481 50.318  1.00 87.57  ? 123 ASN C O   1 
ATOM   9180  C CB  . ASN C 1 123 ? -21.000 -14.242 49.720  1.00 95.88  ? 123 ASN C CB  1 
ATOM   9181  C CG  . ASN C 1 123 ? -20.571 -13.264 48.635  1.00 92.25  ? 123 ASN C CG  1 
ATOM   9182  O OD1 . ASN C 1 123 ? -19.506 -12.654 48.706  1.00 95.41  ? 123 ASN C OD1 1 
ATOM   9183  N ND2 . ASN C 1 123 ? -21.411 -13.115 47.619  1.00 101.75 ? 123 ASN C ND2 1 
ATOM   9184  N N   . ARG C 1 124 ? -18.759 -16.043 49.259  1.00 91.03  ? 124 ARG C N   1 
ATOM   9185  C CA  . ARG C 1 124 ? -17.612 -16.563 48.521  1.00 92.47  ? 124 ARG C CA  1 
ATOM   9186  C C   . ARG C 1 124 ? -17.046 -15.521 47.561  1.00 89.18  ? 124 ARG C C   1 
ATOM   9187  O O   . ARG C 1 124 ? -15.828 -15.440 47.371  1.00 96.59  ? 124 ARG C O   1 
ATOM   9188  C CB  . ARG C 1 124 ? -18.008 -17.824 47.756  1.00 95.26  ? 124 ARG C CB  1 
ATOM   9189  C CG  . ARG C 1 124 ? -16.828 -18.626 47.245  1.00 93.98  ? 124 ARG C CG  1 
ATOM   9190  C CD  . ARG C 1 124 ? -17.282 -19.784 46.371  1.00 93.58  ? 124 ARG C CD  1 
ATOM   9191  N NE  . ARG C 1 124 ? -16.321 -20.076 45.314  1.00 97.36  ? 124 ARG C NE  1 
ATOM   9192  C CZ  . ARG C 1 124 ? -16.213 -19.393 44.184  1.00 94.58  ? 124 ARG C CZ  1 
ATOM   9193  N NH1 . ARG C 1 124 ? -17.020 -18.381 43.907  1.00 96.41  ? 124 ARG C NH1 1 
ATOM   9194  N NH2 . ARG C 1 124 ? -15.268 -19.731 43.311  1.00 99.76  ? 124 ARG C NH2 1 
ATOM   9195  N N   . GLU C 1 125 ? -17.916 -14.720 46.945  1.00 89.47  ? 125 GLU C N   1 
ATOM   9196  C CA  . GLU C 1 125 ? -17.463 -13.694 46.011  1.00 83.69  ? 125 GLU C CA  1 
ATOM   9197  C C   . GLU C 1 125 ? -16.583 -12.667 46.711  1.00 87.98  ? 125 GLU C C   1 
ATOM   9198  O O   . GLU C 1 125 ? -15.453 -12.401 46.281  1.00 93.10  ? 125 GLU C O   1 
ATOM   9199  C CB  . GLU C 1 125 ? -18.668 -13.010 45.364  1.00 88.55  ? 125 GLU C CB  1 
ATOM   9200  C CG  . GLU C 1 125 ? -19.405 -13.847 44.309  1.00 106.33 ? 125 GLU C CG  1 
ATOM   9201  C CD  . GLU C 1 125 ? -19.920 -15.178 44.843  1.00 112.95 ? 125 GLU C CD  1 
ATOM   9202  O OE1 . GLU C 1 125 ? -20.882 -15.173 45.645  1.00 108.02 ? 125 GLU C OE1 1 
ATOM   9203  O OE2 . GLU C 1 125 ? -19.357 -16.229 44.467  1.00 110.37 ? 125 GLU C OE2 1 
ATOM   9204  N N   . GLU C 1 126 ? -17.087 -12.085 47.804  1.00 86.14  ? 126 GLU C N   1 
ATOM   9205  C CA  . GLU C 1 126 ? -16.341 -11.054 48.520  1.00 86.78  ? 126 GLU C CA  1 
ATOM   9206  C C   . GLU C 1 126 ? -15.066 -11.620 49.134  1.00 88.46  ? 126 GLU C C   1 
ATOM   9207  O O   . GLU C 1 126 ? -14.020 -10.961 49.134  1.00 82.73  ? 126 GLU C O   1 
ATOM   9208  C CB  . GLU C 1 126 ? -17.231 -10.420 49.593  1.00 88.26  ? 126 GLU C CB  1 
ATOM   9209  C CG  . GLU C 1 126 ? -18.412 -9.626  49.018  1.00 97.97  ? 126 GLU C CG  1 
ATOM   9210  C CD  . GLU C 1 126 ? -19.697 -9.779  49.823  1.00 104.64 ? 126 GLU C CD  1 
ATOM   9211  O OE1 . GLU C 1 126 ? -19.752 -10.672 50.693  1.00 111.51 ? 126 GLU C OE1 1 
ATOM   9212  O OE2 . GLU C 1 126 ? -20.660 -9.018  49.573  1.00 104.57 ? 126 GLU C OE2 1 
ATOM   9213  N N   . LEU C 1 127 ? -15.130 -12.846 49.651  1.00 87.50  ? 127 LEU C N   1 
ATOM   9214  C CA  . LEU C 1 127 ? -13.941 -13.469 50.217  1.00 81.29  ? 127 LEU C CA  1 
ATOM   9215  C C   . LEU C 1 127 ? -12.847 -13.617 49.163  1.00 80.92  ? 127 LEU C C   1 
ATOM   9216  O O   . LEU C 1 127 ? -11.679 -13.298 49.420  1.00 78.30  ? 127 LEU C O   1 
ATOM   9217  C CB  . LEU C 1 127 ? -14.311 -14.819 50.825  1.00 79.92  ? 127 LEU C CB  1 
ATOM   9218  C CG  . LEU C 1 127 ? -14.783 -14.780 52.279  1.00 82.62  ? 127 LEU C CG  1 
ATOM   9219  C CD1 . LEU C 1 127 ? -14.529 -16.115 52.950  1.00 91.37  ? 127 LEU C CD1 1 
ATOM   9220  C CD2 . LEU C 1 127 ? -14.120 -13.647 53.063  1.00 82.91  ? 127 LEU C CD2 1 
ATOM   9221  N N   . LEU C 1 128 ? -13.210 -14.094 47.963  1.00 74.99  ? 128 LEU C N   1 
ATOM   9222  C CA  . LEU C 1 128 ? -12.257 -14.146 46.851  1.00 77.89  ? 128 LEU C CA  1 
ATOM   9223  C C   . LEU C 1 128 ? -11.576 -12.804 46.639  1.00 79.73  ? 128 LEU C C   1 
ATOM   9224  O O   . LEU C 1 128 ? -10.346 -12.726 46.534  1.00 77.21  ? 128 LEU C O   1 
ATOM   9225  C CB  . LEU C 1 128 ? -12.958 -14.595 45.564  1.00 77.38  ? 128 LEU C CB  1 
ATOM   9226  C CG  . LEU C 1 128 ? -12.275 -15.646 44.684  1.00 76.36  ? 128 LEU C CG  1 
ATOM   9227  C CD1 . LEU C 1 128 ? -11.877 -16.881 45.468  1.00 74.96  ? 128 LEU C CD1 1 
ATOM   9228  C CD2 . LEU C 1 128 ? -13.234 -16.040 43.575  1.00 77.93  ? 128 LEU C CD2 1 
ATOM   9229  N N   . ASP C 1 129 ? -12.369 -11.732 46.583  1.00 74.84  ? 129 ASP C N   1 
ATOM   9230  C CA  . ASP C 1 129 ? -11.820 -10.402 46.332  1.00 75.87  ? 129 ASP C CA  1 
ATOM   9231  C C   . ASP C 1 129 ? -10.935 -9.931  47.483  1.00 74.97  ? 129 ASP C C   1 
ATOM   9232  O O   . ASP C 1 129 ? -9.867  -9.351  47.253  1.00 68.58  ? 129 ASP C O   1 
ATOM   9233  C CB  . ASP C 1 129 ? -12.963 -9.423  46.074  1.00 74.42  ? 129 ASP C CB  1 
ATOM   9234  C CG  . ASP C 1 129 ? -13.685 -9.719  44.773  1.00 96.64  ? 129 ASP C CG  1 
ATOM   9235  O OD1 . ASP C 1 129 ? -13.396 -10.786 44.185  1.00 101.08 ? 129 ASP C OD1 1 
ATOM   9236  O OD2 . ASP C 1 129 ? -14.537 -8.914  44.339  1.00 98.54  ? 129 ASP C OD2 1 
ATOM   9237  N N   . LEU C 1 130 ? -11.350 -10.181 48.728  1.00 75.95  ? 130 LEU C N   1 
ATOM   9238  C CA  . LEU C 1 130 ? -10.504 -9.820  49.862  1.00 72.65  ? 130 LEU C CA  1 
ATOM   9239  C C   . LEU C 1 130 ? -9.177  -10.565 49.810  1.00 77.19  ? 130 LEU C C   1 
ATOM   9240  O O   . LEU C 1 130 ? -8.117  -9.981  50.068  1.00 77.87  ? 130 LEU C O   1 
ATOM   9241  C CB  . LEU C 1 130 ? -11.228 -10.100 51.179  1.00 72.60  ? 130 LEU C CB  1 
ATOM   9242  C CG  . LEU C 1 130 ? -10.683 -9.367  52.410  1.00 78.10  ? 130 LEU C CG  1 
ATOM   9243  C CD1 . LEU C 1 130 ? -11.202 -7.932  52.487  1.00 79.06  ? 130 LEU C CD1 1 
ATOM   9244  C CD2 . LEU C 1 130 ? -11.019 -10.143 53.677  1.00 76.66  ? 130 LEU C CD2 1 
ATOM   9245  N N   . GLN C 1 131 ? -9.216  -11.857 49.474  1.00 73.74  ? 131 GLN C N   1 
ATOM   9246  C CA  . GLN C 1 131 ? -7.983  -12.619 49.294  1.00 78.55  ? 131 GLN C CA  1 
ATOM   9247  C C   . GLN C 1 131 ? -7.095  -11.977 48.235  1.00 73.90  ? 131 GLN C C   1 
ATOM   9248  O O   . GLN C 1 131 ? -5.922  -11.676 48.482  1.00 72.11  ? 131 GLN C O   1 
ATOM   9249  C CB  . GLN C 1 131 ? -8.309  -14.059 48.895  1.00 80.83  ? 131 GLN C CB  1 
ATOM   9250  C CG  . GLN C 1 131 ? -8.915  -14.927 49.970  1.00 72.41  ? 131 GLN C CG  1 
ATOM   9251  C CD  . GLN C 1 131 ? -9.312  -16.277 49.415  1.00 71.14  ? 131 GLN C CD  1 
ATOM   9252  O OE1 . GLN C 1 131 ? -9.766  -16.375 48.275  1.00 74.81  ? 131 GLN C OE1 1 
ATOM   9253  N NE2 . GLN C 1 131 ? -9.130  -17.327 50.205  1.00 73.91  ? 131 GLN C NE2 1 
ATOM   9254  N N   . THR C 1 132 ? -7.654  -11.750 47.043  1.00 76.37  ? 132 THR C N   1 
ATOM   9255  C CA  . THR C 1 132 ? -6.858  -11.295 45.907  1.00 73.02  ? 132 THR C CA  1 
ATOM   9256  C C   . THR C 1 132 ? -6.403  -9.854  46.078  1.00 68.71  ? 132 THR C C   1 
ATOM   9257  O O   . THR C 1 132 ? -5.309  -9.485  45.637  1.00 68.89  ? 132 THR C O   1 
ATOM   9258  C CB  . THR C 1 132 ? -7.667  -11.434 44.621  1.00 67.46  ? 132 THR C CB  1 
ATOM   9259  O OG1 . THR C 1 132 ? -8.236  -12.745 44.560  1.00 67.96  ? 132 THR C OG1 1 
ATOM   9260  C CG2 . THR C 1 132 ? -6.767  -11.221 43.418  1.00 70.59  ? 132 THR C CG2 1 
ATOM   9261  N N   . LEU C 1 133 ? -7.243  -9.014  46.684  1.00 71.73  ? 133 LEU C N   1 
ATOM   9262  C CA  . LEU C 1 133 ? -6.872  -7.614  46.857  1.00 72.01  ? 133 LEU C CA  1 
ATOM   9263  C C   . LEU C 1 133 ? -5.773  -7.467  47.897  1.00 68.83  ? 133 LEU C C   1 
ATOM   9264  O O   . LEU C 1 133 ? -4.879  -6.623  47.751  1.00 70.97  ? 133 LEU C O   1 
ATOM   9265  C CB  . LEU C 1 133 ? -8.093  -6.791  47.252  1.00 74.78  ? 133 LEU C CB  1 
ATOM   9266  C CG  . LEU C 1 133 ? -8.997  -6.325  46.116  1.00 67.81  ? 133 LEU C CG  1 
ATOM   9267  C CD1 . LEU C 1 133 ? -10.132 -5.523  46.702  1.00 71.30  ? 133 LEU C CD1 1 
ATOM   9268  C CD2 . LEU C 1 133 ? -8.222  -5.495  45.111  1.00 67.22  ? 133 LEU C CD2 1 
ATOM   9269  N N   . ASN C 1 134 ? -5.829  -8.272  48.960  1.00 69.56  ? 134 ASN C N   1 
ATOM   9270  C CA  . ASN C 1 134 ? -4.714  -8.315  49.899  1.00 72.92  ? 134 ASN C CA  1 
ATOM   9271  C C   . ASN C 1 134 ? -3.425  -8.676  49.178  1.00 66.67  ? 134 ASN C C   1 
ATOM   9272  O O   . ASN C 1 134 ? -2.353  -8.162  49.511  1.00 72.57  ? 134 ASN C O   1 
ATOM   9273  C CB  . ASN C 1 134 ? -4.999  -9.315  51.023  1.00 78.62  ? 134 ASN C CB  1 
ATOM   9274  C CG  . ASN C 1 134 ? -5.639  -8.670  52.240  1.00 72.82  ? 134 ASN C CG  1 
ATOM   9275  O OD1 . ASN C 1 134 ? -4.954  -8.307  53.198  1.00 67.74  ? 134 ASN C OD1 1 
ATOM   9276  N ND2 . ASN C 1 134 ? -6.959  -8.534  52.210  1.00 81.71  ? 134 ASN C ND2 1 
ATOM   9277  N N   . LEU C 1 135 ? -3.513  -9.544  48.169  1.00 58.89  ? 135 LEU C N   1 
ATOM   9278  C CA  . LEU C 1 135 ? -2.325  -9.897  47.402  1.00 59.29  ? 135 LEU C CA  1 
ATOM   9279  C C   . LEU C 1 135 ? -1.849  -8.734  46.548  1.00 57.48  ? 135 LEU C C   1 
ATOM   9280  O O   . LEU C 1 135 ? -0.643  -8.488  46.438  1.00 72.55  ? 135 LEU C O   1 
ATOM   9281  C CB  . LEU C 1 135 ? -2.605  -11.104 46.518  1.00 58.79  ? 135 LEU C CB  1 
ATOM   9282  C CG  . LEU C 1 135 ? -2.102  -12.445 47.032  1.00 58.64  ? 135 LEU C CG  1 
ATOM   9283  C CD1 . LEU C 1 135 ? -2.318  -13.437 45.934  1.00 66.69  ? 135 LEU C CD1 1 
ATOM   9284  C CD2 . LEU C 1 135 ? -0.638  -12.416 47.438  1.00 56.98  ? 135 LEU C CD2 1 
ATOM   9285  N N   . LEU C 1 136 ? -2.777  -8.006  45.936  1.00 58.90  ? 136 LEU C N   1 
ATOM   9286  C CA  . LEU C 1 136 ? -2.415  -6.973  44.974  1.00 68.52  ? 136 LEU C CA  1 
ATOM   9287  C C   . LEU C 1 136 ? -1.931  -5.695  45.645  1.00 61.66  ? 136 LEU C C   1 
ATOM   9288  O O   . LEU C 1 136 ? -1.283  -4.869  44.993  1.00 62.16  ? 136 LEU C O   1 
ATOM   9289  C CB  . LEU C 1 136 ? -3.613  -6.672  44.065  1.00 65.18  ? 136 LEU C CB  1 
ATOM   9290  C CG  . LEU C 1 136 ? -3.695  -7.436  42.738  1.00 66.63  ? 136 LEU C CG  1 
ATOM   9291  C CD1 . LEU C 1 136 ? -3.227  -8.863  42.921  1.00 62.63  ? 136 LEU C CD1 1 
ATOM   9292  C CD2 . LEU C 1 136 ? -5.118  -7.422  42.172  1.00 75.73  ? 136 LEU C CD2 1 
ATOM   9293  N N   . ALA C 1 137 ? -2.230  -5.510  46.931  1.00 59.16  ? 137 ALA C N   1 
ATOM   9294  C CA  . ALA C 1 137 ? -1.778  -4.303  47.611  1.00 67.76  ? 137 ALA C CA  1 
ATOM   9295  C C   . ALA C 1 137 ? -0.264  -4.305  47.794  1.00 68.22  ? 137 ALA C C   1 
ATOM   9296  O O   . ALA C 1 137 ? 0.351   -3.238  47.908  1.00 67.85  ? 137 ALA C O   1 
ATOM   9297  C CB  . ALA C 1 137 ? -2.504  -4.154  48.951  1.00 67.04  ? 137 ALA C CB  1 
ATOM   9298  N N   . TRP C 1 138 ? 0.352   -5.489  47.794  1.00 62.93  ? 138 TRP C N   1 
ATOM   9299  C CA  . TRP C 1 138 ? 1.793   -5.651  47.901  1.00 59.90  ? 138 TRP C CA  1 
ATOM   9300  C C   . TRP C 1 138 ? 2.465   -5.786  46.541  1.00 65.05  ? 138 TRP C C   1 
ATOM   9301  O O   . TRP C 1 138 ? 3.573   -6.330  46.447  1.00 74.02  ? 138 TRP C O   1 
ATOM   9302  C CB  . TRP C 1 138 ? 2.112   -6.865  48.771  1.00 65.17  ? 138 TRP C CB  1 
ATOM   9303  C CG  . TRP C 1 138 ? 1.431   -6.820  50.103  1.00 67.54  ? 138 TRP C CG  1 
ATOM   9304  C CD1 . TRP C 1 138 ? 0.200   -7.311  50.407  1.00 67.33  ? 138 TRP C CD1 1 
ATOM   9305  C CD2 . TRP C 1 138 ? 1.943   -6.247  51.310  1.00 64.68  ? 138 TRP C CD2 1 
ATOM   9306  N NE1 . TRP C 1 138 ? -0.091  -7.084  51.729  1.00 69.73  ? 138 TRP C NE1 1 
ATOM   9307  C CE2 . TRP C 1 138 ? 0.965   -6.431  52.307  1.00 66.50  ? 138 TRP C CE2 1 
ATOM   9308  C CE3 . TRP C 1 138 ? 3.133   -5.598  51.646  1.00 67.95  ? 138 TRP C CE3 1 
ATOM   9309  C CZ2 . TRP C 1 138 ? 1.141   -5.989  53.615  1.00 70.35  ? 138 TRP C CZ2 1 
ATOM   9310  C CZ3 . TRP C 1 138 ? 3.305   -5.158  52.945  1.00 75.59  ? 138 TRP C CZ3 1 
ATOM   9311  C CH2 . TRP C 1 138 ? 2.316   -5.356  53.914  1.00 67.69  ? 138 TRP C CH2 1 
ATOM   9312  N N   . CYS C 1 139 ? 1.824   -5.290  45.492  1.00 67.06  ? 139 CYS C N   1 
ATOM   9313  C CA  . CYS C 1 139 ? 2.369   -5.432  44.153  1.00 71.09  ? 139 CYS C CA  1 
ATOM   9314  C C   . CYS C 1 139 ? 3.576   -4.522  43.950  1.00 67.53  ? 139 CYS C C   1 
ATOM   9315  O O   . CYS C 1 139 ? 3.497   -3.310  44.176  1.00 67.95  ? 139 CYS C O   1 
ATOM   9316  C CB  . CYS C 1 139 ? 1.297   -5.123  43.118  1.00 64.96  ? 139 CYS C CB  1 
ATOM   9317  S SG  . CYS C 1 139 ? 1.661   -5.957  41.595  1.00 71.46  ? 139 CYS C SG  1 
ATOM   9318  N N   . GLY C 1 140 ? 4.688   -5.108  43.498  1.00 63.47  ? 140 GLY C N   1 
ATOM   9319  C CA  . GLY C 1 140 ? 5.889   -4.345  43.238  1.00 64.42  ? 140 GLY C CA  1 
ATOM   9320  C C   . GLY C 1 140 ? 5.861   -3.641  41.896  1.00 61.63  ? 140 GLY C C   1 
ATOM   9321  O O   . GLY C 1 140 ? 5.033   -3.936  41.037  1.00 73.20  ? 140 GLY C O   1 
ATOM   9322  N N   . ARG C 1 141 ? 6.816   -2.719  41.725  1.00 62.53  ? 141 ARG C N   1 
ATOM   9323  C CA  . ARG C 1 141 ? 6.802   -1.803  40.585  1.00 64.93  ? 141 ARG C CA  1 
ATOM   9324  C C   . ARG C 1 141 ? 6.707   -2.544  39.257  1.00 71.19  ? 141 ARG C C   1 
ATOM   9325  O O   . ARG C 1 141 ? 5.912   -2.177  38.385  1.00 66.91  ? 141 ARG C O   1 
ATOM   9326  C CB  . ARG C 1 141 ? 8.049   -0.917  40.601  1.00 58.19  ? 141 ARG C CB  1 
ATOM   9327  C CG  . ARG C 1 141 ? 8.009   0.242   39.614  1.00 66.64  ? 141 ARG C CG  1 
ATOM   9328  C CD  . ARG C 1 141 ? 9.092   1.247   39.948  1.00 58.46  ? 141 ARG C CD  1 
ATOM   9329  N NE  . ARG C 1 141 ? 10.397  0.681   39.638  1.00 62.14  ? 141 ARG C NE  1 
ATOM   9330  C CZ  . ARG C 1 141 ? 11.102  0.944   38.548  1.00 61.10  ? 141 ARG C CZ  1 
ATOM   9331  N NH1 . ARG C 1 141 ? 10.715  1.859   37.676  1.00 68.02  ? 141 ARG C NH1 1 
ATOM   9332  N NH2 . ARG C 1 141 ? 12.227  0.272   38.330  1.00 64.57  ? 141 ARG C NH2 1 
ATOM   9333  N N   . THR C 1 142 ? 7.519   -3.591  39.088  1.00 65.33  ? 142 THR C N   1 
ATOM   9334  C CA  . THR C 1 142 ? 7.512   -4.341  37.837  1.00 68.00  ? 142 THR C CA  1 
ATOM   9335  C C   . THR C 1 142 ? 6.129   -4.896  37.537  1.00 67.67  ? 142 THR C C   1 
ATOM   9336  O O   . THR C 1 142 ? 5.610   -4.742  36.426  1.00 77.22  ? 142 THR C O   1 
ATOM   9337  C CB  . THR C 1 142 ? 8.524   -5.483  37.902  1.00 71.68  ? 142 THR C CB  1 
ATOM   9338  O OG1 . THR C 1 142 ? 9.841   -4.948  38.078  1.00 79.26  ? 142 THR C OG1 1 
ATOM   9339  C CG2 . THR C 1 142 ? 8.474   -6.302  36.616  1.00 63.91  ? 142 THR C CG2 1 
ATOM   9340  N N   . LEU C 1 143 ? 5.515   -5.550  38.521  1.00 65.15  ? 143 LEU C N   1 
ATOM   9341  C CA  . LEU C 1 143 ? 4.271   -6.254  38.256  1.00 73.18  ? 143 LEU C CA  1 
ATOM   9342  C C   . LEU C 1 143 ? 3.060   -5.332  38.200  1.00 75.95  ? 143 LEU C C   1 
ATOM   9343  O O   . LEU C 1 143 ? 2.031   -5.734  37.644  1.00 72.95  ? 143 LEU C O   1 
ATOM   9344  C CB  . LEU C 1 143 ? 4.056   -7.361  39.290  1.00 66.54  ? 143 LEU C CB  1 
ATOM   9345  C CG  . LEU C 1 143 ? 4.694   -8.706  38.914  1.00 69.32  ? 143 LEU C CG  1 
ATOM   9346  C CD1 . LEU C 1 143 ? 3.997   -9.857  39.618  1.00 61.02  ? 143 LEU C CD1 1 
ATOM   9347  C CD2 . LEU C 1 143 ? 4.714   -8.936  37.399  1.00 74.48  ? 143 LEU C CD2 1 
ATOM   9348  N N   . ARG C 1 144 ? 3.151   -4.108  38.738  1.00 66.20  ? 144 ARG C N   1 
ATOM   9349  C CA  . ARG C 1 144 ? 2.054   -3.163  38.543  1.00 72.55  ? 144 ARG C CA  1 
ATOM   9350  C C   . ARG C 1 144 ? 1.881   -2.823  37.069  1.00 69.06  ? 144 ARG C C   1 
ATOM   9351  O O   . ARG C 1 144 ? 0.763   -2.548  36.620  1.00 72.01  ? 144 ARG C O   1 
ATOM   9352  C CB  . ARG C 1 144 ? 2.276   -1.876  39.342  1.00 70.01  ? 144 ARG C CB  1 
ATOM   9353  C CG  . ARG C 1 144 ? 2.644   -2.068  40.794  1.00 63.65  ? 144 ARG C CG  1 
ATOM   9354  C CD  . ARG C 1 144 ? 2.480   -0.766  41.559  1.00 62.62  ? 144 ARG C CD  1 
ATOM   9355  N NE  . ARG C 1 144 ? 1.625   -0.896  42.732  1.00 68.30  ? 144 ARG C NE  1 
ATOM   9356  C CZ  . ARG C 1 144 ? 1.334   0.101   43.557  1.00 72.70  ? 144 ARG C CZ  1 
ATOM   9357  N NH1 . ARG C 1 144 ? 1.758   1.335   43.328  1.00 76.16  ? 144 ARG C NH1 1 
ATOM   9358  N NH2 . ARG C 1 144 ? 0.591   -0.144  44.633  1.00 75.94  ? 144 ARG C NH2 1 
ATOM   9359  N N   . LYS C 1 145 ? 2.973   -2.842  36.302  1.00 70.64  ? 145 LYS C N   1 
ATOM   9360  C CA  . LYS C 1 145 ? 2.872   -2.578  34.872  1.00 77.31  ? 145 LYS C CA  1 
ATOM   9361  C C   . LYS C 1 145 ? 2.281   -3.770  34.129  1.00 80.13  ? 145 LYS C C   1 
ATOM   9362  O O   . LYS C 1 145 ? 1.501   -3.596  33.184  1.00 76.69  ? 145 LYS C O   1 
ATOM   9363  C CB  . LYS C 1 145 ? 4.246   -2.222  34.310  1.00 70.96  ? 145 LYS C CB  1 
ATOM   9364  C CG  . LYS C 1 145 ? 4.974   -1.175  35.135  1.00 69.78  ? 145 LYS C CG  1 
ATOM   9365  C CD  . LYS C 1 145 ? 6.230   -0.666  34.442  1.00 75.28  ? 145 LYS C CD  1 
ATOM   9366  C CE  . LYS C 1 145 ? 7.438   -1.572  34.663  1.00 81.05  ? 145 LYS C CE  1 
ATOM   9367  N NZ  . LYS C 1 145 ? 7.301   -2.920  34.042  1.00 92.61  ? 145 LYS C NZ  1 
ATOM   9368  N N   . ASP C 1 146 ? 2.634   -4.988  34.545  1.00 79.31  ? 146 ASP C N   1 
ATOM   9369  C CA  . ASP C 1 146 ? 2.183   -6.183  33.846  1.00 78.03  ? 146 ASP C CA  1 
ATOM   9370  C C   . ASP C 1 146 ? 0.784   -6.613  34.259  1.00 78.55  ? 146 ASP C C   1 
ATOM   9371  O O   . ASP C 1 146 ? 0.108   -7.298  33.483  1.00 85.77  ? 146 ASP C O   1 
ATOM   9372  C CB  . ASP C 1 146 ? 3.163   -7.335  34.083  1.00 88.42  ? 146 ASP C CB  1 
ATOM   9373  C CG  . ASP C 1 146 ? 4.403   -7.240  33.208  1.00 101.58 ? 146 ASP C CG  1 
ATOM   9374  O OD1 . ASP C 1 146 ? 4.862   -6.108  32.945  1.00 103.81 ? 146 ASP C OD1 1 
ATOM   9375  O OD2 . ASP C 1 146 ? 4.922   -8.296  32.784  1.00 109.34 ? 146 ASP C OD2 1 
ATOM   9376  N N   . LEU C 1 147 ? 0.332   -6.228  35.448  1.00 78.14  ? 147 LEU C N   1 
ATOM   9377  C CA  . LEU C 1 147 ? -0.996  -6.564  35.944  1.00 72.49  ? 147 LEU C CA  1 
ATOM   9378  C C   . LEU C 1 147 ? -1.826  -5.311  36.171  1.00 71.21  ? 147 LEU C C   1 
ATOM   9379  O O   . LEU C 1 147 ? -2.551  -5.197  37.159  1.00 76.00  ? 147 LEU C O   1 
ATOM   9380  C CB  . LEU C 1 147 ? -0.918  -7.377  37.233  1.00 79.59  ? 147 LEU C CB  1 
ATOM   9381  C CG  . LEU C 1 147 ? 0.125   -8.487  37.279  1.00 87.22  ? 147 LEU C CG  1 
ATOM   9382  C CD1 . LEU C 1 147 ? 0.210   -9.084  38.683  1.00 77.33  ? 147 LEU C CD1 1 
ATOM   9383  C CD2 . LEU C 1 147 ? -0.212  -9.543  36.236  1.00 83.44  ? 147 LEU C CD2 1 
ATOM   9384  N N   . LYS C 1 148 ? -1.720  -4.347  35.257  1.00 74.04  ? 148 LYS C N   1 
ATOM   9385  C CA  . LYS C 1 148 ? -2.560  -3.159  35.344  1.00 78.54  ? 148 LYS C CA  1 
ATOM   9386  C C   . LYS C 1 148 ? -4.030  -3.499  35.121  1.00 87.81  ? 148 LYS C C   1 
ATOM   9387  O O   . LYS C 1 148 ? -4.909  -2.855  35.707  1.00 93.80  ? 148 LYS C O   1 
ATOM   9388  C CB  . LYS C 1 148 ? -2.097  -2.114  34.330  1.00 74.48  ? 148 LYS C CB  1 
ATOM   9389  C CG  . LYS C 1 148 ? -2.686  -0.731  34.541  1.00 72.31  ? 148 LYS C CG  1 
ATOM   9390  C CD  . LYS C 1 148 ? -2.449  0.182   33.342  1.00 82.73  ? 148 LYS C CD  1 
ATOM   9391  C CE  . LYS C 1 148 ? -1.213  -0.199  32.534  1.00 77.85  ? 148 LYS C CE  1 
ATOM   9392  N NZ  . LYS C 1 148 ? 0.064   0.073   33.252  1.00 74.42  ? 148 LYS C NZ  1 
ATOM   9393  N N   . ASP C 1 149 ? -4.313  -4.507  34.290  1.00 86.55  ? 149 ASP C N   1 
ATOM   9394  C CA  . ASP C 1 149 ? -5.693  -4.908  34.034  1.00 90.87  ? 149 ASP C CA  1 
ATOM   9395  C C   . ASP C 1 149 ? -6.394  -5.324  35.325  1.00 92.30  ? 149 ASP C C   1 
ATOM   9396  O O   . ASP C 1 149 ? -7.373  -4.696  35.746  1.00 95.11  ? 149 ASP C O   1 
ATOM   9397  C CB  . ASP C 1 149 ? -5.729  -6.040  33.002  1.00 95.52  ? 149 ASP C CB  1 
ATOM   9398  C CG  . ASP C 1 149 ? -4.810  -7.197  33.364  1.00 101.08 ? 149 ASP C CG  1 
ATOM   9399  O OD1 . ASP C 1 149 ? -3.951  -7.028  34.256  1.00 99.92  ? 149 ASP C OD1 1 
ATOM   9400  O OD2 . ASP C 1 149 ? -4.959  -8.284  32.768  1.00 108.33 ? 149 ASP C OD2 1 
ATOM   9401  N N   . LEU C 1 150 ? -5.894  -6.380  35.976  1.00 89.50  ? 150 LEU C N   1 
ATOM   9402  C CA  . LEU C 1 150 ? -6.508  -6.853  37.212  1.00 83.53  ? 150 LEU C CA  1 
ATOM   9403  C C   . LEU C 1 150 ? -6.505  -5.780  38.290  1.00 85.21  ? 150 LEU C C   1 
ATOM   9404  O O   . LEU C 1 150 ? -7.435  -5.717  39.100  1.00 89.26  ? 150 LEU C O   1 
ATOM   9405  C CB  . LEU C 1 150 ? -5.784  -8.103  37.713  1.00 76.32  ? 150 LEU C CB  1 
ATOM   9406  C CG  . LEU C 1 150 ? -5.844  -9.334  36.808  1.00 81.96  ? 150 LEU C CG  1 
ATOM   9407  C CD1 . LEU C 1 150 ? -4.965  -10.426 37.384  1.00 69.16  ? 150 LEU C CD1 1 
ATOM   9408  C CD2 . LEU C 1 150 ? -7.285  -9.826  36.604  1.00 91.70  ? 150 LEU C CD2 1 
ATOM   9409  N N   . LEU C 1 151 ? -5.482  -4.923  38.307  1.00 85.46  ? 151 LEU C N   1 
ATOM   9410  C CA  . LEU C 1 151 ? -5.377  -3.901  39.344  1.00 89.15  ? 151 LEU C CA  1 
ATOM   9411  C C   . LEU C 1 151 ? -6.508  -2.885  39.239  1.00 97.14  ? 151 LEU C C   1 
ATOM   9412  O O   . LEU C 1 151 ? -7.138  -2.538  40.245  1.00 95.88  ? 151 LEU C O   1 
ATOM   9413  C CB  . LEU C 1 151 ? -4.016  -3.212  39.251  1.00 79.94  ? 151 LEU C CB  1 
ATOM   9414  C CG  . LEU C 1 151 ? -2.935  -3.783  40.171  1.00 74.73  ? 151 LEU C CG  1 
ATOM   9415  C CD1 . LEU C 1 151 ? -1.543  -3.325  39.741  1.00 62.71  ? 151 LEU C CD1 1 
ATOM   9416  C CD2 . LEU C 1 151 ? -3.214  -3.425  41.630  1.00 71.22  ? 151 LEU C CD2 1 
ATOM   9417  N N   . ASN C 1 152 ? -6.783  -2.393  38.028  1.00 95.00  ? 152 ASN C N   1 
ATOM   9418  C CA  . ASN C 1 152 ? -7.812  -1.376  37.855  1.00 94.97  ? 152 ASN C CA  1 
ATOM   9419  C C   . ASN C 1 152 ? -9.223  -1.948  37.917  1.00 92.56  ? 152 ASN C C   1 
ATOM   9420  O O   . ASN C 1 152 ? -10.172 -1.194  38.163  1.00 92.57  ? 152 ASN C O   1 
ATOM   9421  C CB  . ASN C 1 152 ? -7.599  -0.639  36.532  1.00 100.00 ? 152 ASN C CB  1 
ATOM   9422  C CG  . ASN C 1 152 ? -6.945  0.721   36.722  1.00 100.18 ? 152 ASN C CG  1 
ATOM   9423  O OD1 . ASN C 1 152 ? -7.619  1.716   36.993  1.00 104.83 ? 152 ASN C OD1 1 
ATOM   9424  N ND2 . ASN C 1 152 ? -5.624  0.765   36.590  1.00 99.98  ? 152 ASN C ND2 1 
ATOM   9425  N N   . LYS C 1 153 ? -9.380  -3.254  37.691  1.00 90.33  ? 153 LYS C N   1 
ATOM   9426  C CA  . LYS C 1 153 ? -10.671 -3.907  37.893  1.00 94.40  ? 153 LYS C CA  1 
ATOM   9427  C C   . LYS C 1 153 ? -11.225 -3.611  39.286  1.00 100.10 ? 153 LYS C C   1 
ATOM   9428  O O   . LYS C 1 153 ? -12.367 -3.158  39.434  1.00 93.22  ? 153 LYS C O   1 
ATOM   9429  C CB  . LYS C 1 153 ? -10.515 -5.413  37.674  1.00 87.22  ? 153 LYS C CB  1 
ATOM   9430  C CG  . LYS C 1 153 ? -11.791 -6.211  37.761  1.00 92.90  ? 153 LYS C CG  1 
ATOM   9431  C CD  . LYS C 1 153 ? -11.492 -7.704  37.751  1.00 90.19  ? 153 LYS C CD  1 
ATOM   9432  C CE  . LYS C 1 153 ? -12.663 -8.492  37.182  1.00 100.67 ? 153 LYS C CE  1 
ATOM   9433  N NZ  . LYS C 1 153 ? -12.429 -9.964  37.180  1.00 99.69  ? 153 LYS C NZ  1 
ATOM   9434  N N   . GLY C 1 154 ? -10.420 -3.866  40.323  1.00 94.80  ? 154 GLY C N   1 
ATOM   9435  C CA  . GLY C 1 154 ? -10.758 -3.518  41.687  1.00 85.98  ? 154 GLY C CA  1 
ATOM   9436  C C   . GLY C 1 154 ? -11.696 -4.465  42.406  1.00 93.23  ? 154 GLY C C   1 
ATOM   9437  O O   . GLY C 1 154 ? -11.688 -4.496  43.642  1.00 91.50  ? 154 GLY C O   1 
ATOM   9438  N N   . ARG C 1 155 ? -12.504 -5.239  41.685  1.00 92.01  ? 155 ARG C N   1 
ATOM   9439  C CA  . ARG C 1 155 ? -13.509 -6.085  42.320  1.00 94.05  ? 155 ARG C CA  1 
ATOM   9440  C C   . ARG C 1 155 ? -13.835 -7.249  41.395  1.00 94.96  ? 155 ARG C C   1 
ATOM   9441  O O   . ARG C 1 155 ? -13.356 -7.320  40.261  1.00 87.63  ? 155 ARG C O   1 
ATOM   9442  C CB  . ARG C 1 155 ? -14.774 -5.284  42.651  1.00 94.84  ? 155 ARG C CB  1 
ATOM   9443  C CG  . ARG C 1 155 ? -15.353 -4.574  41.437  1.00 97.46  ? 155 ARG C CG  1 
ATOM   9444  C CD  . ARG C 1 155 ? -16.557 -3.726  41.789  1.00 90.45  ? 155 ARG C CD  1 
ATOM   9445  N NE  . ARG C 1 155 ? -16.328 -2.926  42.985  1.00 95.27  ? 155 ARG C NE  1 
ATOM   9446  C CZ  . ARG C 1 155 ? -15.607 -1.813  43.017  1.00 96.51  ? 155 ARG C CZ  1 
ATOM   9447  N NH1 . ARG C 1 155 ? -14.992 -1.354  41.937  1.00 94.43  ? 155 ARG C NH1 1 
ATOM   9448  N NH2 . ARG C 1 155 ? -15.505 -1.140  44.158  1.00 93.83  ? 155 ARG C NH2 1 
ATOM   9449  N N   . ASN C 1 156 ? -14.663 -8.166  41.907  1.00 94.05  ? 156 ASN C N   1 
ATOM   9450  C CA  . ASN C 1 156 ? -15.194 -9.293  41.135  1.00 96.48  ? 156 ASN C CA  1 
ATOM   9451  C C   . ASN C 1 156 ? -14.080 -10.156 40.545  1.00 93.24  ? 156 ASN C C   1 
ATOM   9452  O O   . ASN C 1 156 ? -14.133 -10.567 39.384  1.00 99.39  ? 156 ASN C O   1 
ATOM   9453  C CB  . ASN C 1 156 ? -16.147 -8.809  40.040  1.00 97.60  ? 156 ASN C CB  1 
ATOM   9454  C CG  . ASN C 1 156 ? -17.074 -7.714  40.522  1.00 96.49  ? 156 ASN C CG  1 
ATOM   9455  O OD1 . ASN C 1 156 ? -17.115 -6.626  39.951  1.00 97.32  ? 156 ASN C OD1 1 
ATOM   9456  N ND2 . ASN C 1 156 ? -17.819 -7.995  41.583  1.00 94.68  ? 156 ASN C ND2 1 
ATOM   9457  N N   . TYR C 1 157 ? -13.070 -10.448 41.356  1.00 93.22  ? 157 TYR C N   1 
ATOM   9458  C CA  . TYR C 1 157 ? -11.985 -11.313 40.925  1.00 92.96  ? 157 TYR C CA  1 
ATOM   9459  C C   . TYR C 1 157 ? -12.449 -12.766 40.937  1.00 96.24  ? 157 TYR C C   1 
ATOM   9460  O O   . TYR C 1 157 ? -13.577 -13.086 41.321  1.00 98.26  ? 157 TYR C O   1 
ATOM   9461  C CB  . TYR C 1 157 ? -10.760 -11.103 41.810  1.00 84.29  ? 157 TYR C CB  1 
ATOM   9462  C CG  . TYR C 1 157 ? -10.136 -9.749  41.603  1.00 84.19  ? 157 TYR C CG  1 
ATOM   9463  C CD1 . TYR C 1 157 ? -9.354  -9.491  40.487  1.00 85.72  ? 157 TYR C CD1 1 
ATOM   9464  C CD2 . TYR C 1 157 ? -10.352 -8.721  42.509  1.00 76.65  ? 157 TYR C CD2 1 
ATOM   9465  C CE1 . TYR C 1 157 ? -8.794  -8.251  40.287  1.00 86.30  ? 157 TYR C CE1 1 
ATOM   9466  C CE2 . TYR C 1 157 ? -9.796  -7.475  42.316  1.00 78.36  ? 157 TYR C CE2 1 
ATOM   9467  C CZ  . TYR C 1 157 ? -9.017  -7.245  41.203  1.00 87.03  ? 157 TYR C CZ  1 
ATOM   9468  O OH  . TYR C 1 157 ? -8.454  -6.006  40.999  1.00 97.15  ? 157 TYR C OH  1 
ATOM   9469  N N   . THR C 1 158 ? -11.572 -13.658 40.482  1.00 88.97  ? 158 THR C N   1 
ATOM   9470  C CA  . THR C 1 158 ? -11.878 -15.076 40.381  1.00 88.72  ? 158 THR C CA  1 
ATOM   9471  C C   . THR C 1 158 ? -10.748 -15.882 41.014  1.00 80.67  ? 158 THR C C   1 
ATOM   9472  O O   . THR C 1 158 ? -9.684  -15.351 41.345  1.00 73.48  ? 158 THR C O   1 
ATOM   9473  C CB  . THR C 1 158 ? -12.102 -15.499 38.917  1.00 83.24  ? 158 THR C CB  1 
ATOM   9474  O OG1 . THR C 1 158 ? -10.870 -15.975 38.360  1.00 88.82  ? 158 THR C OG1 1 
ATOM   9475  C CG2 . THR C 1 158 ? -12.613 -14.336 38.079  1.00 80.71  ? 158 THR C CG2 1 
ATOM   9476  N N   . GLN C 1 159 ? -11.000 -17.180 41.202  1.00 77.20  ? 159 GLN C N   1 
ATOM   9477  C CA  . GLN C 1 159 ? -9.940  -18.077 41.651  1.00 75.54  ? 159 GLN C CA  1 
ATOM   9478  C C   . GLN C 1 159 ? -8.829  -18.162 40.611  1.00 82.13  ? 159 GLN C C   1 
ATOM   9479  O O   . GLN C 1 159 ? -7.642  -18.161 40.955  1.00 84.11  ? 159 GLN C O   1 
ATOM   9480  C CB  . GLN C 1 159 ? -10.520 -19.462 41.942  1.00 77.39  ? 159 GLN C CB  1 
ATOM   9481  C CG  . GLN C 1 159 ? -9.496  -20.511 42.342  1.00 83.23  ? 159 GLN C CG  1 
ATOM   9482  C CD  . GLN C 1 159 ? -8.972  -20.315 43.748  1.00 77.08  ? 159 GLN C CD  1 
ATOM   9483  O OE1 . GLN C 1 159 ? -9.573  -19.609 44.555  1.00 80.18  ? 159 GLN C OE1 1 
ATOM   9484  N NE2 . GLN C 1 159 ? -7.836  -20.934 44.045  1.00 78.22  ? 159 GLN C NE2 1 
ATOM   9485  N N   . GLU C 1 160 ? -9.201  -18.199 39.329  1.00 85.04  ? 160 GLU C N   1 
ATOM   9486  C CA  . GLU C 1 160 ? -8.225  -18.315 38.247  1.00 80.93  ? 160 GLU C CA  1 
ATOM   9487  C C   . GLU C 1 160 ? -7.373  -17.055 38.121  1.00 83.76  ? 160 GLU C C   1 
ATOM   9488  O O   . GLU C 1 160 ? -6.156  -17.138 37.906  1.00 82.24  ? 160 GLU C O   1 
ATOM   9489  C CB  . GLU C 1 160 ? -8.952  -18.613 36.930  1.00 80.17  ? 160 GLU C CB  1 
ATOM   9490  C CG  . GLU C 1 160 ? -9.953  -19.793 36.964  1.00 88.11  ? 160 GLU C CG  1 
ATOM   9491  C CD  . GLU C 1 160 ? -11.236 -19.507 37.749  1.00 96.78  ? 160 GLU C CD  1 
ATOM   9492  O OE1 . GLU C 1 160 ? -12.154 -20.355 37.729  1.00 100.26 ? 160 GLU C OE1 1 
ATOM   9493  O OE2 . GLU C 1 160 ? -11.319 -18.447 38.405  1.00 95.43  ? 160 GLU C OE2 1 
ATOM   9494  N N   . GLU C 1 161 ? -7.994  -15.878 38.241  1.00 81.23  ? 161 GLU C N   1 
ATOM   9495  C CA  . GLU C 1 161 ? -7.237  -14.626 38.232  1.00 76.01  ? 161 GLU C CA  1 
ATOM   9496  C C   . GLU C 1 161 ? -6.280  -14.555 39.418  1.00 77.63  ? 161 GLU C C   1 
ATOM   9497  O O   . GLU C 1 161 ? -5.097  -14.226 39.260  1.00 78.62  ? 161 GLU C O   1 
ATOM   9498  C CB  . GLU C 1 161 ? -8.201  -13.439 38.244  1.00 74.90  ? 161 GLU C CB  1 
ATOM   9499  C CG  . GLU C 1 161 ? -9.127  -13.403 37.042  1.00 91.64  ? 161 GLU C CG  1 
ATOM   9500  C CD  . GLU C 1 161 ? -9.981  -12.150 36.981  1.00 94.58  ? 161 GLU C CD  1 
ATOM   9501  O OE1 . GLU C 1 161 ? -10.496 -11.717 38.035  1.00 98.96  ? 161 GLU C OE1 1 
ATOM   9502  O OE2 . GLU C 1 161 ? -10.142 -11.602 35.872  1.00 87.11  ? 161 GLU C OE2 1 
ATOM   9503  N N   . LYS C 1 162 ? -6.781  -14.858 40.619  1.00 73.63  ? 162 LYS C N   1 
ATOM   9504  C CA  . LYS C 1 162 ? -5.940  -14.838 41.810  1.00 68.95  ? 162 LYS C CA  1 
ATOM   9505  C C   . LYS C 1 162 ? -4.743  -15.765 41.650  1.00 67.55  ? 162 LYS C C   1 
ATOM   9506  O O   . LYS C 1 162 ? -3.616  -15.400 42.006  1.00 65.55  ? 162 LYS C O   1 
ATOM   9507  C CB  . LYS C 1 162 ? -6.774  -15.225 43.037  1.00 68.38  ? 162 LYS C CB  1 
ATOM   9508  C CG  . LYS C 1 162 ? -6.038  -15.162 44.375  1.00 74.85  ? 162 LYS C CG  1 
ATOM   9509  C CD  . LYS C 1 162 ? -6.854  -15.796 45.505  1.00 69.89  ? 162 LYS C CD  1 
ATOM   9510  C CE  . LYS C 1 162 ? -7.796  -16.885 44.999  1.00 70.51  ? 162 LYS C CE  1 
ATOM   9511  N NZ  . LYS C 1 162 ? -8.277  -17.781 46.089  1.00 69.54  ? 162 LYS C NZ  1 
ATOM   9512  N N   . GLU C 1 163 ? -4.962  -16.963 41.099  1.00 68.12  ? 163 GLU C N   1 
ATOM   9513  C CA  . GLU C 1 163 ? -3.866  -17.914 40.934  1.00 76.01  ? 163 GLU C CA  1 
ATOM   9514  C C   . GLU C 1 163 ? -2.856  -17.437 39.896  1.00 80.58  ? 163 GLU C C   1 
ATOM   9515  O O   . GLU C 1 163 ? -1.662  -17.740 40.010  1.00 73.48  ? 163 GLU C O   1 
ATOM   9516  C CB  . GLU C 1 163 ? -4.419  -19.288 40.560  1.00 69.65  ? 163 GLU C CB  1 
ATOM   9517  C CG  . GLU C 1 163 ? -5.268  -19.922 41.644  1.00 78.55  ? 163 GLU C CG  1 
ATOM   9518  C CD  . GLU C 1 163 ? -5.448  -21.412 41.452  1.00 91.76  ? 163 GLU C CD  1 
ATOM   9519  O OE1 . GLU C 1 163 ? -4.784  -21.983 40.562  1.00 95.22  ? 163 GLU C OE1 1 
ATOM   9520  O OE2 . GLU C 1 163 ? -6.271  -22.011 42.178  1.00 91.01  ? 163 GLU C OE2 1 
ATOM   9521  N N   . TYR C 1 164 ? -3.314  -16.697 38.883  1.00 76.21  ? 164 TYR C N   1 
ATOM   9522  C CA  . TYR C 1 164 ? -2.398  -16.078 37.929  1.00 70.69  ? 164 TYR C CA  1 
ATOM   9523  C C   . TYR C 1 164 ? -1.480  -15.076 38.623  1.00 73.31  ? 164 TYR C C   1 
ATOM   9524  O O   . TYR C 1 164 ? -0.256  -15.108 38.445  1.00 68.93  ? 164 TYR C O   1 
ATOM   9525  C CB  . TYR C 1 164 ? -3.199  -15.404 36.817  1.00 69.68  ? 164 TYR C CB  1 
ATOM   9526  C CG  . TYR C 1 164 ? -2.383  -14.552 35.871  1.00 70.07  ? 164 TYR C CG  1 
ATOM   9527  C CD1 . TYR C 1 164 ? -1.500  -15.135 34.974  1.00 78.54  ? 164 TYR C CD1 1 
ATOM   9528  C CD2 . TYR C 1 164 ? -2.513  -13.169 35.855  1.00 69.04  ? 164 TYR C CD2 1 
ATOM   9529  C CE1 . TYR C 1 164 ? -0.759  -14.367 34.094  1.00 76.59  ? 164 TYR C CE1 1 
ATOM   9530  C CE2 . TYR C 1 164 ? -1.773  -12.390 34.976  1.00 69.24  ? 164 TYR C CE2 1 
ATOM   9531  C CZ  . TYR C 1 164 ? -0.893  -12.997 34.097  1.00 75.07  ? 164 TYR C CZ  1 
ATOM   9532  O OH  . TYR C 1 164 ? -0.142  -12.251 33.212  1.00 69.99  ? 164 TYR C OH  1 
ATOM   9533  N N   . VAL C 1 165 ? -2.064  -14.170 39.416  1.00 74.23  ? 165 VAL C N   1 
ATOM   9534  C CA  . VAL C 1 165 ? -1.277  -13.234 40.221  1.00 74.33  ? 165 VAL C CA  1 
ATOM   9535  C C   . VAL C 1 165 ? -0.282  -13.983 41.094  1.00 68.18  ? 165 VAL C C   1 
ATOM   9536  O O   . VAL C 1 165 ? 0.883   -13.586 41.219  1.00 72.91  ? 165 VAL C O   1 
ATOM   9537  C CB  . VAL C 1 165 ? -2.207  -12.347 41.072  1.00 75.73  ? 165 VAL C CB  1 
ATOM   9538  C CG1 . VAL C 1 165 ? -1.456  -11.774 42.271  1.00 65.66  ? 165 VAL C CG1 1 
ATOM   9539  C CG2 . VAL C 1 165 ? -2.817  -11.242 40.224  1.00 78.62  ? 165 VAL C CG2 1 
ATOM   9540  N N   . LEU C 1 166 ? -0.731  -15.074 41.720  1.00 65.16  ? 166 LEU C N   1 
ATOM   9541  C CA  . LEU C 1 166 ? 0.143   -15.862 42.584  1.00 66.67  ? 166 LEU C CA  1 
ATOM   9542  C C   . LEU C 1 166 ? 1.349   -16.395 41.820  1.00 65.84  ? 166 LEU C C   1 
ATOM   9543  O O   . LEU C 1 166 ? 2.490   -16.254 42.271  1.00 69.56  ? 166 LEU C O   1 
ATOM   9544  C CB  . LEU C 1 166 ? -0.646  -17.008 43.213  1.00 66.63  ? 166 LEU C CB  1 
ATOM   9545  C CG  . LEU C 1 166 ? -1.468  -16.634 44.442  1.00 70.58  ? 166 LEU C CG  1 
ATOM   9546  C CD1 . LEU C 1 166 ? -2.579  -17.653 44.667  1.00 69.18  ? 166 LEU C CD1 1 
ATOM   9547  C CD2 . LEU C 1 166 ? -0.552  -16.528 45.667  1.00 59.34  ? 166 LEU C CD2 1 
ATOM   9548  N N   . ASN C 1 167 ? 1.116   -17.004 40.653  1.00 68.42  ? 167 ASN C N   1 
ATOM   9549  C CA  . ASN C 1 167 ? 2.224   -17.514 39.851  1.00 69.27  ? 167 ASN C CA  1 
ATOM   9550  C C   . ASN C 1 167 ? 3.124   -16.393 39.353  1.00 71.46  ? 167 ASN C C   1 
ATOM   9551  O O   . ASN C 1 167 ? 4.340   -16.588 39.231  1.00 69.58  ? 167 ASN C O   1 
ATOM   9552  C CB  . ASN C 1 167 ? 1.693   -18.326 38.677  1.00 71.59  ? 167 ASN C CB  1 
ATOM   9553  C CG  . ASN C 1 167 ? 1.216   -19.693 39.101  1.00 85.00  ? 167 ASN C CG  1 
ATOM   9554  O OD1 . ASN C 1 167 ? 0.020   -19.987 39.070  1.00 81.89  ? 167 ASN C OD1 1 
ATOM   9555  N ND2 . ASN C 1 167 ? 2.148   -20.528 39.540  1.00 89.40  ? 167 ASN C ND2 1 
ATOM   9556  N N   . LYS C 1 168 ? 2.551   -15.223 39.056  1.00 69.74  ? 168 LYS C N   1 
ATOM   9557  C CA  . LYS C 1 168 ? 3.368   -14.055 38.746  1.00 66.68  ? 168 LYS C CA  1 
ATOM   9558  C C   . LYS C 1 168 ? 4.222   -13.653 39.941  1.00 67.98  ? 168 LYS C C   1 
ATOM   9559  O O   . LYS C 1 168 ? 5.419   -13.375 39.797  1.00 75.29  ? 168 LYS C O   1 
ATOM   9560  C CB  . LYS C 1 168 ? 2.480   -12.886 38.315  1.00 73.13  ? 168 LYS C CB  1 
ATOM   9561  C CG  . LYS C 1 168 ? 2.005   -12.956 36.875  1.00 71.76  ? 168 LYS C CG  1 
ATOM   9562  C CD  . LYS C 1 168 ? 3.110   -13.462 35.967  1.00 73.06  ? 168 LYS C CD  1 
ATOM   9563  C CE  . LYS C 1 168 ? 2.535   -14.318 34.859  1.00 81.60  ? 168 LYS C CE  1 
ATOM   9564  N NZ  . LYS C 1 168 ? 2.166   -15.668 35.373  1.00 76.65  ? 168 LYS C NZ  1 
ATOM   9565  N N   . TYR C 1 169 ? 3.622   -13.619 41.130  1.00 63.64  ? 169 TYR C N   1 
ATOM   9566  C CA  . TYR C 1 169 ? 4.374   -13.275 42.328  1.00 59.68  ? 169 TYR C CA  1 
ATOM   9567  C C   . TYR C 1 169 ? 5.512   -14.263 42.564  1.00 67.62  ? 169 TYR C C   1 
ATOM   9568  O O   . TYR C 1 169 ? 6.630   -13.860 42.908  1.00 71.02  ? 169 TYR C O   1 
ATOM   9569  C CB  . TYR C 1 169 ? 3.432   -13.224 43.534  1.00 64.14  ? 169 TYR C CB  1 
ATOM   9570  C CG  . TYR C 1 169 ? 2.675   -11.919 43.675  1.00 68.92  ? 169 TYR C CG  1 
ATOM   9571  C CD1 . TYR C 1 169 ? 2.721   -10.955 42.678  1.00 68.62  ? 169 TYR C CD1 1 
ATOM   9572  C CD2 . TYR C 1 169 ? 1.924   -11.645 44.811  1.00 66.41  ? 169 TYR C CD2 1 
ATOM   9573  C CE1 . TYR C 1 169 ? 2.037   -9.760  42.802  1.00 64.46  ? 169 TYR C CE1 1 
ATOM   9574  C CE2 . TYR C 1 169 ? 1.236   -10.448 44.944  1.00 60.11  ? 169 TYR C CE2 1 
ATOM   9575  C CZ  . TYR C 1 169 ? 1.298   -9.509  43.935  1.00 60.91  ? 169 TYR C CZ  1 
ATOM   9576  O OH  . TYR C 1 169 ? 0.626   -8.312  44.045  1.00 60.52  ? 169 TYR C OH  1 
ATOM   9577  N N   . PHE C 1 170 ? 5.255   -15.563 42.369  1.00 68.30  ? 170 PHE C N   1 
ATOM   9578  C CA  . PHE C 1 170 ? 6.272   -16.566 42.680  1.00 70.93  ? 170 PHE C CA  1 
ATOM   9579  C C   . PHE C 1 170 ? 7.407   -16.543 41.669  1.00 71.47  ? 170 PHE C C   1 
ATOM   9580  O O   . PHE C 1 170 ? 8.552   -16.861 42.013  1.00 65.48  ? 170 PHE C O   1 
ATOM   9581  C CB  . PHE C 1 170 ? 5.653   -17.966 42.755  1.00 66.22  ? 170 PHE C CB  1 
ATOM   9582  C CG  . PHE C 1 170 ? 5.088   -18.310 44.114  1.00 77.99  ? 170 PHE C CG  1 
ATOM   9583  C CD1 . PHE C 1 170 ? 3.852   -17.822 44.517  1.00 69.62  ? 170 PHE C CD1 1 
ATOM   9584  C CD2 . PHE C 1 170 ? 5.807   -19.104 45.001  1.00 85.05  ? 170 PHE C CD2 1 
ATOM   9585  C CE1 . PHE C 1 170 ? 3.335   -18.133 45.771  1.00 74.80  ? 170 PHE C CE1 1 
ATOM   9586  C CE2 . PHE C 1 170 ? 5.295   -19.415 46.260  1.00 82.82  ? 170 PHE C CE2 1 
ATOM   9587  C CZ  . PHE C 1 170 ? 4.057   -18.927 46.642  1.00 78.79  ? 170 PHE C CZ  1 
ATOM   9588  N N   . GLU C 1 171 ? 7.111   -16.161 40.428  1.00 71.04  ? 171 GLU C N   1 
ATOM   9589  C CA  . GLU C 1 171 ? 8.170   -15.991 39.444  1.00 71.86  ? 171 GLU C CA  1 
ATOM   9590  C C   . GLU C 1 171 ? 9.135   -14.889 39.865  1.00 75.53  ? 171 GLU C C   1 
ATOM   9591  O O   . GLU C 1 171 ? 10.349  -14.997 39.645  1.00 74.28  ? 171 GLU C O   1 
ATOM   9592  C CB  . GLU C 1 171 ? 7.563   -15.698 38.075  1.00 70.17  ? 171 GLU C CB  1 
ATOM   9593  C CG  . GLU C 1 171 ? 7.329   -16.951 37.242  1.00 88.12  ? 171 GLU C CG  1 
ATOM   9594  C CD  . GLU C 1 171 ? 8.460   -17.973 37.369  1.00 101.49 ? 171 GLU C CD  1 
ATOM   9595  O OE1 . GLU C 1 171 ? 9.452   -17.876 36.611  1.00 95.44  ? 171 GLU C OE1 1 
ATOM   9596  O OE2 . GLU C 1 171 ? 8.343   -18.892 38.208  1.00 99.84  ? 171 GLU C OE2 1 
ATOM   9597  N N   . ILE C 1 172 ? 8.613   -13.832 40.490  1.00 65.75  ? 172 ILE C N   1 
ATOM   9598  C CA  . ILE C 1 172 ? 9.466   -12.763 41.001  1.00 66.96  ? 172 ILE C CA  1 
ATOM   9599  C C   . ILE C 1 172 ? 10.418  -13.303 42.059  1.00 68.83  ? 172 ILE C C   1 
ATOM   9600  O O   . ILE C 1 172 ? 11.609  -12.960 42.081  1.00 65.64  ? 172 ILE C O   1 
ATOM   9601  C CB  . ILE C 1 172 ? 8.594   -11.622 41.550  1.00 61.86  ? 172 ILE C CB  1 
ATOM   9602  C CG1 . ILE C 1 172 ? 8.199   -10.678 40.425  1.00 60.79  ? 172 ILE C CG1 1 
ATOM   9603  C CG2 . ILE C 1 172 ? 9.312   -10.862 42.657  1.00 62.32  ? 172 ILE C CG2 1 
ATOM   9604  C CD1 . ILE C 1 172 ? 7.392   -9.514  40.914  1.00 67.76  ? 172 ILE C CD1 1 
ATOM   9605  N N   . ILE C 1 173 ? 9.908   -14.159 42.947  1.00 65.03  ? 173 ILE C N   1 
ATOM   9606  C CA  . ILE C 1 173 ? 10.734  -14.746 43.999  1.00 62.18  ? 173 ILE C CA  1 
ATOM   9607  C C   . ILE C 1 173 ? 11.843  -15.603 43.394  1.00 66.38  ? 173 ILE C C   1 
ATOM   9608  O O   . ILE C 1 173 ? 13.018  -15.488 43.768  1.00 71.57  ? 173 ILE C O   1 
ATOM   9609  C CB  . ILE C 1 173 ? 9.855   -15.555 44.972  1.00 65.80  ? 173 ILE C CB  1 
ATOM   9610  C CG1 . ILE C 1 173 ? 8.900   -14.626 45.739  1.00 63.24  ? 173 ILE C CG1 1 
ATOM   9611  C CG2 . ILE C 1 173 ? 10.726  -16.363 45.926  1.00 60.19  ? 173 ILE C CG2 1 
ATOM   9612  C CD1 . ILE C 1 173 ? 7.542   -15.244 46.062  1.00 56.59  ? 173 ILE C CD1 1 
ATOM   9613  N N   . LYS C 1 174 ? 11.488  -16.471 42.438  1.00 69.88  ? 174 LYS C N   1 
ATOM   9614  C CA  . LYS C 1 174 ? 12.481  -17.328 41.791  1.00 67.41  ? 174 LYS C CA  1 
ATOM   9615  C C   . LYS C 1 174 ? 13.526  -16.538 41.013  1.00 66.71  ? 174 LYS C C   1 
ATOM   9616  O O   . LYS C 1 174 ? 14.621  -17.055 40.770  1.00 69.59  ? 174 LYS C O   1 
ATOM   9617  C CB  . LYS C 1 174 ? 11.792  -18.333 40.864  1.00 72.60  ? 174 LYS C CB  1 
ATOM   9618  C CG  . LYS C 1 174 ? 10.805  -19.233 41.579  1.00 76.83  ? 174 LYS C CG  1 
ATOM   9619  C CD  . LYS C 1 174 ? 9.995   -20.113 40.629  1.00 83.86  ? 174 LYS C CD  1 
ATOM   9620  C CE  . LYS C 1 174 ? 10.765  -20.567 39.399  1.00 81.46  ? 174 LYS C CE  1 
ATOM   9621  N NZ  . LYS C 1 174 ? 12.089  -21.147 39.747  1.00 84.02  ? 174 LYS C NZ  1 
ATOM   9622  N N   . LYS C 1 175 ? 13.220  -15.304 40.622  1.00 67.77  ? 175 LYS C N   1 
ATOM   9623  C CA  . LYS C 1 175 ? 14.169  -14.443 39.930  1.00 66.23  ? 175 LYS C CA  1 
ATOM   9624  C C   . LYS C 1 175 ? 14.816  -13.424 40.854  1.00 67.49  ? 175 LYS C C   1 
ATOM   9625  O O   . LYS C 1 175 ? 15.707  -12.688 40.415  1.00 66.32  ? 175 LYS C O   1 
ATOM   9626  C CB  . LYS C 1 175 ? 13.478  -13.718 38.771  1.00 69.75  ? 175 LYS C CB  1 
ATOM   9627  C CG  . LYS C 1 175 ? 13.411  -14.514 37.476  1.00 67.67  ? 175 LYS C CG  1 
ATOM   9628  C CD  . LYS C 1 175 ? 14.641  -14.255 36.605  1.00 87.72  ? 175 LYS C CD  1 
ATOM   9629  C CE  . LYS C 1 175 ? 14.269  -13.991 35.145  1.00 87.83  ? 175 LYS C CE  1 
ATOM   9630  N NZ  . LYS C 1 175 ? 15.295  -14.483 34.169  1.00 78.56  ? 175 LYS C NZ  1 
ATOM   9631  N N   . THR C 1 176 ? 14.398  -13.380 42.124  1.00 68.33  ? 176 THR C N   1 
ATOM   9632  C CA  . THR C 1 176 ? 14.810  -12.302 43.018  1.00 58.16  ? 176 THR C CA  1 
ATOM   9633  C C   . THR C 1 176 ? 16.294  -12.382 43.334  1.00 61.17  ? 176 THR C C   1 
ATOM   9634  O O   . THR C 1 176 ? 17.014  -11.382 43.234  1.00 64.19  ? 176 THR C O   1 
ATOM   9635  C CB  . THR C 1 176 ? 13.984  -12.338 44.302  1.00 51.83  ? 176 THR C CB  1 
ATOM   9636  O OG1 . THR C 1 176 ? 12.627  -11.998 43.996  1.00 72.69  ? 176 THR C OG1 1 
ATOM   9637  C CG2 . THR C 1 176 ? 14.519  -11.342 45.313  1.00 52.06  ? 176 THR C CG2 1 
ATOM   9638  N N   . LEU C 1 177 ? 16.777  -13.561 43.724  1.00 60.18  ? 177 LEU C N   1 
ATOM   9639  C CA  . LEU C 1 177 ? 18.186  -13.657 44.084  1.00 66.60  ? 177 LEU C CA  1 
ATOM   9640  C C   . LEU C 1 177 ? 19.101  -13.464 42.879  1.00 66.63  ? 177 LEU C C   1 
ATOM   9641  O O   . LEU C 1 177 ? 20.265  -13.090 43.054  1.00 65.83  ? 177 LEU C O   1 
ATOM   9642  C CB  . LEU C 1 177 ? 18.474  -14.996 44.770  1.00 61.86  ? 177 LEU C CB  1 
ATOM   9643  C CG  . LEU C 1 177 ? 17.844  -15.140 46.163  1.00 61.23  ? 177 LEU C CG  1 
ATOM   9644  C CD1 . LEU C 1 177 ? 18.261  -16.425 46.863  1.00 55.25  ? 177 LEU C CD1 1 
ATOM   9645  C CD2 . LEU C 1 177 ? 18.187  -13.944 47.028  1.00 59.11  ? 177 LEU C CD2 1 
ATOM   9646  N N   . SER C 1 178 ? 18.594  -13.675 41.664  1.00 65.41  ? 178 SER C N   1 
ATOM   9647  C CA  . SER C 1 178 ? 19.434  -13.512 40.484  1.00 69.45  ? 178 SER C CA  1 
ATOM   9648  C C   . SER C 1 178 ? 19.695  -12.045 40.185  1.00 68.90  ? 178 SER C C   1 
ATOM   9649  O O   . SER C 1 178 ? 20.765  -11.698 39.665  1.00 61.48  ? 178 SER C O   1 
ATOM   9650  C CB  . SER C 1 178 ? 18.776  -14.184 39.286  1.00 69.07  ? 178 SER C CB  1 
ATOM   9651  O OG  . SER C 1 178 ? 18.021  -15.298 39.722  1.00 71.85  ? 178 SER C OG  1 
ATOM   9652  N N   . ILE C 1 179 ? 18.731  -11.174 40.497  1.00 62.37  ? 179 ILE C N   1 
ATOM   9653  C CA  . ILE C 1 179 ? 18.907  -9.757  40.207  1.00 65.25  ? 179 ILE C CA  1 
ATOM   9654  C C   . ILE C 1 179 ? 20.062  -9.192  41.015  1.00 64.08  ? 179 ILE C C   1 
ATOM   9655  O O   . ILE C 1 179 ? 20.775  -8.293  40.555  1.00 66.34  ? 179 ILE C O   1 
ATOM   9656  C CB  . ILE C 1 179 ? 17.594  -8.978  40.452  1.00 62.39  ? 179 ILE C CB  1 
ATOM   9657  C CG1 . ILE C 1 179 ? 17.573  -7.703  39.613  1.00 61.35  ? 179 ILE C CG1 1 
ATOM   9658  C CG2 . ILE C 1 179 ? 17.409  -8.620  41.912  1.00 56.76  ? 179 ILE C CG2 1 
ATOM   9659  C CD1 . ILE C 1 179 ? 16.194  -7.262  39.242  1.00 58.01  ? 179 ILE C CD1 1 
ATOM   9660  N N   . TYR C 1 180 ? 20.296  -9.725  42.209  1.00 63.03  ? 180 TYR C N   1 
ATOM   9661  C CA  . TYR C 1 180 ? 21.375  -9.185  43.019  1.00 62.54  ? 180 TYR C CA  1 
ATOM   9662  C C   . TYR C 1 180 ? 22.730  -9.568  42.439  1.00 61.86  ? 180 TYR C C   1 
ATOM   9663  O O   . TYR C 1 180 ? 23.653  -8.744  42.411  1.00 62.55  ? 180 TYR C O   1 
ATOM   9664  C CB  . TYR C 1 180 ? 21.219  -9.660  44.457  1.00 59.33  ? 180 TYR C CB  1 
ATOM   9665  C CG  . TYR C 1 180 ? 20.125  -8.934  45.205  1.00 61.73  ? 180 TYR C CG  1 
ATOM   9666  C CD1 . TYR C 1 180 ? 20.340  -7.665  45.727  1.00 60.75  ? 180 TYR C CD1 1 
ATOM   9667  C CD2 . TYR C 1 180 ? 18.871  -9.509  45.375  1.00 62.24  ? 180 TYR C CD2 1 
ATOM   9668  C CE1 . TYR C 1 180 ? 19.346  -6.996  46.418  1.00 54.70  ? 180 TYR C CE1 1 
ATOM   9669  C CE2 . TYR C 1 180 ? 17.865  -8.842  46.067  1.00 61.06  ? 180 TYR C CE2 1 
ATOM   9670  C CZ  . TYR C 1 180 ? 18.112  -7.583  46.586  1.00 56.81  ? 180 TYR C CZ  1 
ATOM   9671  O OH  . TYR C 1 180 ? 17.135  -6.897  47.275  1.00 55.30  ? 180 TYR C OH  1 
ATOM   9672  N N   . ARG C 1 181 ? 22.866  -10.802 41.948  1.00 57.77  ? 181 ARG C N   1 
ATOM   9673  C CA  . ARG C 1 181 ? 24.101  -11.177 41.268  1.00 61.28  ? 181 ARG C CA  1 
ATOM   9674  C C   . ARG C 1 181 ? 24.325  -10.307 40.038  1.00 64.12  ? 181 ARG C C   1 
ATOM   9675  O O   . ARG C 1 181 ? 25.414  -9.755  39.846  1.00 66.89  ? 181 ARG C O   1 
ATOM   9676  C CB  . ARG C 1 181 ? 24.076  -12.660 40.896  1.00 61.95  ? 181 ARG C CB  1 
ATOM   9677  C CG  . ARG C 1 181 ? 23.195  -13.498 41.797  1.00 61.78  ? 181 ARG C CG  1 
ATOM   9678  C CD  . ARG C 1 181 ? 23.492  -14.982 41.634  1.00 65.90  ? 181 ARG C CD  1 
ATOM   9679  N NE  . ARG C 1 181 ? 22.411  -15.804 42.168  1.00 74.66  ? 181 ARG C NE  1 
ATOM   9680  C CZ  . ARG C 1 181 ? 22.531  -17.080 42.510  1.00 78.89  ? 181 ARG C CZ  1 
ATOM   9681  N NH1 . ARG C 1 181 ? 23.685  -17.719 42.399  1.00 76.72  ? 181 ARG C NH1 1 
ATOM   9682  N NH2 . ARG C 1 181 ? 21.464  -17.732 42.965  1.00 76.00  ? 181 ARG C NH2 1 
ATOM   9683  N N   . GLU C 1 182 ? 23.281  -10.127 39.223  1.00 64.91  ? 182 GLU C N   1 
ATOM   9684  C CA  . GLU C 1 182 ? 23.434  -9.403  37.964  1.00 63.55  ? 182 GLU C CA  1 
ATOM   9685  C C   . GLU C 1 182 ? 23.907  -7.967  38.188  1.00 66.37  ? 182 GLU C C   1 
ATOM   9686  O O   . GLU C 1 182 ? 24.789  -7.484  37.469  1.00 67.76  ? 182 GLU C O   1 
ATOM   9687  C CB  . GLU C 1 182 ? 22.122  -9.448  37.175  1.00 71.90  ? 182 GLU C CB  1 
ATOM   9688  C CG  . GLU C 1 182 ? 21.134  -8.345  37.503  1.00 79.74  ? 182 GLU C CG  1 
ATOM   9689  C CD  . GLU C 1 182 ? 20.167  -8.055  36.376  1.00 93.00  ? 182 GLU C CD  1 
ATOM   9690  O OE1 . GLU C 1 182 ? 20.008  -6.864  36.037  1.00 96.71  ? 182 GLU C OE1 1 
ATOM   9691  O OE2 . GLU C 1 182 ? 19.549  -9.004  35.845  1.00 92.08  ? 182 GLU C OE2 1 
ATOM   9692  N N   . ILE C 1 183 ? 23.361  -7.273  39.192  1.00 63.22  ? 183 ILE C N   1 
ATOM   9693  C CA  . ILE C 1 183 ? 23.784  -5.891  39.404  1.00 63.32  ? 183 ILE C CA  1 
ATOM   9694  C C   . ILE C 1 183 ? 25.188  -5.860  39.981  1.00 60.90  ? 183 ILE C C   1 
ATOM   9695  O O   . ILE C 1 183 ? 25.942  -4.905  39.753  1.00 59.99  ? 183 ILE C O   1 
ATOM   9696  C CB  . ILE C 1 183 ? 22.790  -5.126  40.299  1.00 63.02  ? 183 ILE C CB  1 
ATOM   9697  C CG1 . ILE C 1 183 ? 22.767  -5.714  41.710  1.00 64.73  ? 183 ILE C CG1 1 
ATOM   9698  C CG2 . ILE C 1 183 ? 21.398  -5.121  39.673  1.00 67.07  ? 183 ILE C CG2 1 
ATOM   9699  C CD1 . ILE C 1 183 ? 23.382  -4.801  42.748  1.00 56.23  ? 183 ILE C CD1 1 
ATOM   9700  N N   . LYS C 1 184 ? 25.568  -6.907  40.717  1.00 60.55  ? 184 LYS C N   1 
ATOM   9701  C CA  . LYS C 1 184 ? 26.920  -6.987  41.254  1.00 65.31  ? 184 LYS C CA  1 
ATOM   9702  C C   . LYS C 1 184 ? 27.933  -7.288  40.154  1.00 68.43  ? 184 LYS C C   1 
ATOM   9703  O O   . LYS C 1 184 ? 29.041  -6.740  40.161  1.00 62.74  ? 184 LYS C O   1 
ATOM   9704  C CB  . LYS C 1 184 ? 26.979  -8.043  42.357  1.00 55.17  ? 184 LYS C CB  1 
ATOM   9705  C CG  . LYS C 1 184 ? 28.260  -8.016  43.161  1.00 62.96  ? 184 LYS C CG  1 
ATOM   9706  C CD  . LYS C 1 184 ? 28.347  -9.200  44.110  1.00 67.20  ? 184 LYS C CD  1 
ATOM   9707  C CE  . LYS C 1 184 ? 29.396  -10.206 43.657  1.00 70.82  ? 184 LYS C CE  1 
ATOM   9708  N NZ  . LYS C 1 184 ? 30.766  -9.626  43.599  1.00 80.04  ? 184 LYS C NZ  1 
ATOM   9709  N N   . GLU C 1 185 ? 27.572  -8.142  39.191  1.00 70.69  ? 185 GLU C N   1 
ATOM   9710  C CA  . GLU C 1 185 ? 28.499  -8.460  38.111  1.00 69.50  ? 185 GLU C CA  1 
ATOM   9711  C C   . GLU C 1 185 ? 28.563  -7.377  37.042  1.00 68.59  ? 185 GLU C C   1 
ATOM   9712  O O   . GLU C 1 185 ? 29.541  -7.340  36.288  1.00 75.32  ? 185 GLU C O   1 
ATOM   9713  C CB  . GLU C 1 185 ? 28.138  -9.789  37.440  1.00 68.99  ? 185 GLU C CB  1 
ATOM   9714  C CG  . GLU C 1 185 ? 27.684  -10.930 38.356  1.00 73.44  ? 185 GLU C CG  1 
ATOM   9715  C CD  . GLU C 1 185 ? 28.696  -11.370 39.414  1.00 91.60  ? 185 GLU C CD  1 
ATOM   9716  O OE1 . GLU C 1 185 ? 29.562  -10.575 39.844  1.00 90.67  ? 185 GLU C OE1 1 
ATOM   9717  O OE2 . GLU C 1 185 ? 28.602  -12.542 39.836  1.00 97.54  ? 185 GLU C OE2 1 
ATOM   9718  N N   . GLU C 1 186 ? 27.548  -6.515  36.941  1.00 66.11  ? 186 GLU C N   1 
ATOM   9719  C CA  . GLU C 1 186 ? 27.537  -5.432  35.962  1.00 70.97  ? 186 GLU C CA  1 
ATOM   9720  C C   . GLU C 1 186 ? 27.992  -4.110  36.558  1.00 61.05  ? 186 GLU C C   1 
ATOM   9721  O O   . GLU C 1 186 ? 27.951  -3.082  35.874  1.00 57.44  ? 186 GLU C O   1 
ATOM   9722  C CB  . GLU C 1 186 ? 26.145  -5.275  35.343  1.00 68.59  ? 186 GLU C CB  1 
ATOM   9723  C CG  . GLU C 1 186 ? 25.816  -6.300  34.275  1.00 65.61  ? 186 GLU C CG  1 
ATOM   9724  C CD  . GLU C 1 186 ? 24.328  -6.383  33.999  1.00 93.27  ? 186 GLU C CD  1 
ATOM   9725  O OE1 . GLU C 1 186 ? 23.593  -5.480  34.452  1.00 96.63  ? 186 GLU C OE1 1 
ATOM   9726  O OE2 . GLU C 1 186 ? 23.891  -7.345  33.330  1.00 102.10 ? 186 GLU C OE2 1 
ATOM   9727  N N   . GLY C 1 187 ? 28.412  -4.115  37.819  1.00 54.97  ? 187 GLY C N   1 
ATOM   9728  C CA  . GLY C 1 187 ? 28.975  -2.933  38.422  1.00 54.50  ? 187 GLY C CA  1 
ATOM   9729  C C   . GLY C 1 187 ? 27.973  -1.893  38.846  1.00 56.78  ? 187 GLY C C   1 
ATOM   9730  O O   . GLY C 1 187 ? 28.378  -0.806  39.272  1.00 57.75  ? 187 GLY C O   1 
ATOM   9731  N N   . LYS C 1 188 ? 26.677  -2.187  38.753  1.00 56.82  ? 188 LYS C N   1 
ATOM   9732  C CA  . LYS C 1 188 ? 25.686  -1.203  39.157  1.00 55.73  ? 188 LYS C CA  1 
ATOM   9733  C C   . LYS C 1 188 ? 25.577  -1.085  40.673  1.00 50.80  ? 188 LYS C C   1 
ATOM   9734  O O   . LYS C 1 188 ? 24.986  -0.120  41.163  1.00 53.22  ? 188 LYS C O   1 
ATOM   9735  C CB  . LYS C 1 188 ? 24.332  -1.551  38.539  1.00 57.86  ? 188 LYS C CB  1 
ATOM   9736  C CG  . LYS C 1 188 ? 24.308  -1.427  37.023  1.00 56.49  ? 188 LYS C CG  1 
ATOM   9737  C CD  . LYS C 1 188 ? 23.173  -0.528  36.549  1.00 70.15  ? 188 LYS C CD  1 
ATOM   9738  C CE  . LYS C 1 188 ? 23.581  0.944   36.565  1.00 71.93  ? 188 LYS C CE  1 
ATOM   9739  N NZ  . LYS C 1 188 ? 22.410  1.875   36.590  1.00 71.87  ? 188 LYS C NZ  1 
ATOM   9740  N N   . GLY C 1 189 ? 26.134  -2.027  41.427  1.00 49.91  ? 189 GLY C N   1 
ATOM   9741  C CA  . GLY C 1 189 ? 26.093  -1.915  42.877  1.00 51.89  ? 189 GLY C CA  1 
ATOM   9742  C C   . GLY C 1 189 ? 26.869  -3.033  43.534  1.00 47.85  ? 189 GLY C C   1 
ATOM   9743  O O   . GLY C 1 189 ? 27.249  -4.015  42.893  1.00 58.11  ? 189 GLY C O   1 
ATOM   9744  N N   . SER C 1 190 ? 27.115  -2.865  44.831  1.00 46.59  ? 190 SER C N   1 
ATOM   9745  C CA  . SER C 1 190 ? 27.813  -3.867  45.627  1.00 53.59  ? 190 SER C CA  1 
ATOM   9746  C C   . SER C 1 190 ? 26.836  -4.513  46.601  1.00 57.00  ? 190 SER C C   1 
ATOM   9747  O O   . SER C 1 190 ? 25.902  -3.862  47.080  1.00 58.05  ? 190 SER C O   1 
ATOM   9748  C CB  . SER C 1 190 ? 29.007  -3.269  46.392  1.00 55.90  ? 190 SER C CB  1 
ATOM   9749  O OG  . SER C 1 190 ? 29.925  -2.587  45.544  1.00 53.85  ? 190 SER C OG  1 
ATOM   9750  N N   . VAL C 1 191 ? 27.032  -5.801  46.870  1.00 60.13  ? 191 VAL C N   1 
ATOM   9751  C CA  . VAL C 1 191 ? 26.156  -6.559  47.756  1.00 57.30  ? 191 VAL C CA  1 
ATOM   9752  C C   . VAL C 1 191 ? 26.928  -6.925  49.012  1.00 53.23  ? 191 VAL C C   1 
ATOM   9753  O O   . VAL C 1 191 ? 28.054  -7.430  48.937  1.00 53.01  ? 191 VAL C O   1 
ATOM   9754  C CB  . VAL C 1 191 ? 25.593  -7.822  47.083  1.00 54.09  ? 191 VAL C CB  1 
ATOM   9755  C CG1 . VAL C 1 191 ? 24.361  -8.272  47.825  1.00 60.54  ? 191 VAL C CG1 1 
ATOM   9756  C CG2 . VAL C 1 191 ? 25.248  -7.561  45.633  1.00 56.26  ? 191 VAL C CG2 1 
ATOM   9757  N N   . SER C 1 192 ? 26.318  -6.684  50.162  1.00 54.47  ? 192 SER C N   1 
ATOM   9758  C CA  . SER C 1 192 ? 26.917  -7.023  51.439  1.00 56.95  ? 192 SER C CA  1 
ATOM   9759  C C   . SER C 1 192 ? 26.003  -7.992  52.173  1.00 60.04  ? 192 SER C C   1 
ATOM   9760  O O   . SER C 1 192 ? 24.895  -8.308  51.724  1.00 62.26  ? 192 SER C O   1 
ATOM   9761  C CB  . SER C 1 192 ? 27.171  -5.766  52.285  1.00 49.20  ? 192 SER C CB  1 
ATOM   9762  O OG  . SER C 1 192 ? 25.954  -5.109  52.594  1.00 47.62  ? 192 SER C OG  1 
ATOM   9763  N N   . THR C 1 193 ? 26.479  -8.469  53.316  1.00 52.77  ? 193 THR C N   1 
ATOM   9764  C CA  . THR C 1 193 ? 25.696  -9.358  54.156  1.00 51.88  ? 193 THR C CA  1 
ATOM   9765  C C   . THR C 1 193 ? 25.841  -8.914  55.607  1.00 53.15  ? 193 THR C C   1 
ATOM   9766  O O   . THR C 1 193 ? 26.534  -7.942  55.913  1.00 51.66  ? 193 THR C O   1 
ATOM   9767  C CB  . THR C 1 193 ? 26.119  -10.817 53.947  1.00 54.66  ? 193 THR C CB  1 
ATOM   9768  O OG1 . THR C 1 193 ? 25.261  -11.681 54.707  1.00 61.80  ? 193 THR C OG1 1 
ATOM   9769  C CG2 . THR C 1 193 ? 27.579  -11.024 54.352  1.00 54.02  ? 193 THR C CG2 1 
ATOM   9770  N N   . SER C 1 194 ? 25.147  -9.601  56.502  1.00 55.12  ? 194 SER C N   1 
ATOM   9771  C CA  . SER C 1 194 ? 25.261  -9.398  57.939  1.00 54.71  ? 194 SER C CA  1 
ATOM   9772  C C   . SER C 1 194 ? 25.579  -10.729 58.592  1.00 52.76  ? 194 SER C C   1 
ATOM   9773  O O   . SER C 1 194 ? 25.588  -11.766 57.924  1.00 57.57  ? 194 SER C O   1 
ATOM   9774  C CB  . SER C 1 194 ? 23.965  -8.811  58.521  1.00 53.59  ? 194 SER C CB  1 
ATOM   9775  O OG  . SER C 1 194 ? 23.718  -7.505  58.027  1.00 55.46  ? 194 SER C OG  1 
ATOM   9776  N N   . PRO C 1 195 ? 25.894  -10.737 59.892  1.00 55.42  ? 195 PRO C N   1 
ATOM   9777  C CA  . PRO C 1 195 ? 25.880  -12.003 60.628  1.00 56.21  ? 195 PRO C CA  1 
ATOM   9778  C C   . PRO C 1 195 ? 24.571  -12.740 60.381  1.00 52.36  ? 195 PRO C C   1 
ATOM   9779  O O   . PRO C 1 195 ? 23.514  -12.123 60.227  1.00 48.06  ? 195 PRO C O   1 
ATOM   9780  C CB  . PRO C 1 195 ? 26.027  -11.561 62.089  1.00 60.81  ? 195 PRO C CB  1 
ATOM   9781  C CG  . PRO C 1 195 ? 26.913  -10.369 61.990  1.00 58.19  ? 195 PRO C CG  1 
ATOM   9782  C CD  . PRO C 1 195 ? 26.501  -9.658  60.697  1.00 57.01  ? 195 PRO C CD  1 
ATOM   9783  N N   . TYR C 1 196 ? 24.662  -14.076 60.363  1.00 49.72  ? 196 TYR C N   1 
ATOM   9784  C CA  . TYR C 1 196 ? 23.646  -14.916 59.725  1.00 51.19  ? 196 TYR C CA  1 
ATOM   9785  C C   . TYR C 1 196 ? 22.230  -14.565 60.158  1.00 55.20  ? 196 TYR C C   1 
ATOM   9786  O O   . TYR C 1 196 ? 21.359  -14.321 59.316  1.00 52.49  ? 196 TYR C O   1 
ATOM   9787  C CB  . TYR C 1 196 ? 23.926  -16.394 60.010  1.00 50.66  ? 196 TYR C CB  1 
ATOM   9788  C CG  . TYR C 1 196 ? 23.439  -17.313 58.913  1.00 52.31  ? 196 TYR C CG  1 
ATOM   9789  C CD1 . TYR C 1 196 ? 22.087  -17.635 58.791  1.00 54.01  ? 196 TYR C CD1 1 
ATOM   9790  C CD2 . TYR C 1 196 ? 24.324  -17.853 57.997  1.00 48.30  ? 196 TYR C CD2 1 
ATOM   9791  C CE1 . TYR C 1 196 ? 21.640  -18.479 57.783  1.00 55.85  ? 196 TYR C CE1 1 
ATOM   9792  C CE2 . TYR C 1 196 ? 23.890  -18.693 56.991  1.00 49.67  ? 196 TYR C CE2 1 
ATOM   9793  C CZ  . TYR C 1 196 ? 22.551  -19.004 56.885  1.00 55.56  ? 196 TYR C CZ  1 
ATOM   9794  O OH  . TYR C 1 196 ? 22.142  -19.845 55.874  1.00 51.45  ? 196 TYR C OH  1 
ATOM   9795  N N   . TYR C 1 197 ? 21.973  -14.548 61.467  1.00 51.64  ? 197 TYR C N   1 
ATOM   9796  C CA  . TYR C 1 197 ? 20.616  -14.391 61.982  1.00 53.21  ? 197 TYR C CA  1 
ATOM   9797  C C   . TYR C 1 197 ? 20.376  -13.028 62.631  1.00 55.07  ? 197 TYR C C   1 
ATOM   9798  O O   . TYR C 1 197 ? 19.567  -12.919 63.552  1.00 63.41  ? 197 TYR C O   1 
ATOM   9799  C CB  . TYR C 1 197 ? 20.285  -15.512 62.968  1.00 54.05  ? 197 TYR C CB  1 
ATOM   9800  C CG  . TYR C 1 197 ? 20.251  -16.882 62.331  1.00 54.37  ? 197 TYR C CG  1 
ATOM   9801  C CD1 . TYR C 1 197 ? 19.122  -17.328 61.653  1.00 49.42  ? 197 TYR C CD1 1 
ATOM   9802  C CD2 . TYR C 1 197 ? 21.345  -17.730 62.410  1.00 53.78  ? 197 TYR C CD2 1 
ATOM   9803  C CE1 . TYR C 1 197 ? 19.089  -18.574 61.068  1.00 50.09  ? 197 TYR C CE1 1 
ATOM   9804  C CE2 . TYR C 1 197 ? 21.323  -18.977 61.831  1.00 55.10  ? 197 TYR C CE2 1 
ATOM   9805  C CZ  . TYR C 1 197 ? 20.193  -19.396 61.159  1.00 59.75  ? 197 TYR C CZ  1 
ATOM   9806  O OH  . TYR C 1 197 ? 20.172  -20.643 60.580  1.00 71.96  ? 197 TYR C OH  1 
ATOM   9807  N N   . HIS C 1 198 ? 21.039  -11.981 62.149  1.00 45.37  ? 198 HIS C N   1 
ATOM   9808  C CA  . HIS C 1 198 ? 20.844  -10.620 62.641  1.00 55.83  ? 198 HIS C CA  1 
ATOM   9809  C C   . HIS C 1 198 ? 20.944  -10.469 64.167  1.00 52.73  ? 198 HIS C C   1 
ATOM   9810  O O   . HIS C 1 198 ? 20.051  -9.904  64.800  1.00 47.08  ? 198 HIS C O   1 
ATOM   9811  C CB  . HIS C 1 198 ? 19.513  -10.072 62.139  1.00 42.28  ? 198 HIS C CB  1 
ATOM   9812  C CG  . HIS C 1 198 ? 19.540  -8.610  61.814  1.00 43.44  ? 198 HIS C CG  1 
ATOM   9813  N ND1 . HIS C 1 198 ? 18.993  -7.648  62.637  1.00 44.07  ? 198 HIS C ND1 1 
ATOM   9814  C CD2 . HIS C 1 198 ? 20.090  -7.943  60.772  1.00 47.04  ? 198 HIS C CD2 1 
ATOM   9815  C CE1 . HIS C 1 198 ? 19.181  -6.455  62.102  1.00 41.71  ? 198 HIS C CE1 1 
ATOM   9816  N NE2 . HIS C 1 198 ? 19.847  -6.606  60.972  1.00 48.13  ? 198 HIS C NE2 1 
ATOM   9817  N N   . PRO C 1 199 ? 22.031  -10.936 64.780  1.00 54.44  ? 199 PRO C N   1 
ATOM   9818  C CA  . PRO C 1 199 ? 22.198  -10.767 66.223  1.00 49.03  ? 199 PRO C CA  1 
ATOM   9819  C C   . PRO C 1 199 ? 22.843  -9.422  66.544  1.00 57.71  ? 199 PRO C C   1 
ATOM   9820  O O   . PRO C 1 199 ? 23.291  -8.684  65.665  1.00 62.13  ? 199 PRO C O   1 
ATOM   9821  C CB  . PRO C 1 199 ? 23.138  -11.921 66.580  1.00 53.18  ? 199 PRO C CB  1 
ATOM   9822  C CG  . PRO C 1 199 ? 24.056  -11.974 65.400  1.00 50.05  ? 199 PRO C CG  1 
ATOM   9823  C CD  . PRO C 1 199 ? 23.195  -11.629 64.192  1.00 56.68  ? 199 PRO C CD  1 
ATOM   9824  N N   . LEU C 1 200 ? 22.890  -9.114  67.838  1.00 52.54  ? 200 LEU C N   1 
ATOM   9825  C CA  . LEU C 1 200 ? 23.641  -7.955  68.332  1.00 49.41  ? 200 LEU C CA  1 
ATOM   9826  C C   . LEU C 1 200 ? 25.031  -8.447  68.712  1.00 49.55  ? 200 LEU C C   1 
ATOM   9827  O O   . LEU C 1 200 ? 25.265  -8.840  69.851  1.00 58.69  ? 200 LEU C O   1 
ATOM   9828  C CB  . LEU C 1 200 ? 22.927  -7.284  69.503  1.00 53.62  ? 200 LEU C CB  1 
ATOM   9829  C CG  . LEU C 1 200 ? 21.573  -6.666  69.164  1.00 59.28  ? 200 LEU C CG  1 
ATOM   9830  C CD1 . LEU C 1 200 ? 20.867  -6.182  70.415  1.00 49.31  ? 200 LEU C CD1 1 
ATOM   9831  C CD2 . LEU C 1 200 ? 21.704  -5.525  68.146  1.00 56.98  ? 200 LEU C CD2 1 
ATOM   9832  N N   . ILE C 1 201 ? 25.954  -8.424  67.733  1.00 49.01  ? 201 ILE C N   1 
ATOM   9833  C CA  . ILE C 1 201 ? 27.278  -9.013  67.944  1.00 45.58  ? 201 ILE C CA  1 
ATOM   9834  C C   . ILE C 1 201 ? 27.993  -8.420  69.148  1.00 44.74  ? 201 ILE C C   1 
ATOM   9835  O O   . ILE C 1 201 ? 28.575  -9.191  69.924  1.00 51.48  ? 201 ILE C O   1 
ATOM   9836  C CB  . ILE C 1 201 ? 28.101  -8.947  66.649  1.00 52.07  ? 201 ILE C CB  1 
ATOM   9837  C CG1 . ILE C 1 201 ? 27.538  -9.960  65.628  1.00 61.80  ? 201 ILE C CG1 1 
ATOM   9838  C CG2 . ILE C 1 201 ? 29.538  -9.313  66.906  1.00 49.39  ? 201 ILE C CG2 1 
ATOM   9839  C CD1 . ILE C 1 201 ? 27.545  -11.401 66.152  1.00 59.42  ? 201 ILE C CD1 1 
ATOM   9840  N N   . PRO C 1 202 ? 27.976  -7.106  69.401  1.00 38.00  ? 202 PRO C N   1 
ATOM   9841  C CA  . PRO C 1 202 ? 28.657  -6.601  70.611  1.00 41.60  ? 202 PRO C CA  1 
ATOM   9842  C C   . PRO C 1 202 ? 28.197  -7.245  71.912  1.00 44.84  ? 202 PRO C C   1 
ATOM   9843  O O   . PRO C 1 202 ? 29.036  -7.565  72.759  1.00 54.49  ? 202 PRO C O   1 
ATOM   9844  C CB  . PRO C 1 202 ? 28.350  -5.096  70.574  1.00 40.52  ? 202 PRO C CB  1 
ATOM   9845  C CG  . PRO C 1 202 ? 28.287  -4.795  69.123  1.00 42.14  ? 202 PRO C CG  1 
ATOM   9846  C CD  . PRO C 1 202 ? 27.569  -5.990  68.530  1.00 43.95  ? 202 PRO C CD  1 
ATOM   9847  N N   . ILE C 1 203 ? 26.896  -7.470  72.085  1.00 46.73  ? 203 ILE C N   1 
ATOM   9848  C CA  . ILE C 1 203 ? 26.425  -8.106  73.309  1.00 52.94  ? 203 ILE C CA  1 
ATOM   9849  C C   . ILE C 1 203 ? 26.929  -9.538  73.397  1.00 53.84  ? 203 ILE C C   1 
ATOM   9850  O O   . ILE C 1 203 ? 27.310  -10.008 74.473  1.00 59.06  ? 203 ILE C O   1 
ATOM   9851  C CB  . ILE C 1 203 ? 24.894  -8.051  73.390  1.00 50.76  ? 203 ILE C CB  1 
ATOM   9852  C CG1 . ILE C 1 203 ? 24.428  -6.603  73.540  1.00 50.23  ? 203 ILE C CG1 1 
ATOM   9853  C CG2 . ILE C 1 203 ? 24.421  -8.905  74.554  1.00 51.12  ? 203 ILE C CG2 1 
ATOM   9854  C CD1 . ILE C 1 203 ? 23.121  -6.457  74.269  1.00 45.49  ? 203 ILE C CD1 1 
ATOM   9855  N N   . LEU C 1 204 ? 26.925  -10.259 72.274  1.00 51.77  ? 204 LEU C N   1 
ATOM   9856  C CA  . LEU C 1 204 ? 27.383  -11.644 72.285  1.00 55.14  ? 204 LEU C CA  1 
ATOM   9857  C C   . LEU C 1 204 ? 28.860  -11.730 72.640  1.00 58.21  ? 204 LEU C C   1 
ATOM   9858  O O   . LEU C 1 204 ? 29.270  -12.581 73.440  1.00 63.00  ? 204 LEU C O   1 
ATOM   9859  C CB  . LEU C 1 204 ? 27.129  -12.288 70.927  1.00 55.81  ? 204 LEU C CB  1 
ATOM   9860  C CG  . LEU C 1 204 ? 25.672  -12.404 70.512  1.00 48.30  ? 204 LEU C CG  1 
ATOM   9861  C CD1 . LEU C 1 204 ? 25.572  -13.320 69.319  1.00 60.08  ? 204 LEU C CD1 1 
ATOM   9862  C CD2 . LEU C 1 204 ? 24.854  -12.938 71.670  1.00 54.50  ? 204 LEU C CD2 1 
ATOM   9863  N N   . LEU C 1 205 ? 29.678  -10.856 72.048  1.00 53.55  ? 205 LEU C N   1 
ATOM   9864  C CA  . LEU C 1 205 ? 31.106  -10.851 72.339  1.00 54.15  ? 205 LEU C CA  1 
ATOM   9865  C C   . LEU C 1 205 ? 31.367  -10.477 73.793  1.00 54.42  ? 205 LEU C C   1 
ATOM   9866  O O   . LEU C 1 205 ? 31.920  -11.270 74.560  1.00 60.34  ? 205 LEU C O   1 
ATOM   9867  C CB  . LEU C 1 205 ? 31.831  -9.898  71.391  1.00 53.21  ? 205 LEU C CB  1 
ATOM   9868  C CG  . LEU C 1 205 ? 31.891  -10.393 69.949  1.00 52.68  ? 205 LEU C CG  1 
ATOM   9869  C CD1 . LEU C 1 205 ? 32.407  -9.307  69.035  1.00 51.06  ? 205 LEU C CD1 1 
ATOM   9870  C CD2 . LEU C 1 205 ? 32.765  -11.634 69.845  1.00 46.94  ? 205 LEU C CD2 1 
ATOM   9871  N N   . ASN C 1 206 ? 30.976  -9.277  74.193  1.00 51.72  ? 206 ASN C N   1 
ATOM   9872  C CA  . ASN C 1 206 ? 31.099  -8.933  75.603  1.00 56.09  ? 206 ASN C CA  1 
ATOM   9873  C C   . ASN C 1 206 ? 29.859  -8.163  76.043  1.00 57.79  ? 206 ASN C C   1 
ATOM   9874  O O   . ASN C 1 206 ? 29.649  -7.018  75.622  1.00 57.43  ? 206 ASN C O   1 
ATOM   9875  C CB  . ASN C 1 206 ? 32.379  -8.130  75.859  1.00 59.86  ? 206 ASN C CB  1 
ATOM   9876  C CG  . ASN C 1 206 ? 32.456  -7.568  77.270  1.00 67.05  ? 206 ASN C CG  1 
ATOM   9877  O OD1 . ASN C 1 206 ? 32.985  -6.475  77.481  1.00 70.33  ? 206 ASN C OD1 1 
ATOM   9878  N ND2 . ASN C 1 206 ? 31.941  -8.318  78.243  1.00 66.77  ? 206 ASN C ND2 1 
ATOM   9879  N N   . PRO C 1 207 ? 29.016  -8.757  76.893  1.00 55.92  ? 207 PRO C N   1 
ATOM   9880  C CA  . PRO C 1 207 ? 27.798  -8.064  77.333  1.00 53.84  ? 207 PRO C CA  1 
ATOM   9881  C C   . PRO C 1 207 ? 28.055  -6.805  78.152  1.00 49.71  ? 207 PRO C C   1 
ATOM   9882  O O   . PRO C 1 207 ? 27.097  -6.077  78.430  1.00 55.92  ? 207 PRO C O   1 
ATOM   9883  C CB  . PRO C 1 207 ? 27.074  -9.131  78.169  1.00 58.98  ? 207 PRO C CB  1 
ATOM   9884  C CG  . PRO C 1 207 ? 27.684  -10.447 77.727  1.00 53.35  ? 207 PRO C CG  1 
ATOM   9885  C CD  . PRO C 1 207 ? 29.116  -10.102 77.482  1.00 52.82  ? 207 PRO C CD  1 
ATOM   9886  N N   . ASN C 1 208 ? 29.297  -6.514  78.547  1.00 49.30  ? 208 ASN C N   1 
ATOM   9887  C CA  . ASN C 1 208 ? 29.557  -5.285  79.292  1.00 55.17  ? 208 ASN C CA  1 
ATOM   9888  C C   . ASN C 1 208 ? 29.514  -4.048  78.409  1.00 52.30  ? 208 ASN C C   1 
ATOM   9889  O O   . ASN C 1 208 ? 29.587  -2.929  78.933  1.00 48.64  ? 208 ASN C O   1 
ATOM   9890  C CB  . ASN C 1 208 ? 30.909  -5.357  80.004  1.00 49.63  ? 208 ASN C CB  1 
ATOM   9891  C CG  . ASN C 1 208 ? 30.890  -6.286  81.193  1.00 48.29  ? 208 ASN C CG  1 
ATOM   9892  O OD1 . ASN C 1 208 ? 31.557  -7.318  81.203  1.00 53.04  ? 208 ASN C OD1 1 
ATOM   9893  N ND2 . ASN C 1 208 ? 30.117  -5.925  82.206  1.00 54.55  ? 208 ASN C ND2 1 
ATOM   9894  N N   . CYS C 1 209 ? 29.384  -4.225  77.092  1.00 52.45  ? 209 CYS C N   1 
ATOM   9895  C CA  . CYS C 1 209 ? 29.329  -3.097  76.171  1.00 54.19  ? 209 CYS C CA  1 
ATOM   9896  C C   . CYS C 1 209 ? 28.117  -2.207  76.412  1.00 53.64  ? 209 CYS C C   1 
ATOM   9897  O O   . CYS C 1 209 ? 28.123  -1.045  75.992  1.00 52.93  ? 209 CYS C O   1 
ATOM   9898  C CB  . CYS C 1 209 ? 29.308  -3.602  74.728  1.00 52.23  ? 209 CYS C CB  1 
ATOM   9899  S SG  . CYS C 1 209 ? 27.878  -4.630  74.305  1.00 54.23  ? 209 CYS C SG  1 
ATOM   9900  N N   . VAL C 1 210 ? 27.077  -2.724  77.072  1.00 50.18  ? 210 VAL C N   1 
ATOM   9901  C CA  . VAL C 1 210 ? 25.884  -1.919  77.315  1.00 52.94  ? 210 VAL C CA  1 
ATOM   9902  C C   . VAL C 1 210 ? 26.164  -0.804  78.323  1.00 61.66  ? 210 VAL C C   1 
ATOM   9903  O O   . VAL C 1 210 ? 25.488  0.231   78.315  1.00 61.26  ? 210 VAL C O   1 
ATOM   9904  C CB  . VAL C 1 210 ? 24.718  -2.824  77.760  1.00 59.60  ? 210 VAL C CB  1 
ATOM   9905  C CG1 . VAL C 1 210 ? 24.598  -4.028  76.809  1.00 47.90  ? 210 VAL C CG1 1 
ATOM   9906  C CG2 . VAL C 1 210 ? 24.878  -3.271  79.223  1.00 56.04  ? 210 VAL C CG2 1 
ATOM   9907  N N   . TYR C 1 211 ? 27.175  -0.970  79.178  1.00 59.23  ? 211 TYR C N   1 
ATOM   9908  C CA  . TYR C 1 211 ? 27.484  0.048   80.173  1.00 56.09  ? 211 TYR C CA  1 
ATOM   9909  C C   . TYR C 1 211 ? 28.318  1.194   79.618  1.00 60.77  ? 211 TYR C C   1 
ATOM   9910  O O   . TYR C 1 211 ? 28.547  2.176   80.334  1.00 70.17  ? 211 TYR C O   1 
ATOM   9911  C CB  . TYR C 1 211 ? 28.220  -0.576  81.360  1.00 55.69  ? 211 TYR C CB  1 
ATOM   9912  C CG  . TYR C 1 211 ? 27.535  -1.781  81.977  1.00 60.76  ? 211 TYR C CG  1 
ATOM   9913  C CD1 . TYR C 1 211 ? 26.306  -1.661  82.617  1.00 58.36  ? 211 TYR C CD1 1 
ATOM   9914  C CD2 . TYR C 1 211 ? 28.125  -3.039  81.929  1.00 59.49  ? 211 TYR C CD2 1 
ATOM   9915  C CE1 . TYR C 1 211 ? 25.682  -2.759  83.192  1.00 53.91  ? 211 TYR C CE1 1 
ATOM   9916  C CE2 . TYR C 1 211 ? 27.504  -4.147  82.500  1.00 52.85  ? 211 TYR C CE2 1 
ATOM   9917  C CZ  . TYR C 1 211 ? 26.283  -4.002  83.132  1.00 54.42  ? 211 TYR C CZ  1 
ATOM   9918  O OH  . TYR C 1 211 ? 25.660  -5.094  83.706  1.00 52.32  ? 211 TYR C OH  1 
ATOM   9919  N N   . GLU C 1 212 ? 28.793  1.095   78.377  1.00 53.95  ? 212 GLU C N   1 
ATOM   9920  C CA  . GLU C 1 212 ? 29.585  2.189   77.829  1.00 60.17  ? 212 GLU C CA  1 
ATOM   9921  C C   . GLU C 1 212 ? 28.708  3.390   77.519  1.00 57.30  ? 212 GLU C C   1 
ATOM   9922  O O   . GLU C 1 212 ? 29.152  4.537   77.649  1.00 63.30  ? 212 GLU C O   1 
ATOM   9923  C CB  . GLU C 1 212 ? 30.336  1.719   76.583  1.00 59.76  ? 212 GLU C CB  1 
ATOM   9924  C CG  . GLU C 1 212 ? 30.879  0.303   76.699  1.00 61.43  ? 212 GLU C CG  1 
ATOM   9925  C CD  . GLU C 1 212 ? 31.967  0.003   75.684  1.00 67.72  ? 212 GLU C CD  1 
ATOM   9926  O OE1 . GLU C 1 212 ? 32.281  0.889   74.859  1.00 59.93  ? 212 GLU C OE1 1 
ATOM   9927  O OE2 . GLU C 1 212 ? 32.510  -1.123  75.715  1.00 70.05  ? 212 GLU C OE2 1 
ATOM   9928  N N   . THR C 1 213 ? 27.457  3.141   77.136  1.00 60.45  ? 213 THR C N   1 
ATOM   9929  C CA  . THR C 1 213 ? 26.481  4.187   76.874  1.00 64.52  ? 213 THR C CA  1 
ATOM   9930  C C   . THR C 1 213 ? 25.357  4.252   77.898  1.00 65.85  ? 213 THR C C   1 
ATOM   9931  O O   . THR C 1 213 ? 24.718  5.300   78.020  1.00 63.68  ? 213 THR C O   1 
ATOM   9932  C CB  . THR C 1 213 ? 25.860  3.990   75.487  1.00 56.12  ? 213 THR C CB  1 
ATOM   9933  O OG1 . THR C 1 213 ? 25.629  2.590   75.267  1.00 53.84  ? 213 THR C OG1 1 
ATOM   9934  C CG2 . THR C 1 213 ? 26.795  4.522   74.426  1.00 48.85  ? 213 THR C CG2 1 
ATOM   9935  N N   . THR C 1 214 ? 25.095  3.164   78.622  1.00 64.58  ? 214 THR C N   1 
ATOM   9936  C CA  . THR C 1 214 ? 24.040  3.121   79.634  1.00 62.47  ? 214 THR C CA  1 
ATOM   9937  C C   . THR C 1 214 ? 24.623  2.435   80.865  1.00 52.90  ? 214 THR C C   1 
ATOM   9938  O O   . THR C 1 214 ? 24.508  1.215   81.027  1.00 58.98  ? 214 THR C O   1 
ATOM   9939  C CB  . THR C 1 214 ? 22.781  2.413   79.116  1.00 56.36  ? 214 THR C CB  1 
ATOM   9940  O OG1 . THR C 1 214 ? 23.131  1.372   78.194  1.00 56.45  ? 214 THR C OG1 1 
ATOM   9941  C CG2 . THR C 1 214 ? 21.871  3.409   78.401  1.00 53.88  ? 214 THR C CG2 1 
ATOM   9942  N N   . PRO C 1 215 ? 25.260  3.201   81.760  1.00 54.66  ? 215 PRO C N   1 
ATOM   9943  C CA  . PRO C 1 215 ? 26.087  2.588   82.818  1.00 58.17  ? 215 PRO C CA  1 
ATOM   9944  C C   . PRO C 1 215 ? 25.326  1.851   83.910  1.00 60.69  ? 215 PRO C C   1 
ATOM   9945  O O   . PRO C 1 215 ? 25.868  0.883   84.457  1.00 53.62  ? 215 PRO C O   1 
ATOM   9946  C CB  . PRO C 1 215 ? 26.836  3.796   83.399  1.00 53.70  ? 215 PRO C CB  1 
ATOM   9947  C CG  . PRO C 1 215 ? 26.850  4.780   82.287  1.00 54.18  ? 215 PRO C CG  1 
ATOM   9948  C CD  . PRO C 1 215 ? 25.482  4.651   81.692  1.00 60.43  ? 215 PRO C CD  1 
ATOM   9949  N N   . ASN C 1 216 ? 24.121  2.287   84.279  1.00 64.00  ? 216 ASN C N   1 
ATOM   9950  C CA  . ASN C 1 216 ? 23.408  1.720   85.419  1.00 64.50  ? 216 ASN C CA  1 
ATOM   9951  C C   . ASN C 1 216 ? 22.235  0.836   85.001  1.00 62.79  ? 216 ASN C C   1 
ATOM   9952  O O   . ASN C 1 216 ? 21.245  0.724   85.727  1.00 71.11  ? 216 ASN C O   1 
ATOM   9953  C CB  . ASN C 1 216 ? 22.922  2.825   86.357  1.00 69.95  ? 216 ASN C CB  1 
ATOM   9954  C CG  . ASN C 1 216 ? 23.165  2.493   87.826  1.00 76.43  ? 216 ASN C CG  1 
ATOM   9955  O OD1 . ASN C 1 216 ? 22.934  1.364   88.265  1.00 71.76  ? 216 ASN C OD1 1 
ATOM   9956  N ND2 . ASN C 1 216 ? 23.623  3.480   88.592  1.00 74.22  ? 216 ASN C ND2 1 
ATOM   9957  N N   . VAL C 1 217 ? 22.336  0.185   83.858  1.00 59.95  ? 217 VAL C N   1 
ATOM   9958  C CA  . VAL C 1 217 ? 21.271  -0.697  83.401  1.00 60.22  ? 217 VAL C CA  1 
ATOM   9959  C C   . VAL C 1 217 ? 21.369  -2.027  84.140  1.00 55.75  ? 217 VAL C C   1 
ATOM   9960  O O   . VAL C 1 217 ? 22.468  -2.533  84.398  1.00 57.48  ? 217 VAL C O   1 
ATOM   9961  C CB  . VAL C 1 217 ? 21.356  -0.883  81.876  1.00 54.03  ? 217 VAL C CB  1 
ATOM   9962  C CG1 . VAL C 1 217 ? 22.750  -1.346  81.479  1.00 61.44  ? 217 VAL C CG1 1 
ATOM   9963  C CG2 . VAL C 1 217 ? 20.317  -1.854  81.399  1.00 48.31  ? 217 VAL C CG2 1 
ATOM   9964  N N   . LYS C 1 218 ? 20.218  -2.594  84.498  1.00 62.24  ? 218 LYS C N   1 
ATOM   9965  C CA  . LYS C 1 218 ? 20.159  -3.934  85.072  1.00 64.08  ? 218 LYS C CA  1 
ATOM   9966  C C   . LYS C 1 218 ? 19.963  -4.940  83.943  1.00 62.64  ? 218 LYS C C   1 
ATOM   9967  O O   . LYS C 1 218 ? 18.958  -4.886  83.225  1.00 59.24  ? 218 LYS C O   1 
ATOM   9968  C CB  . LYS C 1 218 ? 19.028  -4.047  86.097  1.00 64.74  ? 218 LYS C CB  1 
ATOM   9969  C CG  . LYS C 1 218 ? 18.280  -2.738  86.347  1.00 73.74  ? 218 LYS C CG  1 
ATOM   9970  C CD  . LYS C 1 218 ? 18.398  -2.250  87.793  1.00 71.59  ? 218 LYS C CD  1 
ATOM   9971  C CE  . LYS C 1 218 ? 18.105  -0.751  87.899  1.00 71.14  ? 218 LYS C CE  1 
ATOM   9972  N NZ  . LYS C 1 218 ? 19.250  0.090   87.441  1.00 68.42  ? 218 LYS C NZ  1 
ATOM   9973  N N   . ILE C 1 219 ? 20.928  -5.839  83.773  1.00 64.00  ? 219 ILE C N   1 
ATOM   9974  C CA  . ILE C 1 219 ? 20.831  -6.890  82.762  1.00 64.35  ? 219 ILE C CA  1 
ATOM   9975  C C   . ILE C 1 219 ? 21.080  -8.244  83.419  1.00 66.28  ? 219 ILE C C   1 
ATOM   9976  O O   . ILE C 1 219 ? 21.756  -8.318  84.458  1.00 52.97  ? 219 ILE C O   1 
ATOM   9977  C CB  . ILE C 1 219 ? 21.806  -6.648  81.599  1.00 57.48  ? 219 ILE C CB  1 
ATOM   9978  C CG1 . ILE C 1 219 ? 23.257  -6.748  82.072  1.00 51.11  ? 219 ILE C CG1 1 
ATOM   9979  C CG2 . ILE C 1 219 ? 21.530  -5.319  80.957  1.00 57.34  ? 219 ILE C CG2 1 
ATOM   9980  C CD1 . ILE C 1 219 ? 24.266  -6.575  80.957  1.00 50.51  ? 219 ILE C CD1 1 
ATOM   9981  N N   . PRO C 1 220 ? 20.557  -9.330  82.847  1.00 67.45  ? 220 PRO C N   1 
ATOM   9982  C CA  . PRO C 1 220 ? 20.731  -10.650 83.463  1.00 64.76  ? 220 PRO C CA  1 
ATOM   9983  C C   . PRO C 1 220 ? 22.198  -11.040 83.542  1.00 61.82  ? 220 PRO C C   1 
ATOM   9984  O O   . PRO C 1 220 ? 23.033  -10.559 82.774  1.00 68.14  ? 220 PRO C O   1 
ATOM   9985  C CB  . PRO C 1 220 ? 19.957  -11.575 82.517  1.00 63.75  ? 220 PRO C CB  1 
ATOM   9986  C CG  . PRO C 1 220 ? 19.966  -10.833 81.205  1.00 58.63  ? 220 PRO C CG  1 
ATOM   9987  C CD  . PRO C 1 220 ? 19.770  -9.414  81.605  1.00 56.99  ? 220 PRO C CD  1 
ATOM   9988  N N   . ASP C 1 221 ? 22.513  -11.915 84.490  1.00 56.04  ? 221 ASP C N   1 
ATOM   9989  C CA  . ASP C 1 221 ? 23.875  -12.416 84.610  1.00 61.81  ? 221 ASP C CA  1 
ATOM   9990  C C   . ASP C 1 221 ? 24.195  -13.317 83.420  1.00 61.19  ? 221 ASP C C   1 
ATOM   9991  O O   . ASP C 1 221 ? 23.523  -14.331 83.205  1.00 66.78  ? 221 ASP C O   1 
ATOM   9992  C CB  . ASP C 1 221 ? 24.043  -13.165 85.930  1.00 64.28  ? 221 ASP C CB  1 
ATOM   9993  C CG  . ASP C 1 221 ? 25.339  -13.948 85.999  1.00 74.09  ? 221 ASP C CG  1 
ATOM   9994  O OD1 . ASP C 1 221 ? 26.351  -13.489 85.424  1.00 72.55  ? 221 ASP C OD1 1 
ATOM   9995  O OD2 . ASP C 1 221 ? 25.346  -15.026 86.632  1.00 73.83  ? 221 ASP C OD2 1 
ATOM   9996  N N   . PHE C 1 222 ? 25.210  -12.938 82.638  1.00 61.08  ? 222 PHE C N   1 
ATOM   9997  C CA  . PHE C 1 222 ? 25.644  -13.714 81.473  1.00 61.18  ? 222 PHE C CA  1 
ATOM   9998  C C   . PHE C 1 222 ? 26.723  -14.697 81.911  1.00 58.72  ? 222 PHE C C   1 
ATOM   9999  O O   . PHE C 1 222 ? 27.922  -14.496 81.705  1.00 70.45  ? 222 PHE C O   1 
ATOM   10000 C CB  . PHE C 1 222 ? 26.153  -12.800 80.365  1.00 60.36  ? 222 PHE C CB  1 
ATOM   10001 C CG  . PHE C 1 222 ? 25.068  -12.137 79.575  1.00 59.77  ? 222 PHE C CG  1 
ATOM   10002 C CD1 . PHE C 1 222 ? 24.375  -11.066 80.105  1.00 57.39  ? 222 PHE C CD1 1 
ATOM   10003 C CD2 . PHE C 1 222 ? 24.758  -12.566 78.292  1.00 59.86  ? 222 PHE C CD2 1 
ATOM   10004 C CE1 . PHE C 1 222 ? 23.375  -10.444 79.385  1.00 55.46  ? 222 PHE C CE1 1 
ATOM   10005 C CE2 . PHE C 1 222 ? 23.760  -11.946 77.562  1.00 50.76  ? 222 PHE C CE2 1 
ATOM   10006 C CZ  . PHE C 1 222 ? 23.069  -10.881 78.112  1.00 55.53  ? 222 PHE C CZ  1 
ATOM   10007 N N   . ALA C 1 223 ? 26.276  -15.791 82.524  1.00 56.82  ? 223 ALA C N   1 
ATOM   10008 C CA  . ALA C 1 223 ? 27.171  -16.860 82.943  1.00 60.30  ? 223 ALA C CA  1 
ATOM   10009 C C   . ALA C 1 223 ? 27.441  -17.869 81.829  1.00 56.21  ? 223 ALA C C   1 
ATOM   10010 O O   . ALA C 1 223 ? 27.782  -19.025 82.110  1.00 57.17  ? 223 ALA C O   1 
ATOM   10011 C CB  . ALA C 1 223 ? 26.607  -17.553 84.184  1.00 67.51  ? 223 ALA C CB  1 
ATOM   10012 N N   . VAL C 1 224 ? 27.290  -17.458 80.565  1.00 60.39  ? 224 VAL C N   1 
ATOM   10013 C CA  . VAL C 1 224 ? 27.690  -18.256 79.412  1.00 55.43  ? 224 VAL C CA  1 
ATOM   10014 C C   . VAL C 1 224 ? 28.397  -17.361 78.411  1.00 58.70  ? 224 VAL C C   1 
ATOM   10015 O O   . VAL C 1 224 ? 28.172  -16.150 78.352  1.00 57.41  ? 224 VAL C O   1 
ATOM   10016 C CB  . VAL C 1 224 ? 26.513  -18.938 78.701  1.00 52.74  ? 224 VAL C CB  1 
ATOM   10017 C CG1 . VAL C 1 224 ? 26.370  -20.362 79.169  1.00 64.71  ? 224 VAL C CG1 1 
ATOM   10018 C CG2 . VAL C 1 224 ? 25.248  -18.141 78.918  1.00 62.26  ? 224 VAL C CG2 1 
ATOM   10019 N N   . SER C 1 225 ? 29.227  -17.989 77.586  1.00 64.59  ? 225 SER C N   1 
ATOM   10020 C CA  . SER C 1 225 ? 29.972  -17.297 76.547  1.00 58.25  ? 225 SER C CA  1 
ATOM   10021 C C   . SER C 1 225 ? 29.217  -17.421 75.232  1.00 59.23  ? 225 SER C C   1 
ATOM   10022 O O   . SER C 1 225 ? 28.921  -18.531 74.775  1.00 58.80  ? 225 SER C O   1 
ATOM   10023 C CB  . SER C 1 225 ? 31.386  -17.862 76.417  1.00 63.02  ? 225 SER C CB  1 
ATOM   10024 O OG  . SER C 1 225 ? 31.940  -17.577 75.143  1.00 64.50  ? 225 SER C OG  1 
ATOM   10025 N N   . PHE C 1 226 ? 28.884  -16.279 74.646  1.00 58.42  ? 226 PHE C N   1 
ATOM   10026 C CA  . PHE C 1 226 ? 28.322  -16.220 73.312  1.00 55.58  ? 226 PHE C CA  1 
ATOM   10027 C C   . PHE C 1 226 ? 29.372  -15.828 72.278  1.00 57.53  ? 226 PHE C C   1 
ATOM   10028 O O   . PHE C 1 226 ? 29.019  -15.492 71.144  1.00 54.09  ? 226 PHE C O   1 
ATOM   10029 C CB  . PHE C 1 226 ? 27.150  -15.234 73.288  1.00 63.35  ? 226 PHE C CB  1 
ATOM   10030 C CG  . PHE C 1 226 ? 25.909  -15.725 74.001  1.00 58.46  ? 226 PHE C CG  1 
ATOM   10031 C CD1 . PHE C 1 226 ? 25.180  -16.797 73.503  1.00 53.90  ? 226 PHE C CD1 1 
ATOM   10032 C CD2 . PHE C 1 226 ? 25.460  -15.100 75.155  1.00 58.29  ? 226 PHE C CD2 1 
ATOM   10033 C CE1 . PHE C 1 226 ? 24.036  -17.240 74.149  1.00 53.60  ? 226 PHE C CE1 1 
ATOM   10034 C CE2 . PHE C 1 226 ? 24.310  -15.542 75.807  1.00 57.11  ? 226 PHE C CE2 1 
ATOM   10035 C CZ  . PHE C 1 226 ? 23.602  -16.612 75.303  1.00 55.87  ? 226 PHE C CZ  1 
ATOM   10036 N N   . ARG C 1 227 ? 30.658  -15.858 72.646  1.00 64.30  ? 227 ARG C N   1 
ATOM   10037 C CA  . ARG C 1 227 ? 31.693  -15.360 71.743  1.00 60.47  ? 227 ARG C CA  1 
ATOM   10038 C C   . ARG C 1 227 ? 31.894  -16.294 70.560  1.00 59.54  ? 227 ARG C C   1 
ATOM   10039 O O   . ARG C 1 227 ? 32.096  -15.834 69.430  1.00 65.81  ? 227 ARG C O   1 
ATOM   10040 C CB  . ARG C 1 227 ? 33.009  -15.162 72.496  1.00 55.73  ? 227 ARG C CB  1 
ATOM   10041 C CG  . ARG C 1 227 ? 32.936  -14.151 73.629  1.00 64.21  ? 227 ARG C CG  1 
ATOM   10042 C CD  . ARG C 1 227 ? 33.209  -14.819 74.971  1.00 65.86  ? 227 ARG C CD  1 
ATOM   10043 N NE  . ARG C 1 227 ? 33.279  -13.888 76.093  1.00 69.92  ? 227 ARG C NE  1 
ATOM   10044 C CZ  . ARG C 1 227 ? 32.226  -13.329 76.677  1.00 70.69  ? 227 ARG C CZ  1 
ATOM   10045 N NH1 . ARG C 1 227 ? 30.996  -13.517 76.215  1.00 71.57  ? 227 ARG C NH1 1 
ATOM   10046 N NH2 . ARG C 1 227 ? 32.412  -12.561 77.750  1.00 65.38  ? 227 ARG C NH2 1 
ATOM   10047 N N   . GLU C 1 228 ? 31.850  -17.607 70.794  1.00 59.84  ? 228 GLU C N   1 
ATOM   10048 C CA  . GLU C 1 228 ? 32.016  -18.539 69.684  1.00 68.20  ? 228 GLU C CA  1 
ATOM   10049 C C   . GLU C 1 228 ? 30.821  -18.502 68.739  1.00 63.92  ? 228 GLU C C   1 
ATOM   10050 O O   . GLU C 1 228 ? 30.979  -18.739 67.536  1.00 64.99  ? 228 GLU C O   1 
ATOM   10051 C CB  . GLU C 1 228 ? 32.248  -19.961 70.202  1.00 70.33  ? 228 GLU C CB  1 
ATOM   10052 C CG  . GLU C 1 228 ? 32.712  -20.981 69.132  1.00 82.99  ? 228 GLU C CG  1 
ATOM   10053 C CD  . GLU C 1 228 ? 34.014  -20.613 68.401  1.00 93.92  ? 228 GLU C CD  1 
ATOM   10054 O OE1 . GLU C 1 228 ? 34.443  -21.407 67.531  1.00 90.76  ? 228 GLU C OE1 1 
ATOM   10055 O OE2 . GLU C 1 228 ? 34.628  -19.564 68.705  1.00 85.68  ? 228 GLU C OE2 1 
ATOM   10056 N N   . ASP C 1 229 ? 29.626  -18.207 69.260  1.00 65.33  ? 229 ASP C N   1 
ATOM   10057 C CA  . ASP C 1 229 ? 28.462  -18.047 68.396  1.00 58.93  ? 229 ASP C CA  1 
ATOM   10058 C C   . ASP C 1 229 ? 28.597  -16.815 67.508  1.00 64.46  ? 229 ASP C C   1 
ATOM   10059 O O   . ASP C 1 229 ? 28.174  -16.841 66.346  1.00 64.92  ? 229 ASP C O   1 
ATOM   10060 C CB  . ASP C 1 229 ? 27.190  -17.973 69.238  1.00 54.69  ? 229 ASP C CB  1 
ATOM   10061 C CG  . ASP C 1 229 ? 26.769  -19.335 69.782  1.00 69.37  ? 229 ASP C CG  1 
ATOM   10062 O OD1 . ASP C 1 229 ? 27.444  -20.336 69.459  1.00 73.31  ? 229 ASP C OD1 1 
ATOM   10063 O OD2 . ASP C 1 229 ? 25.774  -19.408 70.538  1.00 63.27  ? 229 ASP C OD2 1 
ATOM   10064 N N   . ALA C 1 230 ? 29.199  -15.740 68.025  1.00 61.34  ? 230 ALA C N   1 
ATOM   10065 C CA  . ALA C 1 230 ? 29.422  -14.552 67.207  1.00 59.00  ? 230 ALA C CA  1 
ATOM   10066 C C   . ALA C 1 230 ? 30.280  -14.874 65.986  1.00 62.67  ? 230 ALA C C   1 
ATOM   10067 O O   . ALA C 1 230 ? 29.980  -14.424 64.873  1.00 64.90  ? 230 ALA C O   1 
ATOM   10068 C CB  . ALA C 1 230 ? 30.067  -13.450 68.044  1.00 55.72  ? 230 ALA C CB  1 
ATOM   10069 N N   . SER C 1 231 ? 31.350  -15.657 66.172  1.00 57.62  ? 231 SER C N   1 
ATOM   10070 C CA  . SER C 1 231 ? 32.170  -16.069 65.034  1.00 59.79  ? 231 SER C CA  1 
ATOM   10071 C C   . SER C 1 231 ? 31.373  -16.928 64.062  1.00 62.21  ? 231 SER C C   1 
ATOM   10072 O O   . SER C 1 231 ? 31.551  -16.824 62.841  1.00 57.56  ? 231 SER C O   1 
ATOM   10073 C CB  . SER C 1 231 ? 33.415  -16.826 65.507  1.00 62.68  ? 231 SER C CB  1 
ATOM   10074 O OG  . SER C 1 231 ? 34.555  -15.984 65.575  1.00 69.39  ? 231 SER C OG  1 
ATOM   10075 N N   . LYS C 1 232 ? 30.489  -17.785 64.588  1.00 63.66  ? 232 LYS C N   1 
ATOM   10076 C CA  . LYS C 1 232 ? 29.657  -18.631 63.735  1.00 59.80  ? 232 LYS C CA  1 
ATOM   10077 C C   . LYS C 1 232 ? 28.776  -17.795 62.816  1.00 53.92  ? 232 LYS C C   1 
ATOM   10078 O O   . LYS C 1 232 ? 28.672  -18.074 61.617  1.00 55.01  ? 232 LYS C O   1 
ATOM   10079 C CB  . LYS C 1 232 ? 28.799  -19.563 64.594  1.00 59.21  ? 232 LYS C CB  1 
ATOM   10080 C CG  . LYS C 1 232 ? 29.546  -20.776 65.113  1.00 64.12  ? 232 LYS C CG  1 
ATOM   10081 C CD  . LYS C 1 232 ? 28.767  -21.481 66.204  1.00 61.18  ? 232 LYS C CD  1 
ATOM   10082 C CE  . LYS C 1 232 ? 28.398  -22.886 65.782  1.00 66.88  ? 232 LYS C CE  1 
ATOM   10083 N NZ  . LYS C 1 232 ? 29.514  -23.837 66.030  1.00 71.33  ? 232 LYS C NZ  1 
ATOM   10084 N N   . HIS C 1 233 ? 28.128  -16.766 63.367  1.00 54.60  ? 233 HIS C N   1 
ATOM   10085 C CA  . HIS C 1 233 ? 27.285  -15.890 62.560  1.00 55.45  ? 233 HIS C CA  1 
ATOM   10086 C C   . HIS C 1 233 ? 28.065  -15.301 61.388  1.00 56.90  ? 233 HIS C C   1 
ATOM   10087 O O   . HIS C 1 233 ? 27.592  -15.311 60.244  1.00 50.59  ? 233 HIS C O   1 
ATOM   10088 C CB  . HIS C 1 233 ? 26.706  -14.779 63.434  1.00 54.95  ? 233 HIS C CB  1 
ATOM   10089 C CG  . HIS C 1 233 ? 25.569  -15.219 64.302  1.00 61.47  ? 233 HIS C CG  1 
ATOM   10090 N ND1 . HIS C 1 233 ? 24.272  -15.302 63.844  1.00 55.75  ? 233 HIS C ND1 1 
ATOM   10091 C CD2 . HIS C 1 233 ? 25.532  -15.585 65.606  1.00 61.67  ? 233 HIS C CD2 1 
ATOM   10092 C CE1 . HIS C 1 233 ? 23.486  -15.706 64.826  1.00 57.29  ? 233 HIS C CE1 1 
ATOM   10093 N NE2 . HIS C 1 233 ? 24.225  -15.884 65.906  1.00 56.97  ? 233 HIS C NE2 1 
ATOM   10094 N N   . VAL C 1 234 ? 29.275  -14.801 61.654  1.00 56.16  ? 234 VAL C N   1 
ATOM   10095 C CA  . VAL C 1 234 ? 30.065  -14.158 60.606  1.00 54.04  ? 234 VAL C CA  1 
ATOM   10096 C C   . VAL C 1 234 ? 30.581  -15.185 59.606  1.00 54.46  ? 234 VAL C C   1 
ATOM   10097 O O   . VAL C 1 234 ? 30.592  -14.936 58.395  1.00 56.42  ? 234 VAL C O   1 
ATOM   10098 C CB  . VAL C 1 234 ? 31.225  -13.348 61.212  1.00 56.22  ? 234 VAL C CB  1 
ATOM   10099 C CG1 . VAL C 1 234 ? 31.916  -12.555 60.116  1.00 50.84  ? 234 VAL C CG1 1 
ATOM   10100 C CG2 . VAL C 1 234 ? 30.741  -12.421 62.331  1.00 53.12  ? 234 VAL C CG2 1 
ATOM   10101 N N   . GLU C 1 235 ? 31.028  -16.348 60.092  1.00 54.92  ? 235 GLU C N   1 
ATOM   10102 C CA  . GLU C 1 235 ? 31.600  -17.352 59.196  1.00 58.07  ? 235 GLU C CA  1 
ATOM   10103 C C   . GLU C 1 235 ? 30.523  -18.046 58.371  1.00 60.61  ? 235 GLU C C   1 
ATOM   10104 O O   . GLU C 1 235 ? 30.722  -18.307 57.180  1.00 63.88  ? 235 GLU C O   1 
ATOM   10105 C CB  . GLU C 1 235 ? 32.401  -18.383 59.990  1.00 60.27  ? 235 GLU C CB  1 
ATOM   10106 C CG  . GLU C 1 235 ? 33.636  -17.824 60.681  1.00 71.02  ? 235 GLU C CG  1 
ATOM   10107 C CD  . GLU C 1 235 ? 34.900  -17.985 59.857  1.00 78.75  ? 235 GLU C CD  1 
ATOM   10108 O OE1 . GLU C 1 235 ? 35.001  -17.345 58.788  1.00 81.85  ? 235 GLU C OE1 1 
ATOM   10109 O OE2 . GLU C 1 235 ? 35.797  -18.744 60.280  1.00 79.86  ? 235 GLU C OE2 1 
ATOM   10110 N N   . LEU C 1 236 ? 29.379  -18.359 58.983  1.00 56.54  ? 236 LEU C N   1 
ATOM   10111 C CA  . LEU C 1 236 ? 28.305  -18.988 58.223  1.00 56.55  ? 236 LEU C CA  1 
ATOM   10112 C C   . LEU C 1 236 ? 27.721  -18.033 57.191  1.00 51.69  ? 236 LEU C C   1 
ATOM   10113 O O   . LEU C 1 236 ? 27.240  -18.474 56.140  1.00 53.31  ? 236 LEU C O   1 
ATOM   10114 C CB  . LEU C 1 236 ? 27.220  -19.492 59.170  1.00 50.54  ? 236 LEU C CB  1 
ATOM   10115 C CG  . LEU C 1 236 ? 27.603  -20.744 59.957  1.00 49.38  ? 236 LEU C CG  1 
ATOM   10116 C CD1 . LEU C 1 236 ? 26.507  -21.127 60.934  1.00 59.61  ? 236 LEU C CD1 1 
ATOM   10117 C CD2 . LEU C 1 236 ? 27.884  -21.885 58.995  1.00 50.53  ? 236 LEU C CD2 1 
ATOM   10118 N N   . ALA C 1 237 ? 27.762  -16.729 57.469  1.00 52.99  ? 237 ALA C N   1 
ATOM   10119 C CA  . ALA C 1 237 ? 27.298  -15.743 56.500  1.00 55.36  ? 237 ALA C CA  1 
ATOM   10120 C C   . ALA C 1 237 ? 28.200  -15.709 55.280  1.00 58.32  ? 237 ALA C C   1 
ATOM   10121 O O   . ALA C 1 237 ? 27.721  -15.636 54.142  1.00 54.71  ? 237 ALA C O   1 
ATOM   10122 C CB  . ALA C 1 237 ? 27.249  -14.360 57.147  1.00 53.15  ? 237 ALA C CB  1 
ATOM   10123 N N   . LYS C 1 238 ? 29.516  -15.752 55.507  1.00 62.19  ? 238 LYS C N   1 
ATOM   10124 C CA  . LYS C 1 238 ? 30.474  -15.687 54.410  1.00 62.03  ? 238 LYS C CA  1 
ATOM   10125 C C   . LYS C 1 238 ? 30.345  -16.893 53.493  1.00 59.60  ? 238 LYS C C   1 
ATOM   10126 O O   . LYS C 1 238 ? 30.551  -16.775 52.281  1.00 63.62  ? 238 LYS C O   1 
ATOM   10127 C CB  . LYS C 1 238 ? 31.894  -15.573 54.972  1.00 60.83  ? 238 LYS C CB  1 
ATOM   10128 C CG  . LYS C 1 238 ? 32.142  -14.298 55.780  1.00 59.22  ? 238 LYS C CG  1 
ATOM   10129 C CD  . LYS C 1 238 ? 33.606  -14.126 56.199  1.00 64.36  ? 238 LYS C CD  1 
ATOM   10130 C CE  . LYS C 1 238 ? 34.596  -14.587 55.136  1.00 59.56  ? 238 LYS C CE  1 
ATOM   10131 N NZ  . LYS C 1 238 ? 35.844  -15.099 55.768  1.00 53.39  ? 238 LYS C NZ  1 
ATOM   10132 N N   . GLU C 1 239 ? 29.986  -18.055 54.045  1.00 57.34  ? 239 GLU C N   1 
ATOM   10133 C CA  . GLU C 1 239 ? 29.738  -19.222 53.205  1.00 59.92  ? 239 GLU C CA  1 
ATOM   10134 C C   . GLU C 1 239 ? 28.446  -19.068 52.410  1.00 63.83  ? 239 GLU C C   1 
ATOM   10135 O O   . GLU C 1 239 ? 28.391  -19.436 51.230  1.00 62.44  ? 239 GLU C O   1 
ATOM   10136 C CB  . GLU C 1 239 ? 29.699  -20.490 54.060  1.00 68.37  ? 239 GLU C CB  1 
ATOM   10137 C CG  . GLU C 1 239 ? 28.665  -21.519 53.612  1.00 84.90  ? 239 GLU C CG  1 
ATOM   10138 C CD  . GLU C 1 239 ? 28.684  -22.778 54.457  1.00 93.76  ? 239 GLU C CD  1 
ATOM   10139 O OE1 . GLU C 1 239 ? 28.284  -23.843 53.943  1.00 98.04  ? 239 GLU C OE1 1 
ATOM   10140 O OE2 . GLU C 1 239 ? 29.090  -22.702 55.637  1.00 101.12 ? 239 GLU C OE2 1 
ATOM   10141 N N   . LYS C 1 240 ? 27.396  -18.516 53.029  1.00 60.07  ? 240 LYS C N   1 
ATOM   10142 C CA  . LYS C 1 240 ? 26.151  -18.320 52.293  1.00 60.80  ? 240 LYS C CA  1 
ATOM   10143 C C   . LYS C 1 240 ? 26.320  -17.267 51.205  1.00 57.69  ? 240 LYS C C   1 
ATOM   10144 O O   . LYS C 1 240 ? 25.782  -17.415 50.102  1.00 63.64  ? 240 LYS C O   1 
ATOM   10145 C CB  . LYS C 1 240 ? 25.015  -17.946 53.244  1.00 54.17  ? 240 LYS C CB  1 
ATOM   10146 C CG  . LYS C 1 240 ? 23.657  -18.034 52.585  1.00 52.10  ? 240 LYS C CG  1 
ATOM   10147 C CD  . LYS C 1 240 ? 23.507  -19.390 51.922  1.00 57.89  ? 240 LYS C CD  1 
ATOM   10148 C CE  . LYS C 1 240 ? 22.060  -19.768 51.727  1.00 60.03  ? 240 LYS C CE  1 
ATOM   10149 N NZ  . LYS C 1 240 ? 21.749  -21.064 52.384  1.00 57.32  ? 240 LYS C NZ  1 
ATOM   10150 N N   . TYR C 1 241 ? 27.087  -16.215 51.484  1.00 51.39  ? 241 TYR C N   1 
ATOM   10151 C CA  . TYR C 1 241 ? 27.418  -15.262 50.432  1.00 60.91  ? 241 TYR C CA  1 
ATOM   10152 C C   . TYR C 1 241 ? 28.179  -15.946 49.301  1.00 65.22  ? 241 TYR C C   1 
ATOM   10153 O O   . TYR C 1 241 ? 27.933  -15.666 48.122  1.00 69.98  ? 241 TYR C O   1 
ATOM   10154 C CB  . TYR C 1 241 ? 28.220  -14.102 51.022  1.00 58.87  ? 241 TYR C CB  1 
ATOM   10155 C CG  . TYR C 1 241 ? 28.447  -12.926 50.098  1.00 51.24  ? 241 TYR C CG  1 
ATOM   10156 C CD1 . TYR C 1 241 ? 29.501  -12.928 49.203  1.00 61.97  ? 241 TYR C CD1 1 
ATOM   10157 C CD2 . TYR C 1 241 ? 27.634  -11.802 50.150  1.00 50.77  ? 241 TYR C CD2 1 
ATOM   10158 C CE1 . TYR C 1 241 ? 29.737  -11.860 48.368  1.00 67.82  ? 241 TYR C CE1 1 
ATOM   10159 C CE2 . TYR C 1 241 ? 27.861  -10.720 49.316  1.00 55.04  ? 241 TYR C CE2 1 
ATOM   10160 C CZ  . TYR C 1 241 ? 28.918  -10.758 48.425  1.00 56.93  ? 241 TYR C CZ  1 
ATOM   10161 O OH  . TYR C 1 241 ? 29.171  -9.703  47.580  1.00 62.73  ? 241 TYR C OH  1 
ATOM   10162 N N   . PHE C 1 242 ? 29.083  -16.873 49.640  1.00 55.34  ? 242 PHE C N   1 
ATOM   10163 C CA  . PHE C 1 242 ? 29.849  -17.566 48.608  1.00 60.22  ? 242 PHE C CA  1 
ATOM   10164 C C   . PHE C 1 242 ? 28.950  -18.456 47.760  1.00 60.87  ? 242 PHE C C   1 
ATOM   10165 O O   . PHE C 1 242 ? 29.159  -18.579 46.549  1.00 66.81  ? 242 PHE C O   1 
ATOM   10166 C CB  . PHE C 1 242 ? 30.980  -18.379 49.241  1.00 61.10  ? 242 PHE C CB  1 
ATOM   10167 C CG  . PHE C 1 242 ? 31.796  -19.171 48.250  1.00 68.63  ? 242 PHE C CG  1 
ATOM   10168 C CD1 . PHE C 1 242 ? 31.384  -20.430 47.830  1.00 63.19  ? 242 PHE C CD1 1 
ATOM   10169 C CD2 . PHE C 1 242 ? 32.989  -18.666 47.756  1.00 73.80  ? 242 PHE C CD2 1 
ATOM   10170 C CE1 . PHE C 1 242 ? 32.133  -21.153 46.924  1.00 62.96  ? 242 PHE C CE1 1 
ATOM   10171 C CE2 . PHE C 1 242 ? 33.745  -19.390 46.848  1.00 64.13  ? 242 PHE C CE2 1 
ATOM   10172 C CZ  . PHE C 1 242 ? 33.318  -20.631 46.434  1.00 63.64  ? 242 PHE C CZ  1 
ATOM   10173 N N   . GLU C 1 243 ? 27.947  -19.086 48.373  1.00 59.36  ? 243 GLU C N   1 
ATOM   10174 C CA  . GLU C 1 243 ? 27.036  -19.930 47.606  1.00 62.48  ? 243 GLU C CA  1 
ATOM   10175 C C   . GLU C 1 243 ? 26.295  -19.118 46.552  1.00 62.22  ? 243 GLU C C   1 
ATOM   10176 O O   . GLU C 1 243 ? 26.179  -19.536 45.395  1.00 68.35  ? 243 GLU C O   1 
ATOM   10177 C CB  . GLU C 1 243 ? 26.049  -20.625 48.543  1.00 66.34  ? 243 GLU C CB  1 
ATOM   10178 C CG  . GLU C 1 243 ? 24.639  -20.732 47.976  1.00 79.48  ? 243 GLU C CG  1 
ATOM   10179 C CD  . GLU C 1 243 ? 23.791  -21.772 48.681  1.00 87.97  ? 243 GLU C CD  1 
ATOM   10180 O OE1 . GLU C 1 243 ? 22.693  -22.086 48.173  1.00 85.44  ? 243 GLU C OE1 1 
ATOM   10181 O OE2 . GLU C 1 243 ? 24.216  -22.271 49.745  1.00 93.04  ? 243 GLU C OE2 1 
ATOM   10182 N N   . ILE C 1 244 ? 25.809  -17.938 46.928  1.00 64.35  ? 244 ILE C N   1 
ATOM   10183 C CA  . ILE C 1 244 ? 25.010  -17.144 46.004  1.00 64.75  ? 244 ILE C CA  1 
ATOM   10184 C C   . ILE C 1 244 ? 25.893  -16.437 44.985  1.00 65.15  ? 244 ILE C C   1 
ATOM   10185 O O   . ILE C 1 244 ? 25.687  -16.560 43.773  1.00 63.49  ? 244 ILE C O   1 
ATOM   10186 C CB  . ILE C 1 244 ? 24.143  -16.143 46.779  1.00 62.63  ? 244 ILE C CB  1 
ATOM   10187 C CG1 . ILE C 1 244 ? 23.401  -16.844 47.920  1.00 58.73  ? 244 ILE C CG1 1 
ATOM   10188 C CG2 . ILE C 1 244 ? 23.188  -15.451 45.828  1.00 62.37  ? 244 ILE C CG2 1 
ATOM   10189 C CD1 . ILE C 1 244 ? 22.380  -17.844 47.460  1.00 55.26  ? 244 ILE C CD1 1 
ATOM   10190 N N   . PHE C 1 245 ? 26.891  -15.691 45.459  1.00 69.23  ? 245 PHE C N   1 
ATOM   10191 C CA  . PHE C 1 245 ? 27.679  -14.804 44.613  1.00 69.34  ? 245 PHE C CA  1 
ATOM   10192 C C   . PHE C 1 245 ? 29.052  -15.350 44.248  1.00 65.98  ? 245 PHE C C   1 
ATOM   10193 O O   . PHE C 1 245 ? 29.828  -14.638 43.604  1.00 68.40  ? 245 PHE C O   1 
ATOM   10194 C CB  . PHE C 1 245 ? 27.850  -13.440 45.286  1.00 66.01  ? 245 PHE C CB  1 
ATOM   10195 C CG  . PHE C 1 245 ? 26.559  -12.798 45.681  1.00 71.35  ? 245 PHE C CG  1 
ATOM   10196 C CD1 . PHE C 1 245 ? 25.790  -12.125 44.744  1.00 68.04  ? 245 PHE C CD1 1 
ATOM   10197 C CD2 . PHE C 1 245 ? 26.116  -12.859 46.989  1.00 64.45  ? 245 PHE C CD2 1 
ATOM   10198 C CE1 . PHE C 1 245 ? 24.604  -11.533 45.104  1.00 57.03  ? 245 PHE C CE1 1 
ATOM   10199 C CE2 . PHE C 1 245 ? 24.931  -12.265 47.355  1.00 59.12  ? 245 PHE C CE2 1 
ATOM   10200 C CZ  . PHE C 1 245 ? 24.173  -11.603 46.410  1.00 61.98  ? 245 PHE C CZ  1 
ATOM   10201 N N   . GLY C 1 246 ? 29.380  -16.578 44.638  1.00 60.88  ? 246 GLY C N   1 
ATOM   10202 C CA  . GLY C 1 246 ? 30.591  -17.208 44.148  1.00 60.74  ? 246 GLY C CA  1 
ATOM   10203 C C   . GLY C 1 246 ? 31.881  -16.683 44.729  1.00 72.69  ? 246 GLY C C   1 
ATOM   10204 O O   . GLY C 1 246 ? 32.950  -17.198 44.378  1.00 77.89  ? 246 GLY C O   1 
ATOM   10205 N N   . GLU C 1 247 ? 31.818  -15.681 45.603  1.00 77.53  ? 247 GLU C N   1 
ATOM   10206 C CA  . GLU C 1 247 ? 32.987  -15.106 46.248  1.00 71.83  ? 247 GLU C CA  1 
ATOM   10207 C C   . GLU C 1 247 ? 32.634  -14.832 47.702  1.00 71.10  ? 247 GLU C C   1 
ATOM   10208 O O   . GLU C 1 247 ? 31.462  -14.828 48.084  1.00 66.80  ? 247 GLU C O   1 
ATOM   10209 C CB  . GLU C 1 247 ? 33.445  -13.816 45.549  1.00 58.55  ? 247 GLU C CB  1 
ATOM   10210 C CG  . GLU C 1 247 ? 34.922  -13.484 45.737  1.00 80.17  ? 247 GLU C CG  1 
ATOM   10211 C CD  . GLU C 1 247 ? 35.801  -14.716 45.949  1.00 91.80  ? 247 GLU C CD  1 
ATOM   10212 O OE1 . GLU C 1 247 ? 36.141  -15.390 44.952  1.00 98.30  ? 247 GLU C OE1 1 
ATOM   10213 O OE2 . GLU C 1 247 ? 36.169  -15.000 47.111  1.00 91.56  ? 247 GLU C OE2 1 
ATOM   10214 N N   . HIS C 1 248 ? 33.667  -14.625 48.519  1.00 69.90  ? 248 HIS C N   1 
ATOM   10215 C CA  . HIS C 1 248 ? 33.409  -14.265 49.900  1.00 64.63  ? 248 HIS C CA  1 
ATOM   10216 C C   . HIS C 1 248 ? 33.136  -12.764 49.996  1.00 62.16  ? 248 HIS C C   1 
ATOM   10217 O O   . HIS C 1 248 ? 33.596  -11.988 49.156  1.00 66.97  ? 248 HIS C O   1 
ATOM   10218 C CB  . HIS C 1 248 ? 34.587  -14.664 50.791  1.00 64.03  ? 248 HIS C CB  1 
ATOM   10219 C CG  . HIS C 1 248 ? 34.486  -16.060 51.331  1.00 66.77  ? 248 HIS C CG  1 
ATOM   10220 N ND1 . HIS C 1 248 ? 35.546  -16.942 51.324  1.00 65.68  ? 248 HIS C ND1 1 
ATOM   10221 C CD2 . HIS C 1 248 ? 33.446  -16.731 51.880  1.00 71.41  ? 248 HIS C CD2 1 
ATOM   10222 C CE1 . HIS C 1 248 ? 35.164  -18.093 51.849  1.00 78.15  ? 248 HIS C CE1 1 
ATOM   10223 N NE2 . HIS C 1 248 ? 33.893  -17.992 52.194  1.00 81.03  ? 248 HIS C NE2 1 
ATOM   10224 N N   . PRO C 1 249 ? 32.355  -12.337 50.989  1.00 61.79  ? 249 PRO C N   1 
ATOM   10225 C CA  . PRO C 1 249 ? 31.967  -10.921 51.080  1.00 58.61  ? 249 PRO C CA  1 
ATOM   10226 C C   . PRO C 1 249 ? 33.049  -10.081 51.752  1.00 66.46  ? 249 PRO C C   1 
ATOM   10227 O O   . PRO C 1 249 ? 33.571  -10.439 52.815  1.00 64.39  ? 249 PRO C O   1 
ATOM   10228 C CB  . PRO C 1 249 ? 30.695  -10.965 51.932  1.00 62.08  ? 249 PRO C CB  1 
ATOM   10229 C CG  . PRO C 1 249 ? 30.938  -12.133 52.843  1.00 62.98  ? 249 PRO C CG  1 
ATOM   10230 C CD  . PRO C 1 249 ? 31.699  -13.151 52.026  1.00 61.81  ? 249 PRO C CD  1 
ATOM   10231 N N   . VAL C 1 250 ? 33.370  -8.943  51.134  1.00 68.32  ? 250 VAL C N   1 
ATOM   10232 C CA  . VAL C 1 250 ? 34.317  -7.993  51.711  1.00 60.45  ? 250 VAL C CA  1 
ATOM   10233 C C   . VAL C 1 250 ? 33.634  -6.878  52.494  1.00 55.94  ? 250 VAL C C   1 
ATOM   10234 O O   . VAL C 1 250 ? 34.308  -6.177  53.264  1.00 51.80  ? 250 VAL C O   1 
ATOM   10235 C CB  . VAL C 1 250 ? 35.215  -7.377  50.620  1.00 52.24  ? 250 VAL C CB  1 
ATOM   10236 C CG1 . VAL C 1 250 ? 36.292  -8.349  50.244  1.00 50.65  ? 250 VAL C CG1 1 
ATOM   10237 C CG2 . VAL C 1 250 ? 34.372  -6.997  49.395  1.00 60.43  ? 250 VAL C CG2 1 
ATOM   10238 N N   . TYR C 1 251 ? 32.333  -6.679  52.307  1.00 60.60  ? 251 TYR C N   1 
ATOM   10239 C CA  . TYR C 1 251 ? 31.585  -5.610  52.950  1.00 55.52  ? 251 TYR C CA  1 
ATOM   10240 C C   . TYR C 1 251 ? 30.463  -6.217  53.782  1.00 59.85  ? 251 TYR C C   1 
ATOM   10241 O O   . TYR C 1 251 ? 29.825  -7.193  53.370  1.00 59.45  ? 251 TYR C O   1 
ATOM   10242 C CB  . TYR C 1 251 ? 31.022  -4.619  51.904  1.00 50.06  ? 251 TYR C CB  1 
ATOM   10243 C CG  . TYR C 1 251 ? 32.064  -4.164  50.908  1.00 56.00  ? 251 TYR C CG  1 
ATOM   10244 C CD1 . TYR C 1 251 ? 33.291  -3.687  51.342  1.00 62.20  ? 251 TYR C CD1 1 
ATOM   10245 C CD2 . TYR C 1 251 ? 31.842  -4.247  49.535  1.00 58.63  ? 251 TYR C CD2 1 
ATOM   10246 C CE1 . TYR C 1 251 ? 34.265  -3.289  50.445  1.00 68.07  ? 251 TYR C CE1 1 
ATOM   10247 C CE2 . TYR C 1 251 ? 32.818  -3.849  48.626  1.00 57.53  ? 251 TYR C CE2 1 
ATOM   10248 C CZ  . TYR C 1 251 ? 34.027  -3.371  49.090  1.00 61.58  ? 251 TYR C CZ  1 
ATOM   10249 O OH  . TYR C 1 251 ? 35.006  -2.976  48.206  1.00 72.38  ? 251 TYR C OH  1 
ATOM   10250 N N   . MET C 1 252 ? 30.231  -5.647  54.963  1.00 60.89  ? 252 MET C N   1 
ATOM   10251 C CA  . MET C 1 252 ? 29.185  -6.144  55.843  1.00 59.95  ? 252 MET C CA  1 
ATOM   10252 C C   . MET C 1 252 ? 28.438  -4.985  56.481  1.00 58.07  ? 252 MET C C   1 
ATOM   10253 O O   . MET C 1 252 ? 29.005  -3.913  56.719  1.00 52.69  ? 252 MET C O   1 
ATOM   10254 C CB  . MET C 1 252 ? 29.753  -7.056  56.934  1.00 54.96  ? 252 MET C CB  1 
ATOM   10255 C CG  . MET C 1 252 ? 29.523  -8.521  56.635  1.00 61.40  ? 252 MET C CG  1 
ATOM   10256 S SD  . MET C 1 252 ? 30.152  -9.603  57.913  1.00 65.66  ? 252 MET C SD  1 
ATOM   10257 C CE  . MET C 1 252 ? 29.947  -11.210 57.139  1.00 46.40  ? 252 MET C CE  1 
ATOM   10258 N N   . TRP C 1 253 ? 27.151  -5.209  56.745  1.00 57.03  ? 253 TRP C N   1 
ATOM   10259 C CA  . TRP C 1 253 ? 26.370  -4.268  57.531  1.00 56.78  ? 253 TRP C CA  1 
ATOM   10260 C C   . TRP C 1 253 ? 26.177  -4.836  58.928  1.00 56.47  ? 253 TRP C C   1 
ATOM   10261 O O   . TRP C 1 253 ? 25.481  -5.857  59.079  1.00 52.62  ? 253 TRP C O   1 
ATOM   10262 C CB  . TRP C 1 253 ? 25.018  -3.995  56.884  1.00 45.06  ? 253 TRP C CB  1 
ATOM   10263 C CG  . TRP C 1 253 ? 24.076  -3.323  57.824  1.00 49.12  ? 253 TRP C CG  1 
ATOM   10264 C CD1 . TRP C 1 253 ? 22.941  -3.853  58.364  1.00 48.71  ? 253 TRP C CD1 1 
ATOM   10265 C CD2 . TRP C 1 253 ? 24.181  -1.987  58.340  1.00 53.56  ? 253 TRP C CD2 1 
ATOM   10266 N NE1 . TRP C 1 253 ? 22.332  -2.932  59.185  1.00 54.28  ? 253 TRP C NE1 1 
ATOM   10267 C CE2 . TRP C 1 253 ? 23.072  -1.779  59.186  1.00 56.20  ? 253 TRP C CE2 1 
ATOM   10268 C CE3 . TRP C 1 253 ? 25.103  -0.947  58.166  1.00 53.99  ? 253 TRP C CE3 1 
ATOM   10269 C CZ2 . TRP C 1 253 ? 22.860  -0.575  59.860  1.00 57.19  ? 253 TRP C CZ2 1 
ATOM   10270 C CZ3 . TRP C 1 253 ? 24.890  0.252   58.838  1.00 54.47  ? 253 TRP C CZ3 1 
ATOM   10271 C CH2 . TRP C 1 253 ? 23.777  0.425   59.673  1.00 53.86  ? 253 TRP C CH2 1 
ATOM   10272 N N   . PRO C 1 254 ? 26.756  -4.236  59.966  1.00 49.80  ? 254 PRO C N   1 
ATOM   10273 C CA  . PRO C 1 254 ? 26.487  -4.697  61.328  1.00 53.38  ? 254 PRO C CA  1 
ATOM   10274 C C   . PRO C 1 254 ? 25.012  -4.548  61.646  1.00 50.98  ? 254 PRO C C   1 
ATOM   10275 O O   . PRO C 1 254 ? 24.421  -3.478  61.421  1.00 43.46  ? 254 PRO C O   1 
ATOM   10276 C CB  . PRO C 1 254 ? 27.344  -3.772  62.205  1.00 50.58  ? 254 PRO C CB  1 
ATOM   10277 C CG  . PRO C 1 254 ? 27.625  -2.603  61.365  1.00 53.62  ? 254 PRO C CG  1 
ATOM   10278 C CD  . PRO C 1 254 ? 27.664  -3.079  59.946  1.00 48.66  ? 254 PRO C CD  1 
ATOM   10279 N N   . PRO C 1 255 ? 24.381  -5.608  62.146  1.00 50.11  ? 255 PRO C N   1 
ATOM   10280 C CA  . PRO C 1 255 ? 22.946  -5.546  62.441  1.00 50.22  ? 255 PRO C CA  1 
ATOM   10281 C C   . PRO C 1 255 ? 22.648  -4.493  63.495  1.00 48.45  ? 255 PRO C C   1 
ATOM   10282 O O   . PRO C 1 255 ? 23.303  -4.424  64.539  1.00 47.54  ? 255 PRO C O   1 
ATOM   10283 C CB  . PRO C 1 255 ? 22.624  -6.965  62.927  1.00 38.92  ? 255 PRO C CB  1 
ATOM   10284 C CG  . PRO C 1 255 ? 23.734  -7.801  62.366  1.00 45.89  ? 255 PRO C CG  1 
ATOM   10285 C CD  . PRO C 1 255 ? 24.939  -6.927  62.467  1.00 48.19  ? 255 PRO C CD  1 
ATOM   10286 N N   . GLN C 1 256 ? 21.651  -3.660  63.197  1.00 52.44  ? 256 GLN C N   1 
ATOM   10287 C CA  . GLN C 1 256 ? 21.249  -2.533  64.027  1.00 53.71  ? 256 GLN C CA  1 
ATOM   10288 C C   . GLN C 1 256 ? 22.354  -1.499  64.166  1.00 52.63  ? 256 GLN C C   1 
ATOM   10289 O O   . GLN C 1 256 ? 22.339  -0.702  65.109  1.00 51.13  ? 256 GLN C O   1 
ATOM   10290 C CB  . GLN C 1 256 ? 20.776  -3.004  65.407  1.00 56.63  ? 256 GLN C CB  1 
ATOM   10291 C CG  . GLN C 1 256 ? 19.593  -3.966  65.355  1.00 48.84  ? 256 GLN C CG  1 
ATOM   10292 C CD  . GLN C 1 256 ? 18.317  -3.314  64.842  1.00 48.65  ? 256 GLN C CD  1 
ATOM   10293 O OE1 . GLN C 1 256 ? 18.131  -2.103  64.955  1.00 49.83  ? 256 GLN C OE1 1 
ATOM   10294 N NE2 . GLN C 1 256 ? 17.434  -4.122  64.269  1.00 46.24  ? 256 GLN C NE2 1 
ATOM   10295 N N   . ALA C 1 257 ? 23.310  -1.496  63.232  1.00 54.63  ? 257 ALA C N   1 
ATOM   10296 C CA  . ALA C 1 257 ? 24.472  -0.605  63.253  1.00 55.07  ? 257 ALA C CA  1 
ATOM   10297 C C   . ALA C 1 257 ? 25.329  -0.811  64.498  1.00 54.75  ? 257 ALA C C   1 
ATOM   10298 O O   . ALA C 1 257 ? 26.165  0.036   64.827  1.00 56.89  ? 257 ALA C O   1 
ATOM   10299 C CB  . ALA C 1 257 ? 24.054  0.864   63.131  1.00 51.57  ? 257 ALA C CB  1 
ATOM   10300 N N   . SER C 1 258 ? 25.146  -1.943  65.183  1.00 53.11  ? 258 SER C N   1 
ATOM   10301 C CA  . SER C 1 258 ? 25.834  -2.198  66.444  1.00 54.62  ? 258 SER C CA  1 
ATOM   10302 C C   . SER C 1 258 ? 27.327  -2.357  66.207  1.00 59.18  ? 258 SER C C   1 
ATOM   10303 O O   . SER C 1 258 ? 27.755  -3.210  65.422  1.00 57.76  ? 258 SER C O   1 
ATOM   10304 C CB  . SER C 1 258 ? 25.272  -3.448  67.115  1.00 52.90  ? 258 SER C CB  1 
ATOM   10305 O OG  . SER C 1 258 ? 24.051  -3.164  67.769  1.00 69.70  ? 258 SER C OG  1 
ATOM   10306 N N   . VAL C 1 259 ? 28.117  -1.549  66.897  1.00 55.24  ? 259 VAL C N   1 
ATOM   10307 C CA  . VAL C 1 259 ? 29.562  -1.598  66.763  1.00 54.66  ? 259 VAL C CA  1 
ATOM   10308 C C   . VAL C 1 259 ? 30.187  -1.472  68.142  1.00 57.00  ? 259 VAL C C   1 
ATOM   10309 O O   . VAL C 1 259 ? 29.606  -0.894  69.066  1.00 57.80  ? 259 VAL C O   1 
ATOM   10310 C CB  . VAL C 1 259 ? 30.094  -0.493  65.827  1.00 59.70  ? 259 VAL C CB  1 
ATOM   10311 C CG1 . VAL C 1 259 ? 29.884  -0.888  64.364  1.00 55.81  ? 259 VAL C CG1 1 
ATOM   10312 C CG2 . VAL C 1 259 ? 29.431  0.842   66.157  1.00 53.48  ? 259 VAL C CG2 1 
ATOM   10313 N N   . SER C 1 260 ? 31.384  -2.028  68.268  1.00 55.77  ? 260 SER C N   1 
ATOM   10314 C CA  . SER C 1 260 ? 32.178  -1.931  69.481  1.00 53.43  ? 260 SER C CA  1 
ATOM   10315 C C   . SER C 1 260 ? 33.628  -2.169  69.088  1.00 59.94  ? 260 SER C C   1 
ATOM   10316 O O   . SER C 1 260 ? 33.919  -2.640  67.985  1.00 56.54  ? 260 SER C O   1 
ATOM   10317 C CB  . SER C 1 260 ? 31.711  -2.935  70.539  1.00 51.05  ? 260 SER C CB  1 
ATOM   10318 O OG  . SER C 1 260 ? 32.229  -4.226  70.265  1.00 60.79  ? 260 SER C OG  1 
ATOM   10319 N N   . ASN C 1 261 ? 34.540  -1.820  69.999  1.00 62.51  ? 261 ASN C N   1 
ATOM   10320 C CA  . ASN C 1 261 ? 35.944  -2.153  69.784  1.00 56.40  ? 261 ASN C CA  1 
ATOM   10321 C C   . ASN C 1 261 ? 36.105  -3.634  69.465  1.00 61.96  ? 261 ASN C C   1 
ATOM   10322 O O   . ASN C 1 261 ? 36.777  -4.004  68.494  1.00 67.28  ? 261 ASN C O   1 
ATOM   10323 C CB  . ASN C 1 261 ? 36.784  -1.775  71.010  1.00 58.01  ? 261 ASN C CB  1 
ATOM   10324 C CG  . ASN C 1 261 ? 36.639  -0.315  71.397  1.00 61.04  ? 261 ASN C CG  1 
ATOM   10325 O OD1 . ASN C 1 261 ? 36.426  0.547   70.542  1.00 59.46  ? 261 ASN C OD1 1 
ATOM   10326 N ND2 . ASN C 1 261 ? 36.802  -0.023  72.686  1.00 47.65  ? 261 ASN C ND2 1 
ATOM   10327 N N   . GLU C 1 262 ? 35.466  -4.498  70.259  1.00 52.82  ? 262 GLU C N   1 
ATOM   10328 C CA  . GLU C 1 262 ? 35.627  -5.937  70.072  1.00 57.06  ? 262 GLU C CA  1 
ATOM   10329 C C   . GLU C 1 262 ? 34.958  -6.410  68.788  1.00 56.26  ? 262 GLU C C   1 
ATOM   10330 O O   . GLU C 1 262 ? 35.485  -7.287  68.093  1.00 50.98  ? 262 GLU C O   1 
ATOM   10331 C CB  . GLU C 1 262 ? 35.063  -6.683  71.283  1.00 61.79  ? 262 GLU C CB  1 
ATOM   10332 C CG  . GLU C 1 262 ? 35.676  -6.253  72.616  1.00 63.99  ? 262 GLU C CG  1 
ATOM   10333 C CD  . GLU C 1 262 ? 34.719  -5.441  73.488  1.00 84.36  ? 262 GLU C CD  1 
ATOM   10334 O OE1 . GLU C 1 262 ? 35.203  -4.776  74.431  1.00 84.28  ? 262 GLU C OE1 1 
ATOM   10335 O OE2 . GLU C 1 262 ? 33.492  -5.459  73.234  1.00 84.98  ? 262 GLU C OE2 1 
ATOM   10336 N N   . ALA C 1 263 ? 33.795  -5.845  68.458  1.00 58.16  ? 263 ALA C N   1 
ATOM   10337 C CA  . ALA C 1 263 ? 33.079  -6.280  67.265  1.00 53.46  ? 263 ALA C CA  1 
ATOM   10338 C C   . ALA C 1 263 ? 33.878  -5.961  66.011  1.00 57.74  ? 263 ALA C C   1 
ATOM   10339 O O   . ALA C 1 263 ? 34.078  -6.824  65.146  1.00 57.32  ? 263 ALA C O   1 
ATOM   10340 C CB  . ALA C 1 263 ? 31.700  -5.628  67.212  1.00 47.07  ? 263 ALA C CB  1 
ATOM   10341 N N   . LEU C 1 264 ? 34.368  -4.726  65.911  1.00 57.32  ? 264 LEU C N   1 
ATOM   10342 C CA  . LEU C 1 264 ? 35.191  -4.354  64.770  1.00 63.06  ? 264 LEU C CA  1 
ATOM   10343 C C   . LEU C 1 264 ? 36.430  -5.241  64.652  1.00 67.37  ? 264 LEU C C   1 
ATOM   10344 O O   . LEU C 1 264 ? 36.898  -5.503  63.538  1.00 71.34  ? 264 LEU C O   1 
ATOM   10345 C CB  . LEU C 1 264 ? 35.586  -2.883  64.880  1.00 66.59  ? 264 LEU C CB  1 
ATOM   10346 C CG  . LEU C 1 264 ? 34.531  -1.861  64.469  1.00 53.94  ? 264 LEU C CG  1 
ATOM   10347 C CD1 . LEU C 1 264 ? 34.619  -0.667  65.385  1.00 53.54  ? 264 LEU C CD1 1 
ATOM   10348 C CD2 . LEU C 1 264 ? 34.756  -1.449  63.037  1.00 54.45  ? 264 LEU C CD2 1 
ATOM   10349 N N   . GLU C 1 265 ? 36.965  -5.725  65.778  1.00 53.59  ? 265 GLU C N   1 
ATOM   10350 C CA  . GLU C 1 265 ? 38.086  -6.662  65.712  1.00 58.42  ? 265 GLU C CA  1 
ATOM   10351 C C   . GLU C 1 265 ? 37.667  -7.990  65.088  1.00 61.78  ? 265 GLU C C   1 
ATOM   10352 O O   . GLU C 1 265 ? 38.450  -8.618  64.365  1.00 64.34  ? 265 GLU C O   1 
ATOM   10353 C CB  . GLU C 1 265 ? 38.658  -6.898  67.109  1.00 60.41  ? 265 GLU C CB  1 
ATOM   10354 C CG  . GLU C 1 265 ? 39.366  -5.697  67.689  1.00 64.78  ? 265 GLU C CG  1 
ATOM   10355 C CD  . GLU C 1 265 ? 39.931  -5.965  69.066  1.00 64.28  ? 265 GLU C CD  1 
ATOM   10356 O OE1 . GLU C 1 265 ? 40.367  -7.108  69.314  1.00 69.74  ? 265 GLU C OE1 1 
ATOM   10357 O OE2 . GLU C 1 265 ? 39.948  -5.033  69.898  1.00 64.50  ? 265 GLU C OE2 1 
ATOM   10358 N N   . LEU C 1 266 ? 36.437  -8.437  65.363  1.00 56.22  ? 266 LEU C N   1 
ATOM   10359 C CA  . LEU C 1 266 ? 35.974  -9.717  64.834  1.00 58.62  ? 266 LEU C CA  1 
ATOM   10360 C C   . LEU C 1 266 ? 35.690  -9.630  63.337  1.00 64.37  ? 266 LEU C C   1 
ATOM   10361 O O   . LEU C 1 266 ? 35.906  -10.599 62.599  1.00 59.61  ? 266 LEU C O   1 
ATOM   10362 C CB  . LEU C 1 266 ? 34.730  -10.178 65.601  1.00 58.21  ? 266 LEU C CB  1 
ATOM   10363 C CG  . LEU C 1 266 ? 33.870  -11.306 65.017  1.00 60.70  ? 266 LEU C CG  1 
ATOM   10364 C CD1 . LEU C 1 266 ? 34.364  -12.658 65.471  1.00 61.52  ? 266 LEU C CD1 1 
ATOM   10365 C CD2 . LEU C 1 266 ? 32.427  -11.125 65.428  1.00 63.50  ? 266 LEU C CD2 1 
ATOM   10366 N N   . TYR C 1 267 ? 35.202  -8.479  62.868  1.00 56.74  ? 267 TYR C N   1 
ATOM   10367 C CA  . TYR C 1 267 ? 34.972  -8.316  61.438  1.00 58.50  ? 267 TYR C CA  1 
ATOM   10368 C C   . TYR C 1 267 ? 36.285  -8.260  60.673  1.00 61.51  ? 267 TYR C C   1 
ATOM   10369 O O   . TYR C 1 267 ? 36.376  -8.764  59.548  1.00 67.22  ? 267 TYR C O   1 
ATOM   10370 C CB  . TYR C 1 267 ? 34.146  -7.059  61.173  1.00 66.58  ? 267 TYR C CB  1 
ATOM   10371 C CG  . TYR C 1 267 ? 32.689  -7.171  61.576  1.00 64.38  ? 267 TYR C CG  1 
ATOM   10372 C CD1 . TYR C 1 267 ? 31.866  -8.150  61.028  1.00 58.06  ? 267 TYR C CD1 1 
ATOM   10373 C CD2 . TYR C 1 267 ? 32.133  -6.285  62.488  1.00 61.65  ? 267 TYR C CD2 1 
ATOM   10374 C CE1 . TYR C 1 267 ? 30.533  -8.249  61.391  1.00 54.38  ? 267 TYR C CE1 1 
ATOM   10375 C CE2 . TYR C 1 267 ? 30.801  -6.375  62.856  1.00 57.54  ? 267 TYR C CE2 1 
ATOM   10376 C CZ  . TYR C 1 267 ? 30.004  -7.357  62.306  1.00 57.40  ? 267 TYR C CZ  1 
ATOM   10377 O OH  . TYR C 1 267 ? 28.678  -7.441  62.677  1.00 54.06  ? 267 TYR C OH  1 
ATOM   10378 N N   . TYR C 1 268 ? 37.316  -7.655  61.273  1.00 65.15  ? 268 TYR C N   1 
ATOM   10379 C CA  . TYR C 1 268 ? 38.625  -7.579  60.628  1.00 61.16  ? 268 TYR C CA  1 
ATOM   10380 C C   . TYR C 1 268 ? 39.262  -8.954  60.512  1.00 59.10  ? 268 TYR C C   1 
ATOM   10381 O O   . TYR C 1 268 ? 39.836  -9.291  59.471  1.00 64.81  ? 268 TYR C O   1 
ATOM   10382 C CB  . TYR C 1 268 ? 39.543  -6.644  61.414  1.00 59.83  ? 268 TYR C CB  1 
ATOM   10383 C CG  . TYR C 1 268 ? 41.026  -6.897  61.226  1.00 70.39  ? 268 TYR C CG  1 
ATOM   10384 C CD1 . TYR C 1 268 ? 41.666  -6.596  60.025  1.00 71.51  ? 268 TYR C CD1 1 
ATOM   10385 C CD2 . TYR C 1 268 ? 41.787  -7.453  62.250  1.00 76.24  ? 268 TYR C CD2 1 
ATOM   10386 C CE1 . TYR C 1 268 ? 43.033  -6.829  59.859  1.00 67.94  ? 268 TYR C CE1 1 
ATOM   10387 C CE2 . TYR C 1 268 ? 43.149  -7.692  62.093  1.00 67.65  ? 268 TYR C CE2 1 
ATOM   10388 C CZ  . TYR C 1 268 ? 43.765  -7.382  60.897  1.00 65.71  ? 268 TYR C CZ  1 
ATOM   10389 O OH  . TYR C 1 268 ? 45.112  -7.624  60.753  1.00 77.91  ? 268 TYR C OH  1 
ATOM   10390 N N   . GLU C 1 269 ? 39.187  -9.758  61.574  1.00 60.21  ? 269 GLU C N   1 
ATOM   10391 C CA  . GLU C 1 269 ? 39.810  -11.072 61.539  1.00 66.37  ? 269 GLU C CA  1 
ATOM   10392 C C   . GLU C 1 269 ? 39.049  -12.043 60.646  1.00 66.02  ? 269 GLU C C   1 
ATOM   10393 O O   . GLU C 1 269 ? 39.623  -13.054 60.223  1.00 65.35  ? 269 GLU C O   1 
ATOM   10394 C CB  . GLU C 1 269 ? 39.943  -11.628 62.955  1.00 68.78  ? 269 GLU C CB  1 
ATOM   10395 C CG  . GLU C 1 269 ? 41.142  -11.055 63.715  1.00 84.28  ? 269 GLU C CG  1 
ATOM   10396 C CD  . GLU C 1 269 ? 42.468  -11.713 63.336  1.00 96.61  ? 269 GLU C CD  1 
ATOM   10397 O OE1 . GLU C 1 269 ? 43.380  -10.999 62.859  1.00 92.51  ? 269 GLU C OE1 1 
ATOM   10398 O OE2 . GLU C 1 269 ? 42.607  -12.939 63.533  1.00 99.49  ? 269 GLU C OE2 1 
ATOM   10399 N N   . LYS C 1 270 ? 37.785  -11.748 60.336  1.00 64.13  ? 270 LYS C N   1 
ATOM   10400 C CA  . LYS C 1 270 ? 36.978  -12.544 59.419  1.00 62.53  ? 270 LYS C CA  1 
ATOM   10401 C C   . LYS C 1 270 ? 37.032  -12.013 57.994  1.00 59.66  ? 270 LYS C C   1 
ATOM   10402 O O   . LYS C 1 270 ? 36.298  -12.504 57.130  1.00 63.42  ? 270 LYS C O   1 
ATOM   10403 C CB  . LYS C 1 270 ? 35.527  -12.594 59.897  1.00 58.20  ? 270 LYS C CB  1 
ATOM   10404 C CG  . LYS C 1 270 ? 35.313  -13.429 61.149  1.00 58.03  ? 270 LYS C CG  1 
ATOM   10405 C CD  . LYS C 1 270 ? 35.729  -14.870 60.941  1.00 59.06  ? 270 LYS C CD  1 
ATOM   10406 C CE  . LYS C 1 270 ? 36.172  -15.512 62.245  1.00 65.70  ? 270 LYS C CE  1 
ATOM   10407 N NZ  . LYS C 1 270 ? 37.576  -15.149 62.590  1.00 74.60  ? 270 LYS C NZ  1 
ATOM   10408 N N   . GLY C 1 271 ? 37.868  -11.014 57.735  1.00 50.15  ? 271 GLY C N   1 
ATOM   10409 C CA  . GLY C 1 271 ? 38.144  -10.602 56.383  1.00 60.14  ? 271 GLY C CA  1 
ATOM   10410 C C   . GLY C 1 271 ? 37.337  -9.433  55.878  1.00 61.80  ? 271 GLY C C   1 
ATOM   10411 O O   . GLY C 1 271 ? 37.487  -9.062  54.706  1.00 64.82  ? 271 GLY C O   1 
ATOM   10412 N N   . ILE C 1 272 ? 36.501  -8.832  56.715  1.00 56.53  ? 272 ILE C N   1 
ATOM   10413 C CA  . ILE C 1 272 ? 35.660  -7.719  56.286  1.00 61.40  ? 272 ILE C CA  1 
ATOM   10414 C C   . ILE C 1 272 ? 36.511  -6.454  56.235  1.00 60.95  ? 272 ILE C C   1 
ATOM   10415 O O   . ILE C 1 272 ? 37.112  -6.055  57.240  1.00 60.87  ? 272 ILE C O   1 
ATOM   10416 C CB  . ILE C 1 272 ? 34.454  -7.544  57.221  1.00 56.48  ? 272 ILE C CB  1 
ATOM   10417 C CG1 . ILE C 1 272 ? 33.685  -8.865  57.363  1.00 56.16  ? 272 ILE C CG1 1 
ATOM   10418 C CG2 . ILE C 1 272 ? 33.547  -6.448  56.714  1.00 53.86  ? 272 ILE C CG2 1 
ATOM   10419 C CD1 . ILE C 1 272 ? 33.324  -9.520  56.039  1.00 52.34  ? 272 ILE C CD1 1 
ATOM   10420 N N   . ASN C 1 273 ? 36.567  -5.822  55.057  1.00 58.27  ? 273 ASN C N   1 
ATOM   10421 C CA  . ASN C 1 273 ? 37.360  -4.612  54.870  1.00 60.62  ? 273 ASN C CA  1 
ATOM   10422 C C   . ASN C 1 273 ? 36.601  -3.330  55.194  1.00 61.98  ? 273 ASN C C   1 
ATOM   10423 O O   . ASN C 1 273 ? 37.239  -2.294  55.415  1.00 63.78  ? 273 ASN C O   1 
ATOM   10424 C CB  . ASN C 1 273 ? 37.882  -4.523  53.428  1.00 56.64  ? 273 ASN C CB  1 
ATOM   10425 C CG  . ASN C 1 273 ? 38.751  -5.706  53.038  1.00 62.62  ? 273 ASN C CG  1 
ATOM   10426 O OD1 . ASN C 1 273 ? 39.167  -6.501  53.882  1.00 68.43  ? 273 ASN C OD1 1 
ATOM   10427 N ND2 . ASN C 1 273 ? 39.022  -5.831  51.744  1.00 72.55  ? 273 ASN C ND2 1 
ATOM   10428 N N   . MET C 1 274 ? 35.268  -3.360  55.227  1.00 56.94  ? 274 MET C N   1 
ATOM   10429 C CA  . MET C 1 274 ? 34.516  -2.138  55.472  1.00 60.62  ? 274 MET C CA  1 
ATOM   10430 C C   . MET C 1 274 ? 33.175  -2.463  56.122  1.00 55.33  ? 274 MET C C   1 
ATOM   10431 O O   . MET C 1 274 ? 32.629  -3.553  55.944  1.00 55.72  ? 274 MET C O   1 
ATOM   10432 C CB  . MET C 1 274 ? 34.303  -1.358  54.170  1.00 63.18  ? 274 MET C CB  1 
ATOM   10433 C CG  . MET C 1 274 ? 33.723  0.022   54.378  1.00 58.63  ? 274 MET C CG  1 
ATOM   10434 S SD  . MET C 1 274 ? 31.969  0.026   53.980  1.00 75.45  ? 274 MET C SD  1 
ATOM   10435 C CE  . MET C 1 274 ? 31.978  -0.621  52.298  1.00 68.59  ? 274 MET C CE  1 
ATOM   10436 N N   . LEU C 1 275 ? 32.659  -1.506  56.891  1.00 55.02  ? 275 LEU C N   1 
ATOM   10437 C CA  . LEU C 1 275 ? 31.310  -1.574  57.443  1.00 56.90  ? 275 LEU C CA  1 
ATOM   10438 C C   . LEU C 1 275 ? 30.830  -0.144  57.680  1.00 58.07  ? 275 LEU C C   1 
ATOM   10439 O O   . LEU C 1 275 ? 31.530  0.825   57.369  1.00 54.22  ? 275 LEU C O   1 
ATOM   10440 C CB  . LEU C 1 275 ? 31.266  -2.438  58.714  1.00 48.52  ? 275 LEU C CB  1 
ATOM   10441 C CG  . LEU C 1 275 ? 31.948  -1.950  59.995  1.00 54.81  ? 275 LEU C CG  1 
ATOM   10442 C CD1 . LEU C 1 275 ? 31.000  -1.226  60.925  1.00 60.22  ? 275 LEU C CD1 1 
ATOM   10443 C CD2 . LEU C 1 275 ? 32.549  -3.140  60.715  1.00 63.36  ? 275 LEU C CD2 1 
ATOM   10444 N N   . ALA C 1 276 ? 29.616  -0.015  58.214  1.00 59.55  ? 276 ALA C N   1 
ATOM   10445 C CA  . ALA C 1 276 ? 29.041  1.297   58.478  1.00 58.56  ? 276 ALA C CA  1 
ATOM   10446 C C   . ALA C 1 276 ? 28.208  1.240   59.750  1.00 54.15  ? 276 ALA C C   1 
ATOM   10447 O O   . ALA C 1 276 ? 27.757  0.173   60.166  1.00 52.16  ? 276 ALA C O   1 
ATOM   10448 C CB  . ALA C 1 276 ? 28.183  1.784   57.304  1.00 58.26  ? 276 ALA C CB  1 
ATOM   10449 N N   . THR C 1 277 ? 28.005  2.407   60.360  1.00 49.49  ? 277 THR C N   1 
ATOM   10450 C CA  . THR C 1 277 ? 27.172  2.535   61.552  1.00 51.38  ? 277 THR C CA  1 
ATOM   10451 C C   . THR C 1 277 ? 26.624  3.962   61.599  1.00 55.14  ? 277 THR C C   1 
ATOM   10452 O O   . THR C 1 277 ? 26.936  4.791   60.742  1.00 61.23  ? 277 THR C O   1 
ATOM   10453 C CB  . THR C 1 277 ? 27.962  2.163   62.815  1.00 54.37  ? 277 THR C CB  1 
ATOM   10454 O OG1 . THR C 1 277 ? 27.254  2.604   63.980  1.00 58.07  ? 277 THR C OG1 1 
ATOM   10455 C CG2 . THR C 1 277 ? 29.353  2.787   62.790  1.00 48.67  ? 277 THR C CG2 1 
ATOM   10456 N N   . ASP C 1 278 ? 25.791  4.241   62.606  1.00 55.49  ? 278 ASP C N   1 
ATOM   10457 C CA  . ASP C 1 278 ? 25.127  5.537   62.729  1.00 59.27  ? 278 ASP C CA  1 
ATOM   10458 C C   . ASP C 1 278 ? 26.087  6.601   63.252  1.00 58.92  ? 278 ASP C C   1 
ATOM   10459 O O   . ASP C 1 278 ? 27.018  6.309   64.006  1.00 60.34  ? 278 ASP C O   1 
ATOM   10460 C CB  . ASP C 1 278 ? 23.915  5.431   63.663  1.00 58.62  ? 278 ASP C CB  1 
ATOM   10461 C CG  . ASP C 1 278 ? 22.839  6.477   63.367  1.00 65.61  ? 278 ASP C CG  1 
ATOM   10462 O OD1 . ASP C 1 278 ? 22.728  6.903   62.198  1.00 75.91  ? 278 ASP C OD1 1 
ATOM   10463 O OD2 . ASP C 1 278 ? 22.098  6.867   64.298  1.00 66.19  ? 278 ASP C OD2 1 
ATOM   10464 N N   . GLU C 1 279 ? 25.837  7.858   62.856  1.00 60.30  ? 279 GLU C N   1 
ATOM   10465 C CA  . GLU C 1 279 ? 26.679  8.959   63.320  1.00 61.79  ? 279 GLU C CA  1 
ATOM   10466 C C   . GLU C 1 279 ? 26.504  9.233   64.806  1.00 63.42  ? 279 GLU C C   1 
ATOM   10467 O O   . GLU C 1 279 ? 27.363  9.895   65.399  1.00 65.02  ? 279 GLU C O   1 
ATOM   10468 C CB  . GLU C 1 279 ? 26.401  10.247  62.531  1.00 58.84  ? 279 GLU C CB  1 
ATOM   10469 C CG  . GLU C 1 279 ? 24.933  10.569  62.289  1.00 66.98  ? 279 GLU C CG  1 
ATOM   10470 C CD  . GLU C 1 279 ? 24.723  11.934  61.639  1.00 68.39  ? 279 GLU C CD  1 
ATOM   10471 O OE1 . GLU C 1 279 ? 25.681  12.737  61.593  1.00 60.00  ? 279 GLU C OE1 1 
ATOM   10472 O OE2 . GLU C 1 279 ? 23.594  12.203  61.170  1.00 74.84  ? 279 GLU C OE2 1 
ATOM   10473 N N   . VAL C 1 280 ? 25.415  8.747   65.416  1.00 63.99  ? 280 VAL C N   1 
ATOM   10474 C CA  . VAL C 1 280 ? 25.235  8.893   66.861  1.00 65.20  ? 280 VAL C CA  1 
ATOM   10475 C C   . VAL C 1 280 ? 26.386  8.223   67.603  1.00 60.98  ? 280 VAL C C   1 
ATOM   10476 O O   . VAL C 1 280 ? 26.901  8.756   68.594  1.00 63.23  ? 280 VAL C O   1 
ATOM   10477 C CB  . VAL C 1 280 ? 23.864  8.330   67.294  1.00 64.30  ? 280 VAL C CB  1 
ATOM   10478 C CG1 . VAL C 1 280 ? 23.766  8.251   68.803  1.00 61.58  ? 280 VAL C CG1 1 
ATOM   10479 C CG2 . VAL C 1 280 ? 22.737  9.184   66.757  1.00 66.08  ? 280 VAL C CG2 1 
ATOM   10480 N N   . ILE C 1 281 ? 26.815  7.050   67.127  1.00 58.13  ? 281 ILE C N   1 
ATOM   10481 C CA  . ILE C 1 281 ? 27.989  6.389   67.693  1.00 64.73  ? 281 ILE C CA  1 
ATOM   10482 C C   . ILE C 1 281 ? 29.235  7.232   67.463  1.00 63.23  ? 281 ILE C C   1 
ATOM   10483 O O   . ILE C 1 281 ? 30.099  7.348   68.342  1.00 60.72  ? 281 ILE C O   1 
ATOM   10484 C CB  . ILE C 1 281 ? 28.147  4.977   67.099  1.00 61.14  ? 281 ILE C CB  1 
ATOM   10485 C CG1 . ILE C 1 281 ? 26.827  4.219   67.199  1.00 55.36  ? 281 ILE C CG1 1 
ATOM   10486 C CG2 . ILE C 1 281 ? 29.268  4.215   67.795  1.00 51.38  ? 281 ILE C CG2 1 
ATOM   10487 C CD1 . ILE C 1 281 ? 26.268  4.173   68.603  1.00 63.20  ? 281 ILE C CD1 1 
ATOM   10488 N N   . LEU C 1 282 ? 29.348  7.832   66.276  1.00 64.35  ? 282 LEU C N   1 
ATOM   10489 C CA  . LEU C 1 282 ? 30.489  8.691   65.991  1.00 62.33  ? 282 LEU C CA  1 
ATOM   10490 C C   . LEU C 1 282 ? 30.539  9.870   66.956  1.00 61.47  ? 282 LEU C C   1 
ATOM   10491 O O   . LEU C 1 282 ? 31.609  10.218  67.468  1.00 67.77  ? 282 LEU C O   1 
ATOM   10492 C CB  . LEU C 1 282 ? 30.423  9.167   64.540  1.00 59.95  ? 282 LEU C CB  1 
ATOM   10493 C CG  . LEU C 1 282 ? 31.373  10.288  64.128  1.00 61.71  ? 282 LEU C CG  1 
ATOM   10494 C CD1 . LEU C 1 282 ? 32.759  9.749   63.771  1.00 60.89  ? 282 LEU C CD1 1 
ATOM   10495 C CD2 . LEU C 1 282 ? 30.759  11.059  62.972  1.00 60.61  ? 282 LEU C CD2 1 
ATOM   10496 N N   . LYS C 1 283 ? 29.383  10.473  67.244  1.00 58.14  ? 283 LYS C N   1 
ATOM   10497 C CA  . LYS C 1 283 ? 29.341  11.618  68.149  1.00 65.12  ? 283 LYS C CA  1 
ATOM   10498 C C   . LYS C 1 283 ? 29.829  11.245  69.544  1.00 71.86  ? 283 LYS C C   1 
ATOM   10499 O O   . LYS C 1 283 ? 30.509  12.038  70.206  1.00 70.03  ? 283 LYS C O   1 
ATOM   10500 C CB  . LYS C 1 283 ? 27.922  12.175  68.206  1.00 63.46  ? 283 LYS C CB  1 
ATOM   10501 C CG  . LYS C 1 283 ? 27.494  12.865  66.925  1.00 74.13  ? 283 LYS C CG  1 
ATOM   10502 C CD  . LYS C 1 283 ? 28.657  13.597  66.239  1.00 73.99  ? 283 LYS C CD  1 
ATOM   10503 C CE  . LYS C 1 283 ? 28.408  13.750  64.740  1.00 74.59  ? 283 LYS C CE  1 
ATOM   10504 N NZ  . LYS C 1 283 ? 27.939  15.123  64.369  1.00 83.37  ? 283 LYS C NZ  1 
ATOM   10505 N N   . ASN C 1 284 ? 29.490  10.039  70.009  1.00 67.83  ? 284 ASN C N   1 
ATOM   10506 C CA  . ASN C 1 284 ? 29.941  9.596   71.323  1.00 62.94  ? 284 ASN C CA  1 
ATOM   10507 C C   . ASN C 1 284 ? 31.406  9.187   71.312  1.00 62.71  ? 284 ASN C C   1 
ATOM   10508 O O   . ASN C 1 284 ? 32.068  9.235   72.356  1.00 65.77  ? 284 ASN C O   1 
ATOM   10509 C CB  . ASN C 1 284 ? 29.076  8.436   71.807  1.00 61.51  ? 284 ASN C CB  1 
ATOM   10510 C CG  . ASN C 1 284 ? 27.602  8.735   71.702  1.00 57.34  ? 284 ASN C CG  1 
ATOM   10511 O OD1 . ASN C 1 284 ? 27.208  9.853   71.372  1.00 56.94  ? 284 ASN C OD1 1 
ATOM   10512 N ND2 . ASN C 1 284 ? 26.776  7.738   71.987  1.00 57.33  ? 284 ASN C ND2 1 
ATOM   10513 N N   . SER C 1 285 ? 31.930  8.791   70.152  1.00 65.14  ? 285 SER C N   1 
ATOM   10514 C CA  . SER C 1 285 ? 33.281  8.247   70.084  1.00 66.86  ? 285 SER C CA  1 
ATOM   10515 C C   . SER C 1 285 ? 34.336  9.287   69.721  1.00 68.05  ? 285 SER C C   1 
ATOM   10516 O O   . SER C 1 285 ? 35.440  9.246   70.269  1.00 73.45  ? 285 SER C O   1 
ATOM   10517 C CB  . SER C 1 285 ? 33.329  7.084   69.091  1.00 66.60  ? 285 SER C CB  1 
ATOM   10518 O OG  . SER C 1 285 ? 32.352  6.110   69.420  1.00 67.82  ? 285 SER C OG  1 
ATOM   10519 N N   . VAL C 1 286 ? 34.038  10.225  68.823  1.00 67.90  ? 286 VAL C N   1 
ATOM   10520 C CA  . VAL C 1 286 ? 35.018  11.211  68.380  1.00 71.27  ? 286 VAL C CA  1 
ATOM   10521 C C   . VAL C 1 286 ? 34.522  12.605  68.729  1.00 74.16  ? 286 VAL C C   1 
ATOM   10522 O O   . VAL C 1 286 ? 33.335  12.905  68.567  1.00 75.48  ? 286 VAL C O   1 
ATOM   10523 C CB  . VAL C 1 286 ? 35.292  11.117  66.870  1.00 68.65  ? 286 VAL C CB  1 
ATOM   10524 C CG1 . VAL C 1 286 ? 36.151  12.286  66.424  1.00 70.86  ? 286 VAL C CG1 1 
ATOM   10525 C CG2 . VAL C 1 286 ? 35.960  9.815   66.531  1.00 67.61  ? 286 VAL C CG2 1 
ATOM   10526 N N   . GLU C 1 287 ? 35.451  13.460  69.171  1.00 74.47  ? 287 GLU C N   1 
ATOM   10527 C CA  . GLU C 1 287 ? 35.176  14.805  69.671  1.00 84.87  ? 287 GLU C CA  1 
ATOM   10528 C C   . GLU C 1 287 ? 34.254  15.605  68.755  1.00 94.16  ? 287 GLU C C   1 
ATOM   10529 O O   . GLU C 1 287 ? 33.032  15.608  68.943  1.00 98.32  ? 287 GLU C O   1 
ATOM   10530 C CB  . GLU C 1 287 ? 36.489  15.562  69.871  1.00 88.89  ? 287 GLU C CB  1 
ATOM   10531 C CG  . GLU C 1 287 ? 36.543  16.437  71.115  1.00 95.96  ? 287 GLU C CG  1 
ATOM   10532 C CD  . GLU C 1 287 ? 37.548  17.569  70.974  1.00 110.99 ? 287 GLU C CD  1 
ATOM   10533 O OE1 . GLU C 1 287 ? 38.631  17.332  70.393  1.00 105.63 ? 287 GLU C OE1 1 
ATOM   10534 O OE2 . GLU C 1 287 ? 37.257  18.692  71.439  1.00 115.43 ? 287 GLU C OE2 1 
ATOM   10535 N N   . ARG C 1 288 ? 34.820  16.306  67.779  1.00 83.34  ? 288 ARG C N   1 
ATOM   10536 C CA  . ARG C 1 288 ? 34.026  17.012  66.776  1.00 86.86  ? 288 ARG C CA  1 
ATOM   10537 C C   . ARG C 1 288 ? 34.315  16.351  65.432  1.00 86.24  ? 288 ARG C C   1 
ATOM   10538 O O   . ARG C 1 288 ? 35.353  16.612  64.818  1.00 99.41  ? 288 ARG C O   1 
ATOM   10539 C CB  . ARG C 1 288 ? 34.341  18.505  66.753  1.00 93.63  ? 288 ARG C CB  1 
ATOM   10540 C CG  . ARG C 1 288 ? 33.144  19.350  66.334  1.00 100.87 ? 288 ARG C CG  1 
ATOM   10541 C CD  . ARG C 1 288 ? 33.552  20.644  65.646  1.00 107.10 ? 288 ARG C CD  1 
ATOM   10542 N NE  . ARG C 1 288 ? 32.391  21.380  65.155  1.00 118.51 ? 288 ARG C NE  1 
ATOM   10543 C CZ  . ARG C 1 288 ? 31.885  21.266  63.934  1.00 117.47 ? 288 ARG C CZ  1 
ATOM   10544 N NH1 . ARG C 1 288 ? 32.442  20.482  63.024  1.00 113.09 ? 288 ARG C NH1 1 
ATOM   10545 N NH2 . ARG C 1 288 ? 30.791  21.954  63.618  1.00 115.65 ? 288 ARG C NH2 1 
ATOM   10546 N N   . ALA C 1 289 ? 33.405  15.492  64.974  1.00 78.07  ? 289 ALA C N   1 
ATOM   10547 C CA  . ALA C 1 289 ? 33.630  14.678  63.785  1.00 73.12  ? 289 ALA C CA  1 
ATOM   10548 C C   . ALA C 1 289 ? 32.534  14.887  62.751  1.00 66.56  ? 289 ALA C C   1 
ATOM   10549 O O   . ALA C 1 289 ? 31.345  14.887  63.083  1.00 63.65  ? 289 ALA C O   1 
ATOM   10550 C CB  . ALA C 1 289 ? 33.700  13.191  64.142  1.00 70.33  ? 289 ALA C CB  1 
ATOM   10551 N N   . SER C 1 290 ? 32.941  15.047  61.493  1.00 68.70  ? 290 SER C N   1 
ATOM   10552 C CA  . SER C 1 290 ? 31.959  15.014  60.420  1.00 73.81  ? 290 SER C CA  1 
ATOM   10553 C C   . SER C 1 290 ? 31.692  13.572  59.993  1.00 63.86  ? 290 SER C C   1 
ATOM   10554 O O   . SER C 1 290 ? 32.602  12.738  60.010  1.00 60.88  ? 290 SER C O   1 
ATOM   10555 C CB  . SER C 1 290 ? 32.434  15.817  59.218  1.00 71.54  ? 290 SER C CB  1 
ATOM   10556 O OG  . SER C 1 290 ? 31.926  15.246  58.022  1.00 64.45  ? 290 SER C OG  1 
ATOM   10557 N N   . PRO C 1 291 ? 30.468  13.254  59.612  1.00 62.06  ? 291 PRO C N   1 
ATOM   10558 C CA  . PRO C 1 291 ? 30.177  11.888  59.169  1.00 65.55  ? 291 PRO C CA  1 
ATOM   10559 C C   . PRO C 1 291 ? 30.498  11.678  57.696  1.00 60.70  ? 291 PRO C C   1 
ATOM   10560 O O   . PRO C 1 291 ? 29.998  10.734  57.082  1.00 61.10  ? 291 PRO C O   1 
ATOM   10561 C CB  . PRO C 1 291 ? 28.677  11.755  59.457  1.00 54.05  ? 291 PRO C CB  1 
ATOM   10562 C CG  . PRO C 1 291 ? 28.160  13.136  59.256  1.00 55.94  ? 291 PRO C CG  1 
ATOM   10563 C CD  . PRO C 1 291 ? 29.241  14.058  59.766  1.00 58.45  ? 291 PRO C CD  1 
ATOM   10564 N N   . TYR C 1 292 ? 31.351  12.531  57.125  1.00 57.63  ? 292 TYR C N   1 
ATOM   10565 C CA  . TYR C 1 292 ? 31.587  12.541  55.686  1.00 66.55  ? 292 TYR C CA  1 
ATOM   10566 C C   . TYR C 1 292 ? 33.011  12.135  55.317  1.00 68.52  ? 292 TYR C C   1 
ATOM   10567 O O   . TYR C 1 292 ? 33.491  12.472  54.229  1.00 70.58  ? 292 TYR C O   1 
ATOM   10568 C CB  . TYR C 1 292 ? 31.249  13.920  55.115  1.00 67.04  ? 292 TYR C CB  1 
ATOM   10569 C CG  . TYR C 1 292 ? 29.868  14.408  55.510  1.00 67.36  ? 292 TYR C CG  1 
ATOM   10570 C CD1 . TYR C 1 292 ? 28.741  13.641  55.247  1.00 62.53  ? 292 TYR C CD1 1 
ATOM   10571 C CD2 . TYR C 1 292 ? 29.689  15.634  56.146  1.00 63.36  ? 292 TYR C CD2 1 
ATOM   10572 C CE1 . TYR C 1 292 ? 27.473  14.075  55.608  1.00 63.63  ? 292 TYR C CE1 1 
ATOM   10573 C CE2 . TYR C 1 292 ? 28.425  16.075  56.513  1.00 58.64  ? 292 TYR C CE2 1 
ATOM   10574 C CZ  . TYR C 1 292 ? 27.320  15.293  56.241  1.00 63.31  ? 292 TYR C CZ  1 
ATOM   10575 O OH  . TYR C 1 292 ? 26.060  15.724  56.600  1.00 65.23  ? 292 TYR C OH  1 
ATOM   10576 N N   . LEU C 1 293 ? 33.687  11.400  56.192  1.00 65.31  ? 293 LEU C N   1 
ATOM   10577 C CA  . LEU C 1 293 ? 35.065  10.990  55.972  1.00 65.55  ? 293 LEU C CA  1 
ATOM   10578 C C   . LEU C 1 293 ? 35.180  9.494   56.178  1.00 63.94  ? 293 LEU C C   1 
ATOM   10579 O O   . LEU C 1 293 ? 34.575  8.937   57.098  1.00 69.63  ? 293 LEU C O   1 
ATOM   10580 C CB  . LEU C 1 293 ? 36.041  11.684  56.926  1.00 64.00  ? 293 LEU C CB  1 
ATOM   10581 C CG  . LEU C 1 293 ? 36.064  13.197  57.111  1.00 66.81  ? 293 LEU C CG  1 
ATOM   10582 C CD1 . LEU C 1 293 ? 34.898  13.695  57.939  1.00 66.33  ? 293 LEU C CD1 1 
ATOM   10583 C CD2 . LEU C 1 293 ? 37.365  13.555  57.785  1.00 65.19  ? 293 LEU C CD2 1 
ATOM   10584 N N   . ARG C 1 294 ? 35.957  8.845   55.330  1.00 59.59  ? 294 ARG C N   1 
ATOM   10585 C CA  . ARG C 1 294 ? 36.279  7.457   55.593  1.00 59.16  ? 294 ARG C CA  1 
ATOM   10586 C C   . ARG C 1 294 ? 37.150  7.389   56.836  1.00 67.81  ? 294 ARG C C   1 
ATOM   10587 O O   . ARG C 1 294 ? 38.174  8.073   56.925  1.00 66.66  ? 294 ARG C O   1 
ATOM   10588 C CB  . ARG C 1 294 ? 36.992  6.835   54.399  1.00 59.01  ? 294 ARG C CB  1 
ATOM   10589 C CG  . ARG C 1 294 ? 36.934  5.334   54.410  1.00 66.80  ? 294 ARG C CG  1 
ATOM   10590 C CD  . ARG C 1 294 ? 38.055  4.719   53.603  1.00 72.90  ? 294 ARG C CD  1 
ATOM   10591 N NE  . ARG C 1 294 ? 37.936  4.846   52.156  1.00 73.81  ? 294 ARG C NE  1 
ATOM   10592 C CZ  . ARG C 1 294 ? 38.694  5.637   51.407  1.00 81.14  ? 294 ARG C CZ  1 
ATOM   10593 N NH1 . ARG C 1 294 ? 39.583  6.460   51.947  1.00 74.80  ? 294 ARG C NH1 1 
ATOM   10594 N NH2 . ARG C 1 294 ? 38.558  5.602   50.084  1.00 77.17  ? 294 ARG C NH2 1 
ATOM   10595 N N   . TYR C 1 295 ? 36.718  6.617   57.820  1.00 59.55  ? 295 TYR C N   1 
ATOM   10596 C CA  . TYR C 1 295 ? 37.503  6.434   59.028  1.00 58.72  ? 295 TYR C CA  1 
ATOM   10597 C C   . TYR C 1 295 ? 38.163  5.063   59.002  1.00 59.58  ? 295 TYR C C   1 
ATOM   10598 O O   . TYR C 1 295 ? 37.553  4.079   58.577  1.00 61.64  ? 295 TYR C O   1 
ATOM   10599 C CB  . TYR C 1 295 ? 36.636  6.598   60.277  1.00 59.34  ? 295 TYR C CB  1 
ATOM   10600 C CG  . TYR C 1 295 ? 36.160  8.019   60.509  1.00 57.39  ? 295 TYR C CG  1 
ATOM   10601 C CD1 . TYR C 1 295 ? 36.955  8.939   61.176  1.00 59.18  ? 295 TYR C CD1 1 
ATOM   10602 C CD2 . TYR C 1 295 ? 34.915  8.436   60.060  1.00 57.24  ? 295 TYR C CD2 1 
ATOM   10603 C CE1 . TYR C 1 295 ? 36.522  10.235  61.395  1.00 63.90  ? 295 TYR C CE1 1 
ATOM   10604 C CE2 . TYR C 1 295 ? 34.470  9.732   60.273  1.00 61.17  ? 295 TYR C CE2 1 
ATOM   10605 C CZ  . TYR C 1 295 ? 35.279  10.629  60.942  1.00 68.29  ? 295 TYR C CZ  1 
ATOM   10606 O OH  . TYR C 1 295 ? 34.850  11.921  61.158  1.00 67.95  ? 295 TYR C OH  1 
ATOM   10607 N N   . TYR C 1 296 ? 39.428  5.014   59.414  1.00 58.06  ? 296 TYR C N   1 
ATOM   10608 C CA  . TYR C 1 296 ? 40.155  3.762   59.578  1.00 54.88  ? 296 TYR C CA  1 
ATOM   10609 C C   . TYR C 1 296 ? 40.185  3.450   61.065  1.00 65.01  ? 296 TYR C C   1 
ATOM   10610 O O   . TYR C 1 296 ? 40.699  4.247   61.858  1.00 68.06  ? 296 TYR C O   1 
ATOM   10611 C CB  . TYR C 1 296 ? 41.579  3.859   59.023  1.00 63.52  ? 296 TYR C CB  1 
ATOM   10612 C CG  . TYR C 1 296 ? 41.686  3.978   57.512  1.00 74.14  ? 296 TYR C CG  1 
ATOM   10613 C CD1 . TYR C 1 296 ? 40.554  3.939   56.706  1.00 80.26  ? 296 TYR C CD1 1 
ATOM   10614 C CD2 . TYR C 1 296 ? 42.916  4.167   56.893  1.00 79.40  ? 296 TYR C CD2 1 
ATOM   10615 C CE1 . TYR C 1 296 ? 40.636  4.053   55.342  1.00 77.05  ? 296 TYR C CE1 1 
ATOM   10616 C CE2 . TYR C 1 296 ? 43.002  4.292   55.500  1.00 84.77  ? 296 TYR C CE2 1 
ATOM   10617 C CZ  . TYR C 1 296 ? 41.851  4.232   54.736  1.00 83.81  ? 296 TYR C CZ  1 
ATOM   10618 O OH  . TYR C 1 296 ? 41.886  4.345   53.362  1.00 84.80  ? 296 TYR C OH  1 
ATOM   10619 N N   . PHE C 1 297 ? 39.635  2.304   61.446  1.00 63.86  ? 297 PHE C N   1 
ATOM   10620 C CA  . PHE C 1 297 ? 39.626  1.891   62.844  1.00 60.29  ? 297 PHE C CA  1 
ATOM   10621 C C   . PHE C 1 297 ? 40.932  1.164   63.137  1.00 64.43  ? 297 PHE C C   1 
ATOM   10622 O O   . PHE C 1 297 ? 41.129  0.029   62.689  1.00 67.51  ? 297 PHE C O   1 
ATOM   10623 C CB  . PHE C 1 297 ? 38.415  1.012   63.136  1.00 53.02  ? 297 PHE C CB  1 
ATOM   10624 C CG  . PHE C 1 297 ? 38.303  0.603   64.567  1.00 58.12  ? 297 PHE C CG  1 
ATOM   10625 C CD1 . PHE C 1 297 ? 37.674  1.428   65.484  1.00 61.83  ? 297 PHE C CD1 1 
ATOM   10626 C CD2 . PHE C 1 297 ? 38.845  -0.591  65.007  1.00 56.72  ? 297 PHE C CD2 1 
ATOM   10627 C CE1 . PHE C 1 297 ? 37.572  1.066   66.810  1.00 58.73  ? 297 PHE C CE1 1 
ATOM   10628 C CE2 . PHE C 1 297 ? 38.747  -0.960  66.336  1.00 53.12  ? 297 PHE C CE2 1 
ATOM   10629 C CZ  . PHE C 1 297 ? 38.110  -0.131  67.238  1.00 58.46  ? 297 PHE C CZ  1 
ATOM   10630 N N   . ARG C 1 298 ? 41.832  1.827   63.869  1.00 63.48  ? 298 ARG C N   1 
ATOM   10631 C CA  . ARG C 1 298 ? 43.146  1.285   64.214  1.00 58.98  ? 298 ARG C CA  1 
ATOM   10632 C C   . ARG C 1 298 ? 43.928  0.845   62.985  1.00 67.55  ? 298 ARG C C   1 
ATOM   10633 O O   . ARG C 1 298 ? 44.784  -0.042  63.079  1.00 77.63  ? 298 ARG C O   1 
ATOM   10634 C CB  . ARG C 1 298 ? 43.021  0.117   65.192  1.00 52.48  ? 298 ARG C CB  1 
ATOM   10635 C CG  . ARG C 1 298 ? 42.243  0.467   66.428  1.00 56.01  ? 298 ARG C CG  1 
ATOM   10636 C CD  . ARG C 1 298 ? 42.545  -0.443  67.604  1.00 51.91  ? 298 ARG C CD  1 
ATOM   10637 N NE  . ARG C 1 298 ? 41.538  -0.227  68.628  1.00 51.02  ? 298 ARG C NE  1 
ATOM   10638 C CZ  . ARG C 1 298 ? 40.800  -1.179  69.175  1.00 53.41  ? 298 ARG C CZ  1 
ATOM   10639 N NH1 . ARG C 1 298 ? 41.004  -2.461  68.903  1.00 49.28  ? 298 ARG C NH1 1 
ATOM   10640 N NH2 . ARG C 1 298 ? 39.829  -0.833  70.011  1.00 54.10  ? 298 ARG C NH2 1 
ATOM   10641 N N   . GLU C 1 299 ? 43.617  1.438   61.829  1.00 69.00  ? 299 GLU C N   1 
ATOM   10642 C CA  . GLU C 1 299 ? 44.145  1.073   60.514  1.00 71.87  ? 299 GLU C CA  1 
ATOM   10643 C C   . GLU C 1 299 ? 43.689  -0.324  60.092  1.00 74.21  ? 299 GLU C C   1 
ATOM   10644 O O   . GLU C 1 299 ? 44.004  -0.766  58.985  1.00 77.15  ? 299 GLU C O   1 
ATOM   10645 C CB  . GLU C 1 299 ? 45.682  1.156   60.474  1.00 69.09  ? 299 GLU C CB  1 
ATOM   10646 C CG  . GLU C 1 299 ? 46.317  2.121   59.412  1.00 90.51  ? 299 GLU C CG  1 
ATOM   10647 C CD  . GLU C 1 299 ? 46.145  1.759   57.921  1.00 97.95  ? 299 GLU C CD  1 
ATOM   10648 O OE1 . GLU C 1 299 ? 46.783  2.457   57.085  1.00 87.22  ? 299 GLU C OE1 1 
ATOM   10649 O OE2 . GLU C 1 299 ? 45.403  0.807   57.587  1.00 90.41  ? 299 GLU C OE2 1 
ATOM   10650 N N   . LEU C 1 300 ? 42.940  -1.036  60.931  1.00 66.15  ? 300 LEU C N   1 
ATOM   10651 C CA  . LEU C 1 300 ? 42.604  -2.406  60.563  1.00 67.44  ? 300 LEU C CA  1 
ATOM   10652 C C   . LEU C 1 300 ? 41.477  -2.436  59.531  1.00 64.08  ? 300 LEU C C   1 
ATOM   10653 O O   . LEU C 1 300 ? 41.639  -2.993  58.440  1.00 58.38  ? 300 LEU C O   1 
ATOM   10654 C CB  . LEU C 1 300 ? 42.274  -3.206  61.823  1.00 66.21  ? 300 LEU C CB  1 
ATOM   10655 C CG  . LEU C 1 300 ? 43.532  -3.362  62.700  1.00 74.88  ? 300 LEU C CG  1 
ATOM   10656 C CD1 . LEU C 1 300 ? 43.409  -4.559  63.613  1.00 78.88  ? 300 LEU C CD1 1 
ATOM   10657 C CD2 . LEU C 1 300 ? 44.836  -3.485  61.877  1.00 58.27  ? 300 LEU C CD2 1 
ATOM   10658 N N   . ILE C 1 301 ? 40.357  -1.778  59.823  1.00 56.39  ? 301 ILE C N   1 
ATOM   10659 C CA  . ILE C 1 301 ? 39.183  -1.814  58.962  1.00 52.63  ? 301 ILE C CA  1 
ATOM   10660 C C   . ILE C 1 301 ? 38.665  -0.398  58.746  1.00 60.35  ? 301 ILE C C   1 
ATOM   10661 O O   . ILE C 1 301 ? 38.811  0.477   59.608  1.00 57.28  ? 301 ILE C O   1 
ATOM   10662 C CB  . ILE C 1 301 ? 38.087  -2.719  59.562  1.00 55.77  ? 301 ILE C CB  1 
ATOM   10663 C CG1 . ILE C 1 301 ? 36.882  -2.818  58.627  1.00 56.68  ? 301 ILE C CG1 1 
ATOM   10664 C CG2 . ILE C 1 301 ? 37.671  -2.204  60.932  1.00 58.53  ? 301 ILE C CG2 1 
ATOM   10665 C CD1 . ILE C 1 301 ? 35.759  -3.622  59.196  1.00 57.75  ? 301 ILE C CD1 1 
ATOM   10666 N N   . SER C 1 302 ? 38.061  -0.175  57.577  1.00 56.48  ? 302 SER C N   1 
ATOM   10667 C CA  . SER C 1 302 ? 37.493  1.119   57.223  1.00 55.79  ? 302 SER C CA  1 
ATOM   10668 C C   . SER C 1 302 ? 36.027  1.172   57.623  1.00 59.34  ? 302 SER C C   1 
ATOM   10669 O O   . SER C 1 302 ? 35.249  0.269   57.296  1.00 55.45  ? 302 SER C O   1 
ATOM   10670 C CB  . SER C 1 302 ? 37.624  1.383   55.724  1.00 59.64  ? 302 SER C CB  1 
ATOM   10671 O OG  . SER C 1 302 ? 38.922  1.062   55.268  1.00 73.43  ? 302 SER C OG  1 
ATOM   10672 N N   . VAL C 1 303 ? 35.657  2.231   58.328  1.00 55.24  ? 303 VAL C N   1 
ATOM   10673 C CA  . VAL C 1 303 ? 34.290  2.438   58.773  1.00 53.19  ? 303 VAL C CA  1 
ATOM   10674 C C   . VAL C 1 303 ? 33.764  3.710   58.138  1.00 54.15  ? 303 VAL C C   1 
ATOM   10675 O O   . VAL C 1 303 ? 34.492  4.697   57.993  1.00 56.36  ? 303 VAL C O   1 
ATOM   10676 C CB  . VAL C 1 303 ? 34.182  2.531   60.307  1.00 54.81  ? 303 VAL C CB  1 
ATOM   10677 C CG1 . VAL C 1 303 ? 32.756  2.287   60.735  1.00 53.00  ? 303 VAL C CG1 1 
ATOM   10678 C CG2 . VAL C 1 303 ? 35.115  1.542   60.968  1.00 59.43  ? 303 VAL C CG2 1 
ATOM   10679 N N   . PHE C 1 304 ? 32.495  3.679   57.763  1.00 57.34  ? 304 PHE C N   1 
ATOM   10680 C CA  . PHE C 1 304 ? 31.773  4.865   57.348  1.00 59.62  ? 304 PHE C CA  1 
ATOM   10681 C C   . PHE C 1 304 ? 30.620  5.108   58.311  1.00 58.49  ? 304 PHE C C   1 
ATOM   10682 O O   . PHE C 1 304 ? 30.042  4.168   58.862  1.00 57.51  ? 304 PHE C O   1 
ATOM   10683 C CB  . PHE C 1 304 ? 31.233  4.718   55.935  1.00 49.54  ? 304 PHE C CB  1 
ATOM   10684 C CG  . PHE C 1 304 ? 32.255  4.930   54.862  1.00 48.05  ? 304 PHE C CG  1 
ATOM   10685 C CD1 . PHE C 1 304 ? 32.583  6.209   54.448  1.00 51.64  ? 304 PHE C CD1 1 
ATOM   10686 C CD2 . PHE C 1 304 ? 32.857  3.854   54.237  1.00 50.08  ? 304 PHE C CD2 1 
ATOM   10687 C CE1 . PHE C 1 304 ? 33.504  6.412   53.446  1.00 54.08  ? 304 PHE C CE1 1 
ATOM   10688 C CE2 . PHE C 1 304 ? 33.780  4.051   53.230  1.00 51.41  ? 304 PHE C CE2 1 
ATOM   10689 C CZ  . PHE C 1 304 ? 34.098  5.331   52.828  1.00 55.84  ? 304 PHE C CZ  1 
ATOM   10690 N N   . PHE C 1 305 ? 30.288  6.374   58.512  1.00 53.39  ? 305 PHE C N   1 
ATOM   10691 C CA  . PHE C 1 305 ? 29.166  6.749   59.356  1.00 56.74  ? 305 PHE C CA  1 
ATOM   10692 C C   . PHE C 1 305 ? 28.078  7.356   58.481  1.00 62.57  ? 305 PHE C C   1 
ATOM   10693 O O   . PHE C 1 305 ? 28.358  8.231   57.654  1.00 66.20  ? 305 PHE C O   1 
ATOM   10694 C CB  . PHE C 1 305 ? 29.616  7.717   60.450  1.00 55.37  ? 305 PHE C CB  1 
ATOM   10695 C CG  . PHE C 1 305 ? 30.599  7.112   61.409  1.00 58.66  ? 305 PHE C CG  1 
ATOM   10696 C CD1 . PHE C 1 305 ? 30.164  6.367   62.495  1.00 55.78  ? 305 PHE C CD1 1 
ATOM   10697 C CD2 . PHE C 1 305 ? 31.964  7.263   61.211  1.00 59.62  ? 305 PHE C CD2 1 
ATOM   10698 C CE1 . PHE C 1 305 ? 31.074  5.800   63.376  1.00 57.67  ? 305 PHE C CE1 1 
ATOM   10699 C CE2 . PHE C 1 305 ? 32.876  6.696   62.084  1.00 56.36  ? 305 PHE C CE2 1 
ATOM   10700 C CZ  . PHE C 1 305 ? 32.433  5.967   63.166  1.00 61.79  ? 305 PHE C CZ  1 
ATOM   10701 N N   . ARG C 1 306 ? 26.848  6.875   58.648  1.00 54.14  ? 306 ARG C N   1 
ATOM   10702 C CA  . ARG C 1 306 ? 25.734  7.313   57.825  1.00 58.02  ? 306 ARG C CA  1 
ATOM   10703 C C   . ARG C 1 306 ? 25.219  8.674   58.292  1.00 64.37  ? 306 ARG C C   1 
ATOM   10704 O O   . ARG C 1 306 ? 25.591  9.181   59.355  1.00 66.01  ? 306 ARG C O   1 
ATOM   10705 C CB  . ARG C 1 306 ? 24.603  6.286   57.865  1.00 64.29  ? 306 ARG C CB  1 
ATOM   10706 C CG  . ARG C 1 306 ? 23.578  6.567   58.955  1.00 66.21  ? 306 ARG C CG  1 
ATOM   10707 C CD  . ARG C 1 306 ? 22.496  5.506   59.044  1.00 67.44  ? 306 ARG C CD  1 
ATOM   10708 N NE  . ARG C 1 306 ? 21.770  5.618   60.304  1.00 59.47  ? 306 ARG C NE  1 
ATOM   10709 C CZ  . ARG C 1 306 ? 20.454  5.712   60.408  1.00 59.86  ? 306 ARG C CZ  1 
ATOM   10710 N NH1 . ARG C 1 306 ? 19.670  5.632   59.343  1.00 66.55  ? 306 ARG C NH1 1 
ATOM   10711 N NH2 . ARG C 1 306 ? 19.912  5.889   61.609  1.00 61.72  ? 306 ARG C NH2 1 
ATOM   10712 N N   . ASP C 1 307 ? 24.338  9.262   57.479  1.00 64.22  ? 307 ASP C N   1 
ATOM   10713 C CA  . ASP C 1 307 ? 23.695  10.539  57.786  1.00 65.47  ? 307 ASP C CA  1 
ATOM   10714 C C   . ASP C 1 307 ? 22.318  10.233  58.365  1.00 67.10  ? 307 ASP C C   1 
ATOM   10715 O O   . ASP C 1 307 ? 21.389  9.871   57.636  1.00 63.08  ? 307 ASP C O   1 
ATOM   10716 C CB  . ASP C 1 307 ? 23.609  11.420  56.543  1.00 66.06  ? 307 ASP C CB  1 
ATOM   10717 C CG  . ASP C 1 307 ? 23.240  12.859  56.869  1.00 73.20  ? 307 ASP C CG  1 
ATOM   10718 O OD1 . ASP C 1 307 ? 22.191  13.081  57.512  1.00 69.60  ? 307 ASP C OD1 1 
ATOM   10719 O OD2 . ASP C 1 307 ? 24.003  13.774  56.487  1.00 71.58  ? 307 ASP C OD2 1 
ATOM   10720 N N   . LYS C 1 308 ? 22.195  10.382  59.686  1.00 70.37  ? 308 LYS C N   1 
ATOM   10721 C CA  . LYS C 1 308 ? 20.949  10.050  60.368  1.00 65.56  ? 308 LYS C CA  1 
ATOM   10722 C C   . LYS C 1 308 ? 19.803  10.923  59.871  1.00 62.46  ? 308 LYS C C   1 
ATOM   10723 O O   . LYS C 1 308 ? 18.739  10.414  59.505  1.00 60.66  ? 308 LYS C O   1 
ATOM   10724 C CB  . LYS C 1 308 ? 21.131  10.194  61.880  1.00 61.52  ? 308 LYS C CB  1 
ATOM   10725 C CG  . LYS C 1 308 ? 19.979  9.638   62.696  1.00 71.51  ? 308 LYS C CG  1 
ATOM   10726 C CD  . LYS C 1 308 ? 20.318  9.516   64.175  1.00 73.15  ? 308 LYS C CD  1 
ATOM   10727 C CE  . LYS C 1 308 ? 19.169  10.034  65.033  1.00 69.40  ? 308 LYS C CE  1 
ATOM   10728 N NZ  . LYS C 1 308 ? 18.216  8.959   65.429  1.00 71.14  ? 308 LYS C NZ  1 
ATOM   10729 N N   . THR C 1 309 ? 20.011  12.244  59.842  1.00 64.11  ? 309 THR C N   1 
ATOM   10730 C CA  . THR C 1 309 ? 18.969  13.168  59.389  1.00 66.40  ? 309 THR C CA  1 
ATOM   10731 C C   . THR C 1 309 ? 18.474  12.802  57.995  1.00 66.37  ? 309 THR C C   1 
ATOM   10732 O O   . THR C 1 309 ? 17.264  12.695  57.756  1.00 62.97  ? 309 THR C O   1 
ATOM   10733 C CB  . THR C 1 309 ? 19.503  14.601  59.400  1.00 66.51  ? 309 THR C CB  1 
ATOM   10734 O OG1 . THR C 1 309 ? 19.678  15.041  60.750  1.00 62.11  ? 309 THR C OG1 1 
ATOM   10735 C CG2 . THR C 1 309 ? 18.543  15.543  58.678  1.00 58.96  ? 309 THR C CG2 1 
ATOM   10736 N N   . LEU C 1 310 ? 19.405  12.592  57.064  1.00 63.98  ? 310 LEU C N   1 
ATOM   10737 C CA  . LEU C 1 310 ? 19.027  12.267  55.692  1.00 66.92  ? 310 LEU C CA  1 
ATOM   10738 C C   . LEU C 1 310 ? 18.339  10.909  55.619  1.00 67.86  ? 310 LEU C C   1 
ATOM   10739 O O   . LEU C 1 310 ? 17.284  10.766  54.987  1.00 68.47  ? 310 LEU C O   1 
ATOM   10740 C CB  . LEU C 1 310 ? 20.266  12.300  54.796  1.00 69.67  ? 310 LEU C CB  1 
ATOM   10741 C CG  . LEU C 1 310 ? 20.463  13.546  53.920  1.00 66.35  ? 310 LEU C CG  1 
ATOM   10742 C CD1 . LEU C 1 310 ? 20.190  14.864  54.665  1.00 64.95  ? 310 LEU C CD1 1 
ATOM   10743 C CD2 . LEU C 1 310 ? 21.856  13.535  53.297  1.00 77.29  ? 310 LEU C CD2 1 
ATOM   10744 N N   . SER C 1 311 ? 18.917  9.898   56.273  1.00 63.29  ? 311 SER C N   1 
ATOM   10745 C CA  . SER C 1 311 ? 18.373  8.548   56.178  1.00 59.35  ? 311 SER C CA  1 
ATOM   10746 C C   . SER C 1 311 ? 17.009  8.445   56.846  1.00 55.39  ? 311 SER C C   1 
ATOM   10747 O O   . SER C 1 311 ? 16.125  7.739   56.349  1.00 57.18  ? 311 SER C O   1 
ATOM   10748 C CB  . SER C 1 311 ? 19.347  7.547   56.794  1.00 65.62  ? 311 SER C CB  1 
ATOM   10749 O OG  . SER C 1 311 ? 20.615  7.612   56.163  1.00 62.46  ? 311 SER C OG  1 
ATOM   10750 N N   . ASP C 1 312 ? 16.818  9.136   57.976  1.00 61.85  ? 312 ASP C N   1 
ATOM   10751 C CA  . ASP C 1 312 ? 15.526  9.080   58.653  1.00 61.47  ? 312 ASP C CA  1 
ATOM   10752 C C   . ASP C 1 312 ? 14.445  9.797   57.853  1.00 63.31  ? 312 ASP C C   1 
ATOM   10753 O O   . ASP C 1 312 ? 13.265  9.440   57.954  1.00 61.75  ? 312 ASP C O   1 
ATOM   10754 C CB  . ASP C 1 312 ? 15.612  9.680   60.061  1.00 55.93  ? 312 ASP C CB  1 
ATOM   10755 C CG  . ASP C 1 312 ? 16.493  8.870   61.014  1.00 63.44  ? 312 ASP C CG  1 
ATOM   10756 O OD1 . ASP C 1 312 ? 16.723  7.660   60.783  1.00 57.59  ? 312 ASP C OD1 1 
ATOM   10757 O OD2 . ASP C 1 312 ? 16.938  9.458   62.024  1.00 61.70  ? 312 ASP C OD2 1 
ATOM   10758 N N   . LEU C 1 313 ? 14.822  10.811  57.068  1.00 60.85  ? 313 LEU C N   1 
ATOM   10759 C CA  . LEU C 1 313 ? 13.839  11.525  56.260  1.00 56.98  ? 313 LEU C CA  1 
ATOM   10760 C C   . LEU C 1 313 ? 13.212  10.599  55.228  1.00 62.05  ? 313 LEU C C   1 
ATOM   10761 O O   . LEU C 1 313 ? 11.990  10.588  55.047  1.00 62.69  ? 313 LEU C O   1 
ATOM   10762 C CB  . LEU C 1 313 ? 14.486  12.725  55.577  1.00 61.88  ? 313 LEU C CB  1 
ATOM   10763 C CG  . LEU C 1 313 ? 14.723  13.963  56.436  1.00 62.35  ? 313 LEU C CG  1 
ATOM   10764 C CD1 . LEU C 1 313 ? 15.835  14.799  55.835  1.00 62.28  ? 313 LEU C CD1 1 
ATOM   10765 C CD2 . LEU C 1 313 ? 13.455  14.766  56.556  1.00 57.43  ? 313 LEU C CD2 1 
ATOM   10766 N N   . ILE C 1 314 ? 14.037  9.811   54.537  1.00 64.80  ? 314 ILE C N   1 
ATOM   10767 C CA  . ILE C 1 314 ? 13.496  8.824   53.610  1.00 61.95  ? 314 ILE C CA  1 
ATOM   10768 C C   . ILE C 1 314 ? 12.759  7.735   54.371  1.00 62.92  ? 314 ILE C C   1 
ATOM   10769 O O   . ILE C 1 314 ? 11.725  7.230   53.915  1.00 62.59  ? 314 ILE C O   1 
ATOM   10770 C CB  . ILE C 1 314 ? 14.612  8.237   52.729  1.00 64.80  ? 314 ILE C CB  1 
ATOM   10771 C CG1 . ILE C 1 314 ? 15.646  9.311   52.378  1.00 65.47  ? 314 ILE C CG1 1 
ATOM   10772 C CG2 . ILE C 1 314 ? 14.011  7.620   51.480  1.00 65.60  ? 314 ILE C CG2 1 
ATOM   10773 C CD1 . ILE C 1 314 ? 16.671  8.866   51.356  1.00 57.66  ? 314 ILE C CD1 1 
ATOM   10774 N N   . GLY C 1 315 ? 13.273  7.362   55.542  1.00 62.05  ? 315 GLY C N   1 
ATOM   10775 C CA  . GLY C 1 315 ? 12.609  6.400   56.397  1.00 56.24  ? 315 GLY C CA  1 
ATOM   10776 C C   . GLY C 1 315 ? 11.248  6.870   56.860  1.00 63.78  ? 315 GLY C C   1 
ATOM   10777 O O   . GLY C 1 315 ? 10.222  6.285   56.501  1.00 74.93  ? 315 GLY C O   1 
ATOM   10778 N N   . PHE C 1 316 ? 11.221  7.963   57.618  1.00 64.31  ? 316 PHE C N   1 
ATOM   10779 C CA  . PHE C 1 316 ? 10.035  8.337   58.377  1.00 65.60  ? 316 PHE C CA  1 
ATOM   10780 C C   . PHE C 1 316 ? 9.265   9.506   57.767  1.00 63.80  ? 316 PHE C C   1 
ATOM   10781 O O   . PHE C 1 316 ? 8.061   9.394   57.522  1.00 71.14  ? 316 PHE C O   1 
ATOM   10782 C CB  . PHE C 1 316 ? 10.460  8.630   59.820  1.00 62.23  ? 316 PHE C CB  1 
ATOM   10783 C CG  . PHE C 1 316 ? 11.277  7.524   60.426  1.00 54.77  ? 316 PHE C CG  1 
ATOM   10784 C CD1 . PHE C 1 316 ? 10.692  6.299   60.710  1.00 57.20  ? 316 PHE C CD1 1 
ATOM   10785 C CD2 . PHE C 1 316 ? 12.624  7.695   60.692  1.00 58.09  ? 316 PHE C CD2 1 
ATOM   10786 C CE1 . PHE C 1 316 ? 11.426  5.268   61.261  1.00 58.07  ? 316 PHE C CE1 1 
ATOM   10787 C CE2 . PHE C 1 316 ? 13.372  6.659   61.248  1.00 63.17  ? 316 PHE C CE2 1 
ATOM   10788 C CZ  . PHE C 1 316 ? 12.769  5.447   61.531  1.00 60.93  ? 316 PHE C CZ  1 
ATOM   10789 N N   . SER C 1 317 ? 9.932   10.628  57.506  1.00 58.37  ? 317 SER C N   1 
ATOM   10790 C CA  . SER C 1 317 ? 9.172   11.845  57.231  1.00 62.97  ? 317 SER C CA  1 
ATOM   10791 C C   . SER C 1 317 ? 8.639   11.901  55.805  1.00 68.39  ? 317 SER C C   1 
ATOM   10792 O O   . SER C 1 317 ? 7.503   12.337  55.585  1.00 71.85  ? 317 SER C O   1 
ATOM   10793 C CB  . SER C 1 317 ? 10.020  13.082  57.516  1.00 63.24  ? 317 SER C CB  1 
ATOM   10794 O OG  . SER C 1 317 ? 10.832  12.887  58.655  1.00 73.98  ? 317 SER C OG  1 
ATOM   10795 N N   . TYR C 1 318 ? 9.435   11.476  54.826  1.00 69.60  ? 318 TYR C N   1 
ATOM   10796 C CA  . TYR C 1 318 ? 9.127   11.834  53.444  1.00 71.83  ? 318 TYR C CA  1 
ATOM   10797 C C   . TYR C 1 318 ? 7.890   11.142  52.890  1.00 67.76  ? 318 TYR C C   1 
ATOM   10798 O O   . TYR C 1 318 ? 7.446   11.514  51.798  1.00 70.77  ? 318 TYR C O   1 
ATOM   10799 C CB  . TYR C 1 318 ? 10.323  11.541  52.538  1.00 67.14  ? 318 TYR C CB  1 
ATOM   10800 C CG  . TYR C 1 318 ? 11.373  12.632  52.517  1.00 68.98  ? 318 TYR C CG  1 
ATOM   10801 C CD1 . TYR C 1 318 ? 11.070  13.932  52.902  1.00 66.77  ? 318 TYR C CD1 1 
ATOM   10802 C CD2 . TYR C 1 318 ? 12.672  12.356  52.111  1.00 71.89  ? 318 TYR C CD2 1 
ATOM   10803 C CE1 . TYR C 1 318 ? 12.033  14.926  52.880  1.00 73.65  ? 318 TYR C CE1 1 
ATOM   10804 C CE2 . TYR C 1 318 ? 13.642  13.343  52.086  1.00 68.34  ? 318 TYR C CE2 1 
ATOM   10805 C CZ  . TYR C 1 318 ? 13.319  14.626  52.471  1.00 71.66  ? 318 TYR C CZ  1 
ATOM   10806 O OH  . TYR C 1 318 ? 14.281  15.611  52.448  1.00 71.06  ? 318 TYR C OH  1 
ATOM   10807 N N   . HIS C 1 319 ? 7.324   10.158  53.596  1.00 68.83  ? 319 HIS C N   1 
ATOM   10808 C CA  . HIS C 1 319 ? 6.074   9.569   53.124  1.00 67.80  ? 319 HIS C CA  1 
ATOM   10809 C C   . HIS C 1 319 ? 4.940   10.584  53.163  1.00 71.49  ? 319 HIS C C   1 
ATOM   10810 O O   . HIS C 1 319 ? 4.027   10.526  52.329  1.00 65.93  ? 319 HIS C O   1 
ATOM   10811 C CB  . HIS C 1 319 ? 5.716   8.327   53.944  1.00 61.50  ? 319 HIS C CB  1 
ATOM   10812 C CG  . HIS C 1 319 ? 5.110   8.635   55.275  1.00 65.59  ? 319 HIS C CG  1 
ATOM   10813 N ND1 . HIS C 1 319 ? 5.806   9.274   56.278  1.00 69.18  ? 319 HIS C ND1 1 
ATOM   10814 C CD2 . HIS C 1 319 ? 3.870   8.404   55.763  1.00 71.07  ? 319 HIS C CD2 1 
ATOM   10815 C CE1 . HIS C 1 319 ? 5.023   9.414   57.332  1.00 66.67  ? 319 HIS C CE1 1 
ATOM   10816 N NE2 . HIS C 1 319 ? 3.842   8.897   57.045  1.00 76.88  ? 319 HIS C NE2 1 
ATOM   10817 N N   . ALA C 1 320 ? 4.991   11.528  54.110  1.00 66.89  ? 320 ALA C N   1 
ATOM   10818 C CA  . ALA C 1 320 ? 4.022   12.617  54.139  1.00 71.09  ? 320 ALA C CA  1 
ATOM   10819 C C   . ALA C 1 320 ? 4.257   13.623  53.014  1.00 77.33  ? 320 ALA C C   1 
ATOM   10820 O O   . ALA C 1 320 ? 3.296   14.208  52.502  1.00 78.75  ? 320 ALA C O   1 
ATOM   10821 C CB  . ALA C 1 320 ? 4.074   13.324  55.495  1.00 63.14  ? 320 ALA C CB  1 
ATOM   10822 N N   . TRP C 1 321 ? 5.511   13.836  52.617  1.00 84.52  ? 321 TRP C N   1 
ATOM   10823 C CA  . TRP C 1 321 ? 5.828   14.848  51.617  1.00 78.12  ? 321 TRP C CA  1 
ATOM   10824 C C   . TRP C 1 321 ? 5.432   14.386  50.222  1.00 83.27  ? 321 TRP C C   1 
ATOM   10825 O O   . TRP C 1 321 ? 5.524   13.203  49.886  1.00 86.75  ? 321 TRP C O   1 
ATOM   10826 C CB  . TRP C 1 321 ? 7.323   15.157  51.604  1.00 77.25  ? 321 TRP C CB  1 
ATOM   10827 C CG  . TRP C 1 321 ? 7.915   15.645  52.888  1.00 82.84  ? 321 TRP C CG  1 
ATOM   10828 C CD1 . TRP C 1 321 ? 7.643   15.199  54.149  1.00 74.33  ? 321 TRP C CD1 1 
ATOM   10829 C CD2 . TRP C 1 321 ? 8.922   16.653  53.028  1.00 87.33  ? 321 TRP C CD2 1 
ATOM   10830 N NE1 . TRP C 1 321 ? 8.404   15.881  55.065  1.00 82.00  ? 321 TRP C NE1 1 
ATOM   10831 C CE2 . TRP C 1 321 ? 9.200   16.778  54.402  1.00 91.21  ? 321 TRP C CE2 1 
ATOM   10832 C CE3 . TRP C 1 321 ? 9.610   17.469  52.122  1.00 78.90  ? 321 TRP C CE3 1 
ATOM   10833 C CZ2 . TRP C 1 321 ? 10.136  17.684  54.894  1.00 95.04  ? 321 TRP C CZ2 1 
ATOM   10834 C CZ3 . TRP C 1 321 ? 10.535  18.366  52.611  1.00 79.93  ? 321 TRP C CZ3 1 
ATOM   10835 C CH2 . TRP C 1 321 ? 10.792  18.468  53.984  1.00 90.88  ? 321 TRP C CH2 1 
ATOM   10836 N N   . ASN C 1 322 ? 5.025   15.345  49.394  1.00 85.41  ? 322 ASN C N   1 
ATOM   10837 C CA  . ASN C 1 322 ? 4.905   15.089  47.966  1.00 82.38  ? 322 ASN C CA  1 
ATOM   10838 C C   . ASN C 1 322 ? 6.288   14.854  47.368  1.00 87.11  ? 322 ASN C C   1 
ATOM   10839 O O   . ASN C 1 322 ? 7.294   15.378  47.854  1.00 88.55  ? 322 ASN C O   1 
ATOM   10840 C CB  . ASN C 1 322 ? 4.214   16.254  47.266  1.00 82.94  ? 322 ASN C CB  1 
ATOM   10841 C CG  . ASN C 1 322 ? 2.723   16.262  47.505  1.00 92.23  ? 322 ASN C CG  1 
ATOM   10842 O OD1 . ASN C 1 322 ? 2.022   17.202  47.129  1.00 98.53  ? 322 ASN C OD1 1 
ATOM   10843 N ND2 . ASN C 1 322 ? 2.227   15.206  48.137  1.00 91.09  ? 322 ASN C ND2 1 
ATOM   10844 N N   . ALA C 1 323 ? 6.330   14.054  46.298  1.00 86.79  ? 323 ALA C N   1 
ATOM   10845 C CA  . ALA C 1 323 ? 7.604   13.529  45.809  1.00 82.77  ? 323 ALA C CA  1 
ATOM   10846 C C   . ALA C 1 323 ? 8.534   14.645  45.345  1.00 84.99  ? 323 ALA C C   1 
ATOM   10847 O O   . ALA C 1 323 ? 9.725   14.650  45.678  1.00 87.08  ? 323 ALA C O   1 
ATOM   10848 C CB  . ALA C 1 323 ? 7.362   12.525  44.681  1.00 82.98  ? 323 ALA C CB  1 
ATOM   10849 N N   . GLU C 1 324 ? 8.013   15.596  44.566  1.00 80.60  ? 324 GLU C N   1 
ATOM   10850 C CA  . GLU C 1 324 ? 8.855   16.692  44.092  1.00 80.54  ? 324 GLU C CA  1 
ATOM   10851 C C   . GLU C 1 324 ? 9.401   17.511  45.251  1.00 83.72  ? 324 GLU C C   1 
ATOM   10852 O O   . GLU C 1 324 ? 10.550  17.968  45.210  1.00 87.73  ? 324 GLU C O   1 
ATOM   10853 C CB  . GLU C 1 324 ? 8.077   17.590  43.136  1.00 84.55  ? 324 GLU C CB  1 
ATOM   10854 C CG  . GLU C 1 324 ? 8.175   17.168  41.692  1.00 87.94  ? 324 GLU C CG  1 
ATOM   10855 C CD  . GLU C 1 324 ? 6.856   16.677  41.152  1.00 97.62  ? 324 GLU C CD  1 
ATOM   10856 O OE1 . GLU C 1 324 ? 6.138   15.971  41.892  1.00 102.68 ? 324 GLU C OE1 1 
ATOM   10857 O OE2 . GLU C 1 324 ? 6.535   17.008  39.992  1.00 104.81 ? 324 GLU C OE2 1 
ATOM   10858 N N   . ASP C 1 325 ? 8.592   17.710  46.294  1.00 76.70  ? 325 ASP C N   1 
ATOM   10859 C CA  . ASP C 1 325 ? 9.063   18.425  47.476  1.00 78.47  ? 325 ASP C CA  1 
ATOM   10860 C C   . ASP C 1 325 ? 10.127  17.628  48.218  1.00 80.22  ? 325 ASP C C   1 
ATOM   10861 O O   . ASP C 1 325 ? 11.125  18.194  48.682  1.00 80.34  ? 325 ASP C O   1 
ATOM   10862 C CB  . ASP C 1 325 ? 7.887   18.733  48.400  1.00 88.65  ? 325 ASP C CB  1 
ATOM   10863 C CG  . ASP C 1 325 ? 6.708   19.337  47.663  1.00 95.53  ? 325 ASP C CG  1 
ATOM   10864 O OD1 . ASP C 1 325 ? 6.132   18.651  46.792  1.00 93.66  ? 325 ASP C OD1 1 
ATOM   10865 O OD2 . ASP C 1 325 ? 6.367   20.507  47.943  1.00 99.61  ? 325 ASP C OD2 1 
ATOM   10866 N N   . ALA C 1 326 ? 9.930   16.313  48.341  1.00 80.36  ? 326 ALA C N   1 
ATOM   10867 C CA  . ALA C 1 326 ? 10.880  15.478  49.071  1.00 78.69  ? 326 ALA C CA  1 
ATOM   10868 C C   . ALA C 1 326 ? 12.225  15.415  48.359  1.00 74.11  ? 326 ALA C C   1 
ATOM   10869 O O   . ALA C 1 326 ? 13.278  15.606  48.979  1.00 70.98  ? 326 ALA C O   1 
ATOM   10870 C CB  . ALA C 1 326 ? 10.303  14.076  49.256  1.00 77.37  ? 326 ALA C CB  1 
ATOM   10871 N N   . VAL C 1 327 ? 12.209  15.138  47.055  1.00 71.99  ? 327 VAL C N   1 
ATOM   10872 C CA  . VAL C 1 327 ? 13.455  15.063  46.301  1.00 72.36  ? 327 VAL C CA  1 
ATOM   10873 C C   . VAL C 1 327 ? 14.152  16.418  46.298  1.00 66.68  ? 327 VAL C C   1 
ATOM   10874 O O   . VAL C 1 327 ? 15.382  16.500  46.404  1.00 69.46  ? 327 VAL C O   1 
ATOM   10875 C CB  . VAL C 1 327 ? 13.184  14.543  44.877  1.00 71.92  ? 327 VAL C CB  1 
ATOM   10876 C CG1 . VAL C 1 327 ? 14.482  14.435  44.093  1.00 71.90  ? 327 VAL C CG1 1 
ATOM   10877 C CG2 . VAL C 1 327 ? 12.479  13.189  44.934  1.00 60.58  ? 327 VAL C CG2 1 
ATOM   10878 N N   . ARG C 1 328 ? 13.379  17.502  46.210  1.00 69.29  ? 328 ARG C N   1 
ATOM   10879 C CA  . ARG C 1 328 ? 13.986  18.827  46.241  1.00 74.92  ? 328 ARG C CA  1 
ATOM   10880 C C   . ARG C 1 328 ? 14.706  19.078  47.563  1.00 74.54  ? 328 ARG C C   1 
ATOM   10881 O O   . ARG C 1 328 ? 15.805  19.643  47.578  1.00 83.24  ? 328 ARG C O   1 
ATOM   10882 C CB  . ARG C 1 328 ? 12.923  19.900  46.004  1.00 76.06  ? 328 ARG C CB  1 
ATOM   10883 C CG  . ARG C 1 328 ? 13.385  21.125  45.241  1.00 78.87  ? 328 ARG C CG  1 
ATOM   10884 C CD  . ARG C 1 328 ? 14.130  22.002  46.210  1.00 85.38  ? 328 ARG C CD  1 
ATOM   10885 N NE  . ARG C 1 328 ? 14.085  23.423  45.907  1.00 91.66  ? 328 ARG C NE  1 
ATOM   10886 C CZ  . ARG C 1 328 ? 15.107  24.260  46.022  1.00 97.95  ? 328 ARG C CZ  1 
ATOM   10887 N NH1 . ARG C 1 328 ? 16.326  23.834  46.326  1.00 99.53  ? 328 ARG C NH1 1 
ATOM   10888 N NH2 . ARG C 1 328 ? 14.906  25.555  45.795  1.00 86.78  ? 328 ARG C NH2 1 
ATOM   10889 N N   . ASP C 1 329 ? 14.075  18.721  48.685  1.00 70.78  ? 329 ASP C N   1 
ATOM   10890 C CA  . ASP C 1 329 ? 14.710  18.901  49.990  1.00 72.26  ? 329 ASP C CA  1 
ATOM   10891 C C   . ASP C 1 329 ? 15.998  18.093  50.087  1.00 71.32  ? 329 ASP C C   1 
ATOM   10892 O O   . ASP C 1 329 ? 17.065  18.632  50.410  1.00 69.51  ? 329 ASP C O   1 
ATOM   10893 C CB  . ASP C 1 329 ? 13.738  18.498  51.100  1.00 74.21  ? 329 ASP C CB  1 
ATOM   10894 C CG  . ASP C 1 329 ? 14.195  18.940  52.474  1.00 77.06  ? 329 ASP C CG  1 
ATOM   10895 O OD1 . ASP C 1 329 ? 14.258  20.167  52.703  1.00 80.38  ? 329 ASP C OD1 1 
ATOM   10896 O OD2 . ASP C 1 329 ? 14.457  18.065  53.329  1.00 68.71  ? 329 ASP C OD2 1 
ATOM   10897 N N   . PHE C 1 330 ? 15.909  16.789  49.816  1.00 69.47  ? 330 PHE C N   1 
ATOM   10898 C CA  . PHE C 1 330 ? 17.083  15.923  49.822  1.00 71.44  ? 330 PHE C CA  1 
ATOM   10899 C C   . PHE C 1 330 ? 18.199  16.500  48.959  1.00 71.45  ? 330 PHE C C   1 
ATOM   10900 O O   . PHE C 1 330 ? 19.323  16.707  49.430  1.00 76.17  ? 330 PHE C O   1 
ATOM   10901 C CB  . PHE C 1 330 ? 16.689  14.528  49.332  1.00 65.15  ? 330 PHE C CB  1 
ATOM   10902 C CG  . PHE C 1 330 ? 17.599  13.439  49.804  1.00 65.76  ? 330 PHE C CG  1 
ATOM   10903 C CD1 . PHE C 1 330 ? 17.639  13.079  51.142  1.00 66.26  ? 330 PHE C CD1 1 
ATOM   10904 C CD2 . PHE C 1 330 ? 18.426  12.779  48.909  1.00 75.08  ? 330 PHE C CD2 1 
ATOM   10905 C CE1 . PHE C 1 330 ? 18.482  12.070  51.579  1.00 72.63  ? 330 PHE C CE1 1 
ATOM   10906 C CE2 . PHE C 1 330 ? 19.273  11.771  49.335  1.00 76.37  ? 330 PHE C CE2 1 
ATOM   10907 C CZ  . PHE C 1 330 ? 19.299  11.415  50.677  1.00 74.11  ? 330 PHE C CZ  1 
ATOM   10908 N N   . ILE C 1 331 ? 17.894  16.782  47.690  1.00 67.15  ? 331 ILE C N   1 
ATOM   10909 C CA  . ILE C 1 331 ? 18.892  17.338  46.778  1.00 73.14  ? 331 ILE C CA  1 
ATOM   10910 C C   . ILE C 1 331 ? 19.459  18.636  47.342  1.00 74.26  ? 331 ILE C C   1 
ATOM   10911 O O   . ILE C 1 331 ? 20.678  18.844  47.366  1.00 78.03  ? 331 ILE C O   1 
ATOM   10912 C CB  . ILE C 1 331 ? 18.283  17.548  45.380  1.00 73.51  ? 331 ILE C CB  1 
ATOM   10913 C CG1 . ILE C 1 331 ? 18.066  16.200  44.675  1.00 71.06  ? 331 ILE C CG1 1 
ATOM   10914 C CG2 . ILE C 1 331 ? 19.145  18.503  44.562  1.00 70.81  ? 331 ILE C CG2 1 
ATOM   10915 C CD1 . ILE C 1 331 ? 19.215  15.731  43.812  1.00 73.03  ? 331 ILE C CD1 1 
ATOM   10916 N N   . GLY C 1 332 ? 18.580  19.523  47.816  1.00 69.95  ? 332 GLY C N   1 
ATOM   10917 C CA  . GLY C 1 332 ? 19.039  20.755  48.434  1.00 72.19  ? 332 GLY C CA  1 
ATOM   10918 C C   . GLY C 1 332 ? 19.796  20.528  49.726  1.00 72.60  ? 332 GLY C C   1 
ATOM   10919 O O   . GLY C 1 332 ? 20.720  21.281  50.047  1.00 77.06  ? 332 GLY C O   1 
ATOM   10920 N N   . ARG C 1 333 ? 19.428  19.487  50.480  1.00 68.05  ? 333 ARG C N   1 
ATOM   10921 C CA  . ARG C 1 333 ? 20.153  19.166  51.706  1.00 69.89  ? 333 ARG C CA  1 
ATOM   10922 C C   . ARG C 1 333 ? 21.585  18.722  51.415  1.00 75.74  ? 333 ARG C C   1 
ATOM   10923 O O   . ARG C 1 333 ? 22.503  19.049  52.176  1.00 78.11  ? 333 ARG C O   1 
ATOM   10924 C CB  . ARG C 1 333 ? 19.404  18.092  52.493  1.00 65.69  ? 333 ARG C CB  1 
ATOM   10925 C CG  . ARG C 1 333 ? 18.216  18.622  53.268  1.00 69.10  ? 333 ARG C CG  1 
ATOM   10926 C CD  . ARG C 1 333 ? 18.105  17.998  54.644  1.00 71.47  ? 333 ARG C CD  1 
ATOM   10927 N NE  . ARG C 1 333 ? 16.733  18.056  55.129  1.00 69.93  ? 333 ARG C NE  1 
ATOM   10928 C CZ  . ARG C 1 333 ? 16.382  18.408  56.358  1.00 76.83  ? 333 ARG C CZ  1 
ATOM   10929 N NH1 . ARG C 1 333 ? 17.287  18.725  57.272  1.00 74.03  ? 333 ARG C NH1 1 
ATOM   10930 N NH2 . ARG C 1 333 ? 15.089  18.444  56.675  1.00 73.67  ? 333 ARG C NH2 1 
ATOM   10931 N N   . LEU C 1 334 ? 21.800  17.971  50.328  1.00 68.18  ? 334 LEU C N   1 
ATOM   10932 C CA  . LEU C 1 334 ? 23.163  17.596  49.961  1.00 73.09  ? 334 LEU C CA  1 
ATOM   10933 C C   . LEU C 1 334 ? 23.946  18.795  49.445  1.00 71.81  ? 334 LEU C C   1 
ATOM   10934 O O   . LEU C 1 334 ? 25.171  18.847  49.603  1.00 71.87  ? 334 LEU C O   1 
ATOM   10935 C CB  . LEU C 1 334 ? 23.154  16.481  48.911  1.00 72.88  ? 334 LEU C CB  1 
ATOM   10936 C CG  . LEU C 1 334 ? 22.267  15.260  49.184  1.00 69.04  ? 334 LEU C CG  1 
ATOM   10937 C CD1 . LEU C 1 334 ? 21.660  14.723  47.902  1.00 70.96  ? 334 LEU C CD1 1 
ATOM   10938 C CD2 . LEU C 1 334 ? 23.032  14.164  49.892  1.00 65.42  ? 334 LEU C CD2 1 
ATOM   10939 N N   . LYS C 1 335 ? 23.257  19.755  48.821  1.00 71.60  ? 335 LYS C N   1 
ATOM   10940 C CA  . LYS C 1 335 ? 23.909  20.989  48.393  1.00 81.15  ? 335 LYS C CA  1 
ATOM   10941 C C   . LYS C 1 335 ? 24.531  21.711  49.577  1.00 85.90  ? 335 LYS C C   1 
ATOM   10942 O O   . LYS C 1 335 ? 25.672  22.183  49.504  1.00 86.14  ? 335 LYS C O   1 
ATOM   10943 C CB  . LYS C 1 335 ? 22.907  21.904  47.686  1.00 88.23  ? 335 LYS C CB  1 
ATOM   10944 C CG  . LYS C 1 335 ? 22.896  21.766  46.175  1.00 85.49  ? 335 LYS C CG  1 
ATOM   10945 C CD  . LYS C 1 335 ? 21.918  22.729  45.516  1.00 92.78  ? 335 LYS C CD  1 
ATOM   10946 C CE  . LYS C 1 335 ? 22.431  23.216  44.158  1.00 96.51  ? 335 LYS C CE  1 
ATOM   10947 N NZ  . LYS C 1 335 ? 21.608  22.720  43.014  1.00 76.01  ? 335 LYS C NZ  1 
ATOM   10948 N N   . LYS C 1 336 ? 23.784  21.815  50.678  1.00 82.03  ? 336 LYS C N   1 
ATOM   10949 C CA  . LYS C 1 336 ? 24.325  22.445  51.876  1.00 87.44  ? 336 LYS C CA  1 
ATOM   10950 C C   . LYS C 1 336 ? 25.561  21.706  52.369  1.00 90.53  ? 336 LYS C C   1 
ATOM   10951 O O   . LYS C 1 336 ? 26.540  22.332  52.790  1.00 99.52  ? 336 LYS C O   1 
ATOM   10952 C CB  . LYS C 1 336 ? 23.255  22.508  52.965  1.00 79.85  ? 336 LYS C CB  1 
ATOM   10953 C CG  . LYS C 1 336 ? 21.987  23.227  52.531  1.00 84.33  ? 336 LYS C CG  1 
ATOM   10954 C CD  . LYS C 1 336 ? 22.267  24.657  52.079  1.00 87.51  ? 336 LYS C CD  1 
ATOM   10955 C CE  . LYS C 1 336 ? 21.954  25.662  53.183  1.00 86.58  ? 336 LYS C CE  1 
ATOM   10956 N NZ  . LYS C 1 336 ? 22.885  26.828  53.183  1.00 80.75  ? 336 LYS C NZ  1 
ATOM   10957 N N   . ILE C 1 337 ? 25.549  20.373  52.299  1.00 74.13  ? 337 ILE C N   1 
ATOM   10958 C CA  . ILE C 1 337 ? 26.728  19.609  52.690  1.00 78.92  ? 337 ILE C CA  1 
ATOM   10959 C C   . ILE C 1 337 ? 27.887  19.886  51.740  1.00 84.10  ? 337 ILE C C   1 
ATOM   10960 O O   . ILE C 1 337 ? 29.048  19.964  52.161  1.00 82.69  ? 337 ILE C O   1 
ATOM   10961 C CB  . ILE C 1 337 ? 26.399  18.107  52.759  1.00 77.34  ? 337 ILE C CB  1 
ATOM   10962 C CG1 . ILE C 1 337 ? 25.164  17.867  53.638  1.00 75.79  ? 337 ILE C CG1 1 
ATOM   10963 C CG2 . ILE C 1 337 ? 27.601  17.328  53.277  1.00 74.47  ? 337 ILE C CG2 1 
ATOM   10964 C CD1 . ILE C 1 337 ? 24.532  16.494  53.470  1.00 66.29  ? 337 ILE C CD1 1 
ATOM   10965 N N   . HIS C 1 338 ? 27.593  20.047  50.447  1.00 86.11  ? 338 HIS C N   1 
ATOM   10966 C CA  . HIS C 1 338 ? 28.651  20.292  49.469  1.00 87.72  ? 338 HIS C CA  1 
ATOM   10967 C C   . HIS C 1 338 ? 29.421  21.568  49.794  1.00 88.97  ? 338 HIS C C   1 
ATOM   10968 O O   . HIS C 1 338 ? 30.654  21.560  49.883  1.00 84.19  ? 338 HIS C O   1 
ATOM   10969 C CB  . HIS C 1 338 ? 28.054  20.367  48.068  1.00 80.08  ? 338 HIS C CB  1 
ATOM   10970 C CG  . HIS C 1 338 ? 29.074  20.272  46.979  1.00 85.94  ? 338 HIS C CG  1 
ATOM   10971 N ND1 . HIS C 1 338 ? 29.363  21.327  46.139  1.00 86.22  ? 338 HIS C ND1 1 
ATOM   10972 C CD2 . HIS C 1 338 ? 29.865  19.247  46.584  1.00 83.75  ? 338 HIS C CD2 1 
ATOM   10973 C CE1 . HIS C 1 338 ? 30.295  20.959  45.279  1.00 82.51  ? 338 HIS C CE1 1 
ATOM   10974 N NE2 . HIS C 1 338 ? 30.613  19.700  45.524  1.00 88.03  ? 338 HIS C NE2 1 
ATOM   10975 N N   . GLU C 1 339 ? 28.705  22.677  49.988  1.00 90.34  ? 339 GLU C N   1 
ATOM   10976 C CA  . GLU C 1 339 ? 29.339  23.935  50.365  1.00 93.12  ? 339 GLU C CA  1 
ATOM   10977 C C   . GLU C 1 339 ? 29.870  23.931  51.798  1.00 88.52  ? 339 GLU C C   1 
ATOM   10978 O O   . GLU C 1 339 ? 30.685  24.796  52.134  1.00 88.16  ? 339 GLU C O   1 
ATOM   10979 C CB  . GLU C 1 339 ? 28.348  25.090  50.177  1.00 96.69  ? 339 GLU C CB  1 
ATOM   10980 C CG  . GLU C 1 339 ? 27.435  24.940  48.962  1.00 96.02  ? 339 GLU C CG  1 
ATOM   10981 C CD  . GLU C 1 339 ? 26.057  25.546  49.186  1.00 98.87  ? 339 GLU C CD  1 
ATOM   10982 O OE1 . GLU C 1 339 ? 25.817  26.106  50.276  1.00 98.14  ? 339 GLU C OE1 1 
ATOM   10983 O OE2 . GLU C 1 339 ? 25.205  25.445  48.278  1.00 95.19  ? 339 GLU C OE2 1 
ATOM   10984 N N   . SER C 1 340 ? 29.446  22.984  52.642  1.00 83.19  ? 340 SER C N   1 
ATOM   10985 C CA  . SER C 1 340 ? 29.841  22.977  54.049  1.00 86.42  ? 340 SER C CA  1 
ATOM   10986 C C   . SER C 1 340 ? 31.227  22.393  54.296  1.00 90.02  ? 340 SER C C   1 
ATOM   10987 O O   . SER C 1 340 ? 31.728  22.498  55.422  1.00 87.89  ? 340 SER C O   1 
ATOM   10988 C CB  . SER C 1 340 ? 28.813  22.204  54.886  1.00 79.19  ? 340 SER C CB  1 
ATOM   10989 O OG  . SER C 1 340 ? 29.113  20.819  54.932  1.00 79.94  ? 340 SER C OG  1 
ATOM   10990 N N   . VAL C 1 341 ? 31.857  21.785  53.290  1.00 87.78  ? 341 VAL C N   1 
ATOM   10991 C CA  . VAL C 1 341 ? 33.141  21.116  53.468  1.00 86.28  ? 341 VAL C CA  1 
ATOM   10992 C C   . VAL C 1 341 ? 34.082  21.514  52.342  1.00 88.91  ? 341 VAL C C   1 
ATOM   10993 O O   . VAL C 1 341 ? 33.661  21.735  51.202  1.00 91.97  ? 341 VAL C O   1 
ATOM   10994 C CB  . VAL C 1 341 ? 32.995  19.577  53.521  1.00 85.77  ? 341 VAL C CB  1 
ATOM   10995 C CG1 . VAL C 1 341 ? 32.264  19.148  54.786  1.00 88.76  ? 341 VAL C CG1 1 
ATOM   10996 C CG2 . VAL C 1 341 ? 32.285  19.056  52.275  1.00 85.05  ? 341 VAL C CG2 1 
ATOM   10997 N N   . ASP C 1 342 ? 35.372  21.601  52.674  1.00 89.06  ? 342 ASP C N   1 
ATOM   10998 C CA  . ASP C 1 342 ? 36.399  21.876  51.673  1.00 92.52  ? 342 ASP C CA  1 
ATOM   10999 C C   . ASP C 1 342 ? 36.752  20.632  50.865  1.00 89.65  ? 342 ASP C C   1 
ATOM   11000 O O   . ASP C 1 342 ? 37.070  20.737  49.675  1.00 86.14  ? 342 ASP C O   1 
ATOM   11001 C CB  . ASP C 1 342 ? 37.656  22.426  52.351  1.00 97.89  ? 342 ASP C CB  1 
ATOM   11002 C CG  . ASP C 1 342 ? 37.988  21.691  53.642  1.00 107.35 ? 342 ASP C CG  1 
ATOM   11003 O OD1 . ASP C 1 342 ? 37.051  21.342  54.396  1.00 102.98 ? 342 ASP C OD1 1 
ATOM   11004 O OD2 . ASP C 1 342 ? 39.187  21.457  53.903  1.00 108.18 ? 342 ASP C OD2 1 
ATOM   11005 N N   . PHE C 1 343 ? 36.705  19.460  51.493  1.00 87.88  ? 343 PHE C N   1 
ATOM   11006 C CA  . PHE C 1 343 ? 37.011  18.201  50.836  1.00 80.19  ? 343 PHE C CA  1 
ATOM   11007 C C   . PHE C 1 343 ? 35.806  17.711  50.039  1.00 78.50  ? 343 PHE C C   1 
ATOM   11008 O O   . PHE C 1 343 ? 34.704  18.256  50.128  1.00 80.70  ? 343 PHE C O   1 
ATOM   11009 C CB  . PHE C 1 343 ? 37.430  17.149  51.866  1.00 81.88  ? 343 PHE C CB  1 
ATOM   11010 C CG  . PHE C 1 343 ? 36.413  16.923  52.962  1.00 79.42  ? 343 PHE C CG  1 
ATOM   11011 C CD1 . PHE C 1 343 ? 36.408  17.712  54.101  1.00 79.90  ? 343 PHE C CD1 1 
ATOM   11012 C CD2 . PHE C 1 343 ? 35.467  15.914  52.853  1.00 82.22  ? 343 PHE C CD2 1 
ATOM   11013 C CE1 . PHE C 1 343 ? 35.474  17.502  55.108  1.00 77.39  ? 343 PHE C CE1 1 
ATOM   11014 C CE2 . PHE C 1 343 ? 34.532  15.701  53.856  1.00 80.36  ? 343 PHE C CE2 1 
ATOM   11015 C CZ  . PHE C 1 343 ? 34.539  16.498  54.985  1.00 71.20  ? 343 PHE C CZ  1 
ATOM   11016 N N   . GLN C 1 344 ? 36.027  16.659  49.255  1.00 79.90  ? 344 GLN C N   1 
ATOM   11017 C CA  . GLN C 1 344 ? 34.939  15.989  48.550  1.00 76.36  ? 344 GLN C CA  1 
ATOM   11018 C C   . GLN C 1 344 ? 34.150  15.118  49.520  1.00 73.17  ? 344 GLN C C   1 
ATOM   11019 O O   . GLN C 1 344 ? 34.650  14.073  49.960  1.00 74.77  ? 344 GLN C O   1 
ATOM   11020 C CB  . GLN C 1 344 ? 35.484  15.153  47.394  1.00 75.66  ? 344 GLN C CB  1 
ATOM   11021 C CG  . GLN C 1 344 ? 35.245  15.776  46.038  1.00 79.63  ? 344 GLN C CG  1 
ATOM   11022 C CD  . GLN C 1 344 ? 36.189  15.246  44.990  1.00 76.56  ? 344 GLN C CD  1 
ATOM   11023 O OE1 . GLN C 1 344 ? 37.354  14.978  45.279  1.00 78.08  ? 344 GLN C OE1 1 
ATOM   11024 N NE2 . GLN C 1 344 ? 35.698  15.095  43.765  1.00 75.51  ? 344 GLN C NE2 1 
ATOM   11025 N N   . PRO C 1 345 ? 32.923  15.500  49.870  1.00 73.42  ? 345 PRO C N   1 
ATOM   11026 C CA  . PRO C 1 345 ? 32.209  14.796  50.936  1.00 70.60  ? 345 PRO C CA  1 
ATOM   11027 C C   . PRO C 1 345 ? 31.687  13.445  50.482  1.00 64.97  ? 345 PRO C C   1 
ATOM   11028 O O   . PRO C 1 345 ? 31.306  13.249  49.325  1.00 65.83  ? 345 PRO C O   1 
ATOM   11029 C CB  . PRO C 1 345 ? 31.054  15.747  51.264  1.00 68.32  ? 345 PRO C CB  1 
ATOM   11030 C CG  . PRO C 1 345 ? 30.756  16.378  49.956  1.00 71.66  ? 345 PRO C CG  1 
ATOM   11031 C CD  . PRO C 1 345 ? 32.103  16.580  49.293  1.00 76.54  ? 345 PRO C CD  1 
ATOM   11032 N N   . VAL C 1 346 ? 31.683  12.504  51.418  1.00 65.12  ? 346 VAL C N   1 
ATOM   11033 C CA  . VAL C 1 346 ? 31.098  11.184  51.214  1.00 62.70  ? 346 VAL C CA  1 
ATOM   11034 C C   . VAL C 1 346 ? 29.917  11.058  52.167  1.00 64.66  ? 346 VAL C C   1 
ATOM   11035 O O   . VAL C 1 346 ? 30.093  11.041  53.392  1.00 62.85  ? 346 VAL C O   1 
ATOM   11036 C CB  . VAL C 1 346 ? 32.119  10.062  51.436  1.00 57.43  ? 346 VAL C CB  1 
ATOM   11037 C CG1 . VAL C 1 346 ? 31.400  8.754   51.689  1.00 61.55  ? 346 VAL C CG1 1 
ATOM   11038 C CG2 . VAL C 1 346 ? 32.998  9.930   50.225  1.00 63.41  ? 346 VAL C CG2 1 
ATOM   11039 N N   . VAL C 1 347 ? 28.713  10.968  51.606  1.00 61.76  ? 347 VAL C N   1 
ATOM   11040 C CA  . VAL C 1 347 ? 27.476  10.875  52.374  1.00 58.95  ? 347 VAL C CA  1 
ATOM   11041 C C   . VAL C 1 347 ? 26.911  9.470   52.210  1.00 61.51  ? 347 VAL C C   1 
ATOM   11042 O O   . VAL C 1 347 ? 26.646  9.023   51.085  1.00 59.58  ? 347 VAL C O   1 
ATOM   11043 C CB  . VAL C 1 347 ? 26.455  11.935  51.933  1.00 57.49  ? 347 VAL C CB  1 
ATOM   11044 C CG1 . VAL C 1 347 ? 25.162  11.776  52.718  1.00 64.97  ? 347 VAL C CG1 1 
ATOM   11045 C CG2 . VAL C 1 347 ? 27.022  13.325  52.111  1.00 58.15  ? 347 VAL C CG2 1 
ATOM   11046 N N   . PHE C 1 348 ? 26.722  8.780   53.332  1.00 63.47  ? 348 PHE C N   1 
ATOM   11047 C CA  . PHE C 1 348 ? 26.119  7.453   53.364  1.00 59.20  ? 348 PHE C CA  1 
ATOM   11048 C C   . PHE C 1 348 ? 24.673  7.578   53.827  1.00 62.87  ? 348 PHE C C   1 
ATOM   11049 O O   . PHE C 1 348 ? 24.400  8.131   54.899  1.00 62.39  ? 348 PHE C O   1 
ATOM   11050 C CB  . PHE C 1 348 ? 26.881  6.522   54.311  1.00 57.63  ? 348 PHE C CB  1 
ATOM   11051 C CG  . PHE C 1 348 ? 27.916  5.652   53.639  1.00 56.10  ? 348 PHE C CG  1 
ATOM   11052 C CD1 . PHE C 1 348 ? 29.008  6.212   52.999  1.00 53.98  ? 348 PHE C CD1 1 
ATOM   11053 C CD2 . PHE C 1 348 ? 27.821  4.267   53.695  1.00 54.39  ? 348 PHE C CD2 1 
ATOM   11054 C CE1 . PHE C 1 348 ? 29.974  5.408   52.398  1.00 47.49  ? 348 PHE C CE1 1 
ATOM   11055 C CE2 . PHE C 1 348 ? 28.782  3.462   53.099  1.00 47.33  ? 348 PHE C CE2 1 
ATOM   11056 C CZ  . PHE C 1 348 ? 29.858  4.035   52.451  1.00 45.54  ? 348 PHE C CZ  1 
ATOM   11057 N N   . VAL C 1 349 ? 23.758  7.066   53.026  1.00 64.53  ? 349 VAL C N   1 
ATOM   11058 C CA  . VAL C 1 349 ? 22.347  7.013   53.374  1.00 56.54  ? 349 VAL C CA  1 
ATOM   11059 C C   . VAL C 1 349 ? 22.010  5.541   53.562  1.00 56.57  ? 349 VAL C C   1 
ATOM   11060 O O   . VAL C 1 349 ? 21.837  4.801   52.587  1.00 57.23  ? 349 VAL C O   1 
ATOM   11061 C CB  . VAL C 1 349 ? 21.475  7.669   52.301  1.00 57.68  ? 349 VAL C CB  1 
ATOM   11062 C CG1 . VAL C 1 349 ? 20.013  7.569   52.684  1.00 61.51  ? 349 VAL C CG1 1 
ATOM   11063 C CG2 . VAL C 1 349 ? 21.900  9.122   52.110  1.00 61.31  ? 349 VAL C CG2 1 
ATOM   11064 N N   . VAL C 1 350 ? 21.942  5.103   54.814  1.00 58.01  ? 350 VAL C N   1 
ATOM   11065 C CA  . VAL C 1 350 ? 21.727  3.699   55.146  1.00 64.28  ? 350 VAL C CA  1 
ATOM   11066 C C   . VAL C 1 350 ? 20.427  3.579   55.932  1.00 62.50  ? 350 VAL C C   1 
ATOM   11067 O O   . VAL C 1 350 ? 20.301  4.148   57.025  1.00 62.16  ? 350 VAL C O   1 
ATOM   11068 C CB  . VAL C 1 350 ? 22.907  3.117   55.940  1.00 56.53  ? 350 VAL C CB  1 
ATOM   11069 C CG1 . VAL C 1 350 ? 22.647  1.654   56.259  1.00 59.30  ? 350 VAL C CG1 1 
ATOM   11070 C CG2 . VAL C 1 350 ? 24.207  3.275   55.153  1.00 47.46  ? 350 VAL C CG2 1 
ATOM   11071 N N   . LEU C 1 351 ? 19.464  2.837   55.380  1.00 53.60  ? 351 LEU C N   1 
ATOM   11072 C CA  . LEU C 1 351 ? 18.204  2.580   56.067  1.00 57.48  ? 351 LEU C CA  1 
ATOM   11073 C C   . LEU C 1 351 ? 17.625  1.255   55.586  1.00 56.85  ? 351 LEU C C   1 
ATOM   11074 O O   . LEU C 1 351 ? 18.128  0.636   54.642  1.00 53.34  ? 351 LEU C O   1 
ATOM   11075 C CB  . LEU C 1 351 ? 17.201  3.715   55.850  1.00 52.57  ? 351 LEU C CB  1 
ATOM   11076 C CG  . LEU C 1 351 ? 16.722  3.875   54.409  1.00 63.32  ? 351 LEU C CG  1 
ATOM   11077 C CD1 . LEU C 1 351 ? 15.251  4.279   54.372  1.00 48.38  ? 351 LEU C CD1 1 
ATOM   11078 C CD2 . LEU C 1 351 ? 17.602  4.887   53.671  1.00 60.20  ? 351 LEU C CD2 1 
ATOM   11079 N N   . ASP C 1 352 ? 16.555  0.822   56.256  1.00 55.48  ? 352 ASP C N   1 
ATOM   11080 C CA  . ASP C 1 352 ? 15.878  -0.412  55.870  1.00 55.09  ? 352 ASP C CA  1 
ATOM   11081 C C   . ASP C 1 352 ? 15.214  -0.228  54.514  1.00 57.06  ? 352 ASP C C   1 
ATOM   11082 O O   . ASP C 1 352 ? 14.543  0.781   54.274  1.00 66.66  ? 352 ASP C O   1 
ATOM   11083 C CB  . ASP C 1 352 ? 14.838  -0.814  56.921  1.00 57.20  ? 352 ASP C CB  1 
ATOM   11084 C CG  . ASP C 1 352 ? 15.465  -1.119  58.276  1.00 69.49  ? 352 ASP C CG  1 
ATOM   11085 O OD1 . ASP C 1 352 ? 16.706  -1.250  58.348  1.00 65.60  ? 352 ASP C OD1 1 
ATOM   11086 O OD2 . ASP C 1 352 ? 14.719  -1.220  59.276  1.00 72.90  ? 352 ASP C OD2 1 
ATOM   11087 N N   . GLY C 1 353 ? 15.402  -1.208  53.627  1.00 56.52  ? 353 GLY C N   1 
ATOM   11088 C CA  . GLY C 1 353 ? 14.993  -1.102  52.242  1.00 53.62  ? 353 GLY C CA  1 
ATOM   11089 C C   . GLY C 1 353 ? 13.587  -1.534  51.913  1.00 60.00  ? 353 GLY C C   1 
ATOM   11090 O O   . GLY C 1 353 ? 13.152  -1.360  50.771  1.00 62.30  ? 353 GLY C O   1 
ATOM   11091 N N   . GLU C 1 354 ? 12.839  -2.083  52.868  1.00 66.60  ? 354 GLU C N   1 
ATOM   11092 C CA  . GLU C 1 354 ? 11.517  -2.603  52.565  1.00 62.45  ? 354 GLU C CA  1 
ATOM   11093 C C   . GLU C 1 354 ? 10.398  -2.002  53.397  1.00 60.85  ? 354 GLU C C   1 
ATOM   11094 O O   . GLU C 1 354 ? 9.235   -2.102  52.989  1.00 68.56  ? 354 GLU C O   1 
ATOM   11095 C CB  . GLU C 1 354 ? 11.487  -4.129  52.750  1.00 57.49  ? 354 GLU C CB  1 
ATOM   11096 C CG  . GLU C 1 354 ? 11.558  -4.579  54.211  1.00 64.33  ? 354 GLU C CG  1 
ATOM   11097 C CD  . GLU C 1 354 ? 12.970  -4.899  54.689  1.00 62.72  ? 354 GLU C CD  1 
ATOM   11098 O OE1 . GLU C 1 354 ? 13.364  -6.085  54.646  1.00 63.02  ? 354 GLU C OE1 1 
ATOM   11099 O OE2 . GLU C 1 354 ? 13.684  -3.967  55.119  1.00 60.52  ? 354 GLU C OE2 1 
ATOM   11100 N N   . ASN C 1 355 ? 10.698  -1.392  54.538  1.00 59.84  ? 355 ASN C N   1 
ATOM   11101 C CA  . ASN C 1 355 ? 9.614   -1.090  55.464  1.00 65.61  ? 355 ASN C CA  1 
ATOM   11102 C C   . ASN C 1 355 ? 8.974   0.267   55.208  1.00 61.15  ? 355 ASN C C   1 
ATOM   11103 O O   . ASN C 1 355 ? 7.765   0.423   55.404  1.00 68.18  ? 355 ASN C O   1 
ATOM   11104 C CB  . ASN C 1 355 ? 10.107  -1.169  56.917  1.00 64.84  ? 355 ASN C CB  1 
ATOM   11105 C CG  . ASN C 1 355 ? 10.674  -2.541  57.281  1.00 57.12  ? 355 ASN C CG  1 
ATOM   11106 O OD1 . ASN C 1 355 ? 10.005  -3.566  57.134  1.00 53.89  ? 355 ASN C OD1 1 
ATOM   11107 N ND2 . ASN C 1 355 ? 11.908  -2.557  57.777  1.00 63.59  ? 355 ASN C ND2 1 
ATOM   11108 N N   . CYS C 1 356 ? 9.747   1.258   54.773  1.00 62.53  ? 356 CYS C N   1 
ATOM   11109 C CA  . CYS C 1 356 ? 9.200   2.607   54.697  1.00 57.74  ? 356 CYS C CA  1 
ATOM   11110 C C   . CYS C 1 356 ? 8.209   2.767   53.559  1.00 57.82  ? 356 CYS C C   1 
ATOM   11111 O O   . CYS C 1 356 ? 7.374   3.675   53.607  1.00 63.41  ? 356 CYS C O   1 
ATOM   11112 C CB  . CYS C 1 356 ? 10.319  3.625   54.516  1.00 57.70  ? 356 CYS C CB  1 
ATOM   11113 S SG  . CYS C 1 356 ? 11.480  3.132   53.228  1.00 56.86  ? 356 CYS C SG  1 
ATOM   11114 N N   . TRP C 1 357 ? 8.273   1.902   52.545  1.00 63.80  ? 357 TRP C N   1 
ATOM   11115 C CA  . TRP C 1 357 ? 7.598   2.189   51.283  1.00 64.49  ? 357 TRP C CA  1 
ATOM   11116 C C   . TRP C 1 357 ? 6.095   1.983   51.349  1.00 63.56  ? 357 TRP C C   1 
ATOM   11117 O O   . TRP C 1 357 ? 5.352   2.648   50.622  1.00 70.86  ? 357 TRP C O   1 
ATOM   11118 C CB  . TRP C 1 357 ? 8.186   1.334   50.166  1.00 57.06  ? 357 TRP C CB  1 
ATOM   11119 C CG  . TRP C 1 357 ? 9.653   1.511   50.002  1.00 55.17  ? 357 TRP C CG  1 
ATOM   11120 C CD1 . TRP C 1 357 ? 10.578  0.525   49.835  1.00 59.67  ? 357 TRP C CD1 1 
ATOM   11121 C CD2 . TRP C 1 357 ? 10.378  2.753   49.969  1.00 58.50  ? 357 TRP C CD2 1 
ATOM   11122 N NE1 . TRP C 1 357 ? 11.834  1.070   49.706  1.00 63.67  ? 357 TRP C NE1 1 
ATOM   11123 C CE2 . TRP C 1 357 ? 11.738  2.435   49.784  1.00 63.51  ? 357 TRP C CE2 1 
ATOM   11124 C CE3 . TRP C 1 357 ? 10.010  4.101   50.076  1.00 55.72  ? 357 TRP C CE3 1 
ATOM   11125 C CZ2 . TRP C 1 357 ? 12.730  3.412   49.712  1.00 60.88  ? 357 TRP C CZ2 1 
ATOM   11126 C CZ3 . TRP C 1 357 ? 10.995  5.067   50.001  1.00 57.06  ? 357 TRP C CZ3 1 
ATOM   11127 C CH2 . TRP C 1 357 ? 12.338  4.719   49.820  1.00 54.92  ? 357 TRP C CH2 1 
ATOM   11128 N N   . GLU C 1 358 ? 5.627   1.077   52.197  1.00 67.58  ? 358 GLU C N   1 
ATOM   11129 C CA  . GLU C 1 358 ? 4.197   0.811   52.284  1.00 70.02  ? 358 GLU C CA  1 
ATOM   11130 C C   . GLU C 1 358 ? 3.401   2.002   52.822  1.00 73.75  ? 358 GLU C C   1 
ATOM   11131 O O   . GLU C 1 358 ? 2.201   2.110   52.544  1.00 78.11  ? 358 GLU C O   1 
ATOM   11132 C CB  . GLU C 1 358 ? 4.006   -0.438  53.137  1.00 73.33  ? 358 GLU C CB  1 
ATOM   11133 C CG  . GLU C 1 358 ? 4.114   -0.163  54.632  1.00 77.92  ? 358 GLU C CG  1 
ATOM   11134 C CD  . GLU C 1 358 ? 3.562   -1.297  55.450  1.00 86.71  ? 358 GLU C CD  1 
ATOM   11135 O OE1 . GLU C 1 358 ? 2.895   -2.174  54.859  1.00 93.55  ? 358 GLU C OE1 1 
ATOM   11136 O OE2 . GLU C 1 358 ? 3.855   -1.351  56.665  1.00 91.09  ? 358 GLU C OE2 1 
ATOM   11137 N N   . TYR C 1 359 ? 4.036   2.891   53.583  1.00 72.33  ? 359 TYR C N   1 
ATOM   11138 C CA  . TYR C 1 359 ? 3.407   4.118   54.055  1.00 68.40  ? 359 TYR C CA  1 
ATOM   11139 C C   . TYR C 1 359 ? 3.592   5.273   53.084  1.00 73.62  ? 359 TYR C C   1 
ATOM   11140 O O   . TYR C 1 359 ? 3.115   6.383   53.354  1.00 73.19  ? 359 TYR C O   1 
ATOM   11141 C CB  . TYR C 1 359 ? 3.966   4.507   55.421  1.00 67.84  ? 359 TYR C CB  1 
ATOM   11142 C CG  . TYR C 1 359 ? 3.878   3.390   56.417  1.00 69.44  ? 359 TYR C CG  1 
ATOM   11143 C CD1 . TYR C 1 359 ? 2.683   3.101   57.055  1.00 76.14  ? 359 TYR C CD1 1 
ATOM   11144 C CD2 . TYR C 1 359 ? 4.987   2.612   56.714  1.00 69.46  ? 359 TYR C CD2 1 
ATOM   11145 C CE1 . TYR C 1 359 ? 2.594   2.073   57.972  1.00 84.11  ? 359 TYR C CE1 1 
ATOM   11146 C CE2 . TYR C 1 359 ? 4.910   1.582   57.628  1.00 84.92  ? 359 TYR C CE2 1 
ATOM   11147 C CZ  . TYR C 1 359 ? 3.710   1.314   58.254  1.00 88.30  ? 359 TYR C CZ  1 
ATOM   11148 O OH  . TYR C 1 359 ? 3.626   0.289   59.167  1.00 88.65  ? 359 TYR C OH  1 
ATOM   11149 N N   . TYR C 1 360 ? 4.289   5.041   51.980  1.00 73.21  ? 360 TYR C N   1 
ATOM   11150 C CA  . TYR C 1 360 ? 4.393   6.012   50.907  1.00 67.78  ? 360 TYR C CA  1 
ATOM   11151 C C   . TYR C 1 360 ? 3.215   5.857   49.954  1.00 71.98  ? 360 TYR C C   1 
ATOM   11152 O O   . TYR C 1 360 ? 2.499   4.851   49.964  1.00 72.44  ? 360 TYR C O   1 
ATOM   11153 C CB  . TYR C 1 360 ? 5.689   5.828   50.120  1.00 63.68  ? 360 TYR C CB  1 
ATOM   11154 C CG  . TYR C 1 360 ? 6.909   6.551   50.639  1.00 61.73  ? 360 TYR C CG  1 
ATOM   11155 C CD1 . TYR C 1 360 ? 7.548   6.134   51.799  1.00 60.87  ? 360 TYR C CD1 1 
ATOM   11156 C CD2 . TYR C 1 360 ? 7.452   7.619   49.939  1.00 57.21  ? 360 TYR C CD2 1 
ATOM   11157 C CE1 . TYR C 1 360 ? 8.686   6.781   52.265  1.00 60.95  ? 360 TYR C CE1 1 
ATOM   11158 C CE2 . TYR C 1 360 ? 8.588   8.272   50.397  1.00 68.67  ? 360 TYR C CE2 1 
ATOM   11159 C CZ  . TYR C 1 360 ? 9.201   7.849   51.560  1.00 64.52  ? 360 TYR C CZ  1 
ATOM   11160 O OH  . TYR C 1 360 ? 10.328  8.497   52.009  1.00 63.15  ? 360 TYR C OH  1 
ATOM   11161 N N   . GLU C 1 361 ? 3.043   6.865   49.106  1.00 76.52  ? 361 GLU C N   1 
ATOM   11162 C CA  . GLU C 1 361 ? 2.087   6.777   48.014  1.00 73.48  ? 361 GLU C CA  1 
ATOM   11163 C C   . GLU C 1 361 ? 2.612   5.839   46.937  1.00 72.57  ? 361 GLU C C   1 
ATOM   11164 O O   . GLU C 1 361 ? 3.720   6.024   46.425  1.00 76.30  ? 361 GLU C O   1 
ATOM   11165 C CB  . GLU C 1 361 ? 1.833   8.160   47.423  1.00 78.40  ? 361 GLU C CB  1 
ATOM   11166 C CG  . GLU C 1 361 ? 0.608   8.842   47.997  1.00 94.50  ? 361 GLU C CG  1 
ATOM   11167 C CD  . GLU C 1 361 ? -0.673  8.434   47.294  1.00 101.97 ? 361 GLU C CD  1 
ATOM   11168 O OE1 . GLU C 1 361 ? -0.673  8.364   46.046  1.00 103.68 ? 361 GLU C OE1 1 
ATOM   11169 O OE2 . GLU C 1 361 ? -1.680  8.185   47.991  1.00 102.29 ? 361 GLU C OE2 1 
ATOM   11170 N N   . GLU C 1 362 ? 1.812   4.828   46.601  1.00 77.53  ? 362 GLU C N   1 
ATOM   11171 C CA  . GLU C 1 362 ? 2.141   3.875   45.539  1.00 76.61  ? 362 GLU C CA  1 
ATOM   11172 C C   . GLU C 1 362 ? 3.460   3.165   45.829  1.00 71.87  ? 362 GLU C C   1 
ATOM   11173 O O   . GLU C 1 362 ? 4.287   2.962   44.936  1.00 68.76  ? 362 GLU C O   1 
ATOM   11174 C CB  . GLU C 1 362 ? 2.175   4.561   44.170  1.00 64.31  ? 362 GLU C CB  1 
ATOM   11175 C CG  . GLU C 1 362 ? 1.042   5.548   43.942  1.00 72.31  ? 362 GLU C CG  1 
ATOM   11176 C CD  . GLU C 1 362 ? 0.033   5.043   42.930  1.00 88.95  ? 362 GLU C CD  1 
ATOM   11177 O OE1 . GLU C 1 362 ? 0.395   4.156   42.127  1.00 95.88  ? 362 GLU C OE1 1 
ATOM   11178 O OE2 . GLU C 1 362 ? -1.119  5.528   42.935  1.00 88.28  ? 362 GLU C OE2 1 
ATOM   11179 N N   . ASN C 1 363 ? 3.657   2.797   47.097  1.00 70.05  ? 363 ASN C N   1 
ATOM   11180 C CA  . ASN C 1 363 ? 4.874   2.120   47.568  1.00 65.90  ? 363 ASN C CA  1 
ATOM   11181 C C   . ASN C 1 363 ? 6.135   2.926   47.281  1.00 67.34  ? 363 ASN C C   1 
ATOM   11182 O O   . ASN C 1 363 ? 7.211   2.368   47.050  1.00 63.75  ? 363 ASN C O   1 
ATOM   11183 C CB  . ASN C 1 363 ? 4.992   0.711   46.990  1.00 57.81  ? 363 ASN C CB  1 
ATOM   11184 C CG  . ASN C 1 363 ? 5.467   -0.280  48.016  1.00 65.88  ? 363 ASN C CG  1 
ATOM   11185 O OD1 . ASN C 1 363 ? 4.715   -0.646  48.915  1.00 72.40  ? 363 ASN C OD1 1 
ATOM   11186 N ND2 . ASN C 1 363 ? 6.712   -0.723  47.895  1.00 66.78  ? 363 ASN C ND2 1 
ATOM   11187 N N   . GLY C 1 364 ? 6.010   4.250   47.318  1.00 68.75  ? 364 GLY C N   1 
ATOM   11188 C CA  . GLY C 1 364 ? 7.129   5.126   47.032  1.00 67.21  ? 364 GLY C CA  1 
ATOM   11189 C C   . GLY C 1 364 ? 7.630   5.085   45.606  1.00 63.34  ? 364 GLY C C   1 
ATOM   11190 O O   . GLY C 1 364 ? 8.678   5.677   45.335  1.00 71.10  ? 364 GLY C O   1 
ATOM   11191 N N   . ILE C 1 365 ? 6.929   4.399   44.696  1.00 55.59  ? 365 ILE C N   1 
ATOM   11192 C CA  . ILE C 1 365 ? 7.380   4.339   43.316  1.00 56.43  ? 365 ILE C CA  1 
ATOM   11193 C C   . ILE C 1 365 ? 7.557   5.737   42.747  1.00 61.20  ? 365 ILE C C   1 
ATOM   11194 O O   . ILE C 1 365 ? 8.587   5.988   42.108  1.00 65.60  ? 365 ILE C O   1 
ATOM   11195 C CB  . ILE C 1 365 ? 6.440   3.450   42.490  1.00 61.31  ? 365 ILE C CB  1 
ATOM   11196 C CG1 . ILE C 1 365 ? 6.857   1.977   42.660  1.00 57.19  ? 365 ILE C CG1 1 
ATOM   11197 C CG2 . ILE C 1 365 ? 6.475   3.860   41.041  1.00 59.16  ? 365 ILE C CG2 1 
ATOM   11198 C CD1 . ILE C 1 365 ? 5.723   1.016   42.591  1.00 56.66  ? 365 ILE C CD1 1 
ATOM   11199 N N   . PRO C 1 366 ? 6.660   6.701   42.975  1.00 59.71  ? 366 PRO C N   1 
ATOM   11200 C CA  . PRO C 1 366 ? 6.931   8.058   42.474  1.00 60.65  ? 366 PRO C CA  1 
ATOM   11201 C C   . PRO C 1 366 ? 8.165   8.691   43.086  1.00 59.78  ? 366 PRO C C   1 
ATOM   11202 O O   . PRO C 1 366 ? 8.967   9.302   42.371  1.00 66.76  ? 366 PRO C O   1 
ATOM   11203 C CB  . PRO C 1 366 ? 5.658   8.827   42.858  1.00 62.31  ? 366 PRO C CB  1 
ATOM   11204 C CG  . PRO C 1 366 ? 4.601   7.788   42.936  1.00 63.71  ? 366 PRO C CG  1 
ATOM   11205 C CD  . PRO C 1 366 ? 5.301   6.604   43.533  1.00 69.75  ? 366 PRO C CD  1 
ATOM   11206 N N   . PHE C 1 367 ? 8.335   8.559   44.403  1.00 63.82  ? 367 PHE C N   1 
ATOM   11207 C CA  . PHE C 1 367 ? 9.461   9.194   45.077  1.00 60.02  ? 367 PHE C CA  1 
ATOM   11208 C C   . PHE C 1 367 ? 10.780  8.640   44.565  1.00 59.76  ? 367 PHE C C   1 
ATOM   11209 O O   . PHE C 1 367 ? 11.699  9.396   44.232  1.00 60.50  ? 367 PHE C O   1 
ATOM   11210 C CB  . PHE C 1 367 ? 9.338   8.993   46.587  1.00 60.42  ? 367 PHE C CB  1 
ATOM   11211 C CG  . PHE C 1 367 ? 10.556  9.411   47.356  1.00 64.43  ? 367 PHE C CG  1 
ATOM   11212 C CD1 . PHE C 1 367 ? 10.787  10.748  47.646  1.00 68.69  ? 367 PHE C CD1 1 
ATOM   11213 C CD2 . PHE C 1 367 ? 11.474  8.469   47.789  1.00 58.45  ? 367 PHE C CD2 1 
ATOM   11214 C CE1 . PHE C 1 367 ? 11.912  11.135  48.360  1.00 62.18  ? 367 PHE C CE1 1 
ATOM   11215 C CE2 . PHE C 1 367 ? 12.598  8.852   48.500  1.00 69.21  ? 367 PHE C CE2 1 
ATOM   11216 C CZ  . PHE C 1 367 ? 12.816  10.186  48.787  1.00 64.09  ? 367 PHE C CZ  1 
ATOM   11217 N N   . LEU C 1 368 ? 10.890  7.313   44.498  1.00 63.31  ? 368 LEU C N   1 
ATOM   11218 C CA  . LEU C 1 368 ? 12.138  6.697   44.070  1.00 61.49  ? 368 LEU C CA  1 
ATOM   11219 C C   . LEU C 1 368 ? 12.430  6.994   42.608  1.00 61.93  ? 368 LEU C C   1 
ATOM   11220 O O   . LEU C 1 368 ? 13.577  7.276   42.244  1.00 61.41  ? 368 LEU C O   1 
ATOM   11221 C CB  . LEU C 1 368 ? 12.088  5.191   44.310  1.00 59.04  ? 368 LEU C CB  1 
ATOM   11222 C CG  . LEU C 1 368 ? 12.871  4.663   45.515  1.00 63.22  ? 368 LEU C CG  1 
ATOM   11223 C CD1 . LEU C 1 368 ? 13.592  5.774   46.281  1.00 59.59  ? 368 LEU C CD1 1 
ATOM   11224 C CD2 . LEU C 1 368 ? 11.936  3.897   46.420  1.00 61.95  ? 368 LEU C CD2 1 
ATOM   11225 N N   . GLU C 1 369 ? 11.410  6.933   41.752  1.00 58.35  ? 369 GLU C N   1 
ATOM   11226 C CA  . GLU C 1 369 ? 11.627  7.247   40.346  1.00 58.35  ? 369 GLU C CA  1 
ATOM   11227 C C   . GLU C 1 369 ? 12.018  8.707   40.178  1.00 60.67  ? 369 GLU C C   1 
ATOM   11228 O O   . GLU C 1 369 ? 12.846  9.041   39.324  1.00 60.43  ? 369 GLU C O   1 
ATOM   11229 C CB  . GLU C 1 369 ? 10.375  6.919   39.536  1.00 67.02  ? 369 GLU C CB  1 
ATOM   11230 C CG  . GLU C 1 369 ? 10.249  5.446   39.149  1.00 71.84  ? 369 GLU C CG  1 
ATOM   11231 C CD  . GLU C 1 369 ? 8.935   5.120   38.447  1.00 76.90  ? 369 GLU C CD  1 
ATOM   11232 O OE1 . GLU C 1 369 ? 8.005   5.956   38.485  1.00 78.34  ? 369 GLU C OE1 1 
ATOM   11233 O OE2 . GLU C 1 369 ? 8.834   4.026   37.852  1.00 85.01  ? 369 GLU C OE2 1 
ATOM   11234 N N   . LYS C 1 370 ? 11.441  9.591   40.994  1.00 62.94  ? 370 LYS C N   1 
ATOM   11235 C CA  . LYS C 1 370 ? 11.827  10.997  40.948  1.00 61.52  ? 370 LYS C CA  1 
ATOM   11236 C C   . LYS C 1 370 ? 13.254  11.184  41.436  1.00 63.39  ? 370 LYS C C   1 
ATOM   11237 O O   . LYS C 1 370 ? 14.071  11.825  40.766  1.00 72.04  ? 370 LYS C O   1 
ATOM   11238 C CB  . LYS C 1 370 ? 10.870  11.838  41.788  1.00 62.38  ? 370 LYS C CB  1 
ATOM   11239 C CG  . LYS C 1 370 ? 11.087  13.335  41.644  1.00 68.27  ? 370 LYS C CG  1 
ATOM   11240 C CD  . LYS C 1 370 ? 10.444  13.882  40.370  1.00 73.92  ? 370 LYS C CD  1 
ATOM   11241 C CE  . LYS C 1 370 ? 11.241  15.038  39.768  1.00 80.51  ? 370 LYS C CE  1 
ATOM   11242 N NZ  . LYS C 1 370 ? 10.358  16.070  39.132  1.00 83.98  ? 370 LYS C NZ  1 
ATOM   11243 N N   . LEU C 1 371 ? 13.568  10.636  42.609  1.00 61.44  ? 371 LEU C N   1 
ATOM   11244 C CA  . LEU C 1 371 ? 14.898  10.816  43.176  1.00 62.69  ? 371 LEU C CA  1 
ATOM   11245 C C   . LEU C 1 371 ? 15.964  10.244  42.256  1.00 57.44  ? 371 LEU C C   1 
ATOM   11246 O O   . LEU C 1 371 ? 16.880  10.956  41.835  1.00 58.37  ? 371 LEU C O   1 
ATOM   11247 C CB  . LEU C 1 371 ? 14.963  10.169  44.557  1.00 60.49  ? 371 LEU C CB  1 
ATOM   11248 C CG  . LEU C 1 371 ? 16.359  10.015  45.146  1.00 57.04  ? 371 LEU C CG  1 
ATOM   11249 C CD1 . LEU C 1 371 ? 16.929  11.359  45.589  1.00 58.45  ? 371 LEU C CD1 1 
ATOM   11250 C CD2 . LEU C 1 371 ? 16.305  9.037   46.304  1.00 59.74  ? 371 LEU C CD2 1 
ATOM   11251 N N   . TYR C 1 372 ? 15.831  8.964   41.899  1.00 57.62  ? 372 TYR C N   1 
ATOM   11252 C CA  . TYR C 1 372 ? 16.810  8.305   41.041  1.00 57.43  ? 372 TYR C CA  1 
ATOM   11253 C C   . TYR C 1 372 ? 16.954  8.994   39.686  1.00 64.99  ? 372 TYR C C   1 
ATOM   11254 O O   . TYR C 1 372 ? 18.059  9.035   39.130  1.00 66.71  ? 372 TYR C O   1 
ATOM   11255 C CB  . TYR C 1 372 ? 16.419  6.843   40.855  1.00 55.24  ? 372 TYR C CB  1 
ATOM   11256 C CG  . TYR C 1 372 ? 16.514  6.017   42.116  1.00 56.68  ? 372 TYR C CG  1 
ATOM   11257 C CD1 . TYR C 1 372 ? 17.192  6.488   43.233  1.00 58.91  ? 372 TYR C CD1 1 
ATOM   11258 C CD2 . TYR C 1 372 ? 15.936  4.756   42.187  1.00 56.87  ? 372 TYR C CD2 1 
ATOM   11259 C CE1 . TYR C 1 372 ? 17.289  5.729   44.382  1.00 50.74  ? 372 TYR C CE1 1 
ATOM   11260 C CE2 . TYR C 1 372 ? 16.030  3.994   43.328  1.00 53.85  ? 372 TYR C CE2 1 
ATOM   11261 C CZ  . TYR C 1 372 ? 16.708  4.483   44.424  1.00 49.91  ? 372 TYR C CZ  1 
ATOM   11262 O OH  . TYR C 1 372 ? 16.800  3.719   45.565  1.00 54.39  ? 372 TYR C OH  1 
ATOM   11263 N N   . SER C 1 373 ? 15.867  9.541   39.137  1.00 59.81  ? 373 SER C N   1 
ATOM   11264 C CA  . SER C 1 373 ? 15.986  10.289  37.888  1.00 66.62  ? 373 SER C CA  1 
ATOM   11265 C C   . SER C 1 373 ? 16.689  11.621  38.107  1.00 68.43  ? 373 SER C C   1 
ATOM   11266 O O   . SER C 1 373 ? 17.484  12.053  37.265  1.00 74.18  ? 373 SER C O   1 
ATOM   11267 C CB  . SER C 1 373 ? 14.612  10.527  37.275  1.00 64.70  ? 373 SER C CB  1 
ATOM   11268 O OG  . SER C 1 373 ? 13.972  11.602  37.938  1.00 68.66  ? 373 SER C OG  1 
ATOM   11269 N N   . THR C 1 374 ? 16.396  12.293  39.226  1.00 62.73  ? 374 THR C N   1 
ATOM   11270 C CA  . THR C 1 374 ? 17.018  13.585  39.508  1.00 63.95  ? 374 THR C CA  1 
ATOM   11271 C C   . THR C 1 374 ? 18.518  13.442  39.760  1.00 72.58  ? 374 THR C C   1 
ATOM   11272 O O   . THR C 1 374 ? 19.320  14.204  39.207  1.00 81.66  ? 374 THR C O   1 
ATOM   11273 C CB  . THR C 1 374 ? 16.334  14.258  40.701  1.00 65.14  ? 374 THR C CB  1 
ATOM   11274 O OG1 . THR C 1 374 ? 14.929  14.373  40.451  1.00 71.97  ? 374 THR C OG1 1 
ATOM   11275 C CG2 . THR C 1 374 ? 16.907  15.649  40.924  1.00 65.60  ? 374 THR C CG2 1 
ATOM   11276 N N   . LEU C 1 375 ? 18.922  12.471  40.592  1.00 66.22  ? 375 LEU C N   1 
ATOM   11277 C CA  . LEU C 1 375 ? 20.349  12.248  40.825  1.00 65.63  ? 375 LEU C CA  1 
ATOM   11278 C C   . LEU C 1 375 ? 21.081  11.927  39.532  1.00 69.18  ? 375 LEU C C   1 
ATOM   11279 O O   . LEU C 1 375 ? 22.279  12.209  39.406  1.00 66.01  ? 375 LEU C O   1 
ATOM   11280 C CB  . LEU C 1 375 ? 20.576  11.109  41.818  1.00 57.92  ? 375 LEU C CB  1 
ATOM   11281 C CG  . LEU C 1 375 ? 19.798  11.070  43.125  1.00 59.89  ? 375 LEU C CG  1 
ATOM   11282 C CD1 . LEU C 1 375 ? 19.555  9.622   43.527  1.00 58.82  ? 375 LEU C CD1 1 
ATOM   11283 C CD2 . LEU C 1 375 ? 20.536  11.825  44.214  1.00 62.79  ? 375 LEU C CD2 1 
ATOM   11284 N N   . GLU C 1 376 ? 20.385  11.310  38.576  1.00 70.47  ? 376 GLU C N   1 
ATOM   11285 C CA  . GLU C 1 376 ? 20.968  11.054  37.266  1.00 71.16  ? 376 GLU C CA  1 
ATOM   11286 C C   . GLU C 1 376 ? 21.409  12.355  36.607  1.00 76.17  ? 376 GLU C C   1 
ATOM   11287 O O   . GLU C 1 376 ? 22.545  12.473  36.133  1.00 74.74  ? 376 GLU C O   1 
ATOM   11288 C CB  . GLU C 1 376 ? 19.953  10.313  36.393  1.00 72.42  ? 376 GLU C CB  1 
ATOM   11289 C CG  . GLU C 1 376 ? 20.506  9.127   35.632  1.00 77.78  ? 376 GLU C CG  1 
ATOM   11290 C CD  . GLU C 1 376 ? 19.577  8.681   34.520  1.00 81.43  ? 376 GLU C CD  1 
ATOM   11291 O OE1 . GLU C 1 376 ? 18.500  8.130   34.833  1.00 79.66  ? 376 GLU C OE1 1 
ATOM   11292 O OE2 . GLU C 1 376 ? 19.921  8.887   33.336  1.00 89.92  ? 376 GLU C OE2 1 
ATOM   11293 N N   . LYS C 1 377 ? 20.523  13.354  36.587  1.00 76.27  ? 377 LYS C N   1 
ATOM   11294 C CA  . LYS C 1 377 ? 20.810  14.656  35.998  1.00 81.86  ? 377 LYS C CA  1 
ATOM   11295 C C   . LYS C 1 377 ? 21.638  15.561  36.905  1.00 82.39  ? 377 LYS C C   1 
ATOM   11296 O O   . LYS C 1 377 ? 22.037  16.646  36.465  1.00 89.52  ? 377 LYS C O   1 
ATOM   11297 C CB  . LYS C 1 377 ? 19.504  15.367  35.628  1.00 87.39  ? 377 LYS C CB  1 
ATOM   11298 C CG  . LYS C 1 377 ? 19.226  15.409  34.128  1.00 96.43  ? 377 LYS C CG  1 
ATOM   11299 C CD  . LYS C 1 377 ? 19.259  14.012  33.501  1.00 98.63  ? 377 LYS C CD  1 
ATOM   11300 C CE  . LYS C 1 377 ? 17.853  13.442  33.292  1.00 93.08  ? 377 LYS C CE  1 
ATOM   11301 N NZ  . LYS C 1 377 ? 17.846  12.047  32.744  1.00 79.85  ? 377 LYS C NZ  1 
ATOM   11302 N N   . GLU C 1 378 ? 21.903  15.155  38.145  1.00 76.13  ? 378 GLU C N   1 
ATOM   11303 C CA  . GLU C 1 378 ? 22.716  15.943  39.072  1.00 78.13  ? 378 GLU C CA  1 
ATOM   11304 C C   . GLU C 1 378 ? 24.179  15.564  38.875  1.00 78.25  ? 378 GLU C C   1 
ATOM   11305 O O   . GLU C 1 378 ? 24.662  14.580  39.436  1.00 80.86  ? 378 GLU C O   1 
ATOM   11306 C CB  . GLU C 1 378 ? 22.285  15.709  40.513  1.00 77.76  ? 378 GLU C CB  1 
ATOM   11307 C CG  . GLU C 1 378 ? 21.341  16.775  41.066  1.00 83.79  ? 378 GLU C CG  1 
ATOM   11308 C CD  . GLU C 1 378 ? 21.524  18.147  40.424  1.00 87.95  ? 378 GLU C CD  1 
ATOM   11309 O OE1 . GLU C 1 378 ? 20.569  18.609  39.761  1.00 93.94  ? 378 GLU C OE1 1 
ATOM   11310 O OE2 . GLU C 1 378 ? 22.602  18.767  40.596  1.00 85.04  ? 378 GLU C OE2 1 
ATOM   11311 N N   . GLU C 1 379 ? 24.895  16.365  38.096  1.00 77.85  ? 379 GLU C N   1 
ATOM   11312 C CA  . GLU C 1 379 ? 26.266  16.048  37.717  1.00 83.35  ? 379 GLU C CA  1 
ATOM   11313 C C   . GLU C 1 379 ? 27.286  16.290  38.836  1.00 78.00  ? 379 GLU C C   1 
ATOM   11314 O O   . GLU C 1 379 ? 28.388  15.729  38.784  1.00 75.88  ? 379 GLU C O   1 
ATOM   11315 C CB  . GLU C 1 379 ? 26.567  16.858  36.457  1.00 92.06  ? 379 GLU C CB  1 
ATOM   11316 C CG  . GLU C 1 379 ? 25.930  18.239  36.520  1.00 94.82  ? 379 GLU C CG  1 
ATOM   11317 C CD  . GLU C 1 379 ? 26.927  19.295  36.895  1.00 100.68 ? 379 GLU C CD  1 
ATOM   11318 O OE1 . GLU C 1 379 ? 28.042  19.284  36.323  1.00 103.18 ? 379 GLU C OE1 1 
ATOM   11319 O OE2 . GLU C 1 379 ? 26.614  20.126  37.776  1.00 100.54 ? 379 GLU C OE2 1 
ATOM   11320 N N   . TRP C 1 380 ? 26.942  17.079  39.853  1.00 77.97  ? 380 TRP C N   1 
ATOM   11321 C CA  . TRP C 1 380 ? 27.813  17.251  41.010  1.00 76.25  ? 380 TRP C CA  1 
ATOM   11322 C C   . TRP C 1 380 ? 27.611  16.179  42.078  1.00 76.51  ? 380 TRP C C   1 
ATOM   11323 O O   . TRP C 1 380 ? 28.391  16.130  43.039  1.00 76.54  ? 380 TRP C O   1 
ATOM   11324 C CB  . TRP C 1 380 ? 27.615  18.639  41.642  1.00 79.44  ? 380 TRP C CB  1 
ATOM   11325 C CG  . TRP C 1 380 ? 26.238  18.873  42.195  1.00 78.41  ? 380 TRP C CG  1 
ATOM   11326 C CD1 . TRP C 1 380 ? 25.147  19.319  41.507  1.00 74.93  ? 380 TRP C CD1 1 
ATOM   11327 C CD2 . TRP C 1 380 ? 25.797  18.657  43.549  1.00 81.72  ? 380 TRP C CD2 1 
ATOM   11328 N NE1 . TRP C 1 380 ? 24.061  19.402  42.345  1.00 86.24  ? 380 TRP C NE1 1 
ATOM   11329 C CE2 . TRP C 1 380 ? 24.432  19.002  43.601  1.00 78.42  ? 380 TRP C CE2 1 
ATOM   11330 C CE3 . TRP C 1 380 ? 26.424  18.211  44.719  1.00 81.94  ? 380 TRP C CE3 1 
ATOM   11331 C CZ2 . TRP C 1 380 ? 23.680  18.911  44.769  1.00 67.40  ? 380 TRP C CZ2 1 
ATOM   11332 C CZ3 . TRP C 1 380 ? 25.673  18.127  45.884  1.00 78.93  ? 380 TRP C CZ3 1 
ATOM   11333 C CH2 . TRP C 1 380 ? 24.316  18.478  45.897  1.00 73.40  ? 380 TRP C CH2 1 
ATOM   11334 N N   . ILE C 1 381 ? 26.591  15.332  41.945  1.00 72.57  ? 381 ILE C N   1 
ATOM   11335 C CA  . ILE C 1 381 ? 26.381  14.187  42.827  1.00 69.99  ? 381 ILE C CA  1 
ATOM   11336 C C   . ILE C 1 381 ? 26.797  12.940  42.058  1.00 67.62  ? 381 ILE C C   1 
ATOM   11337 O O   . ILE C 1 381 ? 26.291  12.684  40.958  1.00 66.14  ? 381 ILE C O   1 
ATOM   11338 C CB  . ILE C 1 381 ? 24.921  14.084  43.307  1.00 67.23  ? 381 ILE C CB  1 
ATOM   11339 C CG1 . ILE C 1 381 ? 24.568  15.275  44.196  1.00 69.02  ? 381 ILE C CG1 1 
ATOM   11340 C CG2 . ILE C 1 381 ? 24.687  12.789  44.100  1.00 58.36  ? 381 ILE C CG2 1 
ATOM   11341 C CD1 . ILE C 1 381 ? 23.098  15.394  44.508  1.00 66.57  ? 381 ILE C CD1 1 
ATOM   11342 N N   . GLU C 1 382 ? 27.720  12.170  42.629  1.00 59.70  ? 382 GLU C N   1 
ATOM   11343 C CA  . GLU C 1 382 ? 28.193  10.927  42.030  1.00 58.91  ? 382 GLU C CA  1 
ATOM   11344 C C   . GLU C 1 382 ? 27.794  9.772   42.940  1.00 57.87  ? 382 GLU C C   1 
ATOM   11345 O O   . GLU C 1 382 ? 28.344  9.624   44.036  1.00 64.53  ? 382 GLU C O   1 
ATOM   11346 C CB  . GLU C 1 382 ? 29.705  10.967  41.819  1.00 67.84  ? 382 GLU C CB  1 
ATOM   11347 C CG  . GLU C 1 382 ? 30.277  9.681   41.240  1.00 82.42  ? 382 GLU C CG  1 
ATOM   11348 C CD  . GLU C 1 382 ? 31.768  9.758   40.974  1.00 81.17  ? 382 GLU C CD  1 
ATOM   11349 O OE1 . GLU C 1 382 ? 32.352  10.852  41.135  1.00 91.23  ? 382 GLU C OE1 1 
ATOM   11350 O OE2 . GLU C 1 382 ? 32.358  8.722   40.601  1.00 85.15  ? 382 GLU C OE2 1 
ATOM   11351 N N   . THR C 1 383 ? 26.825  8.968   42.498  1.00 66.91  ? 383 THR C N   1 
ATOM   11352 C CA  . THR C 1 383 ? 26.487  7.745   43.218  1.00 64.97  ? 383 THR C CA  1 
ATOM   11353 C C   . THR C 1 383 ? 27.610  6.729   43.047  1.00 64.22  ? 383 THR C C   1 
ATOM   11354 O O   . THR C 1 383 ? 28.213  6.621   41.975  1.00 64.73  ? 383 THR C O   1 
ATOM   11355 C CB  . THR C 1 383 ? 25.154  7.159   42.730  1.00 64.01  ? 383 THR C CB  1 
ATOM   11356 O OG1 . THR C 1 383 ? 25.158  7.034   41.300  1.00 66.26  ? 383 THR C OG1 1 
ATOM   11357 C CG2 . THR C 1 383 ? 23.970  8.028   43.174  1.00 54.05  ? 383 THR C CG2 1 
ATOM   11358 N N   . LEU C 1 384 ? 27.892  5.987   44.114  1.00 67.52  ? 384 LEU C N   1 
ATOM   11359 C CA  . LEU C 1 384 ? 29.059  5.120   44.182  1.00 63.67  ? 384 LEU C CA  1 
ATOM   11360 C C   . LEU C 1 384 ? 28.671  3.757   44.733  1.00 65.88  ? 384 LEU C C   1 
ATOM   11361 O O   . LEU C 1 384 ? 27.863  3.660   45.662  1.00 63.66  ? 384 LEU C O   1 
ATOM   11362 C CB  . LEU C 1 384 ? 30.144  5.751   45.073  1.00 56.10  ? 384 LEU C CB  1 
ATOM   11363 C CG  . LEU C 1 384 ? 30.979  6.898   44.498  1.00 63.31  ? 384 LEU C CG  1 
ATOM   11364 C CD1 . LEU C 1 384 ? 32.306  7.005   45.234  1.00 69.08  ? 384 LEU C CD1 1 
ATOM   11365 C CD2 . LEU C 1 384 ? 31.218  6.734   42.993  1.00 70.31  ? 384 LEU C CD2 1 
ATOM   11366 N N   . THR C 1 385 ? 29.242  2.704   44.156  1.00 61.20  ? 385 THR C N   1 
ATOM   11367 C CA  . THR C 1 385 ? 29.148  1.402   44.790  1.00 55.23  ? 385 THR C CA  1 
ATOM   11368 C C   . THR C 1 385 ? 29.994  1.393   46.053  1.00 53.22  ? 385 THR C C   1 
ATOM   11369 O O   . THR C 1 385 ? 30.803  2.291   46.294  1.00 62.37  ? 385 THR C O   1 
ATOM   11370 C CB  . THR C 1 385 ? 29.614  0.295   43.849  1.00 55.83  ? 385 THR C CB  1 
ATOM   11371 O OG1 . THR C 1 385 ? 31.033  0.122   43.984  1.00 66.30  ? 385 THR C OG1 1 
ATOM   11372 C CG2 . THR C 1 385 ? 29.288  0.658   42.412  1.00 53.92  ? 385 THR C CG2 1 
ATOM   11373 N N   . LEU C 1 386 ? 29.794  0.361   46.874  1.00 58.67  ? 386 LEU C N   1 
ATOM   11374 C CA  . LEU C 1 386 ? 30.604  0.225   48.079  1.00 60.28  ? 386 LEU C CA  1 
ATOM   11375 C C   . LEU C 1 386 ? 32.081  0.103   47.724  1.00 60.83  ? 386 LEU C C   1 
ATOM   11376 O O   . LEU C 1 386 ? 32.932  0.772   48.322  1.00 61.15  ? 386 LEU C O   1 
ATOM   11377 C CB  . LEU C 1 386 ? 30.135  -0.983  48.891  1.00 54.66  ? 386 LEU C CB  1 
ATOM   11378 C CG  . LEU C 1 386 ? 28.705  -0.955  49.433  1.00 49.88  ? 386 LEU C CG  1 
ATOM   11379 C CD1 . LEU C 1 386 ? 28.532  -1.980  50.534  1.00 49.61  ? 386 LEU C CD1 1 
ATOM   11380 C CD2 . LEU C 1 386 ? 28.351  0.420   49.945  1.00 49.22  ? 386 LEU C CD2 1 
ATOM   11381 N N   . GLU C 1 387 ? 32.394  -0.724  46.724  1.00 59.57  ? 387 GLU C N   1 
ATOM   11382 C CA  . GLU C 1 387 ? 33.779  -0.901  46.307  1.00 61.90  ? 387 GLU C CA  1 
ATOM   11383 C C   . GLU C 1 387 ? 34.361  0.400   45.774  1.00 63.40  ? 387 GLU C C   1 
ATOM   11384 O O   . GLU C 1 387 ? 35.508  0.746   46.076  1.00 71.62  ? 387 GLU C O   1 
ATOM   11385 C CB  . GLU C 1 387 ? 33.861  -2.003  45.253  1.00 67.56  ? 387 GLU C CB  1 
ATOM   11386 C CG  . GLU C 1 387 ? 35.257  -2.311  44.802  1.00 79.57  ? 387 GLU C CG  1 
ATOM   11387 C CD  . GLU C 1 387 ? 35.472  -2.036  43.338  1.00 95.93  ? 387 GLU C CD  1 
ATOM   11388 O OE1 . GLU C 1 387 ? 34.469  -1.969  42.594  1.00 92.76  ? 387 GLU C OE1 1 
ATOM   11389 O OE2 . GLU C 1 387 ? 36.645  -1.883  42.935  1.00 101.11 ? 387 GLU C OE2 1 
ATOM   11390 N N   . GLU C 1 388 ? 33.578  1.141   44.988  1.00 61.13  ? 388 GLU C N   1 
ATOM   11391 C CA  . GLU C 1 388 ? 34.047  2.411   44.445  1.00 64.10  ? 388 GLU C CA  1 
ATOM   11392 C C   . GLU C 1 388 ? 34.329  3.416   45.553  1.00 60.19  ? 388 GLU C C   1 
ATOM   11393 O O   . GLU C 1 388 ? 35.326  4.147   45.502  1.00 70.77  ? 388 GLU C O   1 
ATOM   11394 C CB  . GLU C 1 388 ? 33.016  2.963   43.466  1.00 65.78  ? 388 GLU C CB  1 
ATOM   11395 C CG  . GLU C 1 388 ? 32.938  2.170   42.175  1.00 63.93  ? 388 GLU C CG  1 
ATOM   11396 C CD  . GLU C 1 388 ? 31.876  2.689   41.229  1.00 66.35  ? 388 GLU C CD  1 
ATOM   11397 O OE1 . GLU C 1 388 ? 31.142  3.636   41.596  1.00 66.90  ? 388 GLU C OE1 1 
ATOM   11398 O OE2 . GLU C 1 388 ? 31.773  2.142   40.113  1.00 68.60  ? 388 GLU C OE2 1 
ATOM   11399 N N   . ALA C 1 389 ? 33.460  3.471   46.565  1.00 58.14  ? 389 ALA C N   1 
ATOM   11400 C CA  . ALA C 1 389 ? 33.743  4.300   47.733  1.00 65.95  ? 389 ALA C CA  1 
ATOM   11401 C C   . ALA C 1 389 ? 35.012  3.846   48.439  1.00 69.40  ? 389 ALA C C   1 
ATOM   11402 O O   . ALA C 1 389 ? 35.747  4.666   49.003  1.00 70.47  ? 389 ALA C O   1 
ATOM   11403 C CB  . ALA C 1 389 ? 32.572  4.260   48.713  1.00 55.93  ? 389 ALA C CB  1 
ATOM   11404 N N   . MET C 1 390 ? 35.285  2.545   48.418  1.00 66.74  ? 390 MET C N   1 
ATOM   11405 C CA  . MET C 1 390 ? 36.487  2.039   49.065  1.00 71.53  ? 390 MET C CA  1 
ATOM   11406 C C   . MET C 1 390 ? 37.748  2.403   48.293  1.00 74.19  ? 390 MET C C   1 
ATOM   11407 O O   . MET C 1 390 ? 38.835  2.473   48.876  1.00 67.24  ? 390 MET C O   1 
ATOM   11408 C CB  . MET C 1 390 ? 36.388  0.526   49.225  1.00 66.58  ? 390 MET C CB  1 
ATOM   11409 C CG  . MET C 1 390 ? 35.746  0.034   50.507  1.00 68.80  ? 390 MET C CG  1 
ATOM   11410 S SD  . MET C 1 390 ? 36.798  0.266   51.962  1.00 79.26  ? 390 MET C SD  1 
ATOM   11411 C CE  . MET C 1 390 ? 36.383  1.932   52.469  1.00 65.47  ? 390 MET C CE  1 
ATOM   11412 N N   . ARG C 1 391 ? 37.628  2.619   46.990  1.00 69.47  ? 391 ARG C N   1 
ATOM   11413 C CA  . ARG C 1 391 ? 38.777  2.851   46.133  1.00 68.51  ? 391 ARG C CA  1 
ATOM   11414 C C   . ARG C 1 391 ? 39.016  4.331   45.869  1.00 75.58  ? 391 ARG C C   1 
ATOM   11415 O O   . ARG C 1 391 ? 40.086  4.699   45.367  1.00 70.11  ? 391 ARG C O   1 
ATOM   11416 C CB  . ARG C 1 391 ? 38.581  2.098   44.812  1.00 75.14  ? 391 ARG C CB  1 
ATOM   11417 C CG  . ARG C 1 391 ? 38.512  0.573   44.929  1.00 80.17  ? 391 ARG C CG  1 
ATOM   11418 C CD  . ARG C 1 391 ? 39.266  0.099   46.154  1.00 86.77  ? 391 ARG C CD  1 
ATOM   11419 N NE  . ARG C 1 391 ? 39.952  -1.170  45.955  1.00 90.34  ? 391 ARG C NE  1 
ATOM   11420 C CZ  . ARG C 1 391 ? 39.362  -2.357  45.875  1.00 96.40  ? 391 ARG C CZ  1 
ATOM   11421 N NH1 . ARG C 1 391 ? 38.051  -2.499  46.016  1.00 84.49  ? 391 ARG C NH1 1 
ATOM   11422 N NH2 . ARG C 1 391 ? 40.104  -3.430  45.618  1.00 95.60  ? 391 ARG C NH2 1 
ATOM   11423 N N   . LYS C 1 392 ? 38.056  5.184   46.220  1.00 75.31  ? 392 LYS C N   1 
ATOM   11424 C CA  . LYS C 1 392 ? 38.164  6.612   45.954  1.00 81.79  ? 392 LYS C CA  1 
ATOM   11425 C C   . LYS C 1 392 ? 39.236  7.239   46.843  1.00 86.04  ? 392 LYS C C   1 
ATOM   11426 O O   . LYS C 1 392 ? 39.103  7.254   48.072  1.00 86.04  ? 392 LYS C O   1 
ATOM   11427 C CB  . LYS C 1 392 ? 36.807  7.278   46.177  1.00 75.87  ? 392 LYS C CB  1 
ATOM   11428 C CG  . LYS C 1 392 ? 36.632  8.573   45.413  1.00 81.23  ? 392 LYS C CG  1 
ATOM   11429 C CD  . LYS C 1 392 ? 36.559  8.319   43.916  1.00 76.93  ? 392 LYS C CD  1 
ATOM   11430 C CE  . LYS C 1 392 ? 35.124  8.376   43.418  1.00 76.79  ? 392 LYS C CE  1 
ATOM   11431 N NZ  . LYS C 1 392 ? 34.873  7.448   42.278  1.00 80.60  ? 392 LYS C NZ  1 
ATOM   11432 N N   . GLU C 1 393 ? 40.306  7.740   46.223  1.00 89.56  ? 393 GLU C N   1 
ATOM   11433 C CA  . GLU C 1 393 ? 41.366  8.431   46.946  1.00 87.96  ? 393 GLU C CA  1 
ATOM   11434 C C   . GLU C 1 393 ? 41.065  9.907   47.192  1.00 84.18  ? 393 GLU C C   1 
ATOM   11435 O O   . GLU C 1 393 ? 41.766  10.535  47.993  1.00 87.32  ? 393 GLU C O   1 
ATOM   11436 C CB  . GLU C 1 393 ? 42.700  8.301   46.198  1.00 88.96  ? 393 GLU C CB  1 
ATOM   11437 C CG  . GLU C 1 393 ? 43.587  7.170   46.708  1.00 92.81  ? 393 GLU C CG  1 
ATOM   11438 C CD  . GLU C 1 393 ? 44.103  6.286   45.593  1.00 104.09 ? 393 GLU C CD  1 
ATOM   11439 O OE1 . GLU C 1 393 ? 44.023  6.704   44.417  1.00 108.78 ? 393 GLU C OE1 1 
ATOM   11440 O OE2 . GLU C 1 393 ? 44.575  5.168   45.889  1.00 109.99 ? 393 GLU C OE2 1 
ATOM   11441 N N   . ASP C 1 394 ? 40.040  10.469  46.541  1.00 86.24  ? 394 ASP C N   1 
ATOM   11442 C CA  . ASP C 1 394 ? 39.657  11.865  46.745  1.00 79.58  ? 394 ASP C CA  1 
ATOM   11443 C C   . ASP C 1 394 ? 39.063  12.122  48.122  1.00 77.78  ? 394 ASP C C   1 
ATOM   11444 O O   . ASP C 1 394 ? 38.875  13.289  48.487  1.00 76.97  ? 394 ASP C O   1 
ATOM   11445 C CB  . ASP C 1 394 ? 38.630  12.305  45.702  1.00 80.16  ? 394 ASP C CB  1 
ATOM   11446 C CG  . ASP C 1 394 ? 38.757  11.555  44.399  1.00 85.23  ? 394 ASP C CG  1 
ATOM   11447 O OD1 . ASP C 1 394 ? 39.757  10.829  44.225  1.00 94.70  ? 394 ASP C OD1 1 
ATOM   11448 O OD2 . ASP C 1 394 ? 37.854  11.695  43.546  1.00 82.03  ? 394 ASP C OD2 1 
ATOM   11449 N N   . VAL C 1 395 ? 38.752  11.073  48.872  1.00 78.06  ? 395 VAL C N   1 
ATOM   11450 C CA  . VAL C 1 395 ? 38.046  11.202  50.141  1.00 75.67  ? 395 VAL C CA  1 
ATOM   11451 C C   . VAL C 1 395 ? 39.004  11.622  51.243  1.00 73.13  ? 395 VAL C C   1 
ATOM   11452 O O   . VAL C 1 395 ? 40.130  11.118  51.339  1.00 69.15  ? 395 VAL C O   1 
ATOM   11453 C CB  . VAL C 1 395 ? 37.350  9.880   50.506  1.00 74.67  ? 395 VAL C CB  1 
ATOM   11454 C CG1 . VAL C 1 395 ? 36.291  10.128  51.560  1.00 74.13  ? 395 VAL C CG1 1 
ATOM   11455 C CG2 . VAL C 1 395 ? 36.740  9.245   49.272  1.00 78.00  ? 395 VAL C CG2 1 
ATOM   11456 N N   . LYS C 1 396 ? 38.541  12.530  52.100  1.00 74.45  ? 396 LYS C N   1 
ATOM   11457 C CA  . LYS C 1 396 ? 39.262  12.840  53.327  1.00 68.07  ? 396 LYS C CA  1 
ATOM   11458 C C   . LYS C 1 396 ? 39.169  11.649  54.277  1.00 70.39  ? 396 LYS C C   1 
ATOM   11459 O O   . LYS C 1 396 ? 38.092  11.064  54.450  1.00 61.94  ? 396 LYS C O   1 
ATOM   11460 C CB  . LYS C 1 396 ? 38.693  14.101  53.980  1.00 63.62  ? 396 LYS C CB  1 
ATOM   11461 C CG  . LYS C 1 396 ? 39.735  14.952  54.712  1.00 83.48  ? 396 LYS C CG  1 
ATOM   11462 C CD  . LYS C 1 396 ? 39.087  15.907  55.717  1.00 79.58  ? 396 LYS C CD  1 
ATOM   11463 C CE  . LYS C 1 396 ? 39.849  15.953  57.040  1.00 78.57  ? 396 LYS C CE  1 
ATOM   11464 N NZ  . LYS C 1 396 ? 39.036  16.592  58.113  1.00 76.54  ? 396 LYS C NZ  1 
ATOM   11465 N N   . THR C 1 397 ? 40.299  11.286  54.886  1.00 69.28  ? 397 THR C N   1 
ATOM   11466 C CA  . THR C 1 397 ? 40.408  10.072  55.686  1.00 62.30  ? 397 THR C CA  1 
ATOM   11467 C C   . THR C 1 397 ? 41.029  10.378  57.042  1.00 60.10  ? 397 THR C C   1 
ATOM   11468 O O   . THR C 1 397 ? 41.991  11.147  57.142  1.00 62.28  ? 397 THR C O   1 
ATOM   11469 C CB  . THR C 1 397 ? 41.243  9.007   54.963  1.00 67.13  ? 397 THR C CB  1 
ATOM   11470 O OG1 . THR C 1 397 ? 41.026  9.102   53.551  1.00 66.16  ? 397 THR C OG1 1 
ATOM   11471 C CG2 . THR C 1 397 ? 40.850  7.611   55.429  1.00 70.08  ? 397 THR C CG2 1 
ATOM   11472 N N   . GLU C 1 398 ? 40.475  9.757   58.079  1.00 60.81  ? 398 GLU C N   1 
ATOM   11473 C CA  . GLU C 1 398 ? 40.913  9.944   59.453  1.00 59.55  ? 398 GLU C CA  1 
ATOM   11474 C C   . GLU C 1 398 ? 41.006  8.589   60.135  1.00 62.83  ? 398 GLU C C   1 
ATOM   11475 O O   . GLU C 1 398 ? 40.207  7.686   59.872  1.00 57.74  ? 398 GLU C O   1 
ATOM   11476 C CB  . GLU C 1 398 ? 39.948  10.865  60.231  1.00 66.93  ? 398 GLU C CB  1 
ATOM   11477 C CG  . GLU C 1 398 ? 40.189  10.908  61.739  1.00 76.37  ? 398 GLU C CG  1 
ATOM   11478 C CD  . GLU C 1 398 ? 40.190  12.322  62.300  1.00 89.81  ? 398 GLU C CD  1 
ATOM   11479 O OE1 . GLU C 1 398 ? 39.135  12.992  62.252  1.00 85.92  ? 398 GLU C OE1 1 
ATOM   11480 O OE2 . GLU C 1 398 ? 41.257  12.766  62.781  1.00 92.52  ? 398 GLU C OE2 1 
ATOM   11481 N N   . VAL C 1 399 ? 41.995  8.447   61.009  1.00 65.50  ? 399 VAL C N   1 
ATOM   11482 C CA  . VAL C 1 399 ? 42.177  7.228   61.788  1.00 68.94  ? 399 VAL C CA  1 
ATOM   11483 C C   . VAL C 1 399 ? 41.540  7.415   63.156  1.00 66.88  ? 399 VAL C C   1 
ATOM   11484 O O   . VAL C 1 399 ? 41.644  8.491   63.759  1.00 70.99  ? 399 VAL C O   1 
ATOM   11485 C CB  . VAL C 1 399 ? 43.670  6.868   61.906  1.00 65.95  ? 399 VAL C CB  1 
ATOM   11486 C CG1 . VAL C 1 399 ? 43.922  5.990   63.121  1.00 67.20  ? 399 VAL C CG1 1 
ATOM   11487 C CG2 . VAL C 1 399 ? 44.133  6.172   60.639  1.00 71.91  ? 399 VAL C CG2 1 
ATOM   11488 N N   . ILE C 1 400 ? 40.858  6.374   63.638  1.00 63.65  ? 400 ILE C N   1 
ATOM   11489 C CA  . ILE C 1 400 ? 40.271  6.358   64.973  1.00 70.62  ? 400 ILE C CA  1 
ATOM   11490 C C   . ILE C 1 400 ? 40.722  5.092   65.692  1.00 66.74  ? 400 ILE C C   1 
ATOM   11491 O O   . ILE C 1 400 ? 40.963  4.053   65.070  1.00 68.79  ? 400 ILE C O   1 
ATOM   11492 C CB  . ILE C 1 400 ? 38.723  6.444   64.936  1.00 73.05  ? 400 ILE C CB  1 
ATOM   11493 C CG1 . ILE C 1 400 ? 38.120  5.237   64.228  1.00 66.37  ? 400 ILE C CG1 1 
ATOM   11494 C CG2 . ILE C 1 400 ? 38.245  7.735   64.280  1.00 68.74  ? 400 ILE C CG2 1 
ATOM   11495 C CD1 . ILE C 1 400 ? 36.841  4.791   64.872  1.00 62.75  ? 400 ILE C CD1 1 
ATOM   11496 N N   . GLU C 1 401 ? 40.821  5.177   67.018  1.00 65.55  ? 401 GLU C N   1 
ATOM   11497 C CA  . GLU C 1 401 ? 41.327  4.067   67.818  1.00 64.02  ? 401 GLU C CA  1 
ATOM   11498 C C   . GLU C 1 401 ? 40.285  3.445   68.743  1.00 60.31  ? 401 GLU C C   1 
ATOM   11499 O O   . GLU C 1 401 ? 40.603  2.479   69.446  1.00 53.06  ? 401 GLU C O   1 
ATOM   11500 C CB  . GLU C 1 401 ? 42.542  4.521   68.637  1.00 56.04  ? 401 GLU C CB  1 
ATOM   11501 C CG  . GLU C 1 401 ? 43.545  5.390   67.860  1.00 64.68  ? 401 GLU C CG  1 
ATOM   11502 C CD  . GLU C 1 401 ? 44.647  4.590   67.162  1.00 65.65  ? 401 GLU C CD  1 
ATOM   11503 O OE1 . GLU C 1 401 ? 44.791  3.376   67.435  1.00 62.64  ? 401 GLU C OE1 1 
ATOM   11504 O OE2 . GLU C 1 401 ? 45.393  5.191   66.357  1.00 60.01  ? 401 GLU C OE2 1 
ATOM   11505 N N   . SER C 1 402 ? 39.050  3.945   68.750  1.00 64.30  ? 402 SER C N   1 
ATOM   11506 C CA  . SER C 1 402 ? 38.074  3.490   69.734  1.00 62.01  ? 402 SER C CA  1 
ATOM   11507 C C   . SER C 1 402 ? 36.674  3.861   69.262  1.00 54.91  ? 402 SER C C   1 
ATOM   11508 O O   . SER C 1 402 ? 36.496  4.777   68.455  1.00 64.13  ? 402 SER C O   1 
ATOM   11509 C CB  . SER C 1 402 ? 38.377  4.090   71.121  1.00 51.92  ? 402 SER C CB  1 
ATOM   11510 O OG  . SER C 1 402 ? 37.218  4.220   71.927  1.00 64.76  ? 402 SER C OG  1 
ATOM   11511 N N   . VAL C 1 403 ? 35.683  3.135   69.775  1.00 47.85  ? 403 VAL C N   1 
ATOM   11512 C CA  . VAL C 1 403 ? 34.276  3.441   69.517  1.00 54.63  ? 403 VAL C CA  1 
ATOM   11513 C C   . VAL C 1 403 ? 33.470  3.078   70.752  1.00 53.76  ? 403 VAL C C   1 
ATOM   11514 O O   . VAL C 1 403 ? 33.647  1.997   71.325  1.00 54.59  ? 403 VAL C O   1 
ATOM   11515 C CB  . VAL C 1 403 ? 33.715  2.685   68.295  1.00 54.84  ? 403 VAL C CB  1 
ATOM   11516 C CG1 . VAL C 1 403 ? 34.087  3.393   67.016  1.00 54.88  ? 403 VAL C CG1 1 
ATOM   11517 C CG2 . VAL C 1 403 ? 34.201  1.249   68.294  1.00 55.47  ? 403 VAL C CG2 1 
ATOM   11518 N N   . LYS C 1 404 ? 32.571  3.971   71.151  1.00 54.03  ? 404 LYS C N   1 
ATOM   11519 C CA  . LYS C 1 404 ? 31.634  3.670   72.223  1.00 57.26  ? 404 LYS C CA  1 
ATOM   11520 C C   . LYS C 1 404 ? 30.507  2.796   71.686  1.00 56.69  ? 404 LYS C C   1 
ATOM   11521 O O   . LYS C 1 404 ? 29.840  3.158   70.712  1.00 60.39  ? 404 LYS C O   1 
ATOM   11522 C CB  . LYS C 1 404 ? 31.078  4.960   72.823  1.00 55.27  ? 404 LYS C CB  1 
ATOM   11523 C CG  . LYS C 1 404 ? 30.800  4.871   74.310  1.00 58.14  ? 404 LYS C CG  1 
ATOM   11524 C CD  . LYS C 1 404 ? 30.962  6.223   74.990  1.00 55.77  ? 404 LYS C CD  1 
ATOM   11525 C CE  . LYS C 1 404 ? 32.425  6.644   75.095  1.00 67.00  ? 404 LYS C CE  1 
ATOM   11526 N NZ  . LYS C 1 404 ? 33.090  6.153   76.337  1.00 77.26  ? 404 LYS C NZ  1 
ATOM   11527 N N   . ALA C 1 405 ? 30.300  1.644   72.321  1.00 54.52  ? 405 ALA C N   1 
ATOM   11528 C CA  . ALA C 1 405 ? 29.360  0.663   71.797  1.00 49.10  ? 405 ALA C CA  1 
ATOM   11529 C C   . ALA C 1 405 ? 27.942  1.213   71.782  1.00 59.89  ? 405 ALA C C   1 
ATOM   11530 O O   . ALA C 1 405 ? 27.525  1.938   72.690  1.00 65.96  ? 405 ALA C O   1 
ATOM   11531 C CB  . ALA C 1 405 ? 29.411  -0.622  72.620  1.00 51.54  ? 405 ALA C CB  1 
ATOM   11532 N N   . GLY C 1 406 ? 27.201  0.862   70.740  1.00 56.47  ? 406 GLY C N   1 
ATOM   11533 C CA  . GLY C 1 406 ? 25.817  1.271   70.662  1.00 53.11  ? 406 GLY C CA  1 
ATOM   11534 C C   . GLY C 1 406 ? 25.182  0.793   69.377  1.00 56.38  ? 406 GLY C C   1 
ATOM   11535 O O   . GLY C 1 406 ? 25.750  -0.013  68.638  1.00 54.45  ? 406 GLY C O   1 
ATOM   11536 N N   . THR C 1 407 ? 23.983  1.304   69.135  1.00 55.08  ? 407 THR C N   1 
ATOM   11537 C CA  . THR C 1 407 ? 23.171  1.026   67.963  1.00 54.99  ? 407 THR C CA  1 
ATOM   11538 C C   . THR C 1 407 ? 22.803  2.348   67.303  1.00 61.16  ? 407 THR C C   1 
ATOM   11539 O O   . THR C 1 407 ? 23.158  3.427   67.787  1.00 60.63  ? 407 THR C O   1 
ATOM   11540 C CB  . THR C 1 407 ? 21.892  0.273   68.339  1.00 60.46  ? 407 THR C CB  1 
ATOM   11541 O OG1 . THR C 1 407 ? 21.023  1.154   69.072  1.00 59.84  ? 407 THR C OG1 1 
ATOM   11542 C CG2 . THR C 1 407 ? 22.204  -0.943  69.196  1.00 51.98  ? 407 THR C CG2 1 
ATOM   11543 N N   . TRP C 1 408 ? 22.067  2.267   66.195  1.00 59.43  ? 408 TRP C N   1 
ATOM   11544 C CA  . TRP C 1 408 ? 21.506  3.477   65.613  1.00 56.31  ? 408 TRP C CA  1 
ATOM   11545 C C   . TRP C 1 408 ? 20.252  3.933   66.333  1.00 60.93  ? 408 TRP C C   1 
ATOM   11546 O O   . TRP C 1 408 ? 19.547  4.812   65.827  1.00 61.22  ? 408 TRP C O   1 
ATOM   11547 C CB  . TRP C 1 408 ? 21.220  3.285   64.123  1.00 55.44  ? 408 TRP C CB  1 
ATOM   11548 C CG  . TRP C 1 408 ? 20.281  2.171   63.752  1.00 62.38  ? 408 TRP C CG  1 
ATOM   11549 C CD1 . TRP C 1 408 ? 19.522  1.401   64.589  1.00 65.09  ? 408 TRP C CD1 1 
ATOM   11550 C CD2 . TRP C 1 408 ? 20.001  1.712   62.422  1.00 59.29  ? 408 TRP C CD2 1 
ATOM   11551 N NE1 . TRP C 1 408 ? 18.793  0.486   63.860  1.00 59.45  ? 408 TRP C NE1 1 
ATOM   11552 C CE2 . TRP C 1 408 ? 19.071  0.658   62.528  1.00 56.58  ? 408 TRP C CE2 1 
ATOM   11553 C CE3 . TRP C 1 408 ? 20.454  2.088   61.152  1.00 51.29  ? 408 TRP C CE3 1 
ATOM   11554 C CZ2 . TRP C 1 408 ? 18.585  -0.021  61.413  1.00 64.67  ? 408 TRP C CZ2 1 
ATOM   11555 C CZ3 . TRP C 1 408 ? 19.971  1.415   60.050  1.00 50.90  ? 408 TRP C CZ3 1 
ATOM   11556 C CH2 . TRP C 1 408 ? 19.047  0.373   60.185  1.00 61.45  ? 408 TRP C CH2 1 
ATOM   11557 N N   . PHE C 1 409 ? 19.978  3.361   67.502  1.00 56.43  ? 409 PHE C N   1 
ATOM   11558 C CA  . PHE C 1 409 ? 18.773  3.624   68.282  1.00 62.98  ? 409 PHE C CA  1 
ATOM   11559 C C   . PHE C 1 409 ? 19.214  4.273   69.589  1.00 64.79  ? 409 PHE C C   1 
ATOM   11560 O O   . PHE C 1 409 ? 19.474  3.582   70.579  1.00 65.24  ? 409 PHE C O   1 
ATOM   11561 C CB  . PHE C 1 409 ? 17.988  2.325   68.524  1.00 65.06  ? 409 PHE C CB  1 
ATOM   11562 C CG  . PHE C 1 409 ? 16.504  2.520   68.613  1.00 66.92  ? 409 PHE C CG  1 
ATOM   11563 C CD1 . PHE C 1 409 ? 15.722  2.543   67.469  1.00 72.06  ? 409 PHE C CD1 1 
ATOM   11564 C CD2 . PHE C 1 409 ? 15.891  2.706   69.843  1.00 72.40  ? 409 PHE C CD2 1 
ATOM   11565 C CE1 . PHE C 1 409 ? 14.348  2.732   67.553  1.00 77.67  ? 409 PHE C CE1 1 
ATOM   11566 C CE2 . PHE C 1 409 ? 14.520  2.898   69.932  1.00 68.21  ? 409 PHE C CE2 1 
ATOM   11567 C CZ  . PHE C 1 409 ? 13.749  2.910   68.786  1.00 68.18  ? 409 PHE C CZ  1 
ATOM   11568 N N   . ASP C 1 410 ? 19.318  5.601   69.579  1.00 61.32  ? 410 ASP C N   1 
ATOM   11569 C CA  . ASP C 1 410 ? 19.743  6.409   70.718  1.00 60.93  ? 410 ASP C CA  1 
ATOM   11570 C C   . ASP C 1 410 ? 21.187  6.141   71.132  1.00 58.08  ? 410 ASP C C   1 
ATOM   11571 O O   . ASP C 1 410 ? 21.626  6.640   72.174  1.00 66.92  ? 410 ASP C O   1 
ATOM   11572 C CB  . ASP C 1 410 ? 18.818  6.216   71.925  1.00 60.11  ? 410 ASP C CB  1 
ATOM   11573 C CG  . ASP C 1 410 ? 17.418  6.724   71.674  1.00 76.27  ? 410 ASP C CG  1 
ATOM   11574 O OD1 . ASP C 1 410 ? 17.280  7.889   71.243  1.00 98.31  ? 410 ASP C OD1 1 
ATOM   11575 O OD2 . ASP C 1 410 ? 16.457  5.959   71.901  1.00 80.13  ? 410 ASP C OD2 1 
ATOM   11576 N N   . GLY C 1 411 ? 21.938  5.368   70.349  1.00 58.71  ? 411 GLY C N   1 
ATOM   11577 C CA  . GLY C 1 411 ? 23.303  5.038   70.699  1.00 52.84  ? 411 GLY C CA  1 
ATOM   11578 C C   . GLY C 1 411 ? 23.457  3.978   71.763  1.00 60.83  ? 411 GLY C C   1 
ATOM   11579 O O   . GLY C 1 411 ? 24.580  3.742   72.216  1.00 61.19  ? 411 GLY C O   1 
ATOM   11580 N N   . ASN C 1 412 ? 22.372  3.327   72.175  1.00 58.91  ? 412 ASN C N   1 
ATOM   11581 C CA  . ASN C 1 412 ? 22.418  2.333   73.234  1.00 48.88  ? 412 ASN C CA  1 
ATOM   11582 C C   . ASN C 1 412 ? 21.690  1.075   72.785  1.00 55.26  ? 412 ASN C C   1 
ATOM   11583 O O   . ASN C 1 412 ? 21.052  1.044   71.729  1.00 61.89  ? 412 ASN C O   1 
ATOM   11584 C CB  . ASN C 1 412 ? 21.810  2.881   74.533  1.00 53.95  ? 412 ASN C CB  1 
ATOM   11585 C CG  . ASN C 1 412 ? 20.371  3.323   74.368  1.00 53.74  ? 412 ASN C CG  1 
ATOM   11586 O OD1 . ASN C 1 412 ? 19.514  2.544   73.954  1.00 65.80  ? 412 ASN C OD1 1 
ATOM   11587 N ND2 . ASN C 1 412 ? 20.097  4.580   74.694  1.00 60.43  ? 412 ASN C ND2 1 
ATOM   11588 N N   . PHE C 1 413 ? 21.782  0.030   73.610  1.00 58.23  ? 413 PHE C N   1 
ATOM   11589 C CA  . PHE C 1 413 ? 21.123  -1.245  73.354  1.00 53.87  ? 413 PHE C CA  1 
ATOM   11590 C C   . PHE C 1 413 ? 19.805  -1.390  74.118  1.00 53.95  ? 413 PHE C C   1 
ATOM   11591 O O   . PHE C 1 413 ? 19.365  -2.517  74.368  1.00 56.34  ? 413 PHE C O   1 
ATOM   11592 C CB  . PHE C 1 413 ? 22.059  -2.405  73.709  1.00 57.90  ? 413 PHE C CB  1 
ATOM   11593 C CG  . PHE C 1 413 ? 23.420  -2.309  73.089  1.00 51.94  ? 413 PHE C CG  1 
ATOM   11594 C CD1 . PHE C 1 413 ? 24.441  -1.636  73.736  1.00 51.11  ? 413 PHE C CD1 1 
ATOM   11595 C CD2 . PHE C 1 413 ? 23.677  -2.881  71.853  1.00 50.75  ? 413 PHE C CD2 1 
ATOM   11596 C CE1 . PHE C 1 413 ? 25.691  -1.535  73.169  1.00 50.67  ? 413 PHE C CE1 1 
ATOM   11597 C CE2 . PHE C 1 413 ? 24.931  -2.788  71.279  1.00 48.75  ? 413 PHE C CE2 1 
ATOM   11598 C CZ  . PHE C 1 413 ? 25.938  -2.113  71.937  1.00 54.59  ? 413 PHE C CZ  1 
ATOM   11599 N N   . LEU C 1 414 ? 19.158  -0.280  74.484  1.00 55.63  ? 414 LEU C N   1 
ATOM   11600 C CA  . LEU C 1 414 ? 18.008  -0.351  75.382  1.00 54.10  ? 414 LEU C CA  1 
ATOM   11601 C C   . LEU C 1 414 ? 16.734  -0.797  74.680  1.00 53.99  ? 414 LEU C C   1 
ATOM   11602 O O   . LEU C 1 414 ? 15.729  -1.053  75.349  1.00 53.76  ? 414 LEU C O   1 
ATOM   11603 C CB  . LEU C 1 414 ? 17.777  1.001   76.064  1.00 46.91  ? 414 LEU C CB  1 
ATOM   11604 C CG  . LEU C 1 414 ? 18.506  1.254   77.390  1.00 53.60  ? 414 LEU C CG  1 
ATOM   11605 C CD1 . LEU C 1 414 ? 17.753  0.689   78.587  1.00 47.29  ? 414 LEU C CD1 1 
ATOM   11606 C CD2 . LEU C 1 414 ? 19.904  0.671   77.339  1.00 61.49  ? 414 LEU C CD2 1 
ATOM   11607 N N   . LYS C 1 415 ? 16.748  -0.894  73.359  1.00 55.26  ? 415 LYS C N   1 
ATOM   11608 C CA  . LYS C 1 415 ? 15.631  -1.472  72.635  1.00 57.53  ? 415 LYS C CA  1 
ATOM   11609 C C   . LYS C 1 415 ? 15.589  -2.995  72.740  1.00 64.19  ? 415 LYS C C   1 
ATOM   11610 O O   . LYS C 1 415 ? 14.551  -3.592  72.439  1.00 70.27  ? 415 LYS C O   1 
ATOM   11611 C CB  . LYS C 1 415 ? 15.704  -1.019  71.172  1.00 63.44  ? 415 LYS C CB  1 
ATOM   11612 C CG  . LYS C 1 415 ? 14.567  -1.468  70.294  1.00 67.60  ? 415 LYS C CG  1 
ATOM   11613 C CD  . LYS C 1 415 ? 13.529  -0.377  70.137  1.00 75.18  ? 415 LYS C CD  1 
ATOM   11614 C CE  . LYS C 1 415 ? 12.141  -0.966  69.928  1.00 80.89  ? 415 LYS C CE  1 
ATOM   11615 N NZ  . LYS C 1 415 ? 11.824  -2.029  70.926  1.00 75.12  ? 415 LYS C NZ  1 
ATOM   11616 N N   . TRP C 1 416 ? 16.670  -3.638  73.195  1.00 62.04  ? 416 TRP C N   1 
ATOM   11617 C CA  . TRP C 1 416 ? 16.737  -5.096  73.256  1.00 57.64  ? 416 TRP C CA  1 
ATOM   11618 C C   . TRP C 1 416 ? 17.129  -5.643  74.619  1.00 57.70  ? 416 TRP C C   1 
ATOM   11619 O O   . TRP C 1 416 ? 17.103  -6.863  74.800  1.00 60.42  ? 416 TRP C O   1 
ATOM   11620 C CB  . TRP C 1 416 ? 17.731  -5.638  72.214  1.00 58.88  ? 416 TRP C CB  1 
ATOM   11621 C CG  . TRP C 1 416 ? 17.503  -5.109  70.829  1.00 63.54  ? 416 TRP C CG  1 
ATOM   11622 C CD1 . TRP C 1 416 ? 16.840  -5.730  69.811  1.00 61.14  ? 416 TRP C CD1 1 
ATOM   11623 C CD2 . TRP C 1 416 ? 17.931  -3.843  70.313  1.00 62.50  ? 416 TRP C CD2 1 
ATOM   11624 N NE1 . TRP C 1 416 ? 16.833  -4.931  68.689  1.00 57.96  ? 416 TRP C NE1 1 
ATOM   11625 C CE2 . TRP C 1 416 ? 17.496  -3.767  68.974  1.00 56.42  ? 416 TRP C CE2 1 
ATOM   11626 C CE3 . TRP C 1 416 ? 18.644  -2.769  70.854  1.00 59.96  ? 416 TRP C CE3 1 
ATOM   11627 C CZ2 . TRP C 1 416 ? 17.749  -2.659  68.171  1.00 53.51  ? 416 TRP C CZ2 1 
ATOM   11628 C CZ3 . TRP C 1 416 ? 18.892  -1.668  70.054  1.00 59.62  ? 416 TRP C CZ3 1 
ATOM   11629 C CH2 . TRP C 1 416 ? 18.447  -1.622  68.729  1.00 58.41  ? 416 TRP C CH2 1 
ATOM   11630 N N   . ILE C 1 417 ? 17.498  -4.792  75.573  1.00 52.89  ? 417 ILE C N   1 
ATOM   11631 C CA  . ILE C 1 417 ? 17.937  -5.239  76.885  1.00 55.05  ? 417 ILE C CA  1 
ATOM   11632 C C   . ILE C 1 417 ? 17.680  -4.114  77.873  1.00 59.62  ? 417 ILE C C   1 
ATOM   11633 O O   . ILE C 1 417 ? 17.440  -2.968  77.490  1.00 61.29  ? 417 ILE C O   1 
ATOM   11634 C CB  . ILE C 1 417 ? 19.435  -5.643  76.873  1.00 53.42  ? 417 ILE C CB  1 
ATOM   11635 C CG1 . ILE C 1 417 ? 19.733  -6.642  77.984  1.00 55.81  ? 417 ILE C CG1 1 
ATOM   11636 C CG2 . ILE C 1 417 ? 20.331  -4.430  76.994  1.00 51.57  ? 417 ILE C CG2 1 
ATOM   11637 C CD1 . ILE C 1 417 ? 20.709  -7.697  77.567  1.00 49.51  ? 417 ILE C CD1 1 
ATOM   11638 N N   . GLY C 1 418 ? 17.685  -4.457  79.161  1.00 52.10  ? 418 GLY C N   1 
ATOM   11639 C CA  . GLY C 1 418 ? 17.668  -3.457  80.203  1.00 49.05  ? 418 GLY C CA  1 
ATOM   11640 C C   . GLY C 1 418 ? 16.346  -3.190  80.893  1.00 59.36  ? 418 GLY C C   1 
ATOM   11641 O O   . GLY C 1 418 ? 16.325  -2.376  81.823  1.00 67.47  ? 418 GLY C O   1 
ATOM   11642 N N   . ASN C 1 419 ? 15.244  -3.817  80.470  1.00 68.03  ? 419 ASN C N   1 
ATOM   11643 C CA  . ASN C 1 419 ? 13.984  -3.790  81.216  1.00 68.27  ? 419 ASN C CA  1 
ATOM   11644 C C   . ASN C 1 419 ? 13.585  -5.208  81.619  1.00 65.86  ? 419 ASN C C   1 
ATOM   11645 O O   . ASN C 1 419 ? 14.134  -6.196  81.125  1.00 70.48  ? 419 ASN C O   1 
ATOM   11646 C CB  . ASN C 1 419 ? 12.856  -3.079  80.426  1.00 62.88  ? 419 ASN C CB  1 
ATOM   11647 C CG  . ASN C 1 419 ? 12.441  -3.805  79.142  1.00 67.94  ? 419 ASN C CG  1 
ATOM   11648 O OD1 . ASN C 1 419 ? 12.665  -4.999  78.964  1.00 74.69  ? 419 ASN C OD1 1 
ATOM   11649 N ND2 . ASN C 1 419 ? 11.816  -3.059  78.242  1.00 66.52  ? 419 ASN C ND2 1 
ATOM   11650 N N   . LYS C 1 420 ? 12.619  -5.301  82.540  1.00 65.65  ? 420 LYS C N   1 
ATOM   11651 C CA  . LYS C 1 420 ? 12.248  -6.604  83.087  1.00 65.72  ? 420 LYS C CA  1 
ATOM   11652 C C   . LYS C 1 420 ? 11.813  -7.569  81.988  1.00 75.04  ? 420 LYS C C   1 
ATOM   11653 O O   . LYS C 1 420 ? 12.217  -8.740  81.985  1.00 72.12  ? 420 LYS C O   1 
ATOM   11654 C CB  . LYS C 1 420 ? 11.142  -6.443  84.130  1.00 67.61  ? 420 LYS C CB  1 
ATOM   11655 C CG  . LYS C 1 420 ? 10.421  -7.738  84.460  1.00 82.84  ? 420 LYS C CG  1 
ATOM   11656 C CD  . LYS C 1 420 ? 8.951   -7.495  84.754  1.00 83.71  ? 420 LYS C CD  1 
ATOM   11657 C CE  . LYS C 1 420 ? 8.127   -8.737  84.460  1.00 85.25  ? 420 LYS C CE  1 
ATOM   11658 N NZ  . LYS C 1 420 ? 8.897   -9.985  84.726  1.00 88.44  ? 420 LYS C NZ  1 
ATOM   11659 N N   . GLU C 1 421 ? 11.019  -7.086  81.023  1.00 72.58  ? 421 GLU C N   1 
ATOM   11660 C CA  . GLU C 1 421 ? 10.479  -7.968  79.990  1.00 64.45  ? 421 GLU C CA  1 
ATOM   11661 C C   . GLU C 1 421 ? 11.561  -8.436  79.021  1.00 70.30  ? 421 GLU C C   1 
ATOM   11662 O O   . GLU C 1 421 ? 11.616  -9.622  78.677  1.00 73.10  ? 421 GLU C O   1 
ATOM   11663 C CB  . GLU C 1 421 ? 9.337   -7.271  79.233  1.00 69.52  ? 421 GLU C CB  1 
ATOM   11664 C CG  . GLU C 1 421 ? 8.356   -6.421  80.081  1.00 79.71  ? 421 GLU C CG  1 
ATOM   11665 C CD  . GLU C 1 421 ? 8.903   -5.057  80.458  1.00 83.70  ? 421 GLU C CD  1 
ATOM   11666 O OE1 . GLU C 1 421 ? 8.122   -4.202  80.942  1.00 77.41  ? 421 GLU C OE1 1 
ATOM   11667 O OE2 . GLU C 1 421 ? 10.128  -4.861  80.285  1.00 84.70  ? 421 GLU C OE2 1 
ATOM   11668 N N   . LYS C 1 422 ? 12.433  -7.529  78.569  1.00 66.84  ? 422 LYS C N   1 
ATOM   11669 C CA  . LYS C 1 422 ? 13.476  -7.925  77.623  1.00 60.83  ? 422 LYS C CA  1 
ATOM   11670 C C   . LYS C 1 422 ? 14.553  -8.784  78.280  1.00 56.79  ? 422 LYS C C   1 
ATOM   11671 O O   . LYS C 1 422 ? 15.108  -9.683  77.637  1.00 54.46  ? 422 LYS C O   1 
ATOM   11672 C CB  . LYS C 1 422 ? 14.110  -6.689  76.993  1.00 65.01  ? 422 LYS C CB  1 
ATOM   11673 C CG  . LYS C 1 422 ? 13.296  -6.102  75.855  1.00 63.81  ? 422 LYS C CG  1 
ATOM   11674 C CD  . LYS C 1 422 ? 13.827  -4.740  75.456  1.00 62.03  ? 422 LYS C CD  1 
ATOM   11675 C CE  . LYS C 1 422 ? 12.713  -3.779  75.089  1.00 63.65  ? 422 LYS C CE  1 
ATOM   11676 N NZ  . LYS C 1 422 ? 12.158  -4.069  73.737  1.00 66.07  ? 422 LYS C NZ  1 
ATOM   11677 N N   . ASN C 1 423 ? 14.858  -8.529  79.554  1.00 60.84  ? 423 ASN C N   1 
ATOM   11678 C CA  . ASN C 1 423 ? 15.854  -9.341  80.242  1.00 52.93  ? 423 ASN C CA  1 
ATOM   11679 C C   . ASN C 1 423 ? 15.388  -10.782 80.390  1.00 55.66  ? 423 ASN C C   1 
ATOM   11680 O O   . ASN C 1 423 ? 16.218  -11.695 80.469  1.00 58.15  ? 423 ASN C O   1 
ATOM   11681 C CB  . ASN C 1 423 ? 16.174  -8.742  81.614  1.00 53.98  ? 423 ASN C CB  1 
ATOM   11682 C CG  . ASN C 1 423 ? 16.835  -7.375  81.525  1.00 54.39  ? 423 ASN C CG  1 
ATOM   11683 O OD1 . ASN C 1 423 ? 17.417  -7.009  80.503  1.00 58.32  ? 423 ASN C OD1 1 
ATOM   11684 N ND2 . ASN C 1 423 ? 16.737  -6.608  82.603  1.00 51.80  ? 423 ASN C ND2 1 
ATOM   11685 N N   . GLU C 1 424 ? 14.071  -11.010 80.425  1.00 62.88  ? 424 GLU C N   1 
ATOM   11686 C CA  . GLU C 1 424 ? 13.567  -12.371 80.577  1.00 61.92  ? 424 GLU C CA  1 
ATOM   11687 C C   . GLU C 1 424 ? 13.901  -13.222 79.358  1.00 59.91  ? 424 GLU C C   1 
ATOM   11688 O O   . GLU C 1 424 ? 14.272  -14.394 79.497  1.00 64.56  ? 424 GLU C O   1 
ATOM   11689 C CB  . GLU C 1 424 ? 12.061  -12.351 80.833  1.00 57.66  ? 424 GLU C CB  1 
ATOM   11690 C CG  . GLU C 1 424 ? 11.620  -13.296 81.942  1.00 72.65  ? 424 GLU C CG  1 
ATOM   11691 C CD  . GLU C 1 424 ? 11.227  -14.664 81.419  1.00 83.22  ? 424 GLU C CD  1 
ATOM   11692 O OE1 . GLU C 1 424 ? 10.637  -14.726 80.319  1.00 83.34  ? 424 GLU C OE1 1 
ATOM   11693 O OE2 . GLU C 1 424 ? 11.510  -15.675 82.101  1.00 82.24  ? 424 GLU C OE2 1 
ATOM   11694 N N   . TYR C 1 425 ? 13.790  -12.648 78.157  1.00 50.72  ? 425 TYR C N   1 
ATOM   11695 C CA  . TYR C 1 425 ? 14.230  -13.360 76.964  1.00 52.32  ? 425 TYR C CA  1 
ATOM   11696 C C   . TYR C 1 425 ? 15.713  -13.687 77.044  1.00 55.12  ? 425 TYR C C   1 
ATOM   11697 O O   . TYR C 1 425 ? 16.143  -14.777 76.648  1.00 59.68  ? 425 TYR C O   1 
ATOM   11698 C CB  . TYR C 1 425 ? 13.949  -12.529 75.717  1.00 56.94  ? 425 TYR C CB  1 
ATOM   11699 C CG  . TYR C 1 425 ? 12.665  -12.869 74.993  1.00 62.22  ? 425 TYR C CG  1 
ATOM   11700 C CD1 . TYR C 1 425 ? 11.550  -13.331 75.682  1.00 60.15  ? 425 TYR C CD1 1 
ATOM   11701 C CD2 . TYR C 1 425 ? 12.567  -12.716 73.615  1.00 55.99  ? 425 TYR C CD2 1 
ATOM   11702 C CE1 . TYR C 1 425 ? 10.383  -13.632 75.020  1.00 60.80  ? 425 TYR C CE1 1 
ATOM   11703 C CE2 . TYR C 1 425 ? 11.405  -13.015 72.948  1.00 55.94  ? 425 TYR C CE2 1 
ATOM   11704 C CZ  . TYR C 1 425 ? 10.313  -13.475 73.655  1.00 64.81  ? 425 TYR C CZ  1 
ATOM   11705 O OH  . TYR C 1 425 ? 9.134   -13.779 73.006  1.00 68.36  ? 425 TYR C OH  1 
ATOM   11706 N N   . TRP C 1 426 ? 16.509  -12.758 77.567  1.00 54.00  ? 426 TRP C N   1 
ATOM   11707 C CA  . TRP C 1 426 ? 17.939  -13.005 77.697  1.00 62.07  ? 426 TRP C CA  1 
ATOM   11708 C C   . TRP C 1 426 ? 18.222  -14.098 78.723  1.00 61.49  ? 426 TRP C C   1 
ATOM   11709 O O   . TRP C 1 426 ? 19.146  -14.900 78.541  1.00 68.74  ? 426 TRP C O   1 
ATOM   11710 C CB  . TRP C 1 426 ? 18.652  -11.706 78.058  1.00 60.02  ? 426 TRP C CB  1 
ATOM   11711 C CG  . TRP C 1 426 ? 18.786  -10.801 76.878  1.00 60.52  ? 426 TRP C CG  1 
ATOM   11712 C CD1 . TRP C 1 426 ? 18.000  -9.729  76.567  1.00 57.41  ? 426 TRP C CD1 1 
ATOM   11713 C CD2 . TRP C 1 426 ? 19.754  -10.906 75.831  1.00 50.45  ? 426 TRP C CD2 1 
ATOM   11714 N NE1 . TRP C 1 426 ? 18.428  -9.153  75.394  1.00 48.95  ? 426 TRP C NE1 1 
ATOM   11715 C CE2 . TRP C 1 426 ? 19.504  -9.858  74.922  1.00 50.86  ? 426 TRP C CE2 1 
ATOM   11716 C CE3 . TRP C 1 426 ? 20.810  -11.783 75.576  1.00 43.78  ? 426 TRP C CE3 1 
ATOM   11717 C CZ2 . TRP C 1 426 ? 20.273  -9.665  73.781  1.00 46.04  ? 426 TRP C CZ2 1 
ATOM   11718 C CZ3 . TRP C 1 426 ? 21.570  -11.590 74.446  1.00 46.83  ? 426 TRP C CZ3 1 
ATOM   11719 C CH2 . TRP C 1 426 ? 21.299  -10.540 73.561  1.00 48.77  ? 426 TRP C CH2 1 
ATOM   11720 N N   . LYS C 1 427 ? 17.429  -14.162 79.796  1.00 58.83  ? 427 LYS C N   1 
ATOM   11721 C CA  . LYS C 1 427 ? 17.590  -15.253 80.751  1.00 58.63  ? 427 LYS C CA  1 
ATOM   11722 C C   . LYS C 1 427 ? 17.190  -16.591 80.141  1.00 57.78  ? 427 LYS C C   1 
ATOM   11723 O O   . LYS C 1 427 ? 17.757  -17.630 80.500  1.00 58.09  ? 427 LYS C O   1 
ATOM   11724 C CB  . LYS C 1 427 ? 16.772  -14.979 82.015  1.00 60.06  ? 427 LYS C CB  1 
ATOM   11725 C CG  . LYS C 1 427 ? 17.574  -14.442 83.193  1.00 62.26  ? 427 LYS C CG  1 
ATOM   11726 C CD  . LYS C 1 427 ? 18.730  -15.376 83.585  1.00 66.64  ? 427 LYS C CD  1 
ATOM   11727 C CE  . LYS C 1 427 ? 19.858  -14.625 84.328  1.00 67.50  ? 427 LYS C CE  1 
ATOM   11728 N NZ  . LYS C 1 427 ? 21.243  -15.148 84.082  1.00 57.55  ? 427 LYS C NZ  1 
ATOM   11729 N N   . ILE C 1 428 ? 16.210  -16.584 79.231  1.00 52.30  ? 428 ILE C N   1 
ATOM   11730 C CA  . ILE C 1 428 ? 15.823  -17.807 78.531  1.00 50.77  ? 428 ILE C CA  1 
ATOM   11731 C C   . ILE C 1 428 ? 16.930  -18.251 77.592  1.00 54.35  ? 428 ILE C C   1 
ATOM   11732 O O   . ILE C 1 428 ? 17.269  -19.439 77.522  1.00 54.65  ? 428 ILE C O   1 
ATOM   11733 C CB  . ILE C 1 428 ? 14.503  -17.596 77.769  1.00 57.33  ? 428 ILE C CB  1 
ATOM   11734 C CG1 . ILE C 1 428 ? 13.346  -17.424 78.741  1.00 55.09  ? 428 ILE C CG1 1 
ATOM   11735 C CG2 . ILE C 1 428 ? 14.223  -18.755 76.838  1.00 54.03  ? 428 ILE C CG2 1 
ATOM   11736 C CD1 . ILE C 1 428 ? 12.255  -16.545 78.217  1.00 51.29  ? 428 ILE C CD1 1 
ATOM   11737 N N   . LEU C 1 429 ? 17.500  -17.305 76.845  1.00 56.59  ? 429 LEU C N   1 
ATOM   11738 C CA  . LEU C 1 429 ? 18.556  -17.637 75.898  1.00 53.19  ? 429 LEU C CA  1 
ATOM   11739 C C   . LEU C 1 429 ? 19.825  -18.068 76.620  1.00 56.18  ? 429 LEU C C   1 
ATOM   11740 O O   . LEU C 1 429 ? 20.466  -19.046 76.223  1.00 59.84  ? 429 LEU C O   1 
ATOM   11741 C CB  . LEU C 1 429 ? 18.817  -16.438 74.992  1.00 49.91  ? 429 LEU C CB  1 
ATOM   11742 C CG  . LEU C 1 429 ? 20.040  -16.484 74.088  1.00 52.80  ? 429 LEU C CG  1 
ATOM   11743 C CD1 . LEU C 1 429 ? 19.687  -17.162 72.778  1.00 54.79  ? 429 LEU C CD1 1 
ATOM   11744 C CD2 . LEU C 1 429 ? 20.562  -15.081 73.851  1.00 51.22  ? 429 LEU C CD2 1 
ATOM   11745 N N   . ILE C 1 430 ? 20.195  -17.361 77.692  1.00 54.15  ? 430 ILE C N   1 
ATOM   11746 C CA  . ILE C 1 430 ? 21.378  -17.734 78.467  1.00 59.77  ? 430 ILE C CA  1 
ATOM   11747 C C   . ILE C 1 430 ? 21.247  -19.161 78.977  1.00 63.75  ? 430 ILE C C   1 
ATOM   11748 O O   . ILE C 1 430 ? 22.197  -19.953 78.913  1.00 64.28  ? 430 ILE C O   1 
ATOM   11749 C CB  . ILE C 1 430 ? 21.595  -16.738 79.621  1.00 63.63  ? 430 ILE C CB  1 
ATOM   11750 C CG1 . ILE C 1 430 ? 22.378  -15.521 79.144  1.00 60.20  ? 430 ILE C CG1 1 
ATOM   11751 C CG2 . ILE C 1 430 ? 22.290  -17.398 80.812  1.00 56.06  ? 430 ILE C CG2 1 
ATOM   11752 C CD1 . ILE C 1 430 ? 22.045  -14.292 79.925  1.00 59.65  ? 430 ILE C CD1 1 
ATOM   11753 N N   . GLU C 1 431 ? 20.059  -19.515 79.472  1.00 61.22  ? 431 GLU C N   1 
ATOM   11754 C CA  . GLU C 1 431 ? 19.860  -20.836 80.055  1.00 65.24  ? 431 GLU C CA  1 
ATOM   11755 C C   . GLU C 1 431 ? 19.872  -21.920 78.988  1.00 66.73  ? 431 GLU C C   1 
ATOM   11756 O O   . GLU C 1 431 ? 20.418  -23.007 79.206  1.00 75.86  ? 431 GLU C O   1 
ATOM   11757 C CB  . GLU C 1 431 ? 18.547  -20.870 80.837  1.00 65.79  ? 431 GLU C CB  1 
ATOM   11758 C CG  . GLU C 1 431 ? 18.670  -20.463 82.300  1.00 76.88  ? 431 GLU C CG  1 
ATOM   11759 C CD  . GLU C 1 431 ? 19.609  -21.365 83.090  1.00 82.73  ? 431 GLU C CD  1 
ATOM   11760 O OE1 . GLU C 1 431 ? 20.844  -21.263 82.916  1.00 78.94  ? 431 GLU C OE1 1 
ATOM   11761 O OE2 . GLU C 1 431 ? 19.107  -22.191 83.884  1.00 83.32  ? 431 GLU C OE2 1 
ATOM   11762 N N   . ALA C 1 432 ? 19.262  -21.650 77.833  1.00 61.32  ? 432 ALA C N   1 
ATOM   11763 C CA  . ALA C 1 432 ? 19.277  -22.635 76.761  1.00 64.61  ? 432 ALA C CA  1 
ATOM   11764 C C   . ALA C 1 432 ? 20.694  -22.850 76.234  1.00 55.78  ? 432 ALA C C   1 
ATOM   11765 O O   . ALA C 1 432 ? 21.104  -23.991 75.992  1.00 53.54  ? 432 ALA C O   1 
ATOM   11766 C CB  . ALA C 1 432 ? 18.322  -22.209 75.645  1.00 58.80  ? 432 ALA C CB  1 
ATOM   11767 N N   . LYS C 1 433 ? 21.470  -21.771 76.092  1.00 53.20  ? 433 LYS C N   1 
ATOM   11768 C CA  . LYS C 1 433 ? 22.839  -21.892 75.598  1.00 59.41  ? 433 LYS C CA  1 
ATOM   11769 C C   . LYS C 1 433 ? 23.672  -22.841 76.462  1.00 66.72  ? 433 LYS C C   1 
ATOM   11770 O O   . LYS C 1 433 ? 24.581  -23.511 75.954  1.00 63.19  ? 433 LYS C O   1 
ATOM   11771 C CB  . LYS C 1 433 ? 23.480  -20.501 75.518  1.00 52.55  ? 433 LYS C CB  1 
ATOM   11772 C CG  . LYS C 1 433 ? 24.967  -20.500 75.204  1.00 58.48  ? 433 LYS C CG  1 
ATOM   11773 C CD  . LYS C 1 433 ? 25.210  -20.589 73.707  1.00 62.25  ? 433 LYS C CD  1 
ATOM   11774 C CE  . LYS C 1 433 ? 26.695  -20.596 73.381  1.00 65.21  ? 433 LYS C CE  1 
ATOM   11775 N NZ  . LYS C 1 433 ? 27.221  -21.984 73.222  1.00 74.66  ? 433 LYS C NZ  1 
ATOM   11776 N N   . LYS C 1 434 ? 23.363  -22.938 77.758  1.00 65.02  ? 434 LYS C N   1 
ATOM   11777 C CA  . LYS C 1 434 ? 24.048  -23.909 78.608  1.00 63.35  ? 434 LYS C CA  1 
ATOM   11778 C C   . LYS C 1 434 ? 23.762  -25.336 78.163  1.00 60.57  ? 434 LYS C C   1 
ATOM   11779 O O   . LYS C 1 434 ? 24.657  -26.187 78.151  1.00 67.68  ? 434 LYS C O   1 
ATOM   11780 C CB  . LYS C 1 434 ? 23.628  -23.717 80.059  1.00 63.69  ? 434 LYS C CB  1 
ATOM   11781 C CG  . LYS C 1 434 ? 23.646  -22.268 80.486  1.00 67.38  ? 434 LYS C CG  1 
ATOM   11782 C CD  . LYS C 1 434 ? 23.813  -22.147 81.984  1.00 63.93  ? 434 LYS C CD  1 
ATOM   11783 C CE  . LYS C 1 434 ? 24.326  -20.772 82.390  1.00 66.96  ? 434 LYS C CE  1 
ATOM   11784 N NZ  . LYS C 1 434 ? 24.503  -20.648 83.871  1.00 87.40  ? 434 LYS C NZ  1 
ATOM   11785 N N   . LYS C 1 435 ? 22.519  -25.616 77.792  1.00 66.49  ? 435 LYS C N   1 
ATOM   11786 C CA  . LYS C 1 435 ? 22.123  -26.938 77.344  1.00 63.09  ? 435 LYS C CA  1 
ATOM   11787 C C   . LYS C 1 435 ? 21.955  -26.999 75.832  1.00 62.97  ? 435 LYS C C   1 
ATOM   11788 O O   . LYS C 1 435 ? 21.340  -27.940 75.322  1.00 69.55  ? 435 LYS C O   1 
ATOM   11789 C CB  . LYS C 1 435 ? 20.831  -27.353 78.049  1.00 69.09  ? 435 LYS C CB  1 
ATOM   11790 C CG  . LYS C 1 435 ? 20.836  -27.065 79.551  1.00 78.24  ? 435 LYS C CG  1 
ATOM   11791 C CD  . LYS C 1 435 ? 19.430  -26.873 80.113  1.00 80.72  ? 435 LYS C CD  1 
ATOM   11792 C CE  . LYS C 1 435 ? 19.465  -26.078 81.418  1.00 72.53  ? 435 LYS C CE  1 
ATOM   11793 N NZ  . LYS C 1 435 ? 18.121  -25.902 82.032  1.00 71.24  ? 435 LYS C NZ  1 
ATOM   11794 N N   . ALA C 1 436 ? 22.478  -26.015 75.104  1.00 60.04  ? 436 ALA C N   1 
ATOM   11795 C CA  . ALA C 1 436 ? 22.280  -25.965 73.662  1.00 59.82  ? 436 ALA C CA  1 
ATOM   11796 C C   . ALA C 1 436 ? 23.185  -26.973 72.972  1.00 61.26  ? 436 ALA C C   1 
ATOM   11797 O O   . ALA C 1 436 ? 24.390  -27.029 73.239  1.00 67.04  ? 436 ALA C O   1 
ATOM   11798 C CB  . ALA C 1 436 ? 22.541  -24.562 73.116  1.00 60.21  ? 436 ALA C CB  1 
ATOM   11799 N N   . LYS C 1 437 ? 22.595  -27.768 72.081  1.00 65.24  ? 437 LYS C N   1 
ATOM   11800 C CA  . LYS C 1 437 ? 23.318  -28.799 71.359  1.00 60.41  ? 437 LYS C CA  1 
ATOM   11801 C C   . LYS C 1 437 ? 23.149  -28.716 69.845  1.00 60.80  ? 437 LYS C C   1 
ATOM   11802 O O   . LYS C 1 437 ? 23.641  -29.603 69.138  1.00 61.21  ? 437 LYS C O   1 
ATOM   11803 C CB  . LYS C 1 437 ? 22.884  -30.184 71.863  1.00 54.98  ? 437 LYS C CB  1 
ATOM   11804 C CG  . LYS C 1 437 ? 22.907  -30.294 73.382  1.00 58.16  ? 437 LYS C CG  1 
ATOM   11805 C CD  . LYS C 1 437 ? 22.373  -31.631 73.844  1.00 69.88  ? 437 LYS C CD  1 
ATOM   11806 C CE  . LYS C 1 437 ? 21.104  -31.476 74.663  1.00 68.96  ? 437 LYS C CE  1 
ATOM   11807 N NZ  . LYS C 1 437 ? 21.318  -31.813 76.094  1.00 73.40  ? 437 LYS C NZ  1 
ATOM   11808 N N   . ASN C 1 438 ? 22.478  -27.684 69.325  1.00 60.24  ? 438 ASN C N   1 
ATOM   11809 C CA  . ASN C 1 438 ? 22.389  -27.460 67.886  1.00 61.31  ? 438 ASN C CA  1 
ATOM   11810 C C   . ASN C 1 438 ? 22.327  -25.966 67.602  1.00 58.71  ? 438 ASN C C   1 
ATOM   11811 O O   . ASN C 1 438 ? 22.220  -25.139 68.511  1.00 65.56  ? 438 ASN C O   1 
ATOM   11812 C CB  . ASN C 1 438 ? 21.189  -28.175 67.252  1.00 65.81  ? 438 ASN C CB  1 
ATOM   11813 C CG  . ASN C 1 438 ? 19.861  -27.755 67.841  1.00 71.77  ? 438 ASN C CG  1 
ATOM   11814 O OD1 . ASN C 1 438 ? 19.215  -26.821 67.361  1.00 70.16  ? 438 ASN C OD1 1 
ATOM   11815 N ND2 . ASN C 1 438 ? 19.426  -28.471 68.868  1.00 75.02  ? 438 ASN C ND2 1 
ATOM   11816 N N   . ASP C 1 439 ? 22.397  -25.622 66.317  1.00 58.53  ? 439 ASP C N   1 
ATOM   11817 C CA  . ASP C 1 439 ? 22.640  -24.238 65.928  1.00 63.65  ? 439 ASP C CA  1 
ATOM   11818 C C   . ASP C 1 439 ? 21.386  -23.381 65.960  1.00 61.33  ? 439 ASP C C   1 
ATOM   11819 O O   . ASP C 1 439 ? 21.448  -22.199 65.597  1.00 61.69  ? 439 ASP C O   1 
ATOM   11820 C CB  . ASP C 1 439 ? 23.289  -24.182 64.538  1.00 61.68  ? 439 ASP C CB  1 
ATOM   11821 C CG  . ASP C 1 439 ? 24.819  -24.285 64.597  1.00 73.95  ? 439 ASP C CG  1 
ATOM   11822 O OD1 . ASP C 1 439 ? 25.408  -24.031 65.672  1.00 68.49  ? 439 ASP C OD1 1 
ATOM   11823 O OD2 . ASP C 1 439 ? 25.438  -24.627 63.565  1.00 72.95  ? 439 ASP C OD2 1 
ATOM   11824 N N   . TYR C 1 440 ? 20.260  -23.930 66.408  1.00 65.89  ? 440 TYR C N   1 
ATOM   11825 C CA  . TYR C 1 440 ? 19.065  -23.111 66.548  1.00 63.61  ? 440 TYR C CA  1 
ATOM   11826 C C   . TYR C 1 440 ? 19.228  -22.045 67.618  1.00 62.52  ? 440 TYR C C   1 
ATOM   11827 O O   . TYR C 1 440 ? 18.423  -21.109 67.675  1.00 57.15  ? 440 TYR C O   1 
ATOM   11828 C CB  . TYR C 1 440 ? 17.867  -23.993 66.855  1.00 58.11  ? 440 TYR C CB  1 
ATOM   11829 C CG  . TYR C 1 440 ? 17.092  -24.374 65.622  1.00 65.23  ? 440 TYR C CG  1 
ATOM   11830 C CD1 . TYR C 1 440 ? 16.167  -23.501 65.068  1.00 63.80  ? 440 TYR C CD1 1 
ATOM   11831 C CD2 . TYR C 1 440 ? 17.292  -25.597 65.002  1.00 62.06  ? 440 TYR C CD2 1 
ATOM   11832 C CE1 . TYR C 1 440 ? 15.452  -23.842 63.944  1.00 60.59  ? 440 TYR C CE1 1 
ATOM   11833 C CE2 . TYR C 1 440 ? 16.578  -25.949 63.876  1.00 62.49  ? 440 TYR C CE2 1 
ATOM   11834 C CZ  . TYR C 1 440 ? 15.659  -25.066 63.349  1.00 63.68  ? 440 TYR C CZ  1 
ATOM   11835 O OH  . TYR C 1 440 ? 14.942  -25.405 62.222  1.00 71.55  ? 440 TYR C OH  1 
ATOM   11836 N N   . ILE C 1 441 ? 20.259  -22.166 68.459  1.00 64.76  ? 441 ILE C N   1 
ATOM   11837 C CA  . ILE C 1 441 ? 20.583  -21.099 69.398  1.00 62.15  ? 441 ILE C CA  1 
ATOM   11838 C C   . ILE C 1 441 ? 21.043  -19.858 68.640  1.00 57.38  ? 441 ILE C C   1 
ATOM   11839 O O   . ILE C 1 441 ? 20.851  -18.727 69.105  1.00 59.73  ? 441 ILE C O   1 
ATOM   11840 C CB  . ILE C 1 441 ? 21.632  -21.600 70.424  1.00 61.41  ? 441 ILE C CB  1 
ATOM   11841 C CG1 . ILE C 1 441 ? 21.752  -20.647 71.619  1.00 56.18  ? 441 ILE C CG1 1 
ATOM   11842 C CG2 . ILE C 1 441 ? 22.983  -21.858 69.767  1.00 62.22  ? 441 ILE C CG2 1 
ATOM   11843 C CD1 . ILE C 1 441 ? 20.544  -20.670 72.524  1.00 61.34  ? 441 ILE C CD1 1 
ATOM   11844 N N   . LEU C 1 442 ? 21.627  -20.041 67.452  1.00 55.41  ? 442 LEU C N   1 
ATOM   11845 C CA  . LEU C 1 442 ? 22.015  -18.892 66.641  1.00 56.81  ? 442 LEU C CA  1 
ATOM   11846 C C   . LEU C 1 442 ? 20.789  -18.192 66.077  1.00 54.66  ? 442 LEU C C   1 
ATOM   11847 O O   . LEU C 1 442 ? 20.775  -16.963 65.938  1.00 55.22  ? 442 LEU C O   1 
ATOM   11848 C CB  . LEU C 1 442 ? 22.948  -19.332 65.513  1.00 60.05  ? 442 LEU C CB  1 
ATOM   11849 C CG  . LEU C 1 442 ? 24.209  -20.080 65.935  1.00 54.55  ? 442 LEU C CG  1 
ATOM   11850 C CD1 . LEU C 1 442 ? 24.885  -20.693 64.732  1.00 53.22  ? 442 LEU C CD1 1 
ATOM   11851 C CD2 . LEU C 1 442 ? 25.145  -19.128 66.623  1.00 56.90  ? 442 LEU C CD2 1 
ATOM   11852 N N   . VAL C 1 443 ? 19.752  -18.961 65.739  1.00 54.66  ? 443 VAL C N   1 
ATOM   11853 C CA  . VAL C 1 443 ? 18.490  -18.352 65.330  1.00 58.22  ? 443 VAL C CA  1 
ATOM   11854 C C   . VAL C 1 443 ? 17.895  -17.553 66.482  1.00 53.39  ? 443 VAL C C   1 
ATOM   11855 O O   . VAL C 1 443 ? 17.460  -16.407 66.306  1.00 47.95  ? 443 VAL C O   1 
ATOM   11856 C CB  . VAL C 1 443 ? 17.506  -19.425 64.824  1.00 53.32  ? 443 VAL C CB  1 
ATOM   11857 C CG1 . VAL C 1 443 ? 16.413  -18.768 64.042  1.00 47.28  ? 443 VAL C CG1 1 
ATOM   11858 C CG2 . VAL C 1 443 ? 18.222  -20.458 63.969  1.00 57.93  ? 443 VAL C CG2 1 
ATOM   11859 N N   . ALA C 1 444 ? 17.877  -18.141 67.683  1.00 57.43  ? 444 ALA C N   1 
ATOM   11860 C CA  . ALA C 1 444 ? 17.308  -17.470 68.847  1.00 59.92  ? 444 ALA C CA  1 
ATOM   11861 C C   . ALA C 1 444 ? 18.104  -16.239 69.243  1.00 57.48  ? 444 ALA C C   1 
ATOM   11862 O O   . ALA C 1 444 ? 17.587  -15.387 69.975  1.00 63.94  ? 444 ALA C O   1 
ATOM   11863 C CB  . ALA C 1 444 ? 17.227  -18.437 70.031  1.00 55.40  ? 444 ALA C CB  1 
ATOM   11864 N N   . GLU C 1 445 ? 19.342  -16.128 68.774  1.00 47.24  ? 445 GLU C N   1 
ATOM   11865 C CA  . GLU C 1 445 ? 20.166  -14.964 69.039  1.00 49.99  ? 445 GLU C CA  1 
ATOM   11866 C C   . GLU C 1 445 ? 19.829  -13.782 68.138  1.00 49.65  ? 445 GLU C C   1 
ATOM   11867 O O   . GLU C 1 445 ? 20.530  -12.767 68.192  1.00 57.87  ? 445 GLU C O   1 
ATOM   11868 C CB  . GLU C 1 445 ? 21.645  -15.336 68.901  1.00 56.25  ? 445 GLU C CB  1 
ATOM   11869 C CG  . GLU C 1 445 ? 22.227  -15.961 70.160  1.00 55.98  ? 445 GLU C CG  1 
ATOM   11870 C CD  . GLU C 1 445 ? 23.266  -17.017 69.860  1.00 60.70  ? 445 GLU C CD  1 
ATOM   11871 O OE1 . GLU C 1 445 ? 24.006  -16.854 68.867  1.00 67.30  ? 445 GLU C OE1 1 
ATOM   11872 O OE2 . GLU C 1 445 ? 23.338  -18.012 70.611  1.00 61.95  ? 445 GLU C OE2 1 
ATOM   11873 N N   . GLY C 1 446 ? 18.781  -13.881 67.325  1.00 49.10  ? 446 GLY C N   1 
ATOM   11874 C CA  . GLY C 1 446 ? 18.428  -12.782 66.450  1.00 50.28  ? 446 GLY C CA  1 
ATOM   11875 C C   . GLY C 1 446 ? 17.873  -11.599 67.219  1.00 50.73  ? 446 GLY C C   1 
ATOM   11876 O O   . GLY C 1 446 ? 17.232  -11.743 68.258  1.00 55.15  ? 446 GLY C O   1 
ATOM   11877 N N   . SER C 1 447 ? 18.128  -10.403 66.690  1.00 52.44  ? 447 SER C N   1 
ATOM   11878 C CA  . SER C 1 447 ? 17.742  -9.190  67.402  1.00 57.12  ? 447 SER C CA  1 
ATOM   11879 C C   . SER C 1 447 ? 16.237  -8.972  67.382  1.00 56.86  ? 447 SER C C   1 
ATOM   11880 O O   . SER C 1 447 ? 15.701  -8.301  68.271  1.00 56.95  ? 447 SER C O   1 
ATOM   11881 C CB  . SER C 1 447 ? 18.466  -7.965  66.815  1.00 55.72  ? 447 SER C CB  1 
ATOM   11882 O OG  . SER C 1 447 ? 18.142  -7.756  65.444  1.00 56.42  ? 447 SER C OG  1 
ATOM   11883 N N   . ASP C 1 448 ? 15.542  -9.551  66.410  1.00 53.02  ? 448 ASP C N   1 
ATOM   11884 C CA  . ASP C 1 448 ? 14.128  -9.254  66.254  1.00 53.03  ? 448 ASP C CA  1 
ATOM   11885 C C   . ASP C 1 448 ? 13.322  -9.754  67.445  1.00 52.11  ? 448 ASP C C   1 
ATOM   11886 O O   . ASP C 1 448 ? 12.456  -9.033  67.953  1.00 53.32  ? 448 ASP C O   1 
ATOM   11887 C CB  . ASP C 1 448 ? 13.646  -9.844  64.934  1.00 54.06  ? 448 ASP C CB  1 
ATOM   11888 C CG  . ASP C 1 448 ? 14.624  -9.565  63.796  1.00 55.92  ? 448 ASP C CG  1 
ATOM   11889 O OD1 . ASP C 1 448 ? 15.579  -10.352 63.619  1.00 54.04  ? 448 ASP C OD1 1 
ATOM   11890 O OD2 . ASP C 1 448 ? 14.461  -8.538  63.100  1.00 55.73  ? 448 ASP C OD2 1 
ATOM   11891 N N   . TRP C 1 449 ? 13.640  -10.948 67.953  1.00 50.38  ? 449 TRP C N   1 
ATOM   11892 C CA  . TRP C 1 449 ? 12.874  -11.503 69.066  1.00 49.69  ? 449 TRP C CA  1 
ATOM   11893 C C   . TRP C 1 449 ? 12.850  -10.556 70.261  1.00 54.64  ? 449 TRP C C   1 
ATOM   11894 O O   . TRP C 1 449 ? 11.813  -10.400 70.916  1.00 64.80  ? 449 TRP C O   1 
ATOM   11895 C CB  . TRP C 1 449 ? 13.446  -12.863 69.461  1.00 49.41  ? 449 TRP C CB  1 
ATOM   11896 C CG  . TRP C 1 449 ? 13.790  -13.706 68.283  1.00 47.13  ? 449 TRP C CG  1 
ATOM   11897 C CD1 . TRP C 1 449 ? 14.999  -14.261 68.008  1.00 51.43  ? 449 TRP C CD1 1 
ATOM   11898 C CD2 . TRP C 1 449 ? 12.914  -14.097 67.211  1.00 53.57  ? 449 TRP C CD2 1 
ATOM   11899 N NE1 . TRP C 1 449 ? 14.942  -14.966 66.830  1.00 56.96  ? 449 TRP C NE1 1 
ATOM   11900 C CE2 . TRP C 1 449 ? 13.673  -14.885 66.322  1.00 55.33  ? 449 TRP C CE2 1 
ATOM   11901 C CE3 . TRP C 1 449 ? 11.565  -13.857 66.916  1.00 47.75  ? 449 TRP C CE3 1 
ATOM   11902 C CZ2 . TRP C 1 449 ? 13.133  -15.433 65.160  1.00 51.64  ? 449 TRP C CZ2 1 
ATOM   11903 C CZ3 . TRP C 1 449 ? 11.031  -14.401 65.761  1.00 52.72  ? 449 TRP C CZ3 1 
ATOM   11904 C CH2 . TRP C 1 449 ? 11.814  -15.181 64.897  1.00 54.36  ? 449 TRP C CH2 1 
ATOM   11905 N N   . PHE C 1 450 ? 13.970  -9.884  70.536  1.00 51.87  ? 450 PHE C N   1 
ATOM   11906 C CA  . PHE C 1 450 ? 14.047  -8.980  71.678  1.00 55.16  ? 450 PHE C CA  1 
ATOM   11907 C C   . PHE C 1 450 ? 13.368  -7.639  71.411  1.00 57.83  ? 450 PHE C C   1 
ATOM   11908 O O   . PHE C 1 450 ? 12.918  -6.980  72.357  1.00 57.82  ? 450 PHE C O   1 
ATOM   11909 C CB  . PHE C 1 450 ? 15.518  -8.774  72.064  1.00 65.06  ? 450 PHE C CB  1 
ATOM   11910 C CG  . PHE C 1 450 ? 16.243  -10.060 72.398  1.00 56.92  ? 450 PHE C CG  1 
ATOM   11911 C CD1 . PHE C 1 450 ? 16.118  -10.641 73.652  1.00 55.24  ? 450 PHE C CD1 1 
ATOM   11912 C CD2 . PHE C 1 450 ? 17.014  -10.708 71.444  1.00 51.99  ? 450 PHE C CD2 1 
ATOM   11913 C CE1 . PHE C 1 450 ? 16.772  -11.833 73.955  1.00 52.93  ? 450 PHE C CE1 1 
ATOM   11914 C CE2 . PHE C 1 450 ? 17.665  -11.901 71.740  1.00 52.66  ? 450 PHE C CE2 1 
ATOM   11915 C CZ  . PHE C 1 450 ? 17.543  -12.463 72.997  1.00 54.98  ? 450 PHE C CZ  1 
ATOM   11916 N N   . TRP C 1 451 ? 13.248  -7.245  70.142  1.00 62.86  ? 451 TRP C N   1 
ATOM   11917 C CA  . TRP C 1 451 ? 12.720  -5.925  69.818  1.00 62.42  ? 451 TRP C CA  1 
ATOM   11918 C C   . TRP C 1 451 ? 11.252  -5.801  70.214  1.00 62.75  ? 451 TRP C C   1 
ATOM   11919 O O   . TRP C 1 451 ? 10.835  -4.771  70.755  1.00 67.88  ? 451 TRP C O   1 
ATOM   11920 C CB  . TRP C 1 451 ? 12.937  -5.655  68.328  1.00 58.85  ? 451 TRP C CB  1 
ATOM   11921 C CG  . TRP C 1 451 ? 12.090  -4.589  67.711  1.00 70.39  ? 451 TRP C CG  1 
ATOM   11922 C CD1 . TRP C 1 451 ? 10.764  -4.673  67.403  1.00 74.93  ? 451 TRP C CD1 1 
ATOM   11923 C CD2 . TRP C 1 451 ? 12.523  -3.298  67.259  1.00 74.47  ? 451 TRP C CD2 1 
ATOM   11924 N NE1 . TRP C 1 451 ? 10.336  -3.506  66.821  1.00 79.62  ? 451 TRP C NE1 1 
ATOM   11925 C CE2 . TRP C 1 451 ? 11.397  -2.647  66.716  1.00 76.03  ? 451 TRP C CE2 1 
ATOM   11926 C CE3 . TRP C 1 451 ? 13.750  -2.627  67.268  1.00 69.94  ? 451 TRP C CE3 1 
ATOM   11927 C CZ2 . TRP C 1 451 ? 11.459  -1.358  66.193  1.00 76.31  ? 451 TRP C CZ2 1 
ATOM   11928 C CZ3 . TRP C 1 451 ? 13.808  -1.345  66.751  1.00 71.12  ? 451 TRP C CZ3 1 
ATOM   11929 C CH2 . TRP C 1 451 ? 12.671  -0.725  66.220  1.00 78.55  ? 451 TRP C CH2 1 
ATOM   11930 N N   . TRP C 1 452 ? 10.455  -6.842  69.970  1.00 58.57  ? 452 TRP C N   1 
ATOM   11931 C CA  . TRP C 1 452 ? 9.023   -6.763  70.231  1.00 64.08  ? 452 TRP C CA  1 
ATOM   11932 C C   . TRP C 1 452 ? 8.667   -6.982  71.692  1.00 73.23  ? 452 TRP C C   1 
ATOM   11933 O O   . TRP C 1 452 ? 7.588   -6.556  72.120  1.00 82.06  ? 452 TRP C O   1 
ATOM   11934 C CB  . TRP C 1 452 ? 8.277   -7.784  69.375  1.00 68.30  ? 452 TRP C CB  1 
ATOM   11935 C CG  . TRP C 1 452 ? 8.618   -7.697  67.929  1.00 61.89  ? 452 TRP C CG  1 
ATOM   11936 C CD1 . TRP C 1 452 ? 9.307   -8.611  67.194  1.00 56.08  ? 452 TRP C CD1 1 
ATOM   11937 C CD2 . TRP C 1 452 ? 8.281   -6.633  67.037  1.00 60.12  ? 452 TRP C CD2 1 
ATOM   11938 N NE1 . TRP C 1 452 ? 9.428   -8.181  65.896  1.00 57.00  ? 452 TRP C NE1 1 
ATOM   11939 C CE2 . TRP C 1 452 ? 8.805   -6.968  65.774  1.00 62.04  ? 452 TRP C CE2 1 
ATOM   11940 C CE3 . TRP C 1 452 ? 7.589   -5.427  67.184  1.00 66.59  ? 452 TRP C CE3 1 
ATOM   11941 C CZ2 . TRP C 1 452 ? 8.656   -6.144  64.664  1.00 69.45  ? 452 TRP C CZ2 1 
ATOM   11942 C CZ3 . TRP C 1 452 ? 7.442   -4.607  66.081  1.00 75.07  ? 452 TRP C CZ3 1 
ATOM   11943 C CH2 . TRP C 1 452 ? 7.972   -4.970  64.835  1.00 72.40  ? 452 TRP C CH2 1 
ATOM   11944 N N   . GLN C 1 453 ? 9.540   -7.634  72.457  1.00 71.54  ? 453 GLN C N   1 
ATOM   11945 C CA  . GLN C 1 453 ? 9.255   -7.906  73.859  1.00 69.00  ? 453 GLN C CA  1 
ATOM   11946 C C   . GLN C 1 453 ? 9.113   -6.613  74.646  1.00 68.70  ? 453 GLN C C   1 
ATOM   11947 O O   . GLN C 1 453 ? 9.959   -5.719  74.557  1.00 75.48  ? 453 GLN C O   1 
ATOM   11948 C CB  . GLN C 1 453 ? 10.361  -8.763  74.466  1.00 67.91  ? 453 GLN C CB  1 
ATOM   11949 C CG  . GLN C 1 453 ? 10.015  -10.227 74.513  1.00 72.19  ? 453 GLN C CG  1 
ATOM   11950 C CD  . GLN C 1 453 ? 8.616   -10.480 75.045  1.00 73.49  ? 453 GLN C CD  1 
ATOM   11951 O OE1 . GLN C 1 453 ? 7.673   -10.693 74.279  1.00 58.65  ? 453 GLN C OE1 1 
ATOM   11952 N NE2 . GLN C 1 453 ? 8.478   -10.469 76.365  1.00 78.26  ? 453 GLN C NE2 1 
ATOM   11953 N N   . GLY C 1 454 ? 8.041   -6.520  75.425  1.00 70.84  ? 454 GLY C N   1 
ATOM   11954 C CA  . GLY C 1 454 ? 7.815   -5.359  76.253  1.00 81.44  ? 454 GLY C CA  1 
ATOM   11955 C C   . GLY C 1 454 ? 7.416   -4.108  75.508  1.00 95.45  ? 454 GLY C C   1 
ATOM   11956 O O   . GLY C 1 454 ? 7.196   -3.073  76.149  1.00 101.65 ? 454 GLY C O   1 
ATOM   11957 N N   . GLU C 1 455 ? 7.320   -4.161  74.182  1.00 98.27  ? 455 GLU C N   1 
ATOM   11958 C CA  . GLU C 1 455 ? 6.860   -3.011  73.422  1.00 110.95 ? 455 GLU C CA  1 
ATOM   11959 C C   . GLU C 1 455 ? 5.380   -2.759  73.686  1.00 114.76 ? 455 GLU C C   1 
ATOM   11960 O O   . GLU C 1 455 ? 4.657   -3.621  74.194  1.00 113.22 ? 455 GLU C O   1 
ATOM   11961 C CB  . GLU C 1 455 ? 7.096   -3.219  71.924  1.00 104.25 ? 455 GLU C CB  1 
ATOM   11962 C CG  . GLU C 1 455 ? 7.652   -1.990  71.230  1.00 109.65 ? 455 GLU C CG  1 
ATOM   11963 C CD  . GLU C 1 455 ? 8.795   -1.380  72.010  1.00 106.86 ? 455 GLU C CD  1 
ATOM   11964 O OE1 . GLU C 1 455 ? 9.888   -1.984  72.016  1.00 100.41 ? 455 GLU C OE1 1 
ATOM   11965 O OE2 . GLU C 1 455 ? 8.604   -0.296  72.606  1.00 109.73 ? 455 GLU C OE2 1 
ATOM   11966 N N   . GLU C 1 456 ? 4.932   -1.550  73.332  1.00 113.48 ? 456 GLU C N   1 
ATOM   11967 C CA  . GLU C 1 456 ? 3.512   -1.213  73.336  1.00 120.15 ? 456 GLU C CA  1 
ATOM   11968 C C   . GLU C 1 456 ? 2.724   -2.263  72.560  1.00 122.58 ? 456 GLU C C   1 
ATOM   11969 O O   . GLU C 1 456 ? 3.329   -3.091  71.868  1.00 122.51 ? 456 GLU C O   1 
ATOM   11970 C CB  . GLU C 1 456 ? 3.288   0.175   72.724  1.00 125.30 ? 456 GLU C CB  1 
ATOM   11971 C CG  . GLU C 1 456 ? 2.965   0.145   71.224  1.00 121.59 ? 456 GLU C CG  1 
ATOM   11972 C CD  . GLU C 1 456 ? 3.054   1.511   70.562  1.00 122.22 ? 456 GLU C CD  1 
ATOM   11973 O OE1 . GLU C 1 456 ? 4.176   2.049   70.452  1.00 126.59 ? 456 GLU C OE1 1 
ATOM   11974 O OE2 . GLU C 1 456 ? 2.005   2.042   70.135  1.00 120.54 ? 456 GLU C OE2 1 
ATOM   11975 N N   . LYS C 1 457 ? 1.386   -2.245  72.669  1.00 125.96 ? 457 LYS C N   1 
ATOM   11976 C CA  . LYS C 1 457 ? 0.518   -3.104  71.858  1.00 126.51 ? 457 LYS C CA  1 
ATOM   11977 C C   . LYS C 1 457 ? 1.109   -3.183  70.453  1.00 123.42 ? 457 LYS C C   1 
ATOM   11978 O O   . LYS C 1 457 ? 1.161   -2.179  69.735  1.00 123.36 ? 457 LYS C O   1 
ATOM   11979 C CB  . LYS C 1 457 ? -0.927  -2.569  71.834  1.00 125.08 ? 457 LYS C CB  1 
ATOM   11980 C CG  . LYS C 1 457 ? -1.810  -3.005  70.634  1.00 117.62 ? 457 LYS C CG  1 
ATOM   11981 C CD  . LYS C 1 457 ? -1.681  -4.488  70.223  1.00 119.89 ? 457 LYS C CD  1 
ATOM   11982 C CE  . LYS C 1 457 ? -2.498  -4.803  68.972  1.00 113.04 ? 457 LYS C CE  1 
ATOM   11983 N NZ  . LYS C 1 457 ? -2.078  -6.109  68.359  1.00 106.86 ? 457 LYS C NZ  1 
ATOM   11984 N N   . ALA C 1 458 ? 1.602   -4.362  70.077  1.00 119.37 ? 458 ALA C N   1 
ATOM   11985 C CA  . ALA C 1 458 ? 2.302   -4.552  68.818  1.00 115.24 ? 458 ALA C CA  1 
ATOM   11986 C C   . ALA C 1 458 ? 1.743   -5.767  68.093  1.00 111.37 ? 458 ALA C C   1 
ATOM   11987 O O   . ALA C 1 458 ? 1.191   -6.679  68.722  1.00 106.92 ? 458 ALA C O   1 
ATOM   11988 C CB  . ALA C 1 458 ? 3.813   -4.715  69.039  1.00 110.74 ? 458 ALA C CB  1 
ATOM   11989 N N   . PRO C 1 459 ? 1.863   -5.796  66.765  1.00 107.51 ? 459 PRO C N   1 
ATOM   11990 C CA  . PRO C 1 459 ? 1.165   -6.810  65.966  1.00 93.85  ? 459 PRO C CA  1 
ATOM   11991 C C   . PRO C 1 459 ? 1.845   -8.169  66.048  1.00 88.95  ? 459 PRO C C   1 
ATOM   11992 O O   . PRO C 1 459 ? 3.064   -8.280  65.897  1.00 95.13  ? 459 PRO C O   1 
ATOM   11993 C CB  . PRO C 1 459 ? 1.230   -6.236  64.544  1.00 88.23  ? 459 PRO C CB  1 
ATOM   11994 C CG  . PRO C 1 459 ? 1.461   -4.755  64.761  1.00 91.33  ? 459 PRO C CG  1 
ATOM   11995 C CD  . PRO C 1 459 ? 2.413   -4.742  65.903  1.00 101.40 ? 459 PRO C CD  1 
ATOM   11996 N N   . PHE C 1 460 ? 1.032   -9.203  66.281  1.00 77.89  ? 460 PHE C N   1 
ATOM   11997 C CA  . PHE C 1 460 ? 1.474   -10.599 66.309  1.00 68.50  ? 460 PHE C CA  1 
ATOM   11998 C C   . PHE C 1 460 ? 2.731   -10.800 67.149  1.00 74.39  ? 460 PHE C C   1 
ATOM   11999 O O   . PHE C 1 460 ? 3.573   -11.640 66.828  1.00 79.43  ? 460 PHE C O   1 
ATOM   12000 C CB  . PHE C 1 460 ? 1.712   -11.142 64.901  1.00 70.87  ? 460 PHE C CB  1 
ATOM   12001 C CG  . PHE C 1 460 ? 0.772   -10.603 63.862  1.00 83.88  ? 460 PHE C CG  1 
ATOM   12002 C CD1 . PHE C 1 460 ? -0.597  -10.787 63.974  1.00 78.38  ? 460 PHE C CD1 1 
ATOM   12003 C CD2 . PHE C 1 460 ? 1.266   -9.940  62.751  1.00 83.76  ? 460 PHE C CD2 1 
ATOM   12004 C CE1 . PHE C 1 460 ? -1.458  -10.300 63.007  1.00 74.98  ? 460 PHE C CE1 1 
ATOM   12005 C CE2 . PHE C 1 460 ? 0.414   -9.454  61.781  1.00 84.92  ? 460 PHE C CE2 1 
ATOM   12006 C CZ  . PHE C 1 460 ? -0.951  -9.633  61.907  1.00 83.64  ? 460 PHE C CZ  1 
ATOM   12007 N N   . VAL C 1 461 ? 2.879   -10.031 68.229  1.00 75.90  ? 461 VAL C N   1 
ATOM   12008 C CA  . VAL C 1 461 ? 4.005   -10.265 69.129  1.00 72.69  ? 461 VAL C CA  1 
ATOM   12009 C C   . VAL C 1 461 ? 3.940   -11.675 69.693  1.00 71.37  ? 461 VAL C C   1 
ATOM   12010 O O   . VAL C 1 461 ? 4.974   -12.293 69.985  1.00 74.64  ? 461 VAL C O   1 
ATOM   12011 C CB  . VAL C 1 461 ? 4.028   -9.195  70.237  1.00 77.86  ? 461 VAL C CB  1 
ATOM   12012 C CG1 . VAL C 1 461 ? 4.790   -9.681  71.460  1.00 77.68  ? 461 VAL C CG1 1 
ATOM   12013 C CG2 . VAL C 1 461 ? 4.661   -7.945  69.708  1.00 79.35  ? 461 VAL C CG2 1 
ATOM   12014 N N   . GLU C 1 462 ? 2.730   -12.217 69.822  1.00 61.90  ? 462 GLU C N   1 
ATOM   12015 C CA  . GLU C 1 462 ? 2.574   -13.596 70.261  1.00 66.78  ? 462 GLU C CA  1 
ATOM   12016 C C   . GLU C 1 462 ? 3.222   -14.556 69.275  1.00 69.33  ? 462 GLU C C   1 
ATOM   12017 O O   . GLU C 1 462 ? 3.862   -15.536 69.678  1.00 70.37  ? 462 GLU C O   1 
ATOM   12018 C CB  . GLU C 1 462 ? 1.091   -13.923 70.435  1.00 77.50  ? 462 GLU C CB  1 
ATOM   12019 C CG  . GLU C 1 462 ? 0.219   -12.742 70.877  1.00 86.40  ? 462 GLU C CG  1 
ATOM   12020 C CD  . GLU C 1 462 ? -0.153  -11.796 69.739  1.00 88.04  ? 462 GLU C CD  1 
ATOM   12021 O OE1 . GLU C 1 462 ? -0.075  -10.565 69.949  1.00 88.52  ? 462 GLU C OE1 1 
ATOM   12022 O OE2 . GLU C 1 462 ? -0.520  -12.279 68.642  1.00 79.72  ? 462 GLU C OE2 1 
ATOM   12023 N N   . VAL C 1 463 ? 3.089   -14.277 67.975  1.00 63.93  ? 463 VAL C N   1 
ATOM   12024 C CA  . VAL C 1 463 ? 3.671   -15.151 66.960  1.00 58.88  ? 463 VAL C CA  1 
ATOM   12025 C C   . VAL C 1 463 ? 5.192   -15.145 67.056  1.00 59.85  ? 463 VAL C C   1 
ATOM   12026 O O   . VAL C 1 463 ? 5.835   -16.199 66.975  1.00 61.02  ? 463 VAL C O   1 
ATOM   12027 C CB  . VAL C 1 463 ? 3.182   -14.736 65.561  1.00 54.90  ? 463 VAL C CB  1 
ATOM   12028 C CG1 . VAL C 1 463 ? 3.711   -15.690 64.506  1.00 53.63  ? 463 VAL C CG1 1 
ATOM   12029 C CG2 . VAL C 1 463 ? 1.668   -14.689 65.536  1.00 59.76  ? 463 VAL C CG2 1 
ATOM   12030 N N   . PHE C 1 464 ? 5.794   -13.966 67.238  1.00 58.85  ? 464 PHE C N   1 
ATOM   12031 C CA  . PHE C 1 464 ? 7.234   -13.911 67.467  1.00 62.48  ? 464 PHE C CA  1 
ATOM   12032 C C   . PHE C 1 464 ? 7.618   -14.622 68.757  1.00 62.81  ? 464 PHE C C   1 
ATOM   12033 O O   . PHE C 1 464 ? 8.701   -15.215 68.845  1.00 61.55  ? 464 PHE C O   1 
ATOM   12034 C CB  . PHE C 1 464 ? 7.719   -12.460 67.506  1.00 54.99  ? 464 PHE C CB  1 
ATOM   12035 C CG  . PHE C 1 464 ? 7.674   -11.771 66.177  1.00 58.66  ? 464 PHE C CG  1 
ATOM   12036 C CD1 . PHE C 1 464 ? 6.505   -11.179 65.731  1.00 67.24  ? 464 PHE C CD1 1 
ATOM   12037 C CD2 . PHE C 1 464 ? 8.799   -11.710 65.370  1.00 57.72  ? 464 PHE C CD2 1 
ATOM   12038 C CE1 . PHE C 1 464 ? 6.454   -10.542 64.504  1.00 63.11  ? 464 PHE C CE1 1 
ATOM   12039 C CE2 . PHE C 1 464 ? 8.755   -11.076 64.143  1.00 54.76  ? 464 PHE C CE2 1 
ATOM   12040 C CZ  . PHE C 1 464 ? 7.581   -10.491 63.709  1.00 59.26  ? 464 PHE C CZ  1 
ATOM   12041 N N   . ASP C 1 465 ? 6.746   -14.582 69.765  1.00 58.82  ? 465 ASP C N   1 
ATOM   12042 C CA  . ASP C 1 465 ? 7.083   -15.221 71.030  1.00 68.52  ? 465 ASP C CA  1 
ATOM   12043 C C   . ASP C 1 465 ? 7.041   -16.739 70.903  1.00 60.95  ? 465 ASP C C   1 
ATOM   12044 O O   . ASP C 1 465 ? 7.878   -17.440 71.484  1.00 54.74  ? 465 ASP C O   1 
ATOM   12045 C CB  . ASP C 1 465 ? 6.143   -14.733 72.129  1.00 67.99  ? 465 ASP C CB  1 
ATOM   12046 C CG  . ASP C 1 465 ? 6.397   -15.417 73.444  1.00 64.78  ? 465 ASP C CG  1 
ATOM   12047 O OD1 . ASP C 1 465 ? 7.400   -15.077 74.106  1.00 65.97  ? 465 ASP C OD1 1 
ATOM   12048 O OD2 . ASP C 1 465 ? 5.600   -16.305 73.806  1.00 66.40  ? 465 ASP C OD2 1 
ATOM   12049 N N   . LYS C 1 466 ? 6.070   -17.259 70.147  1.00 56.95  ? 466 LYS C N   1 
ATOM   12050 C CA  . LYS C 1 466 ? 6.019   -18.690 69.861  1.00 58.43  ? 466 LYS C CA  1 
ATOM   12051 C C   . LYS C 1 466 ? 7.326   -19.158 69.229  1.00 61.63  ? 466 LYS C C   1 
ATOM   12052 O O   . LYS C 1 466 ? 7.941   -20.134 69.681  1.00 61.68  ? 466 LYS C O   1 
ATOM   12053 C CB  . LYS C 1 466 ? 4.824   -18.988 68.943  1.00 52.20  ? 466 LYS C CB  1 
ATOM   12054 C CG  . LYS C 1 466 ? 4.287   -20.417 69.015  1.00 53.98  ? 466 LYS C CG  1 
ATOM   12055 C CD  . LYS C 1 466 ? 5.197   -21.435 68.330  1.00 68.18  ? 466 LYS C CD  1 
ATOM   12056 C CE  . LYS C 1 466 ? 5.036   -22.851 68.911  1.00 73.80  ? 466 LYS C CE  1 
ATOM   12057 N NZ  . LYS C 1 466 ? 5.516   -22.981 70.331  1.00 71.39  ? 466 LYS C NZ  1 
ATOM   12058 N N   . LEU C 1 467 ? 7.775   -18.452 68.188  1.00 61.46  ? 467 LEU C N   1 
ATOM   12059 C CA  . LEU C 1 467 ? 8.987   -18.845 67.476  1.00 57.48  ? 467 LEU C CA  1 
ATOM   12060 C C   . LEU C 1 467 ? 10.204  -18.800 68.391  1.00 58.05  ? 467 LEU C C   1 
ATOM   12061 O O   . LEU C 1 467 ? 10.976  -19.764 68.459  1.00 59.65  ? 467 LEU C O   1 
ATOM   12062 C CB  . LEU C 1 467 ? 9.199   -17.936 66.267  1.00 56.45  ? 467 LEU C CB  1 
ATOM   12063 C CG  . LEU C 1 467 ? 8.224   -18.079 65.101  1.00 55.19  ? 467 LEU C CG  1 
ATOM   12064 C CD1 . LEU C 1 467 ? 8.085   -16.742 64.407  1.00 50.26  ? 467 LEU C CD1 1 
ATOM   12065 C CD2 . LEU C 1 467 ? 8.694   -19.139 64.125  1.00 54.31  ? 467 LEU C CD2 1 
ATOM   12066 N N   . PHE C 1 468 ? 10.397  -17.683 69.099  1.00 51.82  ? 468 PHE C N   1 
ATOM   12067 C CA  . PHE C 1 468 ? 11.556  -17.563 69.975  1.00 48.86  ? 468 PHE C CA  1 
ATOM   12068 C C   . PHE C 1 468 ? 11.619  -18.733 70.948  1.00 59.72  ? 468 PHE C C   1 
ATOM   12069 O O   . PHE C 1 468 ? 12.676  -19.346 71.136  1.00 63.40  ? 468 PHE C O   1 
ATOM   12070 C CB  . PHE C 1 468 ? 11.522  -16.233 70.730  1.00 49.51  ? 468 PHE C CB  1 
ATOM   12071 C CG  . PHE C 1 468 ? 12.628  -16.084 71.742  1.00 54.15  ? 468 PHE C CG  1 
ATOM   12072 C CD1 . PHE C 1 468 ? 13.923  -15.803 71.336  1.00 55.97  ? 468 PHE C CD1 1 
ATOM   12073 C CD2 . PHE C 1 468 ? 12.373  -16.237 73.097  1.00 50.17  ? 468 PHE C CD2 1 
ATOM   12074 C CE1 . PHE C 1 468 ? 14.947  -15.668 72.265  1.00 54.97  ? 468 PHE C CE1 1 
ATOM   12075 C CE2 . PHE C 1 468 ? 13.391  -16.102 74.031  1.00 58.85  ? 468 PHE C CE2 1 
ATOM   12076 C CZ  . PHE C 1 468 ? 14.681  -15.816 73.614  1.00 53.84  ? 468 PHE C CZ  1 
ATOM   12077 N N   . ARG C 1 469 ? 10.478  -19.080 71.552  1.00 59.57  ? 469 ARG C N   1 
ATOM   12078 C CA  . ARG C 1 469 ? 10.453  -20.186 72.503  1.00 55.33  ? 469 ARG C CA  1 
ATOM   12079 C C   . ARG C 1 469 ? 10.615  -21.526 71.804  1.00 60.00  ? 469 ARG C C   1 
ATOM   12080 O O   . ARG C 1 469 ? 11.242  -22.442 72.352  1.00 60.04  ? 469 ARG C O   1 
ATOM   12081 C CB  . ARG C 1 469 ? 9.160   -20.150 73.312  1.00 43.47  ? 469 ARG C CB  1 
ATOM   12082 C CG  . ARG C 1 469 ? 9.073   -18.926 74.199  1.00 52.86  ? 469 ARG C CG  1 
ATOM   12083 C CD  . ARG C 1 469 ? 7.721   -18.775 74.872  1.00 61.45  ? 469 ARG C CD  1 
ATOM   12084 N NE  . ARG C 1 469 ? 7.602   -17.485 75.544  1.00 64.84  ? 469 ARG C NE  1 
ATOM   12085 C CZ  . ARG C 1 469 ? 8.082   -17.212 76.750  1.00 64.65  ? 469 ARG C CZ  1 
ATOM   12086 N NH1 . ARG C 1 469 ? 8.683   -18.135 77.482  1.00 65.37  ? 469 ARG C NH1 1 
ATOM   12087 N NH2 . ARG C 1 469 ? 7.947   -15.981 77.237  1.00 62.03  ? 469 ARG C NH2 1 
ATOM   12088 N N   . SER C 1 470 ? 10.084  -21.643 70.587  1.00 54.27  ? 470 SER C N   1 
ATOM   12089 C CA  . SER C 1 470 ? 10.229  -22.878 69.830  1.00 53.97  ? 470 SER C CA  1 
ATOM   12090 C C   . SER C 1 470 ? 11.672  -23.106 69.397  1.00 54.63  ? 470 SER C C   1 
ATOM   12091 O O   . SER C 1 470 ? 12.157  -24.244 69.420  1.00 55.03  ? 470 SER C O   1 
ATOM   12092 C CB  . SER C 1 470 ? 9.311   -22.846 68.619  1.00 57.95  ? 470 SER C CB  1 
ATOM   12093 O OG  . SER C 1 470 ? 8.895   -24.158 68.309  1.00 74.68  ? 470 SER C OG  1 
ATOM   12094 N N   . PHE C 1 471 ? 12.366  -22.042 68.976  1.00 53.92  ? 471 PHE C N   1 
ATOM   12095 C CA  . PHE C 1 471 ? 13.774  -22.174 68.608  1.00 51.58  ? 471 PHE C CA  1 
ATOM   12096 C C   . PHE C 1 471 ? 14.628  -22.454 69.831  1.00 55.93  ? 471 PHE C C   1 
ATOM   12097 O O   . PHE C 1 471 ? 15.596  -23.218 69.758  1.00 60.78  ? 471 PHE C O   1 
ATOM   12098 C CB  . PHE C 1 471 ? 14.275  -20.910 67.911  1.00 47.21  ? 471 PHE C CB  1 
ATOM   12099 C CG  . PHE C 1 471 ? 13.601  -20.625 66.610  1.00 52.56  ? 471 PHE C CG  1 
ATOM   12100 C CD1 . PHE C 1 471 ? 13.425  -21.625 65.674  1.00 60.63  ? 471 PHE C CD1 1 
ATOM   12101 C CD2 . PHE C 1 471 ? 13.136  -19.353 66.319  1.00 59.86  ? 471 PHE C CD2 1 
ATOM   12102 C CE1 . PHE C 1 471 ? 12.800  -21.366 64.470  1.00 61.33  ? 471 PHE C CE1 1 
ATOM   12103 C CE2 . PHE C 1 471 ? 12.505  -19.088 65.117  1.00 59.56  ? 471 PHE C CE2 1 
ATOM   12104 C CZ  . PHE C 1 471 ? 12.336  -20.099 64.191  1.00 61.36  ? 471 PHE C CZ  1 
ATOM   12105 N N   . VAL C 1 472 ? 14.298  -21.825 70.959  1.00 52.95  ? 472 VAL C N   1 
ATOM   12106 C CA  . VAL C 1 472 ? 15.035  -22.099 72.185  1.00 60.81  ? 472 VAL C CA  1 
ATOM   12107 C C   . VAL C 1 472 ? 14.898  -23.567 72.560  1.00 62.42  ? 472 VAL C C   1 
ATOM   12108 O O   . VAL C 1 472 ? 15.867  -24.207 72.981  1.00 65.95  ? 472 VAL C O   1 
ATOM   12109 C CB  . VAL C 1 472 ? 14.559  -21.175 73.320  1.00 56.79  ? 472 VAL C CB  1 
ATOM   12110 C CG1 . VAL C 1 472 ? 14.627  -21.899 74.644  1.00 57.55  ? 472 VAL C CG1 1 
ATOM   12111 C CG2 . VAL C 1 472 ? 15.415  -19.937 73.376  1.00 54.04  ? 472 VAL C CG2 1 
ATOM   12112 N N   . ARG C 1 473 ? 13.698  -24.129 72.396  1.00 57.37  ? 473 ARG C N   1 
ATOM   12113 C CA  . ARG C 1 473 ? 13.493  -25.535 72.730  1.00 64.00  ? 473 ARG C CA  1 
ATOM   12114 C C   . ARG C 1 473 ? 14.241  -26.441 71.762  1.00 61.63  ? 473 ARG C C   1 
ATOM   12115 O O   . ARG C 1 473 ? 14.947  -27.368 72.180  1.00 62.74  ? 473 ARG C O   1 
ATOM   12116 C CB  . ARG C 1 473 ? 11.999  -25.860 72.732  1.00 66.12  ? 473 ARG C CB  1 
ATOM   12117 C CG  . ARG C 1 473 ? 11.646  -27.271 73.188  1.00 67.25  ? 473 ARG C CG  1 
ATOM   12118 C CD  . ARG C 1 473 ? 10.151  -27.533 73.043  1.00 68.89  ? 473 ARG C CD  1 
ATOM   12119 N NE  . ARG C 1 473 ? 9.398   -26.336 72.681  1.00 85.11  ? 473 ARG C NE  1 
ATOM   12120 C CZ  . ARG C 1 473 ? 8.858   -25.490 73.551  1.00 89.39  ? 473 ARG C CZ  1 
ATOM   12121 N NH1 . ARG C 1 473 ? 8.969   -25.679 74.857  1.00 81.95  ? 473 ARG C NH1 1 
ATOM   12122 N NH2 . ARG C 1 473 ? 8.187   -24.430 73.097  1.00 83.49  ? 473 ARG C NH2 1 
ATOM   12123 N N   . ARG C 1 474 ? 14.096  -26.187 70.457  1.00 64.00  ? 474 ARG C N   1 
ATOM   12124 C CA  . ARG C 1 474 ? 14.776  -27.005 69.457  1.00 69.43  ? 474 ARG C CA  1 
ATOM   12125 C C   . ARG C 1 474 ? 16.286  -26.966 69.637  1.00 61.12  ? 474 ARG C C   1 
ATOM   12126 O O   . ARG C 1 474 ? 16.965  -27.979 69.430  1.00 63.77  ? 474 ARG C O   1 
ATOM   12127 C CB  . ARG C 1 474 ? 14.398  -26.546 68.049  1.00 64.55  ? 474 ARG C CB  1 
ATOM   12128 C CG  . ARG C 1 474 ? 15.179  -27.262 66.974  1.00 67.00  ? 474 ARG C CG  1 
ATOM   12129 C CD  . ARG C 1 474 ? 14.430  -28.450 66.399  1.00 77.96  ? 474 ARG C CD  1 
ATOM   12130 N NE  . ARG C 1 474 ? 15.159  -29.071 65.299  1.00 79.26  ? 474 ARG C NE  1 
ATOM   12131 C CZ  . ARG C 1 474 ? 14.669  -30.034 64.532  1.00 91.62  ? 474 ARG C CZ  1 
ATOM   12132 N NH1 . ARG C 1 474 ? 13.432  -30.485 64.694  1.00 81.13  ? 474 ARG C NH1 1 
ATOM   12133 N NH2 . ARG C 1 474 ? 15.436  -30.551 63.576  1.00 93.70  ? 474 ARG C NH2 1 
ATOM   12134 N N   . ALA C 1 475 ? 16.823  -25.816 70.049  1.00 61.89  ? 475 ALA C N   1 
ATOM   12135 C CA  . ALA C 1 475 ? 18.255  -25.686 70.283  1.00 61.43  ? 475 ALA C CA  1 
ATOM   12136 C C   . ALA C 1 475 ? 18.746  -26.569 71.425  1.00 56.92  ? 475 ALA C C   1 
ATOM   12137 O O   . ALA C 1 475 ? 19.939  -26.870 71.477  1.00 61.01  ? 475 ALA C O   1 
ATOM   12138 C CB  . ALA C 1 475 ? 18.605  -24.225 70.558  1.00 60.12  ? 475 ALA C CB  1 
ATOM   12139 N N   . GLN C 1 476 ? 17.862  -26.996 72.331  1.00 59.86  ? 476 GLN C N   1 
ATOM   12140 C CA  . GLN C 1 476 ? 18.219  -27.893 73.427  1.00 62.56  ? 476 GLN C CA  1 
ATOM   12141 C C   . GLN C 1 476 ? 17.965  -29.357 73.078  1.00 65.03  ? 476 GLN C C   1 
ATOM   12142 O O   . GLN C 1 476 ? 17.610  -30.152 73.953  1.00 69.73  ? 476 GLN C O   1 
ATOM   12143 C CB  . GLN C 1 476 ? 17.455  -27.506 74.692  1.00 62.47  ? 476 GLN C CB  1 
ATOM   12144 C CG  . GLN C 1 476 ? 17.380  -26.012 74.910  1.00 63.41  ? 476 GLN C CG  1 
ATOM   12145 C CD  . GLN C 1 476 ? 17.178  -25.622 76.354  1.00 67.36  ? 476 GLN C CD  1 
ATOM   12146 O OE1 . GLN C 1 476 ? 16.309  -24.807 76.665  1.00 75.78  ? 476 GLN C OE1 1 
ATOM   12147 N NE2 . GLN C 1 476 ? 17.974  -26.196 77.247  1.00 72.09  ? 476 GLN C NE2 1 
ATOM   12148 N N   . GLU C 1 477 ? 18.138  -29.724 71.809  1.00 69.59  ? 477 GLU C N   1 
ATOM   12149 C CA  . GLU C 1 477 ? 17.982  -31.094 71.341  1.00 66.51  ? 477 GLU C CA  1 
ATOM   12150 C C   . GLU C 1 477 ? 19.219  -31.521 70.568  1.00 71.86  ? 477 GLU C C   1 
ATOM   12151 O O   . GLU C 1 477 ? 19.917  -30.691 69.978  1.00 75.67  ? 477 GLU C O   1 
ATOM   12152 C CB  . GLU C 1 477 ? 16.765  -31.251 70.426  1.00 60.83  ? 477 GLU C CB  1 
ATOM   12153 C CG  . GLU C 1 477 ? 15.437  -30.971 71.095  1.00 73.81  ? 477 GLU C CG  1 
ATOM   12154 C CD  . GLU C 1 477 ? 14.249  -31.288 70.201  1.00 75.84  ? 477 GLU C CD  1 
ATOM   12155 O OE1 . GLU C 1 477 ? 14.128  -30.653 69.131  1.00 78.70  ? 477 GLU C OE1 1 
ATOM   12156 O OE2 . GLU C 1 477 ? 13.426  -32.150 70.577  1.00 73.26  ? 477 GLU C OE2 1 
ATOM   12157 N N   . LEU C 1 478 ? 19.478  -32.826 70.561  1.00 74.13  ? 478 LEU C N   1 
ATOM   12158 C CA  . LEU C 1 478 ? 20.487  -33.365 69.660  1.00 73.04  ? 478 LEU C CA  1 
ATOM   12159 C C   . LEU C 1 478 ? 19.973  -33.343 68.226  1.00 76.78  ? 478 LEU C C   1 
ATOM   12160 O O   . LEU C 1 478 ? 18.779  -33.521 67.966  1.00 86.30  ? 478 LEU C O   1 
ATOM   12161 C CB  . LEU C 1 478 ? 20.867  -34.795 70.042  1.00 72.83  ? 478 LEU C CB  1 
ATOM   12162 C CG  . LEU C 1 478 ? 21.162  -35.160 71.493  1.00 74.15  ? 478 LEU C CG  1 
ATOM   12163 C CD1 . LEU C 1 478 ? 21.112  -36.668 71.637  1.00 69.79  ? 478 LEU C CD1 1 
ATOM   12164 C CD2 . LEU C 1 478 ? 22.525  -34.629 71.935  1.00 77.00  ? 478 LEU C CD2 1 
ATOM   12165 N N   . GLU C 1 479 ? 20.884  -33.123 67.287  1.00 70.26  ? 479 GLU C N   1 
ATOM   12166 C CA  . GLU C 1 479 ? 20.487  -32.993 65.894  1.00 86.45  ? 479 GLU C CA  1 
ATOM   12167 C C   . GLU C 1 479 ? 20.673  -34.264 65.087  1.00 86.42  ? 479 GLU C C   1 
ATOM   12168 O O   . GLU C 1 479 ? 20.372  -34.264 63.891  1.00 92.03  ? 479 GLU C O   1 
ATOM   12169 C CB  . GLU C 1 479 ? 21.257  -31.857 65.217  1.00 94.14  ? 479 GLU C CB  1 
ATOM   12170 C CG  . GLU C 1 479 ? 20.444  -30.575 65.073  1.00 104.79 ? 479 GLU C CG  1 
ATOM   12171 C CD  . GLU C 1 479 ? 18.996  -30.798 64.630  1.00 107.17 ? 479 GLU C CD  1 
ATOM   12172 O OE1 . GLU C 1 479 ? 18.768  -31.103 63.439  1.00 105.33 ? 479 GLU C OE1 1 
ATOM   12173 O OE2 . GLU C 1 479 ? 18.078  -30.644 65.471  1.00 84.94  ? 479 GLU C OE2 1 
ATOM   12174 N N   . HIS C 1 480 ? 21.140  -35.348 65.693  1.00 80.50  ? 480 HIS C N   1 
ATOM   12175 C CA  . HIS C 1 480 ? 21.523  -36.516 64.915  1.00 83.16  ? 480 HIS C CA  1 
ATOM   12176 C C   . HIS C 1 480 ? 20.524  -37.665 64.990  1.00 84.32  ? 480 HIS C C   1 
ATOM   12177 O O   . HIS C 1 480 ? 20.790  -38.721 64.402  1.00 91.29  ? 480 HIS C O   1 
ATOM   12178 C CB  . HIS C 1 480 ? 22.903  -37.011 65.350  1.00 74.63  ? 480 HIS C CB  1 
ATOM   12179 C CG  . HIS C 1 480 ? 24.043  -36.341 64.647  1.00 69.90  ? 480 HIS C CG  1 
ATOM   12180 N ND1 . HIS C 1 480 ? 23.916  -35.727 63.420  1.00 75.76  ? 480 HIS C ND1 1 
ATOM   12181 C CD2 . HIS C 1 480 ? 25.348  -36.225 64.988  1.00 76.13  ? 480 HIS C CD2 1 
ATOM   12182 C CE1 . HIS C 1 480 ? 25.088  -35.242 63.047  1.00 83.59  ? 480 HIS C CE1 1 
ATOM   12183 N NE2 . HIS C 1 480 ? 25.975  -35.534 63.980  1.00 87.04  ? 480 HIS C NE2 1 
ATOM   12184 N N   . HIS C 1 481 ? 19.398  -37.489 65.695  1.00 66.08  ? 481 HIS C N   1 
ATOM   12185 C CA  . HIS C 1 481 ? 18.334  -38.490 65.808  1.00 66.32  ? 481 HIS C CA  1 
ATOM   12186 C C   . HIS C 1 481 ? 18.771  -39.681 66.657  1.00 63.12  ? 481 HIS C C   1 
ATOM   12187 O O   . HIS C 1 481 ? 19.768  -40.340 66.349  1.00 71.31  ? 481 HIS C O   1 
ATOM   12188 C CB  . HIS C 1 481 ? 17.882  -38.968 64.427  1.00 64.38  ? 481 HIS C CB  1 
ATOM   12189 C CG  . HIS C 1 481 ? 16.695  -38.234 63.890  1.00 75.06  ? 481 HIS C CG  1 
ATOM   12190 N ND1 . HIS C 1 481 ? 16.085  -38.574 62.702  1.00 69.08  ? 481 HIS C ND1 1 
ATOM   12191 C CD2 . HIS C 1 481 ? 16.009  -37.172 64.376  1.00 76.02  ? 481 HIS C CD2 1 
ATOM   12192 C CE1 . HIS C 1 481 ? 15.072  -37.757 62.481  1.00 73.19  ? 481 HIS C CE1 1 
ATOM   12193 N NE2 . HIS C 1 481 ? 15.003  -36.897 63.482  1.00 67.21  ? 481 HIS C NE2 1 
ATOM   12194 N N   . HIS C 1 482 ? 18.031  -39.988 67.716  1.00 60.53  ? 482 HIS C N   1 
ATOM   12195 C CA  . HIS C 1 482 ? 18.570  -40.885 68.728  1.00 61.48  ? 482 HIS C CA  1 
ATOM   12196 C C   . HIS C 1 482 ? 17.447  -41.554 69.511  1.00 62.39  ? 482 HIS C C   1 
ATOM   12197 O O   . HIS C 1 482 ? 16.288  -41.140 69.464  1.00 64.48  ? 482 HIS C O   1 
ATOM   12198 C CB  . HIS C 1 482 ? 19.471  -40.111 69.677  1.00 60.58  ? 482 HIS C CB  1 
ATOM   12199 C CG  . HIS C 1 482 ? 18.764  -38.984 70.359  1.00 66.18  ? 482 HIS C CG  1 
ATOM   12200 N ND1 . HIS C 1 482 ? 18.348  -39.049 71.671  1.00 64.74  ? 482 HIS C ND1 1 
ATOM   12201 C CD2 . HIS C 1 482 ? 18.364  -37.775 69.896  1.00 67.22  ? 482 HIS C CD2 1 
ATOM   12202 C CE1 . HIS C 1 482 ? 17.740  -37.922 71.994  1.00 70.39  ? 482 HIS C CE1 1 
ATOM   12203 N NE2 . HIS C 1 482 ? 17.737  -37.132 70.935  1.00 72.69  ? 482 HIS C NE2 1 
ATOM   12204 N N   . HIS C 1 483 ? 17.823  -42.593 70.254  1.00 65.23  ? 483 HIS C N   1 
ATOM   12205 C CA  . HIS C 1 483 ? 16.960  -43.228 71.238  1.00 62.36  ? 483 HIS C CA  1 
ATOM   12206 C C   . HIS C 1 483 ? 17.813  -43.622 72.439  1.00 68.75  ? 483 HIS C C   1 
ATOM   12207 O O   . HIS C 1 483 ? 19.045  -43.544 72.406  1.00 62.98  ? 483 HIS C O   1 
ATOM   12208 C CB  . HIS C 1 483 ? 16.235  -44.447 70.652  1.00 63.10  ? 483 HIS C CB  1 
ATOM   12209 C CG  . HIS C 1 483 ? 17.155  -45.526 70.168  1.00 72.89  ? 483 HIS C CG  1 
ATOM   12210 N ND1 . HIS C 1 483 ? 17.854  -46.354 71.021  1.00 73.89  ? 483 HIS C ND1 1 
ATOM   12211 C CD2 . HIS C 1 483 ? 17.498  -45.906 68.914  1.00 81.75  ? 483 HIS C CD2 1 
ATOM   12212 C CE1 . HIS C 1 483 ? 18.583  -47.199 70.314  1.00 74.88  ? 483 HIS C CE1 1 
ATOM   12213 N NE2 . HIS C 1 483 ? 18.386  -46.948 69.033  1.00 78.04  ? 483 HIS C NE2 1 
ATOM   12214 N N   . HIS C 1 484 ? 17.153  -44.048 73.509  1.00 70.84  ? 484 HIS C N   1 
ATOM   12215 C CA  . HIS C 1 484 ? 17.862  -44.460 74.716  1.00 65.81  ? 484 HIS C CA  1 
ATOM   12216 C C   . HIS C 1 484 ? 18.057  -45.978 74.770  1.00 65.44  ? 484 HIS C C   1 
ATOM   12217 O O   . HIS C 1 484 ? 19.148  -46.467 75.077  1.00 66.96  ? 484 HIS C O   1 
ATOM   12218 C CB  . HIS C 1 484 ? 17.108  -43.976 75.953  1.00 63.93  ? 484 HIS C CB  1 
ATOM   12219 C CG  . HIS C 1 484 ? 17.997  -43.524 77.067  1.00 62.02  ? 484 HIS C CG  1 
ATOM   12220 N ND1 . HIS C 1 484 ? 18.434  -44.376 78.060  1.00 65.06  ? 484 HIS C ND1 1 
ATOM   12221 C CD2 . HIS C 1 484 ? 18.523  -42.310 77.354  1.00 63.80  ? 484 HIS C CD2 1 
ATOM   12222 C CE1 . HIS C 1 484 ? 19.196  -43.708 78.907  1.00 66.95  ? 484 HIS C CE1 1 
ATOM   12223 N NE2 . HIS C 1 484 ? 19.266  -42.452 78.503  1.00 68.20  ? 484 HIS C NE2 1 
ATOM   12224 N N   . MET D 1 1   ? -25.917 13.917  57.898  1.00 106.37 ? 1   MET D N   1 
ATOM   12225 C CA  . MET D 1 1   ? -24.761 13.328  58.568  1.00 97.59  ? 1   MET D CA  1 
ATOM   12226 C C   . MET D 1 1   ? -24.541 13.960  59.937  1.00 102.96 ? 1   MET D C   1 
ATOM   12227 O O   . MET D 1 1   ? -25.373 14.727  60.428  1.00 108.95 ? 1   MET D O   1 
ATOM   12228 C CB  . MET D 1 1   ? -23.494 13.500  57.727  1.00 98.81  ? 1   MET D CB  1 
ATOM   12229 C CG  . MET D 1 1   ? -23.283 14.918  57.220  1.00 111.06 ? 1   MET D CG  1 
ATOM   12230 S SD  . MET D 1 1   ? -21.827 15.115  56.171  1.00 126.71 ? 1   MET D SD  1 
ATOM   12231 C CE  . MET D 1 1   ? -20.803 13.759  56.738  1.00 103.66 ? 1   MET D CE  1 
ATOM   12232 N N   . LYS D 1 2   ? -23.402 13.638  60.542  1.00 98.83  ? 2   LYS D N   1 
ATOM   12233 C CA  . LYS D 1 2   ? -22.983 14.215  61.813  1.00 88.32  ? 2   LYS D CA  1 
ATOM   12234 C C   . LYS D 1 2   ? -21.778 15.100  61.548  1.00 91.82  ? 2   LYS D C   1 
ATOM   12235 O O   . LYS D 1 2   ? -20.688 14.604  61.240  1.00 89.80  ? 2   LYS D O   1 
ATOM   12236 C CB  . LYS D 1 2   ? -22.643 13.133  62.829  1.00 87.66  ? 2   LYS D CB  1 
ATOM   12237 C CG  . LYS D 1 2   ? -23.549 13.089  64.026  1.00 89.96  ? 2   LYS D CG  1 
ATOM   12238 C CD  . LYS D 1 2   ? -22.744 12.700  65.245  1.00 91.09  ? 2   LYS D CD  1 
ATOM   12239 C CE  . LYS D 1 2   ? -23.653 12.369  66.401  1.00 99.55  ? 2   LYS D CE  1 
ATOM   12240 N NZ  . LYS D 1 2   ? -22.924 12.281  67.688  1.00 97.19  ? 2   LYS D NZ  1 
ATOM   12241 N N   . LYS D 1 3   ? -21.975 16.403  61.669  1.00 92.34  ? 3   LYS D N   1 
ATOM   12242 C CA  . LYS D 1 3   ? -20.922 17.378  61.462  1.00 91.14  ? 3   LYS D CA  1 
ATOM   12243 C C   . LYS D 1 3   ? -20.640 18.092  62.773  1.00 91.86  ? 3   LYS D C   1 
ATOM   12244 O O   . LYS D 1 3   ? -21.563 18.385  63.544  1.00 87.32  ? 3   LYS D O   1 
ATOM   12245 C CB  . LYS D 1 3   ? -21.319 18.386  60.380  1.00 81.93  ? 3   LYS D CB  1 
ATOM   12246 C CG  . LYS D 1 3   ? -20.822 18.029  58.987  1.00 88.36  ? 3   LYS D CG  1 
ATOM   12247 C CD  . LYS D 1 3   ? -21.759 18.563  57.909  1.00 93.06  ? 3   LYS D CD  1 
ATOM   12248 C CE  . LYS D 1 3   ? -21.102 18.547  56.535  1.00 93.57  ? 3   LYS D CE  1 
ATOM   12249 N NZ  . LYS D 1 3   ? -21.052 19.900  55.914  1.00 87.56  ? 3   LYS D NZ  1 
ATOM   12250 N N   . LEU D 1 4   ? -19.363 18.351  63.033  1.00 85.43  ? 4   LEU D N   1 
ATOM   12251 C CA  . LEU D 1 4   ? -18.962 19.155  64.181  1.00 78.75  ? 4   LEU D CA  1 
ATOM   12252 C C   . LEU D 1 4   ? -18.995 20.611  63.734  1.00 83.32  ? 4   LEU D C   1 
ATOM   12253 O O   . LEU D 1 4   ? -18.101 21.079  63.023  1.00 87.88  ? 4   LEU D O   1 
ATOM   12254 C CB  . LEU D 1 4   ? -17.592 18.727  64.694  1.00 81.24  ? 4   LEU D CB  1 
ATOM   12255 C CG  . LEU D 1 4   ? -17.064 19.491  65.912  1.00 84.12  ? 4   LEU D CG  1 
ATOM   12256 C CD1 . LEU D 1 4   ? -16.226 18.567  66.775  1.00 82.18  ? 4   LEU D CD1 1 
ATOM   12257 C CD2 . LEU D 1 4   ? -16.250 20.725  65.515  1.00 76.10  ? 4   LEU D CD2 1 
ATOM   12258 N N   . PHE D 1 5   ? -20.054 21.318  64.113  1.00 82.49  ? 5   PHE D N   1 
ATOM   12259 C CA  . PHE D 1 5   ? -20.144 22.744  63.827  1.00 81.41  ? 5   PHE D CA  1 
ATOM   12260 C C   . PHE D 1 5   ? -19.159 23.497  64.715  1.00 74.97  ? 5   PHE D C   1 
ATOM   12261 O O   . PHE D 1 5   ? -19.241 23.430  65.945  1.00 73.51  ? 5   PHE D O   1 
ATOM   12262 C CB  . PHE D 1 5   ? -21.574 23.237  64.038  1.00 76.89  ? 5   PHE D CB  1 
ATOM   12263 C CG  . PHE D 1 5   ? -22.572 22.621  63.096  1.00 77.74  ? 5   PHE D CG  1 
ATOM   12264 C CD1 . PHE D 1 5   ? -22.167 22.095  61.878  1.00 81.57  ? 5   PHE D CD1 1 
ATOM   12265 C CD2 . PHE D 1 5   ? -23.918 22.577  63.425  1.00 81.73  ? 5   PHE D CD2 1 
ATOM   12266 C CE1 . PHE D 1 5   ? -23.088 21.528  61.009  1.00 87.29  ? 5   PHE D CE1 1 
ATOM   12267 C CE2 . PHE D 1 5   ? -24.842 22.009  62.559  1.00 87.09  ? 5   PHE D CE2 1 
ATOM   12268 C CZ  . PHE D 1 5   ? -24.424 21.486  61.349  1.00 86.35  ? 5   PHE D CZ  1 
ATOM   12269 N N   . LEU D 1 6   ? -18.222 24.205  64.092  1.00 78.61  ? 6   LEU D N   1 
ATOM   12270 C CA  . LEU D 1 6   ? -17.156 24.910  64.793  1.00 78.19  ? 6   LEU D CA  1 
ATOM   12271 C C   . LEU D 1 6   ? -17.283 26.402  64.528  1.00 77.07  ? 6   LEU D C   1 
ATOM   12272 O O   . LEU D 1 6   ? -17.454 26.819  63.377  1.00 73.30  ? 6   LEU D O   1 
ATOM   12273 C CB  . LEU D 1 6   ? -15.783 24.397  64.343  1.00 74.48  ? 6   LEU D CB  1 
ATOM   12274 C CG  . LEU D 1 6   ? -14.534 25.192  64.731  1.00 71.95  ? 6   LEU D CG  1 
ATOM   12275 C CD1 . LEU D 1 6   ? -14.470 25.420  66.232  1.00 76.75  ? 6   LEU D CD1 1 
ATOM   12276 C CD2 . LEU D 1 6   ? -13.294 24.459  64.252  1.00 68.28  ? 6   LEU D CD2 1 
ATOM   12277 N N   . VAL D 1 7   ? -17.196 27.200  65.590  1.00 71.27  ? 7   VAL D N   1 
ATOM   12278 C CA  . VAL D 1 7   ? -17.257 28.653  65.499  1.00 70.21  ? 7   VAL D CA  1 
ATOM   12279 C C   . VAL D 1 7   ? -15.931 29.207  66.004  1.00 70.04  ? 7   VAL D C   1 
ATOM   12280 O O   . VAL D 1 7   ? -15.534 28.940  67.146  1.00 70.38  ? 7   VAL D O   1 
ATOM   12281 C CB  . VAL D 1 7   ? -18.439 29.230  66.299  1.00 61.82  ? 7   VAL D CB  1 
ATOM   12282 C CG1 . VAL D 1 7   ? -18.505 30.747  66.148  1.00 59.07  ? 7   VAL D CG1 1 
ATOM   12283 C CG2 . VAL D 1 7   ? -19.742 28.585  65.867  1.00 58.88  ? 7   VAL D CG2 1 
ATOM   12284 N N   . PHE D 1 8   ? -15.247 29.963  65.151  1.00 65.16  ? 8   PHE D N   1 
ATOM   12285 C CA  . PHE D 1 8   ? -14.036 30.684  65.520  1.00 63.25  ? 8   PHE D CA  1 
ATOM   12286 C C   . PHE D 1 8   ? -14.409 32.139  65.788  1.00 63.86  ? 8   PHE D C   1 
ATOM   12287 O O   . PHE D 1 8   ? -14.969 32.808  64.914  1.00 69.42  ? 8   PHE D O   1 
ATOM   12288 C CB  . PHE D 1 8   ? -12.995 30.602  64.403  1.00 68.84  ? 8   PHE D CB  1 
ATOM   12289 C CG  . PHE D 1 8   ? -12.032 29.454  64.536  1.00 66.72  ? 8   PHE D CG  1 
ATOM   12290 C CD1 . PHE D 1 8   ? -11.056 29.463  65.517  1.00 74.53  ? 8   PHE D CD1 1 
ATOM   12291 C CD2 . PHE D 1 8   ? -12.092 28.377  63.666  1.00 61.05  ? 8   PHE D CD2 1 
ATOM   12292 C CE1 . PHE D 1 8   ? -10.163 28.409  65.638  1.00 75.83  ? 8   PHE D CE1 1 
ATOM   12293 C CE2 . PHE D 1 8   ? -11.205 27.323  63.781  1.00 69.45  ? 8   PHE D CE2 1 
ATOM   12294 C CZ  . PHE D 1 8   ? -10.239 27.339  64.767  1.00 73.78  ? 8   PHE D CZ  1 
ATOM   12295 N N   . TRP D 1 9   ? -14.099 32.629  66.984  1.00 66.64  ? 9   TRP D N   1 
ATOM   12296 C CA  . TRP D 1 9   ? -14.397 34.009  67.364  1.00 64.79  ? 9   TRP D CA  1 
ATOM   12297 C C   . TRP D 1 9   ? -13.119 34.640  67.904  1.00 59.88  ? 9   TRP D C   1 
ATOM   12298 O O   . TRP D 1 9   ? -12.613 34.226  68.953  1.00 63.42  ? 9   TRP D O   1 
ATOM   12299 C CB  . TRP D 1 9   ? -15.530 34.051  68.393  1.00 67.08  ? 9   TRP D CB  1 
ATOM   12300 C CG  . TRP D 1 9   ? -16.243 35.362  68.512  1.00 61.33  ? 9   TRP D CG  1 
ATOM   12301 C CD1 . TRP D 1 9   ? -15.856 36.560  67.991  1.00 62.02  ? 9   TRP D CD1 1 
ATOM   12302 C CD2 . TRP D 1 9   ? -17.467 35.606  69.216  1.00 63.81  ? 9   TRP D CD2 1 
ATOM   12303 N NE1 . TRP D 1 9   ? -16.765 37.536  68.325  1.00 63.44  ? 9   TRP D NE1 1 
ATOM   12304 C CE2 . TRP D 1 9   ? -17.764 36.974  69.078  1.00 64.99  ? 9   TRP D CE2 1 
ATOM   12305 C CE3 . TRP D 1 9   ? -18.342 34.797  69.950  1.00 63.53  ? 9   TRP D CE3 1 
ATOM   12306 C CZ2 . TRP D 1 9   ? -18.899 37.553  69.646  1.00 64.00  ? 9   TRP D CZ2 1 
ATOM   12307 C CZ3 . TRP D 1 9   ? -19.468 35.375  70.513  1.00 63.58  ? 9   TRP D CZ3 1 
ATOM   12308 C CH2 . TRP D 1 9   ? -19.736 36.739  70.356  1.00 63.55  ? 9   TRP D CH2 1 
ATOM   12309 N N   . TRP D 1 10  ? -12.591 35.625  67.181  1.00 59.61  ? 10  TRP D N   1 
ATOM   12310 C CA  . TRP D 1 10  ? -11.361 36.317  67.548  1.00 62.26  ? 10  TRP D CA  1 
ATOM   12311 C C   . TRP D 1 10  ? -11.700 37.689  68.118  1.00 61.19  ? 10  TRP D C   1 
ATOM   12312 O O   . TRP D 1 10  ? -12.418 38.471  67.485  1.00 62.36  ? 10  TRP D O   1 
ATOM   12313 C CB  . TRP D 1 10  ? -10.431 36.467  66.338  1.00 61.31  ? 10  TRP D CB  1 
ATOM   12314 C CG  . TRP D 1 10  ? -10.054 35.173  65.651  1.00 67.60  ? 10  TRP D CG  1 
ATOM   12315 C CD1 . TRP D 1 10  ? -10.585 34.674  64.494  1.00 70.74  ? 10  TRP D CD1 1 
ATOM   12316 C CD2 . TRP D 1 10  ? -9.065  34.222  66.077  1.00 66.08  ? 10  TRP D CD2 1 
ATOM   12317 N NE1 . TRP D 1 10  ? -9.991  33.474  64.176  1.00 69.89  ? 10  TRP D NE1 1 
ATOM   12318 C CE2 . TRP D 1 10  ? -9.055  33.175  65.131  1.00 69.66  ? 10  TRP D CE2 1 
ATOM   12319 C CE3 . TRP D 1 10  ? -8.188  34.155  67.166  1.00 66.64  ? 10  TRP D CE3 1 
ATOM   12320 C CZ2 . TRP D 1 10  ? -8.204  32.075  65.240  1.00 71.12  ? 10  TRP D CZ2 1 
ATOM   12321 C CZ3 . TRP D 1 10  ? -7.343  33.062  67.271  1.00 66.61  ? 10  TRP D CZ3 1 
ATOM   12322 C CH2 . TRP D 1 10  ? -7.358  32.038  66.316  1.00 73.36  ? 10  TRP D CH2 1 
ATOM   12323 N N   . HIS D 1 11  ? -11.179 37.980  69.304  1.00 59.01  ? 11  HIS D N   1 
ATOM   12324 C CA  . HIS D 1 11  ? -11.464 39.226  70.002  1.00 54.64  ? 11  HIS D CA  1 
ATOM   12325 C C   . HIS D 1 11  ? -10.321 40.212  69.787  1.00 62.03  ? 11  HIS D C   1 
ATOM   12326 O O   . HIS D 1 11  ? -9.160  39.894  70.070  1.00 66.99  ? 11  HIS D O   1 
ATOM   12327 C CB  . HIS D 1 11  ? -11.681 38.954  71.492  1.00 50.46  ? 11  HIS D CB  1 
ATOM   12328 C CG  . HIS D 1 11  ? -11.549 40.166  72.352  1.00 50.77  ? 11  HIS D CG  1 
ATOM   12329 N ND1 . HIS D 1 11  ? -12.575 41.070  72.519  1.00 56.03  ? 11  HIS D ND1 1 
ATOM   12330 C CD2 . HIS D 1 11  ? -10.525 40.614  73.115  1.00 56.70  ? 11  HIS D CD2 1 
ATOM   12331 C CE1 . HIS D 1 11  ? -12.183 42.033  73.332  1.00 55.30  ? 11  HIS D CE1 1 
ATOM   12332 N NE2 . HIS D 1 11  ? -10.944 41.777  73.712  1.00 59.05  ? 11  HIS D NE2 1 
ATOM   12333 N N   . MET D 1 12  ? -10.649 41.402  69.284  1.00 53.06  ? 12  MET D N   1 
ATOM   12334 C CA  . MET D 1 12  ? -9.653  42.426  68.977  1.00 54.51  ? 12  MET D CA  1 
ATOM   12335 C C   . MET D 1 12  ? -9.954  43.687  69.771  1.00 54.31  ? 12  MET D C   1 
ATOM   12336 O O   . MET D 1 12  ? -10.990 44.326  69.558  1.00 59.77  ? 12  MET D O   1 
ATOM   12337 C CB  . MET D 1 12  ? -9.622  42.727  67.479  1.00 54.16  ? 12  MET D CB  1 
ATOM   12338 C CG  . MET D 1 12  ? -8.472  42.053  66.745  1.00 53.88  ? 12  MET D CG  1 
ATOM   12339 S SD  . MET D 1 12  ? -8.742  40.295  66.486  1.00 63.13  ? 12  MET D SD  1 
ATOM   12340 C CE  . MET D 1 12  ? -7.363  39.851  65.435  1.00 67.10  ? 12  MET D CE  1 
ATOM   12341 N N   . HIS D 1 13  ? -9.045  44.048  70.673  1.00 51.41  ? 13  HIS D N   1 
ATOM   12342 C CA  . HIS D 1 13  ? -9.254  45.194  71.545  1.00 53.66  ? 13  HIS D CA  1 
ATOM   12343 C C   . HIS D 1 13  ? -7.914  45.816  71.920  1.00 55.00  ? 13  HIS D C   1 
ATOM   12344 O O   . HIS D 1 13  ? -6.931  45.102  72.136  1.00 55.12  ? 13  HIS D O   1 
ATOM   12345 C CB  . HIS D 1 13  ? -10.031 44.779  72.802  1.00 51.10  ? 13  HIS D CB  1 
ATOM   12346 C CG  . HIS D 1 13  ? -9.948  45.767  73.919  1.00 52.53  ? 13  HIS D CG  1 
ATOM   12347 N ND1 . HIS D 1 13  ? -10.516 47.021  73.846  1.00 52.23  ? 13  HIS D ND1 1 
ATOM   12348 C CD2 . HIS D 1 13  ? -9.365  45.687  75.138  1.00 52.12  ? 13  HIS D CD2 1 
ATOM   12349 C CE1 . HIS D 1 13  ? -10.279 47.674  74.970  1.00 53.05  ? 13  HIS D CE1 1 
ATOM   12350 N NE2 . HIS D 1 13  ? -9.585  46.886  75.772  1.00 52.44  ? 13  HIS D NE2 1 
ATOM   12351 N N   . GLN D 1 14  ? -7.881  47.153  71.968  1.00 52.54  ? 14  GLN D N   1 
ATOM   12352 C CA  . GLN D 1 14  ? -6.771  47.917  72.530  1.00 50.57  ? 14  GLN D CA  1 
ATOM   12353 C C   . GLN D 1 14  ? -7.342  48.972  73.470  1.00 52.43  ? 14  GLN D C   1 
ATOM   12354 O O   . GLN D 1 14  ? -8.315  49.655  73.106  1.00 57.77  ? 14  GLN D O   1 
ATOM   12355 C CB  . GLN D 1 14  ? -5.927  48.596  71.438  1.00 55.25  ? 14  GLN D CB  1 
ATOM   12356 C CG  . GLN D 1 14  ? -5.007  47.661  70.662  1.00 59.43  ? 14  GLN D CG  1 
ATOM   12357 C CD  . GLN D 1 14  ? -4.069  46.881  71.559  1.00 56.14  ? 14  GLN D CD  1 
ATOM   12358 O OE1 . GLN D 1 14  ? -3.571  47.401  72.557  1.00 53.14  ? 14  GLN D OE1 1 
ATOM   12359 N NE2 . GLN D 1 14  ? -3.825  45.622  71.207  1.00 56.05  ? 14  GLN D NE2 1 
ATOM   12360 N N   . PRO D 1 15  ? -6.789  49.138  74.670  1.00 52.20  ? 15  PRO D N   1 
ATOM   12361 C CA  . PRO D 1 15  ? -7.226  50.240  75.539  1.00 51.29  ? 15  PRO D CA  1 
ATOM   12362 C C   . PRO D 1 15  ? -6.871  51.593  74.930  1.00 52.79  ? 15  PRO D C   1 
ATOM   12363 O O   . PRO D 1 15  ? -6.132  51.690  73.951  1.00 50.51  ? 15  PRO D O   1 
ATOM   12364 C CB  . PRO D 1 15  ? -6.462  49.988  76.842  1.00 49.13  ? 15  PRO D CB  1 
ATOM   12365 C CG  . PRO D 1 15  ? -5.264  49.204  76.423  1.00 56.57  ? 15  PRO D CG  1 
ATOM   12366 C CD  . PRO D 1 15  ? -5.753  48.315  75.313  1.00 53.92  ? 15  PRO D CD  1 
ATOM   12367 N N   . LEU D 1 16  ? -7.414  52.652  75.525  1.00 60.30  ? 16  LEU D N   1 
ATOM   12368 C CA  . LEU D 1 16  ? -7.239  54.006  74.990  1.00 61.30  ? 16  LEU D CA  1 
ATOM   12369 C C   . LEU D 1 16  ? -5.886  54.565  75.413  1.00 48.30  ? 16  LEU D C   1 
ATOM   12370 O O   . LEU D 1 16  ? -5.728  55.040  76.538  1.00 53.41  ? 16  LEU D O   1 
ATOM   12371 C CB  . LEU D 1 16  ? -8.362  54.923  75.462  1.00 54.21  ? 16  LEU D CB  1 
ATOM   12372 C CG  . LEU D 1 16  ? -8.318  56.309  74.817  1.00 49.93  ? 16  LEU D CG  1 
ATOM   12373 C CD1 . LEU D 1 16  ? -8.399  56.190  73.301  1.00 51.88  ? 16  LEU D CD1 1 
ATOM   12374 C CD2 . LEU D 1 16  ? -9.402  57.221  75.359  1.00 50.49  ? 16  LEU D CD2 1 
ATOM   12375 N N   . TYR D 1 17  ? -4.907  54.533  74.503  1.00 49.03  ? 17  TYR D N   1 
ATOM   12376 C CA  . TYR D 1 17  ? -3.561  55.036  74.775  1.00 53.50  ? 17  TYR D CA  1 
ATOM   12377 C C   . TYR D 1 17  ? -3.424  56.536  74.546  1.00 58.79  ? 17  TYR D C   1 
ATOM   12378 O O   . TYR D 1 17  ? -2.308  57.059  74.633  1.00 52.46  ? 17  TYR D O   1 
ATOM   12379 C CB  . TYR D 1 17  ? -2.519  54.314  73.909  1.00 46.76  ? 17  TYR D CB  1 
ATOM   12380 C CG  . TYR D 1 17  ? -2.472  52.823  74.108  1.00 46.03  ? 17  TYR D CG  1 
ATOM   12381 C CD1 . TYR D 1 17  ? -2.338  52.275  75.376  1.00 46.08  ? 17  TYR D CD1 1 
ATOM   12382 C CD2 . TYR D 1 17  ? -2.561  51.958  73.027  1.00 46.50  ? 17  TYR D CD2 1 
ATOM   12383 C CE1 . TYR D 1 17  ? -2.296  50.909  75.564  1.00 45.66  ? 17  TYR D CE1 1 
ATOM   12384 C CE2 . TYR D 1 17  ? -2.520  50.590  73.203  1.00 48.38  ? 17  TYR D CE2 1 
ATOM   12385 C CZ  . TYR D 1 17  ? -2.386  50.070  74.473  1.00 45.14  ? 17  TYR D CZ  1 
ATOM   12386 O OH  . TYR D 1 17  ? -2.350  48.708  74.647  1.00 45.89  ? 17  TYR D OH  1 
ATOM   12387 N N   . ARG D 1 18  ? -4.514  57.236  74.244  1.00 54.14  ? 18  ARG D N   1 
ATOM   12388 C CA  . ARG D 1 18  ? -4.448  58.652  73.908  1.00 52.81  ? 18  ARG D CA  1 
ATOM   12389 C C   . ARG D 1 18  ? -4.649  59.478  75.171  1.00 54.24  ? 18  ARG D C   1 
ATOM   12390 O O   . ARG D 1 18  ? -5.731  59.453  75.763  1.00 59.30  ? 18  ARG D O   1 
ATOM   12391 C CB  . ARG D 1 18  ? -5.498  59.011  72.861  1.00 57.34  ? 18  ARG D CB  1 
ATOM   12392 C CG  . ARG D 1 18  ? -5.448  60.470  72.437  1.00 62.56  ? 18  ARG D CG  1 
ATOM   12393 C CD  . ARG D 1 18  ? -6.686  60.870  71.660  1.00 59.89  ? 18  ARG D CD  1 
ATOM   12394 N NE  . ARG D 1 18  ? -6.478  62.071  70.855  1.00 68.88  ? 18  ARG D NE  1 
ATOM   12395 C CZ  . ARG D 1 18  ? -6.679  63.313  71.279  1.00 68.37  ? 18  ARG D CZ  1 
ATOM   12396 N NH1 . ARG D 1 18  ? -7.087  63.566  72.513  1.00 68.10  ? 18  ARG D NH1 1 
ATOM   12397 N NH2 . ARG D 1 18  ? -6.487  64.325  70.438  1.00 61.06  ? 18  ARG D NH2 1 
ATOM   12398 N N   . GLU D 1 19  ? -3.615  60.205  75.582  1.00 65.28  ? 19  GLU D N   1 
ATOM   12399 C CA  . GLU D 1 19  ? -3.741  61.048  76.758  1.00 62.29  ? 19  GLU D CA  1 
ATOM   12400 C C   . GLU D 1 19  ? -4.771  62.146  76.489  1.00 67.49  ? 19  GLU D C   1 
ATOM   12401 O O   . GLU D 1 19  ? -4.768  62.740  75.405  1.00 66.68  ? 19  GLU D O   1 
ATOM   12402 C CB  . GLU D 1 19  ? -2.387  61.658  77.122  1.00 63.73  ? 19  GLU D CB  1 
ATOM   12403 C CG  . GLU D 1 19  ? -2.126  61.800  78.619  1.00 71.58  ? 19  GLU D CG  1 
ATOM   12404 C CD  . GLU D 1 19  ? -2.346  63.217  79.120  1.00 76.32  ? 19  GLU D CD  1 
ATOM   12405 O OE1 . GLU D 1 19  ? -2.931  64.029  78.372  1.00 78.89  ? 19  GLU D OE1 1 
ATOM   12406 O OE2 . GLU D 1 19  ? -1.920  63.524  80.254  1.00 79.06  ? 19  GLU D OE2 1 
ATOM   12407 N N   . PRO D 1 20  ? -5.681  62.425  77.433  1.00 76.57  ? 20  PRO D N   1 
ATOM   12408 C CA  . PRO D 1 20  ? -6.740  63.414  77.146  1.00 68.18  ? 20  PRO D CA  1 
ATOM   12409 C C   . PRO D 1 20  ? -6.224  64.820  76.882  1.00 71.72  ? 20  PRO D C   1 
ATOM   12410 O O   . PRO D 1 20  ? -6.649  65.459  75.911  1.00 78.55  ? 20  PRO D O   1 
ATOM   12411 C CB  . PRO D 1 20  ? -7.613  63.362  78.409  1.00 65.77  ? 20  PRO D CB  1 
ATOM   12412 C CG  . PRO D 1 20  ? -6.736  62.784  79.466  1.00 71.42  ? 20  PRO D CG  1 
ATOM   12413 C CD  . PRO D 1 20  ? -5.852  61.804  78.757  1.00 73.46  ? 20  PRO D CD  1 
ATOM   12414 N N   . TYR D 1 21  ? -5.314  65.322  77.719  1.00 69.54  ? 21  TYR D N   1 
ATOM   12415 C CA  . TYR D 1 21  ? -4.858  66.704  77.598  1.00 70.48  ? 21  TYR D CA  1 
ATOM   12416 C C   . TYR D 1 21  ? -3.886  66.885  76.432  1.00 73.83  ? 21  TYR D C   1 
ATOM   12417 O O   . TYR D 1 21  ? -4.127  67.700  75.534  1.00 78.21  ? 21  TYR D O   1 
ATOM   12418 C CB  . TYR D 1 21  ? -4.216  67.160  78.914  1.00 70.91  ? 21  TYR D CB  1 
ATOM   12419 C CG  . TYR D 1 21  ? -5.100  66.968  80.127  1.00 73.22  ? 21  TYR D CG  1 
ATOM   12420 C CD1 . TYR D 1 21  ? -5.139  65.752  80.794  1.00 73.37  ? 21  TYR D CD1 1 
ATOM   12421 C CD2 . TYR D 1 21  ? -5.899  68.003  80.605  1.00 66.51  ? 21  TYR D CD2 1 
ATOM   12422 C CE1 . TYR D 1 21  ? -5.944  65.570  81.898  1.00 69.68  ? 21  TYR D CE1 1 
ATOM   12423 C CE2 . TYR D 1 21  ? -6.704  67.831  81.709  1.00 65.77  ? 21  TYR D CE2 1 
ATOM   12424 C CZ  . TYR D 1 21  ? -6.722  66.612  82.352  1.00 69.39  ? 21  TYR D CZ  1 
ATOM   12425 O OH  . TYR D 1 21  ? -7.523  66.426  83.453  1.00 73.66  ? 21  TYR D OH  1 
ATOM   12426 N N   . THR D 1 22  ? -2.779  66.132  76.426  1.00 72.27  ? 22  THR D N   1 
ATOM   12427 C CA  . THR D 1 22  ? -1.774  66.290  75.375  1.00 75.18  ? 22  THR D CA  1 
ATOM   12428 C C   . THR D 1 22  ? -2.212  65.681  74.048  1.00 68.62  ? 22  THR D C   1 
ATOM   12429 O O   . THR D 1 22  ? -1.628  66.008  73.009  1.00 63.65  ? 22  THR D O   1 
ATOM   12430 C CB  . THR D 1 22  ? -0.433  65.678  75.806  1.00 65.60  ? 22  THR D CB  1 
ATOM   12431 O OG1 . THR D 1 22  ? -0.436  64.264  75.560  1.00 68.46  ? 22  THR D OG1 1 
ATOM   12432 C CG2 . THR D 1 22  ? -0.172  65.936  77.286  1.00 64.80  ? 22  THR D CG2 1 
ATOM   12433 N N   . GLY D 1 23  ? -3.227  64.820  74.054  1.00 64.02  ? 23  GLY D N   1 
ATOM   12434 C CA  . GLY D 1 23  ? -3.676  64.189  72.825  1.00 69.31  ? 23  GLY D CA  1 
ATOM   12435 C C   . GLY D 1 23  ? -2.651  63.282  72.184  1.00 69.37  ? 23  GLY D C   1 
ATOM   12436 O O   . GLY D 1 23  ? -2.694  63.063  70.968  1.00 71.33  ? 23  GLY D O   1 
ATOM   12437 N N   . GLU D 1 24  ? -1.730  62.738  72.972  1.00 70.07  ? 24  GLU D N   1 
ATOM   12438 C CA  . GLU D 1 24  ? -0.646  61.919  72.455  1.00 67.98  ? 24  GLU D CA  1 
ATOM   12439 C C   . GLU D 1 24  ? -0.890  60.452  72.777  1.00 65.65  ? 24  GLU D C   1 
ATOM   12440 O O   . GLU D 1 24  ? -1.493  60.112  73.801  1.00 59.22  ? 24  GLU D O   1 
ATOM   12441 C CB  . GLU D 1 24  ? 0.699   62.365  73.035  1.00 63.56  ? 24  GLU D CB  1 
ATOM   12442 C CG  . GLU D 1 24  ? 1.110   63.756  72.590  1.00 68.18  ? 24  GLU D CG  1 
ATOM   12443 C CD  . GLU D 1 24  ? 2.267   64.310  73.396  1.00 71.62  ? 24  GLU D CD  1 
ATOM   12444 O OE1 . GLU D 1 24  ? 2.725   63.619  74.332  1.00 65.78  ? 24  GLU D OE1 1 
ATOM   12445 O OE2 . GLU D 1 24  ? 2.706   65.444  73.106  1.00 77.28  ? 24  GLU D OE2 1 
ATOM   12446 N N   . TYR D 1 25  ? -0.415  59.585  71.883  1.00 63.25  ? 25  TYR D N   1 
ATOM   12447 C CA  . TYR D 1 25  ? -0.484  58.139  72.077  1.00 56.67  ? 25  TYR D CA  1 
ATOM   12448 C C   . TYR D 1 25  ? 0.775   57.722  72.820  1.00 57.53  ? 25  TYR D C   1 
ATOM   12449 O O   . TYR D 1 25  ? 1.865   57.670  72.246  1.00 63.76  ? 25  TYR D O   1 
ATOM   12450 C CB  . TYR D 1 25  ? -0.632  57.413  70.746  1.00 61.55  ? 25  TYR D CB  1 
ATOM   12451 C CG  . TYR D 1 25  ? -2.068  57.352  70.267  1.00 67.32  ? 25  TYR D CG  1 
ATOM   12452 C CD1 . TYR D 1 25  ? -2.703  58.486  69.783  1.00 67.84  ? 25  TYR D CD1 1 
ATOM   12453 C CD2 . TYR D 1 25  ? -2.797  56.168  70.320  1.00 64.52  ? 25  TYR D CD2 1 
ATOM   12454 C CE1 . TYR D 1 25  ? -4.010  58.448  69.352  1.00 68.69  ? 25  TYR D CE1 1 
ATOM   12455 C CE2 . TYR D 1 25  ? -4.117  56.117  69.890  1.00 59.78  ? 25  TYR D CE2 1 
ATOM   12456 C CZ  . TYR D 1 25  ? -4.716  57.267  69.404  1.00 68.71  ? 25  TYR D CZ  1 
ATOM   12457 O OH  . TYR D 1 25  ? -6.022  57.266  68.964  1.00 63.72  ? 25  TYR D OH  1 
ATOM   12458 N N   . LEU D 1 26  ? 0.626   57.442  74.111  1.00 53.71  ? 26  LEU D N   1 
ATOM   12459 C CA  . LEU D 1 26  ? 1.774   57.142  74.947  1.00 52.07  ? 26  LEU D CA  1 
ATOM   12460 C C   . LEU D 1 26  ? 2.332   55.747  74.705  1.00 51.15  ? 26  LEU D C   1 
ATOM   12461 O O   . LEU D 1 26  ? 3.461   55.473  75.126  1.00 48.77  ? 26  LEU D O   1 
ATOM   12462 C CB  . LEU D 1 26  ? 1.397   57.319  76.418  1.00 53.76  ? 26  LEU D CB  1 
ATOM   12463 C CG  . LEU D 1 26  ? 0.814   58.686  76.798  1.00 55.25  ? 26  LEU D CG  1 
ATOM   12464 C CD1 . LEU D 1 26  ? 0.698   58.810  78.307  1.00 57.47  ? 26  LEU D CD1 1 
ATOM   12465 C CD2 . LEU D 1 26  ? 1.651   59.825  76.227  1.00 56.94  ? 26  LEU D CD2 1 
ATOM   12466 N N   . LEU D 1 27  ? 1.578   54.866  74.045  1.00 47.68  ? 27  LEU D N   1 
ATOM   12467 C CA  . LEU D 1 27  ? 2.037   53.518  73.741  1.00 47.05  ? 27  LEU D CA  1 
ATOM   12468 C C   . LEU D 1 27  ? 1.701   53.178  72.297  1.00 52.80  ? 27  LEU D C   1 
ATOM   12469 O O   . LEU D 1 27  ? 0.594   53.462  71.824  1.00 53.44  ? 27  LEU D O   1 
ATOM   12470 C CB  . LEU D 1 27  ? 1.406   52.471  74.675  1.00 46.68  ? 27  LEU D CB  1 
ATOM   12471 C CG  . LEU D 1 27  ? 2.073   52.302  76.046  1.00 54.33  ? 27  LEU D CG  1 
ATOM   12472 C CD1 . LEU D 1 27  ? 1.551   51.090  76.827  1.00 50.40  ? 27  LEU D CD1 1 
ATOM   12473 C CD2 . LEU D 1 27  ? 3.589   52.238  75.911  1.00 53.77  ? 27  LEU D CD2 1 
ATOM   12474 N N   . PRO D 1 28  ? 2.637   52.564  71.576  1.00 55.99  ? 28  PRO D N   1 
ATOM   12475 C CA  . PRO D 1 28  ? 2.427   52.277  70.156  1.00 53.56  ? 28  PRO D CA  1 
ATOM   12476 C C   . PRO D 1 28  ? 1.690   50.979  69.875  1.00 57.15  ? 28  PRO D C   1 
ATOM   12477 O O   . PRO D 1 28  ? 1.626   50.569  68.713  1.00 58.51  ? 28  PRO D O   1 
ATOM   12478 C CB  . PRO D 1 28  ? 3.870   52.204  69.642  1.00 59.33  ? 28  PRO D CB  1 
ATOM   12479 C CG  . PRO D 1 28  ? 4.592   51.550  70.778  1.00 56.69  ? 28  PRO D CG  1 
ATOM   12480 C CD  . PRO D 1 28  ? 3.985   52.164  72.022  1.00 55.01  ? 28  PRO D CD  1 
ATOM   12481 N N   . TRP D 1 29  ? 1.116   50.349  70.903  1.00 57.62  ? 29  TRP D N   1 
ATOM   12482 C CA  . TRP D 1 29  ? 0.636   48.980  70.760  1.00 52.83  ? 29  TRP D CA  1 
ATOM   12483 C C   . TRP D 1 29  ? -0.466  48.880  69.717  1.00 58.37  ? 29  TRP D C   1 
ATOM   12484 O O   . TRP D 1 29  ? -0.541  47.889  68.981  1.00 63.55  ? 29  TRP D O   1 
ATOM   12485 C CB  . TRP D 1 29  ? 0.153   48.445  72.110  1.00 57.96  ? 29  TRP D CB  1 
ATOM   12486 C CG  . TRP D 1 29  ? 1.261   48.151  73.083  1.00 57.54  ? 29  TRP D CG  1 
ATOM   12487 C CD1 . TRP D 1 29  ? 1.334   48.557  74.381  1.00 54.50  ? 29  TRP D CD1 1 
ATOM   12488 C CD2 . TRP D 1 29  ? 2.451   47.383  72.833  1.00 65.58  ? 29  TRP D CD2 1 
ATOM   12489 N NE1 . TRP D 1 29  ? 2.494   48.094  74.959  1.00 61.46  ? 29  TRP D NE1 1 
ATOM   12490 C CE2 . TRP D 1 29  ? 3.197   47.370  74.030  1.00 67.45  ? 29  TRP D CE2 1 
ATOM   12491 C CE3 . TRP D 1 29  ? 2.955   46.702  71.716  1.00 56.34  ? 29  TRP D CE3 1 
ATOM   12492 C CZ2 . TRP D 1 29  ? 4.422   46.710  74.143  1.00 67.61  ? 29  TRP D CZ2 1 
ATOM   12493 C CZ3 . TRP D 1 29  ? 4.172   46.048  71.830  1.00 66.44  ? 29  TRP D CZ3 1 
ATOM   12494 C CH2 . TRP D 1 29  ? 4.892   46.057  73.034  1.00 65.37  ? 29  TRP D CH2 1 
ATOM   12495 N N   . THR D 1 30  ? -1.326  49.900  69.631  1.00 60.11  ? 30  THR D N   1 
ATOM   12496 C CA  . THR D 1 30  ? -2.436  49.835  68.684  1.00 61.71  ? 30  THR D CA  1 
ATOM   12497 C C   . THR D 1 30  ? -1.927  49.852  67.247  1.00 58.41  ? 30  THR D C   1 
ATOM   12498 O O   . THR D 1 30  ? -2.448  49.129  66.389  1.00 57.40  ? 30  THR D O   1 
ATOM   12499 C CB  . THR D 1 30  ? -3.428  50.982  68.932  1.00 63.23  ? 30  THR D CB  1 
ATOM   12500 O OG1 . THR D 1 30  ? -3.921  50.924  70.278  1.00 55.35  ? 30  THR D OG1 1 
ATOM   12501 C CG2 . THR D 1 30  ? -4.607  50.882  67.982  1.00 56.22  ? 30  THR D CG2 1 
ATOM   12502 N N   . PHE D 1 31  ? -0.884  50.641  66.972  1.00 62.33  ? 31  PHE D N   1 
ATOM   12503 C CA  . PHE D 1 31  ? -0.363  50.721  65.609  1.00 68.16  ? 31  PHE D CA  1 
ATOM   12504 C C   . PHE D 1 31  ? 0.270   49.397  65.187  1.00 62.79  ? 31  PHE D C   1 
ATOM   12505 O O   . PHE D 1 31  ? -0.028  48.869  64.108  1.00 54.20  ? 31  PHE D O   1 
ATOM   12506 C CB  . PHE D 1 31  ? 0.638   51.877  65.496  1.00 61.13  ? 31  PHE D CB  1 
ATOM   12507 C CG  . PHE D 1 31  ? 1.505   51.818  64.268  1.00 65.00  ? 31  PHE D CG  1 
ATOM   12508 C CD1 . PHE D 1 31  ? 1.048   52.307  63.052  1.00 67.17  ? 31  PHE D CD1 1 
ATOM   12509 C CD2 . PHE D 1 31  ? 2.787   51.292  64.331  1.00 68.80  ? 31  PHE D CD2 1 
ATOM   12510 C CE1 . PHE D 1 31  ? 1.845   52.255  61.921  1.00 65.51  ? 31  PHE D CE1 1 
ATOM   12511 C CE2 . PHE D 1 31  ? 3.587   51.238  63.201  1.00 65.54  ? 31  PHE D CE2 1 
ATOM   12512 C CZ  . PHE D 1 31  ? 3.113   51.721  61.996  1.00 61.92  ? 31  PHE D CZ  1 
ATOM   12513 N N   . PHE D 1 32  ? 1.118   48.827  66.048  1.00 59.65  ? 32  PHE D N   1 
ATOM   12514 C CA  . PHE D 1 32  ? 1.844   47.610  65.688  1.00 58.31  ? 32  PHE D CA  1 
ATOM   12515 C C   . PHE D 1 32  ? 0.910   46.420  65.504  1.00 61.88  ? 32  PHE D C   1 
ATOM   12516 O O   . PHE D 1 32  ? 1.173   45.548  64.667  1.00 61.55  ? 32  PHE D O   1 
ATOM   12517 C CB  . PHE D 1 32  ? 2.902   47.304  66.749  1.00 61.31  ? 32  PHE D CB  1 
ATOM   12518 C CG  . PHE D 1 32  ? 4.058   48.263  66.735  1.00 64.06  ? 32  PHE D CG  1 
ATOM   12519 C CD1 . PHE D 1 32  ? 4.715   48.550  65.550  1.00 60.64  ? 32  PHE D CD1 1 
ATOM   12520 C CD2 . PHE D 1 32  ? 4.482   48.885  67.897  1.00 65.82  ? 32  PHE D CD2 1 
ATOM   12521 C CE1 . PHE D 1 32  ? 5.771   49.435  65.519  1.00 62.56  ? 32  PHE D CE1 1 
ATOM   12522 C CE2 . PHE D 1 32  ? 5.549   49.777  67.871  1.00 67.11  ? 32  PHE D CE2 1 
ATOM   12523 C CZ  . PHE D 1 32  ? 6.191   50.051  66.680  1.00 61.23  ? 32  PHE D CZ  1 
ATOM   12524 N N   . HIS D 1 33  ? -0.183  46.361  66.263  1.00 64.15  ? 33  HIS D N   1 
ATOM   12525 C CA  . HIS D 1 33  ? -1.103  45.242  66.114  1.00 57.82  ? 33  HIS D CA  1 
ATOM   12526 C C   . HIS D 1 33  ? -2.044  45.416  64.927  1.00 56.92  ? 33  HIS D C   1 
ATOM   12527 O O   . HIS D 1 33  ? -2.580  44.421  64.424  1.00 54.98  ? 33  HIS D O   1 
ATOM   12528 C CB  . HIS D 1 33  ? -1.891  45.040  67.407  1.00 54.00  ? 33  HIS D CB  1 
ATOM   12529 C CG  . HIS D 1 33  ? -1.145  44.260  68.448  1.00 64.84  ? 33  HIS D CG  1 
ATOM   12530 N ND1 . HIS D 1 33  ? -0.446  44.861  69.474  1.00 62.85  ? 33  HIS D ND1 1 
ATOM   12531 C CD2 . HIS D 1 33  ? -0.972  42.926  68.608  1.00 62.76  ? 33  HIS D CD2 1 
ATOM   12532 C CE1 . HIS D 1 33  ? 0.111   43.932  70.230  1.00 59.37  ? 33  HIS D CE1 1 
ATOM   12533 N NE2 . HIS D 1 33  ? -0.192  42.749  69.726  1.00 61.17  ? 33  HIS D NE2 1 
ATOM   12534 N N   . ALA D 1 34  ? -2.242  46.648  64.453  1.00 58.68  ? 34  ALA D N   1 
ATOM   12535 C CA  . ALA D 1 34  ? -3.037  46.851  63.246  1.00 58.41  ? 34  ALA D CA  1 
ATOM   12536 C C   . ALA D 1 34  ? -2.271  46.420  62.003  1.00 59.05  ? 34  ALA D C   1 
ATOM   12537 O O   . ALA D 1 34  ? -2.840  45.794  61.101  1.00 65.28  ? 34  ALA D O   1 
ATOM   12538 C CB  . ALA D 1 34  ? -3.465  48.313  63.130  1.00 60.88  ? 34  ALA D CB  1 
ATOM   12539 N N   . VAL D 1 35  ? -0.976  46.737  61.939  1.00 59.78  ? 35  VAL D N   1 
ATOM   12540 C CA  . VAL D 1 35  ? -0.175  46.313  60.794  1.00 65.29  ? 35  VAL D CA  1 
ATOM   12541 C C   . VAL D 1 35  ? 0.023   44.800  60.810  1.00 66.90  ? 35  VAL D C   1 
ATOM   12542 O O   . VAL D 1 35  ? 0.069   44.156  59.755  1.00 67.54  ? 35  VAL D O   1 
ATOM   12543 C CB  . VAL D 1 35  ? 1.168   47.075  60.758  1.00 60.58  ? 35  VAL D CB  1 
ATOM   12544 C CG1 . VAL D 1 35  ? 0.939   48.560  60.966  1.00 63.03  ? 35  VAL D CG1 1 
ATOM   12545 C CG2 . VAL D 1 35  ? 2.145   46.540  61.796  1.00 58.90  ? 35  VAL D CG2 1 
ATOM   12546 N N   . LYS D 1 36  ? 0.104   44.201  61.999  1.00 67.52  ? 36  LYS D N   1 
ATOM   12547 C CA  . LYS D 1 36  ? 0.409   42.777  62.085  1.00 64.17  ? 36  LYS D CA  1 
ATOM   12548 C C   . LYS D 1 36  ? -0.845  41.931  61.910  1.00 65.95  ? 36  LYS D C   1 
ATOM   12549 O O   . LYS D 1 36  ? -0.929  41.106  60.994  1.00 72.59  ? 36  LYS D O   1 
ATOM   12550 C CB  . LYS D 1 36  ? 1.085   42.460  63.422  1.00 62.95  ? 36  LYS D CB  1 
ATOM   12551 C CG  . LYS D 1 36  ? 2.079   41.316  63.356  1.00 65.60  ? 36  LYS D CG  1 
ATOM   12552 C CD  . LYS D 1 36  ? 2.841   41.159  64.666  1.00 63.00  ? 36  LYS D CD  1 
ATOM   12553 C CE  . LYS D 1 36  ? 1.927   41.171  65.892  1.00 71.32  ? 36  LYS D CE  1 
ATOM   12554 N NZ  . LYS D 1 36  ? 1.161   39.910  66.129  1.00 70.11  ? 36  LYS D NZ  1 
ATOM   12555 N N   . ASP D 1 37  ? -1.839  42.135  62.776  1.00 63.92  ? 37  ASP D N   1 
ATOM   12556 C CA  . ASP D 1 37  ? -2.954  41.208  62.899  1.00 57.41  ? 37  ASP D CA  1 
ATOM   12557 C C   . ASP D 1 37  ? -4.325  41.788  62.584  1.00 58.05  ? 37  ASP D C   1 
ATOM   12558 O O   . ASP D 1 37  ? -5.198  41.031  62.157  1.00 63.68  ? 37  ASP D O   1 
ATOM   12559 C CB  . ASP D 1 37  ? -3.010  40.613  64.316  1.00 64.63  ? 37  ASP D CB  1 
ATOM   12560 C CG  . ASP D 1 37  ? -1.655  40.599  65.013  1.00 65.21  ? 37  ASP D CG  1 
ATOM   12561 O OD1 . ASP D 1 37  ? -0.849  39.691  64.714  1.00 72.48  ? 37  ASP D OD1 1 
ATOM   12562 O OD2 . ASP D 1 37  ? -1.409  41.466  65.882  1.00 53.54  ? 37  ASP D OD2 1 
ATOM   12563 N N   . TYR D 1 38  ? -4.558  43.090  62.785  1.00 54.63  ? 38  TYR D N   1 
ATOM   12564 C CA  . TYR D 1 38  ? -5.943  43.564  62.755  1.00 60.38  ? 38  TYR D CA  1 
ATOM   12565 C C   . TYR D 1 38  ? -6.530  43.537  61.346  1.00 72.59  ? 38  TYR D C   1 
ATOM   12566 O O   . TYR D 1 38  ? -7.742  43.334  61.187  1.00 71.00  ? 38  TYR D O   1 
ATOM   12567 C CB  . TYR D 1 38  ? -6.067  44.964  63.371  1.00 53.09  ? 38  TYR D CB  1 
ATOM   12568 C CG  . TYR D 1 38  ? -5.833  44.986  64.869  1.00 54.88  ? 38  TYR D CG  1 
ATOM   12569 C CD1 . TYR D 1 38  ? -5.794  43.806  65.595  1.00 58.27  ? 38  TYR D CD1 1 
ATOM   12570 C CD2 . TYR D 1 38  ? -5.627  46.179  65.553  1.00 52.72  ? 38  TYR D CD2 1 
ATOM   12571 C CE1 . TYR D 1 38  ? -5.562  43.807  66.957  1.00 57.45  ? 38  TYR D CE1 1 
ATOM   12572 C CE2 . TYR D 1 38  ? -5.393  46.189  66.926  1.00 52.94  ? 38  TYR D CE2 1 
ATOM   12573 C CZ  . TYR D 1 38  ? -5.365  44.996  67.623  1.00 56.68  ? 38  TYR D CZ  1 
ATOM   12574 O OH  . TYR D 1 38  ? -5.137  44.972  68.985  1.00 55.94  ? 38  TYR D OH  1 
ATOM   12575 N N   . TYR D 1 39  ? -5.703  43.721  60.318  1.00 64.30  ? 39  TYR D N   1 
ATOM   12576 C CA  . TYR D 1 39  ? -6.183  43.508  58.959  1.00 66.22  ? 39  TYR D CA  1 
ATOM   12577 C C   . TYR D 1 39  ? -5.910  42.090  58.479  1.00 73.61  ? 39  TYR D C   1 
ATOM   12578 O O   . TYR D 1 39  ? -6.726  41.521  57.742  1.00 73.61  ? 39  TYR D O   1 
ATOM   12579 C CB  . TYR D 1 39  ? -5.556  44.533  57.999  1.00 68.05  ? 39  TYR D CB  1 
ATOM   12580 C CG  . TYR D 1 39  ? -5.665  44.216  56.512  1.00 70.25  ? 39  TYR D CG  1 
ATOM   12581 C CD1 . TYR D 1 39  ? -4.889  43.221  55.913  1.00 74.12  ? 39  TYR D CD1 1 
ATOM   12582 C CD2 . TYR D 1 39  ? -6.533  44.932  55.703  1.00 79.03  ? 39  TYR D CD2 1 
ATOM   12583 C CE1 . TYR D 1 39  ? -4.995  42.943  54.560  1.00 78.06  ? 39  TYR D CE1 1 
ATOM   12584 C CE2 . TYR D 1 39  ? -6.641  44.666  54.343  1.00 85.10  ? 39  TYR D CE2 1 
ATOM   12585 C CZ  . TYR D 1 39  ? -5.871  43.671  53.779  1.00 81.55  ? 39  TYR D CZ  1 
ATOM   12586 O OH  . TYR D 1 39  ? -5.975  43.405  52.432  1.00 80.17  ? 39  TYR D OH  1 
ATOM   12587 N N   . ASP D 1 40  ? -4.788  41.500  58.893  1.00 72.73  ? 40  ASP D N   1 
ATOM   12588 C CA  . ASP D 1 40  ? -4.377  40.225  58.319  1.00 67.99  ? 40  ASP D CA  1 
ATOM   12589 C C   . ASP D 1 40  ? -5.292  39.087  58.752  1.00 66.02  ? 40  ASP D C   1 
ATOM   12590 O O   . ASP D 1 40  ? -5.569  38.180  57.961  1.00 70.14  ? 40  ASP D O   1 
ATOM   12591 C CB  . ASP D 1 40  ? -2.932  39.923  58.699  1.00 66.87  ? 40  ASP D CB  1 
ATOM   12592 C CG  . ASP D 1 40  ? -1.946  40.538  57.735  1.00 82.48  ? 40  ASP D CG  1 
ATOM   12593 O OD1 . ASP D 1 40  ? -1.788  39.997  56.618  1.00 78.19  ? 40  ASP D OD1 1 
ATOM   12594 O OD2 . ASP D 1 40  ? -1.344  41.575  58.086  1.00 87.79  ? 40  ASP D OD2 1 
ATOM   12595 N N   . MET D 1 41  ? -5.772  39.116  59.995  1.00 66.50  ? 41  MET D N   1 
ATOM   12596 C CA  . MET D 1 41  ? -6.605  38.017  60.481  1.00 68.89  ? 41  MET D CA  1 
ATOM   12597 C C   . MET D 1 41  ? -7.906  37.882  59.703  1.00 67.20  ? 41  MET D C   1 
ATOM   12598 O O   . MET D 1 41  ? -8.225  36.760  59.270  1.00 66.06  ? 41  MET D O   1 
ATOM   12599 C CB  . MET D 1 41  ? -6.847  38.169  61.988  1.00 66.00  ? 41  MET D CB  1 
ATOM   12600 C CG  . MET D 1 41  ? -5.598  37.973  62.820  1.00 64.34  ? 41  MET D CG  1 
ATOM   12601 S SD  . MET D 1 41  ? -5.174  36.231  63.055  1.00 83.15  ? 41  MET D SD  1 
ATOM   12602 C CE  . MET D 1 41  ? -6.689  35.557  63.741  1.00 71.07  ? 41  MET D CE  1 
ATOM   12603 N N   . PRO D 1 42  ? -8.694  38.940  59.477  1.00 66.70  ? 42  PRO D N   1 
ATOM   12604 C CA  . PRO D 1 42  ? -9.829  38.797  58.552  1.00 62.39  ? 42  PRO D CA  1 
ATOM   12605 C C   . PRO D 1 42  ? -9.398  38.625  57.104  1.00 66.49  ? 42  PRO D C   1 
ATOM   12606 O O   . PRO D 1 42  ? -10.220 38.206  56.278  1.00 68.66  ? 42  PRO D O   1 
ATOM   12607 C CB  . PRO D 1 42  ? -10.622 40.094  58.759  1.00 59.28  ? 42  PRO D CB  1 
ATOM   12608 C CG  . PRO D 1 42  ? -9.622  41.069  59.274  1.00 63.83  ? 42  PRO D CG  1 
ATOM   12609 C CD  . PRO D 1 42  ? -8.672  40.271  60.112  1.00 65.24  ? 42  PRO D CD  1 
ATOM   12610 N N   . ALA D 1 43  ? -8.133  38.912  56.773  1.00 67.44  ? 43  ALA D N   1 
ATOM   12611 C CA  . ALA D 1 43  ? -7.645  38.736  55.409  1.00 68.73  ? 43  ALA D CA  1 
ATOM   12612 C C   . ALA D 1 43  ? -7.422  37.276  55.043  1.00 66.65  ? 43  ALA D C   1 
ATOM   12613 O O   . ALA D 1 43  ? -7.416  36.946  53.853  1.00 70.22  ? 43  ALA D O   1 
ATOM   12614 C CB  . ALA D 1 43  ? -6.341  39.510  55.203  1.00 69.95  ? 43  ALA D CB  1 
ATOM   12615 N N   . TYR D 1 44  ? -7.230  36.398  56.029  1.00 71.33  ? 44  TYR D N   1 
ATOM   12616 C CA  . TYR D 1 44  ? -7.122  34.976  55.733  1.00 70.48  ? 44  TYR D CA  1 
ATOM   12617 C C   . TYR D 1 44  ? -8.353  34.452  55.004  1.00 68.82  ? 44  TYR D C   1 
ATOM   12618 O O   . TYR D 1 44  ? -8.253  33.447  54.294  1.00 69.71  ? 44  TYR D O   1 
ATOM   12619 C CB  . TYR D 1 44  ? -6.913  34.177  57.021  1.00 69.13  ? 44  TYR D CB  1 
ATOM   12620 C CG  . TYR D 1 44  ? -5.503  34.195  57.571  1.00 66.97  ? 44  TYR D CG  1 
ATOM   12621 C CD1 . TYR D 1 44  ? -5.053  35.252  58.344  1.00 62.71  ? 44  TYR D CD1 1 
ATOM   12622 C CD2 . TYR D 1 44  ? -4.627  33.143  57.325  1.00 70.10  ? 44  TYR D CD2 1 
ATOM   12623 C CE1 . TYR D 1 44  ? -3.771  35.269  58.856  1.00 71.59  ? 44  TYR D CE1 1 
ATOM   12624 C CE2 . TYR D 1 44  ? -3.345  33.150  57.831  1.00 67.33  ? 44  TYR D CE2 1 
ATOM   12625 C CZ  . TYR D 1 44  ? -2.920  34.214  58.597  1.00 67.64  ? 44  TYR D CZ  1 
ATOM   12626 O OH  . TYR D 1 44  ? -1.641  34.226  59.103  1.00 64.86  ? 44  TYR D OH  1 
ATOM   12627 N N   . LEU D 1 45  ? -9.504  35.120  55.151  1.00 61.55  ? 45  LEU D N   1 
ATOM   12628 C CA  . LEU D 1 45  ? -10.750 34.643  54.555  1.00 71.70  ? 45  LEU D CA  1 
ATOM   12629 C C   . LEU D 1 45  ? -10.749 34.731  53.029  1.00 73.43  ? 45  LEU D C   1 
ATOM   12630 O O   . LEU D 1 45  ? -11.530 34.027  52.378  1.00 65.91  ? 45  LEU D O   1 
ATOM   12631 C CB  . LEU D 1 45  ? -11.924 35.435  55.129  1.00 65.38  ? 45  LEU D CB  1 
ATOM   12632 C CG  . LEU D 1 45  ? -12.322 35.042  56.551  1.00 69.41  ? 45  LEU D CG  1 
ATOM   12633 C CD1 . LEU D 1 45  ? -13.482 35.885  57.049  1.00 71.49  ? 45  LEU D CD1 1 
ATOM   12634 C CD2 . LEU D 1 45  ? -12.675 33.560  56.611  1.00 74.90  ? 45  LEU D CD2 1 
ATOM   12635 N N   . LYS D 1 46  ? -9.894  35.580  52.449  1.00 72.93  ? 46  LYS D N   1 
ATOM   12636 C CA  . LYS D 1 46  ? -9.796  35.665  50.994  1.00 69.61  ? 46  LYS D CA  1 
ATOM   12637 C C   . LYS D 1 46  ? -9.129  34.427  50.409  1.00 68.64  ? 46  LYS D C   1 
ATOM   12638 O O   . LYS D 1 46  ? -9.537  33.936  49.350  1.00 70.91  ? 46  LYS D O   1 
ATOM   12639 C CB  . LYS D 1 46  ? -9.020  36.916  50.580  1.00 68.49  ? 46  LYS D CB  1 
ATOM   12640 C CG  . LYS D 1 46  ? -9.895  38.096  50.171  1.00 84.06  ? 46  LYS D CG  1 
ATOM   12641 C CD  . LYS D 1 46  ? -10.379 37.973  48.723  1.00 83.79  ? 46  LYS D CD  1 
ATOM   12642 C CE  . LYS D 1 46  ? -11.777 38.573  48.547  1.00 79.57  ? 46  LYS D CE  1 
ATOM   12643 N NZ  . LYS D 1 46  ? -12.841 37.778  49.235  1.00 74.51  ? 46  LYS D NZ  1 
ATOM   12644 N N   . ASP D 1 47  ? -8.099  33.911  51.076  1.00 74.72  ? 47  ASP D N   1 
ATOM   12645 C CA  . ASP D 1 47  ? -7.333  32.797  50.534  1.00 79.17  ? 47  ASP D CA  1 
ATOM   12646 C C   . ASP D 1 47  ? -7.905  31.433  50.910  1.00 76.28  ? 47  ASP D C   1 
ATOM   12647 O O   . ASP D 1 47  ? -7.648  30.451  50.202  1.00 72.06  ? 47  ASP D O   1 
ATOM   12648 C CB  . ASP D 1 47  ? -5.869  32.897  50.994  1.00 71.17  ? 47  ASP D CB  1 
ATOM   12649 C CG  . ASP D 1 47  ? -5.277  34.289  50.775  1.00 81.25  ? 47  ASP D CG  1 
ATOM   12650 O OD1 . ASP D 1 47  ? -5.977  35.292  51.034  1.00 77.17  ? 47  ASP D OD1 1 
ATOM   12651 O OD2 . ASP D 1 47  ? -4.109  34.381  50.339  1.00 94.70  ? 47  ASP D OD2 1 
ATOM   12652 N N   . PHE D 1 48  ? -8.682  31.347  51.988  1.00 74.07  ? 48  PHE D N   1 
ATOM   12653 C CA  . PHE D 1 48  ? -9.230  30.080  52.453  1.00 78.61  ? 48  PHE D CA  1 
ATOM   12654 C C   . PHE D 1 48  ? -10.736 30.200  52.628  1.00 83.66  ? 48  PHE D C   1 
ATOM   12655 O O   . PHE D 1 48  ? -11.230 31.188  53.182  1.00 81.11  ? 48  PHE D O   1 
ATOM   12656 C CB  . PHE D 1 48  ? -8.594  29.631  53.786  1.00 77.05  ? 48  PHE D CB  1 
ATOM   12657 C CG  . PHE D 1 48  ? -7.095  29.742  53.819  1.00 76.86  ? 48  PHE D CG  1 
ATOM   12658 C CD1 . PHE D 1 48  ? -6.483  30.938  54.167  1.00 77.62  ? 48  PHE D CD1 1 
ATOM   12659 C CD2 . PHE D 1 48  ? -6.294  28.653  53.506  1.00 81.37  ? 48  PHE D CD2 1 
ATOM   12660 C CE1 . PHE D 1 48  ? -5.102  31.049  54.197  1.00 80.15  ? 48  PHE D CE1 1 
ATOM   12661 C CE2 . PHE D 1 48  ? -4.906  28.760  53.536  1.00 76.45  ? 48  PHE D CE2 1 
ATOM   12662 C CZ  . PHE D 1 48  ? -4.315  29.960  53.880  1.00 75.41  ? 48  PHE D CZ  1 
ATOM   12663 N N   . GLU D 1 49  ? -11.464 29.186  52.166  1.00 89.70  ? 49  GLU D N   1 
ATOM   12664 C CA  . GLU D 1 49  ? -12.905 29.122  52.403  1.00 93.28  ? 49  GLU D CA  1 
ATOM   12665 C C   . GLU D 1 49  ? -13.082 28.469  53.762  1.00 91.98  ? 49  GLU D C   1 
ATOM   12666 O O   . GLU D 1 49  ? -13.038 27.251  53.915  1.00 97.95  ? 49  GLU D O   1 
ATOM   12667 C CB  . GLU D 1 49  ? -13.626 28.363  51.290  1.00 82.99  ? 49  GLU D CB  1 
ATOM   12668 C CG  . GLU D 1 49  ? -15.181 28.561  51.187  1.00 100.76 ? 49  GLU D CG  1 
ATOM   12669 C CD  . GLU D 1 49  ? -16.067 28.277  52.415  1.00 105.44 ? 49  GLU D CD  1 
ATOM   12670 O OE1 . GLU D 1 49  ? -15.769 27.336  53.203  1.00 105.70 ? 49  GLU D OE1 1 
ATOM   12671 O OE2 . GLU D 1 49  ? -17.086 29.019  52.532  1.00 111.31 ? 49  GLU D OE2 1 
ATOM   12672 N N   . ILE D 1 50  ? -13.240 29.304  54.772  1.00 85.99  ? 50  ILE D N   1 
ATOM   12673 C CA  . ILE D 1 50  ? -13.837 28.876  56.025  1.00 81.93  ? 50  ILE D CA  1 
ATOM   12674 C C   . ILE D 1 50  ? -14.732 30.025  56.437  1.00 85.85  ? 50  ILE D C   1 
ATOM   12675 O O   . ILE D 1 50  ? -14.929 30.979  55.673  1.00 88.86  ? 50  ILE D O   1 
ATOM   12676 C CB  . ILE D 1 50  ? -12.792 28.548  57.104  1.00 80.23  ? 50  ILE D CB  1 
ATOM   12677 C CG1 . ILE D 1 50  ? -11.674 29.594  57.110  1.00 82.86  ? 50  ILE D CG1 1 
ATOM   12678 C CG2 . ILE D 1 50  ? -12.242 27.141  56.913  1.00 84.05  ? 50  ILE D CG2 1 
ATOM   12679 C CD1 . ILE D 1 50  ? -10.900 29.629  58.397  1.00 77.21  ? 50  ILE D CD1 1 
ATOM   12680 N N   . LYS D 1 51  ? -15.291 29.944  57.629  1.00 77.85  ? 51  LYS D N   1 
ATOM   12681 C CA  . LYS D 1 51  ? -16.020 31.058  58.203  1.00 72.00  ? 51  LYS D CA  1 
ATOM   12682 C C   . LYS D 1 51  ? -15.292 31.484  59.465  1.00 73.14  ? 51  LYS D C   1 
ATOM   12683 O O   . LYS D 1 51  ? -15.012 30.651  60.333  1.00 81.85  ? 51  LYS D O   1 
ATOM   12684 C CB  . LYS D 1 51  ? -17.470 30.679  58.494  1.00 77.13  ? 51  LYS D CB  1 
ATOM   12685 C CG  . LYS D 1 51  ? -18.244 30.261  57.261  1.00 79.96  ? 51  LYS D CG  1 
ATOM   12686 C CD  . LYS D 1 51  ? -19.054 31.406  56.689  1.00 81.00  ? 51  LYS D CD  1 
ATOM   12687 C CE  . LYS D 1 51  ? -19.355 31.197  55.218  1.00 84.20  ? 51  LYS D CE  1 
ATOM   12688 N NZ  . LYS D 1 51  ? -18.205 30.593  54.498  1.00 94.36  ? 51  LYS D NZ  1 
ATOM   12689 N N   . LEU D 1 52  ? -14.968 32.769  59.551  1.00 69.01  ? 52  LEU D N   1 
ATOM   12690 C CA  . LEU D 1 52  ? -14.261 33.325  60.695  1.00 71.89  ? 52  LEU D CA  1 
ATOM   12691 C C   . LEU D 1 52  ? -15.053 34.502  61.243  1.00 70.09  ? 52  LEU D C   1 
ATOM   12692 O O   . LEU D 1 52  ? -15.577 35.315  60.477  1.00 66.30  ? 52  LEU D O   1 
ATOM   12693 C CB  . LEU D 1 52  ? -12.847 33.772  60.307  1.00 71.81  ? 52  LEU D CB  1 
ATOM   12694 C CG  . LEU D 1 52  ? -11.807 32.659  60.144  1.00 69.23  ? 52  LEU D CG  1 
ATOM   12695 C CD1 . LEU D 1 52  ? -10.458 33.214  59.707  1.00 62.29  ? 52  LEU D CD1 1 
ATOM   12696 C CD2 . LEU D 1 52  ? -11.661 31.865  61.425  1.00 72.23  ? 52  LEU D CD2 1 
ATOM   12697 N N   . ASN D 1 53  ? -15.142 34.590  62.568  1.00 71.35  ? 53  ASN D N   1 
ATOM   12698 C CA  . ASN D 1 53  ? -15.922 35.621  63.237  1.00 67.72  ? 53  ASN D CA  1 
ATOM   12699 C C   . ASN D 1 53  ? -15.010 36.462  64.116  1.00 63.47  ? 53  ASN D C   1 
ATOM   12700 O O   . ASN D 1 53  ? -14.058 35.952  64.711  1.00 67.38  ? 53  ASN D O   1 
ATOM   12701 C CB  . ASN D 1 53  ? -17.034 34.994  64.064  1.00 62.60  ? 53  ASN D CB  1 
ATOM   12702 C CG  . ASN D 1 53  ? -18.107 34.386  63.201  1.00 68.41  ? 53  ASN D CG  1 
ATOM   12703 O OD1 . ASN D 1 53  ? -19.076 33.827  63.697  1.00 75.53  ? 53  ASN D OD1 1 
ATOM   12704 N ND2 . ASN D 1 53  ? -17.945 34.506  61.890  1.00 70.30  ? 53  ASN D ND2 1 
ATOM   12705 N N   . PHE D 1 54  ? -15.308 37.758  64.194  1.00 61.43  ? 54  PHE D N   1 
ATOM   12706 C CA  . PHE D 1 54  ? -14.410 38.714  64.824  1.00 60.09  ? 54  PHE D CA  1 
ATOM   12707 C C   . PHE D 1 54  ? -15.187 39.670  65.710  1.00 62.38  ? 54  PHE D C   1 
ATOM   12708 O O   . PHE D 1 54  ? -16.324 40.044  65.409  1.00 61.01  ? 54  PHE D O   1 
ATOM   12709 C CB  . PHE D 1 54  ? -13.638 39.524  63.782  1.00 62.47  ? 54  PHE D CB  1 
ATOM   12710 C CG  . PHE D 1 54  ? -12.864 38.682  62.826  1.00 64.31  ? 54  PHE D CG  1 
ATOM   12711 C CD1 . PHE D 1 54  ? -11.740 37.989  63.244  1.00 61.35  ? 54  PHE D CD1 1 
ATOM   12712 C CD2 . PHE D 1 54  ? -13.282 38.554  61.518  1.00 60.38  ? 54  PHE D CD2 1 
ATOM   12713 C CE1 . PHE D 1 54  ? -11.035 37.204  62.359  1.00 69.17  ? 54  PHE D CE1 1 
ATOM   12714 C CE2 . PHE D 1 54  ? -12.586 37.770  60.630  1.00 63.55  ? 54  PHE D CE2 1 
ATOM   12715 C CZ  . PHE D 1 54  ? -11.463 37.091  61.048  1.00 70.27  ? 54  PHE D CZ  1 
ATOM   12716 N N   . ASN D 1 55  ? -14.543 40.078  66.798  1.00 63.46  ? 55  ASN D N   1 
ATOM   12717 C CA  . ASN D 1 55  ? -15.071 41.083  67.709  1.00 59.85  ? 55  ASN D CA  1 
ATOM   12718 C C   . ASN D 1 55  ? -14.186 42.318  67.659  1.00 59.17  ? 55  ASN D C   1 
ATOM   12719 O O   . ASN D 1 55  ? -12.953 42.211  67.696  1.00 53.64  ? 55  ASN D O   1 
ATOM   12720 C CB  . ASN D 1 55  ? -15.151 40.549  69.139  1.00 57.80  ? 55  ASN D CB  1 
ATOM   12721 C CG  . ASN D 1 55  ? -15.798 41.533  70.084  1.00 60.18  ? 55  ASN D CG  1 
ATOM   12722 O OD1 . ASN D 1 55  ? -17.023 41.575  70.212  1.00 65.86  ? 55  ASN D OD1 1 
ATOM   12723 N ND2 . ASN D 1 55  ? -14.979 42.331  70.758  1.00 58.20  ? 55  ASN D ND2 1 
ATOM   12724 N N   . LEU D 1 56  ? -14.822 43.485  67.594  1.00 56.00  ? 56  LEU D N   1 
ATOM   12725 C CA  . LEU D 1 56  ? -14.134 44.768  67.502  1.00 58.51  ? 56  LEU D CA  1 
ATOM   12726 C C   . LEU D 1 56  ? -14.645 45.666  68.620  1.00 57.08  ? 56  LEU D C   1 
ATOM   12727 O O   . LEU D 1 56  ? -15.810 46.075  68.600  1.00 64.11  ? 56  LEU D O   1 
ATOM   12728 C CB  . LEU D 1 56  ? -14.378 45.408  66.134  1.00 56.01  ? 56  LEU D CB  1 
ATOM   12729 C CG  . LEU D 1 56  ? -13.189 45.390  65.176  1.00 63.64  ? 56  LEU D CG  1 
ATOM   12730 C CD1 . LEU D 1 56  ? -12.689 43.973  64.951  1.00 62.59  ? 56  LEU D CD1 1 
ATOM   12731 C CD2 . LEU D 1 56  ? -13.567 46.041  63.863  1.00 61.30  ? 56  LEU D CD2 1 
ATOM   12732 N N   . THR D 1 57  ? -13.799 45.980  69.595  1.00 46.55  ? 57  THR D N   1 
ATOM   12733 C CA  . THR D 1 57  ? -14.242 46.892  70.641  1.00 48.48  ? 57  THR D CA  1 
ATOM   12734 C C   . THR D 1 57  ? -14.305 48.321  70.109  1.00 48.85  ? 57  THR D C   1 
ATOM   12735 O O   . THR D 1 57  ? -13.453 48.722  69.312  1.00 51.28  ? 57  THR D O   1 
ATOM   12736 C CB  . THR D 1 57  ? -13.325 46.851  71.857  1.00 48.51  ? 57  THR D CB  1 
ATOM   12737 O OG1 . THR D 1 57  ? -11.972 47.067  71.443  1.00 59.97  ? 57  THR D OG1 1 
ATOM   12738 C CG2 . THR D 1 57  ? -13.446 45.519  72.552  1.00 52.10  ? 57  THR D CG2 1 
ATOM   12739 N N   . PRO D 1 58  ? -15.284 49.116  70.556  1.00 52.07  ? 58  PRO D N   1 
ATOM   12740 C CA  . PRO D 1 58  ? -15.399 50.503  70.065  1.00 55.51  ? 58  PRO D CA  1 
ATOM   12741 C C   . PRO D 1 58  ? -14.181 51.377  70.317  1.00 54.27  ? 58  PRO D C   1 
ATOM   12742 O O   . PRO D 1 58  ? -13.850 52.214  69.469  1.00 59.58  ? 58  PRO D O   1 
ATOM   12743 C CB  . PRO D 1 58  ? -16.621 51.022  70.831  1.00 53.60  ? 58  PRO D CB  1 
ATOM   12744 C CG  . PRO D 1 58  ? -17.429 49.787  71.104  1.00 52.14  ? 58  PRO D CG  1 
ATOM   12745 C CD  . PRO D 1 58  ? -16.403 48.759  71.445  1.00 48.58  ? 58  PRO D CD  1 
ATOM   12746 N N   . VAL D 1 59  ? -13.521 51.240  71.467  1.00 49.56  ? 59  VAL D N   1 
ATOM   12747 C CA  . VAL D 1 59  ? -12.332 52.046  71.723  1.00 55.62  ? 59  VAL D CA  1 
ATOM   12748 C C   . VAL D 1 59  ? -11.240 51.711  70.708  1.00 54.13  ? 59  VAL D C   1 
ATOM   12749 O O   . VAL D 1 59  ? -10.475 52.585  70.281  1.00 47.56  ? 59  VAL D O   1 
ATOM   12750 C CB  . VAL D 1 59  ? -11.863 51.844  73.178  1.00 50.88  ? 59  VAL D CB  1 
ATOM   12751 C CG1 . VAL D 1 59  ? -11.958 50.389  73.544  1.00 46.58  ? 59  VAL D CG1 1 
ATOM   12752 C CG2 . VAL D 1 59  ? -10.439 52.367  73.378  1.00 57.48  ? 59  VAL D CG2 1 
ATOM   12753 N N   . LEU D 1 60  ? -11.172 50.445  70.280  1.00 48.41  ? 60  LEU D N   1 
ATOM   12754 C CA  . LEU D 1 60  ? -10.189 50.066  69.271  1.00 50.26  ? 60  LEU D CA  1 
ATOM   12755 C C   . LEU D 1 60  ? -10.511 50.688  67.921  1.00 51.45  ? 60  LEU D C   1 
ATOM   12756 O O   . LEU D 1 60  ? -9.611  51.184  67.235  1.00 61.36  ? 60  LEU D O   1 
ATOM   12757 C CB  . LEU D 1 60  ? -10.104 48.545  69.149  1.00 55.24  ? 60  LEU D CB  1 
ATOM   12758 C CG  . LEU D 1 60  ? -9.231  48.037  67.996  1.00 52.42  ? 60  LEU D CG  1 
ATOM   12759 C CD1 . LEU D 1 60  ? -7.806  48.545  68.129  1.00 45.57  ? 60  LEU D CD1 1 
ATOM   12760 C CD2 . LEU D 1 60  ? -9.251  46.525  67.946  1.00 46.10  ? 60  LEU D CD2 1 
ATOM   12761 N N   . ILE D 1 61  ? -11.785 50.675  67.524  1.00 48.11  ? 61  ILE D N   1 
ATOM   12762 C CA  . ILE D 1 61  ? -12.166 51.260  66.240  1.00 58.65  ? 61  ILE D CA  1 
ATOM   12763 C C   . ILE D 1 61  ? -11.824 52.746  66.204  1.00 63.90  ? 61  ILE D C   1 
ATOM   12764 O O   . ILE D 1 61  ? -11.260 53.240  65.219  1.00 60.34  ? 61  ILE D O   1 
ATOM   12765 C CB  . ILE D 1 61  ? -13.660 51.009  65.957  1.00 54.83  ? 61  ILE D CB  1 
ATOM   12766 C CG1 . ILE D 1 61  ? -13.962 49.509  65.984  1.00 55.94  ? 61  ILE D CG1 1 
ATOM   12767 C CG2 . ILE D 1 61  ? -14.058 51.609  64.622  1.00 55.59  ? 61  ILE D CG2 1 
ATOM   12768 C CD1 . ILE D 1 61  ? -15.377 49.184  66.398  1.00 54.16  ? 61  ILE D CD1 1 
ATOM   12769 N N   . ASP D 1 62  ? -12.142 53.478  67.277  1.00 65.44  ? 62  ASP D N   1 
ATOM   12770 C CA  . ASP D 1 62  ? -11.825 54.904  67.322  1.00 64.45  ? 62  ASP D CA  1 
ATOM   12771 C C   . ASP D 1 62  ? -10.333 55.127  67.148  1.00 60.15  ? 62  ASP D C   1 
ATOM   12772 O O   . ASP D 1 62  ? -9.908  56.017  66.402  1.00 63.51  ? 62  ASP D O   1 
ATOM   12773 C CB  . ASP D 1 62  ? -12.299 55.513  68.642  1.00 63.52  ? 62  ASP D CB  1 
ATOM   12774 C CG  . ASP D 1 62  ? -13.745 55.962  68.595  1.00 74.85  ? 62  ASP D CG  1 
ATOM   12775 O OD1 . ASP D 1 62  ? -14.022 57.062  68.060  1.00 77.53  ? 62  ASP D OD1 1 
ATOM   12776 O OD2 . ASP D 1 62  ? -14.605 55.222  69.118  1.00 72.85  ? 62  ASP D OD2 1 
ATOM   12777 N N   . GLN D 1 63  ? -9.523  54.309  67.825  1.00 57.85  ? 63  GLN D N   1 
ATOM   12778 C CA  . GLN D 1 63  ? -8.072  54.464  67.772  1.00 61.56  ? 63  GLN D CA  1 
ATOM   12779 C C   . GLN D 1 63  ? -7.531  54.199  66.375  1.00 66.44  ? 63  GLN D C   1 
ATOM   12780 O O   . GLN D 1 63  ? -6.588  54.864  65.928  1.00 57.95  ? 63  GLN D O   1 
ATOM   12781 C CB  . GLN D 1 63  ? -7.412  53.531  68.780  1.00 54.55  ? 63  GLN D CB  1 
ATOM   12782 C CG  . GLN D 1 63  ? -7.572  53.975  70.211  1.00 53.15  ? 63  GLN D CG  1 
ATOM   12783 C CD  . GLN D 1 63  ? -6.773  53.121  71.162  1.00 53.36  ? 63  GLN D CD  1 
ATOM   12784 O OE1 . GLN D 1 63  ? -5.616  53.423  71.452  1.00 66.58  ? 63  GLN D OE1 1 
ATOM   12785 N NE2 . GLN D 1 63  ? -7.376  52.042  71.646  1.00 49.71  ? 63  GLN D NE2 1 
ATOM   12786 N N   . ILE D 1 64  ? -8.111  53.228  65.669  1.00 67.08  ? 64  ILE D N   1 
ATOM   12787 C CA  . ILE D 1 64  ? -7.666  52.969  64.306  1.00 59.24  ? 64  ILE D CA  1 
ATOM   12788 C C   . ILE D 1 64  ? -8.048  54.127  63.402  1.00 63.42  ? 64  ILE D C   1 
ATOM   12789 O O   . ILE D 1 64  ? -7.250  54.565  62.565  1.00 72.69  ? 64  ILE D O   1 
ATOM   12790 C CB  . ILE D 1 64  ? -8.249  51.652  63.779  1.00 63.79  ? 64  ILE D CB  1 
ATOM   12791 C CG1 . ILE D 1 64  ? -7.430  50.472  64.286  1.00 62.96  ? 64  ILE D CG1 1 
ATOM   12792 C CG2 . ILE D 1 64  ? -8.185  51.655  62.257  1.00 72.97  ? 64  ILE D CG2 1 
ATOM   12793 C CD1 . ILE D 1 64  ? -8.184  49.165  64.276  1.00 63.09  ? 64  ILE D CD1 1 
ATOM   12794 N N   . GLN D 1 65  ? -9.279  54.627  63.539  1.00 65.33  ? 65  GLN D N   1 
ATOM   12795 C CA  . GLN D 1 65  ? -9.729  55.728  62.695  1.00 68.10  ? 65  GLN D CA  1 
ATOM   12796 C C   . GLN D 1 65  ? -8.771  56.905  62.788  1.00 76.87  ? 65  GLN D C   1 
ATOM   12797 O O   . GLN D 1 65  ? -8.342  57.451  61.766  1.00 78.77  ? 65  GLN D O   1 
ATOM   12798 C CB  . GLN D 1 65  ? -11.150 56.153  63.076  1.00 66.41  ? 65  GLN D CB  1 
ATOM   12799 C CG  . GLN D 1 65  ? -12.234 55.452  62.265  1.00 75.80  ? 65  GLN D CG  1 
ATOM   12800 C CD  . GLN D 1 65  ? -13.641 55.743  62.758  1.00 80.23  ? 65  GLN D CD  1 
ATOM   12801 O OE1 . GLN D 1 65  ? -14.622 55.364  62.115  1.00 75.11  ? 65  GLN D OE1 1 
ATOM   12802 N NE2 . GLN D 1 65  ? -13.749 56.405  63.906  1.00 77.21  ? 65  GLN D NE2 1 
ATOM   12803 N N   . GLU D 1 66  ? -8.402  57.288  64.015  1.00 77.44  ? 66  GLU D N   1 
ATOM   12804 C CA  . GLU D 1 66  ? -7.461  58.389  64.204  1.00 73.45  ? 66  GLU D CA  1 
ATOM   12805 C C   . GLU D 1 66  ? -6.163  58.128  63.456  1.00 72.02  ? 66  GLU D C   1 
ATOM   12806 O O   . GLU D 1 66  ? -5.659  59.000  62.738  1.00 76.73  ? 66  GLU D O   1 
ATOM   12807 C CB  . GLU D 1 66  ? -7.184  58.603  65.692  1.00 70.55  ? 66  GLU D CB  1 
ATOM   12808 C CG  . GLU D 1 66  ? -7.154  60.068  66.101  1.00 82.61  ? 66  GLU D CG  1 
ATOM   12809 C CD  . GLU D 1 66  ? -6.964  60.263  67.596  1.00 88.26  ? 66  GLU D CD  1 
ATOM   12810 O OE1 . GLU D 1 66  ? -7.855  59.846  68.369  1.00 85.09  ? 66  GLU D OE1 1 
ATOM   12811 O OE2 . GLU D 1 66  ? -5.930  60.840  67.999  1.00 81.90  ? 66  GLU D OE2 1 
ATOM   12812 N N   . TYR D 1 67  ? -5.613  56.923  63.604  1.00 66.55  ? 67  TYR D N   1 
ATOM   12813 C CA  . TYR D 1 67  ? -4.371  56.600  62.914  1.00 69.98  ? 67  TYR D CA  1 
ATOM   12814 C C   . TYR D 1 67  ? -4.543  56.697  61.402  1.00 73.33  ? 67  TYR D C   1 
ATOM   12815 O O   . TYR D 1 67  ? -3.631  57.141  60.695  1.00 74.47  ? 67  TYR D O   1 
ATOM   12816 C CB  . TYR D 1 67  ? -3.894  55.209  63.317  1.00 60.00  ? 67  TYR D CB  1 
ATOM   12817 C CG  . TYR D 1 67  ? -2.998  55.187  64.535  1.00 66.26  ? 67  TYR D CG  1 
ATOM   12818 C CD1 . TYR D 1 67  ? -1.731  55.764  64.516  1.00 64.22  ? 67  TYR D CD1 1 
ATOM   12819 C CD2 . TYR D 1 67  ? -3.420  54.577  65.706  1.00 70.92  ? 67  TYR D CD2 1 
ATOM   12820 C CE1 . TYR D 1 67  ? -0.915  55.728  65.642  1.00 61.78  ? 67  TYR D CE1 1 
ATOM   12821 C CE2 . TYR D 1 67  ? -2.621  54.537  66.823  1.00 60.82  ? 67  TYR D CE2 1 
ATOM   12822 C CZ  . TYR D 1 67  ? -1.378  55.106  66.796  1.00 61.52  ? 67  TYR D CZ  1 
ATOM   12823 O OH  . TYR D 1 67  ? -0.634  55.031  67.949  1.00 65.89  ? 67  TYR D OH  1 
ATOM   12824 N N   . ALA D 1 68  ? -5.713  56.307  60.889  1.00 71.51  ? 68  ALA D N   1 
ATOM   12825 C CA  . ALA D 1 68  ? -5.926  56.326  59.445  1.00 73.08  ? 68  ALA D CA  1 
ATOM   12826 C C   . ALA D 1 68  ? -6.032  57.751  58.920  1.00 76.55  ? 68  ALA D C   1 
ATOM   12827 O O   . ALA D 1 68  ? -5.565  58.047  57.813  1.00 78.94  ? 68  ALA D O   1 
ATOM   12828 C CB  . ALA D 1 68  ? -7.178  55.529  59.082  1.00 59.22  ? 68  ALA D CB  1 
ATOM   12829 N N   . GLN D 1 69  ? -6.639  58.645  59.697  1.00 78.75  ? 69  GLN D N   1 
ATOM   12830 C CA  . GLN D 1 69  ? -6.732  60.047  59.315  1.00 76.08  ? 69  GLN D CA  1 
ATOM   12831 C C   . GLN D 1 69  ? -5.435  60.814  59.546  1.00 77.10  ? 69  GLN D C   1 
ATOM   12832 O O   . GLN D 1 69  ? -5.397  62.014  59.262  1.00 82.06  ? 69  GLN D O   1 
ATOM   12833 C CB  . GLN D 1 69  ? -7.874  60.734  60.076  1.00 83.92  ? 69  GLN D CB  1 
ATOM   12834 C CG  . GLN D 1 69  ? -9.136  59.889  60.249  1.00 79.14  ? 69  GLN D CG  1 
ATOM   12835 C CD  . GLN D 1 69  ? -10.129 60.511  61.221  1.00 86.22  ? 69  GLN D CD  1 
ATOM   12836 O OE1 . GLN D 1 69  ? -10.004 61.678  61.599  1.00 88.49  ? 69  GLN D OE1 1 
ATOM   12837 N NE2 . GLN D 1 69  ? -11.108 59.722  61.648  1.00 84.03  ? 69  GLN D NE2 1 
ATOM   12838 N N   . GLY D 1 70  ? -4.383  60.160  60.044  1.00 77.40  ? 70  GLY D N   1 
ATOM   12839 C CA  . GLY D 1 70  ? -3.128  60.829  60.338  1.00 75.23  ? 70  GLY D CA  1 
ATOM   12840 C C   . GLY D 1 70  ? -3.160  61.770  61.523  1.00 81.78  ? 70  GLY D C   1 
ATOM   12841 O O   . GLY D 1 70  ? -2.212  62.541  61.710  1.00 77.34  ? 70  GLY D O   1 
ATOM   12842 N N   . LYS D 1 71  ? -4.218  61.718  62.335  1.00 79.19  ? 71  LYS D N   1 
ATOM   12843 C CA  . LYS D 1 71  ? -4.422  62.632  63.451  1.00 76.69  ? 71  LYS D CA  1 
ATOM   12844 C C   . LYS D 1 71  ? -3.846  62.119  64.767  1.00 77.66  ? 71  LYS D C   1 
ATOM   12845 O O   . LYS D 1 71  ? -3.938  62.819  65.781  1.00 85.11  ? 71  LYS D O   1 
ATOM   12846 C CB  . LYS D 1 71  ? -5.921  62.916  63.639  1.00 81.18  ? 71  LYS D CB  1 
ATOM   12847 C CG  . LYS D 1 71  ? -6.395  64.243  63.049  1.00 87.31  ? 71  LYS D CG  1 
ATOM   12848 C CD  . LYS D 1 71  ? -7.348  64.979  63.993  1.00 85.62  ? 71  LYS D CD  1 
ATOM   12849 C CE  . LYS D 1 71  ? -7.304  66.484  63.742  1.00 82.97  ? 71  LYS D CE  1 
ATOM   12850 N NZ  . LYS D 1 71  ? -8.162  67.250  64.690  1.00 81.46  ? 71  LYS D NZ  1 
ATOM   12851 N N   . ALA D 1 72  ? -3.268  60.924  64.788  1.00 67.42  ? 72  ALA D N   1 
ATOM   12852 C CA  . ALA D 1 72  ? -2.753  60.417  66.045  1.00 69.55  ? 72  ALA D CA  1 
ATOM   12853 C C   . ALA D 1 72  ? -1.376  61.008  66.340  1.00 76.26  ? 72  ALA D C   1 
ATOM   12854 O O   . ALA D 1 72  ? -0.671  61.490  65.448  1.00 79.55  ? 72  ALA D O   1 
ATOM   12855 C CB  . ALA D 1 72  ? -2.692  58.892  66.022  1.00 70.22  ? 72  ALA D CB  1 
ATOM   12856 N N   . LYS D 1 73  ? -1.005  60.972  67.617  1.00 72.56  ? 73  LYS D N   1 
ATOM   12857 C CA  . LYS D 1 73  ? 0.256   61.522  68.101  1.00 63.71  ? 73  LYS D CA  1 
ATOM   12858 C C   . LYS D 1 73  ? 0.980   60.418  68.870  1.00 66.98  ? 73  LYS D C   1 
ATOM   12859 O O   . LYS D 1 73  ? 1.083   60.452  70.097  1.00 69.62  ? 73  LYS D O   1 
ATOM   12860 C CB  . LYS D 1 73  ? 0.022   62.753  68.973  1.00 66.54  ? 73  LYS D CB  1 
ATOM   12861 C CG  . LYS D 1 73  ? 0.229   64.077  68.263  1.00 66.66  ? 73  LYS D CG  1 
ATOM   12862 C CD  . LYS D 1 73  ? 1.575   64.113  67.551  1.00 82.95  ? 73  LYS D CD  1 
ATOM   12863 C CE  . LYS D 1 73  ? 1.841   65.473  66.904  1.00 92.69  ? 73  LYS D CE  1 
ATOM   12864 N NZ  . LYS D 1 73  ? 2.851   65.419  65.803  1.00 81.29  ? 73  LYS D NZ  1 
ATOM   12865 N N   . ASP D 1 74  ? 1.459   59.420  68.137  1.00 68.93  ? 74  ASP D N   1 
ATOM   12866 C CA  . ASP D 1 74  ? 2.215   58.318  68.723  1.00 64.02  ? 74  ASP D CA  1 
ATOM   12867 C C   . ASP D 1 74  ? 3.645   58.783  68.963  1.00 64.84  ? 74  ASP D C   1 
ATOM   12868 O O   . ASP D 1 74  ? 4.423   58.929  68.014  1.00 66.51  ? 74  ASP D O   1 
ATOM   12869 C CB  . ASP D 1 74  ? 2.170   57.107  67.795  1.00 69.72  ? 74  ASP D CB  1 
ATOM   12870 C CG  . ASP D 1 74  ? 2.565   55.819  68.487  1.00 68.40  ? 74  ASP D CG  1 
ATOM   12871 O OD1 . ASP D 1 74  ? 3.734   55.696  68.918  1.00 71.02  ? 74  ASP D OD1 1 
ATOM   12872 O OD2 . ASP D 1 74  ? 1.702   54.923  68.586  1.00 64.74  ? 74  ASP D OD2 1 
ATOM   12873 N N   . VAL D 1 75  ? 3.994   59.019  70.232  1.00 61.34  ? 75  VAL D N   1 
ATOM   12874 C CA  . VAL D 1 75  ? 5.327   59.521  70.553  1.00 55.96  ? 75  VAL D CA  1 
ATOM   12875 C C   . VAL D 1 75  ? 6.396   58.535  70.107  1.00 54.36  ? 75  VAL D C   1 
ATOM   12876 O O   . VAL D 1 75  ? 7.477   58.940  69.665  1.00 60.52  ? 75  VAL D O   1 
ATOM   12877 C CB  . VAL D 1 75  ? 5.425   59.842  72.061  1.00 51.81  ? 75  VAL D CB  1 
ATOM   12878 C CG1 . VAL D 1 75  ? 4.151   60.506  72.528  1.00 56.98  ? 75  VAL D CG1 1 
ATOM   12879 C CG2 . VAL D 1 75  ? 5.707   58.597  72.892  1.00 57.20  ? 75  VAL D CG2 1 
ATOM   12880 N N   . PHE D 1 76  ? 6.108   57.232  70.173  1.00 55.77  ? 76  PHE D N   1 
ATOM   12881 C CA  . PHE D 1 76  ? 7.108   56.247  69.781  1.00 59.02  ? 76  PHE D CA  1 
ATOM   12882 C C   . PHE D 1 76  ? 7.282   56.214  68.271  1.00 66.85  ? 76  PHE D C   1 
ATOM   12883 O O   . PHE D 1 76  ? 8.402   56.044  67.777  1.00 66.12  ? 76  PHE D O   1 
ATOM   12884 C CB  . PHE D 1 76  ? 6.733   54.863  70.308  1.00 57.57  ? 76  PHE D CB  1 
ATOM   12885 C CG  . PHE D 1 76  ? 7.804   53.826  70.099  1.00 65.18  ? 76  PHE D CG  1 
ATOM   12886 C CD1 . PHE D 1 76  ? 8.966   53.840  70.857  1.00 67.57  ? 76  PHE D CD1 1 
ATOM   12887 C CD2 . PHE D 1 76  ? 7.657   52.848  69.127  1.00 70.32  ? 76  PHE D CD2 1 
ATOM   12888 C CE1 . PHE D 1 76  ? 9.953   52.888  70.658  1.00 68.94  ? 76  PHE D CE1 1 
ATOM   12889 C CE2 . PHE D 1 76  ? 8.641   51.895  68.923  1.00 63.96  ? 76  PHE D CE2 1 
ATOM   12890 C CZ  . PHE D 1 76  ? 9.788   51.916  69.688  1.00 68.11  ? 76  PHE D CZ  1 
ATOM   12891 N N   . LEU D 1 77  ? 6.185   56.382  67.522  1.00 66.43  ? 77  LEU D N   1 
ATOM   12892 C CA  . LEU D 1 77  ? 6.263   56.365  66.064  1.00 62.91  ? 77  LEU D CA  1 
ATOM   12893 C C   . LEU D 1 77  ? 7.065   57.540  65.521  1.00 65.16  ? 77  LEU D C   1 
ATOM   12894 O O   . LEU D 1 77  ? 7.712   57.413  64.475  1.00 62.90  ? 77  LEU D O   1 
ATOM   12895 C CB  . LEU D 1 77  ? 4.860   56.365  65.461  1.00 64.63  ? 77  LEU D CB  1 
ATOM   12896 C CG  . LEU D 1 77  ? 4.260   54.981  65.199  1.00 76.95  ? 77  LEU D CG  1 
ATOM   12897 C CD1 . LEU D 1 77  ? 3.193   55.049  64.103  1.00 73.70  ? 77  LEU D CD1 1 
ATOM   12898 C CD2 . LEU D 1 77  ? 5.344   53.952  64.857  1.00 61.81  ? 77  LEU D CD2 1 
ATOM   12899 N N   . GLU D 1 78  ? 7.034   58.686  66.205  1.00 68.19  ? 78  GLU D N   1 
ATOM   12900 C CA  . GLU D 1 78  ? 7.872   59.804  65.791  1.00 74.89  ? 78  GLU D CA  1 
ATOM   12901 C C   . GLU D 1 78  ? 9.345   59.524  66.055  1.00 76.95  ? 78  GLU D C   1 
ATOM   12902 O O   . GLU D 1 78  ? 10.209  60.020  65.321  1.00 81.26  ? 78  GLU D O   1 
ATOM   12903 C CB  . GLU D 1 78  ? 7.441   61.086  66.499  1.00 73.44  ? 78  GLU D CB  1 
ATOM   12904 C CG  . GLU D 1 78  ? 7.189   62.242  65.554  1.00 83.61  ? 78  GLU D CG  1 
ATOM   12905 C CD  . GLU D 1 78  ? 5.904   62.072  64.775  1.00 91.57  ? 78  GLU D CD  1 
ATOM   12906 O OE1 . GLU D 1 78  ? 5.972   61.933  63.535  1.00 93.34  ? 78  GLU D OE1 1 
ATOM   12907 O OE2 . GLU D 1 78  ? 4.826   62.074  65.408  1.00 92.83  ? 78  GLU D OE2 1 
ATOM   12908 N N   . ALA D 1 79  ? 9.652   58.733  67.087  1.00 63.42  ? 79  ALA D N   1 
ATOM   12909 C CA  . ALA D 1 79  ? 11.038  58.338  67.318  1.00 76.64  ? 79  ALA D CA  1 
ATOM   12910 C C   . ALA D 1 79  ? 11.578  57.518  66.150  1.00 74.95  ? 79  ALA D C   1 
ATOM   12911 O O   . ALA D 1 79  ? 12.712  57.729  65.707  1.00 76.43  ? 79  ALA D O   1 
ATOM   12912 C CB  . ALA D 1 79  ? 11.151  57.557  68.628  1.00 75.35  ? 79  ALA D CB  1 
ATOM   12913 N N   . ILE D 1 80  ? 10.772  56.590  65.626  1.00 68.56  ? 80  ILE D N   1 
ATOM   12914 C CA  . ILE D 1 80  ? 11.217  55.766  64.506  1.00 71.33  ? 80  ILE D CA  1 
ATOM   12915 C C   . ILE D 1 80  ? 11.280  56.588  63.226  1.00 68.72  ? 80  ILE D C   1 
ATOM   12916 O O   . ILE D 1 80  ? 12.201  56.432  62.417  1.00 67.76  ? 80  ILE D O   1 
ATOM   12917 C CB  . ILE D 1 80  ? 10.303  54.539  64.344  1.00 71.06  ? 80  ILE D CB  1 
ATOM   12918 C CG1 . ILE D 1 80  ? 10.568  53.524  65.452  1.00 68.83  ? 80  ILE D CG1 1 
ATOM   12919 C CG2 . ILE D 1 80  ? 10.517  53.876  62.990  1.00 76.08  ? 80  ILE D CG2 1 
ATOM   12920 C CD1 . ILE D 1 80  ? 9.603   52.366  65.436  1.00 68.24  ? 80  ILE D CD1 1 
ATOM   12921 N N   . ARG D 1 81  ? 10.311  57.481  63.023  1.00 67.83  ? 81  ARG D N   1 
ATOM   12922 C CA  . ARG D 1 81  ? 10.228  58.199  61.754  1.00 73.45  ? 81  ARG D CA  1 
ATOM   12923 C C   . ARG D 1 81  ? 11.360  59.215  61.622  1.00 78.59  ? 81  ARG D C   1 
ATOM   12924 O O   . ARG D 1 81  ? 11.997  59.311  60.564  1.00 76.56  ? 81  ARG D O   1 
ATOM   12925 C CB  . ARG D 1 81  ? 8.843   58.858  61.641  1.00 71.01  ? 81  ARG D CB  1 
ATOM   12926 C CG  . ARG D 1 81  ? 8.501   59.654  60.356  1.00 77.20  ? 81  ARG D CG  1 
ATOM   12927 C CD  . ARG D 1 81  ? 9.186   61.022  60.266  1.00 93.61  ? 81  ARG D CD  1 
ATOM   12928 N NE  . ARG D 1 81  ? 8.445   62.059  60.966  1.00 84.64  ? 81  ARG D NE  1 
ATOM   12929 C CZ  . ARG D 1 81  ? 8.995   63.145  61.486  1.00 81.64  ? 81  ARG D CZ  1 
ATOM   12930 N NH1 . ARG D 1 81  ? 10.290  63.398  61.358  1.00 73.57  ? 81  ARG D NH1 1 
ATOM   12931 N NH2 . ARG D 1 81  ? 8.228   63.999  62.154  1.00 90.60  ? 81  ARG D NH2 1 
ATOM   12932 N N   . LYS D 1 82  ? 11.628  59.974  62.682  1.00 74.52  ? 82  LYS D N   1 
ATOM   12933 C CA  . LYS D 1 82  ? 12.651  61.009  62.630  1.00 75.07  ? 82  LYS D CA  1 
ATOM   12934 C C   . LYS D 1 82  ? 14.011  60.422  62.261  1.00 74.18  ? 82  LYS D C   1 
ATOM   12935 O O   . LYS D 1 82  ? 14.335  59.284  62.611  1.00 73.01  ? 82  LYS D O   1 
ATOM   12936 C CB  . LYS D 1 82  ? 12.742  61.725  63.979  1.00 80.60  ? 82  LYS D CB  1 
ATOM   12937 C CG  . LYS D 1 82  ? 12.116  63.110  63.986  1.00 84.43  ? 82  LYS D CG  1 
ATOM   12938 C CD  . LYS D 1 82  ? 11.533  63.480  65.342  1.00 80.19  ? 82  LYS D CD  1 
ATOM   12939 C CE  . LYS D 1 82  ? 12.251  62.781  66.476  1.00 80.18  ? 82  LYS D CE  1 
ATOM   12940 N NZ  . LYS D 1 82  ? 12.186  63.588  67.717  1.00 88.75  ? 82  LYS D NZ  1 
ATOM   12941 N N   . ASP D 1 83  ? 14.798  61.204  61.524  1.00 71.89  ? 83  ASP D N   1 
ATOM   12942 C CA  . ASP D 1 83  ? 16.188  60.842  61.288  1.00 66.76  ? 83  ASP D CA  1 
ATOM   12943 C C   . ASP D 1 83  ? 16.911  60.750  62.630  1.00 75.52  ? 83  ASP D C   1 
ATOM   12944 O O   . ASP D 1 83  ? 16.623  61.538  63.539  1.00 82.86  ? 83  ASP D O   1 
ATOM   12945 C CB  . ASP D 1 83  ? 16.870  61.877  60.390  1.00 69.46  ? 83  ASP D CB  1 
ATOM   12946 C CG  . ASP D 1 83  ? 18.271  61.461  59.964  1.00 72.51  ? 83  ASP D CG  1 
ATOM   12947 O OD1 . ASP D 1 83  ? 19.232  61.698  60.726  1.00 71.70  ? 83  ASP D OD1 1 
ATOM   12948 O OD2 . ASP D 1 83  ? 18.410  60.899  58.857  1.00 71.84  ? 83  ASP D OD2 1 
ATOM   12949 N N   . PRO D 1 84  ? 17.836  59.797  62.798  1.00 71.55  ? 84  PRO D N   1 
ATOM   12950 C CA  . PRO D 1 84  ? 18.519  59.639  64.091  1.00 73.92  ? 84  PRO D CA  1 
ATOM   12951 C C   . PRO D 1 84  ? 19.250  60.883  64.573  1.00 79.94  ? 84  PRO D C   1 
ATOM   12952 O O   . PRO D 1 84  ? 19.537  61.013  65.769  1.00 81.92  ? 84  PRO D O   1 
ATOM   12953 C CB  . PRO D 1 84  ? 19.495  58.493  63.812  1.00 76.75  ? 84  PRO D CB  1 
ATOM   12954 C CG  . PRO D 1 84  ? 18.767  57.666  62.802  1.00 71.29  ? 84  PRO D CG  1 
ATOM   12955 C CD  . PRO D 1 84  ? 18.153  58.688  61.884  1.00 74.24  ? 84  PRO D CD  1 
ATOM   12956 N N   . ASP D 1 85  ? 19.532  61.812  63.659  1.00 77.97  ? 85  ASP D N   1 
ATOM   12957 C CA  . ASP D 1 85  ? 20.258  63.025  64.022  1.00 80.54  ? 85  ASP D CA  1 
ATOM   12958 C C   . ASP D 1 85  ? 19.378  64.040  64.747  1.00 84.65  ? 85  ASP D C   1 
ATOM   12959 O O   . ASP D 1 85  ? 19.870  64.754  65.628  1.00 80.01  ? 85  ASP D O   1 
ATOM   12960 C CB  . ASP D 1 85  ? 20.870  63.659  62.776  1.00 77.10  ? 85  ASP D CB  1 
ATOM   12961 C CG  . ASP D 1 85  ? 21.915  62.772  62.138  1.00 86.26  ? 85  ASP D CG  1 
ATOM   12962 O OD1 . ASP D 1 85  ? 21.772  61.533  62.236  1.00 89.91  ? 85  ASP D OD1 1 
ATOM   12963 O OD2 . ASP D 1 85  ? 22.891  63.307  61.572  1.00 75.20  ? 85  ASP D OD2 1 
ATOM   12964 N N   . ASP D 1 86  ? 18.094  64.128  64.390  1.00 91.48  ? 86  ASP D N   1 
ATOM   12965 C CA  . ASP D 1 86  ? 17.143  65.012  65.058  1.00 88.36  ? 86  ASP D CA  1 
ATOM   12966 C C   . ASP D 1 86  ? 16.494  64.363  66.272  1.00 76.69  ? 86  ASP D C   1 
ATOM   12967 O O   . ASP D 1 86  ? 15.560  64.934  66.842  1.00 81.39  ? 86  ASP D O   1 
ATOM   12968 C CB  . ASP D 1 86  ? 16.045  65.468  64.087  1.00 85.25  ? 86  ASP D CB  1 
ATOM   12969 C CG  . ASP D 1 86  ? 16.566  65.742  62.689  1.00 94.24  ? 86  ASP D CG  1 
ATOM   12970 O OD1 . ASP D 1 86  ? 17.434  66.629  62.536  1.00 104.52 ? 86  ASP D OD1 1 
ATOM   12971 O OD2 . ASP D 1 86  ? 16.095  65.079  61.740  1.00 89.66  ? 86  ASP D OD2 1 
ATOM   12972 N N   . LEU D 1 87  ? 16.966  63.190  66.673  1.00 82.73  ? 87  LEU D N   1 
ATOM   12973 C CA  . LEU D 1 87  ? 16.381  62.464  67.788  1.00 87.37  ? 87  LEU D CA  1 
ATOM   12974 C C   . LEU D 1 87  ? 16.924  62.984  69.113  1.00 85.06  ? 87  LEU D C   1 
ATOM   12975 O O   . LEU D 1 87  ? 18.109  63.307  69.228  1.00 88.23  ? 87  LEU D O   1 
ATOM   12976 C CB  . LEU D 1 87  ? 16.681  60.974  67.649  1.00 86.38  ? 87  LEU D CB  1 
ATOM   12977 C CG  . LEU D 1 87  ? 15.721  60.120  66.822  1.00 80.79  ? 87  LEU D CG  1 
ATOM   12978 C CD1 . LEU D 1 87  ? 16.275  58.714  66.698  1.00 74.04  ? 87  LEU D CD1 1 
ATOM   12979 C CD2 . LEU D 1 87  ? 14.345  60.091  67.463  1.00 83.23  ? 87  LEU D CD2 1 
ATOM   12980 N N   . GLU D 1 88  ? 16.048  63.061  70.114  1.00 86.05  ? 88  GLU D N   1 
ATOM   12981 C CA  . GLU D 1 88  ? 16.458  63.414  71.465  1.00 91.69  ? 88  GLU D CA  1 
ATOM   12982 C C   . GLU D 1 88  ? 17.029  62.193  72.185  1.00 89.82  ? 88  GLU D C   1 
ATOM   12983 O O   . GLU D 1 88  ? 16.822  61.045  71.778  1.00 89.72  ? 88  GLU D O   1 
ATOM   12984 C CB  . GLU D 1 88  ? 15.284  63.990  72.258  1.00 92.70  ? 88  GLU D CB  1 
ATOM   12985 C CG  . GLU D 1 88  ? 14.415  64.971  71.474  1.00 97.93  ? 88  GLU D CG  1 
ATOM   12986 C CD  . GLU D 1 88  ? 13.286  65.563  72.311  1.00 95.62  ? 88  GLU D CD  1 
ATOM   12987 O OE1 . GLU D 1 88  ? 12.120  65.414  71.892  1.00 88.72  ? 88  GLU D OE1 1 
ATOM   12988 O OE2 . GLU D 1 88  ? 13.547  66.175  73.373  1.00 92.82  ? 88  GLU D OE2 1 
ATOM   12989 N N   . LYS D 1 89  ? 17.752  62.456  73.280  1.00 84.33  ? 89  LYS D N   1 
ATOM   12990 C CA  . LYS D 1 89  ? 18.425  61.376  74.000  1.00 83.99  ? 89  LYS D CA  1 
ATOM   12991 C C   . LYS D 1 89  ? 17.428  60.362  74.550  1.00 84.14  ? 89  LYS D C   1 
ATOM   12992 O O   . LYS D 1 89  ? 17.677  59.152  74.504  1.00 84.05  ? 89  LYS D O   1 
ATOM   12993 C CB  . LYS D 1 89  ? 19.288  61.945  75.128  1.00 80.70  ? 89  LYS D CB  1 
ATOM   12994 C CG  . LYS D 1 89  ? 20.779  62.002  74.804  1.00 78.84  ? 89  LYS D CG  1 
ATOM   12995 C CD  . LYS D 1 89  ? 21.602  62.239  76.062  1.00 80.99  ? 89  LYS D CD  1 
ATOM   12996 C CE  . LYS D 1 89  ? 21.104  63.455  76.831  1.00 82.73  ? 89  LYS D CE  1 
ATOM   12997 N NZ  . LYS D 1 89  ? 22.137  64.032  77.737  1.00 70.34  ? 89  LYS D NZ  1 
ATOM   12998 N N   . GLU D 1 90  ? 16.283  60.834  75.053  1.00 91.96  ? 90  GLU D N   1 
ATOM   12999 C CA  . GLU D 1 90  ? 15.289  59.924  75.618  1.00 91.00  ? 90  GLU D CA  1 
ATOM   13000 C C   . GLU D 1 90  ? 14.688  59.016  74.551  1.00 86.86  ? 90  GLU D C   1 
ATOM   13001 O O   . GLU D 1 90  ? 14.470  57.823  74.793  1.00 86.45  ? 90  GLU D O   1 
ATOM   13002 C CB  . GLU D 1 90  ? 14.196  60.721  76.334  1.00 81.33  ? 90  GLU D CB  1 
ATOM   13003 C CG  . GLU D 1 90  ? 14.341  62.231  76.202  1.00 83.00  ? 90  GLU D CG  1 
ATOM   13004 C CD  . GLU D 1 90  ? 13.301  62.993  77.003  1.00 95.00  ? 90  GLU D CD  1 
ATOM   13005 O OE1 . GLU D 1 90  ? 12.772  62.435  77.991  1.00 89.48  ? 90  GLU D OE1 1 
ATOM   13006 O OE2 . GLU D 1 90  ? 13.027  64.161  76.654  1.00 93.49  ? 90  GLU D OE2 1 
ATOM   13007 N N   . GLU D 1 91  ? 14.427  59.563  73.360  1.00 88.90  ? 91  GLU D N   1 
ATOM   13008 C CA  . GLU D 1 91  ? 13.831  58.773  72.285  1.00 84.17  ? 91  GLU D CA  1 
ATOM   13009 C C   . GLU D 1 91  ? 14.689  57.565  71.920  1.00 78.12  ? 91  GLU D C   1 
ATOM   13010 O O   . GLU D 1 91  ? 14.154  56.525  71.515  1.00 70.31  ? 91  GLU D O   1 
ATOM   13011 C CB  . GLU D 1 91  ? 13.607  59.653  71.054  1.00 88.46  ? 91  GLU D CB  1 
ATOM   13012 C CG  . GLU D 1 91  ? 13.441  61.137  71.363  1.00 96.07  ? 91  GLU D CG  1 
ATOM   13013 C CD  . GLU D 1 91  ? 12.970  61.937  70.162  1.00 98.19  ? 91  GLU D CD  1 
ATOM   13014 O OE1 . GLU D 1 91  ? 13.815  62.589  69.512  1.00 95.53  ? 91  GLU D OE1 1 
ATOM   13015 O OE2 . GLU D 1 91  ? 11.755  61.911  69.868  1.00 90.78  ? 91  GLU D OE2 1 
ATOM   13016 N N   . VAL D 1 92  ? 16.013  57.675  72.061  1.00 70.93  ? 92  VAL D N   1 
ATOM   13017 C CA  . VAL D 1 92  ? 16.885  56.539  71.773  1.00 69.37  ? 92  VAL D CA  1 
ATOM   13018 C C   . VAL D 1 92  ? 16.723  55.456  72.832  1.00 69.54  ? 92  VAL D C   1 
ATOM   13019 O O   . VAL D 1 92  ? 16.686  54.260  72.517  1.00 64.72  ? 92  VAL D O   1 
ATOM   13020 C CB  . VAL D 1 92  ? 18.348  56.998  71.657  1.00 73.00  ? 92  VAL D CB  1 
ATOM   13021 C CG1 . VAL D 1 92  ? 19.229  55.839  71.205  1.00 71.63  ? 92  VAL D CG1 1 
ATOM   13022 C CG2 . VAL D 1 92  ? 18.460  58.168  70.697  1.00 74.71  ? 92  VAL D CG2 1 
ATOM   13023 N N   . GLU D 1 93  ? 16.631  55.852  74.104  1.00 74.98  ? 93  GLU D N   1 
ATOM   13024 C CA  . GLU D 1 93  ? 16.392  54.874  75.159  1.00 77.50  ? 93  GLU D CA  1 
ATOM   13025 C C   . GLU D 1 93  ? 15.006  54.256  75.045  1.00 75.23  ? 93  GLU D C   1 
ATOM   13026 O O   . GLU D 1 93  ? 14.813  53.103  75.447  1.00 77.37  ? 93  GLU D O   1 
ATOM   13027 C CB  . GLU D 1 93  ? 16.559  55.517  76.533  1.00 78.50  ? 93  GLU D CB  1 
ATOM   13028 C CG  . GLU D 1 93  ? 17.588  56.628  76.560  1.00 83.00  ? 93  GLU D CG  1 
ATOM   13029 C CD  . GLU D 1 93  ? 17.292  57.671  77.621  1.00 99.08  ? 93  GLU D CD  1 
ATOM   13030 O OE1 . GLU D 1 93  ? 18.254  58.130  78.273  1.00 115.54 ? 93  GLU D OE1 1 
ATOM   13031 O OE2 . GLU D 1 93  ? 16.102  58.016  77.816  1.00 84.40  ? 93  GLU D OE2 1 
ATOM   13032 N N   . LYS D 1 94  ? 14.030  55.001  74.517  1.00 71.26  ? 94  LYS D N   1 
ATOM   13033 C CA  . LYS D 1 94  ? 12.701  54.429  74.325  1.00 71.53  ? 94  LYS D CA  1 
ATOM   13034 C C   . LYS D 1 94  ? 12.739  53.343  73.262  1.00 70.22  ? 94  LYS D C   1 
ATOM   13035 O O   . LYS D 1 94  ? 12.110  52.291  73.418  1.00 71.33  ? 94  LYS D O   1 
ATOM   13036 C CB  . LYS D 1 94  ? 11.680  55.508  73.948  1.00 75.77  ? 94  LYS D CB  1 
ATOM   13037 C CG  . LYS D 1 94  ? 11.589  56.734  74.866  1.00 80.99  ? 94  LYS D CG  1 
ATOM   13038 C CD  . LYS D 1 94  ? 12.181  56.526  76.266  1.00 86.90  ? 94  LYS D CD  1 
ATOM   13039 C CE  . LYS D 1 94  ? 11.594  57.470  77.309  1.00 89.90  ? 94  LYS D CE  1 
ATOM   13040 N NZ  . LYS D 1 94  ? 12.124  57.134  78.667  1.00 82.71  ? 94  LYS D NZ  1 
ATOM   13041 N N   . LEU D 1 95  ? 13.486  53.576  72.179  1.00 73.00  ? 95  LEU D N   1 
ATOM   13042 C CA  . LEU D 1 95  ? 13.676  52.538  71.172  1.00 70.12  ? 95  LEU D CA  1 
ATOM   13043 C C   . LEU D 1 95  ? 14.547  51.403  71.691  1.00 69.26  ? 95  LEU D C   1 
ATOM   13044 O O   . LEU D 1 95  ? 14.354  50.248  71.301  1.00 68.29  ? 95  LEU D O   1 
ATOM   13045 C CB  . LEU D 1 95  ? 14.276  53.138  69.902  1.00 68.59  ? 95  LEU D CB  1 
ATOM   13046 C CG  . LEU D 1 95  ? 13.259  53.367  68.783  1.00 76.45  ? 95  LEU D CG  1 
ATOM   13047 C CD1 . LEU D 1 95  ? 13.767  54.395  67.787  1.00 79.64  ? 95  LEU D CD1 1 
ATOM   13048 C CD2 . LEU D 1 95  ? 12.928  52.051  68.080  1.00 70.79  ? 95  LEU D CD2 1 
ATOM   13049 N N   . ILE D 1 96  ? 15.495  51.703  72.578  1.00 70.40  ? 96  ILE D N   1 
ATOM   13050 C CA  . ILE D 1 96  ? 16.279  50.643  73.206  1.00 71.14  ? 96  ILE D CA  1 
ATOM   13051 C C   . ILE D 1 96  ? 15.379  49.747  74.050  1.00 74.72  ? 96  ILE D C   1 
ATOM   13052 O O   . ILE D 1 96  ? 15.449  48.515  73.966  1.00 79.24  ? 96  ILE D O   1 
ATOM   13053 C CB  . ILE D 1 96  ? 17.424  51.248  74.037  1.00 73.86  ? 96  ILE D CB  1 
ATOM   13054 C CG1 . ILE D 1 96  ? 18.607  51.595  73.141  1.00 70.96  ? 96  ILE D CG1 1 
ATOM   13055 C CG2 . ILE D 1 96  ? 17.880  50.283  75.112  1.00 75.95  ? 96  ILE D CG2 1 
ATOM   13056 C CD1 . ILE D 1 96  ? 19.698  52.313  73.880  1.00 61.70  ? 96  ILE D CD1 1 
ATOM   13057 N N   . GLU D 1 97  ? 14.503  50.352  74.860  1.00 73.52  ? 97  GLU D N   1 
ATOM   13058 C CA  . GLU D 1 97  ? 13.623  49.567  75.725  1.00 75.17  ? 97  GLU D CA  1 
ATOM   13059 C C   . GLU D 1 97  ? 12.674  48.692  74.914  1.00 72.23  ? 97  GLU D C   1 
ATOM   13060 O O   . GLU D 1 97  ? 12.431  47.533  75.272  1.00 75.52  ? 97  GLU D O   1 
ATOM   13061 C CB  . GLU D 1 97  ? 12.834  50.491  76.653  1.00 77.73  ? 97  GLU D CB  1 
ATOM   13062 C CG  . GLU D 1 97  ? 12.558  49.898  78.032  1.00 93.26  ? 97  GLU D CG  1 
ATOM   13063 C CD  . GLU D 1 97  ? 13.763  49.982  78.954  1.00 102.58 ? 97  GLU D CD  1 
ATOM   13064 O OE1 . GLU D 1 97  ? 14.023  49.011  79.698  1.00 114.86 ? 97  GLU D OE1 1 
ATOM   13065 O OE2 . GLU D 1 97  ? 14.459  51.019  78.927  1.00 106.48 ? 97  GLU D OE2 1 
ATOM   13066 N N   . PHE D 1 98  ? 12.133  49.226  73.816  1.00 68.14  ? 98  PHE D N   1 
ATOM   13067 C CA  . PHE D 1 98  ? 11.180  48.469  73.009  1.00 68.94  ? 98  PHE D CA  1 
ATOM   13068 C C   . PHE D 1 98  ? 11.811  47.207  72.430  1.00 73.51  ? 98  PHE D C   1 
ATOM   13069 O O   . PHE D 1 98  ? 11.249  46.112  72.542  1.00 70.88  ? 98  PHE D O   1 
ATOM   13070 C CB  . PHE D 1 98  ? 10.626  49.348  71.892  1.00 61.99  ? 98  PHE D CB  1 
ATOM   13071 C CG  . PHE D 1 98  ? 9.244   48.968  71.461  1.00 68.73  ? 98  PHE D CG  1 
ATOM   13072 C CD1 . PHE D 1 98  ? 8.148   49.292  72.245  1.00 63.87  ? 98  PHE D CD1 1 
ATOM   13073 C CD2 . PHE D 1 98  ? 9.037   48.288  70.274  1.00 71.40  ? 98  PHE D CD2 1 
ATOM   13074 C CE1 . PHE D 1 98  ? 6.872   48.946  71.853  1.00 64.40  ? 98  PHE D CE1 1 
ATOM   13075 C CE2 . PHE D 1 98  ? 7.758   47.939  69.877  1.00 73.08  ? 98  PHE D CE2 1 
ATOM   13076 C CZ  . PHE D 1 98  ? 6.676   48.269  70.669  1.00 62.66  ? 98  PHE D CZ  1 
ATOM   13077 N N   . THR D 1 99  ? 12.976  47.343  71.788  1.00 72.38  ? 99  THR D N   1 
ATOM   13078 C CA  . THR D 1 99  ? 13.665  46.162  71.276  1.00 69.86  ? 99  THR D CA  1 
ATOM   13079 C C   . THR D 1 99  ? 14.005  45.198  72.399  1.00 73.62  ? 99  THR D C   1 
ATOM   13080 O O   . THR D 1 99  ? 13.832  43.983  72.254  1.00 70.07  ? 99  THR D O   1 
ATOM   13081 C CB  . THR D 1 99  ? 14.938  46.557  70.537  1.00 71.96  ? 99  THR D CB  1 
ATOM   13082 O OG1 . THR D 1 99  ? 15.981  46.784  71.493  1.00 81.33  ? 99  THR D OG1 1 
ATOM   13083 C CG2 . THR D 1 99  ? 14.719  47.793  69.727  1.00 67.59  ? 99  THR D CG2 1 
ATOM   13084 N N   . LYS D 1 100 ? 14.493  45.726  73.526  1.00 75.44  ? 100 LYS D N   1 
ATOM   13085 C CA  . LYS D 1 100 ? 14.827  44.878  74.666  1.00 73.79  ? 100 LYS D CA  1 
ATOM   13086 C C   . LYS D 1 100 ? 13.607  44.105  75.154  1.00 73.53  ? 100 LYS D C   1 
ATOM   13087 O O   . LYS D 1 100 ? 13.709  42.920  75.493  1.00 76.91  ? 100 LYS D O   1 
ATOM   13088 C CB  . LYS D 1 100 ? 15.413  45.730  75.793  1.00 74.10  ? 100 LYS D CB  1 
ATOM   13089 C CG  . LYS D 1 100 ? 16.559  45.078  76.556  1.00 73.35  ? 100 LYS D CG  1 
ATOM   13090 C CD  . LYS D 1 100 ? 16.536  45.475  78.026  1.00 79.71  ? 100 LYS D CD  1 
ATOM   13091 C CE  . LYS D 1 100 ? 15.557  44.615  78.821  1.00 79.58  ? 100 LYS D CE  1 
ATOM   13092 N NZ  . LYS D 1 100 ? 15.784  43.153  78.642  1.00 82.23  ? 100 LYS D NZ  1 
ATOM   13093 N N   . LEU D 1 101 ? 12.439  44.755  75.177  1.00 71.66  ? 101 LEU D N   1 
ATOM   13094 C CA  . LEU D 1 101 ? 11.227  44.092  75.651  1.00 72.98  ? 101 LEU D CA  1 
ATOM   13095 C C   . LEU D 1 101 ? 10.786  42.987  74.702  1.00 67.19  ? 101 LEU D C   1 
ATOM   13096 O O   . LEU D 1 101 ? 10.393  41.902  75.145  1.00 70.56  ? 101 LEU D O   1 
ATOM   13097 C CB  . LEU D 1 101 ? 10.103  45.110  75.832  1.00 72.45  ? 101 LEU D CB  1 
ATOM   13098 C CG  . LEU D 1 101 ? 8.716   44.499  76.025  1.00 75.22  ? 101 LEU D CG  1 
ATOM   13099 C CD1 . LEU D 1 101 ? 8.586   43.918  77.422  1.00 72.93  ? 101 LEU D CD1 1 
ATOM   13100 C CD2 . LEU D 1 101 ? 7.629   45.530  75.766  1.00 77.59  ? 101 LEU D CD2 1 
ATOM   13101 N N   . ASN D 1 102 ? 10.840  43.240  73.398  1.00 71.45  ? 102 ASN D N   1 
ATOM   13102 C CA  . ASN D 1 102 ? 10.440  42.257  72.403  1.00 72.97  ? 102 ASN D CA  1 
ATOM   13103 C C   . ASN D 1 102 ? 11.625  41.478  71.846  1.00 72.54  ? 102 ASN D C   1 
ATOM   13104 O O   . ASN D 1 102 ? 11.500  40.852  70.790  1.00 74.92  ? 102 ASN D O   1 
ATOM   13105 C CB  . ASN D 1 102 ? 9.669   42.937  71.271  1.00 64.93  ? 102 ASN D CB  1 
ATOM   13106 C CG  . ASN D 1 102 ? 8.765   44.051  71.768  1.00 69.66  ? 102 ASN D CG  1 
ATOM   13107 O OD1 . ASN D 1 102 ? 7.764   43.800  72.437  1.00 74.23  ? 102 ASN D OD1 1 
ATOM   13108 N ND2 . ASN D 1 102 ? 9.117   45.290  71.444  1.00 66.94  ? 102 ASN D ND2 1 
ATOM   13109 N N   . TYR D 1 103 ? 12.762  41.487  72.553  1.00 70.49  ? 103 TYR D N   1 
ATOM   13110 C CA  . TYR D 1 103 ? 13.983  40.871  72.036  1.00 71.19  ? 103 TYR D CA  1 
ATOM   13111 C C   . TYR D 1 103 ? 13.790  39.388  71.753  1.00 73.36  ? 103 TYR D C   1 
ATOM   13112 O O   . TYR D 1 103 ? 14.170  38.893  70.683  1.00 78.81  ? 103 TYR D O   1 
ATOM   13113 C CB  . TYR D 1 103 ? 15.132  41.074  73.030  1.00 68.00  ? 103 TYR D CB  1 
ATOM   13114 C CG  . TYR D 1 103 ? 16.498  40.781  72.459  1.00 70.73  ? 103 TYR D CG  1 
ATOM   13115 C CD1 . TYR D 1 103 ? 16.857  41.240  71.197  1.00 80.88  ? 103 TYR D CD1 1 
ATOM   13116 C CD2 . TYR D 1 103 ? 17.433  40.048  73.178  1.00 78.90  ? 103 TYR D CD2 1 
ATOM   13117 C CE1 . TYR D 1 103 ? 18.110  40.977  70.667  1.00 88.38  ? 103 TYR D CE1 1 
ATOM   13118 C CE2 . TYR D 1 103 ? 18.692  39.779  72.658  1.00 80.62  ? 103 TYR D CE2 1 
ATOM   13119 C CZ  . TYR D 1 103 ? 19.024  40.245  71.402  1.00 85.98  ? 103 TYR D CZ  1 
ATOM   13120 O OH  . TYR D 1 103 ? 20.270  39.980  70.882  1.00 93.00  ? 103 TYR D OH  1 
ATOM   13121 N N   . GLU D 1 104 ? 13.196  38.665  72.695  1.00 71.22  ? 104 GLU D N   1 
ATOM   13122 C CA  . GLU D 1 104 ? 13.099  37.217  72.623  1.00 63.80  ? 104 GLU D CA  1 
ATOM   13123 C C   . GLU D 1 104 ? 11.874  36.736  71.862  1.00 60.48  ? 104 GLU D C   1 
ATOM   13124 O O   . GLU D 1 104 ? 11.716  35.526  71.677  1.00 67.81  ? 104 GLU D O   1 
ATOM   13125 C CB  . GLU D 1 104 ? 13.113  36.641  74.038  1.00 70.25  ? 104 GLU D CB  1 
ATOM   13126 C CG  . GLU D 1 104 ? 13.942  37.484  74.993  1.00 80.69  ? 104 GLU D CG  1 
ATOM   13127 C CD  . GLU D 1 104 ? 14.736  36.650  75.972  1.00 106.30 ? 104 GLU D CD  1 
ATOM   13128 O OE1 . GLU D 1 104 ? 15.840  37.084  76.363  1.00 115.60 ? 104 GLU D OE1 1 
ATOM   13129 O OE2 . GLU D 1 104 ? 14.257  35.563  76.354  1.00 112.47 ? 104 GLU D OE2 1 
ATOM   13130 N N   . LYS D 1 105 ? 11.014  37.640  71.408  1.00 61.95  ? 105 LYS D N   1 
ATOM   13131 C CA  . LYS D 1 105 ? 9.888   37.220  70.587  1.00 70.35  ? 105 LYS D CA  1 
ATOM   13132 C C   . LYS D 1 105 ? 10.389  36.772  69.215  1.00 71.14  ? 105 LYS D C   1 
ATOM   13133 O O   . LYS D 1 105 ? 11.257  37.427  68.626  1.00 68.13  ? 105 LYS D O   1 
ATOM   13134 C CB  . LYS D 1 105 ? 8.866   38.351  70.441  1.00 65.96  ? 105 LYS D CB  1 
ATOM   13135 C CG  . LYS D 1 105 ? 8.558   39.079  71.743  1.00 69.67  ? 105 LYS D CG  1 
ATOM   13136 C CD  . LYS D 1 105 ? 7.220   39.801  71.696  1.00 69.18  ? 105 LYS D CD  1 
ATOM   13137 C CE  . LYS D 1 105 ? 6.902   40.469  73.027  1.00 66.21  ? 105 LYS D CE  1 
ATOM   13138 N NZ  . LYS D 1 105 ? 5.443   40.733  73.187  1.00 76.05  ? 105 LYS D NZ  1 
ATOM   13139 N N   . PRO D 1 106 ? 9.877   35.654  68.695  1.00 71.12  ? 106 PRO D N   1 
ATOM   13140 C CA  . PRO D 1 106 ? 10.366  35.148  67.402  1.00 75.43  ? 106 PRO D CA  1 
ATOM   13141 C C   . PRO D 1 106 ? 10.267  36.154  66.269  1.00 75.95  ? 106 PRO D C   1 
ATOM   13142 O O   . PRO D 1 106 ? 11.065  36.088  65.326  1.00 71.24  ? 106 PRO D O   1 
ATOM   13143 C CB  . PRO D 1 106 ? 9.464   33.930  67.157  1.00 78.69  ? 106 PRO D CB  1 
ATOM   13144 C CG  . PRO D 1 106 ? 9.107   33.469  68.543  1.00 75.93  ? 106 PRO D CG  1 
ATOM   13145 C CD  . PRO D 1 106 ? 8.889   34.747  69.301  1.00 73.94  ? 106 PRO D CD  1 
ATOM   13146 N N   . ILE D 1 107 ? 9.316   37.088  66.329  1.00 74.61  ? 107 ILE D N   1 
ATOM   13147 C CA  . ILE D 1 107 ? 9.210   38.084  65.272  1.00 73.67  ? 107 ILE D CA  1 
ATOM   13148 C C   . ILE D 1 107 ? 10.404  39.027  65.277  1.00 70.76  ? 107 ILE D C   1 
ATOM   13149 O O   . ILE D 1 107 ? 10.705  39.648  64.252  1.00 56.74  ? 107 ILE D O   1 
ATOM   13150 C CB  . ILE D 1 107 ? 7.885   38.857  65.402  1.00 69.03  ? 107 ILE D CB  1 
ATOM   13151 C CG1 . ILE D 1 107 ? 7.628   39.237  66.862  1.00 73.37  ? 107 ILE D CG1 1 
ATOM   13152 C CG2 . ILE D 1 107 ? 6.737   38.022  64.866  1.00 62.51  ? 107 ILE D CG2 1 
ATOM   13153 C CD1 . ILE D 1 107 ? 6.811   40.503  67.032  1.00 70.67  ? 107 ILE D CD1 1 
ATOM   13154 N N   . TYR D 1 108 ? 11.097  39.141  66.410  1.00 76.58  ? 108 TYR D N   1 
ATOM   13155 C CA  . TYR D 1 108 ? 12.288  39.977  66.551  1.00 76.17  ? 108 TYR D CA  1 
ATOM   13156 C C   . TYR D 1 108 ? 13.569  39.171  66.369  1.00 76.82  ? 108 TYR D C   1 
ATOM   13157 O O   . TYR D 1 108 ? 14.553  39.381  67.084  1.00 76.94  ? 108 TYR D O   1 
ATOM   13158 C CB  . TYR D 1 108 ? 12.290  40.669  67.910  1.00 64.82  ? 108 TYR D CB  1 
ATOM   13159 C CG  . TYR D 1 108 ? 11.592  42.014  67.950  1.00 72.29  ? 108 TYR D CG  1 
ATOM   13160 C CD1 . TYR D 1 108 ? 10.206  42.107  67.887  1.00 68.73  ? 108 TYR D CD1 1 
ATOM   13161 C CD2 . TYR D 1 108 ? 12.320  43.193  68.065  1.00 73.32  ? 108 TYR D CD2 1 
ATOM   13162 C CE1 . TYR D 1 108 ? 9.563   43.338  67.927  1.00 66.75  ? 108 TYR D CE1 1 
ATOM   13163 C CE2 . TYR D 1 108 ? 11.683  44.432  68.108  1.00 73.15  ? 108 TYR D CE2 1 
ATOM   13164 C CZ  . TYR D 1 108 ? 10.305  44.498  68.040  1.00 70.63  ? 108 TYR D CZ  1 
ATOM   13165 O OH  . TYR D 1 108 ? 9.667   45.722  68.081  1.00 65.41  ? 108 TYR D OH  1 
ATOM   13166 N N   . ARG D 1 109 ? 13.594  38.235  65.423  1.00 76.52  ? 109 ARG D N   1 
ATOM   13167 C CA  . ARG D 1 109 ? 14.763  37.381  65.229  1.00 79.23  ? 109 ARG D CA  1 
ATOM   13168 C C   . ARG D 1 109 ? 15.502  37.841  63.976  1.00 76.91  ? 109 ARG D C   1 
ATOM   13169 O O   . ARG D 1 109 ? 15.401  37.255  62.900  1.00 68.53  ? 109 ARG D O   1 
ATOM   13170 C CB  . ARG D 1 109 ? 14.347  35.922  65.152  1.00 78.14  ? 109 ARG D CB  1 
ATOM   13171 C CG  . ARG D 1 109 ? 14.495  35.199  66.470  1.00 81.96  ? 109 ARG D CG  1 
ATOM   13172 C CD  . ARG D 1 109 ? 14.917  33.770  66.247  1.00 88.43  ? 109 ARG D CD  1 
ATOM   13173 N NE  . ARG D 1 109 ? 13.766  32.889  66.090  1.00 87.81  ? 109 ARG D NE  1 
ATOM   13174 C CZ  . ARG D 1 109 ? 12.957  32.519  67.074  1.00 88.78  ? 109 ARG D CZ  1 
ATOM   13175 N NH1 . ARG D 1 109 ? 13.139  32.940  68.317  1.00 89.78  ? 109 ARG D NH1 1 
ATOM   13176 N NH2 . ARG D 1 109 ? 11.949  31.695  66.808  1.00 94.77  ? 109 ARG D NH2 1 
ATOM   13177 N N   . PHE D 1 110 ? 16.251  38.923  64.138  1.00 73.12  ? 110 PHE D N   1 
ATOM   13178 C CA  . PHE D 1 110 ? 17.156  39.429  63.121  1.00 70.33  ? 110 PHE D CA  1 
ATOM   13179 C C   . PHE D 1 110 ? 18.547  39.508  63.725  1.00 77.65  ? 110 PHE D C   1 
ATOM   13180 O O   . PHE D 1 110 ? 18.701  39.912  64.881  1.00 85.35  ? 110 PHE D O   1 
ATOM   13181 C CB  . PHE D 1 110 ? 16.730  40.811  62.619  1.00 75.39  ? 110 PHE D CB  1 
ATOM   13182 C CG  . PHE D 1 110 ? 15.289  40.899  62.194  1.00 76.38  ? 110 PHE D CG  1 
ATOM   13183 C CD1 . PHE D 1 110 ? 14.286  41.102  63.129  1.00 78.35  ? 110 PHE D CD1 1 
ATOM   13184 C CD2 . PHE D 1 110 ? 14.939  40.800  60.858  1.00 61.59  ? 110 PHE D CD2 1 
ATOM   13185 C CE1 . PHE D 1 110 ? 12.960  41.196  62.741  1.00 73.99  ? 110 PHE D CE1 1 
ATOM   13186 C CE2 . PHE D 1 110 ? 13.613  40.893  60.466  1.00 63.31  ? 110 PHE D CE2 1 
ATOM   13187 C CZ  . PHE D 1 110 ? 12.625  41.091  61.409  1.00 65.79  ? 110 PHE D CZ  1 
ATOM   13188 N N   . GLU D 1 111 ? 19.562  39.118  62.950  1.00 87.61  ? 111 GLU D N   1 
ATOM   13189 C CA  . GLU D 1 111 ? 20.925  39.136  63.478  1.00 87.73  ? 111 GLU D CA  1 
ATOM   13190 C C   . GLU D 1 111 ? 21.414  40.561  63.708  1.00 84.60  ? 111 GLU D C   1 
ATOM   13191 O O   . GLU D 1 111 ? 22.129  40.824  64.682  1.00 83.39  ? 111 GLU D O   1 
ATOM   13192 C CB  . GLU D 1 111 ? 21.875  38.381  62.549  1.00 82.57  ? 111 GLU D CB  1 
ATOM   13193 C CG  . GLU D 1 111 ? 23.352  38.603  62.868  1.00 96.13  ? 111 GLU D CG  1 
ATOM   13194 C CD  . GLU D 1 111 ? 23.738  38.108  64.255  1.00 105.52 ? 111 GLU D CD  1 
ATOM   13195 O OE1 . GLU D 1 111 ? 23.111  37.142  64.738  1.00 106.61 ? 111 GLU D OE1 1 
ATOM   13196 O OE2 . GLU D 1 111 ? 24.674  38.678  64.859  1.00 103.43 ? 111 GLU D OE2 1 
ATOM   13197 N N   . ARG D 1 112 ? 21.030  41.495  62.833  1.00 80.25  ? 112 ARG D N   1 
ATOM   13198 C CA  . ARG D 1 112 ? 21.370  42.899  63.049  1.00 83.97  ? 112 ARG D CA  1 
ATOM   13199 C C   . ARG D 1 112 ? 20.865  43.398  64.399  1.00 88.42  ? 112 ARG D C   1 
ATOM   13200 O O   . ARG D 1 112 ? 21.575  44.126  65.102  1.00 87.30  ? 112 ARG D O   1 
ATOM   13201 C CB  . ARG D 1 112 ? 20.801  43.754  61.918  1.00 79.56  ? 112 ARG D CB  1 
ATOM   13202 C CG  . ARG D 1 112 ? 21.156  45.232  61.992  1.00 80.85  ? 112 ARG D CG  1 
ATOM   13203 C CD  . ARG D 1 112 ? 22.590  45.507  61.574  1.00 80.79  ? 112 ARG D CD  1 
ATOM   13204 N NE  . ARG D 1 112 ? 22.788  46.911  61.234  1.00 79.63  ? 112 ARG D NE  1 
ATOM   13205 C CZ  . ARG D 1 112 ? 23.860  47.616  61.564  1.00 78.30  ? 112 ARG D CZ  1 
ATOM   13206 N NH1 . ARG D 1 112 ? 24.851  47.082  62.258  1.00 72.26  ? 112 ARG D NH1 1 
ATOM   13207 N NH2 . ARG D 1 112 ? 23.944  48.889  61.184  1.00 79.53  ? 112 ARG D NH2 1 
ATOM   13208 N N   . ILE D 1 113 ? 19.649  43.001  64.786  1.00 83.90  ? 113 ILE D N   1 
ATOM   13209 C CA  . ILE D 1 113 ? 19.108  43.396  66.087  1.00 83.50  ? 113 ILE D CA  1 
ATOM   13210 C C   . ILE D 1 113 ? 20.032  42.956  67.213  1.00 89.49  ? 113 ILE D C   1 
ATOM   13211 O O   . ILE D 1 113 ? 20.263  43.701  68.173  1.00 94.58  ? 113 ILE D O   1 
ATOM   13212 C CB  . ILE D 1 113 ? 17.694  42.823  66.275  1.00 77.68  ? 113 ILE D CB  1 
ATOM   13213 C CG1 . ILE D 1 113 ? 16.720  43.511  65.322  1.00 76.89  ? 113 ILE D CG1 1 
ATOM   13214 C CG2 . ILE D 1 113 ? 17.256  42.973  67.724  1.00 83.85  ? 113 ILE D CG2 1 
ATOM   13215 C CD1 . ILE D 1 113 ? 15.279  43.250  65.635  1.00 80.14  ? 113 ILE D CD1 1 
ATOM   13216 N N   . ARG D 1 114 ? 20.566  41.738  67.115  1.00 85.72  ? 114 ARG D N   1 
ATOM   13217 C CA  . ARG D 1 114 ? 21.447  41.205  68.149  1.00 87.57  ? 114 ARG D CA  1 
ATOM   13218 C C   . ARG D 1 114 ? 22.697  42.057  68.322  1.00 86.86  ? 114 ARG D C   1 
ATOM   13219 O O   . ARG D 1 114 ? 23.036  42.459  69.441  1.00 90.86  ? 114 ARG D O   1 
ATOM   13220 C CB  . ARG D 1 114 ? 21.811  39.765  67.800  1.00 93.98  ? 114 ARG D CB  1 
ATOM   13221 C CG  . ARG D 1 114 ? 20.650  39.032  67.149  1.00 95.12  ? 114 ARG D CG  1 
ATOM   13222 C CD  . ARG D 1 114 ? 20.777  37.523  67.230  1.00 97.04  ? 114 ARG D CD  1 
ATOM   13223 N NE  . ARG D 1 114 ? 19.465  36.917  67.416  1.00 101.57 ? 114 ARG D NE  1 
ATOM   13224 C CZ  . ARG D 1 114 ? 19.168  35.654  67.140  1.00 101.41 ? 114 ARG D CZ  1 
ATOM   13225 N NH1 . ARG D 1 114 ? 20.080  34.816  66.666  1.00 94.50  ? 114 ARG D NH1 1 
ATOM   13226 N NH2 . ARG D 1 114 ? 17.924  35.224  67.340  1.00 94.71  ? 114 ARG D NH2 1 
ATOM   13227 N N   . GLU D 1 115 ? 23.405  42.332  67.221  1.00 89.79  ? 115 GLU D N   1 
ATOM   13228 C CA  . GLU D 1 115 ? 24.647  43.097  67.303  1.00 93.22  ? 115 GLU D CA  1 
ATOM   13229 C C   . GLU D 1 115 ? 24.395  44.510  67.809  1.00 96.32  ? 115 GLU D C   1 
ATOM   13230 O O   . GLU D 1 115 ? 25.205  45.062  68.566  1.00 97.12  ? 115 GLU D O   1 
ATOM   13231 C CB  . GLU D 1 115 ? 25.334  43.148  65.935  1.00 89.10  ? 115 GLU D CB  1 
ATOM   13232 C CG  . GLU D 1 115 ? 25.040  41.975  65.009  1.00 96.58  ? 115 GLU D CG  1 
ATOM   13233 C CD  . GLU D 1 115 ? 25.548  42.204  63.590  1.00 94.56  ? 115 GLU D CD  1 
ATOM   13234 O OE1 . GLU D 1 115 ? 26.227  43.228  63.355  1.00 83.70  ? 115 GLU D OE1 1 
ATOM   13235 O OE2 . GLU D 1 115 ? 25.269  41.361  62.707  1.00 90.39  ? 115 GLU D OE2 1 
ATOM   13236 N N   . LEU D 1 116 ? 23.284  45.118  67.384  1.00 94.67  ? 116 LEU D N   1 
ATOM   13237 C CA  . LEU D 1 116 ? 22.966  46.486  67.794  1.00 90.93  ? 116 LEU D CA  1 
ATOM   13238 C C   . LEU D 1 116 ? 22.916  46.613  69.315  1.00 88.56  ? 116 LEU D C   1 
ATOM   13239 O O   . LEU D 1 116 ? 23.455  47.569  69.886  1.00 90.91  ? 116 LEU D O   1 
ATOM   13240 C CB  . LEU D 1 116 ? 21.639  46.910  67.154  1.00 83.84  ? 116 LEU D CB  1 
ATOM   13241 C CG  . LEU D 1 116 ? 21.623  47.544  65.749  1.00 85.69  ? 116 LEU D CG  1 
ATOM   13242 C CD1 . LEU D 1 116 ? 21.822  49.045  65.854  1.00 85.95  ? 116 LEU D CD1 1 
ATOM   13243 C CD2 . LEU D 1 116 ? 22.662  46.957  64.800  1.00 73.82  ? 116 LEU D CD2 1 
ATOM   13244 N N   . MET D 1 117 ? 22.295  45.643  69.986  1.00 86.42  ? 117 MET D N   1 
ATOM   13245 C CA  . MET D 1 117 ? 22.232  45.659  71.441  1.00 86.33  ? 117 MET D CA  1 
ATOM   13246 C C   . MET D 1 117 ? 23.588  45.362  72.068  1.00 92.85  ? 117 MET D C   1 
ATOM   13247 O O   . MET D 1 117 ? 23.885  45.859  73.160  1.00 93.98  ? 117 MET D O   1 
ATOM   13248 C CB  . MET D 1 117 ? 21.192  44.652  71.911  1.00 87.09  ? 117 MET D CB  1 
ATOM   13249 C CG  . MET D 1 117 ? 19.861  44.769  71.171  1.00 77.09  ? 117 MET D CG  1 
ATOM   13250 S SD  . MET D 1 117 ? 18.701  46.053  71.735  1.00 83.18  ? 117 MET D SD  1 
ATOM   13251 C CE  . MET D 1 117 ? 19.302  47.617  71.080  1.00 60.55  ? 117 MET D CE  1 
ATOM   13252 N N   . ASN D 1 118 ? 24.422  44.563  71.395  1.00 98.92  ? 118 ASN D N   1 
ATOM   13253 C CA  . ASN D 1 118 ? 25.760  44.287  71.908  1.00 95.42  ? 118 ASN D CA  1 
ATOM   13254 C C   . ASN D 1 118 ? 26.644  45.523  71.803  1.00 96.22  ? 118 ASN D C   1 
ATOM   13255 O O   . ASN D 1 118 ? 27.476  45.775  72.682  1.00 106.23 ? 118 ASN D O   1 
ATOM   13256 C CB  . ASN D 1 118 ? 26.382  43.107  71.157  1.00 93.89  ? 118 ASN D CB  1 
ATOM   13257 C CG  . ASN D 1 118 ? 25.549  41.830  71.259  1.00 104.96 ? 118 ASN D CG  1 
ATOM   13258 O OD1 . ASN D 1 118 ? 25.875  40.824  70.622  1.00 102.67 ? 118 ASN D OD1 1 
ATOM   13259 N ND2 . ASN D 1 118 ? 24.485  41.858  72.056  1.00 102.57 ? 118 ASN D ND2 1 
ATOM   13260 N N   . LYS D 1 119 ? 26.470  46.313  70.745  1.00 93.06  ? 119 LYS D N   1 
ATOM   13261 C CA  . LYS D 1 119 ? 27.227  47.549  70.611  1.00 96.29  ? 119 LYS D CA  1 
ATOM   13262 C C   . LYS D 1 119 ? 26.736  48.578  71.625  1.00 99.81  ? 119 LYS D C   1 
ATOM   13263 O O   . LYS D 1 119 ? 25.535  48.859  71.721  1.00 100.53 ? 119 LYS D O   1 
ATOM   13264 C CB  . LYS D 1 119 ? 27.120  48.089  69.183  1.00 94.33  ? 119 LYS D CB  1 
ATOM   13265 C CG  . LYS D 1 119 ? 28.263  47.650  68.268  1.00 94.83  ? 119 LYS D CG  1 
ATOM   13266 C CD  . LYS D 1 119 ? 29.438  48.626  68.314  1.00 103.79 ? 119 LYS D CD  1 
ATOM   13267 C CE  . LYS D 1 119 ? 30.348  48.479  67.096  1.00 94.67  ? 119 LYS D CE  1 
ATOM   13268 N NZ  . LYS D 1 119 ? 31.078  49.739  66.773  1.00 90.30  ? 119 LYS D NZ  1 
ATOM   13269 N N   . GLU D 1 120 ? 27.687  49.126  72.384  1.00 97.77  ? 120 GLU D N   1 
ATOM   13270 C CA  . GLU D 1 120 ? 27.403  50.091  73.441  1.00 95.28  ? 120 GLU D CA  1 
ATOM   13271 C C   . GLU D 1 120 ? 26.897  51.414  72.875  1.00 101.17 ? 120 GLU D C   1 
ATOM   13272 O O   . GLU D 1 120 ? 25.835  51.907  73.276  1.00 97.70  ? 120 GLU D O   1 
ATOM   13273 C CB  . GLU D 1 120 ? 28.665  50.308  74.277  1.00 100.42 ? 120 GLU D CB  1 
ATOM   13274 C CG  . GLU D 1 120 ? 29.965  50.698  73.507  1.00 112.48 ? 120 GLU D CG  1 
ATOM   13275 C CD  . GLU D 1 120 ? 30.387  49.716  72.409  1.00 110.31 ? 120 GLU D CD  1 
ATOM   13276 O OE1 . GLU D 1 120 ? 31.050  50.150  71.438  1.00 113.60 ? 120 GLU D OE1 1 
ATOM   13277 O OE2 . GLU D 1 120 ? 30.061  48.513  72.517  1.00 109.74 ? 120 GLU D OE2 1 
ATOM   13278 N N   . LYS D 1 121 ? 27.639  51.998  71.936  1.00 100.33 ? 121 LYS D N   1 
ATOM   13279 C CA  . LYS D 1 121 ? 27.296  53.267  71.310  1.00 100.90 ? 121 LYS D CA  1 
ATOM   13280 C C   . LYS D 1 121 ? 26.914  53.026  69.854  1.00 97.31  ? 121 LYS D C   1 
ATOM   13281 O O   . LYS D 1 121 ? 27.493  52.162  69.184  1.00 94.90  ? 121 LYS D O   1 
ATOM   13282 C CB  . LYS D 1 121 ? 28.470  54.251  71.406  1.00 103.64 ? 121 LYS D CB  1 
ATOM   13283 C CG  . LYS D 1 121 ? 28.219  55.630  70.793  1.00 105.65 ? 121 LYS D CG  1 
ATOM   13284 C CD  . LYS D 1 121 ? 26.976  56.294  71.377  1.00 105.93 ? 121 LYS D CD  1 
ATOM   13285 C CE  . LYS D 1 121 ? 27.183  57.790  71.588  1.00 104.10 ? 121 LYS D CE  1 
ATOM   13286 N NZ  . LYS D 1 121 ? 26.504  58.603  70.536  1.00 86.25  ? 121 LYS D NZ  1 
ATOM   13287 N N   . LEU D 1 122 ? 25.936  53.791  69.368  1.00 88.72  ? 122 LEU D N   1 
ATOM   13288 C CA  . LEU D 1 122 ? 25.336  53.552  68.063  1.00 82.28  ? 122 LEU D CA  1 
ATOM   13289 C C   . LEU D 1 122 ? 25.275  54.848  67.266  1.00 80.77  ? 122 LEU D C   1 
ATOM   13290 O O   . LEU D 1 122 ? 25.003  55.914  67.824  1.00 82.06  ? 122 LEU D O   1 
ATOM   13291 C CB  . LEU D 1 122 ? 23.930  52.950  68.222  1.00 82.54  ? 122 LEU D CB  1 
ATOM   13292 C CG  . LEU D 1 122 ? 23.910  51.636  69.011  1.00 88.09  ? 122 LEU D CG  1 
ATOM   13293 C CD1 . LEU D 1 122 ? 22.597  51.449  69.761  1.00 75.36  ? 122 LEU D CD1 1 
ATOM   13294 C CD2 . LEU D 1 122 ? 24.208  50.442  68.118  1.00 88.30  ? 122 LEU D CD2 1 
ATOM   13295 N N   . ASN D 1 123 ? 25.531  54.757  65.961  1.00 82.90  ? 123 ASN D N   1 
ATOM   13296 C CA  . ASN D 1 123 ? 25.512  55.920  65.085  1.00 81.03  ? 123 ASN D CA  1 
ATOM   13297 C C   . ASN D 1 123 ? 24.179  56.007  64.346  1.00 76.99  ? 123 ASN D C   1 
ATOM   13298 O O   . ASN D 1 123 ? 23.240  55.246  64.602  1.00 69.43  ? 123 ASN D O   1 
ATOM   13299 C CB  . ASN D 1 123 ? 26.680  55.879  64.094  1.00 71.71  ? 123 ASN D CB  1 
ATOM   13300 C CG  . ASN D 1 123 ? 26.836  54.530  63.440  1.00 72.29  ? 123 ASN D CG  1 
ATOM   13301 O OD1 . ASN D 1 123 ? 27.674  53.727  63.845  1.00 78.95  ? 123 ASN D OD1 1 
ATOM   13302 N ND2 . ASN D 1 123 ? 26.030  54.269  62.423  1.00 80.97  ? 123 ASN D ND2 1 
ATOM   13303 N N   . ARG D 1 124 ? 24.112  56.950  63.402  1.00 77.62  ? 124 ARG D N   1 
ATOM   13304 C CA  . ARG D 1 124 ? 22.875  57.183  62.663  1.00 77.52  ? 124 ARG D CA  1 
ATOM   13305 C C   . ARG D 1 124 ? 22.469  55.956  61.860  1.00 73.03  ? 124 ARG D C   1 
ATOM   13306 O O   . ARG D 1 124 ? 21.290  55.589  61.828  1.00 74.81  ? 124 ARG D O   1 
ATOM   13307 C CB  . ARG D 1 124 ? 23.034  58.393  61.741  1.00 68.52  ? 124 ARG D CB  1 
ATOM   13308 C CG  . ARG D 1 124 ? 21.917  58.536  60.730  1.00 71.32  ? 124 ARG D CG  1 
ATOM   13309 C CD  . ARG D 1 124 ? 22.178  59.670  59.755  1.00 71.40  ? 124 ARG D CD  1 
ATOM   13310 N NE  . ARG D 1 124 ? 21.159  59.738  58.713  1.00 69.07  ? 124 ARG D NE  1 
ATOM   13311 C CZ  . ARG D 1 124 ? 21.054  58.881  57.706  1.00 72.68  ? 124 ARG D CZ  1 
ATOM   13312 N NH1 . ARG D 1 124 ? 21.895  57.870  57.567  1.00 78.17  ? 124 ARG D NH1 1 
ATOM   13313 N NH2 . ARG D 1 124 ? 20.080  59.044  56.815  1.00 85.27  ? 124 ARG D NH2 1 
ATOM   13314 N N   . GLU D 1 125 ? 23.434  55.303  61.214  1.00 74.86  ? 125 GLU D N   1 
ATOM   13315 C CA  . GLU D 1 125 ? 23.119  54.160  60.366  1.00 77.03  ? 125 GLU D CA  1 
ATOM   13316 C C   . GLU D 1 125 ? 22.621  52.983  61.193  1.00 78.34  ? 125 GLU D C   1 
ATOM   13317 O O   . GLU D 1 125 ? 21.674  52.295  60.796  1.00 85.58  ? 125 GLU D O   1 
ATOM   13318 C CB  . GLU D 1 125 ? 24.346  53.761  59.545  1.00 78.51  ? 125 GLU D CB  1 
ATOM   13319 C CG  . GLU D 1 125 ? 24.777  54.775  58.473  1.00 84.17  ? 125 GLU D CG  1 
ATOM   13320 C CD  . GLU D 1 125 ? 25.135  56.150  59.032  1.00 90.22  ? 125 GLU D CD  1 
ATOM   13321 O OE1 . GLU D 1 125 ? 24.807  57.168  58.381  1.00 95.63  ? 125 GLU D OE1 1 
ATOM   13322 O OE2 . GLU D 1 125 ? 25.746  56.212  60.123  1.00 92.24  ? 125 GLU D OE2 1 
ATOM   13323 N N   . GLU D 1 126 ? 23.235  52.748  62.354  1.00 73.30  ? 126 GLU D N   1 
ATOM   13324 C CA  . GLU D 1 126 ? 22.779  51.680  63.237  1.00 76.47  ? 126 GLU D CA  1 
ATOM   13325 C C   . GLU D 1 126 ? 21.421  52.015  63.845  1.00 76.99  ? 126 GLU D C   1 
ATOM   13326 O O   . GLU D 1 126 ? 20.506  51.183  63.845  1.00 76.44  ? 126 GLU D O   1 
ATOM   13327 C CB  . GLU D 1 126 ? 23.822  51.433  64.326  1.00 72.69  ? 126 GLU D CB  1 
ATOM   13328 C CG  . GLU D 1 126 ? 25.244  51.399  63.791  1.00 82.84  ? 126 GLU D CG  1 
ATOM   13329 C CD  . GLU D 1 126 ? 26.284  51.115  64.859  1.00 92.33  ? 126 GLU D CD  1 
ATOM   13330 O OE1 . GLU D 1 126 ? 26.614  52.037  65.633  1.00 82.67  ? 126 GLU D OE1 1 
ATOM   13331 O OE2 . GLU D 1 126 ? 26.784  49.972  64.919  1.00 97.77  ? 126 GLU D OE2 1 
ATOM   13332 N N   . LEU D 1 127 ? 21.271  53.234  64.369  1.00 75.27  ? 127 LEU D N   1 
ATOM   13333 C CA  . LEU D 1 127 ? 19.984  53.646  64.922  1.00 76.50  ? 127 LEU D CA  1 
ATOM   13334 C C   . LEU D 1 127 ? 18.884  53.561  63.874  1.00 71.97  ? 127 LEU D C   1 
ATOM   13335 O O   . LEU D 1 127 ? 17.780  53.082  64.158  1.00 70.76  ? 127 LEU D O   1 
ATOM   13336 C CB  . LEU D 1 127 ? 20.085  55.066  65.471  1.00 77.75  ? 127 LEU D CB  1 
ATOM   13337 C CG  . LEU D 1 127 ? 20.902  55.227  66.748  1.00 77.79  ? 127 LEU D CG  1 
ATOM   13338 C CD1 . LEU D 1 127 ? 20.808  56.660  67.226  1.00 66.08  ? 127 LEU D CD1 1 
ATOM   13339 C CD2 . LEU D 1 127 ? 20.418  54.262  67.821  1.00 74.75  ? 127 LEU D CD2 1 
ATOM   13340 N N   . LEU D 1 128 ? 19.171  54.022  62.656  1.00 71.88  ? 128 LEU D N   1 
ATOM   13341 C CA  . LEU D 1 128 ? 18.229  53.863  61.556  1.00 72.06  ? 128 LEU D CA  1 
ATOM   13342 C C   . LEU D 1 128 ? 17.872  52.399  61.350  1.00 73.71  ? 128 LEU D C   1 
ATOM   13343 O O   . LEU D 1 128 ? 16.708  52.061  61.104  1.00 73.36  ? 128 LEU D O   1 
ATOM   13344 C CB  . LEU D 1 128 ? 18.825  54.464  60.282  1.00 71.59  ? 128 LEU D CB  1 
ATOM   13345 C CG  . LEU D 1 128 ? 18.091  55.684  59.727  1.00 69.27  ? 128 LEU D CG  1 
ATOM   13346 C CD1 . LEU D 1 128 ? 18.818  56.268  58.550  1.00 73.28  ? 128 LEU D CD1 1 
ATOM   13347 C CD2 . LEU D 1 128 ? 16.725  55.271  59.291  1.00 84.57  ? 128 LEU D CD2 1 
ATOM   13348 N N   . ASP D 1 129 ? 18.858  51.509  61.468  1.00 73.17  ? 129 ASP D N   1 
ATOM   13349 C CA  . ASP D 1 129 ? 18.580  50.088  61.297  1.00 75.20  ? 129 ASP D CA  1 
ATOM   13350 C C   . ASP D 1 129 ? 17.708  49.559  62.426  1.00 70.96  ? 129 ASP D C   1 
ATOM   13351 O O   . ASP D 1 129 ? 16.768  48.797  62.179  1.00 72.86  ? 129 ASP D O   1 
ATOM   13352 C CB  . ASP D 1 129 ? 19.885  49.306  61.199  1.00 75.78  ? 129 ASP D CB  1 
ATOM   13353 C CG  . ASP D 1 129 ? 20.399  49.223  59.779  1.00 84.43  ? 129 ASP D CG  1 
ATOM   13354 O OD1 . ASP D 1 129 ? 20.034  50.104  58.972  1.00 88.79  ? 129 ASP D OD1 1 
ATOM   13355 O OD2 . ASP D 1 129 ? 21.175  48.294  59.468  1.00 85.73  ? 129 ASP D OD2 1 
ATOM   13356 N N   . LEU D 1 130 ? 17.989  49.969  63.666  1.00 67.10  ? 130 LEU D N   1 
ATOM   13357 C CA  . LEU D 1 130 ? 17.133  49.579  64.785  1.00 74.33  ? 130 LEU D CA  1 
ATOM   13358 C C   . LEU D 1 130 ? 15.691  50.017  64.552  1.00 69.40  ? 130 LEU D C   1 
ATOM   13359 O O   . LEU D 1 130 ? 14.757  49.219  64.693  1.00 65.05  ? 130 LEU D O   1 
ATOM   13360 C CB  . LEU D 1 130 ? 17.665  50.171  66.089  1.00 68.80  ? 130 LEU D CB  1 
ATOM   13361 C CG  . LEU D 1 130 ? 17.063  49.517  67.334  1.00 70.05  ? 130 LEU D CG  1 
ATOM   13362 C CD1 . LEU D 1 130 ? 17.634  48.123  67.540  1.00 80.09  ? 130 LEU D CD1 1 
ATOM   13363 C CD2 . LEU D 1 130 ? 17.278  50.370  68.567  1.00 70.61  ? 130 LEU D CD2 1 
ATOM   13364 N N   . GLN D 1 131 ? 15.499  51.289  64.187  1.00 68.39  ? 131 GLN D N   1 
ATOM   13365 C CA  . GLN D 1 131 ? 14.177  51.806  63.843  1.00 70.08  ? 131 GLN D CA  1 
ATOM   13366 C C   . GLN D 1 131 ? 13.474  50.909  62.831  1.00 72.36  ? 131 GLN D C   1 
ATOM   13367 O O   . GLN D 1 131 ? 12.375  50.403  63.081  1.00 73.55  ? 131 GLN D O   1 
ATOM   13368 C CB  . GLN D 1 131 ? 14.305  53.222  63.274  1.00 73.70  ? 131 GLN D CB  1 
ATOM   13369 C CG  . GLN D 1 131 ? 14.769  54.287  64.248  1.00 71.42  ? 131 GLN D CG  1 
ATOM   13370 C CD  . GLN D 1 131 ? 15.000  55.619  63.552  1.00 75.64  ? 131 GLN D CD  1 
ATOM   13371 O OE1 . GLN D 1 131 ? 15.407  55.662  62.388  1.00 70.22  ? 131 GLN D OE1 1 
ATOM   13372 N NE2 . GLN D 1 131 ? 14.740  56.712  64.261  1.00 69.88  ? 131 GLN D NE2 1 
ATOM   13373 N N   . THR D 1 132 ? 14.102  50.713  61.668  1.00 70.79  ? 132 THR D N   1 
ATOM   13374 C CA  . THR D 1 132 ? 13.449  49.985  60.585  1.00 72.58  ? 132 THR D CA  1 
ATOM   13375 C C   . THR D 1 132 ? 13.138  48.550  60.985  1.00 75.01  ? 132 THR D C   1 
ATOM   13376 O O   . THR D 1 132 ? 12.056  48.033  60.677  1.00 72.22  ? 132 THR D O   1 
ATOM   13377 C CB  . THR D 1 132 ? 14.325  50.002  59.332  1.00 71.95  ? 132 THR D CB  1 
ATOM   13378 O OG1 . THR D 1 132 ? 14.635  51.355  58.979  1.00 73.60  ? 132 THR D OG1 1 
ATOM   13379 C CG2 . THR D 1 132 ? 13.586  49.349  58.175  1.00 64.57  ? 132 THR D CG2 1 
ATOM   13380 N N   . LEU D 1 133 ? 14.072  47.890  61.676  1.00 74.68  ? 133 LEU D N   1 
ATOM   13381 C CA  . LEU D 1 133 ? 13.872  46.485  62.018  1.00 71.31  ? 133 LEU D CA  1 
ATOM   13382 C C   . LEU D 1 133 ? 12.731  46.314  63.010  1.00 69.55  ? 133 LEU D C   1 
ATOM   13383 O O   . LEU D 1 133 ? 11.989  45.328  62.941  1.00 72.53  ? 133 LEU D O   1 
ATOM   13384 C CB  . LEU D 1 133 ? 15.165  45.885  62.568  1.00 72.30  ? 133 LEU D CB  1 
ATOM   13385 C CG  . LEU D 1 133 ? 16.320  45.779  61.571  1.00 72.81  ? 133 LEU D CG  1 
ATOM   13386 C CD1 . LEU D 1 133 ? 17.607  45.480  62.308  1.00 73.95  ? 133 LEU D CD1 1 
ATOM   13387 C CD2 . LEU D 1 133 ? 16.037  44.713  60.526  1.00 74.06  ? 133 LEU D CD2 1 
ATOM   13388 N N   . ASN D 1 134 ? 12.570  47.264  63.935  1.00 68.79  ? 134 ASN D N   1 
ATOM   13389 C CA  . ASN D 1 134 ? 11.407  47.239  64.817  1.00 66.45  ? 134 ASN D CA  1 
ATOM   13390 C C   . ASN D 1 134 ? 10.115  47.301  64.014  1.00 69.23  ? 134 ASN D C   1 
ATOM   13391 O O   . ASN D 1 134 ? 9.155   46.583  64.312  1.00 70.06  ? 134 ASN D O   1 
ATOM   13392 C CB  . ASN D 1 134 ? 11.469  48.395  65.810  1.00 65.47  ? 134 ASN D CB  1 
ATOM   13393 C CG  . ASN D 1 134 ? 12.302  48.069  67.033  1.00 66.75  ? 134 ASN D CG  1 
ATOM   13394 O OD1 . ASN D 1 134 ? 11.791  47.572  68.037  1.00 71.07  ? 134 ASN D OD1 1 
ATOM   13395 N ND2 . ASN D 1 134 ? 13.591  48.362  66.956  1.00 68.94  ? 134 ASN D ND2 1 
ATOM   13396 N N   . LEU D 1 135 ? 10.084  48.136  62.974  1.00 68.65  ? 135 LEU D N   1 
ATOM   13397 C CA  . LEU D 1 135 ? 8.916   48.207  62.101  1.00 69.31  ? 135 LEU D CA  1 
ATOM   13398 C C   . LEU D 1 135 ? 8.714   46.908  61.328  1.00 70.50  ? 135 LEU D C   1 
ATOM   13399 O O   . LEU D 1 135 ? 7.581   46.435  61.180  1.00 69.39  ? 135 LEU D O   1 
ATOM   13400 C CB  . LEU D 1 135 ? 9.071   49.375  61.137  1.00 67.59  ? 135 LEU D CB  1 
ATOM   13401 C CG  . LEU D 1 135 ? 8.413   50.671  61.593  1.00 77.66  ? 135 LEU D CG  1 
ATOM   13402 C CD1 . LEU D 1 135 ? 8.366   51.617  60.416  1.00 75.93  ? 135 LEU D CD1 1 
ATOM   13403 C CD2 . LEU D 1 135 ? 7.015   50.416  62.174  1.00 71.44  ? 135 LEU D CD2 1 
ATOM   13404 N N   . LEU D 1 136 ? 9.802   46.316  60.834  1.00 68.12  ? 136 LEU D N   1 
ATOM   13405 C CA  . LEU D 1 136 ? 9.721   45.080  60.064  1.00 63.89  ? 136 LEU D CA  1 
ATOM   13406 C C   . LEU D 1 136 ? 9.355   43.875  60.924  1.00 68.07  ? 136 LEU D C   1 
ATOM   13407 O O   . LEU D 1 136 ? 8.907   42.857  60.386  1.00 66.52  ? 136 LEU D O   1 
ATOM   13408 C CB  . LEU D 1 136 ? 11.056  44.828  59.368  1.00 70.33  ? 136 LEU D CB  1 
ATOM   13409 C CG  . LEU D 1 136 ? 11.463  45.821  58.275  1.00 70.44  ? 136 LEU D CG  1 
ATOM   13410 C CD1 . LEU D 1 136 ? 12.934  45.643  57.935  1.00 70.40  ? 136 LEU D CD1 1 
ATOM   13411 C CD2 . LEU D 1 136 ? 10.598  45.684  57.023  1.00 66.44  ? 136 LEU D CD2 1 
ATOM   13412 N N   . ALA D 1 137 ? 9.538   43.962  62.245  1.00 74.34  ? 137 ALA D N   1 
ATOM   13413 C CA  . ALA D 1 137 ? 9.263   42.815  63.108  1.00 70.51  ? 137 ALA D CA  1 
ATOM   13414 C C   . ALA D 1 137 ? 7.770   42.549  63.248  1.00 74.04  ? 137 ALA D C   1 
ATOM   13415 O O   . ALA D 1 137 ? 7.370   41.416  63.539  1.00 76.66  ? 137 ALA D O   1 
ATOM   13416 C CB  . ALA D 1 137 ? 9.893   43.024  64.481  1.00 68.49  ? 137 ALA D CB  1 
ATOM   13417 N N   . TRP D 1 138 ? 6.933   43.571  63.060  1.00 71.12  ? 138 TRP D N   1 
ATOM   13418 C CA  . TRP D 1 138 ? 5.484   43.419  63.108  1.00 68.85  ? 138 TRP D CA  1 
ATOM   13419 C C   . TRP D 1 138 ? 4.874   43.334  61.715  1.00 67.49  ? 138 TRP D C   1 
ATOM   13420 O O   . TRP D 1 138 ? 3.689   43.641  61.540  1.00 70.63  ? 138 TRP D O   1 
ATOM   13421 C CB  . TRP D 1 138 ? 4.854   44.563  63.907  1.00 68.17  ? 138 TRP D CB  1 
ATOM   13422 C CG  . TRP D 1 138 ? 5.567   44.822  65.208  1.00 67.58  ? 138 TRP D CG  1 
ATOM   13423 C CD1 . TRP D 1 138 ? 6.701   45.554  65.381  1.00 66.62  ? 138 TRP D CD1 1 
ATOM   13424 C CD2 . TRP D 1 138 ? 5.207   44.333  66.510  1.00 68.33  ? 138 TRP D CD2 1 
ATOM   13425 N NE1 . TRP D 1 138 ? 7.069   45.558  66.699  1.00 64.34  ? 138 TRP D NE1 1 
ATOM   13426 C CE2 . TRP D 1 138 ? 6.169   44.818  67.417  1.00 67.50  ? 138 TRP D CE2 1 
ATOM   13427 C CE3 . TRP D 1 138 ? 4.161   43.541  66.996  1.00 71.43  ? 138 TRP D CE3 1 
ATOM   13428 C CZ2 . TRP D 1 138 ? 6.122   44.535  68.784  1.00 68.00  ? 138 TRP D CZ2 1 
ATOM   13429 C CZ3 . TRP D 1 138 ? 4.114   43.259  68.357  1.00 74.87  ? 138 TRP D CZ3 1 
ATOM   13430 C CH2 . TRP D 1 138 ? 5.090   43.757  69.234  1.00 73.42  ? 138 TRP D CH2 1 
ATOM   13431 N N   . CYS D 1 139 ? 5.664   42.924  60.725  1.00 65.86  ? 139 CYS D N   1 
ATOM   13432 C CA  . CYS D 1 139 ? 5.176   42.842  59.357  1.00 74.13  ? 139 CYS D CA  1 
ATOM   13433 C C   . CYS D 1 139 ? 4.163   41.715  59.214  1.00 75.55  ? 139 CYS D C   1 
ATOM   13434 O O   . CYS D 1 139 ? 4.430   40.570  59.598  1.00 75.92  ? 139 CYS D O   1 
ATOM   13435 C CB  . CYS D 1 139 ? 6.336   42.634  58.386  1.00 75.97  ? 139 CYS D CB  1 
ATOM   13436 S SG  . CYS D 1 139 ? 5.835   42.711  56.654  1.00 81.93  ? 139 CYS D SG  1 
ATOM   13437 N N   . GLY D 1 140 ? 2.997   42.049  58.650  1.00 77.85  ? 140 GLY D N   1 
ATOM   13438 C CA  . GLY D 1 140 ? 1.925   41.093  58.489  1.00 76.29  ? 140 GLY D CA  1 
ATOM   13439 C C   . GLY D 1 140 ? 2.048   40.257  57.229  1.00 76.04  ? 140 GLY D C   1 
ATOM   13440 O O   . GLY D 1 140 ? 2.877   40.509  56.359  1.00 80.81  ? 140 GLY D O   1 
ATOM   13441 N N   . ARG D 1 141 ? 1.182   39.248  57.153  1.00 77.66  ? 141 ARG D N   1 
ATOM   13442 C CA  . ARG D 1 141 ? 1.197   38.316  56.033  1.00 79.08  ? 141 ARG D CA  1 
ATOM   13443 C C   . ARG D 1 141 ? 1.061   39.034  54.698  1.00 78.79  ? 141 ARG D C   1 
ATOM   13444 O O   . ARG D 1 141 ? 1.734   38.682  53.722  1.00 83.33  ? 141 ARG D O   1 
ATOM   13445 C CB  . ARG D 1 141 ? 0.067   37.305  56.204  1.00 76.26  ? 141 ARG D CB  1 
ATOM   13446 C CG  . ARG D 1 141 ? 0.402   35.924  55.705  1.00 82.80  ? 141 ARG D CG  1 
ATOM   13447 C CD  . ARG D 1 141 ? -0.809  35.019  55.798  1.00 75.77  ? 141 ARG D CD  1 
ATOM   13448 N NE  . ARG D 1 141 ? -2.012  35.654  55.280  1.00 78.32  ? 141 ARG D NE  1 
ATOM   13449 C CZ  . ARG D 1 141 ? -2.831  35.091  54.404  1.00 79.94  ? 141 ARG D CZ  1 
ATOM   13450 N NH1 . ARG D 1 141 ? -2.600  33.880  53.921  1.00 76.13  ? 141 ARG D NH1 1 
ATOM   13451 N NH2 . ARG D 1 141 ? -3.907  35.760  53.999  1.00 85.96  ? 141 ARG D NH2 1 
ATOM   13452 N N   . THR D 1 142 ? 0.189   40.040  54.634  1.00 83.19  ? 142 THR D N   1 
ATOM   13453 C CA  . THR D 1 142 ? -0.162  40.624  53.345  1.00 83.22  ? 142 THR D CA  1 
ATOM   13454 C C   . THR D 1 142 ? 1.009   41.394  52.744  1.00 79.64  ? 142 THR D C   1 
ATOM   13455 O O   . THR D 1 142 ? 1.299   41.256  51.550  1.00 80.34  ? 142 THR D O   1 
ATOM   13456 C CB  . THR D 1 142 ? -1.394  41.516  53.504  1.00 77.52  ? 142 THR D CB  1 
ATOM   13457 O OG1 . THR D 1 142 ? -2.504  40.709  53.917  1.00 80.46  ? 142 THR D OG1 1 
ATOM   13458 C CG2 . THR D 1 142 ? -1.741  42.198  52.194  1.00 86.80  ? 142 THR D CG2 1 
ATOM   13459 N N   . LEU D 1 143 ? 1.713   42.178  53.556  1.00 81.27  ? 143 LEU D N   1 
ATOM   13460 C CA  . LEU D 1 143 ? 2.811   43.003  53.074  1.00 86.50  ? 143 LEU D CA  1 
ATOM   13461 C C   . LEU D 1 143 ? 4.131   42.255  53.020  1.00 83.23  ? 143 LEU D C   1 
ATOM   13462 O O   . LEU D 1 143 ? 5.170   42.874  52.758  1.00 79.42  ? 143 LEU D O   1 
ATOM   13463 C CB  . LEU D 1 143 ? 2.959   44.248  53.949  1.00 81.11  ? 143 LEU D CB  1 
ATOM   13464 C CG  . LEU D 1 143 ? 2.024   45.402  53.611  1.00 78.09  ? 143 LEU D CG  1 
ATOM   13465 C CD1 . LEU D 1 143 ? 2.406   46.629  54.417  1.00 82.66  ? 143 LEU D CD1 1 
ATOM   13466 C CD2 . LEU D 1 143 ? 2.082   45.696  52.122  1.00 78.89  ? 143 LEU D CD2 1 
ATOM   13467 N N   . ARG D 1 144 ? 4.114   40.942  53.252  1.00 82.92  ? 144 ARG D N   1 
ATOM   13468 C CA  . ARG D 1 144 ? 5.355   40.179  53.228  1.00 82.27  ? 144 ARG D CA  1 
ATOM   13469 C C   . ARG D 1 144 ? 6.001   40.220  51.850  1.00 86.07  ? 144 ARG D C   1 
ATOM   13470 O O   . ARG D 1 144 ? 7.217   40.408  51.736  1.00 92.50  ? 144 ARG D O   1 
ATOM   13471 C CB  . ARG D 1 144 ? 5.102   38.729  53.645  1.00 82.03  ? 144 ARG D CB  1 
ATOM   13472 C CG  . ARG D 1 144 ? 4.872   38.479  55.138  1.00 71.33  ? 144 ARG D CG  1 
ATOM   13473 C CD  . ARG D 1 144 ? 6.081   38.850  56.015  1.00 81.16  ? 144 ARG D CD  1 
ATOM   13474 N NE  . ARG D 1 144 ? 5.923   38.327  57.373  1.00 92.06  ? 144 ARG D NE  1 
ATOM   13475 C CZ  . ARG D 1 144 ? 6.830   38.397  58.344  1.00 96.76  ? 144 ARG D CZ  1 
ATOM   13476 N NH1 . ARG D 1 144 ? 7.986   39.025  58.174  1.00 88.37  ? 144 ARG D NH1 1 
ATOM   13477 N NH2 . ARG D 1 144 ? 6.567   37.824  59.520  1.00 86.16  ? 144 ARG D NH2 1 
ATOM   13478 N N   . LYS D 1 145 ? 5.207   40.050  50.788  1.00 86.38  ? 145 LYS D N   1 
ATOM   13479 C CA  . LYS D 1 145 ? 5.781   39.967  49.445  1.00 82.95  ? 145 LYS D CA  1 
ATOM   13480 C C   . LYS D 1 145 ? 6.363   41.305  49.003  1.00 86.34  ? 145 LYS D C   1 
ATOM   13481 O O   . LYS D 1 145 ? 7.492   41.365  48.500  1.00 91.73  ? 145 LYS D O   1 
ATOM   13482 C CB  . LYS D 1 145 ? 4.732   39.485  48.442  1.00 80.42  ? 145 LYS D CB  1 
ATOM   13483 C CG  . LYS D 1 145 ? 5.184   39.625  46.989  1.00 82.69  ? 145 LYS D CG  1 
ATOM   13484 C CD  . LYS D 1 145 ? 4.420   38.698  46.049  1.00 79.25  ? 145 LYS D CD  1 
ATOM   13485 C CE  . LYS D 1 145 ? 4.381   39.243  44.620  1.00 78.05  ? 145 LYS D CE  1 
ATOM   13486 N NZ  . LYS D 1 145 ? 3.032   39.759  44.241  1.00 80.16  ? 145 LYS D NZ  1 
ATOM   13487 N N   . ASP D 1 146 ? 5.605   42.392  49.176  1.00 88.88  ? 146 ASP D N   1 
ATOM   13488 C CA  . ASP D 1 146 ? 6.085   43.701  48.737  1.00 92.21  ? 146 ASP D CA  1 
ATOM   13489 C C   . ASP D 1 146 ? 7.305   44.140  49.539  1.00 96.05  ? 146 ASP D C   1 
ATOM   13490 O O   . ASP D 1 146 ? 8.253   44.710  48.984  1.00 105.70 ? 146 ASP D O   1 
ATOM   13491 C CB  . ASP D 1 146 ? 4.963   44.738  48.837  1.00 95.18  ? 146 ASP D CB  1 
ATOM   13492 C CG  . ASP D 1 146 ? 5.269   46.016  48.061  1.00 107.98 ? 146 ASP D CG  1 
ATOM   13493 O OD1 . ASP D 1 146 ? 6.093   46.824  48.542  1.00 111.82 ? 146 ASP D OD1 1 
ATOM   13494 O OD2 . ASP D 1 146 ? 4.691   46.212  46.968  1.00 109.59 ? 146 ASP D OD2 1 
ATOM   13495 N N   . LEU D 1 147 ? 7.312   43.865  50.841  1.00 84.63  ? 147 LEU D N   1 
ATOM   13496 C CA  . LEU D 1 147 ? 8.435   44.207  51.701  1.00 89.14  ? 147 LEU D CA  1 
ATOM   13497 C C   . LEU D 1 147 ? 9.422   43.058  51.854  1.00 87.86  ? 147 LEU D C   1 
ATOM   13498 O O   . LEU D 1 147 ? 10.161  43.006  52.844  1.00 92.67  ? 147 LEU D O   1 
ATOM   13499 C CB  . LEU D 1 147 ? 7.929   44.651  53.070  1.00 84.43  ? 147 LEU D CB  1 
ATOM   13500 C CG  . LEU D 1 147 ? 6.950   45.818  53.001  1.00 83.74  ? 147 LEU D CG  1 
ATOM   13501 C CD1 . LEU D 1 147 ? 6.666   46.341  54.392  1.00 84.02  ? 147 LEU D CD1 1 
ATOM   13502 C CD2 . LEU D 1 147 ? 7.484   46.927  52.096  1.00 92.68  ? 147 LEU D CD2 1 
ATOM   13503 N N   . LYS D 1 148 ? 9.451   42.137  50.894  1.00 84.30  ? 148 LYS D N   1 
ATOM   13504 C CA  . LYS D 1 148 ? 10.304  40.964  51.029  1.00 89.96  ? 148 LYS D CA  1 
ATOM   13505 C C   . LYS D 1 148 ? 11.777  41.311  50.894  1.00 82.41  ? 148 LYS D C   1 
ATOM   13506 O O   . LYS D 1 148 ? 12.610  40.853  51.687  1.00 79.00  ? 148 LYS D O   1 
ATOM   13507 C CB  . LYS D 1 148 ? 9.951   39.921  49.989  1.00 91.61  ? 148 LYS D CB  1 
ATOM   13508 C CG  . LYS D 1 148 ? 10.719  38.685  50.300  1.00 98.66  ? 148 LYS D CG  1 
ATOM   13509 C CD  . LYS D 1 148 ? 9.802   37.524  50.561  1.00 96.82  ? 148 LYS D CD  1 
ATOM   13510 C CE  . LYS D 1 148 ? 10.485  36.441  51.413  1.00 97.73  ? 148 LYS D CE  1 
ATOM   13511 N NZ  . LYS D 1 148 ? 10.208  36.643  52.885  1.00 100.71 ? 148 LYS D NZ  1 
ATOM   13512 N N   . ASP D 1 149 ? 12.124  42.075  49.862  1.00 81.92  ? 149 ASP D N   1 
ATOM   13513 C CA  . ASP D 1 149 ? 13.523  42.401  49.634  1.00 82.84  ? 149 ASP D CA  1 
ATOM   13514 C C   . ASP D 1 149 ? 14.094  43.165  50.819  1.00 85.42  ? 149 ASP D C   1 
ATOM   13515 O O   . ASP D 1 149 ? 15.188  42.853  51.304  1.00 84.96  ? 149 ASP D O   1 
ATOM   13516 C CB  . ASP D 1 149 ? 13.665  43.189  48.335  1.00 84.59  ? 149 ASP D CB  1 
ATOM   13517 C CG  . ASP D 1 149 ? 13.479  42.314  47.109  1.00 97.78  ? 149 ASP D CG  1 
ATOM   13518 O OD1 . ASP D 1 149 ? 13.918  41.144  47.143  1.00 97.16  ? 149 ASP D OD1 1 
ATOM   13519 O OD2 . ASP D 1 149 ? 12.892  42.791  46.114  1.00 100.84 ? 149 ASP D OD2 1 
ATOM   13520 N N   . LEU D 1 150 ? 13.346  44.146  51.327  1.00 78.40  ? 150 LEU D N   1 
ATOM   13521 C CA  . LEU D 1 150 ? 13.810  44.875  52.500  1.00 74.53  ? 150 LEU D CA  1 
ATOM   13522 C C   . LEU D 1 150 ? 14.037  43.928  53.669  1.00 77.77  ? 150 LEU D C   1 
ATOM   13523 O O   . LEU D 1 150 ? 15.029  44.047  54.396  1.00 78.64  ? 150 LEU D O   1 
ATOM   13524 C CB  . LEU D 1 150 ? 12.807  45.962  52.870  1.00 69.09  ? 150 LEU D CB  1 
ATOM   13525 C CG  . LEU D 1 150 ? 12.565  46.979  51.759  1.00 66.74  ? 150 LEU D CG  1 
ATOM   13526 C CD1 . LEU D 1 150 ? 11.134  47.472  51.790  1.00 81.50  ? 150 LEU D CD1 1 
ATOM   13527 C CD2 . LEU D 1 150 ? 13.527  48.125  51.902  1.00 72.53  ? 150 LEU D CD2 1 
ATOM   13528 N N   . LEU D 1 151 ? 13.145  42.952  53.833  1.00 81.67  ? 151 LEU D N   1 
ATOM   13529 C CA  . LEU D 1 151 ? 13.272  42.000  54.928  1.00 75.30  ? 151 LEU D CA  1 
ATOM   13530 C C   . LEU D 1 151 ? 14.527  41.148  54.779  1.00 77.08  ? 151 LEU D C   1 
ATOM   13531 O O   . LEU D 1 151 ? 15.210  40.856  55.767  1.00 77.29  ? 151 LEU D O   1 
ATOM   13532 C CB  . LEU D 1 151 ? 12.023  41.122  54.981  1.00 76.97  ? 151 LEU D CB  1 
ATOM   13533 C CG  . LEU D 1 151 ? 10.951  41.508  55.999  1.00 82.42  ? 151 LEU D CG  1 
ATOM   13534 C CD1 . LEU D 1 151 ? 9.710   40.649  55.794  1.00 87.96  ? 151 LEU D CD1 1 
ATOM   13535 C CD2 . LEU D 1 151 ? 11.488  41.380  57.420  1.00 71.58  ? 151 LEU D CD2 1 
ATOM   13536 N N   . ASN D 1 152 ? 14.860  40.754  53.549  1.00 75.57  ? 152 ASN D N   1 
ATOM   13537 C CA  . ASN D 1 152 ? 15.981  39.842  53.357  1.00 79.24  ? 152 ASN D CA  1 
ATOM   13538 C C   . ASN D 1 152 ? 17.323  40.518  53.604  1.00 80.86  ? 152 ASN D C   1 
ATOM   13539 O O   . ASN D 1 152 ? 18.282  39.849  54.008  1.00 82.64  ? 152 ASN D O   1 
ATOM   13540 C CB  . ASN D 1 152 ? 15.942  39.248  51.953  1.00 86.17  ? 152 ASN D CB  1 
ATOM   13541 C CG  . ASN D 1 152 ? 15.625  37.769  51.961  1.00 89.85  ? 152 ASN D CG  1 
ATOM   13542 O OD1 . ASN D 1 152 ? 16.323  36.975  52.595  1.00 90.87  ? 152 ASN D OD1 1 
ATOM   13543 N ND2 . ASN D 1 152 ? 14.560  37.389  51.268  1.00 98.61  ? 152 ASN D ND2 1 
ATOM   13544 N N   . LYS D 1 153 ? 17.420  41.828  53.364  1.00 80.87  ? 153 LYS D N   1 
ATOM   13545 C CA  . LYS D 1 153 ? 18.658  42.551  53.647  1.00 80.15  ? 153 LYS D CA  1 
ATOM   13546 C C   . LYS D 1 153 ? 19.053  42.400  55.112  1.00 77.59  ? 153 LYS D C   1 
ATOM   13547 O O   . LYS D 1 153 ? 20.145  41.924  55.437  1.00 74.83  ? 153 LYS D O   1 
ATOM   13548 C CB  . LYS D 1 153 ? 18.499  44.031  53.293  1.00 81.71  ? 153 LYS D CB  1 
ATOM   13549 C CG  . LYS D 1 153 ? 17.969  44.302  51.893  1.00 82.93  ? 153 LYS D CG  1 
ATOM   13550 C CD  . LYS D 1 153 ? 17.812  45.796  51.652  1.00 81.86  ? 153 LYS D CD  1 
ATOM   13551 C CE  . LYS D 1 153 ? 18.932  46.590  52.296  1.00 81.17  ? 153 LYS D CE  1 
ATOM   13552 N NZ  . LYS D 1 153 ? 20.006  46.838  51.308  1.00 77.52  ? 153 LYS D NZ  1 
ATOM   13553 N N   . GLY D 1 154 ? 18.158  42.789  56.015  1.00 82.87  ? 154 GLY D N   1 
ATOM   13554 C CA  . GLY D 1 154 ? 18.440  42.719  57.428  1.00 87.70  ? 154 GLY D CA  1 
ATOM   13555 C C   . GLY D 1 154 ? 19.293  43.844  57.969  1.00 85.09  ? 154 GLY D C   1 
ATOM   13556 O O   . GLY D 1 154 ? 19.403  43.974  59.193  1.00 90.54  ? 154 GLY D O   1 
ATOM   13557 N N   . ARG D 1 155 ? 19.889  44.667  57.113  1.00 78.97  ? 155 ARG D N   1 
ATOM   13558 C CA  . ARG D 1 155 ? 20.746  45.762  57.557  1.00 82.35  ? 155 ARG D CA  1 
ATOM   13559 C C   . ARG D 1 155 ? 20.818  46.804  56.445  1.00 85.52  ? 155 ARG D C   1 
ATOM   13560 O O   . ARG D 1 155 ? 20.152  46.682  55.410  1.00 79.48  ? 155 ARG D O   1 
ATOM   13561 C CB  . ARG D 1 155 ? 22.143  45.251  57.934  1.00 86.51  ? 155 ARG D CB  1 
ATOM   13562 C CG  . ARG D 1 155 ? 22.605  44.047  57.114  1.00 86.06  ? 155 ARG D CG  1 
ATOM   13563 C CD  . ARG D 1 155 ? 23.916  43.459  57.618  1.00 85.66  ? 155 ARG D CD  1 
ATOM   13564 N NE  . ARG D 1 155 ? 23.978  43.402  59.075  1.00 85.97  ? 155 ARG D NE  1 
ATOM   13565 C CZ  . ARG D 1 155 ? 23.836  42.294  59.792  1.00 91.17  ? 155 ARG D CZ  1 
ATOM   13566 N NH1 . ARG D 1 155 ? 23.612  41.122  59.221  1.00 94.88  ? 155 ARG D NH1 1 
ATOM   13567 N NH2 . ARG D 1 155 ? 23.922  42.364  61.115  1.00 95.03  ? 155 ARG D NH2 1 
ATOM   13568 N N   . ASN D 1 156 ? 21.647  47.829  56.658  1.00 84.42  ? 156 ASN D N   1 
ATOM   13569 C CA  . ASN D 1 156 ? 21.971  48.819  55.631  1.00 90.34  ? 156 ASN D CA  1 
ATOM   13570 C C   . ASN D 1 156 ? 20.734  49.580  55.151  1.00 85.49  ? 156 ASN D C   1 
ATOM   13571 O O   . ASN D 1 156 ? 20.699  50.086  54.026  1.00 90.19  ? 156 ASN D O   1 
ATOM   13572 C CB  . ASN D 1 156 ? 22.691  48.168  54.443  1.00 93.08  ? 156 ASN D CB  1 
ATOM   13573 C CG  . ASN D 1 156 ? 23.557  46.982  54.854  1.00 91.70  ? 156 ASN D CG  1 
ATOM   13574 O OD1 . ASN D 1 156 ? 23.310  45.847  54.441  1.00 94.96  ? 156 ASN D OD1 1 
ATOM   13575 N ND2 . ASN D 1 156 ? 24.573  47.242  55.671  1.00 86.72  ? 156 ASN D ND2 1 
ATOM   13576 N N   . TYR D 1 157 ? 19.714  49.671  56.000  1.00 82.08  ? 157 TYR D N   1 
ATOM   13577 C CA  . TYR D 1 157 ? 18.502  50.395  55.642  1.00 82.23  ? 157 TYR D CA  1 
ATOM   13578 C C   . TYR D 1 157 ? 18.758  51.896  55.615  1.00 85.06  ? 157 TYR D C   1 
ATOM   13579 O O   . TYR D 1 157 ? 19.553  52.429  56.395  1.00 95.15  ? 157 TYR D O   1 
ATOM   13580 C CB  . TYR D 1 157 ? 17.377  50.082  56.625  1.00 71.33  ? 157 TYR D CB  1 
ATOM   13581 C CG  . TYR D 1 157 ? 16.972  48.630  56.632  1.00 74.26  ? 157 TYR D CG  1 
ATOM   13582 C CD1 . TYR D 1 157 ? 16.091  48.125  55.683  1.00 73.18  ? 157 TYR D CD1 1 
ATOM   13583 C CD2 . TYR D 1 157 ? 17.481  47.758  57.582  1.00 75.07  ? 157 TYR D CD2 1 
ATOM   13584 C CE1 . TYR D 1 157 ? 15.724  46.789  55.690  1.00 72.15  ? 157 TYR D CE1 1 
ATOM   13585 C CE2 . TYR D 1 157 ? 17.121  46.425  57.595  1.00 79.89  ? 157 TYR D CE2 1 
ATOM   13586 C CZ  . TYR D 1 157 ? 16.245  45.942  56.650  1.00 74.49  ? 157 TYR D CZ  1 
ATOM   13587 O OH  . TYR D 1 157 ? 15.897  44.610  56.675  1.00 73.87  ? 157 TYR D OH  1 
ATOM   13588 N N   . THR D 1 158 ? 18.081  52.574  54.695  1.00 82.92  ? 158 THR D N   1 
ATOM   13589 C CA  . THR D 1 158 ? 18.105  54.025  54.598  1.00 84.98  ? 158 THR D CA  1 
ATOM   13590 C C   . THR D 1 158 ? 16.787  54.593  55.106  1.00 78.61  ? 158 THR D C   1 
ATOM   13591 O O   . THR D 1 158 ? 15.812  53.870  55.331  1.00 80.33  ? 158 THR D O   1 
ATOM   13592 C CB  . THR D 1 158 ? 18.376  54.482  53.155  1.00 75.97  ? 158 THR D CB  1 
ATOM   13593 O OG1 . THR D 1 158 ? 17.184  54.367  52.366  1.00 74.99  ? 158 THR D OG1 1 
ATOM   13594 C CG2 . THR D 1 158 ? 19.476  53.648  52.537  1.00 75.45  ? 158 THR D CG2 1 
ATOM   13595 N N   . GLN D 1 159 ? 16.776  55.909  55.313  1.00 80.20  ? 159 GLN D N   1 
ATOM   13596 C CA  . GLN D 1 159 ? 15.545  56.561  55.740  1.00 78.72  ? 159 GLN D CA  1 
ATOM   13597 C C   . GLN D 1 159 ? 14.426  56.315  54.737  1.00 79.68  ? 159 GLN D C   1 
ATOM   13598 O O   . GLN D 1 159 ? 13.310  55.957  55.124  1.00 80.71  ? 159 GLN D O   1 
ATOM   13599 C CB  . GLN D 1 159 ? 15.784  58.056  55.944  1.00 83.42  ? 159 GLN D CB  1 
ATOM   13600 C CG  . GLN D 1 159 ? 14.532  58.822  56.328  1.00 88.61  ? 159 GLN D CG  1 
ATOM   13601 C CD  . GLN D 1 159 ? 14.523  59.270  57.780  1.00 82.54  ? 159 GLN D CD  1 
ATOM   13602 O OE1 . GLN D 1 159 ? 14.757  58.476  58.692  1.00 76.47  ? 159 GLN D OE1 1 
ATOM   13603 N NE2 . GLN D 1 159 ? 14.245  60.551  57.998  1.00 80.77  ? 159 GLN D NE2 1 
ATOM   13604 N N   . GLU D 1 160 ? 14.726  56.441  53.440  1.00 76.24  ? 160 GLU D N   1 
ATOM   13605 C CA  . GLU D 1 160 ? 13.707  56.289  52.401  1.00 78.91  ? 160 GLU D CA  1 
ATOM   13606 C C   . GLU D 1 160 ? 12.985  54.949  52.510  1.00 81.25  ? 160 GLU D C   1 
ATOM   13607 O O   . GLU D 1 160 ? 11.747  54.896  52.532  1.00 79.18  ? 160 GLU D O   1 
ATOM   13608 C CB  . GLU D 1 160 ? 14.347  56.440  51.021  1.00 75.84  ? 160 GLU D CB  1 
ATOM   13609 C CG  . GLU D 1 160 ? 14.647  57.878  50.650  1.00 77.29  ? 160 GLU D CG  1 
ATOM   13610 C CD  . GLU D 1 160 ? 15.884  58.422  51.351  1.00 88.97  ? 160 GLU D CD  1 
ATOM   13611 O OE1 . GLU D 1 160 ? 16.953  57.774  51.286  1.00 89.35  ? 160 GLU D OE1 1 
ATOM   13612 O OE2 . GLU D 1 160 ? 15.782  59.500  51.973  1.00 87.44  ? 160 GLU D OE2 1 
ATOM   13613 N N   . GLU D 1 161 ? 13.745  53.850  52.572  1.00 82.56  ? 161 GLU D N   1 
ATOM   13614 C CA  . GLU D 1 161 ? 13.128  52.537  52.740  1.00 79.92  ? 161 GLU D CA  1 
ATOM   13615 C C   . GLU D 1 161 ? 12.345  52.443  54.040  1.00 73.58  ? 161 GLU D C   1 
ATOM   13616 O O   . GLU D 1 161 ? 11.347  51.716  54.105  1.00 81.13  ? 161 GLU D O   1 
ATOM   13617 C CB  . GLU D 1 161 ? 14.185  51.430  52.687  1.00 79.96  ? 161 GLU D CB  1 
ATOM   13618 C CG  . GLU D 1 161 ? 15.228  51.606  51.605  1.00 84.94  ? 161 GLU D CG  1 
ATOM   13619 C CD  . GLU D 1 161 ? 16.499  50.820  51.876  1.00 90.87  ? 161 GLU D CD  1 
ATOM   13620 O OE1 . GLU D 1 161 ? 16.651  49.720  51.303  1.00 93.82  ? 161 GLU D OE1 1 
ATOM   13621 O OE2 . GLU D 1 161 ? 17.346  51.301  52.657  1.00 86.53  ? 161 GLU D OE2 1 
ATOM   13622 N N   . LYS D 1 162 ? 12.779  53.154  55.085  1.00 68.28  ? 162 LYS D N   1 
ATOM   13623 C CA  . LYS D 1 162 ? 12.003  53.184  56.319  1.00 70.58  ? 162 LYS D CA  1 
ATOM   13624 C C   . LYS D 1 162 ? 10.662  53.877  56.101  1.00 75.88  ? 162 LYS D C   1 
ATOM   13625 O O   . LYS D 1 162 ? 9.610   53.346  56.476  1.00 73.87  ? 162 LYS D O   1 
ATOM   13626 C CB  . LYS D 1 162 ? 12.786  53.873  57.437  1.00 73.46  ? 162 LYS D CB  1 
ATOM   13627 C CG  . LYS D 1 162 ? 12.312  53.483  58.829  1.00 84.48  ? 162 LYS D CG  1 
ATOM   13628 C CD  . LYS D 1 162 ? 12.205  54.700  59.740  1.00 80.19  ? 162 LYS D CD  1 
ATOM   13629 C CE  . LYS D 1 162 ? 13.492  55.507  59.741  1.00 70.16  ? 162 LYS D CE  1 
ATOM   13630 N NZ  . LYS D 1 162 ? 13.361  56.890  60.292  1.00 63.29  ? 162 LYS D NZ  1 
ATOM   13631 N N   . GLU D 1 163 ? 10.679  55.073  55.501  1.00 75.92  ? 163 GLU D N   1 
ATOM   13632 C CA  . GLU D 1 163 ? 9.428   55.776  55.225  1.00 67.52  ? 163 GLU D CA  1 
ATOM   13633 C C   . GLU D 1 163 ? 8.557   55.001  54.249  1.00 70.23  ? 163 GLU D C   1 
ATOM   13634 O O   . GLU D 1 163 ? 7.326   55.074  54.328  1.00 74.65  ? 163 GLU D O   1 
ATOM   13635 C CB  . GLU D 1 163 ? 9.713   57.178  54.685  1.00 70.99  ? 163 GLU D CB  1 
ATOM   13636 C CG  . GLU D 1 163 ? 10.974  57.791  55.264  1.00 82.74  ? 163 GLU D CG  1 
ATOM   13637 C CD  . GLU D 1 163 ? 11.145  59.262  54.947  1.00 89.53  ? 163 GLU D CD  1 
ATOM   13638 O OE1 . GLU D 1 163 ? 11.558  59.570  53.810  1.00 98.53  ? 163 GLU D OE1 1 
ATOM   13639 O OE2 . GLU D 1 163 ? 10.901  60.106  55.837  1.00 97.80  ? 163 GLU D OE2 1 
ATOM   13640 N N   . TYR D 1 164 ? 9.170   54.257  53.325  1.00 70.31  ? 164 TYR D N   1 
ATOM   13641 C CA  . TYR D 1 164 ? 8.388   53.375  52.465  1.00 78.82  ? 164 TYR D CA  1 
ATOM   13642 C C   . TYR D 1 164 ? 7.602   52.366  53.290  1.00 78.00  ? 164 TYR D C   1 
ATOM   13643 O O   . TYR D 1 164 ? 6.424   52.107  53.014  1.00 84.03  ? 164 TYR D O   1 
ATOM   13644 C CB  . TYR D 1 164 ? 9.302   52.655  51.475  1.00 75.74  ? 164 TYR D CB  1 
ATOM   13645 C CG  . TYR D 1 164 ? 8.581   51.679  50.574  1.00 81.37  ? 164 TYR D CG  1 
ATOM   13646 C CD1 . TYR D 1 164 ? 7.562   52.106  49.734  1.00 89.94  ? 164 TYR D CD1 1 
ATOM   13647 C CD2 . TYR D 1 164 ? 8.920   50.332  50.560  1.00 83.06  ? 164 TYR D CD2 1 
ATOM   13648 C CE1 . TYR D 1 164 ? 6.900   51.222  48.902  1.00 92.76  ? 164 TYR D CE1 1 
ATOM   13649 C CE2 . TYR D 1 164 ? 8.263   49.438  49.730  1.00 91.67  ? 164 TYR D CE2 1 
ATOM   13650 C CZ  . TYR D 1 164 ? 7.252   49.891  48.902  1.00 95.82  ? 164 TYR D CZ  1 
ATOM   13651 O OH  . TYR D 1 164 ? 6.586   49.020  48.069  1.00 99.66  ? 164 TYR D OH  1 
ATOM   13652 N N   . VAL D 1 165 ? 8.237   51.791  54.313  1.00 69.95  ? 165 VAL D N   1 
ATOM   13653 C CA  . VAL D 1 165 ? 7.566   50.811  55.162  1.00 71.96  ? 165 VAL D CA  1 
ATOM   13654 C C   . VAL D 1 165 ? 6.379   51.451  55.871  1.00 68.80  ? 165 VAL D C   1 
ATOM   13655 O O   . VAL D 1 165 ? 5.280   50.885  55.917  1.00 72.15  ? 165 VAL D O   1 
ATOM   13656 C CB  . VAL D 1 165 ? 8.567   50.206  56.166  1.00 74.84  ? 165 VAL D CB  1 
ATOM   13657 C CG1 . VAL D 1 165 ? 7.833   49.541  57.341  1.00 66.11  ? 165 VAL D CG1 1 
ATOM   13658 C CG2 . VAL D 1 165 ? 9.515   49.230  55.465  1.00 64.44  ? 165 VAL D CG2 1 
ATOM   13659 N N   . LEU D 1 166 ? 6.582   52.647  56.429  1.00 67.45  ? 166 LEU D N   1 
ATOM   13660 C CA  . LEU D 1 166 ? 5.519   53.295  57.190  1.00 70.37  ? 166 LEU D CA  1 
ATOM   13661 C C   . LEU D 1 166 ? 4.331   53.622  56.299  1.00 75.13  ? 166 LEU D C   1 
ATOM   13662 O O   . LEU D 1 166 ? 3.174   53.453  56.702  1.00 74.69  ? 166 LEU D O   1 
ATOM   13663 C CB  . LEU D 1 166 ? 6.048   54.560  57.871  1.00 68.03  ? 166 LEU D CB  1 
ATOM   13664 C CG  . LEU D 1 166 ? 6.572   54.365  59.296  1.00 65.20  ? 166 LEU D CG  1 
ATOM   13665 C CD1 . LEU D 1 166 ? 7.497   55.499  59.741  1.00 59.18  ? 166 LEU D CD1 1 
ATOM   13666 C CD2 . LEU D 1 166 ? 5.414   54.191  60.263  1.00 66.78  ? 166 LEU D CD2 1 
ATOM   13667 N N   . ASN D 1 167 ? 4.599   54.080  55.077  1.00 70.65  ? 167 ASN D N   1 
ATOM   13668 C CA  . ASN D 1 167 ? 3.514   54.342  54.142  1.00 74.53  ? 167 ASN D CA  1 
ATOM   13669 C C   . ASN D 1 167 ? 2.795   53.058  53.755  1.00 74.51  ? 167 ASN D C   1 
ATOM   13670 O O   . ASN D 1 167 ? 1.570   53.054  53.584  1.00 81.49  ? 167 ASN D O   1 
ATOM   13671 C CB  . ASN D 1 167 ? 4.056   55.061  52.915  1.00 74.73  ? 167 ASN D CB  1 
ATOM   13672 C CG  . ASN D 1 167 ? 3.950   56.550  53.048  1.00 82.48  ? 167 ASN D CG  1 
ATOM   13673 O OD1 . ASN D 1 167 ? 4.834   57.198  53.607  1.00 86.72  ? 167 ASN D OD1 1 
ATOM   13674 N ND2 . ASN D 1 167 ? 2.857   57.109  52.550  1.00 84.83  ? 167 ASN D ND2 1 
ATOM   13675 N N   . LYS D 1 168 ? 3.537   51.958  53.619  1.00 68.16  ? 168 LYS D N   1 
ATOM   13676 C CA  . LYS D 1 168 ? 2.896   50.671  53.375  1.00 74.61  ? 168 LYS D CA  1 
ATOM   13677 C C   . LYS D 1 168 ? 2.078   50.236  54.583  1.00 76.55  ? 168 LYS D C   1 
ATOM   13678 O O   . LYS D 1 168 ? 0.946   49.761  54.436  1.00 79.47  ? 168 LYS D O   1 
ATOM   13679 C CB  . LYS D 1 168 ? 3.945   49.616  53.028  1.00 71.40  ? 168 LYS D CB  1 
ATOM   13680 C CG  . LYS D 1 168 ? 4.450   49.689  51.604  1.00 79.17  ? 168 LYS D CG  1 
ATOM   13681 C CD  . LYS D 1 168 ? 3.502   48.986  50.649  1.00 85.79  ? 168 LYS D CD  1 
ATOM   13682 C CE  . LYS D 1 168 ? 3.455   49.690  49.309  1.00 87.04  ? 168 LYS D CE  1 
ATOM   13683 N NZ  . LYS D 1 168 ? 3.308   51.163  49.482  1.00 90.20  ? 168 LYS D NZ  1 
ATOM   13684 N N   . TYR D 1 169 ? 2.635   50.398  55.785  1.00 75.05  ? 169 TYR D N   1 
ATOM   13685 C CA  . TYR D 1 169 ? 1.909   50.034  56.994  1.00 69.34  ? 169 TYR D CA  1 
ATOM   13686 C C   . TYR D 1 169 ? 0.643   50.864  57.138  1.00 67.87  ? 169 TYR D C   1 
ATOM   13687 O O   . TYR D 1 169 ? -0.432  50.327  57.426  1.00 69.93  ? 169 TYR D O   1 
ATOM   13688 C CB  . TYR D 1 169 ? 2.808   50.212  58.216  1.00 66.92  ? 169 TYR D CB  1 
ATOM   13689 C CG  . TYR D 1 169 ? 3.848   49.125  58.380  1.00 70.90  ? 169 TYR D CG  1 
ATOM   13690 C CD1 . TYR D 1 169 ? 4.021   48.143  57.410  1.00 72.95  ? 169 TYR D CD1 1 
ATOM   13691 C CD2 . TYR D 1 169 ? 4.645   49.070  59.513  1.00 67.33  ? 169 TYR D CD2 1 
ATOM   13692 C CE1 . TYR D 1 169 ? 4.969   47.148  57.561  1.00 74.72  ? 169 TYR D CE1 1 
ATOM   13693 C CE2 . TYR D 1 169 ? 5.589   48.081  59.676  1.00 68.22  ? 169 TYR D CE2 1 
ATOM   13694 C CZ  . TYR D 1 169 ? 5.752   47.119  58.699  1.00 77.88  ? 169 TYR D CZ  1 
ATOM   13695 O OH  . TYR D 1 169 ? 6.701   46.129  58.860  1.00 83.06  ? 169 TYR D OH  1 
ATOM   13696 N N   . PHE D 1 170 ? 0.751   52.181  56.926  1.00 69.05  ? 170 PHE D N   1 
ATOM   13697 C CA  . PHE D 1 170 ? -0.405  53.054  57.108  1.00 74.84  ? 170 PHE D CA  1 
ATOM   13698 C C   . PHE D 1 170 ? -1.492  52.753  56.089  1.00 71.30  ? 170 PHE D C   1 
ATOM   13699 O O   . PHE D 1 170 ? -2.680  52.959  56.367  1.00 73.98  ? 170 PHE D O   1 
ATOM   13700 C CB  . PHE D 1 170 ? 0.018   54.525  57.032  1.00 73.64  ? 170 PHE D CB  1 
ATOM   13701 C CG  . PHE D 1 170 ? 0.273   55.154  58.382  1.00 77.86  ? 170 PHE D CG  1 
ATOM   13702 C CD1 . PHE D 1 170 ? -0.769  55.351  59.281  1.00 81.15  ? 170 PHE D CD1 1 
ATOM   13703 C CD2 . PHE D 1 170 ? 1.551   55.539  58.757  1.00 74.68  ? 170 PHE D CD2 1 
ATOM   13704 C CE1 . PHE D 1 170 ? -0.538  55.925  60.530  1.00 81.80  ? 170 PHE D CE1 1 
ATOM   13705 C CE2 . PHE D 1 170 ? 1.788   56.112  60.003  1.00 76.28  ? 170 PHE D CE2 1 
ATOM   13706 C CZ  . PHE D 1 170 ? 0.744   56.305  60.888  1.00 79.90  ? 170 PHE D CZ  1 
ATOM   13707 N N   . GLU D 1 171 ? -1.107  52.255  54.914  1.00 68.43  ? 171 GLU D N   1 
ATOM   13708 C CA  . GLU D 1 171 ? -2.090  51.784  53.946  1.00 69.65  ? 171 GLU D CA  1 
ATOM   13709 C C   . GLU D 1 171 ? -2.928  50.650  54.519  1.00 69.96  ? 171 GLU D C   1 
ATOM   13710 O O   . GLU D 1 171 ? -4.153  50.626  54.349  1.00 78.36  ? 171 GLU D O   1 
ATOM   13711 C CB  . GLU D 1 171 ? -1.384  51.330  52.674  1.00 74.36  ? 171 GLU D CB  1 
ATOM   13712 C CG  . GLU D 1 171 ? -1.595  52.238  51.492  1.00 84.54  ? 171 GLU D CG  1 
ATOM   13713 C CD  . GLU D 1 171 ? -0.954  51.689  50.237  1.00 91.14  ? 171 GLU D CD  1 
ATOM   13714 O OE1 . GLU D 1 171 ? -0.844  50.449  50.116  1.00 82.43  ? 171 GLU D OE1 1 
ATOM   13715 O OE2 . GLU D 1 171 ? -0.563  52.498  49.371  1.00 92.16  ? 171 GLU D OE2 1 
ATOM   13716 N N   . ILE D 1 172 ? -2.283  49.697  55.194  1.00 64.16  ? 172 ILE D N   1 
ATOM   13717 C CA  . ILE D 1 172 ? -3.006  48.609  55.845  1.00 65.03  ? 172 ILE D CA  1 
ATOM   13718 C C   . ILE D 1 172 ? -3.969  49.159  56.880  1.00 66.21  ? 172 ILE D C   1 
ATOM   13719 O O   . ILE D 1 172 ? -5.080  48.646  57.055  1.00 77.17  ? 172 ILE D O   1 
ATOM   13720 C CB  . ILE D 1 172 ? -2.016  47.623  56.485  1.00 74.51  ? 172 ILE D CB  1 
ATOM   13721 C CG1 . ILE D 1 172 ? -1.009  47.135  55.440  1.00 71.66  ? 172 ILE D CG1 1 
ATOM   13722 C CG2 . ILE D 1 172 ? -2.770  46.493  57.192  1.00 64.15  ? 172 ILE D CG2 1 
ATOM   13723 C CD1 . ILE D 1 172 ? -1.365  45.824  54.796  1.00 78.70  ? 172 ILE D CD1 1 
ATOM   13724 N N   . ILE D 1 173 ? -3.552  50.203  57.594  1.00 60.81  ? 173 ILE D N   1 
ATOM   13725 C CA  . ILE D 1 173 ? -4.429  50.814  58.583  1.00 64.75  ? 173 ILE D CA  1 
ATOM   13726 C C   . ILE D 1 173 ? -5.648  51.421  57.905  1.00 66.36  ? 173 ILE D C   1 
ATOM   13727 O O   . ILE D 1 173 ? -6.779  51.293  58.391  1.00 61.90  ? 173 ILE D O   1 
ATOM   13728 C CB  . ILE D 1 173 ? -3.652  51.859  59.398  1.00 66.22  ? 173 ILE D CB  1 
ATOM   13729 C CG1 . ILE D 1 173 ? -2.564  51.171  60.216  1.00 64.67  ? 173 ILE D CG1 1 
ATOM   13730 C CG2 . ILE D 1 173 ? -4.597  52.638  60.290  1.00 68.97  ? 173 ILE D CG2 1 
ATOM   13731 C CD1 . ILE D 1 173 ? -1.672  52.128  60.940  1.00 66.21  ? 173 ILE D CD1 1 
ATOM   13732 N N   . LYS D 1 174 ? -5.440  52.073  56.759  1.00 66.20  ? 174 LYS D N   1 
ATOM   13733 C CA  . LYS D 1 174 ? -6.537  52.722  56.053  1.00 66.95  ? 174 LYS D CA  1 
ATOM   13734 C C   . LYS D 1 174 ? -7.532  51.725  55.472  1.00 66.02  ? 174 LYS D C   1 
ATOM   13735 O O   . LYS D 1 174 ? -8.690  52.092  55.241  1.00 61.15  ? 174 LYS D O   1 
ATOM   13736 C CB  . LYS D 1 174 ? -5.985  53.620  54.947  1.00 65.08  ? 174 LYS D CB  1 
ATOM   13737 C CG  . LYS D 1 174 ? -5.463  54.960  55.442  1.00 60.10  ? 174 LYS D CG  1 
ATOM   13738 C CD  . LYS D 1 174 ? -4.812  55.740  54.313  1.00 66.31  ? 174 LYS D CD  1 
ATOM   13739 C CE  . LYS D 1 174 ? -3.299  55.757  54.451  1.00 74.00  ? 174 LYS D CE  1 
ATOM   13740 N NZ  . LYS D 1 174 ? -2.710  57.027  53.944  1.00 76.13  ? 174 LYS D NZ  1 
ATOM   13741 N N   . LYS D 1 175 ? -7.117  50.479  55.241  1.00 63.54  ? 175 LYS D N   1 
ATOM   13742 C CA  . LYS D 1 175 ? -8.002  49.439  54.728  1.00 70.10  ? 175 LYS D CA  1 
ATOM   13743 C C   . LYS D 1 175 ? -8.561  48.527  55.814  1.00 69.57  ? 175 LYS D C   1 
ATOM   13744 O O   . LYS D 1 175 ? -9.332  47.614  55.496  1.00 67.99  ? 175 LYS D O   1 
ATOM   13745 C CB  . LYS D 1 175 ? -7.267  48.589  53.689  1.00 63.64  ? 175 LYS D CB  1 
ATOM   13746 C CG  . LYS D 1 175 ? -6.566  49.404  52.631  1.00 77.96  ? 175 LYS D CG  1 
ATOM   13747 C CD  . LYS D 1 175 ? -6.130  48.537  51.467  1.00 84.69  ? 175 LYS D CD  1 
ATOM   13748 C CE  . LYS D 1 175 ? -5.638  47.178  51.940  1.00 83.02  ? 175 LYS D CE  1 
ATOM   13749 N NZ  . LYS D 1 175 ? -5.263  46.305  50.793  1.00 89.71  ? 175 LYS D NZ  1 
ATOM   13750 N N   . THR D 1 176 ? -8.201  48.751  57.080  1.00 66.96  ? 176 THR D N   1 
ATOM   13751 C CA  . THR D 1 176 ? -8.515  47.786  58.132  1.00 67.45  ? 176 THR D CA  1 
ATOM   13752 C C   . THR D 1 176 ? -10.021 47.635  58.323  1.00 64.91  ? 176 THR D C   1 
ATOM   13753 O O   . THR D 1 176 ? -10.561 46.528  58.233  1.00 63.12  ? 176 THR D O   1 
ATOM   13754 C CB  . THR D 1 176 ? -7.829  48.198  59.438  1.00 62.18  ? 176 THR D CB  1 
ATOM   13755 O OG1 . THR D 1 176 ? -6.416  48.273  59.215  1.00 66.85  ? 176 THR D OG1 1 
ATOM   13756 C CG2 . THR D 1 176 ? -8.100  47.185  60.549  1.00 54.16  ? 176 THR D CG2 1 
ATOM   13757 N N   . LEU D 1 177 ? -10.725 48.735  58.592  1.00 59.52  ? 177 LEU D N   1 
ATOM   13758 C CA  . LEU D 1 177 ? -12.146 48.599  58.902  1.00 63.76  ? 177 LEU D CA  1 
ATOM   13759 C C   . LEU D 1 177 ? -12.938 48.125  57.693  1.00 67.68  ? 177 LEU D C   1 
ATOM   13760 O O   . LEU D 1 177 ? -13.969 47.458  57.846  1.00 70.67  ? 177 LEU D O   1 
ATOM   13761 C CB  . LEU D 1 177 ? -12.717 49.916  59.433  1.00 58.36  ? 177 LEU D CB  1 
ATOM   13762 C CG  . LEU D 1 177 ? -12.521 50.224  60.922  1.00 63.58  ? 177 LEU D CG  1 
ATOM   13763 C CD1 . LEU D 1 177 ? -13.249 49.215  61.767  1.00 76.73  ? 177 LEU D CD1 1 
ATOM   13764 C CD2 . LEU D 1 177 ? -11.065 50.225  61.316  1.00 65.98  ? 177 LEU D CD2 1 
ATOM   13765 N N   . SER D 1 178 ? -12.466 48.434  56.488  1.00 59.87  ? 178 SER D N   1 
ATOM   13766 C CA  . SER D 1 178 ? -13.194 48.028  55.294  1.00 68.36  ? 178 SER D CA  1 
ATOM   13767 C C   . SER D 1 178 ? -13.217 46.513  55.140  1.00 72.49  ? 178 SER D C   1 
ATOM   13768 O O   . SER D 1 178 ? -14.204 45.950  54.649  1.00 78.64  ? 178 SER D O   1 
ATOM   13769 C CB  . SER D 1 178 ? -12.571 48.686  54.071  1.00 66.31  ? 178 SER D CB  1 
ATOM   13770 O OG  . SER D 1 178 ? -12.040 49.937  54.457  1.00 75.96  ? 178 SER D OG  1 
ATOM   13771 N N   . ILE D 1 179 ? -12.145 45.830  55.550  1.00 62.19  ? 179 ILE D N   1 
ATOM   13772 C CA  . ILE D 1 179 ? -12.137 44.383  55.368  1.00 66.04  ? 179 ILE D CA  1 
ATOM   13773 C C   . ILE D 1 179 ? -13.096 43.728  56.348  1.00 64.05  ? 179 ILE D C   1 
ATOM   13774 O O   . ILE D 1 179 ? -13.672 42.675  56.052  1.00 68.34  ? 179 ILE D O   1 
ATOM   13775 C CB  . ILE D 1 179 ? -10.716 43.797  55.490  1.00 74.06  ? 179 ILE D CB  1 
ATOM   13776 C CG1 . ILE D 1 179 ? -10.713 42.330  55.046  1.00 74.33  ? 179 ILE D CG1 1 
ATOM   13777 C CG2 . ILE D 1 179 ? -10.204 43.886  56.908  1.00 73.46  ? 179 ILE D CG2 1 
ATOM   13778 C CD1 . ILE D 1 179 ? -9.403  41.861  54.458  1.00 64.11  ? 179 ILE D CD1 1 
ATOM   13779 N N   . TYR D 1 180 ? -13.304 44.336  57.515  1.00 65.15  ? 180 TYR D N   1 
ATOM   13780 C CA  . TYR D 1 180 ? -14.333 43.822  58.405  1.00 63.06  ? 180 TYR D CA  1 
ATOM   13781 C C   . TYR D 1 180 ? -15.714 44.075  57.823  1.00 66.15  ? 180 TYR D C   1 
ATOM   13782 O O   . TYR D 1 180 ? -16.609 43.232  57.943  1.00 73.24  ? 180 TYR D O   1 
ATOM   13783 C CB  . TYR D 1 180 ? -14.199 44.446  59.791  1.00 54.73  ? 180 TYR D CB  1 
ATOM   13784 C CG  . TYR D 1 180 ? -12.981 43.975  60.544  1.00 59.66  ? 180 TYR D CG  1 
ATOM   13785 C CD1 . TYR D 1 180 ? -13.010 42.806  61.293  1.00 61.55  ? 180 TYR D CD1 1 
ATOM   13786 C CD2 . TYR D 1 180 ? -11.797 44.698  60.503  1.00 57.14  ? 180 TYR D CD2 1 
ATOM   13787 C CE1 . TYR D 1 180 ? -11.893 42.372  61.984  1.00 57.08  ? 180 TYR D CE1 1 
ATOM   13788 C CE2 . TYR D 1 180 ? -10.675 44.273  61.189  1.00 62.14  ? 180 TYR D CE2 1 
ATOM   13789 C CZ  . TYR D 1 180 ? -10.727 43.110  61.931  1.00 61.17  ? 180 TYR D CZ  1 
ATOM   13790 O OH  . TYR D 1 180 ? -9.610  42.682  62.618  1.00 59.75  ? 180 TYR D OH  1 
ATOM   13791 N N   . ARG D 1 181 ? -15.902 45.222  57.168  1.00 61.89  ? 181 ARG D N   1 
ATOM   13792 C CA  . ARG D 1 181 ? -17.186 45.484  56.529  1.00 67.76  ? 181 ARG D CA  1 
ATOM   13793 C C   . ARG D 1 181 ? -17.458 44.472  55.430  1.00 62.70  ? 181 ARG D C   1 
ATOM   13794 O O   . ARG D 1 181 ? -18.603 44.048  55.236  1.00 70.19  ? 181 ARG D O   1 
ATOM   13795 C CB  . ARG D 1 181 ? -17.226 46.902  55.973  1.00 66.49  ? 181 ARG D CB  1 
ATOM   13796 C CG  . ARG D 1 181 ? -18.153 47.813  56.750  1.00 74.38  ? 181 ARG D CG  1 
ATOM   13797 C CD  . ARG D 1 181 ? -18.111 49.225  56.212  1.00 74.40  ? 181 ARG D CD  1 
ATOM   13798 N NE  . ARG D 1 181 ? -16.836 49.875  56.495  1.00 82.11  ? 181 ARG D NE  1 
ATOM   13799 C CZ  . ARG D 1 181 ? -16.703 51.129  56.905  1.00 80.06  ? 181 ARG D CZ  1 
ATOM   13800 N NH1 . ARG D 1 181 ? -17.756 51.907  57.106  1.00 84.30  ? 181 ARG D NH1 1 
ATOM   13801 N NH2 . ARG D 1 181 ? -15.483 51.620  57.109  1.00 70.68  ? 181 ARG D NH2 1 
ATOM   13802 N N   . GLU D 1 182 ? -16.408 44.051  54.723  1.00 73.88  ? 182 GLU D N   1 
ATOM   13803 C CA  . GLU D 1 182 ? -16.562 43.090  53.636  1.00 77.65  ? 182 GLU D CA  1 
ATOM   13804 C C   . GLU D 1 182 ? -17.055 41.746  54.160  1.00 77.21  ? 182 GLU D C   1 
ATOM   13805 O O   . GLU D 1 182 ? -18.139 41.283  53.789  1.00 84.25  ? 182 GLU D O   1 
ATOM   13806 C CB  . GLU D 1 182 ? -15.239 42.922  52.879  1.00 79.69  ? 182 GLU D CB  1 
ATOM   13807 C CG  . GLU D 1 182 ? -15.104 41.586  52.123  1.00 91.05  ? 182 GLU D CG  1 
ATOM   13808 C CD  . GLU D 1 182 ? -13.660 41.173  51.878  1.00 97.44  ? 182 GLU D CD  1 
ATOM   13809 O OE1 . GLU D 1 182 ? -12.765 42.033  52.032  1.00 100.74 ? 182 GLU D OE1 1 
ATOM   13810 O OE2 . GLU D 1 182 ? -13.422 40.003  51.496  1.00 84.89  ? 182 GLU D OE2 1 
ATOM   13811 N N   . ILE D 1 183 ? -16.273 41.113  55.043  1.00 70.19  ? 183 ILE D N   1 
ATOM   13812 C CA  . ILE D 1 183 ? -16.597 39.764  55.498  1.00 63.35  ? 183 ILE D CA  1 
ATOM   13813 C C   . ILE D 1 183 ? -18.000 39.712  56.079  1.00 72.68  ? 183 ILE D C   1 
ATOM   13814 O O   . ILE D 1 183 ? -18.685 38.687  55.974  1.00 74.80  ? 183 ILE D O   1 
ATOM   13815 C CB  . ILE D 1 183 ? -15.554 39.267  56.518  1.00 65.60  ? 183 ILE D CB  1 
ATOM   13816 C CG1 . ILE D 1 183 ? -15.683 40.051  57.823  1.00 64.18  ? 183 ILE D CG1 1 
ATOM   13817 C CG2 . ILE D 1 183 ? -14.135 39.376  55.953  1.00 70.91  ? 183 ILE D CG2 1 
ATOM   13818 C CD1 . ILE D 1 183 ? -15.568 39.202  59.055  1.00 64.51  ? 183 ILE D CD1 1 
ATOM   13819 N N   . LYS D 1 184 ? -18.462 40.819  56.670  1.00 72.86  ? 184 LYS D N   1 
ATOM   13820 C CA  . LYS D 1 184 ? -19.807 40.873  57.232  1.00 67.51  ? 184 LYS D CA  1 
ATOM   13821 C C   . LYS D 1 184 ? -20.858 40.864  56.131  1.00 70.58  ? 184 LYS D C   1 
ATOM   13822 O O   . LYS D 1 184 ? -21.811 40.076  56.174  1.00 70.72  ? 184 LYS D O   1 
ATOM   13823 C CB  . LYS D 1 184 ? -19.957 42.117  58.106  1.00 63.90  ? 184 LYS D CB  1 
ATOM   13824 C CG  . LYS D 1 184 ? -21.038 41.998  59.168  1.00 68.72  ? 184 LYS D CG  1 
ATOM   13825 C CD  . LYS D 1 184 ? -21.493 43.368  59.654  1.00 67.16  ? 184 LYS D CD  1 
ATOM   13826 C CE  . LYS D 1 184 ? -22.996 43.430  59.790  1.00 72.33  ? 184 LYS D CE  1 
ATOM   13827 N NZ  . LYS D 1 184 ? -23.632 44.036  58.586  1.00 72.98  ? 184 LYS D NZ  1 
ATOM   13828 N N   . GLU D 1 185 ? -20.702 41.737  55.133  1.00 69.95  ? 185 GLU D N   1 
ATOM   13829 C CA  . GLU D 1 185 ? -21.656 41.772  54.029  1.00 82.26  ? 185 GLU D CA  1 
ATOM   13830 C C   . GLU D 1 185 ? -21.541 40.529  53.153  1.00 74.61  ? 185 GLU D C   1 
ATOM   13831 O O   . GLU D 1 185 ? -22.558 39.979  52.713  1.00 70.47  ? 185 GLU D O   1 
ATOM   13832 C CB  . GLU D 1 185 ? -21.453 43.040  53.194  1.00 85.83  ? 185 GLU D CB  1 
ATOM   13833 C CG  . GLU D 1 185 ? -22.605 44.053  53.273  1.00 90.21  ? 185 GLU D CG  1 
ATOM   13834 C CD  . GLU D 1 185 ? -23.972 43.462  52.952  1.00 97.28  ? 185 GLU D CD  1 
ATOM   13835 O OE1 . GLU D 1 185 ? -24.991 44.099  53.302  1.00 105.64 ? 185 GLU D OE1 1 
ATOM   13836 O OE2 . GLU D 1 185 ? -24.032 42.386  52.319  1.00 108.54 ? 185 GLU D OE2 1 
ATOM   13837 N N   . GLU D 1 186 ? -20.318 40.058  52.905  1.00 73.20  ? 186 GLU D N   1 
ATOM   13838 C CA  . GLU D 1 186 ? -20.093 38.947  51.986  1.00 72.49  ? 186 GLU D CA  1 
ATOM   13839 C C   . GLU D 1 186 ? -20.473 37.591  52.573  1.00 75.67  ? 186 GLU D C   1 
ATOM   13840 O O   . GLU D 1 186 ? -20.271 36.569  51.906  1.00 78.44  ? 186 GLU D O   1 
ATOM   13841 C CB  . GLU D 1 186 ? -18.629 38.927  51.535  1.00 71.69  ? 186 GLU D CB  1 
ATOM   13842 C CG  . GLU D 1 186 ? -18.145 40.258  50.960  1.00 81.73  ? 186 GLU D CG  1 
ATOM   13843 C CD  . GLU D 1 186 ? -17.373 40.107  49.662  1.00 89.24  ? 186 GLU D CD  1 
ATOM   13844 O OE1 . GLU D 1 186 ? -16.820 39.012  49.421  1.00 92.13  ? 186 GLU D OE1 1 
ATOM   13845 O OE2 . GLU D 1 186 ? -17.319 41.085  48.884  1.00 86.13  ? 186 GLU D OE2 1 
ATOM   13846 N N   . GLY D 1 187 ? -21.024 37.550  53.783  1.00 70.15  ? 187 GLY D N   1 
ATOM   13847 C CA  . GLY D 1 187 ? -21.323 36.275  54.398  1.00 68.22  ? 187 GLY D CA  1 
ATOM   13848 C C   . GLY D 1 187 ? -20.115 35.444  54.761  1.00 77.64  ? 187 GLY D C   1 
ATOM   13849 O O   . GLY D 1 187 ? -20.272 34.260  55.069  1.00 80.66  ? 187 GLY D O   1 
ATOM   13850 N N   . LYS D 1 188 ? -18.908 36.018  54.727  1.00 73.95  ? 188 LYS D N   1 
ATOM   13851 C CA  . LYS D 1 188 ? -17.729 35.258  55.131  1.00 75.04  ? 188 LYS D CA  1 
ATOM   13852 C C   . LYS D 1 188 ? -17.651 35.107  56.642  1.00 68.99  ? 188 LYS D C   1 
ATOM   13853 O O   . LYS D 1 188 ? -17.094 34.120  57.134  1.00 68.07  ? 188 LYS D O   1 
ATOM   13854 C CB  . LYS D 1 188 ? -16.452 35.919  54.607  1.00 76.93  ? 188 LYS D CB  1 
ATOM   13855 C CG  . LYS D 1 188 ? -15.861 35.273  53.351  1.00 78.35  ? 188 LYS D CG  1 
ATOM   13856 C CD  . LYS D 1 188 ? -16.160 36.094  52.106  1.00 74.53  ? 188 LYS D CD  1 
ATOM   13857 C CE  . LYS D 1 188 ? -15.243 35.709  50.957  1.00 87.34  ? 188 LYS D CE  1 
ATOM   13858 N NZ  . LYS D 1 188 ? -15.739 34.507  50.235  1.00 96.86  ? 188 LYS D NZ  1 
ATOM   13859 N N   . GLY D 1 189 ? -18.202 36.056  57.389  1.00 61.66  ? 189 GLY D N   1 
ATOM   13860 C CA  . GLY D 1 189 ? -18.121 35.975  58.834  1.00 70.32  ? 189 GLY D CA  1 
ATOM   13861 C C   . GLY D 1 189 ? -18.989 37.016  59.498  1.00 67.11  ? 189 GLY D C   1 
ATOM   13862 O O   . GLY D 1 189 ? -19.577 37.884  58.846  1.00 69.92  ? 189 GLY D O   1 
ATOM   13863 N N   . SER D 1 190 ? -19.060 36.913  60.819  1.00 65.94  ? 190 SER D N   1 
ATOM   13864 C CA  . SER D 1 190 ? -19.864 37.804  61.640  1.00 75.65  ? 190 SER D CA  1 
ATOM   13865 C C   . SER D 1 190 ? -18.936 38.688  62.458  1.00 56.32  ? 190 SER D C   1 
ATOM   13866 O O   . SER D 1 190 ? -17.864 38.246  62.884  1.00 56.23  ? 190 SER D O   1 
ATOM   13867 C CB  . SER D 1 190 ? -20.800 37.011  62.564  1.00 73.21  ? 190 SER D CB  1 
ATOM   13868 O OG  . SER D 1 190 ? -22.054 36.756  61.948  1.00 75.82  ? 190 SER D OG  1 
ATOM   13869 N N   . VAL D 1 191 ? -19.336 39.941  62.654  1.00 53.30  ? 191 VAL D N   1 
ATOM   13870 C CA  . VAL D 1 191 ? -18.574 40.887  63.458  1.00 67.49  ? 191 VAL D CA  1 
ATOM   13871 C C   . VAL D 1 191 ? -19.431 41.302  64.647  1.00 66.32  ? 191 VAL D C   1 
ATOM   13872 O O   . VAL D 1 191 ? -20.647 41.496  64.523  1.00 60.65  ? 191 VAL D O   1 
ATOM   13873 C CB  . VAL D 1 191 ? -18.101 42.111  62.640  1.00 63.91  ? 191 VAL D CB  1 
ATOM   13874 C CG1 . VAL D 1 191 ? -19.266 42.962  62.199  1.00 67.49  ? 191 VAL D CG1 1 
ATOM   13875 C CG2 . VAL D 1 191 ? -17.113 42.941  63.448  1.00 63.31  ? 191 VAL D CG2 1 
ATOM   13876 N N   . SER D 1 192 ? -18.793 41.406  65.805  1.00 58.01  ? 192 SER D N   1 
ATOM   13877 C CA  . SER D 1 192 ? -19.459 41.712  67.054  1.00 55.40  ? 192 SER D CA  1 
ATOM   13878 C C   . SER D 1 192 ? -18.738 42.870  67.711  1.00 56.48  ? 192 SER D C   1 
ATOM   13879 O O   . SER D 1 192 ? -17.717 43.356  67.219  1.00 62.32  ? 192 SER D O   1 
ATOM   13880 C CB  . SER D 1 192 ? -19.469 40.499  67.983  1.00 59.77  ? 192 SER D CB  1 
ATOM   13881 O OG  . SER D 1 192 ? -18.142 40.120  68.296  1.00 59.29  ? 192 SER D OG  1 
ATOM   13882 N N   . THR D 1 193 ? -19.258 43.302  68.850  1.00 56.26  ? 193 THR D N   1 
ATOM   13883 C CA  . THR D 1 193 ? -18.614 44.364  69.596  1.00 60.67  ? 193 THR D CA  1 
ATOM   13884 C C   . THR D 1 193 ? -18.726 44.042  71.080  1.00 60.28  ? 193 THR D C   1 
ATOM   13885 O O   . THR D 1 193 ? -19.277 43.011  71.476  1.00 62.04  ? 193 THR D O   1 
ATOM   13886 C CB  . THR D 1 193 ? -19.218 45.725  69.229  1.00 52.97  ? 193 THR D CB  1 
ATOM   13887 O OG1 . THR D 1 193 ? -18.299 46.767  69.585  1.00 62.93  ? 193 THR D OG1 1 
ATOM   13888 C CG2 . THR D 1 193 ? -20.550 45.939  69.932  1.00 48.01  ? 193 THR D CG2 1 
ATOM   13889 N N   . SER D 1 194 ? -18.154 44.908  71.898  1.00 52.78  ? 194 SER D N   1 
ATOM   13890 C CA  . SER D 1 194 ? -18.233 44.836  73.348  1.00 53.10  ? 194 SER D CA  1 
ATOM   13891 C C   . SER D 1 194 ? -18.721 46.183  73.838  1.00 57.96  ? 194 SER D C   1 
ATOM   13892 O O   . SER D 1 194 ? -18.813 47.136  73.057  1.00 52.84  ? 194 SER D O   1 
ATOM   13893 C CB  . SER D 1 194 ? -16.857 44.506  73.954  1.00 58.23  ? 194 SER D CB  1 
ATOM   13894 O OG  . SER D 1 194 ? -16.334 43.292  73.437  1.00 56.96  ? 194 SER D OG  1 
ATOM   13895 N N   . PRO D 1 195 ? -19.058 46.301  75.129  1.00 65.79  ? 195 PRO D N   1 
ATOM   13896 C CA  . PRO D 1 195 ? -19.249 47.634  75.713  1.00 58.09  ? 195 PRO D CA  1 
ATOM   13897 C C   . PRO D 1 195 ? -18.014 48.494  75.491  1.00 61.30  ? 195 PRO D C   1 
ATOM   13898 O O   . PRO D 1 195 ? -16.882 48.005  75.534  1.00 58.99  ? 195 PRO D O   1 
ATOM   13899 C CB  . PRO D 1 195 ? -19.468 47.338  77.197  1.00 61.22  ? 195 PRO D CB  1 
ATOM   13900 C CG  . PRO D 1 195 ? -20.106 45.996  77.190  1.00 58.95  ? 195 PRO D CG  1 
ATOM   13901 C CD  . PRO D 1 195 ? -19.386 45.242  76.103  1.00 58.29  ? 195 PRO D CD  1 
ATOM   13902 N N   . TYR D 1 196 ? -18.254 49.799  75.311  1.00 63.69  ? 196 TYR D N   1 
ATOM   13903 C CA  . TYR D 1 196 ? -17.325 50.686  74.607  1.00 62.09  ? 196 TYR D CA  1 
ATOM   13904 C C   . TYR D 1 196 ? -15.863 50.478  75.011  1.00 55.07  ? 196 TYR D C   1 
ATOM   13905 O O   . TYR D 1 196 ? -15.022 50.147  74.171  1.00 54.50  ? 196 TYR D O   1 
ATOM   13906 C CB  . TYR D 1 196 ? -17.743 52.148  74.806  1.00 53.46  ? 196 TYR D CB  1 
ATOM   13907 C CG  . TYR D 1 196 ? -17.463 53.014  73.596  1.00 55.39  ? 196 TYR D CG  1 
ATOM   13908 C CD1 . TYR D 1 196 ? -16.193 53.529  73.366  1.00 54.78  ? 196 TYR D CD1 1 
ATOM   13909 C CD2 . TYR D 1 196 ? -18.460 53.294  72.670  1.00 54.92  ? 196 TYR D CD2 1 
ATOM   13910 C CE1 . TYR D 1 196 ? -15.929 54.317  72.256  1.00 58.37  ? 196 TYR D CE1 1 
ATOM   13911 C CE2 . TYR D 1 196 ? -18.204 54.079  71.559  1.00 55.89  ? 196 TYR D CE2 1 
ATOM   13912 C CZ  . TYR D 1 196 ? -16.941 54.588  71.353  1.00 60.43  ? 196 TYR D CZ  1 
ATOM   13913 O OH  . TYR D 1 196 ? -16.716 55.369  70.236  1.00 63.09  ? 196 TYR D OH  1 
ATOM   13914 N N   . TYR D 1 197 ? -15.539 50.654  76.291  1.00 53.14  ? 197 TYR D N   1 
ATOM   13915 C CA  . TYR D 1 197 ? -14.148 50.695  76.740  1.00 55.28  ? 197 TYR D CA  1 
ATOM   13916 C C   . TYR D 1 197 ? -13.721 49.415  77.457  1.00 57.16  ? 197 TYR D C   1 
ATOM   13917 O O   . TYR D 1 197 ? -12.987 49.459  78.448  1.00 58.07  ? 197 TYR D O   1 
ATOM   13918 C CB  . TYR D 1 197 ? -13.915 51.915  77.627  1.00 53.01  ? 197 TYR D CB  1 
ATOM   13919 C CG  . TYR D 1 197 ? -14.141 53.219  76.897  1.00 55.74  ? 197 TYR D CG  1 
ATOM   13920 C CD1 . TYR D 1 197 ? -13.187 53.713  76.019  1.00 59.46  ? 197 TYR D CD1 1 
ATOM   13921 C CD2 . TYR D 1 197 ? -15.313 53.945  77.069  1.00 55.96  ? 197 TYR D CD2 1 
ATOM   13922 C CE1 . TYR D 1 197 ? -13.387 54.893  75.336  1.00 54.67  ? 197 TYR D CE1 1 
ATOM   13923 C CE2 . TYR D 1 197 ? -15.522 55.131  76.390  1.00 54.63  ? 197 TYR D CE2 1 
ATOM   13924 C CZ  . TYR D 1 197 ? -14.552 55.598  75.524  1.00 52.82  ? 197 TYR D CZ  1 
ATOM   13925 O OH  . TYR D 1 197 ? -14.736 56.772  74.837  1.00 59.84  ? 197 TYR D OH  1 
ATOM   13926 N N   . HIS D 1 198 ? -14.147 48.261  76.939  1.00 60.33  ? 198 HIS D N   1 
ATOM   13927 C CA  . HIS D 1 198 ? -13.853 46.953  77.518  1.00 57.96  ? 198 HIS D CA  1 
ATOM   13928 C C   . HIS D 1 198 ? -14.041 46.918  79.032  1.00 61.18  ? 198 HIS D C   1 
ATOM   13929 O O   . HIS D 1 198 ? -13.130 46.487  79.750  1.00 62.85  ? 198 HIS D O   1 
ATOM   13930 C CB  . HIS D 1 198 ? -12.420 46.543  77.187  1.00 54.83  ? 198 HIS D CB  1 
ATOM   13931 C CG  . HIS D 1 198 ? -12.219 45.066  77.062  1.00 55.60  ? 198 HIS D CG  1 
ATOM   13932 N ND1 . HIS D 1 198 ? -11.326 44.370  77.852  1.00 55.08  ? 198 HIS D ND1 1 
ATOM   13933 C CD2 . HIS D 1 198 ? -12.771 44.157  76.224  1.00 49.49  ? 198 HIS D CD2 1 
ATOM   13934 C CE1 . HIS D 1 198 ? -11.348 43.093  77.514  1.00 55.67  ? 198 HIS D CE1 1 
ATOM   13935 N NE2 . HIS D 1 198 ? -12.216 42.937  76.530  1.00 56.21  ? 198 HIS D NE2 1 
ATOM   13936 N N   . PRO D 1 199 ? -15.180 47.354  79.560  1.00 56.35  ? 199 PRO D N   1 
ATOM   13937 C CA  . PRO D 1 199 ? -15.367 47.371  81.010  1.00 54.56  ? 199 PRO D CA  1 
ATOM   13938 C C   . PRO D 1 199 ? -15.857 46.019  81.521  1.00 65.32  ? 199 PRO D C   1 
ATOM   13939 O O   . PRO D 1 199 ? -16.242 45.132  80.757  1.00 67.91  ? 199 PRO D O   1 
ATOM   13940 C CB  . PRO D 1 199 ? -16.441 48.450  81.191  1.00 60.24  ? 199 PRO D CB  1 
ATOM   13941 C CG  . PRO D 1 199 ? -17.307 48.265  79.988  1.00 61.73  ? 199 PRO D CG  1 
ATOM   13942 C CD  . PRO D 1 199 ? -16.383 47.842  78.860  1.00 56.81  ? 199 PRO D CD  1 
ATOM   13943 N N   . LEU D 1 200 ? -15.844 45.883  82.848  1.00 66.74  ? 200 LEU D N   1 
ATOM   13944 C CA  . LEU D 1 200 ? -16.367 44.696  83.531  1.00 66.42  ? 200 LEU D CA  1 
ATOM   13945 C C   . LEU D 1 200 ? -17.792 44.994  83.995  1.00 60.00  ? 200 LEU D C   1 
ATOM   13946 O O   . LEU D 1 200 ? -18.021 45.392  85.141  1.00 60.15  ? 200 LEU D O   1 
ATOM   13947 C CB  . LEU D 1 200 ? -15.470 44.301  84.699  1.00 62.46  ? 200 LEU D CB  1 
ATOM   13948 C CG  . LEU D 1 200 ? -14.080 43.783  84.336  1.00 58.02  ? 200 LEU D CG  1 
ATOM   13949 C CD1 . LEU D 1 200 ? -13.112 44.079  85.460  1.00 57.62  ? 200 LEU D CD1 1 
ATOM   13950 C CD2 . LEU D 1 200 ? -14.112 42.293  84.028  1.00 56.36  ? 200 LEU D CD2 1 
ATOM   13951 N N   . ILE D 1 201 ? -18.758 44.778  83.092  1.00 61.99  ? 201 ILE D N   1 
ATOM   13952 C CA  . ILE D 1 201 ? -20.150 45.149  83.387  1.00 60.45  ? 201 ILE D CA  1 
ATOM   13953 C C   . ILE D 1 201 ? -20.698 44.466  84.633  1.00 58.21  ? 201 ILE D C   1 
ATOM   13954 O O   . ILE D 1 201 ? -21.371 45.140  85.429  1.00 58.95  ? 201 ILE D O   1 
ATOM   13955 C CB  . ILE D 1 201 ? -21.030 44.929  82.149  1.00 50.30  ? 201 ILE D CB  1 
ATOM   13956 C CG1 . ILE D 1 201 ? -20.536 45.786  80.981  1.00 58.59  ? 201 ILE D CG1 1 
ATOM   13957 C CG2 . ILE D 1 201 ? -22.469 45.282  82.455  1.00 48.54  ? 201 ILE D CG2 1 
ATOM   13958 C CD1 . ILE D 1 201 ? -20.717 47.274  81.198  1.00 57.41  ? 201 ILE D CD1 1 
ATOM   13959 N N   . PRO D 1 202 ? -20.494 43.155  84.866  1.00 51.65  ? 202 PRO D N   1 
ATOM   13960 C CA  . PRO D 1 202 ? -20.989 42.554  86.119  1.00 52.73  ? 202 PRO D CA  1 
ATOM   13961 C C   . PRO D 1 202 ? -20.670 43.350  87.373  1.00 56.49  ? 202 PRO D C   1 
ATOM   13962 O O   . PRO D 1 202 ? -21.552 43.523  88.223  1.00 58.82  ? 202 PRO D O   1 
ATOM   13963 C CB  . PRO D 1 202 ? -20.297 41.187  86.128  1.00 48.54  ? 202 PRO D CB  1 
ATOM   13964 C CG  . PRO D 1 202 ? -20.253 40.823  84.703  1.00 58.74  ? 202 PRO D CG  1 
ATOM   13965 C CD  . PRO D 1 202 ? -19.968 42.117  83.960  1.00 58.71  ? 202 PRO D CD  1 
ATOM   13966 N N   . ILE D 1 203 ? -19.438 43.851  87.503  1.00 58.17  ? 203 ILE D N   1 
ATOM   13967 C CA  . ILE D 1 203 ? -19.059 44.624  88.683  1.00 57.10  ? 203 ILE D CA  1 
ATOM   13968 C C   . ILE D 1 203 ? -19.754 45.983  88.686  1.00 58.19  ? 203 ILE D C   1 
ATOM   13969 O O   . ILE D 1 203 ? -20.215 46.456  89.732  1.00 60.76  ? 203 ILE D O   1 
ATOM   13970 C CB  . ILE D 1 203 ? -17.526 44.765  88.754  1.00 57.70  ? 203 ILE D CB  1 
ATOM   13971 C CG1 . ILE D 1 203 ? -16.866 43.426  88.417  1.00 55.85  ? 203 ILE D CG1 1 
ATOM   13972 C CG2 . ILE D 1 203 ? -17.079 45.278  90.129  1.00 57.71  ? 203 ILE D CG2 1 
ATOM   13973 C CD1 . ILE D 1 203 ? -15.401 43.354  88.770  1.00 54.38  ? 203 ILE D CD1 1 
ATOM   13974 N N   . LEU D 1 204 ? -19.850 46.627  87.518  1.00 52.07  ? 204 LEU D N   1 
ATOM   13975 C CA  . LEU D 1 204 ? -20.457 47.954  87.451  1.00 53.53  ? 204 LEU D CA  1 
ATOM   13976 C C   . LEU D 1 204 ? -21.934 47.942  87.841  1.00 62.84  ? 204 LEU D C   1 
ATOM   13977 O O   . LEU D 1 204 ? -22.423 48.931  88.400  1.00 61.27  ? 204 LEU D O   1 
ATOM   13978 C CB  . LEU D 1 204 ? -20.292 48.540  86.053  1.00 57.51  ? 204 LEU D CB  1 
ATOM   13979 C CG  . LEU D 1 204 ? -18.867 48.924  85.663  1.00 63.50  ? 204 LEU D CG  1 
ATOM   13980 C CD1 . LEU D 1 204 ? -18.877 49.594  84.299  1.00 60.08  ? 204 LEU D CD1 1 
ATOM   13981 C CD2 . LEU D 1 204 ? -18.219 49.821  86.719  1.00 56.65  ? 204 LEU D CD2 1 
ATOM   13982 N N   . LEU D 1 205 ? -22.665 46.857  87.555  1.00 58.64  ? 205 LEU D N   1 
ATOM   13983 C CA  . LEU D 1 205 ? -24.065 46.756  87.966  1.00 58.65  ? 205 LEU D CA  1 
ATOM   13984 C C   . LEU D 1 205 ? -24.174 46.442  89.450  1.00 63.29  ? 205 LEU D C   1 
ATOM   13985 O O   . LEU D 1 205 ? -24.671 47.261  90.229  1.00 77.81  ? 205 LEU D O   1 
ATOM   13986 C CB  . LEU D 1 205 ? -24.812 45.694  87.154  1.00 57.01  ? 205 LEU D CB  1 
ATOM   13987 C CG  . LEU D 1 205 ? -24.686 45.797  85.635  1.00 57.04  ? 205 LEU D CG  1 
ATOM   13988 C CD1 . LEU D 1 205 ? -24.868 44.440  85.007  1.00 50.70  ? 205 LEU D CD1 1 
ATOM   13989 C CD2 . LEU D 1 205 ? -25.678 46.802  85.058  1.00 57.73  ? 205 LEU D CD2 1 
ATOM   13990 N N   . ASN D 1 206 ? -23.729 45.259  89.851  1.00 54.84  ? 206 ASN D N   1 
ATOM   13991 C CA  . ASN D 1 206 ? -23.671 44.911  91.270  1.00 57.39  ? 206 ASN D CA  1 
ATOM   13992 C C   . ASN D 1 206 ? -22.261 44.479  91.643  1.00 59.21  ? 206 ASN D C   1 
ATOM   13993 O O   . ASN D 1 206 ? -21.845 43.360  91.286  1.00 54.99  ? 206 ASN D O   1 
ATOM   13994 C CB  . ASN D 1 206 ? -24.674 43.812  91.607  1.00 52.53  ? 206 ASN D CB  1 
ATOM   13995 C CG  . ASN D 1 206 ? -24.578 43.371  93.049  1.00 65.53  ? 206 ASN D CG  1 
ATOM   13996 O OD1 . ASN D 1 206 ? -24.097 44.116  93.904  1.00 65.50  ? 206 ASN D OD1 1 
ATOM   13997 N ND2 . ASN D 1 206 ? -25.051 42.163  93.335  1.00 66.25  ? 206 ASN D ND2 1 
ATOM   13998 N N   . PRO D 1 207 ? -21.500 45.308  92.364  1.00 60.92  ? 207 PRO D N   1 
ATOM   13999 C CA  . PRO D 1 207 ? -20.140 44.906  92.765  1.00 57.81  ? 207 PRO D CA  1 
ATOM   14000 C C   . PRO D 1 207 ? -20.089 43.653  93.622  1.00 55.85  ? 207 PRO D C   1 
ATOM   14001 O O   . PRO D 1 207 ? -19.028 43.025  93.706  1.00 58.53  ? 207 PRO D O   1 
ATOM   14002 C CB  . PRO D 1 207 ? -19.629 46.133  93.533  1.00 55.90  ? 207 PRO D CB  1 
ATOM   14003 C CG  . PRO D 1 207 ? -20.451 47.269  93.000  1.00 55.30  ? 207 PRO D CG  1 
ATOM   14004 C CD  . PRO D 1 207 ? -21.811 46.679  92.799  1.00 60.05  ? 207 PRO D CD  1 
ATOM   14005 N N   . ASN D 1 208 ? -21.194 43.253  94.239  1.00 54.54  ? 208 ASN D N   1 
ATOM   14006 C CA  . ASN D 1 208 ? -21.211 42.045  95.051  1.00 55.18  ? 208 ASN D CA  1 
ATOM   14007 C C   . ASN D 1 208 ? -21.216 40.765  94.230  1.00 56.77  ? 208 ASN D C   1 
ATOM   14008 O O   . ASN D 1 208 ? -21.292 39.680  94.814  1.00 57.53  ? 208 ASN D O   1 
ATOM   14009 C CB  . ASN D 1 208 ? -22.422 42.063  95.973  1.00 63.40  ? 208 ASN D CB  1 
ATOM   14010 C CG  . ASN D 1 208 ? -22.365 43.192  96.945  1.00 62.25  ? 208 ASN D CG  1 
ATOM   14011 O OD1 . ASN D 1 208 ? -21.395 43.330  97.688  1.00 66.34  ? 208 ASN D OD1 1 
ATOM   14012 N ND2 . ASN D 1 208 ? -23.389 44.034  96.934  1.00 57.79  ? 208 ASN D ND2 1 
ATOM   14013 N N   . CYS D 1 209 ? -21.150 40.856  92.903  1.00 62.61  ? 209 CYS D N   1 
ATOM   14014 C CA  . CYS D 1 209 ? -21.004 39.658  92.085  1.00 61.47  ? 209 CYS D CA  1 
ATOM   14015 C C   . CYS D 1 209 ? -19.690 38.934  92.351  1.00 57.73  ? 209 CYS D C   1 
ATOM   14016 O O   . CYS D 1 209 ? -19.579 37.743  92.045  1.00 59.52  ? 209 CYS D O   1 
ATOM   14017 C CB  . CYS D 1 209 ? -21.100 40.033  90.610  1.00 53.93  ? 209 CYS D CB  1 
ATOM   14018 S SG  . CYS D 1 209 ? -19.863 41.260  90.140  1.00 62.08  ? 209 CYS D SG  1 
ATOM   14019 N N   . VAL D 1 210 ? -18.692 39.627  92.909  1.00 58.69  ? 210 VAL D N   1 
ATOM   14020 C CA  . VAL D 1 210 ? -17.393 39.003  93.144  1.00 61.87  ? 210 VAL D CA  1 
ATOM   14021 C C   . VAL D 1 210 ? -17.490 37.922  94.215  1.00 61.42  ? 210 VAL D C   1 
ATOM   14022 O O   . VAL D 1 210 ? -16.709 36.961  94.210  1.00 65.77  ? 210 VAL D O   1 
ATOM   14023 C CB  . VAL D 1 210 ? -16.347 40.074  93.511  1.00 59.66  ? 210 VAL D CB  1 
ATOM   14024 C CG1 . VAL D 1 210 ? -16.168 41.050  92.361  1.00 61.40  ? 210 VAL D CG1 1 
ATOM   14025 C CG2 . VAL D 1 210 ? -16.750 40.812  94.789  1.00 62.21  ? 210 VAL D CG2 1 
ATOM   14026 N N   . TYR D 1 211 ? -18.443 38.045  95.136  1.00 52.36  ? 211 TYR D N   1 
ATOM   14027 C CA  . TYR D 1 211 ? -18.529 37.125  96.261  1.00 58.18  ? 211 TYR D CA  1 
ATOM   14028 C C   . TYR D 1 211 ? -19.162 35.793  95.895  1.00 55.24  ? 211 TYR D C   1 
ATOM   14029 O O   . TYR D 1 211 ? -19.116 34.858  96.704  1.00 55.77  ? 211 TYR D O   1 
ATOM   14030 C CB  . TYR D 1 211 ? -19.305 37.780  97.404  1.00 54.21  ? 211 TYR D CB  1 
ATOM   14031 C CG  . TYR D 1 211 ? -18.646 39.034  97.918  1.00 53.61  ? 211 TYR D CG  1 
ATOM   14032 C CD1 . TYR D 1 211 ? -17.490 38.971  98.685  1.00 52.28  ? 211 TYR D CD1 1 
ATOM   14033 C CD2 . TYR D 1 211 ? -19.163 40.284  97.611  1.00 56.25  ? 211 TYR D CD2 1 
ATOM   14034 C CE1 . TYR D 1 211 ? -16.883 40.120  99.153  1.00 53.40  ? 211 TYR D CE1 1 
ATOM   14035 C CE2 . TYR D 1 211 ? -18.565 41.432  98.068  1.00 56.92  ? 211 TYR D CE2 1 
ATOM   14036 C CZ  . TYR D 1 211 ? -17.428 41.349  98.837  1.00 57.09  ? 211 TYR D CZ  1 
ATOM   14037 O OH  . TYR D 1 211 ? -16.849 42.510  99.287  1.00 56.95  ? 211 TYR D OH  1 
ATOM   14038 N N   . GLU D 1 212 ? -19.747 35.679  94.704  1.00 53.35  ? 212 GLU D N   1 
ATOM   14039 C CA  . GLU D 1 212 ? -20.288 34.394  94.277  1.00 61.73  ? 212 GLU D CA  1 
ATOM   14040 C C   . GLU D 1 212 ? -19.177 33.357  94.166  1.00 55.68  ? 212 GLU D C   1 
ATOM   14041 O O   . GLU D 1 212 ? -19.287 32.248  94.701  1.00 66.58  ? 212 GLU D O   1 
ATOM   14042 C CB  . GLU D 1 212 ? -21.034 34.561  92.952  1.00 55.83  ? 212 GLU D CB  1 
ATOM   14043 C CG  . GLU D 1 212 ? -21.779 35.883  92.858  1.00 60.50  ? 212 GLU D CG  1 
ATOM   14044 C CD  . GLU D 1 212 ? -22.888 35.862  91.827  1.00 71.02  ? 212 GLU D CD  1 
ATOM   14045 O OE1 . GLU D 1 212 ? -22.912 34.923  91.002  1.00 75.29  ? 212 GLU D OE1 1 
ATOM   14046 O OE2 . GLU D 1 212 ? -23.736 36.781  91.843  1.00 58.74  ? 212 GLU D OE2 1 
ATOM   14047 N N   . THR D 1 213 ? -18.080 33.719  93.509  1.00 55.67  ? 213 THR D N   1 
ATOM   14048 C CA  . THR D 1 213 ? -16.949 32.818  93.347  1.00 60.76  ? 213 THR D CA  1 
ATOM   14049 C C   . THR D 1 213 ? -15.903 32.970  94.438  1.00 63.12  ? 213 THR D C   1 
ATOM   14050 O O   . THR D 1 213 ? -15.206 32.002  94.751  1.00 56.45  ? 213 THR D O   1 
ATOM   14051 C CB  . THR D 1 213 ? -16.284 33.054  91.996  1.00 60.92  ? 213 THR D CB  1 
ATOM   14052 O OG1 . THR D 1 213 ? -16.306 34.458  91.702  1.00 68.40  ? 213 THR D OG1 1 
ATOM   14053 C CG2 . THR D 1 213 ? -17.039 32.302  90.918  1.00 61.25  ? 213 THR D CG2 1 
ATOM   14054 N N   . THR D 1 214 ? -15.772 34.156  95.025  1.00 66.70  ? 214 THR D N   1 
ATOM   14055 C CA  . THR D 1 214 ? -14.731 34.444  96.009  1.00 61.54  ? 214 THR D CA  1 
ATOM   14056 C C   . THR D 1 214 ? -15.386 35.087  97.225  1.00 56.90  ? 214 THR D C   1 
ATOM   14057 O O   . THR D 1 214 ? -15.494 36.319  97.309  1.00 56.76  ? 214 THR D O   1 
ATOM   14058 C CB  . THR D 1 214 ? -13.644 35.331  95.405  1.00 64.50  ? 214 THR D CB  1 
ATOM   14059 O OG1 . THR D 1 214 ? -14.229 36.520  94.848  1.00 65.78  ? 214 THR D OG1 1 
ATOM   14060 C CG2 . THR D 1 214 ? -12.879 34.585  94.323  1.00 63.74  ? 214 THR D CG2 1 
ATOM   14061 N N   . PRO D 1 215 ? -15.827 34.282  98.197  1.00 59.30  ? 215 PRO D N   1 
ATOM   14062 C CA  . PRO D 1 215 ? -16.680 34.828  99.264  1.00 59.28  ? 215 PRO D CA  1 
ATOM   14063 C C   . PRO D 1 215 ? -15.939 35.660  100.301 1.00 65.86  ? 215 PRO D C   1 
ATOM   14064 O O   . PRO D 1 215 ? -16.571 36.506  100.946 1.00 63.62  ? 215 PRO D O   1 
ATOM   14065 C CB  . PRO D 1 215 ? -17.298 33.566  99.889  1.00 51.99  ? 215 PRO D CB  1 
ATOM   14066 C CG  . PRO D 1 215 ? -17.093 32.486  98.857  1.00 57.91  ? 215 PRO D CG  1 
ATOM   14067 C CD  . PRO D 1 215 ? -15.769 32.816  98.263  1.00 59.49  ? 215 PRO D CD  1 
ATOM   14068 N N   . ASN D 1 216 ? -14.639 35.453  100.510 1.00 64.48  ? 216 ASN D N   1 
ATOM   14069 C CA  . ASN D 1 216 ? -13.936 36.156  101.576 1.00 58.35  ? 216 ASN D CA  1 
ATOM   14070 C C   . ASN D 1 216 ? -13.001 37.247  101.066 1.00 60.95  ? 216 ASN D C   1 
ATOM   14071 O O   . ASN D 1 216 ? -12.161 37.732  101.830 1.00 60.09  ? 216 ASN D O   1 
ATOM   14072 C CB  . ASN D 1 216 ? -13.163 35.167  102.449 1.00 57.52  ? 216 ASN D CB  1 
ATOM   14073 C CG  . ASN D 1 216 ? -13.332 35.444  103.942 1.00 74.71  ? 216 ASN D CG  1 
ATOM   14074 O OD1 . ASN D 1 216 ? -14.419 35.796  104.410 1.00 88.67  ? 216 ASN D OD1 1 
ATOM   14075 N ND2 . ASN D 1 216 ? -12.248 35.301  104.692 1.00 73.38  ? 216 ASN D ND2 1 
ATOM   14076 N N   . VAL D 1 217 ? -13.143 37.675  99.808  1.00 53.69  ? 217 VAL D N   1 
ATOM   14077 C CA  . VAL D 1 217 ? -12.325 38.779  99.321  1.00 49.88  ? 217 VAL D CA  1 
ATOM   14078 C C   . VAL D 1 217 ? -12.783 40.101  99.925  1.00 54.99  ? 217 VAL D C   1 
ATOM   14079 O O   . VAL D 1 217 ? -13.937 40.265  100.349 1.00 60.11  ? 217 VAL D O   1 
ATOM   14080 C CB  . VAL D 1 217 ? -12.353 38.853  97.787  1.00 60.26  ? 217 VAL D CB  1 
ATOM   14081 C CG1 . VAL D 1 217 ? -11.850 37.564  97.224  1.00 69.72  ? 217 VAL D CG1 1 
ATOM   14082 C CG2 . VAL D 1 217 ? -13.760 39.166  97.290  1.00 57.51  ? 217 VAL D CG2 1 
ATOM   14083 N N   . LYS D 1 218 ? -11.871 41.060  99.948  1.00 54.86  ? 218 LYS D N   1 
ATOM   14084 C CA  . LYS D 1 218 ? -12.146 42.401  100.432 1.00 56.82  ? 218 LYS D CA  1 
ATOM   14085 C C   . LYS D 1 218 ? -12.114 43.348  99.244  1.00 54.43  ? 218 LYS D C   1 
ATOM   14086 O O   . LYS D 1 218 ? -11.125 43.401  98.504  1.00 50.76  ? 218 LYS D O   1 
ATOM   14087 C CB  . LYS D 1 218 ? -11.144 42.815  101.512 1.00 51.60  ? 218 LYS D CB  1 
ATOM   14088 C CG  . LYS D 1 218 ? -11.357 42.094  102.839 1.00 63.82  ? 218 LYS D CG  1 
ATOM   14089 C CD  . LYS D 1 218 ? -10.510 42.687  103.968 1.00 69.39  ? 218 LYS D CD  1 
ATOM   14090 C CE  . LYS D 1 218 ? -9.147  42.003  104.080 1.00 65.35  ? 218 LYS D CE  1 
ATOM   14091 N NZ  . LYS D 1 218 ? -8.114  42.907  104.660 1.00 64.46  ? 218 LYS D NZ  1 
ATOM   14092 N N   . ILE D 1 219 ? -13.203 44.075  99.059  1.00 56.06  ? 219 ILE D N   1 
ATOM   14093 C CA  . ILE D 1 219 ? -13.310 45.067  97.995  1.00 59.95  ? 219 ILE D CA  1 
ATOM   14094 C C   . ILE D 1 219 ? -13.615 46.400  98.658  1.00 59.77  ? 219 ILE D C   1 
ATOM   14095 O O   . ILE D 1 219 ? -14.063 46.445  99.818  1.00 52.68  ? 219 ILE D O   1 
ATOM   14096 C CB  . ILE D 1 219 ? -14.383 44.676  96.953  1.00 57.93  ? 219 ILE D CB  1 
ATOM   14097 C CG1 . ILE D 1 219 ? -15.780 44.761  97.578  1.00 56.57  ? 219 ILE D CG1 1 
ATOM   14098 C CG2 . ILE D 1 219 ? -14.088 43.299  96.388  1.00 58.75  ? 219 ILE D CG2 1 
ATOM   14099 C CD1 . ILE D 1 219 ? -16.905 44.719  96.584  1.00 48.76  ? 219 ILE D CD1 1 
ATOM   14100 N N   . PRO D 1 220 ? -13.359 47.505  97.968  1.00 61.24  ? 220 PRO D N   1 
ATOM   14101 C CA  . PRO D 1 220 ? -13.677 48.810  98.543  1.00 55.97  ? 220 PRO D CA  1 
ATOM   14102 C C   . PRO D 1 220 ? -15.182 48.986  98.665  1.00 57.20  ? 220 PRO D C   1 
ATOM   14103 O O   . PRO D 1 220 ? -15.973 48.219  98.112  1.00 58.54  ? 220 PRO D O   1 
ATOM   14104 C CB  . PRO D 1 220 ? -13.078 49.788  97.532  1.00 57.54  ? 220 PRO D CB  1 
ATOM   14105 C CG  . PRO D 1 220 ? -13.161 49.038  96.241  1.00 56.68  ? 220 PRO D CG  1 
ATOM   14106 C CD  . PRO D 1 220 ? -12.822 47.630  96.600  1.00 54.87  ? 220 PRO D CD  1 
ATOM   14107 N N   . ASP D 1 221 ? -15.573 50.001  99.432  1.00 58.68  ? 221 ASP D N   1 
ATOM   14108 C CA  . ASP D 1 221 ? -16.979 50.355  99.567  1.00 55.07  ? 221 ASP D CA  1 
ATOM   14109 C C   . ASP D 1 221 ? -17.384 51.202  98.372  1.00 64.98  ? 221 ASP D C   1 
ATOM   14110 O O   . ASP D 1 221 ? -16.797 52.264  98.135  1.00 66.35  ? 221 ASP D O   1 
ATOM   14111 C CB  . ASP D 1 221 ? -17.232 51.109  100.871 1.00 60.23  ? 221 ASP D CB  1 
ATOM   14112 C CG  . ASP D 1 221 ? -18.652 51.672  100.964 1.00 76.25  ? 221 ASP D CG  1 
ATOM   14113 O OD1 . ASP D 1 221 ? -19.612 50.955  100.604 1.00 83.67  ? 221 ASP D OD1 1 
ATOM   14114 O OD2 . ASP D 1 221 ? -18.817 52.831  101.403 1.00 78.67  ? 221 ASP D OD2 1 
ATOM   14115 N N   . PHE D 1 222 ? -18.377 50.729  97.618  1.00 56.15  ? 222 PHE D N   1 
ATOM   14116 C CA  . PHE D 1 222 ? -18.882 51.445  96.448  1.00 57.50  ? 222 PHE D CA  1 
ATOM   14117 C C   . PHE D 1 222 ? -20.008 52.365  96.900  1.00 61.44  ? 222 PHE D C   1 
ATOM   14118 O O   . PHE D 1 222 ? -21.181 51.990  96.909  1.00 59.37  ? 222 PHE D O   1 
ATOM   14119 C CB  . PHE D 1 222 ? -19.357 50.471  95.376  1.00 62.31  ? 222 PHE D CB  1 
ATOM   14120 C CG  . PHE D 1 222 ? -18.241 49.737  94.684  1.00 56.82  ? 222 PHE D CG  1 
ATOM   14121 C CD1 . PHE D 1 222 ? -17.427 48.867  95.387  1.00 47.54  ? 222 PHE D CD1 1 
ATOM   14122 C CD2 . PHE D 1 222 ? -18.008 49.921  93.331  1.00 45.07  ? 222 PHE D CD2 1 
ATOM   14123 C CE1 . PHE D 1 222 ? -16.404 48.196  94.753  1.00 57.40  ? 222 PHE D CE1 1 
ATOM   14124 C CE2 . PHE D 1 222 ? -16.987 49.253  92.694  1.00 47.13  ? 222 PHE D CE2 1 
ATOM   14125 C CZ  . PHE D 1 222 ? -16.183 48.389  93.405  1.00 53.89  ? 222 PHE D CZ  1 
ATOM   14126 N N   . ALA D 1 223 ? -19.645 53.591  97.279  1.00 60.84  ? 223 ALA D N   1 
ATOM   14127 C CA  . ALA D 1 223 ? -20.603 54.605  97.691  1.00 61.62  ? 223 ALA D CA  1 
ATOM   14128 C C   . ALA D 1 223 ? -21.175 55.377  96.512  1.00 57.23  ? 223 ALA D C   1 
ATOM   14129 O O   . ALA D 1 223 ? -21.657 56.501  96.688  1.00 61.98  ? 223 ALA D O   1 
ATOM   14130 C CB  . ALA D 1 223 ? -19.958 55.573  98.686  1.00 61.64  ? 223 ALA D CB  1 
ATOM   14131 N N   . VAL D 1 224 ? -21.115 54.808  95.312  1.00 57.98  ? 224 VAL D N   1 
ATOM   14132 C CA  . VAL D 1 224 ? -21.726 55.395  94.130  1.00 66.08  ? 224 VAL D CA  1 
ATOM   14133 C C   . VAL D 1 224 ? -22.312 54.264  93.301  1.00 62.62  ? 224 VAL D C   1 
ATOM   14134 O O   . VAL D 1 224 ? -21.964 53.093  93.467  1.00 61.17  ? 224 VAL D O   1 
ATOM   14135 C CB  . VAL D 1 224 ? -20.718 56.219  93.293  1.00 70.34  ? 224 VAL D CB  1 
ATOM   14136 C CG1 . VAL D 1 224 ? -19.948 55.309  92.327  1.00 62.89  ? 224 VAL D CG1 1 
ATOM   14137 C CG2 . VAL D 1 224 ? -21.437 57.342  92.549  1.00 57.50  ? 224 VAL D CG2 1 
ATOM   14138 N N   . SER D 1 225 ? -23.221 54.625  92.407  1.00 63.64  ? 225 SER D N   1 
ATOM   14139 C CA  . SER D 1 225 ? -23.785 53.673  91.466  1.00 63.48  ? 225 SER D CA  1 
ATOM   14140 C C   . SER D 1 225 ? -23.019 53.774  90.154  1.00 64.71  ? 225 SER D C   1 
ATOM   14141 O O   . SER D 1 225 ? -22.687 54.877  89.709  1.00 64.37  ? 225 SER D O   1 
ATOM   14142 C CB  . SER D 1 225 ? -25.276 53.936  91.249  1.00 59.69  ? 225 SER D CB  1 
ATOM   14143 O OG  . SER D 1 225 ? -25.775 53.217  90.135  1.00 68.42  ? 225 SER D OG  1 
ATOM   14144 N N   . PHE D 1 226 ? -22.697 52.623  89.565  1.00 60.54  ? 226 PHE D N   1 
ATOM   14145 C CA  . PHE D 1 226 ? -22.156 52.560  88.213  1.00 60.29  ? 226 PHE D CA  1 
ATOM   14146 C C   . PHE D 1 226 ? -23.133 51.903  87.247  1.00 69.45  ? 226 PHE D C   1 
ATOM   14147 O O   . PHE D 1 226 ? -22.765 51.620  86.100  1.00 70.92  ? 226 PHE D O   1 
ATOM   14148 C CB  . PHE D 1 226 ? -20.826 51.804  88.196  1.00 61.60  ? 226 PHE D CB  1 
ATOM   14149 C CG  . PHE D 1 226 ? -19.642 52.610  88.679  1.00 56.46  ? 226 PHE D CG  1 
ATOM   14150 C CD1 . PHE D 1 226 ? -19.098 53.613  87.897  1.00 53.77  ? 226 PHE D CD1 1 
ATOM   14151 C CD2 . PHE D 1 226 ? -19.054 52.332  89.905  1.00 58.44  ? 226 PHE D CD2 1 
ATOM   14152 C CE1 . PHE D 1 226 ? -18.003 54.337  88.336  1.00 63.93  ? 226 PHE D CE1 1 
ATOM   14153 C CE2 . PHE D 1 226 ? -17.960 53.050  90.352  1.00 56.00  ? 226 PHE D CE2 1 
ATOM   14154 C CZ  . PHE D 1 226 ? -17.430 54.056  89.567  1.00 61.92  ? 226 PHE D CZ  1 
ATOM   14155 N N   . ARG D 1 227 ? -24.373 51.662  87.688  1.00 70.57  ? 227 ARG D N   1 
ATOM   14156 C CA  . ARG D 1 227 ? -25.348 50.933  86.881  1.00 65.81  ? 227 ARG D CA  1 
ATOM   14157 C C   . ARG D 1 227 ? -25.713 51.700  85.613  1.00 68.65  ? 227 ARG D C   1 
ATOM   14158 O O   . ARG D 1 227 ? -25.890 51.100  84.544  1.00 65.39  ? 227 ARG D O   1 
ATOM   14159 C CB  . ARG D 1 227 ? -26.593 50.649  87.725  1.00 62.74  ? 227 ARG D CB  1 
ATOM   14160 C CG  . ARG D 1 227 ? -27.159 49.246  87.589  1.00 75.44  ? 227 ARG D CG  1 
ATOM   14161 C CD  . ARG D 1 227 ? -27.797 48.808  88.891  1.00 76.45  ? 227 ARG D CD  1 
ATOM   14162 N NE  . ARG D 1 227 ? -28.324 49.953  89.621  1.00 86.07  ? 227 ARG D NE  1 
ATOM   14163 C CZ  . ARG D 1 227 ? -28.122 50.178  90.912  1.00 86.46  ? 227 ARG D CZ  1 
ATOM   14164 N NH1 . ARG D 1 227 ? -27.449 49.320  91.664  1.00 86.82  ? 227 ARG D NH1 1 
ATOM   14165 N NH2 . ARG D 1 227 ? -28.607 51.290  91.462  1.00 73.25  ? 227 ARG D NH2 1 
ATOM   14166 N N   . GLU D 1 228 ? -25.832 53.023  85.707  1.00 67.52  ? 228 GLU D N   1 
ATOM   14167 C CA  . GLU D 1 228 ? -26.102 53.813  84.513  1.00 61.36  ? 228 GLU D CA  1 
ATOM   14168 C C   . GLU D 1 228 ? -24.927 53.778  83.544  1.00 66.34  ? 228 GLU D C   1 
ATOM   14169 O O   . GLU D 1 228 ? -25.135 53.786  82.327  1.00 66.86  ? 228 GLU D O   1 
ATOM   14170 C CB  . GLU D 1 228 ? -26.423 55.258  84.887  1.00 65.22  ? 228 GLU D CB  1 
ATOM   14171 C CG  . GLU D 1 228 ? -25.380 55.940  85.769  1.00 85.53  ? 228 GLU D CG  1 
ATOM   14172 C CD  . GLU D 1 228 ? -25.354 55.452  87.219  1.00 87.96  ? 228 GLU D CD  1 
ATOM   14173 O OE1 . GLU D 1 228 ? -26.266 54.699  87.651  1.00 72.98  ? 228 GLU D OE1 1 
ATOM   14174 O OE2 . GLU D 1 228 ? -24.409 55.855  87.931  1.00 86.71  ? 228 GLU D OE2 1 
ATOM   14175 N N   . ASP D 1 229 ? -23.693 53.726  84.060  1.00 64.39  ? 229 ASP D N   1 
ATOM   14176 C CA  . ASP D 1 229 ? -22.521 53.696  83.191  1.00 57.33  ? 229 ASP D CA  1 
ATOM   14177 C C   . ASP D 1 229 ? -22.427 52.393  82.409  1.00 62.56  ? 229 ASP D C   1 
ATOM   14178 O O   . ASP D 1 229 ? -21.866 52.375  81.306  1.00 63.26  ? 229 ASP D O   1 
ATOM   14179 C CB  . ASP D 1 229 ? -21.255 53.909  84.010  1.00 61.63  ? 229 ASP D CB  1 
ATOM   14180 C CG  . ASP D 1 229 ? -21.069 55.354  84.419  1.00 69.82  ? 229 ASP D CG  1 
ATOM   14181 O OD1 . ASP D 1 229 ? -21.824 56.218  83.916  1.00 71.72  ? 229 ASP D OD1 1 
ATOM   14182 O OD2 . ASP D 1 229 ? -20.160 55.630  85.230  1.00 58.23  ? 229 ASP D OD2 1 
ATOM   14183 N N   . ALA D 1 230 ? -22.958 51.298  82.959  1.00 58.70  ? 230 ALA D N   1 
ATOM   14184 C CA  . ALA D 1 230 ? -23.035 50.053  82.201  1.00 56.77  ? 230 ALA D CA  1 
ATOM   14185 C C   . ALA D 1 230 ? -23.989 50.181  81.018  1.00 65.97  ? 230 ALA D C   1 
ATOM   14186 O O   . ALA D 1 230 ? -23.711 49.664  79.927  1.00 63.41  ? 230 ALA D O   1 
ATOM   14187 C CB  . ALA D 1 230 ? -23.465 48.907  83.113  1.00 55.82  ? 230 ALA D CB  1 
ATOM   14188 N N   . SER D 1 231 ? -25.123 50.863  81.211  1.00 67.64  ? 231 SER D N   1 
ATOM   14189 C CA  . SER D 1 231 ? -26.026 51.108  80.091  1.00 63.44  ? 231 SER D CA  1 
ATOM   14190 C C   . SER D 1 231 ? -25.341 51.920  79.006  1.00 61.05  ? 231 SER D C   1 
ATOM   14191 O O   . SER D 1 231 ? -25.500 51.634  77.815  1.00 66.11  ? 231 SER D O   1 
ATOM   14192 C CB  . SER D 1 231 ? -27.283 51.827  80.568  1.00 62.79  ? 231 SER D CB  1 
ATOM   14193 O OG  . SER D 1 231 ? -28.023 51.002  81.441  1.00 78.07  ? 231 SER D OG  1 
ATOM   14194 N N   . LYS D 1 232 ? -24.573 52.938  79.402  1.00 56.82  ? 232 LYS D N   1 
ATOM   14195 C CA  . LYS D 1 232 ? -23.924 53.798  78.420  1.00 63.26  ? 232 LYS D CA  1 
ATOM   14196 C C   . LYS D 1 232 ? -22.868 53.043  77.626  1.00 62.16  ? 232 LYS D C   1 
ATOM   14197 O O   . LYS D 1 232 ? -22.710 53.281  76.425  1.00 58.77  ? 232 LYS D O   1 
ATOM   14198 C CB  . LYS D 1 232 ? -23.310 55.021  79.109  1.00 57.89  ? 232 LYS D CB  1 
ATOM   14199 C CG  . LYS D 1 232 ? -24.256 55.724  80.071  1.00 59.71  ? 232 LYS D CG  1 
ATOM   14200 C CD  . LYS D 1 232 ? -24.185 57.245  79.961  1.00 65.55  ? 232 LYS D CD  1 
ATOM   14201 C CE  . LYS D 1 232 ? -23.318 57.860  81.045  1.00 71.55  ? 232 LYS D CE  1 
ATOM   14202 N NZ  . LYS D 1 232 ? -23.472 59.343  81.067  1.00 67.68  ? 232 LYS D NZ  1 
ATOM   14203 N N   . HIS D 1 233 ? -22.145 52.128  78.271  1.00 60.57  ? 233 HIS D N   1 
ATOM   14204 C CA  . HIS D 1 233 ? -21.112 51.387  77.559  1.00 63.73  ? 233 HIS D CA  1 
ATOM   14205 C C   . HIS D 1 233 ? -21.711 50.525  76.456  1.00 65.12  ? 233 HIS D C   1 
ATOM   14206 O O   . HIS D 1 233 ? -21.105 50.368  75.389  1.00 64.46  ? 233 HIS D O   1 
ATOM   14207 C CB  . HIS D 1 233 ? -20.318 50.524  78.533  1.00 61.84  ? 233 HIS D CB  1 
ATOM   14208 C CG  . HIS D 1 233 ? -19.173 51.232  79.186  1.00 57.91  ? 233 HIS D CG  1 
ATOM   14209 N ND1 . HIS D 1 233 ? -19.181 51.581  80.519  1.00 59.06  ? 233 HIS D ND1 1 
ATOM   14210 C CD2 . HIS D 1 233 ? -17.976 51.634  78.699  1.00 58.82  ? 233 HIS D CD2 1 
ATOM   14211 C CE1 . HIS D 1 233 ? -18.042 52.175  80.825  1.00 51.34  ? 233 HIS D CE1 1 
ATOM   14212 N NE2 . HIS D 1 233 ? -17.292 52.219  79.739  1.00 57.82  ? 233 HIS D NE2 1 
ATOM   14213 N N   . VAL D 1 234 ? -22.901 49.963  76.689  1.00 62.48  ? 234 VAL D N   1 
ATOM   14214 C CA  . VAL D 1 234 ? -23.520 49.095  75.691  1.00 66.61  ? 234 VAL D CA  1 
ATOM   14215 C C   . VAL D 1 234 ? -24.264 49.917  74.639  1.00 66.24  ? 234 VAL D C   1 
ATOM   14216 O O   . VAL D 1 234 ? -24.307 49.535  73.462  1.00 61.91  ? 234 VAL D O   1 
ATOM   14217 C CB  . VAL D 1 234 ? -24.443 48.066  76.374  1.00 58.03  ? 234 VAL D CB  1 
ATOM   14218 C CG1 . VAL D 1 234 ? -25.021 47.104  75.356  1.00 59.16  ? 234 VAL D CG1 1 
ATOM   14219 C CG2 . VAL D 1 234 ? -23.683 47.294  77.434  1.00 50.60  ? 234 VAL D CG2 1 
ATOM   14220 N N   . GLU D 1 235 ? -24.839 51.057  75.036  1.00 68.42  ? 235 GLU D N   1 
ATOM   14221 C CA  . GLU D 1 235 ? -25.576 51.891  74.091  1.00 61.72  ? 235 GLU D CA  1 
ATOM   14222 C C   . GLU D 1 235 ? -24.632 52.593  73.126  1.00 61.60  ? 235 GLU D C   1 
ATOM   14223 O O   . GLU D 1 235 ? -24.870 52.608  71.913  1.00 68.99  ? 235 GLU D O   1 
ATOM   14224 C CB  . GLU D 1 235 ? -26.433 52.911  74.843  1.00 69.49  ? 235 GLU D CB  1 
ATOM   14225 C CG  . GLU D 1 235 ? -27.591 52.297  75.612  1.00 74.67  ? 235 GLU D CG  1 
ATOM   14226 C CD  . GLU D 1 235 ? -28.952 52.766  75.127  1.00 93.22  ? 235 GLU D CD  1 
ATOM   14227 O OE1 . GLU D 1 235 ? -29.421 52.248  74.090  1.00 84.38  ? 235 GLU D OE1 1 
ATOM   14228 O OE2 . GLU D 1 235 ? -29.558 53.637  75.790  1.00 101.73 ? 235 GLU D OE2 1 
ATOM   14229 N N   . LEU D 1 236 ? -23.554 53.190  73.648  1.00 63.86  ? 236 LEU D N   1 
ATOM   14230 C CA  . LEU D 1 236 ? -22.582 53.857  72.784  1.00 60.44  ? 236 LEU D CA  1 
ATOM   14231 C C   . LEU D 1 236 ? -21.862 52.868  71.878  1.00 58.09  ? 236 LEU D C   1 
ATOM   14232 O O   . LEU D 1 236 ? -21.436 53.234  70.777  1.00 58.23  ? 236 LEU D O   1 
ATOM   14233 C CB  . LEU D 1 236 ? -21.566 54.638  73.620  1.00 56.03  ? 236 LEU D CB  1 
ATOM   14234 C CG  . LEU D 1 236 ? -22.093 55.820  74.438  1.00 57.80  ? 236 LEU D CG  1 
ATOM   14235 C CD1 . LEU D 1 236 ? -21.254 56.071  75.695  1.00 44.72  ? 236 LEU D CD1 1 
ATOM   14236 C CD2 . LEU D 1 236 ? -22.196 57.069  73.570  1.00 54.84  ? 236 LEU D CD2 1 
ATOM   14237 N N   . ALA D 1 237 ? -21.705 51.621  72.326  1.00 57.47  ? 237 ALA D N   1 
ATOM   14238 C CA  . ALA D 1 237 ? -21.171 50.583  71.453  1.00 55.32  ? 237 ALA D CA  1 
ATOM   14239 C C   . ALA D 1 237 ? -22.121 50.299  70.300  1.00 60.93  ? 237 ALA D C   1 
ATOM   14240 O O   . ALA D 1 237 ? -21.684 50.083  69.162  1.00 62.79  ? 237 ALA D O   1 
ATOM   14241 C CB  . ALA D 1 237 ? -20.913 49.308  72.248  1.00 52.58  ? 237 ALA D CB  1 
ATOM   14242 N N   . LYS D 1 238 ? -23.427 50.283  70.580  1.00 61.34  ? 238 LYS D N   1 
ATOM   14243 C CA  . LYS D 1 238 ? -24.407 50.037  69.527  1.00 64.13  ? 238 LYS D CA  1 
ATOM   14244 C C   . LYS D 1 238 ? -24.361 51.131  68.473  1.00 63.91  ? 238 LYS D C   1 
ATOM   14245 O O   . LYS D 1 238 ? -24.558 50.868  67.283  1.00 60.71  ? 238 LYS D O   1 
ATOM   14246 C CB  . LYS D 1 238 ? -25.813 49.924  70.121  1.00 69.08  ? 238 LYS D CB  1 
ATOM   14247 C CG  . LYS D 1 238 ? -26.166 48.531  70.623  1.00 72.75  ? 238 LYS D CG  1 
ATOM   14248 C CD  . LYS D 1 238 ? -27.674 48.326  70.782  1.00 71.10  ? 238 LYS D CD  1 
ATOM   14249 C CE  . LYS D 1 238 ? -28.374 49.557  71.324  1.00 71.20  ? 238 LYS D CE  1 
ATOM   14250 N NZ  . LYS D 1 238 ? -29.699 49.194  71.895  1.00 68.05  ? 238 LYS D NZ  1 
ATOM   14251 N N   . GLU D 1 239 ? -24.082 52.365  68.890  1.00 70.33  ? 239 GLU D N   1 
ATOM   14252 C CA  . GLU D 1 239 ? -24.025 53.473  67.944  1.00 71.44  ? 239 GLU D CA  1 
ATOM   14253 C C   . GLU D 1 239 ? -22.734 53.467  67.135  1.00 67.49  ? 239 GLU D C   1 
ATOM   14254 O O   . GLU D 1 239 ? -22.742 53.832  65.955  1.00 73.72  ? 239 GLU D O   1 
ATOM   14255 C CB  . GLU D 1 239 ? -24.186 54.797  68.685  1.00 70.70  ? 239 GLU D CB  1 
ATOM   14256 C CG  . GLU D 1 239 ? -25.521 54.937  69.410  1.00 70.60  ? 239 GLU D CG  1 
ATOM   14257 C CD  . GLU D 1 239 ? -26.720 54.357  68.640  1.00 92.35  ? 239 GLU D CD  1 
ATOM   14258 O OE1 . GLU D 1 239 ? -26.836 54.560  67.405  1.00 97.91  ? 239 GLU D OE1 1 
ATOM   14259 O OE2 . GLU D 1 239 ? -27.564 53.698  69.288  1.00 89.47  ? 239 GLU D OE2 1 
ATOM   14260 N N   . LYS D 1 240 ? -21.619 53.053  67.742  1.00 56.96  ? 240 LYS D N   1 
ATOM   14261 C CA  . LYS D 1 240 ? -20.382 52.940  66.977  1.00 62.32  ? 240 LYS D CA  1 
ATOM   14262 C C   . LYS D 1 240 ? -20.475 51.816  65.952  1.00 65.35  ? 240 LYS D C   1 
ATOM   14263 O O   . LYS D 1 240 ? -19.942 51.934  64.841  1.00 66.70  ? 240 LYS D O   1 
ATOM   14264 C CB  . LYS D 1 240 ? -19.195 52.729  67.913  1.00 54.70  ? 240 LYS D CB  1 
ATOM   14265 C CG  . LYS D 1 240 ? -17.847 52.919  67.238  1.00 61.63  ? 240 LYS D CG  1 
ATOM   14266 C CD  . LYS D 1 240 ? -17.611 54.371  66.862  1.00 64.95  ? 240 LYS D CD  1 
ATOM   14267 C CE  . LYS D 1 240 ? -16.330 54.517  66.059  1.00 67.38  ? 240 LYS D CE  1 
ATOM   14268 N NZ  . LYS D 1 240 ? -15.857 55.926  66.015  1.00 74.08  ? 240 LYS D NZ  1 
ATOM   14269 N N   . TYR D 1 241 ? -21.143 50.715  66.311  1.00 58.73  ? 241 TYR D N   1 
ATOM   14270 C CA  . TYR D 1 241 ? -21.359 49.628  65.360  1.00 62.10  ? 241 TYR D CA  1 
ATOM   14271 C C   . TYR D 1 241 ? -22.247 50.077  64.204  1.00 65.18  ? 241 TYR D C   1 
ATOM   14272 O O   . TYR D 1 241 ? -22.075 49.617  63.066  1.00 62.43  ? 241 TYR D O   1 
ATOM   14273 C CB  . TYR D 1 241 ? -21.965 48.428  66.088  1.00 60.90  ? 241 TYR D CB  1 
ATOM   14274 C CG  . TYR D 1 241 ? -21.991 47.128  65.313  1.00 62.53  ? 241 TYR D CG  1 
ATOM   14275 C CD1 . TYR D 1 241 ? -23.060 46.815  64.488  1.00 65.08  ? 241 TYR D CD1 1 
ATOM   14276 C CD2 . TYR D 1 241 ? -20.969 46.196  65.439  1.00 62.87  ? 241 TYR D CD2 1 
ATOM   14277 C CE1 . TYR D 1 241 ? -23.106 45.627  63.789  1.00 66.11  ? 241 TYR D CE1 1 
ATOM   14278 C CE2 . TYR D 1 241 ? -21.005 44.994  64.738  1.00 67.02  ? 241 TYR D CE2 1 
ATOM   14279 C CZ  . TYR D 1 241 ? -22.079 44.718  63.915  1.00 62.22  ? 241 TYR D CZ  1 
ATOM   14280 O OH  . TYR D 1 241 ? -22.138 43.535  63.214  1.00 67.53  ? 241 TYR D OH  1 
ATOM   14281 N N   . PHE D 1 242 ? -23.192 50.982  64.476  1.00 69.59  ? 242 PHE D N   1 
ATOM   14282 C CA  . PHE D 1 242 ? -24.009 51.546  63.407  1.00 70.30  ? 242 PHE D CA  1 
ATOM   14283 C C   . PHE D 1 242 ? -23.159 52.386  62.464  1.00 70.20  ? 242 PHE D C   1 
ATOM   14284 O O   . PHE D 1 242 ? -23.422 52.440  61.256  1.00 74.61  ? 242 PHE D O   1 
ATOM   14285 C CB  . PHE D 1 242 ? -25.144 52.386  63.999  1.00 64.89  ? 242 PHE D CB  1 
ATOM   14286 C CG  . PHE D 1 242 ? -26.365 52.468  63.127  1.00 75.01  ? 242 PHE D CG  1 
ATOM   14287 C CD1 . PHE D 1 242 ? -27.270 51.419  63.065  1.00 81.39  ? 242 PHE D CD1 1 
ATOM   14288 C CD2 . PHE D 1 242 ? -26.609 53.602  62.368  1.00 69.47  ? 242 PHE D CD2 1 
ATOM   14289 C CE1 . PHE D 1 242 ? -28.403 51.503  62.258  1.00 72.87  ? 242 PHE D CE1 1 
ATOM   14290 C CE2 . PHE D 1 242 ? -27.734 53.691  61.563  1.00 66.99  ? 242 PHE D CE2 1 
ATOM   14291 C CZ  . PHE D 1 242 ? -28.631 52.642  61.508  1.00 67.09  ? 242 PHE D CZ  1 
ATOM   14292 N N   . GLU D 1 243 ? -22.136 53.052  63.002  1.00 67.16  ? 243 GLU D N   1 
ATOM   14293 C CA  . GLU D 1 243 ? -21.267 53.884  62.179  1.00 72.32  ? 243 GLU D CA  1 
ATOM   14294 C C   . GLU D 1 243 ? -20.571 53.050  61.113  1.00 75.33  ? 243 GLU D C   1 
ATOM   14295 O O   . GLU D 1 243 ? -20.655 53.341  59.914  1.00 77.00  ? 243 GLU D O   1 
ATOM   14296 C CB  . GLU D 1 243 ? -20.238 54.598  63.059  1.00 70.58  ? 243 GLU D CB  1 
ATOM   14297 C CG  . GLU D 1 243 ? -19.727 55.904  62.471  1.00 74.56  ? 243 GLU D CG  1 
ATOM   14298 C CD  . GLU D 1 243 ? -18.466 56.401  63.155  1.00 80.11  ? 243 GLU D CD  1 
ATOM   14299 O OE1 . GLU D 1 243 ? -18.505 56.649  64.380  1.00 80.40  ? 243 GLU D OE1 1 
ATOM   14300 O OE2 . GLU D 1 243 ? -17.429 56.533  62.470  1.00 79.61  ? 243 GLU D OE2 1 
ATOM   14301 N N   . ILE D 1 244 ? -19.896 51.986  61.539  1.00 68.79  ? 244 ILE D N   1 
ATOM   14302 C CA  . ILE D 1 244 ? -19.100 51.194  60.611  1.00 67.53  ? 244 ILE D CA  1 
ATOM   14303 C C   . ILE D 1 244 ? -20.000 50.364  59.705  1.00 72.10  ? 244 ILE D C   1 
ATOM   14304 O O   . ILE D 1 244 ? -19.963 50.489  58.476  1.00 75.09  ? 244 ILE D O   1 
ATOM   14305 C CB  . ILE D 1 244 ? -18.116 50.306  61.383  1.00 63.82  ? 244 ILE D CB  1 
ATOM   14306 C CG1 . ILE D 1 244 ? -17.512 51.087  62.549  1.00 70.52  ? 244 ILE D CG1 1 
ATOM   14307 C CG2 . ILE D 1 244 ? -17.047 49.803  60.445  1.00 74.81  ? 244 ILE D CG2 1 
ATOM   14308 C CD1 . ILE D 1 244 ? -16.788 52.360  62.139  1.00 64.59  ? 244 ILE D CD1 1 
ATOM   14309 N N   . PHE D 1 245 ? -20.829 49.514  60.297  1.00 70.18  ? 245 PHE D N   1 
ATOM   14310 C CA  . PHE D 1 245 ? -21.520 48.475  59.549  1.00 75.24  ? 245 PHE D CA  1 
ATOM   14311 C C   . PHE D 1 245 ? -22.959 48.828  59.197  1.00 73.96  ? 245 PHE D C   1 
ATOM   14312 O O   . PHE D 1 245 ? -23.632 48.029  58.539  1.00 65.47  ? 245 PHE D O   1 
ATOM   14313 C CB  . PHE D 1 245 ? -21.463 47.161  60.332  1.00 69.21  ? 245 PHE D CB  1 
ATOM   14314 C CG  . PHE D 1 245 ? -20.092 46.839  60.839  1.00 72.61  ? 245 PHE D CG  1 
ATOM   14315 C CD1 . PHE D 1 245 ? -19.175 46.195  60.025  1.00 73.13  ? 245 PHE D CD1 1 
ATOM   14316 C CD2 . PHE D 1 245 ? -19.703 47.219  62.113  1.00 68.79  ? 245 PHE D CD2 1 
ATOM   14317 C CE1 . PHE D 1 245 ? -17.903 45.913  60.486  1.00 67.90  ? 245 PHE D CE1 1 
ATOM   14318 C CE2 . PHE D 1 245 ? -18.435 46.944  62.573  1.00 62.74  ? 245 PHE D CE2 1 
ATOM   14319 C CZ  . PHE D 1 245 ? -17.534 46.288  61.758  1.00 63.42  ? 245 PHE D CZ  1 
ATOM   14320 N N   . GLY D 1 246 ? -23.440 50.000  59.599  1.00 69.04  ? 246 GLY D N   1 
ATOM   14321 C CA  . GLY D 1 246 ? -24.746 50.451  59.171  1.00 63.26  ? 246 GLY D CA  1 
ATOM   14322 C C   . GLY D 1 246 ? -25.926 49.834  59.884  1.00 68.57  ? 246 GLY D C   1 
ATOM   14323 O O   . GLY D 1 246 ? -27.068 50.125  59.514  1.00 73.84  ? 246 GLY D O   1 
ATOM   14324 N N   . GLU D 1 247 ? -25.705 49.002  60.898  1.00 69.28  ? 247 GLU D N   1 
ATOM   14325 C CA  . GLU D 1 247 ? -26.813 48.362  61.593  1.00 69.88  ? 247 GLU D CA  1 
ATOM   14326 C C   . GLU D 1 247 ? -26.468 48.216  63.069  1.00 69.08  ? 247 GLU D C   1 
ATOM   14327 O O   . GLU D 1 247 ? -25.337 48.466  63.495  1.00 67.33  ? 247 GLU D O   1 
ATOM   14328 C CB  . GLU D 1 247 ? -27.163 47.013  60.953  1.00 72.64  ? 247 GLU D CB  1 
ATOM   14329 C CG  . GLU D 1 247 ? -26.037 45.985  60.972  1.00 76.22  ? 247 GLU D CG  1 
ATOM   14330 C CD  . GLU D 1 247 ? -26.554 44.564  60.846  1.00 88.56  ? 247 GLU D CD  1 
ATOM   14331 O OE1 . GLU D 1 247 ? -27.584 44.249  61.482  1.00 97.14  ? 247 GLU D OE1 1 
ATOM   14332 O OE2 . GLU D 1 247 ? -25.944 43.766  60.106  1.00 78.99  ? 247 GLU D OE2 1 
ATOM   14333 N N   . HIS D 1 248 ? -27.446 47.849  63.835  1.00 66.80  ? 248 HIS D N   1 
ATOM   14334 C CA  . HIS D 1 248 ? -27.089 47.734  65.239  1.00 69.41  ? 248 HIS D CA  1 
ATOM   14335 C C   . HIS D 1 248 ? -26.576 46.326  65.533  1.00 66.82  ? 248 HIS D C   1 
ATOM   14336 O O   . HIS D 1 248 ? -26.944 45.367  64.846  1.00 65.31  ? 248 HIS D O   1 
ATOM   14337 C CB  . HIS D 1 248 ? -28.295 48.060  66.124  1.00 63.74  ? 248 HIS D CB  1 
ATOM   14338 C CG  . HIS D 1 248 ? -28.557 49.531  66.277  1.00 69.59  ? 248 HIS D CG  1 
ATOM   14339 N ND1 . HIS D 1 248 ? -27.602 50.418  66.726  1.00 77.19  ? 248 HIS D ND1 1 
ATOM   14340 C CD2 . HIS D 1 248 ? -29.664 50.271  66.028  1.00 74.52  ? 248 HIS D CD2 1 
ATOM   14341 C CE1 . HIS D 1 248 ? -28.112 51.637  66.758  1.00 78.86  ? 248 HIS D CE1 1 
ATOM   14342 N NE2 . HIS D 1 248 ? -29.362 51.576  66.337  1.00 77.63  ? 248 HIS D NE2 1 
ATOM   14343 N N   . PRO D 1 249 ? -25.693 46.171  66.521  1.00 65.16  ? 249 PRO D N   1 
ATOM   14344 C CA  . PRO D 1 249 ? -25.123 44.847  66.788  1.00 64.54  ? 249 PRO D CA  1 
ATOM   14345 C C   . PRO D 1 249 ? -26.128 43.974  67.528  1.00 69.97  ? 249 PRO D C   1 
ATOM   14346 O O   . PRO D 1 249 ? -26.806 44.424  68.456  1.00 71.25  ? 249 PRO D O   1 
ATOM   14347 C CB  . PRO D 1 249 ? -23.897 45.159  67.653  1.00 57.77  ? 249 PRO D CB  1 
ATOM   14348 C CG  . PRO D 1 249 ? -24.316 46.372  68.404  1.00 58.07  ? 249 PRO D CG  1 
ATOM   14349 C CD  . PRO D 1 249 ? -25.146 47.189  67.435  1.00 62.44  ? 249 PRO D CD  1 
ATOM   14350 N N   . VAL D 1 250 ? -26.237 42.721  67.091  1.00 72.02  ? 250 VAL D N   1 
ATOM   14351 C CA  . VAL D 1 250 ? -27.097 41.739  67.745  1.00 68.21  ? 250 VAL D CA  1 
ATOM   14352 C C   . VAL D 1 250 ? -26.309 40.668  68.479  1.00 69.94  ? 250 VAL D C   1 
ATOM   14353 O O   . VAL D 1 250 ? -26.909 39.890  69.239  1.00 68.82  ? 250 VAL D O   1 
ATOM   14354 C CB  . VAL D 1 250 ? -28.065 41.077  66.741  1.00 78.32  ? 250 VAL D CB  1 
ATOM   14355 C CG1 . VAL D 1 250 ? -29.041 42.103  66.162  1.00 70.51  ? 250 VAL D CG1 1 
ATOM   14356 C CG2 . VAL D 1 250 ? -27.275 40.409  65.628  1.00 72.82  ? 250 VAL D CG2 1 
ATOM   14357 N N   . TYR D 1 251 ? -24.998 40.589  68.269  1.00 67.81  ? 251 TYR D N   1 
ATOM   14358 C CA  . TYR D 1 251 ? -24.126 39.684  69.002  1.00 62.53  ? 251 TYR D CA  1 
ATOM   14359 C C   . TYR D 1 251 ? -23.041 40.509  69.680  1.00 62.13  ? 251 TYR D C   1 
ATOM   14360 O O   . TYR D 1 251 ? -22.498 41.437  69.071  1.00 65.25  ? 251 TYR D O   1 
ATOM   14361 C CB  . TYR D 1 251 ? -23.499 38.624  68.077  1.00 68.93  ? 251 TYR D CB  1 
ATOM   14362 C CG  . TYR D 1 251 ? -24.429 38.082  67.012  1.00 75.17  ? 251 TYR D CG  1 
ATOM   14363 C CD1 . TYR D 1 251 ? -25.421 37.174  67.341  1.00 77.39  ? 251 TYR D CD1 1 
ATOM   14364 C CD2 . TYR D 1 251 ? -24.295 38.454  65.672  1.00 71.34  ? 251 TYR D CD2 1 
ATOM   14365 C CE1 . TYR D 1 251 ? -26.276 36.669  66.384  1.00 77.71  ? 251 TYR D CE1 1 
ATOM   14366 C CE2 . TYR D 1 251 ? -25.149 37.944  64.698  1.00 73.44  ? 251 TYR D CE2 1 
ATOM   14367 C CZ  . TYR D 1 251 ? -26.138 37.052  65.064  1.00 73.12  ? 251 TYR D CZ  1 
ATOM   14368 O OH  . TYR D 1 251 ? -27.003 36.538  64.121  1.00 82.01  ? 251 TYR D OH  1 
ATOM   14369 N N   . MET D 1 252 ? -22.748 40.196  70.943  1.00 60.93  ? 252 MET D N   1 
ATOM   14370 C CA  . MET D 1 252 ? -21.729 40.925  71.686  1.00 60.75  ? 252 MET D CA  1 
ATOM   14371 C C   . MET D 1 252 ? -20.849 39.957  72.458  1.00 60.94  ? 252 MET D C   1 
ATOM   14372 O O   . MET D 1 252 ? -21.316 38.932  72.961  1.00 60.05  ? 252 MET D O   1 
ATOM   14373 C CB  . MET D 1 252 ? -22.327 41.936  72.679  1.00 54.72  ? 252 MET D CB  1 
ATOM   14374 C CG  . MET D 1 252 ? -22.211 43.391  72.243  1.00 57.00  ? 252 MET D CG  1 
ATOM   14375 S SD  . MET D 1 252 ? -23.139 44.496  73.321  1.00 70.32  ? 252 MET D SD  1 
ATOM   14376 C CE  . MET D 1 252 ? -22.959 46.087  72.513  1.00 50.36  ? 252 MET D CE  1 
ATOM   14377 N N   . TRP D 1 253 ? -19.566 40.304  72.565  1.00 61.24  ? 253 TRP D N   1 
ATOM   14378 C CA  . TRP D 1 253 ? -18.647 39.551  73.404  1.00 59.66  ? 253 TRP D CA  1 
ATOM   14379 C C   . TRP D 1 253 ? -18.462 40.278  74.725  1.00 56.40  ? 253 TRP D C   1 
ATOM   14380 O O   . TRP D 1 253 ? -17.971 41.417  74.722  1.00 49.71  ? 253 TRP D O   1 
ATOM   14381 C CB  . TRP D 1 253 ? -17.302 39.373  72.717  1.00 52.64  ? 253 TRP D CB  1 
ATOM   14382 C CG  . TRP D 1 253 ? -16.210 38.947  73.651  1.00 51.26  ? 253 TRP D CG  1 
ATOM   14383 C CD1 . TRP D 1 253 ? -15.155 39.703  74.076  1.00 54.70  ? 253 TRP D CD1 1 
ATOM   14384 C CD2 . TRP D 1 253 ? -16.052 37.659  74.263  1.00 53.31  ? 253 TRP D CD2 1 
ATOM   14385 N NE1 . TRP D 1 253 ? -14.357 38.972  74.919  1.00 55.60  ? 253 TRP D NE1 1 
ATOM   14386 C CE2 . TRP D 1 253 ? -14.883 37.713  75.050  1.00 60.24  ? 253 TRP D CE2 1 
ATOM   14387 C CE3 . TRP D 1 253 ? -16.785 36.468  74.223  1.00 57.06  ? 253 TRP D CE3 1 
ATOM   14388 C CZ2 . TRP D 1 253 ? -14.430 36.620  75.796  1.00 59.35  ? 253 TRP D CZ2 1 
ATOM   14389 C CZ3 . TRP D 1 253 ? -16.330 35.382  74.963  1.00 63.78  ? 253 TRP D CZ3 1 
ATOM   14390 C CH2 . TRP D 1 253 ? -15.164 35.468  75.738  1.00 53.97  ? 253 TRP D CH2 1 
ATOM   14391 N N   . PRO D 1 254 ? -18.824 39.686  75.861  1.00 59.62  ? 254 PRO D N   1 
ATOM   14392 C CA  . PRO D 1 254 ? -18.566 40.337  77.140  1.00 55.38  ? 254 PRO D CA  1 
ATOM   14393 C C   . PRO D 1 254 ? -17.072 40.400  77.404  1.00 54.52  ? 254 PRO D C   1 
ATOM   14394 O O   . PRO D 1 254 ? -16.354 39.407  77.207  1.00 50.31  ? 254 PRO D O   1 
ATOM   14395 C CB  . PRO D 1 254 ? -19.276 39.426  78.151  1.00 53.46  ? 254 PRO D CB  1 
ATOM   14396 C CG  . PRO D 1 254 ? -19.246 38.097  77.514  1.00 53.55  ? 254 PRO D CG  1 
ATOM   14397 C CD  . PRO D 1 254 ? -19.459 38.369  76.043  1.00 53.95  ? 254 PRO D CD  1 
ATOM   14398 N N   . PRO D 1 255 ? -16.563 41.558  77.818  1.00 56.36  ? 255 PRO D N   1 
ATOM   14399 C CA  . PRO D 1 255 ? -15.133 41.674  78.111  1.00 54.17  ? 255 PRO D CA  1 
ATOM   14400 C C   . PRO D 1 255 ? -14.720 40.703  79.204  1.00 59.77  ? 255 PRO D C   1 
ATOM   14401 O O   . PRO D 1 255 ? -15.418 40.536  80.210  1.00 57.95  ? 255 PRO D O   1 
ATOM   14402 C CB  . PRO D 1 255 ? -14.985 43.132  78.552  1.00 51.57  ? 255 PRO D CB  1 
ATOM   14403 C CG  . PRO D 1 255 ? -16.123 43.823  77.878  1.00 54.13  ? 255 PRO D CG  1 
ATOM   14404 C CD  . PRO D 1 255 ? -17.249 42.845  77.989  1.00 63.67  ? 255 PRO D CD  1 
ATOM   14405 N N   . GLN D 1 256 ? -13.581 40.049  78.980  1.00 53.84  ? 256 GLN D N   1 
ATOM   14406 C CA  . GLN D 1 256 ? -13.018 39.047  79.878  1.00 52.08  ? 256 GLN D CA  1 
ATOM   14407 C C   . GLN D 1 256 ? -13.969 37.876  80.107  1.00 55.06  ? 256 GLN D C   1 
ATOM   14408 O O   . GLN D 1 256 ? -13.842 37.162  81.106  1.00 59.01  ? 256 GLN D O   1 
ATOM   14409 C CB  . GLN D 1 256 ? -12.610 39.672  81.219  1.00 55.82  ? 256 GLN D CB  1 
ATOM   14410 C CG  . GLN D 1 256 ? -11.910 41.019  81.099  1.00 49.46  ? 256 GLN D CG  1 
ATOM   14411 C CD  . GLN D 1 256 ? -10.447 40.875  80.741  1.00 55.95  ? 256 GLN D CD  1 
ATOM   14412 O OE1 . GLN D 1 256 ? -9.968  39.767  80.500  1.00 50.37  ? 256 GLN D OE1 1 
ATOM   14413 N NE2 . GLN D 1 256 ? -9.726  41.994  80.700  1.00 56.71  ? 256 GLN D NE2 1 
ATOM   14414 N N   . ALA D 1 257 ? -14.923 37.666  79.197  1.00 56.32  ? 257 ALA D N   1 
ATOM   14415 C CA  . ALA D 1 257 ? -15.977 36.662  79.340  1.00 55.76  ? 257 ALA D CA  1 
ATOM   14416 C C   . ALA D 1 257 ? -16.840 36.899  80.582  1.00 59.95  ? 257 ALA D C   1 
ATOM   14417 O O   . ALA D 1 257 ? -17.589 36.010  81.004  1.00 58.64  ? 257 ALA D O   1 
ATOM   14418 C CB  . ALA D 1 257 ? -15.395 35.243  79.353  1.00 51.13  ? 257 ALA D CB  1 
ATOM   14419 N N   . SER D 1 258 ? -16.769 38.095  81.167  1.00 54.63  ? 258 SER D N   1 
ATOM   14420 C CA  . SER D 1 258 ? -17.468 38.368  82.415  1.00 54.31  ? 258 SER D CA  1 
ATOM   14421 C C   . SER D 1 258 ? -18.971 38.359  82.189  1.00 55.47  ? 258 SER D C   1 
ATOM   14422 O O   . SER D 1 258 ? -19.490 39.097  81.344  1.00 60.71  ? 258 SER D O   1 
ATOM   14423 C CB  . SER D 1 258 ? -17.022 39.705  82.999  1.00 59.05  ? 258 SER D CB  1 
ATOM   14424 O OG  . SER D 1 258 ? -17.662 40.777  82.333  1.00 68.54  ? 258 SER D OG  1 
ATOM   14425 N N   . VAL D 1 259 ? -19.668 37.514  82.942  1.00 67.38  ? 259 VAL D N   1 
ATOM   14426 C CA  . VAL D 1 259 ? -21.117 37.404  82.875  1.00 54.01  ? 259 VAL D CA  1 
ATOM   14427 C C   . VAL D 1 259 ? -21.666 37.435  84.289  1.00 57.23  ? 259 VAL D C   1 
ATOM   14428 O O   . VAL D 1 259 ? -21.015 37.007  85.249  1.00 54.02  ? 259 VAL D O   1 
ATOM   14429 C CB  . VAL D 1 259 ? -21.594 36.122  82.156  1.00 52.54  ? 259 VAL D CB  1 
ATOM   14430 C CG1 . VAL D 1 259 ? -21.495 36.290  80.654  1.00 56.09  ? 259 VAL D CG1 1 
ATOM   14431 C CG2 . VAL D 1 259 ? -20.815 34.900  82.641  1.00 54.84  ? 259 VAL D CG2 1 
ATOM   14432 N N   . SER D 1 260 ? -22.881 37.954  84.401  1.00 62.86  ? 260 SER D N   1 
ATOM   14433 C CA  . SER D 1 260 ? -23.652 37.926  85.629  1.00 58.08  ? 260 SER D CA  1 
ATOM   14434 C C   . SER D 1 260 ? -25.114 37.844  85.233  1.00 54.18  ? 260 SER D C   1 
ATOM   14435 O O   . SER D 1 260 ? -25.483 38.156  84.099  1.00 54.07  ? 260 SER D O   1 
ATOM   14436 C CB  . SER D 1 260 ? -23.387 39.163  86.490  1.00 53.91  ? 260 SER D CB  1 
ATOM   14437 O OG  . SER D 1 260 ? -24.228 40.227  86.085  1.00 58.08  ? 260 SER D OG  1 
ATOM   14438 N N   . ASN D 1 261 ? -25.947 37.409  86.178  1.00 56.28  ? 261 ASN D N   1 
ATOM   14439 C CA  . ASN D 1 261 ? -27.382 37.393  85.924  1.00 56.27  ? 261 ASN D CA  1 
ATOM   14440 C C   . ASN D 1 261 ? -27.890 38.789  85.581  1.00 60.52  ? 261 ASN D C   1 
ATOM   14441 O O   . ASN D 1 261 ? -28.702 38.955  84.663  1.00 60.68  ? 261 ASN D O   1 
ATOM   14442 C CB  . ASN D 1 261 ? -28.128 36.824  87.132  1.00 55.61  ? 261 ASN D CB  1 
ATOM   14443 C CG  . ASN D 1 261 ? -27.821 35.357  87.371  1.00 63.89  ? 261 ASN D CG  1 
ATOM   14444 O OD1 . ASN D 1 261 ? -28.001 34.516  86.488  1.00 65.61  ? 261 ASN D OD1 1 
ATOM   14445 N ND2 . ASN D 1 261 ? -27.374 35.040  88.580  1.00 68.67  ? 261 ASN D ND2 1 
ATOM   14446 N N   . GLU D 1 262 ? -27.408 39.810  86.292  1.00 58.30  ? 262 GLU D N   1 
ATOM   14447 C CA  . GLU D 1 262 ? -27.812 41.176  85.972  1.00 63.69  ? 262 GLU D CA  1 
ATOM   14448 C C   . GLU D 1 262 ? -27.252 41.620  84.625  1.00 59.89  ? 262 GLU D C   1 
ATOM   14449 O O   . GLU D 1 262 ? -27.944 42.292  83.851  1.00 59.17  ? 262 GLU D O   1 
ATOM   14450 C CB  . GLU D 1 262 ? -27.365 42.127  87.083  1.00 63.07  ? 262 GLU D CB  1 
ATOM   14451 C CG  . GLU D 1 262 ? -27.643 41.600  88.479  1.00 68.25  ? 262 GLU D CG  1 
ATOM   14452 C CD  . GLU D 1 262 ? -26.409 40.985  89.113  1.00 80.86  ? 262 GLU D CD  1 
ATOM   14453 O OE1 . GLU D 1 262 ? -26.264 39.747  89.049  1.00 77.46  ? 262 GLU D OE1 1 
ATOM   14454 O OE2 . GLU D 1 262 ? -25.578 41.736  89.662  1.00 80.58  ? 262 GLU D OE2 1 
ATOM   14455 N N   . ALA D 1 263 ? -26.002 41.255  84.326  1.00 57.06  ? 263 ALA D N   1 
ATOM   14456 C CA  . ALA D 1 263 ? -25.408 41.648  83.053  1.00 58.07  ? 263 ALA D CA  1 
ATOM   14457 C C   . ALA D 1 263 ? -26.159 41.022  81.888  1.00 58.90  ? 263 ALA D C   1 
ATOM   14458 O O   . ALA D 1 263 ? -26.449 41.694  80.891  1.00 57.92  ? 263 ALA D O   1 
ATOM   14459 C CB  . ALA D 1 263 ? -23.929 41.266  83.014  1.00 53.44  ? 263 ALA D CB  1 
ATOM   14460 N N   . LEU D 1 264 ? -26.505 39.740  82.009  1.00 53.21  ? 264 LEU D N   1 
ATOM   14461 C CA  . LEU D 1 264 ? -27.299 39.088  80.975  1.00 58.02  ? 264 LEU D CA  1 
ATOM   14462 C C   . LEU D 1 264 ? -28.601 39.844  80.729  1.00 58.29  ? 264 LEU D C   1 
ATOM   14463 O O   . LEU D 1 264 ? -29.009 40.033  79.578  1.00 61.37  ? 264 LEU D O   1 
ATOM   14464 C CB  . LEU D 1 264 ? -27.569 37.634  81.372  1.00 58.18  ? 264 LEU D CB  1 
ATOM   14465 C CG  . LEU D 1 264 ? -26.347 36.702  81.460  1.00 54.51  ? 264 LEU D CG  1 
ATOM   14466 C CD1 . LEU D 1 264 ? -26.710 35.278  81.133  1.00 55.20  ? 264 LEU D CD1 1 
ATOM   14467 C CD2 . LEU D 1 264 ? -25.230 37.151  80.543  1.00 54.24  ? 264 LEU D CD2 1 
ATOM   14468 N N   . GLU D 1 265 ? -29.254 40.309  81.798  1.00 64.01  ? 265 GLU D N   1 
ATOM   14469 C CA  . GLU D 1 265 ? -30.487 41.071  81.633  1.00 60.19  ? 265 GLU D CA  1 
ATOM   14470 C C   . GLU D 1 265 ? -30.230 42.418  80.974  1.00 62.98  ? 265 GLU D C   1 
ATOM   14471 O O   . GLU D 1 265 ? -31.108 42.939  80.278  1.00 69.36  ? 265 GLU D O   1 
ATOM   14472 C CB  . GLU D 1 265 ? -31.173 41.260  82.984  1.00 64.93  ? 265 GLU D CB  1 
ATOM   14473 C CG  . GLU D 1 265 ? -31.432 39.957  83.730  1.00 65.38  ? 265 GLU D CG  1 
ATOM   14474 C CD  . GLU D 1 265 ? -31.739 40.163  85.205  1.00 63.61  ? 265 GLU D CD  1 
ATOM   14475 O OE1 . GLU D 1 265 ? -31.744 41.327  85.660  1.00 60.22  ? 265 GLU D OE1 1 
ATOM   14476 O OE2 . GLU D 1 265 ? -31.978 39.158  85.909  1.00 56.39  ? 265 GLU D OE2 1 
ATOM   14477 N N   . LEU D 1 266 ? -29.041 42.990  81.170  1.00 58.76  ? 266 LEU D N   1 
ATOM   14478 C CA  . LEU D 1 266 ? -28.736 44.267  80.537  1.00 62.02  ? 266 LEU D CA  1 
ATOM   14479 C C   . LEU D 1 266 ? -28.541 44.102  79.034  1.00 61.75  ? 266 LEU D C   1 
ATOM   14480 O O   . LEU D 1 266 ? -29.013 44.933  78.247  1.00 60.08  ? 266 LEU D O   1 
ATOM   14481 C CB  . LEU D 1 266 ? -27.498 44.890  81.182  1.00 58.84  ? 266 LEU D CB  1 
ATOM   14482 C CG  . LEU D 1 266 ? -27.009 46.174  80.508  1.00 60.99  ? 266 LEU D CG  1 
ATOM   14483 C CD1 . LEU D 1 266 ? -28.017 47.318  80.623  1.00 61.38  ? 266 LEU D CD1 1 
ATOM   14484 C CD2 . LEU D 1 266 ? -25.656 46.579  81.053  1.00 52.96  ? 266 LEU D CD2 1 
ATOM   14485 N N   . TYR D 1 267 ? -27.867 43.023  78.617  1.00 58.62  ? 267 TYR D N   1 
ATOM   14486 C CA  . TYR D 1 267 ? -27.635 42.783  77.193  1.00 58.19  ? 267 TYR D CA  1 
ATOM   14487 C C   . TYR D 1 267 ? -28.937 42.492  76.454  1.00 61.35  ? 267 TYR D C   1 
ATOM   14488 O O   . TYR D 1 267 ? -29.140 42.972  75.334  1.00 63.35  ? 267 TYR D O   1 
ATOM   14489 C CB  . TYR D 1 267 ? -26.650 41.630  77.005  1.00 57.16  ? 267 TYR D CB  1 
ATOM   14490 C CG  . TYR D 1 267 ? -25.218 41.973  77.345  1.00 61.94  ? 267 TYR D CG  1 
ATOM   14491 C CD1 . TYR D 1 267 ? -24.451 42.772  76.505  1.00 64.36  ? 267 TYR D CD1 1 
ATOM   14492 C CD2 . TYR D 1 267 ? -24.625 41.485  78.501  1.00 58.54  ? 267 TYR D CD2 1 
ATOM   14493 C CE1 . TYR D 1 267 ? -23.135 43.082  76.816  1.00 60.31  ? 267 TYR D CE1 1 
ATOM   14494 C CE2 . TYR D 1 267 ? -23.316 41.792  78.819  1.00 55.78  ? 267 TYR D CE2 1 
ATOM   14495 C CZ  . TYR D 1 267 ? -22.572 42.588  77.976  1.00 57.53  ? 267 TYR D CZ  1 
ATOM   14496 O OH  . TYR D 1 267 ? -21.263 42.887  78.299  1.00 62.95  ? 267 TYR D OH  1 
ATOM   14497 N N   . TYR D 1 268 ? -29.827 41.700  77.055  1.00 64.71  ? 268 TYR D N   1 
ATOM   14498 C CA  . TYR D 1 268 ? -31.134 41.476  76.448  1.00 63.69  ? 268 TYR D CA  1 
ATOM   14499 C C   . TYR D 1 268 ? -31.901 42.786  76.316  1.00 62.72  ? 268 TYR D C   1 
ATOM   14500 O O   . TYR D 1 268 ? -32.551 43.033  75.294  1.00 71.07  ? 268 TYR D O   1 
ATOM   14501 C CB  . TYR D 1 268 ? -31.916 40.451  77.273  1.00 63.51  ? 268 TYR D CB  1 
ATOM   14502 C CG  . TYR D 1 268 ? -33.427 40.521  77.158  1.00 72.01  ? 268 TYR D CG  1 
ATOM   14503 C CD1 . TYR D 1 268 ? -34.102 39.813  76.171  1.00 72.79  ? 268 TYR D CD1 1 
ATOM   14504 C CD2 . TYR D 1 268 ? -34.179 41.271  78.054  1.00 66.07  ? 268 TYR D CD2 1 
ATOM   14505 C CE1 . TYR D 1 268 ? -35.477 39.864  76.072  1.00 65.99  ? 268 TYR D CE1 1 
ATOM   14506 C CE2 . TYR D 1 268 ? -35.549 41.328  77.958  1.00 69.87  ? 268 TYR D CE2 1 
ATOM   14507 C CZ  . TYR D 1 268 ? -36.194 40.623  76.966  1.00 62.67  ? 268 TYR D CZ  1 
ATOM   14508 O OH  . TYR D 1 268 ? -37.564 40.675  76.866  1.00 66.27  ? 268 TYR D OH  1 
ATOM   14509 N N   . GLU D 1 269 ? -31.813 43.653  77.330  1.00 65.48  ? 269 GLU D N   1 
ATOM   14510 C CA  . GLU D 1 269 ? -32.537 44.921  77.289  1.00 71.32  ? 269 GLU D CA  1 
ATOM   14511 C C   . GLU D 1 269 ? -31.998 45.834  76.199  1.00 64.00  ? 269 GLU D C   1 
ATOM   14512 O O   . GLU D 1 269 ? -32.736 46.662  75.651  1.00 57.93  ? 269 GLU D O   1 
ATOM   14513 C CB  . GLU D 1 269 ? -32.456 45.618  78.649  1.00 66.08  ? 269 GLU D CB  1 
ATOM   14514 C CG  . GLU D 1 269 ? -33.437 45.087  79.689  1.00 71.23  ? 269 GLU D CG  1 
ATOM   14515 C CD  . GLU D 1 269 ? -33.338 45.813  81.024  1.00 77.68  ? 269 GLU D CD  1 
ATOM   14516 O OE1 . GLU D 1 269 ? -32.207 46.142  81.442  1.00 59.84  ? 269 GLU D OE1 1 
ATOM   14517 O OE2 . GLU D 1 269 ? -34.389 46.050  81.659  1.00 88.33  ? 269 GLU D OE2 1 
ATOM   14518 N N   . LYS D 1 270 ? -30.719 45.696  75.868  1.00 57.16  ? 270 LYS D N   1 
ATOM   14519 C CA  . LYS D 1 270 ? -30.085 46.535  74.868  1.00 57.39  ? 270 LYS D CA  1 
ATOM   14520 C C   . LYS D 1 270 ? -30.077 45.884  73.488  1.00 63.25  ? 270 LYS D C   1 
ATOM   14521 O O   . LYS D 1 270 ? -29.355 46.340  72.597  1.00 71.82  ? 270 LYS D O   1 
ATOM   14522 C CB  . LYS D 1 270 ? -28.670 46.887  75.315  1.00 57.89  ? 270 LYS D CB  1 
ATOM   14523 C CG  . LYS D 1 270 ? -28.633 47.651  76.629  1.00 65.05  ? 270 LYS D CG  1 
ATOM   14524 C CD  . LYS D 1 270 ? -28.741 49.141  76.386  1.00 65.50  ? 270 LYS D CD  1 
ATOM   14525 C CE  . LYS D 1 270 ? -29.317 49.875  77.585  1.00 65.67  ? 270 LYS D CE  1 
ATOM   14526 N NZ  . LYS D 1 270 ? -30.658 49.365  77.954  1.00 61.44  ? 270 LYS D NZ  1 
ATOM   14527 N N   . GLY D 1 271 ? -30.864 44.827  73.299  1.00 57.36  ? 271 GLY D N   1 
ATOM   14528 C CA  . GLY D 1 271 ? -31.086 44.252  71.991  1.00 60.38  ? 271 GLY D CA  1 
ATOM   14529 C C   . GLY D 1 271 ? -30.205 43.079  71.624  1.00 65.66  ? 271 GLY D C   1 
ATOM   14530 O O   . GLY D 1 271 ? -30.342 42.550  70.514  1.00 71.49  ? 271 GLY D O   1 
ATOM   14531 N N   . ILE D 1 272 ? -29.314 42.650  72.506  1.00 62.45  ? 272 ILE D N   1 
ATOM   14532 C CA  . ILE D 1 272 ? -28.403 41.561  72.177  1.00 67.72  ? 272 ILE D CA  1 
ATOM   14533 C C   . ILE D 1 272 ? -29.155 40.238  72.245  1.00 67.53  ? 272 ILE D C   1 
ATOM   14534 O O   . ILE D 1 272 ? -29.886 39.972  73.206  1.00 73.10  ? 272 ILE D O   1 
ATOM   14535 C CB  . ILE D 1 272 ? -27.187 41.567  73.116  1.00 65.99  ? 272 ILE D CB  1 
ATOM   14536 C CG1 . ILE D 1 272 ? -26.546 42.960  73.157  1.00 61.79  ? 272 ILE D CG1 1 
ATOM   14537 C CG2 . ILE D 1 272 ? -26.169 40.527  72.674  1.00 62.32  ? 272 ILE D CG2 1 
ATOM   14538 C CD1 . ILE D 1 272 ? -26.312 43.584  71.789  1.00 58.07  ? 272 ILE D CD1 1 
ATOM   14539 N N   . ASN D 1 273 ? -28.995 39.412  71.210  1.00 68.69  ? 273 ASN D N   1 
ATOM   14540 C CA  . ASN D 1 273 ? -29.605 38.089  71.182  1.00 73.54  ? 273 ASN D CA  1 
ATOM   14541 C C   . ASN D 1 273 ? -28.646 36.977  71.577  1.00 67.40  ? 273 ASN D C   1 
ATOM   14542 O O   . ASN D 1 273 ? -29.105 35.911  72.001  1.00 64.82  ? 273 ASN D O   1 
ATOM   14543 C CB  . ASN D 1 273 ? -30.166 37.773  69.784  1.00 77.85  ? 273 ASN D CB  1 
ATOM   14544 C CG  . ASN D 1 273 ? -30.823 38.971  69.122  1.00 77.06  ? 273 ASN D CG  1 
ATOM   14545 O OD1 . ASN D 1 273 ? -31.476 39.782  69.779  1.00 91.51  ? 273 ASN D OD1 1 
ATOM   14546 N ND2 . ASN D 1 273 ? -30.658 39.083  67.810  1.00 68.79  ? 273 ASN D ND2 1 
ATOM   14547 N N   . MET D 1 274 ? -27.335 37.189  71.446  1.00 70.15  ? 274 MET D N   1 
ATOM   14548 C CA  . MET D 1 274 ? -26.368 36.131  71.701  1.00 73.30  ? 274 MET D CA  1 
ATOM   14549 C C   . MET D 1 274 ? -25.114 36.706  72.346  1.00 65.10  ? 274 MET D C   1 
ATOM   14550 O O   . MET D 1 274 ? -24.706 37.835  72.061  1.00 61.06  ? 274 MET D O   1 
ATOM   14551 C CB  . MET D 1 274 ? -25.973 35.380  70.420  1.00 67.81  ? 274 MET D CB  1 
ATOM   14552 C CG  . MET D 1 274 ? -25.214 34.096  70.731  1.00 70.28  ? 274 MET D CG  1 
ATOM   14553 S SD  . MET D 1 274 ? -23.422 34.249  70.702  1.00 69.74  ? 274 MET D SD  1 
ATOM   14554 C CE  . MET D 1 274 ? -23.214 35.360  69.315  1.00 71.74  ? 274 MET D CE  1 
ATOM   14555 N N   . LEU D 1 275 ? -24.510 35.911  73.227  1.00 60.60  ? 275 LEU D N   1 
ATOM   14556 C CA  . LEU D 1 275 ? -23.231 36.234  73.842  1.00 62.65  ? 275 LEU D CA  1 
ATOM   14557 C C   . LEU D 1 275 ? -22.555 34.922  74.218  1.00 61.33  ? 275 LEU D C   1 
ATOM   14558 O O   . LEU D 1 275 ? -23.171 33.854  74.188  1.00 61.77  ? 275 LEU D O   1 
ATOM   14559 C CB  . LEU D 1 275 ? -23.400 37.144  75.067  1.00 59.02  ? 275 LEU D CB  1 
ATOM   14560 C CG  . LEU D 1 275 ? -24.135 36.503  76.251  1.00 65.13  ? 275 LEU D CG  1 
ATOM   14561 C CD1 . LEU D 1 275 ? -23.162 36.168  77.372  1.00 66.04  ? 275 LEU D CD1 1 
ATOM   14562 C CD2 . LEU D 1 275 ? -25.269 37.381  76.773  1.00 64.52  ? 275 LEU D CD2 1 
ATOM   14563 N N   . ALA D 1 276 ? -21.281 35.010  74.591  1.00 59.28  ? 276 ALA D N   1 
ATOM   14564 C CA  . ALA D 1 276 ? -20.495 33.825  74.909  1.00 66.13  ? 276 ALA D CA  1 
ATOM   14565 C C   . ALA D 1 276 ? -19.642 34.082  76.144  1.00 62.99  ? 276 ALA D C   1 
ATOM   14566 O O   . ALA D 1 276 ? -19.284 35.222  76.441  1.00 61.68  ? 276 ALA D O   1 
ATOM   14567 C CB  . ALA D 1 276 ? -19.608 33.414  73.727  1.00 60.70  ? 276 ALA D CB  1 
ATOM   14568 N N   . THR D 1 277 ? -19.308 33.010  76.858  1.00 61.28  ? 277 THR D N   1 
ATOM   14569 C CA  . THR D 1 277 ? -18.486 33.124  78.054  1.00 61.58  ? 277 THR D CA  1 
ATOM   14570 C C   . THR D 1 277 ? -17.680 31.840  78.230  1.00 65.81  ? 277 THR D C   1 
ATOM   14571 O O   . THR D 1 277 ? -17.790 30.896  77.442  1.00 61.90  ? 277 THR D O   1 
ATOM   14572 C CB  . THR D 1 277 ? -19.349 33.429  79.282  1.00 65.05  ? 277 THR D CB  1 
ATOM   14573 O OG1 . THR D 1 277 ? -18.570 33.243  80.473  1.00 69.76  ? 277 THR D OG1 1 
ATOM   14574 C CG2 . THR D 1 277 ? -20.562 32.515  79.315  1.00 61.73  ? 277 THR D CG2 1 
ATOM   14575 N N   . ASP D 1 278 ? -16.863 31.815  79.281  1.00 63.51  ? 278 ASP D N   1 
ATOM   14576 C CA  . ASP D 1 278 ? -15.989 30.680  79.536  1.00 66.32  ? 278 ASP D CA  1 
ATOM   14577 C C   . ASP D 1 278 ? -16.774 29.504  80.103  1.00 67.12  ? 278 ASP D C   1 
ATOM   14578 O O   . ASP D 1 278 ? -17.777 29.674  80.800  1.00 69.78  ? 278 ASP D O   1 
ATOM   14579 C CB  . ASP D 1 278 ? -14.872 31.075  80.503  1.00 66.90  ? 278 ASP D CB  1 
ATOM   14580 C CG  . ASP D 1 278 ? -13.670 30.152  80.417  1.00 71.75  ? 278 ASP D CG  1 
ATOM   14581 O OD1 . ASP D 1 278 ? -13.429 29.565  79.339  1.00 71.40  ? 278 ASP D OD1 1 
ATOM   14582 O OD2 . ASP D 1 278 ? -12.964 30.011  81.436  1.00 77.49  ? 278 ASP D OD2 1 
ATOM   14583 N N   . GLU D 1 279 ? -16.298 28.292  79.802  1.00 68.91  ? 279 GLU D N   1 
ATOM   14584 C CA  . GLU D 1 279 ? -16.982 27.095  80.273  1.00 67.29  ? 279 GLU D CA  1 
ATOM   14585 C C   . GLU D 1 279 ? -16.778 26.839  81.760  1.00 72.73  ? 279 GLU D C   1 
ATOM   14586 O O   . GLU D 1 279 ? -17.513 26.033  82.336  1.00 77.52  ? 279 GLU D O   1 
ATOM   14587 C CB  . GLU D 1 279 ? -16.532 25.869  79.476  1.00 65.11  ? 279 GLU D CB  1 
ATOM   14588 C CG  . GLU D 1 279 ? -15.062 25.542  79.596  1.00 64.71  ? 279 GLU D CG  1 
ATOM   14589 C CD  . GLU D 1 279 ? -14.708 24.214  78.958  1.00 65.19  ? 279 GLU D CD  1 
ATOM   14590 O OE1 . GLU D 1 279 ? -15.518 23.265  79.045  1.00 64.75  ? 279 GLU D OE1 1 
ATOM   14591 O OE2 . GLU D 1 279 ? -13.615 24.119  78.368  1.00 67.02  ? 279 GLU D OE2 1 
ATOM   14592 N N   . VAL D 1 280 ? -15.811 27.494  82.401  1.00 69.77  ? 280 VAL D N   1 
ATOM   14593 C CA  . VAL D 1 280 ? -15.721 27.380  83.850  1.00 67.12  ? 280 VAL D CA  1 
ATOM   14594 C C   . VAL D 1 280 ? -16.966 27.946  84.511  1.00 72.41  ? 280 VAL D C   1 
ATOM   14595 O O   . VAL D 1 280 ? -17.401 27.457  85.561  1.00 79.17  ? 280 VAL D O   1 
ATOM   14596 C CB  . VAL D 1 280 ? -14.454 28.079  84.354  1.00 63.79  ? 280 VAL D CB  1 
ATOM   14597 C CG1 . VAL D 1 280 ? -14.390 28.023  85.867  1.00 65.50  ? 280 VAL D CG1 1 
ATOM   14598 C CG2 . VAL D 1 280 ? -13.251 27.421  83.743  1.00 72.92  ? 280 VAL D CG2 1 
ATOM   14599 N N   . ILE D 1 281 ? -17.553 28.987  83.919  1.00 67.84  ? 281 ILE D N   1 
ATOM   14600 C CA  . ILE D 1 281 ? -18.793 29.542  84.451  1.00 68.88  ? 281 ILE D CA  1 
ATOM   14601 C C   . ILE D 1 281 ? -19.907 28.504  84.359  1.00 75.56  ? 281 ILE D C   1 
ATOM   14602 O O   . ILE D 1 281 ? -20.673 28.297  85.309  1.00 75.04  ? 281 ILE D O   1 
ATOM   14603 C CB  . ILE D 1 281 ? -19.169 30.850  83.719  1.00 68.07  ? 281 ILE D CB  1 
ATOM   14604 C CG1 . ILE D 1 281 ? -18.247 32.042  84.059  1.00 69.38  ? 281 ILE D CG1 1 
ATOM   14605 C CG2 . ILE D 1 281 ? -20.595 31.257  84.028  1.00 66.74  ? 281 ILE D CG2 1 
ATOM   14606 C CD1 . ILE D 1 281 ? -16.769 31.908  83.736  1.00 70.40  ? 281 ILE D CD1 1 
ATOM   14607 N N   . LEU D 1 282 ? -19.994 27.818  83.216  1.00 74.00  ? 282 LEU D N   1 
ATOM   14608 C CA  . LEU D 1 282 ? -21.006 26.780  83.039  1.00 70.60  ? 282 LEU D CA  1 
ATOM   14609 C C   . LEU D 1 282 ? -20.840 25.663  84.065  1.00 75.08  ? 282 LEU D C   1 
ATOM   14610 O O   . LEU D 1 282 ? -21.818 25.222  84.685  1.00 71.79  ? 282 LEU D O   1 
ATOM   14611 C CB  . LEU D 1 282 ? -20.918 26.231  81.620  1.00 68.54  ? 282 LEU D CB  1 
ATOM   14612 C CG  . LEU D 1 282 ? -21.902 25.129  81.259  1.00 67.32  ? 282 LEU D CG  1 
ATOM   14613 C CD1 . LEU D 1 282 ? -23.349 25.589  81.455  1.00 59.84  ? 282 LEU D CD1 1 
ATOM   14614 C CD2 . LEU D 1 282 ? -21.625 24.707  79.829  1.00 59.71  ? 282 LEU D CD2 1 
ATOM   14615 N N   . LYS D 1 283 ? -19.597 25.215  84.283  1.00 76.36  ? 283 LYS D N   1 
ATOM   14616 C CA  . LYS D 1 283 ? -19.351 24.188  85.292  1.00 78.99  ? 283 LYS D CA  1 
ATOM   14617 C C   . LYS D 1 283 ? -19.666 24.693  86.700  1.00 75.67  ? 283 LYS D C   1 
ATOM   14618 O O   . LYS D 1 283 ? -20.001 23.889  87.577  1.00 70.69  ? 283 LYS D O   1 
ATOM   14619 C CB  . LYS D 1 283 ? -17.905 23.663  85.170  1.00 78.91  ? 283 LYS D CB  1 
ATOM   14620 C CG  . LYS D 1 283 ? -16.819 24.180  86.143  1.00 78.09  ? 283 LYS D CG  1 
ATOM   14621 C CD  . LYS D 1 283 ? -16.792 23.363  87.449  1.00 87.32  ? 283 LYS D CD  1 
ATOM   14622 C CE  . LYS D 1 283 ? -15.831 23.952  88.484  1.00 84.64  ? 283 LYS D CE  1 
ATOM   14623 N NZ  . LYS D 1 283 ? -15.975 23.307  89.828  1.00 79.78  ? 283 LYS D NZ  1 
ATOM   14624 N N   . ASN D 1 284 ? -19.555 26.007  86.937  1.00 78.02  ? 284 ASN D N   1 
ATOM   14625 C CA  . ASN D 1 284 ? -19.984 26.622  88.191  1.00 71.39  ? 284 ASN D CA  1 
ATOM   14626 C C   . ASN D 1 284 ? -21.478 26.911  88.231  1.00 71.21  ? 284 ASN D C   1 
ATOM   14627 O O   . ASN D 1 284 ? -22.037 27.032  89.324  1.00 67.45  ? 284 ASN D O   1 
ATOM   14628 C CB  . ASN D 1 284 ? -19.223 27.928  88.434  1.00 70.78  ? 284 ASN D CB  1 
ATOM   14629 C CG  . ASN D 1 284 ? -17.737 27.712  88.561  1.00 77.60  ? 284 ASN D CG  1 
ATOM   14630 O OD1 . ASN D 1 284 ? -17.277 26.578  88.586  1.00 83.90  ? 284 ASN D OD1 1 
ATOM   14631 N ND2 . ASN D 1 284 ? -16.977 28.798  88.663  1.00 74.55  ? 284 ASN D ND2 1 
ATOM   14632 N N   . SER D 1 285 ? -22.138 27.002  87.072  1.00 70.51  ? 285 SER D N   1 
ATOM   14633 C CA  . SER D 1 285 ? -23.541 27.389  87.000  1.00 67.96  ? 285 SER D CA  1 
ATOM   14634 C C   . SER D 1 285 ? -24.487 26.216  86.771  1.00 70.17  ? 285 SER D C   1 
ATOM   14635 O O   . SER D 1 285 ? -25.673 26.326  87.102  1.00 77.44  ? 285 SER D O   1 
ATOM   14636 C CB  . SER D 1 285 ? -23.742 28.419  85.887  1.00 64.85  ? 285 SER D CB  1 
ATOM   14637 O OG  . SER D 1 285 ? -22.885 29.528  86.081  1.00 64.78  ? 285 SER D OG  1 
ATOM   14638 N N   . VAL D 1 286 ? -24.008 25.117  86.183  1.00 74.53  ? 286 VAL D N   1 
ATOM   14639 C CA  . VAL D 1 286 ? -24.785 23.893  86.005  1.00 72.20  ? 286 VAL D CA  1 
ATOM   14640 C C   . VAL D 1 286 ? -23.868 22.726  86.357  1.00 78.08  ? 286 VAL D C   1 
ATOM   14641 O O   . VAL D 1 286 ? -22.643 22.846  86.316  1.00 79.44  ? 286 VAL D O   1 
ATOM   14642 C CB  . VAL D 1 286 ? -25.356 23.730  84.568  1.00 60.39  ? 286 VAL D CB  1 
ATOM   14643 C CG1 . VAL D 1 286 ? -26.523 22.783  84.577  1.00 65.45  ? 286 VAL D CG1 1 
ATOM   14644 C CG2 . VAL D 1 286 ? -25.801 25.063  83.986  1.00 56.28  ? 286 VAL D CG2 1 
ATOM   14645 N N   . GLU D 1 287 ? -24.474 21.583  86.709  1.00 84.12  ? 287 GLU D N   1 
ATOM   14646 C CA  . GLU D 1 287 ? -23.728 20.427  87.219  1.00 81.20  ? 287 GLU D CA  1 
ATOM   14647 C C   . GLU D 1 287 ? -22.611 19.971  86.279  1.00 90.05  ? 287 GLU D C   1 
ATOM   14648 O O   . GLU D 1 287 ? -21.461 20.394  86.428  1.00 101.30 ? 287 GLU D O   1 
ATOM   14649 C CB  . GLU D 1 287 ? -24.667 19.253  87.506  1.00 76.25  ? 287 GLU D CB  1 
ATOM   14650 C CG  . GLU D 1 287 ? -24.042 18.156  88.387  1.00 88.54  ? 287 GLU D CG  1 
ATOM   14651 C CD  . GLU D 1 287 ? -25.067 17.391  89.227  1.00 95.53  ? 287 GLU D CD  1 
ATOM   14652 O OE1 . GLU D 1 287 ? -26.260 17.376  88.852  1.00 90.97  ? 287 GLU D OE1 1 
ATOM   14653 O OE2 . GLU D 1 287 ? -24.682 16.811  90.268  1.00 83.77  ? 287 GLU D OE2 1 
ATOM   14654 N N   . ARG D 1 288 ? -22.916 19.086  85.334  1.00 81.33  ? 288 ARG D N   1 
ATOM   14655 C CA  . ARG D 1 288 ? -21.929 18.608  84.372  1.00 78.76  ? 288 ARG D CA  1 
ATOM   14656 C C   . ARG D 1 288 ? -22.381 18.891  82.946  1.00 71.67  ? 288 ARG D C   1 
ATOM   14657 O O   . ARG D 1 288 ? -22.230 18.061  82.048  1.00 74.81  ? 288 ARG D O   1 
ATOM   14658 C CB  . ARG D 1 288 ? -21.642 17.122  84.557  1.00 81.27  ? 288 ARG D CB  1 
ATOM   14659 C CG  . ARG D 1 288 ? -22.849 16.285  84.956  1.00 83.93  ? 288 ARG D CG  1 
ATOM   14660 C CD  . ARG D 1 288 ? -22.443 14.890  85.412  1.00 83.86  ? 288 ARG D CD  1 
ATOM   14661 N NE  . ARG D 1 288 ? -23.319 14.406  86.467  1.00 73.55  ? 288 ARG D NE  1 
ATOM   14662 C CZ  . ARG D 1 288 ? -23.118 14.622  87.758  1.00 76.93  ? 288 ARG D CZ  1 
ATOM   14663 N NH1 . ARG D 1 288 ? -22.065 15.297  88.188  1.00 78.10  ? 288 ARG D NH1 1 
ATOM   14664 N NH2 . ARG D 1 288 ? -23.999 14.159  88.638  1.00 84.91  ? 288 ARG D NH2 1 
ATOM   14665 N N   . ALA D 1 289 ? -22.945 20.077  82.726  1.00 70.38  ? 289 ALA D N   1 
ATOM   14666 C CA  . ALA D 1 289 ? -23.437 20.440  81.405  1.00 64.25  ? 289 ALA D CA  1 
ATOM   14667 C C   . ALA D 1 289 ? -22.273 20.636  80.442  1.00 67.96  ? 289 ALA D C   1 
ATOM   14668 O O   . ALA D 1 289 ? -21.252 21.231  80.796  1.00 68.88  ? 289 ALA D O   1 
ATOM   14669 C CB  . ALA D 1 289 ? -24.285 21.709  81.489  1.00 64.37  ? 289 ALA D CB  1 
ATOM   14670 N N   . SER D 1 290 ? -22.420 20.119  79.225  1.00 65.39  ? 290 SER D N   1 
ATOM   14671 C CA  . SER D 1 290 ? -21.359 20.243  78.241  1.00 70.66  ? 290 SER D CA  1 
ATOM   14672 C C   . SER D 1 290 ? -21.324 21.653  77.668  1.00 67.10  ? 290 SER D C   1 
ATOM   14673 O O   . SER D 1 290 ? -22.316 22.386  77.730  1.00 66.39  ? 290 SER D O   1 
ATOM   14674 C CB  . SER D 1 290 ? -21.544 19.226  77.117  1.00 66.33  ? 290 SER D CB  1 
ATOM   14675 O OG  . SER D 1 290 ? -20.315 18.609  76.767  1.00 70.92  ? 290 SER D OG  1 
ATOM   14676 N N   . PRO D 1 291 ? -20.176 22.068  77.122  1.00 61.94  ? 291 PRO D N   1 
ATOM   14677 C CA  . PRO D 1 291 ? -20.111 23.372  76.453  1.00 62.67  ? 291 PRO D CA  1 
ATOM   14678 C C   . PRO D 1 291 ? -20.618 23.342  75.022  1.00 62.81  ? 291 PRO D C   1 
ATOM   14679 O O   . PRO D 1 291 ? -20.844 24.413  74.441  1.00 72.61  ? 291 PRO D O   1 
ATOM   14680 C CB  . PRO D 1 291 ? -18.615 23.703  76.508  1.00 64.47  ? 291 PRO D CB  1 
ATOM   14681 C CG  . PRO D 1 291 ? -17.962 22.357  76.436  1.00 66.63  ? 291 PRO D CG  1 
ATOM   14682 C CD  . PRO D 1 291 ? -18.840 21.465  77.283  1.00 58.75  ? 291 PRO D CD  1 
ATOM   14683 N N   . TYR D 1 292 ? -20.835 22.157  74.453  1.00 64.87  ? 292 TYR D N   1 
ATOM   14684 C CA  . TYR D 1 292 ? -21.178 21.992  73.039  1.00 69.10  ? 292 TYR D CA  1 
ATOM   14685 C C   . TYR D 1 292 ? -22.680 22.016  72.792  1.00 69.37  ? 292 TYR D C   1 
ATOM   14686 O O   . TYR D 1 292 ? -23.212 21.225  72.008  1.00 68.96  ? 292 TYR D O   1 
ATOM   14687 C CB  . TYR D 1 292 ? -20.553 20.700  72.527  1.00 64.96  ? 292 TYR D CB  1 
ATOM   14688 C CG  . TYR D 1 292 ? -19.161 20.496  73.069  1.00 61.20  ? 292 TYR D CG  1 
ATOM   14689 C CD1 . TYR D 1 292 ? -18.125 21.353  72.717  1.00 63.61  ? 292 TYR D CD1 1 
ATOM   14690 C CD2 . TYR D 1 292 ? -18.886 19.469  73.961  1.00 66.38  ? 292 TYR D CD2 1 
ATOM   14691 C CE1 . TYR D 1 292 ? -16.846 21.180  73.227  1.00 63.88  ? 292 TYR D CE1 1 
ATOM   14692 C CE2 . TYR D 1 292 ? -17.613 19.289  74.474  1.00 63.37  ? 292 TYR D CE2 1 
ATOM   14693 C CZ  . TYR D 1 292 ? -16.600 20.144  74.106  1.00 59.98  ? 292 TYR D CZ  1 
ATOM   14694 O OH  . TYR D 1 292 ? -15.341 19.951  74.624  1.00 68.81  ? 292 TYR D OH  1 
ATOM   14695 N N   . LEU D 1 293 ? -23.386 22.921  73.460  1.00 71.01  ? 293 LEU D N   1 
ATOM   14696 C CA  . LEU D 1 293 ? -24.825 23.073  73.308  1.00 72.17  ? 293 LEU D CA  1 
ATOM   14697 C C   . LEU D 1 293 ? -25.148 24.553  73.238  1.00 70.77  ? 293 LEU D C   1 
ATOM   14698 O O   . LEU D 1 293 ? -24.354 25.403  73.649  1.00 74.02  ? 293 LEU D O   1 
ATOM   14699 C CB  . LEU D 1 293 ? -25.615 22.453  74.471  1.00 69.90  ? 293 LEU D CB  1 
ATOM   14700 C CG  . LEU D 1 293 ? -25.367 21.019  74.927  1.00 72.06  ? 293 LEU D CG  1 
ATOM   14701 C CD1 . LEU D 1 293 ? -24.098 20.928  75.713  1.00 74.08  ? 293 LEU D CD1 1 
ATOM   14702 C CD2 . LEU D 1 293 ? -26.522 20.560  75.791  1.00 76.39  ? 293 LEU D CD2 1 
ATOM   14703 N N   . ARG D 1 294 ? -26.330 24.859  72.726  1.00 65.86  ? 294 ARG D N   1 
ATOM   14704 C CA  . ARG D 1 294 ? -26.829 26.221  72.792  1.00 71.61  ? 294 ARG D CA  1 
ATOM   14705 C C   . ARG D 1 294 ? -27.697 26.361  74.032  1.00 72.83  ? 294 ARG D C   1 
ATOM   14706 O O   . ARG D 1 294 ? -28.605 25.554  74.261  1.00 71.10  ? 294 ARG D O   1 
ATOM   14707 C CB  . ARG D 1 294 ? -27.628 26.597  71.547  1.00 78.36  ? 294 ARG D CB  1 
ATOM   14708 C CG  . ARG D 1 294 ? -28.057 28.047  71.578  1.00 73.95  ? 294 ARG D CG  1 
ATOM   14709 C CD  . ARG D 1 294 ? -29.352 28.289  70.843  1.00 82.65  ? 294 ARG D CD  1 
ATOM   14710 N NE  . ARG D 1 294 ? -29.511 27.480  69.642  1.00 87.10  ? 294 ARG D NE  1 
ATOM   14711 C CZ  . ARG D 1 294 ? -29.484 27.981  68.416  1.00 87.25  ? 294 ARG D CZ  1 
ATOM   14712 N NH1 . ARG D 1 294 ? -29.271 29.270  68.208  1.00 87.70  ? 294 ARG D NH1 1 
ATOM   14713 N NH2 . ARG D 1 294 ? -29.680 27.174  67.376  1.00 84.42  ? 294 ARG D NH2 1 
ATOM   14714 N N   . TYR D 1 295 ? -27.405 27.372  74.835  1.00 67.87  ? 295 TYR D N   1 
ATOM   14715 C CA  . TYR D 1 295 ? -28.122 27.613  76.074  1.00 66.17  ? 295 TYR D CA  1 
ATOM   14716 C C   . TYR D 1 295 ? -28.956 28.879  75.935  1.00 71.55  ? 295 TYR D C   1 
ATOM   14717 O O   . TYR D 1 295 ? -28.478 29.888  75.402  1.00 69.25  ? 295 TYR D O   1 
ATOM   14718 C CB  . TYR D 1 295 ? -27.141 27.706  77.242  1.00 70.57  ? 295 TYR D CB  1 
ATOM   14719 C CG  . TYR D 1 295 ? -26.480 26.376  77.547  1.00 76.04  ? 295 TYR D CG  1 
ATOM   14720 C CD1 . TYR D 1 295 ? -25.305 25.995  76.907  1.00 65.38  ? 295 TYR D CD1 1 
ATOM   14721 C CD2 . TYR D 1 295 ? -27.046 25.491  78.454  1.00 74.03  ? 295 TYR D CD2 1 
ATOM   14722 C CE1 . TYR D 1 295 ? -24.707 24.776  77.177  1.00 66.93  ? 295 TYR D CE1 1 
ATOM   14723 C CE2 . TYR D 1 295 ? -26.458 24.276  78.731  1.00 69.79  ? 295 TYR D CE2 1 
ATOM   14724 C CZ  . TYR D 1 295 ? -25.289 23.920  78.090  1.00 74.71  ? 295 TYR D CZ  1 
ATOM   14725 O OH  . TYR D 1 295 ? -24.704 22.704  78.366  1.00 70.74  ? 295 TYR D OH  1 
ATOM   14726 N N   . TYR D 1 296 ? -30.215 28.802  76.373  1.00 66.49  ? 296 TYR D N   1 
ATOM   14727 C CA  . TYR D 1 296 ? -31.140 29.932  76.405  1.00 66.61  ? 296 TYR D CA  1 
ATOM   14728 C C   . TYR D 1 296 ? -31.307 30.364  77.855  1.00 68.44  ? 296 TYR D C   1 
ATOM   14729 O O   . TYR D 1 296 ? -31.883 29.628  78.663  1.00 79.80  ? 296 TYR D O   1 
ATOM   14730 C CB  . TYR D 1 296 ? -32.499 29.567  75.810  1.00 79.54  ? 296 TYR D CB  1 
ATOM   14731 C CG  . TYR D 1 296 ? -32.482 29.163  74.356  1.00 83.84  ? 296 TYR D CG  1 
ATOM   14732 C CD1 . TYR D 1 296 ? -32.237 27.848  73.981  1.00 84.48  ? 296 TYR D CD1 1 
ATOM   14733 C CD2 . TYR D 1 296 ? -32.753 30.090  73.357  1.00 84.71  ? 296 TYR D CD2 1 
ATOM   14734 C CE1 . TYR D 1 296 ? -32.234 27.474  72.644  1.00 89.42  ? 296 TYR D CE1 1 
ATOM   14735 C CE2 . TYR D 1 296 ? -32.751 29.725  72.018  1.00 90.28  ? 296 TYR D CE2 1 
ATOM   14736 C CZ  . TYR D 1 296 ? -32.497 28.416  71.668  1.00 90.63  ? 296 TYR D CZ  1 
ATOM   14737 O OH  . TYR D 1 296 ? -32.495 28.055  70.338  1.00 90.65  ? 296 TYR D OH  1 
ATOM   14738 N N   . PHE D 1 297 ? -30.829 31.560  78.182  1.00 64.41  ? 297 PHE D N   1 
ATOM   14739 C CA  . PHE D 1 297 ? -30.880 32.060  79.555  1.00 66.24  ? 297 PHE D CA  1 
ATOM   14740 C C   . PHE D 1 297 ? -32.276 32.619  79.810  1.00 58.70  ? 297 PHE D C   1 
ATOM   14741 O O   . PHE D 1 297 ? -32.620 33.697  79.322  1.00 62.72  ? 297 PHE D O   1 
ATOM   14742 C CB  . PHE D 1 297 ? -29.787 33.106  79.773  1.00 61.25  ? 297 PHE D CB  1 
ATOM   14743 C CG  . PHE D 1 297 ? -29.709 33.626  81.179  1.00 58.08  ? 297 PHE D CG  1 
ATOM   14744 C CD1 . PHE D 1 297 ? -29.001 32.935  82.153  1.00 62.94  ? 297 PHE D CD1 1 
ATOM   14745 C CD2 . PHE D 1 297 ? -30.323 34.820  81.526  1.00 64.44  ? 297 PHE D CD2 1 
ATOM   14746 C CE1 . PHE D 1 297 ? -28.926 33.414  83.456  1.00 60.63  ? 297 PHE D CE1 1 
ATOM   14747 C CE2 . PHE D 1 297 ? -30.252 35.306  82.829  1.00 67.11  ? 297 PHE D CE2 1 
ATOM   14748 C CZ  . PHE D 1 297 ? -29.552 34.600  83.793  1.00 64.21  ? 297 PHE D CZ  1 
ATOM   14749 N N   . ARG D 1 298 ? -33.097 31.875  80.563  1.00 57.00  ? 298 ARG D N   1 
ATOM   14750 C CA  . ARG D 1 298 ? -34.467 32.269  80.909  1.00 63.18  ? 298 ARG D CA  1 
ATOM   14751 C C   . ARG D 1 298 ? -35.321 32.579  79.679  1.00 71.48  ? 298 ARG D C   1 
ATOM   14752 O O   . ARG D 1 298 ? -36.277 33.357  79.768  1.00 69.97  ? 298 ARG D O   1 
ATOM   14753 C CB  . ARG D 1 298 ? -34.481 33.472  81.861  1.00 58.20  ? 298 ARG D CB  1 
ATOM   14754 C CG  . ARG D 1 298 ? -33.528 33.349  83.025  1.00 61.35  ? 298 ARG D CG  1 
ATOM   14755 C CD  . ARG D 1 298 ? -33.615 34.542  83.952  1.00 57.00  ? 298 ARG D CD  1 
ATOM   14756 N NE  . ARG D 1 298 ? -32.665 34.426  85.053  1.00 60.82  ? 298 ARG D NE  1 
ATOM   14757 C CZ  . ARG D 1 298 ? -32.265 35.436  85.813  1.00 62.50  ? 298 ARG D CZ  1 
ATOM   14758 N NH1 . ARG D 1 298 ? -32.712 36.666  85.621  1.00 63.59  ? 298 ARG D NH1 1 
ATOM   14759 N NH2 . ARG D 1 298 ? -31.399 35.206  86.795  1.00 62.85  ? 298 ARG D NH2 1 
ATOM   14760 N N   . GLU D 1 299 ? -34.977 31.993  78.530  1.00 72.80  ? 299 GLU D N   1 
ATOM   14761 C CA  . GLU D 1 299 ? -35.612 32.192  77.231  1.00 67.86  ? 299 GLU D CA  1 
ATOM   14762 C C   . GLU D 1 299 ? -35.538 33.627  76.722  1.00 73.64  ? 299 GLU D C   1 
ATOM   14763 O O   . GLU D 1 299 ? -36.300 33.987  75.812  1.00 78.02  ? 299 GLU D O   1 
ATOM   14764 C CB  . GLU D 1 299 ? -37.073 31.737  77.247  1.00 73.77  ? 299 GLU D CB  1 
ATOM   14765 C CG  . GLU D 1 299 ? -37.322 30.417  76.547  1.00 92.73  ? 299 GLU D CG  1 
ATOM   14766 C CD  . GLU D 1 299 ? -38.543 29.700  77.091  1.00 107.56 ? 299 GLU D CD  1 
ATOM   14767 O OE1 . GLU D 1 299 ? -39.454 30.375  77.619  1.00 105.56 ? 299 GLU D OE1 1 
ATOM   14768 O OE2 . GLU D 1 299 ? -38.585 28.457  77.000  1.00 116.60 ? 299 GLU D OE2 1 
ATOM   14769 N N   . LEU D 1 300 ? -34.638 34.453  77.262  1.00 67.48  ? 300 LEU D N   1 
ATOM   14770 C CA  . LEU D 1 300 ? -34.488 35.847  76.852  1.00 67.14  ? 300 LEU D CA  1 
ATOM   14771 C C   . LEU D 1 300 ? -33.264 36.083  75.976  1.00 68.06  ? 300 LEU D C   1 
ATOM   14772 O O   . LEU D 1 300 ? -33.317 36.893  75.042  1.00 62.24  ? 300 LEU D O   1 
ATOM   14773 C CB  . LEU D 1 300 ? -34.419 36.753  78.090  1.00 67.85  ? 300 LEU D CB  1 
ATOM   14774 C CG  . LEU D 1 300 ? -35.537 36.546  79.125  1.00 71.43  ? 300 LEU D CG  1 
ATOM   14775 C CD1 . LEU D 1 300 ? -35.071 36.801  80.557  1.00 65.76  ? 300 LEU D CD1 1 
ATOM   14776 C CD2 . LEU D 1 300 ? -36.754 37.399  78.807  1.00 68.17  ? 300 LEU D CD2 1 
ATOM   14777 N N   . ILE D 1 301 ? -32.160 35.394  76.251  1.00 71.54  ? 301 ILE D N   1 
ATOM   14778 C CA  . ILE D 1 301 ? -30.926 35.557  75.496  1.00 66.20  ? 301 ILE D CA  1 
ATOM   14779 C C   . ILE D 1 301 ? -30.271 34.190  75.333  1.00 69.75  ? 301 ILE D C   1 
ATOM   14780 O O   . ILE D 1 301 ? -30.397 33.310  76.192  1.00 66.88  ? 301 ILE D O   1 
ATOM   14781 C CB  . ILE D 1 301 ? -29.969 36.559  76.183  1.00 64.65  ? 301 ILE D CB  1 
ATOM   14782 C CG1 . ILE D 1 301 ? -28.861 37.001  75.223  1.00 68.92  ? 301 ILE D CG1 1 
ATOM   14783 C CG2 . ILE D 1 301 ? -29.402 35.962  77.459  1.00 64.33  ? 301 ILE D CG2 1 
ATOM   14784 C CD1 . ILE D 1 301 ? -28.404 38.422  75.452  1.00 64.93  ? 301 ILE D CD1 1 
ATOM   14785 N N   . SER D 1 302 ? -29.585 34.011  74.205  1.00 68.71  ? 302 SER D N   1 
ATOM   14786 C CA  . SER D 1 302 ? -28.886 32.773  73.891  1.00 66.44  ? 302 SER D CA  1 
ATOM   14787 C C   . SER D 1 302 ? -27.428 32.898  74.301  1.00 65.67  ? 302 SER D C   1 
ATOM   14788 O O   . SER D 1 302 ? -26.804 33.946  74.107  1.00 61.82  ? 302 SER D O   1 
ATOM   14789 C CB  . SER D 1 302 ? -28.982 32.448  72.399  1.00 64.09  ? 302 SER D CB  1 
ATOM   14790 O OG  . SER D 1 302 ? -30.329 32.461  71.961  1.00 78.52  ? 302 SER D OG  1 
ATOM   14791 N N   . VAL D 1 303 ? -26.889 31.829  74.880  1.00 61.50  ? 303 VAL D N   1 
ATOM   14792 C CA  . VAL D 1 303 ? -25.514 31.820  75.359  1.00 66.49  ? 303 VAL D CA  1 
ATOM   14793 C C   . VAL D 1 303 ? -24.816 30.572  74.841  1.00 65.56  ? 303 VAL D C   1 
ATOM   14794 O O   . VAL D 1 303 ? -25.414 29.491  74.781  1.00 66.46  ? 303 VAL D O   1 
ATOM   14795 C CB  . VAL D 1 303 ? -25.440 31.890  76.902  1.00 62.69  ? 303 VAL D CB  1 
ATOM   14796 C CG1 . VAL D 1 303 ? -23.988 32.018  77.362  1.00 57.03  ? 303 VAL D CG1 1 
ATOM   14797 C CG2 . VAL D 1 303 ? -26.288 33.046  77.433  1.00 50.33  ? 303 VAL D CG2 1 
ATOM   14798 N N   . PHE D 1 304 ? -23.556 30.739  74.444  1.00 63.69  ? 304 PHE D N   1 
ATOM   14799 C CA  . PHE D 1 304 ? -22.671 29.653  74.059  1.00 64.74  ? 304 PHE D CA  1 
ATOM   14800 C C   . PHE D 1 304 ? -21.449 29.694  74.958  1.00 62.16  ? 304 PHE D C   1 
ATOM   14801 O O   . PHE D 1 304 ? -20.945 30.773  75.278  1.00 63.32  ? 304 PHE D O   1 
ATOM   14802 C CB  . PHE D 1 304 ? -22.235 29.776  72.604  1.00 58.97  ? 304 PHE D CB  1 
ATOM   14803 C CG  . PHE D 1 304 ? -23.257 29.300  71.624  1.00 65.51  ? 304 PHE D CG  1 
ATOM   14804 C CD1 . PHE D 1 304 ? -23.543 27.954  71.506  1.00 69.20  ? 304 PHE D CD1 1 
ATOM   14805 C CD2 . PHE D 1 304 ? -23.931 30.200  70.816  1.00 65.44  ? 304 PHE D CD2 1 
ATOM   14806 C CE1 . PHE D 1 304 ? -24.482 27.515  70.594  1.00 68.90  ? 304 PHE D CE1 1 
ATOM   14807 C CE2 . PHE D 1 304 ? -24.870 29.767  69.907  1.00 67.16  ? 304 PHE D CE2 1 
ATOM   14808 C CZ  . PHE D 1 304 ? -25.146 28.422  69.795  1.00 71.16  ? 304 PHE D CZ  1 
ATOM   14809 N N   . PHE D 1 305 ? -20.965 28.527  75.359  1.00 61.46  ? 305 PHE D N   1 
ATOM   14810 C CA  . PHE D 1 305 ? -19.822 28.439  76.257  1.00 63.99  ? 305 PHE D CA  1 
ATOM   14811 C C   . PHE D 1 305 ? -18.615 27.931  75.478  1.00 68.22  ? 305 PHE D C   1 
ATOM   14812 O O   . PHE D 1 305 ? -18.681 26.870  74.848  1.00 74.47  ? 305 PHE D O   1 
ATOM   14813 C CB  . PHE D 1 305 ? -20.140 27.536  77.444  1.00 64.35  ? 305 PHE D CB  1 
ATOM   14814 C CG  . PHE D 1 305 ? -21.231 28.069  78.325  1.00 59.96  ? 305 PHE D CG  1 
ATOM   14815 C CD1 . PHE D 1 305 ? -20.931 28.918  79.374  1.00 62.42  ? 305 PHE D CD1 1 
ATOM   14816 C CD2 . PHE D 1 305 ? -22.557 27.734  78.096  1.00 68.31  ? 305 PHE D CD2 1 
ATOM   14817 C CE1 . PHE D 1 305 ? -21.932 29.414  80.193  1.00 71.49  ? 305 PHE D CE1 1 
ATOM   14818 C CE2 . PHE D 1 305 ? -23.564 28.229  78.909  1.00 64.53  ? 305 PHE D CE2 1 
ATOM   14819 C CZ  . PHE D 1 305 ? -23.250 29.069  79.959  1.00 66.94  ? 305 PHE D CZ  1 
ATOM   14820 N N   . ARG D 1 306 ? -17.521 28.691  75.518  1.00 69.00  ? 306 ARG D N   1 
ATOM   14821 C CA  . ARG D 1 306 ? -16.331 28.325  74.765  1.00 75.35  ? 306 ARG D CA  1 
ATOM   14822 C C   . ARG D 1 306 ? -15.687 27.075  75.358  1.00 77.16  ? 306 ARG D C   1 
ATOM   14823 O O   . ARG D 1 306 ? -16.012 26.634  76.465  1.00 73.44  ? 306 ARG D O   1 
ATOM   14824 C CB  . ARG D 1 306 ? -15.310 29.466  74.753  1.00 67.14  ? 306 ARG D CB  1 
ATOM   14825 C CG  . ARG D 1 306 ? -14.410 29.494  75.983  1.00 70.01  ? 306 ARG D CG  1 
ATOM   14826 C CD  . ARG D 1 306 ? -13.108 30.256  75.750  1.00 63.11  ? 306 ARG D CD  1 
ATOM   14827 N NE  . ARG D 1 306 ? -12.343 30.330  76.990  1.00 65.35  ? 306 ARG D NE  1 
ATOM   14828 C CZ  . ARG D 1 306 ? -11.219 31.011  77.151  1.00 61.42  ? 306 ARG D CZ  1 
ATOM   14829 N NH1 . ARG D 1 306 ? -10.672 31.688  76.154  1.00 63.85  ? 306 ARG D NH1 1 
ATOM   14830 N NH2 . ARG D 1 306 ? -10.633 31.018  78.346  1.00 63.83  ? 306 ARG D NH2 1 
ATOM   14831 N N   . ASP D 1 307 ? -14.748 26.508  74.600  1.00 72.20  ? 307 ASP D N   1 
ATOM   14832 C CA  . ASP D 1 307 ? -13.930 25.394  75.062  1.00 68.46  ? 307 ASP D CA  1 
ATOM   14833 C C   . ASP D 1 307 ? -12.595 25.971  75.514  1.00 67.81  ? 307 ASP D C   1 
ATOM   14834 O O   . ASP D 1 307 ? -11.817 26.467  74.694  1.00 71.80  ? 307 ASP D O   1 
ATOM   14835 C CB  . ASP D 1 307 ? -13.757 24.349  73.962  1.00 71.01  ? 307 ASP D CB  1 
ATOM   14836 C CG  . ASP D 1 307 ? -13.042 23.097  74.445  1.00 78.26  ? 307 ASP D CG  1 
ATOM   14837 O OD1 . ASP D 1 307 ? -11.956 23.208  75.057  1.00 82.29  ? 307 ASP D OD1 1 
ATOM   14838 O OD2 . ASP D 1 307 ? -13.564 21.992  74.189  1.00 81.66  ? 307 ASP D OD2 1 
ATOM   14839 N N   . LYS D 1 308 ? -12.339 25.911  76.823  1.00 73.52  ? 308 LYS D N   1 
ATOM   14840 C CA  . LYS D 1 308 ? -11.117 26.487  77.375  1.00 69.82  ? 308 LYS D CA  1 
ATOM   14841 C C   . LYS D 1 308 ? -9.879  25.816  76.794  1.00 63.70  ? 308 LYS D C   1 
ATOM   14842 O O   . LYS D 1 308 ? -8.948  26.495  76.351  1.00 68.06  ? 308 LYS D O   1 
ATOM   14843 C CB  . LYS D 1 308 ? -11.128 26.375  78.902  1.00 64.02  ? 308 LYS D CB  1 
ATOM   14844 C CG  . LYS D 1 308 ? -10.512 27.565  79.619  1.00 68.47  ? 308 LYS D CG  1 
ATOM   14845 C CD  . LYS D 1 308 ? -9.979  27.185  80.993  1.00 60.28  ? 308 LYS D CD  1 
ATOM   14846 C CE  . LYS D 1 308 ? -9.181  28.327  81.612  1.00 66.44  ? 308 LYS D CE  1 
ATOM   14847 N NZ  . LYS D 1 308 ? -9.830  29.658  81.420  1.00 69.30  ? 308 LYS D NZ  1 
ATOM   14848 N N   . THR D 1 309 ? -9.863  24.480  76.772  1.00 61.53  ? 309 THR D N   1 
ATOM   14849 C CA  . THR D 1 309 ? -8.693  23.740  76.302  1.00 58.76  ? 309 THR D CA  1 
ATOM   14850 C C   . THR D 1 309 ? -8.355  24.101  74.862  1.00 66.22  ? 309 THR D C   1 
ATOM   14851 O O   . THR D 1 309 ? -7.205  24.423  74.543  1.00 62.42  ? 309 THR D O   1 
ATOM   14852 C CB  . THR D 1 309 ? -8.935  22.235  76.426  1.00 55.53  ? 309 THR D CB  1 
ATOM   14853 O OG1 . THR D 1 309 ? -10.175 21.894  75.796  1.00 67.95  ? 309 THR D OG1 1 
ATOM   14854 C CG2 . THR D 1 309 ? -9.023  21.834  77.887  1.00 58.53  ? 309 THR D CG2 1 
ATOM   14855 N N   . LEU D 1 310 ? -9.350  24.063  73.976  1.00 65.95  ? 310 LEU D N   1 
ATOM   14856 C CA  . LEU D 1 310 ? -9.098  24.380  72.575  1.00 64.03  ? 310 LEU D CA  1 
ATOM   14857 C C   . LEU D 1 310 ? -8.667  25.833  72.404  1.00 66.22  ? 310 LEU D C   1 
ATOM   14858 O O   . LEU D 1 310 ? -7.696  26.126  71.698  1.00 62.92  ? 310 LEU D O   1 
ATOM   14859 C CB  . LEU D 1 310 ? -10.346 24.081  71.749  1.00 70.98  ? 310 LEU D CB  1 
ATOM   14860 C CG  . LEU D 1 310 ? -10.467 22.684  71.133  1.00 72.50  ? 310 LEU D CG  1 
ATOM   14861 C CD1 . LEU D 1 310 ? -10.125 21.546  72.102  1.00 74.37  ? 310 LEU D CD1 1 
ATOM   14862 C CD2 . LEU D 1 310 ? -11.860 22.531  70.567  1.00 68.21  ? 310 LEU D CD2 1 
ATOM   14863 N N   . SER D 1 311 ? -9.375  26.760  73.055  1.00 69.42  ? 311 SER D N   1 
ATOM   14864 C CA  . SER D 1 311 ? -9.049  28.175  72.907  1.00 70.71  ? 311 SER D CA  1 
ATOM   14865 C C   . SER D 1 311 ? -7.731  28.526  73.588  1.00 67.48  ? 311 SER D C   1 
ATOM   14866 O O   . SER D 1 311 ? -6.968  29.354  73.078  1.00 71.68  ? 311 SER D O   1 
ATOM   14867 C CB  . SER D 1 311 ? -10.186 29.036  73.451  1.00 65.82  ? 311 SER D CB  1 
ATOM   14868 O OG  . SER D 1 311 ? -11.359 28.831  72.685  1.00 63.86  ? 311 SER D OG  1 
ATOM   14869 N N   . ASP D 1 312 ? -7.439  27.906  74.733  1.00 60.65  ? 312 ASP D N   1 
ATOM   14870 C CA  . ASP D 1 312 ? -6.186  28.206  75.418  1.00 65.28  ? 312 ASP D CA  1 
ATOM   14871 C C   . ASP D 1 312 ? -4.994  27.509  74.769  1.00 71.70  ? 312 ASP D C   1 
ATOM   14872 O O   . ASP D 1 312 ? -3.873  28.029  74.832  1.00 69.95  ? 312 ASP D O   1 
ATOM   14873 C CB  . ASP D 1 312 ? -6.283  27.825  76.895  1.00 69.43  ? 312 ASP D CB  1 
ATOM   14874 C CG  . ASP D 1 312 ? -6.551  29.022  77.790  1.00 86.07  ? 312 ASP D CG  1 
ATOM   14875 O OD1 . ASP D 1 312 ? -7.315  29.926  77.379  1.00 88.93  ? 312 ASP D OD1 1 
ATOM   14876 O OD2 . ASP D 1 312 ? -5.997  29.057  78.909  1.00 96.92  ? 312 ASP D OD2 1 
ATOM   14877 N N   . LEU D 1 313 ? -5.208  26.351  74.137  1.00 68.62  ? 313 LEU D N   1 
ATOM   14878 C CA  . LEU D 1 313 ? -4.124  25.698  73.407  1.00 62.98  ? 313 LEU D CA  1 
ATOM   14879 C C   . LEU D 1 313 ? -3.546  26.627  72.343  1.00 64.55  ? 313 LEU D C   1 
ATOM   14880 O O   . LEU D 1 313 ? -2.330  26.839  72.284  1.00 69.55  ? 313 LEU D O   1 
ATOM   14881 C CB  . LEU D 1 313 ? -4.622  24.397  72.771  1.00 66.46  ? 313 LEU D CB  1 
ATOM   14882 C CG  . LEU D 1 313 ? -4.486  23.108  73.589  1.00 64.52  ? 313 LEU D CG  1 
ATOM   14883 C CD1 . LEU D 1 313 ? -5.510  22.088  73.135  1.00 60.70  ? 313 LEU D CD1 1 
ATOM   14884 C CD2 . LEU D 1 313 ? -3.103  22.534  73.474  1.00 70.45  ? 313 LEU D CD2 1 
ATOM   14885 N N   . ILE D 1 314 ? -4.407  27.205  71.499  1.00 61.94  ? 314 ILE D N   1 
ATOM   14886 C CA  . ILE D 1 314 ? -3.942  28.144  70.478  1.00 63.93  ? 314 ILE D CA  1 
ATOM   14887 C C   . ILE D 1 314 ? -3.277  29.355  71.116  1.00 64.52  ? 314 ILE D C   1 
ATOM   14888 O O   . ILE D 1 314 ? -2.289  29.888  70.592  1.00 58.35  ? 314 ILE D O   1 
ATOM   14889 C CB  . ILE D 1 314 ? -5.107  28.571  69.569  1.00 60.03  ? 314 ILE D CB  1 
ATOM   14890 C CG1 . ILE D 1 314 ? -6.123  27.448  69.448  1.00 68.49  ? 314 ILE D CG1 1 
ATOM   14891 C CG2 . ILE D 1 314 ? -4.606  28.975  68.202  1.00 57.81  ? 314 ILE D CG2 1 
ATOM   14892 C CD1 . ILE D 1 314 ? -7.328  27.845  68.665  1.00 75.80  ? 314 ILE D CD1 1 
ATOM   14893 N N   . GLY D 1 315 ? -3.808  29.815  72.247  1.00 62.35  ? 315 GLY D N   1 
ATOM   14894 C CA  . GLY D 1 315 ? -3.312  31.051  72.828  1.00 65.77  ? 315 GLY D CA  1 
ATOM   14895 C C   . GLY D 1 315 ? -1.997  30.883  73.566  1.00 66.83  ? 315 GLY D C   1 
ATOM   14896 O O   . GLY D 1 315 ? -1.144  31.776  73.543  1.00 61.25  ? 315 GLY D O   1 
ATOM   14897 N N   . PHE D 1 316 ? -1.806  29.743  74.227  1.00 66.26  ? 316 PHE D N   1 
ATOM   14898 C CA  . PHE D 1 316 ? -0.657  29.583  75.108  1.00 63.38  ? 316 PHE D CA  1 
ATOM   14899 C C   . PHE D 1 316 ? 0.149   28.314  74.903  1.00 62.11  ? 316 PHE D C   1 
ATOM   14900 O O   . PHE D 1 316 ? 1.286   28.259  75.387  1.00 75.95  ? 316 PHE D O   1 
ATOM   14901 C CB  . PHE D 1 316 ? -1.098  29.638  76.577  1.00 60.91  ? 316 PHE D CB  1 
ATOM   14902 C CG  . PHE D 1 316 ? -1.895  30.861  76.923  1.00 62.25  ? 316 PHE D CG  1 
ATOM   14903 C CD1 . PHE D 1 316 ? -1.263  32.063  77.197  1.00 64.32  ? 316 PHE D CD1 1 
ATOM   14904 C CD2 . PHE D 1 316 ? -3.277  30.808  76.977  1.00 68.12  ? 316 PHE D CD2 1 
ATOM   14905 C CE1 . PHE D 1 316 ? -1.999  33.189  77.515  1.00 65.00  ? 316 PHE D CE1 1 
ATOM   14906 C CE2 . PHE D 1 316 ? -4.017  31.928  77.295  1.00 68.16  ? 316 PHE D CE2 1 
ATOM   14907 C CZ  . PHE D 1 316 ? -3.377  33.122  77.564  1.00 58.08  ? 316 PHE D CZ  1 
ATOM   14908 N N   . SER D 1 317 ? -0.371  27.303  74.214  1.00 58.93  ? 317 SER D N   1 
ATOM   14909 C CA  . SER D 1 317 ? 0.344   26.037  74.099  1.00 61.05  ? 317 SER D CA  1 
ATOM   14910 C C   . SER D 1 317 ? 0.991   25.825  72.736  1.00 73.36  ? 317 SER D C   1 
ATOM   14911 O O   . SER D 1 317 ? 2.162   25.439  72.664  1.00 80.51  ? 317 SER D O   1 
ATOM   14912 C CB  . SER D 1 317 ? -0.598  24.873  74.403  1.00 60.18  ? 317 SER D CB  1 
ATOM   14913 O OG  . SER D 1 317 ? -0.845  24.783  75.791  1.00 71.41  ? 317 SER D OG  1 
ATOM   14914 N N   . TYR D 1 318 ? 0.256   26.059  71.649  1.00 64.85  ? 318 TYR D N   1 
ATOM   14915 C CA  . TYR D 1 318 ? 0.751   25.646  70.342  1.00 68.71  ? 318 TYR D CA  1 
ATOM   14916 C C   . TYR D 1 318 ? 1.929   26.477  69.845  1.00 72.21  ? 318 TYR D C   1 
ATOM   14917 O O   . TYR D 1 318 ? 2.554   26.080  68.856  1.00 81.56  ? 318 TYR D O   1 
ATOM   14918 C CB  . TYR D 1 318 ? -0.373  25.692  69.304  1.00 70.01  ? 318 TYR D CB  1 
ATOM   14919 C CG  . TYR D 1 318 ? -1.440  24.628  69.443  1.00 71.91  ? 318 TYR D CG  1 
ATOM   14920 C CD1 . TYR D 1 318 ? -1.146  23.360  69.941  1.00 72.48  ? 318 TYR D CD1 1 
ATOM   14921 C CD2 . TYR D 1 318 ? -2.751  24.899  69.081  1.00 71.36  ? 318 TYR D CD2 1 
ATOM   14922 C CE1 . TYR D 1 318 ? -2.138  22.395  70.064  1.00 73.59  ? 318 TYR D CE1 1 
ATOM   14923 C CE2 . TYR D 1 318 ? -3.743  23.948  69.203  1.00 76.67  ? 318 TYR D CE2 1 
ATOM   14924 C CZ  . TYR D 1 318 ? -3.433  22.699  69.695  1.00 80.89  ? 318 TYR D CZ  1 
ATOM   14925 O OH  . TYR D 1 318 ? -4.422  21.751  69.819  1.00 80.82  ? 318 TYR D OH  1 
ATOM   14926 N N   . HIS D 1 319 ? 2.252   27.605  70.487  1.00 66.25  ? 319 HIS D N   1 
ATOM   14927 C CA  . HIS D 1 319 ? 3.374   28.418  70.018  1.00 66.04  ? 319 HIS D CA  1 
ATOM   14928 C C   . HIS D 1 319 ? 4.697   27.660  70.050  1.00 71.05  ? 319 HIS D C   1 
ATOM   14929 O O   . HIS D 1 319 ? 5.610   28.000  69.290  1.00 73.03  ? 319 HIS D O   1 
ATOM   14930 C CB  . HIS D 1 319 ? 3.513   29.688  70.857  1.00 60.50  ? 319 HIS D CB  1 
ATOM   14931 C CG  . HIS D 1 319 ? 4.085   29.440  72.216  1.00 70.21  ? 319 HIS D CG  1 
ATOM   14932 N ND1 . HIS D 1 319 ? 3.331   28.951  73.261  1.00 69.05  ? 319 HIS D ND1 1 
ATOM   14933 C CD2 . HIS D 1 319 ? 5.342   29.593  72.698  1.00 68.26  ? 319 HIS D CD2 1 
ATOM   14934 C CE1 . HIS D 1 319 ? 4.096   28.824  74.330  1.00 70.51  ? 319 HIS D CE1 1 
ATOM   14935 N NE2 . HIS D 1 319 ? 5.320   29.207  74.016  1.00 63.93  ? 319 HIS D NE2 1 
ATOM   14936 N N   . ALA D 1 320 ? 4.826   26.649  70.912  1.00 70.72  ? 320 ALA D N   1 
ATOM   14937 C CA  . ALA D 1 320 ? 6.050   25.869  71.039  1.00 73.15  ? 320 ALA D CA  1 
ATOM   14938 C C   . ALA D 1 320 ? 5.942   24.511  70.347  1.00 72.91  ? 320 ALA D C   1 
ATOM   14939 O O   . ALA D 1 320 ? 6.554   23.532  70.782  1.00 68.95  ? 320 ALA D O   1 
ATOM   14940 C CB  . ALA D 1 320 ? 6.416   25.690  72.510  1.00 73.80  ? 320 ALA D CB  1 
ATOM   14941 N N   . TRP D 1 321 ? 5.169   24.441  69.266  1.00 71.05  ? 321 TRP D N   1 
ATOM   14942 C CA  . TRP D 1 321 ? 4.929   23.202  68.540  1.00 75.92  ? 321 TRP D CA  1 
ATOM   14943 C C   . TRP D 1 321 ? 5.268   23.403  67.070  1.00 78.45  ? 321 TRP D C   1 
ATOM   14944 O O   . TRP D 1 321 ? 5.340   24.531  66.578  1.00 85.66  ? 321 TRP D O   1 
ATOM   14945 C CB  . TRP D 1 321 ? 3.457   22.750  68.654  1.00 81.25  ? 321 TRP D CB  1 
ATOM   14946 C CG  . TRP D 1 321 ? 3.013   22.260  70.019  1.00 81.41  ? 321 TRP D CG  1 
ATOM   14947 C CD1 . TRP D 1 321 ? 3.490   22.660  71.236  1.00 83.99  ? 321 TRP D CD1 1 
ATOM   14948 C CD2 . TRP D 1 321 ? 1.995   21.288  70.291  1.00 76.29  ? 321 TRP D CD2 1 
ATOM   14949 N NE1 . TRP D 1 321 ? 2.839   21.994  72.245  1.00 78.29  ? 321 TRP D NE1 1 
ATOM   14950 C CE2 . TRP D 1 321 ? 1.915   21.147  71.692  1.00 85.68  ? 321 TRP D CE2 1 
ATOM   14951 C CE3 . TRP D 1 321 ? 1.145   20.522  69.487  1.00 82.29  ? 321 TRP D CE3 1 
ATOM   14952 C CZ2 . TRP D 1 321 ? 1.018   20.270  72.306  1.00 93.01  ? 321 TRP D CZ2 1 
ATOM   14953 C CZ3 . TRP D 1 321 ? 0.253   19.651  70.099  1.00 82.33  ? 321 TRP D CZ3 1 
ATOM   14954 C CH2 . TRP D 1 321 ? 0.197   19.533  71.494  1.00 85.66  ? 321 TRP D CH2 1 
ATOM   14955 N N   . ASN D 1 322 ? 5.458   22.298  66.358  1.00 70.44  ? 322 ASN D N   1 
ATOM   14956 C CA  . ASN D 1 322 ? 5.455   22.384  64.908  1.00 77.84  ? 322 ASN D CA  1 
ATOM   14957 C C   . ASN D 1 322 ? 4.023   22.588  64.421  1.00 79.57  ? 322 ASN D C   1 
ATOM   14958 O O   . ASN D 1 322 ? 3.064   22.159  65.067  1.00 81.02  ? 322 ASN D O   1 
ATOM   14959 C CB  . ASN D 1 322 ? 6.070   21.126  64.291  1.00 81.17  ? 322 ASN D CB  1 
ATOM   14960 C CG  . ASN D 1 322 ? 5.719   20.963  62.830  1.00 82.12  ? 322 ASN D CG  1 
ATOM   14961 O OD1 . ASN D 1 322 ? 4.621   20.526  62.485  1.00 85.98  ? 322 ASN D OD1 1 
ATOM   14962 N ND2 . ASN D 1 322 ? 6.641   21.348  61.960  1.00 84.20  ? 322 ASN D ND2 1 
ATOM   14963 N N   . ALA D 1 323 ? 3.885   23.269  63.277  1.00 83.33  ? 323 ALA D N   1 
ATOM   14964 C CA  . ALA D 1 323 ? 2.563   23.613  62.750  1.00 83.49  ? 323 ALA D CA  1 
ATOM   14965 C C   . ALA D 1 323 ? 1.708   22.372  62.499  1.00 79.49  ? 323 ALA D C   1 
ATOM   14966 O O   . ALA D 1 323 ? 0.558   22.299  62.948  1.00 87.05  ? 323 ALA D O   1 
ATOM   14967 C CB  . ALA D 1 323 ? 2.708   24.431  61.466  1.00 81.99  ? 323 ALA D CB  1 
ATOM   14968 N N   . GLU D 1 324 ? 2.244   21.391  61.767  1.00 73.17  ? 324 GLU D N   1 
ATOM   14969 C CA  . GLU D 1 324 ? 1.459   20.199  61.454  1.00 82.03  ? 324 GLU D CA  1 
ATOM   14970 C C   . GLU D 1 324 ? 1.071   19.444  62.718  1.00 81.89  ? 324 GLU D C   1 
ATOM   14971 O O   . GLU D 1 324 ? -0.063  18.968  62.844  1.00 84.95  ? 324 GLU D O   1 
ATOM   14972 C CB  . GLU D 1 324 ? 2.232   19.279  60.506  1.00 94.70  ? 324 GLU D CB  1 
ATOM   14973 C CG  . GLU D 1 324 ? 3.125   19.988  59.490  1.00 101.68 ? 324 GLU D CG  1 
ATOM   14974 C CD  . GLU D 1 324 ? 4.020   19.018  58.728  1.00 111.52 ? 324 GLU D CD  1 
ATOM   14975 O OE1 . GLU D 1 324 ? 4.194   17.873  59.200  1.00 99.81  ? 324 GLU D OE1 1 
ATOM   14976 O OE2 . GLU D 1 324 ? 4.549   19.396  57.660  1.00 119.15 ? 324 GLU D OE2 1 
ATOM   14977 N N   . ASP D 1 325 ? 2.001   19.331  63.671  1.00 78.50  ? 325 ASP D N   1 
ATOM   14978 C CA  . ASP D 1 325 ? 1.707   18.635  64.921  1.00 81.43  ? 325 ASP D CA  1 
ATOM   14979 C C   . ASP D 1 325 ? 0.628   19.348  65.723  1.00 81.15  ? 325 ASP D C   1 
ATOM   14980 O O   . ASP D 1 325 ? -0.166  18.700  66.416  1.00 81.07  ? 325 ASP D O   1 
ATOM   14981 C CB  . ASP D 1 325 ? 2.983   18.497  65.747  1.00 80.31  ? 325 ASP D CB  1 
ATOM   14982 C CG  . ASP D 1 325 ? 3.963   17.521  65.138  1.00 87.12  ? 325 ASP D CG  1 
ATOM   14983 O OD1 . ASP D 1 325 ? 3.894   17.297  63.910  1.00 92.95  ? 325 ASP D OD1 1 
ATOM   14984 O OD2 . ASP D 1 325 ? 4.799   16.972  65.884  1.00 93.09  ? 325 ASP D OD2 1 
ATOM   14985 N N   . ALA D 1 326 ? 0.582   20.678  65.641  1.00 75.38  ? 326 ALA D N   1 
ATOM   14986 C CA  . ALA D 1 326 ? -0.468  21.429  66.315  1.00 73.09  ? 326 ALA D CA  1 
ATOM   14987 C C   . ALA D 1 326 ? -1.818  21.193  65.652  1.00 81.11  ? 326 ALA D C   1 
ATOM   14988 O O   . ALA D 1 326 ? -2.815  20.917  66.333  1.00 81.19  ? 326 ALA D O   1 
ATOM   14989 C CB  . ALA D 1 326 ? -0.122  22.916  66.325  1.00 66.39  ? 326 ALA D CB  1 
ATOM   14990 N N   . VAL D 1 327 ? -1.871  21.302  64.321  1.00 74.82  ? 327 VAL D N   1 
ATOM   14991 C CA  . VAL D 1 327 ? -3.123  21.044  63.616  1.00 76.45  ? 327 VAL D CA  1 
ATOM   14992 C C   . VAL D 1 327 ? -3.583  19.611  63.857  1.00 79.51  ? 327 VAL D C   1 
ATOM   14993 O O   . VAL D 1 327 ? -4.782  19.352  64.016  1.00 76.76  ? 327 VAL D O   1 
ATOM   14994 C CB  . VAL D 1 327 ? -2.974  21.355  62.113  1.00 77.87  ? 327 VAL D CB  1 
ATOM   14995 C CG1 . VAL D 1 327 ? -4.327  21.274  61.415  1.00 73.33  ? 327 VAL D CG1 1 
ATOM   14996 C CG2 . VAL D 1 327 ? -2.367  22.735  61.915  1.00 76.44  ? 327 VAL D CG2 1 
ATOM   14997 N N   . ARG D 1 328 ? -2.639  18.662  63.912  1.00 79.89  ? 328 ARG D N   1 
ATOM   14998 C CA  . ARG D 1 328 ? -2.985  17.276  64.223  1.00 78.62  ? 328 ARG D CA  1 
ATOM   14999 C C   . ARG D 1 328 ? -3.716  17.178  65.550  1.00 75.69  ? 328 ARG D C   1 
ATOM   15000 O O   . ARG D 1 328 ? -4.765  16.529  65.649  1.00 79.57  ? 328 ARG D O   1 
ATOM   15001 C CB  . ARG D 1 328 ? -1.729  16.405  64.248  1.00 83.50  ? 328 ARG D CB  1 
ATOM   15002 C CG  . ARG D 1 328 ? -1.977  14.987  63.777  1.00 84.60  ? 328 ARG D CG  1 
ATOM   15003 C CD  . ARG D 1 328 ? -0.677  14.302  63.438  1.00 84.19  ? 328 ARG D CD  1 
ATOM   15004 N NE  . ARG D 1 328 ? -0.154  14.824  62.184  1.00 95.98  ? 328 ARG D NE  1 
ATOM   15005 C CZ  . ARG D 1 328 ? 0.941   15.566  62.086  1.00 100.16 ? 328 ARG D CZ  1 
ATOM   15006 N NH1 . ARG D 1 328 ? 1.708   15.807  63.137  1.00 100.13 ? 328 ARG D NH1 1 
ATOM   15007 N NH2 . ARG D 1 328 ? 1.287   16.061  60.900  1.00 98.45  ? 328 ARG D NH2 1 
ATOM   15008 N N   . ASP D 1 329 ? -3.172  17.815  66.586  1.00 74.77  ? 329 ASP D N   1 
ATOM   15009 C CA  . ASP D 1 329 ? -3.838  17.809  67.882  1.00 75.58  ? 329 ASP D CA  1 
ATOM   15010 C C   . ASP D 1 329 ? -5.233  18.412  67.779  1.00 76.96  ? 329 ASP D C   1 
ATOM   15011 O O   . ASP D 1 329 ? -6.217  17.807  68.224  1.00 79.16  ? 329 ASP D O   1 
ATOM   15012 C CB  . ASP D 1 329 ? -2.995  18.563  68.905  1.00 76.56  ? 329 ASP D CB  1 
ATOM   15013 C CG  . ASP D 1 329 ? -3.115  17.977  70.288  1.00 76.14  ? 329 ASP D CG  1 
ATOM   15014 O OD1 . ASP D 1 329 ? -2.863  16.764  70.439  1.00 80.61  ? 329 ASP D OD1 1 
ATOM   15015 O OD2 . ASP D 1 329 ? -3.467  18.728  71.219  1.00 75.47  ? 329 ASP D OD2 1 
ATOM   15016 N N   . PHE D 1 330 ? -5.338  19.592  67.163  1.00 69.51  ? 330 PHE D N   1 
ATOM   15017 C CA  . PHE D 1 330 ? -6.622  20.281  67.078  1.00 74.46  ? 330 PHE D CA  1 
ATOM   15018 C C   . PHE D 1 330 ? -7.671  19.426  66.371  1.00 74.30  ? 330 PHE D C   1 
ATOM   15019 O O   . PHE D 1 330 ? -8.764  19.202  66.903  1.00 75.69  ? 330 PHE D O   1 
ATOM   15020 C CB  . PHE D 1 330 ? -6.444  21.625  66.370  1.00 71.93  ? 330 PHE D CB  1 
ATOM   15021 C CG  . PHE D 1 330 ? -7.635  22.524  66.484  1.00 71.65  ? 330 PHE D CG  1 
ATOM   15022 C CD1 . PHE D 1 330 ? -7.889  23.210  67.660  1.00 75.37  ? 330 PHE D CD1 1 
ATOM   15023 C CD2 . PHE D 1 330 ? -8.509  22.678  65.418  1.00 72.48  ? 330 PHE D CD2 1 
ATOM   15024 C CE1 . PHE D 1 330 ? -8.995  24.037  67.773  1.00 78.60  ? 330 PHE D CE1 1 
ATOM   15025 C CE2 . PHE D 1 330 ? -9.613  23.503  65.523  1.00 73.12  ? 330 PHE D CE2 1 
ATOM   15026 C CZ  . PHE D 1 330 ? -9.857  24.183  66.703  1.00 77.50  ? 330 PHE D CZ  1 
ATOM   15027 N N   . ILE D 1 331 ? -7.348  18.925  65.175  1.00 71.88  ? 331 ILE D N   1 
ATOM   15028 C CA  . ILE D 1 331 ? -8.303  18.111  64.422  1.00 72.73  ? 331 ILE D CA  1 
ATOM   15029 C C   . ILE D 1 331 ? -8.653  16.839  65.188  1.00 71.14  ? 331 ILE D C   1 
ATOM   15030 O O   . ILE D 1 331 ? -9.823  16.439  65.251  1.00 72.66  ? 331 ILE D O   1 
ATOM   15031 C CB  . ILE D 1 331 ? -7.746  17.802  63.019  1.00 71.79  ? 331 ILE D CB  1 
ATOM   15032 C CG1 . ILE D 1 331 ? -7.370  19.099  62.302  1.00 73.77  ? 331 ILE D CG1 1 
ATOM   15033 C CG2 . ILE D 1 331 ? -8.758  17.027  62.193  1.00 76.53  ? 331 ILE D CG2 1 
ATOM   15034 C CD1 . ILE D 1 331 ? -8.555  19.925  61.900  1.00 68.50  ? 331 ILE D CD1 1 
ATOM   15035 N N   . GLY D 1 332 ? -7.653  16.186  65.785  1.00 67.78  ? 332 GLY D N   1 
ATOM   15036 C CA  . GLY D 1 332 ? -7.932  14.991  66.567  1.00 73.50  ? 332 GLY D CA  1 
ATOM   15037 C C   . GLY D 1 332 ? -8.757  15.284  67.806  1.00 80.25  ? 332 GLY D C   1 
ATOM   15038 O O   . GLY D 1 332 ? -9.640  14.503  68.177  1.00 76.67  ? 332 GLY D O   1 
ATOM   15039 N N   . ARG D 1 333 ? -8.480  16.414  68.463  1.00 76.27  ? 333 ARG D N   1 
ATOM   15040 C CA  . ARG D 1 333 ? -9.277  16.822  69.616  1.00 75.02  ? 333 ARG D CA  1 
ATOM   15041 C C   . ARG D 1 333 ? -10.727 17.071  69.224  1.00 80.14  ? 333 ARG D C   1 
ATOM   15042 O O   . ARG D 1 333 ? -11.651 16.700  69.956  1.00 81.51  ? 333 ARG D O   1 
ATOM   15043 C CB  . ARG D 1 333 ? -8.670  18.070  70.252  1.00 70.86  ? 333 ARG D CB  1 
ATOM   15044 C CG  . ARG D 1 333 ? -7.479  17.772  71.127  1.00 68.79  ? 333 ARG D CG  1 
ATOM   15045 C CD  . ARG D 1 333 ? -7.225  18.865  72.137  1.00 62.95  ? 333 ARG D CD  1 
ATOM   15046 N NE  . ARG D 1 333 ? -5.852  18.793  72.612  1.00 71.75  ? 333 ARG D NE  1 
ATOM   15047 C CZ  . ARG D 1 333 ? -5.498  18.344  73.808  1.00 72.94  ? 333 ARG D CZ  1 
ATOM   15048 N NH1 . ARG D 1 333 ? -6.398  17.951  74.691  1.00 72.25  ? 333 ARG D NH1 1 
ATOM   15049 N NH2 . ARG D 1 333 ? -4.206  18.287  74.125  1.00 82.02  ? 333 ARG D NH2 1 
ATOM   15050 N N   . LEU D 1 334 ? -10.942 17.710  68.073  1.00 76.93  ? 334 LEU D N   1 
ATOM   15051 C CA  . LEU D 1 334 ? -12.290 17.862  67.542  1.00 74.35  ? 334 LEU D CA  1 
ATOM   15052 C C   . LEU D 1 334 ? -12.913 16.506  67.225  1.00 81.42  ? 334 LEU D C   1 
ATOM   15053 O O   . LEU D 1 334 ? -14.124 16.322  67.394  1.00 88.22  ? 334 LEU D O   1 
ATOM   15054 C CB  . LEU D 1 334 ? -12.245 18.750  66.297  1.00 72.12  ? 334 LEU D CB  1 
ATOM   15055 C CG  . LEU D 1 334 ? -12.442 20.263  66.461  1.00 76.82  ? 334 LEU D CG  1 
ATOM   15056 C CD1 . LEU D 1 334 ? -11.387 20.894  67.368  1.00 70.07  ? 334 LEU D CD1 1 
ATOM   15057 C CD2 . LEU D 1 334 ? -12.446 20.949  65.099  1.00 73.16  ? 334 LEU D CD2 1 
ATOM   15058 N N   . LYS D 1 335 ? -12.100 15.545  66.773  1.00 81.21  ? 335 LYS D N   1 
ATOM   15059 C CA  . LYS D 1 335 ? -12.604 14.202  66.499  1.00 82.40  ? 335 LYS D CA  1 
ATOM   15060 C C   . LYS D 1 335 ? -13.137 13.550  67.769  1.00 88.01  ? 335 LYS D C   1 
ATOM   15061 O O   . LYS D 1 335 ? -14.243 12.996  67.781  1.00 87.76  ? 335 LYS D O   1 
ATOM   15062 C CB  . LYS D 1 335 ? -11.496 13.346  65.879  1.00 88.67  ? 335 LYS D CB  1 
ATOM   15063 C CG  . LYS D 1 335 ? -11.710 12.958  64.416  1.00 88.76  ? 335 LYS D CG  1 
ATOM   15064 C CD  . LYS D 1 335 ? -13.085 12.335  64.180  1.00 96.02  ? 335 LYS D CD  1 
ATOM   15065 C CE  . LYS D 1 335 ? -13.183 11.701  62.789  1.00 88.90  ? 335 LYS D CE  1 
ATOM   15066 N NZ  . LYS D 1 335 ? -14.588 11.602  62.280  1.00 80.46  ? 335 LYS D NZ  1 
ATOM   15067 N N   . LYS D 1 336 ? -12.360 13.613  68.855  1.00 82.92  ? 336 LYS D N   1 
ATOM   15068 C CA  . LYS D 1 336 ? -12.815 13.047  70.121  1.00 85.19  ? 336 LYS D CA  1 
ATOM   15069 C C   . LYS D 1 336 ? -14.133 13.673  70.559  1.00 84.62  ? 336 LYS D C   1 
ATOM   15070 O O   . LYS D 1 336 ? -15.030 12.971  71.040  1.00 86.51  ? 336 LYS D O   1 
ATOM   15071 C CB  . LYS D 1 336 ? -11.742 13.228  71.196  1.00 76.21  ? 336 LYS D CB  1 
ATOM   15072 C CG  . LYS D 1 336 ? -10.688 12.128  71.218  1.00 83.18  ? 336 LYS D CG  1 
ATOM   15073 C CD  . LYS D 1 336 ? -10.361 11.707  72.643  1.00 95.28  ? 336 LYS D CD  1 
ATOM   15074 C CE  . LYS D 1 336 ? -8.860  11.603  72.862  1.00 101.86 ? 336 LYS D CE  1 
ATOM   15075 N NZ  . LYS D 1 336 ? -8.439  12.287  74.119  1.00 99.62  ? 336 LYS D NZ  1 
ATOM   15076 N N   . ILE D 1 337 ? -14.275 14.990  70.384  1.00 76.37  ? 337 ILE D N   1 
ATOM   15077 C CA  . ILE D 1 337 ? -15.539 15.656  70.692  1.00 82.66  ? 337 ILE D CA  1 
ATOM   15078 C C   . ILE D 1 337 ? -16.674 15.036  69.889  1.00 86.58  ? 337 ILE D C   1 
ATOM   15079 O O   . ILE D 1 337 ? -17.774 14.810  70.410  1.00 84.21  ? 337 ILE D O   1 
ATOM   15080 C CB  . ILE D 1 337 ? -15.428 17.172  70.432  1.00 80.04  ? 337 ILE D CB  1 
ATOM   15081 C CG1 . ILE D 1 337 ? -14.278 17.779  71.233  1.00 75.87  ? 337 ILE D CG1 1 
ATOM   15082 C CG2 . ILE D 1 337 ? -16.740 17.882  70.760  1.00 65.66  ? 337 ILE D CG2 1 
ATOM   15083 C CD1 . ILE D 1 337 ? -14.038 19.235  70.921  1.00 67.07  ? 337 ILE D CD1 1 
ATOM   15084 N N   . HIS D 1 338 ? -16.420 14.738  68.612  1.00 82.61  ? 338 HIS D N   1 
ATOM   15085 C CA  . HIS D 1 338 ? -17.457 14.181  67.750  1.00 85.83  ? 338 HIS D CA  1 
ATOM   15086 C C   . HIS D 1 338 ? -17.963 12.844  68.281  1.00 86.32  ? 338 HIS D C   1 
ATOM   15087 O O   . HIS D 1 338 ? -19.174 12.631  68.410  1.00 85.50  ? 338 HIS D O   1 
ATOM   15088 C CB  . HIS D 1 338 ? -16.917 14.025  66.330  1.00 91.83  ? 338 HIS D CB  1 
ATOM   15089 C CG  . HIS D 1 338 ? -17.976 14.065  65.276  1.00 92.90  ? 338 HIS D CG  1 
ATOM   15090 N ND1 . HIS D 1 338 ? -18.815 15.146  65.108  1.00 92.68  ? 338 HIS D ND1 1 
ATOM   15091 C CD2 . HIS D 1 338 ? -18.336 13.157  64.339  1.00 84.40  ? 338 HIS D CD2 1 
ATOM   15092 C CE1 . HIS D 1 338 ? -19.644 14.903  64.109  1.00 91.44  ? 338 HIS D CE1 1 
ATOM   15093 N NE2 . HIS D 1 338 ? -19.374 13.704  63.625  1.00 90.80  ? 338 HIS D NE2 1 
ATOM   15094 N N   . GLU D 1 339 ? -17.043 11.926  68.589  1.00 88.04  ? 339 GLU D N   1 
ATOM   15095 C CA  . GLU D 1 339 ? -17.427 10.627  69.130  1.00 87.93  ? 339 GLU D CA  1 
ATOM   15096 C C   . GLU D 1 339 ? -17.866 10.713  70.586  1.00 84.43  ? 339 GLU D C   1 
ATOM   15097 O O   . GLU D 1 339 ? -18.466 9.763   71.097  1.00 88.68  ? 339 GLU D O   1 
ATOM   15098 C CB  . GLU D 1 339 ? -16.264 9.641   68.998  1.00 85.97  ? 339 GLU D CB  1 
ATOM   15099 C CG  . GLU D 1 339 ? -15.655 9.580   67.603  1.00 91.20  ? 339 GLU D CG  1 
ATOM   15100 C CD  . GLU D 1 339 ? -14.134 9.574   67.620  1.00 94.32  ? 339 GLU D CD  1 
ATOM   15101 O OE1 . GLU D 1 339 ? -13.527 9.512   66.529  1.00 89.64  ? 339 GLU D OE1 1 
ATOM   15102 O OE2 . GLU D 1 339 ? -13.545 9.645   68.720  1.00 91.58  ? 339 GLU D OE2 1 
ATOM   15103 N N   . SER D 1 340 ? -17.585 11.826  71.265  1.00 86.72  ? 340 SER D N   1 
ATOM   15104 C CA  . SER D 1 340 ? -17.946 11.948  72.671  1.00 84.69  ? 340 SER D CA  1 
ATOM   15105 C C   . SER D 1 340 ? -19.423 12.267  72.875  1.00 83.28  ? 340 SER D C   1 
ATOM   15106 O O   . SER D 1 340 ? -19.973 11.947  73.932  1.00 85.10  ? 340 SER D O   1 
ATOM   15107 C CB  . SER D 1 340 ? -17.085 13.024  73.336  1.00 79.03  ? 340 SER D CB  1 
ATOM   15108 O OG  . SER D 1 340 ? -17.875 14.124  73.745  1.00 74.12  ? 340 SER D OG  1 
ATOM   15109 N N   . VAL D 1 341 ? -20.082 12.886  71.896  1.00 85.21  ? 341 VAL D N   1 
ATOM   15110 C CA  . VAL D 1 341 ? -21.454 13.357  72.062  1.00 81.83  ? 341 VAL D CA  1 
ATOM   15111 C C   . VAL D 1 341 ? -22.353 12.742  70.995  1.00 89.65  ? 341 VAL D C   1 
ATOM   15112 O O   . VAL D 1 341 ? -21.920 12.464  69.872  1.00 91.88  ? 341 VAL D O   1 
ATOM   15113 C CB  . VAL D 1 341 ? -21.527 14.901  72.019  1.00 83.08  ? 341 VAL D CB  1 
ATOM   15114 C CG1 . VAL D 1 341 ? -20.778 15.507  73.194  1.00 89.24  ? 341 VAL D CG1 1 
ATOM   15115 C CG2 . VAL D 1 341 ? -20.956 15.428  70.715  1.00 80.60  ? 341 VAL D CG2 1 
ATOM   15116 N N   . ASP D 1 342 ? -23.626 12.542  71.357  1.00 93.26  ? 342 ASP D N   1 
ATOM   15117 C CA  . ASP D 1 342 ? -24.622 11.979  70.446  1.00 90.36  ? 342 ASP D CA  1 
ATOM   15118 C C   . ASP D 1 342 ? -25.292 13.034  69.574  1.00 94.44  ? 342 ASP D C   1 
ATOM   15119 O O   . ASP D 1 342 ? -25.826 12.700  68.510  1.00 103.53 ? 342 ASP D O   1 
ATOM   15120 C CB  . ASP D 1 342 ? -25.700 11.228  71.234  1.00 88.34  ? 342 ASP D CB  1 
ATOM   15121 C CG  . ASP D 1 342 ? -26.794 12.154  71.755  1.00 98.39  ? 342 ASP D CG  1 
ATOM   15122 O OD1 . ASP D 1 342 ? -27.704 12.521  70.979  1.00 101.32 ? 342 ASP D OD1 1 
ATOM   15123 O OD2 . ASP D 1 342 ? -26.733 12.528  72.945  1.00 108.53 ? 342 ASP D OD2 1 
ATOM   15124 N N   . PHE D 1 343 ? -25.306 14.284  70.018  1.00 92.45  ? 343 PHE D N   1 
ATOM   15125 C CA  . PHE D 1 343 ? -25.877 15.382  69.255  1.00 91.11  ? 343 PHE D CA  1 
ATOM   15126 C C   . PHE D 1 343 ? -24.828 15.950  68.298  1.00 82.92  ? 343 PHE D C   1 
ATOM   15127 O O   . PHE D 1 343 ? -23.666 15.546  68.308  1.00 81.04  ? 343 PHE D O   1 
ATOM   15128 C CB  . PHE D 1 343 ? -26.426 16.467  70.196  1.00 85.90  ? 343 PHE D CB  1 
ATOM   15129 C CG  . PHE D 1 343 ? -25.563 16.730  71.409  1.00 87.28  ? 343 PHE D CG  1 
ATOM   15130 C CD1 . PHE D 1 343 ? -25.527 15.847  72.481  1.00 84.34  ? 343 PHE D CD1 1 
ATOM   15131 C CD2 . PHE D 1 343 ? -24.811 17.893  71.486  1.00 86.75  ? 343 PHE D CD2 1 
ATOM   15132 C CE1 . PHE D 1 343 ? -24.735 16.108  73.590  1.00 86.51  ? 343 PHE D CE1 1 
ATOM   15133 C CE2 . PHE D 1 343 ? -24.016 18.156  72.593  1.00 78.55  ? 343 PHE D CE2 1 
ATOM   15134 C CZ  . PHE D 1 343 ? -23.979 17.267  73.642  1.00 77.77  ? 343 PHE D CZ  1 
ATOM   15135 N N   . GLN D 1 344 ? -25.257 16.876  67.436  1.00 84.54  ? 344 GLN D N   1 
ATOM   15136 C CA  . GLN D 1 344 ? -24.294 17.586  66.596  1.00 85.20  ? 344 GLN D CA  1 
ATOM   15137 C C   . GLN D 1 344 ? -23.667 18.701  67.421  1.00 79.67  ? 344 GLN D C   1 
ATOM   15138 O O   . GLN D 1 344 ? -24.336 19.693  67.741  1.00 78.37  ? 344 GLN D O   1 
ATOM   15139 C CB  . GLN D 1 344 ? -24.951 18.143  65.331  1.00 85.42  ? 344 GLN D CB  1 
ATOM   15140 C CG  . GLN D 1 344 ? -24.607 17.351  64.084  1.00 88.50  ? 344 GLN D CG  1 
ATOM   15141 C CD  . GLN D 1 344 ? -25.403 17.784  62.873  1.00 84.44  ? 344 GLN D CD  1 
ATOM   15142 O OE1 . GLN D 1 344 ? -26.285 18.633  62.967  1.00 82.09  ? 344 GLN D OE1 1 
ATOM   15143 N NE2 . GLN D 1 344 ? -25.113 17.177  61.729  1.00 87.02  ? 344 GLN D NE2 1 
ATOM   15144 N N   . PRO D 1 345 ? -22.397 18.572  67.794  1.00 82.64  ? 345 PRO D N   1 
ATOM   15145 C CA  . PRO D 1 345 ? -21.805 19.526  68.736  1.00 81.54  ? 345 PRO D CA  1 
ATOM   15146 C C   . PRO D 1 345 ? -21.483 20.855  68.073  1.00 76.16  ? 345 PRO D C   1 
ATOM   15147 O O   . PRO D 1 345 ? -21.070 20.915  66.911  1.00 78.73  ? 345 PRO D O   1 
ATOM   15148 C CB  . PRO D 1 345 ? -20.528 18.810  69.193  1.00 79.80  ? 345 PRO D CB  1 
ATOM   15149 C CG  . PRO D 1 345 ? -20.129 18.026  67.981  1.00 80.49  ? 345 PRO D CG  1 
ATOM   15150 C CD  . PRO D 1 345 ? -21.430 17.537  67.386  1.00 81.75  ? 345 PRO D CD  1 
ATOM   15151 N N   . VAL D 1 346 ? -21.694 21.931  68.827  1.00 69.75  ? 346 VAL D N   1 
ATOM   15152 C CA  . VAL D 1 346 ? -21.256 23.266  68.439  1.00 70.73  ? 346 VAL D CA  1 
ATOM   15153 C C   . VAL D 1 346 ? -20.068 23.635  69.324  1.00 69.33  ? 346 VAL D C   1 
ATOM   15154 O O   . VAL D 1 346 ? -20.179 23.700  70.557  1.00 70.87  ? 346 VAL D O   1 
ATOM   15155 C CB  . VAL D 1 346 ? -22.395 24.298  68.512  1.00 68.65  ? 346 VAL D CB  1 
ATOM   15156 C CG1 . VAL D 1 346 ? -22.879 24.533  69.945  1.00 72.34  ? 346 VAL D CG1 1 
ATOM   15157 C CG2 . VAL D 1 346 ? -21.951 25.604  67.864  1.00 67.74  ? 346 VAL D CG2 1 
ATOM   15158 N N   . VAL D 1 347 ? -18.910 23.822  68.696  1.00 74.46  ? 347 VAL D N   1 
ATOM   15159 C CA  . VAL D 1 347 ? -17.667 24.116  69.399  1.00 70.07  ? 347 VAL D CA  1 
ATOM   15160 C C   . VAL D 1 347 ? -17.310 25.572  69.140  1.00 70.30  ? 347 VAL D C   1 
ATOM   15161 O O   . VAL D 1 347 ? -17.086 25.973  67.989  1.00 74.75  ? 347 VAL D O   1 
ATOM   15162 C CB  . VAL D 1 347 ? -16.528 23.179  68.971  1.00 66.28  ? 347 VAL D CB  1 
ATOM   15163 C CG1 . VAL D 1 347 ? -15.346 23.361  69.901  1.00 70.66  ? 347 VAL D CG1 1 
ATOM   15164 C CG2 . VAL D 1 347 ? -16.991 21.738  68.976  1.00 65.23  ? 347 VAL D CG2 1 
ATOM   15165 N N   . PHE D 1 348 ? -17.253 26.351  70.214  1.00 66.81  ? 348 PHE D N   1 
ATOM   15166 C CA  . PHE D 1 348 ? -16.921 27.769  70.174  1.00 64.09  ? 348 PHE D CA  1 
ATOM   15167 C C   . PHE D 1 348 ? -15.486 27.938  70.644  1.00 62.29  ? 348 PHE D C   1 
ATOM   15168 O O   . PHE D 1 348 ? -15.174 27.650  71.805  1.00 62.81  ? 348 PHE D O   1 
ATOM   15169 C CB  . PHE D 1 348 ? -17.861 28.575  71.069  1.00 69.27  ? 348 PHE D CB  1 
ATOM   15170 C CG  . PHE D 1 348 ? -18.996 29.231  70.337  1.00 60.65  ? 348 PHE D CG  1 
ATOM   15171 C CD1 . PHE D 1 348 ? -19.983 28.470  69.740  1.00 62.24  ? 348 PHE D CD1 1 
ATOM   15172 C CD2 . PHE D 1 348 ? -19.078 30.611  70.255  1.00 59.32  ? 348 PHE D CD2 1 
ATOM   15173 C CE1 . PHE D 1 348 ? -21.028 29.070  69.074  1.00 63.69  ? 348 PHE D CE1 1 
ATOM   15174 C CE2 . PHE D 1 348 ? -20.117 31.220  69.587  1.00 55.87  ? 348 PHE D CE2 1 
ATOM   15175 C CZ  . PHE D 1 348 ? -21.095 30.447  68.994  1.00 63.92  ? 348 PHE D CZ  1 
ATOM   15176 N N   . VAL D 1 349 ? -14.621 28.392  69.749  1.00 62.16  ? 349 VAL D N   1 
ATOM   15177 C CA  . VAL D 1 349 ? -13.215 28.620  70.051  1.00 64.87  ? 349 VAL D CA  1 
ATOM   15178 C C   . VAL D 1 349 ? -13.008 30.128  70.053  1.00 67.11  ? 349 VAL D C   1 
ATOM   15179 O O   . VAL D 1 349 ? -12.914 30.762  68.994  1.00 62.18  ? 349 VAL D O   1 
ATOM   15180 C CB  . VAL D 1 349 ? -12.289 27.922  69.052  1.00 64.02  ? 349 VAL D CB  1 
ATOM   15181 C CG1 . VAL D 1 349 ? -10.868 28.407  69.237  1.00 66.56  ? 349 VAL D CG1 1 
ATOM   15182 C CG2 . VAL D 1 349 ? -12.367 26.413  69.228  1.00 70.30  ? 349 VAL D CG2 1 
ATOM   15183 N N   . VAL D 1 350 ? -12.933 30.705  71.248  1.00 70.30  ? 350 VAL D N   1 
ATOM   15184 C CA  . VAL D 1 350 ? -12.881 32.148  71.435  1.00 69.31  ? 350 VAL D CA  1 
ATOM   15185 C C   . VAL D 1 350 ? -11.588 32.491  72.159  1.00 67.80  ? 350 VAL D C   1 
ATOM   15186 O O   . VAL D 1 350 ? -11.325 31.971  73.250  1.00 68.36  ? 350 VAL D O   1 
ATOM   15187 C CB  . VAL D 1 350 ? -14.098 32.655  72.222  1.00 64.97  ? 350 VAL D CB  1 
ATOM   15188 C CG1 . VAL D 1 350 ? -14.018 34.165  72.402  1.00 62.56  ? 350 VAL D CG1 1 
ATOM   15189 C CG2 . VAL D 1 350 ? -15.389 32.243  71.522  1.00 64.56  ? 350 VAL D CG2 1 
ATOM   15190 N N   . LEU D 1 351 ? -10.791 33.372  71.561  1.00 64.01  ? 351 LEU D N   1 
ATOM   15191 C CA  . LEU D 1 351 ? -9.561  33.836  72.185  1.00 63.09  ? 351 LEU D CA  1 
ATOM   15192 C C   . LEU D 1 351 ? -9.179  35.165  71.553  1.00 66.64  ? 351 LEU D C   1 
ATOM   15193 O O   . LEU D 1 351 ? -9.773  35.599  70.563  1.00 65.50  ? 351 LEU D O   1 
ATOM   15194 C CB  . LEU D 1 351 ? -8.439  32.805  72.042  1.00 60.09  ? 351 LEU D CB  1 
ATOM   15195 C CG  . LEU D 1 351 ? -8.013  32.430  70.623  1.00 69.97  ? 351 LEU D CG  1 
ATOM   15196 C CD1 . LEU D 1 351 ? -6.562  31.949  70.592  1.00 66.15  ? 351 LEU D CD1 1 
ATOM   15197 C CD2 . LEU D 1 351 ? -8.947  31.378  70.029  1.00 72.73  ? 351 LEU D CD2 1 
ATOM   15198 N N   . ASP D 1 352 ? -8.179  35.810  72.145  1.00 68.37  ? 352 ASP D N   1 
ATOM   15199 C CA  . ASP D 1 352 ? -7.672  37.059  71.593  1.00 64.20  ? 352 ASP D CA  1 
ATOM   15200 C C   . ASP D 1 352 ? -6.914  36.778  70.304  1.00 68.22  ? 352 ASP D C   1 
ATOM   15201 O O   . ASP D 1 352 ? -6.055  35.890  70.258  1.00 70.58  ? 352 ASP D O   1 
ATOM   15202 C CB  . ASP D 1 352 ? -6.763  37.761  72.598  1.00 62.86  ? 352 ASP D CB  1 
ATOM   15203 C CG  . ASP D 1 352 ? -7.435  37.978  73.935  1.00 67.23  ? 352 ASP D CG  1 
ATOM   15204 O OD1 . ASP D 1 352 ? -8.677  37.879  73.999  1.00 65.19  ? 352 ASP D OD1 1 
ATOM   15205 O OD2 . ASP D 1 352 ? -6.719  38.255  74.923  1.00 71.55  ? 352 ASP D OD2 1 
ATOM   15206 N N   . GLY D 1 353 ? -7.225  37.541  69.260  1.00 69.68  ? 353 GLY D N   1 
ATOM   15207 C CA  . GLY D 1 353 ? -6.669  37.340  67.939  1.00 68.64  ? 353 GLY D CA  1 
ATOM   15208 C C   . GLY D 1 353 ? -5.370  38.053  67.620  1.00 69.33  ? 353 GLY D C   1 
ATOM   15209 O O   . GLY D 1 353 ? -4.940  38.004  66.464  1.00 72.99  ? 353 GLY D O   1 
ATOM   15210 N N   . GLU D 1 354 ? -4.716  38.699  68.588  1.00 69.71  ? 354 GLU D N   1 
ATOM   15211 C CA  . GLU D 1 354 ? -3.510  39.472  68.302  1.00 64.30  ? 354 GLU D CA  1 
ATOM   15212 C C   . GLU D 1 354 ? -2.328  39.173  69.213  1.00 68.72  ? 354 GLU D C   1 
ATOM   15213 O O   . GLU D 1 354 ? -1.193  39.494  68.835  1.00 72.55  ? 354 GLU D O   1 
ATOM   15214 C CB  . GLU D 1 354 ? -3.806  40.978  68.381  1.00 63.52  ? 354 GLU D CB  1 
ATOM   15215 C CG  . GLU D 1 354 ? -4.051  41.492  69.792  1.00 67.99  ? 354 GLU D CG  1 
ATOM   15216 C CD  . GLU D 1 354 ? -5.496  41.352  70.217  1.00 71.58  ? 354 GLU D CD  1 
ATOM   15217 O OE1 . GLU D 1 354 ? -5.914  40.214  70.520  1.00 75.54  ? 354 GLU D OE1 1 
ATOM   15218 O OE2 . GLU D 1 354 ? -6.211  42.380  70.250  1.00 65.67  ? 354 GLU D OE2 1 
ATOM   15219 N N   . ASN D 1 355 ? -2.540  38.575  70.383  1.00 67.14  ? 355 ASN D N   1 
ATOM   15220 C CA  . ASN D 1 355 ? -1.472  38.455  71.366  1.00 66.33  ? 355 ASN D CA  1 
ATOM   15221 C C   . ASN D 1 355 ? -0.686  37.155  71.253  1.00 58.67  ? 355 ASN D C   1 
ATOM   15222 O O   . ASN D 1 355 ? 0.493   37.128  71.616  1.00 68.60  ? 355 ASN D O   1 
ATOM   15223 C CB  . ASN D 1 355 ? -2.045  38.595  72.784  1.00 72.23  ? 355 ASN D CB  1 
ATOM   15224 C CG  . ASN D 1 355 ? -2.916  39.840  72.952  1.00 68.68  ? 355 ASN D CG  1 
ATOM   15225 O OD1 . ASN D 1 355 ? -2.499  40.957  72.634  1.00 64.18  ? 355 ASN D OD1 1 
ATOM   15226 N ND2 . ASN D 1 355 ? -4.126  39.650  73.474  1.00 66.26  ? 355 ASN D ND2 1 
ATOM   15227 N N   . CYS D 1 356 ? -1.291  36.074  70.757  1.00 61.75  ? 356 CYS D N   1 
ATOM   15228 C CA  . CYS D 1 356 ? -0.580  34.800  70.742  1.00 62.31  ? 356 CYS D CA  1 
ATOM   15229 C C   . CYS D 1 356 ? 0.381   34.686  69.574  1.00 67.07  ? 356 CYS D C   1 
ATOM   15230 O O   . CYS D 1 356 ? 1.305   33.865  69.624  1.00 68.50  ? 356 CYS D O   1 
ATOM   15231 C CB  . CYS D 1 356 ? -1.550  33.621  70.670  1.00 61.08  ? 356 CYS D CB  1 
ATOM   15232 S SG  . CYS D 1 356 ? -2.705  33.687  69.285  1.00 66.65  ? 356 CYS D SG  1 
ATOM   15233 N N   . TRP D 1 357 ? 0.194   35.497  68.533  1.00 66.73  ? 357 TRP D N   1 
ATOM   15234 C CA  . TRP D 1 357 ? 0.890   35.255  67.275  1.00 72.73  ? 357 TRP D CA  1 
ATOM   15235 C C   . TRP D 1 357 ? 2.344   35.710  67.309  1.00 68.82  ? 357 TRP D C   1 
ATOM   15236 O O   . TRP D 1 357 ? 3.194   35.088  66.661  1.00 63.96  ? 357 TRP D O   1 
ATOM   15237 C CB  . TRP D 1 357 ? 0.127   35.928  66.136  1.00 71.43  ? 357 TRP D CB  1 
ATOM   15238 C CG  . TRP D 1 357 ? -1.326  35.535  66.115  1.00 71.61  ? 357 TRP D CG  1 
ATOM   15239 C CD1 . TRP D 1 357 ? -2.405  36.372  66.110  1.00 71.55  ? 357 TRP D CD1 1 
ATOM   15240 C CD2 . TRP D 1 357 ? -1.855  34.201  66.098  1.00 71.34  ? 357 TRP D CD2 1 
ATOM   15241 N NE1 . TRP D 1 357 ? -3.571  35.642  66.090  1.00 72.59  ? 357 TRP D NE1 1 
ATOM   15242 C CE2 . TRP D 1 357 ? -3.260  34.308  66.081  1.00 72.90  ? 357 TRP D CE2 1 
ATOM   15243 C CE3 . TRP D 1 357 ? -1.276  32.928  66.095  1.00 77.43  ? 357 TRP D CE3 1 
ATOM   15244 C CZ2 . TRP D 1 357 ? -4.094  33.191  66.065  1.00 74.25  ? 357 TRP D CZ2 1 
ATOM   15245 C CZ3 . TRP D 1 357 ? -2.106  31.820  66.078  1.00 79.05  ? 357 TRP D CZ3 1 
ATOM   15246 C CH2 . TRP D 1 357 ? -3.499  31.959  66.063  1.00 71.69  ? 357 TRP D CH2 1 
ATOM   15247 N N   . GLU D 1 358 ? 2.656   36.775  68.051  1.00 70.75  ? 358 GLU D N   1 
ATOM   15248 C CA  . GLU D 1 358 ? 4.045   37.215  68.132  1.00 62.00  ? 358 GLU D CA  1 
ATOM   15249 C C   . GLU D 1 358 ? 4.928   36.107  68.679  1.00 65.51  ? 358 GLU D C   1 
ATOM   15250 O O   . GLU D 1 358 ? 6.102   35.995  68.307  1.00 69.72  ? 358 GLU D O   1 
ATOM   15251 C CB  . GLU D 1 358 ? 4.170   38.459  69.007  1.00 65.70  ? 358 GLU D CB  1 
ATOM   15252 C CG  . GLU D 1 358 ? 3.193   38.490  70.159  1.00 70.27  ? 358 GLU D CG  1 
ATOM   15253 C CD  . GLU D 1 358 ? 2.965   39.886  70.689  1.00 74.49  ? 358 GLU D CD  1 
ATOM   15254 O OE1 . GLU D 1 358 ? 2.366   40.704  69.961  1.00 74.06  ? 358 GLU D OE1 1 
ATOM   15255 O OE2 . GLU D 1 358 ? 3.376   40.163  71.836  1.00 78.81  ? 358 GLU D OE2 1 
ATOM   15256 N N   . TYR D 1 359 ? 4.378   35.270  69.561  1.00 60.87  ? 359 TYR D N   1 
ATOM   15257 C CA  . TYR D 1 359 ? 5.151   34.183  70.143  1.00 61.25  ? 359 TYR D CA  1 
ATOM   15258 C C   . TYR D 1 359 ? 5.162   32.942  69.264  1.00 64.20  ? 359 TYR D C   1 
ATOM   15259 O O   . TYR D 1 359 ? 5.998   32.055  69.474  1.00 63.08  ? 359 TYR D O   1 
ATOM   15260 C CB  . TYR D 1 359 ? 4.611   33.848  71.528  1.00 65.30  ? 359 TYR D CB  1 
ATOM   15261 C CG  . TYR D 1 359 ? 4.668   35.017  72.476  1.00 67.24  ? 359 TYR D CG  1 
ATOM   15262 C CD1 . TYR D 1 359 ? 5.797   35.253  73.247  1.00 66.12  ? 359 TYR D CD1 1 
ATOM   15263 C CD2 . TYR D 1 359 ? 3.594   35.889  72.600  1.00 65.48  ? 359 TYR D CD2 1 
ATOM   15264 C CE1 . TYR D 1 359 ? 5.855   36.322  74.119  1.00 70.91  ? 359 TYR D CE1 1 
ATOM   15265 C CE2 . TYR D 1 359 ? 3.642   36.959  73.468  1.00 69.54  ? 359 TYR D CE2 1 
ATOM   15266 C CZ  . TYR D 1 359 ? 4.774   37.172  74.226  1.00 79.19  ? 359 TYR D CZ  1 
ATOM   15267 O OH  . TYR D 1 359 ? 4.822   38.239  75.093  1.00 83.79  ? 359 TYR D OH  1 
ATOM   15268 N N   . TYR D 1 360 ? 4.261   32.864  68.290  1.00 64.31  ? 360 TYR D N   1 
ATOM   15269 C CA  . TYR D 1 360 ? 4.352   31.832  67.272  1.00 61.91  ? 360 TYR D CA  1 
ATOM   15270 C C   . TYR D 1 360 ? 5.495   32.150  66.315  1.00 79.87  ? 360 TYR D C   1 
ATOM   15271 O O   . TYR D 1 360 ? 5.856   33.313  66.105  1.00 78.20  ? 360 TYR D O   1 
ATOM   15272 C CB  . TYR D 1 360 ? 3.060   31.737  66.469  1.00 66.06  ? 360 TYR D CB  1 
ATOM   15273 C CG  . TYR D 1 360 ? 1.970   30.844  67.022  1.00 74.47  ? 360 TYR D CG  1 
ATOM   15274 C CD1 . TYR D 1 360 ? 1.322   31.163  68.207  1.00 72.55  ? 360 TYR D CD1 1 
ATOM   15275 C CD2 . TYR D 1 360 ? 1.538   29.724  66.324  1.00 70.56  ? 360 TYR D CD2 1 
ATOM   15276 C CE1 . TYR D 1 360 ? 0.303   30.370  68.709  1.00 77.36  ? 360 TYR D CE1 1 
ATOM   15277 C CE2 . TYR D 1 360 ? 0.513   28.922  66.818  1.00 75.09  ? 360 TYR D CE2 1 
ATOM   15278 C CZ  . TYR D 1 360 ? -0.101  29.253  68.012  1.00 73.85  ? 360 TYR D CZ  1 
ATOM   15279 O OH  . TYR D 1 360 ? -1.120  28.474  68.515  1.00 67.65  ? 360 TYR D OH  1 
ATOM   15280 N N   . GLU D 1 361 ? 6.048   31.101  65.707  1.00 89.07  ? 361 GLU D N   1 
ATOM   15281 C CA  . GLU D 1 361 ? 7.073   31.263  64.685  1.00 79.54  ? 361 GLU D CA  1 
ATOM   15282 C C   . GLU D 1 361 ? 6.453   31.715  63.371  1.00 76.97  ? 361 GLU D C   1 
ATOM   15283 O O   . GLU D 1 361 ? 5.457   31.145  62.913  1.00 77.46  ? 361 GLU D O   1 
ATOM   15284 C CB  . GLU D 1 361 ? 7.824   29.950  64.465  1.00 83.36  ? 361 GLU D CB  1 
ATOM   15285 C CG  . GLU D 1 361 ? 8.338   29.333  65.741  1.00 92.28  ? 361 GLU D CG  1 
ATOM   15286 C CD  . GLU D 1 361 ? 9.705   29.849  66.124  1.00 102.24 ? 361 GLU D CD  1 
ATOM   15287 O OE1 . GLU D 1 361 ? 10.337  30.539  65.294  1.00 109.33 ? 361 GLU D OE1 1 
ATOM   15288 O OE2 . GLU D 1 361 ? 10.149  29.571  67.262  1.00 102.17 ? 361 GLU D OE2 1 
ATOM   15289 N N   . GLU D 1 362 ? 7.069   32.723  62.755  1.00 77.03  ? 362 GLU D N   1 
ATOM   15290 C CA  . GLU D 1 362 ? 6.549   33.380  61.557  1.00 81.71  ? 362 GLU D CA  1 
ATOM   15291 C C   . GLU D 1 362 ? 5.098   33.828  61.776  1.00 82.04  ? 362 GLU D C   1 
ATOM   15292 O O   . GLU D 1 362 ? 4.151   33.397  61.105  1.00 82.86  ? 362 GLU D O   1 
ATOM   15293 C CB  . GLU D 1 362 ? 6.685   32.462  60.342  1.00 86.65  ? 362 GLU D CB  1 
ATOM   15294 C CG  . GLU D 1 362 ? 6.180   33.087  59.042  1.00 90.10  ? 362 GLU D CG  1 
ATOM   15295 C CD  . GLU D 1 362 ? 7.056   32.772  57.865  1.00 85.58  ? 362 GLU D CD  1 
ATOM   15296 O OE1 . GLU D 1 362 ? 8.174   32.260  58.072  1.00 102.30 ? 362 GLU D OE1 1 
ATOM   15297 O OE2 . GLU D 1 362 ? 6.606   33.003  56.725  1.00 80.26  ? 362 GLU D OE2 1 
ATOM   15298 N N   . ASN D 1 363 ? 4.960   34.696  62.780  1.00 86.13  ? 363 ASN D N   1 
ATOM   15299 C CA  . ASN D 1 363 ? 3.696   35.256  63.246  1.00 72.23  ? 363 ASN D CA  1 
ATOM   15300 C C   . ASN D 1 363 ? 2.527   34.278  63.181  1.00 73.06  ? 363 ASN D C   1 
ATOM   15301 O O   . ASN D 1 363 ? 1.377   34.698  63.021  1.00 81.06  ? 363 ASN D O   1 
ATOM   15302 C CB  . ASN D 1 363 ? 3.360   36.513  62.453  1.00 63.65  ? 363 ASN D CB  1 
ATOM   15303 C CG  . ASN D 1 363 ? 2.763   37.575  63.316  1.00 63.73  ? 363 ASN D CG  1 
ATOM   15304 O OD1 . ASN D 1 363 ? 3.252   37.858  64.408  1.00 62.13  ? 363 ASN D OD1 1 
ATOM   15305 N ND2 . ASN D 1 363 ? 1.688   38.174  62.840  1.00 71.48  ? 363 ASN D ND2 1 
ATOM   15306 N N   . GLY D 1 364 ? 2.805   32.980  63.330  1.00 67.30  ? 364 GLY D N   1 
ATOM   15307 C CA  . GLY D 1 364 ? 1.816   31.940  63.178  1.00 75.10  ? 364 GLY D CA  1 
ATOM   15308 C C   . GLY D 1 364 ? 1.256   31.746  61.788  1.00 73.37  ? 364 GLY D C   1 
ATOM   15309 O O   . GLY D 1 364 ? 0.269   31.010  61.634  1.00 76.60  ? 364 GLY D O   1 
ATOM   15310 N N   . ILE D 1 365 ? 1.820   32.393  60.767  1.00 70.24  ? 365 ILE D N   1 
ATOM   15311 C CA  . ILE D 1 365 ? 1.344   32.161  59.400  1.00 74.41  ? 365 ILE D CA  1 
ATOM   15312 C C   . ILE D 1 365 ? 1.415   30.691  59.016  1.00 79.84  ? 365 ILE D C   1 
ATOM   15313 O O   . ILE D 1 365 ? 0.479   30.194  58.364  1.00 78.24  ? 365 ILE D O   1 
ATOM   15314 C CB  . ILE D 1 365 ? 2.080   33.079  58.416  1.00 75.64  ? 365 ILE D CB  1 
ATOM   15315 C CG1 . ILE D 1 365 ? 1.823   34.549  58.760  1.00 76.38  ? 365 ILE D CG1 1 
ATOM   15316 C CG2 . ILE D 1 365 ? 1.705   32.766  56.973  1.00 70.45  ? 365 ILE D CG2 1 
ATOM   15317 C CD1 . ILE D 1 365 ? 3.046   35.248  59.151  1.00 81.41  ? 365 ILE D CD1 1 
ATOM   15318 N N   . PRO D 1 366 ? 2.472   29.944  59.342  1.00 81.67  ? 366 PRO D N   1 
ATOM   15319 C CA  . PRO D 1 366 ? 2.438   28.500  59.046  1.00 76.34  ? 366 PRO D CA  1 
ATOM   15320 C C   . PRO D 1 366 ? 1.289   27.785  59.729  1.00 75.71  ? 366 PRO D C   1 
ATOM   15321 O O   . PRO D 1 366 ? 0.641   26.933  59.110  1.00 78.76  ? 366 PRO D O   1 
ATOM   15322 C CB  . PRO D 1 366 ? 3.797   28.026  59.551  1.00 72.23  ? 366 PRO D CB  1 
ATOM   15323 C CG  . PRO D 1 366 ? 4.660   29.231  59.430  1.00 74.50  ? 366 PRO D CG  1 
ATOM   15324 C CD  . PRO D 1 366 ? 3.811   30.381  59.788  1.00 76.09  ? 366 PRO D CD  1 
ATOM   15325 N N   . PHE D 1 367 ? 1.017   28.110  60.994  1.00 73.39  ? 367 PHE D N   1 
ATOM   15326 C CA  . PHE D 1 367 ? -0.025  27.405  61.733  1.00 73.82  ? 367 PHE D CA  1 
ATOM   15327 C C   . PHE D 1 367 ? -1.405  27.722  61.177  1.00 72.48  ? 367 PHE D C   1 
ATOM   15328 O O   . PHE D 1 367 ? -2.165  26.817  60.812  1.00 76.27  ? 367 PHE D O   1 
ATOM   15329 C CB  . PHE D 1 367 ? 0.053   27.769  63.213  1.00 73.07  ? 367 PHE D CB  1 
ATOM   15330 C CG  . PHE D 1 367 ? -1.075  27.218  64.034  1.00 68.70  ? 367 PHE D CG  1 
ATOM   15331 C CD1 . PHE D 1 367 ? -1.195  25.853  64.251  1.00 76.91  ? 367 PHE D CD1 1 
ATOM   15332 C CD2 . PHE D 1 367 ? -2.013  28.066  64.595  1.00 67.73  ? 367 PHE D CD2 1 
ATOM   15333 C CE1 . PHE D 1 367 ? -2.232  25.348  65.011  1.00 73.60  ? 367 PHE D CE1 1 
ATOM   15334 C CE2 . PHE D 1 367 ? -3.052  27.566  65.357  1.00 69.01  ? 367 PHE D CE2 1 
ATOM   15335 C CZ  . PHE D 1 367 ? -3.162  26.208  65.565  1.00 65.71  ? 367 PHE D CZ  1 
ATOM   15336 N N   . LEU D 1 368 ? -1.746  29.011  61.109  1.00 70.81  ? 368 LEU D N   1 
ATOM   15337 C CA  . LEU D 1 368 ? -3.081  29.403  60.671  1.00 74.98  ? 368 LEU D CA  1 
ATOM   15338 C C   . LEU D 1 368 ? -3.380  28.870  59.278  1.00 70.73  ? 368 LEU D C   1 
ATOM   15339 O O   . LEU D 1 368 ? -4.487  28.392  59.012  1.00 77.88  ? 368 LEU D O   1 
ATOM   15340 C CB  . LEU D 1 368 ? -3.224  30.926  60.717  1.00 74.73  ? 368 LEU D CB  1 
ATOM   15341 C CG  . LEU D 1 368 ? -3.600  31.513  62.085  1.00 67.69  ? 368 LEU D CG  1 
ATOM   15342 C CD1 . LEU D 1 368 ? -3.787  33.015  61.998  1.00 63.47  ? 368 LEU D CD1 1 
ATOM   15343 C CD2 . LEU D 1 368 ? -4.855  30.855  62.638  1.00 66.54  ? 368 LEU D CD2 1 
ATOM   15344 N N   . GLU D 1 369 ? -2.398  28.912  58.383  1.00 73.94  ? 369 GLU D N   1 
ATOM   15345 C CA  . GLU D 1 369 ? -2.627  28.392  57.041  1.00 81.24  ? 369 GLU D CA  1 
ATOM   15346 C C   . GLU D 1 369 ? -2.781  26.874  57.052  1.00 80.06  ? 369 GLU D C   1 
ATOM   15347 O O   . GLU D 1 369 ? -3.679  26.336  56.396  1.00 88.13  ? 369 GLU D O   1 
ATOM   15348 C CB  . GLU D 1 369 ? -1.495  28.833  56.120  1.00 74.20  ? 369 GLU D CB  1 
ATOM   15349 C CG  . GLU D 1 369 ? -1.494  30.335  55.896  1.00 75.91  ? 369 GLU D CG  1 
ATOM   15350 C CD  . GLU D 1 369 ? -0.393  30.788  54.976  1.00 83.57  ? 369 GLU D CD  1 
ATOM   15351 O OE1 . GLU D 1 369 ? 0.719   30.231  55.068  1.00 94.80  ? 369 GLU D OE1 1 
ATOM   15352 O OE2 . GLU D 1 369 ? -0.637  31.704  54.163  1.00 93.01  ? 369 GLU D OE2 1 
ATOM   15353 N N   . LYS D 1 370 ? -1.934  26.171  57.807  1.00 76.80  ? 370 LYS D N   1 
ATOM   15354 C CA  . LYS D 1 370 ? -2.075  24.723  57.932  1.00 76.87  ? 370 LYS D CA  1 
ATOM   15355 C C   . LYS D 1 370 ? -3.422  24.360  58.545  1.00 83.17  ? 370 LYS D C   1 
ATOM   15356 O O   . LYS D 1 370 ? -4.109  23.448  58.069  1.00 84.09  ? 370 LYS D O   1 
ATOM   15357 C CB  . LYS D 1 370 ? -0.927  24.160  58.770  1.00 77.46  ? 370 LYS D CB  1 
ATOM   15358 C CG  . LYS D 1 370 ? -0.718  22.651  58.673  1.00 88.48  ? 370 LYS D CG  1 
ATOM   15359 C CD  . LYS D 1 370 ? -1.074  22.074  57.313  1.00 85.95  ? 370 LYS D CD  1 
ATOM   15360 C CE  . LYS D 1 370 ? -0.545  20.651  57.193  1.00 82.38  ? 370 LYS D CE  1 
ATOM   15361 N NZ  . LYS D 1 370 ? -1.133  19.927  56.036  1.00 81.94  ? 370 LYS D NZ  1 
ATOM   15362 N N   . LEU D 1 371 ? -3.815  25.072  59.606  1.00 81.99  ? 371 LEU D N   1 
ATOM   15363 C CA  . LEU D 1 371 ? -5.131  24.874  60.208  1.00 76.40  ? 371 LEU D CA  1 
ATOM   15364 C C   . LEU D 1 371 ? -6.236  25.140  59.188  1.00 75.45  ? 371 LEU D C   1 
ATOM   15365 O O   . LEU D 1 371 ? -7.024  24.247  58.857  1.00 78.79  ? 371 LEU D O   1 
ATOM   15366 C CB  . LEU D 1 371 ? -5.281  25.794  61.430  1.00 76.15  ? 371 LEU D CB  1 
ATOM   15367 C CG  . LEU D 1 371 ? -6.563  25.825  62.284  1.00 73.71  ? 371 LEU D CG  1 
ATOM   15368 C CD1 . LEU D 1 371 ? -7.186  24.433  62.460  1.00 71.07  ? 371 LEU D CD1 1 
ATOM   15369 C CD2 . LEU D 1 371 ? -6.302  26.455  63.649  1.00 72.16  ? 371 LEU D CD2 1 
ATOM   15370 N N   . TYR D 1 372 ? -6.281  26.367  58.650  1.00 77.12  ? 372 TYR D N   1 
ATOM   15371 C CA  . TYR D 1 372 ? -7.386  26.771  57.782  1.00 79.73  ? 372 TYR D CA  1 
ATOM   15372 C C   . TYR D 1 372 ? -7.454  25.937  56.509  1.00 79.36  ? 372 TYR D C   1 
ATOM   15373 O O   . TYR D 1 372 ? -8.553  25.670  56.006  1.00 75.34  ? 372 TYR D O   1 
ATOM   15374 C CB  . TYR D 1 372 ? -7.276  28.256  57.437  1.00 71.72  ? 372 TYR D CB  1 
ATOM   15375 C CG  . TYR D 1 372 ? -7.488  29.175  58.621  1.00 76.61  ? 372 TYR D CG  1 
ATOM   15376 C CD1 . TYR D 1 372 ? -7.970  28.686  59.832  1.00 71.40  ? 372 TYR D CD1 1 
ATOM   15377 C CD2 . TYR D 1 372 ? -7.199  30.530  58.530  1.00 71.25  ? 372 TYR D CD2 1 
ATOM   15378 C CE1 . TYR D 1 372 ? -8.163  29.522  60.915  1.00 66.16  ? 372 TYR D CE1 1 
ATOM   15379 C CE2 . TYR D 1 372 ? -7.386  31.373  59.611  1.00 71.50  ? 372 TYR D CE2 1 
ATOM   15380 C CZ  . TYR D 1 372 ? -7.869  30.865  60.800  1.00 70.38  ? 372 TYR D CZ  1 
ATOM   15381 O OH  . TYR D 1 372 ? -8.056  31.702  61.876  1.00 72.75  ? 372 TYR D OH  1 
ATOM   15382 N N   . SER D 1 373 ? -6.306  25.511  55.974  1.00 72.71  ? 373 SER D N   1 
ATOM   15383 C CA  . SER D 1 373 ? -6.330  24.650  54.791  1.00 80.87  ? 373 SER D CA  1 
ATOM   15384 C C   . SER D 1 373 ? -6.885  23.272  55.123  1.00 88.01  ? 373 SER D C   1 
ATOM   15385 O O   . SER D 1 373 ? -7.674  22.713  54.353  1.00 92.60  ? 373 SER D O   1 
ATOM   15386 C CB  . SER D 1 373 ? -4.931  24.520  54.192  1.00 78.85  ? 373 SER D CB  1 
ATOM   15387 O OG  . SER D 1 373 ? -4.049  23.893  55.107  1.00 83.41  ? 373 SER D OG  1 
ATOM   15388 N N   . THR D 1 374 ? -6.482  22.708  56.264  1.00 79.30  ? 374 THR D N   1 
ATOM   15389 C CA  . THR D 1 374 ? -6.986  21.396  56.661  1.00 82.79  ? 374 THR D CA  1 
ATOM   15390 C C   . THR D 1 374 ? -8.496  21.421  56.863  1.00 84.67  ? 374 THR D C   1 
ATOM   15391 O O   . THR D 1 374 ? -9.186  20.441  56.557  1.00 90.48  ? 374 THR D O   1 
ATOM   15392 C CB  . THR D 1 374 ? -6.282  20.929  57.935  1.00 84.60  ? 374 THR D CB  1 
ATOM   15393 O OG1 . THR D 1 374 ? -4.904  21.318  57.889  1.00 83.54  ? 374 THR D OG1 1 
ATOM   15394 C CG2 . THR D 1 374 ? -6.376  19.415  58.091  1.00 89.52  ? 374 THR D CG2 1 
ATOM   15395 N N   . LEU D 1 375 ? -9.030  22.540  57.362  1.00 79.60  ? 375 LEU D N   1 
ATOM   15396 C CA  . LEU D 1 375 ? -10.457 22.616  57.676  1.00 81.80  ? 375 LEU D CA  1 
ATOM   15397 C C   . LEU D 1 375 ? -11.307 22.596  56.413  1.00 83.20  ? 375 LEU D C   1 
ATOM   15398 O O   . LEU D 1 375 ? -12.416 22.048  56.411  1.00 85.75  ? 375 LEU D O   1 
ATOM   15399 C CB  . LEU D 1 375 ? -10.738 23.869  58.511  1.00 72.51  ? 375 LEU D CB  1 
ATOM   15400 C CG  . LEU D 1 375 ? -10.564 23.801  60.034  1.00 70.88  ? 375 LEU D CG  1 
ATOM   15401 C CD1 . LEU D 1 375 ? -11.828 23.287  60.693  1.00 76.52  ? 375 LEU D CD1 1 
ATOM   15402 C CD2 . LEU D 1 375 ? -9.420  22.877  60.393  1.00 78.77  ? 375 LEU D CD2 1 
ATOM   15403 N N   . GLU D 1 376 ? -10.807 23.200  55.335  1.00 83.43  ? 376 GLU D N   1 
ATOM   15404 C CA  . GLU D 1 376 ? -11.483 23.133  54.042  1.00 87.50  ? 376 GLU D CA  1 
ATOM   15405 C C   . GLU D 1 376 ? -11.648 21.691  53.569  1.00 92.19  ? 376 GLU D C   1 
ATOM   15406 O O   . GLU D 1 376 ? -12.736 21.292  53.134  1.00 89.57  ? 376 GLU D O   1 
ATOM   15407 C CB  . GLU D 1 376 ? -10.694 23.937  53.014  1.00 86.00  ? 376 GLU D CB  1 
ATOM   15408 C CG  . GLU D 1 376 ? -11.177 25.334  52.826  1.00 85.31  ? 376 GLU D CG  1 
ATOM   15409 C CD  . GLU D 1 376 ? -10.244 26.158  51.974  1.00 90.54  ? 376 GLU D CD  1 
ATOM   15410 O OE1 . GLU D 1 376 ? -9.024  25.896  52.008  1.00 90.76  ? 376 GLU D OE1 1 
ATOM   15411 O OE2 . GLU D 1 376 ? -10.731 27.069  51.273  1.00 95.36  ? 376 GLU D OE2 1 
ATOM   15412 N N   . LYS D 1 377 ? -10.559 20.898  53.625  1.00 91.68  ? 377 LYS D N   1 
ATOM   15413 C CA  . LYS D 1 377 ? -10.605 19.515  53.155  1.00 92.75  ? 377 LYS D CA  1 
ATOM   15414 C C   . LYS D 1 377 ? -11.417 18.655  54.124  1.00 92.96  ? 377 LYS D C   1 
ATOM   15415 O O   . LYS D 1 377 ? -12.189 17.798  53.680  1.00 98.82  ? 377 LYS D O   1 
ATOM   15416 C CB  . LYS D 1 377 ? -9.168  18.969  52.894  1.00 93.41  ? 377 LYS D CB  1 
ATOM   15417 C CG  . LYS D 1 377 ? -9.012  17.423  52.780  1.00 98.35  ? 377 LYS D CG  1 
ATOM   15418 C CD  . LYS D 1 377 ? -9.021  16.721  54.145  1.00 107.58 ? 377 LYS D CD  1 
ATOM   15419 C CE  . LYS D 1 377 ? -9.414  15.256  54.031  1.00 106.01 ? 377 LYS D CE  1 
ATOM   15420 N NZ  . LYS D 1 377 ? -9.117  14.471  55.271  1.00 95.30  ? 377 LYS D NZ  1 
ATOM   15421 N N   . GLU D 1 378 ? -11.305 18.886  55.434  1.00 91.42  ? 378 GLU D N   1 
ATOM   15422 C CA  . GLU D 1 378 ? -11.983 18.039  56.420  1.00 95.76  ? 378 GLU D CA  1 
ATOM   15423 C C   . GLU D 1 378 ? -13.479 18.341  56.407  1.00 89.88  ? 378 GLU D C   1 
ATOM   15424 O O   . GLU D 1 378 ? -13.928 19.365  56.935  1.00 88.34  ? 378 GLU D O   1 
ATOM   15425 C CB  . GLU D 1 378 ? -11.383 18.226  57.813  1.00 95.73  ? 378 GLU D CB  1 
ATOM   15426 C CG  . GLU D 1 378 ? -9.958  17.679  57.952  1.00 97.62  ? 378 GLU D CG  1 
ATOM   15427 C CD  . GLU D 1 378 ? -9.915  16.260  58.496  1.00 102.62 ? 378 GLU D CD  1 
ATOM   15428 O OE1 . GLU D 1 378 ? -10.939 15.551  58.397  1.00 107.03 ? 378 GLU D OE1 1 
ATOM   15429 O OE2 . GLU D 1 378 ? -8.857  15.851  59.019  1.00 102.93 ? 378 GLU D OE2 1 
ATOM   15430 N N   . GLU D 1 379 ? -14.243 17.438  55.804  1.00 90.58  ? 379 GLU D N   1 
ATOM   15431 C CA  . GLU D 1 379 ? -15.656 17.652  55.539  1.00 88.78  ? 379 GLU D CA  1 
ATOM   15432 C C   . GLU D 1 379 ? -16.532 17.401  56.754  1.00 91.99  ? 379 GLU D C   1 
ATOM   15433 O O   . GLU D 1 379 ? -17.689 17.833  56.763  1.00 93.54  ? 379 GLU D O   1 
ATOM   15434 C CB  . GLU D 1 379 ? -16.123 16.748  54.392  1.00 93.59  ? 379 GLU D CB  1 
ATOM   15435 C CG  . GLU D 1 379 ? -15.984 15.231  54.626  1.00 97.17  ? 379 GLU D CG  1 
ATOM   15436 C CD  . GLU D 1 379 ? -14.573 14.777  54.987  1.00 107.79 ? 379 GLU D CD  1 
ATOM   15437 O OE1 . GLU D 1 379 ? -13.600 15.374  54.468  1.00 107.34 ? 379 GLU D OE1 1 
ATOM   15438 O OE2 . GLU D 1 379 ? -14.440 13.840  55.805  1.00 109.57 ? 379 GLU D OE2 1 
ATOM   15439 N N   . TRP D 1 380 ? -16.024 16.708  57.771  1.00 92.62  ? 380 TRP D N   1 
ATOM   15440 C CA  . TRP D 1 380 ? -16.824 16.476  58.963  1.00 85.06  ? 380 TRP D CA  1 
ATOM   15441 C C   . TRP D 1 380 ? -16.862 17.687  59.886  1.00 88.73  ? 380 TRP D C   1 
ATOM   15442 O O   . TRP D 1 380 ? -17.644 17.689  60.842  1.00 92.26  ? 380 TRP D O   1 
ATOM   15443 C CB  . TRP D 1 380 ? -16.307 15.245  59.714  1.00 81.89  ? 380 TRP D CB  1 
ATOM   15444 C CG  . TRP D 1 380 ? -14.953 15.424  60.313  1.00 87.50  ? 380 TRP D CG  1 
ATOM   15445 C CD1 . TRP D 1 380 ? -13.752 15.233  59.696  1.00 89.31  ? 380 TRP D CD1 1 
ATOM   15446 C CD2 . TRP D 1 380 ? -14.655 15.823  61.656  1.00 90.89  ? 380 TRP D CD2 1 
ATOM   15447 N NE1 . TRP D 1 380 ? -12.724 15.493  60.570  1.00 92.50  ? 380 TRP D NE1 1 
ATOM   15448 C CE2 . TRP D 1 380 ? -13.252 15.858  61.780  1.00 89.92  ? 380 TRP D CE2 1 
ATOM   15449 C CE3 . TRP D 1 380 ? -15.439 16.157  62.766  1.00 92.55  ? 380 TRP D CE3 1 
ATOM   15450 C CZ2 . TRP D 1 380 ? -12.617 16.211  62.967  1.00 90.60  ? 380 TRP D CZ2 1 
ATOM   15451 C CZ3 . TRP D 1 380 ? -14.805 16.510  63.944  1.00 92.81  ? 380 TRP D CZ3 1 
ATOM   15452 C CH2 . TRP D 1 380 ? -13.410 16.536  64.033  1.00 91.12  ? 380 TRP D CH2 1 
ATOM   15453 N N   . ILE D 1 381 ? -16.051 18.711  59.621  1.00 85.43  ? 381 ILE D N   1 
ATOM   15454 C CA  . ILE D 1 381 ? -16.083 19.970  60.358  1.00 84.91  ? 381 ILE D CA  1 
ATOM   15455 C C   . ILE D 1 381 ? -16.671 21.038  59.449  1.00 86.08  ? 381 ILE D C   1 
ATOM   15456 O O   . ILE D 1 381 ? -16.260 21.172  58.289  1.00 84.03  ? 381 ILE D O   1 
ATOM   15457 C CB  . ILE D 1 381 ? -14.685 20.389  60.850  1.00 78.32  ? 381 ILE D CB  1 
ATOM   15458 C CG1 . ILE D 1 381 ? -13.994 19.238  61.571  1.00 81.43  ? 381 ILE D CG1 1 
ATOM   15459 C CG2 . ILE D 1 381 ? -14.772 21.595  61.773  1.00 76.44  ? 381 ILE D CG2 1 
ATOM   15460 C CD1 . ILE D 1 381 ? -12.490 19.355  61.563  1.00 80.72  ? 381 ILE D CD1 1 
ATOM   15461 N N   . GLU D 1 382 ? -17.627 21.798  59.974  1.00 84.99  ? 382 GLU D N   1 
ATOM   15462 C CA  . GLU D 1 382 ? -18.221 22.925  59.262  1.00 82.70  ? 382 GLU D CA  1 
ATOM   15463 C C   . GLU D 1 382 ? -17.959 24.191  60.067  1.00 80.59  ? 382 GLU D C   1 
ATOM   15464 O O   . GLU D 1 382 ? -18.464 24.337  61.185  1.00 75.81  ? 382 GLU D O   1 
ATOM   15465 C CB  . GLU D 1 382 ? -19.719 22.713  59.044  1.00 88.14  ? 382 GLU D CB  1 
ATOM   15466 C CG  . GLU D 1 382 ? -20.269 23.412  57.811  1.00 90.86  ? 382 GLU D CG  1 
ATOM   15467 C CD  . GLU D 1 382 ? -21.785 23.458  57.795  1.00 89.55  ? 382 GLU D CD  1 
ATOM   15468 O OE1 . GLU D 1 382 ? -22.343 24.575  57.802  1.00 92.77  ? 382 GLU D OE1 1 
ATOM   15469 O OE2 . GLU D 1 382 ? -22.417 22.381  57.770  1.00 90.90  ? 382 GLU D OE2 1 
ATOM   15470 N N   . THR D 1 383 ? -17.158 25.093  59.510  1.00 83.23  ? 383 THR D N   1 
ATOM   15471 C CA  . THR D 1 383 ? -17.001 26.412  60.104  1.00 73.49  ? 383 THR D CA  1 
ATOM   15472 C C   . THR D 1 383 ? -18.257 27.240  59.856  1.00 81.21  ? 383 THR D C   1 
ATOM   15473 O O   . THR D 1 383 ? -18.831 27.223  58.762  1.00 82.85  ? 383 THR D O   1 
ATOM   15474 C CB  . THR D 1 383 ? -15.770 27.104  59.532  1.00 70.77  ? 383 THR D CB  1 
ATOM   15475 O OG1 . THR D 1 383 ? -15.887 27.183  58.108  1.00 73.71  ? 383 THR D OG1 1 
ATOM   15476 C CG2 . THR D 1 383 ? -14.528 26.309  59.881  1.00 76.41  ? 383 THR D CG2 1 
ATOM   15477 N N   . LEU D 1 384 ? -18.694 27.953  60.888  1.00 80.28  ? 384 LEU D N   1 
ATOM   15478 C CA  . LEU D 1 384 ? -19.965 28.656  60.865  1.00 77.89  ? 384 LEU D CA  1 
ATOM   15479 C C   . LEU D 1 384 ? -19.771 30.089  61.342  1.00 79.00  ? 384 LEU D C   1 
ATOM   15480 O O   . LEU D 1 384 ? -18.823 30.402  62.068  1.00 75.80  ? 384 LEU D O   1 
ATOM   15481 C CB  . LEU D 1 384 ? -21.004 27.935  61.745  1.00 78.37  ? 384 LEU D CB  1 
ATOM   15482 C CG  . LEU D 1 384 ? -21.952 26.928  61.081  1.00 79.61  ? 384 LEU D CG  1 
ATOM   15483 C CD1 . LEU D 1 384 ? -21.303 25.568  60.958  1.00 79.07  ? 384 LEU D CD1 1 
ATOM   15484 C CD2 . LEU D 1 384 ? -23.235 26.802  61.877  1.00 70.11  ? 384 LEU D CD2 1 
ATOM   15485 N N   . THR D 1 385 ? -20.677 30.960  60.911  1.00 79.22  ? 385 THR D N   1 
ATOM   15486 C CA  . THR D 1 385 ? -20.749 32.309  61.446  1.00 75.57  ? 385 THR D CA  1 
ATOM   15487 C C   . THR D 1 385 ? -21.610 32.327  62.702  1.00 70.57  ? 385 THR D C   1 
ATOM   15488 O O   . THR D 1 385 ? -22.292 31.354  63.036  1.00 71.35  ? 385 THR D O   1 
ATOM   15489 C CB  . THR D 1 385 ? -21.326 33.290  60.426  1.00 79.58  ? 385 THR D CB  1 
ATOM   15490 O OG1 . THR D 1 385 ? -22.666 32.902  60.094  1.00 77.81  ? 385 THR D OG1 1 
ATOM   15491 C CG2 . THR D 1 385 ? -20.477 33.318  59.170  1.00 74.24  ? 385 THR D CG2 1 
ATOM   15492 N N   . LEU D 1 386 ? -21.574 33.467  63.397  1.00 71.28  ? 386 LEU D N   1 
ATOM   15493 C CA  . LEU D 1 386 ? -22.418 33.648  64.574  1.00 65.14  ? 386 LEU D CA  1 
ATOM   15494 C C   . LEU D 1 386 ? -23.896 33.619  64.198  1.00 69.22  ? 386 LEU D C   1 
ATOM   15495 O O   . LEU D 1 386 ? -24.717 33.044  64.922  1.00 68.63  ? 386 LEU D O   1 
ATOM   15496 C CB  . LEU D 1 386 ? -22.063 34.961  65.277  1.00 71.47  ? 386 LEU D CB  1 
ATOM   15497 C CG  . LEU D 1 386 ? -20.698 35.076  65.968  1.00 58.91  ? 386 LEU D CG  1 
ATOM   15498 C CD1 . LEU D 1 386 ? -20.620 36.334  66.817  1.00 59.91  ? 386 LEU D CD1 1 
ATOM   15499 C CD2 . LEU D 1 386 ? -20.377 33.838  66.795  1.00 57.00  ? 386 LEU D CD2 1 
ATOM   15500 N N   . GLU D 1 387 ? -24.254 34.227  63.061  1.00 77.75  ? 387 GLU D N   1 
ATOM   15501 C CA  . GLU D 1 387 ? -25.635 34.165  62.594  1.00 79.18  ? 387 GLU D CA  1 
ATOM   15502 C C   . GLU D 1 387 ? -26.015 32.756  62.161  1.00 78.95  ? 387 GLU D C   1 
ATOM   15503 O O   . GLU D 1 387 ? -27.175 32.357  62.313  1.00 83.47  ? 387 GLU D O   1 
ATOM   15504 C CB  . GLU D 1 387 ? -25.860 35.153  61.449  1.00 76.36  ? 387 GLU D CB  1 
ATOM   15505 C CG  . GLU D 1 387 ? -25.297 34.698  60.114  1.00 92.81  ? 387 GLU D CG  1 
ATOM   15506 C CD  . GLU D 1 387 ? -25.246 35.806  59.085  1.00 103.90 ? 387 GLU D CD  1 
ATOM   15507 O OE1 . GLU D 1 387 ? -25.924 36.836  59.286  1.00 113.10 ? 387 GLU D OE1 1 
ATOM   15508 O OE2 . GLU D 1 387 ? -24.533 35.646  58.072  1.00 102.10 ? 387 GLU D OE2 1 
ATOM   15509 N N   . GLU D 1 388 ? -25.061 31.990  61.625  1.00 74.32  ? 388 GLU D N   1 
ATOM   15510 C CA  . GLU D 1 388 ? -25.347 30.602  61.284  1.00 77.76  ? 388 GLU D CA  1 
ATOM   15511 C C   . GLU D 1 388 ? -25.577 29.774  62.544  1.00 77.71  ? 388 GLU D C   1 
ATOM   15512 O O   . GLU D 1 388 ? -26.542 29.005  62.621  1.00 78.90  ? 388 GLU D O   1 
ATOM   15513 C CB  . GLU D 1 388 ? -24.211 30.011  60.442  1.00 79.00  ? 388 GLU D CB  1 
ATOM   15514 C CG  . GLU D 1 388 ? -24.288 30.326  58.946  1.00 81.56  ? 388 GLU D CG  1 
ATOM   15515 C CD  . GLU D 1 388 ? -22.970 30.068  58.226  1.00 83.70  ? 388 GLU D CD  1 
ATOM   15516 O OE1 . GLU D 1 388 ? -22.521 28.902  58.209  1.00 82.75  ? 388 GLU D OE1 1 
ATOM   15517 O OE2 . GLU D 1 388 ? -22.380 31.029  57.684  1.00 82.15  ? 388 GLU D OE2 1 
ATOM   15518 N N   . ALA D 1 389 ? -24.713 29.937  63.555  1.00 76.60  ? 389 ALA D N   1 
ATOM   15519 C CA  . ALA D 1 389 ? -24.858 29.164  64.787  1.00 71.94  ? 389 ALA D CA  1 
ATOM   15520 C C   . ALA D 1 389 ? -26.205 29.420  65.449  1.00 76.77  ? 389 ALA D C   1 
ATOM   15521 O O   . ALA D 1 389 ? -26.771 28.528  66.092  1.00 84.14  ? 389 ALA D O   1 
ATOM   15522 C CB  . ALA D 1 389 ? -23.724 29.486  65.758  1.00 64.96  ? 389 ALA D CB  1 
ATOM   15523 N N   . MET D 1 390 ? -26.737 30.633  65.300  1.00 77.76  ? 390 MET D N   1 
ATOM   15524 C CA  . MET D 1 390 ? -28.049 30.933  65.861  1.00 73.99  ? 390 MET D CA  1 
ATOM   15525 C C   . MET D 1 390 ? -29.153 30.250  65.065  1.00 68.19  ? 390 MET D C   1 
ATOM   15526 O O   . MET D 1 390 ? -29.990 29.542  65.633  1.00 72.22  ? 390 MET D O   1 
ATOM   15527 C CB  . MET D 1 390 ? -28.266 32.443  65.907  1.00 77.32  ? 390 MET D CB  1 
ATOM   15528 C CG  . MET D 1 390 ? -27.551 33.123  67.064  1.00 78.83  ? 390 MET D CG  1 
ATOM   15529 S SD  . MET D 1 390 ? -28.323 32.755  68.645  1.00 83.74  ? 390 MET D SD  1 
ATOM   15530 C CE  . MET D 1 390 ? -29.682 33.928  68.622  1.00 83.40  ? 390 MET D CE  1 
ATOM   15531 N N   . ARG D 1 391 ? -29.149 30.425  63.741  1.00 74.30  ? 391 ARG D N   1 
ATOM   15532 C CA  . ARG D 1 391 ? -30.229 29.920  62.901  1.00 76.86  ? 391 ARG D CA  1 
ATOM   15533 C C   . ARG D 1 391 ? -30.224 28.402  62.760  1.00 75.16  ? 391 ARG D C   1 
ATOM   15534 O O   . ARG D 1 391 ? -31.237 27.836  62.335  1.00 75.73  ? 391 ARG D O   1 
ATOM   15535 C CB  . ARG D 1 391 ? -30.150 30.554  61.515  1.00 79.63  ? 391 ARG D CB  1 
ATOM   15536 C CG  . ARG D 1 391 ? -30.398 32.047  61.498  1.00 85.16  ? 391 ARG D CG  1 
ATOM   15537 C CD  . ARG D 1 391 ? -29.944 32.643  60.178  1.00 82.07  ? 391 ARG D CD  1 
ATOM   15538 N NE  . ARG D 1 391 ? -30.522 33.959  59.943  1.00 84.07  ? 391 ARG D NE  1 
ATOM   15539 C CZ  . ARG D 1 391 ? -30.175 34.759  58.945  1.00 92.38  ? 391 ARG D CZ  1 
ATOM   15540 N NH1 . ARG D 1 391 ? -29.250 34.407  58.068  1.00 93.47  ? 391 ARG D NH1 1 
ATOM   15541 N NH2 . ARG D 1 391 ? -30.776 35.939  58.820  1.00 96.07  ? 391 ARG D NH2 1 
ATOM   15542 N N   . LYS D 1 392 ? -29.121 27.731  63.089  1.00 79.28  ? 392 LYS D N   1 
ATOM   15543 C CA  . LYS D 1 392 ? -29.035 26.288  62.883  1.00 84.46  ? 392 LYS D CA  1 
ATOM   15544 C C   . LYS D 1 392 ? -29.898 25.553  63.899  1.00 81.08  ? 392 LYS D C   1 
ATOM   15545 O O   . LYS D 1 392 ? -29.720 25.710  65.112  1.00 73.36  ? 392 LYS D O   1 
ATOM   15546 C CB  . LYS D 1 392 ? -27.587 25.814  62.970  1.00 76.00  ? 392 LYS D CB  1 
ATOM   15547 C CG  . LYS D 1 392 ? -26.785 26.059  61.712  1.00 67.92  ? 392 LYS D CG  1 
ATOM   15548 C CD  . LYS D 1 392 ? -26.368 24.772  61.037  1.00 73.35  ? 392 LYS D CD  1 
ATOM   15549 C CE  . LYS D 1 392 ? -25.703 25.071  59.711  1.00 77.03  ? 392 LYS D CE  1 
ATOM   15550 N NZ  . LYS D 1 392 ? -24.904 23.922  59.231  1.00 79.91  ? 392 LYS D NZ  1 
ATOM   15551 N N   . GLU D 1 393 ? -30.818 24.731  63.395  1.00 88.65  ? 393 GLU D N   1 
ATOM   15552 C CA  . GLU D 1 393 ? -31.779 24.021  64.225  1.00 91.80  ? 393 GLU D CA  1 
ATOM   15553 C C   . GLU D 1 393 ? -31.289 22.645  64.659  1.00 92.84  ? 393 GLU D C   1 
ATOM   15554 O O   . GLU D 1 393 ? -31.759 22.131  65.680  1.00 101.83 ? 393 GLU D O   1 
ATOM   15555 C CB  . GLU D 1 393 ? -33.117 23.901  63.473  1.00 93.13  ? 393 GLU D CB  1 
ATOM   15556 C CG  . GLU D 1 393 ? -34.243 23.180  64.225  1.00 102.80 ? 393 GLU D CG  1 
ATOM   15557 C CD  . GLU D 1 393 ? -34.987 24.075  65.209  1.00 109.97 ? 393 GLU D CD  1 
ATOM   15558 O OE1 . GLU D 1 393 ? -35.912 24.803  64.788  1.00 107.83 ? 393 GLU D OE1 1 
ATOM   15559 O OE2 . GLU D 1 393 ? -34.653 24.040  66.412  1.00 113.30 ? 393 GLU D OE2 1 
ATOM   15560 N N   . ASP D 1 394 ? -30.337 22.049  63.941  1.00 86.56  ? 394 ASP D N   1 
ATOM   15561 C CA  . ASP D 1 394 ? -29.891 20.699  64.264  1.00 80.53  ? 394 ASP D CA  1 
ATOM   15562 C C   . ASP D 1 394 ? -29.013 20.633  65.513  1.00 83.10  ? 394 ASP D C   1 
ATOM   15563 O O   . ASP D 1 394 ? -28.524 19.548  65.842  1.00 84.55  ? 394 ASP D O   1 
ATOM   15564 C CB  . ASP D 1 394 ? -29.141 20.086  63.074  1.00 91.63  ? 394 ASP D CB  1 
ATOM   15565 C CG  . ASP D 1 394 ? -28.459 21.131  62.203  1.00 96.67  ? 394 ASP D CG  1 
ATOM   15566 O OD1 . ASP D 1 394 ? -28.126 22.216  62.724  1.00 97.20  ? 394 ASP D OD1 1 
ATOM   15567 O OD2 . ASP D 1 394 ? -28.240 20.863  61.001  1.00 91.68  ? 394 ASP D OD2 1 
ATOM   15568 N N   . VAL D 1 395 ? -28.811 21.744  66.224  1.00 84.18  ? 395 VAL D N   1 
ATOM   15569 C CA  . VAL D 1 395 ? -27.994 21.736  67.433  1.00 83.49  ? 395 VAL D CA  1 
ATOM   15570 C C   . VAL D 1 395 ? -28.869 21.425  68.639  1.00 80.34  ? 395 VAL D C   1 
ATOM   15571 O O   . VAL D 1 395 ? -30.078 21.681  68.644  1.00 76.68  ? 395 VAL D O   1 
ATOM   15572 C CB  . VAL D 1 395 ? -27.261 23.078  67.619  1.00 76.17  ? 395 VAL D CB  1 
ATOM   15573 C CG1 . VAL D 1 395 ? -26.202 23.249  66.551  1.00 79.76  ? 395 VAL D CG1 1 
ATOM   15574 C CG2 . VAL D 1 395 ? -28.253 24.224  67.602  1.00 78.81  ? 395 VAL D CG2 1 
ATOM   15575 N N   . LYS D 1 396 ? -28.247 20.873  69.677  1.00 79.10  ? 396 LYS D N   1 
ATOM   15576 C CA  . LYS D 1 396 ? -28.950 20.636  70.928  1.00 78.63  ? 396 LYS D CA  1 
ATOM   15577 C C   . LYS D 1 396 ? -29.121 21.943  71.695  1.00 80.20  ? 396 LYS D C   1 
ATOM   15578 O O   . LYS D 1 396 ? -28.362 22.902  71.522  1.00 75.97  ? 396 LYS D O   1 
ATOM   15579 C CB  . LYS D 1 396 ? -28.200 19.616  71.787  1.00 70.97  ? 396 LYS D CB  1 
ATOM   15580 C CG  . LYS D 1 396 ? -29.105 18.750  72.645  1.00 75.03  ? 396 LYS D CG  1 
ATOM   15581 C CD  . LYS D 1 396 ? -28.338 18.053  73.758  1.00 79.16  ? 396 LYS D CD  1 
ATOM   15582 C CE  . LYS D 1 396 ? -29.197 17.901  75.009  1.00 84.57  ? 396 LYS D CE  1 
ATOM   15583 N NZ  . LYS D 1 396 ? -28.980 16.595  75.698  1.00 84.60  ? 396 LYS D NZ  1 
ATOM   15584 N N   . THR D 1 397 ? -30.132 21.971  72.561  1.00 81.03  ? 397 THR D N   1 
ATOM   15585 C CA  . THR D 1 397 ? -30.457 23.178  73.301  1.00 80.93  ? 397 THR D CA  1 
ATOM   15586 C C   . THR D 1 397 ? -30.820 22.840  74.740  1.00 81.50  ? 397 THR D C   1 
ATOM   15587 O O   . THR D 1 397 ? -31.233 21.720  75.051  1.00 83.27  ? 397 THR D O   1 
ATOM   15588 C CB  . THR D 1 397 ? -31.609 23.942  72.642  1.00 73.73  ? 397 THR D CB  1 
ATOM   15589 O OG1 . THR D 1 397 ? -32.381 24.597  73.654  1.00 83.14  ? 397 THR D OG1 1 
ATOM   15590 C CG2 . THR D 1 397 ? -32.503 22.985  71.869  1.00 78.78  ? 397 THR D CG2 1 
ATOM   15591 N N   . GLU D 1 398 ? -30.655 23.832  75.616  1.00 79.54  ? 398 GLU D N   1 
ATOM   15592 C CA  . GLU D 1 398 ? -31.046 23.728  77.014  1.00 77.87  ? 398 GLU D CA  1 
ATOM   15593 C C   . GLU D 1 398 ? -31.377 25.117  77.540  1.00 75.94  ? 398 GLU D C   1 
ATOM   15594 O O   . GLU D 1 398 ? -30.788 26.114  77.112  1.00 73.01  ? 398 GLU D O   1 
ATOM   15595 C CB  . GLU D 1 398 ? -29.942 23.089  77.866  1.00 75.03  ? 398 GLU D CB  1 
ATOM   15596 C CG  . GLU D 1 398 ? -30.458 22.320  79.070  1.00 79.02  ? 398 GLU D CG  1 
ATOM   15597 C CD  . GLU D 1 398 ? -31.143 21.024  78.683  1.00 94.78  ? 398 GLU D CD  1 
ATOM   15598 O OE1 . GLU D 1 398 ? -32.369 20.912  78.895  1.00 100.69 ? 398 GLU D OE1 1 
ATOM   15599 O OE2 . GLU D 1 398 ? -30.453 20.117  78.169  1.00 100.08 ? 398 GLU D OE2 1 
ATOM   15600 N N   . VAL D 1 399 ? -32.322 25.175  78.476  1.00 75.00  ? 399 VAL D N   1 
ATOM   15601 C CA  . VAL D 1 399 ? -32.705 26.420  79.134  1.00 69.88  ? 399 VAL D CA  1 
ATOM   15602 C C   . VAL D 1 399 ? -32.089 26.446  80.527  1.00 72.22  ? 399 VAL D C   1 
ATOM   15603 O O   . VAL D 1 399 ? -32.259 25.500  81.310  1.00 75.38  ? 399 VAL D O   1 
ATOM   15604 C CB  . VAL D 1 399 ? -34.234 26.571  79.208  1.00 69.02  ? 399 VAL D CB  1 
ATOM   15605 C CG1 . VAL D 1 399 ? -34.600 27.717  80.143  1.00 73.30  ? 399 VAL D CG1 1 
ATOM   15606 C CG2 . VAL D 1 399 ? -34.828 26.791  77.815  1.00 76.67  ? 399 VAL D CG2 1 
ATOM   15607 N N   . ILE D 1 400 ? -31.366 27.522  80.832  1.00 66.75  ? 400 ILE D N   1 
ATOM   15608 C CA  . ILE D 1 400 ? -30.774 27.745  82.147  1.00 71.73  ? 400 ILE D CA  1 
ATOM   15609 C C   . ILE D 1 400 ? -31.300 29.065  82.695  1.00 71.78  ? 400 ILE D C   1 
ATOM   15610 O O   . ILE D 1 400 ? -31.609 29.994  81.941  1.00 73.20  ? 400 ILE D O   1 
ATOM   15611 C CB  . ILE D 1 400 ? -29.228 27.737  82.098  1.00 69.53  ? 400 ILE D CB  1 
ATOM   15612 C CG1 . ILE D 1 400 ? -28.677 29.062  81.583  1.00 60.00  ? 400 ILE D CG1 1 
ATOM   15613 C CG2 . ILE D 1 400 ? -28.722 26.613  81.228  1.00 78.23  ? 400 ILE D CG2 1 
ATOM   15614 C CD1 . ILE D 1 400 ? -27.313 29.358  82.128  1.00 63.29  ? 400 ILE D CD1 1 
ATOM   15615 N N   . GLU D 1 401 ? -31.413 29.142  84.020  1.00 62.03  ? 401 GLU D N   1 
ATOM   15616 C CA  . GLU D 1 401 ? -32.054 30.285  84.649  1.00 63.96  ? 401 GLU D CA  1 
ATOM   15617 C C   . GLU D 1 401 ? -31.145 31.096  85.559  1.00 66.39  ? 401 GLU D C   1 
ATOM   15618 O O   . GLU D 1 401 ? -31.592 32.128  86.073  1.00 68.29  ? 401 GLU D O   1 
ATOM   15619 C CB  . GLU D 1 401 ? -33.287 29.836  85.449  1.00 77.09  ? 401 GLU D CB  1 
ATOM   15620 C CG  . GLU D 1 401 ? -34.434 29.329  84.579  1.00 77.97  ? 401 GLU D CG  1 
ATOM   15621 C CD  . GLU D 1 401 ? -35.617 30.281  84.549  1.00 80.25  ? 401 GLU D CD  1 
ATOM   15622 O OE1 . GLU D 1 401 ? -36.422 30.182  83.600  1.00 79.58  ? 401 GLU D OE1 1 
ATOM   15623 O OE2 . GLU D 1 401 ? -35.744 31.126  85.467  1.00 78.87  ? 401 GLU D OE2 1 
ATOM   15624 N N   . SER D 1 402 ? -29.899 30.672  85.778  1.00 69.50  ? 402 SER D N   1 
ATOM   15625 C CA  . SER D 1 402 ? -28.962 31.448  86.582  1.00 64.98  ? 402 SER D CA  1 
ATOM   15626 C C   . SER D 1 402 ? -27.533 31.069  86.222  1.00 64.94  ? 402 SER D C   1 
ATOM   15627 O O   . SER D 1 402 ? -27.251 29.927  85.846  1.00 65.02  ? 402 SER D O   1 
ATOM   15628 C CB  . SER D 1 402 ? -29.176 31.239  88.086  1.00 62.81  ? 402 SER D CB  1 
ATOM   15629 O OG  . SER D 1 402 ? -28.239 30.310  88.609  1.00 69.11  ? 402 SER D OG  1 
ATOM   15630 N N   . VAL D 1 403 ? -26.630 32.039  86.361  1.00 55.80  ? 403 VAL D N   1 
ATOM   15631 C CA  . VAL D 1 403 ? -25.204 31.814  86.178  1.00 59.35  ? 403 VAL D CA  1 
ATOM   15632 C C   . VAL D 1 403 ? -24.479 32.237  87.446  1.00 60.63  ? 403 VAL D C   1 
ATOM   15633 O O   . VAL D 1 403 ? -24.980 33.034  88.243  1.00 62.97  ? 403 VAL D O   1 
ATOM   15634 C CB  . VAL D 1 403 ? -24.633 32.573  84.964  1.00 58.95  ? 403 VAL D CB  1 
ATOM   15635 C CG1 . VAL D 1 403 ? -25.087 31.919  83.679  1.00 55.24  ? 403 VAL D CG1 1 
ATOM   15636 C CG2 . VAL D 1 403 ? -25.036 34.042  85.018  1.00 57.07  ? 403 VAL D CG2 1 
ATOM   15637 N N   . LYS D 1 404 ? -23.281 31.688  87.626  1.00 61.46  ? 404 LYS D N   1 
ATOM   15638 C CA  . LYS D 1 404 ? -22.367 32.142  88.667  1.00 61.45  ? 404 LYS D CA  1 
ATOM   15639 C C   . LYS D 1 404 ? -21.449 33.194  88.064  1.00 64.24  ? 404 LYS D C   1 
ATOM   15640 O O   . LYS D 1 404 ? -20.761 32.925  87.072  1.00 64.64  ? 404 LYS D O   1 
ATOM   15641 C CB  . LYS D 1 404 ? -21.543 30.988  89.230  1.00 62.53  ? 404 LYS D CB  1 
ATOM   15642 C CG  . LYS D 1 404 ? -22.288 30.115  90.224  1.00 72.85  ? 404 LYS D CG  1 
ATOM   15643 C CD  . LYS D 1 404 ? -22.644 30.872  91.497  1.00 74.45  ? 404 LYS D CD  1 
ATOM   15644 C CE  . LYS D 1 404 ? -23.863 30.260  92.175  1.00 75.91  ? 404 LYS D CE  1 
ATOM   15645 N NZ  . LYS D 1 404 ? -25.122 30.983  91.847  1.00 75.85  ? 404 LYS D NZ  1 
ATOM   15646 N N   . ALA D 1 405 ? -21.444 34.384  88.654  1.00 55.59  ? 405 ALA D N   1 
ATOM   15647 C CA  . ALA D 1 405 ? -20.703 35.495  88.074  1.00 59.92  ? 405 ALA D CA  1 
ATOM   15648 C C   . ALA D 1 405 ? -19.211 35.184  88.045  1.00 63.80  ? 405 ALA D C   1 
ATOM   15649 O O   . ALA D 1 405 ? -18.616 34.847  89.073  1.00 73.51  ? 405 ALA D O   1 
ATOM   15650 C CB  . ALA D 1 405 ? -20.979 36.774  88.861  1.00 55.15  ? 405 ALA D CB  1 
ATOM   15651 N N   . GLY D 1 406 ? -18.609 35.281  86.863  1.00 53.43  ? 406 GLY D N   1 
ATOM   15652 C CA  . GLY D 1 406 ? -17.187 35.018  86.748  1.00 58.22  ? 406 GLY D CA  1 
ATOM   15653 C C   . GLY D 1 406 ? -16.605 35.545  85.454  1.00 52.31  ? 406 GLY D C   1 
ATOM   15654 O O   . GLY D 1 406 ? -17.268 36.235  84.679  1.00 55.16  ? 406 GLY D O   1 
ATOM   15655 N N   . THR D 1 407 ? -15.335 35.214  85.236  1.00 54.59  ? 407 THR D N   1 
ATOM   15656 C CA  . THR D 1 407 ? -14.578 35.606  84.054  1.00 56.21  ? 407 THR D CA  1 
ATOM   15657 C C   . THR D 1 407 ? -13.828 34.388  83.525  1.00 57.88  ? 407 THR D C   1 
ATOM   15658 O O   . THR D 1 407 ? -13.862 33.307  84.118  1.00 60.61  ? 407 THR D O   1 
ATOM   15659 C CB  . THR D 1 407 ? -13.584 36.734  84.364  1.00 51.44  ? 407 THR D CB  1 
ATOM   15660 O OG1 . THR D 1 407 ? -12.533 36.217  85.192  1.00 56.89  ? 407 THR D OG1 1 
ATOM   15661 C CG2 . THR D 1 407 ? -14.263 37.885  85.075  1.00 57.07  ? 407 THR D CG2 1 
ATOM   15662 N N   . TRP D 1 408 ? -13.130 34.562  82.403  1.00 55.56  ? 408 TRP D N   1 
ATOM   15663 C CA  . TRP D 1 408 ? -12.299 33.477  81.898  1.00 55.57  ? 408 TRP D CA  1 
ATOM   15664 C C   . TRP D 1 408 ? -10.965 33.362  82.627  1.00 53.79  ? 408 TRP D C   1 
ATOM   15665 O O   . TRP D 1 408 ? -10.147 32.514  82.250  1.00 63.46  ? 408 TRP D O   1 
ATOM   15666 C CB  . TRP D 1 408 ? -12.053 33.618  80.388  1.00 57.35  ? 408 TRP D CB  1 
ATOM   15667 C CG  . TRP D 1 408 ? -11.439 34.906  79.925  1.00 50.30  ? 408 TRP D CG  1 
ATOM   15668 C CD1 . TRP D 1 408 ? -10.957 35.925  80.697  1.00 57.45  ? 408 TRP D CD1 1 
ATOM   15669 C CD2 . TRP D 1 408 ? -11.248 35.308  78.568  1.00 49.60  ? 408 TRP D CD2 1 
ATOM   15670 N NE1 . TRP D 1 408 ? -10.477 36.936  79.900  1.00 55.00  ? 408 TRP D NE1 1 
ATOM   15671 C CE2 . TRP D 1 408 ? -10.646 36.580  78.587  1.00 53.92  ? 408 TRP D CE2 1 
ATOM   15672 C CE3 . TRP D 1 408 ? -11.529 34.714  77.334  1.00 51.04  ? 408 TRP D CE3 1 
ATOM   15673 C CZ2 . TRP D 1 408 ? -10.322 37.269  77.420  1.00 56.88  ? 408 TRP D CZ2 1 
ATOM   15674 C CZ3 . TRP D 1 408 ? -11.207 35.398  76.178  1.00 48.75  ? 408 TRP D CZ3 1 
ATOM   15675 C CH2 . TRP D 1 408 ? -10.611 36.660  76.228  1.00 50.07  ? 408 TRP D CH2 1 
ATOM   15676 N N   . PHE D 1 409 ? -10.730 34.169  83.663  1.00 50.20  ? 409 PHE D N   1 
ATOM   15677 C CA  . PHE D 1 409 ? -9.528  34.042  84.488  1.00 61.77  ? 409 PHE D CA  1 
ATOM   15678 C C   . PHE D 1 409 ? -9.913  33.341  85.792  1.00 59.06  ? 409 PHE D C   1 
ATOM   15679 O O   . PHE D 1 409 ? -10.176 33.973  86.815  1.00 59.15  ? 409 PHE D O   1 
ATOM   15680 C CB  . PHE D 1 409 ? -8.907  35.415  84.736  1.00 64.86  ? 409 PHE D CB  1 
ATOM   15681 C CG  . PHE D 1 409 ? -7.461  35.372  85.156  1.00 67.24  ? 409 PHE D CG  1 
ATOM   15682 C CD1 . PHE D 1 409 ? -7.093  34.904  86.411  1.00 79.48  ? 409 PHE D CD1 1 
ATOM   15683 C CD2 . PHE D 1 409 ? -6.469  35.815  84.296  1.00 73.88  ? 409 PHE D CD2 1 
ATOM   15684 C CE1 . PHE D 1 409 ? -5.758  34.875  86.796  1.00 83.35  ? 409 PHE D CE1 1 
ATOM   15685 C CE2 . PHE D 1 409 ? -5.137  35.789  84.672  1.00 74.69  ? 409 PHE D CE2 1 
ATOM   15686 C CZ  . PHE D 1 409 ? -4.779  35.320  85.920  1.00 81.68  ? 409 PHE D CZ  1 
ATOM   15687 N N   . ASP D 1 410 ? -9.943  32.005  85.740  1.00 56.31  ? 410 ASP D N   1 
ATOM   15688 C CA  . ASP D 1 410 ? -10.256 31.127  86.868  1.00 62.10  ? 410 ASP D CA  1 
ATOM   15689 C C   . ASP D 1 410 ? -11.671 31.320  87.408  1.00 66.97  ? 410 ASP D C   1 
ATOM   15690 O O   . ASP D 1 410 ? -11.947 30.958  88.560  1.00 68.82  ? 410 ASP D O   1 
ATOM   15691 C CB  . ASP D 1 410 ? -9.246  31.290  88.013  1.00 67.79  ? 410 ASP D CB  1 
ATOM   15692 C CG  . ASP D 1 410 ? -7.818  31.015  87.579  1.00 83.23  ? 410 ASP D CG  1 
ATOM   15693 O OD1 . ASP D 1 410 ? -7.532  29.885  87.123  1.00 79.49  ? 410 ASP D OD1 1 
ATOM   15694 O OD2 . ASP D 1 410 ? -6.979  31.933  87.703  1.00 83.74  ? 410 ASP D OD2 1 
ATOM   15695 N N   . GLY D 1 411 ? -12.582 31.879  86.612  1.00 52.80  ? 411 GLY D N   1 
ATOM   15696 C CA  . GLY D 1 411 ? -13.933 32.096  87.090  1.00 56.20  ? 411 GLY D CA  1 
ATOM   15697 C C   . GLY D 1 411 ? -14.098 33.204  88.106  1.00 54.05  ? 411 GLY D C   1 
ATOM   15698 O O   . GLY D 1 411 ? -15.202 33.378  88.630  1.00 47.56  ? 411 GLY D O   1 
ATOM   15699 N N   . ASN D 1 412 ? -13.045 33.966  88.396  1.00 54.40  ? 412 ASN D N   1 
ATOM   15700 C CA  . ASN D 1 412 ? -13.085 35.022  89.395  1.00 50.36  ? 412 ASN D CA  1 
ATOM   15701 C C   . ASN D 1 412 ? -12.778 36.377  88.762  1.00 45.62  ? 412 ASN D C   1 
ATOM   15702 O O   . ASN D 1 412 ? -12.343 36.465  87.612  1.00 50.97  ? 412 ASN D O   1 
ATOM   15703 C CB  . ASN D 1 412 ? -12.109 34.713  90.545  1.00 45.83  ? 412 ASN D CB  1 
ATOM   15704 C CG  . ASN D 1 412 ? -10.667 34.606  90.088  1.00 52.23  ? 412 ASN D CG  1 
ATOM   15705 O OD1 . ASN D 1 412 ? -10.085 35.559  89.558  1.00 56.46  ? 412 ASN D OD1 1 
ATOM   15706 N ND2 . ASN D 1 412 ? -10.086 33.428  90.273  1.00 60.52  ? 412 ASN D ND2 1 
ATOM   15707 N N   . PHE D 1 413 ? -13.043 37.441  89.518  1.00 49.17  ? 413 PHE D N   1 
ATOM   15708 C CA  . PHE D 1 413 ? -12.666 38.798  89.141  1.00 50.21  ? 413 PHE D CA  1 
ATOM   15709 C C   . PHE D 1 413 ? -11.382 39.246  89.833  1.00 50.88  ? 413 PHE D C   1 
ATOM   15710 O O   . PHE D 1 413 ? -11.069 40.440  89.826  1.00 54.62  ? 413 PHE D O   1 
ATOM   15711 C CB  . PHE D 1 413 ? -13.800 39.786  89.465  1.00 50.95  ? 413 PHE D CB  1 
ATOM   15712 C CG  . PHE D 1 413 ? -15.150 39.387  88.913  1.00 56.94  ? 413 PHE D CG  1 
ATOM   15713 C CD1 . PHE D 1 413 ? -15.990 38.551  89.633  1.00 57.72  ? 413 PHE D CD1 1 
ATOM   15714 C CD2 . PHE D 1 413 ? -15.579 39.852  87.673  1.00 46.04  ? 413 PHE D CD2 1 
ATOM   15715 C CE1 . PHE D 1 413 ? -17.228 38.180  89.127  1.00 63.32  ? 413 PHE D CE1 1 
ATOM   15716 C CE2 . PHE D 1 413 ? -16.806 39.486  87.165  1.00 52.73  ? 413 PHE D CE2 1 
ATOM   15717 C CZ  . PHE D 1 413 ? -17.636 38.649  87.891  1.00 64.36  ? 413 PHE D CZ  1 
ATOM   15718 N N   . LEU D 1 414 ? -10.625 38.308  90.413  1.00 46.64  ? 414 LEU D N   1 
ATOM   15719 C CA  . LEU D 1 414 ? -9.499  38.678  91.264  1.00 51.37  ? 414 LEU D CA  1 
ATOM   15720 C C   . LEU D 1 414 ? -8.392  39.358  90.477  1.00 47.95  ? 414 LEU D C   1 
ATOM   15721 O O   . LEU D 1 414 ? -7.601  40.114  91.051  1.00 56.19  ? 414 LEU D O   1 
ATOM   15722 C CB  . LEU D 1 414 ? -8.950  37.448  91.983  1.00 46.14  ? 414 LEU D CB  1 
ATOM   15723 C CG  . LEU D 1 414 ? -9.768  36.988  93.184  1.00 47.51  ? 414 LEU D CG  1 
ATOM   15724 C CD1 . LEU D 1 414 ? -9.272  35.640  93.674  1.00 49.28  ? 414 LEU D CD1 1 
ATOM   15725 C CD2 . LEU D 1 414 ? -9.716  38.031  94.289  1.00 47.87  ? 414 LEU D CD2 1 
ATOM   15726 N N   . LYS D 1 415 ? -8.313  39.101  89.174  1.00 51.22  ? 415 LYS D N   1 
ATOM   15727 C CA  . LYS D 1 415 ? -7.284  39.736  88.362  1.00 57.67  ? 415 LYS D CA  1 
ATOM   15728 C C   . LYS D 1 415 ? -7.465  41.249  88.300  1.00 54.11  ? 415 LYS D C   1 
ATOM   15729 O O   . LYS D 1 415 ? -6.495  41.973  88.042  1.00 53.39  ? 415 LYS D O   1 
ATOM   15730 C CB  . LYS D 1 415 ? -7.285  39.114  86.960  1.00 59.49  ? 415 LYS D CB  1 
ATOM   15731 C CG  . LYS D 1 415 ? -6.294  39.723  86.000  1.00 64.80  ? 415 LYS D CG  1 
ATOM   15732 C CD  . LYS D 1 415 ? -4.904  39.148  86.211  1.00 68.62  ? 415 LYS D CD  1 
ATOM   15733 C CE  . LYS D 1 415 ? -3.970  39.570  85.101  1.00 67.78  ? 415 LYS D CE  1 
ATOM   15734 N NZ  . LYS D 1 415 ? -2.603  39.889  85.582  1.00 74.29  ? 415 LYS D NZ  1 
ATOM   15735 N N   . TRP D 1 416 ? -8.665  41.747  88.602  1.00 51.67  ? 416 TRP D N   1 
ATOM   15736 C CA  . TRP D 1 416 ? -8.958  43.171  88.544  1.00 50.39  ? 416 TRP D CA  1 
ATOM   15737 C C   . TRP D 1 416 ? -9.372  43.766  89.886  1.00 50.00  ? 416 TRP D C   1 
ATOM   15738 O O   . TRP D 1 416 ? -9.635  44.973  89.950  1.00 51.39  ? 416 TRP D O   1 
ATOM   15739 C CB  . TRP D 1 416 ? -10.056 43.434  87.500  1.00 49.32  ? 416 TRP D CB  1 
ATOM   15740 C CG  . TRP D 1 416 ? -9.804  42.757  86.175  1.00 55.80  ? 416 TRP D CG  1 
ATOM   15741 C CD1 . TRP D 1 416 ? -9.253  43.318  85.060  1.00 49.94  ? 416 TRP D CD1 1 
ATOM   15742 C CD2 . TRP D 1 416 ? -10.082 41.387  85.839  1.00 61.70  ? 416 TRP D CD2 1 
ATOM   15743 N NE1 . TRP D 1 416 ? -9.177  42.387  84.049  1.00 49.04  ? 416 TRP D NE1 1 
ATOM   15744 C CE2 . TRP D 1 416 ? -9.678  41.195  84.501  1.00 51.43  ? 416 TRP D CE2 1 
ATOM   15745 C CE3 . TRP D 1 416 ? -10.634 40.306  86.538  1.00 54.39  ? 416 TRP D CE3 1 
ATOM   15746 C CZ2 . TRP D 1 416 ? -9.810  39.970  83.849  1.00 52.98  ? 416 TRP D CZ2 1 
ATOM   15747 C CZ3 . TRP D 1 416 ? -10.762 39.089  85.889  1.00 54.57  ? 416 TRP D CZ3 1 
ATOM   15748 C CH2 . TRP D 1 416 ? -10.352 38.932  84.558  1.00 59.86  ? 416 TRP D CH2 1 
ATOM   15749 N N   . ILE D 1 417 ? -9.422  42.970  90.956  1.00 51.70  ? 417 ILE D N   1 
ATOM   15750 C CA  . ILE D 1 417 ? -9.896  43.442  92.257  1.00 54.56  ? 417 ILE D CA  1 
ATOM   15751 C C   . ILE D 1 417 ? -9.510  42.418  93.322  1.00 49.57  ? 417 ILE D C   1 
ATOM   15752 O O   . ILE D 1 417 ? -9.217  41.263  93.015  1.00 48.60  ? 417 ILE D O   1 
ATOM   15753 C CB  . ILE D 1 417 ? -11.427 43.688  92.225  1.00 48.02  ? 417 ILE D CB  1 
ATOM   15754 C CG1 . ILE D 1 417 ? -11.820 44.791  93.202  1.00 46.03  ? 417 ILE D CG1 1 
ATOM   15755 C CG2 . ILE D 1 417 ? -12.193 42.411  92.523  1.00 48.98  ? 417 ILE D CG2 1 
ATOM   15756 C CD1 . ILE D 1 417 ? -13.203 45.329  92.956  1.00 50.58  ? 417 ILE D CD1 1 
ATOM   15757 N N   . GLY D 1 418 ? -9.492  42.849  94.589  1.00 48.27  ? 418 GLY D N   1 
ATOM   15758 C CA  . GLY D 1 418 ? -9.322  41.961  95.726  1.00 56.56  ? 418 GLY D CA  1 
ATOM   15759 C C   . GLY D 1 418 ? -8.042  42.172  96.522  1.00 67.47  ? 418 GLY D C   1 
ATOM   15760 O O   . GLY D 1 418 ? -7.999  41.814  97.707  1.00 58.36  ? 418 GLY D O   1 
ATOM   15761 N N   . ASN D 1 419 ? -6.996  42.713  95.894  1.00 72.98  ? 419 ASN D N   1 
ATOM   15762 C CA  . ASN D 1 419 ? -5.732  43.011  96.556  1.00 68.09  ? 419 ASN D CA  1 
ATOM   15763 C C   . ASN D 1 419 ? -5.614  44.509  96.815  1.00 74.03  ? 419 ASN D C   1 
ATOM   15764 O O   . ASN D 1 419 ? -6.445  45.310  96.380  1.00 76.06  ? 419 ASN D O   1 
ATOM   15765 C CB  . ASN D 1 419 ? -4.535  42.482  95.741  1.00 69.99  ? 419 ASN D CB  1 
ATOM   15766 C CG  . ASN D 1 419 ? -4.391  43.130  94.361  1.00 76.30  ? 419 ASN D CG  1 
ATOM   15767 O OD1 . ASN D 1 419 ? -4.806  44.266  94.135  1.00 70.69  ? 419 ASN D OD1 1 
ATOM   15768 N ND2 . ASN D 1 419 ? -3.746  42.415  93.447  1.00 77.78  ? 419 ASN D ND2 1 
ATOM   15769 N N   . LYS D 1 420 ? -4.562  44.887  97.542  1.00 75.83  ? 420 LYS D N   1 
ATOM   15770 C CA  . LYS D 1 420 ? -4.452  46.274  97.982  1.00 72.92  ? 420 LYS D CA  1 
ATOM   15771 C C   . LYS D 1 420 ? -4.193  47.210  96.808  1.00 77.53  ? 420 LYS D C   1 
ATOM   15772 O O   . LYS D 1 420 ? -4.802  48.283  96.723  1.00 81.75  ? 420 LYS D O   1 
ATOM   15773 C CB  . LYS D 1 420 ? -3.360  46.404  99.042  1.00 69.67  ? 420 LYS D CB  1 
ATOM   15774 C CG  . LYS D 1 420 ? -2.551  47.686  98.958  1.00 76.81  ? 420 LYS D CG  1 
ATOM   15775 C CD  . LYS D 1 420 ? -1.260  47.566  99.745  1.00 78.71  ? 420 LYS D CD  1 
ATOM   15776 C CE  . LYS D 1 420 ? -0.445  46.372  99.284  1.00 74.66  ? 420 LYS D CE  1 
ATOM   15777 N NZ  . LYS D 1 420 ? 0.653   46.052  100.236 1.00 89.65  ? 420 LYS D NZ  1 
ATOM   15778 N N   . GLU D 1 421 ? -3.311  46.819  95.883  1.00 78.22  ? 421 GLU D N   1 
ATOM   15779 C CA  . GLU D 1 421 ? -2.998  47.686  94.748  1.00 78.04  ? 421 GLU D CA  1 
ATOM   15780 C C   . GLU D 1 421 ? -4.221  47.905  93.862  1.00 69.20  ? 421 GLU D C   1 
ATOM   15781 O O   . GLU D 1 421 ? -4.519  49.039  93.470  1.00 71.12  ? 421 GLU D O   1 
ATOM   15782 C CB  . GLU D 1 421 ? -1.841  47.102  93.931  1.00 76.48  ? 421 GLU D CB  1 
ATOM   15783 C CG  . GLU D 1 421 ? -0.734  46.387  94.733  1.00 94.14  ? 421 GLU D CG  1 
ATOM   15784 C CD  . GLU D 1 421 ? -1.105  44.976  95.183  1.00 101.09 ? 421 GLU D CD  1 
ATOM   15785 O OE1 . GLU D 1 421 ? -2.312  44.711  95.398  1.00 94.53  ? 421 GLU D OE1 1 
ATOM   15786 O OE2 . GLU D 1 421 ? -0.190  44.129  95.306  1.00 113.05 ? 421 GLU D OE2 1 
ATOM   15787 N N   . LYS D 1 422 ? -4.946  46.830  93.537  1.00 63.34  ? 422 LYS D N   1 
ATOM   15788 C CA  . LYS D 1 422 ? -6.067  46.957  92.607  1.00 68.74  ? 422 LYS D CA  1 
ATOM   15789 C C   . LYS D 1 422 ? -7.252  47.666  93.255  1.00 65.01  ? 422 LYS D C   1 
ATOM   15790 O O   . LYS D 1 422 ? -7.974  48.417  92.588  1.00 53.11  ? 422 LYS D O   1 
ATOM   15791 C CB  . LYS D 1 422 ? -6.495  45.584  92.096  1.00 64.65  ? 422 LYS D CB  1 
ATOM   15792 C CG  . LYS D 1 422 ? -5.640  45.028  90.974  1.00 61.33  ? 422 LYS D CG  1 
ATOM   15793 C CD  . LYS D 1 422 ? -5.729  43.515  90.931  1.00 54.55  ? 422 LYS D CD  1 
ATOM   15794 C CE  . LYS D 1 422 ? -4.499  42.913  90.294  1.00 58.91  ? 422 LYS D CE  1 
ATOM   15795 N NZ  . LYS D 1 422 ? -4.729  41.500  89.898  1.00 59.83  ? 422 LYS D NZ  1 
ATOM   15796 N N   . ASN D 1 423 ? -7.470  47.435  94.553  1.00 69.40  ? 423 ASN D N   1 
ATOM   15797 C CA  . ASN D 1 423 ? -8.553  48.110  95.257  1.00 57.18  ? 423 ASN D CA  1 
ATOM   15798 C C   . ASN D 1 423 ? -8.312  49.608  95.349  1.00 54.48  ? 423 ASN D C   1 
ATOM   15799 O O   . ASN D 1 423 ? -9.270  50.385  95.426  1.00 52.54  ? 423 ASN D O   1 
ATOM   15800 C CB  . ASN D 1 423 ? -8.722  47.521  96.655  1.00 59.24  ? 423 ASN D CB  1 
ATOM   15801 C CG  . ASN D 1 423 ? -9.248  46.100  96.631  1.00 55.25  ? 423 ASN D CG  1 
ATOM   15802 O OD1 . ASN D 1 423 ? -10.024 45.730  95.757  1.00 58.65  ? 423 ASN D OD1 1 
ATOM   15803 N ND2 . ASN D 1 423 ? -8.823  45.296  97.594  1.00 64.74  ? 423 ASN D ND2 1 
ATOM   15804 N N   . GLU D 1 424 ? -7.046  50.031  95.349  1.00 61.70  ? 424 GLU D N   1 
ATOM   15805 C CA  . GLU D 1 424 ? -6.747  51.458  95.350  1.00 67.91  ? 424 GLU D CA  1 
ATOM   15806 C C   . GLU D 1 424 ? -7.168  52.121  94.044  1.00 62.55  ? 424 GLU D C   1 
ATOM   15807 O O   . GLU D 1 424 ? -7.566  53.291  94.048  1.00 65.66  ? 424 GLU D O   1 
ATOM   15808 C CB  . GLU D 1 424 ? -5.259  51.688  95.613  1.00 65.27  ? 424 GLU D CB  1 
ATOM   15809 C CG  . GLU D 1 424 ? -4.882  53.127  95.945  1.00 74.05  ? 424 GLU D CG  1 
ATOM   15810 C CD  . GLU D 1 424 ? -5.700  53.721  97.079  1.00 84.76  ? 424 GLU D CD  1 
ATOM   15811 O OE1 . GLU D 1 424 ? -5.942  53.016  98.084  1.00 87.63  ? 424 GLU D OE1 1 
ATOM   15812 O OE2 . GLU D 1 424 ? -6.096  54.901  96.966  1.00 88.50  ? 424 GLU D OE2 1 
ATOM   15813 N N   . TYR D 1 425 ? -7.091  51.404  92.922  1.00 51.20  ? 425 TYR D N   1 
ATOM   15814 C CA  . TYR D 1 425 ? -7.614  51.963  91.684  1.00 52.20  ? 425 TYR D CA  1 
ATOM   15815 C C   . TYR D 1 425 ? -9.123  52.131  91.764  1.00 55.85  ? 425 TYR D C   1 
ATOM   15816 O O   . TYR D 1 425 ? -9.675  53.122  91.270  1.00 55.28  ? 425 TYR D O   1 
ATOM   15817 C CB  . TYR D 1 425 ? -7.254  51.079  90.491  1.00 61.24  ? 425 TYR D CB  1 
ATOM   15818 C CG  . TYR D 1 425 ? -6.088  51.572  89.667  1.00 64.60  ? 425 TYR D CG  1 
ATOM   15819 C CD1 . TYR D 1 425 ? -5.053  52.294  90.249  1.00 62.54  ? 425 TYR D CD1 1 
ATOM   15820 C CD2 . TYR D 1 425 ? -6.003  51.276  88.312  1.00 60.76  ? 425 TYR D CD2 1 
ATOM   15821 C CE1 . TYR D 1 425 ? -3.978  52.727  89.505  1.00 60.61  ? 425 TYR D CE1 1 
ATOM   15822 C CE2 . TYR D 1 425 ? -4.927  51.709  87.557  1.00 66.56  ? 425 TYR D CE2 1 
ATOM   15823 C CZ  . TYR D 1 425 ? -3.917  52.436  88.163  1.00 68.93  ? 425 TYR D CZ  1 
ATOM   15824 O OH  . TYR D 1 425 ? -2.835  52.879  87.441  1.00 70.79  ? 425 TYR D OH  1 
ATOM   15825 N N   . TRP D 1 426 ? -9.812  51.161  92.364  1.00 54.45  ? 426 TRP D N   1 
ATOM   15826 C CA  . TRP D 1 426 ? -11.262 51.253  92.460  1.00 49.84  ? 426 TRP D CA  1 
ATOM   15827 C C   . TRP D 1 426 ? -11.676 52.419  93.345  1.00 52.84  ? 426 TRP D C   1 
ATOM   15828 O O   . TRP D 1 426 ? -12.636 53.132  93.028  1.00 53.67  ? 426 TRP D O   1 
ATOM   15829 C CB  . TRP D 1 426 ? -11.836 49.938  92.976  1.00 46.81  ? 426 TRP D CB  1 
ATOM   15830 C CG  . TRP D 1 426 ? -11.861 48.877  91.925  1.00 53.29  ? 426 TRP D CG  1 
ATOM   15831 C CD1 . TRP D 1 426 ? -11.017 47.812  91.815  1.00 55.28  ? 426 TRP D CD1 1 
ATOM   15832 C CD2 . TRP D 1 426 ? -12.770 48.785  90.826  1.00 51.43  ? 426 TRP D CD2 1 
ATOM   15833 N NE1 . TRP D 1 426 ? -11.348 47.059  90.714  1.00 48.78  ? 426 TRP D NE1 1 
ATOM   15834 C CE2 . TRP D 1 426 ? -12.422 47.635  90.091  1.00 46.30  ? 426 TRP D CE2 1 
ATOM   15835 C CE3 . TRP D 1 426 ? -13.849 49.563  90.393  1.00 51.67  ? 426 TRP D CE3 1 
ATOM   15836 C CZ2 . TRP D 1 426 ? -13.112 47.243  88.950  1.00 51.03  ? 426 TRP D CZ2 1 
ATOM   15837 C CZ3 . TRP D 1 426 ? -14.534 49.174  89.261  1.00 56.68  ? 426 TRP D CZ3 1 
ATOM   15838 C CH2 . TRP D 1 426 ? -14.163 48.025  88.550  1.00 58.38  ? 426 TRP D CH2 1 
ATOM   15839 N N   . LYS D 1 427 ? -10.947 52.649  94.442  1.00 55.94  ? 427 LYS D N   1 
ATOM   15840 C CA  . LYS D 1 427 ? -11.240 53.809  95.279  1.00 56.03  ? 427 LYS D CA  1 
ATOM   15841 C C   . LYS D 1 427 ? -11.120 55.100  94.480  1.00 54.25  ? 427 LYS D C   1 
ATOM   15842 O O   . LYS D 1 427 ? -11.931 56.019  94.649  1.00 53.08  ? 427 LYS D O   1 
ATOM   15843 C CB  . LYS D 1 427 ? -10.317 53.844  96.500  1.00 48.15  ? 427 LYS D CB  1 
ATOM   15844 C CG  . LYS D 1 427 ? -10.607 52.761  97.523  1.00 53.17  ? 427 LYS D CG  1 
ATOM   15845 C CD  . LYS D 1 427 ? -9.410  52.522  98.433  1.00 58.96  ? 427 LYS D CD  1 
ATOM   15846 C CE  . LYS D 1 427 ? -9.229  51.037  98.723  1.00 58.80  ? 427 LYS D CE  1 
ATOM   15847 N NZ  . LYS D 1 427 ? -7.817  50.579  98.530  1.00 66.37  ? 427 LYS D NZ  1 
ATOM   15848 N N   . ILE D 1 428 ? -10.122 55.183  93.597  1.00 54.60  ? 428 ILE D N   1 
ATOM   15849 C CA  . ILE D 1 428 ? -9.944  56.385  92.786  1.00 53.31  ? 428 ILE D CA  1 
ATOM   15850 C C   . ILE D 1 428 ? -11.132 56.577  91.860  1.00 53.14  ? 428 ILE D C   1 
ATOM   15851 O O   . ILE D 1 428 ? -11.705 57.670  91.771  1.00 60.13  ? 428 ILE D O   1 
ATOM   15852 C CB  . ILE D 1 428 ? -8.629  56.308  91.996  1.00 54.49  ? 428 ILE D CB  1 
ATOM   15853 C CG1 . ILE D 1 428 ? -7.449  56.235  92.954  1.00 47.70  ? 428 ILE D CG1 1 
ATOM   15854 C CG2 . ILE D 1 428 ? -8.507  57.495  91.062  1.00 53.90  ? 428 ILE D CG2 1 
ATOM   15855 C CD1 . ILE D 1 428 ? -6.148  56.124  92.248  1.00 48.84  ? 428 ILE D CD1 1 
ATOM   15856 N N   . LEU D 1 429 ? -11.513 55.515  91.152  1.00 50.93  ? 429 LEU D N   1 
ATOM   15857 C CA  . LEU D 1 429 ? -12.660 55.598  90.258  1.00 51.76  ? 429 LEU D CA  1 
ATOM   15858 C C   . LEU D 1 429 ? -13.933 55.911  91.038  1.00 55.71  ? 429 LEU D C   1 
ATOM   15859 O O   . LEU D 1 429 ? -14.773 56.696  90.580  1.00 57.24  ? 429 LEU D O   1 
ATOM   15860 C CB  . LEU D 1 429 ? -12.793 54.292  89.471  1.00 51.42  ? 429 LEU D CB  1 
ATOM   15861 C CG  . LEU D 1 429 ? -13.744 54.271  88.272  1.00 55.69  ? 429 LEU D CG  1 
ATOM   15862 C CD1 . LEU D 1 429 ? -13.313 55.303  87.259  1.00 53.72  ? 429 LEU D CD1 1 
ATOM   15863 C CD2 . LEU D 1 429 ? -13.800 52.891  87.623  1.00 52.85  ? 429 LEU D CD2 1 
ATOM   15864 N N   . ILE D 1 430 ? -14.078 55.329  92.234  1.00 50.29  ? 430 ILE D N   1 
ATOM   15865 C CA  . ILE D 1 430 ? -15.272 55.574  93.046  1.00 54.58  ? 430 ILE D CA  1 
ATOM   15866 C C   . ILE D 1 430 ? -15.345 57.038  93.461  1.00 58.49  ? 430 ILE D C   1 
ATOM   15867 O O   . ILE D 1 430 ? -16.422 57.648  93.470  1.00 63.13  ? 430 ILE D O   1 
ATOM   15868 C CB  . ILE D 1 430 ? -15.299 54.636  94.271  1.00 48.14  ? 430 ILE D CB  1 
ATOM   15869 C CG1 . ILE D 1 430 ? -15.715 53.226  93.857  1.00 42.29  ? 430 ILE D CG1 1 
ATOM   15870 C CG2 . ILE D 1 430 ? -16.238 55.175  95.344  1.00 57.98  ? 430 ILE D CG2 1 
ATOM   15871 C CD1 . ILE D 1 430 ? -15.322 52.158  94.847  1.00 43.55  ? 430 ILE D CD1 1 
ATOM   15872 N N   . GLU D 1 431 ? -14.200 57.627  93.798  1.00 62.56  ? 431 GLU D N   1 
ATOM   15873 C CA  . GLU D 1 431 ? -14.175 59.024  94.212  1.00 64.17  ? 431 GLU D CA  1 
ATOM   15874 C C   . GLU D 1 431 ? -14.426 59.950  93.024  1.00 62.74  ? 431 GLU D C   1 
ATOM   15875 O O   . GLU D 1 431 ? -15.188 60.919  93.134  1.00 67.35  ? 431 GLU D O   1 
ATOM   15876 C CB  . GLU D 1 431 ? -12.835 59.328  94.876  1.00 52.65  ? 431 GLU D CB  1 
ATOM   15877 C CG  . GLU D 1 431 ? -12.780 59.008  96.367  1.00 64.12  ? 431 GLU D CG  1 
ATOM   15878 C CD  . GLU D 1 431 ? -14.064 59.331  97.109  1.00 87.47  ? 431 GLU D CD  1 
ATOM   15879 O OE1 . GLU D 1 431 ? -14.818 58.389  97.444  1.00 91.22  ? 431 GLU D OE1 1 
ATOM   15880 O OE2 . GLU D 1 431 ? -14.307 60.527  97.371  1.00 99.78  ? 431 GLU D OE2 1 
ATOM   15881 N N   . ALA D 1 432 ? -13.813 59.657  91.872  1.00 52.39  ? 432 ALA D N   1 
ATOM   15882 C CA  . ALA D 1 432 ? -14.022 60.495  90.695  1.00 59.31  ? 432 ALA D CA  1 
ATOM   15883 C C   . ALA D 1 432 ? -15.465 60.450  90.219  1.00 58.16  ? 432 ALA D C   1 
ATOM   15884 O O   . ALA D 1 432 ? -15.997 61.466  89.756  1.00 57.93  ? 432 ALA D O   1 
ATOM   15885 C CB  . ALA D 1 432 ? -13.095 60.064  89.558  1.00 65.36  ? 432 ALA D CB  1 
ATOM   15886 N N   . LYS D 1 433 ? -16.108 59.285  90.315  1.00 57.07  ? 433 LYS D N   1 
ATOM   15887 C CA  . LYS D 1 433 ? -17.479 59.162  89.841  1.00 58.17  ? 433 LYS D CA  1 
ATOM   15888 C C   . LYS D 1 433 ? -18.424 60.054  90.638  1.00 61.51  ? 433 LYS D C   1 
ATOM   15889 O O   . LYS D 1 433 ? -19.383 60.597  90.075  1.00 64.13  ? 433 LYS D O   1 
ATOM   15890 C CB  . LYS D 1 433 ? -17.922 57.699  89.900  1.00 57.45  ? 433 LYS D CB  1 
ATOM   15891 C CG  . LYS D 1 433 ? -19.346 57.451  89.416  1.00 58.53  ? 433 LYS D CG  1 
ATOM   15892 C CD  . LYS D 1 433 ? -19.473 57.549  87.898  1.00 56.92  ? 433 LYS D CD  1 
ATOM   15893 C CE  . LYS D 1 433 ? -20.923 57.801  87.478  1.00 62.61  ? 433 LYS D CE  1 
ATOM   15894 N NZ  . LYS D 1 433 ? -21.050 58.282  86.071  1.00 58.08  ? 433 LYS D NZ  1 
ATOM   15895 N N   . LYS D 1 434 ? -18.157 60.242  91.935  1.00 55.38  ? 434 LYS D N   1 
ATOM   15896 C CA  . LYS D 1 434 ? -19.012 61.109  92.739  1.00 53.73  ? 434 LYS D CA  1 
ATOM   15897 C C   . LYS D 1 434 ? -18.939 62.556  92.275  1.00 58.27  ? 434 LYS D C   1 
ATOM   15898 O O   . LYS D 1 434 ? -19.908 63.306  92.440  1.00 68.59  ? 434 LYS D O   1 
ATOM   15899 C CB  . LYS D 1 434 ? -18.629 61.026  94.216  1.00 65.89  ? 434 LYS D CB  1 
ATOM   15900 C CG  . LYS D 1 434 ? -18.692 59.635  94.812  1.00 69.48  ? 434 LYS D CG  1 
ATOM   15901 C CD  . LYS D 1 434 ? -17.596 59.460  95.845  1.00 65.30  ? 434 LYS D CD  1 
ATOM   15902 C CE  . LYS D 1 434 ? -17.992 58.446  96.902  1.00 72.77  ? 434 LYS D CE  1 
ATOM   15903 N NZ  . LYS D 1 434 ? -17.174 58.581  98.144  1.00 80.60  ? 434 LYS D NZ  1 
ATOM   15904 N N   . LYS D 1 435 ? -17.811 62.966  91.697  1.00 59.18  ? 435 LYS D N   1 
ATOM   15905 C CA  . LYS D 1 435 ? -17.631 64.327  91.207  1.00 63.48  ? 435 LYS D CA  1 
ATOM   15906 C C   . LYS D 1 435 ? -17.383 64.353  89.699  1.00 60.35  ? 435 LYS D C   1 
ATOM   15907 O O   . LYS D 1 435 ? -16.691 65.238  89.192  1.00 60.97  ? 435 LYS D O   1 
ATOM   15908 C CB  . LYS D 1 435 ? -16.492 65.022  91.954  1.00 62.71  ? 435 LYS D CB  1 
ATOM   15909 C CG  . LYS D 1 435 ? -16.801 65.368  93.409  1.00 65.66  ? 435 LYS D CG  1 
ATOM   15910 C CD  . LYS D 1 435 ? -17.762 66.552  93.512  1.00 76.06  ? 435 LYS D CD  1 
ATOM   15911 C CE  . LYS D 1 435 ? -17.421 67.454  94.695  1.00 80.64  ? 435 LYS D CE  1 
ATOM   15912 N NZ  . LYS D 1 435 ? -17.180 68.866  94.274  1.00 79.37  ? 435 LYS D NZ  1 
ATOM   15913 N N   . ALA D 1 436 ? -17.946 63.392  88.967  1.00 58.71  ? 436 ALA D N   1 
ATOM   15914 C CA  . ALA D 1 436 ? -17.670 63.273  87.539  1.00 58.50  ? 436 ALA D CA  1 
ATOM   15915 C C   . ALA D 1 436 ? -18.549 64.217  86.729  1.00 55.37  ? 436 ALA D C   1 
ATOM   15916 O O   . ALA D 1 436 ? -19.720 64.429  87.046  1.00 66.55  ? 436 ALA D O   1 
ATOM   15917 C CB  . ALA D 1 436 ? -17.885 61.835  87.067  1.00 56.93  ? 436 ALA D CB  1 
ATOM   15918 N N   . LYS D 1 437 ? -17.981 64.782  85.672  1.00 49.78  ? 437 LYS D N   1 
ATOM   15919 C CA  . LYS D 1 437 ? -18.690 65.767  84.876  1.00 54.12  ? 437 LYS D CA  1 
ATOM   15920 C C   . LYS D 1 437 ? -18.788 65.420  83.398  1.00 48.19  ? 437 LYS D C   1 
ATOM   15921 O O   . LYS D 1 437 ? -19.566 66.058  82.683  1.00 42.92  ? 437 LYS D O   1 
ATOM   15922 C CB  . LYS D 1 437 ? -18.025 67.144  85.016  1.00 45.67  ? 437 LYS D CB  1 
ATOM   15923 C CG  . LYS D 1 437 ? -17.629 67.496  86.435  1.00 52.88  ? 437 LYS D CG  1 
ATOM   15924 C CD  . LYS D 1 437 ? -18.814 68.060  87.210  1.00 62.15  ? 437 LYS D CD  1 
ATOM   15925 C CE  . LYS D 1 437 ? -18.537 68.113  88.711  1.00 69.12  ? 437 LYS D CE  1 
ATOM   15926 N NZ  . LYS D 1 437 ? -19.613 67.499  89.537  1.00 69.00  ? 437 LYS D NZ  1 
ATOM   15927 N N   . ASN D 1 438 ? -18.030 64.439  82.923  1.00 53.45  ? 438 ASN D N   1 
ATOM   15928 C CA  . ASN D 1 438 ? -18.031 64.074  81.515  1.00 50.88  ? 438 ASN D CA  1 
ATOM   15929 C C   . ASN D 1 438 ? -17.822 62.568  81.410  1.00 59.47  ? 438 ASN D C   1 
ATOM   15930 O O   . ASN D 1 438 ? -17.596 61.874  82.407  1.00 57.19  ? 438 ASN D O   1 
ATOM   15931 C CB  . ASN D 1 438 ? -16.966 64.835  80.700  1.00 42.89  ? 438 ASN D CB  1 
ATOM   15932 C CG  . ASN D 1 438 ? -15.639 65.037  81.453  1.00 57.36  ? 438 ASN D CG  1 
ATOM   15933 O OD1 . ASN D 1 438 ? -15.564 65.743  82.463  1.00 54.49  ? 438 ASN D OD1 1 
ATOM   15934 N ND2 . ASN D 1 438 ? -14.584 64.409  80.945  1.00 60.39  ? 438 ASN D ND2 1 
ATOM   15935 N N   . ASP D 1 439 ? -17.900 62.056  80.188  1.00 56.28  ? 439 ASP D N   1 
ATOM   15936 C CA  . ASP D 1 439 ? -17.872 60.620  79.969  1.00 49.25  ? 439 ASP D CA  1 
ATOM   15937 C C   . ASP D 1 439 ? -16.463 60.060  79.890  1.00 55.87  ? 439 ASP D C   1 
ATOM   15938 O O   . ASP D 1 439 ? -16.290 58.901  79.500  1.00 55.89  ? 439 ASP D O   1 
ATOM   15939 C CB  . ASP D 1 439 ? -18.666 60.266  78.714  1.00 57.69  ? 439 ASP D CB  1 
ATOM   15940 C CG  . ASP D 1 439 ? -20.152 60.550  78.873  1.00 78.03  ? 439 ASP D CG  1 
ATOM   15941 O OD1 . ASP D 1 439 ? -20.612 60.767  80.020  1.00 80.65  ? 439 ASP D OD1 1 
ATOM   15942 O OD2 . ASP D 1 439 ? -20.864 60.554  77.850  1.00 79.14  ? 439 ASP D OD2 1 
ATOM   15943 N N   . TYR D 1 440 ? -15.455 60.846  80.267  1.00 59.46  ? 440 TYR D N   1 
ATOM   15944 C CA  . TYR D 1 440 ? -14.124 60.288  80.467  1.00 53.91  ? 440 TYR D CA  1 
ATOM   15945 C C   . TYR D 1 440 ? -14.069 59.376  81.683  1.00 53.75  ? 440 TYR D C   1 
ATOM   15946 O O   . TYR D 1 440 ? -13.045 58.721  81.907  1.00 56.65  ? 440 TYR D O   1 
ATOM   15947 C CB  . TYR D 1 440 ? -13.100 61.407  80.610  1.00 50.46  ? 440 TYR D CB  1 
ATOM   15948 C CG  . TYR D 1 440 ? -12.397 61.769  79.324  1.00 54.21  ? 440 TYR D CG  1 
ATOM   15949 C CD1 . TYR D 1 440 ? -11.567 60.861  78.671  1.00 55.79  ? 440 TYR D CD1 1 
ATOM   15950 C CD2 . TYR D 1 440 ? -12.538 63.031  78.779  1.00 57.44  ? 440 TYR D CD2 1 
ATOM   15951 C CE1 . TYR D 1 440 ? -10.912 61.209  77.492  1.00 52.57  ? 440 TYR D CE1 1 
ATOM   15952 C CE2 . TYR D 1 440 ? -11.893 63.387  77.611  1.00 63.00  ? 440 TYR D CE2 1 
ATOM   15953 C CZ  . TYR D 1 440 ? -11.081 62.477  76.968  1.00 55.25  ? 440 TYR D CZ  1 
ATOM   15954 O OH  . TYR D 1 440 ? -10.449 62.850  75.803  1.00 62.40  ? 440 TYR D OH  1 
ATOM   15955 N N   . ILE D 1 441 ? -15.141 59.334  82.476  1.00 51.53  ? 441 ILE D N   1 
ATOM   15956 C CA  . ILE D 1 441 ? -15.248 58.343  83.536  1.00 54.30  ? 441 ILE D CA  1 
ATOM   15957 C C   . ILE D 1 441 ? -15.490 56.963  82.941  1.00 55.00  ? 441 ILE D C   1 
ATOM   15958 O O   . ILE D 1 441 ? -15.176 55.943  83.566  1.00 55.42  ? 441 ILE D O   1 
ATOM   15959 C CB  . ILE D 1 441 ? -16.365 58.744  84.521  1.00 61.00  ? 441 ILE D CB  1 
ATOM   15960 C CG1 . ILE D 1 441 ? -16.135 58.117  85.900  1.00 65.15  ? 441 ILE D CG1 1 
ATOM   15961 C CG2 . ILE D 1 441 ? -17.741 58.389  83.963  1.00 52.30  ? 441 ILE D CG2 1 
ATOM   15962 C CD1 . ILE D 1 441 ? -14.800 58.486  86.524  1.00 55.05  ? 441 ILE D CD1 1 
ATOM   15963 N N   . LEU D 1 442 ? -16.052 56.901  81.732  1.00 53.01  ? 442 LEU D N   1 
ATOM   15964 C CA  . LEU D 1 442 ? -16.303 55.610  81.107  1.00 54.85  ? 442 LEU D CA  1 
ATOM   15965 C C   . LEU D 1 442 ? -15.031 55.022  80.531  1.00 53.78  ? 442 LEU D C   1 
ATOM   15966 O O   . LEU D 1 442 ? -14.920 53.799  80.393  1.00 53.09  ? 442 LEU D O   1 
ATOM   15967 C CB  . LEU D 1 442 ? -17.358 55.744  80.012  1.00 56.02  ? 442 LEU D CB  1 
ATOM   15968 C CG  . LEU D 1 442 ? -18.670 56.388  80.451  1.00 57.33  ? 442 LEU D CG  1 
ATOM   15969 C CD1 . LEU D 1 442 ? -19.526 56.714  79.242  1.00 53.37  ? 442 LEU D CD1 1 
ATOM   15970 C CD2 . LEU D 1 442 ? -19.413 55.472  81.399  1.00 56.06  ? 442 LEU D CD2 1 
ATOM   15971 N N   . VAL D 1 443 ? -14.068 55.869  80.186  1.00 55.05  ? 443 VAL D N   1 
ATOM   15972 C CA  . VAL D 1 443 ? -12.776 55.351  79.775  1.00 51.08  ? 443 VAL D CA  1 
ATOM   15973 C C   . VAL D 1 443 ? -12.100 54.664  80.943  1.00 47.10  ? 443 VAL D C   1 
ATOM   15974 O O   . VAL D 1 443 ? -11.598 53.541  80.818  1.00 41.95  ? 443 VAL D O   1 
ATOM   15975 C CB  . VAL D 1 443 ? -11.900 56.476  79.216  1.00 45.50  ? 443 VAL D CB  1 
ATOM   15976 C CG1 . VAL D 1 443 ? -10.781 55.869  78.417  1.00 48.97  ? 443 VAL D CG1 1 
ATOM   15977 C CG2 . VAL D 1 443 ? -12.742 57.401  78.382  1.00 47.15  ? 443 VAL D CG2 1 
ATOM   15978 N N   . ALA D 1 444 ? -12.091 55.327  82.101  1.00 44.15  ? 444 ALA D N   1 
ATOM   15979 C CA  . ALA D 1 444 ? -11.403 54.809  83.273  1.00 47.03  ? 444 ALA D CA  1 
ATOM   15980 C C   . ALA D 1 444 ? -12.074 53.571  83.836  1.00 47.33  ? 444 ALA D C   1 
ATOM   15981 O O   . ALA D 1 444 ? -11.467 52.872  84.653  1.00 52.69  ? 444 ALA D O   1 
ATOM   15982 C CB  . ALA D 1 444 ? -11.317 55.887  84.349  1.00 47.37  ? 444 ALA D CB  1 
ATOM   15983 N N   . GLU D 1 445 ? -13.297 53.285  83.417  1.00 50.30  ? 445 GLU D N   1 
ATOM   15984 C CA  . GLU D 1 445 ? -13.968 52.064  83.823  1.00 48.78  ? 445 GLU D CA  1 
ATOM   15985 C C   . GLU D 1 445 ? -13.493 50.852  83.038  1.00 54.64  ? 445 GLU D C   1 
ATOM   15986 O O   . GLU D 1 445 ? -14.093 49.780  83.165  1.00 52.18  ? 445 GLU D O   1 
ATOM   15987 C CB  . GLU D 1 445 ? -15.477 52.230  83.674  1.00 50.23  ? 445 GLU D CB  1 
ATOM   15988 C CG  . GLU D 1 445 ? -16.099 52.975  84.838  1.00 61.41  ? 445 GLU D CG  1 
ATOM   15989 C CD  . GLU D 1 445 ? -17.286 53.817  84.431  1.00 57.87  ? 445 GLU D CD  1 
ATOM   15990 O OE1 . GLU D 1 445 ? -18.018 53.407  83.507  1.00 56.45  ? 445 GLU D OE1 1 
ATOM   15991 O OE2 . GLU D 1 445 ? -17.496 54.882  85.045  1.00 60.53  ? 445 GLU D OE2 1 
ATOM   15992 N N   . GLY D 1 446 ? -12.441 51.005  82.233  1.00 54.68  ? 446 GLY D N   1 
ATOM   15993 C CA  . GLY D 1 446 ? -11.964 49.903  81.428  1.00 50.81  ? 446 GLY D CA  1 
ATOM   15994 C C   . GLY D 1 446 ? -11.146 48.930  82.250  1.00 55.00  ? 446 GLY D C   1 
ATOM   15995 O O   . GLY D 1 446 ? -10.523 49.285  83.251  1.00 59.08  ? 446 GLY D O   1 
ATOM   15996 N N   . SER D 1 447 ? -11.153 47.673  81.814  1.00 52.39  ? 447 SER D N   1 
ATOM   15997 C CA  . SER D 1 447 ? -10.597 46.625  82.654  1.00 52.13  ? 447 SER D CA  1 
ATOM   15998 C C   . SER D 1 447 ? -9.081  46.678  82.665  1.00 57.17  ? 447 SER D C   1 
ATOM   15999 O O   . SER D 1 447 ? -8.451  46.215  83.627  1.00 54.50  ? 447 SER D O   1 
ATOM   16000 C CB  . SER D 1 447 ? -11.097 45.256  82.190  1.00 50.17  ? 447 SER D CB  1 
ATOM   16001 O OG  . SER D 1 447 ? -11.021 45.138  80.780  1.00 54.76  ? 447 SER D OG  1 
ATOM   16002 N N   . ASP D 1 448 ? -8.488  47.267  81.622  1.00 57.80  ? 448 ASP D N   1 
ATOM   16003 C CA  . ASP D 1 448 ? -7.050  47.150  81.405  1.00 52.10  ? 448 ASP D CA  1 
ATOM   16004 C C   . ASP D 1 448 ? -6.259  47.772  82.544  1.00 52.68  ? 448 ASP D C   1 
ATOM   16005 O O   . ASP D 1 448 ? -5.280  47.186  83.016  1.00 61.41  ? 448 ASP D O   1 
ATOM   16006 C CB  . ASP D 1 448 ? -6.673  47.787  80.069  1.00 56.83  ? 448 ASP D CB  1 
ATOM   16007 C CG  . ASP D 1 448 ? -7.380  47.134  78.888  1.00 66.40  ? 448 ASP D CG  1 
ATOM   16008 O OD1 . ASP D 1 448 ? -8.630  47.203  78.810  1.00 60.58  ? 448 ASP D OD1 1 
ATOM   16009 O OD2 . ASP D 1 448 ? -6.681  46.543  78.035  1.00 67.96  ? 448 ASP D OD2 1 
ATOM   16010 N N   . TRP D 1 449 ? -6.693  48.935  83.028  1.00 52.96  ? 449 TRP D N   1 
ATOM   16011 C CA  . TRP D 1 449 ? -5.936  49.633  84.061  1.00 54.07  ? 449 TRP D CA  1 
ATOM   16012 C C   . TRP D 1 449 ? -5.820  48.798  85.331  1.00 56.46  ? 449 TRP D C   1 
ATOM   16013 O O   . TRP D 1 449 ? -4.763  48.770  85.971  1.00 64.55  ? 449 TRP D O   1 
ATOM   16014 C CB  . TRP D 1 449 ? -6.589  50.980  84.351  1.00 56.08  ? 449 TRP D CB  1 
ATOM   16015 C CG  . TRP D 1 449 ? -7.219  51.622  83.146  1.00 55.26  ? 449 TRP D CG  1 
ATOM   16016 C CD1 . TRP D 1 449 ? -8.547  51.877  82.956  1.00 55.64  ? 449 TRP D CD1 1 
ATOM   16017 C CD2 . TRP D 1 449 ? -6.547  52.110  81.973  1.00 52.27  ? 449 TRP D CD2 1 
ATOM   16018 N NE1 . TRP D 1 449 ? -8.746  52.488  81.735  1.00 46.89  ? 449 TRP D NE1 1 
ATOM   16019 C CE2 . TRP D 1 449 ? -7.535  52.643  81.115  1.00 47.15  ? 449 TRP D CE2 1 
ATOM   16020 C CE3 . TRP D 1 449 ? -5.208  52.149  81.564  1.00 51.13  ? 449 TRP D CE3 1 
ATOM   16021 C CZ2 . TRP D 1 449 ? -7.226  53.203  79.875  1.00 56.58  ? 449 TRP D CZ2 1 
ATOM   16022 C CZ3 . TRP D 1 449 ? -4.906  52.708  80.330  1.00 47.78  ? 449 TRP D CZ3 1 
ATOM   16023 C CH2 . TRP D 1 449 ? -5.909  53.226  79.502  1.00 49.66  ? 449 TRP D CH2 1 
ATOM   16024 N N   . PHE D 1 450 ? -6.890  48.093  85.697  1.00 56.31  ? 450 PHE D N   1 
ATOM   16025 C CA  . PHE D 1 450 ? -6.865  47.246  86.885  1.00 55.97  ? 450 PHE D CA  1 
ATOM   16026 C C   . PHE D 1 450 ? -6.120  45.939  86.643  1.00 59.81  ? 450 PHE D C   1 
ATOM   16027 O O   . PHE D 1 450 ? -5.664  45.305  87.601  1.00 61.62  ? 450 PHE D O   1 
ATOM   16028 C CB  . PHE D 1 450 ? -8.291  46.948  87.348  1.00 53.17  ? 450 PHE D CB  1 
ATOM   16029 C CG  . PHE D 1 450 ? -9.134  48.176  87.553  1.00 56.17  ? 450 PHE D CG  1 
ATOM   16030 C CD1 . PHE D 1 450 ? -9.814  48.762  86.493  1.00 46.96  ? 450 PHE D CD1 1 
ATOM   16031 C CD2 . PHE D 1 450 ? -9.247  48.747  88.811  1.00 57.47  ? 450 PHE D CD2 1 
ATOM   16032 C CE1 . PHE D 1 450 ? -10.588 49.898  86.688  1.00 44.98  ? 450 PHE D CE1 1 
ATOM   16033 C CE2 . PHE D 1 450 ? -10.025 49.881  89.008  1.00 56.41  ? 450 PHE D CE2 1 
ATOM   16034 C CZ  . PHE D 1 450 ? -10.690 50.455  87.943  1.00 50.02  ? 450 PHE D CZ  1 
ATOM   16035 N N   . TRP D 1 451 ? -5.996  45.514  85.382  1.00 63.01  ? 451 TRP D N   1 
ATOM   16036 C CA  . TRP D 1 451 ? -5.270  44.284  85.074  1.00 59.60  ? 451 TRP D CA  1 
ATOM   16037 C C   . TRP D 1 451 ? -3.799  44.425  85.440  1.00 70.01  ? 451 TRP D C   1 
ATOM   16038 O O   . TRP D 1 451 ? -3.235  43.582  86.147  1.00 71.45  ? 451 TRP D O   1 
ATOM   16039 C CB  . TRP D 1 451 ? -5.445  43.939  83.592  1.00 56.22  ? 451 TRP D CB  1 
ATOM   16040 C CG  . TRP D 1 451 ? -4.599  42.807  83.052  1.00 63.66  ? 451 TRP D CG  1 
ATOM   16041 C CD1 . TRP D 1 451 ? -3.243  42.807  82.867  1.00 66.95  ? 451 TRP D CD1 1 
ATOM   16042 C CD2 . TRP D 1 451 ? -5.064  41.531  82.584  1.00 64.84  ? 451 TRP D CD2 1 
ATOM   16043 N NE1 . TRP D 1 451 ? -2.835  41.606  82.333  1.00 68.07  ? 451 TRP D NE1 1 
ATOM   16044 C CE2 . TRP D 1 451 ? -3.933  40.809  82.143  1.00 68.81  ? 451 TRP D CE2 1 
ATOM   16045 C CE3 . TRP D 1 451 ? -6.322  40.926  82.501  1.00 61.38  ? 451 TRP D CE3 1 
ATOM   16046 C CZ2 . TRP D 1 451 ? -4.026  39.511  81.638  1.00 70.26  ? 451 TRP D CZ2 1 
ATOM   16047 C CZ3 . TRP D 1 451 ? -6.410  39.639  81.993  1.00 60.38  ? 451 TRP D CZ3 1 
ATOM   16048 C CH2 . TRP D 1 451 ? -5.270  38.947  81.570  1.00 68.33  ? 451 TRP D CH2 1 
ATOM   16049 N N   . TRP D 1 452 ? -3.172  45.508  84.987  1.00 70.28  ? 452 TRP D N   1 
ATOM   16050 C CA  . TRP D 1 452 ? -1.757  45.744  85.220  1.00 69.75  ? 452 TRP D CA  1 
ATOM   16051 C C   . TRP D 1 452 ? -1.455  46.219  86.629  1.00 72.85  ? 452 TRP D C   1 
ATOM   16052 O O   . TRP D 1 452 ? -0.283  46.221  87.023  1.00 83.76  ? 452 TRP D O   1 
ATOM   16053 C CB  . TRP D 1 452 ? -1.243  46.767  84.215  1.00 60.96  ? 452 TRP D CB  1 
ATOM   16054 C CG  . TRP D 1 452 ? -1.547  46.366  82.832  1.00 63.76  ? 452 TRP D CG  1 
ATOM   16055 C CD1 . TRP D 1 452 ? -2.441  46.950  81.982  1.00 60.65  ? 452 TRP D CD1 1 
ATOM   16056 C CD2 . TRP D 1 452 ? -0.975  45.264  82.124  1.00 64.04  ? 452 TRP D CD2 1 
ATOM   16057 N NE1 . TRP D 1 452 ? -2.449  46.284  80.778  1.00 62.51  ? 452 TRP D NE1 1 
ATOM   16058 C CE2 . TRP D 1 452 ? -1.556  45.245  80.841  1.00 64.07  ? 452 TRP D CE2 1 
ATOM   16059 C CE3 . TRP D 1 452 ? -0.019  44.296  82.448  1.00 68.56  ? 452 TRP D CE3 1 
ATOM   16060 C CZ2 . TRP D 1 452 ? -1.215  44.294  79.884  1.00 67.04  ? 452 TRP D CZ2 1 
ATOM   16061 C CZ3 . TRP D 1 452 ? 0.320   43.356  81.497  1.00 68.75  ? 452 TRP D CZ3 1 
ATOM   16062 C CH2 . TRP D 1 452 ? -0.276  43.361  80.230  1.00 70.88  ? 452 TRP D CH2 1 
ATOM   16063 N N   . GLN D 1 453 ? -2.470  46.614  87.390  1.00 69.05  ? 453 GLN D N   1 
ATOM   16064 C CA  . GLN D 1 453 ? -2.233  47.146  88.721  1.00 75.20  ? 453 GLN D CA  1 
ATOM   16065 C C   . GLN D 1 453 ? -1.680  46.080  89.647  1.00 76.89  ? 453 GLN D C   1 
ATOM   16066 O O   . GLN D 1 453 ? -2.246  44.990  89.764  1.00 76.94  ? 453 GLN D O   1 
ATOM   16067 C CB  . GLN D 1 453 ? -3.518  47.715  89.304  1.00 68.31  ? 453 GLN D CB  1 
ATOM   16068 C CG  . GLN D 1 453 ? -3.521  49.216  89.293  1.00 71.35  ? 453 GLN D CG  1 
ATOM   16069 C CD  . GLN D 1 453 ? -2.232  49.802  89.835  1.00 77.37  ? 453 GLN D CD  1 
ATOM   16070 O OE1 . GLN D 1 453 ? -1.330  50.165  89.072  1.00 71.07  ? 453 GLN D OE1 1 
ATOM   16071 N NE2 . GLN D 1 453 ? -2.139  49.903  91.158  1.00 72.05  ? 453 GLN D NE2 1 
ATOM   16072 N N   . GLY D 1 454 ? -0.577  46.408  90.314  1.00 85.72  ? 454 GLY D N   1 
ATOM   16073 C CA  . GLY D 1 454 ? -0.046  45.539  91.341  1.00 85.94  ? 454 GLY D CA  1 
ATOM   16074 C C   . GLY D 1 454 ? 0.301   44.147  90.882  1.00 90.85  ? 454 GLY D C   1 
ATOM   16075 O O   . GLY D 1 454 ? 0.307   43.219  91.695  1.00 87.35  ? 454 GLY D O   1 
ATOM   16076 N N   . GLU D 1 455 ? 0.583   43.965  89.595  1.00 96.13  ? 455 GLU D N   1 
ATOM   16077 C CA  . GLU D 1 455 ? 1.156   42.703  89.150  1.00 103.32 ? 455 GLU D CA  1 
ATOM   16078 C C   . GLU D 1 455 ? 2.615   42.637  89.597  1.00 110.13 ? 455 GLU D C   1 
ATOM   16079 O O   . GLU D 1 455 ? 2.928   42.968  90.747  1.00 108.59 ? 455 GLU D O   1 
ATOM   16080 C CB  . GLU D 1 455 ? 1.008   42.541  87.636  1.00 94.90  ? 455 GLU D CB  1 
ATOM   16081 C CG  . GLU D 1 455 ? -0.438  42.347  87.179  1.00 89.31  ? 455 GLU D CG  1 
ATOM   16082 C CD  . GLU D 1 455 ? -1.181  41.258  87.954  1.00 95.25  ? 455 GLU D CD  1 
ATOM   16083 O OE1 . GLU D 1 455 ? -0.605  40.171  88.185  1.00 98.72  ? 455 GLU D OE1 1 
ATOM   16084 O OE2 . GLU D 1 455 ? -2.356  41.487  88.311  1.00 86.71  ? 455 GLU D OE2 1 
ATOM   16085 N N   . GLU D 1 456 ? 3.519   42.217  88.713  1.00 116.61 ? 456 GLU D N   1 
ATOM   16086 C CA  . GLU D 1 456 ? 4.884   41.937  89.148  1.00 121.22 ? 456 GLU D CA  1 
ATOM   16087 C C   . GLU D 1 456 ? 5.902   42.903  88.550  1.00 125.17 ? 456 GLU D C   1 
ATOM   16088 O O   . GLU D 1 456 ? 6.875   42.442  87.943  1.00 124.60 ? 456 GLU D O   1 
ATOM   16089 C CB  . GLU D 1 456 ? 5.310   40.515  88.760  1.00 117.67 ? 456 GLU D CB  1 
ATOM   16090 C CG  . GLU D 1 456 ? 4.363   39.365  89.110  1.00 117.54 ? 456 GLU D CG  1 
ATOM   16091 C CD  . GLU D 1 456 ? 3.619   39.540  90.419  1.00 119.65 ? 456 GLU D CD  1 
ATOM   16092 O OE1 . GLU D 1 456 ? 4.248   39.348  91.483  1.00 114.82 ? 456 GLU D OE1 1 
ATOM   16093 O OE2 . GLU D 1 456 ? 2.397   39.818  90.379  1.00 118.74 ? 456 GLU D OE2 1 
ATOM   16094 N N   . LYS D 1 457 ? 5.731   44.219  88.732  1.00 123.65 ? 457 LYS D N   1 
ATOM   16095 C CA  . LYS D 1 457 ? 6.505   45.206  87.972  1.00 119.62 ? 457 LYS D CA  1 
ATOM   16096 C C   . LYS D 1 457 ? 6.455   44.786  86.503  1.00 124.41 ? 457 LYS D C   1 
ATOM   16097 O O   . LYS D 1 457 ? 7.445   44.378  85.896  1.00 127.44 ? 457 LYS D O   1 
ATOM   16098 C CB  . LYS D 1 457 ? 7.942   45.330  88.529  1.00 121.11 ? 457 LYS D CB  1 
ATOM   16099 C CG  . LYS D 1 457 ? 9.077   46.089  87.735  1.00 129.16 ? 457 LYS D CG  1 
ATOM   16100 C CD  . LYS D 1 457 ? 8.633   47.128  86.711  1.00 134.19 ? 457 LYS D CD  1 
ATOM   16101 C CE  . LYS D 1 457 ? 9.805   47.662  85.869  1.00 129.54 ? 457 LYS D CE  1 
ATOM   16102 N NZ  . LYS D 1 457 ? 9.280   48.528  84.756  1.00 125.45 ? 457 LYS D NZ  1 
ATOM   16103 N N   . ALA D 1 458 ? 5.240   44.793  85.970  1.00 120.76 ? 458 ALA D N   1 
ATOM   16104 C CA  . ALA D 1 458 ? 5.018   44.331  84.609  1.00 120.73 ? 458 ALA D CA  1 
ATOM   16105 C C   . ALA D 1 458 ? 5.564   45.406  83.668  1.00 119.62 ? 458 ALA D C   1 
ATOM   16106 O O   . ALA D 1 458 ? 5.989   46.475  84.137  1.00 113.95 ? 458 ALA D O   1 
ATOM   16107 C CB  . ALA D 1 458 ? 3.529   44.008  84.391  1.00 109.35 ? 458 ALA D CB  1 
ATOM   16108 N N   . PRO D 1 459 ? 5.623   45.161  82.358  1.00 116.19 ? 459 PRO D N   1 
ATOM   16109 C CA  . PRO D 1 459 ? 6.281   46.127  81.470  1.00 110.32 ? 459 PRO D CA  1 
ATOM   16110 C C   . PRO D 1 459 ? 5.396   47.330  81.159  1.00 97.58  ? 459 PRO D C   1 
ATOM   16111 O O   . PRO D 1 459 ? 4.193   47.202  80.911  1.00 91.80  ? 459 PRO D O   1 
ATOM   16112 C CB  . PRO D 1 459 ? 6.578   45.295  80.214  1.00 97.09  ? 459 PRO D CB  1 
ATOM   16113 C CG  . PRO D 1 459 ? 5.493   44.290  80.201  1.00 96.94  ? 459 PRO D CG  1 
ATOM   16114 C CD  . PRO D 1 459 ? 5.220   43.943  81.628  1.00 105.14 ? 459 PRO D CD  1 
ATOM   16115 N N   . PHE D 1 460 ? 6.016   48.515  81.194  1.00 89.94  ? 460 PHE D N   1 
ATOM   16116 C CA  . PHE D 1 460 ? 5.366   49.786  80.860  1.00 83.48  ? 460 PHE D CA  1 
ATOM   16117 C C   . PHE D 1 460 ? 4.114   50.041  81.696  1.00 77.37  ? 460 PHE D C   1 
ATOM   16118 O O   . PHE D 1 460 ? 3.234   50.804  81.282  1.00 69.80  ? 460 PHE D O   1 
ATOM   16119 C CB  . PHE D 1 460 ? 5.017   49.857  79.370  1.00 78.21  ? 460 PHE D CB  1 
ATOM   16120 C CG  . PHE D 1 460 ? 6.203   50.057  78.475  1.00 85.66  ? 460 PHE D CG  1 
ATOM   16121 C CD1 . PHE D 1 460 ? 7.215   50.938  78.822  1.00 86.13  ? 460 PHE D CD1 1 
ATOM   16122 C CD2 . PHE D 1 460 ? 6.303   49.366  77.274  1.00 88.49  ? 460 PHE D CD2 1 
ATOM   16123 C CE1 . PHE D 1 460 ? 8.311   51.122  77.989  1.00 100.03 ? 460 PHE D CE1 1 
ATOM   16124 C CE2 . PHE D 1 460 ? 7.397   49.544  76.438  1.00 83.51  ? 460 PHE D CE2 1 
ATOM   16125 C CZ  . PHE D 1 460 ? 8.401   50.424  76.797  1.00 90.81  ? 460 PHE D CZ  1 
ATOM   16126 N N   . VAL D 1 461 ? 4.007   49.417  82.872  1.00 76.32  ? 461 VAL D N   1 
ATOM   16127 C CA  . VAL D 1 461 ? 2.843   49.645  83.717  1.00 73.63  ? 461 VAL D CA  1 
ATOM   16128 C C   . VAL D 1 461 ? 2.742   51.093  84.143  1.00 73.55  ? 461 VAL D C   1 
ATOM   16129 O O   . VAL D 1 461 ? 1.652   51.563  84.491  1.00 74.11  ? 461 VAL D O   1 
ATOM   16130 C CB  . VAL D 1 461 ? 2.879   48.722  84.948  1.00 85.70  ? 461 VAL D CB  1 
ATOM   16131 C CG1 . VAL D 1 461 ? 2.880   47.304  84.497  1.00 86.24  ? 461 VAL D CG1 1 
ATOM   16132 C CG2 . VAL D 1 461 ? 4.112   49.012  85.806  1.00 89.61  ? 461 VAL D CG2 1 
ATOM   16133 N N   . GLU D 1 462 ? 3.858   51.822  84.126  1.00 68.20  ? 462 GLU D N   1 
ATOM   16134 C CA  . GLU D 1 462 ? 3.806   53.233  84.478  1.00 65.63  ? 462 GLU D CA  1 
ATOM   16135 C C   . GLU D 1 462 ? 2.924   53.997  83.505  1.00 64.12  ? 462 GLU D C   1 
ATOM   16136 O O   . GLU D 1 462 ? 2.135   54.856  83.910  1.00 70.05  ? 462 GLU D O   1 
ATOM   16137 C CB  . GLU D 1 462 ? 5.213   53.824  84.510  1.00 71.19  ? 462 GLU D CB  1 
ATOM   16138 C CG  . GLU D 1 462 ? 5.241   55.353  84.662  1.00 85.65  ? 462 GLU D CG  1 
ATOM   16139 C CD  . GLU D 1 462 ? 4.511   55.916  85.904  1.00 102.92 ? 462 GLU D CD  1 
ATOM   16140 O OE1 . GLU D 1 462 ? 4.100   55.156  86.818  1.00 100.68 ? 462 GLU D OE1 1 
ATOM   16141 O OE2 . GLU D 1 462 ? 4.349   57.159  85.947  1.00 100.92 ? 462 GLU D OE2 1 
ATOM   16142 N N   . VAL D 1 463 ? 3.037   53.683  82.215  1.00 62.02  ? 463 VAL D N   1 
ATOM   16143 C CA  . VAL D 1 463 ? 2.236   54.367  81.208  1.00 61.45  ? 463 VAL D CA  1 
ATOM   16144 C C   . VAL D 1 463 ? 0.750   54.154  81.467  1.00 64.20  ? 463 VAL D C   1 
ATOM   16145 O O   . VAL D 1 463 ? -0.061  55.084  81.353  1.00 62.18  ? 463 VAL D O   1 
ATOM   16146 C CB  . VAL D 1 463 ? 2.642   53.884  79.807  1.00 61.04  ? 463 VAL D CB  1 
ATOM   16147 C CG1 . VAL D 1 463 ? 2.230   54.904  78.781  1.00 59.96  ? 463 VAL D CG1 1 
ATOM   16148 C CG2 . VAL D 1 463 ? 4.132   53.631  79.759  1.00 64.77  ? 463 VAL D CG2 1 
ATOM   16149 N N   . PHE D 1 464 ? 0.369   52.929  81.827  1.00 57.16  ? 464 PHE D N   1 
ATOM   16150 C CA  . PHE D 1 464 ? -1.037  52.648  82.083  1.00 58.41  ? 464 PHE D CA  1 
ATOM   16151 C C   . PHE D 1 464 ? -1.530  53.411  83.302  1.00 61.91  ? 464 PHE D C   1 
ATOM   16152 O O   . PHE D 1 464 ? -2.687  53.847  83.346  1.00 63.95  ? 464 PHE D O   1 
ATOM   16153 C CB  . PHE D 1 464 ? -1.246  51.146  82.257  1.00 54.53  ? 464 PHE D CB  1 
ATOM   16154 C CG  . PHE D 1 464 ? -1.168  50.377  80.978  1.00 55.16  ? 464 PHE D CG  1 
ATOM   16155 C CD1 . PHE D 1 464 ? -2.271  50.280  80.145  1.00 60.01  ? 464 PHE D CD1 1 
ATOM   16156 C CD2 . PHE D 1 464 ? 0.009   49.763  80.596  1.00 57.98  ? 464 PHE D CD2 1 
ATOM   16157 C CE1 . PHE D 1 464 ? -2.203  49.572  78.958  1.00 56.95  ? 464 PHE D CE1 1 
ATOM   16158 C CE2 . PHE D 1 464 ? 0.086   49.056  79.409  1.00 58.78  ? 464 PHE D CE2 1 
ATOM   16159 C CZ  . PHE D 1 464 ? -1.021  48.959  78.590  1.00 56.82  ? 464 PHE D CZ  1 
ATOM   16160 N N   . ASP D 1 465 ? -0.667  53.588  84.301  1.00 58.00  ? 465 ASP D N   1 
ATOM   16161 C CA  . ASP D 1 465 ? -1.048  54.387  85.457  1.00 63.01  ? 465 ASP D CA  1 
ATOM   16162 C C   . ASP D 1 465 ? -1.221  55.851  85.069  1.00 62.29  ? 465 ASP D C   1 
ATOM   16163 O O   . ASP D 1 465 ? -2.242  56.474  85.391  1.00 59.43  ? 465 ASP D O   1 
ATOM   16164 C CB  . ASP D 1 465 ? -0.008  54.232  86.565  1.00 63.31  ? 465 ASP D CB  1 
ATOM   16165 C CG  . ASP D 1 465 ? -0.206  55.228  87.682  1.00 72.01  ? 465 ASP D CG  1 
ATOM   16166 O OD1 . ASP D 1 465 ? -1.094  55.007  88.536  1.00 70.77  ? 465 ASP D OD1 1 
ATOM   16167 O OD2 . ASP D 1 465 ? 0.521   56.243  87.695  1.00 68.95  ? 465 ASP D OD2 1 
ATOM   16168 N N   . LYS D 1 466 ? -0.237  56.402  84.352  1.00 55.34  ? 466 LYS D N   1 
ATOM   16169 C CA  . LYS D 1 466 ? -0.312  57.779  83.875  1.00 59.39  ? 466 LYS D CA  1 
ATOM   16170 C C   . LYS D 1 466 ? -1.611  58.038  83.118  1.00 62.55  ? 466 LYS D C   1 
ATOM   16171 O O   . LYS D 1 466 ? -2.267  59.066  83.324  1.00 59.83  ? 466 LYS D O   1 
ATOM   16172 C CB  . LYS D 1 466 ? 0.900   58.078  82.988  1.00 59.27  ? 466 LYS D CB  1 
ATOM   16173 C CG  . LYS D 1 466 ? 0.949   59.491  82.448  1.00 62.29  ? 466 LYS D CG  1 
ATOM   16174 C CD  . LYS D 1 466 ? 2.284   60.142  82.760  1.00 59.92  ? 466 LYS D CD  1 
ATOM   16175 C CE  . LYS D 1 466 ? 2.730   61.071  81.641  1.00 71.29  ? 466 LYS D CE  1 
ATOM   16176 N NZ  . LYS D 1 466 ? 1.594   61.850  81.072  1.00 81.65  ? 466 LYS D NZ  1 
ATOM   16177 N N   . LEU D 1 467 ? -2.004  57.103  82.247  1.00 60.04  ? 467 LEU D N   1 
ATOM   16178 C CA  . LEU D 1 467 ? -3.229  57.273  81.470  1.00 58.14  ? 467 LEU D CA  1 
ATOM   16179 C C   . LEU D 1 467 ? -4.468  57.174  82.351  1.00 58.68  ? 467 LEU D C   1 
ATOM   16180 O O   . LEU D 1 467 ? -5.391  57.986  82.225  1.00 58.20  ? 467 LEU D O   1 
ATOM   16181 C CB  . LEU D 1 467 ? -3.293  56.237  80.349  1.00 56.62  ? 467 LEU D CB  1 
ATOM   16182 C CG  . LEU D 1 467 ? -2.502  56.566  79.080  1.00 63.66  ? 467 LEU D CG  1 
ATOM   16183 C CD1 . LEU D 1 467 ? -2.236  55.306  78.262  1.00 51.51  ? 467 LEU D CD1 1 
ATOM   16184 C CD2 . LEU D 1 467 ? -3.207  57.634  78.237  1.00 59.26  ? 467 LEU D CD2 1 
ATOM   16185 N N   . PHE D 1 468 ? -4.519  56.173  83.236  1.00 52.04  ? 468 PHE D N   1 
ATOM   16186 C CA  . PHE D 1 468 ? -5.693  55.999  84.083  1.00 49.82  ? 468 PHE D CA  1 
ATOM   16187 C C   . PHE D 1 468 ? -5.938  57.243  84.923  1.00 56.80  ? 468 PHE D C   1 
ATOM   16188 O O   . PHE D 1 468 ? -7.070  57.725  85.026  1.00 51.72  ? 468 PHE D O   1 
ATOM   16189 C CB  . PHE D 1 468 ? -5.528  54.770  84.978  1.00 55.35  ? 468 PHE D CB  1 
ATOM   16190 C CG  . PHE D 1 468 ? -6.629  54.606  86.005  1.00 56.96  ? 468 PHE D CG  1 
ATOM   16191 C CD1 . PHE D 1 468 ? -7.915  54.255  85.625  1.00 52.77  ? 468 PHE D CD1 1 
ATOM   16192 C CD2 . PHE D 1 468 ? -6.369  54.809  87.352  1.00 59.51  ? 468 PHE D CD2 1 
ATOM   16193 C CE1 . PHE D 1 468 ? -8.919  54.104  86.574  1.00 57.60  ? 468 PHE D CE1 1 
ATOM   16194 C CE2 . PHE D 1 468 ? -7.368  54.661  88.302  1.00 57.14  ? 468 PHE D CE2 1 
ATOM   16195 C CZ  . PHE D 1 468 ? -8.643  54.309  87.914  1.00 51.77  ? 468 PHE D CZ  1 
ATOM   16196 N N   . ARG D 1 469 ? -4.875  57.798  85.509  1.00 56.30  ? 469 ARG D N   1 
ATOM   16197 C CA  . ARG D 1 469 ? -5.046  58.957  86.378  1.00 54.46  ? 469 ARG D CA  1 
ATOM   16198 C C   . ARG D 1 469 ? -5.363  60.213  85.579  1.00 56.61  ? 469 ARG D C   1 
ATOM   16199 O O   . ARG D 1 469 ? -5.963  61.155  86.113  1.00 65.64  ? 469 ARG D O   1 
ATOM   16200 C CB  . ARG D 1 469 ? -3.801  59.169  87.234  1.00 57.65  ? 469 ARG D CB  1 
ATOM   16201 C CG  . ARG D 1 469 ? -3.464  57.995  88.131  1.00 57.72  ? 469 ARG D CG  1 
ATOM   16202 C CD  . ARG D 1 469 ? -2.153  58.233  88.860  1.00 63.07  ? 469 ARG D CD  1 
ATOM   16203 N NE  . ARG D 1 469 ? -1.959  57.282  89.948  1.00 70.24  ? 469 ARG D NE  1 
ATOM   16204 C CZ  . ARG D 1 469 ? -2.495  57.408  91.154  1.00 71.96  ? 469 ARG D CZ  1 
ATOM   16205 N NH1 . ARG D 1 469 ? -3.244  58.453  91.471  1.00 60.96  ? 469 ARG D NH1 1 
ATOM   16206 N NH2 . ARG D 1 469 ? -2.277  56.460  92.062  1.00 61.66  ? 469 ARG D NH2 1 
ATOM   16207 N N   . SER D 1 470 ? -4.978  60.246  84.304  1.00 54.16  ? 470 SER D N   1 
ATOM   16208 C CA  . SER D 1 470 ? -5.360  61.372  83.459  1.00 58.69  ? 470 SER D CA  1 
ATOM   16209 C C   . SER D 1 470 ? -6.831  61.313  83.067  1.00 57.14  ? 470 SER D C   1 
ATOM   16210 O O   . SER D 1 470 ? -7.515  62.344  83.072  1.00 58.59  ? 470 SER D O   1 
ATOM   16211 C CB  . SER D 1 470 ? -4.472  61.424  82.219  1.00 56.71  ? 470 SER D CB  1 
ATOM   16212 O OG  . SER D 1 470 ? -3.138  61.669  82.619  1.00 69.20  ? 470 SER D OG  1 
ATOM   16213 N N   . PHE D 1 471 ? -7.339  60.119  82.732  1.00 57.02  ? 471 PHE D N   1 
ATOM   16214 C CA  . PHE D 1 471 ? -8.764  59.982  82.444  1.00 56.99  ? 471 PHE D CA  1 
ATOM   16215 C C   . PHE D 1 471 ? -9.603  60.277  83.675  1.00 55.05  ? 471 PHE D C   1 
ATOM   16216 O O   . PHE D 1 471 ? -10.716 60.806  83.559  1.00 53.37  ? 471 PHE D O   1 
ATOM   16217 C CB  . PHE D 1 471 ? -9.084  58.575  81.925  1.00 50.15  ? 471 PHE D CB  1 
ATOM   16218 C CG  . PHE D 1 471 ? -8.389  58.220  80.646  1.00 46.73  ? 471 PHE D CG  1 
ATOM   16219 C CD1 . PHE D 1 471 ? -8.426  59.082  79.566  1.00 58.32  ? 471 PHE D CD1 1 
ATOM   16220 C CD2 . PHE D 1 471 ? -7.715  57.021  80.516  1.00 51.46  ? 471 PHE D CD2 1 
ATOM   16221 C CE1 . PHE D 1 471 ? -7.789  58.764  78.383  1.00 55.56  ? 471 PHE D CE1 1 
ATOM   16222 C CE2 . PHE D 1 471 ? -7.075  56.694  79.332  1.00 56.54  ? 471 PHE D CE2 1 
ATOM   16223 C CZ  . PHE D 1 471 ? -7.114  57.570  78.263  1.00 54.67  ? 471 PHE D CZ  1 
ATOM   16224 N N   . VAL D 1 472 ? -9.086  59.940  84.857  1.00 54.83  ? 472 VAL D N   1 
ATOM   16225 C CA  . VAL D 1 472 ? -9.808  60.198  86.096  1.00 54.55  ? 472 VAL D CA  1 
ATOM   16226 C C   . VAL D 1 472 ? -9.876  61.697  86.373  1.00 55.10  ? 472 VAL D C   1 
ATOM   16227 O O   . VAL D 1 472 ? -10.925 62.221  86.765  1.00 53.16  ? 472 VAL D O   1 
ATOM   16228 C CB  . VAL D 1 472 ? -9.159  59.419  87.256  1.00 57.45  ? 472 VAL D CB  1 
ATOM   16229 C CG1 . VAL D 1 472 ? -9.682  59.906  88.599  1.00 63.54  ? 472 VAL D CG1 1 
ATOM   16230 C CG2 . VAL D 1 472 ? -9.429  57.931  87.095  1.00 50.00  ? 472 VAL D CG2 1 
ATOM   16231 N N   . ARG D 1 473 ? -8.774  62.418  86.163  1.00 55.61  ? 473 ARG D N   1 
ATOM   16232 C CA  . ARG D 1 473 ? -8.824  63.858  86.402  1.00 63.84  ? 473 ARG D CA  1 
ATOM   16233 C C   . ARG D 1 473 ? -9.652  64.565  85.334  1.00 59.68  ? 473 ARG D C   1 
ATOM   16234 O O   . ARG D 1 473 ? -10.375 65.523  85.633  1.00 62.49  ? 473 ARG D O   1 
ATOM   16235 C CB  . ARG D 1 473 ? -7.414  64.447  86.466  1.00 58.88  ? 473 ARG D CB  1 
ATOM   16236 C CG  . ARG D 1 473 ? -7.411  65.951  86.700  1.00 65.97  ? 473 ARG D CG  1 
ATOM   16237 C CD  . ARG D 1 473 ? -6.000  66.523  86.808  1.00 76.87  ? 473 ARG D CD  1 
ATOM   16238 N NE  . ARG D 1 473 ? -5.094  66.051  85.763  1.00 84.66  ? 473 ARG D NE  1 
ATOM   16239 C CZ  . ARG D 1 473 ? -4.466  66.840  84.898  1.00 87.44  ? 473 ARG D CZ  1 
ATOM   16240 N NH1 . ARG D 1 473 ? -4.671  68.148  84.878  1.00 81.21  ? 473 ARG D NH1 1 
ATOM   16241 N NH2 . ARG D 1 473 ? -3.603  66.303  84.036  1.00 80.80  ? 473 ARG D NH2 1 
ATOM   16242 N N   . ARG D 1 474 ? -9.568  64.100  84.086  1.00 56.78  ? 474 ARG D N   1 
ATOM   16243 C CA  . ARG D 1 474 ? -10.281 64.764  83.001  1.00 57.05  ? 474 ARG D CA  1 
ATOM   16244 C C   . ARG D 1 474 ? -11.790 64.614  83.148  1.00 53.35  ? 474 ARG D C   1 
ATOM   16245 O O   . ARG D 1 474 ? -12.542 65.530  82.794  1.00 55.81  ? 474 ARG D O   1 
ATOM   16246 C CB  . ARG D 1 474 ? -9.808  64.208  81.657  1.00 57.33  ? 474 ARG D CB  1 
ATOM   16247 C CG  . ARG D 1 474 ? -10.352 64.924  80.434  1.00 57.23  ? 474 ARG D CG  1 
ATOM   16248 C CD  . ARG D 1 474 ? -10.398 66.437  80.581  1.00 62.73  ? 474 ARG D CD  1 
ATOM   16249 N NE  . ARG D 1 474 ? -10.552 67.078  79.281  1.00 64.88  ? 474 ARG D NE  1 
ATOM   16250 C CZ  . ARG D 1 474 ? -11.709 67.503  78.794  1.00 71.65  ? 474 ARG D CZ  1 
ATOM   16251 N NH1 . ARG D 1 474 ? -12.837 67.367  79.477  1.00 68.14  ? 474 ARG D NH1 1 
ATOM   16252 N NH2 . ARG D 1 474 ? -11.737 68.076  77.593  1.00 66.68  ? 474 ARG D NH2 1 
ATOM   16253 N N   . ALA D 1 475 ? -12.248 63.484  83.686  1.00 50.71  ? 475 ALA D N   1 
ATOM   16254 C CA  . ALA D 1 475 ? -13.674 63.271  83.894  1.00 56.83  ? 475 ALA D CA  1 
ATOM   16255 C C   . ALA D 1 475 ? -14.265 64.215  84.932  1.00 49.16  ? 475 ALA D C   1 
ATOM   16256 O O   . ALA D 1 475 ? -15.491 64.335  85.008  1.00 53.97  ? 475 ALA D O   1 
ATOM   16257 C CB  . ALA D 1 475 ? -13.934 61.821  84.310  1.00 54.38  ? 475 ALA D CB  1 
ATOM   16258 N N   . GLN D 1 476 ? -13.433 64.883  85.724  1.00 49.87  ? 476 GLN D N   1 
ATOM   16259 C CA  . GLN D 1 476 ? -13.888 65.791  86.764  1.00 58.13  ? 476 GLN D CA  1 
ATOM   16260 C C   . GLN D 1 476 ? -13.740 67.255  86.376  1.00 60.62  ? 476 GLN D C   1 
ATOM   16261 O O   . GLN D 1 476 ? -14.023 68.132  87.198  1.00 69.42  ? 476 GLN D O   1 
ATOM   16262 C CB  . GLN D 1 476 ? -13.125 65.519  88.066  1.00 59.27  ? 476 GLN D CB  1 
ATOM   16263 C CG  . GLN D 1 476 ? -13.204 64.074  88.537  1.00 57.45  ? 476 GLN D CG  1 
ATOM   16264 C CD  . GLN D 1 476 ? -12.230 63.771  89.659  1.00 61.80  ? 476 GLN D CD  1 
ATOM   16265 O OE1 . GLN D 1 476 ? -12.527 63.973  90.839  1.00 61.59  ? 476 GLN D OE1 1 
ATOM   16266 N NE2 . GLN D 1 476 ? -11.048 63.293  89.292  1.00 57.13  ? 476 GLN D NE2 1 
ATOM   16267 N N   . GLU D 1 477 ? -13.319 67.540  85.146  1.00 57.57  ? 477 GLU D N   1 
ATOM   16268 C CA  . GLU D 1 477 ? -13.123 68.915  84.716  1.00 58.13  ? 477 GLU D CA  1 
ATOM   16269 C C   . GLU D 1 477 ? -14.446 69.559  84.314  1.00 59.30  ? 477 GLU D C   1 
ATOM   16270 O O   . GLU D 1 477 ? -15.372 68.896  83.834  1.00 59.70  ? 477 GLU D O   1 
ATOM   16271 C CB  . GLU D 1 477 ? -12.129 68.978  83.559  1.00 52.88  ? 477 GLU D CB  1 
ATOM   16272 C CG  . GLU D 1 477 ? -10.739 68.477  83.941  1.00 68.55  ? 477 GLU D CG  1 
ATOM   16273 C CD  . GLU D 1 477 ? -9.768  69.601  84.269  1.00 76.60  ? 477 GLU D CD  1 
ATOM   16274 O OE1 . GLU D 1 477 ? -10.202 70.608  84.868  1.00 83.95  ? 477 GLU D OE1 1 
ATOM   16275 O OE2 . GLU D 1 477 ? -8.565  69.464  83.951  1.00 76.86  ? 477 GLU D OE2 1 
ATOM   16276 N N   . LEU D 1 478 ? -14.519 70.869  84.517  1.00 55.74  ? 478 LEU D N   1 
ATOM   16277 C CA  . LEU D 1 478 ? -15.722 71.634  84.243  1.00 54.33  ? 478 LEU D CA  1 
ATOM   16278 C C   . LEU D 1 478 ? -15.835 71.953  82.760  1.00 54.26  ? 478 LEU D C   1 
ATOM   16279 O O   . LEU D 1 478 ? -14.837 72.043  82.041  1.00 57.96  ? 478 LEU D O   1 
ATOM   16280 C CB  . LEU D 1 478 ? -15.732 72.925  85.059  1.00 56.18  ? 478 LEU D CB  1 
ATOM   16281 C CG  . LEU D 1 478 ? -16.434 72.804  86.414  1.00 66.94  ? 478 LEU D CG  1 
ATOM   16282 C CD1 . LEU D 1 478 ? -16.086 71.503  87.143  1.00 64.35  ? 478 LEU D CD1 1 
ATOM   16283 C CD2 . LEU D 1 478 ? -16.128 74.008  87.280  1.00 70.68  ? 478 LEU D CD2 1 
ATOM   16284 N N   . GLU D 1 479 ? -17.076 72.131  82.305  1.00 60.00  ? 479 GLU D N   1 
ATOM   16285 C CA  . GLU D 1 479 ? -17.312 72.243  80.872  1.00 60.34  ? 479 GLU D CA  1 
ATOM   16286 C C   . GLU D 1 479 ? -16.733 73.527  80.301  1.00 65.15  ? 479 GLU D C   1 
ATOM   16287 O O   . GLU D 1 479 ? -16.373 73.568  79.118  1.00 64.77  ? 479 GLU D O   1 
ATOM   16288 C CB  . GLU D 1 479 ? -18.808 72.159  80.577  1.00 56.53  ? 479 GLU D CB  1 
ATOM   16289 C CG  . GLU D 1 479 ? -19.130 71.578  79.217  1.00 66.30  ? 479 GLU D CG  1 
ATOM   16290 C CD  . GLU D 1 479 ? -20.444 72.097  78.692  1.00 70.80  ? 479 GLU D CD  1 
ATOM   16291 O OE1 . GLU D 1 479 ? -20.609 72.225  77.456  1.00 74.26  ? 479 GLU D OE1 1 
ATOM   16292 O OE2 . GLU D 1 479 ? -21.313 72.394  79.535  1.00 66.93  ? 479 GLU D OE2 1 
ATOM   16293 N N   . HIS D 1 480 ? -16.618 74.571  81.117  1.00 65.32  ? 480 HIS D N   1 
ATOM   16294 C CA  . HIS D 1 480 ? -16.254 75.891  80.635  1.00 62.10  ? 480 HIS D CA  1 
ATOM   16295 C C   . HIS D 1 480 ? -15.096 76.454  81.441  1.00 63.38  ? 480 HIS D C   1 
ATOM   16296 O O   . HIS D 1 480 ? -14.909 76.119  82.613  1.00 59.89  ? 480 HIS D O   1 
ATOM   16297 C CB  . HIS D 1 480 ? -17.445 76.854  80.697  1.00 64.11  ? 480 HIS D CB  1 
ATOM   16298 C CG  . HIS D 1 480 ? -18.630 76.406  79.899  1.00 65.12  ? 480 HIS D CG  1 
ATOM   16299 N ND1 . HIS D 1 480 ? -18.773 76.692  78.558  1.00 67.56  ? 480 HIS D ND1 1 
ATOM   16300 C CD2 . HIS D 1 480 ? -19.740 75.716  80.255  1.00 64.43  ? 480 HIS D CD2 1 
ATOM   16301 C CE1 . HIS D 1 480 ? -19.913 76.187  78.119  1.00 68.31  ? 480 HIS D CE1 1 
ATOM   16302 N NE2 . HIS D 1 480 ? -20.519 75.590  79.129  1.00 68.88  ? 480 HIS D NE2 1 
ATOM   16303 N N   . HIS D 1 481 ? -14.316 77.314  80.788  1.00 64.69  ? 481 HIS D N   1 
ATOM   16304 C CA  . HIS D 1 481 ? -13.272 78.048  81.484  1.00 63.60  ? 481 HIS D CA  1 
ATOM   16305 C C   . HIS D 1 481 ? -13.902 78.930  82.552  1.00 64.70  ? 481 HIS D C   1 
ATOM   16306 O O   . HIS D 1 481 ? -14.998 79.467  82.370  1.00 66.52  ? 481 HIS D O   1 
ATOM   16307 C CB  . HIS D 1 481 ? -12.466 78.893  80.497  1.00 66.27  ? 481 HIS D CB  1 
ATOM   16308 C CG  . HIS D 1 481 ? -11.944 78.124  79.324  1.00 72.67  ? 481 HIS D CG  1 
ATOM   16309 N ND1 . HIS D 1 481 ? -10.648 77.659  79.256  1.00 72.56  ? 481 HIS D ND1 1 
ATOM   16310 C CD2 . HIS D 1 481 ? -12.540 77.740  78.171  1.00 77.78  ? 481 HIS D CD2 1 
ATOM   16311 C CE1 . HIS D 1 481 ? -10.469 77.019  78.115  1.00 71.10  ? 481 HIS D CE1 1 
ATOM   16312 N NE2 . HIS D 1 481 ? -11.602 77.054  77.437  1.00 80.96  ? 481 HIS D NE2 1 
ATOM   16313 N N   . HIS D 1 482 ? -13.212 79.074  83.676  1.00 63.90  ? 482 HIS D N   1 
ATOM   16314 C CA  . HIS D 1 482 ? -13.816 79.784  84.793  1.00 64.83  ? 482 HIS D CA  1 
ATOM   16315 C C   . HIS D 1 482 ? -12.733 80.278  85.733  1.00 68.34  ? 482 HIS D C   1 
ATOM   16316 O O   . HIS D 1 482 ? -11.593 79.805  85.710  1.00 73.65  ? 482 HIS D O   1 
ATOM   16317 C CB  . HIS D 1 482 ? -14.786 78.884  85.550  1.00 62.81  ? 482 HIS D CB  1 
ATOM   16318 C CG  . HIS D 1 482 ? -14.130 77.672  86.121  1.00 61.81  ? 482 HIS D CG  1 
ATOM   16319 N ND1 . HIS D 1 482 ? -14.064 76.476  85.440  1.00 59.88  ? 482 HIS D ND1 1 
ATOM   16320 C CD2 . HIS D 1 482 ? -13.479 77.478  87.291  1.00 58.90  ? 482 HIS D CD2 1 
ATOM   16321 C CE1 . HIS D 1 482 ? -13.412 75.592  86.172  1.00 55.83  ? 482 HIS D CE1 1 
ATOM   16322 N NE2 . HIS D 1 482 ? -13.049 76.173  87.301  1.00 60.52  ? 482 HIS D NE2 1 
ATOM   16323 N N   . HIS D 1 483 ? -13.123 81.234  86.569  1.00 73.39  ? 483 HIS D N   1 
ATOM   16324 C CA  . HIS D 1 483 ? -12.286 81.758  87.634  1.00 72.23  ? 483 HIS D CA  1 
ATOM   16325 C C   . HIS D 1 483 ? -13.181 82.081  88.820  1.00 73.07  ? 483 HIS D C   1 
ATOM   16326 O O   . HIS D 1 483 ? -14.396 82.232  88.682  1.00 69.23  ? 483 HIS D O   1 
ATOM   16327 C CB  . HIS D 1 483 ? -11.488 83.001  87.194  1.00 70.51  ? 483 HIS D CB  1 
ATOM   16328 C CG  . HIS D 1 483 ? -12.269 83.978  86.364  1.00 76.07  ? 483 HIS D CG  1 
ATOM   16329 N ND1 . HIS D 1 483 ? -12.704 85.192  86.854  1.00 85.29  ? 483 HIS D ND1 1 
ATOM   16330 C CD2 . HIS D 1 483 ? -12.673 83.931  85.071  1.00 79.27  ? 483 HIS D CD2 1 
ATOM   16331 C CE1 . HIS D 1 483 ? -13.344 85.848  85.900  1.00 92.58  ? 483 HIS D CE1 1 
ATOM   16332 N NE2 . HIS D 1 483 ? -13.343 85.102  84.810  1.00 90.09  ? 483 HIS D NE2 1 
ATOM   16333 N N   . HIS D 1 484 ? -12.574 82.169  89.993  1.00 74.63  ? 484 HIS D N   1 
ATOM   16334 C CA  . HIS D 1 484 ? -13.327 82.505  91.187  1.00 68.74  ? 484 HIS D CA  1 
ATOM   16335 C C   . HIS D 1 484 ? -13.524 84.012  91.292  1.00 72.28  ? 484 HIS D C   1 
ATOM   16336 O O   . HIS D 1 484 ? -12.673 84.800  90.872  1.00 79.31  ? 484 HIS D O   1 
ATOM   16337 C CB  . HIS D 1 484 ? -12.615 81.974  92.425  1.00 67.60  ? 484 HIS D CB  1 
ATOM   16338 C CG  . HIS D 1 484 ? -13.544 81.487  93.490  1.00 76.91  ? 484 HIS D CG  1 
ATOM   16339 N ND1 . HIS D 1 484 ? -14.089 82.325  94.442  1.00 78.63  ? 484 HIS D ND1 1 
ATOM   16340 C CD2 . HIS D 1 484 ? -14.036 80.251  93.748  1.00 67.09  ? 484 HIS D CD2 1 
ATOM   16341 C CE1 . HIS D 1 484 ? -14.869 81.624  95.245  1.00 71.53  ? 484 HIS D CE1 1 
ATOM   16342 N NE2 . HIS D 1 484 ? -14.856 80.365  94.845  1.00 73.68  ? 484 HIS D NE2 1 
ATOM   16343 N N   . HIS D 1 485 ? -14.669 84.411  91.839  1.00 73.62  ? 485 HIS D N   1 
ATOM   16344 C CA  . HIS D 1 485 ? -14.936 85.825  92.087  1.00 81.02  ? 485 HIS D CA  1 
ATOM   16345 C C   . HIS D 1 485 ? -14.218 86.261  93.358  1.00 88.61  ? 485 HIS D C   1 
ATOM   16346 O O   . HIS D 1 485 ? -13.889 85.428  94.205  1.00 94.16  ? 485 HIS D O   1 
ATOM   16347 C CB  . HIS D 1 485 ? -16.443 86.097  92.201  1.00 78.84  ? 485 HIS D CB  1 
ATOM   16348 C CG  . HIS D 1 485 ? -16.813 87.543  92.045  1.00 83.02  ? 485 HIS D CG  1 
ATOM   16349 N ND1 . HIS D 1 485 ? -17.330 88.057  90.874  1.00 85.08  ? 485 HIS D ND1 1 
ATOM   16350 C CD2 . HIS D 1 485 ? -16.752 88.580  92.914  1.00 85.83  ? 485 HIS D CD2 1 
ATOM   16351 C CE1 . HIS D 1 485 ? -17.563 89.348  91.026  1.00 89.03  ? 485 HIS D CE1 1 
ATOM   16352 N NE2 . HIS D 1 485 ? -17.225 89.690  92.256  1.00 89.50  ? 485 HIS D NE2 1 
HETATM 16353 C C1  . GLC E 2 .   ? 12.750  2.674   0.884   1.00 47.75  ? 1   GLC E C1  1 
HETATM 16354 C C2  . GLC E 2 .   ? 12.821  1.624   1.953   1.00 52.28  ? 1   GLC E C2  1 
HETATM 16355 C C3  . GLC E 2 .   ? 14.084  1.789   2.741   1.00 51.00  ? 1   GLC E C3  1 
HETATM 16356 C C4  . GLC E 2 .   ? 15.288  1.702   1.859   1.00 50.18  ? 1   GLC E C4  1 
HETATM 16357 C C5  . GLC E 2 .   ? 15.163  2.806   0.847   1.00 51.10  ? 1   GLC E C5  1 
HETATM 16358 C C6  . GLC E 2 .   ? 16.145  2.558   -0.246  1.00 49.64  ? 1   GLC E C6  1 
HETATM 16359 O O1  . GLC E 2 .   ? 12.583  3.913   1.508   1.00 55.56  ? 1   GLC E O1  1 
HETATM 16360 O O2  . GLC E 2 .   ? 11.737  1.812   2.830   1.00 53.04  ? 1   GLC E O2  1 
HETATM 16361 O O3  . GLC E 2 .   ? 14.136  0.730   3.656   1.00 50.09  ? 1   GLC E O3  1 
HETATM 16362 O O4  . GLC E 2 .   ? 16.410  1.983   2.670   1.00 51.29  ? 1   GLC E O4  1 
HETATM 16363 O O5  . GLC E 2 .   ? 13.955  2.712   0.155   1.00 54.57  ? 1   GLC E O5  1 
HETATM 16364 O O6  . GLC E 2 .   ? 15.528  1.556   -1.018  1.00 56.98  ? 1   GLC E O6  1 
HETATM 16365 C C1  . GLC E 2 .   ? 17.361  0.942   2.745   1.00 47.22  ? 2   GLC E C1  1 
HETATM 16366 C C2  . GLC E 2 .   ? 18.018  1.101   4.125   1.00 50.03  ? 2   GLC E C2  1 
HETATM 16367 C C3  . GLC E 2 .   ? 19.113  2.160   4.143   1.00 45.64  ? 2   GLC E C3  1 
HETATM 16368 C C4  . GLC E 2 .   ? 20.085  1.698   3.066   1.00 53.49  ? 2   GLC E C4  1 
HETATM 16369 C C5  . GLC E 2 .   ? 19.381  1.853   1.707   1.00 51.00  ? 2   GLC E C5  1 
HETATM 16370 C C6  . GLC E 2 .   ? 20.197  1.440   0.499   1.00 52.41  ? 2   GLC E C6  1 
HETATM 16371 O O2  . GLC E 2 .   ? 17.029  1.399   5.086   1.00 46.35  ? 2   GLC E O2  1 
HETATM 16372 O O3  . GLC E 2 .   ? 19.736  2.168   5.403   1.00 48.18  ? 2   GLC E O3  1 
HETATM 16373 O O4  . GLC E 2 .   ? 21.470  2.026   3.311   1.00 54.40  ? 2   GLC E O4  1 
HETATM 16374 O O5  . GLC E 2 .   ? 18.306  0.932   1.679   1.00 47.37  ? 2   GLC E O5  1 
HETATM 16375 O O6  . GLC E 2 .   ? 19.258  1.065   -0.480  1.00 42.01  ? 2   GLC E O6  1 
HETATM 16376 C C1  . GLC E 2 .   ? 22.228  3.202   2.863   1.00 48.54  ? 3   GLC E C1  1 
HETATM 16377 C C2  . GLC E 2 .   ? 22.482  4.095   4.099   1.00 53.02  ? 3   GLC E C2  1 
HETATM 16378 C C3  . GLC E 2 .   ? 22.564  5.558   3.679   1.00 57.39  ? 3   GLC E C3  1 
HETATM 16379 C C4  . GLC E 2 .   ? 23.392  5.551   2.387   1.00 63.90  ? 3   GLC E C4  1 
HETATM 16380 C C5  . GLC E 2 .   ? 22.509  4.960   1.289   1.00 64.04  ? 3   GLC E C5  1 
HETATM 16381 C C6  . GLC E 2 .   ? 23.366  4.316   0.195   1.00 60.93  ? 3   GLC E C6  1 
HETATM 16382 O O2  . GLC E 2 .   ? 21.519  3.906   5.109   1.00 58.26  ? 3   GLC E O2  1 
HETATM 16383 O O3  . GLC E 2 .   ? 23.178  6.270   4.724   1.00 70.99  ? 3   GLC E O3  1 
HETATM 16384 O O4  . GLC E 2 .   ? 24.180  6.690   2.001   1.00 69.04  ? 3   GLC E O4  1 
HETATM 16385 O O5  . GLC E 2 .   ? 21.601  4.034   1.890   1.00 52.60  ? 3   GLC E O5  1 
HETATM 16386 O O6  . GLC E 2 .   ? 24.679  4.042   0.645   1.00 52.41  ? 3   GLC E O6  1 
HETATM 16387 C C1  . GLC E 2 .   ? 23.596  8.012   1.838   1.00 69.75  ? 4   GLC E C1  1 
HETATM 16388 C C2  . GLC E 2 .   ? 24.123  8.930   2.959   1.00 71.22  ? 4   GLC E C2  1 
HETATM 16389 C C3  . GLC E 2 .   ? 23.114  10.007  3.323   1.00 74.27  ? 4   GLC E C3  1 
HETATM 16390 C C4  . GLC E 2 .   ? 22.304  10.462  2.118   1.00 84.16  ? 4   GLC E C4  1 
HETATM 16391 C C5  . GLC E 2 .   ? 21.678  9.256   1.421   1.00 86.77  ? 4   GLC E C5  1 
HETATM 16392 C C6  . GLC E 2 .   ? 21.942  9.304   -0.073  1.00 84.72  ? 4   GLC E C6  1 
HETATM 16393 O O2  . GLC E 2 .   ? 24.408  8.230   4.147   1.00 60.17  ? 4   GLC E O2  1 
HETATM 16394 O O3  . GLC E 2 .   ? 23.790  11.103  3.901   1.00 77.77  ? 4   GLC E O3  1 
HETATM 16395 O O4  . GLC E 2 .   ? 21.280  11.287  2.622   1.00 98.02  ? 4   GLC E O4  1 
HETATM 16396 O O5  . GLC E 2 .   ? 22.187  8.037   1.927   1.00 78.24  ? 4   GLC E O5  1 
HETATM 16397 O O6  . GLC E 2 .   ? 22.298  10.618  -0.422  1.00 82.49  ? 4   GLC E O6  1 
HETATM 16398 C C1  . GLC E 2 .   ? 20.907  12.363  1.743   1.00 100.86 ? 5   GLC E C1  1 
HETATM 16399 C C2  . GLC E 2 .   ? 20.589  13.568  2.623   1.00 104.54 ? 5   GLC E C2  1 
HETATM 16400 C C3  . GLC E 2 .   ? 20.119  14.745  1.777   1.00 118.66 ? 5   GLC E C3  1 
HETATM 16401 C C4  . GLC E 2 .   ? 18.966  14.321  0.866   1.00 123.89 ? 5   GLC E C4  1 
HETATM 16402 C C5  . GLC E 2 .   ? 19.249  13.015  0.109   1.00 114.02 ? 5   GLC E C5  1 
HETATM 16403 C C6  . GLC E 2 .   ? 20.143  13.212  -1.117  1.00 104.55 ? 5   GLC E C6  1 
HETATM 16404 O O2  . GLC E 2 .   ? 19.592  13.229  3.568   1.00 102.08 ? 5   GLC E O2  1 
HETATM 16405 O O3  . GLC E 2 .   ? 21.195  15.272  1.029   1.00 120.28 ? 5   GLC E O3  1 
HETATM 16406 O O4  . GLC E 2 .   ? 17.785  14.187  1.633   1.00 134.19 ? 5   GLC E O4  1 
HETATM 16407 O O5  . GLC E 2 .   ? 19.775  12.012  0.969   1.00 114.40 ? 5   GLC E O5  1 
HETATM 16408 O O6  . GLC E 2 .   ? 20.090  12.066  -1.940  1.00 92.28  ? 5   GLC E O6  1 
HETATM 16409 C C1  . GLC F 2 .   ? -10.715 34.899  17.871  1.00 57.14  ? 1   GLC F C1  1 
HETATM 16410 C C2  . GLC F 2 .   ? -10.853 36.255  18.519  1.00 55.78  ? 1   GLC F C2  1 
HETATM 16411 C C3  . GLC F 2 .   ? -12.130 36.363  19.287  1.00 49.44  ? 1   GLC F C3  1 
HETATM 16412 C C4  . GLC F 2 .   ? -13.271 36.066  18.362  1.00 48.78  ? 1   GLC F C4  1 
HETATM 16413 C C5  . GLC F 2 .   ? -13.100 34.786  17.563  1.00 60.29  ? 1   GLC F C5  1 
HETATM 16414 C C6  . GLC F 2 .   ? -13.249 34.954  16.071  1.00 49.99  ? 1   GLC F C6  1 
HETATM 16415 O O1  . GLC F 2 .   ? -9.913  34.177  18.760  1.00 62.80  ? 1   GLC F O1  1 
HETATM 16416 O O2  . GLC F 2 .   ? -9.762  36.407  19.405  1.00 53.10  ? 1   GLC F O2  1 
HETATM 16417 O O3  . GLC F 2 .   ? -12.258 37.668  19.786  1.00 48.14  ? 1   GLC F O3  1 
HETATM 16418 O O4  . GLC F 2 .   ? -14.365 35.834  19.207  1.00 50.85  ? 1   GLC F O4  1 
HETATM 16419 O O5  . GLC F 2 .   ? -11.882 34.115  17.837  1.00 62.88  ? 1   GLC F O5  1 
HETATM 16420 O O6  . GLC F 2 .   ? -12.905 36.261  15.689  1.00 49.21  ? 1   GLC F O6  1 
HETATM 16421 C C1  . GLC F 2 .   ? -15.169 36.990  19.245  1.00 56.44  ? 2   GLC F C1  1 
HETATM 16422 C C2  . GLC F 2 .   ? -15.809 37.083  20.650  1.00 54.16  ? 2   GLC F C2  1 
HETATM 16423 C C3  . GLC F 2 .   ? -16.974 36.103  20.796  1.00 51.25  ? 2   GLC F C3  1 
HETATM 16424 C C4  . GLC F 2 .   ? -17.921 36.407  19.639  1.00 55.34  ? 2   GLC F C4  1 
HETATM 16425 C C5  . GLC F 2 .   ? -17.234 36.035  18.318  1.00 49.09  ? 2   GLC F C5  1 
HETATM 16426 C C6  . GLC F 2 .   ? -18.102 36.295  17.093  1.00 53.17  ? 2   GLC F C6  1 
HETATM 16427 O O2  . GLC F 2 .   ? -14.817 36.868  21.635  1.00 82.13  ? 2   GLC F O2  1 
HETATM 16428 O O3  . GLC F 2 .   ? -17.662 36.298  22.009  1.00 52.73  ? 2   GLC F O3  1 
HETATM 16429 O O4  . GLC F 2 .   ? -19.325 36.191  19.915  1.00 61.43  ? 2   GLC F O4  1 
HETATM 16430 O O5  . GLC F 2 .   ? -16.148 36.932  18.198  1.00 41.81  ? 2   GLC F O5  1 
HETATM 16431 O O6  . GLC F 2 .   ? -17.311 36.658  15.975  1.00 40.67  ? 2   GLC F O6  1 
HETATM 16432 C C1  . GLC F 2 .   ? -20.120 34.967  19.762  1.00 48.43  ? 3   GLC F C1  1 
HETATM 16433 C C2  . GLC F 2 .   ? -20.345 34.322  21.155  1.00 52.29  ? 3   GLC F C2  1 
HETATM 16434 C C3  . GLC F 2 .   ? -20.381 32.811  20.993  1.00 57.26  ? 3   GLC F C3  1 
HETATM 16435 C C4  . GLC F 2 .   ? -21.310 32.633  19.796  1.00 65.61  ? 3   GLC F C4  1 
HETATM 16436 C C5  . GLC F 2 .   ? -20.544 33.019  18.525  1.00 57.50  ? 3   GLC F C5  1 
HETATM 16437 C C6  . GLC F 2 .   ? -21.455 33.712  17.515  1.00 54.95  ? 3   GLC F C6  1 
HETATM 16438 O O2  . GLC F 2 .   ? -19.396 34.687  22.129  1.00 54.38  ? 3   GLC F O2  1 
HETATM 16439 O O3  . GLC F 2 .   ? -20.885 32.235  22.172  1.00 68.71  ? 3   GLC F O3  1 
HETATM 16440 O O4  . GLC F 2 .   ? -22.147 31.474  19.792  1.00 78.37  ? 3   GLC F O4  1 
HETATM 16441 O O5  . GLC F 2 .   ? -19.551 33.948  18.936  1.00 58.81  ? 3   GLC F O5  1 
HETATM 16442 O O6  . GLC F 2 .   ? -22.614 32.954  17.230  1.00 57.54  ? 3   GLC F O6  1 
HETATM 16443 C C1  . GLC F 2 .   ? -21.618 30.145  19.527  1.00 70.29  ? 4   GLC F C1  1 
HETATM 16444 C C2  . GLC F 2 .   ? -21.773 29.327  20.823  1.00 70.11  ? 4   GLC F C2  1 
HETATM 16445 C C3  . GLC F 2 .   ? -20.581 28.418  21.043  1.00 77.96  ? 4   GLC F C3  1 
HETATM 16446 C C4  . GLC F 2 .   ? -20.181 27.768  19.728  1.00 81.22  ? 4   GLC F C4  1 
HETATM 16447 C C5  . GLC F 2 .   ? -19.882 28.833  18.677  1.00 77.34  ? 4   GLC F C5  1 
HETATM 16448 C C6  . GLC F 2 .   ? -20.561 28.552  17.335  1.00 74.02  ? 4   GLC F C6  1 
HETATM 16449 O O2  . GLC F 2 .   ? -21.937 30.136  21.961  1.00 71.29  ? 4   GLC F O2  1 
HETATM 16450 O O3  . GLC F 2 .   ? -20.938 27.440  21.992  1.00 82.99  ? 4   GLC F O3  1 
HETATM 16451 O O4  . GLC F 2 .   ? -19.004 27.050  19.964  1.00 90.96  ? 4   GLC F O4  1 
HETATM 16452 O O5  . GLC F 2 .   ? -20.245 30.113  19.166  1.00 78.39  ? 4   GLC F O5  1 
HETATM 16453 O O6  . GLC F 2 .   ? -21.732 27.789  17.495  1.00 80.47  ? 4   GLC F O6  1 
HETATM 16454 C C1  . GLC F 2 .   ? -19.035 25.848  19.188  1.00 100.42 ? 5   GLC F C1  1 
HETATM 16455 C C2  . GLC F 2 .   ? -19.130 24.677  20.155  1.00 108.38 ? 5   GLC F C2  1 
HETATM 16456 C C3  . GLC F 2 .   ? -19.192 23.382  19.359  1.00 118.41 ? 5   GLC F C3  1 
HETATM 16457 C C4  . GLC F 2 .   ? -18.050 23.313  18.341  1.00 118.36 ? 5   GLC F C4  1 
HETATM 16458 C C5  . GLC F 2 .   ? -17.887 24.610  17.541  1.00 115.75 ? 5   GLC F C5  1 
HETATM 16459 C C6  . GLC F 2 .   ? -18.971 24.812  16.481  1.00 113.98 ? 5   GLC F C6  1 
HETATM 16460 O O2  . GLC F 2 .   ? -18.008 24.669  21.013  1.00 112.25 ? 5   GLC F O2  1 
HETATM 16461 O O3  . GLC F 2 .   ? -20.452 23.293  18.728  1.00 119.87 ? 5   GLC F O3  1 
HETATM 16462 O O4  . GLC F 2 .   ? -16.840 23.028  19.011  1.00 122.60 ? 5   GLC F O4  1 
HETATM 16463 O O5  . GLC F 2 .   ? -17.857 25.716  18.421  1.00 116.95 ? 5   GLC F O5  1 
HETATM 16464 O O6  . GLC F 2 .   ? -18.372 25.169  15.253  1.00 111.42 ? 5   GLC F O6  1 
HETATM 16465 C C1  . GLC G 2 .   ? 15.679  -3.499  62.376  1.00 63.93  ? 1   GLC G C1  1 
HETATM 16466 C C2  . GLC G 2 .   ? 15.773  -4.229  61.062  1.00 60.89  ? 1   GLC G C2  1 
HETATM 16467 C C3  . GLC G 2 .   ? 14.425  -4.520  60.473  1.00 65.40  ? 1   GLC G C3  1 
HETATM 16468 C C4  . GLC G 2 .   ? 13.622  -5.245  61.488  1.00 61.98  ? 1   GLC G C4  1 
HETATM 16469 C C5  . GLC G 2 .   ? 13.411  -4.399  62.730  1.00 63.03  ? 1   GLC G C5  1 
HETATM 16470 C C6  . GLC G 2 .   ? 13.401  -5.247  63.978  1.00 60.84  ? 1   GLC G C6  1 
HETATM 16471 O O1  . GLC G 2 .   ? 16.063  -2.198  62.016  1.00 69.67  ? 1   GLC G O1  1 
HETATM 16472 O O2  . GLC G 2 .   ? 16.431  -3.301  60.232  1.00 62.84  ? 1   GLC G O2  1 
HETATM 16473 O O3  . GLC G 2 .   ? 14.482  -5.420  59.385  1.00 68.76  ? 1   GLC G O3  1 
HETATM 16474 O O4  . GLC G 2 .   ? 12.444  -5.426  60.766  1.00 56.04  ? 1   GLC G O4  1 
HETATM 16475 O O5  . GLC G 2 .   ? 14.370  -3.360  62.902  1.00 63.77  ? 1   GLC G O5  1 
HETATM 16476 O O6  . GLC G 2 .   ? 14.468  -6.171  63.919  1.00 51.66  ? 1   GLC G O6  1 
HETATM 16477 C C1  . GLC G 2 .   ? 12.572  -6.681  60.153  1.00 57.56  ? 2   GLC G C1  1 
HETATM 16478 C C2  . GLC G 2 .   ? 11.906  -6.564  58.778  1.00 61.76  ? 2   GLC G C2  1 
HETATM 16479 C C3  . GLC G 2 .   ? 10.407  -6.276  58.892  1.00 55.59  ? 2   GLC G C3  1 
HETATM 16480 C C4  . GLC G 2 .   ? 9.847   -7.452  59.686  1.00 59.05  ? 2   GLC G C4  1 
HETATM 16481 C C5  . GLC G 2 .   ? 10.425  -7.373  61.108  1.00 64.84  ? 2   GLC G C5  1 
HETATM 16482 C C6  . GLC G 2 .   ? 9.930   -8.432  62.089  1.00 70.19  ? 2   GLC G C6  1 
HETATM 16483 O O2  . GLC G 2 .   ? 12.617  -5.595  58.032  1.00 53.40  ? 2   GLC G O2  1 
HETATM 16484 O O3  . GLC G 2 .   ? 9.839   -6.247  57.610  1.00 55.33  ? 2   GLC G O3  1 
HETATM 16485 O O4  . GLC G 2 .   ? 8.474   -7.786  59.400  1.00 69.51  ? 2   GLC G O4  1 
HETATM 16486 O O5  . GLC G 2 .   ? 11.837  -7.551  61.019  1.00 53.22  ? 2   GLC G O5  1 
HETATM 16487 O O6  . GLC G 2 .   ? 10.914  -8.551  63.100  1.00 63.03  ? 2   GLC G O6  1 
HETATM 16488 C C1  . GLC G 2 .   ? 7.255   -7.336  60.085  1.00 64.56  ? 3   GLC G C1  1 
HETATM 16489 C C2  . GLC G 2 .   ? 6.434   -6.571  59.015  1.00 60.46  ? 3   GLC G C2  1 
HETATM 16490 C C3  . GLC G 2 .   ? 5.628   -5.443  59.646  1.00 68.89  ? 3   GLC G C3  1 
HETATM 16491 C C4  . GLC G 2 .   ? 5.063   -6.072  60.916  1.00 77.46  ? 3   GLC G C4  1 
HETATM 16492 C C5  . GLC G 2 .   ? 6.206   -6.232  61.925  1.00 75.37  ? 3   GLC G C5  1 
HETATM 16493 C C6  . GLC G 2 .   ? 5.909   -7.378  62.888  1.00 76.03  ? 3   GLC G C6  1 
HETATM 16494 O O2  . GLC G 2 .   ? 7.240   -6.098  57.965  1.00 58.00  ? 3   GLC G O2  1 
HETATM 16495 O O3  . GLC G 2 .   ? 4.614   -4.999  58.771  1.00 80.23  ? 3   GLC G O3  1 
HETATM 16496 O O4  . GLC G 2 .   ? 3.804   -5.578  61.388  1.00 86.43  ? 3   GLC G O4  1 
HETATM 16497 O O5  . GLC G 2 .   ? 7.424   -6.470  61.214  1.00 70.32  ? 3   GLC G O5  1 
HETATM 16498 O O6  . GLC G 2 .   ? 4.760   -8.084  62.469  1.00 74.45  ? 3   GLC G O6  1 
HETATM 16499 C C1  . GLC G 2 .   ? 3.682   -4.270  62.002  1.00 83.73  ? 4   GLC G C1  1 
HETATM 16500 C C2  . GLC G 2 .   ? 2.551   -3.571  61.246  1.00 82.81  ? 4   GLC G C2  1 
HETATM 16501 C C3  . GLC G 2 .   ? 2.770   -2.069  61.140  1.00 90.10  ? 4   GLC G C3  1 
HETATM 16502 C C4  . GLC G 2 .   ? 3.464   -1.487  62.374  1.00 101.56 ? 4   GLC G C4  1 
HETATM 16503 C C5  . GLC G 2 .   ? 4.698   -2.308  62.752  1.00 97.53  ? 4   GLC G C5  1 
HETATM 16504 C C6  . GLC G 2 .   ? 4.661   -2.754  64.211  1.00 94.59  ? 4   GLC G C6  1 
HETATM 16505 O O2  . GLC G 2 .   ? 2.448   -4.100  59.944  1.00 79.80  ? 4   GLC G O2  1 
HETATM 16506 O O3  . GLC G 2 .   ? 1.514   -1.456  60.932  1.00 81.47  ? 4   GLC G O3  1 
HETATM 16507 O O4  . GLC G 2 .   ? 3.889   -0.178  62.055  1.00 109.82 ? 4   GLC G O4  1 
HETATM 16508 O O5  . GLC G 2 .   ? 4.822   -3.441  61.911  1.00 85.85  ? 4   GLC G O5  1 
HETATM 16509 O O6  . GLC G 2 .   ? 3.903   -1.847  64.981  1.00 102.28 ? 4   GLC G O6  1 
HETATM 16510 C C1  . GLC G 2 .   ? 3.795   0.744   63.162  1.00 116.12 ? 5   GLC G C1  1 
HETATM 16511 C C2  . GLC G 2 .   ? 3.440   2.108   62.578  1.00 121.17 ? 5   GLC G C2  1 
HETATM 16512 C C3  . GLC G 2 .   ? 3.338   3.164   63.675  1.00 124.75 ? 5   GLC G C3  1 
HETATM 16513 C C4  . GLC G 2 .   ? 4.612   3.168   64.519  1.00 123.43 ? 5   GLC G C4  1 
HETATM 16514 C C5  . GLC G 2 .   ? 5.034   1.762   64.961  1.00 123.41 ? 5   GLC G C5  1 
HETATM 16515 C C6  . GLC G 2 .   ? 4.215   1.236   66.140  1.00 118.23 ? 5   GLC G C6  1 
HETATM 16516 O O2  . GLC G 2 .   ? 4.418   2.487   61.628  1.00 121.09 ? 5   GLC G O2  1 
HETATM 16517 O O3  . GLC G 2 .   ? 2.189   2.950   64.471  1.00 130.06 ? 5   GLC G O3  1 
HETATM 16518 O O4  . GLC G 2 .   ? 5.663   3.760   63.785  1.00 128.18 ? 5   GLC G O4  1 
HETATM 16519 O O5  . GLC G 2 .   ? 5.015   0.843   63.876  1.00 122.88 ? 5   GLC G O5  1 
HETATM 16520 O O6  . GLC G 2 .   ? 4.945   0.223   66.800  1.00 115.62 ? 5   GLC G O6  1 
HETATM 16521 C C1  . GLC H 2 .   ? -7.723  40.255  77.900  1.00 60.67  ? 1   GLC H C1  1 
HETATM 16522 C C2  . GLC H 2 .   ? -8.287  40.773  76.587  1.00 68.26  ? 1   GLC H C2  1 
HETATM 16523 C C3  . GLC H 2 .   ? -7.300  41.581  75.784  1.00 63.86  ? 1   GLC H C3  1 
HETATM 16524 C C4  . GLC H 2 .   ? -6.388  42.459  76.607  1.00 59.32  ? 1   GLC H C4  1 
HETATM 16525 C C5  . GLC H 2 .   ? -5.883  41.692  77.800  1.00 61.88  ? 1   GLC H C5  1 
HETATM 16526 C C6  . GLC H 2 .   ? -5.225  42.660  78.718  1.00 63.72  ? 1   GLC H C6  1 
HETATM 16527 O O1  . GLC H 2 .   ? -6.847  39.171  77.695  1.00 70.02  ? 1   GLC H O1  1 
HETATM 16528 O O2  . GLC H 2 .   ? -8.672  39.696  75.748  1.00 63.67  ? 1   GLC H O2  1 
HETATM 16529 O O3  . GLC H 2 .   ? -8.085  42.364  74.915  1.00 54.29  ? 1   GLC H O3  1 
HETATM 16530 O O4  . GLC H 2 .   ? -5.229  42.767  75.848  1.00 63.85  ? 1   GLC H O4  1 
HETATM 16531 O O5  . GLC H 2 .   ? -6.982  41.255  78.539  1.00 54.21  ? 1   GLC H O5  1 
HETATM 16532 O O6  . GLC H 2 .   ? -6.300  43.492  79.105  1.00 65.90  ? 1   GLC H O6  1 
HETATM 16533 C C1  . GLC H 2 .   ? -5.200  44.097  75.347  1.00 60.45  ? 2   GLC H C1  1 
HETATM 16534 C C2  . GLC H 2 .   ? -4.474  44.026  74.000  1.00 58.78  ? 2   GLC H C2  1 
HETATM 16535 C C3  . GLC H 2 .   ? -2.969  43.986  74.162  1.00 52.54  ? 2   GLC H C3  1 
HETATM 16536 C C4  . GLC H 2 .   ? -2.620  45.261  74.907  1.00 60.82  ? 2   GLC H C4  1 
HETATM 16537 C C5  . GLC H 2 .   ? -3.186  45.103  76.323  1.00 55.73  ? 2   GLC H C5  1 
HETATM 16538 C C6  . GLC H 2 .   ? -2.885  46.260  77.257  1.00 58.07  ? 2   GLC H C6  1 
HETATM 16539 O O2  . GLC H 2 .   ? -4.879  42.881  73.287  1.00 59.34  ? 2   GLC H O2  1 
HETATM 16540 O O3  . GLC H 2 .   ? -2.405  43.984  72.880  1.00 61.89  ? 2   GLC H O3  1 
HETATM 16541 O O4  . GLC H 2 .   ? -1.303  45.766  74.607  1.00 68.09  ? 2   GLC H O4  1 
HETATM 16542 O O5  . GLC H 2 .   ? -4.598  45.065  76.210  1.00 56.80  ? 2   GLC H O5  1 
HETATM 16543 O O6  . GLC H 2 .   ? -3.874  46.254  78.256  1.00 54.21  ? 2   GLC H O6  1 
HETATM 16544 C C1  . GLC H 2 .   ? -0.047  45.528  75.334  1.00 60.73  ? 3   GLC H C1  1 
HETATM 16545 C C2  . GLC H 2 .   ? 0.863   44.751  74.354  1.00 64.31  ? 3   GLC H C2  1 
HETATM 16546 C C3  . GLC H 2 .   ? 1.802   43.826  75.107  1.00 67.34  ? 3   GLC H C3  1 
HETATM 16547 C C4  . GLC H 2 .   ? 2.283   44.655  76.288  1.00 71.78  ? 3   GLC H C4  1 
HETATM 16548 C C5  . GLC H 2 .   ? 1.124   44.774  77.269  1.00 68.11  ? 3   GLC H C5  1 
HETATM 16549 C C6  . GLC H 2 .   ? 1.275   46.049  78.088  1.00 64.78  ? 3   GLC H C6  1 
HETATM 16550 O O2  . GLC H 2 .   ? 0.139   44.021  73.396  1.00 63.92  ? 3   GLC H O2  1 
HETATM 16551 O O3  . GLC H 2 .   ? 2.854   43.461  74.257  1.00 77.03  ? 3   GLC H O3  1 
HETATM 16552 O O4  . GLC H 2 .   ? 3.560   44.358  76.852  1.00 80.91  ? 3   GLC H O4  1 
HETATM 16553 O O5  . GLC H 2 .   ? -0.106  44.762  76.542  1.00 65.49  ? 3   GLC H O5  1 
HETATM 16554 O O6  . GLC H 2 .   ? 2.355   46.829  77.624  1.00 64.75  ? 3   GLC H O6  1 
HETATM 16555 C C1  . GLC H 2 .   ? 3.859   43.065  77.462  1.00 84.28  ? 4   GLC H C1  1 
HETATM 16556 C C2  . GLC H 2 .   ? 4.971   42.411  76.612  1.00 84.31  ? 4   GLC H C2  1 
HETATM 16557 C C3  . GLC H 2 .   ? 4.964   40.898  76.729  1.00 90.74  ? 4   GLC H C3  1 
HETATM 16558 C C4  . GLC H 2 .   ? 4.411   40.405  78.060  1.00 102.34 ? 4   GLC H C4  1 
HETATM 16559 C C5  . GLC H 2 .   ? 3.093   41.089  78.431  1.00 94.37  ? 4   GLC H C5  1 
HETATM 16560 C C6  . GLC H 2 .   ? 3.128   41.645  79.854  1.00 94.28  ? 4   GLC H C6  1 
HETATM 16561 O O2  . GLC H 2 .   ? 4.854   42.699  75.236  1.00 75.68  ? 4   GLC H O2  1 
HETATM 16562 O O3  . GLC H 2 .   ? 6.282   40.422  76.547  1.00 95.77  ? 4   GLC H O3  1 
HETATM 16563 O O4  . GLC H 2 .   ? 4.174   39.025  77.891  1.00 108.97 ? 4   GLC H O4  1 
HETATM 16564 O O5  . GLC H 2 .   ? 2.784   42.137  77.526  1.00 86.21  ? 4   GLC H O5  1 
HETATM 16565 O O6  . GLC H 2 .   ? 4.190   41.087  80.598  1.00 99.33  ? 4   GLC H O6  1 
HETATM 16566 C C1  . GLC H 2 .   ? 4.519   38.284  79.078  1.00 115.55 ? 5   GLC H C1  1 
HETATM 16567 C C2  . GLC H 2 .   ? 5.061   36.939  78.598  1.00 120.93 ? 5   GLC H C2  1 
HETATM 16568 C C3  . GLC H 2 .   ? 5.393   36.037  79.783  1.00 131.86 ? 5   GLC H C3  1 
HETATM 16569 C C4  . GLC H 2 .   ? 4.179   35.934  80.702  1.00 132.45 ? 5   GLC H C4  1 
HETATM 16570 C C5  . GLC H 2 .   ? 3.595   37.303  81.059  1.00 123.53 ? 5   GLC H C5  1 
HETATM 16571 C C6  . GLC H 2 .   ? 4.441   38.065  82.076  1.00 120.93 ? 5   GLC H C6  1 
HETATM 16572 O O2  . GLC H 2 .   ? 4.120   36.309  77.756  1.00 108.59 ? 5   GLC H O2  1 
HETATM 16573 O O3  . GLC H 2 .   ? 6.529   36.509  80.478  1.00 130.95 ? 5   GLC H O3  1 
HETATM 16574 O O4  . GLC H 2 .   ? 3.192   35.157  80.060  1.00 137.70 ? 5   GLC H O4  1 
HETATM 16575 O O5  . GLC H 2 .   ? 3.376   38.084  79.893  1.00 117.80 ? 5   GLC H O5  1 
HETATM 16576 O O6  . GLC H 2 .   ? 3.686   39.135  82.596  1.00 122.59 ? 5   GLC H O6  1 
HETATM 16577 O O   . HOH I 3 .   ? -0.211  2.859   24.617  1.00 36.59  ? 501 HOH A O   1 
HETATM 16578 O O   . HOH I 3 .   ? 10.639  2.660   18.762  1.00 52.12  ? 502 HOH A O   1 
HETATM 16579 O O   . HOH I 3 .   ? 7.341   -3.147  29.305  1.00 62.57  ? 503 HOH A O   1 
HETATM 16580 O O   . HOH I 3 .   ? 52.797  3.798   11.493  1.00 53.83  ? 504 HOH A O   1 
HETATM 16581 O O   . HOH I 3 .   ? -1.488  6.336   26.407  1.00 65.66  ? 505 HOH A O   1 
HETATM 16582 O O   . HOH I 3 .   ? -9.408  2.655   -7.548  1.00 53.83  ? 506 HOH A O   1 
HETATM 16583 O O   . HOH I 3 .   ? -5.361  -12.111 11.672  1.00 39.75  ? 507 HOH A O   1 
HETATM 16584 O O   . HOH I 3 .   ? 8.233   10.606  -8.495  1.00 53.83  ? 508 HOH A O   1 
HETATM 16585 O O   . HOH I 3 .   ? 8.099   8.387   -7.984  1.00 50.70  ? 509 HOH A O   1 
HETATM 16586 O O   . HOH I 3 .   ? -16.424 -7.413  -2.486  1.00 55.74  ? 510 HOH A O   1 
HETATM 16587 O O   . HOH I 3 .   ? 16.900  0.983   23.124  1.00 43.51  ? 511 HOH A O   1 
HETATM 16588 O O   . HOH I 3 .   ? 9.921   1.476   -25.895 1.00 73.18  ? 512 HOH A O   1 
HETATM 16589 O O   . HOH I 3 .   ? 39.428  -5.661  24.286  1.00 54.74  ? 513 HOH A O   1 
HETATM 16590 O O   . HOH I 3 .   ? 19.647  8.244   5.251   1.00 57.35  ? 514 HOH A O   1 
HETATM 16591 O O   . HOH I 3 .   ? -5.235  11.526  29.695  1.00 61.62  ? 515 HOH A O   1 
HETATM 16592 O O   . HOH I 3 .   ? 26.790  -23.698 -10.808 1.00 59.45  ? 516 HOH A O   1 
HETATM 16593 O O   . HOH I 3 .   ? -6.420  13.373  6.261   1.00 43.73  ? 517 HOH A O   1 
HETATM 16594 O O   . HOH I 3 .   ? 33.819  0.304   1.487   1.00 53.83  ? 518 HOH A O   1 
HETATM 16595 O O   . HOH I 3 .   ? 29.208  10.752  -2.602  1.00 71.17  ? 519 HOH A O   1 
HETATM 16596 O O   . HOH I 3 .   ? 33.270  2.871   1.602   1.00 53.83  ? 520 HOH A O   1 
HETATM 16597 O O   . HOH I 3 .   ? 31.412  10.474  -2.645  1.00 51.96  ? 521 HOH A O   1 
HETATM 16598 O O   . HOH J 3 .   ? -1.452  30.730  4.209   1.00 53.83  ? 501 HOH B O   1 
HETATM 16599 O O   . HOH J 3 .   ? 7.007   37.112  6.993   1.00 52.04  ? 502 HOH B O   1 
HETATM 16600 O O   . HOH J 3 .   ? 17.557  43.194  8.495   1.00 52.30  ? 503 HOH B O   1 
HETATM 16601 O O   . HOH J 3 .   ? -9.116  36.553  -8.834  1.00 73.78  ? 504 HOH B O   1 
HETATM 16602 O O   . HOH J 3 .   ? -42.295 47.577  35.225  1.00 52.01  ? 505 HOH B O   1 
HETATM 16603 O O   . HOH J 3 .   ? -2.947  59.711  8.333   1.00 57.06  ? 506 HOH B O   1 
HETATM 16604 O O   . HOH J 3 .   ? -37.221 40.249  18.059  1.00 55.73  ? 507 HOH B O   1 
HETATM 16605 O O   . HOH J 3 .   ? -23.829 50.377  12.227  1.00 58.95  ? 508 HOH B O   1 
HETATM 16606 O O   . HOH J 3 .   ? 16.831  18.196  20.783  1.00 41.69  ? 509 HOH B O   1 
HETATM 16607 O O   . HOH J 3 .   ? 18.644  27.329  28.937  1.00 46.28  ? 510 HOH B O   1 
HETATM 16608 O O   . HOH K 3 .   ? -21.577 -4.460  47.697  1.00 58.84  ? 501 HOH C O   1 
HETATM 16609 O O   . HOH K 3 .   ? 18.471  -46.688 77.973  1.00 53.34  ? 502 HOH C O   1 
HETATM 16610 O O   . HOH K 3 .   ? 7.321   -6.515  41.103  1.00 58.64  ? 503 HOH C O   1 
HETATM 16611 O O   . HOH K 3 .   ? 1.796   -1.704  46.513  1.00 60.07  ? 504 HOH C O   1 
HETATM 16612 O O   . HOH K 3 .   ? 31.892  8.987   57.308  1.00 46.02  ? 505 HOH C O   1 
HETATM 16613 O O   . HOH K 3 .   ? 30.736  -13.580 82.334  1.00 53.83  ? 506 HOH C O   1 
HETATM 16614 O O   . HOH K 3 .   ? 16.093  -35.162 67.679  1.00 54.09  ? 507 HOH C O   1 
HETATM 16615 O O   . HOH K 3 .   ? 0.466   5.369   63.605  1.00 61.07  ? 508 HOH C O   1 
HETATM 16616 O O   . HOH L 3 .   ? -19.611 11.415  75.984  1.00 47.06  ? 501 HOH D O   1 
HETATM 16617 O O   . HOH L 3 .   ? 19.676  38.675  55.236  1.00 66.09  ? 502 HOH D O   1 
HETATM 16618 O O   . HOH L 3 .   ? 3.601   55.663  71.145  1.00 43.36  ? 503 HOH D O   1 
HETATM 16619 O O   . HOH L 3 .   ? -22.994 50.048  90.323  1.00 57.13  ? 504 HOH D O   1 
HETATM 16620 O O   . HOH L 3 .   ? -1.984  59.445  63.157  1.00 64.15  ? 505 HOH D O   1 
HETATM 16621 O O   . HOH L 3 .   ? -4.711  60.625  91.096  1.00 60.56  ? 506 HOH D O   1 
HETATM 16622 O O   . HOH L 3 .   ? -8.259  30.410  84.306  1.00 59.36  ? 507 HOH D O   1 
HETATM 16623 O O   . HOH L 3 .   ? -24.817 57.165  92.874  1.00 57.78  ? 508 HOH D O   1 
HETATM 16624 O O   . HOH L 3 .   ? -7.648  31.621  79.950  1.00 55.95  ? 509 HOH D O   1 
HETATM 16625 O O   . HOH L 3 .   ? -21.858 45.818  56.662  1.00 55.78  ? 510 HOH D O   1 
HETATM 16626 O O   . HOH L 3 .   ? -35.954 44.223  74.233  1.00 49.02  ? 511 HOH D O   1 
HETATM 16627 O O   . HOH L 3 .   ? -37.407 44.940  75.979  1.00 47.63  ? 512 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   . MET A 1   ? 0.9942 1.5333 1.1454 0.0281  0.1416  -0.1060 1   MET A N   
2     C CA  . MET A 1   ? 0.8805 1.3775 1.0367 0.0398  0.1328  -0.1152 1   MET A CA  
3     C C   . MET A 1   ? 0.7446 1.2045 0.9053 0.0347  0.1219  -0.0980 1   MET A C   
4     O O   . MET A 1   ? 0.9689 1.4131 1.1107 0.0188  0.1189  -0.0798 1   MET A O   
5     C CB  . MET A 1   ? 0.6427 1.1215 0.7726 0.0366  0.1326  -0.1204 1   MET A CB  
6     C CG  . MET A 1   ? 0.8294 1.2593 0.9593 0.0423  0.1222  -0.1227 1   MET A CG  
7     S SD  . MET A 1   ? 1.0113 1.4156 1.1072 0.0319  0.1194  -0.1179 1   MET A SD  
8     C CE  . MET A 1   ? 0.8441 1.2533 0.9439 0.0479  0.1217  -0.1483 1   MET A CE  
9     N N   . LYS A 2   ? 0.7113 1.1580 0.8974 0.0483  0.1159  -0.1035 2   LYS A N   
10    C CA  . LYS A 2   ? 0.6334 1.0439 0.8223 0.0446  0.1050  -0.0887 2   LYS A CA  
11    C C   . LYS A 2   ? 0.5957 0.9657 0.7643 0.0411  0.0995  -0.0876 2   LYS A C   
12    O O   . LYS A 2   ? 0.6282 0.9859 0.7987 0.0518  0.0991  -0.1032 2   LYS A O   
13    C CB  . LYS A 2   ? 0.5749 0.9807 0.7957 0.0606  0.0993  -0.0940 2   LYS A CB  
14    C CG  . LYS A 2   ? 0.4625 0.8427 0.6874 0.0550  0.0888  -0.0756 2   LYS A CG  
15    C CD  . LYS A 2   ? 0.6096 0.9996 0.8677 0.0685  0.0842  -0.0761 2   LYS A CD  
16    C CE  . LYS A 2   ? 0.6847 1.0522 0.9615 0.0867  0.0798  -0.0898 2   LYS A CE  
17    N NZ  . LYS A 2   ? 0.7390 1.1300 1.0311 0.1019  0.0878  -0.1132 2   LYS A NZ  
18    N N   . LYS A 3   ? 0.5822 0.9322 0.7324 0.0262  0.0953  -0.0700 3   LYS A N   
19    C CA  . LYS A 3   ? 0.5479 0.8629 0.6780 0.0216  0.0906  -0.0674 3   LYS A CA  
20    C C   . LYS A 3   ? 0.5534 0.8354 0.6884 0.0204  0.0806  -0.0565 3   LYS A C   
21    O O   . LYS A 3   ? 0.4996 0.7871 0.6473 0.0185  0.0774  -0.0470 3   LYS A O   
22    C CB  . LYS A 3   ? 0.5252 0.8437 0.6281 0.0056  0.0942  -0.0566 3   LYS A CB  
23    C CG  . LYS A 3   ? 0.6014 0.9505 0.6947 0.0061  0.1036  -0.0666 3   LYS A CG  
24    C CD  . LYS A 3   ? 0.6098 0.9605 0.6773 -0.0101 0.1060  -0.0525 3   LYS A CD  
25    C CE  . LYS A 3   ? 0.6991 1.0193 0.7474 -0.0115 0.1014  -0.0524 3   LYS A CE  
26    N NZ  . LYS A 3   ? 0.8828 1.2181 0.9225 -0.0047 0.1061  -0.0680 3   LYS A NZ  
27    N N   . LEU A 4   ? 0.5553 0.8057 0.6804 0.0214  0.0757  -0.0583 4   LEU A N   
28    C CA  . LEU A 4   ? 0.5256 0.7448 0.6493 0.0177  0.0670  -0.0470 4   LEU A CA  
29    C C   . LEU A 4   ? 0.4515 0.6545 0.5488 0.0043  0.0664  -0.0377 4   LEU A C   
30    O O   . LEU A 4   ? 0.5097 0.7074 0.5925 0.0041  0.0687  -0.0440 4   LEU A O   
31    C CB  . LEU A 4   ? 0.5574 0.7529 0.6934 0.0293  0.0614  -0.0556 4   LEU A CB  
32    C CG  . LEU A 4   ? 0.5804 0.7473 0.7184 0.0266  0.0524  -0.0436 4   LEU A CG  
33    C CD1 . LEU A 4   ? 0.5834 0.7369 0.7447 0.0397  0.0472  -0.0499 4   LEU A CD1 
34    C CD2 . LEU A 4   ? 0.4641 0.6067 0.5790 0.0171  0.0500  -0.0380 4   LEU A CD2 
35    N N   . PHE A 5   ? 0.5000 0.6957 0.5918 -0.0063 0.0630  -0.0234 5   PHE A N   
36    C CA  . PHE A 5   ? 0.5416 0.7211 0.6113 -0.0186 0.0620  -0.0142 5   PHE A CA  
37    C C   . PHE A 5   ? 0.5424 0.6903 0.6085 -0.0178 0.0548  -0.0114 5   PHE A C   
38    O O   . PHE A 5   ? 0.5274 0.6681 0.6028 -0.0179 0.0496  -0.0055 5   PHE A O   
39    C CB  . PHE A 5   ? 0.4491 0.6397 0.5154 -0.0314 0.0628  -0.0022 5   PHE A CB  
40    C CG  . PHE A 5   ? 0.5036 0.7276 0.5734 -0.0340 0.0703  -0.0033 5   PHE A CG  
41    C CD1 . PHE A 5   ? 0.5230 0.7571 0.5788 -0.0371 0.0764  -0.0054 5   PHE A CD1 
42    C CD2 . PHE A 5   ? 0.5339 0.7818 0.6211 -0.0337 0.0712  -0.0014 5   PHE A CD2 
43    C CE1 . PHE A 5   ? 0.4552 0.7232 0.5137 -0.0403 0.0839  -0.0056 5   PHE A CE1 
44    C CE2 . PHE A 5   ? 0.5368 0.8184 0.6280 -0.0366 0.0786  -0.0023 5   PHE A CE2 
45    C CZ  . PHE A 5   ? 0.4522 0.7440 0.5287 -0.0402 0.0852  -0.0043 5   PHE A CZ  
46    N N   . LEU A 6   ? 0.5179 0.6499 0.5706 -0.0174 0.0546  -0.0153 6   LEU A N   
47    C CA  . LEU A 6   ? 0.5958 0.7004 0.6450 -0.0164 0.0486  -0.0139 6   LEU A CA  
48    C C   . LEU A 6   ? 0.5420 0.6324 0.5728 -0.0272 0.0473  -0.0047 6   LEU A C   
49    O O   . LEU A 6   ? 0.5989 0.6928 0.6158 -0.0318 0.0507  -0.0037 6   LEU A O   
50    C CB  . LEU A 6   ? 0.5176 0.6149 0.5675 -0.0078 0.0486  -0.0261 6   LEU A CB  
51    C CG  . LEU A 6   ? 0.4912 0.5642 0.5457 -0.0045 0.0423  -0.0263 6   LEU A CG  
52    C CD1 . LEU A 6   ? 0.4870 0.5580 0.5596 -0.0013 0.0381  -0.0210 6   LEU A CD1 
53    C CD2 . LEU A 6   ? 0.5197 0.5885 0.5776 0.0036  0.0424  -0.0402 6   LEU A CD2 
54    N N   . VAL A 7   ? 0.4831 0.5582 0.5142 -0.0308 0.0423  0.0021  7   VAL A N   
55    C CA  . VAL A 7   ? 0.5425 0.6021 0.5587 -0.0396 0.0405  0.0089  7   VAL A CA  
56    C C   . VAL A 7   ? 0.5484 0.5877 0.5632 -0.0363 0.0360  0.0076  7   VAL A C   
57    O O   . VAL A 7   ? 0.5039 0.5397 0.5290 -0.0336 0.0323  0.0091  7   VAL A O   
58    C CB  . VAL A 7   ? 0.5121 0.5754 0.5289 -0.0486 0.0392  0.0169  7   VAL A CB  
59    C CG1 . VAL A 7   ? 0.5154 0.5596 0.5195 -0.0559 0.0366  0.0213  7   VAL A CG1 
60    C CG2 . VAL A 7   ? 0.4870 0.5700 0.5039 -0.0541 0.0439  0.0192  7   VAL A CG2 
61    N N   . PHE A 8   ? 0.5272 0.5549 0.5299 -0.0369 0.0361  0.0060  8   PHE A N   
62    C CA  . PHE A 8   ? 0.5594 0.5697 0.5597 -0.0352 0.0323  0.0053  8   PHE A CA  
63    C C   . PHE A 8   ? 0.5404 0.5396 0.5302 -0.0426 0.0309  0.0116  8   PHE A C   
64    O O   . PHE A 8   ? 0.5737 0.5715 0.5533 -0.0471 0.0328  0.0142  8   PHE A O   
65    C CB  . PHE A 8   ? 0.5187 0.5253 0.5141 -0.0303 0.0328  -0.0016 8   PHE A CB  
66    C CG  . PHE A 8   ? 0.5015 0.5132 0.5094 -0.0221 0.0327  -0.0106 8   PHE A CG  
67    C CD1 . PHE A 8   ? 0.5009 0.5034 0.5212 -0.0185 0.0287  -0.0114 8   PHE A CD1 
68    C CD2 . PHE A 8   ? 0.4537 0.4797 0.4616 -0.0182 0.0365  -0.0185 8   PHE A CD2 
69    C CE1 . PHE A 8   ? 0.5150 0.5192 0.5493 -0.0109 0.0280  -0.0201 8   PHE A CE1 
70    C CE2 . PHE A 8   ? 0.4993 0.5291 0.5202 -0.0100 0.0363  -0.0292 8   PHE A CE2 
71    C CZ  . PHE A 8   ? 0.5515 0.5686 0.5864 -0.0062 0.0318  -0.0302 8   PHE A CZ  
72    N N   . TRP A 9   ? 0.5542 0.5462 0.5470 -0.0440 0.0276  0.0141  9   TRP A N   
73    C CA  . TRP A 9   ? 0.6201 0.6024 0.6042 -0.0502 0.0264  0.0174  9   TRP A CA  
74    C C   . TRP A 9   ? 0.5766 0.5483 0.5601 -0.0474 0.0237  0.0159  9   TRP A C   
75    O O   . TRP A 9   ? 0.6620 0.6357 0.6529 -0.0464 0.0214  0.0175  9   TRP A O   
76    C CB  . TRP A 9   ? 0.5108 0.5003 0.4980 -0.0563 0.0253  0.0213  9   TRP A CB  
77    C CG  . TRP A 9   ? 0.5524 0.5342 0.5305 -0.0640 0.0252  0.0225  9   TRP A CG  
78    C CD1 . TRP A 9   ? 0.5772 0.5449 0.5465 -0.0645 0.0254  0.0211  9   TRP A CD1 
79    C CD2 . TRP A 9   ? 0.5839 0.5715 0.5625 -0.0719 0.0243  0.0243  9   TRP A CD2 
80    N NE1 . TRP A 9   ? 0.4953 0.4576 0.4604 -0.0718 0.0248  0.0213  9   TRP A NE1 
81    C CE2 . TRP A 9   ? 0.5052 0.4797 0.4754 -0.0770 0.0241  0.0228  9   TRP A CE2 
82    C CE3 . TRP A 9   ? 0.5299 0.5331 0.5163 -0.0750 0.0231  0.0268  9   TRP A CE3 
83    C CZ2 . TRP A 9   ? 0.5692 0.5446 0.5381 -0.0858 0.0230  0.0222  9   TRP A CZ2 
84    C CZ3 . TRP A 9   ? 0.5665 0.5728 0.5507 -0.0841 0.0218  0.0272  9   TRP A CZ3 
85    C CH2 . TRP A 9   ? 0.5710 0.5629 0.5464 -0.0898 0.0218  0.0242  9   TRP A CH2 
86    N N   . TRP A 10  ? 0.5275 0.4898 0.5031 -0.0463 0.0240  0.0139  10  TRP A N   
87    C CA  . TRP A 10  ? 0.5567 0.5111 0.5321 -0.0436 0.0219  0.0121  10  TRP A CA  
88    C C   . TRP A 10  ? 0.5735 0.5216 0.5431 -0.0477 0.0213  0.0132  10  TRP A C   
89    O O   . TRP A 10  ? 0.6121 0.5537 0.5745 -0.0496 0.0222  0.0132  10  TRP A O   
90    C CB  . TRP A 10  ? 0.5819 0.5324 0.5534 -0.0393 0.0220  0.0086  10  TRP A CB  
91    C CG  . TRP A 10  ? 0.5320 0.4893 0.5085 -0.0348 0.0226  0.0044  10  TRP A CG  
92    C CD1 . TRP A 10  ? 0.5226 0.4864 0.4943 -0.0337 0.0248  0.0026  10  TRP A CD1 
93    C CD2 . TRP A 10  ? 0.5310 0.4896 0.5189 -0.0310 0.0209  0.0007  10  TRP A CD2 
94    N NE1 . TRP A 10  ? 0.4671 0.4375 0.4460 -0.0288 0.0250  -0.0040 10  TRP A NE1 
95    C CE2 . TRP A 10  ? 0.5016 0.4671 0.4915 -0.0269 0.0223  -0.0054 10  TRP A CE2 
96    C CE3 . TRP A 10  ? 0.5974 0.5524 0.5946 -0.0309 0.0182  0.0025  10  TRP A CE3 
97    C CZ2 . TRP A 10  ? 0.5056 0.4721 0.5077 -0.0222 0.0209  -0.0117 10  TRP A CZ2 
98    C CZ3 . TRP A 10  ? 0.5099 0.4649 0.5196 -0.0269 0.0165  -0.0013 10  TRP A CZ3 
99    C CH2 . TRP A 10  ? 0.5421 0.5016 0.5547 -0.0222 0.0177  -0.0091 10  TRP A CH2 
100   N N   . HIS A 11  ? 0.5540 0.5044 0.5272 -0.0489 0.0198  0.0141  11  HIS A N   
101   C CA  . HIS A 11  ? 0.6138 0.5618 0.5820 -0.0526 0.0196  0.0131  11  HIS A CA  
102   C C   . HIS A 11  ? 0.5581 0.5008 0.5248 -0.0492 0.0194  0.0102  11  HIS A C   
103   O O   . HIS A 11  ? 0.5915 0.5371 0.5637 -0.0467 0.0183  0.0110  11  HIS A O   
104   C CB  . HIS A 11  ? 0.5484 0.5067 0.5200 -0.0566 0.0183  0.0160  11  HIS A CB  
105   C CG  . HIS A 11  ? 0.5489 0.5086 0.5154 -0.0597 0.0183  0.0133  11  HIS A CG  
106   N ND1 . HIS A 11  ? 0.5844 0.5388 0.5441 -0.0629 0.0194  0.0081  11  HIS A ND1 
107   C CD2 . HIS A 11  ? 0.5056 0.4726 0.4733 -0.0603 0.0177  0.0145  11  HIS A CD2 
108   C CE1 . HIS A 11  ? 0.5827 0.5417 0.5396 -0.0645 0.0196  0.0044  11  HIS A CE1 
109   N NE2 . HIS A 11  ? 0.6021 0.5704 0.5631 -0.0633 0.0188  0.0088  11  HIS A NE2 
110   N N   . MET A 12  ? 0.4875 0.4226 0.4483 -0.0492 0.0201  0.0069  12  MET A N   
111   C CA  . MET A 12  ? 0.6096 0.5411 0.5699 -0.0452 0.0199  0.0038  12  MET A CA  
112   C C   . MET A 12  ? 0.5472 0.4794 0.5051 -0.0473 0.0208  -0.0006 12  MET A C   
113   O O   . MET A 12  ? 0.5101 0.4359 0.4643 -0.0499 0.0213  -0.0033 12  MET A O   
114   C CB  . MET A 12  ? 0.5896 0.5119 0.5469 -0.0411 0.0195  0.0035  12  MET A CB  
115   C CG  . MET A 12  ? 0.5737 0.4974 0.5306 -0.0405 0.0194  0.0067  12  MET A CG  
116   S SD  . MET A 12  ? 0.9406 0.8712 0.9038 -0.0365 0.0181  0.0055  12  MET A SD  
117   C CE  . MET A 12  ? 0.7178 0.6470 0.6757 -0.0329 0.0176  0.0055  12  MET A CE  
118   N N   . HIS A 13  ? 0.5460 0.4865 0.5064 -0.0467 0.0210  -0.0020 13  HIS A N   
119   C CA  . HIS A 13  ? 0.5473 0.4925 0.5051 -0.0484 0.0225  -0.0078 13  HIS A CA  
120   C C   . HIS A 13  ? 0.5157 0.4692 0.4770 -0.0453 0.0233  -0.0096 13  HIS A C   
121   O O   . HIS A 13  ? 0.5363 0.4966 0.5024 -0.0455 0.0225  -0.0043 13  HIS A O   
122   C CB  . HIS A 13  ? 0.5239 0.4801 0.4797 -0.0551 0.0225  -0.0063 13  HIS A CB  
123   C CG  . HIS A 13  ? 0.4899 0.4572 0.4426 -0.0574 0.0241  -0.0126 13  HIS A CG  
124   N ND1 . HIS A 13  ? 0.5023 0.4635 0.4521 -0.0559 0.0256  -0.0229 13  HIS A ND1 
125   C CD2 . HIS A 13  ? 0.4676 0.4529 0.4200 -0.0610 0.0246  -0.0102 13  HIS A CD2 
126   C CE1 . HIS A 13  ? 0.5425 0.5189 0.4898 -0.0581 0.0274  -0.0286 13  HIS A CE1 
127   N NE2 . HIS A 13  ? 0.6024 0.5948 0.5504 -0.0617 0.0269  -0.0202 13  HIS A NE2 
128   N N   . GLN A 14  ? 0.4767 0.4296 0.4369 -0.0424 0.0250  -0.0175 14  GLN A N   
129   C CA  . GLN A 14  ? 0.5312 0.4978 0.4948 -0.0407 0.0268  -0.0206 14  GLN A CA  
130   C C   . GLN A 14  ? 0.5680 0.5413 0.5280 -0.0417 0.0294  -0.0305 14  GLN A C   
131   O O   . GLN A 14  ? 0.6644 0.6251 0.6234 -0.0384 0.0296  -0.0381 14  GLN A O   
132   C CB  . GLN A 14  ? 0.6081 0.5702 0.5770 -0.0333 0.0261  -0.0219 14  GLN A CB  
133   C CG  . GLN A 14  ? 0.5468 0.5057 0.5194 -0.0326 0.0234  -0.0145 14  GLN A CG  
134   C CD  . GLN A 14  ? 0.5541 0.5266 0.5319 -0.0368 0.0232  -0.0090 14  GLN A CD  
135   O OE1 . GLN A 14  ? 0.4840 0.4711 0.4630 -0.0396 0.0253  -0.0096 14  GLN A OE1 
136   N NE2 . GLN A 14  ? 0.6172 0.5853 0.5984 -0.0376 0.0206  -0.0036 14  GLN A NE2 
137   N N   . PRO A 15  ? 0.5889 0.5822 0.5472 -0.0463 0.0314  -0.0308 15  PRO A N   
138   C CA  . PRO A 15  ? 0.5116 0.5149 0.4659 -0.0471 0.0344  -0.0426 15  PRO A CA  
139   C C   . PRO A 15  ? 0.6461 0.6473 0.6056 -0.0386 0.0366  -0.0529 15  PRO A C   
140   O O   . PRO A 15  ? 0.6730 0.6713 0.6390 -0.0332 0.0359  -0.0491 15  PRO A O   
141   C CB  . PRO A 15  ? 0.5748 0.6045 0.5268 -0.0536 0.0360  -0.0375 15  PRO A CB  
142   C CG  . PRO A 15  ? 0.5806 0.6119 0.5395 -0.0533 0.0345  -0.0252 15  PRO A CG  
143   C CD  . PRO A 15  ? 0.5945 0.6032 0.5552 -0.0510 0.0309  -0.0203 15  PRO A CD  
144   N N   . LEU A 16  ? 0.6396 0.6429 0.5971 -0.0371 0.0390  -0.0668 16  LEU A N   
145   C CA  . LEU A 16  ? 0.6349 0.6355 0.5993 -0.0277 0.0410  -0.0783 16  LEU A CA  
146   C C   . LEU A 16  ? 0.5930 0.6192 0.5618 -0.0258 0.0444  -0.0783 16  LEU A C   
147   O O   . LEU A 16  ? 0.6092 0.6593 0.5743 -0.0297 0.0483  -0.0840 16  LEU A O   
148   C CB  . LEU A 16  ? 0.6210 0.6181 0.5836 -0.0267 0.0428  -0.0952 16  LEU A CB  
149   C CG  . LEU A 16  ? 0.5841 0.5759 0.5565 -0.0153 0.0446  -0.1082 16  LEU A CG  
150   C CD1 . LEU A 16  ? 0.6025 0.5716 0.5826 -0.0078 0.0406  -0.0995 16  LEU A CD1 
151   C CD2 . LEU A 16  ? 0.5796 0.5622 0.5519 -0.0142 0.0455  -0.1261 16  LEU A CD2 
152   N N   . TYR A 17  ? 0.6409 0.6640 0.6175 -0.0204 0.0430  -0.0719 17  TYR A N   
153   C CA  . TYR A 17  ? 0.6524 0.6993 0.6354 -0.0188 0.0459  -0.0712 17  TYR A CA  
154   C C   . TYR A 17  ? 0.6126 0.6668 0.6035 -0.0089 0.0492  -0.0858 17  TYR A C   
155   O O   . TYR A 17  ? 0.6627 0.7394 0.6604 -0.0069 0.0521  -0.0865 17  TYR A O   
156   C CB  . TYR A 17  ? 0.6212 0.6632 0.6102 -0.0182 0.0424  -0.0586 17  TYR A CB  
157   C CG  . TYR A 17  ? 0.5185 0.5570 0.5033 -0.0270 0.0395  -0.0449 17  TYR A CG  
158   C CD1 . TYR A 17  ? 0.5497 0.6076 0.5316 -0.0360 0.0412  -0.0384 17  TYR A CD1 
159   C CD2 . TYR A 17  ? 0.4905 0.5076 0.4750 -0.0260 0.0350  -0.0380 17  TYR A CD2 
160   C CE1 . TYR A 17  ? 0.5102 0.5635 0.4909 -0.0428 0.0381  -0.0256 17  TYR A CE1 
161   C CE2 . TYR A 17  ? 0.5930 0.6073 0.5756 -0.0327 0.0325  -0.0272 17  TYR A CE2 
162   C CZ  . TYR A 17  ? 0.5869 0.6180 0.5685 -0.0407 0.0339  -0.0211 17  TYR A CZ  
163   O OH  . TYR A 17  ? 0.5550 0.5819 0.5372 -0.0462 0.0310  -0.0103 17  TYR A OH  
164   N N   . ARG A 18  ? 0.6400 0.6759 0.6319 -0.0024 0.0487  -0.0973 18  ARG A N   
165   C CA  . ARG A 18  ? 0.7113 0.7496 0.7138 0.0093  0.0509  -0.1116 18  ARG A CA  
166   C C   . ARG A 18  ? 0.6724 0.7349 0.6723 0.0081  0.0572  -0.1276 18  ARG A C   
167   O O   . ARG A 18  ? 0.6758 0.7327 0.6679 0.0038  0.0579  -0.1362 18  ARG A O   
168   C CB  . ARG A 18  ? 0.7058 0.7110 0.7125 0.0169  0.0469  -0.1160 18  ARG A CB  
169   C CG  . ARG A 18  ? 0.7815 0.7854 0.8024 0.0309  0.0480  -0.1292 18  ARG A CG  
170   C CD  . ARG A 18  ? 0.8504 0.8199 0.8764 0.0375  0.0438  -0.1338 18  ARG A CD  
171   N NE  . ARG A 18  ? 0.8775 0.8471 0.9130 0.0465  0.0469  -0.1546 18  ARG A NE  
172   C CZ  . ARG A 18  ? 0.8340 0.8137 0.8640 0.0422  0.0513  -0.1707 18  ARG A CZ  
173   N NH1 . ARG A 18  ? 0.7488 0.7389 0.7636 0.0286  0.0528  -0.1671 18  ARG A NH1 
174   N NH2 . ARG A 18  ? 0.7729 0.7533 0.8136 0.0521  0.0541  -0.1914 18  ARG A NH2 
175   N N   . GLU A 19  ? 0.6671 0.7588 0.6737 0.0115  0.0619  -0.1321 19  GLU A N   
176   C CA  . GLU A 19  ? 0.6637 0.7831 0.6683 0.0115  0.0687  -0.1488 19  GLU A CA  
177   C C   . GLU A 19  ? 0.7038 0.8059 0.7144 0.0220  0.0692  -0.1696 19  GLU A C   
178   O O   . GLU A 19  ? 0.7678 0.8518 0.7917 0.0341  0.0667  -0.1726 19  GLU A O   
179   C CB  . GLU A 19  ? 0.6868 0.8412 0.7000 0.0143  0.0738  -0.1492 19  GLU A CB  
180   C CG  . GLU A 19  ? 0.6936 0.8876 0.7007 0.0091  0.0816  -0.1599 19  GLU A CG  
181   C CD  . GLU A 19  ? 0.7506 0.9555 0.7665 0.0213  0.0869  -0.1852 19  GLU A CD  
182   O OE1 . GLU A 19  ? 0.7561 0.9345 0.7838 0.0340  0.0839  -0.1933 19  GLU A OE1 
183   O OE2 . GLU A 19  ? 0.8386 1.0786 0.8496 0.0183  0.0940  -0.1970 19  GLU A OE2 
184   N N   . PRO A 20  ? 0.7076 0.8143 0.7097 0.0177  0.0719  -0.1844 20  PRO A N   
185   C CA  . PRO A 20  ? 0.7915 0.8763 0.8009 0.0270  0.0714  -0.2049 20  PRO A CA  
186   C C   . PRO A 20  ? 0.8155 0.9100 0.8419 0.0425  0.0752  -0.2214 20  PRO A C   
187   O O   . PRO A 20  ? 0.8628 0.9282 0.9027 0.0541  0.0714  -0.2259 20  PRO A O   
188   C CB  . PRO A 20  ? 0.7176 0.8158 0.7135 0.0174  0.0744  -0.2184 20  PRO A CB  
189   C CG  . PRO A 20  ? 0.7222 0.8612 0.7071 0.0073  0.0788  -0.2092 20  PRO A CG  
190   C CD  . PRO A 20  ? 0.6771 0.8091 0.6635 0.0043  0.0749  -0.1832 20  PRO A CD  
191   N N   . TYR A 21  ? 0.6787 0.8143 0.7057 0.0432  0.0826  -0.2298 21  TYR A N   
192   C CA  . TYR A 21  ? 0.7281 0.8774 0.7719 0.0585  0.0872  -0.2495 21  TYR A CA  
193   C C   . TYR A 21  ? 0.7182 0.8589 0.7790 0.0699  0.0838  -0.2383 21  TYR A C   
194   O O   . TYR A 21  ? 0.6139 0.7351 0.6914 0.0848  0.0817  -0.2487 21  TYR A O   
195   C CB  . TYR A 21  ? 0.6290 0.8296 0.6679 0.0548  0.0966  -0.2605 21  TYR A CB  
196   C CG  . TYR A 21  ? 0.7173 0.9300 0.7401 0.0451  0.0999  -0.2747 21  TYR A CG  
197   C CD1 . TYR A 21  ? 0.6765 0.8893 0.7043 0.0532  0.1033  -0.3043 21  TYR A CD1 
198   C CD2 . TYR A 21  ? 0.7919 1.0155 0.7954 0.0280  0.0988  -0.2589 21  TYR A CD2 
199   C CE1 . TYR A 21  ? 0.6588 0.8842 0.6713 0.0438  0.1058  -0.3188 21  TYR A CE1 
200   C CE2 . TYR A 21  ? 0.8054 1.0422 0.7937 0.0189  0.1010  -0.2715 21  TYR A CE2 
201   C CZ  . TYR A 21  ? 0.7444 0.9829 0.7367 0.0264  0.1045  -0.3019 21  TYR A CZ  
202   O OH  . TYR A 21  ? 0.8057 1.0592 0.7828 0.0170  0.1063  -0.3163 21  TYR A OH  
203   N N   . THR A 22  ? 0.7093 0.8645 0.7671 0.0630  0.0828  -0.2172 22  THR A N   
204   C CA  . THR A 22  ? 0.7214 0.8732 0.7946 0.0724  0.0793  -0.2067 22  THR A CA  
205   C C   . THR A 22  ? 0.7878 0.8968 0.8619 0.0743  0.0699  -0.1918 22  THR A C   
206   O O   . THR A 22  ? 0.7891 0.8905 0.8770 0.0844  0.0658  -0.1856 22  THR A O   
207   C CB  . THR A 22  ? 0.7396 0.9251 0.8109 0.0637  0.0817  -0.1913 22  THR A CB  
208   O OG1 . THR A 22  ? 0.7717 0.9495 0.8264 0.0478  0.0787  -0.1731 22  THR A OG1 
209   C CG2 . THR A 22  ? 0.6971 0.9292 0.7691 0.0623  0.0915  -0.2045 22  THR A CG2 
210   N N   . GLY A 23  ? 0.7665 0.8501 0.8266 0.0646  0.0664  -0.1858 23  GLY A N   
211   C CA  . GLY A 23  ? 0.7829 0.8305 0.8421 0.0643  0.0582  -0.1700 23  GLY A CA  
212   C C   . GLY A 23  ? 0.8431 0.8970 0.9020 0.0607  0.0547  -0.1495 23  GLY A C   
213   O O   . GLY A 23  ? 0.8534 0.8854 0.9176 0.0659  0.0483  -0.1390 23  GLY A O   
214   N N   . GLU A 24  ? 0.8052 0.8890 0.8584 0.0513  0.0585  -0.1436 24  GLU A N   
215   C CA  . GLU A 24  ? 0.7373 0.8301 0.7924 0.0473  0.0556  -0.1267 24  GLU A CA  
216   C C   . GLU A 24  ? 0.7067 0.7935 0.7467 0.0325  0.0537  -0.1125 24  GLU A C   
217   O O   . GLU A 24  ? 0.7401 0.8394 0.7700 0.0232  0.0577  -0.1147 24  GLU A O   
218   C CB  . GLU A 24  ? 0.8209 0.9532 0.8849 0.0480  0.0610  -0.1297 24  GLU A CB  
219   C CG  . GLU A 24  ? 0.8725 1.0126 0.9555 0.0631  0.0603  -0.1364 24  GLU A CG  
220   C CD  . GLU A 24  ? 1.0035 1.1849 1.0957 0.0614  0.0651  -0.1361 24  GLU A CD  
221   O OE1 . GLU A 24  ? 1.2348 1.4390 1.3183 0.0486  0.0699  -0.1323 24  GLU A OE1 
222   O OE2 . GLU A 24  ? 1.2746 1.4666 1.3834 0.0724  0.0639  -0.1387 24  GLU A OE2 
223   N N   . TYR A 25  ? 0.6327 0.7016 0.6716 0.0306  0.0476  -0.0983 25  TYR A N   
224   C CA  . TYR A 25  ? 0.6149 0.6788 0.6423 0.0179  0.0457  -0.0852 25  TYR A CA  
225   C C   . TYR A 25  ? 0.6235 0.7160 0.6538 0.0105  0.0480  -0.0782 25  TYR A C   
226   O O   . TYR A 25  ? 0.7008 0.8013 0.7408 0.0133  0.0459  -0.0734 25  TYR A O   
227   C CB  . TYR A 25  ? 0.6326 0.6699 0.6583 0.0190  0.0389  -0.0746 25  TYR A CB  
228   C CG  . TYR A 25  ? 0.6400 0.6488 0.6604 0.0219  0.0366  -0.0776 25  TYR A CG  
229   C CD1 . TYR A 25  ? 0.7356 0.7330 0.7639 0.0330  0.0361  -0.0873 25  TYR A CD1 
230   C CD2 . TYR A 25  ? 0.6676 0.6610 0.6769 0.0134  0.0347  -0.0703 25  TYR A CD2 
231   C CE1 . TYR A 25  ? 0.7366 0.7065 0.7616 0.0344  0.0335  -0.0888 25  TYR A CE1 
232   C CE2 . TYR A 25  ? 0.6320 0.6009 0.6374 0.0146  0.0326  -0.0722 25  TYR A CE2 
233   C CZ  . TYR A 25  ? 0.6482 0.6048 0.6614 0.0245  0.0320  -0.0810 25  TYR A CZ  
234   O OH  . TYR A 25  ? 0.7548 0.6856 0.7657 0.0246  0.0295  -0.0819 25  TYR A OH  
235   N N   . LEU A 26  ? 0.5283 0.6373 0.5509 0.0006  0.0521  -0.0771 26  LEU A N   
236   C CA  . LEU A 26  ? 0.4810 0.6184 0.5069 -0.0077 0.0547  -0.0694 26  LEU A CA  
237   C C   . LEU A 26  ? 0.4945 0.6229 0.5193 -0.0168 0.0498  -0.0530 26  LEU A C   
238   O O   . LEU A 26  ? 0.4860 0.6339 0.5167 -0.0237 0.0507  -0.0450 26  LEU A O   
239   C CB  . LEU A 26  ? 0.5731 0.7342 0.5910 -0.0149 0.0608  -0.0735 26  LEU A CB  
240   C CG  . LEU A 26  ? 0.5133 0.6820 0.5302 -0.0069 0.0658  -0.0928 26  LEU A CG  
241   C CD1 . LEU A 26  ? 0.5755 0.7725 0.5828 -0.0157 0.0716  -0.0959 26  LEU A CD1 
242   C CD2 . LEU A 26  ? 0.5048 0.6872 0.5364 0.0048  0.0684  -0.1031 26  LEU A CD2 
243   N N   . LEU A 27  ? 0.6137 0.7138 0.6321 -0.0171 0.0450  -0.0482 27  LEU A N   
244   C CA  . LEU A 27  ? 0.5997 0.6899 0.6189 -0.0234 0.0402  -0.0355 27  LEU A CA  
245   C C   . LEU A 27  ? 0.6388 0.7029 0.6575 -0.0168 0.0349  -0.0354 27  LEU A C   
246   O O   . LEU A 27  ? 0.6987 0.7470 0.7126 -0.0106 0.0347  -0.0416 27  LEU A O   
247   C CB  . LEU A 27  ? 0.6088 0.6964 0.6193 -0.0335 0.0401  -0.0273 27  LEU A CB  
248   C CG  . LEU A 27  ? 0.6858 0.8006 0.6970 -0.0427 0.0439  -0.0216 27  LEU A CG  
249   C CD1 . LEU A 27  ? 0.6566 0.7675 0.6591 -0.0510 0.0429  -0.0131 27  LEU A CD1 
250   C CD2 . LEU A 27  ? 0.7287 0.8569 0.7518 -0.0476 0.0428  -0.0130 27  LEU A CD2 
251   N N   . PRO A 28  ? 0.6420 0.7016 0.6657 -0.0184 0.0306  -0.0285 28  PRO A N   
252   C CA  . PRO A 28  ? 0.6410 0.6811 0.6639 -0.0117 0.0257  -0.0287 28  PRO A CA  
253   C C   . PRO A 28  ? 0.6316 0.6530 0.6465 -0.0162 0.0228  -0.0227 28  PRO A C   
254   O O   . PRO A 28  ? 0.5909 0.6015 0.6055 -0.0139 0.0186  -0.0205 28  PRO A O   
255   C CB  . PRO A 28  ? 0.6631 0.7149 0.6969 -0.0107 0.0226  -0.0268 28  PRO A CB  
256   C CG  . PRO A 28  ? 0.7097 0.7799 0.7490 -0.0208 0.0248  -0.0220 28  PRO A CG  
257   C CD  . PRO A 28  ? 0.5566 0.6317 0.5888 -0.0258 0.0298  -0.0216 28  PRO A CD  
258   N N   . TRP A 29  ? 0.6557 0.6761 0.6645 -0.0227 0.0251  -0.0203 29  TRP A N   
259   C CA  . TRP A 29  ? 0.6006 0.6074 0.6046 -0.0274 0.0226  -0.0141 29  TRP A CA  
260   C C   . TRP A 29  ? 0.5719 0.5593 0.5687 -0.0226 0.0208  -0.0158 29  TRP A C   
261   O O   . TRP A 29  ? 0.6214 0.5989 0.6161 -0.0240 0.0181  -0.0119 29  TRP A O   
262   C CB  . TRP A 29  ? 0.5336 0.5462 0.5337 -0.0349 0.0250  -0.0101 29  TRP A CB  
263   C CG  . TRP A 29  ? 0.5101 0.5401 0.5174 -0.0418 0.0258  -0.0039 29  TRP A CG  
264   C CD1 . TRP A 29  ? 0.6047 0.6531 0.6109 -0.0467 0.0295  -0.0025 29  TRP A CD1 
265   C CD2 . TRP A 29  ? 0.5342 0.5651 0.5510 -0.0457 0.0226  0.0023  29  TRP A CD2 
266   N NE1 . TRP A 29  ? 0.6282 0.6892 0.6428 -0.0537 0.0289  0.0062  29  TRP A NE1 
267   C CE2 . TRP A 29  ? 0.6180 0.6670 0.6400 -0.0533 0.0245  0.0089  29  TRP A CE2 
268   C CE3 . TRP A 29  ? 0.5993 0.6185 0.6207 -0.0439 0.0183  0.0024  29  TRP A CE3 
269   C CZ2 . TRP A 29  ? 0.5916 0.6444 0.6250 -0.0596 0.0219  0.0164  29  TRP A CZ2 
270   C CZ3 . TRP A 29  ? 0.6094 0.6328 0.6417 -0.0497 0.0158  0.0075  29  TRP A CZ3 
271   C CH2 . TRP A 29  ? 0.6133 0.6519 0.6523 -0.0576 0.0174  0.0148  29  TRP A CH2 
272   N N   . THR A 30  ? 0.6165 0.5988 0.6102 -0.0172 0.0223  -0.0217 30  THR A N   
273   C CA  . THR A 30  ? 0.5404 0.5043 0.5287 -0.0132 0.0203  -0.0217 30  THR A CA  
274   C C   . THR A 30  ? 0.6337 0.5938 0.6249 -0.0078 0.0162  -0.0192 30  THR A C   
275   O O   . THR A 30  ? 0.6737 0.6234 0.6599 -0.0082 0.0138  -0.0151 30  THR A O   
276   C CB  . THR A 30  ? 0.5781 0.5361 0.5653 -0.0089 0.0223  -0.0289 30  THR A CB  
277   O OG1 . THR A 30  ? 0.6748 0.6372 0.6574 -0.0148 0.0256  -0.0320 30  THR A OG1 
278   C CG2 . THR A 30  ? 0.6033 0.5413 0.5867 -0.0055 0.0197  -0.0268 30  THR A CG2 
279   N N   . PHE A 31  ? 0.6514 0.6227 0.6505 -0.0031 0.0154  -0.0216 31  PHE A N   
280   C CA  . PHE A 31  ? 0.6610 0.6318 0.6629 0.0020  0.0108  -0.0192 31  PHE A CA  
281   C C   . PHE A 31  ? 0.6651 0.6379 0.6657 -0.0033 0.0082  -0.0154 31  PHE A C   
282   O O   . PHE A 31  ? 0.7559 0.7227 0.7522 -0.0015 0.0047  -0.0128 31  PHE A O   
283   C CB  . PHE A 31  ? 0.6808 0.6667 0.6933 0.0079  0.0104  -0.0230 31  PHE A CB  
284   C CG  . PHE A 31  ? 0.6373 0.6272 0.6536 0.0127  0.0049  -0.0203 31  PHE A CG  
285   C CD1 . PHE A 31  ? 0.6472 0.6283 0.6629 0.0212  0.0016  -0.0182 31  PHE A CD1 
286   C CD2 . PHE A 31  ? 0.6062 0.6091 0.6274 0.0084  0.0025  -0.0195 31  PHE A CD2 
287   C CE1 . PHE A 31  ? 0.7300 0.7174 0.7483 0.0255  -0.0041 -0.0148 31  PHE A CE1 
288   C CE2 . PHE A 31  ? 0.6636 0.6725 0.6877 0.0123  -0.0030 -0.0180 31  PHE A CE2 
289   C CZ  . PHE A 31  ? 0.7285 0.7310 0.7505 0.0210  -0.0064 -0.0154 31  PHE A CZ  
290   N N   . PHE A 32  ? 0.6075 0.5893 0.6123 -0.0101 0.0097  -0.0152 32  PHE A N   
291   C CA  . PHE A 32  ? 0.6453 0.6286 0.6526 -0.0146 0.0067  -0.0134 32  PHE A CA  
292   C C   . PHE A 32  ? 0.7069 0.6776 0.7065 -0.0173 0.0066  -0.0112 32  PHE A C   
293   O O   . PHE A 32  ? 0.6890 0.6577 0.6878 -0.0176 0.0037  -0.0118 32  PHE A O   
294   C CB  . PHE A 32  ? 0.6471 0.6422 0.6637 -0.0214 0.0078  -0.0124 32  PHE A CB  
295   C CG  . PHE A 32  ? 0.6826 0.6939 0.7092 -0.0200 0.0067  -0.0145 32  PHE A CG  
296   C CD1 . PHE A 32  ? 0.5226 0.5377 0.5527 -0.0170 0.0020  -0.0165 32  PHE A CD1 
297   C CD2 . PHE A 32  ? 0.6340 0.6595 0.6663 -0.0222 0.0105  -0.0144 32  PHE A CD2 
298   C CE1 . PHE A 32  ? 0.6187 0.6510 0.6594 -0.0160 0.0008  -0.0183 32  PHE A CE1 
299   C CE2 . PHE A 32  ? 0.6070 0.6503 0.6498 -0.0212 0.0100  -0.0163 32  PHE A CE2 
300   C CZ  . PHE A 32  ? 0.6447 0.6910 0.6923 -0.0181 0.0049  -0.0182 32  PHE A CZ  
301   N N   . HIS A 33  ? 0.6850 0.6492 0.6795 -0.0193 0.0098  -0.0097 33  HIS A N   
302   C CA  . HIS A 33  ? 0.6500 0.6046 0.6383 -0.0216 0.0100  -0.0076 33  HIS A CA  
303   C C   . HIS A 33  ? 0.6504 0.5961 0.6305 -0.0174 0.0092  -0.0069 33  HIS A C   
304   O O   . HIS A 33  ? 0.6040 0.5454 0.5795 -0.0186 0.0088  -0.0055 33  HIS A O   
305   C CB  . HIS A 33  ? 0.5746 0.5285 0.5615 -0.0262 0.0132  -0.0056 33  HIS A CB  
306   C CG  . HIS A 33  ? 0.5598 0.5204 0.5541 -0.0316 0.0131  -0.0027 33  HIS A CG  
307   N ND1 . HIS A 33  ? 0.6635 0.6206 0.6618 -0.0336 0.0110  -0.0011 33  HIS A ND1 
308   C CD2 . HIS A 33  ? 0.5109 0.4818 0.5100 -0.0356 0.0146  -0.0004 33  HIS A CD2 
309   C CE1 . HIS A 33  ? 0.6205 0.5829 0.6270 -0.0384 0.0107  0.0029  33  HIS A CE1 
310   N NE2 . HIS A 33  ? 0.6248 0.5965 0.6312 -0.0403 0.0129  0.0043  33  HIS A NE2 
311   N N   . ALA A 34  ? 0.5857 0.5293 0.5647 -0.0124 0.0088  -0.0074 34  ALA A N   
312   C CA  . ALA A 34  ? 0.6668 0.6017 0.6393 -0.0087 0.0071  -0.0043 34  ALA A CA  
313   C C   . ALA A 34  ? 0.7493 0.6901 0.7208 -0.0061 0.0031  -0.0031 34  ALA A C   
314   O O   . ALA A 34  ? 0.6651 0.6033 0.6295 -0.0064 0.0021  0.0001  34  ALA A O   
315   C CB  . ALA A 34  ? 0.5723 0.5010 0.5462 -0.0036 0.0073  -0.0049 34  ALA A CB  
316   N N   . VAL A 35  ? 0.6874 0.6388 0.6660 -0.0039 0.0008  -0.0060 35  VAL A N   
317   C CA  . VAL A 35  ? 0.6950 0.6545 0.6728 -0.0020 -0.0036 -0.0060 35  VAL A CA  
318   C C   . VAL A 35  ? 0.6795 0.6422 0.6561 -0.0069 -0.0039 -0.0093 35  VAL A C   
319   O O   . VAL A 35  ? 0.7508 0.7215 0.7258 -0.0062 -0.0075 -0.0115 35  VAL A O   
320   C CB  . VAL A 35  ? 0.6282 0.6000 0.6154 0.0012  -0.0065 -0.0086 35  VAL A CB  
321   C CG1 . VAL A 35  ? 0.6557 0.6250 0.6453 0.0084  -0.0069 -0.0061 35  VAL A CG1 
322   C CG2 . VAL A 35  ? 0.6156 0.5938 0.6122 -0.0038 -0.0042 -0.0127 35  VAL A CG2 
323   N N   . LYS A 36  ? 0.6268 0.5845 0.6050 -0.0116 -0.0005 -0.0103 36  LYS A N   
324   C CA  . LYS A 36  ? 0.6723 0.6318 0.6532 -0.0154 -0.0008 -0.0144 36  LYS A CA  
325   C C   . LYS A 36  ? 0.7206 0.6737 0.6955 -0.0170 0.0020  -0.0130 36  LYS A C   
326   O O   . LYS A 36  ? 0.7645 0.7205 0.7381 -0.0174 0.0013  -0.0169 36  LYS A O   
327   C CB  . LYS A 36  ? 0.6424 0.6038 0.6350 -0.0197 -0.0004 -0.0160 36  LYS A CB  
328   C CG  . LYS A 36  ? 0.5798 0.5406 0.5791 -0.0232 -0.0016 -0.0203 36  LYS A CG  
329   C CD  . LYS A 36  ? 0.6311 0.5931 0.6435 -0.0283 -0.0021 -0.0195 36  LYS A CD  
330   C CE  . LYS A 36  ? 0.6342 0.5919 0.6476 -0.0311 0.0014  -0.0130 36  LYS A CE  
331   N NZ  . LYS A 36  ? 0.5829 0.5334 0.5976 -0.0321 0.0021  -0.0124 36  LYS A NZ  
332   N N   . ASP A 37  ? 0.7634 0.7095 0.7352 -0.0180 0.0051  -0.0085 37  ASP A N   
333   C CA  . ASP A 37  ? 0.6741 0.6164 0.6424 -0.0204 0.0078  -0.0070 37  ASP A CA  
334   C C   . ASP A 37  ? 0.7102 0.6465 0.6700 -0.0204 0.0096  -0.0018 37  ASP A C   
335   O O   . ASP A 37  ? 0.7904 0.7272 0.7451 -0.0216 0.0110  -0.0001 37  ASP A O   
336   C CB  . ASP A 37  ? 0.7706 0.7116 0.7466 -0.0241 0.0094  -0.0067 37  ASP A CB  
337   C CG  . ASP A 37  ? 0.7453 0.6901 0.7319 -0.0253 0.0072  -0.0096 37  ASP A CG  
338   O OD1 . ASP A 37  ? 0.7709 0.7171 0.7625 -0.0252 0.0055  -0.0140 37  ASP A OD1 
339   O OD2 . ASP A 37  ? 0.5701 0.5172 0.5609 -0.0267 0.0073  -0.0079 37  ASP A OD2 
340   N N   . TYR A 38  ? 0.6395 0.5706 0.5986 -0.0190 0.0096  0.0003  38  TYR A N   
341   C CA  . TYR A 38  ? 0.5792 0.5016 0.5329 -0.0203 0.0112  0.0046  38  TYR A CA  
342   C C   . TYR A 38  ? 0.6242 0.5455 0.5706 -0.0189 0.0099  0.0097  38  TYR A C   
343   O O   . TYR A 38  ? 0.6801 0.5978 0.6218 -0.0224 0.0117  0.0139  38  TYR A O   
344   C CB  . TYR A 38  ? 0.6113 0.5276 0.5677 -0.0185 0.0114  0.0035  38  TYR A CB  
345   C CG  . TYR A 38  ? 0.6428 0.5625 0.6039 -0.0216 0.0136  -0.0003 38  TYR A CG  
346   C CD1 . TYR A 38  ? 0.5794 0.5026 0.5411 -0.0265 0.0150  0.0003  38  TYR A CD1 
347   C CD2 . TYR A 38  ? 0.5881 0.5097 0.5534 -0.0195 0.0141  -0.0040 38  TYR A CD2 
348   C CE1 . TYR A 38  ? 0.7296 0.6579 0.6951 -0.0297 0.0164  -0.0010 38  TYR A CE1 
349   C CE2 . TYR A 38  ? 0.5680 0.4963 0.5362 -0.0231 0.0163  -0.0065 38  TYR A CE2 
350   C CZ  . TYR A 38  ? 0.6800 0.6115 0.6478 -0.0285 0.0171  -0.0042 38  TYR A CZ  
351   O OH  . TYR A 38  ? 0.6695 0.6094 0.6397 -0.0325 0.0187  -0.0046 38  TYR A OH  
352   N N   . TYR A 39  ? 0.6431 0.5694 0.5885 -0.0146 0.0067  0.0103  39  TYR A N   
353   C CA  . TYR A 39  ? 0.6349 0.5644 0.5721 -0.0139 0.0052  0.0163  39  TYR A CA  
354   C C   . TYR A 39  ? 0.7105 0.6523 0.6441 -0.0158 0.0061  0.0127  39  TYR A C   
355   O O   . TYR A 39  ? 0.6972 0.6436 0.6231 -0.0178 0.0072  0.0175  39  TYR A O   
356   C CB  . TYR A 39  ? 0.6257 0.5579 0.5628 -0.0083 0.0005  0.0194  39  TYR A CB  
357   C CG  . TYR A 39  ? 0.6982 0.6382 0.6261 -0.0077 -0.0019 0.0266  39  TYR A CG  
358   C CD1 . TYR A 39  ? 0.6578 0.6140 0.5817 -0.0073 -0.0036 0.0221  39  TYR A CD1 
359   C CD2 . TYR A 39  ? 0.6624 0.5943 0.5858 -0.0078 -0.0030 0.0379  39  TYR A CD2 
360   C CE1 . TYR A 39  ? 0.6759 0.6433 0.5898 -0.0072 -0.0058 0.0287  39  TYR A CE1 
361   C CE2 . TYR A 39  ? 0.6317 0.5732 0.5460 -0.0079 -0.0054 0.0468  39  TYR A CE2 
362   C CZ  . TYR A 39  ? 0.6675 0.6284 0.5762 -0.0076 -0.0066 0.0421  39  TYR A CZ  
363   O OH  . TYR A 39  ? 0.6808 0.6548 0.5789 -0.0081 -0.0090 0.0509  39  TYR A OH  
364   N N   . ASP A 40  ? 0.7302 0.6779 0.6700 -0.0155 0.0059  0.0043  40  ASP A N   
365   C CA  . ASP A 40  ? 0.7439 0.7034 0.6820 -0.0157 0.0058  -0.0018 40  ASP A CA  
366   C C   . ASP A 40  ? 0.7171 0.6777 0.6559 -0.0187 0.0100  -0.0036 40  ASP A C   
367   O O   . ASP A 40  ? 0.6374 0.6089 0.5717 -0.0186 0.0112  -0.0067 40  ASP A O   
368   C CB  . ASP A 40  ? 0.7150 0.6788 0.6616 -0.0144 0.0031  -0.0105 40  ASP A CB  
369   C CG  . ASP A 40  ? 0.7365 0.7095 0.6800 -0.0114 -0.0017 -0.0114 40  ASP A CG  
370   O OD1 . ASP A 40  ? 0.7824 0.7672 0.7192 -0.0110 -0.0029 -0.0145 40  ASP A OD1 
371   O OD2 . ASP A 40  ? 0.7116 0.6825 0.6596 -0.0094 -0.0042 -0.0093 40  ASP A OD2 
372   N N   . MET A 41  ? 0.7619 0.7140 0.7063 -0.0211 0.0122  -0.0021 41  MET A N   
373   C CA  . MET A 41  ? 0.6950 0.6496 0.6412 -0.0236 0.0157  -0.0025 41  MET A CA  
374   C C   . MET A 41  ? 0.6666 0.6260 0.6036 -0.0259 0.0182  0.0034  41  MET A C   
375   O O   . MET A 41  ? 0.6676 0.6383 0.6038 -0.0260 0.0206  0.0002  41  MET A O   
376   C CB  . MET A 41  ? 0.6510 0.5973 0.6039 -0.0262 0.0167  -0.0006 41  MET A CB  
377   C CG  . MET A 41  ? 0.7425 0.6871 0.7054 -0.0252 0.0148  -0.0049 41  MET A CG  
378   S SD  . MET A 41  ? 0.9279 0.8787 0.9003 -0.0231 0.0143  -0.0131 41  MET A SD  
379   C CE  . MET A 41  ? 0.5454 0.4975 0.5234 -0.0250 0.0171  -0.0102 41  MET A CE  
380   N N   . PRO A 42  ? 0.6877 0.6398 0.6187 -0.0278 0.0178  0.0121  42  PRO A N   
381   C CA  . PRO A 42  ? 0.6619 0.6196 0.5849 -0.0312 0.0198  0.0195  42  PRO A CA  
382   C C   . PRO A 42  ? 0.6543 0.6251 0.5688 -0.0290 0.0186  0.0203  42  PRO A C   
383   O O   . PRO A 42  ? 0.6740 0.6574 0.5823 -0.0317 0.0213  0.0236  42  PRO A O   
384   C CB  . PRO A 42  ? 0.6548 0.5975 0.5763 -0.0339 0.0186  0.0284  42  PRO A CB  
385   C CG  . PRO A 42  ? 0.7143 0.6459 0.6431 -0.0318 0.0171  0.0235  42  PRO A CG  
386   C CD  . PRO A 42  ? 0.7291 0.6679 0.6617 -0.0273 0.0156  0.0154  42  PRO A CD  
387   N N   . ALA A 43  ? 0.6714 0.6421 0.5855 -0.0246 0.0145  0.0175  43  ALA A N   
388   C CA  . ALA A 43  ? 0.6858 0.6717 0.5913 -0.0227 0.0125  0.0178  43  ALA A CA  
389   C C   . ALA A 43  ? 0.6603 0.6637 0.5646 -0.0225 0.0153  0.0075  43  ALA A C   
390   O O   . ALA A 43  ? 0.7262 0.7467 0.6212 -0.0222 0.0149  0.0073  43  ALA A O   
391   C CB  . ALA A 43  ? 0.6191 0.6034 0.5268 -0.0181 0.0072  0.0148  43  ALA A CB  
392   N N   . TYR A 44  ? 0.6196 0.6202 0.5337 -0.0224 0.0180  -0.0011 44  TYR A N   
393   C CA  . TYR A 44  ? 0.7113 0.7274 0.6271 -0.0211 0.0210  -0.0119 44  TYR A CA  
394   C C   . TYR A 44  ? 0.7096 0.7403 0.6170 -0.0244 0.0257  -0.0062 44  TYR A C   
395   O O   . TYR A 44  ? 0.6792 0.7300 0.5816 -0.0233 0.0279  -0.0131 44  TYR A O   
396   C CB  . TYR A 44  ? 0.6985 0.7064 0.6288 -0.0198 0.0222  -0.0198 44  TYR A CB  
397   C CG  . TYR A 44  ? 0.7577 0.7588 0.6975 -0.0167 0.0183  -0.0293 44  TYR A CG  
398   C CD1 . TYR A 44  ? 0.7664 0.7777 0.7095 -0.0137 0.0175  -0.0428 44  TYR A CD1 
399   C CD2 . TYR A 44  ? 0.7066 0.6924 0.6529 -0.0174 0.0156  -0.0254 44  TYR A CD2 
400   C CE1 . TYR A 44  ? 0.6694 0.6737 0.6228 -0.0121 0.0136  -0.0512 44  TYR A CE1 
401   C CE2 . TYR A 44  ? 0.6097 0.5909 0.5656 -0.0159 0.0122  -0.0327 44  TYR A CE2 
402   C CZ  . TYR A 44  ? 0.5902 0.5797 0.5501 -0.0136 0.0110  -0.0452 44  TYR A CZ  
403   O OH  . TYR A 44  ? 0.6533 0.6374 0.6243 -0.0133 0.0072  -0.0525 44  TYR A OH  
404   N N   . LEU A 45  ? 0.6692 0.6915 0.5754 -0.0291 0.0274  0.0061  45  LEU A N   
405   C CA  . LEU A 45  ? 0.6927 0.7289 0.5926 -0.0340 0.0320  0.0133  45  LEU A CA  
406   C C   . LEU A 45  ? 0.6923 0.7441 0.5778 -0.0355 0.0313  0.0207  45  LEU A C   
407   O O   . LEU A 45  ? 0.8022 0.8729 0.6814 -0.0394 0.0357  0.0249  45  LEU A O   
408   C CB  . LEU A 45  ? 0.6782 0.6999 0.5810 -0.0398 0.0329  0.0249  45  LEU A CB  
409   C CG  . LEU A 45  ? 0.5758 0.5870 0.4913 -0.0397 0.0338  0.0194  45  LEU A CG  
410   C CD1 . LEU A 45  ? 0.5737 0.5680 0.4905 -0.0453 0.0328  0.0294  45  LEU A CD1 
411   C CD2 . LEU A 45  ? 0.6101 0.6385 0.5314 -0.0397 0.0386  0.0133  45  LEU A CD2 
412   N N   . LYS A 46  ? 0.7056 0.7524 0.5862 -0.0328 0.0259  0.0230  46  LYS A N   
413   C CA  . LYS A 46  ? 0.7642 0.8287 0.6309 -0.0337 0.0243  0.0302  46  LYS A CA  
414   C C   . LYS A 46  ? 0.7099 0.8000 0.5717 -0.0306 0.0258  0.0155  46  LYS A C   
415   O O   . LYS A 46  ? 0.7908 0.9034 0.6395 -0.0325 0.0263  0.0203  46  LYS A O   
416   C CB  . LYS A 46  ? 0.7103 0.7624 0.5747 -0.0310 0.0173  0.0380  46  LYS A CB  
417   C CG  . LYS A 46  ? 0.7597 0.7847 0.6317 -0.0322 0.0155  0.0479  46  LYS A CG  
418   C CD  . LYS A 46  ? 0.8869 0.9056 0.7532 -0.0320 0.0102  0.0638  46  LYS A CD  
419   C CE  . LYS A 46  ? 0.9559 0.9615 0.8289 -0.0254 0.0045  0.0600  46  LYS A CE  
420   N NZ  . LYS A 46  ? 1.0308 1.0205 0.9052 -0.0244 -0.0001 0.0753  46  LYS A NZ  
421   N N   . ASP A 47  ? 0.7397 0.8272 0.6119 -0.0261 0.0263  -0.0021 47  ASP A N   
422   C CA  . ASP A 47  ? 0.8119 0.9208 0.6821 -0.0226 0.0271  -0.0194 47  ASP A CA  
423   C C   . ASP A 47  ? 0.7510 0.8683 0.6304 -0.0209 0.0333  -0.0326 47  ASP A C   
424   O O   . ASP A 47  ? 0.8096 0.9445 0.6891 -0.0174 0.0346  -0.0494 47  ASP A O   
425   C CB  . ASP A 47  ? 0.7723 0.8717 0.6488 -0.0183 0.0210  -0.0307 47  ASP A CB  
426   C CG  . ASP A 47  ? 0.8370 0.9361 0.7041 -0.0186 0.0146  -0.0203 47  ASP A CG  
427   O OD1 . ASP A 47  ? 0.9768 1.0943 0.8294 -0.0208 0.0143  -0.0109 47  ASP A OD1 
428   O OD2 . ASP A 47  ? 0.8404 0.9224 0.7155 -0.0166 0.0098  -0.0206 47  ASP A OD2 
429   N N   . PHE A 48  ? 0.6870 0.7933 0.5748 -0.0229 0.0367  -0.0264 48  PHE A N   
430   C CA  . PHE A 48  ? 0.7259 0.8416 0.6241 -0.0206 0.0423  -0.0374 48  PHE A CA  
431   C C   . PHE A 48  ? 0.7134 0.8345 0.6101 -0.0264 0.0473  -0.0240 48  PHE A C   
432   O O   . PHE A 48  ? 0.7678 0.8703 0.6657 -0.0309 0.0455  -0.0102 48  PHE A O   
433   C CB  . PHE A 48  ? 0.7650 0.8599 0.6815 -0.0161 0.0400  -0.0469 48  PHE A CB  
434   C CG  . PHE A 48  ? 0.6308 0.7199 0.5513 -0.0116 0.0350  -0.0603 48  PHE A CG  
435   C CD1 . PHE A 48  ? 0.6206 0.7248 0.5450 -0.0068 0.0362  -0.0792 48  PHE A CD1 
436   C CD2 . PHE A 48  ? 0.6685 0.7381 0.5899 -0.0124 0.0291  -0.0548 48  PHE A CD2 
437   C CE1 . PHE A 48  ? 0.5707 0.6690 0.5000 -0.0039 0.0311  -0.0921 48  PHE A CE1 
438   C CE2 . PHE A 48  ? 0.6924 0.7582 0.6186 -0.0095 0.0244  -0.0666 48  PHE A CE2 
439   C CZ  . PHE A 48  ? 0.5308 0.6103 0.4610 -0.0057 0.0252  -0.0852 48  PHE A CZ  
440   N N   . GLU A 49  ? 0.7780 0.9261 0.6729 -0.0267 0.0536  -0.0291 49  GLU A N   
441   C CA  . GLU A 49  ? 0.7369 0.8961 0.6303 -0.0334 0.0589  -0.0165 49  GLU A CA  
442   C C   . GLU A 49  ? 0.5958 0.7453 0.5068 -0.0320 0.0608  -0.0194 49  GLU A C   
443   O O   . GLU A 49  ? 0.7532 0.9223 0.6719 -0.0304 0.0664  -0.0262 49  GLU A O   
444   C CB  . GLU A 49  ? 0.7490 0.9455 0.6331 -0.0345 0.0654  -0.0206 49  GLU A CB  
445   C CG  . GLU A 49  ? 0.8300 1.0399 0.6943 -0.0418 0.0649  -0.0044 49  GLU A CG  
446   C CD  . GLU A 49  ? 1.0624 1.2542 0.9185 -0.0405 0.0569  0.0001  49  GLU A CD  
447   O OE1 . GLU A 49  ? 1.1182 1.2908 0.9709 -0.0456 0.0530  0.0183  49  GLU A OE1 
448   O OE2 . GLU A 49  ? 1.0679 1.2651 0.9224 -0.0342 0.0543  -0.0152 49  GLU A OE2 
449   N N   . ILE A 50  ? 0.6285 0.7493 0.5463 -0.0325 0.0559  -0.0141 50  ILE A N   
450   C CA  . ILE A 50  ? 0.6076 0.7181 0.5412 -0.0317 0.0562  -0.0151 50  ILE A CA  
451   C C   . ILE A 50  ? 0.6228 0.7133 0.5543 -0.0393 0.0535  0.0005  50  ILE A C   
452   O O   . ILE A 50  ? 0.5938 0.6763 0.5137 -0.0440 0.0513  0.0110  50  ILE A O   
453   C CB  . ILE A 50  ? 0.6533 0.7502 0.6003 -0.0233 0.0527  -0.0286 50  ILE A CB  
454   C CG1 . ILE A 50  ? 0.5828 0.6554 0.5263 -0.0232 0.0463  -0.0256 50  ILE A CG1 
455   C CG2 . ILE A 50  ? 0.6863 0.8009 0.6376 -0.0154 0.0549  -0.0465 50  ILE A CG2 
456   C CD1 . ILE A 50  ? 0.5640 0.6180 0.5222 -0.0203 0.0429  -0.0283 50  ILE A CD1 
457   N N   . LYS A 51  ? 0.6246 0.7080 0.5681 -0.0405 0.0534  0.0018  51  LYS A N   
458   C CA  . LYS A 51  ? 0.5656 0.6313 0.5086 -0.0478 0.0509  0.0136  51  LYS A CA  
459   C C   . LYS A 51  ? 0.6071 0.6523 0.5585 -0.0440 0.0462  0.0096  51  LYS A C   
460   O O   . LYS A 51  ? 0.6320 0.6806 0.5960 -0.0393 0.0462  0.0027  51  LYS A O   
461   C CB  . LYS A 51  ? 0.4705 0.5486 0.4188 -0.0548 0.0545  0.0199  51  LYS A CB  
462   C CG  . LYS A 51  ? 0.5020 0.5887 0.4395 -0.0641 0.0572  0.0322  51  LYS A CG  
463   C CD  . LYS A 51  ? 0.5839 0.6976 0.5148 -0.0621 0.0622  0.0290  51  LYS A CD  
464   C CE  . LYS A 51  ? 0.6589 0.7919 0.5858 -0.0724 0.0670  0.0409  51  LYS A CE  
465   N NZ  . LYS A 51  ? 0.7527 0.8679 0.6707 -0.0818 0.0638  0.0570  51  LYS A NZ  
466   N N   . LEU A 52  ? 0.5721 0.5974 0.5176 -0.0459 0.0422  0.0146  52  LEU A N   
467   C CA  . LEU A 52  ? 0.6242 0.6321 0.5761 -0.0440 0.0382  0.0126  52  LEU A CA  
468   C C   . LEU A 52  ? 0.6075 0.6015 0.5563 -0.0510 0.0366  0.0210  52  LEU A C   
469   O O   . LEU A 52  ? 0.7031 0.6930 0.6436 -0.0556 0.0367  0.0283  52  LEU A O   
470   C CB  . LEU A 52  ? 0.5796 0.5782 0.5290 -0.0383 0.0349  0.0074  52  LEU A CB  
471   C CG  . LEU A 52  ? 0.6168 0.6258 0.5709 -0.0314 0.0354  -0.0036 52  LEU A CG  
472   C CD1 . LEU A 52  ? 0.6654 0.6677 0.6149 -0.0279 0.0319  -0.0077 52  LEU A CD1 
473   C CD2 . LEU A 52  ? 0.6142 0.6222 0.5833 -0.0279 0.0348  -0.0089 52  LEU A CD2 
474   N N   . ASN A 53  ? 0.5378 0.5247 0.4938 -0.0519 0.0346  0.0200  53  ASN A N   
475   C CA  . ASN A 53  ? 0.6031 0.5781 0.5572 -0.0584 0.0330  0.0248  53  ASN A CA  
476   C C   . ASN A 53  ? 0.6650 0.6267 0.6202 -0.0555 0.0296  0.0216  53  ASN A C   
477   O O   . ASN A 53  ? 0.6807 0.6448 0.6422 -0.0508 0.0285  0.0174  53  ASN A O   
478   C CB  . ASN A 53  ? 0.6338 0.6181 0.5947 -0.0641 0.0340  0.0267  53  ASN A CB  
479   C CG  . ASN A 53  ? 0.5772 0.5791 0.5392 -0.0666 0.0379  0.0292  53  ASN A CG  
480   O OD1 . ASN A 53  ? 0.6352 0.6372 0.5914 -0.0731 0.0395  0.0355  53  ASN A OD1 
481   N ND2 . ASN A 53  ? 0.5685 0.5859 0.5390 -0.0614 0.0396  0.0247  53  ASN A ND2 
482   N N   . PHE A 54  ? 0.6373 0.5853 0.5875 -0.0586 0.0281  0.0238  54  PHE A N   
483   C CA  . PHE A 54  ? 0.5726 0.5102 0.5230 -0.0555 0.0257  0.0203  54  PHE A CA  
484   C C   . PHE A 54  ? 0.5455 0.4756 0.4959 -0.0611 0.0248  0.0198  54  PHE A C   
485   O O   . PHE A 54  ? 0.6110 0.5368 0.5595 -0.0671 0.0252  0.0228  54  PHE A O   
486   C CB  . PHE A 54  ? 0.6317 0.5607 0.5768 -0.0510 0.0244  0.0207  54  PHE A CB  
487   C CG  . PHE A 54  ? 0.6699 0.6077 0.6138 -0.0461 0.0248  0.0197  54  PHE A CG  
488   C CD1 . PHE A 54  ? 0.6615 0.6032 0.6103 -0.0411 0.0238  0.0140  54  PHE A CD1 
489   C CD2 . PHE A 54  ? 0.5533 0.4961 0.4911 -0.0472 0.0261  0.0242  54  PHE A CD2 
490   C CE1 . PHE A 54  ? 0.6576 0.6073 0.6058 -0.0369 0.0239  0.0108  54  PHE A CE1 
491   C CE2 . PHE A 54  ? 0.6868 0.6405 0.6224 -0.0428 0.0266  0.0215  54  PHE A CE2 
492   C CZ  . PHE A 54  ? 0.6390 0.5956 0.5800 -0.0375 0.0254  0.0137  54  PHE A CZ  
493   N N   . ASN A 55  ? 0.5932 0.5226 0.5460 -0.0595 0.0234  0.0158  55  ASN A N   
494   C CA  . ASN A 55  ? 0.6135 0.5379 0.5654 -0.0639 0.0226  0.0127  55  ASN A CA  
495   C C   . ASN A 55  ? 0.5473 0.4627 0.4975 -0.0593 0.0217  0.0085  55  ASN A C   
496   O O   . ASN A 55  ? 0.6191 0.5388 0.5712 -0.0543 0.0214  0.0074  55  ASN A O   
497   C CB  . ASN A 55  ? 0.5796 0.5161 0.5352 -0.0670 0.0219  0.0117  55  ASN A CB  
498   C CG  . ASN A 55  ? 0.6545 0.5889 0.6077 -0.0719 0.0211  0.0068  55  ASN A CG  
499   O OD1 . ASN A 55  ? 0.6676 0.6036 0.6206 -0.0789 0.0207  0.0061  55  ASN A OD1 
500   N ND2 . ASN A 55  ? 0.6158 0.5485 0.5677 -0.0686 0.0208  0.0024  55  ASN A ND2 
501   N N   . LEU A 56  ? 0.5883 0.4916 0.5363 -0.0609 0.0214  0.0059  56  LEU A N   
502   C CA  . LEU A 56  ? 0.5323 0.4277 0.4803 -0.0558 0.0208  0.0009  56  LEU A CA  
503   C C   . LEU A 56  ? 0.5676 0.4618 0.5158 -0.0596 0.0209  -0.0071 56  LEU A C   
504   O O   . LEU A 56  ? 0.5635 0.4513 0.5114 -0.0658 0.0206  -0.0086 56  LEU A O   
505   C CB  . LEU A 56  ? 0.6015 0.4827 0.5487 -0.0524 0.0197  0.0042  56  LEU A CB  
506   C CG  . LEU A 56  ? 0.5784 0.4628 0.5234 -0.0497 0.0195  0.0120  56  LEU A CG  
507   C CD1 . LEU A 56  ? 0.5932 0.4655 0.5372 -0.0455 0.0175  0.0162  56  LEU A CD1 
508   C CD2 . LEU A 56  ? 0.5451 0.4418 0.4912 -0.0450 0.0196  0.0107  56  LEU A CD2 
509   N N   . THR A 57  ? 0.6019 0.5038 0.5507 -0.0566 0.0215  -0.0126 57  THR A N   
510   C CA  . THR A 57  ? 0.5840 0.4869 0.5320 -0.0598 0.0220  -0.0221 57  THR A CA  
511   C C   . THR A 57  ? 0.5561 0.4427 0.5063 -0.0552 0.0218  -0.0288 57  THR A C   
512   O O   . THR A 57  ? 0.5711 0.4506 0.5236 -0.0480 0.0212  -0.0258 57  THR A O   
513   C CB  . THR A 57  ? 0.6233 0.5440 0.5707 -0.0593 0.0231  -0.0253 57  THR A CB  
514   O OG1 . THR A 57  ? 0.6420 0.5634 0.5919 -0.0518 0.0238  -0.0258 57  THR A OG1 
515   C CG2 . THR A 57  ? 0.5146 0.4498 0.4620 -0.0633 0.0224  -0.0173 57  THR A CG2 
516   N N   . PRO A 58  ? 0.6690 0.5494 0.6196 -0.0591 0.0217  -0.0382 58  PRO A N   
517   C CA  . PRO A 58  ? 0.6781 0.5413 0.6334 -0.0537 0.0212  -0.0460 58  PRO A CA  
518   C C   . PRO A 58  ? 0.6420 0.5124 0.5999 -0.0445 0.0228  -0.0522 58  PRO A C   
519   O O   . PRO A 58  ? 0.6943 0.5525 0.6577 -0.0364 0.0218  -0.0522 58  PRO A O   
520   C CB  . PRO A 58  ? 0.7900 0.6493 0.7453 -0.0609 0.0210  -0.0575 58  PRO A CB  
521   C CG  . PRO A 58  ? 0.7376 0.6055 0.6888 -0.0710 0.0203  -0.0503 58  PRO A CG  
522   C CD  . PRO A 58  ? 0.6271 0.5145 0.5750 -0.0688 0.0214  -0.0423 58  PRO A CD  
523   N N   . VAL A 59  ? 0.5739 0.4655 0.5287 -0.0457 0.0250  -0.0564 59  VAL A N   
524   C CA  . VAL A 59  ? 0.6594 0.5614 0.6174 -0.0381 0.0271  -0.0622 59  VAL A CA  
525   C C   . VAL A 59  ? 0.6033 0.5051 0.5643 -0.0317 0.0261  -0.0519 59  VAL A C   
526   O O   . VAL A 59  ? 0.5827 0.4846 0.5494 -0.0235 0.0264  -0.0553 59  VAL A O   
527   C CB  . VAL A 59  ? 0.5576 0.4851 0.5110 -0.0426 0.0298  -0.0669 59  VAL A CB  
528   C CG1 . VAL A 59  ? 0.6274 0.5671 0.5771 -0.0481 0.0289  -0.0540 59  VAL A CG1 
529   C CG2 . VAL A 59  ? 0.6168 0.5577 0.5741 -0.0356 0.0326  -0.0736 59  VAL A CG2 
530   N N   . LEU A 60  ? 0.5691 0.4717 0.5273 -0.0352 0.0246  -0.0401 60  LEU A N   
531   C CA  . LEU A 60  ? 0.6472 0.5480 0.6077 -0.0298 0.0231  -0.0319 60  LEU A CA  
532   C C   . LEU A 60  ? 0.6472 0.5293 0.6106 -0.0243 0.0207  -0.0298 60  LEU A C   
533   O O   . LEU A 60  ? 0.6242 0.5059 0.5919 -0.0168 0.0194  -0.0283 60  LEU A O   
534   C CB  . LEU A 60  ? 0.5885 0.4944 0.5459 -0.0344 0.0222  -0.0222 60  LEU A CB  
535   C CG  . LEU A 60  ? 0.5436 0.4502 0.5028 -0.0298 0.0205  -0.0155 60  LEU A CG  
536   C CD1 . LEU A 60  ? 0.5857 0.5043 0.5498 -0.0255 0.0209  -0.0180 60  LEU A CD1 
537   C CD2 . LEU A 60  ? 0.5430 0.4539 0.5002 -0.0340 0.0200  -0.0087 60  LEU A CD2 
538   N N   . ILE A 61  ? 0.5574 0.4246 0.5193 -0.0286 0.0197  -0.0288 61  ILE A N   
539   C CA  . ILE A 61  ? 0.6668 0.5149 0.6322 -0.0244 0.0170  -0.0247 61  ILE A CA  
540   C C   . ILE A 61  ? 0.7125 0.5546 0.6860 -0.0153 0.0166  -0.0333 61  ILE A C   
541   O O   . ILE A 61  ? 0.7426 0.5780 0.7208 -0.0075 0.0139  -0.0282 61  ILE A O   
542   C CB  . ILE A 61  ? 0.7759 0.6095 0.7399 -0.0324 0.0162  -0.0227 61  ILE A CB  
543   C CG1 . ILE A 61  ? 0.7193 0.5564 0.6775 -0.0381 0.0158  -0.0104 61  ILE A CG1 
544   C CG2 . ILE A 61  ? 0.7087 0.5197 0.6797 -0.0283 0.0135  -0.0230 61  ILE A CG2 
545   C CD1 . ILE A 61  ? 0.6586 0.4859 0.6160 -0.0474 0.0154  -0.0074 61  ILE A CD1 
546   N N   . ASP A 62  ? 0.6977 0.5443 0.6732 -0.0157 0.0191  -0.0467 62  ASP A N   
547   C CA  . ASP A 62  ? 0.6557 0.4985 0.6402 -0.0063 0.0194  -0.0576 62  ASP A CA  
548   C C   . ASP A 62  ? 0.7414 0.5990 0.7300 0.0023  0.0197  -0.0556 62  ASP A C   
549   O O   . ASP A 62  ? 0.7735 0.6242 0.7712 0.0123  0.0178  -0.0570 62  ASP A O   
550   C CB  . ASP A 62  ? 0.7062 0.5575 0.6904 -0.0092 0.0230  -0.0739 62  ASP A CB  
551   C CG  . ASP A 62  ? 0.8649 0.7007 0.8475 -0.0173 0.0220  -0.0788 62  ASP A CG  
552   O OD1 . ASP A 62  ? 0.9573 0.7713 0.9424 -0.0188 0.0187  -0.0708 62  ASP A OD1 
553   O OD2 . ASP A 62  ? 0.8759 0.7228 0.8548 -0.0228 0.0246  -0.0906 62  ASP A OD2 
554   N N   . GLN A 63  ? 0.6338 0.5119 0.6171 -0.0016 0.0216  -0.0520 63  GLN A N   
555   C CA  . GLN A 63  ? 0.6632 0.5571 0.6513 0.0049  0.0218  -0.0511 63  GLN A CA  
556   C C   . GLN A 63  ? 0.6932 0.5803 0.6833 0.0097  0.0174  -0.0397 63  GLN A C   
557   O O   . GLN A 63  ? 0.6453 0.5361 0.6434 0.0187  0.0158  -0.0404 63  GLN A O   
558   C CB  . GLN A 63  ? 0.6607 0.5765 0.6441 -0.0018 0.0246  -0.0496 63  GLN A CB  
559   C CG  . GLN A 63  ? 0.6684 0.5974 0.6499 -0.0057 0.0288  -0.0604 63  GLN A CG  
560   C CD  . GLN A 63  ? 0.7156 0.6654 0.6926 -0.0133 0.0308  -0.0557 63  GLN A CD  
561   O OE1 . GLN A 63  ? 0.7385 0.7040 0.7197 -0.0118 0.0317  -0.0533 63  GLN A OE1 
562   N NE2 . GLN A 63  ? 0.6642 0.6143 0.6338 -0.0219 0.0310  -0.0535 63  GLN A NE2 
563   N N   . ILE A 64  ? 0.6640 0.5433 0.6469 0.0040  0.0154  -0.0295 64  ILE A N   
564   C CA  . ILE A 64  ? 0.6646 0.5402 0.6471 0.0076  0.0113  -0.0188 64  ILE A CA  
565   C C   . ILE A 64  ? 0.6805 0.5398 0.6697 0.0156  0.0078  -0.0166 64  ILE A C   
566   O O   . ILE A 64  ? 0.6896 0.5518 0.6829 0.0227  0.0042  -0.0110 64  ILE A O   
567   C CB  . ILE A 64  ? 0.6859 0.5583 0.6591 -0.0004 0.0108  -0.0099 64  ILE A CB  
568   C CG1 . ILE A 64  ? 0.7237 0.6118 0.6932 -0.0064 0.0133  -0.0112 64  ILE A CG1 
569   C CG2 . ILE A 64  ? 0.6742 0.5446 0.6455 0.0028  0.0067  0.0005  64  ILE A CG2 
570   C CD1 . ILE A 64  ? 0.6154 0.5024 0.5778 -0.0132 0.0133  -0.0045 64  ILE A CD1 
571   N N   . GLN A 65  ? 0.6737 0.5155 0.6650 0.0143  0.0082  -0.0205 65  GLN A N   
572   C CA  . GLN A 65  ? 0.7288 0.5519 0.7289 0.0221  0.0043  -0.0178 65  GLN A CA  
573   C C   . GLN A 65  ? 0.7631 0.5925 0.7754 0.0340  0.0041  -0.0267 65  GLN A C   
574   O O   . GLN A 65  ? 0.8077 0.6304 0.8284 0.0433  -0.0004 -0.0208 65  GLN A O   
575   C CB  . GLN A 65  ? 0.6946 0.4961 0.6963 0.0172  0.0046  -0.0215 65  GLN A CB  
576   C CG  . GLN A 65  ? 0.6951 0.4899 0.6870 0.0058  0.0044  -0.0114 65  GLN A CG  
577   C CD  . GLN A 65  ? 0.8088 0.5857 0.8028 -0.0011 0.0051  -0.0174 65  GLN A CD  
578   O OE1 . GLN A 65  ? 0.8477 0.6301 0.8410 -0.0047 0.0085  -0.0309 65  GLN A OE1 
579   N NE2 . GLN A 65  ? 0.7946 0.5509 0.7914 -0.0035 0.0015  -0.0069 65  GLN A NE2 
580   N N   . GLU A 66  ? 0.7346 0.5789 0.7485 0.0339  0.0090  -0.0404 66  GLU A N   
581   C CA  . GLU A 66  ? 0.7639 0.6196 0.7899 0.0449  0.0098  -0.0497 66  GLU A CA  
582   C C   . GLU A 66  ? 0.7182 0.5915 0.7461 0.0494  0.0073  -0.0416 66  GLU A C   
583   O O   . GLU A 66  ? 0.7314 0.6068 0.7709 0.0606  0.0043  -0.0413 66  GLU A O   
584   C CB  . GLU A 66  ? 0.7403 0.6128 0.7658 0.0422  0.0161  -0.0653 66  GLU A CB  
585   C CG  . GLU A 66  ? 0.8094 0.6992 0.8474 0.0530  0.0182  -0.0757 66  GLU A CG  
586   C CD  . GLU A 66  ? 0.8084 0.7046 0.8497 0.0540  0.0237  -0.0945 66  GLU A CD  
587   O OE1 . GLU A 66  ? 0.8589 0.7486 0.8913 0.0449  0.0258  -0.0992 66  GLU A OE1 
588   O OE2 . GLU A 66  ? 0.8811 0.7910 0.9342 0.0639  0.0260  -0.1052 66  GLU A OE2 
589   N N   . TYR A 67  ? 0.6146 0.5009 0.6324 0.0409  0.0081  -0.0353 67  TYR A N   
590   C CA  . TYR A 67  ? 0.6272 0.5291 0.6463 0.0434  0.0051  -0.0282 67  TYR A CA  
591   C C   . TYR A 67  ? 0.6900 0.5804 0.7093 0.0483  -0.0015 -0.0158 67  TYR A C   
592   O O   . TYR A 67  ? 0.7618 0.6630 0.7876 0.0554  -0.0054 -0.0120 67  TYR A O   
593   C CB  . TYR A 67  ? 0.5903 0.5047 0.5996 0.0329  0.0070  -0.0252 67  TYR A CB  
594   C CG  . TYR A 67  ? 0.6531 0.5884 0.6654 0.0298  0.0115  -0.0331 67  TYR A CG  
595   C CD1 . TYR A 67  ? 0.6083 0.5632 0.6287 0.0334  0.0107  -0.0339 67  TYR A CD1 
596   C CD2 . TYR A 67  ? 0.6517 0.5887 0.6587 0.0223  0.0163  -0.0386 67  TYR A CD2 
597   C CE1 . TYR A 67  ? 0.5925 0.5676 0.6160 0.0292  0.0150  -0.0393 67  TYR A CE1 
598   C CE2 . TYR A 67  ? 0.6363 0.5940 0.6453 0.0186  0.0203  -0.0434 67  TYR A CE2 
599   C CZ  . TYR A 67  ? 0.6517 0.6279 0.6690 0.0217  0.0199  -0.0434 67  TYR A CZ  
600   O OH  . TYR A 67  ? 0.7059 0.7035 0.7255 0.0166  0.0240  -0.0466 67  TYR A OH  
601   N N   . ALA A 68  ? 0.7991 0.6697 0.8117 0.0440  -0.0030 -0.0086 68  ALA A N   
602   C CA  . ALA A 68  ? 0.7814 0.6423 0.7932 0.0475  -0.0091 0.0053  68  ALA A CA  
603   C C   . ALA A 68  ? 0.7852 0.6328 0.8109 0.0593  -0.0131 0.0062  68  ALA A C   
604   O O   . ALA A 68  ? 0.8098 0.6553 0.8379 0.0649  -0.0192 0.0185  68  ALA A O   
605   C CB  . ALA A 68  ? 0.6774 0.5235 0.6779 0.0379  -0.0089 0.0138  68  ALA A CB  
606   N N   . GLN A 69  ? 0.8320 0.6715 0.8672 0.0634  -0.0099 -0.0067 69  GLN A N   
607   C CA  . GLN A 69  ? 0.8408 0.6670 0.8925 0.0761  -0.0131 -0.0093 69  GLN A CA  
608   C C   . GLN A 69  ? 0.9264 0.7737 0.9909 0.0873  -0.0127 -0.0179 69  GLN A C   
609   O O   . GLN A 69  ? 0.9627 0.8024 1.0435 0.0996  -0.0147 -0.0228 69  GLN A O   
610   C CB  . GLN A 69  ? 0.9030 0.7084 0.9593 0.0746  -0.0097 -0.0211 69  GLN A CB  
611   C CG  . GLN A 69  ? 0.9548 0.7333 1.0060 0.0671  -0.0124 -0.0107 69  GLN A CG  
612   C CD  . GLN A 69  ? 1.0319 0.7968 1.0818 0.0596  -0.0079 -0.0240 69  GLN A CD  
613   O OE1 . GLN A 69  ? 1.0074 0.7713 1.0672 0.0653  -0.0050 -0.0412 69  GLN A OE1 
614   N NE2 . GLN A 69  ? 1.0275 0.7846 1.0655 0.0465  -0.0072 -0.0169 69  GLN A NE2 
615   N N   . GLY A 70  ? 0.9134 0.7872 0.9725 0.0833  -0.0101 -0.0202 70  GLY A N   
616   C CA  . GLY A 70  ? 0.8787 0.7760 0.9501 0.0922  -0.0096 -0.0274 70  GLY A CA  
617   C C   . GLY A 70  ? 0.8836 0.7869 0.9649 0.0968  -0.0033 -0.0456 70  GLY A C   
618   O O   . GLY A 70  ? 0.9876 0.9080 1.0833 0.1071  -0.0030 -0.0522 70  GLY A O   
619   N N   . LYS A 71  ? 0.9296 0.8221 1.0037 0.0892  0.0019  -0.0543 71  LYS A N   
620   C CA  . LYS A 71  ? 0.9431 0.8422 1.0248 0.0930  0.0081  -0.0730 71  LYS A CA  
621   C C   . LYS A 71  ? 0.7890 0.7146 0.8622 0.0834  0.0150  -0.0805 71  LYS A C   
622   O O   . LYS A 71  ? 0.8868 0.8272 0.9661 0.0866  0.0207  -0.0957 71  LYS A O   
623   C CB  . LYS A 71  ? 0.8908 0.7616 0.9718 0.0914  0.0087  -0.0800 71  LYS A CB  
624   C CG  . LYS A 71  ? 0.9953 0.8350 1.0820 0.0965  0.0013  -0.0681 71  LYS A CG  
625   C CD  . LYS A 71  ? 1.1179 0.9495 1.2266 0.1139  -0.0019 -0.0740 71  LYS A CD  
626   C CE  . LYS A 71  ? 1.0831 0.9286 1.2000 0.1236  -0.0076 -0.0613 71  LYS A CE  
627   N NZ  . LYS A 71  ? 1.0800 0.9069 1.2171 0.1393  -0.0141 -0.0582 71  LYS A NZ  
628   N N   . ALA A 72  ? 0.8050 0.7378 0.8649 0.0719  0.0148  -0.0702 72  ALA A N   
629   C CA  . ALA A 72  ? 0.7874 0.7430 0.8402 0.0621  0.0206  -0.0748 72  ALA A CA  
630   C C   . ALA A 72  ? 0.7689 0.7542 0.8324 0.0670  0.0224  -0.0780 72  ALA A C   
631   O O   . ALA A 72  ? 0.8200 0.8120 0.8882 0.0700  0.0178  -0.0691 72  ALA A O   
632   C CB  . ALA A 72  ? 0.7066 0.6593 0.7451 0.0496  0.0192  -0.0628 72  ALA A CB  
633   N N   . LYS A 73  ? 0.7656 0.7708 0.8331 0.0675  0.0290  -0.0908 73  LYS A N   
634   C CA  . LYS A 73  ? 0.7514 0.7886 0.8298 0.0709  0.0317  -0.0943 73  LYS A CA  
635   C C   . LYS A 73  ? 0.7814 0.8389 0.8512 0.0568  0.0346  -0.0880 73  LYS A C   
636   O O   . LYS A 73  ? 0.8399 0.9189 0.9081 0.0515  0.0410  -0.0947 73  LYS A O   
637   C CB  . LYS A 73  ? 0.7377 0.7887 0.8269 0.0801  0.0376  -0.1121 73  LYS A CB  
638   C CG  . LYS A 73  ? 0.7415 0.7718 0.8437 0.0957  0.0341  -0.1189 73  LYS A CG  
639   C CD  . LYS A 73  ? 0.8824 0.9095 0.9874 0.1002  0.0397  -0.1384 73  LYS A CD  
640   C CE  . LYS A 73  ? 0.9602 0.9498 1.0710 0.1091  0.0347  -0.1411 73  LYS A CE  
641   N NZ  . LYS A 73  ? 0.8977 0.8672 0.9962 0.1004  0.0366  -0.1480 73  LYS A NZ  
642   N N   . ASP A 74  ? 0.6878 0.7386 0.7524 0.0507  0.0295  -0.0746 74  ASP A N   
643   C CA  . ASP A 74  ? 0.5928 0.6581 0.6516 0.0377  0.0308  -0.0672 74  ASP A CA  
644   C C   . ASP A 74  ? 0.6270 0.7239 0.6984 0.0380  0.0326  -0.0681 74  ASP A C   
645   O O   . ASP A 74  ? 0.7293 0.8313 0.8106 0.0441  0.0281  -0.0653 74  ASP A O   
646   C CB  . ASP A 74  ? 0.6251 0.6731 0.6766 0.0325  0.0247  -0.0553 74  ASP A CB  
647   C CG  . ASP A 74  ? 0.7214 0.7775 0.7672 0.0193  0.0256  -0.0483 74  ASP A CG  
648   O OD1 . ASP A 74  ? 0.6708 0.7488 0.7244 0.0154  0.0264  -0.0466 74  ASP A OD1 
649   O OD2 . ASP A 74  ? 0.7455 0.7860 0.7803 0.0127  0.0254  -0.0443 74  ASP A OD2 
650   N N   . VAL A 75  ? 0.6905 0.8104 0.7614 0.0305  0.0389  -0.0709 75  VAL A N   
651   C CA  . VAL A 75  ? 0.6626 0.8156 0.7464 0.0297  0.0415  -0.0717 75  VAL A CA  
652   C C   . VAL A 75  ? 0.5769 0.7337 0.6633 0.0208  0.0367  -0.0596 75  VAL A C   
653   O O   . VAL A 75  ? 0.6791 0.8534 0.7785 0.0235  0.0346  -0.0588 75  VAL A O   
654   C CB  . VAL A 75  ? 0.6744 0.8538 0.7564 0.0233  0.0500  -0.0771 75  VAL A CB  
655   C CG1 . VAL A 75  ? 0.6992 0.8934 0.7899 0.0357  0.0552  -0.0930 75  VAL A CG1 
656   C CG2 . VAL A 75  ? 0.6122 0.7776 0.6776 0.0140  0.0517  -0.0745 75  VAL A CG2 
657   N N   . PHE A 76  ? 0.5947 0.7358 0.6701 0.0102  0.0347  -0.0510 76  PHE A N   
658   C CA  . PHE A 76  ? 0.5922 0.7342 0.6709 0.0016  0.0298  -0.0414 76  PHE A CA  
659   C C   . PHE A 76  ? 0.6308 0.7602 0.7127 0.0091  0.0224  -0.0404 76  PHE A C   
660   O O   . PHE A 76  ? 0.6705 0.8132 0.7624 0.0071  0.0187  -0.0378 76  PHE A O   
661   C CB  . PHE A 76  ? 0.6701 0.7963 0.7376 -0.0095 0.0292  -0.0337 76  PHE A CB  
662   C CG  . PHE A 76  ? 0.6379 0.7666 0.7109 -0.0195 0.0253  -0.0253 76  PHE A CG  
663   C CD1 . PHE A 76  ? 0.6926 0.8439 0.7740 -0.0295 0.0280  -0.0204 76  PHE A CD1 
664   C CD2 . PHE A 76  ? 0.5574 0.6667 0.6277 -0.0193 0.0189  -0.0227 76  PHE A CD2 
665   C CE1 . PHE A 76  ? 0.7664 0.9174 0.8549 -0.0393 0.0238  -0.0131 76  PHE A CE1 
666   C CE2 . PHE A 76  ? 0.6672 0.7778 0.7438 -0.0282 0.0150  -0.0174 76  PHE A CE2 
667   C CZ  . PHE A 76  ? 0.7897 0.9195 0.8762 -0.0383 0.0172  -0.0127 76  PHE A CZ  
668   N N   . LEU A 77  ? 0.6539 0.7594 0.7277 0.0170  0.0200  -0.0420 77  LEU A N   
669   C CA  . LEU A 77  ? 0.6284 0.7239 0.7038 0.0240  0.0128  -0.0394 77  LEU A CA  
670   C C   . LEU A 77  ? 0.7105 0.8257 0.8011 0.0341  0.0111  -0.0432 77  LEU A C   
671   O O   . LEU A 77  ? 0.7282 0.8480 0.8239 0.0364  0.0047  -0.0397 77  LEU A O   
672   C CB  . LEU A 77  ? 0.6305 0.6983 0.6952 0.0300  0.0111  -0.0389 77  LEU A CB  
673   C CG  . LEU A 77  ? 0.7316 0.7811 0.7849 0.0242  0.0067  -0.0318 77  LEU A CG  
674   C CD1 . LEU A 77  ? 0.7609 0.7886 0.8074 0.0318  0.0039  -0.0298 77  LEU A CD1 
675   C CD2 . LEU A 77  ? 0.6417 0.7023 0.6999 0.0207  0.0012  -0.0283 77  LEU A CD2 
676   N N   . GLU A 78  ? 0.6799 0.8088 0.7782 0.0405  0.0167  -0.0510 78  GLU A N   
677   C CA  . GLU A 78  ? 0.6808 0.8321 0.7960 0.0506  0.0157  -0.0553 78  GLU A CA  
678   C C   . GLU A 78  ? 0.6635 0.8432 0.7892 0.0422  0.0149  -0.0522 78  GLU A C   
679   O O   . GLU A 78  ? 0.6388 0.8337 0.7770 0.0481  0.0101  -0.0517 78  GLU A O   
680   C CB  . GLU A 78  ? 0.6701 0.8315 0.7919 0.0592  0.0227  -0.0664 78  GLU A CB  
681   C CG  . GLU A 78  ? 0.7865 0.9631 0.9267 0.0750  0.0210  -0.0724 78  GLU A CG  
682   C CD  . GLU A 78  ? 0.9139 1.0735 1.0567 0.0847  0.0114  -0.0657 78  GLU A CD  
683   O OE1 . GLU A 78  ? 0.7238 0.9029 0.8820 0.0927  0.0074  -0.0652 78  GLU A OE1 
684   O OE2 . GLU A 78  ? 0.9800 1.1090 1.1101 0.0846  0.0079  -0.0606 78  GLU A OE2 
685   N N   . ALA A 79  ? 0.5760 0.7635 0.6978 0.0280  0.0191  -0.0494 79  ALA A N   
686   C CA  . ALA A 79  ? 0.6159 0.8264 0.7479 0.0176  0.0176  -0.0449 79  ALA A CA  
687   C C   . ALA A 79  ? 0.6896 0.8884 0.8202 0.0143  0.0086  -0.0395 79  ALA A C   
688   O O   . ALA A 79  ? 0.6731 0.8915 0.8161 0.0117  0.0046  -0.0385 79  ALA A O   
689   C CB  . ALA A 79  ? 0.5979 0.8144 0.7254 0.0027  0.0232  -0.0407 79  ALA A CB  
690   N N   . ILE A 80  ? 0.5935 0.7628 0.7093 0.0140  0.0055  -0.0366 80  ILE A N   
691   C CA  . ILE A 80  ? 0.6303 0.7900 0.7433 0.0122  -0.0028 -0.0332 80  ILE A CA  
692   C C   . ILE A 80  ? 0.6441 0.8096 0.7629 0.0252  -0.0086 -0.0343 80  ILE A C   
693   O O   . ILE A 80  ? 0.6370 0.8151 0.7625 0.0239  -0.0152 -0.0332 80  ILE A O   
694   C CB  . ILE A 80  ? 0.6211 0.7509 0.7169 0.0087  -0.0036 -0.0302 80  ILE A CB  
695   C CG1 . ILE A 80  ? 0.6426 0.7679 0.7344 -0.0030 0.0018  -0.0281 80  ILE A CG1 
696   C CG2 . ILE A 80  ? 0.6553 0.7787 0.7477 0.0061  -0.0114 -0.0283 80  ILE A CG2 
697   C CD1 . ILE A 80  ? 0.5857 0.7146 0.6827 -0.0157 -0.0012 -0.0250 80  ILE A CD1 
698   N N   . ARG A 81  ? 0.6256 0.7829 0.7432 0.0378  -0.0067 -0.0364 81  ARG A N   
699   C CA  . ARG A 81  ? 0.6187 0.7760 0.7410 0.0511  -0.0132 -0.0350 81  ARG A CA  
700   C C   . ARG A 81  ? 0.6919 0.8814 0.8337 0.0561  -0.0157 -0.0373 81  ARG A C   
701   O O   . ARG A 81  ? 0.6548 0.8525 0.8011 0.0604  -0.0238 -0.0338 81  ARG A O   
702   C CB  . ARG A 81  ? 0.6757 0.8139 0.7945 0.0629  -0.0104 -0.0369 81  ARG A CB  
703   C CG  . ARG A 81  ? 0.7646 0.8964 0.8879 0.0772  -0.0175 -0.0329 81  ARG A CG  
704   C CD  . ARG A 81  ? 0.9105 1.0673 1.0549 0.0892  -0.0175 -0.0379 81  ARG A CD  
705   N NE  . ARG A 81  ? 1.0670 1.2241 1.2208 0.1039  -0.0253 -0.0331 81  ARG A NE  
706   C CZ  . ARG A 81  ? 1.1006 1.2576 1.2506 0.1045  -0.0347 -0.0237 81  ARG A CZ  
707   N NH1 . ARG A 81  ? 1.0680 1.2191 1.2026 0.0919  -0.0372 -0.0193 81  ARG A NH1 
708   N NH2 . ARG A 81  ? 1.0192 1.1842 1.1818 0.1185  -0.0419 -0.0190 81  ARG A NH2 
709   N N   . LYS A 82  ? 0.6895 0.9001 0.8428 0.0552  -0.0087 -0.0429 82  LYS A N   
710   C CA  . LYS A 82  ? 0.5502 0.7940 0.7240 0.0616  -0.0098 -0.0460 82  LYS A CA  
711   C C   . LYS A 82  ? 0.6233 0.8875 0.8044 0.0514  -0.0158 -0.0427 82  LYS A C   
712   O O   . LYS A 82  ? 0.7097 0.9674 0.8831 0.0366  -0.0161 -0.0401 82  LYS A O   
713   C CB  . LYS A 82  ? 0.5898 0.8547 0.7729 0.0606  0.0002  -0.0530 82  LYS A CB  
714   C CG  . LYS A 82  ? 0.7534 1.0178 0.9432 0.0772  0.0044  -0.0608 82  LYS A CG  
715   C CD  . LYS A 82  ? 0.6905 0.9723 0.8832 0.0738  0.0156  -0.0690 82  LYS A CD  
716   C CE  . LYS A 82  ? 0.5632 0.8646 0.7552 0.0551  0.0190  -0.0646 82  LYS A CE  
717   N NZ  . LYS A 82  ? 0.6093 0.9391 0.8078 0.0525  0.0295  -0.0713 82  LYS A NZ  
718   N N   . ASP A 83  ? 0.6543 0.9439 0.8521 0.0596  -0.0209 -0.0433 83  ASP A N   
719   C CA  . ASP A 83  ? 0.5867 0.9026 0.7955 0.0492  -0.0258 -0.0421 83  ASP A CA  
720   C C   . ASP A 83  ? 0.5976 0.9316 0.8135 0.0352  -0.0178 -0.0442 83  ASP A C   
721   O O   . ASP A 83  ? 0.6446 0.9896 0.8661 0.0393  -0.0091 -0.0482 83  ASP A O   
722   C CB  . ASP A 83  ? 0.5984 0.9437 0.8266 0.0613  -0.0318 -0.0428 83  ASP A CB  
723   C CG  . ASP A 83  ? 0.6193 0.9910 0.8582 0.0503  -0.0387 -0.0418 83  ASP A CG  
724   O OD1 . ASP A 83  ? 0.6552 1.0551 0.9092 0.0418  -0.0345 -0.0443 83  ASP A OD1 
725   O OD2 . ASP A 83  ? 0.6586 1.0239 0.8907 0.0493  -0.0484 -0.0385 83  ASP A OD2 
726   N N   . PRO A 84  ? 0.6047 0.9423 0.8208 0.0183  -0.0204 -0.0417 84  PRO A N   
727   C CA  . PRO A 84  ? 0.5899 0.9440 0.8136 0.0036  -0.0133 -0.0409 84  PRO A CA  
728   C C   . PRO A 84  ? 0.5710 0.9669 0.8164 0.0059  -0.0093 -0.0436 84  PRO A C   
729   O O   . PRO A 84  ? 0.6353 1.0476 0.8862 -0.0039 -0.0013 -0.0425 84  PRO A O   
730   C CB  . PRO A 84  ? 0.5465 0.8950 0.7698 -0.0132 -0.0197 -0.0378 84  PRO A CB  
731   C CG  . PRO A 84  ? 0.5438 0.8625 0.7506 -0.0076 -0.0269 -0.0380 84  PRO A CG  
732   C CD  . PRO A 84  ? 0.5623 0.8878 0.7714 0.0112  -0.0299 -0.0395 84  PRO A CD  
733   N N   . ASP A 85  ? 0.5297 0.9456 0.7883 0.0187  -0.0146 -0.0464 85  ASP A N   
734   C CA  . ASP A 85  ? 0.5427 1.0005 0.8234 0.0230  -0.0101 -0.0500 85  ASP A CA  
735   C C   . ASP A 85  ? 0.5473 1.0076 0.8276 0.0357  0.0002  -0.0558 85  ASP A C   
736   O O   . ASP A 85  ? 0.6028 1.0986 0.8991 0.0365  0.0072  -0.0597 85  ASP A O   
737   C CB  . ASP A 85  ? 0.5722 1.0518 0.8687 0.0343  -0.0194 -0.0512 85  ASP A CB  
738   C CG  . ASP A 85  ? 0.5820 1.0779 0.8871 0.0193  -0.0280 -0.0481 85  ASP A CG  
739   O OD1 . ASP A 85  ? 0.5287 1.0328 0.8373 0.0004  -0.0247 -0.0461 85  ASP A OD1 
740   O OD2 . ASP A 85  ? 0.6484 1.1492 0.9572 0.0263  -0.0385 -0.0477 85  ASP A OD2 
741   N N   . ASP A 86  ? 0.5664 0.9916 0.8295 0.0452  0.0013  -0.0573 86  ASP A N   
742   C CA  . ASP A 86  ? 0.6045 1.0282 0.8659 0.0566  0.0106  -0.0648 86  ASP A CA  
743   C C   . ASP A 86  ? 0.5794 0.9910 0.8254 0.0439  0.0194  -0.0640 86  ASP A C   
744   O O   . ASP A 86  ? 0.6059 1.0092 0.8452 0.0518  0.0264  -0.0707 86  ASP A O   
745   C CB  . ASP A 86  ? 0.6137 1.0069 0.8679 0.0750  0.0063  -0.0671 86  ASP A CB  
746   C CG  . ASP A 86  ? 0.6499 1.0610 0.9233 0.0921  -0.0004 -0.0689 86  ASP A CG  
747   O OD1 . ASP A 86  ? 0.6272 1.0699 0.9197 0.1013  0.0047  -0.0764 86  ASP A OD1 
748   O OD2 . ASP A 86  ? 0.6172 1.0126 0.8869 0.0965  -0.0108 -0.0625 86  ASP A OD2 
749   N N   . LEU A 87  ? 0.5711 0.9822 0.8122 0.0245  0.0187  -0.0562 87  LEU A N   
750   C CA  . LEU A 87  ? 0.6110 1.0056 0.8362 0.0120  0.0248  -0.0525 87  LEU A CA  
751   C C   . LEU A 87  ? 0.6479 1.0787 0.8821 0.0017  0.0343  -0.0519 87  LEU A C   
752   O O   . LEU A 87  ? 0.6330 1.0904 0.8814 -0.0099 0.0332  -0.0468 87  LEU A O   
753   C CB  . LEU A 87  ? 0.5642 0.9337 0.7796 -0.0023 0.0179  -0.0436 87  LEU A CB  
754   C CG  . LEU A 87  ? 0.5505 0.8778 0.7472 0.0036  0.0129  -0.0430 87  LEU A CG  
755   C CD1 . LEU A 87  ? 0.5597 0.8692 0.7504 -0.0107 0.0068  -0.0362 87  LEU A CD1 
756   C CD2 . LEU A 87  ? 0.5917 0.9020 0.7737 0.0065  0.0203  -0.0453 87  LEU A CD2 
757   N N   . GLU A 88  ? 0.6565 1.0889 0.8820 0.0048  0.0434  -0.0568 88  GLU A N   
758   C CA  . GLU A 88  ? 0.6019 1.0678 0.8314 -0.0065 0.0531  -0.0549 88  GLU A CA  
759   C C   . GLU A 88  ? 0.5875 1.0426 0.8085 -0.0278 0.0520  -0.0409 88  GLU A C   
760   O O   . GLU A 88  ? 0.6868 1.1047 0.8956 -0.0315 0.0455  -0.0356 88  GLU A O   
761   C CB  . GLU A 88  ? 0.6205 1.0904 0.8406 0.0025  0.0626  -0.0652 88  GLU A CB  
762   C CG  . GLU A 88  ? 0.6246 1.1017 0.8545 0.0247  0.0639  -0.0804 88  GLU A CG  
763   C CD  . GLU A 88  ? 0.7149 1.2249 0.9690 0.0304  0.0613  -0.0821 88  GLU A CD  
764   O OE1 . GLU A 88  ? 0.7482 1.3010 1.0152 0.0220  0.0676  -0.0810 88  GLU A OE1 
765   O OE2 . GLU A 88  ? 0.7069 1.2017 0.9675 0.0428  0.0528  -0.0838 88  GLU A OE2 
766   N N   . LYS A 89  ? 0.5561 1.0451 0.7847 -0.0417 0.0585  -0.0345 89  LYS A N   
767   C CA  . LYS A 89  ? 0.5670 1.0484 0.7920 -0.0626 0.0569  -0.0192 89  LYS A CA  
768   C C   . LYS A 89  ? 0.6346 1.0832 0.8376 -0.0649 0.0579  -0.0154 89  LYS A C   
769   O O   . LYS A 89  ? 0.6620 1.0840 0.8595 -0.0759 0.0524  -0.0050 89  LYS A O   
770   C CB  . LYS A 89  ? 0.4951 1.0219 0.7326 -0.0770 0.0644  -0.0115 89  LYS A CB  
771   C CG  . LYS A 89  ? 0.6212 1.1835 0.8828 -0.0786 0.0630  -0.0129 89  LYS A CG  
772   C CD  . LYS A 89  ? 0.6460 1.2301 0.9199 -0.1021 0.0634  0.0029  89  LYS A CD  
773   C CE  . LYS A 89  ? 0.7902 1.3441 1.0693 -0.1129 0.0516  0.0107  89  LYS A CE  
774   N NZ  . LYS A 89  ? 0.6943 1.2731 0.9967 -0.1169 0.0465  0.0093  89  LYS A NZ  
775   N N   . GLU A 90  ? 0.6091 1.0601 0.8006 -0.0546 0.0649  -0.0245 90  GLU A N   
776   C CA  . GLU A 90  ? 0.6636 1.0879 0.8346 -0.0572 0.0660  -0.0214 90  GLU A CA  
777   C C   . GLU A 90  ? 0.7559 1.1329 0.9171 -0.0515 0.0572  -0.0217 90  GLU A C   
778   O O   . GLU A 90  ? 0.6819 1.0339 0.8321 -0.0601 0.0543  -0.0127 90  GLU A O   
779   C CB  . GLU A 90  ? 0.8422 1.2799 1.0040 -0.0465 0.0747  -0.0342 90  GLU A CB  
780   C CG  . GLU A 90  ? 0.8705 1.3178 1.0424 -0.0273 0.0759  -0.0510 90  GLU A CG  
781   C CD  . GLU A 90  ? 0.9400 1.4383 1.1256 -0.0258 0.0850  -0.0579 90  GLU A CD  
782   O OE1 . GLU A 90  ? 0.8032 1.3315 0.9993 -0.0399 0.0869  -0.0472 90  GLU A OE1 
783   O OE2 . GLU A 90  ? 1.1699 1.6787 1.3569 -0.0104 0.0903  -0.0744 90  GLU A OE2 
784   N N   . GLU A 91  ? 0.6972 1.0634 0.8629 -0.0369 0.0527  -0.0313 91  GLU A N   
785   C CA  . GLU A 91  ? 0.6396 0.9649 0.7960 -0.0315 0.0445  -0.0313 91  GLU A CA  
786   C C   . GLU A 91  ? 0.5710 0.8844 0.7320 -0.0441 0.0370  -0.0209 91  GLU A C   
787   O O   . GLU A 91  ? 0.6140 0.8953 0.7641 -0.0467 0.0323  -0.0170 91  GLU A O   
788   C CB  . GLU A 91  ? 0.5657 0.8863 0.7272 -0.0136 0.0411  -0.0419 91  GLU A CB  
789   C CG  . GLU A 91  ? 0.6260 0.9682 0.7921 -0.0009 0.0486  -0.0539 91  GLU A CG  
790   C CD  . GLU A 91  ? 0.6934 1.0285 0.8670 0.0176  0.0442  -0.0627 91  GLU A CD  
791   O OE1 . GLU A 91  ? 0.6152 0.9197 0.7781 0.0271  0.0419  -0.0666 91  GLU A OE1 
792   O OE2 . GLU A 91  ? 0.6787 1.0396 0.8699 0.0223  0.0427  -0.0648 91  GLU A OE2 
793   N N   . VAL A 92  ? 0.5011 0.8409 0.6792 -0.0523 0.0359  -0.0171 92  VAL A N   
794   C CA  . VAL A 92  ? 0.5988 0.9279 0.7834 -0.0654 0.0287  -0.0088 92  VAL A CA  
795   C C   . VAL A 92  ? 0.5836 0.9006 0.7618 -0.0802 0.0302  0.0029  92  VAL A C   
796   O O   . VAL A 92  ? 0.6739 0.9619 0.8480 -0.0855 0.0241  0.0072  92  VAL A O   
797   C CB  . VAL A 92  ? 0.5223 0.8846 0.7285 -0.0719 0.0271  -0.0077 92  VAL A CB  
798   C CG1 . VAL A 92  ? 0.4707 0.8215 0.6848 -0.0877 0.0199  0.0003  92  VAL A CG1 
799   C CG2 . VAL A 92  ? 0.5677 0.9396 0.7810 -0.0564 0.0236  -0.0182 92  VAL A CG2 
800   N N   . GLU A 93  ? 0.5264 0.8667 0.7041 -0.0867 0.0382  0.0084  93  GLU A N   
801   C CA  . GLU A 93  ? 0.6184 0.9481 0.7890 -0.0996 0.0395  0.0211  93  GLU A CA  
802   C C   . GLU A 93  ? 0.6431 0.9378 0.7947 -0.0922 0.0381  0.0187  93  GLU A C   
803   O O   . GLU A 93  ? 0.5882 0.8608 0.7357 -0.1005 0.0346  0.0281  93  GLU A O   
804   C CB  . GLU A 93  ? 0.6466 1.0123 0.8179 -0.1069 0.0487  0.0272  93  GLU A CB  
805   C CG  . GLU A 93  ? 0.7997 1.1731 0.9784 -0.1270 0.0484  0.0460  93  GLU A CG  
806   C CD  . GLU A 93  ? 1.0062 1.3513 1.1712 -0.1316 0.0464  0.0558  93  GLU A CD  
807   O OE1 . GLU A 93  ? 1.0113 1.3311 1.1822 -0.1401 0.0393  0.0649  93  GLU A OE1 
808   O OE2 . GLU A 93  ? 0.9243 1.2734 1.0737 -0.1268 0.0519  0.0539  93  GLU A OE2 
809   N N   . LYS A 94  ? 0.6295 0.9187 0.7708 -0.0768 0.0404  0.0064  94  LYS A N   
810   C CA  . LYS A 94  ? 0.5639 0.8206 0.6883 -0.0700 0.0387  0.0036  94  LYS A CA  
811   C C   . LYS A 94  ? 0.6245 0.8495 0.7484 -0.0694 0.0301  0.0044  94  LYS A C   
812   O O   . LYS A 94  ? 0.5794 0.7792 0.6940 -0.0720 0.0277  0.0088  94  LYS A O   
813   C CB  . LYS A 94  ? 0.6327 0.8898 0.7495 -0.0540 0.0423  -0.0101 94  LYS A CB  
814   C CG  . LYS A 94  ? 0.7340 1.0106 0.8432 -0.0536 0.0509  -0.0133 94  LYS A CG  
815   C CD  . LYS A 94  ? 0.8369 1.1048 0.9386 -0.0376 0.0532  -0.0281 94  LYS A CD  
816   C CE  . LYS A 94  ? 0.7684 1.0059 0.8694 -0.0272 0.0459  -0.0322 94  LYS A CE  
817   N NZ  . LYS A 94  ? 0.7358 0.9662 0.8341 -0.0116 0.0475  -0.0454 94  LYS A NZ  
818   N N   . LEU A 95  ? 0.6375 0.8655 0.7716 -0.0655 0.0253  -0.0006 95  LEU A N   
819   C CA  . LEU A 95  ? 0.5782 0.7807 0.7118 -0.0653 0.0172  -0.0014 95  LEU A CA  
820   C C   . LEU A 95  ? 0.5919 0.7853 0.7320 -0.0802 0.0138  0.0083  95  LEU A C   
821   O O   . LEU A 95  ? 0.6622 0.8284 0.7960 -0.0810 0.0097  0.0093  95  LEU A O   
822   C CB  . LEU A 95  ? 0.6623 0.8761 0.8061 -0.0593 0.0125  -0.0082 95  LEU A CB  
823   C CG  . LEU A 95  ? 0.8214 1.0181 0.9553 -0.0446 0.0090  -0.0160 95  LEU A CG  
824   C CD1 . LEU A 95  ? 0.7509 0.9526 0.8784 -0.0322 0.0149  -0.0213 95  LEU A CD1 
825   C CD2 . LEU A 95  ? 0.6584 0.8649 0.8028 -0.0417 0.0021  -0.0200 95  LEU A CD2 
826   N N   . ILE A 96  ? 0.5557 0.7720 0.7096 -0.0921 0.0156  0.0157  96  ILE A N   
827   C CA  . ILE A 96  ? 0.6040 0.8109 0.7679 -0.1069 0.0115  0.0258  96  ILE A CA  
828   C C   . ILE A 96  ? 0.5879 0.7784 0.7422 -0.1113 0.0136  0.0355  96  ILE A C   
829   O O   . ILE A 96  ? 0.5287 0.6960 0.6861 -0.1172 0.0087  0.0405  96  ILE A O   
830   C CB  . ILE A 96  ? 0.5555 0.7927 0.7380 -0.1195 0.0128  0.0327  96  ILE A CB  
831   C CG1 . ILE A 96  ? 0.5563 0.8129 0.7485 -0.1139 0.0106  0.0226  96  ILE A CG1 
832   C CG2 . ILE A 96  ? 0.5617 0.7855 0.7573 -0.1351 0.0073  0.0426  96  ILE A CG2 
833   C CD1 . ILE A 96  ? 0.5299 0.8190 0.7423 -0.1266 0.0115  0.0284  96  ILE A CD1 
834   N N   . GLU A 97  ? 0.5790 0.7820 0.7223 -0.1079 0.0207  0.0375  97  GLU A N   
835   C CA  . GLU A 97  ? 0.6287 0.8188 0.7621 -0.1117 0.0221  0.0468  97  GLU A CA  
836   C C   . GLU A 97  ? 0.7507 0.9088 0.8712 -0.1019 0.0189  0.0402  97  GLU A C   
837   O O   . GLU A 97  ? 0.7378 0.8770 0.8558 -0.1059 0.0164  0.0476  97  GLU A O   
838   C CB  . GLU A 97  ? 0.6755 0.8911 0.8000 -0.1115 0.0303  0.0493  97  GLU A CB  
839   C CG  . GLU A 97  ? 0.9313 1.1824 1.0676 -0.1229 0.0346  0.0584  97  GLU A CG  
840   C CD  . GLU A 97  ? 1.1067 1.3558 1.2526 -0.1394 0.0318  0.0776  97  GLU A CD  
841   O OE1 . GLU A 97  ? 1.1068 1.3426 1.2676 -0.1462 0.0254  0.0812  97  GLU A OE1 
842   O OE2 . GLU A 97  ? 1.1641 1.4247 1.3031 -0.1456 0.0354  0.0890  97  GLU A OE2 
843   N N   . PHE A 98  ? 0.6689 0.8215 0.7822 -0.0893 0.0187  0.0271  98  PHE A N   
844   C CA  . PHE A 98  ? 0.6142 0.7382 0.7161 -0.0812 0.0155  0.0217  98  PHE A CA  
845   C C   . PHE A 98  ? 0.6747 0.7787 0.7845 -0.0853 0.0085  0.0223  98  PHE A C   
846   O O   . PHE A 98  ? 0.7650 0.8471 0.8695 -0.0846 0.0062  0.0238  98  PHE A O   
847   C CB  . PHE A 98  ? 0.5831 0.7065 0.6773 -0.0678 0.0163  0.0096  98  PHE A CB  
848   C CG  . PHE A 98  ? 0.6917 0.7894 0.7727 -0.0601 0.0144  0.0054  98  PHE A CG  
849   C CD1 . PHE A 98  ? 0.6886 0.7780 0.7579 -0.0592 0.0176  0.0077  98  PHE A CD1 
850   C CD2 . PHE A 98  ? 0.7185 0.8030 0.7987 -0.0542 0.0093  -0.0008 98  PHE A CD2 
851   C CE1 . PHE A 98  ? 0.7027 0.7703 0.7611 -0.0529 0.0160  0.0042  98  PHE A CE1 
852   C CE2 . PHE A 98  ? 0.6731 0.7368 0.7412 -0.0479 0.0080  -0.0038 98  PHE A CE2 
853   C CZ  . PHE A 98  ? 0.7905 0.8454 0.8483 -0.0473 0.0115  -0.0012 98  PHE A CZ  
854   N N   . THR A 99  ? 0.5792 0.6920 0.7027 -0.0897 0.0049  0.0203  99  THR A N   
855   C CA  . THR A 99  ? 0.6190 0.7143 0.7515 -0.0945 -0.0020 0.0188  99  THR A CA  
856   C C   . THR A 99  ? 0.6579 0.7445 0.8003 -0.1062 -0.0033 0.0307  99  THR A C   
857   O O   . THR A 99  ? 0.7259 0.7898 0.8718 -0.1075 -0.0080 0.0297  99  THR A O   
858   C CB  . THR A 99  ? 0.6599 0.7691 0.8053 -0.0972 -0.0059 0.0128  99  THR A CB  
859   O OG1 . THR A 99  ? 0.6554 0.7752 0.7929 -0.0856 -0.0049 0.0040  99  THR A OG1 
860   C CG2 . THR A 99  ? 0.5585 0.6490 0.7113 -0.1007 -0.0134 0.0071  99  THR A CG2 
861   N N   . LYS A 100 ? 0.6033 0.7083 0.7507 -0.1147 0.0007  0.0425  100 LYS A N   
862   C CA  . LYS A 100 ? 0.6621 0.7593 0.8196 -0.1262 -0.0011 0.0569  100 LYS A CA  
863   C C   . LYS A 100 ? 0.6114 0.6898 0.7574 -0.1215 -0.0006 0.0611  100 LYS A C   
864   O O   . LYS A 100 ? 0.6414 0.7010 0.7960 -0.1264 -0.0049 0.0683  100 LYS A O   
865   C CB  . LYS A 100 ? 0.8541 0.9801 1.0187 -0.1370 0.0033  0.0701  100 LYS A CB  
866   C CG  . LYS A 100 ? 0.8727 0.9934 1.0501 -0.1508 0.0008  0.0885  100 LYS A CG  
867   C CD  . LYS A 100 ? 0.8095 0.9392 0.9750 -0.1517 0.0056  0.1012  100 LYS A CD  
868   C CE  . LYS A 100 ? 0.8289 0.9412 1.0041 -0.1605 0.0010  0.1185  100 LYS A CE  
869   N NZ  . LYS A 100 ? 0.7535 0.8716 0.9146 -0.1589 0.0042  0.1290  100 LYS A NZ  
870   N N   . LEU A 101 ? 0.6504 0.7331 0.7785 -0.1120 0.0042  0.0562  101 LEU A N   
871   C CA  . LEU A 101 ? 0.6207 0.6884 0.7377 -0.1078 0.0046  0.0596  101 LEU A CA  
872   C C   . LEU A 101 ? 0.7160 0.7562 0.8325 -0.1013 -0.0002 0.0513  101 LEU A C   
873   O O   . LEU A 101 ? 0.6949 0.7198 0.8112 -0.1011 -0.0020 0.0567  101 LEU A O   
874   C CB  . LEU A 101 ? 0.6352 0.7146 0.7342 -0.0999 0.0107  0.0544  101 LEU A CB  
875   C CG  . LEU A 101 ? 0.8492 0.9163 0.9351 -0.0952 0.0115  0.0557  101 LEU A CG  
876   C CD1 . LEU A 101 ? 0.8169 0.8894 0.9056 -0.1040 0.0114  0.0721  101 LEU A CD1 
877   C CD2 . LEU A 101 ? 0.7430 0.8189 0.8131 -0.0868 0.0167  0.0462  101 LEU A CD2 
878   N N   . ASN A 102 ? 0.7220 0.7580 0.8386 -0.0958 -0.0023 0.0382  102 ASN A N   
879   C CA  . ASN A 102 ? 0.6165 0.6311 0.7307 -0.0893 -0.0062 0.0285  102 ASN A CA  
880   C C   . ASN A 102 ? 0.6157 0.6213 0.7463 -0.0946 -0.0123 0.0241  102 ASN A C   
881   O O   . ASN A 102 ? 0.6123 0.6039 0.7414 -0.0894 -0.0155 0.0134  102 ASN A O   
882   C CB  . ASN A 102 ? 0.5949 0.6115 0.6944 -0.0786 -0.0045 0.0168  102 ASN A CB  
883   C CG  . ASN A 102 ? 0.7139 0.7417 0.8001 -0.0741 0.0013  0.0189  102 ASN A CG  
884   O OD1 . ASN A 102 ? 0.7371 0.7652 0.8192 -0.0764 0.0040  0.0268  102 ASN A OD1 
885   N ND2 . ASN A 102 ? 0.7030 0.7399 0.7829 -0.0673 0.0029  0.0113  102 ASN A ND2 
886   N N   . TYR A 103 ? 0.6878 0.7021 0.8343 -0.1055 -0.0139 0.0318  103 TYR A N   
887   C CA  . TYR A 103 ? 0.6351 0.6427 0.7986 -0.1117 -0.0200 0.0260  103 TYR A CA  
888   C C   . TYR A 103 ? 0.6150 0.5963 0.7858 -0.1106 -0.0247 0.0220  103 TYR A C   
889   O O   . TYR A 103 ? 0.6768 0.6490 0.8547 -0.1103 -0.0295 0.0092  103 TYR A O   
890   C CB  . TYR A 103 ? 0.5833 0.6040 0.7641 -0.1254 -0.0206 0.0380  103 TYR A CB  
891   C CG  . TYR A 103 ? 0.6452 0.6627 0.8450 -0.1337 -0.0269 0.0317  103 TYR A CG  
892   C CD1 . TYR A 103 ? 0.7375 0.7729 0.9385 -0.1338 -0.0279 0.0220  103 TYR A CD1 
893   C CD2 . TYR A 103 ? 0.7079 0.7049 0.9261 -0.1417 -0.0324 0.0354  103 TYR A CD2 
894   C CE1 . TYR A 103 ? 0.6873 0.7215 0.9061 -0.1425 -0.0342 0.0155  103 TYR A CE1 
895   C CE2 . TYR A 103 ? 0.8078 0.8010 1.0447 -0.1503 -0.0386 0.0284  103 TYR A CE2 
896   C CZ  . TYR A 103 ? 0.7146 0.7271 0.9512 -0.1512 -0.0395 0.0182  103 TYR A CZ  
897   O OH  . TYR A 103 ? 0.7706 0.7800 1.0264 -0.1609 -0.0462 0.0106  103 TYR A OH  
898   N N   . GLU A 104 ? 0.6073 0.5776 0.7772 -0.1098 -0.0235 0.0321  104 GLU A N   
899   C CA  . GLU A 104 ? 0.6786 0.6248 0.8590 -0.1084 -0.0279 0.0296  104 GLU A CA  
900   C C   . GLU A 104 ? 0.6626 0.5994 0.8280 -0.0960 -0.0262 0.0200  104 GLU A C   
901   O O   . GLU A 104 ? 0.7111 0.6298 0.8845 -0.0929 -0.0290 0.0170  104 GLU A O   
902   C CB  . GLU A 104 ? 0.7278 0.6675 0.9215 -0.1158 -0.0292 0.0486  104 GLU A CB  
903   C CG  . GLU A 104 ? 0.7895 0.7254 1.0070 -0.1287 -0.0342 0.0553  104 GLU A CG  
904   C CD  . GLU A 104 ? 1.0031 0.9523 1.2261 -0.1393 -0.0324 0.0780  104 GLU A CD  
905   O OE1 . GLU A 104 ? 1.2851 1.2308 1.5052 -0.1377 -0.0315 0.0913  104 GLU A OE1 
906   O OE2 . GLU A 104 ? 1.0728 1.0381 1.3035 -0.1495 -0.0321 0.0830  104 GLU A OE2 
907   N N   . LYS A 105 ? 0.6395 0.5882 0.7849 -0.0889 -0.0216 0.0152  105 LYS A N   
908   C CA  . LYS A 105 ? 0.5512 0.4920 0.6833 -0.0785 -0.0202 0.0057  105 LYS A CA  
909   C C   . LYS A 105 ? 0.5744 0.5112 0.7073 -0.0750 -0.0236 -0.0115 105 LYS A C   
910   O O   . LYS A 105 ? 0.6317 0.5787 0.7663 -0.0781 -0.0253 -0.0168 105 LYS A O   
911   C CB  . LYS A 105 ? 0.5804 0.5333 0.6921 -0.0728 -0.0147 0.0074  105 LYS A CB  
912   C CG  . LYS A 105 ? 0.6140 0.5726 0.7221 -0.0755 -0.0113 0.0219  105 LYS A CG  
913   C CD  . LYS A 105 ? 0.6754 0.6489 0.7670 -0.0721 -0.0062 0.0217  105 LYS A CD  
914   C CE  . LYS A 105 ? 0.6188 0.5972 0.7028 -0.0729 -0.0027 0.0320  105 LYS A CE  
915   N NZ  . LYS A 105 ? 0.6340 0.6275 0.7049 -0.0706 0.0022  0.0305  105 LYS A NZ  
916   N N   . PRO A 106 ? 0.5561 0.4807 0.6881 -0.0688 -0.0246 -0.0207 106 PRO A N   
917   C CA  . PRO A 106 ? 0.5944 0.5176 0.7270 -0.0661 -0.0278 -0.0382 106 PRO A CA  
918   C C   . PRO A 106 ? 0.5389 0.4777 0.6545 -0.0623 -0.0265 -0.0447 106 PRO A C   
919   O O   . PRO A 106 ? 0.5538 0.4974 0.6713 -0.0630 -0.0303 -0.0569 106 PRO A O   
920   C CB  . PRO A 106 ? 0.6113 0.5226 0.7430 -0.0588 -0.0271 -0.0453 106 PRO A CB  
921   C CG  . PRO A 106 ? 0.5351 0.4363 0.6771 -0.0607 -0.0265 -0.0311 106 PRO A CG  
922   C CD  . PRO A 106 ? 0.5151 0.4284 0.6480 -0.0645 -0.0232 -0.0161 106 PRO A CD  
923   N N   . ILE A 107 ? 0.5166 0.4637 0.6164 -0.0583 -0.0220 -0.0371 107 ILE A N   
924   C CA  . ILE A 107 ? 0.5688 0.5292 0.6546 -0.0540 -0.0215 -0.0417 107 ILE A CA  
925   C C   . ILE A 107 ? 0.6915 0.6653 0.7841 -0.0591 -0.0237 -0.0402 107 ILE A C   
926   O O   . ILE A 107 ? 0.6350 0.6209 0.7196 -0.0556 -0.0248 -0.0447 107 ILE A O   
927   C CB  . ILE A 107 ? 0.4855 0.4483 0.5547 -0.0480 -0.0163 -0.0347 107 ILE A CB  
928   C CG1 . ILE A 107 ? 0.5665 0.5304 0.6388 -0.0518 -0.0131 -0.0221 107 ILE A CG1 
929   C CG2 . ILE A 107 ? 0.5722 0.5261 0.6332 -0.0427 -0.0144 -0.0378 107 ILE A CG2 
930   C CD1 . ILE A 107 ? 0.4981 0.4701 0.5571 -0.0476 -0.0092 -0.0178 107 ILE A CD1 
931   N N   . TYR A 108 ? 0.6361 0.6098 0.7441 -0.0675 -0.0244 -0.0330 108 TYR A N   
932   C CA  . TYR A 108 ? 0.5646 0.5531 0.6820 -0.0738 -0.0264 -0.0314 108 TYR A CA  
933   C C   . TYR A 108 ? 0.5676 0.5530 0.7023 -0.0815 -0.0326 -0.0395 108 TYR A C   
934   O O   . TYR A 108 ? 0.7382 0.7339 0.8859 -0.0898 -0.0345 -0.0361 108 TYR A O   
935   C CB  . TYR A 108 ? 0.4921 0.4870 0.6149 -0.0794 -0.0225 -0.0170 108 TYR A CB  
936   C CG  . TYR A 108 ? 0.5918 0.6009 0.7013 -0.0737 -0.0175 -0.0126 108 TYR A CG  
937   C CD1 . TYR A 108 ? 0.5686 0.5713 0.6622 -0.0657 -0.0136 -0.0116 108 TYR A CD1 
938   C CD2 . TYR A 108 ? 0.6194 0.6485 0.7339 -0.0763 -0.0165 -0.0104 108 TYR A CD2 
939   C CE1 . TYR A 108 ? 0.5724 0.5857 0.6557 -0.0604 -0.0094 -0.0092 108 TYR A CE1 
940   C CE2 . TYR A 108 ? 0.6164 0.6578 0.7207 -0.0699 -0.0119 -0.0083 108 TYR A CE2 
941   C CZ  . TYR A 108 ? 0.5224 0.5545 0.6113 -0.0620 -0.0085 -0.0081 108 TYR A CZ  
942   O OH  . TYR A 108 ? 0.5993 0.6414 0.6798 -0.0556 -0.0042 -0.0075 108 TYR A OH  
943   N N   . ARG A 109 ? 0.5733 0.5455 0.7092 -0.0793 -0.0357 -0.0509 109 ARG A N   
944   C CA  . ARG A 109 ? 0.5935 0.5595 0.7473 -0.0867 -0.0419 -0.0609 109 ARG A CA  
945   C C   . ARG A 109 ? 0.6641 0.6463 0.8142 -0.0863 -0.0462 -0.0739 109 ARG A C   
946   O O   . ARG A 109 ? 0.6208 0.6015 0.7660 -0.0826 -0.0491 -0.0888 109 ARG A O   
947   C CB  . ARG A 109 ? 0.7146 0.6601 0.8734 -0.0838 -0.0432 -0.0692 109 ARG A CB  
948   C CG  . ARG A 109 ? 0.7915 0.7244 0.9739 -0.0923 -0.0495 -0.0778 109 ARG A CG  
949   C CD  . ARG A 109 ? 0.8629 0.7730 1.0594 -0.0930 -0.0493 -0.0710 109 ARG A CD  
950   N NE  . ARG A 109 ? 0.8172 0.7182 1.0042 -0.0821 -0.0470 -0.0794 109 ARG A NE  
951   C CZ  . ARG A 109 ? 0.8848 0.7740 1.0731 -0.0778 -0.0440 -0.0696 109 ARG A CZ  
952   N NH1 . ARG A 109 ? 0.8593 0.7433 1.0571 -0.0834 -0.0434 -0.0506 109 ARG A NH1 
953   N NH2 . ARG A 109 ? 0.8930 0.7779 1.0729 -0.0679 -0.0417 -0.0786 109 ARG A NH2 
954   N N   . PHE A 110 ? 0.7482 0.7487 0.9005 -0.0900 -0.0464 -0.0679 110 PHE A N   
955   C CA  . PHE A 110 ? 0.6529 0.6721 0.8052 -0.0911 -0.0514 -0.0778 110 PHE A CA  
956   C C   . PHE A 110 ? 0.6764 0.7009 0.8513 -0.1043 -0.0557 -0.0773 110 PHE A C   
957   O O   . PHE A 110 ? 0.7116 0.7393 0.8960 -0.1104 -0.0528 -0.0637 110 PHE A O   
958   C CB  . PHE A 110 ? 0.6125 0.6512 0.7503 -0.0834 -0.0486 -0.0717 110 PHE A CB  
959   C CG  . PHE A 110 ? 0.6130 0.6475 0.7291 -0.0715 -0.0453 -0.0722 110 PHE A CG  
960   C CD1 . PHE A 110 ? 0.5903 0.6142 0.6977 -0.0666 -0.0388 -0.0620 110 PHE A CD1 
961   C CD2 . PHE A 110 ? 0.5862 0.6293 0.6907 -0.0659 -0.0490 -0.0824 110 PHE A CD2 
962   C CE1 . PHE A 110 ? 0.5673 0.5876 0.6562 -0.0570 -0.0360 -0.0619 110 PHE A CE1 
963   C CE2 . PHE A 110 ? 0.5110 0.5513 0.5961 -0.0561 -0.0460 -0.0809 110 PHE A CE2 
964   C CZ  . PHE A 110 ? 0.5141 0.5422 0.5921 -0.0519 -0.0394 -0.0707 110 PHE A CZ  
965   N N   . GLU A 111 ? 0.6677 0.6944 0.8513 -0.1093 -0.0627 -0.0924 111 GLU A N   
966   C CA  . GLU A 111 ? 0.7489 0.7794 0.9560 -0.1234 -0.0678 -0.0935 111 GLU A CA  
967   C C   . GLU A 111 ? 0.7315 0.7874 0.9430 -0.1274 -0.0664 -0.0823 111 GLU A C   
968   O O   . GLU A 111 ? 0.8165 0.8750 1.0466 -0.1392 -0.0667 -0.0735 111 GLU A O   
969   C CB  . GLU A 111 ? 0.8220 0.8553 1.0346 -0.1270 -0.0759 -0.1142 111 GLU A CB  
970   C CG  . GLU A 111 ? 0.8672 0.8967 1.1067 -0.1427 -0.0820 -0.1181 111 GLU A CG  
971   C CD  . GLU A 111 ? 1.0465 1.0455 1.3019 -0.1482 -0.0813 -0.1132 111 GLU A CD  
972   O OE1 . GLU A 111 ? 1.1411 1.1201 1.3902 -0.1405 -0.0802 -0.1208 111 GLU A OE1 
973   O OE2 . GLU A 111 ? 1.1164 1.1132 1.3914 -0.1602 -0.0818 -0.1007 111 GLU A OE2 
974   N N   . ARG A 112 ? 0.5881 0.6639 0.7837 -0.1176 -0.0649 -0.0822 112 ARG A N   
975   C CA  . ARG A 112 ? 0.6647 0.7663 0.8652 -0.1191 -0.0632 -0.0729 112 ARG A CA  
976   C C   . ARG A 112 ? 0.6929 0.7918 0.8966 -0.1214 -0.0556 -0.0560 112 ARG A C   
977   O O   . ARG A 112 ? 0.7046 0.8216 0.9218 -0.1293 -0.0544 -0.0480 112 ARG A O   
978   C CB  . ARG A 112 ? 0.6371 0.7564 0.8201 -0.1059 -0.0629 -0.0751 112 ARG A CB  
979   C CG  . ARG A 112 ? 0.5799 0.7296 0.7709 -0.1063 -0.0633 -0.0701 112 ARG A CG  
980   C CD  . ARG A 112 ? 0.6525 0.8192 0.8640 -0.1192 -0.0705 -0.0766 112 ARG A CD  
981   N NE  . ARG A 112 ? 0.7464 0.9458 0.9617 -0.1155 -0.0725 -0.0754 112 ARG A NE  
982   C CZ  . ARG A 112 ? 0.7656 0.9879 1.0004 -0.1250 -0.0732 -0.0714 112 ARG A CZ  
983   N NH1 . ARG A 112 ? 0.6483 0.8644 0.9010 -0.1405 -0.0728 -0.0677 112 ARG A NH1 
984   N NH2 . ARG A 112 ? 0.7183 0.9714 0.9562 -0.1191 -0.0747 -0.0705 112 ARG A NH2 
985   N N   . ILE A 113 ? 0.6211 0.7002 0.8127 -0.1149 -0.0504 -0.0505 113 ILE A N   
986   C CA  . ILE A 113 ? 0.5913 0.6692 0.7841 -0.1171 -0.0435 -0.0349 113 ILE A CA  
987   C C   . ILE A 113 ? 0.6693 0.7404 0.8835 -0.1324 -0.0452 -0.0273 113 ILE A C   
988   O O   . ILE A 113 ? 0.7721 0.8558 0.9937 -0.1392 -0.0411 -0.0139 113 ILE A O   
989   C CB  . ILE A 113 ? 0.6359 0.6947 0.8113 -0.1074 -0.0386 -0.0316 113 ILE A CB  
990   C CG1 . ILE A 113 ? 0.6843 0.7507 0.8398 -0.0934 -0.0364 -0.0359 113 ILE A CG1 
991   C CG2 . ILE A 113 ? 0.6699 0.7273 0.8478 -0.1117 -0.0327 -0.0159 113 ILE A CG2 
992   C CD1 . ILE A 113 ? 0.5915 0.6716 0.7401 -0.0884 -0.0296 -0.0264 113 ILE A CD1 
993   N N   . ARG A 114 ? 0.6366 0.6880 0.8615 -0.1382 -0.0512 -0.0355 114 ARG A N   
994   C CA  . ARG A 114 ? 0.7112 0.7550 0.9599 -0.1537 -0.0544 -0.0285 114 ARG A CA  
995   C C   . ARG A 114 ? 0.7351 0.8060 0.9988 -0.1648 -0.0561 -0.0254 114 ARG A C   
996   O O   . ARG A 114 ? 0.7442 0.8233 1.0203 -0.1754 -0.0534 -0.0101 114 ARG A O   
997   C CB  . ARG A 114 ? 0.7791 0.7978 1.0389 -0.1573 -0.0615 -0.0419 114 ARG A CB  
998   C CG  . ARG A 114 ? 0.9627 0.9544 1.2358 -0.1631 -0.0618 -0.0317 114 ARG A CG  
999   C CD  . ARG A 114 ? 0.9311 0.8989 1.2196 -0.1669 -0.0694 -0.0473 114 ARG A CD  
1000  N NE  . ARG A 114 ? 1.1000 1.0802 1.4027 -0.1773 -0.0759 -0.0587 114 ARG A NE  
1001  C CZ  . ARG A 114 ? 1.2194 1.1831 1.5408 -0.1849 -0.0835 -0.0729 114 ARG A CZ  
1002  N NH1 . ARG A 114 ? 1.2511 1.1839 1.5806 -0.1825 -0.0857 -0.0780 114 ARG A NH1 
1003  N NH2 . ARG A 114 ? 1.1323 1.1115 1.4652 -0.1947 -0.0894 -0.0834 114 ARG A NH2 
1004  N N   . GLU A 115 ? 0.6681 0.7555 0.9308 -0.1627 -0.0605 -0.0391 115 GLU A N   
1005  C CA  . GLU A 115 ? 0.6998 0.8154 0.9786 -0.1732 -0.0628 -0.0373 115 GLU A CA  
1006  C C   . GLU A 115 ? 0.6516 0.7932 0.9260 -0.1706 -0.0548 -0.0231 115 GLU A C   
1007  O O   . GLU A 115 ? 0.6820 0.8376 0.9721 -0.1830 -0.0527 -0.0108 115 GLU A O   
1008  C CB  . GLU A 115 ? 0.6942 0.8255 0.9707 -0.1695 -0.0694 -0.0545 115 GLU A CB  
1009  C CG  . GLU A 115 ? 0.7036 0.8133 0.9715 -0.1639 -0.0749 -0.0717 115 GLU A CG  
1010  C CD  . GLU A 115 ? 0.7703 0.8997 1.0381 -0.1634 -0.0825 -0.0879 115 GLU A CD  
1011  O OE1 . GLU A 115 ? 0.7796 0.9385 1.0447 -0.1595 -0.0821 -0.0852 115 GLU A OE1 
1012  O OE2 . GLU A 115 ? 0.8415 0.9581 1.1127 -0.1666 -0.0892 -0.1039 115 GLU A OE2 
1013  N N   . LEU A 116 ? 0.6316 0.7804 0.8852 -0.1546 -0.0502 -0.0249 116 LEU A N   
1014  C CA  . LEU A 116 ? 0.6076 0.7836 0.8579 -0.1504 -0.0430 -0.0158 116 LEU A CA  
1015  C C   . LEU A 116 ? 0.6860 0.8602 0.9392 -0.1573 -0.0361 0.0007  116 LEU A C   
1016  O O   . LEU A 116 ? 0.7059 0.9076 0.9663 -0.1620 -0.0312 0.0094  116 LEU A O   
1017  C CB  . LEU A 116 ? 0.4658 0.6436 0.6940 -0.1316 -0.0399 -0.0212 116 LEU A CB  
1018  C CG  . LEU A 116 ? 0.6785 0.8604 0.9010 -0.1235 -0.0468 -0.0352 116 LEU A CG  
1019  C CD1 . LEU A 116 ? 0.6395 0.8127 0.8392 -0.1062 -0.0440 -0.0377 116 LEU A CD1 
1020  C CD2 . LEU A 116 ? 0.5904 0.8064 0.8266 -0.1262 -0.0501 -0.0379 116 LEU A CD2 
1021  N N   . MET A 117 ? 0.6569 0.8018 0.9052 -0.1583 -0.0357 0.0053  117 MET A N   
1022  C CA  . MET A 117 ? 0.6547 0.7987 0.9056 -0.1655 -0.0302 0.0226  117 MET A CA  
1023  C C   . MET A 117 ? 0.6995 0.8491 0.9751 -0.1849 -0.0332 0.0330  117 MET A C   
1024  O O   . MET A 117 ? 0.7183 0.8862 0.9996 -0.1934 -0.0280 0.0484  117 MET A O   
1025  C CB  . MET A 117 ? 0.7268 0.8391 0.9658 -0.1596 -0.0296 0.0250  117 MET A CB  
1026  C CG  . MET A 117 ? 0.7042 0.8137 0.9193 -0.1423 -0.0255 0.0178  117 MET A CG  
1027  S SD  . MET A 117 ? 0.6913 0.8286 0.8950 -0.1373 -0.0155 0.0270  117 MET A SD  
1028  C CE  . MET A 117 ? 0.7002 0.8374 0.9130 -0.1517 -0.0124 0.0476  117 MET A CE  
1029  N N   . ASN A 118 ? 0.7240 0.8592 1.0148 -0.1927 -0.0416 0.0245  118 ASN A N   
1030  C CA  . ASN A 118 ? 0.7023 0.8432 1.0192 -0.2123 -0.0455 0.0329  118 ASN A CA  
1031  C C   . ASN A 118 ? 0.6953 0.8756 1.0223 -0.2183 -0.0444 0.0324  118 ASN A C   
1032  O O   . ASN A 118 ? 0.7776 0.9702 1.1262 -0.2357 -0.0459 0.0425  118 ASN A O   
1033  C CB  . ASN A 118 ? 0.7003 0.8124 1.0313 -0.2185 -0.0552 0.0212  118 ASN A CB  
1034  C CG  . ASN A 118 ? 0.8864 0.9608 1.2110 -0.2124 -0.0563 0.0215  118 ASN A CG  
1035  O OD1 . ASN A 118 ? 0.9555 1.0247 1.2703 -0.2085 -0.0507 0.0353  118 ASN A OD1 
1036  N ND2 . ASN A 118 ? 0.9413 0.9912 1.2719 -0.2115 -0.0637 0.0053  118 ASN A ND2 
1037  N N   . LYS A 119 ? 0.6777 0.8783 0.9909 -0.2045 -0.0420 0.0219  119 LYS A N   
1038  C CA  . LYS A 119 ? 0.7044 0.9443 1.0279 -0.2078 -0.0411 0.0204  119 LYS A CA  
1039  C C   . LYS A 119 ? 0.7499 1.0186 1.0734 -0.2104 -0.0313 0.0358  119 LYS A C   
1040  O O   . LYS A 119 ? 0.7088 0.9737 1.0145 -0.2003 -0.0242 0.0408  119 LYS A O   
1041  C CB  . LYS A 119 ? 0.6666 0.9171 0.9766 -0.1909 -0.0429 0.0043  119 LYS A CB  
1042  C CG  . LYS A 119 ? 0.6961 0.9567 1.0200 -0.1965 -0.0524 -0.0088 119 LYS A CG  
1043  C CD  . LYS A 119 ? 0.7599 1.0183 1.0670 -0.1794 -0.0563 -0.0243 119 LYS A CD  
1044  C CE  . LYS A 119 ? 0.8677 1.1273 1.1855 -0.1860 -0.0672 -0.0388 119 LYS A CE  
1045  N NZ  . LYS A 119 ? 0.9423 1.1992 1.2418 -0.1701 -0.0715 -0.0524 119 LYS A NZ  
1046  N N   . GLU A 120 ? 0.7776 1.0773 1.1216 -0.2248 -0.0309 0.0427  120 GLU A N   
1047  C CA  . GLU A 120 ? 0.8025 1.1340 1.1495 -0.2305 -0.0214 0.0580  120 GLU A CA  
1048  C C   . GLU A 120 ? 0.8426 1.2075 1.1792 -0.2146 -0.0145 0.0505  120 GLU A C   
1049  O O   . GLU A 120 ? 0.8629 1.2406 1.1875 -0.2084 -0.0053 0.0570  120 GLU A O   
1050  C CB  . GLU A 120 ? 0.7441 1.0974 1.1185 -0.2533 -0.0233 0.0692  120 GLU A CB  
1051  C CG  . GLU A 120 ? 0.9268 1.2942 1.3194 -0.2589 -0.0315 0.0565  120 GLU A CG  
1052  C CD  . GLU A 120 ? 0.9564 1.2850 1.3530 -0.2616 -0.0429 0.0447  120 GLU A CD  
1053  O OE1 . GLU A 120 ? 1.0041 1.2969 1.4008 -0.2675 -0.0452 0.0512  120 GLU A OE1 
1054  O OE2 . GLU A 120 ? 0.9599 1.2951 1.3594 -0.2570 -0.0495 0.0283  120 GLU A OE2 
1055  N N   . LYS A 121 ? 0.8100 1.1897 1.1517 -0.2076 -0.0192 0.0366  121 LYS A N   
1056  C CA  . LYS A 121 ? 0.7673 1.1744 1.1011 -0.1902 -0.0144 0.0281  121 LYS A CA  
1057  C C   . LYS A 121 ? 0.8353 1.2231 1.1575 -0.1743 -0.0216 0.0124  121 LYS A C   
1058  O O   . LYS A 121 ? 0.9066 1.2762 1.2340 -0.1801 -0.0309 0.0059  121 LYS A O   
1059  C CB  . LYS A 121 ? 0.7939 1.2496 1.1496 -0.1977 -0.0126 0.0295  121 LYS A CB  
1060  C CG  . LYS A 121 ? 0.8620 1.3456 1.2158 -0.1792 -0.0110 0.0179  121 LYS A CG  
1061  C CD  . LYS A 121 ? 0.9001 1.4285 1.2617 -0.1785 -0.0002 0.0233  121 LYS A CD  
1062  C CE  . LYS A 121 ? 0.8898 1.4362 1.2449 -0.1552 0.0030  0.0115  121 LYS A CE  
1063  N NZ  . LYS A 121 ? 0.5674 1.1274 0.9118 -0.1464 0.0153  0.0138  121 LYS A NZ  
1064  N N   . LEU A 122 ? 0.7904 1.1824 1.0971 -0.1546 -0.0173 0.0062  122 LEU A N   
1065  C CA  . LEU A 122 ? 0.6720 1.0440 0.9645 -0.1387 -0.0232 -0.0058 122 LEU A CA  
1066  C C   . LEU A 122 ? 0.6203 1.0228 0.9170 -0.1246 -0.0238 -0.0133 122 LEU A C   
1067  O O   . LEU A 122 ? 0.6955 1.1215 0.9932 -0.1167 -0.0158 -0.0115 122 LEU A O   
1068  C CB  . LEU A 122 ? 0.6638 1.0038 0.9324 -0.1272 -0.0190 -0.0052 122 LEU A CB  
1069  C CG  . LEU A 122 ? 0.6581 0.9651 0.9224 -0.1386 -0.0199 0.0014  122 LEU A CG  
1070  C CD1 . LEU A 122 ? 0.4348 0.7152 0.6768 -0.1273 -0.0154 0.0023  122 LEU A CD1 
1071  C CD2 . LEU A 122 ? 0.6566 0.9441 0.9267 -0.1455 -0.0303 -0.0057 122 LEU A CD2 
1072  N N   . ASN A 123 ? 0.6215 1.0244 0.9209 -0.1208 -0.0334 -0.0221 123 ASN A N   
1073  C CA  . ASN A 123 ? 0.5262 0.9547 0.8290 -0.1057 -0.0358 -0.0285 123 ASN A CA  
1074  C C   . ASN A 123 ? 0.5586 0.9635 0.8395 -0.0857 -0.0358 -0.0325 123 ASN A C   
1075  O O   . ASN A 123 ? 0.6129 0.9838 0.8761 -0.0843 -0.0335 -0.0310 123 ASN A O   
1076  C CB  . ASN A 123 ? 0.4749 0.9204 0.7922 -0.1123 -0.0469 -0.0347 123 ASN A CB  
1077  C CG  . ASN A 123 ? 0.6357 1.0497 0.9408 -0.1143 -0.0561 -0.0414 123 ASN A CG  
1078  O OD1 . ASN A 123 ? 0.6905 1.0806 0.9755 -0.1010 -0.0568 -0.0443 123 ASN A OD1 
1079  N ND2 . ASN A 123 ? 0.5587 0.9740 0.8771 -0.1315 -0.0631 -0.0447 123 ASN A ND2 
1080  N N   . ARG A 124 ? 0.5492 0.9727 0.8325 -0.0702 -0.0387 -0.0368 124 ARG A N   
1081  C CA  . ARG A 124 ? 0.5391 0.9423 0.8042 -0.0511 -0.0384 -0.0388 124 ARG A CA  
1082  C C   . ARG A 124 ? 0.4637 0.8338 0.7114 -0.0517 -0.0456 -0.0414 124 ARG A C   
1083  O O   . ARG A 124 ? 0.5027 0.8431 0.7317 -0.0448 -0.0426 -0.0403 124 ARG A O   
1084  C CB  . ARG A 124 ? 0.4973 0.9277 0.7719 -0.0349 -0.0418 -0.0417 124 ARG A CB  
1085  C CG  . ARG A 124 ? 0.5461 0.9547 0.8042 -0.0164 -0.0448 -0.0426 124 ARG A CG  
1086  C CD  . ARG A 124 ? 0.5560 0.9901 0.8251 -0.0036 -0.0530 -0.0440 124 ARG A CD  
1087  N NE  . ARG A 124 ? 0.6460 1.0603 0.9012 0.0142  -0.0560 -0.0424 124 ARG A NE  
1088  C CZ  . ARG A 124 ? 0.6292 1.0278 0.8707 0.0161  -0.0648 -0.0414 124 ARG A CZ  
1089  N NH1 . ARG A 124 ? 0.6102 1.0101 0.8496 0.0023  -0.0716 -0.0441 124 ARG A NH1 
1090  N NH2 . ARG A 124 ? 0.5833 0.9651 0.8135 0.0319  -0.0668 -0.0378 124 ARG A NH2 
1091  N N   . GLU A 125 ? 0.5734 0.9504 0.8275 -0.0603 -0.0551 -0.0456 125 GLU A N   
1092  C CA  . GLU A 125 ? 0.6042 0.9551 0.8422 -0.0604 -0.0620 -0.0501 125 GLU A CA  
1093  C C   . GLU A 125 ? 0.5201 0.8379 0.7483 -0.0705 -0.0579 -0.0490 125 GLU A C   
1094  O O   . GLU A 125 ? 0.5859 0.8764 0.7958 -0.0654 -0.0589 -0.0509 125 GLU A O   
1095  C CB  . GLU A 125 ? 0.6002 0.9697 0.8485 -0.0684 -0.0731 -0.0569 125 GLU A CB  
1096  C CG  . GLU A 125 ? 0.6676 1.0656 0.9205 -0.0555 -0.0798 -0.0578 125 GLU A CG  
1097  C CD  . GLU A 125 ? 0.7181 1.1454 0.9876 -0.0482 -0.0745 -0.0531 125 GLU A CD  
1098  O OE1 . GLU A 125 ? 0.8042 1.2465 1.0897 -0.0601 -0.0694 -0.0515 125 GLU A OE1 
1099  O OE2 . GLU A 125 ? 0.6947 1.1306 0.9621 -0.0307 -0.0753 -0.0509 125 GLU A OE2 
1100  N N   . GLU A 126 ? 0.5902 0.9111 0.8310 -0.0847 -0.0534 -0.0451 126 GLU A N   
1101  C CA  . GLU A 126 ? 0.5785 0.8690 0.8118 -0.0930 -0.0492 -0.0417 126 GLU A CA  
1102  C C   . GLU A 126 ? 0.5426 0.8177 0.7603 -0.0820 -0.0403 -0.0362 126 GLU A C   
1103  O O   . GLU A 126 ? 0.6150 0.8603 0.8183 -0.0813 -0.0388 -0.0355 126 GLU A O   
1104  C CB  . GLU A 126 ? 0.6043 0.9044 0.8568 -0.1114 -0.0473 -0.0364 126 GLU A CB  
1105  C CG  . GLU A 126 ? 0.6338 0.9426 0.9023 -0.1248 -0.0567 -0.0430 126 GLU A CG  
1106  C CD  . GLU A 126 ? 0.7013 1.0312 0.9931 -0.1419 -0.0550 -0.0364 126 GLU A CD  
1107  O OE1 . GLU A 126 ? 0.7581 1.1018 1.0529 -0.1416 -0.0463 -0.0268 126 GLU A OE1 
1108  O OE2 . GLU A 126 ? 0.7449 1.0784 1.0522 -0.1561 -0.0623 -0.0409 126 GLU A OE2 
1109  N N   . LEU A 127 ? 0.5383 0.8344 0.7592 -0.0731 -0.0347 -0.0333 127 LEU A N   
1110  C CA  . LEU A 127 ? 0.4856 0.7689 0.6924 -0.0625 -0.0266 -0.0301 127 LEU A CA  
1111  C C   . LEU A 127 ? 0.5444 0.8058 0.7330 -0.0481 -0.0296 -0.0336 127 LEU A C   
1112  O O   . LEU A 127 ? 0.5974 0.8340 0.7707 -0.0444 -0.0254 -0.0317 127 LEU A O   
1113  C CB  . LEU A 127 ? 0.5061 0.8195 0.7230 -0.0560 -0.0202 -0.0289 127 LEU A CB  
1114  C CG  . LEU A 127 ? 0.5483 0.8833 0.7789 -0.0695 -0.0138 -0.0230 127 LEU A CG  
1115  C CD1 . LEU A 127 ? 0.4836 0.8511 0.7232 -0.0601 -0.0073 -0.0247 127 LEU A CD1 
1116  C CD2 . LEU A 127 ? 0.5632 0.8756 0.7827 -0.0772 -0.0080 -0.0164 127 LEU A CD2 
1117  N N   . LEU A 128 ? 0.4985 0.7704 0.6888 -0.0404 -0.0370 -0.0378 128 LEU A N   
1118  C CA  . LEU A 128 ? 0.5738 0.8260 0.7469 -0.0290 -0.0409 -0.0393 128 LEU A CA  
1119  C C   . LEU A 128 ? 0.6126 0.8357 0.7722 -0.0363 -0.0423 -0.0407 128 LEU A C   
1120  O O   . LEU A 128 ? 0.5991 0.7995 0.7421 -0.0292 -0.0403 -0.0394 128 LEU A O   
1121  C CB  . LEU A 128 ? 0.5464 0.8179 0.7246 -0.0229 -0.0502 -0.0423 128 LEU A CB  
1122  C CG  . LEU A 128 ? 0.5412 0.8199 0.7174 -0.0049 -0.0514 -0.0399 128 LEU A CG  
1123  C CD1 . LEU A 128 ? 0.4692 0.7727 0.6538 -0.0012 -0.0616 -0.0414 128 LEU A CD1 
1124  C CD2 . LEU A 128 ? 0.4592 0.7078 0.6148 0.0043  -0.0501 -0.0370 128 LEU A CD2 
1125  N N   . ASP A 129 ? 0.6031 0.8267 0.7711 -0.0505 -0.0456 -0.0436 129 ASP A N   
1126  C CA  . ASP A 129 ? 0.5247 0.7215 0.6827 -0.0566 -0.0470 -0.0465 129 ASP A CA  
1127  C C   . ASP A 129 ? 0.5635 0.7396 0.7158 -0.0591 -0.0390 -0.0406 129 ASP A C   
1128  O O   . ASP A 129 ? 0.6265 0.7786 0.7647 -0.0565 -0.0380 -0.0412 129 ASP A O   
1129  C CB  . ASP A 129 ? 0.6098 0.8119 0.7813 -0.0707 -0.0533 -0.0526 129 ASP A CB  
1130  C CG  . ASP A 129 ? 0.7005 0.9220 0.8746 -0.0686 -0.0625 -0.0601 129 ASP A CG  
1131  O OD1 . ASP A 129 ? 0.7041 0.9379 0.8720 -0.0560 -0.0638 -0.0582 129 ASP A OD1 
1132  O OD2 . ASP A 129 ? 0.6171 0.8419 0.8001 -0.0795 -0.0689 -0.0680 129 ASP A OD2 
1133  N N   . LEU A 130 ? 0.5323 0.7196 0.6948 -0.0643 -0.0332 -0.0345 130 LEU A N   
1134  C CA  . LEU A 130 ? 0.5192 0.6903 0.6750 -0.0663 -0.0258 -0.0279 130 LEU A CA  
1135  C C   . LEU A 130 ? 0.5758 0.7356 0.7145 -0.0525 -0.0216 -0.0274 130 LEU A C   
1136  O O   . LEU A 130 ? 0.7106 0.8486 0.8377 -0.0521 -0.0186 -0.0251 130 LEU A O   
1137  C CB  . LEU A 130 ? 0.5881 0.7785 0.7571 -0.0746 -0.0202 -0.0210 130 LEU A CB  
1138  C CG  . LEU A 130 ? 0.4966 0.6710 0.6609 -0.0814 -0.0148 -0.0130 130 LEU A CG  
1139  C CD1 . LEU A 130 ? 0.4304 0.5838 0.5992 -0.0921 -0.0196 -0.0122 130 LEU A CD1 
1140  C CD2 . LEU A 130 ? 0.5003 0.6975 0.6739 -0.0882 -0.0081 -0.0049 130 LEU A CD2 
1141  N N   . GLN A 131 ? 0.5696 0.7437 0.7080 -0.0412 -0.0219 -0.0295 131 GLN A N   
1142  C CA  . GLN A 131 ? 0.5753 0.7362 0.6992 -0.0282 -0.0193 -0.0293 131 GLN A CA  
1143  C C   . GLN A 131 ? 0.5420 0.6812 0.6516 -0.0249 -0.0239 -0.0311 131 GLN A C   
1144  O O   . GLN A 131 ? 0.5904 0.7084 0.6872 -0.0234 -0.0207 -0.0294 131 GLN A O   
1145  C CB  . GLN A 131 ? 0.6782 0.8582 0.8080 -0.0163 -0.0199 -0.0310 131 GLN A CB  
1146  C CG  . GLN A 131 ? 0.6059 0.8106 0.7494 -0.0170 -0.0142 -0.0306 131 GLN A CG  
1147  C CD  . GLN A 131 ? 0.5449 0.7706 0.6981 -0.0048 -0.0164 -0.0335 131 GLN A CD  
1148  O OE1 . GLN A 131 ? 0.4671 0.6979 0.6227 -0.0007 -0.0242 -0.0345 131 GLN A OE1 
1149  N NE2 . GLN A 131 ? 0.5319 0.7706 0.6908 0.0020  -0.0097 -0.0351 131 GLN A NE2 
1150  N N   . THR A 132 ? 0.5943 0.7413 0.7059 -0.0242 -0.0315 -0.0349 132 THR A N   
1151  C CA  . THR A 132 ? 0.6097 0.7421 0.7068 -0.0200 -0.0358 -0.0368 132 THR A CA  
1152  C C   . THR A 132 ? 0.5383 0.6505 0.6289 -0.0281 -0.0348 -0.0388 132 THR A C   
1153  O O   . THR A 132 ? 0.5978 0.6922 0.6741 -0.0241 -0.0332 -0.0378 132 THR A O   
1154  C CB  . THR A 132 ? 0.5443 0.6944 0.6454 -0.0188 -0.0445 -0.0408 132 THR A CB  
1155  O OG1 . THR A 132 ? 0.5312 0.7049 0.6450 -0.0135 -0.0456 -0.0391 132 THR A OG1 
1156  C CG2 . THR A 132 ? 0.5946 0.7361 0.6793 -0.0108 -0.0482 -0.0400 132 THR A CG2 
1157  N N   . LEU A 133 ? 0.5198 0.6343 0.6221 -0.0396 -0.0358 -0.0415 133 LEU A N   
1158  C CA  . LEU A 133 ? 0.6335 0.7278 0.7329 -0.0464 -0.0350 -0.0433 133 LEU A CA  
1159  C C   . LEU A 133 ? 0.6159 0.6944 0.7082 -0.0449 -0.0277 -0.0365 133 LEU A C   
1160  O O   . LEU A 133 ? 0.5720 0.6322 0.6556 -0.0447 -0.0266 -0.0372 133 LEU A O   
1161  C CB  . LEU A 133 ? 0.6542 0.7524 0.7707 -0.0593 -0.0378 -0.0461 133 LEU A CB  
1162  C CG  . LEU A 133 ? 0.5917 0.7019 0.7150 -0.0631 -0.0460 -0.0558 133 LEU A CG  
1163  C CD1 . LEU A 133 ? 0.5826 0.7030 0.7267 -0.0758 -0.0480 -0.0559 133 LEU A CD1 
1164  C CD2 . LEU A 133 ? 0.5589 0.6540 0.6735 -0.0631 -0.0495 -0.0651 133 LEU A CD2 
1165  N N   . ASN A 134 ? 0.5437 0.6312 0.6397 -0.0437 -0.0227 -0.0306 134 ASN A N   
1166  C CA  . ASN A 134 ? 0.5827 0.6579 0.6708 -0.0423 -0.0162 -0.0251 134 ASN A CA  
1167  C C   . ASN A 134 ? 0.6280 0.6897 0.6997 -0.0325 -0.0153 -0.0258 134 ASN A C   
1168  O O   . ASN A 134 ? 0.6484 0.6938 0.7116 -0.0328 -0.0124 -0.0237 134 ASN A O   
1169  C CB  . ASN A 134 ? 0.5809 0.6722 0.6753 -0.0425 -0.0109 -0.0208 134 ASN A CB  
1170  C CG  . ASN A 134 ? 0.6528 0.7463 0.7557 -0.0539 -0.0078 -0.0146 134 ASN A CG  
1171  O OD1 . ASN A 134 ? 0.6828 0.7637 0.7791 -0.0558 -0.0043 -0.0101 134 ASN A OD1 
1172  N ND2 . ASN A 134 ? 0.6158 0.7262 0.7342 -0.0622 -0.0095 -0.0134 134 ASN A ND2 
1173  N N   . LEU A 135 ? 0.6090 0.6778 0.6772 -0.0239 -0.0182 -0.0278 135 LEU A N   
1174  C CA  . LEU A 135 ? 0.5257 0.5816 0.5793 -0.0156 -0.0183 -0.0269 135 LEU A CA  
1175  C C   . LEU A 135 ? 0.6024 0.6475 0.6479 -0.0181 -0.0214 -0.0298 135 LEU A C   
1176  O O   . LEU A 135 ? 0.5617 0.5920 0.5960 -0.0163 -0.0190 -0.0281 135 LEU A O   
1177  C CB  . LEU A 135 ? 0.5668 0.6336 0.6206 -0.0061 -0.0217 -0.0264 135 LEU A CB  
1178  C CG  . LEU A 135 ? 0.6066 0.6795 0.6653 0.0009  -0.0179 -0.0245 135 LEU A CG  
1179  C CD1 . LEU A 135 ? 0.5754 0.6581 0.6363 0.0108  -0.0231 -0.0236 135 LEU A CD1 
1180  C CD2 . LEU A 135 ? 0.6623 0.7170 0.7111 0.0035  -0.0124 -0.0223 135 LEU A CD2 
1181  N N   . LEU A 136 ? 0.5516 0.6058 0.6033 -0.0224 -0.0268 -0.0353 136 LEU A N   
1182  C CA  . LEU A 136 ? 0.6101 0.6577 0.6544 -0.0240 -0.0300 -0.0409 136 LEU A CA  
1183  C C   . LEU A 136 ? 0.5520 0.5838 0.5976 -0.0300 -0.0269 -0.0425 136 LEU A C   
1184  O O   . LEU A 136 ? 0.6310 0.6549 0.6685 -0.0292 -0.0273 -0.0466 136 LEU A O   
1185  C CB  . LEU A 136 ? 0.5642 0.6275 0.6156 -0.0273 -0.0369 -0.0484 136 LEU A CB  
1186  C CG  . LEU A 136 ? 0.5716 0.6512 0.6186 -0.0200 -0.0417 -0.0469 136 LEU A CG  
1187  C CD1 . LEU A 136 ? 0.5202 0.6173 0.5742 -0.0246 -0.0492 -0.0553 136 LEU A CD1 
1188  C CD2 . LEU A 136 ? 0.5534 0.6260 0.5828 -0.0126 -0.0414 -0.0430 136 LEU A CD2 
1189  N N   . ALA A 137 ? 0.5425 0.5713 0.5985 -0.0357 -0.0238 -0.0388 137 ALA A N   
1190  C CA  . ALA A 137 ? 0.6377 0.6511 0.6959 -0.0404 -0.0214 -0.0382 137 ALA A CA  
1191  C C   . ALA A 137 ? 0.6183 0.6197 0.6630 -0.0352 -0.0170 -0.0341 137 ALA A C   
1192  O O   . ALA A 137 ? 0.6301 0.6201 0.6731 -0.0363 -0.0161 -0.0359 137 ALA A O   
1193  C CB  . ALA A 137 ? 0.5494 0.5641 0.6212 -0.0481 -0.0195 -0.0322 137 ALA A CB  
1194  N N   . TRP A 138 ? 0.5882 0.5923 0.6248 -0.0296 -0.0143 -0.0293 138 TRP A N   
1195  C CA  . TRP A 138 ? 0.5782 0.5715 0.6031 -0.0257 -0.0102 -0.0252 138 TRP A CA  
1196  C C   . TRP A 138 ? 0.5876 0.5794 0.6001 -0.0197 -0.0119 -0.0266 138 TRP A C   
1197  O O   . TRP A 138 ? 0.6001 0.5869 0.6039 -0.0153 -0.0095 -0.0220 138 TRP A O   
1198  C CB  . TRP A 138 ? 0.6273 0.6228 0.6518 -0.0240 -0.0062 -0.0200 138 TRP A CB  
1199  C CG  . TRP A 138 ? 0.6195 0.6194 0.6540 -0.0305 -0.0039 -0.0170 138 TRP A CG  
1200  C CD1 . TRP A 138 ? 0.5896 0.6032 0.6359 -0.0343 -0.0049 -0.0169 138 TRP A CD1 
1201  C CD2 . TRP A 138 ? 0.6724 0.6656 0.7062 -0.0346 -0.0004 -0.0122 138 TRP A CD2 
1202  N NE1 . TRP A 138 ? 0.6100 0.6256 0.6624 -0.0410 -0.0019 -0.0115 138 TRP A NE1 
1203  C CE2 . TRP A 138 ? 0.6545 0.6578 0.6990 -0.0410 0.0006  -0.0084 138 TRP A CE2 
1204  C CE3 . TRP A 138 ? 0.6412 0.6228 0.6667 -0.0338 0.0018  -0.0101 138 TRP A CE3 
1205  C CZ2 . TRP A 138 ? 0.6307 0.6329 0.6769 -0.0464 0.0033  -0.0018 138 TRP A CZ2 
1206  C CZ3 . TRP A 138 ? 0.5657 0.5463 0.5937 -0.0388 0.0043  -0.0045 138 TRP A CZ3 
1207  C CH2 . TRP A 138 ? 0.5669 0.5577 0.6046 -0.0449 0.0049  0.0000  138 TRP A CH2 
1208  N N   . CYS A 139 ? 0.6343 0.6315 0.6461 -0.0200 -0.0161 -0.0326 139 CYS A N   
1209  C CA  . CYS A 139 ? 0.7103 0.7100 0.7095 -0.0151 -0.0179 -0.0328 139 CYS A CA  
1210  C C   . CYS A 139 ? 0.6823 0.6731 0.6733 -0.0156 -0.0150 -0.0338 139 CYS A C   
1211  O O   . CYS A 139 ? 0.5425 0.5304 0.5388 -0.0191 -0.0148 -0.0402 139 CYS A O   
1212  C CB  . CYS A 139 ? 0.6349 0.6489 0.6358 -0.0154 -0.0239 -0.0396 139 CYS A CB  
1213  S SG  . CYS A 139 ? 0.7816 0.8055 0.7679 -0.0087 -0.0274 -0.0353 139 CYS A SG  
1214  N N   . GLY A 140 ? 0.7001 0.6867 0.6796 -0.0121 -0.0128 -0.0274 140 GLY A N   
1215  C CA  . GLY A 140 ? 0.6452 0.6268 0.6170 -0.0127 -0.0097 -0.0276 140 GLY A CA  
1216  C C   . GLY A 140 ? 0.7462 0.7387 0.7109 -0.0121 -0.0121 -0.0340 140 GLY A C   
1217  O O   . GLY A 140 ? 0.6704 0.6746 0.6350 -0.0113 -0.0168 -0.0380 140 GLY A O   
1218  N N   . ARG A 141 ? 0.6860 0.6771 0.6447 -0.0125 -0.0087 -0.0352 141 ARG A N   
1219  C CA  . ARG A 141 ? 0.6012 0.6049 0.5533 -0.0122 -0.0097 -0.0434 141 ARG A CA  
1220  C C   . ARG A 141 ? 0.6718 0.6888 0.6110 -0.0099 -0.0128 -0.0383 141 ARG A C   
1221  O O   . ARG A 141 ? 0.6325 0.6648 0.5676 -0.0098 -0.0163 -0.0462 141 ARG A O   
1222  C CB  . ARG A 141 ? 0.6691 0.6706 0.6178 -0.0126 -0.0044 -0.0444 141 ARG A CB  
1223  C CG  . ARG A 141 ? 0.6452 0.6619 0.5880 -0.0119 -0.0042 -0.0552 141 ARG A CG  
1224  C CD  . ARG A 141 ? 0.5429 0.5592 0.4850 -0.0117 0.0016  -0.0566 141 ARG A CD  
1225  N NE  . ARG A 141 ? 0.6203 0.6436 0.5483 -0.0121 0.0045  -0.0459 141 ARG A NE  
1226  C CZ  . ARG A 141 ? 0.6376 0.6785 0.5555 -0.0119 0.0069  -0.0491 141 ARG A CZ  
1227  N NH1 . ARG A 141 ? 0.6429 0.6965 0.5627 -0.0104 0.0069  -0.0650 141 ARG A NH1 
1228  N NH2 . ARG A 141 ? 0.6819 0.7283 0.5880 -0.0136 0.0094  -0.0365 141 ARG A NH2 
1229  N N   . THR A 142 ? 0.6383 0.6500 0.5713 -0.0082 -0.0122 -0.0250 142 THR A N   
1230  C CA  . THR A 142 ? 0.6383 0.6613 0.5598 -0.0059 -0.0156 -0.0169 142 THR A CA  
1231  C C   . THR A 142 ? 0.7503 0.7841 0.6756 -0.0038 -0.0222 -0.0194 142 THR A C   
1232  O O   . THR A 142 ? 0.7816 0.8335 0.6993 -0.0035 -0.0263 -0.0225 142 THR A O   
1233  C CB  . THR A 142 ? 0.6332 0.6441 0.5512 -0.0045 -0.0141 -0.0019 142 THR A CB  
1234  O OG1 . THR A 142 ? 0.7576 0.7558 0.6771 -0.0073 -0.0081 -0.0011 142 THR A OG1 
1235  C CG2 . THR A 142 ? 0.7966 0.8184 0.7011 -0.0036 -0.0163 0.0087  142 THR A CG2 
1236  N N   . LEU A 143 ? 0.7265 0.7518 0.6634 -0.0025 -0.0234 -0.0185 143 LEU A N   
1237  C CA  . LEU A 143 ? 0.6542 0.6912 0.5966 -0.0004 -0.0297 -0.0199 143 LEU A CA  
1238  C C   . LEU A 143 ? 0.6573 0.7043 0.6071 -0.0042 -0.0323 -0.0345 143 LEU A C   
1239  O O   . LEU A 143 ? 0.6281 0.6897 0.5808 -0.0036 -0.0383 -0.0374 143 LEU A O   
1240  C CB  . LEU A 143 ? 0.6167 0.6442 0.5700 0.0026  -0.0295 -0.0143 143 LEU A CB  
1241  C CG  . LEU A 143 ? 0.6252 0.6454 0.5741 0.0080  -0.0297 -0.0009 143 LEU A CG  
1242  C CD1 . LEU A 143 ? 0.6990 0.7115 0.6604 0.0115  -0.0289 0.0008  143 LEU A CD1 
1243  C CD2 . LEU A 143 ? 0.6900 0.7250 0.6307 0.0119  -0.0361 0.0064  143 LEU A CD2 
1244  N N   . ARG A 144 ? 0.6823 0.7213 0.6365 -0.0082 -0.0285 -0.0435 144 ARG A N   
1245  C CA  . ARG A 144 ? 0.6701 0.7160 0.6325 -0.0122 -0.0313 -0.0583 144 ARG A CA  
1246  C C   . ARG A 144 ? 0.6157 0.6811 0.5672 -0.0121 -0.0352 -0.0661 144 ARG A C   
1247  O O   . ARG A 144 ? 0.6169 0.6935 0.5742 -0.0148 -0.0401 -0.0778 144 ARG A O   
1248  C CB  . ARG A 144 ? 0.5247 0.5563 0.4950 -0.0153 -0.0266 -0.0652 144 ARG A CB  
1249  C CG  . ARG A 144 ? 0.6273 0.6467 0.6136 -0.0184 -0.0258 -0.0636 144 ARG A CG  
1250  C CD  . ARG A 144 ? 0.6334 0.6389 0.6283 -0.0210 -0.0221 -0.0678 144 ARG A CD  
1251  N NE  . ARG A 144 ? 0.7292 0.7249 0.7375 -0.0243 -0.0212 -0.0625 144 ARG A NE  
1252  C CZ  . ARG A 144 ? 0.7536 0.7400 0.7760 -0.0286 -0.0211 -0.0665 144 ARG A CZ  
1253  N NH1 . ARG A 144 ? 0.8666 0.8500 0.8936 -0.0291 -0.0220 -0.0775 144 ARG A NH1 
1254  N NH2 . ARG A 144 ? 0.6411 0.6220 0.6740 -0.0322 -0.0203 -0.0591 144 ARG A NH2 
1255  N N   . LYS A 145 ? 0.5901 0.6615 0.5261 -0.0097 -0.0331 -0.0600 145 LYS A N   
1256  C CA  . LYS A 145 ? 0.6700 0.7644 0.5929 -0.0096 -0.0368 -0.0650 145 LYS A CA  
1257  C C   . LYS A 145 ? 0.7372 0.8464 0.6558 -0.0070 -0.0438 -0.0558 145 LYS A C   
1258  O O   . LYS A 145 ? 0.7765 0.9076 0.6897 -0.0081 -0.0494 -0.0633 145 LYS A O   
1259  C CB  . LYS A 145 ? 0.6955 0.7939 0.6033 -0.0087 -0.0317 -0.0599 145 LYS A CB  
1260  C CG  . LYS A 145 ? 0.7021 0.7884 0.6152 -0.0102 -0.0248 -0.0685 145 LYS A CG  
1261  C CD  . LYS A 145 ? 0.7370 0.8313 0.6359 -0.0098 -0.0196 -0.0635 145 LYS A CD  
1262  C CE  . LYS A 145 ? 0.7627 0.8429 0.6693 -0.0103 -0.0127 -0.0684 145 LYS A CE  
1263  N NZ  . LYS A 145 ? 0.7363 0.8104 0.6356 -0.0104 -0.0078 -0.0525 145 LYS A NZ  
1264  N N   . ASP A 146 ? 0.6907 0.7892 0.6123 -0.0034 -0.0438 -0.0404 146 ASP A N   
1265  C CA  . ASP A 146 ? 0.7156 0.8275 0.6346 0.0007  -0.0507 -0.0300 146 ASP A CA  
1266  C C   . ASP A 146 ? 0.7699 0.8898 0.7033 0.0001  -0.0563 -0.0374 146 ASP A C   
1267  O O   . ASP A 146 ? 0.8652 1.0073 0.7959 0.0005  -0.0637 -0.0391 146 ASP A O   
1268  C CB  . ASP A 146 ? 0.6949 0.7916 0.6133 0.0057  -0.0488 -0.0117 146 ASP A CB  
1269  C CG  . ASP A 146 ? 0.9408 1.0379 0.8432 0.0059  -0.0463 -0.0004 146 ASP A CG  
1270  O OD1 . ASP A 146 ? 0.9190 1.0315 0.8096 0.0026  -0.0457 -0.0064 146 ASP A OD1 
1271  O OD2 . ASP A 146 ? 1.0512 1.1340 0.9534 0.0090  -0.0448 0.0142  146 ASP A OD2 
1272  N N   . LEU A 147 ? 0.7391 0.8435 0.6879 -0.0016 -0.0532 -0.0411 147 LEU A N   
1273  C CA  . LEU A 147 ? 0.6232 0.7356 0.5874 -0.0033 -0.0577 -0.0471 147 LEU A CA  
1274  C C   . LEU A 147 ? 0.6711 0.7883 0.6422 -0.0109 -0.0592 -0.0649 147 LEU A C   
1275  O O   . LEU A 147 ? 0.6653 0.7795 0.6527 -0.0150 -0.0598 -0.0703 147 LEU A O   
1276  C CB  . LEU A 147 ? 0.6512 0.7478 0.6288 -0.0018 -0.0536 -0.0411 147 LEU A CB  
1277  C CG  . LEU A 147 ? 0.6942 0.7782 0.6667 0.0050  -0.0502 -0.0265 147 LEU A CG  
1278  C CD1 . LEU A 147 ? 0.5760 0.6459 0.5612 0.0057  -0.0453 -0.0243 147 LEU A CD1 
1279  C CD2 . LEU A 147 ? 0.5107 0.6094 0.4792 0.0119  -0.0569 -0.0166 147 LEU A CD2 
1280  N N   . LYS A 148 ? 0.6737 0.7987 0.6337 -0.0130 -0.0596 -0.0743 148 LYS A N   
1281  C CA  . LYS A 148 ? 0.6611 0.7871 0.6287 -0.0195 -0.0606 -0.0932 148 LYS A CA  
1282  C C   . LYS A 148 ? 0.7038 0.8447 0.6842 -0.0240 -0.0681 -0.1014 148 LYS A C   
1283  O O   . LYS A 148 ? 0.7744 0.9072 0.7706 -0.0303 -0.0684 -0.1120 148 LYS A O   
1284  C CB  . LYS A 148 ? 0.6422 0.7802 0.5945 -0.0198 -0.0604 -0.1033 148 LYS A CB  
1285  C CG  . LYS A 148 ? 0.8002 0.9330 0.7613 -0.0251 -0.0595 -0.1240 148 LYS A CG  
1286  C CD  . LYS A 148 ? 0.9041 1.0581 0.8510 -0.0254 -0.0614 -0.1380 148 LYS A CD  
1287  C CE  . LYS A 148 ? 0.9817 1.1270 0.9381 -0.0288 -0.0592 -0.1597 148 LYS A CE  
1288  N NZ  . LYS A 148 ? 0.9420 1.0581 0.9183 -0.0307 -0.0555 -0.1584 148 LYS A NZ  
1289  N N   . ASP A 149 ? 0.7262 0.8891 0.7011 -0.0210 -0.0748 -0.0955 149 ASP A N   
1290  C CA  . ASP A 149 ? 0.7766 0.9583 0.7631 -0.0256 -0.0828 -0.1041 149 ASP A CA  
1291  C C   . ASP A 149 ? 0.6873 0.8612 0.6936 -0.0270 -0.0821 -0.0980 149 ASP A C   
1292  O O   . ASP A 149 ? 0.6345 0.8098 0.6569 -0.0348 -0.0846 -0.1084 149 ASP A O   
1293  C CB  . ASP A 149 ? 0.8850 1.0958 0.8595 -0.0217 -0.0907 -0.0988 149 ASP A CB  
1294  C CG  . ASP A 149 ? 0.8550 1.0817 0.8110 -0.0231 -0.0927 -0.1091 149 ASP A CG  
1295  O OD1 . ASP A 149 ? 0.7003 0.9182 0.6565 -0.0278 -0.0891 -0.1251 149 ASP A OD1 
1296  O OD2 . ASP A 149 ? 0.9694 1.2186 0.9110 -0.0192 -0.0979 -0.1010 149 ASP A OD2 
1297  N N   . LEU A 150 ? 0.6193 0.7855 0.6254 -0.0200 -0.0785 -0.0816 150 LEU A N   
1298  C CA  . LEU A 150 ? 0.5565 0.7155 0.5803 -0.0211 -0.0759 -0.0767 150 LEU A CA  
1299  C C   . LEU A 150 ? 0.6903 0.8292 0.7246 -0.0289 -0.0705 -0.0840 150 LEU A C   
1300  O O   . LEU A 150 ? 0.7213 0.8623 0.7730 -0.0356 -0.0715 -0.0875 150 LEU A O   
1301  C CB  . LEU A 150 ? 0.4877 0.6377 0.5081 -0.0118 -0.0715 -0.0606 150 LEU A CB  
1302  C CG  . LEU A 150 ? 0.5208 0.6899 0.5432 -0.0040 -0.0773 -0.0512 150 LEU A CG  
1303  C CD1 . LEU A 150 ? 0.5823 0.7370 0.6000 0.0056  -0.0726 -0.0371 150 LEU A CD1 
1304  C CD2 . LEU A 150 ? 0.6927 0.8774 0.7352 -0.0073 -0.0804 -0.0547 150 LEU A CD2 
1305  N N   . LEU A 151 ? 0.6316 0.7521 0.6563 -0.0285 -0.0651 -0.0856 151 LEU A N   
1306  C CA  . LEU A 151 ? 0.5974 0.6985 0.6324 -0.0350 -0.0607 -0.0916 151 LEU A CA  
1307  C C   . LEU A 151 ? 0.7411 0.8469 0.7868 -0.0436 -0.0658 -0.1082 151 LEU A C   
1308  O O   . LEU A 151 ? 0.6607 0.7543 0.7226 -0.0507 -0.0647 -0.1116 151 LEU A O   
1309  C CB  . LEU A 151 ? 0.5748 0.6583 0.5976 -0.0315 -0.0544 -0.0899 151 LEU A CB  
1310  C CG  . LEU A 151 ? 0.6852 0.7565 0.7028 -0.0259 -0.0481 -0.0749 151 LEU A CG  
1311  C CD1 . LEU A 151 ? 0.6819 0.7450 0.6831 -0.0215 -0.0440 -0.0725 151 LEU A CD1 
1312  C CD2 . LEU A 151 ? 0.5257 0.5822 0.5572 -0.0301 -0.0436 -0.0710 151 LEU A CD2 
1313  N N   . ASN A 152 ? 0.8020 0.9255 0.8392 -0.0436 -0.0718 -0.1185 152 ASN A N   
1314  C CA  . ASN A 152 ? 0.6977 0.8265 0.7453 -0.0520 -0.0773 -0.1369 152 ASN A CA  
1315  C C   . ASN A 152 ? 0.6670 0.8095 0.7321 -0.0589 -0.0833 -0.1379 152 ASN A C   
1316  O O   . ASN A 152 ? 0.8253 0.9637 0.9069 -0.0684 -0.0864 -0.1497 152 ASN A O   
1317  C CB  . ASN A 152 ? 0.8128 0.9595 0.8443 -0.0501 -0.0816 -0.1493 152 ASN A CB  
1318  C CG  . ASN A 152 ? 0.8790 1.0129 0.8987 -0.0465 -0.0757 -0.1549 152 ASN A CG  
1319  O OD1 . ASN A 152 ? 0.8753 1.0211 0.8753 -0.0408 -0.0749 -0.1528 152 ASN A OD1 
1320  N ND2 . ASN A 152 ? 0.9412 1.0516 0.9737 -0.0498 -0.0717 -0.1608 152 ASN A ND2 
1321  N N   . LYS A 153 ? 0.6816 0.8408 0.7451 -0.0543 -0.0851 -0.1257 153 LYS A N   
1322  C CA  . LYS A 153 ? 0.7124 0.8880 0.7936 -0.0603 -0.0903 -0.1254 153 LYS A CA  
1323  C C   . LYS A 153 ? 0.6684 0.8272 0.7698 -0.0688 -0.0864 -0.1237 153 LYS A C   
1324  O O   . LYS A 153 ? 0.5648 0.7267 0.6832 -0.0797 -0.0908 -0.1334 153 LYS A O   
1325  C CB  . LYS A 153 ? 0.6481 0.8405 0.7259 -0.0515 -0.0909 -0.1104 153 LYS A CB  
1326  C CG  . LYS A 153 ? 0.6592 0.8832 0.7353 -0.0504 -0.1006 -0.1138 153 LYS A CG  
1327  C CD  . LYS A 153 ? 0.7484 0.9854 0.8231 -0.0396 -0.1008 -0.0977 153 LYS A CD  
1328  C CE  . LYS A 153 ? 0.6306 0.8810 0.7275 -0.0431 -0.1019 -0.0944 153 LYS A CE  
1329  N NZ  . LYS A 153 ? 0.6866 0.9535 0.7842 -0.0314 -0.1034 -0.0813 153 LYS A NZ  
1330  N N   . GLY A 154 ? 0.5576 0.6989 0.6574 -0.0647 -0.0782 -0.1110 154 GLY A N   
1331  C CA  . GLY A 154 ? 0.5761 0.7028 0.6926 -0.0722 -0.0740 -0.1063 154 GLY A CA  
1332  C C   . GLY A 154 ? 0.6152 0.7585 0.7475 -0.0764 -0.0744 -0.0983 154 GLY A C   
1333  O O   . GLY A 154 ? 0.6249 0.7589 0.7684 -0.0816 -0.0695 -0.0905 154 GLY A O   
1334  N N   . ARG A 155 ? 0.5896 0.7594 0.7236 -0.0743 -0.0801 -0.0994 155 ARG A N   
1335  C CA  . ARG A 155 ? 0.6272 0.8170 0.7787 -0.0786 -0.0807 -0.0934 155 ARG A CA  
1336  C C   . ARG A 155 ? 0.6180 0.8357 0.7655 -0.0699 -0.0859 -0.0917 155 ARG A C   
1337  O O   . ARG A 155 ? 0.6184 0.8385 0.7492 -0.0615 -0.0891 -0.0937 155 ARG A O   
1338  C CB  . ARG A 155 ? 0.5845 0.7782 0.7571 -0.0945 -0.0853 -0.1016 155 ARG A CB  
1339  C CG  . ARG A 155 ? 0.5835 0.7915 0.7571 -0.0990 -0.0953 -0.1170 155 ARG A CG  
1340  C CD  . ARG A 155 ? 0.5311 0.7372 0.7268 -0.1158 -0.0998 -0.1260 155 ARG A CD  
1341  N NE  . ARG A 155 ? 0.6519 0.8254 0.8510 -0.1210 -0.0953 -0.1267 155 ARG A NE  
1342  C CZ  . ARG A 155 ? 0.7076 0.8704 0.9253 -0.1317 -0.0924 -0.1195 155 ARG A CZ  
1343  N NH1 . ARG A 155 ? 0.7192 0.9024 0.9541 -0.1398 -0.0931 -0.1122 155 ARG A NH1 
1344  N NH2 . ARG A 155 ? 0.7371 0.8697 0.9567 -0.1343 -0.0889 -0.1188 155 ARG A NH2 
1345  N N   . ASN A 156 ? 0.6547 0.8951 0.8186 -0.0721 -0.0868 -0.0870 156 ASN A N   
1346  C CA  . ASN A 156 ? 0.6190 0.8894 0.7847 -0.0644 -0.0927 -0.0852 156 ASN A CA  
1347  C C   . ASN A 156 ? 0.6094 0.8758 0.7575 -0.0476 -0.0905 -0.0765 156 ASN A C   
1348  O O   . ASN A 156 ? 0.5646 0.8466 0.7050 -0.0401 -0.0973 -0.0764 156 ASN A O   
1349  C CB  . ASN A 156 ? 0.5659 0.8539 0.7330 -0.0707 -0.1036 -0.0976 156 ASN A CB  
1350  C CG  . ASN A 156 ? 0.6427 0.9304 0.8281 -0.0882 -0.1062 -0.1073 156 ASN A CG  
1351  O OD1 . ASN A 156 ? 0.6044 0.8846 0.8041 -0.0957 -0.1005 -0.1021 156 ASN A OD1 
1352  N ND2 . ASN A 156 ? 0.7386 1.0344 0.9239 -0.0954 -0.1150 -0.1214 156 ASN A ND2 
1353  N N   . TYR A 157 ? 0.4961 0.7418 0.6383 -0.0421 -0.0813 -0.0686 157 TYR A N   
1354  C CA  . TYR A 157 ? 0.5734 0.8125 0.7020 -0.0271 -0.0787 -0.0599 157 TYR A CA  
1355  C C   . TYR A 157 ? 0.5959 0.8583 0.7368 -0.0179 -0.0794 -0.0535 157 TYR A C   
1356  O O   . TYR A 157 ? 0.5339 0.8141 0.6933 -0.0231 -0.0782 -0.0542 157 TYR A O   
1357  C CB  . TYR A 157 ? 0.6156 0.8254 0.7350 -0.0255 -0.0690 -0.0553 157 TYR A CB  
1358  C CG  . TYR A 157 ? 0.6890 0.8760 0.7967 -0.0320 -0.0681 -0.0610 157 TYR A CG  
1359  C CD1 . TYR A 157 ? 0.5406 0.7213 0.6306 -0.0270 -0.0713 -0.0628 157 TYR A CD1 
1360  C CD2 . TYR A 157 ? 0.6319 0.8048 0.7470 -0.0429 -0.0640 -0.0640 157 TYR A CD2 
1361  C CE1 . TYR A 157 ? 0.5143 0.6770 0.5948 -0.0321 -0.0700 -0.0695 157 TYR A CE1 
1362  C CE2 . TYR A 157 ? 0.5251 0.6775 0.6320 -0.0475 -0.0635 -0.0699 157 TYR A CE2 
1363  C CZ  . TYR A 157 ? 0.6045 0.7524 0.6942 -0.0417 -0.0662 -0.0735 157 TYR A CZ  
1364  O OH  . TYR A 157 ? 0.6227 0.7526 0.7054 -0.0455 -0.0650 -0.0806 157 TYR A OH  
1365  N N   . THR A 158 ? 0.5561 0.8190 0.6875 -0.0039 -0.0815 -0.0468 158 THR A N   
1366  C CA  . THR A 158 ? 0.5024 0.7845 0.6453 0.0081  -0.0827 -0.0405 158 THR A CA  
1367  C C   . THR A 158 ? 0.5587 0.8205 0.6962 0.0192  -0.0747 -0.0337 158 THR A C   
1368  O O   . THR A 158 ? 0.5950 0.8292 0.7178 0.0180  -0.0693 -0.0326 158 THR A O   
1369  C CB  . THR A 158 ? 0.6071 0.9084 0.7467 0.0161  -0.0935 -0.0374 158 THR A CB  
1370  O OG1 . THR A 158 ? 0.5877 0.8692 0.7086 0.0257  -0.0936 -0.0298 158 THR A OG1 
1371  C CG2 . THR A 158 ? 0.5235 0.8390 0.6615 0.0042  -0.1015 -0.0462 158 THR A CG2 
1372  N N   . GLN A 159 ? 0.4984 0.7756 0.6496 0.0302  -0.0740 -0.0300 159 GLN A N   
1373  C CA  . GLN A 159 ? 0.5784 0.8380 0.7267 0.0420  -0.0673 -0.0254 159 GLN A CA  
1374  C C   . GLN A 159 ? 0.6792 0.9172 0.8098 0.0504  -0.0706 -0.0183 159 GLN A C   
1375  O O   . GLN A 159 ? 0.7031 0.9143 0.8226 0.0524  -0.0644 -0.0162 159 GLN A O   
1376  C CB  . GLN A 159 ? 0.4660 0.7486 0.6344 0.0538  -0.0671 -0.0245 159 GLN A CB  
1377  C CG  . GLN A 159 ? 0.6364 0.9018 0.8049 0.0661  -0.0599 -0.0226 159 GLN A CG  
1378  C CD  . GLN A 159 ? 0.6424 0.8971 0.8095 0.0581  -0.0485 -0.0279 159 GLN A CD  
1379  O OE1 . GLN A 159 ? 0.5609 0.8291 0.7343 0.0454  -0.0456 -0.0319 159 GLN A OE1 
1380  N NE2 . GLN A 159 ? 0.6073 0.8378 0.7661 0.0647  -0.0426 -0.0273 159 GLN A NE2 
1381  N N   . GLU A 160 ? 0.6764 0.9274 0.8038 0.0543  -0.0806 -0.0140 160 GLU A N   
1382  C CA  . GLU A 160 ? 0.6550 0.8895 0.7659 0.0615  -0.0844 -0.0050 160 GLU A CA  
1383  C C   . GLU A 160 ? 0.6269 0.8391 0.7173 0.0513  -0.0812 -0.0072 160 GLU A C   
1384  O O   . GLU A 160 ? 0.6702 0.8593 0.7472 0.0554  -0.0787 -0.0008 160 GLU A O   
1385  C CB  . GLU A 160 ? 0.7034 0.9625 0.8157 0.0667  -0.0965 0.0009  160 GLU A CB  
1386  C CG  . GLU A 160 ? 0.7442 1.0204 0.8754 0.0818  -0.1007 0.0072  160 GLU A CG  
1387  C CD  . GLU A 160 ? 0.8152 1.1194 0.9690 0.0795  -0.0997 -0.0011 160 GLU A CD  
1388  O OE1 . GLU A 160 ? 0.6813 0.9900 0.8363 0.0652  -0.0959 -0.0108 160 GLU A OE1 
1389  O OE2 . GLU A 160 ? 0.8425 1.1643 1.0142 0.0921  -0.1029 0.0026  160 GLU A OE2 
1390  N N   . GLU A 161 ? 0.6064 0.8252 0.6955 0.0380  -0.0814 -0.0166 161 GLU A N   
1391  C CA  . GLU A 161 ? 0.6172 0.8161 0.6894 0.0291  -0.0782 -0.0204 161 GLU A CA  
1392  C C   . GLU A 161 ? 0.6884 0.8610 0.7581 0.0276  -0.0677 -0.0205 161 GLU A C   
1393  O O   . GLU A 161 ? 0.6704 0.8218 0.7249 0.0269  -0.0644 -0.0181 161 GLU A O   
1394  C CB  . GLU A 161 ? 0.5844 0.7958 0.6595 0.0160  -0.0813 -0.0317 161 GLU A CB  
1395  C CG  . GLU A 161 ? 0.6113 0.8478 0.6836 0.0155  -0.0921 -0.0336 161 GLU A CG  
1396  C CD  . GLU A 161 ? 0.7051 0.9551 0.7846 0.0021  -0.0956 -0.0471 161 GLU A CD  
1397  O OE1 . GLU A 161 ? 0.6959 0.9428 0.7894 -0.0056 -0.0911 -0.0523 161 GLU A OE1 
1398  O OE2 . GLU A 161 ? 0.6769 0.9413 0.7484 -0.0013 -0.1032 -0.0525 161 GLU A OE2 
1399  N N   . LYS A 162 ? 0.6919 0.8679 0.7762 0.0267  -0.0624 -0.0231 162 LYS A N   
1400  C CA  . LYS A 162 ? 0.6336 0.7882 0.7154 0.0254  -0.0529 -0.0230 162 LYS A CA  
1401  C C   . LYS A 162 ? 0.6153 0.7536 0.6905 0.0371  -0.0507 -0.0157 162 LYS A C   
1402  O O   . LYS A 162 ? 0.5902 0.7057 0.6548 0.0356  -0.0452 -0.0145 162 LYS A O   
1403  C CB  . LYS A 162 ? 0.6193 0.7867 0.7179 0.0216  -0.0480 -0.0269 162 LYS A CB  
1404  C CG  . LYS A 162 ? 0.6143 0.7654 0.7110 0.0211  -0.0385 -0.0266 162 LYS A CG  
1405  C CD  . LYS A 162 ? 0.5227 0.6926 0.6360 0.0182  -0.0337 -0.0295 162 LYS A CD  
1406  C CE  . LYS A 162 ? 0.6249 0.8188 0.7531 0.0290  -0.0366 -0.0295 162 LYS A CE  
1407  N NZ  . LYS A 162 ? 0.4354 0.6490 0.5791 0.0284  -0.0301 -0.0327 162 LYS A NZ  
1408  N N   . GLU A 163 ? 0.5998 0.7493 0.6824 0.0487  -0.0556 -0.0107 163 GLU A N   
1409  C CA  . GLU A 163 ? 0.6285 0.7604 0.7075 0.0600  -0.0544 -0.0036 163 GLU A CA  
1410  C C   . GLU A 163 ? 0.6742 0.7904 0.7350 0.0598  -0.0579 0.0041  163 GLU A C   
1411  O O   . GLU A 163 ? 0.6934 0.7872 0.7471 0.0637  -0.0548 0.0093  163 GLU A O   
1412  C CB  . GLU A 163 ? 0.6525 0.8006 0.7475 0.0733  -0.0592 -0.0001 163 GLU A CB  
1413  C CG  . GLU A 163 ? 0.7670 0.9267 0.8798 0.0763  -0.0533 -0.0075 163 GLU A CG  
1414  C CD  . GLU A 163 ? 0.8545 1.0383 0.9865 0.0886  -0.0587 -0.0059 163 GLU A CD  
1415  O OE1 . GLU A 163 ? 0.9462 1.1506 1.0812 0.0883  -0.0672 -0.0028 163 GLU A OE1 
1416  O OE2 . GLU A 163 ? 0.8521 1.0356 0.9968 0.0990  -0.0546 -0.0087 163 GLU A OE2 
1417  N N   . TYR A 164 ? 0.6060 0.7352 0.6592 0.0546  -0.0642 0.0045  164 TYR A N   
1418  C CA  . TYR A 164 ? 0.6182 0.7365 0.6526 0.0526  -0.0664 0.0108  164 TYR A CA  
1419  C C   . TYR A 164 ? 0.6863 0.7834 0.7099 0.0440  -0.0584 0.0063  164 TYR A C   
1420  O O   . TYR A 164 ? 0.6622 0.7406 0.6747 0.0453  -0.0559 0.0128  164 TYR A O   
1421  C CB  . TYR A 164 ? 0.6292 0.7702 0.6579 0.0482  -0.0744 0.0092  164 TYR A CB  
1422  C CG  . TYR A 164 ? 0.6876 0.8218 0.6960 0.0437  -0.0751 0.0123  164 TYR A CG  
1423  C CD1 . TYR A 164 ? 0.6979 0.8245 0.6961 0.0500  -0.0776 0.0262  164 TYR A CD1 
1424  C CD2 . TYR A 164 ? 0.6936 0.8295 0.6943 0.0330  -0.0731 0.0015  164 TYR A CD2 
1425  C CE1 . TYR A 164 ? 0.8554 0.9795 0.8349 0.0451  -0.0776 0.0296  164 TYR A CE1 
1426  C CE2 . TYR A 164 ? 0.8455 0.9784 0.8283 0.0294  -0.0730 0.0029  164 TYR A CE2 
1427  C CZ  . TYR A 164 ? 0.8532 0.9817 0.8248 0.0351  -0.0749 0.0171  164 TYR A CZ  
1428  O OH  . TYR A 164 ? 0.9842 1.1132 0.9378 0.0308  -0.0742 0.0190  164 TYR A OH  
1429  N N   . VAL A 165 ? 0.6558 0.7560 0.6838 0.0349  -0.0547 -0.0041 165 VAL A N   
1430  C CA  . VAL A 165 ? 0.5559 0.6372 0.5765 0.0274  -0.0475 -0.0081 165 VAL A CA  
1431  C C   . VAL A 165 ? 0.5813 0.6433 0.6023 0.0320  -0.0412 -0.0039 165 VAL A C   
1432  O O   . VAL A 165 ? 0.6220 0.6660 0.6320 0.0301  -0.0375 -0.0012 165 VAL A O   
1433  C CB  . VAL A 165 ? 0.4756 0.5638 0.5054 0.0178  -0.0453 -0.0180 165 VAL A CB  
1434  C CG1 . VAL A 165 ? 0.5434 0.6130 0.5717 0.0127  -0.0372 -0.0198 165 VAL A CG1 
1435  C CG2 . VAL A 165 ? 0.4731 0.5708 0.4979 0.0111  -0.0501 -0.0242 165 VAL A CG2 
1436  N N   . LEU A 166 ? 0.6207 0.6877 0.6549 0.0383  -0.0401 -0.0042 166 LEU A N   
1437  C CA  . LEU A 166 ? 0.6137 0.6640 0.6494 0.0422  -0.0338 -0.0035 166 LEU A CA  
1438  C C   . LEU A 166 ? 0.6455 0.6786 0.6732 0.0491  -0.0356 0.0054  166 LEU A C   
1439  O O   . LEU A 166 ? 0.7101 0.7236 0.7321 0.0478  -0.0307 0.0061  166 LEU A O   
1440  C CB  . LEU A 166 ? 0.6876 0.7505 0.7400 0.0482  -0.0322 -0.0076 166 LEU A CB  
1441  C CG  . LEU A 166 ? 0.6376 0.7091 0.6967 0.0398  -0.0262 -0.0151 166 LEU A CG  
1442  C CD1 . LEU A 166 ? 0.6699 0.7643 0.7465 0.0447  -0.0262 -0.0189 166 LEU A CD1 
1443  C CD2 . LEU A 166 ? 0.7275 0.7807 0.7802 0.0369  -0.0187 -0.0168 166 LEU A CD2 
1444  N N   . ASN A 167 ? 0.6171 0.6580 0.6450 0.0558  -0.0430 0.0130  167 ASN A N   
1445  C CA  . ASN A 167 ? 0.6628 0.6870 0.6836 0.0613  -0.0453 0.0241  167 ASN A CA  
1446  C C   . ASN A 167 ? 0.7250 0.7392 0.7280 0.0526  -0.0438 0.0275  167 ASN A C   
1447  O O   . ASN A 167 ? 0.7575 0.7516 0.7542 0.0520  -0.0407 0.0326  167 ASN A O   
1448  C CB  . ASN A 167 ? 0.6876 0.7244 0.7133 0.0706  -0.0544 0.0336  167 ASN A CB  
1449  C CG  . ASN A 167 ? 0.8936 0.9301 0.9375 0.0829  -0.0555 0.0338  167 ASN A CG  
1450  O OD1 . ASN A 167 ? 1.0251 1.0445 1.0744 0.0856  -0.0497 0.0296  167 ASN A OD1 
1451  N ND2 . ASN A 167 ? 0.9100 0.9670 0.9641 0.0906  -0.0629 0.0375  167 ASN A ND2 
1452  N N   . LYS A 168 ? 0.6878 0.7167 0.6835 0.0456  -0.0456 0.0237  168 LYS A N   
1453  C CA  . LYS A 168 ? 0.6310 0.6534 0.6114 0.0377  -0.0430 0.0241  168 LYS A CA  
1454  C C   . LYS A 168 ? 0.6458 0.6506 0.6255 0.0322  -0.0348 0.0186  168 LYS A C   
1455  O O   . LYS A 168 ? 0.7218 0.7140 0.6914 0.0287  -0.0318 0.0226  168 LYS A O   
1456  C CB  . LYS A 168 ? 0.5947 0.6364 0.5707 0.0316  -0.0460 0.0168  168 LYS A CB  
1457  C CG  . LYS A 168 ? 0.7578 0.8180 0.7275 0.0347  -0.0542 0.0235  168 LYS A CG  
1458  C CD  . LYS A 168 ? 0.9610 1.0135 0.9166 0.0358  -0.0549 0.0366  168 LYS A CD  
1459  C CE  . LYS A 168 ? 1.0021 1.0761 0.9439 0.0327  -0.0602 0.0384  168 LYS A CE  
1460  N NZ  . LYS A 168 ? 0.8600 0.9285 0.7855 0.0277  -0.0565 0.0438  168 LYS A NZ  
1461  N N   . TYR A 169 ? 0.5843 0.5903 0.5749 0.0311  -0.0313 0.0102  169 TYR A N   
1462  C CA  . TYR A 169 ? 0.5309 0.5230 0.5209 0.0260  -0.0241 0.0059  169 TYR A CA  
1463  C C   . TYR A 169 ? 0.5957 0.5696 0.5849 0.0302  -0.0215 0.0108  169 TYR A C   
1464  O O   . TYR A 169 ? 0.6680 0.6282 0.6506 0.0254  -0.0171 0.0110  169 TYR A O   
1465  C CB  . TYR A 169 ? 0.4955 0.4961 0.4972 0.0236  -0.0212 -0.0024 169 TYR A CB  
1466  C CG  . TYR A 169 ? 0.5386 0.5486 0.5410 0.0154  -0.0214 -0.0084 169 TYR A CG  
1467  C CD1 . TYR A 169 ? 0.5085 0.5249 0.5040 0.0130  -0.0256 -0.0089 169 TYR A CD1 
1468  C CD2 . TYR A 169 ? 0.5597 0.5728 0.5703 0.0098  -0.0176 -0.0136 169 TYR A CD2 
1469  C CE1 . TYR A 169 ? 0.4951 0.5181 0.4932 0.0059  -0.0262 -0.0161 169 TYR A CE1 
1470  C CE2 . TYR A 169 ? 0.5466 0.5656 0.5603 0.0021  -0.0185 -0.0183 169 TYR A CE2 
1471  C CZ  . TYR A 169 ? 0.5260 0.5488 0.5341 0.0005  -0.0229 -0.0205 169 TYR A CZ  
1472  O OH  . TYR A 169 ? 0.4747 0.5014 0.4872 -0.0066 -0.0242 -0.0270 169 TYR A OH  
1473  N N   . PHE A 170 ? 0.5856 0.5589 0.5828 0.0393  -0.0246 0.0144  170 PHE A N   
1474  C CA  . PHE A 170 ? 0.7401 0.6937 0.7387 0.0434  -0.0226 0.0176  170 PHE A CA  
1475  C C   . PHE A 170 ? 0.6555 0.5965 0.6439 0.0426  -0.0253 0.0293  170 PHE A C   
1476  O O   . PHE A 170 ? 0.6871 0.6092 0.6736 0.0413  -0.0226 0.0316  170 PHE A O   
1477  C CB  . PHE A 170 ? 0.8074 0.7633 0.8206 0.0544  -0.0248 0.0164  170 PHE A CB  
1478  C CG  . PHE A 170 ? 0.8544 0.8150 0.8773 0.0548  -0.0192 0.0046  170 PHE A CG  
1479  C CD1 . PHE A 170 ? 0.9644 0.9095 0.9871 0.0536  -0.0137 -0.0005 170 PHE A CD1 
1480  C CD2 . PHE A 170 ? 0.8255 0.8082 0.8574 0.0556  -0.0192 -0.0013 170 PHE A CD2 
1481  C CE1 . PHE A 170 ? 0.9291 0.8823 0.9593 0.0536  -0.0083 -0.0115 170 PHE A CE1 
1482  C CE2 . PHE A 170 ? 0.8328 0.8232 0.8731 0.0553  -0.0136 -0.0110 170 PHE A CE2 
1483  C CZ  . PHE A 170 ? 0.8446 0.8211 0.8833 0.0545  -0.0080 -0.0162 170 PHE A CZ  
1484  N N   . GLU A 171 ? 0.6571 0.6096 0.6385 0.0425  -0.0305 0.0366  171 GLU A N   
1485  C CA  . GLU A 171 ? 0.7461 0.6907 0.7160 0.0397  -0.0322 0.0486  171 GLU A CA  
1486  C C   . GLU A 171 ? 0.6813 0.6187 0.6411 0.0298  -0.0261 0.0455  171 GLU A C   
1487  O O   . GLU A 171 ? 0.6882 0.6113 0.6427 0.0268  -0.0246 0.0530  171 GLU A O   
1488  C CB  . GLU A 171 ? 0.6968 0.6607 0.6595 0.0406  -0.0387 0.0557  171 GLU A CB  
1489  C CG  . GLU A 171 ? 0.8667 0.8356 0.8380 0.0508  -0.0462 0.0647  171 GLU A CG  
1490  C CD  . GLU A 171 ? 1.0066 1.0020 0.9739 0.0517  -0.0527 0.0663  171 GLU A CD  
1491  O OE1 . GLU A 171 ? 1.1283 1.1342 1.0814 0.0447  -0.0528 0.0674  171 GLU A OE1 
1492  O OE2 . GLU A 171 ? 0.9695 0.9768 0.9482 0.0593  -0.0578 0.0657  171 GLU A OE2 
1493  N N   . ILE A 172 ? 0.6460 0.5932 0.6046 0.0246  -0.0228 0.0348  172 ILE A N   
1494  C CA  . ILE A 172 ? 0.6729 0.6149 0.6247 0.0164  -0.0172 0.0310  172 ILE A CA  
1495  C C   . ILE A 172 ? 0.6474 0.5715 0.6034 0.0150  -0.0126 0.0290  172 ILE A C   
1496  O O   . ILE A 172 ? 0.7342 0.6491 0.6843 0.0095  -0.0094 0.0316  172 ILE A O   
1497  C CB  . ILE A 172 ? 0.5870 0.5422 0.5401 0.0123  -0.0157 0.0203  172 ILE A CB  
1498  C CG1 . ILE A 172 ? 0.6561 0.6262 0.6003 0.0100  -0.0183 0.0203  172 ILE A CG1 
1499  C CG2 . ILE A 172 ? 0.6266 0.5736 0.5794 0.0061  -0.0097 0.0150  172 ILE A CG2 
1500  C CD1 . ILE A 172 ? 0.7196 0.7002 0.6593 0.0147  -0.0247 0.0287  172 ILE A CD1 
1501  N N   . ILE A 173 ? 0.6431 0.5643 0.6096 0.0199  -0.0122 0.0237  173 ILE A N   
1502  C CA  . ILE A 173 ? 0.7288 0.6356 0.6992 0.0188  -0.0080 0.0197  173 ILE A CA  
1503  C C   . ILE A 173 ? 0.7583 0.6467 0.7279 0.0206  -0.0097 0.0281  173 ILE A C   
1504  O O   . ILE A 173 ? 0.7130 0.5884 0.6803 0.0153  -0.0065 0.0276  173 ILE A O   
1505  C CB  . ILE A 173 ? 0.7596 0.6720 0.7414 0.0239  -0.0069 0.0108  173 ILE A CB  
1506  C CG1 . ILE A 173 ? 0.7068 0.6346 0.6894 0.0189  -0.0044 0.0038  173 ILE A CG1 
1507  C CG2 . ILE A 173 ? 0.7373 0.6352 0.7234 0.0248  -0.0036 0.0059  173 ILE A CG2 
1508  C CD1 . ILE A 173 ? 0.7170 0.6553 0.7104 0.0223  -0.0027 -0.0040 173 ILE A CD1 
1509  N N   . LYS A 174 ? 0.7015 0.5891 0.6738 0.0275  -0.0152 0.0367  174 LYS A N   
1510  C CA  . LYS A 174 ? 0.6815 0.5504 0.6548 0.0291  -0.0178 0.0472  174 LYS A CA  
1511  C C   . LYS A 174 ? 0.6977 0.5638 0.6587 0.0202  -0.0169 0.0571  174 LYS A C   
1512  O O   . LYS A 174 ? 0.7641 0.6127 0.7256 0.0176  -0.0172 0.0645  174 LYS A O   
1513  C CB  . LYS A 174 ? 0.7098 0.5806 0.6898 0.0391  -0.0248 0.0563  174 LYS A CB  
1514  C CG  . LYS A 174 ? 0.7408 0.6077 0.7367 0.0496  -0.0257 0.0484  174 LYS A CG  
1515  C CD  . LYS A 174 ? 0.7647 0.6467 0.7673 0.0593  -0.0322 0.0535  174 LYS A CD  
1516  C CE  . LYS A 174 ? 0.8882 0.7781 0.9056 0.0676  -0.0308 0.0406  174 LYS A CE  
1517  N NZ  . LYS A 174 ? 0.9874 0.8606 1.0201 0.0786  -0.0333 0.0411  174 LYS A NZ  
1518  N N   . LYS A 175 ? 0.7099 0.5936 0.6611 0.0154  -0.0158 0.0566  175 LYS A N   
1519  C CA  . LYS A 175 ? 0.6937 0.5801 0.6333 0.0074  -0.0143 0.0646  175 LYS A CA  
1520  C C   . LYS A 175 ? 0.7204 0.6057 0.6571 -0.0007 -0.0080 0.0565  175 LYS A C   
1521  O O   . LYS A 175 ? 0.7483 0.6368 0.6768 -0.0075 -0.0059 0.0619  175 LYS A O   
1522  C CB  . LYS A 175 ? 0.7011 0.6096 0.6318 0.0077  -0.0170 0.0678  175 LYS A CB  
1523  C CG  . LYS A 175 ? 0.6999 0.6129 0.6307 0.0142  -0.0241 0.0801  175 LYS A CG  
1524  C CD  . LYS A 175 ? 0.6916 0.6300 0.6123 0.0137  -0.0270 0.0812  175 LYS A CD  
1525  C CE  . LYS A 175 ? 0.7665 0.7176 0.6829 0.0086  -0.0222 0.0668  175 LYS A CE  
1526  N NZ  . LYS A 175 ? 0.8539 0.8291 0.7643 0.0095  -0.0257 0.0629  175 LYS A NZ  
1527  N N   . THR A 176 ? 0.6820 0.5647 0.6252 -0.0002 -0.0051 0.0445  176 THR A N   
1528  C CA  . THR A 176 ? 0.6443 0.5299 0.5852 -0.0071 0.0000  0.0374  176 THR A CA  
1529  C C   . THR A 176 ? 0.6702 0.5434 0.6090 -0.0140 0.0023  0.0419  176 THR A C   
1530  O O   . THR A 176 ? 0.6662 0.5459 0.5989 -0.0203 0.0048  0.0445  176 THR A O   
1531  C CB  . THR A 176 ? 0.7384 0.6255 0.6868 -0.0053 0.0019  0.0259  176 THR A CB  
1532  O OG1 . THR A 176 ? 0.6529 0.5547 0.6031 -0.0018 0.0003  0.0217  176 THR A OG1 
1533  C CG2 . THR A 176 ? 0.5001 0.3874 0.4474 -0.0125 0.0064  0.0206  176 THR A CG2 
1534  N N   . LEU A 177 ? 0.6979 0.5537 0.6428 -0.0129 0.0016  0.0421  177 LEU A N   
1535  C CA  . LEU A 177 ? 0.7446 0.5884 0.6891 -0.0208 0.0037  0.0442  177 LEU A CA  
1536  C C   . LEU A 177 ? 0.6905 0.5318 0.6294 -0.0257 0.0024  0.0586  177 LEU A C   
1537  O O   . LEU A 177 ? 0.7528 0.5915 0.6896 -0.0344 0.0049  0.0613  177 LEU A O   
1538  C CB  . LEU A 177 ? 0.6971 0.5222 0.6506 -0.0187 0.0029  0.0386  177 LEU A CB  
1539  C CG  . LEU A 177 ? 0.7512 0.5816 0.7093 -0.0154 0.0052  0.0241  177 LEU A CG  
1540  C CD1 . LEU A 177 ? 0.8386 0.6724 0.8026 -0.0046 0.0025  0.0218  177 LEU A CD1 
1541  C CD2 . LEU A 177 ? 0.7646 0.5816 0.7275 -0.0190 0.0068  0.0158  177 LEU A CD2 
1542  N N   . SER A 178 ? 0.6704 0.5149 0.6069 -0.0209 -0.0016 0.0687  178 SER A N   
1543  C CA  . SER A 178 ? 0.7316 0.5778 0.6614 -0.0264 -0.0027 0.0842  178 SER A CA  
1544  C C   . SER A 178 ? 0.7204 0.5881 0.6404 -0.0324 0.0014  0.0839  178 SER A C   
1545  O O   . SER A 178 ? 0.7620 0.6325 0.6772 -0.0403 0.0032  0.0934  178 SER A O   
1546  C CB  . SER A 178 ? 0.6833 0.5312 0.6120 -0.0195 -0.0085 0.0961  178 SER A CB  
1547  O OG  . SER A 178 ? 0.7230 0.5480 0.6620 -0.0155 -0.0127 0.1018  178 SER A OG  
1548  N N   . ILE A 179 ? 0.6675 0.5506 0.5856 -0.0288 0.0030  0.0728  179 ILE A N   
1549  C CA  . ILE A 179 ? 0.6738 0.5766 0.5849 -0.0330 0.0068  0.0701  179 ILE A CA  
1550  C C   . ILE A 179 ? 0.7215 0.6221 0.6353 -0.0402 0.0115  0.0655  179 ILE A C   
1551  O O   . ILE A 179 ? 0.7062 0.6198 0.6154 -0.0456 0.0149  0.0680  179 ILE A O   
1552  C CB  . ILE A 179 ? 0.5626 0.4799 0.4732 -0.0271 0.0063  0.0592  179 ILE A CB  
1553  C CG1 . ILE A 179 ? 0.7103 0.6496 0.6117 -0.0286 0.0076  0.0601  179 ILE A CG1 
1554  C CG2 . ILE A 179 ? 0.6745 0.5901 0.5918 -0.0275 0.0093  0.0465  179 ILE A CG2 
1555  C CD1 . ILE A 179 ? 0.6988 0.6516 0.6003 -0.0235 0.0062  0.0491  179 ILE A CD1 
1556  N N   . TYR A 180 ? 0.6641 0.5507 0.5855 -0.0403 0.0118  0.0585  180 TYR A N   
1557  C CA  . TYR A 180 ? 0.6523 0.5378 0.5764 -0.0477 0.0153  0.0552  180 TYR A CA  
1558  C C   . TYR A 180 ? 0.7345 0.6117 0.6579 -0.0558 0.0156  0.0661  180 TYR A C   
1559  O O   . TYR A 180 ? 0.7257 0.6117 0.6482 -0.0633 0.0188  0.0679  180 TYR A O   
1560  C CB  . TYR A 180 ? 0.6968 0.5722 0.6278 -0.0463 0.0153  0.0449  180 TYR A CB  
1561  C CG  . TYR A 180 ? 0.6650 0.5516 0.5978 -0.0417 0.0162  0.0351  180 TYR A CG  
1562  C CD1 . TYR A 180 ? 0.6340 0.5329 0.5674 -0.0448 0.0189  0.0313  180 TYR A CD1 
1563  C CD2 . TYR A 180 ? 0.5563 0.4411 0.4917 -0.0345 0.0140  0.0305  180 TYR A CD2 
1564  C CE1 . TYR A 180 ? 0.5734 0.4803 0.5102 -0.0411 0.0191  0.0240  180 TYR A CE1 
1565  C CE2 . TYR A 180 ? 0.5863 0.4809 0.5245 -0.0317 0.0146  0.0230  180 TYR A CE2 
1566  C CZ  . TYR A 180 ? 0.6101 0.5143 0.5490 -0.0352 0.0170  0.0202  180 TYR A CZ  
1567  O OH  . TYR A 180 ? 0.5768 0.4886 0.5202 -0.0328 0.0169  0.0143  180 TYR A OH  
1568  N N   . ARG A 181 ? 0.7787 0.6392 0.7039 -0.0545 0.0119  0.0739  181 ARG A N   
1569  C CA  . ARG A 181 ? 0.7341 0.5861 0.6593 -0.0625 0.0112  0.0874  181 ARG A CA  
1570  C C   . ARG A 181 ? 0.7535 0.6260 0.6695 -0.0663 0.0131  0.0984  181 ARG A C   
1571  O O   . ARG A 181 ? 0.7592 0.6376 0.6742 -0.0760 0.0158  0.1053  181 ARG A O   
1572  C CB  . ARG A 181 ? 0.7216 0.5515 0.6520 -0.0584 0.0059  0.0947  181 ARG A CB  
1573  C CG  . ARG A 181 ? 0.7485 0.5545 0.6891 -0.0608 0.0048  0.0886  181 ARG A CG  
1574  C CD  . ARG A 181 ? 0.8351 0.6194 0.7816 -0.0603 -0.0002 0.1015  181 ARG A CD  
1575  N NE  . ARG A 181 ? 0.9232 0.7034 0.8696 -0.0728 0.0003  0.1150  181 ARG A NE  
1576  C CZ  . ARG A 181 ? 0.9152 0.6741 0.8707 -0.0808 -0.0008 0.1156  181 ARG A CZ  
1577  N NH1 . ARG A 181 ? 0.8244 0.5615 0.7902 -0.0767 -0.0030 0.1033  181 ARG A NH1 
1578  N NH2 . ARG A 181 ? 1.0077 0.7679 0.9627 -0.0937 0.0002  0.1285  181 ARG A NH2 
1579  N N   . GLU A 182 ? 0.7358 0.6219 0.6452 -0.0591 0.0117  0.0993  182 GLU A N   
1580  C CA  . GLU A 182 ? 0.7985 0.7068 0.6979 -0.0621 0.0133  0.1087  182 GLU A CA  
1581  C C   . GLU A 182 ? 0.8244 0.7534 0.7215 -0.0668 0.0194  0.1014  182 GLU A C   
1582  O O   . GLU A 182 ? 0.7703 0.7133 0.6629 -0.0744 0.0225  0.1104  182 GLU A O   
1583  C CB  . GLU A 182 ? 0.7735 0.6935 0.6665 -0.0531 0.0101  0.1080  182 GLU A CB  
1584  C CG  . GLU A 182 ? 0.8858 0.8353 0.7677 -0.0549 0.0129  0.1099  182 GLU A CG  
1585  C CD  . GLU A 182 ? 1.1602 1.1231 1.0362 -0.0466 0.0095  0.1054  182 GLU A CD  
1586  O OE1 . GLU A 182 ? 1.1621 1.1130 1.0410 -0.0407 0.0038  0.1095  182 GLU A OE1 
1587  O OE2 . GLU A 182 ? 1.2987 1.2850 1.1683 -0.0458 0.0123  0.0972  182 GLU A OE2 
1588  N N   . ILE A 183 ? 0.7132 0.6455 0.6144 -0.0623 0.0212  0.0858  183 ILE A N   
1589  C CA  . ILE A 183 ? 0.6676 0.6198 0.5688 -0.0651 0.0264  0.0790  183 ILE A CA  
1590  C C   . ILE A 183 ? 0.7628 0.7110 0.6696 -0.0746 0.0291  0.0821  183 ILE A C   
1591  O O   . ILE A 183 ? 0.7190 0.6862 0.6254 -0.0794 0.0336  0.0827  183 ILE A O   
1592  C CB  . ILE A 183 ? 0.5931 0.5495 0.4986 -0.0577 0.0268  0.0632  183 ILE A CB  
1593  C CG1 . ILE A 183 ? 0.6187 0.5561 0.5327 -0.0569 0.0251  0.0570  183 ILE A CG1 
1594  C CG2 . ILE A 183 ? 0.5377 0.5011 0.4381 -0.0501 0.0242  0.0597  183 ILE A CG2 
1595  C CD1 . ILE A 183 ? 0.5264 0.4691 0.4471 -0.0604 0.0282  0.0505  183 ILE A CD1 
1596  N N   . LYS A 184 ? 0.7199 0.6453 0.6329 -0.0774 0.0265  0.0831  184 LYS A N   
1597  C CA  . LYS A 184 ? 0.8124 0.7339 0.7310 -0.0878 0.0283  0.0862  184 LYS A CA  
1598  C C   . LYS A 184 ? 0.8265 0.7522 0.7418 -0.0970 0.0292  0.1023  184 LYS A C   
1599  O O   . LYS A 184 ? 0.7707 0.7108 0.6878 -0.1056 0.0330  0.1055  184 LYS A O   
1600  C CB  . LYS A 184 ? 0.7236 0.6201 0.6494 -0.0888 0.0250  0.0814  184 LYS A CB  
1601  C CG  . LYS A 184 ? 0.7318 0.6313 0.6640 -0.0956 0.0269  0.0743  184 LYS A CG  
1602  C CD  . LYS A 184 ? 0.7141 0.5909 0.6526 -0.0985 0.0238  0.0691  184 LYS A CD  
1603  C CE  . LYS A 184 ? 0.6567 0.5171 0.5984 -0.1079 0.0219  0.0795  184 LYS A CE  
1604  N NZ  . LYS A 184 ? 0.8930 0.7707 0.8348 -0.1186 0.0252  0.0878  184 LYS A NZ  
1605  N N   . GLU A 185 ? 0.8087 0.7230 0.7201 -0.0957 0.0255  0.1137  185 GLU A N   
1606  C CA  . GLU A 185 ? 0.7578 0.6755 0.6663 -0.1052 0.0258  0.1320  185 GLU A CA  
1607  C C   . GLU A 185 ? 0.6478 0.5987 0.5468 -0.1066 0.0305  0.1364  185 GLU A C   
1608  O O   . GLU A 185 ? 0.8217 0.7851 0.7192 -0.1171 0.0334  0.1490  185 GLU A O   
1609  C CB  . GLU A 185 ? 0.9307 0.8280 0.8384 -0.1024 0.0198  0.1445  185 GLU A CB  
1610  C CG  . GLU A 185 ? 1.0800 0.9463 0.9984 -0.1090 0.0161  0.1504  185 GLU A CG  
1611  C CD  . GLU A 185 ? 1.1260 0.9660 1.0497 -0.0989 0.0102  0.1471  185 GLU A CD  
1612  O OE1 . GLU A 185 ? 1.0664 0.9134 0.9846 -0.0882 0.0082  0.1459  185 GLU A OE1 
1613  O OE2 . GLU A 185 ? 1.4001 1.2136 1.3344 -0.1017 0.0074  0.1448  185 GLU A OE2 
1614  N N   . GLU A 186 ? 0.6853 0.5355 0.6337 -0.0524 0.0091  0.1108  186 GLU A N   
1615  C CA  . GLU A 186 ? 0.7808 0.6431 0.7176 -0.0612 0.0135  0.1141  186 GLU A CA  
1616  C C   . GLU A 186 ? 0.7302 0.6125 0.6748 -0.0702 0.0255  0.1075  186 GLU A C   
1617  O O   . GLU A 186 ? 0.6469 0.5406 0.5830 -0.0780 0.0311  0.1086  186 GLU A O   
1618  C CB  . GLU A 186 ? 0.7785 0.6542 0.7166 -0.0526 0.0087  0.1123  186 GLU A CB  
1619  C CG  . GLU A 186 ? 0.8882 0.7503 0.8061 -0.0524 -0.0007 0.1232  186 GLU A CG  
1620  C CD  . GLU A 186 ? 1.0330 0.9054 0.9564 -0.0404 -0.0094 0.1210  186 GLU A CD  
1621  O OE1 . GLU A 186 ? 1.0381 0.9329 0.9683 -0.0404 -0.0050 0.1136  186 GLU A OE1 
1622  O OE2 . GLU A 186 ? 1.0732 0.9313 0.9943 -0.0308 -0.0208 0.1264  186 GLU A OE2 
1623  N N   . GLY A 187 ? 0.7711 0.6583 0.7311 -0.0690 0.0294  0.1005  187 GLY A N   
1624  C CA  . GLY A 187 ? 0.7274 0.6351 0.6972 -0.0748 0.0393  0.0940  187 GLY A CA  
1625  C C   . GLY A 187 ? 0.6857 0.6144 0.6662 -0.0678 0.0427  0.0863  187 GLY A C   
1626  O O   . GLY A 187 ? 0.6771 0.6226 0.6661 -0.0708 0.0504  0.0808  187 GLY A O   
1627  N N   . LYS A 188 ? 0.6464 0.5748 0.6272 -0.0587 0.0369  0.0855  188 LYS A N   
1628  C CA  . LYS A 188 ? 0.5838 0.5297 0.5728 -0.0536 0.0403  0.0781  188 LYS A CA  
1629  C C   . LYS A 188 ? 0.5310 0.4839 0.5368 -0.0474 0.0425  0.0703  188 LYS A C   
1630  O O   . LYS A 188 ? 0.5423 0.5076 0.5548 -0.0440 0.0462  0.0641  188 LYS A O   
1631  C CB  . LYS A 188 ? 0.6028 0.5475 0.5865 -0.0476 0.0331  0.0796  188 LYS A CB  
1632  C CG  . LYS A 188 ? 0.6178 0.5532 0.5821 -0.0532 0.0289  0.0888  188 LYS A CG  
1633  C CD  . LYS A 188 ? 0.7242 0.6633 0.6834 -0.0478 0.0216  0.0894  188 LYS A CD  
1634  C CE  . LYS A 188 ? 0.8358 0.7769 0.7756 -0.0564 0.0226  0.0943  188 LYS A CE  
1635  N NZ  . LYS A 188 ? 0.8997 0.8225 0.8214 -0.0631 0.0189  0.1059  188 LYS A NZ  
1636  N N   . GLY A 189 ? 0.5359 0.4798 0.5470 -0.0466 0.0405  0.0704  189 GLY A N   
1637  C CA  . GLY A 189 ? 0.5224 0.4730 0.5469 -0.0424 0.0429  0.0634  189 GLY A CA  
1638  C C   . GLY A 189 ? 0.6174 0.5551 0.6444 -0.0423 0.0396  0.0637  189 GLY A C   
1639  O O   . GLY A 189 ? 0.6393 0.5604 0.6589 -0.0427 0.0344  0.0688  189 GLY A O   
1640  N N   . SER A 190 ? 0.5929 0.5370 0.6293 -0.0415 0.0424  0.0582  190 SER A N   
1641  C CA  . SER A 190 ? 0.5888 0.5228 0.6280 -0.0420 0.0402  0.0564  190 SER A CA  
1642  C C   . SER A 190 ? 0.6648 0.5982 0.7108 -0.0328 0.0379  0.0504  190 SER A C   
1643  O O   . SER A 190 ? 0.6494 0.5949 0.7007 -0.0286 0.0403  0.0465  190 SER A O   
1644  C CB  . SER A 190 ? 0.5404 0.4839 0.5845 -0.0485 0.0443  0.0540  190 SER A CB  
1645  O OG  . SER A 190 ? 0.5846 0.5264 0.6228 -0.0586 0.0461  0.0589  190 SER A OG  
1646  N N   . VAL A 191 ? 0.6235 0.5421 0.6690 -0.0302 0.0339  0.0494  191 VAL A N   
1647  C CA  . VAL A 191 ? 0.5956 0.5141 0.6481 -0.0220 0.0326  0.0425  191 VAL A CA  
1648  C C   . VAL A 191 ? 0.6224 0.5369 0.6769 -0.0250 0.0340  0.0374  191 VAL A C   
1649  O O   . VAL A 191 ? 0.6965 0.5988 0.7460 -0.0312 0.0329  0.0395  191 VAL A O   
1650  C CB  . VAL A 191 ? 0.6721 0.5782 0.7238 -0.0141 0.0266  0.0435  191 VAL A CB  
1651  C CG1 . VAL A 191 ? 0.5620 0.4734 0.6234 -0.0057 0.0268  0.0348  191 VAL A CG1 
1652  C CG2 . VAL A 191 ? 0.6708 0.5809 0.7185 -0.0123 0.0238  0.0495  191 VAL A CG2 
1653  N N   . SER A 192 ? 0.6817 0.6059 0.7420 -0.0217 0.0365  0.0307  192 SER A N   
1654  C CA  . SER A 192 ? 0.5914 0.5145 0.6525 -0.0244 0.0378  0.0250  192 SER A CA  
1655  C C   . SER A 192 ? 0.6914 0.6130 0.7565 -0.0172 0.0381  0.0173  192 SER A C   
1656  O O   . SER A 192 ? 0.6427 0.5671 0.7119 -0.0101 0.0372  0.0163  192 SER A O   
1657  C CB  . SER A 192 ? 0.6039 0.5424 0.6662 -0.0285 0.0412  0.0248  192 SER A CB  
1658  O OG  . SER A 192 ? 0.6475 0.5959 0.7128 -0.0234 0.0437  0.0217  192 SER A OG  
1659  N N   . THR A 193 ? 0.7516 0.6710 0.8158 -0.0195 0.0394  0.0110  193 THR A N   
1660  C CA  . THR A 193 ? 0.7040 0.6235 0.7714 -0.0138 0.0410  0.0022  193 THR A CA  
1661  C C   . THR A 193 ? 0.6269 0.5547 0.6913 -0.0186 0.0444  -0.0028 193 THR A C   
1662  O O   . THR A 193 ? 0.5541 0.4866 0.6148 -0.0253 0.0442  0.0008  193 THR A O   
1663  C CB  . THR A 193 ? 0.7500 0.6510 0.8172 -0.0101 0.0383  -0.0019 193 THR A CB  
1664  O OG1 . THR A 193 ? 0.7244 0.6290 0.7985 -0.0011 0.0398  -0.0098 193 THR A OG1 
1665  C CG2 . THR A 193 ? 0.6595 0.5510 0.7205 -0.0176 0.0388  -0.0062 193 THR A CG2 
1666  N N   . SER A 194 ? 0.6342 0.5651 0.7001 -0.0151 0.0474  -0.0111 194 SER A N   
1667  C CA  . SER A 194 ? 0.6286 0.5654 0.6888 -0.0199 0.0505  -0.0162 194 SER A CA  
1668  C C   . SER A 194 ? 0.6774 0.6042 0.7358 -0.0193 0.0514  -0.0261 194 SER A C   
1669  O O   . SER A 194 ? 0.6894 0.6055 0.7528 -0.0131 0.0500  -0.0290 194 SER A O   
1670  C CB  . SER A 194 ? 0.6414 0.5919 0.7023 -0.0185 0.0549  -0.0178 194 SER A CB  
1671  O OG  . SER A 194 ? 0.6650 0.6225 0.7270 -0.0187 0.0544  -0.0097 194 SER A OG  
1672  N N   . PRO A 195 ? 0.6886 0.6174 0.7393 -0.0250 0.0533  -0.0315 195 PRO A N   
1673  C CA  . PRO A 195 ? 0.6944 0.6156 0.7429 -0.0239 0.0559  -0.0432 195 PRO A CA  
1674  C C   . PRO A 195 ? 0.7134 0.6395 0.7707 -0.0148 0.0601  -0.0499 195 PRO A C   
1675  O O   . PRO A 195 ? 0.5688 0.5088 0.6301 -0.0129 0.0626  -0.0474 195 PRO A O   
1676  C CB  . PRO A 195 ? 0.6062 0.5350 0.6435 -0.0320 0.0581  -0.0467 195 PRO A CB  
1677  C CG  . PRO A 195 ? 0.6468 0.5801 0.6810 -0.0379 0.0534  -0.0364 195 PRO A CG  
1678  C CD  . PRO A 195 ? 0.5639 0.5015 0.6067 -0.0326 0.0526  -0.0275 195 PRO A CD  
1679  N N   . TYR A 196 ? 0.7063 0.6212 0.7668 -0.0095 0.0610  -0.0593 196 TYR A N   
1680  C CA  . TYR A 196 ? 0.7433 0.6602 0.8165 0.0021  0.0623  -0.0646 196 TYR A CA  
1681  C C   . TYR A 196 ? 0.6987 0.6377 0.7778 0.0038  0.0680  -0.0676 196 TYR A C   
1682  O O   . TYR A 196 ? 0.5723 0.5202 0.6615 0.0096  0.0666  -0.0635 196 TYR A O   
1683  C CB  . TYR A 196 ? 0.6390 0.5424 0.7136 0.0073  0.0641  -0.0773 196 TYR A CB  
1684  C CG  . TYR A 196 ? 0.6758 0.5739 0.7642 0.0214  0.0616  -0.0797 196 TYR A CG  
1685  C CD1 . TYR A 196 ? 0.7628 0.6803 0.8644 0.0296  0.0653  -0.0853 196 TYR A CD1 
1686  C CD2 . TYR A 196 ? 0.6694 0.5436 0.7577 0.0263  0.0551  -0.0760 196 TYR A CD2 
1687  C CE1 . TYR A 196 ? 0.6851 0.6006 0.8011 0.0438  0.0618  -0.0875 196 TYR A CE1 
1688  C CE2 . TYR A 196 ? 0.6249 0.4931 0.7251 0.0406  0.0514  -0.0771 196 TYR A CE2 
1689  C CZ  . TYR A 196 ? 0.7275 0.6177 0.8424 0.0500  0.0543  -0.0830 196 TYR A CZ  
1690  O OH  . TYR A 196 ? 0.9420 0.8291 1.0703 0.0652  0.0495  -0.0842 196 TYR A OH  
1691  N N   . TYR A 197 ? 0.6379 0.5857 0.7097 -0.0022 0.0744  -0.0749 197 TYR A N   
1692  C CA  . TYR A 197 ? 0.6425 0.6099 0.7187 -0.0021 0.0813  -0.0799 197 TYR A CA  
1693  C C   . TYR A 197 ? 0.6492 0.6250 0.7138 -0.0122 0.0831  -0.0722 197 TYR A C   
1694  O O   . TYR A 197 ? 0.6897 0.6762 0.7481 -0.0176 0.0899  -0.0772 197 TYR A O   
1695  C CB  . TYR A 197 ? 0.6909 0.6625 0.7675 -0.0009 0.0888  -0.0956 197 TYR A CB  
1696  C CG  . TYR A 197 ? 0.6609 0.6280 0.7529 0.0121  0.0882  -0.1047 197 TYR A CG  
1697  C CD1 . TYR A 197 ? 0.5891 0.5703 0.6988 0.0218  0.0884  -0.1064 197 TYR A CD1 
1698  C CD2 . TYR A 197 ? 0.7269 0.6751 0.8156 0.0151  0.0869  -0.1119 197 TYR A CD2 
1699  C CE1 . TYR A 197 ? 0.6297 0.6070 0.7543 0.0355  0.0867  -0.1144 197 TYR A CE1 
1700  C CE2 . TYR A 197 ? 0.6968 0.6379 0.7991 0.0284  0.0859  -0.1202 197 TYR A CE2 
1701  C CZ  . TYR A 197 ? 0.7166 0.6726 0.8372 0.0394  0.0854  -0.1210 197 TYR A CZ  
1702  O OH  . TYR A 197 ? 0.7962 0.7451 0.9311 0.0545  0.0832  -0.1289 197 TYR A OH  
1703  N N   . HIS A 198 ? 0.6913 0.6617 0.7523 -0.0147 0.0771  -0.0598 198 HIS A N   
1704  C CA  . HIS A 198 ? 0.6208 0.5967 0.6721 -0.0220 0.0774  -0.0514 198 HIS A CA  
1705  C C   . HIS A 198 ? 0.6986 0.6758 0.7341 -0.0304 0.0811  -0.0550 198 HIS A C   
1706  O O   . HIS A 198 ? 0.6990 0.6837 0.7271 -0.0352 0.0854  -0.0535 198 HIS A O   
1707  C CB  . HIS A 198 ? 0.5215 0.5093 0.5792 -0.0206 0.0808  -0.0494 198 HIS A CB  
1708  C CG  . HIS A 198 ? 0.5865 0.5741 0.6390 -0.0241 0.0781  -0.0379 198 HIS A CG  
1709  N ND1 . HIS A 198 ? 0.6145 0.6052 0.6555 -0.0308 0.0817  -0.0349 198 HIS A ND1 
1710  C CD2 . HIS A 198 ? 0.5955 0.5789 0.6518 -0.0216 0.0727  -0.0290 198 HIS A CD2 
1711  C CE1 . HIS A 198 ? 0.6685 0.6565 0.7077 -0.0311 0.0782  -0.0251 198 HIS A CE1 
1712  N NE2 . HIS A 198 ? 0.6626 0.6475 0.7113 -0.0258 0.0732  -0.0219 198 HIS A NE2 
1713  N N   . PRO A 199 ? 0.7140 0.6830 0.7425 -0.0330 0.0793  -0.0596 199 PRO A N   
1714  C CA  . PRO A 199 ? 0.6837 0.6545 0.6956 -0.0414 0.0822  -0.0634 199 PRO A CA  
1715  C C   . PRO A 199 ? 0.7357 0.7063 0.7363 -0.0470 0.0769  -0.0517 199 PRO A C   
1716  O O   . PRO A 199 ? 0.7568 0.7262 0.7635 -0.0444 0.0716  -0.0420 199 PRO A O   
1717  C CB  . PRO A 199 ? 0.6856 0.6466 0.6954 -0.0419 0.0810  -0.0726 199 PRO A CB  
1718  C CG  . PRO A 199 ? 0.6708 0.6221 0.6902 -0.0376 0.0738  -0.0661 199 PRO A CG  
1719  C CD  . PRO A 199 ? 0.6378 0.5941 0.6709 -0.0301 0.0740  -0.0605 199 PRO A CD  
1720  N N   . LEU A 200 ? 0.7457 0.7182 0.7293 -0.0545 0.0782  -0.0530 200 LEU A N   
1721  C CA  . LEU A 200 ? 0.7302 0.7025 0.7022 -0.0588 0.0717  -0.0425 200 LEU A CA  
1722  C C   . LEU A 200 ? 0.7185 0.6873 0.6842 -0.0632 0.0661  -0.0457 200 LEU A C   
1723  O O   . LEU A 200 ? 0.7404 0.7095 0.6917 -0.0695 0.0678  -0.0524 200 LEU A O   
1724  C CB  . LEU A 200 ? 0.7053 0.6807 0.6606 -0.0644 0.0755  -0.0396 200 LEU A CB  
1725  C CG  . LEU A 200 ? 0.6854 0.6621 0.6449 -0.0617 0.0779  -0.0318 200 LEU A CG  
1726  C CD1 . LEU A 200 ? 0.7804 0.7584 0.7239 -0.0685 0.0848  -0.0325 200 LEU A CD1 
1727  C CD2 . LEU A 200 ? 0.6185 0.5926 0.5792 -0.0586 0.0699  -0.0191 200 LEU A CD2 
1728  N N   . ILE A 201 ? 0.7604 0.7265 0.7364 -0.0609 0.0597  -0.0413 201 ILE A N   
1729  C CA  . ILE A 201 ? 0.7013 0.6637 0.6738 -0.0660 0.0548  -0.0457 201 ILE A CA  
1730  C C   . ILE A 201 ? 0.7005 0.6689 0.6571 -0.0734 0.0494  -0.0428 201 ILE A C   
1731  O O   . ILE A 201 ? 0.7093 0.6756 0.6560 -0.0800 0.0486  -0.0512 201 ILE A O   
1732  C CB  . ILE A 201 ? 0.5880 0.5467 0.5747 -0.0635 0.0499  -0.0410 201 ILE A CB  
1733  C CG1 . ILE A 201 ? 0.5957 0.5457 0.5950 -0.0565 0.0542  -0.0450 201 ILE A CG1 
1734  C CG2 . ILE A 201 ? 0.5469 0.5030 0.5293 -0.0711 0.0445  -0.0445 201 ILE A CG2 
1735  C CD1 . ILE A 201 ? 0.6085 0.5468 0.6069 -0.0575 0.0566  -0.0573 201 ILE A CD1 
1736  N N   . PRO A 202 ? 0.6327 0.6080 0.5857 -0.0724 0.0450  -0.0317 202 PRO A N   
1737  C CA  . PRO A 202 ? 0.6443 0.6255 0.5811 -0.0785 0.0385  -0.0287 202 PRO A CA  
1738  C C   . PRO A 202 ? 0.6940 0.6730 0.6109 -0.0851 0.0431  -0.0367 202 PRO A C   
1739  O O   . PRO A 202 ? 0.7413 0.7231 0.6451 -0.0923 0.0382  -0.0401 202 PRO A O   
1740  C CB  . PRO A 202 ? 0.5762 0.5616 0.5128 -0.0733 0.0349  -0.0155 202 PRO A CB  
1741  C CG  . PRO A 202 ? 0.6072 0.5917 0.5637 -0.0661 0.0366  -0.0118 202 PRO A CG  
1742  C CD  . PRO A 202 ? 0.6117 0.5892 0.5750 -0.0654 0.0445  -0.0213 202 PRO A CD  
1743  N N   . ILE A 203 ? 0.7034 0.6791 0.6178 -0.0836 0.0525  -0.0405 203 ILE A N   
1744  C CA  . ILE A 203 ? 0.7452 0.7204 0.6403 -0.0907 0.0586  -0.0488 203 ILE A CA  
1745  C C   . ILE A 203 ? 0.7212 0.6931 0.6170 -0.0942 0.0623  -0.0642 203 ILE A C   
1746  O O   . ILE A 203 ? 0.7736 0.7459 0.6515 -0.1024 0.0620  -0.0710 203 ILE A O   
1747  C CB  . ILE A 203 ? 0.7466 0.7216 0.6405 -0.0891 0.0684  -0.0487 203 ILE A CB  
1748  C CG1 . ILE A 203 ? 0.7126 0.6871 0.6006 -0.0874 0.0645  -0.0337 203 ILE A CG1 
1749  C CG2 . ILE A 203 ? 0.6672 0.6432 0.5428 -0.0972 0.0770  -0.0594 203 ILE A CG2 
1750  C CD1 . ILE A 203 ? 0.7290 0.7022 0.6072 -0.0904 0.0736  -0.0331 203 ILE A CD1 
1751  N N   . LEU A 204 ? 0.6886 0.6555 0.6036 -0.0879 0.0654  -0.0699 204 LEU A N   
1752  C CA  . LEU A 204 ? 0.7216 0.6816 0.6379 -0.0897 0.0688  -0.0846 204 LEU A CA  
1753  C C   . LEU A 204 ? 0.7695 0.7273 0.6776 -0.0974 0.0605  -0.0862 204 LEU A C   
1754  O O   . LEU A 204 ? 0.8499 0.8038 0.7460 -0.1040 0.0628  -0.0985 204 LEU A O   
1755  C CB  . LEU A 204 ? 0.7057 0.6584 0.6439 -0.0803 0.0714  -0.0876 204 LEU A CB  
1756  C CG  . LEU A 204 ? 0.7302 0.6875 0.6789 -0.0728 0.0792  -0.0879 204 LEU A CG  
1757  C CD1 . LEU A 204 ? 0.7504 0.7003 0.7196 -0.0630 0.0803  -0.0914 204 LEU A CD1 
1758  C CD2 . LEU A 204 ? 0.6621 0.6249 0.5989 -0.0768 0.0889  -0.0990 204 LEU A CD2 
1759  N N   . LEU A 205 ? 0.7621 0.7235 0.6769 -0.0971 0.0511  -0.0749 205 LEU A N   
1760  C CA  . LEU A 205 ? 0.7793 0.7419 0.6888 -0.1051 0.0427  -0.0762 205 LEU A CA  
1761  C C   . LEU A 205 ? 0.6787 0.6502 0.5660 -0.1136 0.0382  -0.0755 205 LEU A C   
1762  O O   . LEU A 205 ? 0.6738 0.6433 0.5478 -0.1225 0.0376  -0.0860 205 LEU A O   
1763  C CB  . LEU A 205 ? 0.7652 0.7329 0.6901 -0.1024 0.0347  -0.0647 205 LEU A CB  
1764  C CG  . LEU A 205 ? 0.7144 0.6721 0.6583 -0.0964 0.0376  -0.0650 205 LEU A CG  
1765  C CD1 . LEU A 205 ? 0.6774 0.6421 0.6339 -0.0962 0.0302  -0.0544 205 LEU A CD1 
1766  C CD2 . LEU A 205 ? 0.6284 0.5710 0.5707 -0.1004 0.0410  -0.0789 205 LEU A CD2 
1767  N N   . ASN A 206 ? 0.6605 0.6406 0.5425 -0.1111 0.0345  -0.0631 206 ASN A N   
1768  C CA  . ASN A 206 ? 0.6938 0.6804 0.5521 -0.1181 0.0300  -0.0608 206 ASN A CA  
1769  C C   . ASN A 206 ? 0.7717 0.7583 0.6208 -0.1142 0.0339  -0.0520 206 ASN A C   
1770  O O   . ASN A 206 ? 0.7468 0.7358 0.6049 -0.1070 0.0300  -0.0391 206 ASN A O   
1771  C CB  . ASN A 206 ? 0.8253 0.8234 0.6834 -0.1210 0.0161  -0.0527 206 ASN A CB  
1772  C CG  . ASN A 206 ? 0.8949 0.9002 0.7293 -0.1254 0.0092  -0.0461 206 ASN A CG  
1773  O OD1 . ASN A 206 ? 1.0440 1.0548 0.8790 -0.1194 0.0026  -0.0323 206 ASN A OD1 
1774  N ND2 . ASN A 206 ? 0.9592 0.9632 0.7714 -0.1355 0.0107  -0.0558 206 ASN A ND2 
1775  N N   . PRO A 207 ? 0.7847 0.7680 0.6154 -0.1195 0.0422  -0.0589 207 PRO A N   
1776  C CA  . PRO A 207 ? 0.7119 0.6937 0.5318 -0.1181 0.0469  -0.0505 207 PRO A CA  
1777  C C   . PRO A 207 ? 0.7822 0.7667 0.5862 -0.1188 0.0361  -0.0354 207 PRO A C   
1778  O O   . PRO A 207 ? 0.7230 0.7032 0.5220 -0.1157 0.0381  -0.0253 207 PRO A O   
1779  C CB  . PRO A 207 ? 0.7739 0.7538 0.5758 -0.1263 0.0581  -0.0637 207 PRO A CB  
1780  C CG  . PRO A 207 ? 0.7166 0.6944 0.5321 -0.1259 0.0625  -0.0794 207 PRO A CG  
1781  C CD  . PRO A 207 ? 0.7635 0.7433 0.5844 -0.1267 0.0499  -0.0760 207 PRO A CD  
1782  N N   . ASN A 208 ? 0.9470 0.9382 0.7433 -0.1228 0.0244  -0.0335 208 ASN A N   
1783  C CA  . ASN A 208 ? 0.8202 0.8155 0.6043 -0.1213 0.0118  -0.0187 208 ASN A CA  
1784  C C   . ASN A 208 ? 0.8235 0.8202 0.6285 -0.1093 0.0066  -0.0058 208 ASN A C   
1785  O O   . ASN A 208 ? 0.8329 0.8327 0.6308 -0.1054 -0.0042 0.0068  208 ASN A O   
1786  C CB  . ASN A 208 ? 0.7563 0.7624 0.5325 -0.1277 -0.0002 -0.0212 208 ASN A CB  
1787  C CG  . ASN A 208 ? 0.8905 0.8950 0.6383 -0.1401 0.0029  -0.0309 208 ASN A CG  
1788  O OD1 . ASN A 208 ? 1.0274 1.0331 0.7759 -0.1471 0.0064  -0.0456 208 ASN A OD1 
1789  N ND2 . ASN A 208 ? 0.8930 0.8927 0.6140 -0.1434 0.0026  -0.0231 208 ASN A ND2 
1790  N N   . CYS A 209 ? 0.7925 0.7869 0.6222 -0.1028 0.0134  -0.0087 209 CYS A N   
1791  C CA  . CYS A 209 ? 0.8226 0.8178 0.6707 -0.0920 0.0099  0.0025  209 CYS A CA  
1792  C C   . CYS A 209 ? 0.8245 0.8094 0.6616 -0.0881 0.0132  0.0126  209 CYS A C   
1793  O O   . CYS A 209 ? 0.9060 0.8901 0.7530 -0.0792 0.0088  0.0230  209 CYS A O   
1794  C CB  . CYS A 209 ? 0.6791 0.6738 0.5535 -0.0874 0.0165  -0.0036 209 CYS A CB  
1795  S SG  . CYS A 209 ? 0.8682 0.8528 0.7435 -0.0891 0.0325  -0.0143 209 CYS A SG  
1796  N N   . VAL A 210 ? 0.7115 0.6881 0.5282 -0.0952 0.0216  0.0092  210 VAL A N   
1797  C CA  . VAL A 210 ? 0.8541 0.8190 0.6594 -0.0935 0.0257  0.0186  210 VAL A CA  
1798  C C   . VAL A 210 ? 0.7915 0.7522 0.5768 -0.0919 0.0140  0.0327  210 VAL A C   
1799  O O   . VAL A 210 ? 0.8437 0.7935 0.6250 -0.0865 0.0131  0.0439  210 VAL A O   
1800  C CB  . VAL A 210 ? 0.8496 0.8086 0.6397 -0.1029 0.0393  0.0103  210 VAL A CB  
1801  C CG1 . VAL A 210 ? 0.7837 0.7491 0.5934 -0.1034 0.0487  -0.0051 210 VAL A CG1 
1802  C CG2 . VAL A 210 ? 0.7581 0.7159 0.5164 -0.1135 0.0370  0.0098  210 VAL A CG2 
1803  N N   . TYR A 211 ? 0.8102 0.7788 0.5827 -0.0961 0.0042  0.0325  211 TYR A N   
1804  C CA  . TYR A 211 ? 0.8648 0.8299 0.6166 -0.0941 -0.0084 0.0462  211 TYR A CA  
1805  C C   . TYR A 211 ? 0.8369 0.8097 0.6083 -0.0810 -0.0210 0.0559  211 TYR A C   
1806  O O   . TYR A 211 ? 0.8013 0.7704 0.5589 -0.0759 -0.0323 0.0686  211 TYR A O   
1807  C CB  . TYR A 211 ? 0.7848 0.7572 0.5136 -0.1043 -0.0149 0.0422  211 TYR A CB  
1808  C CG  . TYR A 211 ? 0.7937 0.7615 0.5035 -0.1177 -0.0022 0.0302  211 TYR A CG  
1809  C CD1 . TYR A 211 ? 0.7904 0.7437 0.4750 -0.1240 0.0060  0.0345  211 TYR A CD1 
1810  C CD2 . TYR A 211 ? 0.7795 0.7575 0.4961 -0.1245 0.0020  0.0142  211 TYR A CD2 
1811  C CE1 . TYR A 211 ? 0.7923 0.7443 0.4602 -0.1365 0.0185  0.0225  211 TYR A CE1 
1812  C CE2 . TYR A 211 ? 0.7654 0.7403 0.4655 -0.1357 0.0141  0.0019  211 TYR A CE2 
1813  C CZ  . TYR A 211 ? 0.8386 0.8021 0.5151 -0.1416 0.0226  0.0059  211 TYR A CZ  
1814  O OH  . TYR A 211 ? 0.9573 0.9204 0.6183 -0.1531 0.0357  -0.0074 211 TYR A OH  
1815  N N   . GLU A 212 ? 0.7896 0.7729 0.5922 -0.0752 -0.0193 0.0503  212 GLU A N   
1816  C CA  . GLU A 212 ? 0.7482 0.7412 0.5713 -0.0630 -0.0295 0.0581  212 GLU A CA  
1817  C C   . GLU A 212 ? 0.7857 0.7636 0.6082 -0.0527 -0.0287 0.0698  212 GLU A C   
1818  O O   . GLU A 212 ? 0.8133 0.7940 0.6392 -0.0423 -0.0398 0.0799  212 GLU A O   
1819  C CB  . GLU A 212 ? 0.6744 0.6804 0.5286 -0.0612 -0.0259 0.0491  212 GLU A CB  
1820  C CG  . GLU A 212 ? 0.7769 0.7938 0.6321 -0.0718 -0.0256 0.0366  212 GLU A CG  
1821  C CD  . GLU A 212 ? 0.9781 1.0113 0.8609 -0.0698 -0.0289 0.0321  212 GLU A CD  
1822  O OE1 . GLU A 212 ? 1.0222 1.0672 0.9187 -0.0613 -0.0377 0.0395  212 GLU A OE1 
1823  O OE2 . GLU A 212 ? 1.1000 1.1340 0.9904 -0.0767 -0.0226 0.0208  212 GLU A OE2 
1824  N N   . THR A 213 ? 0.8572 0.8191 0.6755 -0.0554 -0.0158 0.0680  213 THR A N   
1825  C CA  . THR A 213 ? 0.8334 0.7777 0.6483 -0.0480 -0.0136 0.0778  213 THR A CA  
1826  C C   . THR A 213 ? 0.8993 0.8227 0.6823 -0.0561 -0.0083 0.0828  213 THR A C   
1827  O O   . THR A 213 ? 0.9195 0.8246 0.6940 -0.0511 -0.0081 0.0926  213 THR A O   
1828  C CB  . THR A 213 ? 0.8097 0.7532 0.6489 -0.0444 -0.0030 0.0721  213 THR A CB  
1829  O OG1 . THR A 213 ? 0.8762 0.8213 0.7165 -0.0544 0.0087  0.0603  213 THR A OG1 
1830  C CG2 . THR A 213 ? 0.7562 0.7177 0.6245 -0.0358 -0.0085 0.0699  213 THR A CG2 
1831  N N   . THR A 214 ? 0.8846 0.8094 0.6489 -0.0689 -0.0038 0.0762  214 THR A N   
1832  C CA  . THR A 214 ? 0.8660 0.7731 0.5995 -0.0793 0.0034  0.0793  214 THR A CA  
1833  C C   . THR A 214 ? 0.8835 0.7956 0.5911 -0.0893 -0.0016 0.0778  214 THR A C   
1834  O O   . THR A 214 ? 0.8175 0.7366 0.5203 -0.1003 0.0073  0.0653  214 THR A O   
1835  C CB  . THR A 214 ? 0.9098 0.8146 0.6506 -0.0868 0.0206  0.0685  214 THR A CB  
1836  O OG1 . THR A 214 ? 0.9656 0.8888 0.7319 -0.0864 0.0243  0.0548  214 THR A OG1 
1837  C CG2 . THR A 214 ? 0.8553 0.7467 0.6065 -0.0803 0.0254  0.0742  214 THR A CG2 
1838  N N   . PRO A 215 ? 0.9735 0.8817 0.6629 -0.0855 -0.0162 0.0902  215 PRO A N   
1839  C CA  . PRO A 215 ? 0.8803 0.7990 0.5499 -0.0933 -0.0245 0.0881  215 PRO A CA  
1840  C C   . PRO A 215 ? 0.9809 0.8884 0.6141 -0.1092 -0.0165 0.0864  215 PRO A C   
1841  O O   . PRO A 215 ? 1.1006 1.0196 0.7215 -0.1188 -0.0178 0.0781  215 PRO A O   
1842  C CB  . PRO A 215 ? 0.8817 0.7999 0.5453 -0.0819 -0.0437 0.1035  215 PRO A CB  
1843  C CG  . PRO A 215 ? 0.9637 0.8795 0.6567 -0.0664 -0.0445 0.1083  215 PRO A CG  
1844  C CD  . PRO A 215 ? 0.9161 0.8147 0.6087 -0.0712 -0.0276 0.1052  215 PRO A CD  
1845  N N   . ASN A 216 ? 0.9866 0.8726 0.6009 -0.1135 -0.0081 0.0935  216 ASN A N   
1846  C CA  . ASN A 216 ? 1.0104 0.8860 0.5873 -0.1299 -0.0004 0.0929  216 ASN A CA  
1847  C C   . ASN A 216 ? 1.0292 0.9066 0.6117 -0.1409 0.0203  0.0784  216 ASN A C   
1848  O O   . ASN A 216 ? 1.0407 0.9088 0.5937 -0.1550 0.0298  0.0778  216 ASN A O   
1849  C CB  . ASN A 216 ? 1.0563 0.9050 0.6006 -0.1301 -0.0061 0.1120  216 ASN A CB  
1850  C CG  . ASN A 216 ? 1.1685 1.0143 0.7149 -0.1144 -0.0266 0.1271  216 ASN A CG  
1851  O OD1 . ASN A 216 ? 1.2284 1.0668 0.7951 -0.1005 -0.0300 0.1340  216 ASN A OD1 
1852  N ND2 . ASN A 216 ? 1.1682 1.0214 0.6945 -0.1163 -0.0405 0.1317  216 ASN A ND2 
1853  N N   . VAL A 217 ? 0.9063 0.7967 0.5253 -0.1350 0.0276  0.0664  217 VAL A N   
1854  C CA  . VAL A 217 ? 0.8950 0.7897 0.5214 -0.1439 0.0461  0.0523  217 VAL A CA  
1855  C C   . VAL A 217 ? 0.9951 0.9019 0.6072 -0.1562 0.0522  0.0382  217 VAL A C   
1856  O O   . VAL A 217 ? 0.9269 0.8410 0.5291 -0.1572 0.0420  0.0374  217 VAL A O   
1857  C CB  . VAL A 217 ? 0.7871 0.6925 0.4549 -0.1338 0.0509  0.0434  217 VAL A CB  
1858  C CG1 . VAL A 217 ? 0.8962 0.7890 0.5754 -0.1235 0.0473  0.0556  217 VAL A CG1 
1859  C CG2 . VAL A 217 ? 0.8524 0.7745 0.5410 -0.1269 0.0421  0.0363  217 VAL A CG2 
1860  N N   . LYS A 218 ? 1.1023 1.0127 0.7147 -0.1656 0.0693  0.0260  218 LYS A N   
1861  C CA  . LYS A 218 ? 1.0305 0.9529 0.6325 -0.1769 0.0785  0.0097  218 LYS A CA  
1862  C C   . LYS A 218 ? 0.9323 0.8696 0.5706 -0.1714 0.0885  -0.0077 218 LYS A C   
1863  O O   . LYS A 218 ? 0.8606 0.7985 0.5151 -0.1702 0.0992  -0.0109 218 LYS A O   
1864  C CB  . LYS A 218 ? 0.9120 0.8269 0.4809 -0.1933 0.0911  0.0098  218 LYS A CB  
1865  C CG  . LYS A 218 ? 1.0122 0.9166 0.5373 -0.2031 0.0827  0.0206  218 LYS A CG  
1866  C CD  . LYS A 218 ? 1.1360 1.0540 0.6463 -0.2137 0.0874  0.0048  218 LYS A CD  
1867  C CE  . LYS A 218 ? 1.0658 0.9763 0.5313 -0.2323 0.0956  0.0066  218 LYS A CE  
1868  N NZ  . LYS A 218 ? 1.1062 1.0327 0.5648 -0.2429 0.1067  -0.0144 218 LYS A NZ  
1869  N N   . ILE A 219 ? 0.9507 0.8991 0.6019 -0.1679 0.0840  -0.0185 219 ILE A N   
1870  C CA  . ILE A 219 ? 0.9591 0.9187 0.6430 -0.1619 0.0920  -0.0346 219 ILE A CA  
1871  C C   . ILE A 219 ? 0.9802 0.9485 0.6537 -0.1712 0.1014  -0.0532 219 ILE A C   
1872  O O   . ILE A 219 ? 1.0093 0.9766 0.6543 -0.1804 0.0972  -0.0532 219 ILE A O   
1873  C CB  . ILE A 219 ? 0.8546 0.8170 0.5661 -0.1489 0.0798  -0.0319 219 ILE A CB  
1874  C CG1 . ILE A 219 ? 0.9200 0.8870 0.6224 -0.1516 0.0699  -0.0363 219 ILE A CG1 
1875  C CG2 . ILE A 219 ? 0.7418 0.6958 0.4571 -0.1407 0.0694  -0.0134 219 ILE A CG2 
1876  C CD1 . ILE A 219 ? 0.7703 0.7431 0.5028 -0.1427 0.0647  -0.0427 219 ILE A CD1 
1877  N N   . PRO A 220 ? 0.9988 0.9760 0.6943 -0.1688 0.1139  -0.0695 220 PRO A N   
1878  C CA  . PRO A 220 ? 0.9428 0.9277 0.6296 -0.1765 0.1239  -0.0888 220 PRO A CA  
1879  C C   . PRO A 220 ? 1.0418 1.0267 0.7281 -0.1751 0.1139  -0.0949 220 PRO A C   
1880  O O   . PRO A 220 ? 1.0051 0.9876 0.7106 -0.1656 0.1024  -0.0892 220 PRO A O   
1881  C CB  . PRO A 220 ? 0.9180 0.9120 0.6358 -0.1696 0.1369  -0.1029 220 PRO A CB  
1882  C CG  . PRO A 220 ? 0.9517 0.9419 0.6983 -0.1558 0.1278  -0.0924 220 PRO A CG  
1883  C CD  . PRO A 220 ? 0.9530 0.9337 0.6829 -0.1579 0.1186  -0.0717 220 PRO A CD  
1884  N N   . ASP A 221 ? 1.0991 1.0869 0.7621 -0.1860 0.1189  -0.1073 221 ASP A N   
1885  C CA  . ASP A 221 ? 1.1196 1.1074 0.7798 -0.1873 0.1113  -0.1163 221 ASP A CA  
1886  C C   . ASP A 221 ? 1.0985 1.0874 0.7926 -0.1768 0.1155  -0.1307 221 ASP A C   
1887  O O   . ASP A 221 ? 1.0816 1.0748 0.7842 -0.1763 0.1298  -0.1474 221 ASP A O   
1888  C CB  . ASP A 221 ? 1.1095 1.1000 0.7360 -0.2022 0.1179  -0.1283 221 ASP A CB  
1889  C CG  . ASP A 221 ? 1.3307 1.3195 0.9375 -0.2082 0.1034  -0.1263 221 ASP A CG  
1890  O OD1 . ASP A 221 ? 1.3903 1.3765 0.9835 -0.2089 0.0892  -0.1076 221 ASP A OD1 
1891  O OD2 . ASP A 221 ? 1.4148 1.4049 1.0200 -0.2121 0.1060  -0.1438 221 ASP A OD2 
1892  N N   . PHE A 222 ? 0.9970 0.9820 0.7108 -0.1681 0.1031  -0.1241 222 PHE A N   
1893  C CA  . PHE A 222 ? 0.9107 0.8931 0.6549 -0.1581 0.1054  -0.1350 222 PHE A CA  
1894  C C   . PHE A 222 ? 1.0070 0.9863 0.7419 -0.1644 0.1061  -0.1524 222 PHE A C   
1895  O O   . PHE A 222 ? 1.0098 0.9858 0.7418 -0.1669 0.0944  -0.1502 222 PHE A O   
1896  C CB  . PHE A 222 ? 0.8312 0.8103 0.5977 -0.1483 0.0929  -0.1208 222 PHE A CB  
1897  C CG  . PHE A 222 ? 0.8789 0.8591 0.6662 -0.1384 0.0963  -0.1114 222 PHE A CG  
1898  C CD1 . PHE A 222 ? 0.9730 0.9543 0.7506 -0.1395 0.0935  -0.0953 222 PHE A CD1 
1899  C CD2 . PHE A 222 ? 0.8551 0.8339 0.6707 -0.1281 0.1017  -0.1185 222 PHE A CD2 
1900  C CE1 . PHE A 222 ? 0.8738 0.8555 0.6696 -0.1315 0.0968  -0.0876 222 PHE A CE1 
1901  C CE2 . PHE A 222 ? 0.7119 0.6930 0.5458 -0.1198 0.1042  -0.1103 222 PHE A CE2 
1902  C CZ  . PHE A 222 ? 0.6947 0.6775 0.5187 -0.1221 0.1020  -0.0954 222 PHE A CZ  
1903  N N   . ALA A 223 ? 1.0260 1.0072 0.7563 -0.1674 0.1206  -0.1709 223 ALA A N   
1904  C CA  . ALA A 223 ? 0.8856 0.8625 0.6054 -0.1735 0.1239  -0.1902 223 ALA A CA  
1905  C C   . ALA A 223 ? 0.8995 0.8661 0.6464 -0.1633 0.1236  -0.2009 223 ALA A C   
1906  O O   . ALA A 223 ? 0.8435 0.8029 0.5836 -0.1675 0.1264  -0.2179 223 ALA A O   
1907  C CB  . ALA A 223 ? 0.9510 0.9347 0.6549 -0.1804 0.1408  -0.2068 223 ALA A CB  
1908  N N   . VAL A 224 ? 0.9242 0.8881 0.6998 -0.1505 0.1203  -0.1914 224 VAL A N   
1909  C CA  . VAL A 224 ? 0.9554 0.9070 0.7555 -0.1405 0.1188  -0.1984 224 VAL A CA  
1910  C C   . VAL A 224 ? 0.9103 0.8587 0.7249 -0.1358 0.1051  -0.1798 224 VAL A C   
1911  O O   . VAL A 224 ? 0.9250 0.8817 0.7372 -0.1361 0.0993  -0.1627 224 VAL A O   
1912  C CB  . VAL A 224 ? 0.9532 0.9057 0.7766 -0.1278 0.1311  -0.2087 224 VAL A CB  
1913  C CG1 . VAL A 224 ? 0.9081 0.8668 0.7523 -0.1180 0.1286  -0.1923 224 VAL A CG1 
1914  C CG2 . VAL A 224 ? 0.9913 0.9273 0.8299 -0.1201 0.1323  -0.2233 224 VAL A CG2 
1915  N N   . SER A 225 ? 0.8045 0.7398 0.6332 -0.1317 0.1002  -0.1835 225 SER A N   
1916  C CA  . SER A 225 ? 0.8957 0.8283 0.7390 -0.1280 0.0884  -0.1677 225 SER A CA  
1917  C C   . SER A 225 ? 0.9006 0.8280 0.7711 -0.1135 0.0914  -0.1642 225 SER A C   
1918  O O   . SER A 225 ? 0.8827 0.8001 0.7639 -0.1065 0.0986  -0.1773 225 SER A O   
1919  C CB  . SER A 225 ? 0.9448 0.8666 0.7843 -0.1353 0.0802  -0.1722 225 SER A CB  
1920  O OG  . SER A 225 ? 0.9253 0.8512 0.7736 -0.1355 0.0684  -0.1556 225 SER A OG  
1921  N N   . PHE A 226 ? 0.8240 0.7582 0.7053 -0.1087 0.0856  -0.1468 226 PHE A N   
1922  C CA  . PHE A 226 ? 0.8253 0.7561 0.7308 -0.0961 0.0867  -0.1413 226 PHE A CA  
1923  C C   . PHE A 226 ? 0.8879 0.8103 0.8051 -0.0945 0.0768  -0.1316 226 PHE A C   
1924  O O   . PHE A 226 ? 0.8293 0.7493 0.7644 -0.0852 0.0758  -0.1241 226 PHE A O   
1925  C CB  . PHE A 226 ? 0.7882 0.7327 0.6976 -0.0920 0.0893  -0.1301 226 PHE A CB  
1926  C CG  . PHE A 226 ? 0.8299 0.7828 0.7338 -0.0921 0.1013  -0.1401 226 PHE A CG  
1927  C CD1 . PHE A 226 ? 0.7848 0.7380 0.7064 -0.0821 0.1096  -0.1497 226 PHE A CD1 
1928  C CD2 . PHE A 226 ? 0.8217 0.7833 0.7026 -0.1023 0.1041  -0.1397 226 PHE A CD2 
1929  C CE1 . PHE A 226 ? 0.7771 0.7417 0.6955 -0.0828 0.1214  -0.1600 226 PHE A CE1 
1930  C CE2 . PHE A 226 ? 0.7540 0.7245 0.6291 -0.1041 0.1162  -0.1491 226 PHE A CE2 
1931  C CZ  . PHE A 226 ? 0.8193 0.7925 0.7141 -0.0946 0.1254  -0.1598 226 PHE A CZ  
1932  N N   . ARG A 227 ? 0.8482 0.7671 0.7552 -0.1044 0.0695  -0.1320 227 ARG A N   
1933  C CA  . ARG A 227 ? 0.8104 0.7251 0.7278 -0.1052 0.0605  -0.1221 227 ARG A CA  
1934  C C   . ARG A 227 ? 0.8121 0.7074 0.7437 -0.0987 0.0623  -0.1272 227 ARG A C   
1935  O O   . ARG A 227 ? 0.8210 0.7132 0.7661 -0.0945 0.0580  -0.1167 227 ARG A O   
1936  C CB  . ARG A 227 ? 0.8029 0.7211 0.7065 -0.1185 0.0525  -0.1229 227 ARG A CB  
1937  C CG  . ARG A 227 ? 0.8276 0.7619 0.7127 -0.1249 0.0505  -0.1202 227 ARG A CG  
1938  C CD  . ARG A 227 ? 0.7505 0.6922 0.6238 -0.1372 0.0405  -0.1193 227 ARG A CD  
1939  N NE  . ARG A 227 ? 0.8418 0.7814 0.7290 -0.1394 0.0333  -0.1142 227 ARG A NE  
1940  C CZ  . ARG A 227 ? 0.6748 0.6284 0.5713 -0.1383 0.0251  -0.1000 227 ARG A CZ  
1941  N NH1 . ARG A 227 ? 0.6827 0.6505 0.5773 -0.1331 0.0226  -0.0885 227 ARG A NH1 
1942  N NH2 . ARG A 227 ? 0.6884 0.6411 0.5962 -0.1427 0.0198  -0.0977 227 ARG A NH2 
1943  N N   . GLU A 228 ? 0.8341 0.7152 0.7620 -0.0977 0.0687  -0.1432 228 GLU A N   
1944  C CA  . GLU A 228 ? 0.8476 0.7069 0.7879 -0.0900 0.0700  -0.1479 228 GLU A CA  
1945  C C   . GLU A 228 ? 0.8879 0.7500 0.8458 -0.0752 0.0731  -0.1417 228 GLU A C   
1946  O O   . GLU A 228 ? 0.9510 0.8025 0.9212 -0.0693 0.0693  -0.1338 228 GLU A O   
1947  C CB  . GLU A 228 ? 0.9379 0.7804 0.8700 -0.0910 0.0763  -0.1677 228 GLU A CB  
1948  C CG  . GLU A 228 ? 1.0056 0.8287 0.9521 -0.0768 0.0807  -0.1746 228 GLU A CG  
1949  C CD  . GLU A 228 ? 1.0901 0.8868 1.0403 -0.0778 0.0748  -0.1716 228 GLU A CD  
1950  O OE1 . GLU A 228 ? 1.1412 0.9349 1.0820 -0.0915 0.0687  -0.1679 228 GLU A OE1 
1951  O OE2 . GLU A 228 ? 1.1587 0.9380 1.1209 -0.0652 0.0759  -0.1728 228 GLU A OE2 
1952  N N   . ASP A 229 ? 0.8628 0.7400 0.8215 -0.0701 0.0800  -0.1449 229 ASP A N   
1953  C CA  . ASP A 229 ? 0.8653 0.7488 0.8412 -0.0572 0.0827  -0.1394 229 ASP A CA  
1954  C C   . ASP A 229 ? 0.8247 0.7165 0.8074 -0.0569 0.0758  -0.1209 229 ASP A C   
1955  O O   . ASP A 229 ? 0.8845 0.7749 0.8821 -0.0472 0.0748  -0.1145 229 ASP A O   
1956  C CB  . ASP A 229 ? 0.8334 0.7340 0.8077 -0.0548 0.0920  -0.1469 229 ASP A CB  
1957  C CG  . ASP A 229 ? 0.9994 0.8930 0.9759 -0.0490 0.1006  -0.1662 229 ASP A CG  
1958  O OD1 . ASP A 229 ? 1.0118 0.8843 0.9909 -0.0457 0.0988  -0.1736 229 ASP A OD1 
1959  O OD2 . ASP A 229 ? 0.9730 0.8818 0.9485 -0.0480 0.1095  -0.1745 229 ASP A OD2 
1960  N N   . ALA A 230 ? 0.7878 0.6888 0.7600 -0.0670 0.0707  -0.1124 230 ALA A N   
1961  C CA  . ALA A 230 ? 0.7662 0.6749 0.7453 -0.0662 0.0646  -0.0961 230 ALA A CA  
1962  C C   . ALA A 230 ? 0.8493 0.7437 0.8380 -0.0645 0.0594  -0.0911 230 ALA A C   
1963  O O   . ALA A 230 ? 0.8762 0.7716 0.8766 -0.0578 0.0576  -0.0814 230 ALA A O   
1964  C CB  . ALA A 230 ? 0.7182 0.6395 0.6850 -0.0761 0.0595  -0.0892 230 ALA A CB  
1965  N N   . SER A 231 ? 0.8209 0.7008 0.8034 -0.0714 0.0571  -0.0979 231 SER A N   
1966  C CA  . SER A 231 ? 0.8324 0.6952 0.8213 -0.0717 0.0528  -0.0936 231 SER A CA  
1967  C C   . SER A 231 ? 0.8508 0.6991 0.8507 -0.0587 0.0556  -0.0954 231 SER A C   
1968  O O   . SER A 231 ? 0.7988 0.6395 0.8066 -0.0551 0.0521  -0.0859 231 SER A O   
1969  C CB  . SER A 231 ? 0.8044 0.6526 0.7825 -0.0831 0.0508  -0.1024 231 SER A CB  
1970  O OG  . SER A 231 ? 0.8167 0.6817 0.7856 -0.0946 0.0470  -0.1004 231 SER A OG  
1971  N N   . LYS A 232 ? 0.7847 0.6301 0.7853 -0.0513 0.0618  -0.1077 232 LYS A N   
1972  C CA  . LYS A 232 ? 0.7868 0.6208 0.7998 -0.0371 0.0636  -0.1101 232 LYS A CA  
1973  C C   . LYS A 232 ? 0.7239 0.5725 0.7490 -0.0292 0.0623  -0.0980 232 LYS A C   
1974  O O   . LYS A 232 ? 0.6786 0.5165 0.7129 -0.0205 0.0592  -0.0927 232 LYS A O   
1975  C CB  . LYS A 232 ? 0.7244 0.5584 0.7382 -0.0303 0.0713  -0.1267 232 LYS A CB  
1976  C CG  . LYS A 232 ? 0.8699 0.6877 0.8709 -0.0376 0.0735  -0.1408 232 LYS A CG  
1977  C CD  . LYS A 232 ? 0.8689 0.6698 0.8763 -0.0254 0.0783  -0.1555 232 LYS A CD  
1978  C CE  . LYS A 232 ? 0.9639 0.7729 0.9633 -0.0279 0.0872  -0.1733 232 LYS A CE  
1979  N NZ  . LYS A 232 ? 1.0298 0.8374 1.0421 -0.0121 0.0941  -0.1868 232 LYS A NZ  
1980  N N   . HIS A 233 ? 0.7108 0.5823 0.7345 -0.0323 0.0641  -0.0933 233 HIS A N   
1981  C CA  . HIS A 233 ? 0.7317 0.6164 0.7655 -0.0263 0.0631  -0.0824 233 HIS A CA  
1982  C C   . HIS A 233 ? 0.7063 0.5835 0.7425 -0.0283 0.0563  -0.0693 233 HIS A C   
1983  O O   . HIS A 233 ? 0.7122 0.5852 0.7575 -0.0202 0.0541  -0.0636 233 HIS A O   
1984  C CB  . HIS A 233 ? 0.7394 0.6456 0.7680 -0.0314 0.0660  -0.0792 233 HIS A CB  
1985  C CG  . HIS A 233 ? 0.7549 0.6730 0.7857 -0.0271 0.0737  -0.0886 233 HIS A CG  
1986  N ND1 . HIS A 233 ? 0.6623 0.5887 0.6808 -0.0343 0.0787  -0.0957 233 HIS A ND1 
1987  C CD2 . HIS A 233 ? 0.7055 0.6303 0.7494 -0.0171 0.0774  -0.0922 233 HIS A CD2 
1988  C CE1 . HIS A 233 ? 0.6782 0.6156 0.7018 -0.0297 0.0862  -0.1035 233 HIS A CE1 
1989  N NE2 . HIS A 233 ? 0.7169 0.6548 0.7572 -0.0191 0.0854  -0.1019 233 HIS A NE2 
1990  N N   . VAL A 234 ? 0.7088 0.5854 0.7367 -0.0393 0.0528  -0.0649 234 VAL A N   
1991  C CA  . VAL A 234 ? 0.6765 0.5477 0.7064 -0.0429 0.0475  -0.0537 234 VAL A CA  
1992  C C   . VAL A 234 ? 0.6855 0.5314 0.7168 -0.0396 0.0453  -0.0548 234 VAL A C   
1993  O O   . VAL A 234 ? 0.6839 0.5241 0.7204 -0.0352 0.0425  -0.0460 234 VAL A O   
1994  C CB  . VAL A 234 ? 0.7363 0.6143 0.7584 -0.0558 0.0445  -0.0509 234 VAL A CB  
1995  C CG1 . VAL A 234 ? 0.8185 0.6970 0.8444 -0.0600 0.0403  -0.0394 234 VAL A CG1 
1996  C CG2 . VAL A 234 ? 0.6436 0.5429 0.6620 -0.0575 0.0460  -0.0506 234 VAL A CG2 
1997  N N   . GLU A 235 ? 0.7038 0.5329 0.7294 -0.0413 0.0466  -0.0659 235 GLU A N   
1998  C CA  . GLU A 235 ? 0.7189 0.5191 0.7430 -0.0396 0.0440  -0.0667 235 GLU A CA  
1999  C C   . GLU A 235 ? 0.8221 0.6140 0.8559 -0.0237 0.0437  -0.0660 235 GLU A C   
2000  O O   . GLU A 235 ? 0.8705 0.6456 0.9049 -0.0208 0.0393  -0.0578 235 GLU A O   
2001  C CB  . GLU A 235 ? 0.8486 0.6314 0.8632 -0.0456 0.0457  -0.0801 235 GLU A CB  
2002  C CG  . GLU A 235 ? 0.8913 0.6795 0.8960 -0.0628 0.0439  -0.0798 235 GLU A CG  
2003  C CD  . GLU A 235 ? 1.0903 0.8636 1.0841 -0.0700 0.0459  -0.0944 235 GLU A CD  
2004  O OE1 . GLU A 235 ? 1.1714 0.9153 1.1621 -0.0679 0.0460  -0.1005 235 GLU A OE1 
2005  O OE2 . GLU A 235 ? 1.0881 0.8782 1.0753 -0.0780 0.0471  -0.0999 235 GLU A OE2 
2006  N N   . LEU A 236 ? 0.7805 0.5852 0.8216 -0.0136 0.0481  -0.0744 236 LEU A N   
2007  C CA  . LEU A 236 ? 0.6980 0.4994 0.7508 0.0023  0.0472  -0.0746 236 LEU A CA  
2008  C C   . LEU A 236 ? 0.7376 0.5521 0.7971 0.0055  0.0435  -0.0607 236 LEU A C   
2009  O O   . LEU A 236 ? 0.7336 0.5377 0.7987 0.0153  0.0391  -0.0556 236 LEU A O   
2010  C CB  . LEU A 236 ? 0.8006 0.6173 0.8612 0.0108  0.0537  -0.0881 236 LEU A CB  
2011  C CG  . LEU A 236 ? 0.7766 0.5811 0.8311 0.0095  0.0586  -0.1044 236 LEU A CG  
2012  C CD1 . LEU A 236 ? 0.6376 0.4615 0.7005 0.0174  0.0663  -0.1175 236 LEU A CD1 
2013  C CD2 . LEU A 236 ? 0.8214 0.5917 0.8742 0.0154  0.0548  -0.1076 236 LEU A CD2 
2014  N N   . ALA A 237 ? 0.7176 0.5537 0.7754 -0.0025 0.0449  -0.0544 237 ALA A N   
2015  C CA  . ALA A 237 ? 0.7259 0.5734 0.7884 -0.0010 0.0420  -0.0420 237 ALA A CA  
2016  C C   . ALA A 237 ? 0.7988 0.6279 0.8561 -0.0047 0.0363  -0.0312 237 ALA A C   
2017  O O   . ALA A 237 ? 0.7480 0.5768 0.8091 0.0011  0.0327  -0.0228 237 ALA A O   
2018  C CB  . ALA A 237 ? 0.7423 0.6127 0.8026 -0.0091 0.0448  -0.0383 237 ALA A CB  
2019  N N   . LYS A 238 ? 0.7794 0.5940 0.8271 -0.0155 0.0354  -0.0312 238 LYS A N   
2020  C CA  . LYS A 238 ? 0.8046 0.6007 0.8459 -0.0211 0.0309  -0.0212 238 LYS A CA  
2021  C C   . LYS A 238 ? 0.7948 0.5651 0.8362 -0.0104 0.0268  -0.0204 238 LYS A C   
2022  O O   . LYS A 238 ? 0.8821 0.6417 0.9201 -0.0101 0.0225  -0.0094 238 LYS A O   
2023  C CB  . LYS A 238 ? 0.7200 0.5063 0.7516 -0.0360 0.0313  -0.0232 238 LYS A CB  
2024  C CG  . LYS A 238 ? 0.7133 0.5259 0.7453 -0.0460 0.0334  -0.0221 238 LYS A CG  
2025  C CD  . LYS A 238 ? 0.7788 0.5857 0.8029 -0.0614 0.0328  -0.0237 238 LYS A CD  
2026  C CE  . LYS A 238 ? 0.8831 0.6705 0.9017 -0.0691 0.0301  -0.0156 238 LYS A CE  
2027  N NZ  . LYS A 238 ? 0.8492 0.6253 0.8596 -0.0844 0.0297  -0.0200 238 LYS A NZ  
2028  N N   . GLU A 239 ? 0.7128 0.4727 0.7575 -0.0011 0.0281  -0.0319 239 GLU A N   
2029  C CA  . GLU A 239 ? 0.8440 0.5789 0.8901 0.0116  0.0234  -0.0315 239 GLU A CA  
2030  C C   . GLU A 239 ? 0.7769 0.5272 0.8343 0.0252  0.0204  -0.0263 239 GLU A C   
2031  O O   . GLU A 239 ? 0.7753 0.5096 0.8309 0.0319  0.0138  -0.0175 239 GLU A O   
2032  C CB  . GLU A 239 ? 0.8750 0.5953 0.9227 0.0186  0.0262  -0.0469 239 GLU A CB  
2033  C CG  . GLU A 239 ? 0.8880 0.6058 0.9266 0.0044  0.0310  -0.0557 239 GLU A CG  
2034  C CD  . GLU A 239 ? 1.0886 0.7945 1.1282 0.0109  0.0350  -0.0728 239 GLU A CD  
2035  O OE1 . GLU A 239 ? 1.1704 0.8644 1.1996 -0.0004 0.0375  -0.0805 239 GLU A OE1 
2036  O OE2 . GLU A 239 ? 1.1398 0.8498 1.1910 0.0272  0.0358  -0.0794 239 GLU A OE2 
2037  N N   . LYS A 240 ? 0.6843 0.4654 0.7524 0.0286  0.0247  -0.0315 240 LYS A N   
2038  C CA  . LYS A 240 ? 0.7436 0.5424 0.8224 0.0390  0.0220  -0.0269 240 LYS A CA  
2039  C C   . LYS A 240 ? 0.7173 0.5176 0.7895 0.0324  0.0178  -0.0117 240 LYS A C   
2040  O O   . LYS A 240 ? 0.7424 0.5397 0.8168 0.0406  0.0117  -0.0043 240 LYS A O   
2041  C CB  . LYS A 240 ? 0.6978 0.5285 0.7870 0.0403  0.0286  -0.0353 240 LYS A CB  
2042  C CG  . LYS A 240 ? 0.7225 0.5715 0.8261 0.0531  0.0265  -0.0358 240 LYS A CG  
2043  C CD  . LYS A 240 ? 0.6821 0.5231 0.7968 0.0691  0.0246  -0.0456 240 LYS A CD  
2044  C CE  . LYS A 240 ? 0.7098 0.5517 0.8328 0.0821  0.0159  -0.0385 240 LYS A CE  
2045  N NZ  . LYS A 240 ? 0.7419 0.5947 0.8833 0.0991  0.0154  -0.0498 240 LYS A NZ  
2046  N N   . TYR A 241 ? 0.7592 0.5645 0.8231 0.0177  0.0208  -0.0071 241 TYR A N   
2047  C CA  . TYR A 241 ? 0.7295 0.5356 0.7865 0.0105  0.0180  0.0061  241 TYR A CA  
2048  C C   . TYR A 241 ? 0.7392 0.5148 0.7860 0.0106  0.0118  0.0143  241 TYR A C   
2049  O O   . TYR A 241 ? 0.7656 0.5386 0.8091 0.0134  0.0070  0.0244  241 TYR A O   
2050  C CB  . TYR A 241 ? 0.7106 0.5281 0.7625 -0.0043 0.0226  0.0076  241 TYR A CB  
2051  C CG  . TYR A 241 ? 0.6969 0.5252 0.7452 -0.0114 0.0223  0.0185  241 TYR A CG  
2052  C CD1 . TYR A 241 ? 0.6568 0.4685 0.6950 -0.0184 0.0194  0.0279  241 TYR A CD1 
2053  C CD2 . TYR A 241 ? 0.6536 0.5078 0.7076 -0.0118 0.0257  0.0188  241 TYR A CD2 
2054  C CE1 . TYR A 241 ? 0.5651 0.3880 0.5998 -0.0254 0.0203  0.0366  241 TYR A CE1 
2055  C CE2 . TYR A 241 ? 0.6198 0.4835 0.6707 -0.0177 0.0261  0.0273  241 TYR A CE2 
2056  C CZ  . TYR A 241 ? 0.5326 0.3819 0.5743 -0.0244 0.0237  0.0358  241 TYR A CZ  
2057  O OH  . TYR A 241 ? 0.5791 0.4389 0.6175 -0.0308 0.0251  0.0432  241 TYR A OH  
2058  N N   . PHE A 242 ? 0.7530 0.5034 0.7929 0.0071  0.0118  0.0100  242 PHE A N   
2059  C CA  . PHE A 242 ? 0.8013 0.5175 0.8292 0.0065  0.0061  0.0177  242 PHE A CA  
2060  C C   . PHE A 242 ? 0.8432 0.5483 0.8756 0.0244  -0.0010 0.0200  242 PHE A C   
2061  O O   . PHE A 242 ? 0.8323 0.5185 0.8549 0.0255  -0.0075 0.0317  242 PHE A O   
2062  C CB  . PHE A 242 ? 0.8009 0.4911 0.8209 -0.0005 0.0078  0.0106  242 PHE A CB  
2063  C CG  . PHE A 242 ? 0.8222 0.4745 0.8265 -0.0057 0.0030  0.0195  242 PHE A CG  
2064  C CD1 . PHE A 242 ? 0.8032 0.4266 0.8049 0.0084  -0.0036 0.0213  242 PHE A CD1 
2065  C CD2 . PHE A 242 ? 0.8570 0.5026 0.8490 -0.0249 0.0049  0.0261  242 PHE A CD2 
2066  C CE1 . PHE A 242 ? 0.9490 0.5338 0.9335 0.0031  -0.0084 0.0308  242 PHE A CE1 
2067  C CE2 . PHE A 242 ? 0.8707 0.4803 0.8462 -0.0318 0.0012  0.0348  242 PHE A CE2 
2068  C CZ  . PHE A 242 ? 0.9181 0.4952 0.8885 -0.0180 -0.0056 0.0377  242 PHE A CZ  
2069  N N   . GLU A 243 ? 0.8013 0.5186 0.8483 0.0384  -0.0001 0.0089  243 GLU A N   
2070  C CA  . GLU A 243 ? 0.7085 0.4216 0.7636 0.0569  -0.0072 0.0100  243 GLU A CA  
2071  C C   . GLU A 243 ? 0.7435 0.4736 0.7990 0.0583  -0.0120 0.0217  243 GLU A C   
2072  O O   . GLU A 243 ? 0.8050 0.5177 0.8540 0.0651  -0.0207 0.0318  243 GLU A O   
2073  C CB  . GLU A 243 ? 0.7679 0.5001 0.8414 0.0700  -0.0035 -0.0054 243 GLU A CB  
2074  C CG  . GLU A 243 ? 0.9665 0.6894 1.0502 0.0909  -0.0110 -0.0076 243 GLU A CG  
2075  C CD  . GLU A 243 ? 1.0588 0.8168 1.1643 0.1030  -0.0082 -0.0187 243 GLU A CD  
2076  O OE1 . GLU A 243 ? 1.0404 0.8084 1.1542 0.1039  -0.0003 -0.0334 243 GLU A OE1 
2077  O OE2 . GLU A 243 ? 1.0834 0.8597 1.1971 0.1105  -0.0138 -0.0130 243 GLU A OE2 
2078  N N   . ILE A 244 ? 0.7160 0.4785 0.7771 0.0513  -0.0066 0.0209  244 ILE A N   
2079  C CA  . ILE A 244 ? 0.7279 0.5090 0.7904 0.0529  -0.0103 0.0296  244 ILE A CA  
2080  C C   . ILE A 244 ? 0.7798 0.5475 0.8245 0.0406  -0.0127 0.0437  244 ILE A C   
2081  O O   . ILE A 244 ? 0.7872 0.5512 0.8261 0.0444  -0.0198 0.0537  244 ILE A O   
2082  C CB  . ILE A 244 ? 0.7217 0.5390 0.7954 0.0495  -0.0033 0.0232  244 ILE A CB  
2083  C CG1 . ILE A 244 ? 0.7528 0.5820 0.8410 0.0570  0.0016  0.0083  244 ILE A CG1 
2084  C CG2 . ILE A 244 ? 0.8213 0.6574 0.8983 0.0533  -0.0077 0.0296  244 ILE A CG2 
2085  C CD1 . ILE A 244 ? 0.7662 0.6055 0.8694 0.0739  -0.0034 0.0035  244 ILE A CD1 
2086  N N   . PHE A 245 ? 0.7234 0.4862 0.7594 0.0253  -0.0066 0.0445  245 PHE A N   
2087  C CA  . PHE A 245 ? 0.7047 0.4631 0.7262 0.0116  -0.0063 0.0561  245 PHE A CA  
2088  C C   . PHE A 245 ? 0.8266 0.5511 0.8320 0.0024  -0.0080 0.0622  245 PHE A C   
2089  O O   . PHE A 245 ? 0.9382 0.6561 0.9300 -0.0085 -0.0084 0.0729  245 PHE A O   
2090  C CB  . PHE A 245 ? 0.7320 0.5169 0.7572 -0.0002 0.0021  0.0532  245 PHE A CB  
2091  C CG  . PHE A 245 ? 0.7036 0.5188 0.7411 0.0059  0.0043  0.0488  245 PHE A CG  
2092  C CD1 . PHE A 245 ? 0.6929 0.5205 0.7279 0.0061  0.0022  0.0558  245 PHE A CD1 
2093  C CD2 . PHE A 245 ? 0.7548 0.5854 0.8049 0.0105  0.0086  0.0374  245 PHE A CD2 
2094  C CE1 . PHE A 245 ? 0.8104 0.6641 0.8559 0.0105  0.0044  0.0512  245 PHE A CE1 
2095  C CE2 . PHE A 245 ? 0.7049 0.5614 0.7650 0.0146  0.0111  0.0336  245 PHE A CE2 
2096  C CZ  . PHE A 245 ? 0.7478 0.6154 0.8059 0.0145  0.0089  0.0403  245 PHE A CZ  
2097  N N   . GLY A 246 ? 0.7846 0.4870 0.7900 0.0055  -0.0083 0.0553  246 GLY A N   
2098  C CA  . GLY A 246 ? 0.8122 0.4782 0.8009 -0.0034 -0.0104 0.0611  246 GLY A CA  
2099  C C   . GLY A 246 ? 0.8567 0.5237 0.8390 -0.0233 -0.0033 0.0597  246 GLY A C   
2100  O O   . GLY A 246 ? 0.8513 0.4893 0.8185 -0.0341 -0.0042 0.0650  246 GLY A O   
2101  N N   . GLU A 247 ? 0.8199 0.5193 0.8130 -0.0286 0.0033  0.0530  247 GLU A N   
2102  C CA  . GLU A 247 ? 0.7946 0.5017 0.7848 -0.0462 0.0093  0.0509  247 GLU A CA  
2103  C C   . GLU A 247 ? 0.8436 0.5748 0.8473 -0.0438 0.0139  0.0383  247 GLU A C   
2104  O O   . GLU A 247 ? 0.8968 0.6439 0.9116 -0.0308 0.0138  0.0332  247 GLU A O   
2105  C CB  . GLU A 247 ? 0.8986 0.6240 0.8847 -0.0575 0.0120  0.0603  247 GLU A CB  
2106  C CG  . GLU A 247 ? 1.0272 0.7629 1.0117 -0.0759 0.0178  0.0589  247 GLU A CG  
2107  C CD  . GLU A 247 ? 1.1424 0.8489 1.1170 -0.0865 0.0173  0.0564  247 GLU A CD  
2108  O OE1 . GLU A 247 ? 1.1086 0.7914 1.0684 -0.0965 0.0161  0.0651  247 GLU A OE1 
2109  O OE2 . GLU A 247 ? 1.0404 0.7469 1.0206 -0.0858 0.0185  0.0455  247 GLU A OE2 
2110  N N   . HIS A 248 ? 0.8224 0.5563 0.8245 -0.0570 0.0177  0.0333  248 HIS A N   
2111  C CA  . HIS A 248 ? 0.7502 0.5064 0.7624 -0.0554 0.0214  0.0224  248 HIS A CA  
2112  C C   . HIS A 248 ? 0.6865 0.4770 0.7063 -0.0581 0.0245  0.0253  248 HIS A C   
2113  O O   . HIS A 248 ? 0.7547 0.5523 0.7714 -0.0672 0.0255  0.0332  248 HIS A O   
2114  C CB  . HIS A 248 ? 0.7347 0.4810 0.7419 -0.0678 0.0231  0.0150  248 HIS A CB  
2115  C CG  . HIS A 248 ? 0.8867 0.6091 0.8917 -0.0607 0.0220  0.0051  248 HIS A CG  
2116  N ND1 . HIS A 248 ? 0.9499 0.6529 0.9469 -0.0712 0.0227  -0.0018 248 HIS A ND1 
2117  C CD2 . HIS A 248 ? 0.9463 0.6618 0.9567 -0.0440 0.0206  -0.0002 248 HIS A CD2 
2118  C CE1 . HIS A 248 ? 1.0347 0.7182 1.0314 -0.0608 0.0221  -0.0111 248 HIS A CE1 
2119  N NE2 . HIS A 248 ? 1.0366 0.7284 1.0423 -0.0438 0.0209  -0.0103 248 HIS A NE2 
2120  N N   . PRO A 249 ? 0.6404 0.4518 0.6697 -0.0501 0.0265  0.0190  249 PRO A N   
2121  C CA  . PRO A 249 ? 0.6515 0.4918 0.6870 -0.0513 0.0293  0.0218  249 PRO A CA  
2122  C C   . PRO A 249 ? 0.7093 0.5629 0.7449 -0.0640 0.0314  0.0206  249 PRO A C   
2123  O O   . PRO A 249 ? 0.6821 0.5319 0.7160 -0.0692 0.0315  0.0136  249 PRO A O   
2124  C CB  . PRO A 249 ? 0.5724 0.4257 0.6157 -0.0404 0.0308  0.0146  249 PRO A CB  
2125  C CG  . PRO A 249 ? 0.7191 0.5569 0.7605 -0.0385 0.0305  0.0053  249 PRO A CG  
2126  C CD  . PRO A 249 ? 0.6553 0.4641 0.6893 -0.0396 0.0269  0.0088  249 PRO A CD  
2127  N N   . VAL A 250 ? 0.6600 0.5302 0.6978 -0.0690 0.0330  0.0271  250 VAL A N   
2128  C CA  . VAL A 250 ? 0.6664 0.5552 0.7076 -0.0790 0.0346  0.0260  250 VAL A CA  
2129  C C   . VAL A 250 ? 0.6491 0.5634 0.6985 -0.0729 0.0363  0.0247  250 VAL A C   
2130  O O   . VAL A 250 ? 0.5824 0.5134 0.6358 -0.0782 0.0364  0.0225  250 VAL A O   
2131  C CB  . VAL A 250 ? 0.6400 0.5310 0.6788 -0.0903 0.0360  0.0331  250 VAL A CB  
2132  C CG1 . VAL A 250 ? 0.5580 0.4221 0.5866 -0.0996 0.0345  0.0342  250 VAL A CG1 
2133  C CG2 . VAL A 250 ? 0.5435 0.4393 0.5823 -0.0845 0.0374  0.0403  250 VAL A CG2 
2134  N N   . TYR A 251 ? 0.6361 0.5535 0.6877 -0.0623 0.0371  0.0261  251 TYR A N   
2135  C CA  . TYR A 251 ? 0.6500 0.5873 0.7074 -0.0568 0.0389  0.0256  251 TYR A CA  
2136  C C   . TYR A 251 ? 0.6030 0.5371 0.6604 -0.0482 0.0391  0.0201  251 TYR A C   
2137  O O   . TYR A 251 ? 0.6908 0.6131 0.7472 -0.0423 0.0385  0.0193  251 TYR A O   
2138  C CB  . TYR A 251 ? 0.5859 0.5314 0.6453 -0.0541 0.0410  0.0317  251 TYR A CB  
2139  C CG  . TYR A 251 ? 0.6034 0.5515 0.6618 -0.0630 0.0420  0.0369  251 TYR A CG  
2140  C CD1 . TYR A 251 ? 0.6299 0.5887 0.6917 -0.0719 0.0424  0.0359  251 TYR A CD1 
2141  C CD2 . TYR A 251 ? 0.5665 0.5074 0.6202 -0.0634 0.0427  0.0427  251 TYR A CD2 
2142  C CE1 . TYR A 251 ? 0.6944 0.6579 0.7560 -0.0814 0.0444  0.0398  251 TYR A CE1 
2143  C CE2 . TYR A 251 ? 0.5896 0.5330 0.6407 -0.0731 0.0447  0.0473  251 TYR A CE2 
2144  C CZ  . TYR A 251 ? 0.6580 0.6134 0.7137 -0.0824 0.0461  0.0455  251 TYR A CZ  
2145  O OH  . TYR A 251 ? 0.7444 0.7054 0.7988 -0.0935 0.0490  0.0491  251 TYR A OH  
2146  N N   . MET A 252 ? 0.6024 0.5476 0.6606 -0.0475 0.0397  0.0163  252 MET A N   
2147  C CA  . MET A 252 ? 0.6483 0.5919 0.7054 -0.0412 0.0410  0.0107  252 MET A CA  
2148  C C   . MET A 252 ? 0.5869 0.5451 0.6445 -0.0386 0.0427  0.0116  252 MET A C   
2149  O O   . MET A 252 ? 0.5639 0.5323 0.6217 -0.0420 0.0415  0.0138  252 MET A O   
2150  C CB  . MET A 252 ? 0.6156 0.5503 0.6683 -0.0442 0.0402  0.0030  252 MET A CB  
2151  C CG  . MET A 252 ? 0.7746 0.6900 0.8264 -0.0418 0.0394  0.0001  252 MET A CG  
2152  S SD  . MET A 252 ? 0.7361 0.6383 0.7825 -0.0436 0.0397  -0.0113 252 MET A SD  
2153  C CE  . MET A 252 ? 0.7482 0.6688 0.7916 -0.0452 0.0419  -0.0152 252 MET A CE  
2154  N N   . TRP A 253 ? 0.6262 0.5850 0.6841 -0.0327 0.0453  0.0099  253 TRP A N   
2155  C CA  . TRP A 253 ? 0.5978 0.5659 0.6537 -0.0309 0.0474  0.0105  253 TRP A CA  
2156  C C   . TRP A 253 ? 0.5765 0.5435 0.6261 -0.0322 0.0484  0.0042  253 TRP A C   
2157  O O   . TRP A 253 ? 0.6013 0.5632 0.6512 -0.0301 0.0506  -0.0018 253 TRP A O   
2158  C CB  . TRP A 253 ? 0.5569 0.5265 0.6154 -0.0259 0.0502  0.0118  253 TRP A CB  
2159  C CG  . TRP A 253 ? 0.5911 0.5652 0.6454 -0.0249 0.0533  0.0106  253 TRP A CG  
2160  C CD1 . TRP A 253 ? 0.5547 0.5285 0.6071 -0.0240 0.0566  0.0051  253 TRP A CD1 
2161  C CD2 . TRP A 253 ? 0.5264 0.5049 0.5771 -0.0250 0.0536  0.0151  253 TRP A CD2 
2162  N NE1 . TRP A 253 ? 0.5989 0.5755 0.6450 -0.0252 0.0592  0.0065  253 TRP A NE1 
2163  C CE2 . TRP A 253 ? 0.5889 0.5668 0.6335 -0.0251 0.0570  0.0129  253 TRP A CE2 
2164  C CE3 . TRP A 253 ? 0.5131 0.4962 0.5657 -0.0247 0.0515  0.0205  253 TRP A CE3 
2165  C CZ2 . TRP A 253 ? 0.6662 0.6440 0.7043 -0.0248 0.0578  0.0169  253 TRP A CZ2 
2166  C CZ3 . TRP A 253 ? 0.5310 0.5160 0.5794 -0.0227 0.0521  0.0236  253 TRP A CZ3 
2167  C CH2 . TRP A 253 ? 0.5505 0.5309 0.5908 -0.0228 0.0548  0.0223  253 TRP A CH2 
2168  N N   . PRO A 254 ? 0.5385 0.5109 0.5823 -0.0354 0.0468  0.0049  254 PRO A N   
2169  C CA  . PRO A 254 ? 0.5079 0.4795 0.5428 -0.0377 0.0482  -0.0008 254 PRO A CA  
2170  C C   . PRO A 254 ? 0.5550 0.5273 0.5871 -0.0348 0.0533  -0.0022 254 PRO A C   
2171  O O   . PRO A 254 ? 0.6165 0.5919 0.6488 -0.0327 0.0542  0.0033  254 PRO A O   
2172  C CB  . PRO A 254 ? 0.5312 0.5099 0.5601 -0.0410 0.0440  0.0030  254 PRO A CB  
2173  C CG  . PRO A 254 ? 0.5581 0.5428 0.5941 -0.0380 0.0422  0.0107  254 PRO A CG  
2174  C CD  . PRO A 254 ? 0.5264 0.5072 0.5715 -0.0370 0.0434  0.0109  254 PRO A CD  
2175  N N   . PRO A 255 ? 0.4841 0.4541 0.5140 -0.0351 0.0571  -0.0102 255 PRO A N   
2176  C CA  . PRO A 255 ? 0.5588 0.5320 0.5871 -0.0340 0.0628  -0.0126 255 PRO A CA  
2177  C C   . PRO A 255 ? 0.5515 0.5266 0.5681 -0.0373 0.0636  -0.0076 255 PRO A C   
2178  O O   . PRO A 255 ? 0.5286 0.5031 0.5344 -0.0412 0.0614  -0.0071 255 PRO A O   
2179  C CB  . PRO A 255 ? 0.5484 0.5208 0.5756 -0.0348 0.0668  -0.0234 255 PRO A CB  
2180  C CG  . PRO A 255 ? 0.5735 0.5385 0.6062 -0.0333 0.0628  -0.0260 255 PRO A CG  
2181  C CD  . PRO A 255 ? 0.5759 0.5403 0.6051 -0.0368 0.0571  -0.0184 255 PRO A CD  
2182  N N   . GLN A 256 ? 0.5425 0.5185 0.5602 -0.0358 0.0662  -0.0036 256 GLN A N   
2183  C CA  . GLN A 256 ? 0.5912 0.5647 0.5974 -0.0380 0.0667  0.0025  256 GLN A CA  
2184  C C   . GLN A 256 ? 0.6296 0.6022 0.6327 -0.0365 0.0599  0.0099  256 GLN A C   
2185  O O   . GLN A 256 ? 0.6630 0.6325 0.6536 -0.0382 0.0581  0.0144  256 GLN A O   
2186  C CB  . GLN A 256 ? 0.5348 0.5073 0.5268 -0.0440 0.0713  -0.0015 256 GLN A CB  
2187  C CG  . GLN A 256 ? 0.6092 0.5870 0.6063 -0.0457 0.0785  -0.0114 256 GLN A CG  
2188  C CD  . GLN A 256 ? 0.6195 0.5990 0.6171 -0.0477 0.0844  -0.0112 256 GLN A CD  
2189  O OE1 . GLN A 256 ? 0.6396 0.6133 0.6320 -0.0481 0.0834  -0.0036 256 GLN A OE1 
2190  N NE2 . GLN A 256 ? 0.6570 0.6450 0.6617 -0.0489 0.0905  -0.0202 256 GLN A NE2 
2191  N N   . ALA A 257 ? 0.6022 0.5779 0.6164 -0.0335 0.0558  0.0114  257 ALA A N   
2192  C CA  . ALA A 257 ? 0.5352 0.5145 0.5509 -0.0319 0.0496  0.0173  257 ALA A CA  
2193  C C   . ALA A 257 ? 0.6546 0.6361 0.6605 -0.0357 0.0451  0.0168  257 ALA A C   
2194  O O   . ALA A 257 ? 0.5966 0.5830 0.6018 -0.0342 0.0393  0.0221  257 ALA A O   
2195  C CB  . ALA A 257 ? 0.4563 0.4343 0.4713 -0.0275 0.0493  0.0243  257 ALA A CB  
2196  N N   . SER A 258 ? 0.6405 0.6198 0.6394 -0.0405 0.0475  0.0099  258 SER A N   
2197  C CA  . SER A 258 ? 0.6312 0.6121 0.6176 -0.0454 0.0437  0.0084  258 SER A CA  
2198  C C   . SER A 258 ? 0.5446 0.5316 0.5376 -0.0474 0.0374  0.0073  258 SER A C   
2199  O O   . SER A 258 ? 0.5047 0.4898 0.5056 -0.0490 0.0388  0.0016  258 SER A O   
2200  C CB  . SER A 258 ? 0.6123 0.5894 0.5893 -0.0503 0.0495  -0.0003 258 SER A CB  
2201  O OG  . SER A 258 ? 0.7822 0.7577 0.7700 -0.0495 0.0530  -0.0083 258 SER A OG  
2202  N N   . VAL A 259 ? 0.6302 0.6246 0.6200 -0.0474 0.0302  0.0128  259 VAL A N   
2203  C CA  . VAL A 259 ? 0.4871 0.4910 0.4835 -0.0507 0.0238  0.0119  259 VAL A CA  
2204  C C   . VAL A 259 ? 0.6113 0.6204 0.5938 -0.0554 0.0173  0.0115  259 VAL A C   
2205  O O   . VAL A 259 ? 0.6217 0.6292 0.5914 -0.0535 0.0154  0.0166  259 VAL A O   
2206  C CB  . VAL A 259 ? 0.5057 0.5198 0.5168 -0.0456 0.0201  0.0185  259 VAL A CB  
2207  C CG1 . VAL A 259 ? 0.5298 0.5401 0.5538 -0.0435 0.0255  0.0177  259 VAL A CG1 
2208  C CG2 . VAL A 259 ? 0.4750 0.4909 0.4823 -0.0382 0.0174  0.0268  259 VAL A CG2 
2209  N N   . SER A 260 ? 0.6139 0.6282 0.5974 -0.0625 0.0138  0.0057  260 SER A N   
2210  C CA  . SER A 260 ? 0.5880 0.6112 0.5605 -0.0677 0.0057  0.0054  260 SER A CA  
2211  C C   . SER A 260 ? 0.6464 0.6810 0.6306 -0.0734 0.0005  0.0023  260 SER A C   
2212  O O   . SER A 260 ? 0.7083 0.7390 0.7044 -0.0750 0.0046  -0.0010 260 SER A O   
2213  C CB  . SER A 260 ? 0.5446 0.5592 0.4979 -0.0747 0.0087  -0.0023 260 SER A CB  
2214  O OG  . SER A 260 ? 0.6802 0.6905 0.6362 -0.0817 0.0114  -0.0129 260 SER A OG  
2215  N N   . ASN A 261 ? 0.5828 0.6320 0.5631 -0.0769 -0.0089 0.0038  261 ASN A N   
2216  C CA  . ASN A 261 ? 0.6735 0.7353 0.6636 -0.0851 -0.0139 -0.0007 261 ASN A CA  
2217  C C   . ASN A 261 ? 0.7091 0.7573 0.6942 -0.0951 -0.0086 -0.0119 261 ASN A C   
2218  O O   . ASN A 261 ? 0.7051 0.7554 0.7007 -0.1016 -0.0087 -0.0157 261 ASN A O   
2219  C CB  . ASN A 261 ? 0.6825 0.7630 0.6667 -0.0884 -0.0255 0.0011  261 ASN A CB  
2220  C CG  . ASN A 261 ? 0.6626 0.7561 0.6527 -0.0770 -0.0320 0.0122  261 ASN A CG  
2221  O OD1 . ASN A 261 ? 0.7083 0.8117 0.7174 -0.0710 -0.0317 0.0163  261 ASN A OD1 
2222  N ND2 . ASN A 261 ? 0.6848 0.7777 0.6579 -0.0740 -0.0379 0.0170  261 ASN A ND2 
2223  N N   . GLU A 262 ? 0.7669 0.8005 0.7359 -0.0964 -0.0037 -0.0175 262 GLU A N   
2224  C CA  . GLU A 262 ? 0.7719 0.7907 0.7358 -0.1039 0.0018  -0.0293 262 GLU A CA  
2225  C C   . GLU A 262 ? 0.6588 0.6626 0.6342 -0.0988 0.0102  -0.0303 262 GLU A C   
2226  O O   . GLU A 262 ? 0.6369 0.6316 0.6175 -0.1040 0.0119  -0.0362 262 GLU A O   
2227  C CB  . GLU A 262 ? 0.7701 0.7812 0.7134 -0.1067 0.0047  -0.0359 262 GLU A CB  
2228  C CG  . GLU A 262 ? 0.8448 0.8695 0.7731 -0.1114 -0.0043 -0.0334 262 GLU A CG  
2229  C CD  . GLU A 262 ? 1.0027 1.0277 0.9194 -0.1241 -0.0073 -0.0448 262 GLU A CD  
2230  O OE1 . GLU A 262 ? 1.1114 1.1359 1.0382 -0.1305 -0.0084 -0.0502 262 GLU A OE1 
2231  O OE2 . GLU A 262 ? 0.9985 1.0233 0.8945 -0.1288 -0.0083 -0.0485 262 GLU A OE2 
2232  N N   . ALA A 263 ? 0.5695 0.5697 0.5477 -0.0890 0.0150  -0.0247 263 ALA A N   
2233  C CA  . ALA A 263 ? 0.5945 0.5829 0.5838 -0.0834 0.0216  -0.0248 263 ALA A CA  
2234  C C   . ALA A 263 ? 0.5705 0.5632 0.5747 -0.0845 0.0191  -0.0201 263 ALA A C   
2235  O O   . ALA A 263 ? 0.5402 0.5205 0.5498 -0.0858 0.0222  -0.0232 263 ALA A O   
2236  C CB  . ALA A 263 ? 0.5964 0.5839 0.5864 -0.0740 0.0262  -0.0190 263 ALA A CB  
2237  N N   . LEU A 264 ? 0.6032 0.6132 0.6136 -0.0840 0.0134  -0.0127 264 LEU A N   
2238  C CA  . LEU A 264 ? 0.5839 0.6014 0.6087 -0.0860 0.0120  -0.0088 264 LEU A CA  
2239  C C   . LEU A 264 ? 0.5905 0.6046 0.6153 -0.0981 0.0102  -0.0155 264 LEU A C   
2240  O O   . LEU A 264 ? 0.6076 0.6157 0.6403 -0.1015 0.0125  -0.0148 264 LEU A O   
2241  C CB  . LEU A 264 ? 0.5798 0.6194 0.6121 -0.0824 0.0062  -0.0013 264 LEU A CB  
2242  C CG  . LEU A 264 ? 0.5702 0.6104 0.6038 -0.0704 0.0083  0.0061  264 LEU A CG  
2243  C CD1 . LEU A 264 ? 0.6886 0.7466 0.7227 -0.0664 0.0009  0.0116  264 LEU A CD1 
2244  C CD2 . LEU A 264 ? 0.5612 0.6003 0.6076 -0.0661 0.0131  0.0101  264 LEU A CD2 
2245  N N   . GLU A 265 ? 0.6978 0.7147 0.7124 -0.1057 0.0061  -0.0220 265 GLU A N   
2246  C CA  . GLU A 265 ? 0.6681 0.6776 0.6799 -0.1184 0.0051  -0.0301 265 GLU A CA  
2247  C C   . GLU A 265 ? 0.7009 0.6827 0.7087 -0.1178 0.0120  -0.0360 265 GLU A C   
2248  O O   . GLU A 265 ? 0.7048 0.6755 0.7168 -0.1241 0.0133  -0.0373 265 GLU A O   
2249  C CB  . GLU A 265 ? 0.7755 0.7923 0.7745 -0.1264 -0.0005 -0.0370 265 GLU A CB  
2250  C CG  . GLU A 265 ? 0.6755 0.7209 0.6792 -0.1285 -0.0096 -0.0319 265 GLU A CG  
2251  C CD  . GLU A 265 ? 0.8097 0.8620 0.7973 -0.1311 -0.0153 -0.0354 265 GLU A CD  
2252  O OE1 . GLU A 265 ? 0.8356 0.8709 0.8079 -0.1340 -0.0113 -0.0437 265 GLU A OE1 
2253  O OE2 . GLU A 265 ? 0.8220 0.8970 0.8117 -0.1299 -0.0239 -0.0300 265 GLU A OE2 
2254  N N   . LEU A 266 ? 0.6451 0.6156 0.6450 -0.1101 0.0165  -0.0394 266 LEU A N   
2255  C CA  . LEU A 266 ? 0.6177 0.5639 0.6158 -0.1070 0.0227  -0.0455 266 LEU A CA  
2256  C C   . LEU A 266 ? 0.5867 0.5253 0.5963 -0.1014 0.0250  -0.0381 266 LEU A C   
2257  O O   . LEU A 266 ? 0.6064 0.5259 0.6165 -0.1041 0.0266  -0.0408 266 LEU A O   
2258  C CB  . LEU A 266 ? 0.6802 0.6220 0.6709 -0.0988 0.0275  -0.0500 266 LEU A CB  
2259  C CG  . LEU A 266 ? 0.6073 0.5295 0.6008 -0.0909 0.0340  -0.0548 266 LEU A CG  
2260  C CD1 . LEU A 266 ? 0.6097 0.5117 0.5971 -0.0967 0.0353  -0.0664 266 LEU A CD1 
2261  C CD2 . LEU A 266 ? 0.6754 0.6016 0.6656 -0.0827 0.0391  -0.0572 266 LEU A CD2 
2262  N N   . TYR A 267 ? 0.5305 0.4824 0.5481 -0.0938 0.0252  -0.0287 267 TYR A N   
2263  C CA  . TYR A 267 ? 0.6221 0.5683 0.6489 -0.0893 0.0273  -0.0217 267 TYR A CA  
2264  C C   . TYR A 267 ? 0.6835 0.6293 0.7146 -0.0995 0.0250  -0.0193 267 TYR A C   
2265  O O   . TYR A 267 ? 0.6568 0.5885 0.6903 -0.0994 0.0270  -0.0162 267 TYR A O   
2266  C CB  . TYR A 267 ? 0.5811 0.5427 0.6145 -0.0807 0.0279  -0.0132 267 TYR A CB  
2267  C CG  . TYR A 267 ? 0.6335 0.5921 0.6635 -0.0712 0.0316  -0.0145 267 TYR A CG  
2268  C CD1 . TYR A 267 ? 0.7178 0.6604 0.7472 -0.0661 0.0356  -0.0190 267 TYR A CD1 
2269  C CD2 . TYR A 267 ? 0.7077 0.6795 0.7352 -0.0673 0.0310  -0.0112 267 TYR A CD2 
2270  C CE1 . TYR A 267 ? 0.6890 0.6321 0.7170 -0.0586 0.0395  -0.0211 267 TYR A CE1 
2271  C CE2 . TYR A 267 ? 0.6741 0.6429 0.6976 -0.0607 0.0352  -0.0126 267 TYR A CE2 
2272  C CZ  . TYR A 267 ? 0.6687 0.6249 0.6933 -0.0569 0.0398  -0.0179 267 TYR A CZ  
2273  O OH  . TYR A 267 ? 0.6887 0.6448 0.7112 -0.0514 0.0445  -0.0203 267 TYR A OH  
2274  N N   . TYR A 268 ? 0.5744 0.5359 0.6058 -0.1091 0.0207  -0.0206 268 TYR A N   
2275  C CA  . TYR A 268 ? 0.6181 0.5815 0.6537 -0.1214 0.0191  -0.0197 268 TYR A CA  
2276  C C   . TYR A 268 ? 0.6718 0.6092 0.6981 -0.1305 0.0200  -0.0274 268 TYR A C   
2277  O O   . TYR A 268 ? 0.7848 0.7091 0.8119 -0.1375 0.0214  -0.0251 268 TYR A O   
2278  C CB  . TYR A 268 ? 0.6447 0.6366 0.6854 -0.1284 0.0136  -0.0194 268 TYR A CB  
2279  C CG  . TYR A 268 ? 0.6820 0.6769 0.7234 -0.1453 0.0111  -0.0236 268 TYR A CG  
2280  C CD1 . TYR A 268 ? 0.7077 0.7022 0.7561 -0.1530 0.0135  -0.0195 268 TYR A CD1 
2281  C CD2 . TYR A 268 ? 0.6262 0.6251 0.6603 -0.1549 0.0066  -0.0320 268 TYR A CD2 
2282  C CE1 . TYR A 268 ? 0.7478 0.7453 0.7965 -0.1704 0.0118  -0.0235 268 TYR A CE1 
2283  C CE2 . TYR A 268 ? 0.6238 0.6261 0.6585 -0.1718 0.0044  -0.0366 268 TYR A CE2 
2284  C CZ  . TYR A 268 ? 0.7403 0.7419 0.7828 -0.1799 0.0072  -0.0323 268 TYR A CZ  
2285  O OH  . TYR A 268 ? 0.8859 0.8909 0.9287 -0.1987 0.0056  -0.0370 268 TYR A OH  
2286  N N   . GLU A 269 ? 0.6376 0.5653 0.6539 -0.1309 0.0198  -0.0368 269 GLU A N   
2287  C CA  . GLU A 269 ? 0.6632 0.5645 0.6702 -0.1393 0.0208  -0.0457 269 GLU A CA  
2288  C C   . GLU A 269 ? 0.6892 0.5614 0.6944 -0.1302 0.0251  -0.0455 269 GLU A C   
2289  O O   . GLU A 269 ? 0.7116 0.5574 0.7102 -0.1363 0.0258  -0.0503 269 GLU A O   
2290  C CB  . GLU A 269 ? 0.7047 0.6056 0.7008 -0.1429 0.0196  -0.0572 269 GLU A CB  
2291  C CG  . GLU A 269 ? 0.7630 0.6947 0.7599 -0.1475 0.0143  -0.0563 269 GLU A CG  
2292  C CD  . GLU A 269 ? 1.0538 0.9854 1.0386 -0.1594 0.0112  -0.0678 269 GLU A CD  
2293  O OE1 . GLU A 269 ? 1.1637 1.0902 1.1379 -0.1550 0.0129  -0.0749 269 GLU A OE1 
2294  O OE2 . GLU A 269 ? 1.0021 0.9400 0.9876 -0.1739 0.0073  -0.0701 269 GLU A OE2 
2295  N N   . LYS A 270 ? 0.6518 0.5274 0.6625 -0.1158 0.0274  -0.0400 270 LYS A N   
2296  C CA  . LYS A 270 ? 0.7220 0.5740 0.7330 -0.1060 0.0301  -0.0389 270 LYS A CA  
2297  C C   . LYS A 270 ? 0.6994 0.5503 0.7163 -0.1049 0.0298  -0.0271 270 LYS A C   
2298  O O   . LYS A 270 ? 0.7969 0.6303 0.8141 -0.0961 0.0308  -0.0241 270 LYS A O   
2299  C CB  . LYS A 270 ? 0.7726 0.6285 0.7854 -0.0916 0.0330  -0.0421 270 LYS A CB  
2300  C CG  . LYS A 270 ? 0.7495 0.6158 0.7560 -0.0933 0.0339  -0.0517 270 LYS A CG  
2301  C CD  . LYS A 270 ? 0.7670 0.6121 0.7662 -0.0913 0.0369  -0.0648 270 LYS A CD  
2302  C CE  . LYS A 270 ? 0.9094 0.7316 0.9017 -0.1023 0.0352  -0.0700 270 LYS A CE  
2303  N NZ  . LYS A 270 ? 1.0710 0.8797 1.0534 -0.1045 0.0377  -0.0853 270 LYS A NZ  
2304  N N   . GLY A 271 ? 0.5830 0.4533 0.6047 -0.1134 0.0284  -0.0206 271 GLY A N   
2305  C CA  . GLY A 271 ? 0.6292 0.4976 0.6542 -0.1158 0.0289  -0.0107 271 GLY A CA  
2306  C C   . GLY A 271 ? 0.6871 0.5752 0.7207 -0.1064 0.0301  -0.0024 271 GLY A C   
2307  O O   . GLY A 271 ? 0.7136 0.5981 0.7483 -0.1072 0.0312  0.0054  271 GLY A O   
2308  N N   . ILE A 272 ? 0.6668 0.5740 0.7047 -0.0985 0.0302  -0.0039 272 ILE A N   
2309  C CA  . ILE A 272 ? 0.6242 0.5479 0.6694 -0.0899 0.0316  0.0031  272 ILE A CA  
2310  C C   . ILE A 272 ? 0.7286 0.6753 0.7809 -0.0971 0.0310  0.0077  272 ILE A C   
2311  O O   . ILE A 272 ? 0.7399 0.7025 0.7943 -0.1025 0.0285  0.0045  272 ILE A O   
2312  C CB  . ILE A 272 ? 0.6458 0.5784 0.6914 -0.0797 0.0322  0.0000  272 ILE A CB  
2313  C CG1 . ILE A 272 ? 0.6490 0.5624 0.6903 -0.0722 0.0338  -0.0054 272 ILE A CG1 
2314  C CG2 . ILE A 272 ? 0.6022 0.5504 0.6543 -0.0720 0.0337  0.0067  272 ILE A CG2 
2315  C CD1 . ILE A 272 ? 0.6334 0.5270 0.6743 -0.0691 0.0341  -0.0019 272 ILE A CD1 
2316  N N   . ASN A 273 ? 0.7121 0.6616 0.7680 -0.0971 0.0332  0.0148  273 ASN A N   
2317  C CA  . ASN A 273 ? 0.6044 0.5775 0.6688 -0.1031 0.0338  0.0184  273 ASN A CA  
2318  C C   . ASN A 273 ? 0.6284 0.6236 0.7007 -0.0930 0.0339  0.0200  273 ASN A C   
2319  O O   . ASN A 273 ? 0.6731 0.6914 0.7538 -0.0957 0.0327  0.0201  273 ASN A O   
2320  C CB  . ASN A 273 ? 0.6505 0.6181 0.7141 -0.1080 0.0371  0.0247  273 ASN A CB  
2321  C CG  . ASN A 273 ? 0.6947 0.6408 0.7497 -0.1204 0.0369  0.0244  273 ASN A CG  
2322  O OD1 . ASN A 273 ? 0.7272 0.6629 0.7778 -0.1255 0.0344  0.0184  273 ASN A OD1 
2323  N ND2 . ASN A 273 ? 0.6980 0.6359 0.7489 -0.1262 0.0396  0.0307  273 ASN A ND2 
2324  N N   . MET A 274 ? 0.6508 0.6394 0.7208 -0.0814 0.0352  0.0212  274 MET A N   
2325  C CA  . MET A 274 ? 0.5920 0.5968 0.6675 -0.0723 0.0359  0.0233  274 MET A CA  
2326  C C   . MET A 274 ? 0.6325 0.6276 0.7026 -0.0628 0.0362  0.0215  274 MET A C   
2327  O O   . MET A 274 ? 0.6153 0.5934 0.6804 -0.0608 0.0373  0.0200  274 MET A O   
2328  C CB  . MET A 274 ? 0.6523 0.6644 0.7330 -0.0703 0.0396  0.0285  274 MET A CB  
2329  C CG  . MET A 274 ? 0.5916 0.6162 0.6771 -0.0602 0.0409  0.0302  274 MET A CG  
2330  S SD  . MET A 274 ? 0.8886 0.8979 0.9677 -0.0506 0.0436  0.0313  274 MET A SD  
2331  C CE  . MET A 274 ? 0.6404 0.6428 0.7178 -0.0545 0.0467  0.0353  274 MET A CE  
2332  N N   . LEU A 275 ? 0.6120 0.6185 0.6834 -0.0571 0.0353  0.0217  275 LEU A N   
2333  C CA  . LEU A 275 ? 0.5208 0.5209 0.5869 -0.0493 0.0366  0.0207  275 LEU A CA  
2334  C C   . LEU A 275 ? 0.6184 0.6299 0.6878 -0.0427 0.0373  0.0246  275 LEU A C   
2335  O O   . LEU A 275 ? 0.6239 0.6490 0.7008 -0.0428 0.0365  0.0274  275 LEU A O   
2336  C CB  . LEU A 275 ? 0.5996 0.5954 0.6581 -0.0513 0.0345  0.0153  275 LEU A CB  
2337  C CG  . LEU A 275 ? 0.6828 0.6916 0.7395 -0.0535 0.0299  0.0150  275 LEU A CG  
2338  C CD1 . LEU A 275 ? 0.6882 0.6891 0.7342 -0.0565 0.0289  0.0088  275 LEU A CD1 
2339  C CD2 . LEU A 275 ? 0.6587 0.6813 0.7230 -0.0603 0.0263  0.0160  275 LEU A CD2 
2340  N N   . ALA A 276 ? 0.5854 0.5913 0.6494 -0.0369 0.0390  0.0244  276 ALA A N   
2341  C CA  . ALA A 276 ? 0.5593 0.5706 0.6243 -0.0304 0.0400  0.0281  276 ALA A CA  
2342  C C   . ALA A 276 ? 0.5359 0.5420 0.5911 -0.0279 0.0395  0.0275  276 ALA A C   
2343  O O   . ALA A 276 ? 0.4530 0.4505 0.5017 -0.0299 0.0413  0.0236  276 ALA A O   
2344  C CB  . ALA A 276 ? 0.5090 0.5160 0.5764 -0.0268 0.0446  0.0297  276 ALA A CB  
2345  N N   . THR A 277 ? 0.4640 0.4750 0.5178 -0.0233 0.0374  0.0312  277 THR A N   
2346  C CA  . THR A 277 ? 0.4380 0.4418 0.4797 -0.0217 0.0370  0.0322  277 THR A CA  
2347  C C   . THR A 277 ? 0.4366 0.4383 0.4775 -0.0145 0.0377  0.0371  277 THR A C   
2348  O O   . THR A 277 ? 0.5693 0.5763 0.6198 -0.0105 0.0389  0.0387  277 THR A O   
2349  C CB  . THR A 277 ? 0.4888 0.4974 0.5239 -0.0250 0.0312  0.0316  277 THR A CB  
2350  O OG1 . THR A 277 ? 0.6459 0.6464 0.6667 -0.0239 0.0310  0.0337  277 THR A OG1 
2351  C CG2 . THR A 277 ? 0.5300 0.5539 0.5740 -0.0229 0.0249  0.0348  277 THR A CG2 
2352  N N   . ASP A 278 ? 0.4836 0.4763 0.5117 -0.0133 0.0373  0.0394  278 ASP A N   
2353  C CA  . ASP A 278 ? 0.5698 0.5538 0.5936 -0.0072 0.0390  0.0438  278 ASP A CA  
2354  C C   . ASP A 278 ? 0.6534 0.6431 0.6795 0.0003  0.0325  0.0491  278 ASP A C   
2355  O O   . ASP A 278 ? 0.5862 0.5857 0.6125 -0.0002 0.0257  0.0503  278 ASP A O   
2356  C CB  . ASP A 278 ? 0.5952 0.5644 0.6024 -0.0106 0.0422  0.0442  278 ASP A CB  
2357  C CG  . ASP A 278 ? 0.7248 0.6807 0.7264 -0.0063 0.0454  0.0479  278 ASP A CG  
2358  O OD1 . ASP A 278 ? 0.6826 0.6384 0.6929 -0.0039 0.0494  0.0462  278 ASP A OD1 
2359  O OD2 . ASP A 278 ? 0.7957 0.7397 0.7825 -0.0058 0.0439  0.0525  278 ASP A OD2 
2360  N N   . GLU A 279 ? 0.6406 0.6239 0.6684 0.0076  0.0344  0.0519  279 GLU A N   
2361  C CA  . GLU A 279 ? 0.6707 0.6584 0.7025 0.0174  0.0286  0.0567  279 GLU A CA  
2362  C C   . GLU A 279 ? 0.7121 0.6932 0.7291 0.0191  0.0213  0.0623  279 GLU A C   
2363  O O   . GLU A 279 ? 0.7482 0.7403 0.7703 0.0258  0.0132  0.0658  279 GLU A O   
2364  C CB  . GLU A 279 ? 0.6394 0.6159 0.6724 0.0248  0.0332  0.0576  279 GLU A CB  
2365  C CG  . GLU A 279 ? 0.8385 0.8281 0.8871 0.0355  0.0305  0.0582  279 GLU A CG  
2366  C CD  . GLU A 279 ? 0.9319 0.9072 0.9795 0.0434  0.0354  0.0582  279 GLU A CD  
2367  O OE1 . GLU A 279 ? 0.7819 0.7424 0.8215 0.0380  0.0424  0.0559  279 GLU A OE1 
2368  O OE2 . GLU A 279 ? 0.9032 0.8827 0.9587 0.0550  0.0320  0.0599  279 GLU A OE2 
2369  N N   . VAL A 280 ? 0.6427 0.6072 0.6413 0.0128  0.0239  0.0634  280 VAL A N   
2370  C CA  . VAL A 280 ? 0.7081 0.6643 0.6885 0.0127  0.0175  0.0693  280 VAL A CA  
2371  C C   . VAL A 280 ? 0.7707 0.7452 0.7543 0.0100  0.0095  0.0685  280 VAL A C   
2372  O O   . VAL A 280 ? 0.6722 0.6505 0.6510 0.0154  0.0000  0.0742  280 VAL A O   
2373  C CB  . VAL A 280 ? 0.7380 0.6763 0.6986 0.0033  0.0238  0.0688  280 VAL A CB  
2374  C CG1 . VAL A 280 ? 0.6608 0.5917 0.6002 0.0008  0.0175  0.0746  280 VAL A CG1 
2375  C CG2 . VAL A 280 ? 0.7516 0.6711 0.7073 0.0050  0.0307  0.0702  280 VAL A CG2 
2376  N N   . ILE A 281 ? 0.7471 0.7327 0.7382 0.0017  0.0126  0.0612  281 ILE A N   
2377  C CA  . ILE A 281 ? 0.7076 0.7096 0.7016 -0.0027 0.0058  0.0589  281 ILE A CA  
2378  C C   . ILE A 281 ? 0.6959 0.7174 0.7074 0.0050  -0.0016 0.0610  281 ILE A C   
2379  O O   . ILE A 281 ? 0.6500 0.6835 0.6601 0.0058  -0.0111 0.0633  281 ILE A O   
2380  C CB  . ILE A 281 ? 0.6983 0.7047 0.6978 -0.0124 0.0114  0.0503  281 ILE A CB  
2381  C CG1 . ILE A 281 ? 0.6914 0.6814 0.6783 -0.0179 0.0198  0.0473  281 ILE A CG1 
2382  C CG2 . ILE A 281 ? 0.6344 0.6533 0.6325 -0.0191 0.0051  0.0470  281 ILE A CG2 
2383  C CD1 . ILE A 281 ? 0.6246 0.6063 0.5898 -0.0231 0.0183  0.0485  281 ILE A CD1 
2384  N N   . LEU A 282 ? 0.6950 0.7215 0.7231 0.0104  0.0027  0.0598  282 LEU A N   
2385  C CA  . LEU A 282 ? 0.7054 0.7523 0.7517 0.0183  -0.0029 0.0609  282 LEU A CA  
2386  C C   . LEU A 282 ? 0.6890 0.7339 0.7293 0.0295  -0.0120 0.0685  282 LEU A C   
2387  O O   . LEU A 282 ? 0.7330 0.7969 0.7802 0.0328  -0.0217 0.0701  282 LEU A O   
2388  C CB  . LEU A 282 ? 0.6386 0.6882 0.7004 0.0226  0.0046  0.0583  282 LEU A CB  
2389  C CG  . LEU A 282 ? 0.6326 0.7066 0.7152 0.0302  0.0006  0.0579  282 LEU A CG  
2390  C CD1 . LEU A 282 ? 0.6574 0.7546 0.7505 0.0209  -0.0033 0.0538  282 LEU A CD1 
2391  C CD2 . LEU A 282 ? 0.6100 0.6841 0.7045 0.0348  0.0091  0.0552  282 LEU A CD2 
2392  N N   . LYS A 283 ? 0.6376 0.6589 0.6640 0.0352  -0.0094 0.0734  283 LYS A N   
2393  C CA  . LYS A 283 ? 0.6901 0.7043 0.7088 0.0470  -0.0181 0.0817  283 LYS A CA  
2394  C C   . LYS A 283 ? 0.5958 0.6097 0.5968 0.0430  -0.0279 0.0865  283 LYS A C   
2395  O O   . LYS A 283 ? 0.7101 0.7299 0.7102 0.0526  -0.0391 0.0929  283 LYS A O   
2396  C CB  . LYS A 283 ? 0.7009 0.6854 0.7062 0.0519  -0.0121 0.0856  283 LYS A CB  
2397  C CG  . LYS A 283 ? 0.7682 0.7526 0.7897 0.0574  -0.0035 0.0810  283 LYS A CG  
2398  C CD  . LYS A 283 ? 0.7763 0.7878 0.8236 0.0674  -0.0076 0.0785  283 LYS A CD  
2399  C CE  . LYS A 283 ? 0.7714 0.7958 0.8362 0.0626  0.0022  0.0702  283 LYS A CE  
2400  N NZ  . LYS A 283 ? 0.6772 0.6860 0.7430 0.0687  0.0105  0.0685  283 LYS A NZ  
2401  N N   . ASN A 284 ? 0.6641 0.6724 0.6510 0.0293  -0.0241 0.0831  284 ASN A N   
2402  C CA  . ASN A 284 ? 0.6739 0.6839 0.6432 0.0239  -0.0329 0.0863  284 ASN A CA  
2403  C C   . ASN A 284 ? 0.7612 0.8009 0.7454 0.0212  -0.0409 0.0820  284 ASN A C   
2404  O O   . ASN A 284 ? 0.8516 0.9000 0.8276 0.0222  -0.0524 0.0862  284 ASN A O   
2405  C CB  . ASN A 284 ? 0.7888 0.7837 0.7381 0.0101  -0.0251 0.0826  284 ASN A CB  
2406  C CG  . ASN A 284 ? 0.8056 0.7733 0.7403 0.0099  -0.0164 0.0857  284 ASN A CG  
2407  O OD1 . ASN A 284 ? 0.8758 0.8359 0.8063 0.0006  -0.0061 0.0798  284 ASN A OD1 
2408  N ND2 . ASN A 284 ? 0.8021 0.7550 0.7290 0.0202  -0.0205 0.0947  284 ASN A ND2 
2409  N N   . SER A 285 ? 0.7416 0.7969 0.7468 0.0169  -0.0352 0.0740  285 SER A N   
2410  C CA  . SER A 285 ? 0.6760 0.7567 0.6928 0.0098  -0.0407 0.0684  285 SER A CA  
2411  C C   . SER A 285 ? 0.7256 0.8333 0.7653 0.0192  -0.0488 0.0697  285 SER A C   
2412  O O   . SER A 285 ? 0.7655 0.8943 0.8089 0.0168  -0.0591 0.0691  285 SER A O   
2413  C CB  . SER A 285 ? 0.6283 0.7100 0.6535 -0.0015 -0.0306 0.0592  285 SER A CB  
2414  O OG  . SER A 285 ? 0.6741 0.7332 0.6812 -0.0083 -0.0227 0.0573  285 SER A OG  
2415  N N   . VAL A 286 ? 0.6532 0.7625 0.7090 0.0297  -0.0444 0.0706  286 VAL A N   
2416  C CA  . VAL A 286 ? 0.6748 0.8134 0.7559 0.0382  -0.0501 0.0697  286 VAL A CA  
2417  C C   . VAL A 286 ? 0.7558 0.8876 0.8384 0.0568  -0.0547 0.0771  286 VAL A C   
2418  O O   . VAL A 286 ? 0.7775 0.8813 0.8475 0.0617  -0.0485 0.0807  286 VAL A O   
2419  C CB  . VAL A 286 ? 0.6625 0.8142 0.7649 0.0331  -0.0399 0.0621  286 VAL A CB  
2420  C CG1 . VAL A 286 ? 0.7883 0.9638 0.9157 0.0456  -0.0418 0.0616  286 VAL A CG1 
2421  C CG2 . VAL A 286 ? 0.5955 0.7614 0.7013 0.0167  -0.0395 0.0553  286 VAL A CG2 
2422  N N   . GLU A 287 ? 0.7672 0.9250 0.8659 0.0672  -0.0657 0.0790  287 GLU A N   
2423  C CA  . GLU A 287 ? 0.8374 0.9903 0.9372 0.0869  -0.0736 0.0866  287 GLU A CA  
2424  C C   . GLU A 287 ? 0.9532 1.0875 1.0581 0.0974  -0.0632 0.0864  287 GLU A C   
2425  O O   . GLU A 287 ? 1.1324 1.2324 1.2160 0.1005  -0.0601 0.0920  287 GLU A O   
2426  C CB  . GLU A 287 ? 0.9623 1.1545 1.0871 0.0963  -0.0856 0.0857  287 GLU A CB  
2427  C CG  . GLU A 287 ? 1.0847 1.2727 1.2048 0.1158  -0.0995 0.0955  287 GLU A CG  
2428  C CD  . GLU A 287 ? 1.1142 1.3419 1.2667 0.1304  -0.1085 0.0931  287 GLU A CD  
2429  O OE1 . GLU A 287 ? 1.0727 1.3366 1.2479 0.1213  -0.1073 0.0845  287 GLU A OE1 
2430  O OE2 . GLU A 287 ? 1.0192 1.2420 1.1747 0.1510  -0.1166 0.0997  287 GLU A OE2 
2431  N N   . ARG A 288 ? 0.8321 0.9886 0.9641 0.1022  -0.0574 0.0796  288 ARG A N   
2432  C CA  . ARG A 288 ? 0.8239 0.9648 0.9613 0.1114  -0.0469 0.0776  288 ARG A CA  
2433  C C   . ARG A 288 ? 0.8308 0.9847 0.9826 0.0996  -0.0338 0.0681  288 ARG A C   
2434  O O   . ARG A 288 ? 0.7866 0.9646 0.9624 0.1051  -0.0302 0.0624  288 ARG A O   
2435  C CB  . ARG A 288 ? 0.8625 1.0153 1.0177 0.1333  -0.0532 0.0792  288 ARG A CB  
2436  C CG  . ARG A 288 ? 1.0554 1.2217 1.2108 0.1437  -0.0709 0.0864  288 ARG A CG  
2437  C CD  . ARG A 288 ? 1.0098 1.2015 1.1926 0.1651  -0.0774 0.0851  288 ARG A CD  
2438  N NE  . ARG A 288 ? 1.1116 1.3406 1.3258 0.1618  -0.0693 0.0738  288 ARG A NE  
2439  C CZ  . ARG A 288 ? 1.0644 1.3316 1.2954 0.1507  -0.0727 0.0686  288 ARG A CZ  
2440  N NH1 . ARG A 288 ? 1.1040 1.3782 1.3241 0.1417  -0.0840 0.0727  288 ARG A NH1 
2441  N NH2 . ARG A 288 ? 1.0825 1.3813 1.3407 0.1475  -0.0641 0.0586  288 ARG A NH2 
2442  N N   . ALA A 289 ? 0.7354 0.8730 0.8717 0.0835  -0.0266 0.0666  289 ALA A N   
2443  C CA  . ALA A 289 ? 0.6662 0.8114 0.8118 0.0717  -0.0153 0.0591  289 ALA A CA  
2444  C C   . ALA A 289 ? 0.6689 0.7921 0.8102 0.0750  -0.0038 0.0575  289 ALA A C   
2445  O O   . ALA A 289 ? 0.6893 0.7858 0.8159 0.0825  -0.0035 0.0618  289 ALA A O   
2446  C CB  . ALA A 289 ? 0.6069 0.7459 0.7393 0.0539  -0.0139 0.0577  289 ALA A CB  
2447  N N   . SER A 290 ? 0.6326 0.7669 0.7855 0.0681  0.0055  0.0511  290 SER A N   
2448  C CA  . SER A 290 ? 0.6197 0.7350 0.7668 0.0670  0.0166  0.0486  290 SER A CA  
2449  C C   . SER A 290 ? 0.6336 0.7401 0.7709 0.0506  0.0224  0.0466  290 SER A C   
2450  O O   . SER A 290 ? 0.5018 0.6247 0.6454 0.0402  0.0214  0.0444  290 SER A O   
2451  C CB  . SER A 290 ? 0.6520 0.7861 0.8190 0.0730  0.0234  0.0426  290 SER A CB  
2452  O OG  . SER A 290 ? 0.6491 0.7710 0.8105 0.0658  0.0344  0.0390  290 SER A OG  
2453  N N   . PRO A 291 ? 0.6695 0.7501 0.7915 0.0481  0.0283  0.0472  291 PRO A N   
2454  C CA  . PRO A 291 ? 0.6153 0.6878 0.7295 0.0347  0.0337  0.0451  291 PRO A CA  
2455  C C   . PRO A 291 ? 0.6426 0.7245 0.7663 0.0297  0.0417  0.0404  291 PRO A C   
2456  O O   . PRO A 291 ? 0.6813 0.7531 0.7974 0.0208  0.0461  0.0393  291 PRO A O   
2457  C CB  . PRO A 291 ? 0.6530 0.6972 0.7493 0.0357  0.0364  0.0473  291 PRO A CB  
2458  C CG  . PRO A 291 ? 0.6328 0.6707 0.7316 0.0481  0.0382  0.0477  291 PRO A CG  
2459  C CD  . PRO A 291 ? 0.6827 0.7404 0.7950 0.0577  0.0308  0.0492  291 PRO A CD  
2460  N N   . TYR A 292 ? 0.5814 0.6830 0.7211 0.0354  0.0437  0.0377  292 TYR A N   
2461  C CA  . TYR A 292 ? 0.6137 0.7245 0.7608 0.0308  0.0523  0.0332  292 TYR A CA  
2462  C C   . TYR A 292 ? 0.5999 0.7370 0.7607 0.0223  0.0519  0.0310  292 TYR A C   
2463  O O   . TYR A 292 ? 0.5506 0.7054 0.7234 0.0218  0.0577  0.0271  292 TYR A O   
2464  C CB  . TYR A 292 ? 0.5807 0.6929 0.7344 0.0426  0.0573  0.0300  292 TYR A CB  
2465  C CG  . TYR A 292 ? 0.6077 0.6921 0.7472 0.0504  0.0573  0.0322  292 TYR A CG  
2466  C CD1 . TYR A 292 ? 0.6271 0.6891 0.7498 0.0428  0.0598  0.0336  292 TYR A CD1 
2467  C CD2 . TYR A 292 ? 0.5859 0.6662 0.7285 0.0651  0.0545  0.0330  292 TYR A CD2 
2468  C CE1 . TYR A 292 ? 0.6212 0.6586 0.7305 0.0475  0.0603  0.0352  292 TYR A CE1 
2469  C CE2 . TYR A 292 ? 0.6806 0.7319 0.8077 0.0705  0.0547  0.0354  292 TYR A CE2 
2470  C CZ  . TYR A 292 ? 0.6289 0.6594 0.7392 0.0606  0.0580  0.0364  292 TYR A CZ  
2471  O OH  . TYR A 292 ? 0.5564 0.5593 0.6512 0.0634  0.0590  0.0383  292 TYR A OH  
2472  N N   . LEU A 293 ? 0.6313 0.7707 0.7894 0.0145  0.0456  0.0330  293 LEU A N   
2473  C CA  . LEU A 293 ? 0.5632 0.7264 0.7333 0.0052  0.0438  0.0311  293 LEU A CA  
2474  C C   . LEU A 293 ? 0.4996 0.6504 0.6581 -0.0080 0.0419  0.0323  293 LEU A C   
2475  O O   . LEU A 293 ? 0.5755 0.7067 0.7205 -0.0073 0.0383  0.0346  293 LEU A O   
2476  C CB  . LEU A 293 ? 0.5112 0.6966 0.6943 0.0121  0.0352  0.0311  293 LEU A CB  
2477  C CG  . LEU A 293 ? 0.4944 0.7043 0.6972 0.0241  0.0360  0.0283  293 LEU A CG  
2478  C CD1 . LEU A 293 ? 0.6165 0.8089 0.8135 0.0404  0.0352  0.0305  293 LEU A CD1 
2479  C CD2 . LEU A 293 ? 0.5368 0.7767 0.7557 0.0252  0.0272  0.0274  293 LEU A CD2 
2480  N N   . ARG A 294 ? 0.3980 0.5597 0.5615 -0.0204 0.0446  0.0303  294 ARG A N   
2481  C CA  . ARG A 294 ? 0.4430 0.5956 0.5980 -0.0326 0.0413  0.0307  294 ARG A CA  
2482  C C   . ARG A 294 ? 0.5336 0.7009 0.6941 -0.0332 0.0325  0.0299  294 ARG A C   
2483  O O   . ARG A 294 ? 0.4451 0.6393 0.6215 -0.0306 0.0300  0.0282  294 ARG A O   
2484  C CB  . ARG A 294 ? 0.4034 0.5607 0.5604 -0.0465 0.0467  0.0294  294 ARG A CB  
2485  C CG  . ARG A 294 ? 0.4216 0.5662 0.5693 -0.0589 0.0435  0.0293  294 ARG A CG  
2486  C CD  . ARG A 294 ? 0.5418 0.6940 0.6927 -0.0740 0.0476  0.0283  294 ARG A CD  
2487  N NE  . ARG A 294 ? 0.5677 0.7089 0.7123 -0.0763 0.0551  0.0306  294 ARG A NE  
2488  C CZ  . ARG A 294 ? 0.6355 0.7941 0.7887 -0.0769 0.0616  0.0297  294 ARG A CZ  
2489  N NH1 . ARG A 294 ? 0.6553 0.8441 0.8261 -0.0741 0.0618  0.0263  294 ARG A NH1 
2490  N NH2 . ARG A 294 ? 0.5923 0.7388 0.7364 -0.0801 0.0680  0.0321  294 ARG A NH2 
2491  N N   . TYR A 295 ? 0.5148 0.6660 0.6625 -0.0366 0.0277  0.0306  295 TYR A N   
2492  C CA  . TYR A 295 ? 0.4375 0.6004 0.5867 -0.0384 0.0188  0.0296  295 TYR A CA  
2493  C C   . TYR A 295 ? 0.4286 0.5860 0.5718 -0.0539 0.0178  0.0265  295 TYR A C   
2494  O O   . TYR A 295 ? 0.4972 0.6305 0.6276 -0.0584 0.0211  0.0264  295 TYR A O   
2495  C CB  . TYR A 295 ? 0.4654 0.6142 0.6024 -0.0288 0.0136  0.0325  295 TYR A CB  
2496  C CG  . TYR A 295 ? 0.4632 0.6183 0.6060 -0.0134 0.0119  0.0358  295 TYR A CG  
2497  C CD1 . TYR A 295 ? 0.4883 0.6277 0.6270 -0.0054 0.0183  0.0376  295 TYR A CD1 
2498  C CD2 . TYR A 295 ? 0.5111 0.6871 0.6632 -0.0067 0.0034  0.0369  295 TYR A CD2 
2499  C CE1 . TYR A 295 ? 0.5328 0.6742 0.6755 0.0087  0.0170  0.0401  295 TYR A CE1 
2500  C CE2 . TYR A 295 ? 0.5478 0.7266 0.7047 0.0089  0.0013  0.0401  295 TYR A CE2 
2501  C CZ  . TYR A 295 ? 0.4723 0.6322 0.6240 0.0165  0.0085  0.0416  295 TYR A CZ  
2502  O OH  . TYR A 295 ? 0.4379 0.5969 0.5932 0.0320  0.0068  0.0443  295 TYR A OH  
2503  N N   . TYR A 296 ? 0.5293 0.7094 0.6824 -0.0618 0.0130  0.0236  296 TYR A N   
2504  C CA  . TYR A 296 ? 0.5251 0.6997 0.6714 -0.0767 0.0105  0.0199  296 TYR A CA  
2505  C C   . TYR A 296 ? 0.5622 0.7358 0.6997 -0.0745 0.0016  0.0190  296 TYR A C   
2506  O O   . TYR A 296 ? 0.4783 0.6730 0.6235 -0.0675 -0.0055 0.0201  296 TYR A O   
2507  C CB  . TYR A 296 ? 0.5438 0.7441 0.7047 -0.0895 0.0106  0.0164  296 TYR A CB  
2508  C CG  . TYR A 296 ? 0.5342 0.7325 0.6991 -0.0976 0.0199  0.0167  296 TYR A CG  
2509  C CD1 . TYR A 296 ? 0.5862 0.7539 0.7372 -0.0989 0.0262  0.0191  296 TYR A CD1 
2510  C CD2 . TYR A 296 ? 0.5399 0.7680 0.7220 -0.1046 0.0223  0.0145  296 TYR A CD2 
2511  C CE1 . TYR A 296 ? 0.4600 0.6250 0.6120 -0.1069 0.0340  0.0203  296 TYR A CE1 
2512  C CE2 . TYR A 296 ? 0.6351 0.8616 0.8187 -0.1136 0.0313  0.0150  296 TYR A CE2 
2513  C CZ  . TYR A 296 ? 0.5814 0.7752 0.7487 -0.1149 0.0369  0.0184  296 TYR A CZ  
2514  O OH  . TYR A 296 ? 0.5684 0.7604 0.7350 -0.1244 0.0451  0.0199  296 TYR A OH  
2515  N N   . PHE A 297 ? 0.5910 0.7401 0.7117 -0.0798 0.0019  0.0169  297 PHE A N   
2516  C CA  . PHE A 297 ? 0.5238 0.6711 0.6335 -0.0805 -0.0057 0.0149  297 PHE A CA  
2517  C C   . PHE A 297 ? 0.5183 0.6757 0.6293 -0.0963 -0.0096 0.0088  297 PHE A C   
2518  O O   . PHE A 297 ? 0.5781 0.7172 0.6814 -0.1071 -0.0056 0.0046  297 PHE A O   
2519  C CB  . PHE A 297 ? 0.6460 0.7637 0.7373 -0.0775 -0.0024 0.0146  297 PHE A CB  
2520  C CG  . PHE A 297 ? 0.6775 0.7934 0.7552 -0.0777 -0.0091 0.0128  297 PHE A CG  
2521  C CD1 . PHE A 297 ? 0.6358 0.7583 0.7103 -0.0668 -0.0142 0.0180  297 PHE A CD1 
2522  C CD2 . PHE A 297 ? 0.6115 0.7185 0.6785 -0.0891 -0.0104 0.0059  297 PHE A CD2 
2523  C CE1 . PHE A 297 ? 0.5842 0.7049 0.6438 -0.0680 -0.0206 0.0172  297 PHE A CE1 
2524  C CE2 . PHE A 297 ? 0.5612 0.6677 0.6142 -0.0903 -0.0162 0.0038  297 PHE A CE2 
2525  C CZ  . PHE A 297 ? 0.6426 0.7563 0.6912 -0.0801 -0.0214 0.0098  297 PHE A CZ  
2526  N N   . ARG A 298 ? 0.5934 0.7801 0.7146 -0.0975 -0.0178 0.0081  298 ARG A N   
2527  C CA  . ARG A 298 ? 0.6079 0.8087 0.7309 -0.1133 -0.0231 0.0017  298 ARG A CA  
2528  C C   . ARG A 298 ? 0.6965 0.8928 0.8248 -0.1281 -0.0160 -0.0020 298 ARG A C   
2529  O O   . ARG A 298 ? 0.7687 0.9579 0.8899 -0.1434 -0.0169 -0.0081 298 ARG A O   
2530  C CB  . ARG A 298 ? 0.5577 0.7416 0.6604 -0.1183 -0.0275 -0.0026 298 ARG A CB  
2531  C CG  . ARG A 298 ? 0.5485 0.7272 0.6401 -0.1041 -0.0319 0.0023  298 ARG A CG  
2532  C CD  . ARG A 298 ? 0.5127 0.6974 0.5913 -0.1093 -0.0414 -0.0012 298 ARG A CD  
2533  N NE  . ARG A 298 ? 0.5451 0.7011 0.6023 -0.1151 -0.0375 -0.0065 298 ARG A NE  
2534  C CZ  . ARG A 298 ? 0.5844 0.7281 0.6239 -0.1090 -0.0390 -0.0049 298 ARG A CZ  
2535  N NH1 . ARG A 298 ? 0.5295 0.6828 0.5679 -0.0968 -0.0448 0.0031  298 ARG A NH1 
2536  N NH2 . ARG A 298 ? 0.6477 0.7682 0.6697 -0.1152 -0.0344 -0.0115 298 ARG A NH2 
2537  N N   . GLU A 299 ? 0.6947 0.8927 0.8334 -0.1240 -0.0085 0.0019  299 GLU A N   
2538  C CA  . GLU A 299 ? 0.7171 0.9099 0.8595 -0.1372 -0.0010 0.0005  299 GLU A CA  
2539  C C   . GLU A 299 ? 0.7520 0.9052 0.8759 -0.1429 0.0043  -0.0005 299 GLU A C   
2540  O O   . GLU A 299 ? 0.8146 0.9559 0.9375 -0.1521 0.0106  0.0001  299 GLU A O   
2541  C CB  . GLU A 299 ? 0.6623 0.8811 0.8154 -0.1543 -0.0045 -0.0051 299 GLU A CB  
2542  C CG  . GLU A 299 ? 0.8164 1.0787 0.9915 -0.1482 -0.0098 -0.0047 299 GLU A CG  
2543  C CD  . GLU A 299 ? 0.9238 1.2162 1.1130 -0.1663 -0.0116 -0.0105 299 GLU A CD  
2544  O OE1 . GLU A 299 ? 1.0285 1.3049 1.2082 -0.1848 -0.0088 -0.0147 299 GLU A OE1 
2545  O OE2 . GLU A 299 ? 0.9505 1.2826 1.1608 -0.1619 -0.0159 -0.0112 299 GLU A OE2 
2546  N N   . LEU A 300 ? 0.6849 0.8174 0.7940 -0.1372 0.0017  -0.0020 300 LEU A N   
2547  C CA  . LEU A 300 ? 0.6776 0.7745 0.7711 -0.1418 0.0060  -0.0045 300 LEU A CA  
2548  C C   . LEU A 300 ? 0.7123 0.7899 0.8031 -0.1309 0.0128  0.0011  300 LEU A C   
2549  O O   . LEU A 300 ? 0.7013 0.7581 0.7872 -0.1364 0.0177  0.0019  300 LEU A O   
2550  C CB  . LEU A 300 ? 0.7216 0.8058 0.8008 -0.1405 0.0018  -0.0099 300 LEU A CB  
2551  C CG  . LEU A 300 ? 0.7596 0.8658 0.8394 -0.1486 -0.0067 -0.0150 300 LEU A CG  
2552  C CD1 . LEU A 300 ? 0.6295 0.7309 0.6964 -0.1407 -0.0111 -0.0168 300 LEU A CD1 
2553  C CD2 . LEU A 300 ? 0.7557 0.8537 0.8308 -0.1676 -0.0068 -0.0227 300 LEU A CD2 
2554  N N   . ILE A 301 ? 0.7239 0.8073 0.8170 -0.1158 0.0126  0.0054  301 ILE A N   
2555  C CA  . ILE A 301 ? 0.6545 0.7195 0.7435 -0.1055 0.0181  0.0096  301 ILE A CA  
2556  C C   . ILE A 301 ? 0.5976 0.6804 0.6972 -0.0945 0.0195  0.0150  301 ILE A C   
2557  O O   . ILE A 301 ? 0.5683 0.6747 0.6768 -0.0911 0.0152  0.0156  301 ILE A O   
2558  C CB  . ILE A 301 ? 0.6920 0.7372 0.7680 -0.0985 0.0177  0.0071  301 ILE A CB  
2559  C CG1 . ILE A 301 ? 0.7419 0.7635 0.8127 -0.0931 0.0233  0.0090  301 ILE A CG1 
2560  C CG2 . ILE A 301 ? 0.6766 0.7341 0.7527 -0.0877 0.0146  0.0094  301 ILE A CG2 
2561  C CD1 . ILE A 301 ? 0.7783 0.7829 0.8386 -0.0870 0.0239  0.0052  301 ILE A CD1 
2562  N N   . SER A 302 ? 0.5460 0.6169 0.6445 -0.0887 0.0252  0.0188  302 SER A N   
2563  C CA  . SER A 302 ? 0.5276 0.6108 0.6342 -0.0783 0.0277  0.0230  302 SER A CA  
2564  C C   . SER A 302 ? 0.5101 0.5806 0.6090 -0.0662 0.0279  0.0246  302 SER A C   
2565  O O   . SER A 302 ? 0.5525 0.6020 0.6419 -0.0653 0.0302  0.0239  302 SER A O   
2566  C CB  . SER A 302 ? 0.5142 0.5946 0.6237 -0.0815 0.0341  0.0258  302 SER A CB  
2567  O OG  . SER A 302 ? 0.5904 0.6917 0.7107 -0.0909 0.0349  0.0250  302 SER A OG  
2568  N N   . VAL A 303 ? 0.4710 0.5543 0.5744 -0.0569 0.0256  0.0266  303 VAL A N   
2569  C CA  . VAL A 303 ? 0.5582 0.6299 0.6536 -0.0467 0.0261  0.0284  303 VAL A CA  
2570  C C   . VAL A 303 ? 0.5324 0.6096 0.6345 -0.0376 0.0298  0.0318  303 VAL A C   
2571  O O   . VAL A 303 ? 0.5209 0.6173 0.6345 -0.0347 0.0286  0.0326  303 VAL A O   
2572  C CB  . VAL A 303 ? 0.4520 0.5284 0.5419 -0.0440 0.0194  0.0282  303 VAL A CB  
2573  C CG1 . VAL A 303 ? 0.4696 0.5300 0.5476 -0.0366 0.0209  0.0299  303 VAL A CG1 
2574  C CG2 . VAL A 303 ? 0.4373 0.5125 0.5219 -0.0546 0.0156  0.0235  303 VAL A CG2 
2575  N N   . PHE A 304 ? 0.4917 0.5529 0.5871 -0.0332 0.0343  0.0329  304 PHE A N   
2576  C CA  . PHE A 304 ? 0.4765 0.5385 0.5748 -0.0245 0.0379  0.0352  304 PHE A CA  
2577  C C   . PHE A 304 ? 0.5834 0.6333 0.6718 -0.0174 0.0370  0.0365  304 PHE A C   
2578  O O   . PHE A 304 ? 0.6593 0.6965 0.7377 -0.0202 0.0367  0.0352  304 PHE A O   
2579  C CB  . PHE A 304 ? 0.4422 0.4964 0.5398 -0.0265 0.0441  0.0352  304 PHE A CB  
2580  C CG  . PHE A 304 ? 0.4696 0.5370 0.5762 -0.0322 0.0466  0.0350  304 PHE A CG  
2581  C CD1 . PHE A 304 ? 0.5179 0.6017 0.6347 -0.0276 0.0490  0.0350  304 PHE A CD1 
2582  C CD2 . PHE A 304 ? 0.4702 0.5331 0.5747 -0.0424 0.0470  0.0346  304 PHE A CD2 
2583  C CE1 . PHE A 304 ? 0.4594 0.5575 0.5846 -0.0341 0.0525  0.0342  304 PHE A CE1 
2584  C CE2 . PHE A 304 ? 0.5312 0.6054 0.6421 -0.0496 0.0500  0.0349  304 PHE A CE2 
2585  C CZ  . PHE A 304 ? 0.4723 0.5655 0.5937 -0.0460 0.0531  0.0345  304 PHE A CZ  
2586  N N   . PHE A 305 ? 0.6285 0.6816 0.7193 -0.0086 0.0369  0.0388  305 PHE A N   
2587  C CA  . PHE A 305 ? 0.5257 0.5651 0.6055 -0.0027 0.0362  0.0411  305 PHE A CA  
2588  C C   . PHE A 305 ? 0.6568 0.6857 0.7346 0.0017  0.0425  0.0412  305 PHE A C   
2589  O O   . PHE A 305 ? 0.6885 0.7248 0.7750 0.0062  0.0450  0.0409  305 PHE A O   
2590  C CB  . PHE A 305 ? 0.5828 0.6301 0.6639 0.0045  0.0297  0.0443  305 PHE A CB  
2591  C CG  . PHE A 305 ? 0.6255 0.6844 0.7073 -0.0003 0.0225  0.0439  305 PHE A CG  
2592  C CD1 . PHE A 305 ? 0.5588 0.6384 0.6547 -0.0038 0.0202  0.0419  305 PHE A CD1 
2593  C CD2 . PHE A 305 ? 0.6181 0.6676 0.6855 -0.0028 0.0186  0.0450  305 PHE A CD2 
2594  C CE1 . PHE A 305 ? 0.5743 0.6651 0.6704 -0.0097 0.0134  0.0408  305 PHE A CE1 
2595  C CE2 . PHE A 305 ? 0.5986 0.6589 0.6652 -0.0081 0.0119  0.0438  305 PHE A CE2 
2596  C CZ  . PHE A 305 ? 0.5727 0.6534 0.6537 -0.0116 0.0090  0.0416  305 PHE A CZ  
2597  N N   . ARG A 306 ? 0.6145 0.6274 0.6811 -0.0002 0.0452  0.0407  306 ARG A N   
2598  C CA  . ARG A 306 ? 0.5485 0.5514 0.6122 0.0019  0.0510  0.0400  306 ARG A CA  
2599  C C   . ARG A 306 ? 0.7088 0.7045 0.7689 0.0101  0.0510  0.0426  306 ARG A C   
2600  O O   . ARG A 306 ? 0.6405 0.6347 0.6964 0.0141  0.0460  0.0460  306 ARG A O   
2601  C CB  . ARG A 306 ? 0.5716 0.5627 0.6262 -0.0033 0.0538  0.0379  306 ARG A CB  
2602  C CG  . ARG A 306 ? 0.6805 0.6580 0.7227 -0.0021 0.0546  0.0394  306 ARG A CG  
2603  C CD  . ARG A 306 ? 0.5812 0.5513 0.6165 -0.0081 0.0583  0.0362  306 ARG A CD  
2604  N NE  . ARG A 306 ? 0.6047 0.5644 0.6268 -0.0097 0.0584  0.0378  306 ARG A NE  
2605  C CZ  . ARG A 306 ? 0.6576 0.6084 0.6717 -0.0140 0.0632  0.0358  306 ARG A CZ  
2606  N NH1 . ARG A 306 ? 0.6329 0.5855 0.6521 -0.0165 0.0674  0.0317  306 ARG A NH1 
2607  N NH2 . ARG A 306 ? 0.6089 0.5496 0.6091 -0.0165 0.0637  0.0381  306 ARG A NH2 
2608  N N   . ASP A 307 ? 0.7508 0.7406 0.8112 0.0126  0.0563  0.0410  307 ASP A N   
2609  C CA  . ASP A 307 ? 0.7202 0.6976 0.7753 0.0200  0.0576  0.0425  307 ASP A CA  
2610  C C   . ASP A 307 ? 0.6762 0.6346 0.7159 0.0155  0.0597  0.0432  307 ASP A C   
2611  O O   . ASP A 307 ? 0.6499 0.6036 0.6868 0.0097  0.0645  0.0398  307 ASP A O   
2612  C CB  . ASP A 307 ? 0.5947 0.5737 0.6560 0.0234  0.0631  0.0391  307 ASP A CB  
2613  C CG  . ASP A 307 ? 0.7309 0.6985 0.7897 0.0334  0.0638  0.0400  307 ASP A CG  
2614  O OD1 . ASP A 307 ? 0.7400 0.6869 0.7857 0.0328  0.0660  0.0407  307 ASP A OD1 
2615  O OD2 . ASP A 307 ? 0.7632 0.7423 0.8332 0.0419  0.0624  0.0396  307 ASP A OD2 
2616  N N   . LYS A 308 ? 0.7377 0.6863 0.7672 0.0175  0.0558  0.0476  308 LYS A N   
2617  C CA  . LYS A 308 ? 0.6703 0.6019 0.6841 0.0114  0.0584  0.0483  308 LYS A CA  
2618  C C   . LYS A 308 ? 0.6462 0.5617 0.6539 0.0115  0.0644  0.0466  308 LYS A C   
2619  O O   . LYS A 308 ? 0.6490 0.5575 0.6498 0.0033  0.0692  0.0438  308 LYS A O   
2620  C CB  . LYS A 308 ? 0.6761 0.5991 0.6775 0.0133  0.0528  0.0544  308 LYS A CB  
2621  C CG  . LYS A 308 ? 0.7968 0.7016 0.7797 0.0056  0.0563  0.0556  308 LYS A CG  
2622  C CD  . LYS A 308 ? 0.7174 0.6091 0.6840 0.0078  0.0510  0.0630  308 LYS A CD  
2623  C CE  . LYS A 308 ? 0.7656 0.6500 0.7158 -0.0035 0.0539  0.0629  308 LYS A CE  
2624  N NZ  . LYS A 308 ? 0.8342 0.7352 0.7931 -0.0113 0.0573  0.0556  308 LYS A NZ  
2625  N N   . THR A 309 ? 0.6143 0.5250 0.6255 0.0205  0.0644  0.0474  309 THR A N   
2626  C CA  . THR A 309 ? 0.6711 0.5632 0.6749 0.0209  0.0700  0.0453  309 THR A CA  
2627  C C   . THR A 309 ? 0.6659 0.5645 0.6747 0.0140  0.0761  0.0385  309 THR A C   
2628  O O   . THR A 309 ? 0.6414 0.5292 0.6412 0.0060  0.0806  0.0359  309 THR A O   
2629  C CB  . THR A 309 ? 0.6336 0.5203 0.6417 0.0339  0.0686  0.0465  309 THR A CB  
2630  O OG1 . THR A 309 ? 0.6547 0.5385 0.6594 0.0414  0.0610  0.0536  309 THR A OG1 
2631  C CG2 . THR A 309 ? 0.6358 0.4979 0.6331 0.0343  0.0743  0.0443  309 THR A CG2 
2632  N N   . LEU A 310 ? 0.6157 0.5328 0.6385 0.0163  0.0762  0.0355  310 LEU A N   
2633  C CA  . LEU A 310 ? 0.5895 0.5122 0.6154 0.0104  0.0811  0.0299  310 LEU A CA  
2634  C C   . LEU A 310 ? 0.6193 0.5466 0.6430 0.0007  0.0811  0.0287  310 LEU A C   
2635  O O   . LEU A 310 ? 0.5873 0.5119 0.6076 -0.0056 0.0847  0.0247  310 LEU A O   
2636  C CB  . LEU A 310 ? 0.6421 0.5832 0.6812 0.0138  0.0811  0.0281  310 LEU A CB  
2637  C CG  . LEU A 310 ? 0.6112 0.5534 0.6564 0.0241  0.0821  0.0273  310 LEU A CG  
2638  C CD1 . LEU A 310 ? 0.5792 0.5437 0.6378 0.0248  0.0822  0.0257  310 LEU A CD1 
2639  C CD2 . LEU A 310 ? 0.5868 0.5132 0.6249 0.0256  0.0880  0.0226  310 LEU A CD2 
2640  N N   . SER A 311 ? 0.6969 0.6320 0.7230 -0.0004 0.0768  0.0315  311 SER A N   
2641  C CA  . SER A 311 ? 0.6839 0.6243 0.7096 -0.0080 0.0768  0.0295  311 SER A CA  
2642  C C   . SER A 311 ? 0.6401 0.5678 0.6544 -0.0140 0.0802  0.0283  311 SER A C   
2643  O O   . SER A 311 ? 0.6280 0.5590 0.6428 -0.0204 0.0830  0.0240  311 SER A O   
2644  C CB  . SER A 311 ? 0.6304 0.5800 0.6602 -0.0076 0.0720  0.0318  311 SER A CB  
2645  O OG  . SER A 311 ? 0.6291 0.5904 0.6691 -0.0036 0.0694  0.0328  311 SER A OG  
2646  N N   . ASP A 312 ? 0.6499 0.5635 0.6536 -0.0126 0.0798  0.0322  312 ASP A N   
2647  C CA  . ASP A 312 ? 0.6145 0.5149 0.6053 -0.0203 0.0838  0.0315  312 ASP A CA  
2648  C C   . ASP A 312 ? 0.6112 0.5010 0.5978 -0.0237 0.0890  0.0278  312 ASP A C   
2649  O O   . ASP A 312 ? 0.6760 0.5620 0.6565 -0.0331 0.0933  0.0245  312 ASP A O   
2650  C CB  . ASP A 312 ? 0.5564 0.4416 0.5337 -0.0184 0.0816  0.0378  312 ASP A CB  
2651  C CG  . ASP A 312 ? 0.7452 0.6408 0.7236 -0.0177 0.0767  0.0405  312 ASP A CG  
2652  O OD1 . ASP A 312 ? 0.7976 0.7080 0.7836 -0.0219 0.0770  0.0363  312 ASP A OD1 
2653  O OD2 . ASP A 312 ? 0.7324 0.6207 0.7037 -0.0126 0.0721  0.0465  312 ASP A OD2 
2654  N N   . LEU A 313 ? 0.5875 0.4737 0.5776 -0.0170 0.0892  0.0274  313 LEU A N   
2655  C CA  . LEU A 313 ? 0.6575 0.5337 0.6431 -0.0207 0.0943  0.0225  313 LEU A CA  
2656  C C   . LEU A 313 ? 0.6766 0.5678 0.6683 -0.0291 0.0963  0.0164  313 LEU A C   
2657  O O   . LEU A 313 ? 0.6380 0.5230 0.6232 -0.0380 0.1004  0.0123  313 LEU A O   
2658  C CB  . LEU A 313 ? 0.6781 0.5520 0.6685 -0.0112 0.0945  0.0217  313 LEU A CB  
2659  C CG  . LEU A 313 ? 0.7307 0.5825 0.7125 -0.0032 0.0945  0.0253  313 LEU A CG  
2660  C CD1 . LEU A 313 ? 0.6668 0.5250 0.6589 0.0087  0.0936  0.0243  313 LEU A CD1 
2661  C CD2 . LEU A 313 ? 0.7452 0.5723 0.7121 -0.0096 0.0999  0.0225  313 LEU A CD2 
2662  N N   . ILE A 314 ? 0.6232 0.5340 0.6271 -0.0265 0.0929  0.0160  314 ILE A N   
2663  C CA  . ILE A 314 ? 0.5622 0.4878 0.5724 -0.0326 0.0930  0.0113  314 ILE A CA  
2664  C C   . ILE A 314 ? 0.6053 0.5353 0.6147 -0.0392 0.0935  0.0101  314 ILE A C   
2665  O O   . ILE A 314 ? 0.6526 0.5874 0.6620 -0.0470 0.0960  0.0050  314 ILE A O   
2666  C CB  . ILE A 314 ? 0.5539 0.4954 0.5751 -0.0277 0.0888  0.0125  314 ILE A CB  
2667  C CG1 . ILE A 314 ? 0.5731 0.5139 0.5947 -0.0243 0.0902  0.0114  314 ILE A CG1 
2668  C CG2 . ILE A 314 ? 0.4341 0.3903 0.4621 -0.0318 0.0866  0.0096  314 ILE A CG2 
2669  C CD1 . ILE A 314 ? 0.5059 0.4550 0.5349 -0.0177 0.0873  0.0150  314 ILE A CD1 
2670  N N   . GLY A 315 ? 0.5442 0.4738 0.5529 -0.0368 0.0914  0.0139  315 GLY A N   
2671  C CA  . GLY A 315 ? 0.6005 0.5362 0.6088 -0.0429 0.0927  0.0118  315 GLY A CA  
2672  C C   . GLY A 315 ? 0.5888 0.5134 0.5854 -0.0523 0.0984  0.0098  315 GLY A C   
2673  O O   . GLY A 315 ? 0.5730 0.5073 0.5718 -0.0597 0.1012  0.0051  315 GLY A O   
2674  N N   . PHE A 316 ? 0.5661 0.4698 0.5503 -0.0523 0.1004  0.0130  316 PHE A N   
2675  C CA  . PHE A 316 ? 0.6549 0.5428 0.6243 -0.0622 0.1059  0.0127  316 PHE A CA  
2676  C C   . PHE A 316 ? 0.6834 0.5518 0.6433 -0.0651 0.1094  0.0116  316 PHE A C   
2677  O O   . PHE A 316 ? 0.7249 0.5840 0.6749 -0.0767 0.1149  0.0088  316 PHE A O   
2678  C CB  . PHE A 316 ? 0.5961 0.4704 0.5527 -0.0609 0.1048  0.0197  316 PHE A CB  
2679  C CG  . PHE A 316 ? 0.5476 0.4384 0.5109 -0.0587 0.1018  0.0202  316 PHE A CG  
2680  C CD1 . PHE A 316 ? 0.5387 0.4419 0.5034 -0.0676 0.1056  0.0152  316 PHE A CD1 
2681  C CD2 . PHE A 316 ? 0.5745 0.4694 0.5434 -0.0483 0.0954  0.0246  316 PHE A CD2 
2682  C CE1 . PHE A 316 ? 0.5258 0.4427 0.4961 -0.0653 0.1034  0.0143  316 PHE A CE1 
2683  C CE2 . PHE A 316 ? 0.5243 0.4325 0.4981 -0.0472 0.0927  0.0242  316 PHE A CE2 
2684  C CZ  . PHE A 316 ? 0.5934 0.5114 0.5674 -0.0554 0.0968  0.0188  316 PHE A CZ  
2685  N N   . SER A 317 ? 0.6159 0.4772 0.5778 -0.0559 0.1073  0.0130  317 SER A N   
2686  C CA  . SER A 317 ? 0.6066 0.4447 0.5570 -0.0579 0.1111  0.0117  317 SER A CA  
2687  C C   . SER A 317 ? 0.7488 0.5948 0.7049 -0.0621 0.1135  0.0037  317 SER A C   
2688  O O   . SER A 317 ? 0.7434 0.5763 0.6899 -0.0718 0.1185  -0.0008 317 SER A O   
2689  C CB  . SER A 317 ? 0.7320 0.5542 0.6793 -0.0446 0.1082  0.0172  317 SER A CB  
2690  O OG  . SER A 317 ? 0.8646 0.6764 0.8034 -0.0414 0.1053  0.0251  317 SER A OG  
2691  N N   . TYR A 318 ? 0.7072 0.5735 0.6772 -0.0558 0.1100  0.0020  318 TYR A N   
2692  C CA  . TYR A 318 ? 0.6430 0.5149 0.6159 -0.0581 0.1114  -0.0046 318 TYR A CA  
2693  C C   . TYR A 318 ? 0.7260 0.6096 0.7000 -0.0711 0.1134  -0.0114 318 TYR A C   
2694  O O   . TYR A 318 ? 0.6301 0.5147 0.6025 -0.0756 0.1150  -0.0175 318 TYR A O   
2695  C CB  . TYR A 318 ? 0.6382 0.5289 0.6237 -0.0493 0.1070  -0.0037 318 TYR A CB  
2696  C CG  . TYR A 318 ? 0.7061 0.5882 0.6919 -0.0378 0.1065  -0.0004 318 TYR A CG  
2697  C CD1 . TYR A 318 ? 0.7197 0.5775 0.6953 -0.0343 0.1096  0.0004  318 TYR A CD1 
2698  C CD2 . TYR A 318 ? 0.6749 0.5734 0.6714 -0.0304 0.1031  0.0015  318 TYR A CD2 
2699  C CE1 . TYR A 318 ? 0.6790 0.5317 0.6573 -0.0223 0.1090  0.0025  318 TYR A CE1 
2700  C CE2 . TYR A 318 ? 0.6277 0.5222 0.6266 -0.0203 0.1033  0.0034  318 TYR A CE2 
2701  C CZ  . TYR A 318 ? 0.6629 0.5358 0.6538 -0.0156 0.1061  0.0035  318 TYR A CZ  
2702  O OH  . TYR A 318 ? 0.6465 0.5173 0.6419 -0.0041 0.1061  0.0046  318 TYR A OH  
2703  N N   . HIS A 319 ? 0.7258 0.6198 0.7028 -0.0775 0.1134  -0.0113 319 HIS A N   
2704  C CA  . HIS A 319 ? 0.6001 0.5101 0.5814 -0.0892 0.1149  -0.0186 319 HIS A CA  
2705  C C   . HIS A 319 ? 0.6064 0.4987 0.5745 -0.1013 0.1210  -0.0238 319 HIS A C   
2706  O O   . HIS A 319 ? 0.6540 0.5586 0.6252 -0.1104 0.1217  -0.0312 319 HIS A O   
2707  C CB  . HIS A 319 ? 0.6566 0.5817 0.6444 -0.0935 0.1150  -0.0186 319 HIS A CB  
2708  C CG  . HIS A 319 ? 0.7151 0.6219 0.6893 -0.1012 0.1206  -0.0163 319 HIS A CG  
2709  N ND1 . HIS A 319 ? 0.7344 0.6203 0.6980 -0.0946 0.1204  -0.0084 319 HIS A ND1 
2710  C CD2 . HIS A 319 ? 0.7742 0.6808 0.7427 -0.1157 0.1265  -0.0207 319 HIS A CD2 
2711  C CE1 . HIS A 319 ? 0.6747 0.5463 0.6248 -0.1044 0.1255  -0.0071 319 HIS A CE1 
2712  N NE2 . HIS A 319 ? 0.7337 0.6172 0.6863 -0.1180 0.1300  -0.0147 319 HIS A NE2 
2713  N N   . ALA A 320 ? 0.6064 0.4691 0.5592 -0.1016 0.1249  -0.0200 320 ALA A N   
2714  C CA  . ALA A 320 ? 0.7077 0.5485 0.6456 -0.1139 0.1311  -0.0247 320 ALA A CA  
2715  C C   . ALA A 320 ? 0.7485 0.5781 0.6823 -0.1111 0.1319  -0.0295 320 ALA A C   
2716  O O   . ALA A 320 ? 0.8142 0.6353 0.7397 -0.1234 0.1362  -0.0369 320 ALA A O   
2717  C CB  . ALA A 320 ? 0.6622 0.4717 0.5828 -0.1153 0.1346  -0.0181 320 ALA A CB  
2718  N N   . TRP A 321 ? 0.7338 0.5640 0.6727 -0.0963 0.1283  -0.0262 321 TRP A N   
2719  C CA  . TRP A 321 ? 0.7542 0.5727 0.6884 -0.0926 0.1302  -0.0311 321 TRP A CA  
2720  C C   . TRP A 321 ? 0.7999 0.6435 0.7421 -0.0976 0.1282  -0.0385 321 TRP A C   
2721  O O   . TRP A 321 ? 0.7879 0.6591 0.7423 -0.0993 0.1237  -0.0380 321 TRP A O   
2722  C CB  . TRP A 321 ? 0.6894 0.5019 0.6271 -0.0752 0.1279  -0.0255 321 TRP A CB  
2723  C CG  . TRP A 321 ? 0.6972 0.4927 0.6308 -0.0667 0.1267  -0.0164 321 TRP A CG  
2724  C CD1 . TRP A 321 ? 0.7732 0.5621 0.7009 -0.0724 0.1267  -0.0112 321 TRP A CD1 
2725  C CD2 . TRP A 321 ? 0.8196 0.6038 0.7542 -0.0510 0.1250  -0.0116 321 TRP A CD2 
2726  N NE1 . TRP A 321 ? 0.8375 0.6107 0.7609 -0.0614 0.1243  -0.0028 321 TRP A NE1 
2727  C CE2 . TRP A 321 ? 0.8363 0.6071 0.7650 -0.0476 0.1228  -0.0029 321 TRP A CE2 
2728  C CE3 . TRP A 321 ? 0.7515 0.5376 0.6919 -0.0397 0.1253  -0.0143 321 TRP A CE3 
2729  C CZ2 . TRP A 321 ? 0.8203 0.5802 0.7495 -0.0326 0.1197  0.0035  321 TRP A CZ2 
2730  C CZ3 . TRP A 321 ? 0.7937 0.5704 0.7364 -0.0248 0.1231  -0.0087 321 TRP A CZ3 
2731  C CH2 . TRP A 321 ? 0.8669 0.6310 0.8045 -0.0209 0.1197  0.0002  321 TRP A CH2 
2732  N N   . ASN A 322 ? 0.8256 0.6588 0.7603 -0.0994 0.1314  -0.0455 322 ASN A N   
2733  C CA  . ASN A 322 ? 0.8358 0.6917 0.7761 -0.1016 0.1286  -0.0512 322 ASN A CA  
2734  C C   . ASN A 322 ? 0.8386 0.7114 0.7901 -0.0879 0.1237  -0.0453 322 ASN A C   
2735  O O   . ASN A 322 ? 0.8271 0.6905 0.7806 -0.0761 0.1239  -0.0392 322 ASN A O   
2736  C CB  . ASN A 322 ? 0.8152 0.6544 0.7427 -0.1066 0.1338  -0.0606 322 ASN A CB  
2737  C CG  . ASN A 322 ? 0.9497 0.7675 0.8643 -0.1209 0.1392  -0.0665 322 ASN A CG  
2738  O OD1 . ASN A 322 ? 0.9513 0.7833 0.8679 -0.1345 0.1382  -0.0699 322 ASN A OD1 
2739  N ND2 . ASN A 322 ? 0.9774 0.7605 0.8787 -0.1181 0.1450  -0.0678 322 ASN A ND2 
2740  N N   . ALA A 323 ? 0.7652 0.6796 0.9214 -0.0684 -0.0566 -0.0046 323 ALA A N   
2741  C CA  . ALA A 323 ? 0.6310 0.5634 0.7694 -0.0585 -0.0475 -0.0083 323 ALA A CA  
2742  C C   . ALA A 323 ? 0.7293 0.6532 0.8504 -0.0512 -0.0480 -0.0346 323 ALA A C   
2743  O O   . ALA A 323 ? 0.7544 0.6800 0.8650 -0.0387 -0.0390 -0.0372 323 ALA A O   
2744  C CB  . ALA A 323 ? 0.5608 0.5235 0.6988 -0.0674 -0.0500 0.0001  323 ALA A CB  
2745  N N   . GLU A 324 ? 0.7483 0.6639 0.8674 -0.0594 -0.0579 -0.0555 324 GLU A N   
2746  C CA  . GLU A 324 ? 0.7675 0.6776 0.8724 -0.0520 -0.0565 -0.0834 324 GLU A CA  
2747  C C   . GLU A 324 ? 0.8017 0.6865 0.9147 -0.0365 -0.0516 -0.0861 324 GLU A C   
2748  O O   . GLU A 324 ? 0.7872 0.6760 0.8902 -0.0245 -0.0449 -0.0981 324 GLU A O   
2749  C CB  . GLU A 324 ? 0.8419 0.7459 0.9445 -0.0646 -0.0672 -0.1082 324 GLU A CB  
2750  C CG  . GLU A 324 ? 0.8675 0.7851 0.9488 -0.0617 -0.0642 -0.1371 324 GLU A CG  
2751  C CD  . GLU A 324 ? 1.0788 0.9701 1.1650 -0.0605 -0.0678 -0.1694 324 GLU A CD  
2752  O OE1 . GLU A 324 ? 1.1959 1.0966 1.2674 -0.0552 -0.0625 -0.1958 324 GLU A OE1 
2753  O OE2 . GLU A 324 ? 1.1479 1.0094 1.2545 -0.0650 -0.0755 -0.1685 324 GLU A OE2 
2754  N N   . ASP A 325 ? 0.7829 0.6443 0.9156 -0.0373 -0.0553 -0.0725 325 ASP A N   
2755  C CA  . ASP A 325 ? 0.7547 0.5935 0.8977 -0.0240 -0.0529 -0.0707 325 ASP A CA  
2756  C C   . ASP A 325 ? 0.7582 0.6117 0.8914 -0.0129 -0.0421 -0.0551 325 ASP A C   
2757  O O   . ASP A 325 ? 0.7070 0.5579 0.8367 -0.0001 -0.0382 -0.0631 325 ASP A O   
2758  C CB  . ASP A 325 ? 0.7665 0.5802 0.9331 -0.0305 -0.0605 -0.0551 325 ASP A CB  
2759  C CG  . ASP A 325 ? 0.8501 0.6418 1.0296 -0.0408 -0.0721 -0.0745 325 ASP A CG  
2760  O OD1 . ASP A 325 ? 0.8845 0.6875 1.0508 -0.0473 -0.0743 -0.0972 325 ASP A OD1 
2761  O OD2 . ASP A 325 ? 0.9172 0.6805 1.1197 -0.0434 -0.0793 -0.0673 325 ASP A OD2 
2762  N N   . ALA A 326 ? 0.7004 0.5704 0.8302 -0.0179 -0.0371 -0.0341 326 ALA A N   
2763  C CA  . ALA A 326 ? 0.6191 0.5006 0.7396 -0.0093 -0.0266 -0.0209 326 ALA A CA  
2764  C C   . ALA A 326 ? 0.6152 0.5127 0.7184 -0.0017 -0.0209 -0.0352 326 ALA A C   
2765  O O   . ALA A 326 ? 0.6965 0.5944 0.7940 0.0083  -0.0160 -0.0357 326 ALA A O   
2766  C CB  . ALA A 326 ? 0.6436 0.5401 0.7663 -0.0159 -0.0208 -0.0001 326 ALA A CB  
2767  N N   . VAL A 327 ? 0.6679 0.5815 0.7629 -0.0079 -0.0223 -0.0454 327 VAL A N   
2768  C CA  . VAL A 327 ? 0.6955 0.6270 0.7747 -0.0028 -0.0173 -0.0576 327 VAL A CA  
2769  C C   . VAL A 327 ? 0.6252 0.5471 0.7040 0.0071  -0.0180 -0.0775 327 VAL A C   
2770  O O   . VAL A 327 ? 0.7062 0.6366 0.7784 0.0163  -0.0120 -0.0800 327 VAL A O   
2771  C CB  . VAL A 327 ? 0.6614 0.6141 0.7323 -0.0136 -0.0206 -0.0629 327 VAL A CB  
2772  C CG1 . VAL A 327 ? 0.5915 0.5639 0.6462 -0.0099 -0.0162 -0.0759 327 VAL A CG1 
2773  C CG2 . VAL A 327 ? 0.5848 0.5499 0.6614 -0.0207 -0.0190 -0.0402 327 VAL A CG2 
2774  N N   . ARG A 328 ? 0.6121 0.5160 0.7012 0.0056  -0.0252 -0.0921 328 ARG A N   
2775  C CA  . ARG A 328 ? 0.6628 0.5566 0.7574 0.0170  -0.0250 -0.1125 328 ARG A CA  
2776  C C   . ARG A 328 ? 0.7023 0.5834 0.8087 0.0291  -0.0233 -0.0993 328 ARG A C   
2777  O O   . ARG A 328 ? 0.6742 0.5612 0.7814 0.0408  -0.0194 -0.1082 328 ARG A O   
2778  C CB  . ARG A 328 ? 0.6473 0.5198 0.7542 0.0125  -0.0330 -0.1318 328 ARG A CB  
2779  C CG  . ARG A 328 ? 0.6609 0.5509 0.7520 0.0007  -0.0347 -0.1513 328 ARG A CG  
2780  C CD  . ARG A 328 ? 0.8070 0.6788 0.9063 -0.0003 -0.0394 -0.1820 328 ARG A CD  
2781  N NE  . ARG A 328 ? 0.9392 0.7926 1.0479 -0.0151 -0.0501 -0.1793 328 ARG A NE  
2782  C CZ  . ARG A 328 ? 0.9970 0.8163 1.1307 -0.0141 -0.0567 -0.1727 328 ARG A CZ  
2783  N NH1 . ARG A 328 ? 1.0046 0.8034 1.1571 0.0016  -0.0546 -0.1685 328 ARG A NH1 
2784  N NH2 . ARG A 328 ? 1.0018 0.8091 1.1435 -0.0302 -0.0668 -0.1683 328 ARG A NH2 
2785  N N   . ASP A 329 ? 0.7017 0.5687 0.8177 0.0257  -0.0264 -0.0770 329 ASP A N   
2786  C CA  . ASP A 329 ? 0.6455 0.5065 0.7681 0.0343  -0.0254 -0.0605 329 ASP A CA  
2787  C C   . ASP A 329 ? 0.6562 0.5412 0.7611 0.0387  -0.0168 -0.0562 329 ASP A C   
2788  O O   . ASP A 329 ? 0.6286 0.5174 0.7357 0.0487  -0.0157 -0.0573 329 ASP A O   
2789  C CB  . ASP A 329 ? 0.6459 0.4953 0.7768 0.0265  -0.0285 -0.0358 329 ASP A CB  
2790  C CG  . ASP A 329 ? 0.7751 0.6206 0.9110 0.0327  -0.0289 -0.0165 329 ASP A CG  
2791  O OD1 . ASP A 329 ? 0.7553 0.5824 0.9106 0.0393  -0.0362 -0.0156 329 ASP A OD1 
2792  O OD2 . ASP A 329 ? 0.7383 0.5995 0.8594 0.0306  -0.0221 -0.0023 329 ASP A OD2 
2793  N N   . PHE A 330 ? 0.6455 0.5471 0.7354 0.0309  -0.0112 -0.0513 330 PHE A N   
2794  C CA  . PHE A 330 ? 0.6063 0.5271 0.6812 0.0330  -0.0032 -0.0465 330 PHE A CA  
2795  C C   . PHE A 330 ? 0.6474 0.5825 0.7170 0.0399  -0.0011 -0.0637 330 PHE A C   
2796  O O   . PHE A 330 ? 0.6374 0.5806 0.7039 0.0462  0.0016  -0.0614 330 PHE A O   
2797  C CB  . PHE A 330 ? 0.5600 0.4927 0.6267 0.0238  0.0017  -0.0387 330 PHE A CB  
2798  C CG  . PHE A 330 ? 0.6090 0.5567 0.6636 0.0247  0.0100  -0.0336 330 PHE A CG  
2799  C CD1 . PHE A 330 ? 0.6559 0.6010 0.7071 0.0255  0.0150  -0.0211 330 PHE A CD1 
2800  C CD2 . PHE A 330 ? 0.5649 0.5298 0.6113 0.0232  0.0128  -0.0413 330 PHE A CD2 
2801  C CE1 . PHE A 330 ? 0.8035 0.7597 0.8441 0.0252  0.0227  -0.0195 330 PHE A CE1 
2802  C CE2 . PHE A 330 ? 0.6197 0.5953 0.6581 0.0229  0.0197  -0.0365 330 PHE A CE2 
2803  C CZ  . PHE A 330 ? 0.7862 0.7558 0.8221 0.0240  0.0247  -0.0271 330 PHE A CZ  
2804  N N   . ILE A 331 ? 0.6169 0.5579 0.6850 0.0378  -0.0024 -0.0812 331 ILE A N   
2805  C CA  . ILE A 331 ? 0.6365 0.5949 0.7000 0.0440  0.0011  -0.0983 331 ILE A CA  
2806  C C   . ILE A 331 ? 0.6963 0.6443 0.7764 0.0571  -0.0010 -0.1062 331 ILE A C   
2807  O O   . ILE A 331 ? 0.7385 0.7025 0.8190 0.0650  0.0028  -0.1118 331 ILE A O   
2808  C CB  . ILE A 331 ? 0.6086 0.5790 0.6643 0.0369  0.0007  -0.1159 331 ILE A CB  
2809  C CG1 . ILE A 331 ? 0.5754 0.5570 0.6198 0.0239  0.0006  -0.1028 331 ILE A CG1 
2810  C CG2 . ILE A 331 ? 0.5243 0.5190 0.5733 0.0420  0.0065  -0.1330 331 ILE A CG2 
2811  C CD1 . ILE A 331 ? 0.5509 0.5472 0.5873 0.0229  0.0067  -0.0872 331 ILE A CD1 
2812  N N   . GLY A 332 ? 0.6632 0.5850 0.7604 0.0596  -0.0077 -0.1045 332 GLY A N   
2813  C CA  . GLY A 332 ? 0.5476 0.4573 0.6667 0.0729  -0.0110 -0.1083 332 GLY A CA  
2814  C C   . GLY A 332 ? 0.6298 0.5475 0.7497 0.0784  -0.0109 -0.0891 332 GLY A C   
2815  O O   . GLY A 332 ? 0.6523 0.5795 0.7834 0.0896  -0.0104 -0.0937 332 GLY A O   
2816  N N   . ARG A 333 ? 0.6166 0.5331 0.7249 0.0700  -0.0111 -0.0678 333 ARG A N   
2817  C CA  . ARG A 333 ? 0.6779 0.6043 0.7825 0.0725  -0.0111 -0.0512 333 ARG A CA  
2818  C C   . ARG A 333 ? 0.6416 0.5947 0.7311 0.0725  -0.0043 -0.0578 333 ARG A C   
2819  O O   . ARG A 333 ? 0.6428 0.6084 0.7345 0.0774  -0.0055 -0.0521 333 ARG A O   
2820  C CB  . ARG A 333 ? 0.6127 0.5328 0.7072 0.0628  -0.0112 -0.0299 333 ARG A CB  
2821  C CG  . ARG A 333 ? 0.5276 0.4244 0.6353 0.0589  -0.0169 -0.0221 333 ARG A CG  
2822  C CD  . ARG A 333 ? 0.6393 0.5338 0.7433 0.0530  -0.0184 0.0027  333 ARG A CD  
2823  N NE  . ARG A 333 ? 0.7274 0.6017 0.8456 0.0475  -0.0238 0.0131  333 ARG A NE  
2824  C CZ  . ARG A 333 ? 0.6978 0.5635 0.8261 0.0455  -0.0300 0.0348  333 ARG A CZ  
2825  N NH1 . ARG A 333 ? 0.7820 0.6588 0.9063 0.0484  -0.0323 0.0489  333 ARG A NH1 
2826  N NH2 . ARG A 333 ? 0.7886 0.6360 0.9316 0.0390  -0.0351 0.0442  333 ARG A NH2 
2827  N N   . LEU A 334 ? 0.5831 0.5465 0.6588 0.0660  0.0016  -0.0681 334 LEU A N   
2828  C CA  . LEU A 334 ? 0.6446 0.6331 0.7092 0.0651  0.0075  -0.0739 334 LEU A CA  
2829  C C   . LEU A 334 ? 0.6982 0.7004 0.7757 0.0758  0.0079  -0.0896 334 LEU A C   
2830  O O   . LEU A 334 ? 0.7063 0.7289 0.7834 0.0785  0.0100  -0.0889 334 LEU A O   
2831  C CB  . LEU A 334 ? 0.6663 0.6633 0.7163 0.0550  0.0125  -0.0774 334 LEU A CB  
2832  C CG  . LEU A 334 ? 0.6221 0.6130 0.6617 0.0457  0.0151  -0.0619 334 LEU A CG  
2833  C CD1 . LEU A 334 ? 0.5975 0.6018 0.6278 0.0376  0.0195  -0.0633 334 LEU A CD1 
2834  C CD2 . LEU A 334 ? 0.5926 0.5859 0.6264 0.0455  0.0169  -0.0512 334 LEU A CD2 
2835  N N   . LYS A 335 ? 0.6721 0.6638 0.7626 0.0816  0.0063  -0.1050 335 LYS A N   
2836  C CA  . LYS A 335 ? 0.6384 0.6437 0.7445 0.0936  0.0089  -0.1228 335 LYS A CA  
2837  C C   . LYS A 335 ? 0.6258 0.6294 0.7538 0.1056  0.0040  -0.1127 335 LYS A C   
2838  O O   . LYS A 335 ? 0.7154 0.7403 0.8555 0.1149  0.0070  -0.1204 335 LYS A O   
2839  C CB  . LYS A 335 ? 0.6941 0.6858 0.8099 0.0969  0.0091  -0.1449 335 LYS A CB  
2840  C CG  . LYS A 335 ? 0.8127 0.7749 0.9572 0.1078  0.0020  -0.1450 335 LYS A CG  
2841  C CD  . LYS A 335 ? 0.8841 0.8282 1.0385 0.1093  0.0019  -0.1699 335 LYS A CD  
2842  C CE  . LYS A 335 ? 0.9414 0.8892 1.1225 0.1265  0.0062  -0.1929 335 LYS A CE  
2843  N NZ  . LYS A 335 ? 0.7085 0.6290 0.9067 0.1299  0.0048  -0.2175 335 LYS A NZ  
2844  N N   . LYS A 336 ? 0.6403 0.6225 0.7743 0.1048  -0.0038 -0.0935 336 LYS A N   
2845  C CA  . LYS A 336 ? 0.6833 0.6665 0.8379 0.1144  -0.0107 -0.0791 336 LYS A CA  
2846  C C   . LYS A 336 ? 0.7036 0.7118 0.8431 0.1089  -0.0103 -0.0654 336 LYS A C   
2847  O O   . LYS A 336 ? 0.7229 0.7476 0.8784 0.1171  -0.0138 -0.0602 336 LYS A O   
2848  C CB  . LYS A 336 ? 0.7024 0.6569 0.8677 0.1133  -0.0200 -0.0608 336 LYS A CB  
2849  C CG  . LYS A 336 ? 0.7806 0.7282 0.9806 0.1273  -0.0289 -0.0512 336 LYS A CG  
2850  C CD  . LYS A 336 ? 0.8243 0.7455 1.0342 0.1236  -0.0389 -0.0283 336 LYS A CD  
2851  C CE  . LYS A 336 ? 0.7203 0.6216 0.9132 0.1110  -0.0364 -0.0309 336 LYS A CE  
2852  N NZ  . LYS A 336 ? 0.7832 0.6579 0.9942 0.1090  -0.0463 -0.0107 336 LYS A NZ  
2853  N N   . ILE A 337 ? 0.6029 0.6139 0.7140 0.0949  -0.0063 -0.0597 337 ILE A N   
2854  C CA  . ILE A 337 ? 0.5836 0.6166 0.6792 0.0879  -0.0049 -0.0516 337 ILE A CA  
2855  C C   . ILE A 337 ? 0.5943 0.6552 0.6945 0.0916  0.0003  -0.0651 337 ILE A C   
2856  O O   . ILE A 337 ? 0.6431 0.7254 0.7481 0.0928  -0.0022 -0.0593 337 ILE A O   
2857  C CB  . ILE A 337 ? 0.6561 0.6828 0.7247 0.0734  0.0002  -0.0465 337 ILE A CB  
2858  C CG1 . ILE A 337 ? 0.6388 0.6489 0.7018 0.0686  -0.0043 -0.0292 337 ILE A CG1 
2859  C CG2 . ILE A 337 ? 0.6883 0.7365 0.7423 0.0655  0.0041  -0.0466 337 ILE A CG2 
2860  C CD1 . ILE A 337 ? 0.6243 0.6243 0.6683 0.0576  0.0022  -0.0266 337 ILE A CD1 
2861  N N   . HIS A 338 ? 0.6110 0.6749 0.7098 0.0925  0.0072  -0.0826 338 HIS A N   
2862  C CA  . HIS A 338 ? 0.6750 0.7689 0.7771 0.0949  0.0136  -0.0956 338 HIS A CA  
2863  C C   . HIS A 338 ? 0.6467 0.7562 0.7777 0.1100  0.0113  -0.0989 338 HIS A C   
2864  O O   . HIS A 338 ? 0.6691 0.8086 0.8048 0.1102  0.0133  -0.0982 338 HIS A O   
2865  C CB  . HIS A 338 ? 0.7047 0.7990 0.8005 0.0933  0.0205  -0.1139 338 HIS A CB  
2866  C CG  . HIS A 338 ? 0.5904 0.7188 0.6806 0.0900  0.0286  -0.1243 338 HIS A CG  
2867  N ND1 . HIS A 338 ? 0.7060 0.8568 0.8137 0.1011  0.0340  -0.1407 338 HIS A ND1 
2868  C CD2 . HIS A 338 ? 0.5946 0.7395 0.6656 0.0765  0.0328  -0.1197 338 HIS A CD2 
2869  C CE1 . HIS A 338 ? 0.7396 0.9222 0.8364 0.0934  0.0413  -0.1453 338 HIS A CE1 
2870  N NE2 . HIS A 338 ? 0.6977 0.8763 0.7728 0.0781  0.0399  -0.1314 338 HIS A NE2 
2871  N N   . GLU A 339 ? 0.6418 0.7315 0.7961 0.1226  0.0068  -0.1016 339 GLU A N   
2872  C CA  . GLU A 339 ? 0.6361 0.7374 0.8253 0.1395  0.0041  -0.1033 339 GLU A CA  
2873  C C   . GLU A 339 ? 0.6558 0.7593 0.8552 0.1404  -0.0075 -0.0779 339 GLU A C   
2874  O O   . GLU A 339 ? 0.7250 0.8467 0.9541 0.1528  -0.0110 -0.0742 339 GLU A O   
2875  C CB  . GLU A 339 ? 0.6944 0.7704 0.9086 0.1531  0.0040  -0.1181 339 GLU A CB  
2876  C CG  . GLU A 339 ? 0.8860 0.9660 1.0920 0.1528  0.0155  -0.1473 339 GLU A CG  
2877  C CD  . GLU A 339 ? 0.9459 0.9889 1.1523 0.1521  0.0134  -0.1578 339 GLU A CD  
2878  O OE1 . GLU A 339 ? 0.9638 0.9774 1.1871 0.1563  0.0037  -0.1442 339 GLU A OE1 
2879  O OE2 . GLU A 339 ? 0.9286 0.9736 1.1179 0.1456  0.0205  -0.1780 339 GLU A OE2 
2880  N N   . SER A 340 ? 0.6375 0.7258 0.8138 0.1274  -0.0133 -0.0601 340 SER A N   
2881  C CA  . SER A 340 ? 0.6114 0.7051 0.7918 0.1254  -0.0246 -0.0358 340 SER A CA  
2882  C C   . SER A 340 ? 0.5366 0.6656 0.7095 0.1187  -0.0250 -0.0310 340 SER A C   
2883  O O   . SER A 340 ? 0.5361 0.6817 0.7240 0.1214  -0.0349 -0.0148 340 SER A O   
2884  C CB  . SER A 340 ? 0.6302 0.7005 0.7854 0.1123  -0.0284 -0.0210 340 SER A CB  
2885  O OG  . SER A 340 ? 0.6309 0.7153 0.7566 0.0967  -0.0276 -0.0131 340 SER A OG  
2886  N N   . VAL A 341 ? 0.5688 0.7106 0.7205 0.1090  -0.0157 -0.0432 341 VAL A N   
2887  C CA  . VAL A 341 ? 0.5533 0.7250 0.6954 0.0988  -0.0164 -0.0384 341 VAL A CA  
2888  C C   . VAL A 341 ? 0.6434 0.8446 0.8008 0.1048  -0.0083 -0.0532 341 VAL A C   
2889  O O   . VAL A 341 ? 0.5674 0.7643 0.7285 0.1112  0.0009  -0.0703 341 VAL A O   
2890  C CB  . VAL A 341 ? 0.5939 0.7562 0.6991 0.0793  -0.0130 -0.0365 341 VAL A CB  
2891  C CG1 . VAL A 341 ? 0.6038 0.7416 0.6939 0.0735  -0.0188 -0.0232 341 VAL A CG1 
2892  C CG2 . VAL A 341 ? 0.5292 0.6819 0.6214 0.0757  -0.0017 -0.0515 341 VAL A CG2 
2893  N N   . ASP A 342 ? 0.7229 0.9570 0.8889 0.1015  -0.0120 -0.0462 342 ASP A N   
2894  C CA  . ASP A 342 ? 0.6201 0.8896 0.8009 0.1046  -0.0041 -0.0571 342 ASP A CA  
2895  C C   . ASP A 342 ? 0.6765 0.9584 0.8310 0.0853  0.0012  -0.0588 342 ASP A C   
2896  O O   . ASP A 342 ? 0.7590 1.0757 0.9239 0.0832  0.0058  -0.0623 342 ASP A O   
2897  C CB  . ASP A 342 ? 0.5395 0.8420 0.7538 0.1140  -0.0118 -0.0470 342 ASP A CB  
2898  C CG  . ASP A 342 ? 0.7425 1.0387 0.9945 0.1374  -0.0134 -0.0496 342 ASP A CG  
2899  O OD1 . ASP A 342 ? 0.8518 1.1281 1.1064 0.1468  -0.0042 -0.0674 342 ASP A OD1 
2900  O OD2 . ASP A 342 ? 0.7041 1.0154 0.9846 0.1457  -0.0243 -0.0340 342 ASP A OD2 
2901  N N   . PHE A 343 ? 0.7050 0.9601 0.8289 0.0712  0.0009  -0.0554 343 PHE A N   
2902  C CA  . PHE A 343 ? 0.6378 0.8963 0.7397 0.0538  0.0065  -0.0573 343 PHE A CA  
2903  C C   . PHE A 343 ? 0.5293 0.7623 0.6151 0.0525  0.0145  -0.0657 343 PHE A C   
2904  O O   . PHE A 343 ? 0.6034 0.8206 0.6953 0.0644  0.0162  -0.0725 343 PHE A O   
2905  C CB  . PHE A 343 ? 0.5261 0.7778 0.6096 0.0374  -0.0007 -0.0465 343 PHE A CB  
2906  C CG  . PHE A 343 ? 0.5682 0.7887 0.6376 0.0374  -0.0060 -0.0402 343 PHE A CG  
2907  C CD1 . PHE A 343 ? 0.6219 0.8109 0.6723 0.0336  -0.0002 -0.0437 343 PHE A CD1 
2908  C CD2 . PHE A 343 ? 0.5577 0.7841 0.6342 0.0405  -0.0170 -0.0287 343 PHE A CD2 
2909  C CE1 . PHE A 343 ? 0.6494 0.8139 0.6877 0.0330  -0.0038 -0.0373 343 PHE A CE1 
2910  C CE2 . PHE A 343 ? 0.5714 0.7732 0.6335 0.0387  -0.0215 -0.0210 343 PHE A CE2 
2911  C CZ  . PHE A 343 ? 0.6073 0.7786 0.6503 0.0350  -0.0141 -0.0261 343 PHE A CZ  
2912  N N   . GLN A 344 ? 0.4947 0.7242 0.5624 0.0374  0.0187  -0.0646 344 GLN A N   
2913  C CA  . GLN A 344 ? 0.5467 0.7536 0.6004 0.0347  0.0244  -0.0685 344 GLN A CA  
2914  C C   . GLN A 344 ? 0.5622 0.7357 0.5999 0.0287  0.0215  -0.0618 344 GLN A C   
2915  O O   . GLN A 344 ? 0.5839 0.7528 0.6106 0.0157  0.0214  -0.0568 344 GLN A O   
2916  C CB  . GLN A 344 ? 0.6119 0.8358 0.6598 0.0230  0.0307  -0.0687 344 GLN A CB  
2917  C CG  . GLN A 344 ? 0.5905 0.8385 0.6459 0.0297  0.0375  -0.0791 344 GLN A CG  
2918  C CD  . GLN A 344 ? 0.6454 0.9128 0.6932 0.0160  0.0428  -0.0753 344 GLN A CD  
2919  O OE1 . GLN A 344 ? 0.6026 0.8715 0.6469 0.0024  0.0412  -0.0646 344 GLN A OE1 
2920  N NE2 . GLN A 344 ? 0.6458 0.9286 0.6914 0.0183  0.0489  -0.0838 344 GLN A NE2 
2921  N N   . PRO A 345 ? 0.6238 0.7741 0.6612 0.0372  0.0197  -0.0621 345 PRO A N   
2922  C CA  . PRO A 345 ? 0.6114 0.7359 0.6355 0.0322  0.0174  -0.0548 345 PRO A CA  
2923  C C   . PRO A 345 ? 0.5880 0.6936 0.5989 0.0234  0.0236  -0.0544 345 PRO A C   
2924  O O   . PRO A 345 ? 0.5307 0.6360 0.5433 0.0238  0.0277  -0.0579 345 PRO A O   
2925  C CB  . PRO A 345 ? 0.6030 0.7128 0.6361 0.0445  0.0132  -0.0537 345 PRO A CB  
2926  C CG  . PRO A 345 ? 0.5858 0.7012 0.6304 0.0530  0.0169  -0.0648 345 PRO A CG  
2927  C CD  . PRO A 345 ? 0.5675 0.7149 0.6183 0.0514  0.0198  -0.0699 345 PRO A CD  
2928  N N   . VAL A 346 ? 0.5892 0.6807 0.5877 0.0152  0.0242  -0.0501 346 VAL A N   
2929  C CA  . VAL A 346 ? 0.6799 0.7509 0.6703 0.0090  0.0308  -0.0491 346 VAL A CA  
2930  C C   . VAL A 346 ? 0.6348 0.6865 0.6206 0.0131  0.0307  -0.0454 346 VAL A C   
2931  O O   . VAL A 346 ? 0.6977 0.7488 0.6761 0.0119  0.0273  -0.0421 346 VAL A O   
2932  C CB  . VAL A 346 ? 0.7175 0.7862 0.6999 -0.0036 0.0341  -0.0499 346 VAL A CB  
2933  C CG1 . VAL A 346 ? 0.6461 0.7199 0.6184 -0.0084 0.0293  -0.0503 346 VAL A CG1 
2934  C CG2 . VAL A 346 ? 0.5635 0.6091 0.5426 -0.0072 0.0418  -0.0493 346 VAL A CG2 
2935  N N   . VAL A 347 ? 0.5863 0.6250 0.5761 0.0165  0.0338  -0.0444 347 VAL A N   
2936  C CA  . VAL A 347 ? 0.6693 0.6917 0.6577 0.0198  0.0338  -0.0393 347 VAL A CA  
2937  C C   . VAL A 347 ? 0.4937 0.5023 0.4785 0.0143  0.0424  -0.0373 347 VAL A C   
2938  O O   . VAL A 347 ? 0.5457 0.5511 0.5384 0.0143  0.0451  -0.0366 347 VAL A O   
2939  C CB  . VAL A 347 ? 0.6551 0.6740 0.6551 0.0283  0.0294  -0.0398 347 VAL A CB  
2940  C CG1 . VAL A 347 ? 0.5448 0.5471 0.5453 0.0294  0.0289  -0.0322 347 VAL A CG1 
2941  C CG2 . VAL A 347 ? 0.6062 0.6384 0.6152 0.0360  0.0227  -0.0438 347 VAL A CG2 
2942  N N   . PHE A 348 ? 0.5009 0.5033 0.4748 0.0096  0.0467  -0.0362 348 PHE A N   
2943  C CA  . PHE A 348 ? 0.5684 0.5584 0.5413 0.0057  0.0571  -0.0365 348 PHE A CA  
2944  C C   . PHE A 348 ? 0.5928 0.5746 0.5687 0.0091  0.0590  -0.0292 348 PHE A C   
2945  O O   . PHE A 348 ? 0.6328 0.6161 0.6007 0.0092  0.0558  -0.0246 348 PHE A O   
2946  C CB  . PHE A 348 ? 0.6629 0.6518 0.6211 -0.0023 0.0629  -0.0431 348 PHE A CB  
2947  C CG  . PHE A 348 ? 0.6766 0.6627 0.6389 -0.0079 0.0675  -0.0501 348 PHE A CG  
2948  C CD1 . PHE A 348 ? 0.5083 0.5062 0.4738 -0.0101 0.0606  -0.0513 348 PHE A CD1 
2949  C CD2 . PHE A 348 ? 0.5342 0.5062 0.4997 -0.0111 0.0791  -0.0553 348 PHE A CD2 
2950  C CE1 . PHE A 348 ? 0.4704 0.4655 0.4415 -0.0169 0.0638  -0.0551 348 PHE A CE1 
2951  C CE2 . PHE A 348 ? 0.5482 0.5143 0.5216 -0.0165 0.0824  -0.0605 348 PHE A CE2 
2952  C CZ  . PHE A 348 ? 0.4940 0.4715 0.4697 -0.0203 0.0740  -0.0593 348 PHE A CZ  
2953  N N   . VAL A 349 ? 0.5756 0.5509 0.5646 0.0108  0.0634  -0.0260 349 VAL A N   
2954  C CA  . VAL A 349 ? 0.5959 0.5653 0.5916 0.0127  0.0654  -0.0181 349 VAL A CA  
2955  C C   . VAL A 349 ? 0.6140 0.5782 0.6142 0.0105  0.0788  -0.0183 349 VAL A C   
2956  O O   . VAL A 349 ? 0.5868 0.5489 0.6019 0.0113  0.0824  -0.0174 349 VAL A O   
2957  C CB  . VAL A 349 ? 0.5060 0.4752 0.5162 0.0159  0.0582  -0.0140 349 VAL A CB  
2958  C CG1 . VAL A 349 ? 0.5153 0.4791 0.5351 0.0157  0.0602  -0.0050 349 VAL A CG1 
2959  C CG2 . VAL A 349 ? 0.4749 0.4479 0.4830 0.0195  0.0472  -0.0173 349 VAL A CG2 
2960  N N   . VAL A 350 ? 0.5510 0.5151 0.5397 0.0078  0.0864  -0.0189 350 VAL A N   
2961  C CA  . VAL A 350 ? 0.6510 0.6116 0.6440 0.0066  0.1019  -0.0227 350 VAL A CA  
2962  C C   . VAL A 350 ? 0.6363 0.6007 0.6310 0.0065  0.1074  -0.0138 350 VAL A C   
2963  O O   . VAL A 350 ? 0.6233 0.5934 0.6026 0.0032  0.1034  -0.0090 350 VAL A O   
2964  C CB  . VAL A 350 ? 0.6527 0.6124 0.6277 0.0012  0.1097  -0.0367 350 VAL A CB  
2965  C CG1 . VAL A 350 ? 0.6024 0.5552 0.5880 0.0020  0.1273  -0.0445 350 VAL A CG1 
2966  C CG2 . VAL A 350 ? 0.5487 0.5075 0.5208 -0.0008 0.1015  -0.0430 350 VAL A CG2 
2967  N N   . LEU A 351 ? 0.6311 0.5945 0.6468 0.0095  0.1163  -0.0095 351 LEU A N   
2968  C CA  . LEU A 351 ? 0.6015 0.5718 0.6230 0.0087  0.1237  -0.0003 351 LEU A CA  
2969  C C   . LEU A 351 ? 0.5593 0.5303 0.6062 0.0130  0.1378  -0.0006 351 LEU A C   
2970  O O   . LEU A 351 ? 0.5532 0.5177 0.6155 0.0167  0.1385  -0.0045 351 LEU A O   
2971  C CB  . LEU A 351 ? 0.5723 0.5439 0.6016 0.0082  0.1098  0.0144  351 LEU A CB  
2972  C CG  . LEU A 351 ? 0.6437 0.6115 0.6934 0.0112  0.0993  0.0187  351 LEU A CG  
2973  C CD1 . LEU A 351 ? 0.6785 0.6483 0.7413 0.0089  0.0919  0.0322  351 LEU A CD1 
2974  C CD2 . LEU A 351 ? 0.4705 0.4338 0.5110 0.0123  0.0866  0.0118  351 LEU A CD2 
2975  N N   . ASP A 352 ? 0.6384 0.6190 0.6923 0.0124  0.1491  0.0054  352 ASP A N   
2976  C CA  . ASP A 352 ? 0.6891 0.6739 0.7743 0.0179  0.1621  0.0081  352 ASP A CA  
2977  C C   . ASP A 352 ? 0.6351 0.6186 0.7464 0.0205  0.1487  0.0210  352 ASP A C   
2978  O O   . ASP A 352 ? 0.6238 0.6091 0.7328 0.0168  0.1338  0.0314  352 ASP A O   
2979  C CB  . ASP A 352 ? 0.5828 0.5833 0.6731 0.0161  0.1750  0.0154  352 ASP A CB  
2980  C CG  . ASP A 352 ? 0.6440 0.6510 0.7036 0.0109  0.1875  0.0039  352 ASP A CG  
2981  O OD1 . ASP A 352 ? 0.7057 0.7034 0.7430 0.0092  0.1871  -0.0116 352 ASP A OD1 
2982  O OD2 . ASP A 352 ? 0.6846 0.7082 0.7416 0.0070  0.1972  0.0110  352 ASP A OD2 
2983  N N   . GLY A 353 ? 0.5495 0.5301 0.6860 0.0262  0.1534  0.0203  353 GLY A N   
2984  C CA  . GLY A 353 ? 0.5640 0.5471 0.7224 0.0268  0.1395  0.0332  353 GLY A CA  
2985  C C   . GLY A 353 ? 0.6070 0.6042 0.7988 0.0283  0.1410  0.0496  353 GLY A C   
2986  O O   . GLY A 353 ? 0.6169 0.6191 0.8282 0.0277  0.1293  0.0611  353 GLY A O   
2987  N N   . GLU A 354 ? 0.5153 0.5227 0.7148 0.0290  0.1544  0.0523  354 GLU A N   
2988  C CA  . GLU A 354 ? 0.5530 0.5773 0.7894 0.0306  0.1566  0.0688  354 GLU A CA  
2989  C C   . GLU A 354 ? 0.5992 0.6361 0.8323 0.0238  0.1564  0.0786  354 GLU A C   
2990  O O   . GLU A 354 ? 0.6534 0.7042 0.9123 0.0207  0.1498  0.0950  354 GLU A O   
2991  C CB  . GLU A 354 ? 0.5662 0.5952 0.8336 0.0408  0.1779  0.0653  354 GLU A CB  
2992  C CG  . GLU A 354 ? 0.6128 0.6458 0.8687 0.0430  0.2012  0.0516  354 GLU A CG  
2993  C CD  . GLU A 354 ? 0.6803 0.6953 0.9057 0.0440  0.2096  0.0281  354 GLU A CD  
2994  O OE1 . GLU A 354 ? 0.6221 0.6300 0.8085 0.0363  0.2000  0.0221  354 GLU A OE1 
2995  O OE2 . GLU A 354 ? 0.5900 0.5981 0.8324 0.0521  0.2258  0.0154  354 GLU A OE2 
2996  N N   . ASN A 355 ? 0.6407 0.6744 0.8431 0.0200  0.1621  0.0706  355 ASN A N   
2997  C CA  . ASN A 355 ? 0.5576 0.6062 0.7609 0.0135  0.1664  0.0819  355 ASN A CA  
2998  C C   . ASN A 355 ? 0.5560 0.6000 0.7513 0.0040  0.1449  0.0938  355 ASN A C   
2999  O O   . ASN A 355 ? 0.6066 0.6628 0.8131 -0.0028 0.1443  0.1084  355 ASN A O   
3000  C CB  . ASN A 355 ? 0.5084 0.5601 0.6832 0.0120  0.1825  0.0710  355 ASN A CB  
3001  C CG  . ASN A 355 ? 0.5405 0.5948 0.7224 0.0208  0.2054  0.0545  355 ASN A CG  
3002  O OD1 . ASN A 355 ? 0.5920 0.6568 0.8100 0.0280  0.2171  0.0580  355 ASN A OD1 
3003  N ND2 . ASN A 355 ? 0.5752 0.6194 0.7249 0.0203  0.2116  0.0360  355 ASN A ND2 
3004  N N   . CYS A 356 ? 0.5035 0.5301 0.6813 0.0031  0.1280  0.0873  356 CYS A N   
3005  C CA  . CYS A 356 ? 0.5845 0.6037 0.7555 -0.0050 0.1092  0.0949  356 CYS A CA  
3006  C C   . CYS A 356 ? 0.5976 0.6217 0.7949 -0.0094 0.0961  0.1051  356 CYS A C   
3007  O O   . CYS A 356 ? 0.6826 0.7051 0.8849 -0.0180 0.0844  0.1145  356 CYS A O   
3008  C CB  . CYS A 356 ? 0.5852 0.5860 0.7283 -0.0039 0.0975  0.0825  356 CYS A CB  
3009  S SG  . CYS A 356 ? 0.7637 0.7575 0.9049 0.0026  0.0928  0.0692  356 CYS A SG  
3010  N N   . TRP A 357 ? 0.5353 0.5662 0.7510 -0.0046 0.0974  0.1048  357 TRP A N   
3011  C CA  . TRP A 357 ? 0.5374 0.5741 0.7716 -0.0104 0.0811  0.1130  357 TRP A CA  
3012  C C   . TRP A 357 ? 0.5423 0.5962 0.8050 -0.0179 0.0798  0.1307  357 TRP A C   
3013  O O   . TRP A 357 ? 0.5574 0.6129 0.8280 -0.0277 0.0627  0.1366  357 TRP A O   
3014  C CB  . TRP A 357 ? 0.5275 0.5703 0.7752 -0.0043 0.0819  0.1122  357 TRP A CB  
3015  C CG  . TRP A 357 ? 0.4716 0.4993 0.6941 0.0020  0.0843  0.0964  357 TRP A CG  
3016  C CD1 . TRP A 357 ? 0.5391 0.5652 0.7663 0.0107  0.0975  0.0910  357 TRP A CD1 
3017  C CD2 . TRP A 357 ? 0.4626 0.4753 0.6546 -0.0004 0.0732  0.0838  357 TRP A CD2 
3018  N NE1 . TRP A 357 ? 0.5101 0.5220 0.7102 0.0123  0.0944  0.0769  357 TRP A NE1 
3019  C CE2 . TRP A 357 ? 0.5305 0.5358 0.7092 0.0062  0.0800  0.0727  357 TRP A CE2 
3020  C CE3 . TRP A 357 ? 0.5549 0.5593 0.7325 -0.0071 0.0586  0.0803  357 TRP A CE3 
3021  C CZ2 . TRP A 357 ? 0.5974 0.5915 0.7491 0.0061  0.0728  0.0599  357 TRP A CZ2 
3022  C CZ3 . TRP A 357 ? 0.5565 0.5483 0.7088 -0.0053 0.0525  0.0661  357 TRP A CZ3 
3023  C CH2 . TRP A 357 ? 0.5312 0.5199 0.6707 0.0011  0.0595  0.0569  357 TRP A CH2 
3024  N N   . GLU A 358 ? 0.5393 0.6077 0.8175 -0.0147 0.0980  0.1382  358 GLU A N   
3025  C CA  . GLU A 358 ? 0.5268 0.6163 0.8361 -0.0221 0.0982  0.1568  358 GLU A CA  
3026  C C   . GLU A 358 ? 0.5264 0.6079 0.8264 -0.0354 0.0845  0.1632  358 GLU A C   
3027  O O   . GLU A 358 ? 0.4826 0.5763 0.8066 -0.0459 0.0748  0.1775  358 GLU A O   
3028  C CB  . GLU A 358 ? 0.5926 0.7016 0.9187 -0.0153 0.1234  0.1614  358 GLU A CB  
3029  C CG  . GLU A 358 ? 0.6325 0.7337 0.9271 -0.0137 0.1374  0.1516  358 GLU A CG  
3030  C CD  . GLU A 358 ? 0.6368 0.7554 0.9419 -0.0044 0.1653  0.1471  358 GLU A CD  
3031  O OE1 . GLU A 358 ? 0.5680 0.7107 0.9110 -0.0019 0.1753  0.1584  358 GLU A OE1 
3032  O OE2 . GLU A 358 ? 0.7658 0.8753 1.0425 0.0004  0.1775  0.1311  358 GLU A OE2 
3033  N N   . TYR A 359 ? 0.5519 0.6129 0.8201 -0.0358 0.0825  0.1538  359 TYR A N   
3034  C CA  . TYR A 359 ? 0.5488 0.5978 0.8113 -0.0474 0.0689  0.1605  359 TYR A CA  
3035  C C   . TYR A 359 ? 0.5050 0.5340 0.7607 -0.0524 0.0466  0.1512  359 TYR A C   
3036  O O   . TYR A 359 ? 0.4983 0.5140 0.7551 -0.0624 0.0333  0.1553  359 TYR A O   
3037  C CB  . TYR A 359 ? 0.4965 0.5353 0.7322 -0.0456 0.0763  0.1581  359 TYR A CB  
3038  C CG  . TYR A 359 ? 0.6388 0.6998 0.8760 -0.0423 0.0997  0.1641  359 TYR A CG  
3039  C CD1 . TYR A 359 ? 0.5402 0.6215 0.7957 -0.0514 0.1065  0.1834  359 TYR A CD1 
3040  C CD2 . TYR A 359 ? 0.7360 0.7991 0.9571 -0.0311 0.1158  0.1495  359 TYR A CD2 
3041  C CE1 . TYR A 359 ? 0.5914 0.6968 0.8471 -0.0485 0.1301  0.1867  359 TYR A CE1 
3042  C CE2 . TYR A 359 ? 0.6674 0.7509 0.8885 -0.0283 0.1388  0.1506  359 TYR A CE2 
3043  C CZ  . TYR A 359 ? 0.7069 0.8128 0.9445 -0.0366 0.1466  0.1687  359 TYR A CZ  
3044  O OH  . TYR A 359 ? 0.8129 0.9424 1.0490 -0.0338 0.1717  0.1673  359 TYR A OH  
3045  N N   . TYR A 360 ? 0.4741 0.5013 0.7238 -0.0464 0.0427  0.1388  360 TYR A N   
3046  C CA  . TYR A 360 ? 0.5041 0.5185 0.7465 -0.0516 0.0235  0.1279  360 TYR A CA  
3047  C C   . TYR A 360 ? 0.5381 0.5694 0.8061 -0.0628 0.0123  0.1381  360 TYR A C   
3048  O O   . TYR A 360 ? 0.4818 0.5370 0.7748 -0.0623 0.0200  0.1525  360 TYR A O   
3049  C CB  . TYR A 360 ? 0.5078 0.5182 0.7313 -0.0421 0.0244  0.1122  360 TYR A CB  
3050  C CG  . TYR A 360 ? 0.5410 0.5320 0.7360 -0.0341 0.0274  0.0976  360 TYR A CG  
3051  C CD1 . TYR A 360 ? 0.4670 0.4577 0.6523 -0.0267 0.0427  0.0988  360 TYR A CD1 
3052  C CD2 . TYR A 360 ? 0.5779 0.5548 0.7560 -0.0339 0.0156  0.0816  360 TYR A CD2 
3053  C CE1 . TYR A 360 ? 0.5309 0.5078 0.6916 -0.0206 0.0439  0.0872  360 TYR A CE1 
3054  C CE2 . TYR A 360 ? 0.5249 0.4881 0.6813 -0.0260 0.0182  0.0697  360 TYR A CE2 
3055  C CZ  . TYR A 360 ? 0.5817 0.5450 0.7298 -0.0198 0.0313  0.0737  360 TYR A CZ  
3056  O OH  . TYR A 360 ? 0.5415 0.4943 0.6690 -0.0132 0.0323  0.0636  360 TYR A OH  
3057  N N   . GLU A 361 ? 0.5612 0.5809 0.8236 -0.0727 -0.0062 0.1291  361 GLU A N   
3058  C CA  . GLU A 361 ? 0.5565 0.5932 0.8380 -0.0857 -0.0199 0.1358  361 GLU A CA  
3059  C C   . GLU A 361 ? 0.5969 0.6541 0.8802 -0.0806 -0.0190 0.1363  361 GLU A C   
3060  O O   . GLU A 361 ? 0.6174 0.6666 0.8779 -0.0724 -0.0173 0.1221  361 GLU A O   
3061  C CB  . GLU A 361 ? 0.6137 0.6313 0.8842 -0.0980 -0.0391 0.1207  361 GLU A CB  
3062  C CG  . GLU A 361 ? 0.7646 0.7993 1.0533 -0.1157 -0.0553 0.1272  361 GLU A CG  
3063  C CD  . GLU A 361 ? 0.9523 0.9950 1.2708 -0.1269 -0.0565 0.1478  361 GLU A CD  
3064  O OE1 . GLU A 361 ? 0.8120 0.8857 1.1572 -0.1322 -0.0564 0.1667  361 GLU A OE1 
3065  O OE2 . GLU A 361 ? 1.0106 1.0299 1.3282 -0.1302 -0.0574 0.1468  361 GLU A OE2 
3066  N N   . GLU A 362 ? 0.5842 0.6696 0.8976 -0.0858 -0.0204 0.1552  362 GLU A N   
3067  C CA  . GLU A 362 ? 0.5292 0.6374 0.8530 -0.0820 -0.0211 0.1624  362 GLU A CA  
3068  C C   . GLU A 362 ? 0.5072 0.6093 0.8220 -0.0638 -0.0034 0.1575  362 GLU A C   
3069  O O   . GLU A 362 ? 0.5514 0.6561 0.8554 -0.0599 -0.0062 0.1526  362 GLU A O   
3070  C CB  . GLU A 362 ? 0.6465 0.7582 0.9531 -0.0936 -0.0410 0.1522  362 GLU A CB  
3071  C CG  . GLU A 362 ? 0.7691 0.8926 1.0889 -0.1139 -0.0597 0.1581  362 GLU A CG  
3072  C CD  . GLU A 362 ? 1.0215 1.1462 1.3170 -0.1273 -0.0786 0.1419  362 GLU A CD  
3073  O OE1 . GLU A 362 ? 1.0489 1.1928 1.3383 -0.1265 -0.0824 0.1447  362 GLU A OE1 
3074  O OE2 . GLU A 362 ? 1.2459 1.3528 1.5291 -0.1391 -0.0894 0.1263  362 GLU A OE2 
3075  N N   . ASN A 363 ? 0.5345 0.6292 0.8527 -0.0541 0.0148  0.1588  363 ASN A N   
3076  C CA  . ASN A 363 ? 0.6037 0.6913 0.9136 -0.0383 0.0330  0.1521  363 ASN A CA  
3077  C C   . ASN A 363 ? 0.5616 0.6282 0.8352 -0.0344 0.0292  0.1323  363 ASN A C   
3078  O O   . ASN A 363 ? 0.5576 0.6220 0.8259 -0.0247 0.0377  0.1275  363 ASN A O   
3079  C CB  . ASN A 363 ? 0.4951 0.6039 0.8365 -0.0306 0.0406  0.1656  363 ASN A CB  
3080  C CG  . ASN A 363 ? 0.5087 0.6091 0.8486 -0.0151 0.0623  0.1585  363 ASN A CG  
3081  O OD1 . ASN A 363 ? 0.5623 0.6562 0.8957 -0.0109 0.0771  0.1533  363 ASN A OD1 
3082  N ND2 . ASN A 363 ? 0.4878 0.5887 0.8333 -0.0078 0.0638  0.1582  363 ASN A ND2 
3083  N N   . GLY A 364 ? 0.5299 0.5807 0.7809 -0.0418 0.0169  0.1204  364 GLY A N   
3084  C CA  . GLY A 364 ? 0.5504 0.5840 0.7702 -0.0372 0.0146  0.1015  364 GLY A CA  
3085  C C   . GLY A 364 ? 0.5277 0.5710 0.7401 -0.0390 0.0058  0.0970  364 GLY A C   
3086  O O   . GLY A 364 ? 0.5563 0.5894 0.7446 -0.0348 0.0057  0.0821  364 GLY A O   
3087  N N   . ILE A 365 ? 0.5271 0.5929 0.7601 -0.0460 -0.0020 0.1112  365 ILE A N   
3088  C CA  . ILE A 365 ? 0.5237 0.6032 0.7482 -0.0502 -0.0118 0.1101  365 ILE A CA  
3089  C C   . ILE A 365 ? 0.5665 0.6381 0.7613 -0.0584 -0.0243 0.0898  365 ILE A C   
3090  O O   . ILE A 365 ? 0.5600 0.6319 0.7341 -0.0557 -0.0243 0.0792  365 ILE A O   
3091  C CB  . ILE A 365 ? 0.5485 0.6570 0.8028 -0.0579 -0.0202 0.1325  365 ILE A CB  
3092  C CG1 . ILE A 365 ? 0.4921 0.6082 0.7770 -0.0455 -0.0055 0.1497  365 ILE A CG1 
3093  C CG2 . ILE A 365 ? 0.5175 0.6441 0.7578 -0.0684 -0.0357 0.1319  365 ILE A CG2 
3094  C CD1 . ILE A 365 ? 0.4317 0.5698 0.7582 -0.0481 -0.0060 0.1726  365 ILE A CD1 
3095  N N   . PRO A 366 ? 0.6174 0.6817 0.8101 -0.0684 -0.0343 0.0827  366 PRO A N   
3096  C CA  . PRO A 366 ? 0.5965 0.6499 0.7623 -0.0740 -0.0437 0.0588  366 PRO A CA  
3097  C C   . PRO A 366 ? 0.5485 0.5804 0.6937 -0.0612 -0.0341 0.0416  366 PRO A C   
3098  O O   . PRO A 366 ? 0.6210 0.6570 0.7458 -0.0602 -0.0357 0.0272  366 PRO A O   
3099  C CB  . PRO A 366 ? 0.6021 0.6449 0.7771 -0.0853 -0.0537 0.0560  366 PRO A CB  
3100  C CG  . PRO A 366 ? 0.5605 0.6235 0.7658 -0.0914 -0.0552 0.0814  366 PRO A CG  
3101  C CD  . PRO A 366 ? 0.5624 0.6294 0.7791 -0.0763 -0.0383 0.0954  366 PRO A CD  
3102  N N   . PHE A 367 ? 0.4734 0.4861 0.6235 -0.0522 -0.0245 0.0439  367 PHE A N   
3103  C CA  . PHE A 367 ? 0.4709 0.4664 0.6033 -0.0407 -0.0166 0.0305  367 PHE A CA  
3104  C C   . PHE A 367 ? 0.5572 0.5645 0.6785 -0.0340 -0.0098 0.0289  367 PHE A C   
3105  O O   . PHE A 367 ? 0.5938 0.5990 0.6966 -0.0308 -0.0106 0.0132  367 PHE A O   
3106  C CB  . PHE A 367 ? 0.4674 0.4486 0.6070 -0.0336 -0.0067 0.0390  367 PHE A CB  
3107  C CG  . PHE A 367 ? 0.5315 0.5001 0.6540 -0.0225 0.0008  0.0290  367 PHE A CG  
3108  C CD1 . PHE A 367 ? 0.5036 0.4575 0.6146 -0.0201 -0.0052 0.0128  367 PHE A CD1 
3109  C CD2 . PHE A 367 ? 0.5301 0.5023 0.6498 -0.0148 0.0138  0.0349  367 PHE A CD2 
3110  C CE1 . PHE A 367 ? 0.5596 0.5059 0.6584 -0.0102 0.0004  0.0059  367 PHE A CE1 
3111  C CE2 . PHE A 367 ? 0.4940 0.4574 0.5976 -0.0068 0.0190  0.0262  367 PHE A CE2 
3112  C CZ  . PHE A 367 ? 0.5497 0.5017 0.6435 -0.0045 0.0117  0.0132  367 PHE A CZ  
3113  N N   . LEU A 368 ? 0.4464 0.4662 0.5816 -0.0318 -0.0027 0.0454  368 LEU A N   
3114  C CA  . LEU A 368 ? 0.5119 0.5395 0.6407 -0.0261 0.0038  0.0459  368 LEU A CA  
3115  C C   . LEU A 368 ? 0.5526 0.5986 0.6707 -0.0339 -0.0062 0.0422  368 LEU A C   
3116  O O   . LEU A 368 ? 0.5558 0.6049 0.6585 -0.0309 -0.0037 0.0340  368 LEU A O   
3117  C CB  . LEU A 368 ? 0.4689 0.5033 0.6205 -0.0218 0.0135  0.0639  368 LEU A CB  
3118  C CG  . LEU A 368 ? 0.5156 0.5349 0.6707 -0.0130 0.0279  0.0638  368 LEU A CG  
3119  C CD1 . LEU A 368 ? 0.5360 0.5629 0.7168 -0.0081 0.0391  0.0782  368 LEU A CD1 
3120  C CD2 . LEU A 368 ? 0.5268 0.5327 0.6588 -0.0063 0.0339  0.0491  368 LEU A CD2 
3121  N N   . GLU A 369 ? 0.5552 0.6167 0.6807 -0.0454 -0.0178 0.0485  369 GLU A N   
3122  C CA  . GLU A 369 ? 0.5585 0.6427 0.6711 -0.0554 -0.0279 0.0459  369 GLU A CA  
3123  C C   . GLU A 369 ? 0.5797 0.6583 0.6654 -0.0572 -0.0313 0.0194  369 GLU A C   
3124  O O   . GLU A 369 ? 0.4821 0.5784 0.5508 -0.0612 -0.0333 0.0129  369 GLU A O   
3125  C CB  . GLU A 369 ? 0.5486 0.6539 0.6752 -0.0693 -0.0408 0.0600  369 GLU A CB  
3126  C CG  . GLU A 369 ? 0.5618 0.6836 0.7172 -0.0682 -0.0393 0.0885  369 GLU A CG  
3127  C CD  . GLU A 369 ? 0.6428 0.7924 0.8114 -0.0836 -0.0548 0.1043  369 GLU A CD  
3128  O OE1 . GLU A 369 ? 0.7055 0.8559 0.8634 -0.0952 -0.0655 0.0921  369 GLU A OE1 
3129  O OE2 . GLU A 369 ? 0.5542 0.7248 0.7455 -0.0846 -0.0571 0.1291  369 GLU A OE2 
3130  N N   . LYS A 370 ? 0.5709 0.6266 0.6546 -0.0546 -0.0317 0.0045  370 LYS A N   
3131  C CA  . LYS A 370 ? 0.6182 0.6657 0.6822 -0.0532 -0.0332 -0.0221 370 LYS A CA  
3132  C C   . LYS A 370 ? 0.6249 0.6629 0.6803 -0.0393 -0.0222 -0.0294 370 LYS A C   
3133  O O   . LYS A 370 ? 0.6058 0.6513 0.6452 -0.0377 -0.0211 -0.0466 370 LYS A O   
3134  C CB  . LYS A 370 ? 0.6322 0.6563 0.7020 -0.0555 -0.0390 -0.0343 370 LYS A CB  
3135  C CG  . LYS A 370 ? 0.8142 0.8492 0.8843 -0.0725 -0.0524 -0.0385 370 LYS A CG  
3136  C CD  . LYS A 370 ? 0.8180 0.8473 0.9119 -0.0790 -0.0575 -0.0193 370 LYS A CD  
3137  C CE  . LYS A 370 ? 0.8905 0.9430 0.9867 -0.0980 -0.0716 -0.0146 370 LYS A CE  
3138  N NZ  . LYS A 370 ? 0.8301 0.9161 0.9275 -0.1014 -0.0721 0.0059  370 LYS A NZ  
3139  N N   . LEU A 371 ? 0.6164 0.6410 0.6824 -0.0302 -0.0137 -0.0170 371 LEU A N   
3140  C CA  . LEU A 371 ? 0.5613 0.5798 0.6192 -0.0192 -0.0046 -0.0221 371 LEU A CA  
3141  C C   . LEU A 371 ? 0.5917 0.6317 0.6414 -0.0207 -0.0016 -0.0184 371 LEU A C   
3142  O O   . LEU A 371 ? 0.6286 0.6735 0.6659 -0.0166 0.0016  -0.0303 371 LEU A O   
3143  C CB  . LEU A 371 ? 0.5378 0.5407 0.6063 -0.0121 0.0035  -0.0099 371 LEU A CB  
3144  C CG  . LEU A 371 ? 0.5070 0.5044 0.5666 -0.0028 0.0118  -0.0143 371 LEU A CG  
3145  C CD1 . LEU A 371 ? 0.6485 0.6377 0.6998 0.0023  0.0085  -0.0315 371 LEU A CD1 
3146  C CD2 . LEU A 371 ? 0.4980 0.4835 0.5648 0.0014  0.0199  -0.0032 371 LEU A CD2 
3147  N N   . TYR A 372 ? 0.5426 0.5970 0.6023 -0.0270 -0.0029 -0.0003 372 TYR A N   
3148  C CA  . TYR A 372 ? 0.4976 0.5714 0.5534 -0.0296 -0.0011 0.0075  372 TYR A CA  
3149  C C   . TYR A 372 ? 0.5667 0.6650 0.6054 -0.0391 -0.0083 -0.0019 372 TYR A C   
3150  O O   . TYR A 372 ? 0.6347 0.7481 0.6628 -0.0398 -0.0054 -0.0038 372 TYR A O   
3151  C CB  . TYR A 372 ? 0.5284 0.6092 0.6054 -0.0325 -0.0009 0.0319  372 TYR A CB  
3152  C CG  . TYR A 372 ? 0.5297 0.5898 0.6223 -0.0228 0.0097  0.0386  372 TYR A CG  
3153  C CD1 . TYR A 372 ? 0.5482 0.5895 0.6311 -0.0142 0.0177  0.0257  372 TYR A CD1 
3154  C CD2 . TYR A 372 ? 0.5346 0.5967 0.6526 -0.0225 0.0120  0.0577  372 TYR A CD2 
3155  C CE1 . TYR A 372 ? 0.5549 0.5805 0.6479 -0.0072 0.0279  0.0302  372 TYR A CE1 
3156  C CE2 . TYR A 372 ? 0.6241 0.6693 0.7553 -0.0137 0.0238  0.0606  372 TYR A CE2 
3157  C CZ  . TYR A 372 ? 0.5637 0.5911 0.6801 -0.0070 0.0319  0.0461  372 TYR A CZ  
3158  O OH  . TYR A 372 ? 0.4526 0.4667 0.5789 -0.0002 0.0442  0.0478  372 TYR A OH  
3159  N N   . SER A 373 ? 0.5268 0.6311 0.5616 -0.0477 -0.0175 -0.0086 373 SER A N   
3160  C CA  . SER A 373 ? 0.6631 0.7924 0.6775 -0.0577 -0.0232 -0.0222 373 SER A CA  
3161  C C   . SER A 373 ? 0.6468 0.7681 0.6465 -0.0497 -0.0174 -0.0499 373 SER A C   
3162  O O   . SER A 373 ? 0.6319 0.7758 0.6155 -0.0525 -0.0149 -0.0596 373 SER A O   
3163  C CB  . SER A 373 ? 0.5704 0.7092 0.5835 -0.0712 -0.0353 -0.0241 373 SER A CB  
3164  O OG  . SER A 373 ? 0.7705 0.8819 0.7979 -0.0674 -0.0369 -0.0268 373 SER A OG  
3165  N N   . THR A 374 ? 0.6041 0.6953 0.6113 -0.0397 -0.0150 -0.0612 374 THR A N   
3166  C CA  . THR A 374 ? 0.6427 0.7251 0.6431 -0.0296 -0.0096 -0.0846 374 THR A CA  
3167  C C   . THR A 374 ? 0.6367 0.7287 0.6338 -0.0221 -0.0008 -0.0803 374 THR A C   
3168  O O   . THR A 374 ? 0.6166 0.7257 0.6027 -0.0204 0.0032  -0.0955 374 THR A O   
3169  C CB  . THR A 374 ? 0.6285 0.6765 0.6425 -0.0201 -0.0098 -0.0901 374 THR A CB  
3170  O OG1 . THR A 374 ? 0.5300 0.5681 0.5491 -0.0287 -0.0187 -0.0939 374 THR A OG1 
3171  C CG2 . THR A 374 ? 0.6624 0.7022 0.6748 -0.0085 -0.0053 -0.1125 374 THR A CG2 
3172  N N   . LEU A 375 ? 0.6545 0.7369 0.6618 -0.0184 0.0028  -0.0606 375 LEU A N   
3173  C CA  . LEU A 375 ? 0.6642 0.7529 0.6697 -0.0132 0.0101  -0.0563 375 LEU A CA  
3174  C C   . LEU A 375 ? 0.6371 0.7577 0.6330 -0.0225 0.0103  -0.0507 375 LEU A C   
3175  O O   . LEU A 375 ? 0.7014 0.8344 0.6926 -0.0201 0.0156  -0.0538 375 LEU A O   
3176  C CB  . LEU A 375 ? 0.5799 0.6507 0.5974 -0.0094 0.0140  -0.0388 375 LEU A CB  
3177  C CG  . LEU A 375 ? 0.6139 0.6580 0.6377 -0.0002 0.0160  -0.0425 375 LEU A CG  
3178  C CD1 . LEU A 375 ? 0.6106 0.6421 0.6446 0.0005  0.0205  -0.0259 375 LEU A CD1 
3179  C CD2 . LEU A 375 ? 0.7392 0.7816 0.7580 0.0085  0.0194  -0.0546 375 LEU A CD2 
3180  N N   . GLU A 376 ? 0.6692 0.8060 0.6633 -0.0343 0.0036  -0.0405 376 GLU A N   
3181  C CA  . GLU A 376 ? 0.7805 0.9521 0.7643 -0.0454 0.0022  -0.0327 376 GLU A CA  
3182  C C   . GLU A 376 ? 0.7616 0.9554 0.7262 -0.0467 0.0050  -0.0567 376 GLU A C   
3183  O O   . GLU A 376 ? 0.8464 1.0648 0.8035 -0.0498 0.0095  -0.0548 376 GLU A O   
3184  C CB  . GLU A 376 ? 0.6753 0.8624 0.6615 -0.0588 -0.0076 -0.0155 376 GLU A CB  
3185  C CG  . GLU A 376 ? 0.5978 0.7863 0.6027 -0.0618 -0.0089 0.0154  376 GLU A CG  
3186  C CD  . GLU A 376 ? 0.8436 1.0572 0.8515 -0.0762 -0.0202 0.0350  376 GLU A CD  
3187  O OE1 . GLU A 376 ? 0.8711 1.1191 0.8625 -0.0886 -0.0247 0.0373  376 GLU A OE1 
3188  O OE2 . GLU A 376 ? 0.8735 1.0758 0.9006 -0.0759 -0.0248 0.0489  376 GLU A OE2 
3189  N N   . LYS A 377 ? 0.7182 0.9039 0.6766 -0.0446 0.0031  -0.0801 377 LYS A N   
3190  C CA  . LYS A 377 ? 0.7208 0.9284 0.6627 -0.0454 0.0071  -0.1067 377 LYS A CA  
3191  C C   . LYS A 377 ? 0.6900 0.8872 0.6380 -0.0295 0.0165  -0.1237 377 LYS A C   
3192  O O   . LYS A 377 ? 0.8675 1.0914 0.8060 -0.0289 0.0234  -0.1385 377 LYS A O   
3193  C CB  . LYS A 377 ? 0.6552 0.8579 0.5894 -0.0510 0.0010  -0.1275 377 LYS A CB  
3194  C CG  . LYS A 377 ? 0.7084 0.9091 0.6454 -0.0636 -0.0105 -0.1090 377 LYS A CG  
3195  C CD  . LYS A 377 ? 0.8701 1.0605 0.8021 -0.0697 -0.0177 -0.1306 377 LYS A CD  
3196  C CE  . LYS A 377 ? 0.8673 1.0293 0.8186 -0.0704 -0.0261 -0.1144 377 LYS A CE  
3197  N NZ  . LYS A 377 ? 0.8151 0.9842 0.7596 -0.0867 -0.0380 -0.1210 377 LYS A NZ  
3198  N N   . GLU A 378 ? 0.6723 0.8349 0.6369 -0.0169 0.0169  -0.1213 378 GLU A N   
3199  C CA  . GLU A 378 ? 0.7013 0.8558 0.6747 -0.0020 0.0237  -0.1340 378 GLU A CA  
3200  C C   . GLU A 378 ? 0.7660 0.9416 0.7385 -0.0024 0.0294  -0.1215 378 GLU A C   
3201  O O   . GLU A 378 ? 0.7050 0.8692 0.6839 -0.0033 0.0285  -0.1009 378 GLU A O   
3202  C CB  . GLU A 378 ? 0.5959 0.7118 0.5857 0.0088  0.0210  -0.1296 378 GLU A CB  
3203  C CG  . GLU A 378 ? 0.7092 0.8015 0.7039 0.0093  0.0150  -0.1416 378 GLU A CG  
3204  C CD  . GLU A 378 ? 0.8300 0.9306 0.8214 0.0122  0.0173  -0.1718 378 GLU A CD  
3205  O OE1 . GLU A 378 ? 0.9601 1.0570 0.9624 0.0258  0.0225  -0.1859 378 GLU A OE1 
3206  O OE2 . GLU A 378 ? 0.7696 0.8824 0.7481 0.0006  0.0140  -0.1822 378 GLU A OE2 
3207  N N   . GLU A 379 ? 0.7962 1.0029 0.7620 -0.0022 0.0360  -0.1352 379 GLU A N   
3208  C CA  . GLU A 379 ? 0.8504 1.0822 0.8155 -0.0055 0.0410  -0.1229 379 GLU A CA  
3209  C C   . GLU A 379 ? 0.7230 0.9446 0.7032 0.0074  0.0447  -0.1238 379 GLU A C   
3210  O O   . GLU A 379 ? 0.7571 0.9915 0.7396 0.0034  0.0467  -0.1098 379 GLU A O   
3211  C CB  . GLU A 379 ? 0.8510 1.1278 0.8021 -0.0132 0.0471  -0.1342 379 GLU A CB  
3212  C CG  . GLU A 379 ? 0.8276 1.1324 0.7659 -0.0319 0.0442  -0.1117 379 GLU A CG  
3213  C CD  . GLU A 379 ? 1.1008 1.4027 1.0494 -0.0361 0.0431  -0.0839 379 GLU A CD  
3214  O OE1 . GLU A 379 ? 1.0812 1.3638 1.0432 -0.0262 0.0453  -0.0830 379 GLU A OE1 
3215  O OE2 . GLU A 379 ? 1.1142 1.4333 1.0581 -0.0507 0.0394  -0.0621 379 GLU A OE2 
3216  N N   . TRP A 380 ? 0.6800 0.8793 0.6720 0.0216  0.0444  -0.1380 380 TRP A N   
3217  C CA  . TRP A 380 ? 0.7144 0.9038 0.7211 0.0320  0.0450  -0.1333 380 TRP A CA  
3218  C C   . TRP A 380 ? 0.6785 0.8405 0.6867 0.0291  0.0398  -0.1126 380 TRP A C   
3219  O O   . TRP A 380 ? 0.5968 0.7528 0.6131 0.0343  0.0393  -0.1066 380 TRP A O   
3220  C CB  . TRP A 380 ? 0.6778 0.8530 0.7004 0.0482  0.0451  -0.1512 380 TRP A CB  
3221  C CG  . TRP A 380 ? 0.6117 0.7523 0.6368 0.0507  0.0390  -0.1548 380 TRP A CG  
3222  C CD1 . TRP A 380 ? 0.5870 0.7240 0.6043 0.0457  0.0377  -0.1681 380 TRP A CD1 
3223  C CD2 . TRP A 380 ? 0.6991 0.8064 0.7352 0.0567  0.0328  -0.1440 380 TRP A CD2 
3224  N NE1 . TRP A 380 ? 0.6512 0.7528 0.6764 0.0484  0.0308  -0.1659 380 TRP A NE1 
3225  C CE2 . TRP A 380 ? 0.7208 0.8045 0.7576 0.0553  0.0281  -0.1503 380 TRP A CE2 
3226  C CE3 . TRP A 380 ? 0.6794 0.7771 0.7237 0.0615  0.0303  -0.1292 380 TRP A CE3 
3227  C CZ2 . TRP A 380 ? 0.6874 0.7386 0.7343 0.0589  0.0217  -0.1404 380 TRP A CZ2 
3228  C CZ3 . TRP A 380 ? 0.7385 0.8056 0.7899 0.0649  0.0242  -0.1201 380 TRP A CZ3 
3229  C CH2 . TRP A 380 ? 0.7305 0.7750 0.7841 0.0638  0.0203  -0.1249 380 TRP A CH2 
3230  N N   . ILE A 381 ? 0.6927 0.8405 0.6941 0.0206  0.0362  -0.1021 381 ILE A N   
3231  C CA  . ILE A 381 ? 0.6654 0.7903 0.6688 0.0175  0.0338  -0.0842 381 ILE A CA  
3232  C C   . ILE A 381 ? 0.6079 0.7462 0.6064 0.0050  0.0348  -0.0689 381 ILE A C   
3233  O O   . ILE A 381 ? 0.6720 0.8237 0.6646 -0.0031 0.0332  -0.0663 381 ILE A O   
3234  C CB  . ILE A 381 ? 0.6566 0.7532 0.6630 0.0194  0.0295  -0.0823 381 ILE A CB  
3235  C CG1 . ILE A 381 ? 0.7187 0.8032 0.7321 0.0299  0.0272  -0.0979 381 ILE A CG1 
3236  C CG2 . ILE A 381 ? 0.6431 0.7180 0.6529 0.0193  0.0296  -0.0678 381 ILE A CG2 
3237  C CD1 . ILE A 381 ? 0.6396 0.7016 0.6558 0.0283  0.0220  -0.0978 381 ILE A CD1 
3238  N N   . GLU A 382 ? 0.5285 0.6631 0.5302 0.0024  0.0367  -0.0581 382 GLU A N   
3239  C CA  . GLU A 382 ? 0.5782 0.7174 0.5813 -0.0086 0.0373  -0.0416 382 GLU A CA  
3240  C C   . GLU A 382 ? 0.6098 0.7186 0.6192 -0.0076 0.0378  -0.0326 382 GLU A C   
3241  O O   . GLU A 382 ? 0.5891 0.6853 0.5990 -0.0039 0.0397  -0.0355 382 GLU A O   
3242  C CB  . GLU A 382 ? 0.5961 0.7578 0.5997 -0.0145 0.0398  -0.0383 382 GLU A CB  
3243  C CG  . GLU A 382 ? 0.6283 0.7925 0.6374 -0.0266 0.0397  -0.0196 382 GLU A CG  
3244  C CD  . GLU A 382 ? 0.8487 1.0386 0.8594 -0.0348 0.0414  -0.0152 382 GLU A CD  
3245  O OE1 . GLU A 382 ? 0.9305 1.1421 0.9375 -0.0309 0.0434  -0.0270 382 GLU A OE1 
3246  O OE2 . GLU A 382 ? 0.9688 1.1571 0.9874 -0.0451 0.0408  0.0009  382 GLU A OE2 
3247  N N   . THR A 383 ? 0.5176 0.6173 0.5321 -0.0110 0.0364  -0.0222 383 THR A N   
3248  C CA  . THR A 383 ? 0.5281 0.6031 0.5519 -0.0102 0.0394  -0.0135 383 THR A CA  
3249  C C   . THR A 383 ? 0.5601 0.6347 0.5908 -0.0169 0.0426  -0.0045 383 THR A C   
3250  O O   . THR A 383 ? 0.6400 0.7335 0.6736 -0.0249 0.0406  0.0046  383 THR A O   
3251  C CB  . THR A 383 ? 0.6429 0.7122 0.6756 -0.0117 0.0372  -0.0032 383 THR A CB  
3252  O OG1 . THR A 383 ? 0.6197 0.7121 0.6537 -0.0202 0.0325  0.0068  383 THR A OG1 
3253  C CG2 . THR A 383 ? 0.6111 0.6723 0.6397 -0.0058 0.0343  -0.0121 383 THR A CG2 
3254  N N   . LEU A 384 ? 0.5051 0.5585 0.5386 -0.0148 0.0474  -0.0070 384 LEU A N   
3255  C CA  . LEU A 384 ? 0.5334 0.5815 0.5740 -0.0216 0.0506  -0.0025 384 LEU A CA  
3256  C C   . LEU A 384 ? 0.5752 0.5972 0.6290 -0.0202 0.0569  0.0013  384 LEU A C   
3257  O O   . LEU A 384 ? 0.5643 0.5736 0.6173 -0.0134 0.0601  -0.0026 384 LEU A O   
3258  C CB  . LEU A 384 ? 0.5309 0.5817 0.5606 -0.0225 0.0510  -0.0141 384 LEU A CB  
3259  C CG  . LEU A 384 ? 0.5529 0.6326 0.5765 -0.0251 0.0468  -0.0167 384 LEU A CG  
3260  C CD1 . LEU A 384 ? 0.5012 0.5828 0.5170 -0.0236 0.0462  -0.0273 384 LEU A CD1 
3261  C CD2 . LEU A 384 ? 0.6701 0.7661 0.7020 -0.0361 0.0458  -0.0049 384 LEU A CD2 
3262  N N   . THR A 385 ? 0.5320 0.5469 0.6006 -0.0266 0.0592  0.0091  385 THR A N   
3263  C CA  . THR A 385 ? 0.4522 0.4402 0.5343 -0.0248 0.0676  0.0069  385 THR A CA  
3264  C C   . THR A 385 ? 0.5446 0.5212 0.6128 -0.0274 0.0719  -0.0101 385 THR A C   
3265  O O   . THR A 385 ? 0.5512 0.5415 0.6058 -0.0324 0.0671  -0.0154 385 THR A O   
3266  C CB  . THR A 385 ? 0.4624 0.4431 0.5715 -0.0301 0.0682  0.0222  385 THR A CB  
3267  O OG1 . THR A 385 ? 0.5176 0.4977 0.6263 -0.0399 0.0670  0.0201  385 THR A OG1 
3268  C CG2 . THR A 385 ? 0.4545 0.4565 0.5737 -0.0324 0.0602  0.0425  385 THR A CG2 
3269  N N   . LEU A 386 ? 0.6086 0.5623 0.6811 -0.0245 0.0814  -0.0190 386 LEU A N   
3270  C CA  . LEU A 386 ? 0.5637 0.5066 0.6217 -0.0295 0.0857  -0.0362 386 LEU A CA  
3271  C C   . LEU A 386 ? 0.6542 0.5965 0.7178 -0.0410 0.0823  -0.0362 386 LEU A C   
3272  O O   . LEU A 386 ? 0.7298 0.6765 0.7766 -0.0481 0.0798  -0.0474 386 LEU A O   
3273  C CB  . LEU A 386 ? 0.5998 0.5193 0.6637 -0.0255 0.0987  -0.0467 386 LEU A CB  
3274  C CG  . LEU A 386 ? 0.5611 0.4824 0.6240 -0.0152 0.1032  -0.0441 386 LEU A CG  
3275  C CD1 . LEU A 386 ? 0.6263 0.5277 0.7028 -0.0111 0.1181  -0.0525 386 LEU A CD1 
3276  C CD2 . LEU A 386 ? 0.4983 0.4320 0.5329 -0.0143 0.0991  -0.0505 386 LEU A CD2 
3277  N N   . GLU A 387 ? 0.5737 0.5123 0.6621 -0.0442 0.0811  -0.0217 387 GLU A N   
3278  C CA  . GLU A 387 ? 0.5313 0.4705 0.6277 -0.0569 0.0769  -0.0184 387 GLU A CA  
3279  C C   . GLU A 387 ? 0.6210 0.5931 0.7036 -0.0621 0.0669  -0.0119 387 GLU A C   
3280  O O   . GLU A 387 ? 0.6753 0.6549 0.7495 -0.0716 0.0635  -0.0185 387 GLU A O   
3281  C CB  . GLU A 387 ? 0.5310 0.4572 0.6612 -0.0591 0.0776  -0.0009 387 GLU A CB  
3282  C CG  . GLU A 387 ? 0.7019 0.6395 0.8423 -0.0727 0.0697  0.0128  387 GLU A CG  
3283  C CD  . GLU A 387 ? 0.9035 0.8114 1.0748 -0.0795 0.0731  0.0168  387 GLU A CD  
3284  O OE1 . GLU A 387 ? 1.0940 1.0008 1.2682 -0.0933 0.0690  0.0166  387 GLU A OE1 
3285  O OE2 . GLU A 387 ? 0.7904 0.6759 0.9857 -0.0711 0.0797  0.0203  387 GLU A OE2 
3286  N N   . GLU A 388 ? 0.6093 0.6032 0.6900 -0.0562 0.0625  -0.0002 388 GLU A N   
3287  C CA  . GLU A 388 ? 0.5613 0.5883 0.6291 -0.0592 0.0555  0.0023  388 GLU A CA  
3288  C C   . GLU A 388 ? 0.5147 0.5484 0.5615 -0.0560 0.0547  -0.0144 388 GLU A C   
3289  O O   . GLU A 388 ? 0.5338 0.5890 0.5751 -0.0618 0.0503  -0.0161 388 GLU A O   
3290  C CB  . GLU A 388 ? 0.4639 0.5105 0.5308 -0.0532 0.0523  0.0127  388 GLU A CB  
3291  C CG  . GLU A 388 ? 0.5365 0.5855 0.6234 -0.0582 0.0503  0.0337  388 GLU A CG  
3292  C CD  . GLU A 388 ? 0.6183 0.6876 0.7009 -0.0540 0.0463  0.0421  388 GLU A CD  
3293  O OE1 . GLU A 388 ? 0.5422 0.6100 0.6121 -0.0445 0.0471  0.0305  388 GLU A OE1 
3294  O OE2 . GLU A 388 ? 0.7192 0.8068 0.8112 -0.0616 0.0416  0.0609  388 GLU A OE2 
3295  N N   . ALA A 389 ? 0.5834 0.6020 0.6201 -0.0471 0.0583  -0.0248 389 ALA A N   
3296  C CA  . ALA A 389 ? 0.6147 0.6402 0.6332 -0.0450 0.0561  -0.0370 389 ALA A CA  
3297  C C   . ALA A 389 ? 0.5967 0.6167 0.6110 -0.0564 0.0558  -0.0456 389 ALA A C   
3298  O O   . ALA A 389 ? 0.6501 0.6869 0.6535 -0.0590 0.0505  -0.0509 389 ALA A O   
3299  C CB  . ALA A 389 ? 0.5044 0.5159 0.5134 -0.0353 0.0598  -0.0432 389 ALA A CB  
3300  N N   . MET A 390 ? 0.6138 0.6107 0.6389 -0.0637 0.0610  -0.0471 390 MET A N   
3301  C CA  . MET A 390 ? 0.5900 0.5792 0.6112 -0.0768 0.0605  -0.0578 390 MET A CA  
3302  C C   . MET A 390 ? 0.6519 0.6636 0.6806 -0.0880 0.0528  -0.0497 390 MET A C   
3303  O O   . MET A 390 ? 0.7497 0.7740 0.7687 -0.0968 0.0476  -0.0568 390 MET A O   
3304  C CB  . MET A 390 ? 0.6911 0.6461 0.7254 -0.0807 0.0694  -0.0642 390 MET A CB  
3305  C CG  . MET A 390 ? 0.8078 0.7442 0.8288 -0.0745 0.0784  -0.0797 390 MET A CG  
3306  S SD  . MET A 390 ? 0.8571 0.8051 0.8453 -0.0828 0.0743  -0.0971 390 MET A SD  
3307  C CE  . MET A 390 ? 0.7662 0.6904 0.7591 -0.1009 0.0779  -0.1141 390 MET A CE  
3308  N N   . ARG A 391 ? 0.6473 0.6681 0.6930 -0.0888 0.0515  -0.0334 391 ARG A N   
3309  C CA  . ARG A 391 ? 0.6438 0.6882 0.6986 -0.1011 0.0455  -0.0233 391 ARG A CA  
3310  C C   . ARG A 391 ? 0.6167 0.7015 0.6633 -0.0961 0.0408  -0.0197 391 ARG A C   
3311  O O   . ARG A 391 ? 0.7341 0.8449 0.7867 -0.1061 0.0366  -0.0132 391 ARG A O   
3312  C CB  . ARG A 391 ? 0.5978 0.6371 0.6756 -0.1065 0.0461  -0.0046 391 ARG A CB  
3313  C CG  . ARG A 391 ? 0.6251 0.6232 0.7195 -0.1084 0.0517  -0.0062 391 ARG A CG  
3314  C CD  . ARG A 391 ? 0.6421 0.6201 0.7381 -0.1219 0.0519  -0.0201 391 ARG A CD  
3315  N NE  . ARG A 391 ? 0.7246 0.6651 0.8195 -0.1171 0.0606  -0.0381 391 ARG A NE  
3316  C CZ  . ARG A 391 ? 0.6901 0.6239 0.7627 -0.1181 0.0630  -0.0604 391 ARG A CZ  
3317  N NH1 . ARG A 391 ? 0.6766 0.6372 0.7284 -0.1230 0.0558  -0.0655 391 ARG A NH1 
3318  N NH2 . ARG A 391 ? 0.7291 0.6310 0.8010 -0.1144 0.0730  -0.0772 391 ARG A NH2 
3319  N N   . LYS A 392 ? 0.5679 0.6585 0.6033 -0.0812 0.0418  -0.0241 392 LYS A N   
3320  C CA  . LYS A 392 ? 0.5682 0.6940 0.5998 -0.0743 0.0388  -0.0228 392 LYS A CA  
3321  C C   . LYS A 392 ? 0.7899 0.9362 0.8177 -0.0782 0.0338  -0.0295 392 LYS A C   
3322  O O   . LYS A 392 ? 0.7959 0.9292 0.8138 -0.0776 0.0319  -0.0389 392 LYS A O   
3323  C CB  . LYS A 392 ? 0.5865 0.7075 0.6096 -0.0581 0.0405  -0.0277 392 LYS A CB  
3324  C CG  . LYS A 392 ? 0.6728 0.8244 0.6971 -0.0510 0.0399  -0.0254 392 LYS A CG  
3325  C CD  . LYS A 392 ? 0.6280 0.7761 0.6551 -0.0499 0.0422  -0.0168 392 LYS A CD  
3326  C CE  . LYS A 392 ? 0.6751 0.8604 0.7034 -0.0518 0.0423  -0.0122 392 LYS A CE  
3327  N NZ  . LYS A 392 ? 0.7361 0.9220 0.7657 -0.0546 0.0427  -0.0010 392 LYS A NZ  
3328  N N   . GLU A 393 ? 0.6420 0.8243 0.6781 -0.0826 0.0317  -0.0235 393 GLU A N   
3329  C CA  . GLU A 393 ? 0.5942 0.8029 0.6319 -0.0855 0.0264  -0.0273 393 GLU A CA  
3330  C C   . GLU A 393 ? 0.6078 0.8412 0.6458 -0.0688 0.0260  -0.0320 393 GLU A C   
3331  O O   . GLU A 393 ? 0.7221 0.9818 0.7663 -0.0685 0.0215  -0.0334 393 GLU A O   
3332  C CB  . GLU A 393 ? 0.6822 0.9185 0.7334 -0.1015 0.0247  -0.0177 393 GLU A CB  
3333  C CG  . GLU A 393 ? 0.8522 1.0795 0.9051 -0.1190 0.0188  -0.0198 393 GLU A CG  
3334  C CD  . GLU A 393 ? 0.8098 1.0493 0.8563 -0.1164 0.0122  -0.0287 393 GLU A CD  
3335  O OE1 . GLU A 393 ? 0.9229 1.1911 0.9730 -0.1032 0.0111  -0.0288 393 GLU A OE1 
3336  O OE2 . GLU A 393 ? 0.6356 0.8562 0.6741 -0.1278 0.0077  -0.0356 393 GLU A OE2 
3337  N N   . ASP A 394 ? 0.5893 0.8146 0.6233 -0.0552 0.0301  -0.0345 394 ASP A N   
3338  C CA  . ASP A 394 ? 0.5396 0.7809 0.5762 -0.0386 0.0300  -0.0412 394 ASP A CA  
3339  C C   . ASP A 394 ? 0.6280 0.8438 0.6566 -0.0288 0.0265  -0.0465 394 ASP A C   
3340  O O   . ASP A 394 ? 0.6104 0.8312 0.6432 -0.0141 0.0258  -0.0510 394 ASP A O   
3341  C CB  . ASP A 394 ? 0.7152 0.9637 0.7517 -0.0311 0.0359  -0.0425 394 ASP A CB  
3342  C CG  . ASP A 394 ? 0.7724 1.0396 0.8118 -0.0442 0.0393  -0.0331 394 ASP A CG  
3343  O OD1 . ASP A 394 ? 0.7990 1.0447 0.8360 -0.0552 0.0390  -0.0242 394 ASP A OD1 
3344  O OD2 . ASP A 394 ? 0.7383 1.0427 0.7837 -0.0434 0.0429  -0.0340 394 ASP A OD2 
3345  N N   . VAL A 395 ? 0.6659 0.8552 0.6839 -0.0370 0.0247  -0.0462 395 VAL A N   
3346  C CA  . VAL A 395 ? 0.7073 0.8750 0.7148 -0.0308 0.0221  -0.0494 395 VAL A CA  
3347  C C   . VAL A 395 ? 0.5576 0.7365 0.5617 -0.0391 0.0146  -0.0494 395 VAL A C   
3348  O O   . VAL A 395 ? 0.5732 0.7507 0.5738 -0.0547 0.0137  -0.0503 395 VAL A O   
3349  C CB  . VAL A 395 ? 0.6895 0.8216 0.6861 -0.0339 0.0276  -0.0506 395 VAL A CB  
3350  C CG1 . VAL A 395 ? 0.6018 0.7169 0.5843 -0.0346 0.0255  -0.0540 395 VAL A CG1 
3351  C CG2 . VAL A 395 ? 0.6589 0.7815 0.6586 -0.0234 0.0321  -0.0493 395 VAL A CG2 
3352  N N   . LYS A 396 ? 0.5054 0.6957 0.5121 -0.0297 0.0082  -0.0478 396 LYS A N   
3353  C CA  . LYS A 396 ? 0.5508 0.7581 0.5553 -0.0380 -0.0013 -0.0451 396 LYS A CA  
3354  C C   . LYS A 396 ? 0.5698 0.7530 0.5511 -0.0507 -0.0017 -0.0491 396 LYS A C   
3355  O O   . LYS A 396 ? 0.7000 0.8569 0.6694 -0.0461 0.0033  -0.0513 396 LYS A O   
3356  C CB  . LYS A 396 ? 0.5406 0.7652 0.5568 -0.0238 -0.0089 -0.0389 396 LYS A CB  
3357  C CG  . LYS A 396 ? 0.4913 0.7440 0.5336 -0.0106 -0.0079 -0.0381 396 LYS A CG  
3358  C CD  . LYS A 396 ? 0.5227 0.7964 0.5725 -0.0203 -0.0032 -0.0402 396 LYS A CD  
3359  C CE  . LYS A 396 ? 0.4336 0.7433 0.5095 -0.0080 -0.0016 -0.0402 396 LYS A CE  
3360  N NZ  . LYS A 396 ? 0.4295 0.7589 0.5092 -0.0193 0.0046  -0.0408 396 LYS A NZ  
3361  N N   . THR A 397 ? 0.4447 0.6962 0.6897 0.2216  0.0210  0.0612  397 THR A N   
3362  C CA  . THR A 397 ? 0.4336 0.6804 0.6897 0.1933  0.0157  0.0572  397 THR A CA  
3363  C C   . THR A 397 ? 0.5835 0.8575 0.8687 0.1803  0.0003  0.0499  397 THR A C   
3364  O O   . THR A 397 ? 0.5111 0.8182 0.8270 0.1847  0.0057  0.0495  397 THR A O   
3365  C CB  . THR A 397 ? 0.4531 0.6999 0.7256 0.1791  0.0421  0.0634  397 THR A CB  
3366  O OG1 . THR A 397 ? 0.5200 0.7449 0.7639 0.1975  0.0584  0.0719  397 THR A OG1 
3367  C CG2 . THR A 397 ? 0.4030 0.6361 0.6765 0.1535  0.0353  0.0581  397 THR A CG2 
3368  N N   . GLU A 398 ? 0.5367 0.7976 0.8112 0.1660  -0.0190 0.0436  398 GLU A N   
3369  C CA  . GLU A 398 ? 0.4752 0.7580 0.7702 0.1544  -0.0356 0.0362  398 GLU A CA  
3370  C C   . GLU A 398 ? 0.5132 0.7887 0.8127 0.1282  -0.0367 0.0314  398 GLU A C   
3371  O O   . GLU A 398 ? 0.4995 0.7461 0.7763 0.1220  -0.0325 0.0334  398 GLU A O   
3372  C CB  . GLU A 398 ? 0.5631 0.8340 0.8328 0.1679  -0.0604 0.0338  398 GLU A CB  
3373  C CG  . GLU A 398 ? 0.7206 1.0165 1.0032 0.1890  -0.0656 0.0336  398 GLU A CG  
3374  C CD  . GLU A 398 ? 0.8519 1.1355 1.1119 0.2007  -0.0908 0.0313  398 GLU A CD  
3375  O OE1 . GLU A 398 ? 0.9340 1.2254 1.1922 0.2234  -0.0961 0.0319  398 GLU A OE1 
3376  O OE2 . GLU A 398 ? 0.8851 1.1493 1.1273 0.1881  -0.1040 0.0294  398 GLU A OE2 
3377  N N   . VAL A 399 ? 0.5240 0.8272 0.8535 0.1139  -0.0432 0.0235  399 VAL A N   
3378  C CA  . VAL A 399 ? 0.4848 0.7826 0.8183 0.0902  -0.0461 0.0167  399 VAL A CA  
3379  C C   . VAL A 399 ? 0.4926 0.7871 0.8071 0.0894  -0.0725 0.0107  399 VAL A C   
3380  O O   . VAL A 399 ? 0.3979 0.7142 0.7204 0.1001  -0.0873 0.0074  399 VAL A O   
3381  C CB  . VAL A 399 ? 0.4283 0.7569 0.8094 0.0725  -0.0330 0.0099  399 VAL A CB  
3382  C CG1 . VAL A 399 ? 0.5492 0.9206 0.9654 0.0801  -0.0393 0.0043  399 VAL A CG1 
3383  C CG2 . VAL A 399 ? 0.4985 0.8230 0.8821 0.0500  -0.0413 -0.0005 399 VAL A CG2 
3384  N N   . ILE A 400 ? 0.5328 0.7986 0.8195 0.0789  -0.0774 0.0101  400 ILE A N   
3385  C CA  . ILE A 400 ? 0.4738 0.7310 0.7376 0.0765  -0.0985 0.0062  400 ILE A CA  
3386  C C   . ILE A 400 ? 0.4725 0.7326 0.7438 0.0545  -0.0986 -0.0029 400 ILE A C   
3387  O O   . ILE A 400 ? 0.4701 0.7263 0.7551 0.0412  -0.0820 -0.0043 400 ILE A O   
3388  C CB  . ILE A 400 ? 0.4317 0.6506 0.6537 0.0849  -0.1038 0.0135  400 ILE A CB  
3389  C CG1 . ILE A 400 ? 0.5030 0.6973 0.7136 0.0733  -0.0903 0.0148  400 ILE A CG1 
3390  C CG2 . ILE A 400 ? 0.4542 0.6686 0.6692 0.1071  -0.1043 0.0200  400 ILE A CG2 
3391  C CD1 . ILE A 400 ? 0.5045 0.6676 0.6856 0.0835  -0.0911 0.0204  400 ILE A CD1 
3392  N N   . GLU A 401 ? 0.3850 0.6501 0.6446 0.0523  -0.1175 -0.0090 401 GLU A N   
3393  C CA  . GLU A 401 ? 0.4579 0.7309 0.7253 0.0339  -0.1209 -0.0206 401 GLU A CA  
3394  C C   . GLU A 401 ? 0.5317 0.7737 0.7595 0.0277  -0.1261 -0.0191 401 GLU A C   
3395  O O   . GLU A 401 ? 0.4597 0.7005 0.6901 0.0117  -0.1233 -0.0277 401 GLU A O   
3396  C CB  . GLU A 401 ? 0.5892 0.8994 0.8777 0.0362  -0.1390 -0.0326 401 GLU A CB  
3397  C CG  . GLU A 401 ? 0.6002 0.9389 0.9310 0.0171  -0.1345 -0.0486 401 GLU A CG  
3398  C CD  . GLU A 401 ? 0.6028 0.9630 0.9799 0.0135  -0.1151 -0.0482 401 GLU A CD  
3399  O OE1 . GLU A 401 ? 0.5621 0.9360 0.9480 0.0298  -0.1149 -0.0415 401 GLU A OE1 
3400  O OE2 . GLU A 401 ? 0.6179 0.9790 1.0212 -0.0049 -0.0988 -0.0539 401 GLU A OE2 
3401  N N   . SER A 402 ? 0.6585 0.8747 0.8511 0.0395  -0.1320 -0.0090 402 SER A N   
3402  C CA  . SER A 402 ? 0.6147 0.8032 0.7713 0.0335  -0.1355 -0.0071 402 SER A CA  
3403  C C   . SER A 402 ? 0.5635 0.7191 0.6956 0.0402  -0.1293 0.0042  402 SER A C   
3404  O O   . SER A 402 ? 0.5169 0.6704 0.6541 0.0528  -0.1270 0.0100  402 SER A O   
3405  C CB  . SER A 402 ? 0.5225 0.7159 0.6577 0.0400  -0.1549 -0.0093 402 SER A CB  
3406  O OG  . SER A 402 ? 0.6247 0.8016 0.7356 0.0576  -0.1632 0.0016  402 SER A OG  
3407  N N   . VAL A 403 ? 0.5984 0.7299 0.7056 0.0312  -0.1264 0.0055  403 VAL A N   
3408  C CA  . VAL A 403 ? 0.5765 0.6769 0.6601 0.0349  -0.1229 0.0138  403 VAL A CA  
3409  C C   . VAL A 403 ? 0.6689 0.7509 0.7210 0.0293  -0.1275 0.0161  403 VAL A C   
3410  O O   . VAL A 403 ? 0.6736 0.7659 0.7214 0.0215  -0.1308 0.0101  403 VAL A O   
3411  C CB  . VAL A 403 ? 0.6256 0.7157 0.7177 0.0283  -0.1078 0.0125  403 VAL A CB  
3412  C CG1 . VAL A 403 ? 0.5191 0.6209 0.6333 0.0385  -0.1023 0.0133  403 VAL A CG1 
3413  C CG2 . VAL A 403 ? 0.6699 0.7654 0.7684 0.0122  -0.0998 0.0048  403 VAL A CG2 
3414  N N   . LYS A 404 ? 0.7181 0.7719 0.7480 0.0339  -0.1270 0.0247  404 LYS A N   
3415  C CA  . LYS A 404 ? 0.6476 0.6778 0.6464 0.0278  -0.1256 0.0296  404 LYS A CA  
3416  C C   . LYS A 404 ? 0.7345 0.7490 0.7357 0.0151  -0.1110 0.0280  404 LYS A C   
3417  O O   . LYS A 404 ? 0.7082 0.7125 0.7191 0.0181  -0.1067 0.0289  404 LYS A O   
3418  C CB  . LYS A 404 ? 0.6785 0.6849 0.6518 0.0409  -0.1332 0.0410  404 LYS A CB  
3419  C CG  . LYS A 404 ? 0.7259 0.7434 0.6839 0.0533  -0.1484 0.0431  404 LYS A CG  
3420  C CD  . LYS A 404 ? 0.8272 0.8564 0.7730 0.0445  -0.1500 0.0371  404 LYS A CD  
3421  C CE  . LYS A 404 ? 0.9086 0.9457 0.8319 0.0598  -0.1672 0.0389  404 LYS A CE  
3422  N NZ  . LYS A 404 ? 0.9063 0.9091 0.7940 0.0739  -0.1700 0.0545  404 LYS A NZ  
3423  N N   . ALA A 405 ? 0.7289 0.7431 0.7214 0.0023  -0.1043 0.0241  405 ALA A N   
3424  C CA  . ALA A 405 ? 0.7306 0.7373 0.7306 -0.0094 -0.0906 0.0198  405 ALA A CA  
3425  C C   . ALA A 405 ? 0.7306 0.7108 0.7212 -0.0102 -0.0849 0.0263  405 ALA A C   
3426  O O   . ALA A 405 ? 0.9273 0.8874 0.8934 -0.0087 -0.0862 0.0354  405 ALA A O   
3427  C CB  . ALA A 405 ? 0.7228 0.7335 0.7117 -0.0212 -0.0849 0.0145  405 ALA A CB  
3428  N N   . GLY A 406 ? 0.6493 0.6285 0.6594 -0.0120 -0.0788 0.0210  406 GLY A N   
3429  C CA  . GLY A 406 ? 0.7035 0.6606 0.7122 -0.0152 -0.0733 0.0230  406 GLY A CA  
3430  C C   . GLY A 406 ? 0.7253 0.6891 0.7585 -0.0163 -0.0685 0.0127  406 GLY A C   
3431  O O   . GLY A 406 ? 0.7288 0.7109 0.7750 -0.0168 -0.0656 0.0054  406 GLY A O   
3432  N N   . THR A 407 ? 0.6369 0.5845 0.6758 -0.0158 -0.0679 0.0114  407 THR A N   
3433  C CA  . THR A 407 ? 0.6222 0.5761 0.6835 -0.0147 -0.0660 -0.0006 407 THR A CA  
3434  C C   . THR A 407 ? 0.6282 0.5685 0.6943 -0.0040 -0.0742 -0.0019 407 THR A C   
3435  O O   . THR A 407 ? 0.6284 0.5530 0.6804 0.0018  -0.0800 0.0073  407 THR A O   
3436  C CB  . THR A 407 ? 0.6555 0.6071 0.7254 -0.0302 -0.0545 -0.0072 407 THR A CB  
3437  O OG1 . THR A 407 ? 0.6714 0.5989 0.7293 -0.0400 -0.0491 0.0009  407 THR A OG1 
3438  C CG2 . THR A 407 ? 0.5964 0.5639 0.6637 -0.0379 -0.0466 -0.0091 407 THR A CG2 
3439  N N   . TRP A 408 ? 0.5793 0.5252 0.6643 0.0002  -0.0757 -0.0145 408 TRP A N   
3440  C CA  . TRP A 408 ? 0.6092 0.5411 0.6989 0.0103  -0.0842 -0.0187 408 TRP A CA  
3441  C C   . TRP A 408 ? 0.6116 0.5187 0.7048 -0.0033 -0.0799 -0.0198 408 TRP A C   
3442  O O   . TRP A 408 ? 0.6246 0.5151 0.7230 0.0026  -0.0865 -0.0247 408 TRP A O   
3443  C CB  . TRP A 408 ? 0.5571 0.5049 0.6625 0.0240  -0.0898 -0.0330 408 TRP A CB  
3444  C CG  . TRP A 408 ? 0.5492 0.5113 0.6725 0.0171  -0.0848 -0.0468 408 TRP A CG  
3445  C CD1 . TRP A 408 ? 0.6381 0.6017 0.7687 -0.0016 -0.0745 -0.0486 408 TRP A CD1 
3446  C CD2 . TRP A 408 ? 0.5177 0.4958 0.6532 0.0314  -0.0901 -0.0612 408 TRP A CD2 
3447  N NE1 . TRP A 408 ? 0.4727 0.4541 0.6223 -0.0003 -0.0736 -0.0641 408 TRP A NE1 
3448  C CE2 . TRP A 408 ? 0.5620 0.5519 0.7135 0.0206  -0.0840 -0.0720 408 TRP A CE2 
3449  C CE3 . TRP A 408 ? 0.5086 0.4924 0.6407 0.0542  -0.0992 -0.0659 408 TRP A CE3 
3450  C CZ2 . TRP A 408 ? 0.6415 0.6492 0.8059 0.0329  -0.0885 -0.0878 408 TRP A CZ2 
3451  C CZ3 . TRP A 408 ? 0.5819 0.5810 0.7232 0.0667  -0.1028 -0.0806 408 TRP A CZ3 
3452  C CH2 . TRP A 408 ? 0.5562 0.5672 0.7135 0.0565  -0.0984 -0.0917 408 TRP A CH2 
3453  N N   . PHE A 409 ? 0.6486 0.5509 0.7383 -0.0211 -0.0678 -0.0150 409 PHE A N   
3454  C CA  . PHE A 409 ? 0.7303 0.6072 0.8222 -0.0367 -0.0585 -0.0129 409 PHE A CA  
3455  C C   . PHE A 409 ? 0.8048 0.6584 0.8646 -0.0376 -0.0553 0.0071  409 PHE A C   
3456  O O   . PHE A 409 ? 0.7150 0.5713 0.7591 -0.0460 -0.0462 0.0158  409 PHE A O   
3457  C CB  . PHE A 409 ? 0.6076 0.4978 0.7176 -0.0542 -0.0450 -0.0214 409 PHE A CB  
3458  C CG  . PHE A 409 ? 0.6854 0.5546 0.8102 -0.0716 -0.0337 -0.0242 409 PHE A CG  
3459  C CD1 . PHE A 409 ? 0.8107 0.6452 0.9147 -0.0788 -0.0254 -0.0079 409 PHE A CD1 
3460  C CD2 . PHE A 409 ? 0.8110 0.6956 0.9718 -0.0806 -0.0304 -0.0435 409 PHE A CD2 
3461  C CE1 . PHE A 409 ? 0.7971 0.6094 0.9164 -0.0965 -0.0116 -0.0094 409 PHE A CE1 
3462  C CE2 . PHE A 409 ? 0.8179 0.6855 0.9986 -0.0990 -0.0183 -0.0476 409 PHE A CE2 
3463  C CZ  . PHE A 409 ? 0.8745 0.7043 1.0347 -0.1080 -0.0075 -0.0298 409 PHE A CZ  
3464  N N   . ASP A 410 ? 0.8303 0.6612 0.8785 -0.0264 -0.0640 0.0137  410 ASP A N   
3465  C CA  . ASP A 410 ? 0.7876 0.5928 0.8033 -0.0219 -0.0639 0.0323  410 ASP A CA  
3466  C C   . ASP A 410 ? 0.7855 0.6107 0.7807 -0.0125 -0.0699 0.0409  410 ASP A C   
3467  O O   . ASP A 410 ? 0.8400 0.6489 0.8060 -0.0090 -0.0696 0.0554  410 ASP A O   
3468  C CB  . ASP A 410 ? 0.8235 0.6002 0.8270 -0.0391 -0.0468 0.0424  410 ASP A CB  
3469  C CG  . ASP A 410 ? 0.9837 0.7369 1.0101 -0.0508 -0.0396 0.0345  410 ASP A CG  
3470  O OD1 . ASP A 410 ? 1.0191 0.7606 1.0550 -0.0406 -0.0506 0.0279  410 ASP A OD1 
3471  O OD2 . ASP A 410 ? 1.0567 0.8040 1.0931 -0.0703 -0.0224 0.0337  410 ASP A OD2 
3472  N N   . GLY A 411 ? 0.7774 0.6366 0.7868 -0.0076 -0.0751 0.0319  411 GLY A N   
3473  C CA  . GLY A 411 ? 0.7557 0.6349 0.7516 -0.0010 -0.0804 0.0375  411 GLY A CA  
3474  C C   . GLY A 411 ? 0.7955 0.6773 0.7752 -0.0132 -0.0712 0.0425  411 GLY A C   
3475  O O   . GLY A 411 ? 0.7895 0.6853 0.7557 -0.0080 -0.0769 0.0462  411 GLY A O   
3476  N N   . ASN A 412 ? 0.7317 0.6019 0.7135 -0.0289 -0.0572 0.0414  412 ASN A N   
3477  C CA  . ASN A 412 ? 0.6826 0.5547 0.6475 -0.0398 -0.0464 0.0455  412 ASN A CA  
3478  C C   . ASN A 412 ? 0.6701 0.5575 0.6592 -0.0538 -0.0346 0.0331  412 ASN A C   
3479  O O   . ASN A 412 ? 0.6893 0.5825 0.7065 -0.0551 -0.0350 0.0222  412 ASN A O   
3480  C CB  . ASN A 412 ? 0.7845 0.6219 0.7189 -0.0433 -0.0375 0.0610  412 ASN A CB  
3481  C CG  . ASN A 412 ? 0.7066 0.5174 0.6551 -0.0530 -0.0269 0.0612  412 ASN A CG  
3482  O OD1 . ASN A 412 ? 0.8453 0.6638 0.8187 -0.0674 -0.0154 0.0512  412 ASN A OD1 
3483  N ND2 . ASN A 412 ? 0.6838 0.4633 0.6181 -0.0450 -0.0308 0.0715  412 ASN A ND2 
3484  N N   . PHE A 413 ? 0.6916 0.5867 0.6686 -0.0623 -0.0250 0.0338  413 PHE A N   
3485  C CA  . PHE A 413 ? 0.6641 0.5751 0.6609 -0.0744 -0.0130 0.0224  413 PHE A CA  
3486  C C   . PHE A 413 ? 0.6731 0.5663 0.6686 -0.0893 0.0056  0.0264  413 PHE A C   
3487  O O   . PHE A 413 ? 0.6570 0.5628 0.6607 -0.0996 0.0184  0.0197  413 PHE A O   
3488  C CB  . PHE A 413 ? 0.6532 0.5844 0.6397 -0.0744 -0.0127 0.0187  413 PHE A CB  
3489  C CG  . PHE A 413 ? 0.7147 0.6636 0.7058 -0.0627 -0.0278 0.0146  413 PHE A CG  
3490  C CD1 . PHE A 413 ? 0.7148 0.6610 0.6848 -0.0534 -0.0392 0.0228  413 PHE A CD1 
3491  C CD2 . PHE A 413 ? 0.6160 0.5847 0.6331 -0.0603 -0.0298 0.0027  413 PHE A CD2 
3492  C CE1 . PHE A 413 ? 0.5976 0.5626 0.5775 -0.0446 -0.0511 0.0182  413 PHE A CE1 
3493  C CE2 . PHE A 413 ? 0.6204 0.6032 0.6429 -0.0508 -0.0400 0.0005  413 PHE A CE2 
3494  C CZ  . PHE A 413 ? 0.6719 0.6540 0.6783 -0.0443 -0.0501 0.0078  413 PHE A CZ  
3495  N N   . LEU A 414 ? 0.6686 0.5316 0.6545 -0.0906 0.0088  0.0373  414 LEU A N   
3496  C CA  . LEU A 414 ? 0.7691 0.6107 0.7503 -0.1057 0.0299  0.0443  414 LEU A CA  
3497  C C   . LEU A 414 ? 0.7624 0.6169 0.7868 -0.1201 0.0405  0.0287  414 LEU A C   
3498  O O   . LEU A 414 ? 0.7958 0.6428 0.8241 -0.1353 0.0612  0.0311  414 LEU A O   
3499  C CB  . LEU A 414 ? 0.7084 0.5097 0.6687 -0.1030 0.0315  0.0605  414 LEU A CB  
3500  C CG  . LEU A 414 ? 0.7217 0.5060 0.6332 -0.0890 0.0250  0.0783  414 LEU A CG  
3501  C CD1 . LEU A 414 ? 0.7836 0.5281 0.6787 -0.0822 0.0229  0.0923  414 LEU A CD1 
3502  C CD2 . LEU A 414 ? 0.7518 0.5315 0.6327 -0.0953 0.0421  0.0877  414 LEU A CD2 
3503  N N   . LYS A 415 ? 0.7485 0.6232 0.8051 -0.1146 0.0272  0.0125  415 LYS A N   
3504  C CA  . LYS A 415 ? 0.7147 0.6072 0.8137 -0.1251 0.0338  -0.0055 415 LYS A CA  
3505  C C   . LYS A 415 ? 0.7745 0.6954 0.8814 -0.1308 0.0438  -0.0140 415 LYS A C   
3506  O O   . LYS A 415 ? 0.8212 0.7568 0.9608 -0.1420 0.0543  -0.0271 415 LYS A O   
3507  C CB  . LYS A 415 ? 0.7097 0.6159 0.8341 -0.1128 0.0146  -0.0206 415 LYS A CB  
3508  C CG  . LYS A 415 ? 0.7417 0.6646 0.9106 -0.1205 0.0168  -0.0414 415 LYS A CG  
3509  C CD  . LYS A 415 ? 0.7940 0.6935 0.9795 -0.1384 0.0307  -0.0405 415 LYS A CD  
3510  C CE  . LYS A 415 ? 0.7959 0.7095 1.0284 -0.1413 0.0238  -0.0644 415 LYS A CE  
3511  N NZ  . LYS A 415 ? 0.8985 0.8349 1.1680 -0.1586 0.0396  -0.0788 415 LYS A NZ  
3512  N N   . TRP A 416 ? 0.7492 0.6787 0.8287 -0.1232 0.0406  -0.0082 416 TRP A N   
3513  C CA  . TRP A 416 ? 0.6929 0.6472 0.7767 -0.1259 0.0483  -0.0170 416 TRP A CA  
3514  C C   . TRP A 416 ? 0.6599 0.6059 0.7085 -0.1307 0.0614  -0.0051 416 TRP A C   
3515  O O   . TRP A 416 ? 0.7144 0.6774 0.7675 -0.1359 0.0728  -0.0124 416 TRP A O   
3516  C CB  . TRP A 416 ? 0.6736 0.6491 0.7613 -0.1114 0.0321  -0.0260 416 TRP A CB  
3517  C CG  . TRP A 416 ? 0.5745 0.5567 0.6880 -0.1022 0.0183  -0.0359 416 TRP A CG  
3518  C CD1 . TRP A 416 ? 0.6386 0.6418 0.7845 -0.0997 0.0164  -0.0532 416 TRP A CD1 
3519  C CD2 . TRP A 416 ? 0.6662 0.6348 0.7733 -0.0917 0.0038  -0.0300 416 TRP A CD2 
3520  N NE1 . TRP A 416 ? 0.6837 0.6861 0.8412 -0.0879 0.0014  -0.0584 416 TRP A NE1 
3521  C CE2 . TRP A 416 ? 0.6586 0.6398 0.7932 -0.0833 -0.0058 -0.0442 416 TRP A CE2 
3522  C CE3 . TRP A 416 ? 0.5861 0.5342 0.6658 -0.0867 -0.0026 -0.0148 416 TRP A CE3 
3523  C CZ2 . TRP A 416 ? 0.5245 0.4975 0.6592 -0.0707 -0.0201 -0.0434 416 TRP A CZ2 
3524  C CZ3 . TRP A 416 ? 0.5796 0.5208 0.6623 -0.0747 -0.0167 -0.0140 416 TRP A CZ3 
3525  C CH2 . TRP A 416 ? 0.6486 0.6017 0.7580 -0.0671 -0.0247 -0.0281 416 TRP A CH2 
3526  N N   . ILE A 417 ? 0.7165 0.6373 0.7288 -0.1272 0.0597  0.0121  417 ILE A N   
3527  C CA  . ILE A 417 ? 0.6571 0.5693 0.6297 -0.1279 0.0697  0.0232  417 ILE A CA  
3528  C C   . ILE A 417 ? 0.7238 0.6002 0.6646 -0.1274 0.0748  0.0432  417 ILE A C   
3529  O O   . ILE A 417 ? 0.8027 0.6627 0.7487 -0.1229 0.0649  0.0481  417 ILE A O   
3530  C CB  . ILE A 417 ? 0.6539 0.5815 0.6076 -0.1156 0.0540  0.0195  417 ILE A CB  
3531  C CG1 . ILE A 417 ? 0.6827 0.6109 0.6032 -0.1170 0.0649  0.0226  417 ILE A CG1 
3532  C CG2 . ILE A 417 ? 0.7193 0.6357 0.6569 -0.1028 0.0344  0.0279  417 ILE A CG2 
3533  C CD1 . ILE A 417 ? 0.6364 0.5872 0.5551 -0.1104 0.0540  0.0102  417 ILE A CD1 
3534  N N   . GLY A 418 ? 0.7141 0.5764 0.6198 -0.1304 0.0910  0.0552  418 GLY A N   
3535  C CA  . GLY A 418 ? 0.7642 0.5889 0.6323 -0.1263 0.0960  0.0764  418 GLY A CA  
3536  C C   . GLY A 418 ? 0.8956 0.6955 0.7529 -0.1398 0.1259  0.0891  418 GLY A C   
3537  O O   . GLY A 418 ? 1.0619 0.8343 0.8706 -0.1335 0.1347  0.1080  418 GLY A O   
3538  N N   . ASN A 419 ? 1.0147 0.8240 0.9162 -0.1574 0.1423  0.0792  419 ASN A N   
3539  C CA  . ASN A 419 ? 1.0587 0.8486 0.9586 -0.1734 0.1747  0.0896  419 ASN A CA  
3540  C C   . ASN A 419 ? 1.0677 0.8875 0.9778 -0.1816 0.1919  0.0791  419 ASN A C   
3541  O O   . ASN A 419 ? 0.9681 0.8237 0.8975 -0.1772 0.1786  0.0607  419 ASN A O   
3542  C CB  . ASN A 419 ? 0.9815 0.7574 0.9269 -0.1892 0.1834  0.0862  419 ASN A CB  
3543  C CG  . ASN A 419 ? 1.0955 0.9111 1.1059 -0.2011 0.1819  0.0597  419 ASN A CG  
3544  O OD1 . ASN A 419 ? 1.0767 0.9273 1.0999 -0.2017 0.1839  0.0462  419 ASN A OD1 
3545  N ND2 . ASN A 419 ? 1.1439 0.9529 1.1946 -0.2091 0.1774  0.0512  419 ASN A ND2 
3546  N N   . LYS A 420 ? 1.0087 0.8114 0.9043 -0.1928 0.2236  0.0918  420 LYS A N   
3547  C CA  . LYS A 420 ? 1.0251 0.8539 0.9246 -0.1991 0.2433  0.0839  420 LYS A CA  
3548  C C   . LYS A 420 ? 1.0179 0.8896 0.9818 -0.2086 0.2392  0.0571  420 LYS A C   
3549  O O   . LYS A 420 ? 0.9985 0.9018 0.9657 -0.2029 0.2343  0.0428  420 LYS A O   
3550  C CB  . LYS A 420 ? 1.0302 0.8333 0.9140 -0.2125 0.2821  0.1019  420 LYS A CB  
3551  C CG  . LYS A 420 ? 1.1498 0.9264 0.9578 -0.1980 0.2915  0.1240  420 LYS A CG  
3552  C CD  . LYS A 420 ? 1.1131 0.9007 0.9077 -0.2043 0.3238  0.1259  420 LYS A CD  
3553  C CE  . LYS A 420 ? 1.1810 0.9931 1.0431 -0.2283 0.3479  0.1120  420 LYS A CE  
3554  N NZ  . LYS A 420 ? 1.0557 0.8720 0.9045 -0.2361 0.3863  0.1186  420 LYS A NZ  
3555  N N   . GLU A 421 ? 0.9886 0.8611 1.0033 -0.2213 0.2396  0.0489  421 GLU A N   
3556  C CA  . GLU A 421 ? 0.9557 0.8693 1.0321 -0.2278 0.2336  0.0222  421 GLU A CA  
3557  C C   . GLU A 421 ? 1.0185 0.9574 1.0958 -0.2101 0.2020  0.0076  421 GLU A C   
3558  O O   . GLU A 421 ? 0.9815 0.9536 1.0740 -0.2066 0.2007  -0.0082 421 GLU A O   
3559  C CB  . GLU A 421 ? 0.9908 0.8969 1.1163 -0.2418 0.2345  0.0155  421 GLU A CB  
3560  C CG  . GLU A 421 ? 1.1135 0.9860 1.2378 -0.2606 0.2665  0.0325  421 GLU A CG  
3561  C CD  . GLU A 421 ? 1.1721 0.9927 1.2530 -0.2546 0.2622  0.0565  421 GLU A CD  
3562  O OE1 . GLU A 421 ? 1.1457 0.9427 1.1650 -0.2428 0.2661  0.0775  421 GLU A OE1 
3563  O OE2 . GLU A 421 ? 1.2104 1.0138 1.3181 -0.2602 0.2541  0.0532  421 GLU A OE2 
3564  N N   . LYS A 422 ? 1.0151 0.9373 1.0763 -0.1982 0.1777  0.0130  422 LYS A N   
3565  C CA  . LYS A 422 ? 1.0024 0.9450 1.0618 -0.1817 0.1505  0.0018  422 LYS A CA  
3566  C C   . LYS A 422 ? 0.9299 0.8809 0.9515 -0.1727 0.1509  0.0040  422 LYS A C   
3567  O O   . LYS A 422 ? 0.8855 0.8631 0.9193 -0.1656 0.1410  -0.0111 422 LYS A O   
3568  C CB  . LYS A 422 ? 0.9061 0.8279 0.9512 -0.1707 0.1279  0.0098  422 LYS A CB  
3569  C CG  . LYS A 422 ? 0.8565 0.7800 0.9443 -0.1737 0.1181  -0.0010 422 LYS A CG  
3570  C CD  . LYS A 422 ? 0.8553 0.7398 0.9291 -0.1764 0.1194  0.0149  422 LYS A CD  
3571  C CE  . LYS A 422 ? 0.8868 0.7715 0.9986 -0.1760 0.1051  0.0025  422 LYS A CE  
3572  N NZ  . LYS A 422 ? 0.8755 0.7912 1.0408 -0.1858 0.1093  -0.0205 422 LYS A NZ  
3573  N N   . ASN A 423 ? 0.8730 0.8001 0.8471 -0.1716 0.1622  0.0222  423 ASN A N   
3574  C CA  . ASN A 423 ? 0.8577 0.7921 0.7937 -0.1620 0.1609  0.0223  423 ASN A CA  
3575  C C   . ASN A 423 ? 0.8379 0.7979 0.7893 -0.1684 0.1794  0.0096  423 ASN A C   
3576  O O   . ASN A 423 ? 0.8212 0.7951 0.7547 -0.1596 0.1737  0.0015  423 ASN A O   
3577  C CB  . ASN A 423 ? 0.9295 0.8322 0.8075 -0.1565 0.1680  0.0442  423 ASN A CB  
3578  C CG  . ASN A 423 ? 0.9127 0.7940 0.7696 -0.1450 0.1455  0.0550  423 ASN A CG  
3579  O OD1 . ASN A 423 ? 0.8761 0.7712 0.7500 -0.1373 0.1215  0.0451  423 ASN A OD1 
3580  N ND2 . ASN A 423 ? 0.9489 0.7958 0.7679 -0.1427 0.1546  0.0762  423 ASN A ND2 
3581  N N   . GLU A 424 ? 0.8742 0.8413 0.8606 -0.1833 0.2013  0.0063  424 GLU A N   
3582  C CA  . GLU A 424 ? 0.8897 0.8866 0.8987 -0.1883 0.2178  -0.0085 424 GLU A CA  
3583  C C   . GLU A 424 ? 0.7868 0.8142 0.8238 -0.1787 0.1973  -0.0302 424 GLU A C   
3584  O O   . GLU A 424 ? 0.7873 0.8313 0.8145 -0.1720 0.1991  -0.0399 424 GLU A O   
3585  C CB  . GLU A 424 ? 0.8706 0.8745 0.9237 -0.2068 0.2423  -0.0111 424 GLU A CB  
3586  C CG  . GLU A 424 ? 1.0142 1.0325 1.0663 -0.2143 0.2731  -0.0126 424 GLU A CG  
3587  C CD  . GLU A 424 ? 1.1116 1.1581 1.2286 -0.2302 0.2899  -0.0280 424 GLU A CD  
3588  O OE1 . GLU A 424 ? 1.2328 1.2752 1.3878 -0.2400 0.2851  -0.0308 424 GLU A OE1 
3589  O OE2 . GLU A 424 ? 1.1143 1.1885 1.2457 -0.2323 0.3074  -0.0389 424 GLU A OE2 
3590  N N   . TYR A 425 ? 0.8060 0.8382 0.8751 -0.1765 0.1781  -0.0377 425 TYR A N   
3591  C CA  . TYR A 425 ? 0.7960 0.8537 0.8900 -0.1657 0.1602  -0.0564 425 TYR A CA  
3592  C C   . TYR A 425 ? 0.6757 0.7286 0.7339 -0.1517 0.1442  -0.0554 425 TYR A C   
3593  O O   . TYR A 425 ? 0.6215 0.6928 0.6886 -0.1435 0.1387  -0.0694 425 TYR A O   
3594  C CB  . TYR A 425 ? 0.7422 0.8021 0.8703 -0.1639 0.1430  -0.0624 425 TYR A CB  
3595  C CG  . TYR A 425 ? 0.6925 0.7785 0.8745 -0.1708 0.1494  -0.0798 425 TYR A CG  
3596  C CD1 . TYR A 425 ? 0.6658 0.7619 0.8681 -0.1860 0.1749  -0.0822 425 TYR A CD1 
3597  C CD2 . TYR A 425 ? 0.6379 0.7397 0.8511 -0.1611 0.1299  -0.0945 425 TYR A CD2 
3598  C CE1 . TYR A 425 ? 0.6895 0.8142 0.9470 -0.1925 0.1793  -0.1010 425 TYR A CE1 
3599  C CE2 . TYR A 425 ? 0.6648 0.7934 0.9277 -0.1650 0.1325  -0.1131 425 TYR A CE2 
3600  C CZ  . TYR A 425 ? 0.7479 0.8896 1.0356 -0.1813 0.1564  -0.1174 425 TYR A CZ  
3601  O OH  . TYR A 425 ? 0.6960 0.8688 1.0387 -0.1854 0.1573  -0.1387 425 TYR A OH  
3602  N N   . TRP A 426 ? 0.7030 0.7313 0.7222 -0.1484 0.1364  -0.0399 426 TRP A N   
3603  C CA  . TRP A 426 ? 0.7432 0.7695 0.7333 -0.1367 0.1208  -0.0412 426 TRP A CA  
3604  C C   . TRP A 426 ? 0.6918 0.7226 0.6540 -0.1357 0.1336  -0.0447 426 TRP A C   
3605  O O   . TRP A 426 ? 0.6454 0.6870 0.6050 -0.1282 0.1258  -0.0570 426 TRP A O   
3606  C CB  . TRP A 426 ? 0.6972 0.7006 0.6578 -0.1320 0.1065  -0.0261 426 TRP A CB  
3607  C CG  . TRP A 426 ? 0.6636 0.6638 0.6489 -0.1291 0.0903  -0.0250 426 TRP A CG  
3608  C CD1 . TRP A 426 ? 0.6768 0.6608 0.6688 -0.1338 0.0916  -0.0146 426 TRP A CD1 
3609  C CD2 . TRP A 426 ? 0.6692 0.6809 0.6735 -0.1200 0.0718  -0.0343 426 TRP A CD2 
3610  N NE1 . TRP A 426 ? 0.6329 0.6194 0.6462 -0.1273 0.0739  -0.0183 426 TRP A NE1 
3611  C CE2 . TRP A 426 ? 0.6600 0.6638 0.6805 -0.1186 0.0624  -0.0295 426 TRP A CE2 
3612  C CE3 . TRP A 426 ? 0.6646 0.6900 0.6730 -0.1127 0.0638  -0.0459 426 TRP A CE3 
3613  C CZ2 . TRP A 426 ? 0.6852 0.6963 0.7235 -0.1089 0.0459  -0.0352 426 TRP A CZ2 
3614  C CZ3 . TRP A 426 ? 0.5739 0.6042 0.6009 -0.1044 0.0488  -0.0503 426 TRP A CZ3 
3615  C CH2 . TRP A 426 ? 0.6535 0.6776 0.6942 -0.1020 0.0402  -0.0446 426 TRP A CH2 
3616  N N   . LYS A 427 ? 0.6993 0.7206 0.6406 -0.1427 0.1548  -0.0344 427 LYS A N   
3617  C CA  . LYS A 427 ? 0.7582 0.7845 0.6713 -0.1403 0.1689  -0.0383 427 LYS A CA  
3618  C C   . LYS A 427 ? 0.7256 0.7794 0.6712 -0.1402 0.1759  -0.0579 427 LYS A C   
3619  O O   . LYS A 427 ? 0.6912 0.7520 0.6192 -0.1327 0.1750  -0.0683 427 LYS A O   
3620  C CB  . LYS A 427 ? 0.7802 0.7914 0.6675 -0.1478 0.1947  -0.0223 427 LYS A CB  
3621  C CG  . LYS A 427 ? 0.9124 0.8961 0.7429 -0.1400 0.1892  -0.0051 427 LYS A CG  
3622  C CD  . LYS A 427 ? 0.8873 0.8474 0.6997 -0.1480 0.2131  0.0160  427 LYS A CD  
3623  C CE  . LYS A 427 ? 0.8963 0.8257 0.6710 -0.1403 0.1997  0.0347  427 LYS A CE  
3624  N NZ  . LYS A 427 ? 0.9730 0.8778 0.7562 -0.1511 0.2161  0.0527  427 LYS A NZ  
3625  N N   . ILE A 428 ? 0.6482 0.7180 0.6417 -0.1473 0.1820  -0.0646 428 ILE A N   
3626  C CA  . ILE A 428 ? 0.6123 0.7103 0.6398 -0.1441 0.1860  -0.0842 428 ILE A CA  
3627  C C   . ILE A 428 ? 0.6099 0.7112 0.6398 -0.1310 0.1631  -0.0955 428 ILE A C   
3628  O O   . ILE A 428 ? 0.5805 0.6931 0.6089 -0.1233 0.1645  -0.1088 428 ILE A O   
3629  C CB  . ILE A 428 ? 0.6565 0.7727 0.7368 -0.1531 0.1936  -0.0906 428 ILE A CB  
3630  C CG1 . ILE A 428 ? 0.6266 0.7456 0.7124 -0.1676 0.2234  -0.0840 428 ILE A CG1 
3631  C CG2 . ILE A 428 ? 0.5942 0.7395 0.7113 -0.1440 0.1875  -0.1120 428 ILE A CG2 
3632  C CD1 . ILE A 428 ? 0.6367 0.7554 0.7610 -0.1816 0.2290  -0.0806 428 ILE A CD1 
3633  N N   . LEU A 429 ? 0.6601 0.7502 0.6937 -0.1280 0.1431  -0.0900 429 LEU A N   
3634  C CA  . LEU A 429 ? 0.5843 0.6753 0.6220 -0.1164 0.1239  -0.0984 429 LEU A CA  
3635  C C   . LEU A 429 ? 0.6076 0.6880 0.6084 -0.1113 0.1189  -0.0997 429 LEU A C   
3636  O O   . LEU A 429 ? 0.6332 0.7187 0.6371 -0.1036 0.1148  -0.1123 429 LEU A O   
3637  C CB  . LEU A 429 ? 0.6039 0.6852 0.6518 -0.1146 0.1063  -0.0907 429 LEU A CB  
3638  C CG  . LEU A 429 ? 0.6423 0.7266 0.7044 -0.1029 0.0899  -0.0985 429 LEU A CG  
3639  C CD1 . LEU A 429 ? 0.6284 0.7325 0.7202 -0.0963 0.0950  -0.1138 429 LEU A CD1 
3640  C CD2 . LEU A 429 ? 0.6393 0.7153 0.7107 -0.1004 0.0750  -0.0902 429 LEU A CD2 
3641  N N   . ILE A 430 ? 0.6476 0.7125 0.6130 -0.1146 0.1187  -0.0876 430 ILE A N   
3642  C CA  . ILE A 430 ? 0.7391 0.7958 0.6701 -0.1091 0.1105  -0.0912 430 ILE A CA  
3643  C C   . ILE A 430 ? 0.7738 0.8395 0.6948 -0.1064 0.1239  -0.1044 430 ILE A C   
3644  O O   . ILE A 430 ? 0.8208 0.8871 0.7381 -0.1000 0.1163  -0.1177 430 ILE A O   
3645  C CB  . ILE A 430 ? 0.7918 0.8321 0.6842 -0.1102 0.1073  -0.0761 430 ILE A CB  
3646  C CG1 . ILE A 430 ? 0.7164 0.7478 0.6174 -0.1097 0.0901  -0.0657 430 ILE A CG1 
3647  C CG2 . ILE A 430 ? 0.7869 0.8229 0.6421 -0.1037 0.1002  -0.0833 430 ILE A CG2 
3648  C CD1 . ILE A 430 ? 0.8620 0.8765 0.7337 -0.1111 0.0920  -0.0475 430 ILE A CD1 
3649  N N   . GLU A 431 ? 0.7807 0.8530 0.6987 -0.1114 0.1456  -0.1013 431 GLU A N   
3650  C CA  . GLU A 431 ? 0.7539 0.8365 0.6619 -0.1078 0.1609  -0.1136 431 GLU A CA  
3651  C C   . GLU A 431 ? 0.7276 0.8261 0.6710 -0.1020 0.1592  -0.1309 431 GLU A C   
3652  O O   . GLU A 431 ? 0.8606 0.9621 0.7937 -0.0946 0.1614  -0.1449 431 GLU A O   
3653  C CB  . GLU A 431 ? 0.7248 0.8130 0.6282 -0.1153 0.1873  -0.1052 431 GLU A CB  
3654  C CG  . GLU A 431 ? 0.7823 0.8520 0.6347 -0.1156 0.1938  -0.0904 431 GLU A CG  
3655  C CD  . GLU A 431 ? 0.9557 1.0234 0.7670 -0.1054 0.1942  -0.1009 431 GLU A CD  
3656  O OE1 . GLU A 431 ? 0.9176 0.9997 0.7421 -0.1008 0.1991  -0.1183 431 GLU A OE1 
3657  O OE2 . GLU A 431 ? 1.0483 1.0997 0.8130 -0.1005 0.1888  -0.0926 431 GLU A OE2 
3658  N N   . ALA A 432 ? 0.5967 0.7044 0.5799 -0.1035 0.1549  -0.1308 432 ALA A N   
3659  C CA  . ALA A 432 ? 0.6330 0.7544 0.6462 -0.0944 0.1521  -0.1464 432 ALA A CA  
3660  C C   . ALA A 432 ? 0.8128 0.9196 0.8179 -0.0857 0.1336  -0.1519 432 ALA A C   
3661  O O   . ALA A 432 ? 0.9140 1.0221 0.9204 -0.0766 0.1344  -0.1657 432 ALA A O   
3662  C CB  . ALA A 432 ? 0.6000 0.7367 0.6557 -0.0960 0.1513  -0.1462 432 ALA A CB  
3663  N N   . LYS A 433 ? 0.7172 0.8092 0.7148 -0.0884 0.1181  -0.1414 433 LYS A N   
3664  C CA  . LYS A 433 ? 0.7015 0.7802 0.6954 -0.0824 0.1028  -0.1461 433 LYS A CA  
3665  C C   . LYS A 433 ? 0.7479 0.8186 0.7147 -0.0802 0.1038  -0.1572 433 LYS A C   
3666  O O   . LYS A 433 ? 0.8061 0.8684 0.7771 -0.0741 0.0980  -0.1678 433 LYS A O   
3667  C CB  . LYS A 433 ? 0.8145 0.8822 0.8042 -0.0865 0.0878  -0.1330 433 LYS A CB  
3668  C CG  . LYS A 433 ? 0.7433 0.7993 0.7365 -0.0823 0.0738  -0.1366 433 LYS A CG  
3669  C CD  . LYS A 433 ? 0.6823 0.7392 0.7006 -0.0727 0.0750  -0.1438 433 LYS A CD  
3670  C CE  . LYS A 433 ? 0.8081 0.8498 0.8235 -0.0689 0.0696  -0.1522 433 LYS A CE  
3671  N NZ  . LYS A 433 ? 0.7741 0.8068 0.7836 -0.0751 0.0570  -0.1463 433 LYS A NZ  
3672  N N   . LYS A 434 ? 0.8022 0.8737 0.7398 -0.0842 0.1119  -0.1554 434 LYS A N   
3673  C CA  . LYS A 434 ? 0.8366 0.9027 0.7465 -0.0802 0.1136  -0.1689 434 LYS A CA  
3674  C C   . LYS A 434 ? 0.8235 0.8968 0.7465 -0.0722 0.1246  -0.1846 434 LYS A C   
3675  O O   . LYS A 434 ? 0.8823 0.9470 0.7911 -0.0668 0.1223  -0.1994 434 LYS A O   
3676  C CB  . LYS A 434 ? 0.7051 0.7720 0.5782 -0.0829 0.1232  -0.1629 434 LYS A CB  
3677  C CG  . LYS A 434 ? 0.6941 0.7515 0.5462 -0.0872 0.1115  -0.1484 434 LYS A CG  
3678  C CD  . LYS A 434 ? 0.8295 0.8824 0.6340 -0.0845 0.1171  -0.1472 434 LYS A CD  
3679  C CE  . LYS A 434 ? 0.8764 0.9276 0.6674 -0.0892 0.1305  -0.1266 434 LYS A CE  
3680  N NZ  . LYS A 434 ? 0.8780 0.9261 0.6961 -0.0953 0.1214  -0.1128 434 LYS A NZ  
3681  N N   . LYS A 435 ? 0.7550 0.8443 0.7057 -0.0706 0.1358  -0.1834 435 LYS A N   
3682  C CA  . LYS A 435 ? 0.7372 0.8370 0.7025 -0.0607 0.1462  -0.1984 435 LYS A CA  
3683  C C   . LYS A 435 ? 0.7144 0.8168 0.7142 -0.0526 0.1396  -0.2009 435 LYS A C   
3684  O O   . LYS A 435 ? 0.7976 0.9117 0.8139 -0.0420 0.1474  -0.2123 435 LYS A O   
3685  C CB  . LYS A 435 ? 0.8127 0.9346 0.7811 -0.0632 0.1674  -0.1982 435 LYS A CB  
3686  C CG  . LYS A 435 ? 0.8437 0.9615 0.7749 -0.0711 0.1763  -0.1896 435 LYS A CG  
3687  C CD  . LYS A 435 ? 0.7822 0.9210 0.7219 -0.0759 0.2006  -0.1857 435 LYS A CD  
3688  C CE  . LYS A 435 ? 0.7214 0.8575 0.6186 -0.0748 0.2159  -0.1866 435 LYS A CE  
3689  N NZ  . LYS A 435 ? 0.7813 0.9061 0.6529 -0.0634 0.2072  -0.2034 435 LYS A NZ  
3690  N N   . ALA A 436 ? 0.8523 0.9716 0.6740 -0.1759 0.1174  -0.1501 436 ALA A N   
3691  C CA  . ALA A 436 ? 0.8773 0.9432 0.7115 -0.1641 0.1167  -0.1325 436 ALA A CA  
3692  C C   . ALA A 436 ? 0.8839 0.8678 0.6962 -0.1796 0.1185  -0.1502 436 ALA A C   
3693  O O   . ALA A 436 ? 0.9695 0.9467 0.7660 -0.2165 0.1161  -0.1613 436 ALA A O   
3694  C CB  . ALA A 436 ? 0.7556 0.8598 0.6087 -0.1716 0.1093  -0.1050 436 ALA A CB  
3695  N N   . LYS A 437 ? 0.9633 0.8847 0.7749 -0.1520 0.1220  -0.1519 437 LYS A N   
3696  C CA  . LYS A 437 ? 0.9991 0.8257 0.7879 -0.1593 0.1227  -0.1648 437 LYS A CA  
3697  C C   . LYS A 437 ? 0.9496 0.7302 0.7410 -0.1555 0.1181  -0.1328 437 LYS A C   
3698  O O   . LYS A 437 ? 0.9734 0.6676 0.7427 -0.1654 0.1172  -0.1340 437 LYS A O   
3699  C CB  . LYS A 437 ? 1.0378 0.8213 0.8195 -0.1254 0.1288  -0.1937 437 LYS A CB  
3700  C CG  . LYS A 437 ? 1.0690 0.8826 0.8360 -0.1363 0.1347  -0.2349 437 LYS A CG  
3701  C CD  . LYS A 437 ? 1.1566 0.8838 0.8923 -0.1594 0.1358  -0.2714 437 LYS A CD  
3702  C CE  . LYS A 437 ? 1.2887 1.0074 1.0108 -0.2158 0.1300  -0.2641 437 LYS A CE  
3703  N NZ  . LYS A 437 ? 1.3151 0.9186 1.0085 -0.2418 0.1297  -0.2853 437 LYS A NZ  
3704  N N   . ASN A 438 ? 0.9041 0.7377 0.7194 -0.1423 0.1150  -0.1045 438 ASN A N   
3705  C CA  . ASN A 438 ? 1.0118 0.8215 0.8281 -0.1405 0.1105  -0.0746 438 ASN A CA  
3706  C C   . ASN A 438 ? 0.9645 0.8523 0.8004 -0.1541 0.1078  -0.0565 438 ASN A C   
3707  O O   . ASN A 438 ? 0.8978 0.8488 0.7469 -0.1605 0.1080  -0.0643 438 ASN A O   
3708  C CB  . ASN A 438 ? 0.9626 0.7494 0.7892 -0.0952 0.1088  -0.0646 438 ASN A CB  
3709  C CG  . ASN A 438 ? 0.9845 0.8397 0.8401 -0.0677 0.1110  -0.0701 438 ASN A CG  
3710  O OD1 . ASN A 438 ? 0.9631 0.8707 0.8399 -0.0638 0.1082  -0.0537 438 ASN A OD1 
3711  N ND2 . ASN A 438 ? 0.9996 0.8543 0.8557 -0.0503 0.1166  -0.0946 438 ASN A ND2 
3712  N N   . ASP A 439 ? 0.9760 0.8612 0.8124 -0.1557 0.1048  -0.0322 439 ASP A N   
3713  C CA  . ASP A 439 ? 0.9813 0.9389 0.8347 -0.1678 0.1030  -0.0203 439 ASP A CA  
3714  C C   . ASP A 439 ? 0.8773 0.8824 0.7599 -0.1346 0.1006  -0.0152 439 ASP A C   
3715  O O   . ASP A 439 ? 0.8471 0.9050 0.7450 -0.1372 0.0987  -0.0082 439 ASP A O   
3716  C CB  . ASP A 439 ? 1.0055 0.9504 0.8425 -0.1926 0.1025  0.0005  439 ASP A CB  
3717  C CG  . ASP A 439 ? 1.1998 1.0790 1.0049 -0.2302 0.1050  -0.0010 439 ASP A CG  
3718  O OD1 . ASP A 439 ? 1.4662 1.2658 1.2545 -0.2185 0.1050  -0.0089 439 ASP A OD1 
3719  O OD2 . ASP A 439 ? 1.3843 1.2920 1.1818 -0.2719 0.1071  0.0040  439 ASP A OD2 
3720  N N   . TYR A 440 ? 0.8802 0.8708 0.7719 -0.1050 0.1011  -0.0215 440 TYR A N   
3721  C CA  . TYR A 440 ? 0.7997 0.8373 0.7202 -0.0829 0.0996  -0.0200 440 TYR A CA  
3722  C C   . TYR A 440 ? 0.7797 0.8658 0.7143 -0.0911 0.0996  -0.0248 440 TYR A C   
3723  O O   . TYR A 440 ? 0.8317 0.9502 0.7893 -0.0780 0.0975  -0.0212 440 TYR A O   
3724  C CB  . TYR A 440 ? 0.7590 0.7833 0.6879 -0.0553 0.1015  -0.0264 440 TYR A CB  
3725  C CG  . TYR A 440 ? 0.8270 0.8406 0.7600 -0.0342 0.0971  -0.0162 440 TYR A CG  
3726  C CD1 . TYR A 440 ? 0.8027 0.8587 0.7575 -0.0263 0.0932  -0.0106 440 TYR A CD1 
3727  C CD2 . TYR A 440 ? 0.8011 0.7616 0.7149 -0.0214 0.0956  -0.0127 440 TYR A CD2 
3728  C CE1 . TYR A 440 ? 0.6289 0.6872 0.5857 -0.0084 0.0876  -0.0024 440 TYR A CE1 
3729  C CE2 . TYR A 440 ? 0.8506 0.8087 0.7665 0.0012  0.0891  0.0005  440 TYR A CE2 
3730  C CZ  . TYR A 440 ? 0.7494 0.7629 0.6866 0.0063  0.0850  0.0054  440 TYR A CZ  
3731  O OH  . TYR A 440 ? 0.7529 0.7748 0.6905 0.0278  0.0771  0.0173  440 TYR A OH  
3732  N N   . ILE A 441 ? 0.7159 0.8065 0.6366 -0.1128 0.1007  -0.0327 441 ILE A N   
3733  C CA  . ILE A 441 ? 0.7674 0.9121 0.7001 -0.1182 0.0978  -0.0327 441 ILE A CA  
3734  C C   . ILE A 441 ? 0.7065 0.8910 0.6563 -0.1179 0.0935  -0.0241 441 ILE A C   
3735  O O   . ILE A 441 ? 0.6252 0.8470 0.5954 -0.1043 0.0894  -0.0203 441 ILE A O   
3736  C CB  . ILE A 441 ? 0.6184 0.7713 0.5314 -0.1440 0.0984  -0.0453 441 ILE A CB  
3737  C CG1 . ILE A 441 ? 0.6256 0.8360 0.5482 -0.1405 0.0941  -0.0433 441 ILE A CG1 
3738  C CG2 . ILE A 441 ? 0.7030 0.8595 0.6050 -0.1744 0.0976  -0.0463 441 ILE A CG2 
3739  C CD1 . ILE A 441 ? 0.5519 0.7603 0.4782 -0.1207 0.0968  -0.0403 441 ILE A CD1 
3740  N N   . LEU A 442 ? 0.6562 0.8326 0.5972 -0.1312 0.0945  -0.0206 442 LEU A N   
3741  C CA  . LEU A 442 ? 0.6800 0.9062 0.6359 -0.1316 0.0923  -0.0171 442 LEU A CA  
3742  C C   . LEU A 442 ? 0.6948 0.9286 0.6730 -0.1025 0.0900  -0.0161 442 LEU A C   
3743  O O   . LEU A 442 ? 0.6927 0.9704 0.6917 -0.0912 0.0869  -0.0202 442 LEU A O   
3744  C CB  . LEU A 442 ? 0.7491 0.9691 0.6853 -0.1580 0.0957  -0.0107 442 LEU A CB  
3745  C CG  . LEU A 442 ? 0.7516 0.9498 0.6626 -0.1956 0.0986  -0.0128 442 LEU A CG  
3746  C CD1 . LEU A 442 ? 0.6111 0.8022 0.5019 -0.2265 0.1025  -0.0003 442 LEU A CD1 
3747  C CD2 . LEU A 442 ? 0.6852 0.9436 0.6071 -0.2084 0.0962  -0.0241 442 LEU A CD2 
3748  N N   . VAL A 443 ? 0.6795 0.8738 0.6550 -0.0896 0.0908  -0.0136 443 VAL A N   
3749  C CA  . VAL A 443 ? 0.6099 0.8129 0.6075 -0.0673 0.0881  -0.0167 443 VAL A CA  
3750  C C   . VAL A 443 ? 0.6000 0.8138 0.6181 -0.0559 0.0858  -0.0191 443 VAL A C   
3751  O O   . VAL A 443 ? 0.6575 0.8891 0.6966 -0.0429 0.0823  -0.0241 443 VAL A O   
3752  C CB  . VAL A 443 ? 0.6461 0.8159 0.6384 -0.0573 0.0887  -0.0141 443 VAL A CB  
3753  C CG1 . VAL A 443 ? 0.4678 0.6569 0.4802 -0.0424 0.0851  -0.0200 443 VAL A CG1 
3754  C CG2 . VAL A 443 ? 0.7269 0.8691 0.6915 -0.0678 0.0898  -0.0049 443 VAL A CG2 
3755  N N   . ALA A 444 ? 0.6018 0.8033 0.6119 -0.0606 0.0875  -0.0153 444 ALA A N   
3756  C CA  . ALA A 444 ? 0.6237 0.8329 0.6473 -0.0516 0.0851  -0.0098 444 ALA A CA  
3757  C C   . ALA A 444 ? 0.6162 0.8606 0.6493 -0.0471 0.0788  -0.0071 444 ALA A C   
3758  O O   . ALA A 444 ? 0.5318 0.7770 0.5781 -0.0339 0.0742  0.0017  444 ALA A O   
3759  C CB  . ALA A 444 ? 0.6377 0.8363 0.6459 -0.0588 0.0894  -0.0066 444 ALA A CB  
3760  N N   . GLU A 445 ? 0.6321 0.9073 0.6591 -0.0576 0.0781  -0.0127 445 GLU A N   
3761  C CA  . GLU A 445 ? 0.5470 0.8720 0.5882 -0.0492 0.0718  -0.0133 445 GLU A CA  
3762  C C   . GLU A 445 ? 0.5353 0.8770 0.5990 -0.0296 0.0697  -0.0230 445 GLU A C   
3763  O O   . GLU A 445 ? 0.5761 0.9682 0.6543 -0.0187 0.0654  -0.0286 445 GLU A O   
3764  C CB  . GLU A 445 ? 0.5365 0.9022 0.5633 -0.0745 0.0729  -0.0177 445 GLU A CB  
3765  C CG  . GLU A 445 ? 0.5859 0.9331 0.5872 -0.0977 0.0755  -0.0169 445 GLU A CG  
3766  C CD  . GLU A 445 ? 0.6916 1.0589 0.6755 -0.1324 0.0786  -0.0254 445 GLU A CD  
3767  O OE1 . GLU A 445 ? 0.7388 1.1696 0.7337 -0.1394 0.0754  -0.0286 445 GLU A OE1 
3768  O OE2 . GLU A 445 ? 0.7950 1.1146 0.7550 -0.1532 0.0843  -0.0298 445 GLU A OE2 
3769  N N   . GLY A 446 ? 0.5012 0.8097 0.5694 -0.0236 0.0723  -0.0284 446 GLY A N   
3770  C CA  . GLY A 446 ? 0.4917 0.8170 0.5792 -0.0061 0.0706  -0.0441 446 GLY A CA  
3771  C C   . GLY A 446 ? 0.5397 0.8532 0.6516 0.0216  0.0632  -0.0461 446 GLY A C   
3772  O O   . GLY A 446 ? 0.6098 0.8861 0.7221 0.0248  0.0602  -0.0307 446 GLY A O   
3773  N N   . SER A 447 ? 0.5339 0.8786 0.6650 0.0427  0.0605  -0.0651 447 SER A N   
3774  C CA  . SER A 447 ? 0.5993 0.9266 0.7541 0.0750  0.0519  -0.0678 447 SER A CA  
3775  C C   . SER A 447 ? 0.6127 0.8689 0.7755 0.0788  0.0503  -0.0701 447 SER A C   
3776  O O   . SER A 447 ? 0.6353 0.8478 0.8079 0.0943  0.0434  -0.0570 447 SER A O   
3777  C CB  . SER A 447 ? 0.4740 0.8583 0.6493 0.1011  0.0500  -0.0939 447 SER A CB  
3778  O OG  . SER A 447 ? 0.5439 0.9192 0.7280 0.1079  0.0531  -0.1228 447 SER A OG  
3779  N N   . ASP A 448 ? 0.4893 0.7346 0.6468 0.0623  0.0560  -0.0838 448 ASP A N   
3780  C CA  . ASP A 448 ? 0.5164 0.7078 0.6859 0.0623  0.0544  -0.0939 448 ASP A CA  
3781  C C   . ASP A 448 ? 0.6206 0.7612 0.7853 0.0489  0.0539  -0.0655 448 ASP A C   
3782  O O   . ASP A 448 ? 0.6629 0.7509 0.8407 0.0536  0.0497  -0.0633 448 ASP A O   
3783  C CB  . ASP A 448 ? 0.5582 0.7672 0.7219 0.0464  0.0592  -0.1137 448 ASP A CB  
3784  C CG  . ASP A 448 ? 0.6409 0.9130 0.8008 0.0531  0.0617  -0.1349 448 ASP A CG  
3785  O OD1 . ASP A 448 ? 0.6884 0.9990 0.8306 0.0422  0.0658  -0.1207 448 ASP A OD1 
3786  O OD2 . ASP A 448 ? 0.6099 0.8942 0.7835 0.0669  0.0602  -0.1670 448 ASP A OD2 
3787  N N   . TRP A 449 ? 0.5759 0.7308 0.7206 0.0308  0.0587  -0.0441 449 TRP A N   
3788  C CA  . TRP A 449 ? 0.5009 0.6233 0.6388 0.0168  0.0605  -0.0190 449 TRP A CA  
3789  C C   . TRP A 449 ? 0.5567 0.6503 0.7003 0.0319  0.0529  0.0022  449 TRP A C   
3790  O O   . TRP A 449 ? 0.7856 0.8329 0.9328 0.0239  0.0522  0.0179  449 TRP A O   
3791  C CB  . TRP A 449 ? 0.5725 0.7216 0.6871 0.0011  0.0667  -0.0059 449 TRP A CB  
3792  C CG  . TRP A 449 ? 0.5835 0.7570 0.6883 -0.0072 0.0717  -0.0212 449 TRP A CG  
3793  C CD1 . TRP A 449 ? 0.5003 0.7021 0.5883 -0.0120 0.0736  -0.0216 449 TRP A CD1 
3794  C CD2 . TRP A 449 ? 0.5605 0.7315 0.6701 -0.0130 0.0742  -0.0352 449 TRP A CD2 
3795  N NE1 . TRP A 449 ? 0.4847 0.6920 0.5642 -0.0190 0.0771  -0.0307 449 TRP A NE1 
3796  C CE2 . TRP A 449 ? 0.5020 0.6959 0.5947 -0.0170 0.0768  -0.0390 449 TRP A CE2 
3797  C CE3 . TRP A 449 ? 0.4571 0.6111 0.5831 -0.0173 0.0737  -0.0443 449 TRP A CE3 
3798  C CZ2 . TRP A 449 ? 0.4656 0.6677 0.5559 -0.0192 0.0774  -0.0480 449 TRP A CZ2 
3799  C CZ3 . TRP A 449 ? 0.4899 0.6622 0.6163 -0.0217 0.0746  -0.0583 449 TRP A CZ3 
3800  C CH2 . TRP A 449 ? 0.4909 0.6879 0.5989 -0.0198 0.0758  -0.0582 449 TRP A CH2 
3801  N N   . PHE A 450 ? 0.5429 0.6663 0.6871 0.0533  0.0465  0.0051  450 PHE A N   
3802  C CA  . PHE A 450 ? 0.6314 0.7332 0.7789 0.0733  0.0367  0.0305  450 PHE A CA  
3803  C C   . PHE A 450 ? 0.6402 0.6876 0.8110 0.0983  0.0291  0.0198  450 PHE A C   
3804  O O   . PHE A 450 ? 0.6969 0.6943 0.8695 0.1107  0.0210  0.0460  450 PHE A O   
3805  C CB  . PHE A 450 ? 0.6622 0.8270 0.8050 0.0895  0.0308  0.0359  450 PHE A CB  
3806  C CG  . PHE A 450 ? 0.7043 0.9155 0.8231 0.0622  0.0379  0.0406  450 PHE A CG  
3807  C CD1 . PHE A 450 ? 0.7620 0.9723 0.8598 0.0475  0.0385  0.0671  450 PHE A CD1 
3808  C CD2 . PHE A 450 ? 0.7195 0.9720 0.8344 0.0497  0.0444  0.0175  450 PHE A CD2 
3809  C CE1 . PHE A 450 ? 0.7638 1.0115 0.8392 0.0236  0.0451  0.0641  450 PHE A CE1 
3810  C CE2 . PHE A 450 ? 0.7258 1.0054 0.8176 0.0237  0.0504  0.0198  450 PHE A CE2 
3811  C CZ  . PHE A 450 ? 0.6627 0.9381 0.7358 0.0121  0.0507  0.0399  450 PHE A CZ  
3812  N N   . TRP A 451 ? 0.6315 0.6848 0.8180 0.1053  0.0313  -0.0184 451 TRP A N   
3813  C CA  . TRP A 451 ? 0.6886 0.6914 0.8980 0.1317  0.0243  -0.0393 451 TRP A CA  
3814  C C   . TRP A 451 ? 0.7407 0.6573 0.9520 0.1113  0.0243  -0.0281 451 TRP A C   
3815  O O   . TRP A 451 ? 0.8143 0.6612 1.0348 0.1298  0.0153  -0.0160 451 TRP A O   
3816  C CB  . TRP A 451 ? 0.6651 0.7082 0.8863 0.1383  0.0287  -0.0871 451 TRP A CB  
3817  C CG  . TRP A 451 ? 0.7239 0.7189 0.9679 0.1611  0.0239  -0.1229 451 TRP A CG  
3818  C CD1 . TRP A 451 ? 0.7693 0.6909 1.0199 0.1439  0.0237  -0.1348 451 TRP A CD1 
3819  C CD2 . TRP A 451 ? 0.7484 0.7701 1.0120 0.2036  0.0192  -0.1572 451 TRP A CD2 
3820  N NE1 . TRP A 451 ? 0.8256 0.7161 1.0969 0.1725  0.0186  -0.1757 451 TRP A NE1 
3821  C CE2 . TRP A 451 ? 0.8134 0.7659 1.0933 0.2127  0.0161  -0.1911 451 TRP A CE2 
3822  C CE3 . TRP A 451 ? 0.7450 0.8482 1.0154 0.2338  0.0179  -0.1653 451 TRP A CE3 
3823  C CZ2 . TRP A 451 ? 0.8581 0.8162 1.1600 0.2560  0.0118  -0.2353 451 TRP A CZ2 
3824  C CZ3 . TRP A 451 ? 0.7647 0.8845 1.0591 0.2768  0.0143  -0.2067 451 TRP A CZ3 
3825  C CH2 . TRP A 451 ? 0.8312 0.8766 1.1406 0.2900  0.0113  -0.2424 451 TRP A CH2 
3826  N N   . TRP A 452 ? 0.7096 0.6306 0.9124 0.0724  0.0339  -0.0296 452 TRP A N   
3827  C CA  . TRP A 452 ? 0.7551 0.6109 0.9634 0.0449  0.0357  -0.0264 452 TRP A CA  
3828  C C   . TRP A 452 ? 0.8115 0.6280 1.0062 0.0280  0.0356  0.0229  452 TRP A C   
3829  O O   . TRP A 452 ? 0.8983 0.6585 1.0970 0.0003  0.0376  0.0313  452 TRP A O   
3830  C CB  . TRP A 452 ? 0.7077 0.6008 0.9150 0.0121  0.0453  -0.0477 452 TRP A CB  
3831  C CG  . TRP A 452 ? 0.7113 0.6431 0.9278 0.0237  0.0452  -0.0929 452 TRP A CG  
3832  C CD1 . TRP A 452 ? 0.6419 0.6458 0.8478 0.0259  0.0496  -0.1036 452 TRP A CD1 
3833  C CD2 . TRP A 452 ? 0.7270 0.6279 0.9622 0.0330  0.0407  -0.1337 452 TRP A CD2 
3834  N NE1 . TRP A 452 ? 0.6198 0.6478 0.8349 0.0354  0.0483  -0.1444 452 TRP A NE1 
3835  C CE2 . TRP A 452 ? 0.6830 0.6526 0.9168 0.0408  0.0431  -0.1673 452 TRP A CE2 
3836  C CE3 . TRP A 452 ? 0.8091 0.6270 1.0603 0.0342  0.0348  -0.1459 452 TRP A CE3 
3837  C CZ2 . TRP A 452 ? 0.7123 0.6829 0.9598 0.0508  0.0404  -0.2157 452 TRP A CZ2 
3838  C CZ3 . TRP A 452 ? 0.8420 0.6504 1.1088 0.0447  0.0317  -0.1979 452 TRP A CZ3 
3839  C CH2 . TRP A 452 ? 0.7907 0.6811 1.0554 0.0535  0.0347  -0.2339 452 TRP A CH2 
3840  N N   . GLN A 453 ? 0.8042 0.6537 0.9818 0.0403  0.0333  0.0551  453 GLN A N   
3841  C CA  . GLN A 453 ? 0.8706 0.7080 1.0283 0.0189  0.0357  0.1018  453 GLN A CA  
3842  C C   . GLN A 453 ? 0.9962 0.7588 1.1536 0.0369  0.0237  0.1364  453 GLN A C   
3843  O O   . GLN A 453 ? 1.1333 0.9012 1.2917 0.0773  0.0118  0.1456  453 GLN A O   
3844  C CB  . GLN A 453 ? 0.8505 0.7640 0.9865 0.0204  0.0388  0.1165  453 GLN A CB  
3845  C CG  . GLN A 453 ? 0.9279 0.8900 1.0563 -0.0087 0.0524  0.1003  453 GLN A CG  
3846  C CD  . GLN A 453 ? 1.0262 0.9654 1.1544 -0.0451 0.0618  0.1115  453 GLN A CD  
3847  O OE1 . GLN A 453 ? 1.1260 1.0606 1.2383 -0.0614 0.0647  0.1474  453 GLN A OE1 
3848  N NE2 . GLN A 453 ? 0.9749 0.9109 1.1206 -0.0597 0.0666  0.0809  453 GLN A NE2 
3849  N N   . GLY A 454 ? 1.0562 0.7510 1.2122 0.0064  0.0264  0.1573  454 GLY A N   
3850  C CA  . GLY A 454 ? 1.0525 0.6701 1.1990 0.0137  0.0164  0.2047  454 GLY A CA  
3851  C C   . GLY A 454 ? 1.3083 0.8371 1.4744 0.0522  0.0019  0.1926  454 GLY A C   
3852  O O   . GLY A 454 ? 1.4789 0.9231 1.6369 0.0585  -0.0077 0.2346  454 GLY A O   
3853  N N   . GLU A 455 ? 1.3940 0.9373 1.5841 0.0793  -0.0001 0.1373  455 GLU A N   
3854  C CA  . GLU A 455 ? 1.5309 0.9964 1.7412 0.1238  -0.0136 0.1184  455 GLU A CA  
3855  C C   . GLU A 455 ? 1.6963 1.0365 1.9127 0.0964  -0.0147 0.1210  455 GLU A C   
3856  O O   . GLU A 455 ? 1.7706 1.0146 1.9814 0.1132  -0.0265 0.1596  455 GLU A O   
3857  C CB  . GLU A 455 ? 1.4376 0.9595 1.6708 0.1527  -0.0124 0.0535  455 GLU A CB  
3858  C CG  . GLU A 455 ? 1.5331 1.0197 1.7868 0.2176  -0.0270 0.0332  455 GLU A CG  
3859  C CD  . GLU A 455 ? 1.5644 1.0988 1.8118 0.2637  -0.0389 0.0705  455 GLU A CD  
3860  O OE1 . GLU A 455 ? 1.6812 1.1827 1.9083 0.2588  -0.0456 0.1304  455 GLU A OE1 
3861  O OE2 . GLU A 455 ? 1.3544 0.9665 1.6172 0.3044  -0.0419 0.0400  455 GLU A OE2 
3862  N N   . GLU A 456 ? 1.7207 1.0605 1.9476 0.0529  -0.0035 0.0818  456 GLU A N   
3863  C CA  . GLU A 456 ? 1.8090 1.0411 2.0415 0.0119  -0.0025 0.0813  456 GLU A CA  
3864  C C   . GLU A 456 ? 1.8377 1.1290 2.0739 -0.0483 0.0131  0.0558  456 GLU A C   
3865  O O   . GLU A 456 ? 1.7178 1.1206 1.9519 -0.0499 0.0213  0.0391  456 GLU A O   
3866  C CB  . GLU A 456 ? 1.7601 0.8959 2.0156 0.0458  -0.0134 0.0351  456 GLU A CB  
3867  C CG  . GLU A 456 ? 1.7131 0.9166 1.9899 0.0632  -0.0099 -0.0420 456 GLU A CG  
3868  C CD  . GLU A 456 ? 1.7474 1.0360 2.0281 0.1253  -0.0147 -0.0548 456 GLU A CD  
3869  O OE1 . GLU A 456 ? 1.7892 1.0285 2.0771 0.1809  -0.0278 -0.0483 456 GLU A OE1 
3870  O OE2 . GLU A 456 ? 1.6422 1.0478 1.9190 0.1181  -0.0058 -0.0702 456 GLU A OE2 
3871  N N   . LYS A 457 ? 1.8101 1.0252 2.0520 -0.0985 0.0164  0.0545  457 LYS A N   
3872  C CA  . LYS A 457 ? 1.7098 0.9834 1.9613 -0.1543 0.0290  0.0241  457 LYS A CA  
3873  C C   . LYS A 457 ? 1.6800 0.9913 1.9528 -0.1351 0.0269  -0.0503 457 LYS A C   
3874  O O   . LYS A 457 ? 1.7443 0.9765 2.0313 -0.1161 0.0182  -0.0884 457 LYS A O   
3875  C CB  . LYS A 457 ? 1.7906 0.9767 2.0444 -0.2178 0.0326  0.0410  457 LYS A CB  
3876  C CG  . LYS A 457 ? 1.6057 0.8689 1.8707 -0.2816 0.0461  0.0187  457 LYS A CG  
3877  C CD  . LYS A 457 ? 1.5875 0.9982 1.8493 -0.2683 0.0544  0.0099  457 LYS A CD  
3878  C CE  . LYS A 457 ? 1.5661 1.0608 1.8396 -0.3244 0.0666  -0.0050 457 LYS A CE  
3879  N NZ  . LYS A 457 ? 1.3153 0.9388 1.5844 -0.3015 0.0726  -0.0128 457 LYS A NZ  
3880  N N   . ALA A 458 ? 1.5626 0.9940 1.8355 -0.1389 0.0347  -0.0705 458 ALA A N   
3881  C CA  . ALA A 458 ? 1.4990 0.9904 1.7834 -0.1120 0.0326  -0.1295 458 ALA A CA  
3882  C C   . ALA A 458 ? 1.4277 1.0179 1.7152 -0.1489 0.0415  -0.1490 458 ALA A C   
3883  O O   . ALA A 458 ? 1.3930 1.0124 1.6753 -0.1866 0.0496  -0.1169 458 ALA A O   
3884  C CB  . ALA A 458 ? 1.4044 0.9463 1.6795 -0.0544 0.0291  -0.1223 458 ALA A CB  
3885  N N   . PRO A 459 ? 1.3782 1.0292 1.6737 -0.1368 0.0399  -0.2009 459 PRO A N   
3886  C CA  . PRO A 459 ? 1.2504 0.9912 1.5504 -0.1699 0.0452  -0.2206 459 PRO A CA  
3887  C C   . PRO A 459 ? 1.1077 0.9418 1.3920 -0.1558 0.0512  -0.1922 459 PRO A C   
3888  O O   . PRO A 459 ? 1.0805 0.9392 1.3523 -0.1162 0.0499  -0.1859 459 PRO A O   
3889  C CB  . PRO A 459 ? 1.1857 0.9515 1.4957 -0.1577 0.0392  -0.2851 459 PRO A CB  
3890  C CG  . PRO A 459 ? 1.2018 0.8715 1.5168 -0.1256 0.0323  -0.3023 459 PRO A CG  
3891  C CD  . PRO A 459 ? 1.2108 0.8527 1.5129 -0.0957 0.0328  -0.2482 459 PRO A CD  
3892  N N   . PHE A 460 ? 1.0595 0.9445 1.3456 -0.1897 0.0580  -0.1763 460 PHE A N   
3893  C CA  . PHE A 460 ? 0.8761 0.8496 1.1505 -0.1795 0.0634  -0.1592 460 PHE A CA  
3894  C C   . PHE A 460 ? 0.7722 0.7385 1.0256 -0.1494 0.0661  -0.1211 460 PHE A C   
3895  O O   . PHE A 460 ? 0.7704 0.7948 1.0108 -0.1295 0.0681  -0.1162 460 PHE A O   
3896  C CB  . PHE A 460 ? 0.8360 0.8818 1.1100 -0.1624 0.0588  -0.1952 460 PHE A CB  
3897  C CG  . PHE A 460 ? 0.8888 0.9548 1.1818 -0.1900 0.0540  -0.2386 460 PHE A CG  
3898  C CD1 . PHE A 460 ? 0.7725 0.8544 1.0825 -0.2342 0.0572  -0.2381 460 PHE A CD1 
3899  C CD2 . PHE A 460 ? 0.8707 0.9494 1.1645 -0.1743 0.0466  -0.2825 460 PHE A CD2 
3900  C CE1 . PHE A 460 ? 0.9477 1.0562 1.2763 -0.2640 0.0518  -0.2814 460 PHE A CE1 
3901  C CE2 . PHE A 460 ? 0.8396 0.9435 1.1490 -0.2015 0.0413  -0.3273 460 PHE A CE2 
3902  C CZ  . PHE A 460 ? 0.9314 1.0492 1.2588 -0.2474 0.0432  -0.3272 460 PHE A CZ  
3903  N N   . VAL A 461 ? 0.8794 0.7736 1.1281 -0.1462 0.0651  -0.0936 461 VAL A N   
3904  C CA  . VAL A 461 ? 0.9024 0.7999 1.1308 -0.1236 0.0671  -0.0554 461 VAL A CA  
3905  C C   . VAL A 461 ? 0.8402 0.7954 1.0583 -0.1419 0.0772  -0.0311 461 VAL A C   
3906  O O   . VAL A 461 ? 0.8475 0.8327 1.0473 -0.1234 0.0799  -0.0124 461 VAL A O   
3907  C CB  . VAL A 461 ? 0.9836 0.7969 1.2083 -0.1186 0.0623  -0.0254 461 VAL A CB  
3908  C CG1 . VAL A 461 ? 1.0490 0.8064 1.2858 -0.0901 0.0517  -0.0545 461 VAL A CG1 
3909  C CG2 . VAL A 461 ? 1.0157 0.7872 1.2450 -0.1645 0.0673  -0.0031 461 VAL A CG2 
3910  N N   . GLU A 462 ? 0.7249 0.7004 0.9557 -0.1789 0.0833  -0.0343 462 GLU A N   
3911  C CA  . GLU A 462 ? 0.7079 0.7538 0.9341 -0.1914 0.0936  -0.0213 462 GLU A CA  
3912  C C   . GLU A 462 ? 0.6054 0.7112 0.8239 -0.1612 0.0926  -0.0379 462 GLU A C   
3913  O O   . GLU A 462 ? 0.6768 0.8125 0.8786 -0.1481 0.0982  -0.0216 462 GLU A O   
3914  C CB  . GLU A 462 ? 0.7795 0.8556 1.0279 -0.2341 0.0990  -0.0324 462 GLU A CB  
3915  C CG  . GLU A 462 ? 0.8851 0.8864 1.1459 -0.2691 0.0965  -0.0307 462 GLU A CG  
3916  C CD  . GLU A 462 ? 1.0757 1.0246 1.3208 -0.2860 0.1018  0.0173  462 GLU A CD  
3917  O OE1 . GLU A 462 ? 1.1539 1.1493 1.3825 -0.2818 0.1105  0.0450  462 GLU A OE1 
3918  O OE2 . GLU A 462 ? 1.0376 0.8977 1.2852 -0.3030 0.0970  0.0274  462 GLU A OE2 
3919  N N   . VAL A 463 ? 0.5950 0.7158 0.8230 -0.1508 0.0853  -0.0706 463 VAL A N   
3920  C CA  . VAL A 463 ? 0.5951 0.7692 0.8136 -0.1258 0.0835  -0.0819 463 VAL A CA  
3921  C C   . VAL A 463 ? 0.5523 0.7086 0.7474 -0.0977 0.0827  -0.0675 463 VAL A C   
3922  O O   . VAL A 463 ? 0.5325 0.7189 0.7124 -0.0831 0.0853  -0.0608 463 VAL A O   
3923  C CB  . VAL A 463 ? 0.6661 0.8638 0.8956 -0.1232 0.0750  -0.1169 463 VAL A CB  
3924  C CG1 . VAL A 463 ? 0.5744 0.8338 0.7941 -0.1035 0.0730  -0.1208 463 VAL A CG1 
3925  C CG2 . VAL A 463 ? 0.5762 0.7807 0.8311 -0.1577 0.0741  -0.1360 463 VAL A CG2 
3926  N N   . PHE A 464 ? 0.5816 0.6891 0.7745 -0.0893 0.0785  -0.0639 464 PHE A N   
3927  C CA  . PHE A 464 ? 0.5881 0.6909 0.7625 -0.0656 0.0771  -0.0521 464 PHE A CA  
3928  C C   . PHE A 464 ? 0.5531 0.6591 0.7111 -0.0688 0.0834  -0.0224 464 PHE A C   
3929  O O   . PHE A 464 ? 0.6000 0.7260 0.7400 -0.0567 0.0849  -0.0172 464 PHE A O   
3930  C CB  . PHE A 464 ? 0.5627 0.6232 0.7435 -0.0511 0.0700  -0.0575 464 PHE A CB  
3931  C CG  . PHE A 464 ? 0.5461 0.6152 0.7381 -0.0415 0.0647  -0.0932 464 PHE A CG  
3932  C CD1 . PHE A 464 ? 0.5753 0.6817 0.7571 -0.0222 0.0633  -0.1049 464 PHE A CD1 
3933  C CD2 . PHE A 464 ? 0.5839 0.6283 0.7949 -0.0556 0.0618  -0.1168 464 PHE A CD2 
3934  C CE1 . PHE A 464 ? 0.5509 0.6774 0.7400 -0.0141 0.0597  -0.1388 464 PHE A CE1 
3935  C CE2 . PHE A 464 ? 0.6162 0.6760 0.8354 -0.0470 0.0571  -0.1554 464 PHE A CE2 
3936  C CZ  . PHE A 464 ? 0.5596 0.6643 0.7670 -0.0247 0.0563  -0.1661 464 PHE A CZ  
3937  N N   . ASP A 465 ? 0.6283 0.7163 0.7905 -0.0885 0.0876  -0.0035 465 ASP A N   
3938  C CA  . ASP A 465 ? 0.5956 0.6976 0.7398 -0.0938 0.0946  0.0230  465 ASP A CA  
3939  C C   . ASP A 465 ? 0.6373 0.7905 0.7758 -0.0952 0.1029  0.0146  465 ASP A C   
3940  O O   . ASP A 465 ? 0.6452 0.8161 0.7639 -0.0876 0.1072  0.0222  465 ASP A O   
3941  C CB  . ASP A 465 ? 0.6653 0.7398 0.8129 -0.1182 0.0977  0.0485  465 ASP A CB  
3942  C CG  . ASP A 465 ? 0.7289 0.8244 0.8536 -0.1242 0.1046  0.0782  465 ASP A CG  
3943  O OD1 . ASP A 465 ? 0.6957 0.7780 0.8037 -0.1085 0.0988  0.0954  465 ASP A OD1 
3944  O OD2 . ASP A 465 ? 0.7495 0.8834 0.8737 -0.1448 0.1158  0.0830  465 ASP A OD2 
3945  N N   . LYS A 466 ? 0.5951 0.7743 0.7515 -0.1029 0.1043  -0.0037 466 LYS A N   
3946  C CA  . LYS A 466 ? 0.5583 0.7868 0.7126 -0.0955 0.1102  -0.0129 466 LYS A CA  
3947  C C   . LYS A 466 ? 0.5481 0.7738 0.6844 -0.0695 0.1059  -0.0207 466 LYS A C   
3948  O O   . LYS A 466 ? 0.5647 0.8044 0.6858 -0.0588 0.1110  -0.0199 466 LYS A O   
3949  C CB  . LYS A 466 ? 0.5793 0.8453 0.7590 -0.1058 0.1095  -0.0308 466 LYS A CB  
3950  C CG  . LYS A 466 ? 0.5268 0.8527 0.7104 -0.0943 0.1151  -0.0390 466 LYS A CG  
3951  C CD  . LYS A 466 ? 0.4607 0.8400 0.6744 -0.1152 0.1170  -0.0505 466 LYS A CD  
3952  C CE  . LYS A 466 ? 0.7039 1.1396 0.9278 -0.0910 0.1118  -0.0683 466 LYS A CE  
3953  N NZ  . LYS A 466 ? 0.6191 1.1333 0.8660 -0.0985 0.1201  -0.0744 466 LYS A NZ  
3954  N N   . LEU A 467 ? 0.5780 0.7849 0.7144 -0.0607 0.0972  -0.0296 467 LEU A N   
3955  C CA  . LEU A 467 ? 0.5415 0.7476 0.6591 -0.0429 0.0941  -0.0333 467 LEU A CA  
3956  C C   . LEU A 467 ? 0.5696 0.7571 0.6659 -0.0408 0.0964  -0.0211 467 LEU A C   
3957  O O   . LEU A 467 ? 0.6069 0.7948 0.6848 -0.0345 0.0994  -0.0208 467 LEU A O   
3958  C CB  . LEU A 467 ? 0.5783 0.7834 0.7001 -0.0374 0.0859  -0.0460 467 LEU A CB  
3959  C CG  . LEU A 467 ? 0.5227 0.7585 0.6604 -0.0384 0.0817  -0.0617 467 LEU A CG  
3960  C CD1 . LEU A 467 ? 0.4956 0.7308 0.6422 -0.0398 0.0749  -0.0795 467 LEU A CD1 
3961  C CD2 . LEU A 467 ? 0.4467 0.7044 0.5703 -0.0226 0.0799  -0.0594 467 LEU A CD2 
3962  N N   . PHE A 468 ? 0.6280 0.7986 0.7266 -0.0454 0.0940  -0.0120 468 PHE A N   
3963  C CA  . PHE A 468 ? 0.6567 0.8234 0.7369 -0.0446 0.0945  0.0001  468 PHE A CA  
3964  C C   . PHE A 468 ? 0.6920 0.8721 0.7566 -0.0497 0.1029  0.0041  468 PHE A C   
3965  O O   . PHE A 468 ? 0.6560 0.8371 0.7017 -0.0464 0.1046  -0.0021 468 PHE A O   
3966  C CB  . PHE A 468 ? 0.6116 0.7625 0.6992 -0.0456 0.0899  0.0150  468 PHE A CB  
3967  C CG  . PHE A 468 ? 0.6042 0.7642 0.6742 -0.0426 0.0876  0.0285  468 PHE A CG  
3968  C CD1 . PHE A 468 ? 0.5432 0.7156 0.6078 -0.0341 0.0824  0.0212  468 PHE A CD1 
3969  C CD2 . PHE A 468 ? 0.6404 0.8068 0.6988 -0.0508 0.0905  0.0486  468 PHE A CD2 
3970  C CE1 . PHE A 468 ? 0.5734 0.7665 0.6240 -0.0337 0.0791  0.0309  468 PHE A CE1 
3971  C CE2 . PHE A 468 ? 0.6829 0.8686 0.7237 -0.0482 0.0865  0.0598  468 PHE A CE2 
3972  C CZ  . PHE A 468 ? 0.6094 0.8094 0.6478 -0.0395 0.0802  0.0496  468 PHE A CZ  
3973  N N   . ARG A 469 ? 0.6734 0.8650 0.7458 -0.0596 0.1090  0.0117  469 ARG A N   
3974  C CA  . ARG A 469 ? 0.5646 0.7810 0.6232 -0.0633 0.1188  0.0119  469 ARG A CA  
3975  C C   . ARG A 469 ? 0.6490 0.8736 0.7039 -0.0496 0.1223  -0.0082 469 ARG A C   
3976  O O   . ARG A 469 ? 0.7213 0.9543 0.7584 -0.0453 0.1285  -0.0164 469 ARG A O   
3977  C CB  . ARG A 469 ? 0.5272 0.7651 0.5974 -0.0800 0.1261  0.0244  469 ARG A CB  
3978  C CG  . ARG A 469 ? 0.6376 0.8538 0.7071 -0.0924 0.1216  0.0507  469 ARG A CG  
3979  C CD  . ARG A 469 ? 0.6162 0.8481 0.6923 -0.1164 0.1298  0.0694  469 ARG A CD  
3980  N NE  . ARG A 469 ? 0.7192 0.9176 0.7894 -0.1258 0.1238  0.1010  469 ARG A NE  
3981  C CZ  . ARG A 469 ? 0.6968 0.9035 0.7420 -0.1252 0.1226  0.1242  469 ARG A CZ  
3982  N NH1 . ARG A 469 ? 0.7376 0.9872 0.7608 -0.1203 0.1283  0.1151  469 ARG A NH1 
3983  N NH2 . ARG A 469 ? 0.6653 0.8356 0.7065 -0.1283 0.1143  0.1566  469 ARG A NH2 
3984  N N   . SER A 470 ? 0.7187 0.9396 0.7885 -0.0406 0.1175  -0.0170 470 SER A N   
3985  C CA  . SER A 470 ? 0.6489 0.8702 0.7132 -0.0220 0.1176  -0.0304 470 SER A CA  
3986  C C   . SER A 470 ? 0.6812 0.8659 0.7206 -0.0168 0.1136  -0.0318 470 SER A C   
3987  O O   . SER A 470 ? 0.7296 0.8990 0.7520 -0.0070 0.1168  -0.0406 470 SER A O   
3988  C CB  . SER A 470 ? 0.6073 0.8440 0.6924 -0.0145 0.1115  -0.0353 470 SER A CB  
3989  O OG  . SER A 470 ? 0.7607 1.0159 0.8481 0.0065  0.1126  -0.0446 470 SER A OG  
3990  N N   . PHE A 471 ? 0.6380 0.8088 0.6756 -0.0244 0.1068  -0.0252 471 PHE A N   
3991  C CA  . PHE A 471 ? 0.6448 0.7907 0.6601 -0.0276 0.1040  -0.0251 471 PHE A CA  
3992  C C   . PHE A 471 ? 0.6972 0.8386 0.6935 -0.0376 0.1084  -0.0277 471 PHE A C   
3993  O O   . PHE A 471 ? 0.7746 0.8904 0.7494 -0.0406 0.1094  -0.0350 471 PHE A O   
3994  C CB  . PHE A 471 ? 0.5458 0.6970 0.5670 -0.0339 0.0975  -0.0200 471 PHE A CB  
3995  C CG  . PHE A 471 ? 0.5232 0.6823 0.5560 -0.0261 0.0927  -0.0222 471 PHE A CG  
3996  C CD1 . PHE A 471 ? 0.6272 0.7764 0.6487 -0.0169 0.0909  -0.0215 471 PHE A CD1 
3997  C CD2 . PHE A 471 ? 0.4659 0.6413 0.5191 -0.0266 0.0889  -0.0257 471 PHE A CD2 
3998  C CE1 . PHE A 471 ? 0.5324 0.6998 0.5614 -0.0099 0.0851  -0.0224 471 PHE A CE1 
3999  C CE2 . PHE A 471 ? 0.4468 0.6374 0.5088 -0.0213 0.0842  -0.0331 471 PHE A CE2 
4000  C CZ  . PHE A 471 ? 0.4765 0.6692 0.5256 -0.0137 0.0821  -0.0305 471 PHE A CZ  
4001  N N   . VAL A 472 ? 0.6601 0.8246 0.6618 -0.0448 0.1104  -0.0212 472 VAL A N   
4002  C CA  . VAL A 472 ? 0.6980 0.8722 0.6797 -0.0546 0.1139  -0.0242 472 VAL A CA  
4003  C C   . VAL A 472 ? 0.7655 0.9343 0.7339 -0.0483 0.1224  -0.0420 472 VAL A C   
4004  O O   . VAL A 472 ? 0.8235 0.9779 0.7692 -0.0545 0.1241  -0.0564 472 VAL A O   
4005  C CB  . VAL A 472 ? 0.7289 0.9320 0.7165 -0.0610 0.1135  -0.0074 472 VAL A CB  
4006  C CG1 . VAL A 472 ? 0.7983 1.0220 0.7622 -0.0715 0.1139  -0.0092 472 VAL A CG1 
4007  C CG2 . VAL A 472 ? 0.6438 0.8433 0.6480 -0.0589 0.1042  0.0068  472 VAL A CG2 
4008  N N   . ARG A 473 ? 0.7177 0.9010 0.7014 -0.0360 0.1279  -0.0446 473 ARG A N   
4009  C CA  . ARG A 473 ? 0.7447 0.9337 0.7202 -0.0233 0.1368  -0.0650 473 ARG A CA  
4010  C C   . ARG A 473 ? 0.8234 0.9612 0.7859 -0.0087 0.1337  -0.0794 473 ARG A C   
4011  O O   . ARG A 473 ? 0.8349 0.9501 0.7761 -0.0066 0.1378  -0.0996 473 ARG A O   
4012  C CB  . ARG A 473 ? 0.7336 0.9638 0.7337 -0.0133 0.1430  -0.0642 473 ARG A CB  
4013  C CG  . ARG A 473 ? 0.8589 1.0976 0.8601 0.0120  0.1499  -0.0878 473 ARG A CG  
4014  C CD  . ARG A 473 ? 0.9936 1.2837 1.0260 0.0227  0.1536  -0.0870 473 ARG A CD  
4015  N NE  . ARG A 473 ? 1.0681 1.3881 1.1179 -0.0032 0.1535  -0.0656 473 ARG A NE  
4016  C CZ  . ARG A 473 ? 1.0050 1.3423 1.0816 -0.0056 0.1488  -0.0583 473 ARG A CZ  
4017  N NH1 . ARG A 473 ? 1.0413 1.3791 1.1305 0.0178  0.1425  -0.0675 473 ARG A NH1 
4018  N NH2 . ARG A 473 ? 0.8930 1.2448 0.9825 -0.0325 0.1493  -0.0410 473 ARG A NH2 
4019  N N   . ARG A 474 ? 0.8666 0.9823 0.8390 0.0000  0.1260  -0.0687 474 ARG A N   
4020  C CA  . ARG A 474 ? 0.8499 0.9104 0.8066 0.0124  0.1215  -0.0728 474 ARG A CA  
4021  C C   . ARG A 474 ? 0.8319 0.8511 0.7615 -0.0111 0.1195  -0.0746 474 ARG A C   
4022  O O   . ARG A 474 ? 0.8496 0.8117 0.7586 -0.0073 0.1186  -0.0827 474 ARG A O   
4023  C CB  . ARG A 474 ? 0.7629 0.8231 0.7332 0.0230  0.1128  -0.0560 474 ARG A CB  
4024  C CG  . ARG A 474 ? 0.8278 0.8307 0.7780 0.0328  0.1062  -0.0489 474 ARG A CG  
4025  C CD  . ARG A 474 ? 0.8385 0.8229 0.7893 0.0686  0.1066  -0.0593 474 ARG A CD  
4026  N NE  . ARG A 474 ? 1.0155 0.9474 0.9431 0.0696  0.1121  -0.0787 474 ARG A NE  
4027  C CZ  . ARG A 474 ? 1.0176 0.8730 0.9159 0.0604  0.1087  -0.0756 474 ARG A CZ  
4028  N NH1 . ARG A 474 ? 0.9859 0.8096 0.8726 0.0531  0.1002  -0.0494 474 ARG A NH1 
4029  N NH2 . ARG A 474 ? 0.9931 0.8044 0.8714 0.0548  0.1145  -0.1003 474 ARG A NH2 
4030  N N   . ALA A 475 ? 0.8314 0.8790 0.7612 -0.0355 0.1184  -0.0676 475 ALA A N   
4031  C CA  . ALA A 475 ? 0.8433 0.8717 0.7514 -0.0618 0.1165  -0.0716 475 ALA A CA  
4032  C C   . ALA A 475 ? 0.8558 0.8736 0.7427 -0.0697 0.1223  -0.0969 475 ALA A C   
4033  O O   . ALA A 475 ? 0.9136 0.9037 0.7793 -0.0932 0.1209  -0.1069 475 ALA A O   
4034  C CB  . ALA A 475 ? 0.7003 0.7757 0.6192 -0.0785 0.1121  -0.0578 475 ALA A CB  
4035  N N   . GLN A 476 ? 0.8458 0.8909 0.7372 -0.0539 0.1294  -0.1099 476 GLN A N   
4036  C CA  . GLN A 476 ? 0.9161 0.9623 0.7863 -0.0595 0.1361  -0.1395 476 GLN A CA  
4037  C C   . GLN A 476 ? 1.0135 1.0173 0.8785 -0.0309 0.1421  -0.1647 476 GLN A C   
4038  O O   . GLN A 476 ? 0.9393 0.9656 0.7964 -0.0223 0.1508  -0.1923 476 GLN A O   
4039  C CB  . GLN A 476 ? 0.8848 1.0061 0.7590 -0.0647 0.1409  -0.1368 476 GLN A CB  
4040  C CG  . GLN A 476 ? 0.8398 0.9999 0.7309 -0.0748 0.1341  -0.1033 476 GLN A CG  
4041  C CD  . GLN A 476 ? 0.8663 1.0889 0.7609 -0.0768 0.1384  -0.0914 476 GLN A CD  
4042  O OE1 . GLN A 476 ? 0.8156 1.0724 0.6897 -0.0870 0.1423  -0.1040 476 GLN A OE1 
4043  N NE2 . GLN A 476 ? 0.8600 1.0978 0.7788 -0.0696 0.1377  -0.0667 476 GLN A NE2 
4044  N N   . GLU A 477 ? 0.9022 0.8485 0.7707 -0.0134 0.1370  -0.1556 477 GLU A N   
4045  C CA  . GLU A 477 ? 0.8924 0.7896 0.7566 0.0211  0.1398  -0.1766 477 GLU A CA  
4046  C C   . GLU A 477 ? 0.9045 0.7028 0.7483 0.0194  0.1321  -0.1706 477 GLU A C   
4047  O O   . GLU A 477 ? 0.9507 0.6911 0.7901 0.0530  0.1308  -0.1799 477 GLU A O   
4048  C CB  . GLU A 477 ? 0.9365 0.8777 0.8310 0.0574  0.1407  -0.1665 477 GLU A CB  
4049  C CG  . GLU A 477 ? 1.0062 1.0422 0.9206 0.0533  0.1493  -0.1674 477 GLU A CG  
4050  C CD  . GLU A 477 ? 1.0661 1.1513 1.0136 0.0757  0.1486  -0.1523 477 GLU A CD  
4051  O OE1 . GLU A 477 ? 1.1078 1.1608 1.0625 0.1022  0.1413  -0.1461 477 GLU A OE1 
4052  O OE2 . GLU A 477 ? 1.0543 1.2113 1.0194 0.0653  0.1549  -0.1458 477 GLU A OE2 
4053  N N   . MET B 1   ? 0.9019 1.7253 1.1956 -0.0392 -0.1466 0.2246  1   MET B N   
4054  C CA  . MET B 1   ? 0.8626 1.6558 1.1802 -0.0341 -0.1336 0.2603  1   MET B CA  
4055  C C   . MET B 1   ? 0.7246 1.4187 1.0468 -0.0380 -0.1196 0.2320  1   MET B C   
4056  O O   . MET B 1   ? 0.7673 1.4306 1.0513 -0.0397 -0.1162 0.1904  1   MET B O   
4057  C CB  . MET B 1   ? 0.9105 1.7559 1.1966 -0.0279 -0.1325 0.2729  1   MET B CB  
4058  C CG  . MET B 1   ? 1.0150 1.9623 1.2731 -0.0266 -0.1470 0.2781  1   MET B CG  
4059  S SD  . MET B 1   ? 1.2283 2.1852 1.4253 -0.0319 -0.1522 0.2050  1   MET B SD  
4060  C CE  . MET B 1   ? 0.9874 1.9328 1.1523 -0.0267 -0.1398 0.1963  1   MET B CE  
4061  N N   . LYS B 2   ? 0.6032 1.2507 0.9745 -0.0397 -0.1114 0.2546  2   LYS B N   
4062  C CA  . LYS B 2   ? 0.5108 1.0716 0.8897 -0.0440 -0.0971 0.2338  2   LYS B CA  
4063  C C   . LYS B 2   ? 0.5708 1.1217 0.9251 -0.0398 -0.0885 0.2329  2   LYS B C   
4064  O O   . LYS B 2   ? 0.6010 1.1896 0.9688 -0.0335 -0.0859 0.2717  2   LYS B O   
4065  C CB  . LYS B 2   ? 0.4791 1.0068 0.9204 -0.0461 -0.0881 0.2646  2   LYS B CB  
4066  C CG  . LYS B 2   ? 0.5440 0.9924 0.9973 -0.0512 -0.0721 0.2485  2   LYS B CG  
4067  C CD  . LYS B 2   ? 0.5543 0.9636 1.0638 -0.0573 -0.0647 0.2577  2   LYS B CD  
4068  C CE  . LYS B 2   ? 0.4683 0.8578 1.0273 -0.0563 -0.0498 0.2895  2   LYS B CE  
4069  N NZ  . LYS B 2   ? 0.5701 0.8956 1.1139 -0.0622 -0.0368 0.2601  2   LYS B NZ  
4070  N N   . LYS B 3   ? 0.5237 1.0257 0.8440 -0.0432 -0.0840 0.1900  3   LYS B N   
4071  C CA  . LYS B 3   ? 0.5889 1.0823 0.8821 -0.0392 -0.0771 0.1836  3   LYS B CA  
4072  C C   . LYS B 3   ? 0.5965 1.0126 0.9035 -0.0438 -0.0635 0.1734  3   LYS B C   
4073  O O   . LYS B 3   ? 0.6070 0.9712 0.9148 -0.0511 -0.0615 0.1451  3   LYS B O   
4074  C CB  . LYS B 3   ? 0.5553 1.0663 0.7968 -0.0385 -0.0836 0.1424  3   LYS B CB  
4075  C CG  . LYS B 3   ? 0.6492 1.2445 0.8680 -0.0321 -0.0915 0.1563  3   LYS B CG  
4076  C CD  . LYS B 3   ? 0.6405 1.2556 0.8145 -0.0329 -0.0974 0.1098  3   LYS B CD  
4077  C CE  . LYS B 3   ? 0.7315 1.4415 0.8871 -0.0300 -0.1083 0.1190  3   LYS B CE  
4078  N NZ  . LYS B 3   ? 0.9891 1.7249 1.1027 -0.0288 -0.1086 0.0804  3   LYS B NZ  
4079  N N   . LEU B 4   ? 0.5610 0.9731 0.8803 -0.0402 -0.0542 0.1972  4   LEU B N   
4080  C CA  . LEU B 4   ? 0.5607 0.9089 0.8844 -0.0445 -0.0419 0.1837  4   LEU B CA  
4081  C C   . LEU B 4   ? 0.5571 0.8882 0.8322 -0.0437 -0.0428 0.1470  4   LEU B C   
4082  O O   . LEU B 4   ? 0.5187 0.8928 0.7646 -0.0371 -0.0475 0.1454  4   LEU B O   
4083  C CB  . LEU B 4   ? 0.5286 0.8823 0.8842 -0.0410 -0.0316 0.2203  4   LEU B CB  
4084  C CG  . LEU B 4   ? 0.5284 0.8262 0.8880 -0.0454 -0.0189 0.2081  4   LEU B CG  
4085  C CD1 . LEU B 4   ? 0.5108 0.7984 0.9281 -0.0474 -0.0072 0.2406  4   LEU B CD1 
4086  C CD2 . LEU B 4   ? 0.4435 0.7494 0.7653 -0.0400 -0.0177 0.1987  4   LEU B CD2 
4087  N N   . PHE B 5   ? 0.5861 0.8561 0.8551 -0.0506 -0.0375 0.1184  5   PHE B N   
4088  C CA  . PHE B 5   ? 0.5565 0.8033 0.7873 -0.0502 -0.0373 0.0854  5   PHE B CA  
4089  C C   . PHE B 5   ? 0.5521 0.7663 0.7871 -0.0508 -0.0266 0.0911  5   PHE B C   
4090  O O   . PHE B 5   ? 0.5445 0.7153 0.8018 -0.0584 -0.0188 0.0914  5   PHE B O   
4091  C CB  . PHE B 5   ? 0.4177 0.6241 0.6381 -0.0575 -0.0399 0.0504  5   PHE B CB  
4092  C CG  . PHE B 5   ? 0.5338 0.7731 0.7478 -0.0572 -0.0508 0.0391  5   PHE B CG  
4093  C CD1 . PHE B 5   ? 0.6380 0.9305 0.8268 -0.0506 -0.0586 0.0322  5   PHE B CD1 
4094  C CD2 . PHE B 5   ? 0.5629 0.7826 0.7967 -0.0642 -0.0527 0.0336  5   PHE B CD2 
4095  C CE1 . PHE B 5   ? 0.5570 0.8846 0.7404 -0.0515 -0.0688 0.0193  5   PHE B CE1 
4096  C CE2 . PHE B 5   ? 0.5899 0.8419 0.8192 -0.0644 -0.0631 0.0223  5   PHE B CE2 
4097  C CZ  . PHE B 5   ? 0.5488 0.8557 0.7527 -0.0582 -0.0714 0.0148  5   PHE B CZ  
4098  N N   . LEU B 6   ? 0.5495 0.7875 0.7636 -0.0436 -0.0260 0.0940  6   LEU B N   
4099  C CA  . LEU B 6   ? 0.5324 0.7481 0.7491 -0.0431 -0.0169 0.1004  6   LEU B CA  
4100  C C   . LEU B 6   ? 0.4969 0.6867 0.6804 -0.0426 -0.0174 0.0683  6   LEU B C   
4101  O O   . LEU B 6   ? 0.5256 0.7410 0.6822 -0.0371 -0.0233 0.0517  6   LEU B O   
4102  C CB  . LEU B 6   ? 0.4725 0.7361 0.6956 -0.0348 -0.0147 0.1316  6   LEU B CB  
4103  C CG  . LEU B 6   ? 0.3936 0.6410 0.6281 -0.0341 -0.0045 0.1443  6   LEU B CG  
4104  C CD1 . LEU B 6   ? 0.4583 0.6624 0.7301 -0.0433 0.0043  0.1508  6   LEU B CD1 
4105  C CD2 . LEU B 6   ? 0.4463 0.7471 0.6915 -0.0260 -0.0029 0.1788  6   LEU B CD2 
4106  N N   . VAL B 7   ? 0.4760 0.6180 0.6640 -0.0488 -0.0108 0.0598  7   VAL B N   
4107  C CA  . VAL B 7   ? 0.5694 0.6837 0.7321 -0.0488 -0.0110 0.0337  7   VAL B CA  
4108  C C   . VAL B 7   ? 0.4993 0.6016 0.6664 -0.0484 -0.0034 0.0442  7   VAL B C   
4109  O O   . VAL B 7   ? 0.4593 0.5391 0.6495 -0.0557 0.0034  0.0551  7   VAL B O   
4110  C CB  . VAL B 7   ? 0.5509 0.6200 0.7124 -0.0580 -0.0118 0.0112  7   VAL B CB  
4111  C CG1 . VAL B 7   ? 0.5223 0.5609 0.6658 -0.0585 -0.0102 -0.0072 7   VAL B CG1 
4112  C CG2 . VAL B 7   ? 0.4090 0.4904 0.5637 -0.0577 -0.0197 -0.0043 7   VAL B CG2 
4113  N N   . PHE B 8   ? 0.5506 0.6695 0.6976 -0.0405 -0.0041 0.0392  8   PHE B N   
4114  C CA  . PHE B 8   ? 0.4699 0.5809 0.6185 -0.0391 0.0020  0.0469  8   PHE B CA  
4115  C C   . PHE B 8   ? 0.5382 0.6142 0.6698 -0.0411 0.0011  0.0229  8   PHE B C   
4116  O O   . PHE B 8   ? 0.5748 0.6548 0.6876 -0.0362 -0.0037 0.0031  8   PHE B O   
4117  C CB  . PHE B 8   ? 0.4450 0.6014 0.5854 -0.0285 0.0025  0.0593  8   PHE B CB  
4118  C CG  . PHE B 8   ? 0.4288 0.6171 0.5931 -0.0267 0.0065  0.0923  8   PHE B CG  
4119  C CD1 . PHE B 8   ? 0.3617 0.5353 0.5531 -0.0309 0.0149  0.1109  8   PHE B CD1 
4120  C CD2 . PHE B 8   ? 0.4347 0.6711 0.5972 -0.0211 0.0021  0.1054  8   PHE B CD2 
4121  C CE1 . PHE B 8   ? 0.5421 0.7447 0.7627 -0.0289 0.0198  0.1431  8   PHE B CE1 
4122  C CE2 . PHE B 8   ? 0.4334 0.7019 0.6219 -0.0189 0.0059  0.1405  8   PHE B CE2 
4123  C CZ  . PHE B 8   ? 0.4963 0.7461 0.7160 -0.0225 0.0152  0.1600  8   PHE B CZ  
4124  N N   . TRP B 9   ? 0.5449 0.5892 0.6858 -0.0488 0.0059  0.0248  9   TRP B N   
4125  C CA  . TRP B 9   ? 0.4652 0.4787 0.5933 -0.0516 0.0049  0.0080  9   TRP B CA  
4126  C C   . TRP B 9   ? 0.5269 0.5399 0.6605 -0.0517 0.0102  0.0191  9   TRP B C   
4127  O O   . TRP B 9   ? 0.6279 0.6300 0.7793 -0.0604 0.0157  0.0287  9   TRP B O   
4128  C CB  . TRP B 9   ? 0.4740 0.4517 0.6064 -0.0633 0.0048  -0.0021 9   TRP B CB  
4129  C CG  . TRP B 9   ? 0.4797 0.4308 0.5976 -0.0648 0.0017  -0.0195 9   TRP B CG  
4130  C CD1 . TRP B 9   ? 0.5790 0.5310 0.6860 -0.0578 0.0001  -0.0248 9   TRP B CD1 
4131  C CD2 . TRP B 9   ? 0.4365 0.3576 0.5536 -0.0739 0.0004  -0.0314 9   TRP B CD2 
4132  N NE1 . TRP B 9   ? 0.5512 0.4756 0.6529 -0.0615 -0.0024 -0.0375 9   TRP B NE1 
4133  C CE2 . TRP B 9   ? 0.4946 0.4002 0.6011 -0.0716 -0.0022 -0.0413 9   TRP B CE2 
4134  C CE3 . TRP B 9   ? 0.5546 0.4613 0.6811 -0.0837 0.0016  -0.0338 9   TRP B CE3 
4135  C CZ2 . TRP B 9   ? 0.6542 0.5315 0.7591 -0.0787 -0.0037 -0.0513 9   TRP B CZ2 
4136  C CZ3 . TRP B 9   ? 0.6690 0.5474 0.7912 -0.0912 0.0004  -0.0461 9   TRP B CZ3 
4137  C CH2 . TRP B 9   ? 0.6586 0.5231 0.7699 -0.0887 -0.0022 -0.0537 9   TRP B CH2 
4138  N N   . TRP B 10  ? 0.5340 0.5614 0.6554 -0.0424 0.0091  0.0164  10  TRP B N   
4139  C CA  . TRP B 10  ? 0.4692 0.4993 0.5955 -0.0414 0.0134  0.0261  10  TRP B CA  
4140  C C   . TRP B 10  ? 0.5076 0.5089 0.6262 -0.0455 0.0114  0.0145  10  TRP B C   
4141  O O   . TRP B 10  ? 0.5966 0.5897 0.7028 -0.0409 0.0068  -0.0001 10  TRP B O   
4142  C CB  . TRP B 10  ? 0.4830 0.5474 0.6022 -0.0288 0.0139  0.0308  10  TRP B CB  
4143  C CG  . TRP B 10  ? 0.4170 0.5179 0.5424 -0.0240 0.0156  0.0464  10  TRP B CG  
4144  C CD1 . TRP B 10  ? 0.4533 0.5845 0.5661 -0.0165 0.0120  0.0411  10  TRP B CD1 
4145  C CD2 . TRP B 10  ? 0.4445 0.5602 0.5930 -0.0265 0.0218  0.0712  10  TRP B CD2 
4146  N NE1 . TRP B 10  ? 0.4661 0.6325 0.5899 -0.0140 0.0145  0.0638  10  TRP B NE1 
4147  C CE2 . TRP B 10  ? 0.4671 0.6228 0.6153 -0.0196 0.0208  0.0837  10  TRP B CE2 
4148  C CE3 . TRP B 10  ? 0.4566 0.5577 0.6291 -0.0343 0.0285  0.0835  10  TRP B CE3 
4149  C CZ2 . TRP B 10  ? 0.3843 0.5640 0.5573 -0.0194 0.0263  0.1119  10  TRP B CZ2 
4150  C CZ3 . TRP B 10  ? 0.3594 0.4819 0.5592 -0.0344 0.0348  0.1080  10  TRP B CZ3 
4151  C CH2 . TRP B 10  ? 0.3395 0.4999 0.5403 -0.0266 0.0336  0.1239  10  TRP B CH2 
4152  N N   . HIS B 11  ? 0.5923 0.5809 0.7211 -0.0547 0.0151  0.0211  11  HIS B N   
4153  C CA  . HIS B 11  ? 0.5682 0.5348 0.6906 -0.0604 0.0128  0.0141  11  HIS B CA  
4154  C C   . HIS B 11  ? 0.5304 0.5098 0.6524 -0.0539 0.0134  0.0199  11  HIS B C   
4155  O O   . HIS B 11  ? 0.5465 0.5413 0.6808 -0.0546 0.0185  0.0314  11  HIS B O   
4156  C CB  . HIS B 11  ? 0.5435 0.4935 0.6760 -0.0763 0.0164  0.0150  11  HIS B CB  
4157  C CG  . HIS B 11  ? 0.5475 0.4839 0.6733 -0.0834 0.0140  0.0114  11  HIS B CG  
4158  N ND1 . HIS B 11  ? 0.5877 0.5103 0.6999 -0.0804 0.0078  0.0045  11  HIS B ND1 
4159  C CD2 . HIS B 11  ? 0.5380 0.4754 0.6708 -0.0942 0.0171  0.0145  11  HIS B CD2 
4160  C CE1 . HIS B 11  ? 0.6004 0.5175 0.7104 -0.0883 0.0064  0.0068  11  HIS B CE1 
4161  N NE2 . HIS B 11  ? 0.5633 0.4906 0.6837 -0.0972 0.0117  0.0115  11  HIS B NE2 
4162  N N   . MET B 12  ? 0.5127 0.4854 0.6248 -0.0477 0.0087  0.0123  12  MET B N   
4163  C CA  . MET B 12  ? 0.5131 0.4973 0.6265 -0.0406 0.0086  0.0168  12  MET B CA  
4164  C C   . MET B 12  ? 0.5744 0.5404 0.6864 -0.0467 0.0045  0.0160  12  MET B C   
4165  O O   . MET B 12  ? 0.5704 0.5199 0.6778 -0.0455 0.0001  0.0082  12  MET B O   
4166  C CB  . MET B 12  ? 0.5139 0.5130 0.6221 -0.0258 0.0076  0.0092  12  MET B CB  
4167  C CG  . MET B 12  ? 0.4726 0.4927 0.5779 -0.0209 0.0098  0.0081  12  MET B CG  
4168  S SD  . MET B 12  ? 0.7346 0.7828 0.8510 -0.0209 0.0167  0.0287  12  MET B SD  
4169  C CE  . MET B 12  ? 0.6044 0.6913 0.7127 -0.0075 0.0180  0.0268  12  MET B CE  
4170  N N   . HIS B 13  ? 0.5855 0.5570 0.7036 -0.0537 0.0060  0.0249  13  HIS B N   
4171  C CA  . HIS B 13  ? 0.5486 0.5103 0.6650 -0.0610 0.0015  0.0271  13  HIS B CA  
4172  C C   . HIS B 13  ? 0.5581 0.5375 0.6821 -0.0609 0.0022  0.0360  13  HIS B C   
4173  O O   . HIS B 13  ? 0.4977 0.4920 0.6308 -0.0624 0.0079  0.0402  13  HIS B O   
4174  C CB  . HIS B 13  ? 0.4968 0.4453 0.6107 -0.0780 0.0020  0.0247  13  HIS B CB  
4175  C CG  . HIS B 13  ? 0.4917 0.4413 0.6037 -0.0887 -0.0015 0.0295  13  HIS B CG  
4176  N ND1 . HIS B 13  ? 0.5453 0.4877 0.6525 -0.0858 -0.0084 0.0336  13  HIS B ND1 
4177  C CD2 . HIS B 13  ? 0.5117 0.4715 0.6275 -0.1032 0.0010  0.0308  13  HIS B CD2 
4178  C CE1 . HIS B 13  ? 0.5635 0.5145 0.6689 -0.0978 -0.0110 0.0398  13  HIS B CE1 
4179  N NE2 . HIS B 13  ? 0.5552 0.5176 0.6646 -0.1091 -0.0053 0.0362  13  HIS B NE2 
4180  N N   . GLN B 14  ? 0.5642 0.5427 0.6879 -0.0591 -0.0036 0.0402  14  GLN B N   
4181  C CA  . GLN B 14  ? 0.5206 0.5160 0.6513 -0.0623 -0.0046 0.0489  14  GLN B CA  
4182  C C   . GLN B 14  ? 0.5749 0.5664 0.7021 -0.0703 -0.0120 0.0547  14  GLN B C   
4183  O O   . GLN B 14  ? 0.6633 0.6426 0.7896 -0.0635 -0.0170 0.0565  14  GLN B O   
4184  C CB  . GLN B 14  ? 0.5527 0.5625 0.6915 -0.0466 -0.0038 0.0525  14  GLN B CB  
4185  C CG  . GLN B 14  ? 0.5117 0.5344 0.6544 -0.0400 0.0039  0.0510  14  GLN B CG  
4186  C CD  . GLN B 14  ? 0.5568 0.5933 0.7099 -0.0498 0.0096  0.0565  14  GLN B CD  
4187  O OE1 . GLN B 14  ? 0.5255 0.5657 0.6828 -0.0610 0.0077  0.0588  14  GLN B OE1 
4188  N NE2 . GLN B 14  ? 0.5834 0.6309 0.7435 -0.0457 0.0169  0.0589  14  GLN B NE2 
4189  N N   . PRO B 15  ? 0.5422 0.5461 0.6694 -0.0851 -0.0127 0.0579  15  PRO B N   
4190  C CA  . PRO B 15  ? 0.4878 0.4964 0.6107 -0.0931 -0.0205 0.0665  15  PRO B CA  
4191  C C   . PRO B 15  ? 0.5727 0.5903 0.7048 -0.0805 -0.0268 0.0787  15  PRO B C   
4192  O O   . PRO B 15  ? 0.6380 0.6611 0.7796 -0.0671 -0.0244 0.0786  15  PRO B O   
4193  C CB  . PRO B 15  ? 0.4882 0.5172 0.6112 -0.1115 -0.0183 0.0640  15  PRO B CB  
4194  C CG  . PRO B 15  ? 0.4523 0.4890 0.5875 -0.1084 -0.0099 0.0580  15  PRO B CG  
4195  C CD  . PRO B 15  ? 0.5990 0.6158 0.7328 -0.0965 -0.0056 0.0532  15  PRO B CD  
4196  N N   . LEU B 16  ? 0.5965 0.6178 0.7274 -0.0851 -0.0348 0.0907  16  LEU B N   
4197  C CA  . LEU B 16  ? 0.5377 0.5689 0.6824 -0.0743 -0.0416 0.1057  16  LEU B CA  
4198  C C   . LEU B 16  ? 0.5626 0.6240 0.7127 -0.0789 -0.0432 0.1111  16  LEU B C   
4199  O O   . LEU B 16  ? 0.5416 0.6232 0.6851 -0.0949 -0.0471 0.1157  16  LEU B O   
4200  C CB  . LEU B 16  ? 0.4649 0.4931 0.6104 -0.0782 -0.0496 0.1210  16  LEU B CB  
4201  C CG  . LEU B 16  ? 0.5600 0.5924 0.7275 -0.0643 -0.0561 0.1385  16  LEU B CG  
4202  C CD1 . LEU B 16  ? 0.6344 0.6538 0.8182 -0.0444 -0.0508 0.1287  16  LEU B CD1 
4203  C CD2 . LEU B 16  ? 0.4331 0.4539 0.6061 -0.0657 -0.0616 0.1532  16  LEU B CD2 
4204  N N   . TYR B 17  ? 0.6012 0.6682 0.7638 -0.0657 -0.0398 0.1092  17  TYR B N   
4205  C CA  . TYR B 17  ? 0.5291 0.6238 0.7010 -0.0678 -0.0404 0.1137  17  TYR B CA  
4206  C C   . TYR B 17  ? 0.5267 0.6366 0.7137 -0.0600 -0.0493 0.1312  17  TYR B C   
4207  O O   . TYR B 17  ? 0.6057 0.7399 0.8028 -0.0603 -0.0507 0.1358  17  TYR B O   
4208  C CB  . TYR B 17  ? 0.5368 0.6323 0.7163 -0.0578 -0.0312 0.1043  17  TYR B CB  
4209  C CG  . TYR B 17  ? 0.4812 0.5687 0.6525 -0.0658 -0.0221 0.0910  17  TYR B CG  
4210  C CD1 . TYR B 17  ? 0.4635 0.5607 0.6312 -0.0848 -0.0202 0.0858  17  TYR B CD1 
4211  C CD2 . TYR B 17  ? 0.5363 0.6101 0.7067 -0.0548 -0.0151 0.0836  17  TYR B CD2 
4212  C CE1 . TYR B 17  ? 0.5071 0.5965 0.6746 -0.0916 -0.0111 0.0747  17  TYR B CE1 
4213  C CE2 . TYR B 17  ? 0.6026 0.6712 0.7696 -0.0614 -0.0073 0.0752  17  TYR B CE2 
4214  C CZ  . TYR B 17  ? 0.6140 0.6886 0.7818 -0.0792 -0.0050 0.0713  17  TYR B CZ  
4215  O OH  . TYR B 17  ? 0.5416 0.6101 0.7128 -0.0847 0.0037  0.0640  17  TYR B OH  
4216  N N   . ARG B 18  ? 0.5329 0.6295 0.7257 -0.0528 -0.0550 0.1419  18  ARG B N   
4217  C CA  . ARG B 18  ? 0.6328 0.7408 0.8479 -0.0423 -0.0624 0.1604  18  ARG B CA  
4218  C C   . ARG B 18  ? 0.6396 0.7707 0.8512 -0.0562 -0.0734 0.1800  18  ARG B C   
4219  O O   . ARG B 18  ? 0.6095 0.7312 0.8119 -0.0636 -0.0767 0.1864  18  ARG B O   
4220  C CB  . ARG B 18  ? 0.6136 0.6949 0.8453 -0.0256 -0.0608 0.1606  18  ARG B CB  
4221  C CG  . ARG B 18  ? 0.6507 0.7379 0.9105 -0.0170 -0.0688 0.1832  18  ARG B CG  
4222  C CD  . ARG B 18  ? 0.5817 0.6384 0.8580 -0.0057 -0.0659 0.1805  18  ARG B CD  
4223  N NE  . ARG B 18  ? 0.5353 0.5919 0.8512 0.0109  -0.0673 0.1917  18  ARG B NE  
4224  C CZ  . ARG B 18  ? 0.6235 0.6883 0.9636 0.0120  -0.0759 0.2188  18  ARG B CZ  
4225  N NH1 . ARG B 18  ? 0.7203 0.7985 1.0453 -0.0031 -0.0846 0.2383  18  ARG B NH1 
4226  N NH2 . ARG B 18  ? 0.6237 0.6857 1.0064 0.0283  -0.0752 0.2271  18  ARG B NH2 
4227  N N   . GLU B 19  ? 0.6064 0.7705 0.8256 -0.0601 -0.0790 0.1901  19  GLU B N   
4228  C CA  . GLU B 19  ? 0.6815 0.8766 0.8962 -0.0744 -0.0901 0.2092  19  GLU B CA  
4229  C C   . GLU B 19  ? 0.6631 0.8538 0.8973 -0.0646 -0.0985 0.2356  19  GLU B C   
4230  O O   . GLU B 19  ? 0.6756 0.8551 0.9376 -0.0458 -0.0979 0.2422  19  GLU B O   
4231  C CB  . GLU B 19  ? 0.5719 0.8062 0.7934 -0.0799 -0.0945 0.2129  19  GLU B CB  
4232  C CG  . GLU B 19  ? 0.5751 0.8484 0.7798 -0.1032 -0.1019 0.2175  19  GLU B CG  
4233  C CD  . GLU B 19  ? 0.6716 0.9793 0.8890 -0.1036 -0.1164 0.2484  19  GLU B CD  
4234  O OE1 . GLU B 19  ? 0.6761 0.9707 0.9174 -0.0857 -0.1202 0.2680  19  GLU B OE1 
4235  O OE2 . GLU B 19  ? 0.6323 0.9826 0.8383 -0.1221 -0.1237 0.2532  19  GLU B OE2 
4236  N N   . PRO B 20  ? 0.6563 0.8571 0.8799 -0.0770 -0.1056 0.2513  20  PRO B N   
4237  C CA  . PRO B 20  ? 0.6105 0.8020 0.8572 -0.0672 -0.1117 0.2779  20  PRO B CA  
4238  C C   . PRO B 20  ? 0.7538 0.9714 1.0328 -0.0572 -0.1214 0.3062  20  PRO B C   
4239  O O   . PRO B 20  ? 0.8574 1.0557 1.1706 -0.0396 -0.1211 0.3189  20  PRO B O   
4240  C CB  . PRO B 20  ? 0.7062 0.9102 0.9295 -0.0863 -0.1165 0.2884  20  PRO B CB  
4241  C CG  . PRO B 20  ? 0.7165 0.9542 0.9114 -0.1067 -0.1171 0.2742  20  PRO B CG  
4242  C CD  . PRO B 20  ? 0.6341 0.8516 0.8264 -0.1004 -0.1061 0.2437  20  PRO B CD  
4243  N N   . TYR B 21  ? 0.6536 0.9163 0.9263 -0.0682 -0.1298 0.3162  21  TYR B N   
4244  C CA  . TYR B 21  ? 0.6330 0.9247 0.9380 -0.0594 -0.1403 0.3463  21  TYR B CA  
4245  C C   . TYR B 21  ? 0.6678 0.9469 1.0012 -0.0399 -0.1347 0.3365  21  TYR B C   
4246  O O   . TYR B 21  ? 0.6656 0.9335 1.0380 -0.0220 -0.1358 0.3531  21  TYR B O   
4247  C CB  . TYR B 21  ? 0.7137 1.0626 1.0026 -0.0785 -0.1517 0.3587  21  TYR B CB  
4248  C CG  . TYR B 21  ? 0.7261 1.0959 0.9862 -0.0994 -0.1571 0.3680  21  TYR B CG  
4249  C CD1 . TYR B 21  ? 0.6908 1.0610 0.9636 -0.0972 -0.1638 0.4005  21  TYR B CD1 
4250  C CD2 . TYR B 21  ? 0.7365 1.1264 0.9598 -0.1217 -0.1542 0.3440  21  TYR B CD2 
4251  C CE1 . TYR B 21  ? 0.7431 1.1350 0.9887 -0.1169 -0.1681 0.4099  21  TYR B CE1 
4252  C CE2 . TYR B 21  ? 0.6992 1.1107 0.8961 -0.1417 -0.1579 0.3501  21  TYR B CE2 
4253  C CZ  . TYR B 21  ? 0.7227 1.1361 0.9288 -0.1393 -0.1650 0.3836  21  TYR B CZ  
4254  O OH  . TYR B 21  ? 0.7710 1.2089 0.9499 -0.1597 -0.1681 0.3907  21  TYR B OH  
4255  N N   . THR B 22  ? 0.6553 0.9373 0.9728 -0.0433 -0.1277 0.3097  22  THR B N   
4256  C CA  . THR B 22  ? 0.6491 0.9236 0.9912 -0.0260 -0.1215 0.3002  22  THR B CA  
4257  C C   . THR B 22  ? 0.6485 0.8771 1.0028 -0.0087 -0.1096 0.2835  22  THR B C   
4258  O O   . THR B 22  ? 0.7067 0.9285 1.0911 0.0087  -0.1053 0.2819  22  THR B O   
4259  C CB  . THR B 22  ? 0.6794 0.9711 1.0031 -0.0353 -0.1166 0.2780  22  THR B CB  
4260  O OG1 . THR B 22  ? 0.8571 1.1447 1.2053 -0.0187 -0.1104 0.2710  22  THR B OG1 
4261  C CG2 . THR B 22  ? 0.5771 0.8447 0.8695 -0.0446 -0.1059 0.2502  22  THR B CG2 
4262  N N   . GLY B 23  ? 0.6841 0.8837 1.0170 -0.0134 -0.1039 0.2699  23  GLY B N   
4263  C CA  . GLY B 23  ? 0.7222 0.8829 1.0645 0.0014  -0.0926 0.2509  23  GLY B CA  
4264  C C   . GLY B 23  ? 0.7194 0.8739 1.0513 0.0062  -0.0815 0.2235  23  GLY B C   
4265  O O   . GLY B 23  ? 0.7865 0.9207 1.1340 0.0215  -0.0727 0.2095  23  GLY B O   
4266  N N   . GLU B 24  ? 0.7208 0.8947 1.0289 -0.0069 -0.0809 0.2151  24  GLU B N   
4267  C CA  . GLU B 24  ? 0.6928 0.8673 0.9959 -0.0028 -0.0708 0.1949  24  GLU B CA  
4268  C C   . GLU B 24  ? 0.6072 0.7719 0.8787 -0.0160 -0.0642 0.1764  24  GLU B C   
4269  O O   . GLU B 24  ? 0.6580 0.8319 0.9111 -0.0334 -0.0688 0.1789  24  GLU B O   
4270  C CB  . GLU B 24  ? 0.6407 0.8495 0.9555 -0.0048 -0.0745 0.2029  24  GLU B CB  
4271  C CG  . GLU B 24  ? 0.5683 0.7805 0.9161 0.0143  -0.0719 0.2068  24  GLU B CG  
4272  C CD  . GLU B 24  ? 0.9614 1.2089 1.3286 0.0127  -0.0809 0.2250  24  GLU B CD  
4273  O OE1 . GLU B 24  ? 1.0431 1.3155 1.3954 -0.0044 -0.0886 0.2315  24  GLU B OE1 
4274  O OE2 . GLU B 24  ? 1.2231 1.4758 1.6220 0.0280  -0.0801 0.2314  24  GLU B OE2 
4275  N N   . TYR B 25  ? 0.5708 0.7196 0.8380 -0.0080 -0.0531 0.1580  25  TYR B N   
4276  C CA  . TYR B 25  ? 0.5409 0.6815 0.7844 -0.0186 -0.0458 0.1421  25  TYR B CA  
4277  C C   . TYR B 25  ? 0.5513 0.7170 0.7941 -0.0287 -0.0434 0.1397  25  TYR B C   
4278  O O   . TYR B 25  ? 0.5968 0.7747 0.8537 -0.0199 -0.0386 0.1387  25  TYR B O   
4279  C CB  . TYR B 25  ? 0.6161 0.7368 0.8574 -0.0061 -0.0355 0.1265  25  TYR B CB  
4280  C CG  . TYR B 25  ? 0.5925 0.6866 0.8309 -0.0009 -0.0362 0.1222  25  TYR B CG  
4281  C CD1 . TYR B 25  ? 0.5817 0.6678 0.8424 0.0137  -0.0376 0.1255  25  TYR B CD1 
4282  C CD2 . TYR B 25  ? 0.6347 0.7116 0.8524 -0.0107 -0.0347 0.1139  25  TYR B CD2 
4283  C CE1 . TYR B 25  ? 0.6357 0.6976 0.8989 0.0180  -0.0373 0.1201  25  TYR B CE1 
4284  C CE2 . TYR B 25  ? 0.6478 0.7007 0.8650 -0.0063 -0.0351 0.1093  25  TYR B CE2 
4285  C CZ  . TYR B 25  ? 0.6521 0.6976 0.8925 0.0080  -0.0363 0.1121  25  TYR B CZ  
4286  O OH  . TYR B 25  ? 0.6985 0.7204 0.9443 0.0123  -0.0357 0.1060  25  TYR B OH  
4287  N N   . LEU B 26  ? 0.4820 0.6566 0.7111 -0.0477 -0.0456 0.1376  26  LEU B N   
4288  C CA  . LEU B 26  ? 0.4607 0.6613 0.6940 -0.0598 -0.0434 0.1336  26  LEU B CA  
4289  C C   . LEU B 26  ? 0.5189 0.7121 0.7519 -0.0612 -0.0305 0.1190  26  LEU B C   
4290  O O   . LEU B 26  ? 0.4070 0.6197 0.6495 -0.0710 -0.0263 0.1141  26  LEU B O   
4291  C CB  . LEU B 26  ? 0.4964 0.7144 0.7183 -0.0812 -0.0503 0.1346  26  LEU B CB  
4292  C CG  . LEU B 26  ? 0.5285 0.7577 0.7488 -0.0822 -0.0638 0.1533  26  LEU B CG  
4293  C CD1 . LEU B 26  ? 0.6226 0.8801 0.8305 -0.1054 -0.0700 0.1532  26  LEU B CD1 
4294  C CD2 . LEU B 26  ? 0.3826 0.6287 0.6256 -0.0685 -0.0699 0.1690  26  LEU B CD2 
4295  N N   . LEU B 27  ? 0.6052 0.7732 0.8304 -0.0521 -0.0241 0.1125  27  LEU B N   
4296  C CA  . LEU B 27  ? 0.5411 0.7031 0.7670 -0.0522 -0.0123 0.1028  27  LEU B CA  
4297  C C   . LEU B 27  ? 0.6050 0.7514 0.8279 -0.0344 -0.0076 0.1009  27  LEU B C   
4298  O O   . LEU B 27  ? 0.5554 0.6856 0.7708 -0.0271 -0.0124 0.1010  27  LEU B O   
4299  C CB  . LEU B 27  ? 0.5326 0.6838 0.7474 -0.0684 -0.0092 0.0935  27  LEU B CB  
4300  C CG  . LEU B 27  ? 0.5279 0.6989 0.7504 -0.0883 -0.0083 0.0882  27  LEU B CG  
4301  C CD1 . LEU B 27  ? 0.4354 0.5980 0.6431 -0.1048 -0.0104 0.0805  27  LEU B CD1 
4302  C CD2 . LEU B 27  ? 0.5964 0.7751 0.8385 -0.0907 0.0039  0.0827  27  LEU B CD2 
4303  N N   . PRO B 28  ? 0.6289 0.7822 0.8593 -0.0278 0.0022  0.0989  28  PRO B N   
4304  C CA  . PRO B 28  ? 0.6137 0.7611 0.8408 -0.0114 0.0071  0.0959  28  PRO B CA  
4305  C C   . PRO B 28  ? 0.5646 0.6973 0.7780 -0.0124 0.0120  0.0890  28  PRO B C   
4306  O O   . PRO B 28  ? 0.5466 0.6816 0.7568 -0.0005 0.0170  0.0857  28  PRO B O   
4307  C CB  . PRO B 28  ? 0.5846 0.7547 0.8276 -0.0049 0.0151  0.1005  28  PRO B CB  
4308  C CG  . PRO B 28  ? 0.5254 0.7049 0.7784 -0.0202 0.0185  0.1027  28  PRO B CG  
4309  C CD  . PRO B 28  ? 0.5764 0.7479 0.8221 -0.0352 0.0096  0.1001  28  PRO B CD  
4310  N N   . TRP B 29  ? 0.6017 0.7222 0.8076 -0.0266 0.0106  0.0861  29  TRP B N   
4311  C CA  . TRP B 29  ? 0.5446 0.6549 0.7429 -0.0288 0.0162  0.0814  29  TRP B CA  
4312  C C   . TRP B 29  ? 0.5125 0.6086 0.6965 -0.0183 0.0138  0.0747  29  TRP B C   
4313  O O   . TRP B 29  ? 0.5471 0.6463 0.7269 -0.0122 0.0193  0.0723  29  TRP B O   
4314  C CB  . TRP B 29  ? 0.4818 0.5820 0.6784 -0.0466 0.0155  0.0779  29  TRP B CB  
4315  C CG  . TRP B 29  ? 0.5087 0.6248 0.7232 -0.0583 0.0198  0.0800  29  TRP B CG  
4316  C CD1 . TRP B 29  ? 0.5431 0.6645 0.7600 -0.0730 0.0154  0.0771  29  TRP B CD1 
4317  C CD2 . TRP B 29  ? 0.5179 0.6494 0.7533 -0.0575 0.0299  0.0848  29  TRP B CD2 
4318  N NE1 . TRP B 29  ? 0.5630 0.7015 0.8019 -0.0818 0.0224  0.0764  29  TRP B NE1 
4319  C CE2 . TRP B 29  ? 0.5287 0.6719 0.7812 -0.0722 0.0317  0.0822  29  TRP B CE2 
4320  C CE3 . TRP B 29  ? 0.5152 0.6546 0.7577 -0.0463 0.0378  0.0918  29  TRP B CE3 
4321  C CZ2 . TRP B 29  ? 0.5627 0.7212 0.8431 -0.0756 0.0418  0.0855  29  TRP B CZ2 
4322  C CZ3 . TRP B 29  ? 0.5540 0.7099 0.8226 -0.0493 0.0476  0.0988  29  TRP B CZ3 
4323  C CH2 . TRP B 29  ? 0.5558 0.7192 0.8450 -0.0637 0.0498  0.0953  29  TRP B CH2 
4324  N N   . THR B 30  ? 0.4937 0.5764 0.6723 -0.0163 0.0060  0.0720  30  THR B N   
4325  C CA  . THR B 30  ? 0.5455 0.6146 0.7160 -0.0068 0.0046  0.0630  30  THR B CA  
4326  C C   . THR B 30  ? 0.4524 0.5373 0.6270 0.0086  0.0104  0.0585  30  THR B C   
4327  O O   . THR B 30  ? 0.4735 0.5585 0.6398 0.0138  0.0137  0.0496  30  THR B O   
4328  C CB  . THR B 30  ? 0.5607 0.6150 0.7335 -0.0062 -0.0037 0.0638  30  THR B CB  
4329  O OG1 . THR B 30  ? 0.5385 0.5840 0.7049 -0.0218 -0.0085 0.0687  30  THR B OG1 
4330  C CG2 . THR B 30  ? 0.4909 0.5289 0.6601 0.0018  -0.0040 0.0523  30  THR B CG2 
4331  N N   . PHE B 31  ? 0.5771 0.6793 0.7646 0.0152  0.0120  0.0641  31  PHE B N   
4332  C CA  . PHE B 31  ? 0.5180 0.6381 0.7103 0.0295  0.0182  0.0584  31  PHE B CA  
4333  C C   . PHE B 31  ? 0.5646 0.7038 0.7506 0.0298  0.0266  0.0607  31  PHE B C   
4334  O O   . PHE B 31  ? 0.5427 0.6925 0.7211 0.0377  0.0308  0.0518  31  PHE B O   
4335  C CB  . PHE B 31  ? 0.5219 0.6561 0.7321 0.0357  0.0182  0.0648  31  PHE B CB  
4336  C CG  . PHE B 31  ? 0.5636 0.7214 0.7804 0.0488  0.0265  0.0598  31  PHE B CG  
4337  C CD1 . PHE B 31  ? 0.5375 0.6955 0.7610 0.0607  0.0280  0.0458  31  PHE B CD1 
4338  C CD2 . PHE B 31  ? 0.5668 0.7485 0.7863 0.0487  0.0339  0.0684  31  PHE B CD2 
4339  C CE1 . PHE B 31  ? 0.5221 0.7058 0.7515 0.0717  0.0368  0.0385  31  PHE B CE1 
4340  C CE2 . PHE B 31  ? 0.5472 0.7545 0.7716 0.0601  0.0423  0.0646  31  PHE B CE2 
4341  C CZ  . PHE B 31  ? 0.5293 0.7386 0.7571 0.0713  0.0438  0.0487  31  PHE B CZ  
4342  N N   . PHE B 32  ? 0.5482 0.6942 0.7395 0.0207  0.0293  0.0728  32  PHE B N   
4343  C CA  . PHE B 32  ? 0.5824 0.7488 0.7750 0.0215  0.0379  0.0802  32  PHE B CA  
4344  C C   . PHE B 32  ? 0.4986 0.6586 0.6777 0.0191  0.0383  0.0763  32  PHE B C   
4345  O O   . PHE B 32  ? 0.5203 0.7017 0.6956 0.0250  0.0440  0.0793  32  PHE B O   
4346  C CB  . PHE B 32  ? 0.5849 0.7571 0.7941 0.0113  0.0416  0.0932  32  PHE B CB  
4347  C CG  . PHE B 32  ? 0.5409 0.7305 0.7659 0.0154  0.0440  0.0992  32  PHE B CG  
4348  C CD1 . PHE B 32  ? 0.5082 0.7214 0.7360 0.0281  0.0502  0.1012  32  PHE B CD1 
4349  C CD2 . PHE B 32  ? 0.5669 0.7522 0.8041 0.0060  0.0403  0.1021  32  PHE B CD2 
4350  C CE1 . PHE B 32  ? 0.5903 0.8196 0.8344 0.0319  0.0529  0.1067  32  PHE B CE1 
4351  C CE2 . PHE B 32  ? 0.5909 0.7938 0.8443 0.0096  0.0421  0.1076  32  PHE B CE2 
4352  C CZ  . PHE B 32  ? 0.6139 0.8372 0.8715 0.0229  0.0486  0.1102  32  PHE B CZ  
4353  N N   . HIS B 33  ? 0.5634 0.6973 0.7355 0.0102  0.0322  0.0707  33  HIS B N   
4354  C CA  . HIS B 33  ? 0.5572 0.6849 0.7183 0.0078  0.0322  0.0667  33  HIS B CA  
4355  C C   . HIS B 33  ? 0.5659 0.6932 0.7137 0.0174  0.0296  0.0513  33  HIS B C   
4356  O O   . HIS B 33  ? 0.5709 0.7039 0.7092 0.0183  0.0304  0.0473  33  HIS B O   
4357  C CB  . HIS B 33  ? 0.4552 0.5568 0.6158 -0.0063 0.0282  0.0657  33  HIS B CB  
4358  C CG  . HIS B 33  ? 0.4869 0.5931 0.6636 -0.0168 0.0337  0.0771  33  HIS B CG  
4359  N ND1 . HIS B 33  ? 0.4634 0.5878 0.6504 -0.0152 0.0412  0.0883  33  HIS B ND1 
4360  C CD2 . HIS B 33  ? 0.5354 0.6331 0.7233 -0.0295 0.0336  0.0788  33  HIS B CD2 
4361  C CE1 . HIS B 33  ? 0.4762 0.5996 0.6842 -0.0260 0.0463  0.0959  33  HIS B CE1 
4362  N NE2 . HIS B 33  ? 0.5076 0.6156 0.7154 -0.0353 0.0419  0.0882  33  HIS B NE2 
4363  N N   . ALA B 34  ? 0.5378 0.6610 0.6881 0.0246  0.0269  0.0423  34  ALA B N   
4364  C CA  . ALA B 34  ? 0.5816 0.7085 0.7262 0.0343  0.0268  0.0246  34  ALA B CA  
4365  C C   . ALA B 34  ? 0.6191 0.7830 0.7605 0.0435  0.0343  0.0229  34  ALA B C   
4366  O O   . ALA B 34  ? 0.7030 0.8801 0.8338 0.0470  0.0356  0.0108  34  ALA B O   
4367  C CB  . ALA B 34  ? 0.3880 0.5009 0.5444 0.0398  0.0233  0.0166  34  ALA B CB  
4368  N N   . VAL B 35  ? 0.4916 0.6758 0.6420 0.0467  0.0395  0.0350  35  VAL B N   
4369  C CA  . VAL B 35  ? 0.5148 0.7380 0.6620 0.0553  0.0473  0.0345  35  VAL B CA  
4370  C C   . VAL B 35  ? 0.4993 0.7425 0.6385 0.0511  0.0504  0.0485  35  VAL B C   
4371  O O   . VAL B 35  ? 0.5824 0.8576 0.7112 0.0565  0.0543  0.0445  35  VAL B O   
4372  C CB  . VAL B 35  ? 0.5436 0.7830 0.7054 0.0604  0.0525  0.0433  35  VAL B CB  
4373  C CG1 . VAL B 35  ? 0.4592 0.6830 0.6326 0.0662  0.0495  0.0298  35  VAL B CG1 
4374  C CG2 . VAL B 35  ? 0.5308 0.7627 0.7036 0.0517  0.0525  0.0644  35  VAL B CG2 
4375  N N   . LYS B 36  ? 0.4714 0.6985 0.6170 0.0413  0.0490  0.0646  36  LYS B N   
4376  C CA  . LYS B 36  ? 0.5060 0.7527 0.6526 0.0379  0.0530  0.0818  36  LYS B CA  
4377  C C   . LYS B 36  ? 0.5681 0.8066 0.7022 0.0341  0.0482  0.0751  36  LYS B C   
4378  O O   . LYS B 36  ? 0.6791 0.9473 0.8072 0.0366  0.0506  0.0822  36  LYS B O   
4379  C CB  . LYS B 36  ? 0.5761 0.8123 0.7434 0.0289  0.0559  0.1014  36  LYS B CB  
4380  C CG  . LYS B 36  ? 0.5817 0.8493 0.7620 0.0295  0.0641  0.1252  36  LYS B CG  
4381  C CD  . LYS B 36  ? 0.4586 0.7159 0.6672 0.0205  0.0689  0.1417  36  LYS B CD  
4382  C CE  . LYS B 36  ? 0.5498 0.7689 0.7625 0.0083  0.0636  0.1331  36  LYS B CE  
4383  N NZ  . LYS B 36  ? 0.5686 0.7807 0.7810 0.0032  0.0624  0.1362  36  LYS B NZ  
4384  N N   . ASP B 37  ? 0.5570 0.7587 0.6878 0.0278  0.0414  0.0629  37  ASP B N   
4385  C CA  . ASP B 37  ? 0.4835 0.6727 0.6074 0.0217  0.0373  0.0597  37  ASP B CA  
4386  C C   . ASP B 37  ? 0.5425 0.7122 0.6534 0.0230  0.0309  0.0355  37  ASP B C   
4387  O O   . ASP B 37  ? 0.5932 0.7706 0.6948 0.0228  0.0288  0.0286  37  ASP B O   
4388  C CB  . ASP B 37  ? 0.5690 0.7312 0.7066 0.0094  0.0369  0.0709  37  ASP B CB  
4389  C CG  . ASP B 37  ? 0.6068 0.7821 0.7654 0.0067  0.0441  0.0918  37  ASP B CG  
4390  O OD1 . ASP B 37  ? 0.5008 0.7035 0.6680 0.0091  0.0496  0.1087  37  ASP B OD1 
4391  O OD2 . ASP B 37  ? 0.5083 0.6684 0.6769 0.0018  0.0443  0.0920  37  ASP B OD2 
4392  N N   . TYR B 38  ? 0.5874 0.7345 0.7005 0.0244  0.0280  0.0234  38  TYR B N   
4393  C CA  . TYR B 38  ? 0.5329 0.6548 0.6409 0.0235  0.0224  0.0039  38  TYR B CA  
4394  C C   . TYR B 38  ? 0.5273 0.6696 0.6284 0.0323  0.0234  -0.0171 38  TYR B C   
4395  O O   . TYR B 38  ? 0.4201 0.5477 0.5179 0.0307  0.0197  -0.0336 38  TYR B O   
4396  C CB  . TYR B 38  ? 0.5148 0.6087 0.6320 0.0223  0.0190  0.0015  38  TYR B CB  
4397  C CG  . TYR B 38  ? 0.6221 0.6959 0.7436 0.0107  0.0168  0.0166  38  TYR B CG  
4398  C CD1 . TYR B 38  ? 0.5424 0.6099 0.6611 0.0010  0.0170  0.0232  38  TYR B CD1 
4399  C CD2 . TYR B 38  ? 0.5881 0.6525 0.7187 0.0089  0.0150  0.0232  38  TYR B CD2 
4400  C CE1 . TYR B 38  ? 0.5772 0.6293 0.7022 -0.0109 0.0165  0.0330  38  TYR B CE1 
4401  C CE2 . TYR B 38  ? 0.5260 0.5779 0.6600 -0.0033 0.0133  0.0340  38  TYR B CE2 
4402  C CZ  . TYR B 38  ? 0.5818 0.6274 0.7132 -0.0135 0.0147  0.0373  38  TYR B CZ  
4403  O OH  . TYR B 38  ? 0.5466 0.5822 0.6836 -0.0267 0.0146  0.0440  38  TYR B OH  
4404  N N   . TYR B 39  ? 0.5381 0.7156 0.6384 0.0409  0.0290  -0.0186 39  TYR B N   
4405  C CA  . TYR B 39  ? 0.5651 0.7719 0.6573 0.0474  0.0312  -0.0400 39  TYR B CA  
4406  C C   . TYR B 39  ? 0.5750 0.8201 0.6539 0.0462  0.0326  -0.0299 39  TYR B C   
4407  O O   . TYR B 39  ? 0.5760 0.8368 0.6452 0.0461  0.0307  -0.0458 39  TYR B O   
4408  C CB  . TYR B 39  ? 0.5631 0.7920 0.6625 0.0573  0.0374  -0.0517 39  TYR B CB  
4409  C CG  . TYR B 39  ? 0.5627 0.8300 0.6546 0.0631  0.0416  -0.0771 39  TYR B CG  
4410  C CD1 . TYR B 39  ? 0.5718 0.8900 0.6502 0.0653  0.0463  -0.0699 39  TYR B CD1 
4411  C CD2 . TYR B 39  ? 0.5491 0.8047 0.6500 0.0657  0.0414  -0.1084 39  TYR B CD2 
4412  C CE1 . TYR B 39  ? 0.6156 0.9756 0.6852 0.0692  0.0502  -0.0949 39  TYR B CE1 
4413  C CE2 . TYR B 39  ? 0.6548 0.9489 0.7510 0.0696  0.0461  -0.1362 39  TYR B CE2 
4414  C CZ  . TYR B 39  ? 0.7088 1.0570 0.7872 0.0709  0.0503  -0.1302 39  TYR B CZ  
4415  O OH  . TYR B 39  ? 0.6382 1.0312 0.7099 0.0735  0.0550  -0.1594 39  TYR B OH  
4416  N N   . ASP B 40  ? 0.6086 0.8706 0.6898 0.0451  0.0360  -0.0027 40  ASP B N   
4417  C CA  . ASP B 40  ? 0.5702 0.8769 0.6429 0.0458  0.0385  0.0113  40  ASP B CA  
4418  C C   . ASP B 40  ? 0.5519 0.8495 0.6218 0.0385  0.0330  0.0182  40  ASP B C   
4419  O O   . ASP B 40  ? 0.5688 0.9020 0.6282 0.0394  0.0319  0.0174  40  ASP B O   
4420  C CB  . ASP B 40  ? 0.5478 0.8743 0.6305 0.0471  0.0449  0.0405  40  ASP B CB  
4421  C CG  . ASP B 40  ? 0.6539 1.0082 0.7362 0.0557  0.0515  0.0342  40  ASP B CG  
4422  O OD1 . ASP B 40  ? 0.6967 1.0968 0.7666 0.0608  0.0548  0.0263  40  ASP B OD1 
4423  O OD2 . ASP B 40  ? 0.7081 1.0409 0.8026 0.0569  0.0534  0.0359  40  ASP B OD2 
4424  N N   . MET B 41  ? 0.5919 0.8452 0.6716 0.0307  0.0297  0.0246  41  MET B N   
4425  C CA  . MET B 41  ? 0.6149 0.8577 0.6955 0.0233  0.0254  0.0309  41  MET B CA  
4426  C C   . MET B 41  ? 0.5505 0.7962 0.6180 0.0236  0.0199  0.0060  41  MET B C   
4427  O O   . MET B 41  ? 0.5760 0.8493 0.6384 0.0226  0.0178  0.0117  41  MET B O   
4428  C CB  . MET B 41  ? 0.4745 0.6702 0.5682 0.0139  0.0240  0.0378  41  MET B CB  
4429  C CG  . MET B 41  ? 0.4376 0.6360 0.5500 0.0099  0.0296  0.0650  41  MET B CG  
4430  S SD  . MET B 41  ? 0.6063 0.8265 0.7335 0.0059  0.0317  0.0908  41  MET B SD  
4431  C CE  . MET B 41  ? 0.5860 0.8062 0.6969 0.0047  0.0236  0.0728  41  MET B CE  
4432  N N   . PRO B 42  ? 0.5155 0.7365 0.5801 0.0249  0.0176  -0.0208 42  PRO B N   
4433  C CA  . PRO B 42  ? 0.5421 0.7744 0.5977 0.0260  0.0141  -0.0472 42  PRO B CA  
4434  C C   . PRO B 42  ? 0.4764 0.7651 0.5209 0.0330  0.0172  -0.0573 42  PRO B C   
4435  O O   . PRO B 42  ? 0.4563 0.7684 0.4921 0.0322  0.0142  -0.0742 42  PRO B O   
4436  C CB  . PRO B 42  ? 0.4804 0.6728 0.5436 0.0265  0.0131  -0.0706 42  PRO B CB  
4437  C CG  . PRO B 42  ? 0.4051 0.5834 0.4769 0.0292  0.0165  -0.0583 42  PRO B CG  
4438  C CD  . PRO B 42  ? 0.4407 0.6222 0.5140 0.0245  0.0177  -0.0275 42  PRO B CD  
4439  N N   . ALA B 43  ? 0.5637 0.8779 0.6081 0.0391  0.0234  -0.0480 43  ALA B N   
4440  C CA  . ALA B 43  ? 0.5298 0.9009 0.5630 0.0453  0.0276  -0.0599 43  ALA B CA  
4441  C C   . ALA B 43  ? 0.5175 0.9397 0.5395 0.0439  0.0264  -0.0394 43  ALA B C   
4442  O O   . ALA B 43  ? 0.5738 1.0498 0.5825 0.0469  0.0282  -0.0522 43  ALA B O   
4443  C CB  . ALA B 43  ? 0.5752 0.9583 0.6134 0.0520  0.0353  -0.0546 43  ALA B CB  
4444  N N   . TYR B 44  ? 0.5192 0.9291 0.5487 0.0391  0.0239  -0.0075 44  TYR B N   
4445  C CA  . TYR B 44  ? 0.5688 1.0250 0.5931 0.0377  0.0217  0.0147  44  TYR B CA  
4446  C C   . TYR B 44  ? 0.5872 1.0645 0.5982 0.0353  0.0151  -0.0101 44  TYR B C   
4447  O O   . TYR B 44  ? 0.5549 1.0923 0.5540 0.0363  0.0138  -0.0045 44  TYR B O   
4448  C CB  . TYR B 44  ? 0.4858 0.9159 0.5290 0.0322  0.0206  0.0490  44  TYR B CB  
4449  C CG  . TYR B 44  ? 0.4950 0.9222 0.5550 0.0338  0.0279  0.0793  44  TYR B CG  
4450  C CD1 . TYR B 44  ? 0.6214 1.0043 0.6908 0.0332  0.0312  0.0737  44  TYR B CD1 
4451  C CD2 . TYR B 44  ? 0.5049 0.9753 0.5742 0.0354  0.0316  0.1147  44  TYR B CD2 
4452  C CE1 . TYR B 44  ? 0.5425 0.9240 0.6293 0.0338  0.0380  0.0990  44  TYR B CE1 
4453  C CE2 . TYR B 44  ? 0.4997 0.9668 0.5894 0.0365  0.0393  0.1419  44  TYR B CE2 
4454  C CZ  . TYR B 44  ? 0.6031 1.0254 0.7012 0.0354  0.0425  0.1321  44  TYR B CZ  
4455  O OH  . TYR B 44  ? 0.5534 0.9737 0.6734 0.0357  0.0502  0.1565  44  TYR B OH  
4456  N N   . LEU B 45  ? 0.4798 0.9114 0.4935 0.0317  0.0111  -0.0376 45  LEU B N   
4457  C CA  . LEU B 45  ? 0.5606 1.0060 0.5659 0.0284  0.0049  -0.0632 45  LEU B CA  
4458  C C   . LEU B 45  ? 0.6026 1.1044 0.5930 0.0323  0.0072  -0.0921 45  LEU B C   
4459  O O   . LEU B 45  ? 0.5463 1.0886 0.5263 0.0295  0.0025  -0.1046 45  LEU B O   
4460  C CB  . LEU B 45  ? 0.5288 0.9119 0.5439 0.0244  0.0020  -0.0874 45  LEU B CB  
4461  C CG  . LEU B 45  ? 0.5796 0.9127 0.6071 0.0178  -0.0014 -0.0658 45  LEU B CG  
4462  C CD1 . LEU B 45  ? 0.4950 0.7651 0.5327 0.0153  -0.0012 -0.0821 45  LEU B CD1 
4463  C CD2 . LEU B 45  ? 0.5034 0.8505 0.5298 0.0123  -0.0082 -0.0614 45  LEU B CD2 
4464  N N   . LYS B 46  ? 0.5767 1.0844 0.5672 0.0380  0.0148  -0.1049 46  LYS B N   
4465  C CA  . LYS B 46  ? 0.5348 1.1012 0.5128 0.0411  0.0190  -0.1336 46  LYS B CA  
4466  C C   . LYS B 46  ? 0.5452 1.1865 0.5063 0.0416  0.0191  -0.1087 46  LYS B C   
4467  O O   . LYS B 46  ? 0.5632 1.2655 0.5093 0.0412  0.0200  -0.1316 46  LYS B O   
4468  C CB  . LYS B 46  ? 0.5015 1.0557 0.4879 0.0473  0.0281  -0.1511 46  LYS B CB  
4469  C CG  . LYS B 46  ? 0.6517 1.1309 0.6585 0.0475  0.0279  -0.1625 46  LYS B CG  
4470  C CD  . LYS B 46  ? 0.7723 1.2357 0.7907 0.0541  0.0357  -0.1606 46  LYS B CD  
4471  C CE  . LYS B 46  ? 0.7439 1.2567 0.7599 0.0592  0.0443  -0.1909 46  LYS B CE  
4472  N NZ  . LYS B 46  ? 0.7042 1.1860 0.7416 0.0653  0.0513  -0.2046 46  LYS B NZ  
4473  N N   . ASP B 47  ? 0.5221 1.1627 0.4874 0.0420  0.0186  -0.0623 47  ASP B N   
4474  C CA  . ASP B 47  ? 0.5786 1.2897 0.5331 0.0431  0.0193  -0.0310 47  ASP B CA  
4475  C C   . ASP B 47  ? 0.5683 1.2949 0.5248 0.0384  0.0105  -0.0026 47  ASP B C   
4476  O O   . ASP B 47  ? 0.6471 1.4369 0.5971 0.0391  0.0100  0.0270  47  ASP B O   
4477  C CB  . ASP B 47  ? 0.6070 1.3154 0.5714 0.0478  0.0272  0.0044  47  ASP B CB  
4478  C CG  . ASP B 47  ? 0.7260 1.4412 0.6867 0.0533  0.0365  -0.0191 47  ASP B CG  
4479  O OD1 . ASP B 47  ? 0.9240 1.6325 0.8800 0.0535  0.0374  -0.0636 47  ASP B OD1 
4480  O OD2 . ASP B 47  ? 0.7877 1.5144 0.7540 0.0573  0.0437  0.0065  47  ASP B OD2 
4481  N N   . PHE B 48  ? 0.5233 1.1967 0.4906 0.0336  0.0040  -0.0090 48  PHE B N   
4482  C CA  . PHE B 48  ? 0.5307 1.2113 0.5061 0.0294  -0.0036 0.0199  48  PHE B CA  
4483  C C   . PHE B 48  ? 0.6582 1.3110 0.6330 0.0237  -0.0115 -0.0108 48  PHE B C   
4484  O O   . PHE B 48  ? 0.7182 1.3092 0.6998 0.0222  -0.0106 -0.0365 48  PHE B O   
4485  C CB  . PHE B 48  ? 0.5438 1.1784 0.5450 0.0288  -0.0010 0.0601  48  PHE B CB  
4486  C CG  . PHE B 48  ? 0.6278 1.2906 0.6361 0.0337  0.0069  0.0958  48  PHE B CG  
4487  C CD1 . PHE B 48  ? 0.5935 1.3134 0.6081 0.0348  0.0063  0.1368  48  PHE B CD1 
4488  C CD2 . PHE B 48  ? 0.5603 1.1943 0.5719 0.0373  0.0151  0.0898  48  PHE B CD2 
4489  C CE1 . PHE B 48  ? 0.4546 1.2005 0.4793 0.0392  0.0145  0.1711  48  PHE B CE1 
4490  C CE2 . PHE B 48  ? 0.5202 1.1796 0.5405 0.0414  0.0228  0.1217  48  PHE B CE2 
4491  C CZ  . PHE B 48  ? 0.5028 1.2177 0.5300 0.0423  0.0229  0.1623  48  PHE B CZ  
4492  N N   . GLU B 49  ? 0.7119 1.4131 0.6801 0.0205  -0.0193 -0.0057 49  GLU B N   
4493  C CA  . GLU B 49  ? 0.6454 1.3308 0.6134 0.0147  -0.0273 -0.0338 49  GLU B CA  
4494  C C   . GLU B 49  ? 0.6159 1.2474 0.6064 0.0107  -0.0311 -0.0090 49  GLU B C   
4495  O O   . GLU B 49  ? 0.6520 1.3074 0.6492 0.0075  -0.0382 0.0104  49  GLU B O   
4496  C CB  . GLU B 49  ? 0.5660 1.3334 0.5170 0.0124  -0.0343 -0.0409 49  GLU B CB  
4497  C CG  . GLU B 49  ? 0.7653 1.5670 0.6974 0.0118  -0.0324 -0.0928 49  GLU B CG  
4498  C CD  . GLU B 49  ? 0.9241 1.7981 0.8377 0.0158  -0.0264 -0.0886 49  GLU B CD  
4499  O OE1 . GLU B 49  ? 0.8457 1.7493 0.7600 0.0191  -0.0250 -0.0418 49  GLU B OE1 
4500  O OE2 . GLU B 49  ? 0.9233 1.8255 0.8246 0.0154  -0.0222 -0.1326 49  GLU B OE2 
4501  N N   . ILE B 50  ? 0.5895 1.1501 0.5934 0.0105  -0.0259 -0.0095 50  ILE B N   
4502  C CA  . ILE B 50  ? 0.6091 1.1112 0.6342 0.0054  -0.0277 0.0042  50  ILE B CA  
4503  C C   . ILE B 50  ? 0.5920 1.0268 0.6189 0.0029  -0.0255 -0.0281 50  ILE B C   
4504  O O   . ILE B 50  ? 0.5903 1.0236 0.6062 0.0060  -0.0226 -0.0578 50  ILE B O   
4505  C CB  . ILE B 50  ? 0.5162 1.0058 0.5622 0.0064  -0.0224 0.0485  50  ILE B CB  
4506  C CG1 . ILE B 50  ? 0.6517 1.1257 0.6950 0.0110  -0.0138 0.0488  50  ILE B CG1 
4507  C CG2 . ILE B 50  ? 0.4332 0.9866 0.4854 0.0084  -0.0249 0.0859  50  ILE B CG2 
4508  C CD1 . ILE B 50  ? 0.5901 1.0383 0.6579 0.0104  -0.0075 0.0840  50  ILE B CD1 
4509  N N   . LYS B 51  ? 0.5511 0.9318 0.5945 -0.0028 -0.0263 -0.0213 51  LYS B N   
4510  C CA  . LYS B 51  ? 0.5346 0.8522 0.5815 -0.0062 -0.0246 -0.0456 51  LYS B CA  
4511  C C   . LYS B 51  ? 0.5933 0.8674 0.6537 -0.0078 -0.0186 -0.0240 51  LYS B C   
4512  O O   . LYS B 51  ? 0.5812 0.8524 0.6572 -0.0109 -0.0173 0.0051  51  LYS B O   
4513  C CB  . LYS B 51  ? 0.5389 0.8313 0.5925 -0.0134 -0.0303 -0.0604 51  LYS B CB  
4514  C CG  . LYS B 51  ? 0.4876 0.8212 0.5304 -0.0133 -0.0365 -0.0867 51  LYS B CG  
4515  C CD  . LYS B 51  ? 0.4904 0.8273 0.5229 -0.0096 -0.0338 -0.1238 51  LYS B CD  
4516  C CE  . LYS B 51  ? 0.5215 0.8827 0.5505 -0.0125 -0.0391 -0.1588 51  LYS B CE  
4517  N NZ  . LYS B 51  ? 0.6544 1.0457 0.6747 -0.0081 -0.0355 -0.1928 51  LYS B NZ  
4518  N N   . LEU B 52  ? 0.6013 0.8435 0.6586 -0.0061 -0.0147 -0.0388 52  LEU B N   
4519  C CA  . LEU B 52  ? 0.5271 0.7301 0.5952 -0.0085 -0.0096 -0.0231 52  LEU B CA  
4520  C C   . LEU B 52  ? 0.5541 0.7067 0.6226 -0.0118 -0.0097 -0.0454 52  LEU B C   
4521  O O   . LEU B 52  ? 0.5979 0.7509 0.6595 -0.0079 -0.0106 -0.0709 52  LEU B O   
4522  C CB  . LEU B 52  ? 0.4796 0.7064 0.5453 -0.0015 -0.0040 -0.0093 52  LEU B CB  
4523  C CG  . LEU B 52  ? 0.5185 0.7947 0.5878 0.0019  -0.0021 0.0202  52  LEU B CG  
4524  C CD1 . LEU B 52  ? 0.4491 0.7489 0.5146 0.0091  0.0039  0.0288  52  LEU B CD1 
4525  C CD2 . LEU B 52  ? 0.5752 0.8345 0.6675 -0.0043 -0.0003 0.0485  52  LEU B CD2 
4526  N N   . ASN B 53  ? 0.6072 0.7189 0.6866 -0.0195 -0.0083 -0.0356 53  ASN B N   
4527  C CA  . ASN B 53  ? 0.5610 0.6273 0.6416 -0.0238 -0.0085 -0.0508 53  ASN B CA  
4528  C C   . ASN B 53  ? 0.5101 0.5577 0.5950 -0.0249 -0.0042 -0.0378 53  ASN B C   
4529  O O   . ASN B 53  ? 0.5461 0.6033 0.6384 -0.0264 -0.0005 -0.0165 53  ASN B O   
4530  C CB  . ASN B 53  ? 0.4940 0.5307 0.5818 -0.0339 -0.0106 -0.0534 53  ASN B CB  
4531  C CG  . ASN B 53  ? 0.5179 0.5742 0.6036 -0.0335 -0.0154 -0.0655 53  ASN B CG  
4532  O OD1 . ASN B 53  ? 0.5379 0.5899 0.6196 -0.0319 -0.0181 -0.0898 53  ASN B OD1 
4533  N ND2 . ASN B 53  ? 0.4885 0.5683 0.5803 -0.0352 -0.0163 -0.0485 53  ASN B ND2 
4534  N N   . PHE B 54  ? 0.5279 0.5500 0.6116 -0.0242 -0.0045 -0.0503 54  PHE B N   
4535  C CA  . PHE B 54  ? 0.4694 0.4787 0.5563 -0.0245 -0.0016 -0.0397 54  PHE B CA  
4536  C C   . PHE B 54  ? 0.5688 0.5388 0.6588 -0.0316 -0.0033 -0.0452 54  PHE B C   
4537  O O   . PHE B 54  ? 0.6078 0.5616 0.6983 -0.0322 -0.0060 -0.0609 54  PHE B O   
4538  C CB  . PHE B 54  ? 0.5046 0.5356 0.5883 -0.0133 0.0000  -0.0447 54  PHE B CB  
4539  C CG  . PHE B 54  ? 0.5470 0.6219 0.6258 -0.0066 0.0021  -0.0385 54  PHE B CG  
4540  C CD1 . PHE B 54  ? 0.4523 0.5540 0.5237 -0.0017 0.0002  -0.0547 54  PHE B CD1 
4541  C CD2 . PHE B 54  ? 0.4613 0.5535 0.5444 -0.0061 0.0061  -0.0160 54  PHE B CD2 
4542  C CE1 . PHE B 54  ? 0.4966 0.6448 0.5618 0.0036  0.0017  -0.0467 54  PHE B CE1 
4543  C CE2 . PHE B 54  ? 0.5046 0.6399 0.5845 -0.0001 0.0083  -0.0063 54  PHE B CE2 
4544  C CZ  . PHE B 54  ? 0.5016 0.6666 0.5710 0.0047  0.0058  -0.0207 54  PHE B CZ  
4545  N N   . ASN B 55  ? 0.5962 0.5541 0.6898 -0.0374 -0.0013 -0.0317 55  ASN B N   
4546  C CA  . ASN B 55  ? 0.5944 0.5230 0.6896 -0.0443 -0.0030 -0.0326 55  ASN B CA  
4547  C C   . ASN B 55  ? 0.6064 0.5394 0.7037 -0.0393 -0.0027 -0.0258 55  ASN B C   
4548  O O   . ASN B 55  ? 0.6104 0.5602 0.7094 -0.0385 0.0003  -0.0142 55  ASN B O   
4549  C CB  . ASN B 55  ? 0.5973 0.5110 0.6952 -0.0587 -0.0011 -0.0244 55  ASN B CB  
4550  C CG  . ASN B 55  ? 0.6478 0.5396 0.7450 -0.0670 -0.0027 -0.0224 55  ASN B CG  
4551  O OD1 . ASN B 55  ? 0.5811 0.4773 0.6793 -0.0693 -0.0020 -0.0130 55  ASN B OD1 
4552  N ND2 . ASN B 55  ? 0.5707 0.4415 0.6670 -0.0717 -0.0049 -0.0305 55  ASN B ND2 
4553  N N   . LEU B 56  ? 0.5384 0.4571 0.6394 -0.0358 -0.0054 -0.0320 56  LEU B N   
4554  C CA  . LEU B 56  ? 0.5245 0.4465 0.6310 -0.0306 -0.0059 -0.0248 56  LEU B CA  
4555  C C   . LEU B 56  ? 0.5289 0.4282 0.6391 -0.0388 -0.0093 -0.0180 56  LEU B C   
4556  O O   . LEU B 56  ? 0.5916 0.4720 0.7063 -0.0400 -0.0113 -0.0252 56  LEU B O   
4557  C CB  . LEU B 56  ? 0.6169 0.5494 0.7308 -0.0165 -0.0053 -0.0373 56  LEU B CB  
4558  C CG  . LEU B 56  ? 0.6251 0.5889 0.7336 -0.0083 -0.0017 -0.0425 56  LEU B CG  
4559  C CD1 . LEU B 56  ? 0.6673 0.6361 0.7752 -0.0039 -0.0017 -0.0633 56  LEU B CD1 
4560  C CD2 . LEU B 56  ? 0.6787 0.6607 0.7938 0.0020  0.0008  -0.0405 56  LEU B CD2 
4561  N N   . THR B 57  ? 0.5590 0.4628 0.6684 -0.0450 -0.0099 -0.0038 57  THR B N   
4562  C CA  . THR B 57  ? 0.5172 0.4076 0.6280 -0.0539 -0.0136 0.0056  57  THR B CA  
4563  C C   . THR B 57  ? 0.5509 0.4394 0.6755 -0.0439 -0.0169 0.0100  57  THR B C   
4564  O O   . THR B 57  ? 0.5824 0.4854 0.7138 -0.0330 -0.0158 0.0099  57  THR B O   
4565  C CB  . THR B 57  ? 0.4823 0.3840 0.5880 -0.0657 -0.0129 0.0169  57  THR B CB  
4566  O OG1 . THR B 57  ? 0.6026 0.5249 0.7120 -0.0586 -0.0109 0.0210  57  THR B OG1 
4567  C CG2 . THR B 57  ? 0.5301 0.4281 0.6293 -0.0782 -0.0090 0.0123  57  THR B CG2 
4568  N N   . PRO B 58  ? 0.5513 0.4230 0.6830 -0.0474 -0.0203 0.0152  58  PRO B N   
4569  C CA  . PRO B 58  ? 0.6078 0.4766 0.7603 -0.0373 -0.0229 0.0217  58  PRO B CA  
4570  C C   . PRO B 58  ? 0.5851 0.4729 0.7416 -0.0347 -0.0254 0.0367  58  PRO B C   
4571  O O   . PRO B 58  ? 0.6059 0.4989 0.7806 -0.0218 -0.0251 0.0364  58  PRO B O   
4572  C CB  . PRO B 58  ? 0.5529 0.4030 0.7114 -0.0454 -0.0260 0.0307  58  PRO B CB  
4573  C CG  . PRO B 58  ? 0.5436 0.3818 0.6878 -0.0540 -0.0233 0.0176  58  PRO B CG  
4574  C CD  . PRO B 58  ? 0.5232 0.3777 0.6485 -0.0598 -0.0210 0.0153  58  PRO B CD  
4575  N N   . VAL B 59  ? 0.4721 0.3720 0.6146 -0.0470 -0.0272 0.0478  59  VAL B N   
4576  C CA  . VAL B 59  ? 0.6061 0.5267 0.7533 -0.0455 -0.0300 0.0613  59  VAL B CA  
4577  C C   . VAL B 59  ? 0.6032 0.5376 0.7538 -0.0338 -0.0255 0.0528  59  VAL B C   
4578  O O   . VAL B 59  ? 0.5496 0.4960 0.7140 -0.0247 -0.0268 0.0595  59  VAL B O   
4579  C CB  . VAL B 59  ? 0.5167 0.4509 0.6489 -0.0630 -0.0319 0.0703  59  VAL B CB  
4580  C CG1 . VAL B 59  ? 0.5608 0.4908 0.6780 -0.0728 -0.0261 0.0571  59  VAL B CG1 
4581  C CG2 . VAL B 59  ? 0.5452 0.5043 0.6814 -0.0618 -0.0334 0.0790  59  VAL B CG2 
4582  N N   . LEU B 60  ? 0.5932 0.5282 0.7329 -0.0338 -0.0200 0.0394  60  LEU B N   
4583  C CA  . LEU B 60  ? 0.5849 0.5360 0.7275 -0.0225 -0.0153 0.0326  60  LEU B CA  
4584  C C   . LEU B 60  ? 0.5659 0.5135 0.7235 -0.0073 -0.0142 0.0224  60  LEU B C   
4585  O O   . LEU B 60  ? 0.5751 0.5376 0.7435 0.0032  -0.0122 0.0224  60  LEU B O   
4586  C CB  . LEU B 60  ? 0.5862 0.5416 0.7161 -0.0260 -0.0101 0.0240  60  LEU B CB  
4587  C CG  . LEU B 60  ? 0.6192 0.5946 0.7510 -0.0139 -0.0049 0.0177  60  LEU B CG  
4588  C CD1 . LEU B 60  ? 0.5166 0.5123 0.6542 -0.0122 -0.0032 0.0289  60  LEU B CD1 
4589  C CD2 . LEU B 60  ? 0.5272 0.5081 0.6490 -0.0160 -0.0008 0.0114  60  LEU B CD2 
4590  N N   . ILE B 61  ? 0.5952 0.5238 0.7567 -0.0064 -0.0146 0.0121  61  ILE B N   
4591  C CA  . ILE B 61  ? 0.6163 0.5415 0.7970 0.0068  -0.0122 -0.0021 61  ILE B CA  
4592  C C   . ILE B 61  ? 0.5760 0.5003 0.7821 0.0137  -0.0146 0.0094  61  ILE B C   
4593  O O   . ILE B 61  ? 0.6171 0.5503 0.8419 0.0262  -0.0108 0.0005  61  ILE B O   
4594  C CB  . ILE B 61  ? 0.5735 0.4777 0.7569 0.0044  -0.0120 -0.0156 61  ILE B CB  
4595  C CG1 . ILE B 61  ? 0.5444 0.4531 0.7046 -0.0019 -0.0101 -0.0253 61  ILE B CG1 
4596  C CG2 . ILE B 61  ? 0.6631 0.5648 0.8713 0.0169  -0.0082 -0.0345 61  ILE B CG2 
4597  C CD1 . ILE B 61  ? 0.6980 0.5963 0.8622 -0.0002 -0.0085 -0.0458 61  ILE B CD1 
4598  N N   . ASP B 62  ? 0.5853 0.5021 0.7937 0.0055  -0.0207 0.0297  62  ASP B N   
4599  C CA  . ASP B 62  ? 0.6224 0.5426 0.8563 0.0116  -0.0243 0.0459  62  ASP B CA  
4600  C C   . ASP B 62  ? 0.6470 0.5912 0.8833 0.0184  -0.0227 0.0489  62  ASP B C   
4601  O O   . ASP B 62  ? 0.6530 0.6021 0.9160 0.0308  -0.0208 0.0479  62  ASP B O   
4602  C CB  . ASP B 62  ? 0.5360 0.4535 0.7658 -0.0008 -0.0319 0.0700  62  ASP B CB  
4603  C CG  . ASP B 62  ? 0.6916 0.5857 0.9322 -0.0043 -0.0336 0.0731  62  ASP B CG  
4604  O OD1 . ASP B 62  ? 0.7362 0.6151 1.0010 0.0056  -0.0296 0.0603  62  ASP B OD1 
4605  O OD2 . ASP B 62  ? 0.7018 0.5947 0.9283 -0.0179 -0.0382 0.0876  62  ASP B OD2 
4606  N N   . GLN B 63  ? 0.7029 0.6621 0.9151 0.0104  -0.0225 0.0522  63  GLN B N   
4607  C CA  . GLN B 63  ? 0.6224 0.6050 0.8373 0.0157  -0.0205 0.0560  63  GLN B CA  
4608  C C   . GLN B 63  ? 0.6256 0.6170 0.8478 0.0293  -0.0125 0.0375  63  GLN B C   
4609  O O   . GLN B 63  ? 0.6346 0.6389 0.8757 0.0397  -0.0105 0.0385  63  GLN B O   
4610  C CB  . GLN B 63  ? 0.5159 0.5113 0.7083 0.0033  -0.0203 0.0614  63  GLN B CB  
4611  C CG  . GLN B 63  ? 0.5687 0.5618 0.7538 -0.0117 -0.0273 0.0763  63  GLN B CG  
4612  C CD  . GLN B 63  ? 0.6408 0.6454 0.8085 -0.0253 -0.0253 0.0765  63  GLN B CD  
4613  O OE1 . GLN B 63  ? 0.6638 0.6882 0.8348 -0.0252 -0.0234 0.0800  63  GLN B OE1 
4614  N NE2 . GLN B 63  ? 0.5832 0.5758 0.7362 -0.0374 -0.0249 0.0719  63  GLN B NE2 
4615  N N   . ILE B 64  ? 0.5811 0.5688 0.7891 0.0292  -0.0080 0.0204  64  ILE B N   
4616  C CA  . ILE B 64  ? 0.5950 0.5972 0.8071 0.0407  -0.0004 0.0015  64  ILE B CA  
4617  C C   . ILE B 64  ? 0.6012 0.5976 0.8448 0.0526  0.0016  -0.0086 64  ILE B C   
4618  O O   . ILE B 64  ? 0.6403 0.6548 0.8974 0.0631  0.0075  -0.0179 64  ILE B O   
4619  C CB  . ILE B 64  ? 0.6560 0.6574 0.8491 0.0377  0.0026  -0.0145 64  ILE B CB  
4620  C CG1 . ILE B 64  ? 0.5521 0.5589 0.7213 0.0264  0.0017  -0.0034 64  ILE B CG1 
4621  C CG2 . ILE B 64  ? 0.5946 0.6188 0.7904 0.0486  0.0102  -0.0347 64  ILE B CG2 
4622  C CD1 . ILE B 64  ? 0.4720 0.4797 0.6252 0.0233  0.0038  -0.0155 64  ILE B CD1 
4623  N N   . GLN B 65  ? 0.5868 0.5589 0.8463 0.0508  -0.0022 -0.0069 65  GLN B N   
4624  C CA  . GLN B 65  ? 0.6631 0.6276 0.9617 0.0619  0.0005  -0.0144 65  GLN B CA  
4625  C C   . GLN B 65  ? 0.6045 0.5800 0.9250 0.0681  -0.0014 0.0034  65  GLN B C   
4626  O O   . GLN B 65  ? 0.6220 0.6059 0.9714 0.0800  0.0046  -0.0076 65  GLN B O   
4627  C CB  . GLN B 65  ? 0.6605 0.5963 0.9756 0.0581  -0.0032 -0.0111 65  GLN B CB  
4628  C CG  . GLN B 65  ? 0.6886 0.6137 0.9913 0.0544  -0.0001 -0.0340 65  GLN B CG  
4629  C CD  . GLN B 65  ? 0.7587 0.6552 1.0746 0.0485  -0.0038 -0.0278 65  GLN B CD  
4630  O OE1 . GLN B 65  ? 0.7554 0.6431 1.0635 0.0397  -0.0108 -0.0028 65  GLN B OE1 
4631  N NE2 . GLN B 65  ? 0.7217 0.6063 1.0588 0.0527  0.0014  -0.0514 65  GLN B NE2 
4632  N N   . GLU B 66  ? 0.6118 0.5904 0.9201 0.0595  -0.0092 0.0292  66  GLU B N   
4633  C CA  . GLU B 66  ? 0.5743 0.5668 0.9033 0.0646  -0.0122 0.0473  66  GLU B CA  
4634  C C   . GLU B 66  ? 0.5400 0.5579 0.8638 0.0711  -0.0057 0.0385  66  GLU B C   
4635  O O   . GLU B 66  ? 0.5796 0.6084 0.9316 0.0816  -0.0031 0.0399  66  GLU B O   
4636  C CB  . GLU B 66  ? 0.5640 0.5593 0.8795 0.0520  -0.0224 0.0748  66  GLU B CB  
4637  C CG  . GLU B 66  ? 0.7330 0.7426 1.0753 0.0568  -0.0277 0.0965  66  GLU B CG  
4638  C CD  . GLU B 66  ? 0.7467 0.7605 1.0814 0.0441  -0.0389 0.1239  66  GLU B CD  
4639  O OE1 . GLU B 66  ? 0.6563 0.6748 0.9574 0.0299  -0.0415 0.1253  66  GLU B OE1 
4640  O OE2 . GLU B 66  ? 0.7541 0.7694 1.1188 0.0481  -0.0449 0.1443  66  GLU B OE2 
4641  N N   . TYR B 67  ? 0.5257 0.5541 0.8166 0.0654  -0.0024 0.0305  67  TYR B N   
4642  C CA  . TYR B 67  ? 0.5391 0.5937 0.8253 0.0714  0.0048  0.0238  67  TYR B CA  
4643  C C   . TYR B 67  ? 0.6278 0.6904 0.9291 0.0838  0.0144  -0.0015 67  TYR B C   
4644  O O   . TYR B 67  ? 0.7083 0.7928 1.0207 0.0923  0.0208  -0.0062 67  TYR B O   
4645  C CB  . TYR B 67  ? 0.5365 0.6014 0.7888 0.0620  0.0063  0.0251  67  TYR B CB  
4646  C CG  . TYR B 67  ? 0.6328 0.7055 0.8768 0.0522  0.0014  0.0457  67  TYR B CG  
4647  C CD1 . TYR B 67  ? 0.5332 0.6296 0.7827 0.0556  0.0050  0.0522  67  TYR B CD1 
4648  C CD2 . TYR B 67  ? 0.6114 0.6701 0.8434 0.0387  -0.0059 0.0570  67  TYR B CD2 
4649  C CE1 . TYR B 67  ? 0.5557 0.6610 0.8011 0.0456  0.0012  0.0682  67  TYR B CE1 
4650  C CE2 . TYR B 67  ? 0.6424 0.7120 0.8687 0.0283  -0.0096 0.0717  67  TYR B CE2 
4651  C CZ  . TYR B 67  ? 0.5893 0.6818 0.8232 0.0317  -0.0061 0.0767  67  TYR B CZ  
4652  O OH  . TYR B 67  ? 0.6739 0.7784 0.9053 0.0203  -0.0092 0.0886  67  TYR B OH  
4653  N N   . ALA B 68  ? 0.5135 0.5610 0.8165 0.0844  0.0163  -0.0197 68  ALA B N   
4654  C CA  . ALA B 68  ? 0.5632 0.6224 0.8805 0.0944  0.0262  -0.0486 68  ALA B CA  
4655  C C   . ALA B 68  ? 0.5422 0.5958 0.9067 0.1055  0.0296  -0.0547 68  ALA B C   
4656  O O   . ALA B 68  ? 0.6671 0.7388 1.0485 0.1147  0.0395  -0.0774 68  ALA B O   
4657  C CB  . ALA B 68  ? 0.6627 0.7107 0.9679 0.0903  0.0272  -0.0686 68  ALA B CB  
4658  N N   . GLN B 69  ? 0.5820 0.6132 0.9704 0.1046  0.0222  -0.0349 69  GLN B N   
4659  C CA  . GLN B 69  ? 0.6347 0.6588 1.0754 0.1153  0.0251  -0.0361 69  GLN B CA  
4660  C C   . GLN B 69  ? 0.6083 0.6462 1.0652 0.1197  0.0219  -0.0129 69  GLN B C   
4661  O O   . GLN B 69  ? 0.5725 0.6031 1.0748 0.1273  0.0212  -0.0033 69  GLN B O   
4662  C CB  . GLN B 69  ? 0.6250 0.6179 1.0896 0.1126  0.0196  -0.0270 69  GLN B CB  
4663  C CG  . GLN B 69  ? 0.7339 0.7126 1.1761 0.1055  0.0208  -0.0460 69  GLN B CG  
4664  C CD  . GLN B 69  ? 0.9433 0.8920 1.3972 0.0992  0.0138  -0.0307 69  GLN B CD  
4665  O OE1 . GLN B 69  ? 0.9970 0.9358 1.4792 0.1005  0.0081  -0.0048 69  GLN B OE1 
4666  N NE2 . GLN B 69  ? 0.8553 0.7922 1.2858 0.0915  0.0137  -0.0443 69  GLN B NE2 
4667  N N   . GLY B 70  ? 0.6131 0.6719 1.0376 0.1152  0.0203  -0.0032 70  GLY B N   
4668  C CA  . GLY B 70  ? 0.5488 0.6254 0.9867 0.1191  0.0184  0.0148  70  GLY B CA  
4669  C C   . GLY B 70  ? 0.6241 0.6933 1.0711 0.1135  0.0057  0.0479  70  GLY B C   
4670  O O   . GLY B 70  ? 0.6316 0.7179 1.0914 0.1162  0.0030  0.0637  70  GLY B O   
4671  N N   . LYS B 71  ? 0.6011 0.6490 1.0414 0.1052  -0.0023 0.0593  71  LYS B N   
4672  C CA  . LYS B 71  ? 0.5996 0.6456 1.0504 0.0996  -0.0144 0.0915  71  LYS B CA  
4673  C C   . LYS B 71  ? 0.5654 0.6253 0.9768 0.0853  -0.0223 0.1076  71  LYS B C   
4674  O O   . LYS B 71  ? 0.7453 0.8139 1.1630 0.0798  -0.0324 0.1334  71  LYS B O   
4675  C CB  . LYS B 71  ? 0.6478 0.6681 1.1119 0.0965  -0.0189 0.0987  71  LYS B CB  
4676  C CG  . LYS B 71  ? 0.7416 0.7448 1.2454 0.1085  -0.0097 0.0778  71  LYS B CG  
4677  C CD  . LYS B 71  ? 0.8854 0.8636 1.4056 0.1045  -0.0145 0.0897  71  LYS B CD  
4678  C CE  . LYS B 71  ? 0.7644 0.7225 1.2965 0.1085  -0.0046 0.0582  71  LYS B CE  
4679  N NZ  . LYS B 71  ? 0.7659 0.7109 1.2552 0.0955  -0.0079 0.0536  71  LYS B NZ  
4680  N N   . ALA B 72  ? 0.4960 0.5611 0.8705 0.0789  -0.0176 0.0933  72  ALA B N   
4681  C CA  . ALA B 72  ? 0.6184 0.6956 0.9618 0.0647  -0.0233 0.1056  72  ALA B CA  
4682  C C   . ALA B 72  ? 0.5428 0.6467 0.8965 0.0668  -0.0243 0.1166  72  ALA B C   
4683  O O   . ALA B 72  ? 0.5230 0.6382 0.8932 0.0784  -0.0167 0.1074  72  ALA B O   
4684  C CB  . ALA B 72  ? 0.5934 0.6682 0.9021 0.0581  -0.0170 0.0889  72  ALA B CB  
4685  N N   . LYS B 73  ? 0.6038 0.7201 0.9480 0.0546  -0.0333 0.1349  73  LYS B N   
4686  C CA  . LYS B 73  ? 0.5222 0.6658 0.8748 0.0538  -0.0354 0.1454  73  LYS B CA  
4687  C C   . LYS B 73  ? 0.5501 0.7045 0.8729 0.0391  -0.0340 0.1418  73  LYS B C   
4688  O O   . LYS B 73  ? 0.5414 0.7074 0.8554 0.0252  -0.0421 0.1535  73  LYS B O   
4689  C CB  . LYS B 73  ? 0.5673 0.7228 0.9412 0.0518  -0.0477 0.1703  73  LYS B CB  
4690  C CG  . LYS B 73  ? 0.6316 0.7731 1.0401 0.0642  -0.0500 0.1785  73  LYS B CG  
4691  C CD  . LYS B 73  ? 0.6283 0.7838 1.0526 0.0587  -0.0639 0.2089  73  LYS B CD  
4692  C CE  . LYS B 73  ? 0.6441 0.7819 1.1055 0.0696  -0.0659 0.2203  73  LYS B CE  
4693  N NZ  . LYS B 73  ? 0.7661 0.9060 1.2237 0.0586  -0.0779 0.2460  73  LYS B NZ  
4694  N N   . ASP B 74  ? 0.5792 0.7323 0.8890 0.0416  -0.0233 0.1257  74  ASP B N   
4695  C CA  . ASP B 74  ? 0.6448 0.8079 0.9351 0.0289  -0.0201 0.1232  74  ASP B CA  
4696  C C   . ASP B 74  ? 0.5734 0.7639 0.8789 0.0286  -0.0196 0.1308  74  ASP B C   
4697  O O   . ASP B 74  ? 0.5524 0.7533 0.8733 0.0410  -0.0130 0.1280  74  ASP B O   
4698  C CB  . ASP B 74  ? 0.6987 0.8542 0.9741 0.0324  -0.0091 0.1079  74  ASP B CB  
4699  C CG  . ASP B 74  ? 0.7236 0.8837 0.9830 0.0185  -0.0054 0.1067  74  ASP B CG  
4700  O OD1 . ASP B 74  ? 0.7347 0.8999 0.9914 0.0043  -0.0110 0.1131  74  ASP B OD1 
4701  O OD2 . ASP B 74  ? 0.6924 0.8535 0.9442 0.0217  0.0038  0.0991  74  ASP B OD2 
4702  N N   . VAL B 75  ? 0.6290 0.8334 0.9314 0.0137  -0.0263 0.1392  75  VAL B N   
4703  C CA  . VAL B 75  ? 0.6223 0.8547 0.9420 0.0122  -0.0273 0.1464  75  VAL B CA  
4704  C C   . VAL B 75  ? 0.6022 0.8433 0.9233 0.0135  -0.0148 0.1379  75  VAL B C   
4705  O O   . VAL B 75  ? 0.5740 0.8329 0.9139 0.0213  -0.0108 0.1406  75  VAL B O   
4706  C CB  . VAL B 75  ? 0.6008 0.8501 0.9162 -0.0061 -0.0374 0.1543  75  VAL B CB  
4707  C CG1 . VAL B 75  ? 0.5814 0.8329 0.9039 -0.0042 -0.0504 0.1699  75  VAL B CG1 
4708  C CG2 . VAL B 75  ? 0.6059 0.8438 0.8978 -0.0220 -0.0349 0.1445  75  VAL B CG2 
4709  N N   . PHE B 76  ? 0.5755 0.8052 0.8794 0.0060  -0.0081 0.1291  76  PHE B N   
4710  C CA  . PHE B 76  ? 0.6112 0.8502 0.9196 0.0076  0.0043  0.1250  76  PHE B CA  
4711  C C   . PHE B 76  ? 0.5790 0.8181 0.8911 0.0258  0.0123  0.1217  76  PHE B C   
4712  O O   . PHE B 76  ? 0.5970 0.8541 0.9217 0.0313  0.0209  0.1234  76  PHE B O   
4713  C CB  . PHE B 76  ? 0.5499 0.7769 0.8436 -0.0039 0.0095  0.1187  76  PHE B CB  
4714  C CG  . PHE B 76  ? 0.5452 0.7837 0.8490 -0.0040 0.0221  0.1189  76  PHE B CG  
4715  C CD1 . PHE B 76  ? 0.5797 0.8364 0.9028 -0.0143 0.0255  0.1215  76  PHE B CD1 
4716  C CD2 . PHE B 76  ? 0.5834 0.8175 0.8797 0.0058  0.0309  0.1172  76  PHE B CD2 
4717  C CE1 . PHE B 76  ? 0.6578 0.9249 0.9959 -0.0141 0.0381  0.1243  76  PHE B CE1 
4718  C CE2 . PHE B 76  ? 0.5646 0.8125 0.8724 0.0059  0.0425  0.1220  76  PHE B CE2 
4719  C CZ  . PHE B 76  ? 0.6069 0.8698 0.9373 -0.0038 0.0465  0.1265  76  PHE B CZ  
4720  N N   . LEU B 77  ? 0.5794 0.8010 0.8826 0.0346  0.0102  0.1159  77  LEU B N   
4721  C CA  . LEU B 77  ? 0.5583 0.7835 0.8650 0.0505  0.0186  0.1081  77  LEU B CA  
4722  C C   . LEU B 77  ? 0.5055 0.7483 0.8374 0.0613  0.0194  0.1119  77  LEU B C   
4723  O O   . LEU B 77  ? 0.5753 0.8347 0.9144 0.0706  0.0296  0.1081  77  LEU B O   
4724  C CB  . LEU B 77  ? 0.6182 0.8215 0.9146 0.0563  0.0162  0.0979  77  LEU B CB  
4725  C CG  . LEU B 77  ? 0.7071 0.9113 0.9894 0.0625  0.0259  0.0853  77  LEU B CG  
4726  C CD1 . LEU B 77  ? 0.6596 0.8645 0.9248 0.0513  0.0293  0.0889  77  LEU B CD1 
4727  C CD2 . LEU B 77  ? 0.5900 0.7735 0.8674 0.0677  0.0231  0.0728  77  LEU B CD2 
4728  N N   . GLU B 78  ? 0.4655 0.7078 0.8122 0.0601  0.0090  0.1207  78  GLU B N   
4729  C CA  . GLU B 78  ? 0.6549 0.9146 1.0298 0.0703  0.0091  0.1259  78  GLU B CA  
4730  C C   . GLU B 78  ? 0.5481 0.8330 0.9320 0.0675  0.0156  0.1303  78  GLU B C   
4731  O O   . GLU B 78  ? 0.5215 0.8227 0.9248 0.0786  0.0222  0.1295  78  GLU B O   
4732  C CB  . GLU B 78  ? 0.7808 1.0393 1.1711 0.0678  -0.0048 0.1391  78  GLU B CB  
4733  C CG  . GLU B 78  ? 0.7839 1.0324 1.1968 0.0824  -0.0064 0.1382  78  GLU B CG  
4734  C CD  . GLU B 78  ? 0.8455 1.1118 1.2880 0.0965  0.0011  0.1357  78  GLU B CD  
4735  O OE1 . GLU B 78  ? 0.8897 1.1763 1.3513 0.0956  -0.0035 0.1484  78  GLU B OE1 
4736  O OE2 . GLU B 78  ? 0.7761 1.0385 1.2234 0.1081  0.0120  0.1198  78  GLU B OE2 
4737  N N   . ALA B 79  ? 0.5213 0.8099 0.8945 0.0526  0.0149  0.1340  79  ALA B N   
4738  C CA  . ALA B 79  ? 0.4659 0.7766 0.8508 0.0489  0.0229  0.1374  79  ALA B CA  
4739  C C   . ALA B 79  ? 0.5100 0.8272 0.8918 0.0586  0.0376  0.1322  79  ALA B C   
4740  O O   . ALA B 79  ? 0.5557 0.8941 0.9549 0.0650  0.0456  0.1351  79  ALA B O   
4741  C CB  . ALA B 79  ? 0.4168 0.7273 0.7945 0.0303  0.0211  0.1388  79  ALA B CB  
4742  N N   . ILE B 80  ? 0.4404 0.7426 0.8001 0.0592  0.0412  0.1253  80  ILE B N   
4743  C CA  . ILE B 80  ? 0.3811 0.6946 0.7346 0.0679  0.0541  0.1213  80  ILE B CA  
4744  C C   . ILE B 80  ? 0.4903 0.8146 0.8545 0.0839  0.0584  0.1136  80  ILE B C   
4745  O O   . ILE B 80  ? 0.6108 0.9590 0.9846 0.0909  0.0692  0.1146  80  ILE B O   
4746  C CB  . ILE B 80  ? 0.6230 0.9202 0.9508 0.0649  0.0549  0.1151  80  ILE B CB  
4747  C CG1 . ILE B 80  ? 0.5147 0.7984 0.8359 0.0486  0.0503  0.1206  80  ILE B CG1 
4748  C CG2 . ILE B 80  ? 0.6564 0.9731 0.9772 0.0724  0.0677  0.1138  80  ILE B CG2 
4749  C CD1 . ILE B 80  ? 0.4345 0.7306 0.7603 0.0425  0.0604  0.1288  80  ILE B CD1 
4750  N N   . ARG B 81  ? 0.4634 0.7712 0.8293 0.0895  0.0510  0.1057  81  ARG B N   
4751  C CA  . ARG B 81  ? 0.4433 0.7589 0.8239 0.1045  0.0564  0.0944  81  ARG B CA  
4752  C C   . ARG B 81  ? 0.5298 0.8662 0.9398 0.1105  0.0589  0.1010  81  ARG B C   
4753  O O   . ARG B 81  ? 0.5343 0.8902 0.9555 0.1211  0.0699  0.0930  81  ARG B O   
4754  C CB  . ARG B 81  ? 0.4036 0.6947 0.7883 0.1083  0.0479  0.0865  81  ARG B CB  
4755  C CG  . ARG B 81  ? 0.4222 0.7155 0.8155 0.1217  0.0563  0.0666  81  ARG B CG  
4756  C CD  . ARG B 81  ? 0.4004 0.6790 0.8238 0.1288  0.0496  0.0653  81  ARG B CD  
4757  N NE  . ARG B 81  ? 0.6619 0.9496 1.1099 0.1285  0.0431  0.0832  81  ARG B NE  
4758  C CZ  . ARG B 81  ? 0.6969 1.0051 1.1730 0.1379  0.0494  0.0829  81  ARG B CZ  
4759  N NH1 . ARG B 81  ? 0.5606 0.8833 1.0449 0.1485  0.0632  0.0645  81  ARG B NH1 
4760  N NH2 . ARG B 81  ? 0.5470 0.8642 1.0441 0.1360  0.0416  0.1007  81  ARG B NH2 
4761  N N   . LYS B 82  ? 0.4954 0.8312 0.9185 0.1031  0.0490  0.1147  82  LYS B N   
4762  C CA  . LYS B 82  ? 0.4473 0.8027 0.9011 0.1086  0.0492  0.1217  82  LYS B CA  
4763  C C   . LYS B 82  ? 0.4334 0.8154 0.8924 0.1111  0.0631  0.1224  82  LYS B C   
4764  O O   . LYS B 82  ? 0.5672 0.9535 1.0092 0.1036  0.0692  0.1254  82  LYS B O   
4765  C CB  . LYS B 82  ? 0.4781 0.8342 0.9406 0.0971  0.0357  0.1365  82  LYS B CB  
4766  C CG  . LYS B 82  ? 0.5335 0.8803 1.0127 0.1001  0.0224  0.1428  82  LYS B CG  
4767  C CD  . LYS B 82  ? 0.5646 0.9078 1.0335 0.0841  0.0081  0.1545  82  LYS B CD  
4768  C CE  . LYS B 82  ? 0.5948 0.9646 1.0848 0.0780  0.0022  0.1664  82  LYS B CE  
4769  N NZ  . LYS B 82  ? 0.5408 0.9145 1.0388 0.0717  -0.0149 0.1803  82  LYS B NZ  
4770  N N   . ASP B 83  ? 0.3808 0.7812 0.8665 0.1219  0.0689  0.1209  83  ASP B N   
4771  C CA  . ASP B 83  ? 0.4318 0.8600 0.9281 0.1229  0.0807  0.1256  83  ASP B CA  
4772  C C   . ASP B 83  ? 0.4793 0.9117 0.9807 0.1089  0.0746  0.1403  83  ASP B C   
4773  O O   . ASP B 83  ? 0.5113 0.9360 1.0213 0.1028  0.0609  0.1463  83  ASP B O   
4774  C CB  . ASP B 83  ? 0.5109 0.9575 1.0395 0.1360  0.0864  0.1217  83  ASP B CB  
4775  C CG  . ASP B 83  ? 0.5461 1.0233 1.0864 0.1379  0.1003  0.1261  83  ASP B CG  
4776  O OD1 . ASP B 83  ? 0.5376 1.0239 1.0877 0.1291  0.0982  0.1394  83  ASP B OD1 
4777  O OD2 . ASP B 83  ? 0.5591 1.0533 1.1001 0.1478  0.1142  0.1154  83  ASP B OD2 
4778  N N   . PRO B 84  ? 0.4341 0.8805 0.9322 0.1029  0.0846  0.1462  84  PRO B N   
4779  C CA  . PRO B 84  ? 0.4313 0.8808 0.9385 0.0881  0.0801  0.1563  84  PRO B CA  
4780  C C   . PRO B 84  ? 0.4731 0.9384 1.0109 0.0872  0.0739  0.1618  84  PRO B C   
4781  O O   . PRO B 84  ? 0.5150 0.9822 1.0601 0.0737  0.0659  0.1665  84  PRO B O   
4782  C CB  . PRO B 84  ? 0.4291 0.8939 0.9366 0.0856  0.0956  0.1624  84  PRO B CB  
4783  C CG  . PRO B 84  ? 0.4214 0.8838 0.9048 0.0949  0.1035  0.1559  84  PRO B CG  
4784  C CD  . PRO B 84  ? 0.4319 0.8937 0.9197 0.1082  0.1006  0.1445  84  PRO B CD  
4785  N N   . ASP B 85  ? 0.4528 0.9316 1.0104 0.1007  0.0773  0.1602  85  ASP B N   
4786  C CA  . ASP B 85  ? 0.4203 0.9162 1.0096 0.1006  0.0707  0.1666  85  ASP B CA  
4787  C C   . ASP B 85  ? 0.4039 0.8887 0.9952 0.0968  0.0517  0.1700  85  ASP B C   
4788  O O   . ASP B 85  ? 0.3640 0.8647 0.9760 0.0904  0.0425  0.1777  85  ASP B O   
4789  C CB  . ASP B 85  ? 0.4314 0.9450 1.0442 0.1165  0.0808  0.1637  85  ASP B CB  
4790  C CG  . ASP B 85  ? 0.5049 1.0396 1.1226 0.1181  0.0988  0.1651  85  ASP B CG  
4791  O OD1 . ASP B 85  ? 0.5112 1.0503 1.1272 0.1060  0.1018  0.1722  85  ASP B OD1 
4792  O OD2 . ASP B 85  ? 0.5966 1.1448 1.2223 0.1309  0.1108  0.1591  85  ASP B OD2 
4793  N N   . ASP B 86  ? 0.5361 0.9971 1.1078 0.1000  0.0456  0.1654  86  ASP B N   
4794  C CA  . ASP B 86  ? 0.5512 1.0024 1.1244 0.0963  0.0280  0.1719  86  ASP B CA  
4795  C C   . ASP B 86  ? 0.4920 0.9328 1.0400 0.0785  0.0187  0.1738  86  ASP B C   
4796  O O   . ASP B 86  ? 0.5118 0.9482 1.0576 0.0730  0.0039  0.1806  86  ASP B O   
4797  C CB  . ASP B 86  ? 0.5445 0.9756 1.1167 0.1095  0.0267  0.1665  86  ASP B CB  
4798  C CG  . ASP B 86  ? 0.5951 1.0376 1.1984 0.1267  0.0355  0.1622  86  ASP B CG  
4799  O OD1 . ASP B 86  ? 0.6617 1.1098 1.2603 0.1335  0.0514  0.1506  86  ASP B OD1 
4800  O OD2 . ASP B 86  ? 0.5710 1.0192 1.2049 0.1331  0.0269  0.1708  86  ASP B OD2 
4801  N N   . LEU B 87  ? 0.5210 0.9598 1.0529 0.0690  0.0276  0.1688  87  LEU B N   
4802  C CA  . LEU B 87  ? 0.5697 0.9983 1.0808 0.0517  0.0213  0.1675  87  LEU B CA  
4803  C C   . LEU B 87  ? 0.5476 0.9988 1.0746 0.0372  0.0119  0.1724  87  LEU B C   
4804  O O   . LEU B 87  ? 0.4579 0.9318 1.0091 0.0362  0.0173  0.1741  87  LEU B O   
4805  C CB  . LEU B 87  ? 0.4493 0.8710 0.9469 0.0467  0.0350  0.1619  87  LEU B CB  
4806  C CG  . LEU B 87  ? 0.4890 0.8908 0.9639 0.0568  0.0426  0.1560  87  LEU B CG  
4807  C CD1 . LEU B 87  ? 0.4851 0.8850 0.9503 0.0501  0.0545  0.1550  87  LEU B CD1 
4808  C CD2 . LEU B 87  ? 0.5561 0.9341 1.0104 0.0555  0.0308  0.1529  87  LEU B CD2 
4809  N N   . GLU B 88  ? 0.5873 1.0350 1.1009 0.0251  -0.0018 0.1739  88  GLU B N   
4810  C CA  . GLU B 88  ? 0.5939 1.0677 1.1188 0.0083  -0.0108 0.1753  88  GLU B CA  
4811  C C   . GLU B 88  ? 0.5281 1.0004 1.0459 -0.0091 -0.0029 0.1638  88  GLU B C   
4812  O O   . GLU B 88  ? 0.4800 0.9291 0.9817 -0.0083 0.0071  0.1581  88  GLU B O   
4813  C CB  . GLU B 88  ? 0.5164 0.9953 1.0321 0.0023  -0.0294 0.1837  88  GLU B CB  
4814  C CG  . GLU B 88  ? 0.4720 0.9524 1.0027 0.0193  -0.0377 0.1978  88  GLU B CG  
4815  C CD  . GLU B 88  ? 0.5917 1.0951 1.1567 0.0297  -0.0340 0.2027  88  GLU B CD  
4816  O OE1 . GLU B 88  ? 0.5729 1.1032 1.1526 0.0190  -0.0335 0.2003  88  GLU B OE1 
4817  O OE2 . GLU B 88  ? 0.6104 1.1057 1.1904 0.0482  -0.0308 0.2074  88  GLU B OE2 
4818  N N   . LYS B 89  ? 0.8340 0.8564 0.9395 0.0218  -0.0536 -0.0285 89  LYS B N   
4819  C CA  . LYS B 89  ? 0.8139 0.8351 0.9386 0.0184  -0.0588 -0.0434 89  LYS B CA  
4820  C C   . LYS B 89  ? 0.8011 0.8175 0.8992 0.0187  -0.0531 -0.0539 89  LYS B C   
4821  O O   . LYS B 89  ? 0.8171 0.8273 0.9307 0.0164  -0.0485 -0.0574 89  LYS B O   
4822  C CB  . LYS B 89  ? 0.8104 0.8431 0.9534 0.0179  -0.0764 -0.0597 89  LYS B CB  
4823  C CG  . LYS B 89  ? 0.9675 1.0069 1.1402 0.0174  -0.0832 -0.0513 89  LYS B CG  
4824  C CD  . LYS B 89  ? 0.8403 0.8735 1.0426 0.0138  -0.0729 -0.0344 89  LYS B CD  
4825  C CE  . LYS B 89  ? 0.9086 0.9464 1.1610 0.0089  -0.0819 -0.0386 89  LYS B CE  
4826  N NZ  . LYS B 89  ? 1.0570 1.1069 1.3228 0.0100  -0.0915 -0.0375 89  LYS B NZ  
4827  N N   . GLU B 90  ? 0.8157 0.8365 0.8759 0.0215  -0.0532 -0.0571 90  GLU B N   
4828  C CA  . GLU B 90  ? 0.8094 0.8287 0.8436 0.0212  -0.0472 -0.0680 90  GLU B CA  
4829  C C   . GLU B 90  ? 0.8395 0.8467 0.8682 0.0205  -0.0307 -0.0569 90  GLU B C   
4830  O O   . GLU B 90  ? 0.8117 0.8157 0.8402 0.0193  -0.0261 -0.0663 90  GLU B O   
4831  C CB  . GLU B 90  ? 0.8522 0.8826 0.8472 0.0235  -0.0497 -0.0685 90  GLU B CB  
4832  C CG  . GLU B 90  ? 1.0318 1.0571 1.0117 0.0263  -0.0425 -0.0453 90  GLU B CG  
4833  C CD  . GLU B 90  ? 1.2498 1.2876 1.2323 0.0294  -0.0554 -0.0377 90  GLU B CD  
4834  O OE1 . GLU B 90  ? 1.4026 1.4415 1.3675 0.0325  -0.0527 -0.0210 90  GLU B OE1 
4835  O OE2 . GLU B 90  ? 1.3184 1.3657 1.3246 0.0287  -0.0683 -0.0478 90  GLU B OE2 
4836  N N   . GLU B 91  ? 0.7953 0.7989 0.8230 0.0212  -0.0219 -0.0390 91  GLU B N   
4837  C CA  . GLU B 91  ? 0.7496 0.7485 0.7742 0.0199  -0.0064 -0.0311 91  GLU B CA  
4838  C C   . GLU B 91  ? 0.7937 0.7941 0.8498 0.0172  -0.0060 -0.0292 91  GLU B C   
4839  O O   . GLU B 91  ? 0.8037 0.8036 0.8575 0.0163  0.0018  -0.0300 91  GLU B O   
4840  C CB  . GLU B 91  ? 0.7419 0.7418 0.7655 0.0208  0.0025  -0.0170 91  GLU B CB  
4841  C CG  . GLU B 91  ? 0.6979 0.6944 0.6974 0.0238  0.0039  -0.0136 91  GLU B CG  
4842  C CD  . GLU B 91  ? 0.9479 0.9447 0.9587 0.0251  0.0121  -0.0022 91  GLU B CD  
4843  O OE1 . GLU B 91  ? 0.9964 0.9983 1.0306 0.0261  0.0058  0.0029  91  GLU B OE1 
4844  O OE2 . GLU B 91  ? 0.9721 0.9653 0.9726 0.0248  0.0254  -0.0005 91  GLU B OE2 
4845  N N   . VAL B 92  ? 0.7471 0.7510 0.8352 0.0159  -0.0145 -0.0248 92  VAL B N   
4846  C CA  . VAL B 92  ? 0.7459 0.7523 0.8700 0.0128  -0.0148 -0.0182 92  VAL B CA  
4847  C C   . VAL B 92  ? 0.7009 0.7009 0.8368 0.0127  -0.0206 -0.0328 92  VAL B C   
4848  O O   . VAL B 92  ? 0.7052 0.7053 0.8574 0.0118  -0.0157 -0.0265 92  VAL B O   
4849  C CB  . VAL B 92  ? 0.6652 0.6769 0.8236 0.0106  -0.0227 -0.0107 92  VAL B CB  
4850  C CG1 . VAL B 92  ? 0.6332 0.6474 0.8342 0.0066  -0.0240 -0.0012 92  VAL B CG1 
4851  C CG2 . VAL B 92  ? 0.6078 0.6286 0.7595 0.0106  -0.0149 0.0027  92  VAL B CG2 
4852  N N   . GLU B 93  ? 0.6868 0.6850 0.8166 0.0140  -0.0313 -0.0532 93  GLU B N   
4853  C CA  . GLU B 93  ? 0.7539 0.7492 0.8979 0.0141  -0.0364 -0.0731 93  GLU B CA  
4854  C C   . GLU B 93  ? 0.7025 0.6952 0.8212 0.0156  -0.0254 -0.0749 93  GLU B C   
4855  O O   . GLU B 93  ? 0.6805 0.6699 0.8228 0.0157  -0.0248 -0.0801 93  GLU B O   
4856  C CB  . GLU B 93  ? 0.6731 0.6759 0.8087 0.0147  -0.0486 -0.0982 93  GLU B CB  
4857  C CG  . GLU B 93  ? 0.9987 1.0058 1.1740 0.0126  -0.0618 -0.1042 93  GLU B CG  
4858  C CD  . GLU B 93  ? 1.1735 1.1942 1.3507 0.0124  -0.0749 -0.1358 93  GLU B CD  
4859  O OE1 . GLU B 93  ? 1.1757 1.2086 1.3093 0.0143  -0.0754 -0.1450 93  GLU B OE1 
4860  O OE2 . GLU B 93  ? 1.1511 1.1737 1.3759 0.0099  -0.0846 -0.1517 93  GLU B OE2 
4861  N N   . LYS B 94  ? 0.7252 0.7195 0.8005 0.0168  -0.0165 -0.0701 94  LYS B N   
4862  C CA  . LYS B 94  ? 0.6688 0.6622 0.7187 0.0176  -0.0060 -0.0744 94  LYS B CA  
4863  C C   . LYS B 94  ? 0.7836 0.7778 0.8451 0.0171  0.0044  -0.0578 94  LYS B C   
4864  O O   . LYS B 94  ? 0.7944 0.7892 0.8521 0.0179  0.0102  -0.0627 94  LYS B O   
4865  C CB  . LYS B 94  ? 0.7615 0.7566 0.7669 0.0183  0.0003  -0.0736 94  LYS B CB  
4866  C CG  . LYS B 94  ? 0.7482 0.7504 0.7347 0.0188  -0.0089 -0.0900 94  LYS B CG  
4867  C CD  . LYS B 94  ? 0.8742 0.8794 0.8290 0.0196  -0.0067 -0.0787 94  LYS B CD  
4868  C CE  . LYS B 94  ? 0.8823 0.8793 0.8286 0.0196  0.0077  -0.0604 94  LYS B CE  
4869  N NZ  . LYS B 94  ? 0.9825 0.9801 0.8977 0.0200  0.0136  -0.0529 94  LYS B NZ  
4870  N N   . LEU B 95  ? 0.7136 0.7124 0.7896 0.0156  0.0068  -0.0386 95  LEU B N   
4871  C CA  . LEU B 95  ? 0.6651 0.6736 0.7554 0.0144  0.0151  -0.0218 95  LEU B CA  
4872  C C   . LEU B 95  ? 0.6251 0.6322 0.7558 0.0146  0.0085  -0.0194 95  LEU B C   
4873  O O   . LEU B 95  ? 0.7653 0.7783 0.9012 0.0155  0.0138  -0.0137 95  LEU B O   
4874  C CB  . LEU B 95  ? 0.7500 0.7700 0.8498 0.0120  0.0186  -0.0036 95  LEU B CB  
4875  C CG  . LEU B 95  ? 0.7722 0.8121 0.8652 0.0103  0.0320  0.0102  95  LEU B CG  
4876  C CD1 . LEU B 95  ? 0.6342 0.6878 0.7377 0.0077  0.0345  0.0223  95  LEU B CD1 
4877  C CD2 . LEU B 95  ? 0.8497 0.9015 0.9643 0.0098  0.0331  0.0224  95  LEU B CD2 
4878  N N   . ILE B 96  ? 0.6631 0.6631 0.8268 0.0138  -0.0034 -0.0239 96  ILE B N   
4879  C CA  . ILE B 96  ? 0.7073 0.7031 0.9196 0.0139  -0.0102 -0.0226 96  ILE B CA  
4880  C C   . ILE B 96  ? 0.6402 0.6293 0.8490 0.0171  -0.0112 -0.0454 96  ILE B C   
4881  O O   . ILE B 96  ? 0.6093 0.5987 0.8456 0.0188  -0.0103 -0.0395 96  ILE B O   
4882  C CB  . ILE B 96  ? 0.6273 0.6173 0.8795 0.0115  -0.0223 -0.0269 96  ILE B CB  
4883  C CG1 . ILE B 96  ? 0.5674 0.5671 0.8285 0.0080  -0.0200 -0.0021 96  ILE B CG1 
4884  C CG2 . ILE B 96  ? 0.6241 0.6067 0.9343 0.0116  -0.0295 -0.0299 96  ILE B CG2 
4885  C CD1 . ILE B 96  ? 0.5987 0.5944 0.8860 0.0056  -0.0309 -0.0096 96  ILE B CD1 
4886  N N   . GLU B 97  ? 0.7032 0.6893 0.8794 0.0181  -0.0132 -0.0705 97  GLU B N   
4887  C CA  . GLU B 97  ? 0.7205 0.7051 0.8904 0.0205  -0.0132 -0.0952 97  GLU B CA  
4888  C C   . GLU B 97  ? 0.7382 0.7270 0.8862 0.0222  -0.0012 -0.0864 97  GLU B C   
4889  O O   . GLU B 97  ? 0.7657 0.7540 0.9324 0.0247  -0.0009 -0.0960 97  GLU B O   
4890  C CB  . GLU B 97  ? 0.8102 0.7987 0.9423 0.0201  -0.0162 -0.1192 97  GLU B CB  
4891  C CG  . GLU B 97  ? 0.9762 0.9686 1.1243 0.0209  -0.0236 -0.1533 97  GLU B CG  
4892  C CD  . GLU B 97  ? 1.1321 1.1368 1.2292 0.0205  -0.0208 -0.1726 97  GLU B CD  
4893  O OE1 . GLU B 97  ? 1.1351 1.1416 1.1893 0.0196  -0.0150 -0.1575 97  GLU B OE1 
4894  O OE2 . GLU B 97  ? 1.1447 1.1591 1.2475 0.0207  -0.0240 -0.2025 97  GLU B OE2 
4895  N N   . PHE B 98  ? 0.6778 0.6725 0.7899 0.0210  0.0088  -0.0704 98  PHE B N   
4896  C CA  . PHE B 98  ? 0.7678 0.7707 0.8624 0.0219  0.0204  -0.0625 98  PHE B CA  
4897  C C   . PHE B 98  ? 0.6932 0.7037 0.8278 0.0231  0.0196  -0.0424 98  PHE B C   
4898  O O   . PHE B 98  ? 0.7077 0.7222 0.8513 0.0258  0.0220  -0.0450 98  PHE B O   
4899  C CB  . PHE B 98  ? 0.7207 0.7305 0.7780 0.0197  0.0310  -0.0518 98  PHE B CB  
4900  C CG  . PHE B 98  ? 0.7374 0.7572 0.7711 0.0198  0.0436  -0.0521 98  PHE B CG  
4901  C CD1 . PHE B 98  ? 0.6811 0.6967 0.6856 0.0201  0.0487  -0.0706 98  PHE B CD1 
4902  C CD2 . PHE B 98  ? 0.7482 0.7859 0.7895 0.0191  0.0504  -0.0342 98  PHE B CD2 
4903  C CE1 . PHE B 98  ? 0.7591 0.7844 0.7452 0.0196  0.0606  -0.0722 98  PHE B CE1 
4904  C CE2 . PHE B 98  ? 0.6983 0.7491 0.7198 0.0189  0.0615  -0.0372 98  PHE B CE2 
4905  C CZ  . PHE B 98  ? 0.8215 0.8642 0.8167 0.0191  0.0667  -0.0567 98  PHE B CZ  
4906  N N   . THR B 99  ? 0.6391 0.6540 0.7997 0.0210  0.0161  -0.0206 99  THR B N   
4907  C CA  . THR B 99  ? 0.6403 0.6657 0.8433 0.0215  0.0145  0.0042  99  THR B CA  
4908  C C   . THR B 99  ? 0.6189 0.6323 0.8660 0.0251  0.0060  -0.0059 99  THR B C   
4909  O O   . THR B 99  ? 0.5978 0.6196 0.8647 0.0281  0.0076  0.0053  99  THR B O   
4910  C CB  . THR B 99  ? 0.6788 0.7098 0.9077 0.0176  0.0108  0.0269  99  THR B CB  
4911  O OG1 . THR B 99  ? 0.7181 0.7540 0.9098 0.0148  0.0163  0.0251  99  THR B OG1 
4912  C CG2 . THR B 99  ? 0.5468 0.6014 0.8019 0.0166  0.0140  0.0612  99  THR B CG2 
4913  N N   . LYS B 100 ? 0.7648 0.7614 1.0304 0.0250  -0.0033 -0.0292 100 LYS B N   
4914  C CA  . LYS B 100 ? 0.6275 0.6134 0.9450 0.0281  -0.0116 -0.0438 100 LYS B CA  
4915  C C   . LYS B 100 ? 0.6172 0.6056 0.9216 0.0325  -0.0068 -0.0604 100 LYS B C   
4916  O O   . LYS B 100 ? 0.7356 0.7223 1.0865 0.0364  -0.0100 -0.0573 100 LYS B O   
4917  C CB  . LYS B 100 ? 0.6134 0.5874 0.9463 0.0265  -0.0213 -0.0739 100 LYS B CB  
4918  C CG  . LYS B 100 ? 0.7515 0.7195 1.1387 0.0233  -0.0302 -0.0608 100 LYS B CG  
4919  C CD  . LYS B 100 ? 0.8752 0.8331 1.3396 0.0254  -0.0381 -0.0670 100 LYS B CD  
4920  C CE  . LYS B 100 ? 0.8275 0.7857 1.3472 0.0237  -0.0396 -0.0253 100 LYS B CE  
4921  N NZ  . LYS B 100 ? 0.6215 0.5665 1.2276 0.0254  -0.0481 -0.0307 100 LYS B NZ  
4922  N N   . LEU B 101 ? 0.6807 0.6734 0.9256 0.0320  0.0011  -0.0768 101 LEU B N   
4923  C CA  . LEU B 101 ? 0.6906 0.6878 0.9222 0.0355  0.0067  -0.0928 101 LEU B CA  
4924  C C   . LEU B 101 ? 0.7123 0.7224 0.9566 0.0382  0.0118  -0.0656 101 LEU B C   
4925  O O   . LEU B 101 ? 0.7264 0.7384 0.9952 0.0428  0.0112  -0.0724 101 LEU B O   
4926  C CB  . LEU B 101 ? 0.6876 0.6892 0.8543 0.0333  0.0159  -0.1095 101 LEU B CB  
4927  C CG  . LEU B 101 ? 0.8538 0.8576 1.0086 0.0351  0.0185  -0.1417 101 LEU B CG  
4928  C CD1 . LEU B 101 ? 0.8573 0.8665 0.9494 0.0317  0.0283  -0.1512 101 LEU B CD1 
4929  C CD2 . LEU B 101 ? 0.8266 0.8359 1.0095 0.0400  0.0209  -0.1403 101 LEU B CD2 
4930  N N   . ASN B 102 ? 0.6191 0.6421 0.8484 0.0356  0.0166  -0.0358 102 ASN B N   
4931  C CA  . ASN B 102 ? 0.5601 0.6049 0.7904 0.0374  0.0224  -0.0115 102 ASN B CA  
4932  C C   . ASN B 102 ? 0.6947 0.7496 0.9771 0.0382  0.0162  0.0244  102 ASN B C   
4933  O O   . ASN B 102 ? 0.7087 0.7898 0.9910 0.0389  0.0203  0.0505  102 ASN B O   
4934  C CB  . ASN B 102 ? 0.5804 0.6420 0.7557 0.0335  0.0342  -0.0068 102 ASN B CB  
4935  C CG  . ASN B 102 ? 0.6886 0.7371 0.8174 0.0315  0.0398  -0.0366 102 ASN B CG  
4936  O OD1 . ASN B 102 ? 0.7359 0.7819 0.8508 0.0334  0.0432  -0.0574 102 ASN B OD1 
4937  N ND2 . ASN B 102 ? 0.7828 0.8249 0.8902 0.0276  0.0406  -0.0371 102 ASN B ND2 
4938  N N   . TYR B 103 ? 0.7036 0.7411 1.0332 0.0377  0.0062  0.0266  103 TYR B N   
4939  C CA  . TYR B 103 ? 0.6731 0.7190 1.0574 0.0374  0.0006  0.0642  103 TYR B CA  
4940  C C   . TYR B 103 ? 0.6931 0.7521 1.1148 0.0433  -0.0012 0.0838  103 TYR B C   
4941  O O   . TYR B 103 ? 0.6183 0.7034 1.0561 0.0429  -0.0004 0.1238  103 TYR B O   
4942  C CB  . TYR B 103 ? 0.6684 0.6896 1.1042 0.0359  -0.0099 0.0556  103 TYR B CB  
4943  C CG  . TYR B 103 ? 0.7136 0.7413 1.1986 0.0323  -0.0143 0.0943  103 TYR B CG  
4944  C CD1 . TYR B 103 ? 0.6845 0.7333 1.1413 0.0267  -0.0086 0.1201  103 TYR B CD1 
4945  C CD2 . TYR B 103 ? 0.6943 0.7077 1.2586 0.0342  -0.0237 0.1037  103 TYR B CD2 
4946  C CE1 . TYR B 103 ? 0.8052 0.8636 1.3076 0.0225  -0.0118 0.1565  103 TYR B CE1 
4947  C CE2 . TYR B 103 ? 0.7375 0.7570 1.3510 0.0301  -0.0272 0.1417  103 TYR B CE2 
4948  C CZ  . TYR B 103 ? 0.8186 0.8617 1.3989 0.0240  -0.0211 0.1690  103 TYR B CZ  
4949  O OH  . TYR B 103 ? 0.8603 0.9127 1.4906 0.0190  -0.0238 0.2079  103 TYR B OH  
4950  N N   . GLU B 104 ? 0.7723 0.8178 1.2067 0.0489  -0.0034 0.0560  104 GLU B N   
4951  C CA  . GLU B 104 ? 0.6675 0.7212 1.1458 0.0560  -0.0067 0.0694  104 GLU B CA  
4952  C C   . GLU B 104 ? 0.5966 0.6820 1.0322 0.0579  0.0017  0.0818  104 GLU B C   
4953  O O   . GLU B 104 ? 0.6791 0.7820 1.1494 0.0635  -0.0012 0.1057  104 GLU B O   
4954  C CB  . GLU B 104 ? 0.6527 0.6826 1.1600 0.0611  -0.0112 0.0283  104 GLU B CB  
4955  C CG  . GLU B 104 ? 0.8295 0.8493 1.2765 0.0583  -0.0054 -0.0185 104 GLU B CG  
4956  C CD  . GLU B 104 ? 0.9855 0.9874 1.4272 0.0527  -0.0093 -0.0372 104 GLU B CD  
4957  O OE1 . GLU B 104 ? 0.9956 0.9840 1.4446 0.0532  -0.0126 -0.0769 104 GLU B OE1 
4958  O OE2 . GLU B 104 ? 1.0641 1.0695 1.4934 0.0477  -0.0089 -0.0134 104 GLU B OE2 
4959  N N   . LYS B 105 ? 0.5792 0.6740 0.9451 0.0535  0.0118  0.0662  105 LYS B N   
4960  C CA  . LYS B 105 ? 0.5550 0.6801 0.8825 0.0546  0.0204  0.0703  105 LYS B CA  
4961  C C   . LYS B 105 ? 0.5512 0.7159 0.8859 0.0532  0.0211  0.1152  105 LYS B C   
4962  O O   . LYS B 105 ? 0.5963 0.7675 0.9303 0.0477  0.0212  0.1350  105 LYS B O   
4963  C CB  . LYS B 105 ? 0.5816 0.7051 0.8403 0.0494  0.0315  0.0420  105 LYS B CB  
4964  C CG  . LYS B 105 ? 0.6649 0.7540 0.9115 0.0485  0.0304  0.0040  105 LYS B CG  
4965  C CD  . LYS B 105 ? 0.6751 0.7652 0.8703 0.0472  0.0407  -0.0257 105 LYS B CD  
4966  C CE  . LYS B 105 ? 0.6586 0.7230 0.8514 0.0477  0.0383  -0.0620 105 LYS B CE  
4967  N NZ  . LYS B 105 ? 0.6581 0.7193 0.7923 0.0427  0.0483  -0.0837 105 LYS B NZ  
4968  N N   . PRO B 106 ? 0.5508 0.7469 0.8924 0.0578  0.0217  0.1316  106 PRO B N   
4969  C CA  . PRO B 106 ? 0.5490 0.7938 0.8939 0.0561  0.0225  0.1751  106 PRO B CA  
4970  C C   . PRO B 106 ? 0.5379 0.8088 0.8289 0.0475  0.0329  0.1746  106 PRO B C   
4971  O O   . PRO B 106 ? 0.5388 0.8390 0.8393 0.0435  0.0324  0.2082  106 PRO B O   
4972  C CB  . PRO B 106 ? 0.6213 0.8959 0.9673 0.0625  0.0229  0.1786  106 PRO B CB  
4973  C CG  . PRO B 106 ? 0.5576 0.7921 0.9332 0.0695  0.0177  0.1497  106 PRO B CG  
4974  C CD  . PRO B 106 ? 0.5535 0.7456 0.9034 0.0648  0.0211  0.1112  106 PRO B CD  
4975  N N   . ILE B 107 ? 0.5288 0.7912 0.7671 0.0444  0.0428  0.1375  107 ILE B N   
4976  C CA  . ILE B 107 ? 0.5191 0.8036 0.7128 0.0368  0.0532  0.1322  107 ILE B CA  
4977  C C   . ILE B 107 ? 0.6242 0.8902 0.8245 0.0318  0.0512  0.1395  107 ILE B C   
4978  O O   . ILE B 107 ? 0.5512 0.8408 0.7259 0.0257  0.0587  0.1418  107 ILE B O   
4979  C CB  . ILE B 107 ? 0.5149 0.7864 0.6607 0.0349  0.0637  0.0907  107 ILE B CB  
4980  C CG1 . ILE B 107 ? 0.5920 0.8102 0.7404 0.0375  0.0600  0.0624  107 ILE B CG1 
4981  C CG2 . ILE B 107 ? 0.5961 0.9008 0.7297 0.0374  0.0686  0.0854  107 ILE B CG2 
4982  C CD1 . ILE B 107 ? 0.5188 0.7174 0.6221 0.0329  0.0696  0.0303  107 ILE B CD1 
4983  N N   . TYR B 108 ? 0.6618 0.8883 0.8991 0.0342  0.0414  0.1407  108 TYR B N   
4984  C CA  . TYR B 108 ? 0.6424 0.8508 0.8920 0.0297  0.0381  0.1471  108 TYR B CA  
4985  C C   . TYR B 108 ? 0.6762 0.8989 0.9797 0.0293  0.0301  0.1896  108 TYR B C   
4986  O O   . TYR B 108 ? 0.8029 1.0027 1.1333 0.0267  0.0246  0.1945  108 TYR B O   
4987  C CB  . TYR B 108 ? 0.5779 0.7354 0.8323 0.0312  0.0328  0.1154  108 TYR B CB  
4988  C CG  . TYR B 108 ? 0.6244 0.7671 0.8280 0.0278  0.0402  0.0842  108 TYR B CG  
4989  C CD1 . TYR B 108 ? 0.6266 0.7734 0.7886 0.0284  0.0491  0.0607  108 TYR B CD1 
4990  C CD2 . TYR B 108 ? 0.7012 0.8264 0.9026 0.0239  0.0379  0.0796  108 TYR B CD2 
4991  C CE1 . TYR B 108 ? 0.6511 0.7836 0.7727 0.0252  0.0558  0.0364  108 TYR B CE1 
4992  C CE2 . TYR B 108 ? 0.7130 0.8254 0.8726 0.0216  0.0437  0.0551  108 TYR B CE2 
4993  C CZ  . TYR B 108 ? 0.6918 0.8072 0.8128 0.0222  0.0527  0.0349  108 TYR B CZ  
4994  O OH  . TYR B 108 ? 0.7641 0.8662 0.8496 0.0197  0.0583  0.0149  108 TYR B OH  
4995  N N   . ARG B 109 ? 0.6044 0.8659 0.9266 0.0317  0.0291  0.2218  109 ARG B N   
4996  C CA  . ARG B 109 ? 0.5936 0.8711 0.9719 0.0313  0.0215  0.2685  109 ARG B CA  
4997  C C   . ARG B 109 ? 0.7137 1.0362 1.0747 0.0231  0.0280  0.2951  109 ARG B C   
4998  O O   . ARG B 109 ? 0.7414 1.1195 1.1018 0.0217  0.0305  0.3284  109 ARG B O   
4999  C CB  . ARG B 109 ? 0.5681 0.8682 0.9804 0.0383  0.0159  0.2953  109 ARG B CB  
5000  C CG  . ARG B 109 ? 0.7017 0.9653 1.1883 0.0438  0.0038  0.3083  109 ARG B CG  
5001  C CD  . ARG B 109 ? 0.7912 1.0780 1.3178 0.0518  -0.0024 0.3379  109 ARG B CD  
5002  N NE  . ARG B 109 ? 0.7117 0.9707 1.2394 0.0598  -0.0044 0.3013  109 ARG B NE  
5003  C CZ  . ARG B 109 ? 0.6874 0.9744 1.2013 0.0656  -0.0032 0.3022  109 ARG B CZ  
5004  N NH1 . ARG B 109 ? 0.7281 1.0744 1.2255 0.0646  -0.0007 0.3374  109 ARG B NH1 
5005  N NH2 . ARG B 109 ? 0.7747 1.0339 1.2929 0.0723  -0.0046 0.2661  109 ARG B NH2 
5006  N N   . PHE B 110 ? 0.7194 1.0205 1.0658 0.0176  0.0307  0.2780  110 PHE B N   
5007  C CA  . PHE B 110 ? 0.7019 1.0372 1.0422 0.0095  0.0360  0.2997  110 PHE B CA  
5008  C C   . PHE B 110 ? 0.7613 1.0719 1.1573 0.0070  0.0275  0.3226  110 PHE B C   
5009  O O   . PHE B 110 ? 0.7489 1.0067 1.1652 0.0093  0.0207  0.2992  110 PHE B O   
5010  C CB  . PHE B 110 ? 0.7388 1.0697 1.0270 0.0051  0.0455  0.2636  110 PHE B CB  
5011  C CG  . PHE B 110 ? 0.7658 1.1213 1.0037 0.0061  0.0554  0.2389  110 PHE B CG  
5012  C CD1 . PHE B 110 ? 0.6937 1.1133 0.9100 0.0017  0.0644  0.2518  110 PHE B CD1 
5013  C CD2 . PHE B 110 ? 0.7431 1.0604 0.9569 0.0107  0.0561  0.2010  110 PHE B CD2 
5014  C CE1 . PHE B 110 ? 0.6418 1.0844 0.8167 0.0020  0.0738  0.2246  110 PHE B CE1 
5015  C CE2 . PHE B 110 ? 0.6792 1.0173 0.8517 0.0107  0.0658  0.1779  110 PHE B CE2 
5016  C CZ  . PHE B 110 ? 0.6446 1.0441 0.7995 0.0064  0.0746  0.1885  110 PHE B CZ  
5017  N N   . GLU B 111 ? 0.7354 1.0884 1.1571 0.0015  0.0283  0.3678  111 GLU B N   
5018  C CA  . GLU B 111 ? 0.7426 1.0764 1.2240 -0.0020 0.0211  0.3944  111 GLU B CA  
5019  C C   . GLU B 111 ? 0.7484 1.0517 1.2186 -0.0070 0.0225  0.3665  111 GLU B C   
5020  O O   . GLU B 111 ? 0.6666 0.9292 1.1826 -0.0074 0.0143  0.3639  111 GLU B O   
5021  C CB  . GLU B 111 ? 0.8197 1.2123 1.3279 -0.0080 0.0233  0.4525  111 GLU B CB  
5022  C CG  . GLU B 111 ? 0.9866 1.4333 1.4925 -0.0047 0.0240  0.4865  111 GLU B CG  
5023  C CD  . GLU B 111 ? 1.0869 1.5743 1.5217 -0.0041 0.0339  0.4599  111 GLU B CD  
5024  O OE1 . GLU B 111 ? 1.2840 1.8016 1.7141 0.0011  0.0326  0.4727  111 GLU B OE1 
5025  O OE2 . GLU B 111 ? 1.1482 1.6367 1.5377 -0.0086 0.0426  0.4264  111 GLU B OE2 
5026  N N   . ARG B 112 ? 0.6832 1.0071 1.0977 -0.0107 0.0324  0.3447  112 ARG B N   
5027  C CA  . ARG B 112 ? 0.7203 1.0173 1.1244 -0.0145 0.0331  0.3189  112 ARG B CA  
5028  C C   . ARG B 112 ? 0.7081 0.9439 1.1110 -0.0087 0.0255  0.2783  112 ARG B C   
5029  O O   . ARG B 112 ? 0.7876 0.9919 1.2129 -0.0106 0.0195  0.2669  112 ARG B O   
5030  C CB  . ARG B 112 ? 0.7659 1.0965 1.1146 -0.0182 0.0454  0.3009  112 ARG B CB  
5031  C CG  . ARG B 112 ? 0.7296 1.0897 1.0863 -0.0267 0.0505  0.3165  112 ARG B CG  
5032  C CD  . ARG B 112 ? 0.7131 1.0260 1.0958 -0.0279 0.0429  0.3030  112 ARG B CD  
5033  N NE  . ARG B 112 ? 0.7108 1.0475 1.0864 -0.0347 0.0495  0.3027  112 ARG B NE  
5034  C CZ  . ARG B 112 ? 0.7615 1.0738 1.1636 -0.0378 0.0443  0.2988  112 ARG B CZ  
5035  N NH1 . ARG B 112 ? 0.9222 1.1881 1.3624 -0.0354 0.0323  0.2954  112 ARG B NH1 
5036  N NH2 . ARG B 112 ? 0.7600 1.0981 1.1532 -0.0435 0.0513  0.2964  112 ARG B NH2 
5037  N N   . ILE B 113 ? 0.6805 0.9034 1.0577 -0.0021 0.0257  0.2557  113 ILE B N   
5038  C CA  . ILE B 113 ? 0.6702 0.8424 1.0461 0.0030  0.0190  0.2182  113 ILE B CA  
5039  C C   . ILE B 113 ? 0.6957 0.8378 1.1378 0.0041  0.0070  0.2263  113 ILE B C   
5040  O O   . ILE B 113 ? 0.8454 0.9519 1.2980 0.0046  0.0005  0.1985  113 ILE B O   
5041  C CB  . ILE B 113 ? 0.7882 0.9586 1.1323 0.0093  0.0221  0.1983  113 ILE B CB  
5042  C CG1 . ILE B 113 ? 0.7857 0.9694 1.0665 0.0080  0.0331  0.1749  113 ILE B CG1 
5043  C CG2 . ILE B 113 ? 0.7289 0.8549 1.0866 0.0146  0.0140  0.1675  113 ILE B CG2 
5044  C CD1 . ILE B 113 ? 0.6976 0.8795 0.9494 0.0130  0.0369  0.1547  113 ILE B CD1 
5045  N N   . ARG B 114 ? 0.7641 0.9228 1.2554 0.0044  0.0039  0.2647  114 ARG B N   
5046  C CA  . ARG B 114 ? 0.7620 0.8928 1.3282 0.0049  -0.0068 0.2750  114 ARG B CA  
5047  C C   . ARG B 114 ? 0.8229 0.9444 1.4152 -0.0024 -0.0094 0.2788  114 ARG B C   
5048  O O   . ARG B 114 ? 0.8317 0.9172 1.4627 -0.0022 -0.0180 0.2567  114 ARG B O   
5049  C CB  . ARG B 114 ? 0.7675 0.9223 1.3845 0.0065  -0.0090 0.3230  114 ARG B CB  
5050  C CG  . ARG B 114 ? 0.8361 0.9825 1.4598 0.0158  -0.0121 0.3136  114 ARG B CG  
5051  C CD  . ARG B 114 ? 0.8790 1.0721 1.4575 0.0177  -0.0044 0.3330  114 ARG B CD  
5052  N NE  . ARG B 114 ? 0.8915 1.0783 1.4820 0.0268  -0.0080 0.3262  114 ARG B NE  
5053  C CZ  . ARG B 114 ? 0.8112 0.9732 1.3694 0.0319  -0.0072 0.2806  114 ARG B CZ  
5054  N NH1 . ARG B 114 ? 0.7002 0.8423 1.2085 0.0292  -0.0030 0.2397  114 ARG B NH1 
5055  N NH2 . ARG B 114 ? 0.8176 0.9771 1.3957 0.0399  -0.0107 0.2778  114 ARG B NH2 
5056  N N   . GLU B 115 ? 0.7280 0.8851 1.3016 -0.0093 -0.0020 0.3043  115 GLU B N   
5057  C CA  . GLU B 115 ? 0.7023 0.8547 1.3028 -0.0167 -0.0039 0.3100  115 GLU B CA  
5058  C C   . GLU B 115 ? 0.8484 0.9709 1.4156 -0.0160 -0.0062 0.2626  115 GLU B C   
5059  O O   . GLU B 115 ? 0.8655 0.9608 1.4710 -0.0181 -0.0143 0.2486  115 GLU B O   
5060  C CB  . GLU B 115 ? 0.8144 1.0179 1.3984 -0.0242 0.0060  0.3454  115 GLU B CB  
5061  C CG  . GLU B 115 ? 0.8927 1.1431 1.4635 -0.0233 0.0124  0.3801  115 GLU B CG  
5062  C CD  . GLU B 115 ? 0.8878 1.1976 1.4433 -0.0317 0.0226  0.4130  115 GLU B CD  
5063  O OE1 . GLU B 115 ? 0.8271 1.1400 1.3715 -0.0376 0.0263  0.4019  115 GLU B OE1 
5064  O OE2 . GLU B 115 ? 0.8240 1.1817 1.3784 -0.0325 0.0268  0.4489  115 GLU B OE2 
5065  N N   . LEU B 116 ? 0.7906 0.9204 1.2891 -0.0133 0.0007  0.2383  116 LEU B N   
5066  C CA  . LEU B 116 ? 0.7330 0.8385 1.1980 -0.0122 -0.0015 0.1982  116 LEU B CA  
5067  C C   . LEU B 116 ? 0.6970 0.7625 1.1849 -0.0078 -0.0125 0.1669  116 LEU B C   
5068  O O   . LEU B 116 ? 0.6982 0.7446 1.1963 -0.0092 -0.0195 0.1448  116 LEU B O   
5069  C CB  . LEU B 116 ? 0.7235 0.8420 1.1188 -0.0094 0.0081  0.1804  116 LEU B CB  
5070  C CG  . LEU B 116 ? 0.7401 0.9022 1.1105 -0.0141 0.0199  0.2010  116 LEU B CG  
5071  C CD1 . LEU B 116 ? 0.7260 0.9021 1.0410 -0.0108 0.0295  0.1848  116 LEU B CD1 
5072  C CD2 . LEU B 116 ? 0.7293 0.8920 1.0976 -0.0185 0.0203  0.1941  116 LEU B CD2 
5073  N N   . MET B 117 ? 0.6649 0.7214 1.1637 -0.0024 -0.0144 0.1634  117 MET B N   
5074  C CA  . MET B 117 ? 0.8033 0.8275 1.3218 0.0019  -0.0236 0.1281  117 MET B CA  
5075  C C   . MET B 117 ? 0.8215 0.8286 1.4174 -0.0012 -0.0338 0.1308  117 MET B C   
5076  O O   . MET B 117 ? 0.7468 0.7330 1.3566 -0.0010 -0.0419 0.0958  117 MET B O   
5077  C CB  . MET B 117 ? 0.7699 0.7920 1.2840 0.0085  -0.0221 0.1230  117 MET B CB  
5078  C CG  . MET B 117 ? 0.7479 0.7796 1.1872 0.0115  -0.0132 0.1065  117 MET B CG  
5079  S SD  . MET B 117 ? 1.0272 1.0348 1.4253 0.0140  -0.0165 0.0544  117 MET B SD  
5080  C CE  . MET B 117 ? 0.7799 0.7958 1.1347 0.0092  -0.0126 0.0554  117 MET B CE  
5081  N N   . ASN B 118 ? 0.7764 0.7953 1.4255 -0.0045 -0.0334 0.1722  118 ASN B N   
5082  C CA  . ASN B 118 ? 0.8168 0.8203 1.5468 -0.0088 -0.0418 0.1790  118 ASN B CA  
5083  C C   . ASN B 118 ? 0.6987 0.7064 1.4301 -0.0164 -0.0427 0.1795  118 ASN B C   
5084  O O   . ASN B 118 ? 0.7767 0.7696 1.5726 -0.0206 -0.0502 0.1760  118 ASN B O   
5085  C CB  . ASN B 118 ? 0.8283 0.8442 1.6192 -0.0099 -0.0409 0.2288  118 ASN B CB  
5086  C CG  . ASN B 118 ? 0.7999 0.8061 1.6122 -0.0017 -0.0433 0.2256  118 ASN B CG  
5087  O OD1 . ASN B 118 ? 0.7635 0.7419 1.6291 0.0014  -0.0515 0.1996  118 ASN B OD1 
5088  N ND2 . ASN B 118 ? 0.8513 0.8830 1.6219 0.0019  -0.0362 0.2482  118 ASN B ND2 
5089  N N   . LYS B 119 ? 0.6622 0.6899 1.3292 -0.0181 -0.0352 0.1817  119 LYS B N   
5090  C CA  . LYS B 119 ? 0.7663 0.7983 1.4319 -0.0242 -0.0363 0.1778  119 LYS B CA  
5091  C C   . LYS B 119 ? 0.7952 0.8056 1.4384 -0.0214 -0.0443 0.1290  119 LYS B C   
5092  O O   . LYS B 119 ? 0.7547 0.7577 1.3490 -0.0153 -0.0440 0.1020  119 LYS B O   
5093  C CB  . LYS B 119 ? 0.7791 0.8440 1.3912 -0.0269 -0.0248 0.1981  119 LYS B CB  
5094  C CG  . LYS B 119 ? 0.8652 0.9607 1.5126 -0.0344 -0.0187 0.2460  119 LYS B CG  
5095  C CD  . LYS B 119 ? 0.8237 0.9585 1.4154 -0.0364 -0.0061 0.2604  119 LYS B CD  
5096  C CE  . LYS B 119 ? 0.9092 1.0851 1.5230 -0.0417 0.0017  0.3107  119 LYS B CE  
5097  N NZ  . LYS B 119 ? 0.8621 1.0296 1.5557 -0.0459 -0.0047 0.3420  119 LYS B NZ  
5098  N N   . GLU B 120 ? 0.7873 0.7915 1.4663 -0.0265 -0.0515 0.1192  120 GLU B N   
5099  C CA  . GLU B 120 ? 0.7524 0.7412 1.4223 -0.0245 -0.0616 0.0737  120 GLU B CA  
5100  C C   . GLU B 120 ? 0.7310 0.7306 1.3333 -0.0229 -0.0592 0.0618  120 GLU B C   
5101  O O   . GLU B 120 ? 0.7277 0.7207 1.2894 -0.0181 -0.0635 0.0294  120 GLU B O   
5102  C CB  . GLU B 120 ? 0.6998 0.6796 1.4449 -0.0306 -0.0715 0.0655  120 GLU B CB  
5103  C CG  . GLU B 120 ? 0.9657 0.9361 1.7956 -0.0340 -0.0727 0.0881  120 GLU B CG  
5104  C CD  . GLU B 120 ? 1.0609 1.0498 1.9065 -0.0386 -0.0626 0.1445  120 GLU B CD  
5105  O OE1 . GLU B 120 ? 1.0907 1.0743 2.0037 -0.0407 -0.0631 0.1705  120 GLU B OE1 
5106  O OE2 . GLU B 120 ? 0.9986 1.0103 1.7919 -0.0401 -0.0543 0.1629  120 GLU B OE2 
5107  N N   . LYS B 121 ? 0.6716 0.6902 1.2644 -0.0271 -0.0521 0.0884  121 LYS B N   
5108  C CA  . LYS B 121 ? 0.6151 0.6456 1.1513 -0.0253 -0.0482 0.0817  121 LYS B CA  
5109  C C   . LYS B 121 ? 0.6568 0.7117 1.1663 -0.0268 -0.0338 0.1131  121 LYS B C   
5110  O O   . LYS B 121 ? 0.7722 0.8423 1.3164 -0.0321 -0.0286 0.1451  121 LYS B O   
5111  C CB  . LYS B 121 ? 0.6425 0.6766 1.2014 -0.0294 -0.0556 0.0736  121 LYS B CB  
5112  C CG  . LYS B 121 ? 0.7270 0.7678 1.2331 -0.0254 -0.0555 0.0587  121 LYS B CG  
5113  C CD  . LYS B 121 ? 0.7567 0.7834 1.2348 -0.0193 -0.0657 0.0232  121 LYS B CD  
5114  C CE  . LYS B 121 ? 0.9261 0.9606 1.3626 -0.0155 -0.0679 0.0131  121 LYS B CE  
5115  N NZ  . LYS B 121 ? 0.9354 0.9691 1.3849 -0.0148 -0.0836 -0.0138 121 LYS B NZ  
5116  N N   . LEU B 122 ? 0.6787 0.7406 1.1292 -0.0225 -0.0273 0.1039  122 LEU B N   
5117  C CA  . LEU B 122 ? 0.7112 0.7984 1.1310 -0.0230 -0.0130 0.1242  122 LEU B CA  
5118  C C   . LEU B 122 ? 0.6340 0.7382 1.0281 -0.0237 -0.0073 0.1210  122 LEU B C   
5119  O O   . LEU B 122 ? 0.6609 0.7513 1.0305 -0.0193 -0.0123 0.0977  122 LEU B O   
5120  C CB  . LEU B 122 ? 0.7129 0.7929 1.0903 -0.0170 -0.0085 0.1131  122 LEU B CB  
5121  C CG  . LEU B 122 ? 0.7257 0.7910 1.1283 -0.0152 -0.0132 0.1148  122 LEU B CG  
5122  C CD1 . LEU B 122 ? 0.5807 0.6369 0.9392 -0.0089 -0.0098 0.0968  122 LEU B CD1 
5123  C CD2 . LEU B 122 ? 0.6940 0.7800 1.1351 -0.0198 -0.0085 0.1518  122 LEU B CD2 
5124  N N   . ASN B 123 ? 0.6570 0.7942 1.0576 -0.0290 0.0033  0.1445  123 ASN B N   
5125  C CA  . ASN B 123 ? 0.6911 0.8480 1.0724 -0.0295 0.0103  0.1391  123 ASN B CA  
5126  C C   . ASN B 123 ? 0.6376 0.8028 0.9701 -0.0249 0.0208  0.1280  123 ASN B C   
5127  O O   . ASN B 123 ? 0.6533 0.8085 0.9644 -0.0214 0.0223  0.1239  123 ASN B O   
5128  C CB  . ASN B 123 ? 0.7205 0.9154 1.1311 -0.0380 0.0181  0.1650  123 ASN B CB  
5129  C CG  . ASN B 123 ? 0.7940 1.0120 1.2212 -0.0429 0.0242  0.1959  123 ASN B CG  
5130  O OD1 . ASN B 123 ? 0.8550 1.0547 1.3139 -0.0437 0.0164  0.2073  123 ASN B OD1 
5131  N ND2 . ASN B 123 ? 0.7701 1.0312 1.1782 -0.0459 0.0379  0.2090  123 ASN B ND2 
5132  N N   . ARG B 124 ? 0.5681 0.8893 0.8733 0.0001  0.0530  0.0371  124 ARG B N   
5133  C CA  . ARG B 124 ? 0.6130 0.9268 0.8973 0.0083  0.0527  0.0279  124 ARG B CA  
5134  C C   . ARG B 124 ? 0.6807 0.9961 0.9441 0.0035  0.0571  0.0358  124 ARG B C   
5135  O O   . ARG B 124 ? 0.5739 0.8716 0.8196 0.0068  0.0526  0.0338  124 ARG B O   
5136  C CB  . ARG B 124 ? 0.5729 0.9047 0.8644 0.0155  0.0584  0.0145  124 ARG B CB  
5137  C CG  . ARG B 124 ? 0.5487 0.8818 0.8229 0.0209  0.0627  0.0046  124 ARG B CG  
5138  C CD  . ARG B 124 ? 0.5005 0.8539 0.7879 0.0276  0.0698  -0.0107 124 ARG B CD  
5139  N NE  . ARG B 124 ? 0.6055 0.9532 0.8834 0.0350  0.0711  -0.0245 124 ARG B NE  
5140  C CZ  . ARG B 124 ? 0.6288 0.9886 0.8899 0.0316  0.0785  -0.0291 124 ARG B CZ  
5141  N NH1 . ARG B 124 ? 0.4738 0.8542 0.7238 0.0210  0.0853  -0.0187 124 ARG B NH1 
5142  N NH2 . ARG B 124 ? 0.4725 0.8253 0.7295 0.0387  0.0789  -0.0442 124 ARG B NH2 
5143  N N   . GLU B 125 ? 0.6381 0.9772 0.9036 -0.0049 0.0658  0.0461  125 GLU B N   
5144  C CA  . GLU B 125 ? 0.5149 0.8629 0.7603 -0.0102 0.0700  0.0551  125 GLU B CA  
5145  C C   . GLU B 125 ? 0.6189 0.9440 0.8593 -0.0142 0.0624  0.0691  125 GLU B C   
5146  O O   . GLU B 125 ? 0.6653 0.9844 0.8854 -0.0137 0.0608  0.0708  125 GLU B O   
5147  C CB  . GLU B 125 ? 0.5339 0.9171 0.7846 -0.0194 0.0806  0.0661  125 GLU B CB  
5148  C CG  . GLU B 125 ? 0.6341 1.0456 0.8838 -0.0157 0.0903  0.0495  125 GLU B CG  
5149  C CD  . GLU B 125 ? 0.7142 1.1250 0.9871 -0.0094 0.0899  0.0369  125 GLU B CD  
5150  O OE1 . GLU B 125 ? 0.6599 1.0705 0.9533 -0.0140 0.0883  0.0462  125 GLU B OE1 
5151  O OE2 . GLU B 125 ? 0.7130 1.1243 0.9862 0.0002  0.0909  0.0174  125 GLU B OE2 
5152  N N   . GLU B 126 ? 0.6762 0.9894 0.9374 -0.0183 0.0577  0.0777  126 GLU B N   
5153  C CA  . GLU B 126 ? 0.6172 0.9080 0.8798 -0.0214 0.0504  0.0881  126 GLU B CA  
5154  C C   . GLU B 126 ? 0.5537 0.8190 0.8019 -0.0130 0.0423  0.0747  126 GLU B C   
5155  O O   . GLU B 126 ? 0.6641 0.9171 0.8980 -0.0131 0.0389  0.0792  126 GLU B O   
5156  C CB  . GLU B 126 ? 0.6945 0.9799 0.9882 -0.0276 0.0479  0.0957  126 GLU B CB  
5157  C CG  . GLU B 126 ? 0.7218 1.0312 1.0328 -0.0376 0.0558  0.1134  126 GLU B CG  
5158  C CD  . GLU B 126 ? 0.8057 1.1084 1.1527 -0.0442 0.0533  0.1201  126 GLU B CD  
5159  O OE1 . GLU B 126 ? 0.7733 1.0622 1.1319 -0.0404 0.0475  0.1047  126 GLU B OE1 
5160  O OE2 . GLU B 126 ? 0.8517 1.1654 1.2169 -0.0538 0.0573  0.1408  126 GLU B OE2 
5161  N N   . LEU B 127 ? 0.5769 0.8363 0.8294 -0.0059 0.0389  0.0595  127 LEU B N   
5162  C CA  . LEU B 127 ? 0.5462 0.7852 0.7855 0.0018  0.0315  0.0487  127 LEU B CA  
5163  C C   . LEU B 127 ? 0.5095 0.7479 0.7247 0.0058  0.0339  0.0449  127 LEU B C   
5164  O O   . LEU B 127 ? 0.6376 0.8582 0.8392 0.0083  0.0286  0.0433  127 LEU B O   
5165  C CB  . LEU B 127 ? 0.5061 0.7456 0.7552 0.0086  0.0279  0.0363  127 LEU B CB  
5166  C CG  . LEU B 127 ? 0.4294 0.6617 0.6954 0.0066  0.0206  0.0344  127 LEU B CG  
5167  C CD1 . LEU B 127 ? 0.4198 0.6603 0.6957 0.0128  0.0175  0.0247  127 LEU B CD1 
5168  C CD2 . LEU B 127 ? 0.5016 0.7136 0.7571 0.0072  0.0131  0.0332  127 LEU B CD2 
5169  N N   . LEU B 128 ? 0.4617 0.7216 0.6726 0.0061  0.0423  0.0419  128 LEU B N   
5170  C CA  . LEU B 128 ? 0.5026 0.7660 0.6929 0.0088  0.0454  0.0356  128 LEU B CA  
5171  C C   . LEU B 128 ? 0.6400 0.9006 0.8161 0.0024  0.0443  0.0488  128 LEU B C   
5172  O O   . LEU B 128 ? 0.6405 0.8910 0.7996 0.0050  0.0416  0.0442  128 LEU B O   
5173  C CB  . LEU B 128 ? 0.5532 0.8461 0.7442 0.0087  0.0558  0.0278  128 LEU B CB  
5174  C CG  . LEU B 128 ? 0.5760 0.8737 0.7555 0.0150  0.0594  0.0102  128 LEU B CG  
5175  C CD1 . LEU B 128 ? 0.5524 0.8242 0.7365 0.0249  0.0520  -0.0011 128 LEU B CD1 
5176  C CD2 . LEU B 128 ? 0.5170 0.8461 0.7047 0.0152  0.0701  -0.0009 128 LEU B CD2 
5177  N N   . ASP B 129 ? 0.6023 0.8713 0.7881 -0.0061 0.0456  0.0662  129 ASP B N   
5178  C CA  . ASP B 129 ? 0.6453 0.9126 0.8223 -0.0121 0.0436  0.0820  129 ASP B CA  
5179  C C   . ASP B 129 ? 0.6175 0.8541 0.7949 -0.0095 0.0341  0.0817  129 ASP B C   
5180  O O   . ASP B 129 ? 0.7105 0.9405 0.8736 -0.0100 0.0312  0.0859  129 ASP B O   
5181  C CB  . ASP B 129 ? 0.6091 0.8938 0.8024 -0.0220 0.0473  0.1033  129 ASP B CB  
5182  C CG  . ASP B 129 ? 0.6805 1.0025 0.8649 -0.0270 0.0571  0.1082  129 ASP B CG  
5183  O OD1 . ASP B 129 ? 0.6393 0.9735 0.8075 -0.0223 0.0616  0.0910  129 ASP B OD1 
5184  O OD2 . ASP B 129 ? 0.8047 1.1455 1.0001 -0.0361 0.0606  0.1290  129 ASP B OD2 
5185  N N   . LEU B 130 ? 0.5075 0.7278 0.7008 -0.0069 0.0293  0.0756  130 LEU B N   
5186  C CA  . LEU B 130 ? 0.5544 0.7497 0.7473 -0.0044 0.0210  0.0720  130 LEU B CA  
5187  C C   . LEU B 130 ? 0.6353 0.8204 0.8062 0.0027  0.0184  0.0597  130 LEU B C   
5188  O O   . LEU B 130 ? 0.6821 0.8540 0.8427 0.0030  0.0142  0.0612  130 LEU B O   
5189  C CB  . LEU B 130 ? 0.6330 0.8200 0.8466 -0.0038 0.0168  0.0654  130 LEU B CB  
5190  C CG  . LEU B 130 ? 0.6065 0.7755 0.8311 -0.0060 0.0100  0.0658  130 LEU B CG  
5191  C CD1 . LEU B 130 ? 0.5556 0.7239 0.7914 -0.0129 0.0109  0.0827  130 LEU B CD1 
5192  C CD2 . LEU B 130 ? 0.6116 0.7805 0.8584 -0.0069 0.0071  0.0573  130 LEU B CD2 
5193  N N   . GLN B 131 ? 0.6157 0.8071 0.7823 0.0086  0.0211  0.0476  131 GLN B N   
5194  C CA  . GLN B 131 ? 0.6134 0.7946 0.7647 0.0153  0.0190  0.0363  131 GLN B CA  
5195  C C   . GLN B 131 ? 0.5658 0.7524 0.6989 0.0133  0.0219  0.0380  131 GLN B C   
5196  O O   . GLN B 131 ? 0.6438 0.8158 0.7655 0.0145  0.0174  0.0366  131 GLN B O   
5197  C CB  . GLN B 131 ? 0.6549 0.8438 0.8122 0.0218  0.0220  0.0242  131 GLN B CB  
5198  C CG  . GLN B 131 ? 0.6164 0.8011 0.7902 0.0250  0.0174  0.0217  131 GLN B CG  
5199  C CD  . GLN B 131 ? 0.5508 0.7464 0.7348 0.0314  0.0209  0.0122  131 GLN B CD  
5200  O OE1 . GLN B 131 ? 0.5298 0.7434 0.7155 0.0307  0.0290  0.0087  131 GLN B OE1 
5201  N NE2 . GLN B 131 ? 0.5426 0.7299 0.7346 0.0377  0.0147  0.0080  131 GLN B NE2 
5202  N N   . THR B 132 ? 0.5566 0.7674 0.6867 0.0094  0.0294  0.0408  132 THR B N   
5203  C CA  . THR B 132 ? 0.5865 0.8095 0.6982 0.0070  0.0324  0.0403  132 THR B CA  
5204  C C   . THR B 132 ? 0.5923 0.8092 0.6979 0.0014  0.0277  0.0563  132 THR B C   
5205  O O   . THR B 132 ? 0.6851 0.9004 0.7752 0.0014  0.0259  0.0542  132 THR B O   
5206  C CB  . THR B 132 ? 0.5988 0.8558 0.7088 0.0028  0.0420  0.0400  132 THR B CB  
5207  O OG1 . THR B 132 ? 0.6025 0.8648 0.7233 0.0084  0.0464  0.0248  132 THR B OG1 
5208  C CG2 . THR B 132 ? 0.5996 0.8737 0.6897 0.0006  0.0452  0.0342  132 THR B CG2 
5209  N N   . LEU B 133 ? 0.5753 0.7892 0.6961 -0.0033 0.0256  0.0719  133 LEU B N   
5210  C CA  . LEU B 133 ? 0.5945 0.8033 0.7155 -0.0081 0.0211  0.0881  133 LEU B CA  
5211  C C   . LEU B 133 ? 0.5861 0.7664 0.7064 -0.0040 0.0133  0.0821  133 LEU B C   
5212  O O   . LEU B 133 ? 0.6512 0.8268 0.7641 -0.0056 0.0097  0.0886  133 LEU B O   
5213  C CB  . LEU B 133 ? 0.6671 0.8821 0.8107 -0.0148 0.0218  0.1071  133 LEU B CB  
5214  C CG  . LEU B 133 ? 0.6578 0.9060 0.8004 -0.0217 0.0290  0.1212  133 LEU B CG  
5215  C CD1 . LEU B 133 ? 0.7299 0.9809 0.8988 -0.0289 0.0284  0.1438  133 LEU B CD1 
5216  C CD2 . LEU B 133 ? 0.6635 0.9302 0.7834 -0.0242 0.0298  0.1263  133 LEU B CD2 
5217  N N   . ASN B 134 ? 0.6334 0.7974 0.7615 0.0008  0.0106  0.0704  134 ASN B N   
5218  C CA  . ASN B 134 ? 0.6050 0.7471 0.7286 0.0047  0.0042  0.0625  134 ASN B CA  
5219  C C   . ASN B 134 ? 0.5801 0.7207 0.6823 0.0078  0.0042  0.0546  134 ASN B C   
5220  O O   . ASN B 134 ? 0.6797 0.8084 0.7749 0.0079  -0.0002 0.0550  134 ASN B O   
5221  C CB  . ASN B 134 ? 0.6180 0.7506 0.7505 0.0090  0.0017  0.0516  134 ASN B CB  
5222  C CG  . ASN B 134 ? 0.6505 0.7766 0.8036 0.0057  -0.0019 0.0548  134 ASN B CG  
5223  O OD1 . ASN B 134 ? 0.6346 0.7478 0.7897 0.0055  -0.0069 0.0525  134 ASN B OD1 
5224  N ND2 . ASN B 134 ? 0.5939 0.7304 0.7643 0.0028  0.0011  0.0586  134 ASN B ND2 
5225  N N   . LEU B 135 ? 0.5585 0.7123 0.6527 0.0101  0.0096  0.0462  135 LEU B N   
5226  C CA  . LEU B 135 ? 0.6283 0.7829 0.7062 0.0124  0.0104  0.0362  135 LEU B CA  
5227  C C   . LEU B 135 ? 0.6296 0.7976 0.6956 0.0068  0.0109  0.0454  135 LEU B C   
5228  O O   . LEU B 135 ? 0.7192 0.8782 0.7752 0.0070  0.0070  0.0437  135 LEU B O   
5229  C CB  . LEU B 135 ? 0.5426 0.7107 0.6207 0.0159  0.0168  0.0226  135 LEU B CB  
5230  C CG  . LEU B 135 ? 0.5436 0.6958 0.6304 0.0234  0.0147  0.0108  135 LEU B CG  
5231  C CD1 . LEU B 135 ? 0.6375 0.8052 0.7282 0.0265  0.0217  -0.0028 135 LEU B CD1 
5232  C CD2 . LEU B 135 ? 0.7140 0.8458 0.7939 0.0261  0.0092  0.0062  135 LEU B CD2 
5233  N N   . LEU B 136 ? 0.5797 0.7714 0.6471 0.0013  0.0153  0.0567  136 LEU B N   
5234  C CA  . LEU B 136 ? 0.6330 0.8447 0.6880 -0.0045 0.0158  0.0669  136 LEU B CA  
5235  C C   . LEU B 136 ? 0.7035 0.9016 0.7634 -0.0069 0.0085  0.0828  136 LEU B C   
5236  O O   . LEU B 136 ? 0.7328 0.9410 0.7816 -0.0099 0.0063  0.0890  136 LEU B O   
5237  C CB  . LEU B 136 ? 0.6494 0.8940 0.7056 -0.0106 0.0224  0.0778  136 LEU B CB  
5238  C CG  . LEU B 136 ? 0.6437 0.9093 0.6942 -0.0090 0.0308  0.0600  136 LEU B CG  
5239  C CD1 . LEU B 136 ? 0.6648 0.9678 0.7152 -0.0165 0.0377  0.0724  136 LEU B CD1 
5240  C CD2 . LEU B 136 ? 0.7118 0.9826 0.7457 -0.0068 0.0317  0.0411  136 LEU B CD2 
5241  N N   . ALA B 137 ? 0.6670 0.8443 0.7454 -0.0058 0.0047  0.0881  137 ALA B N   
5242  C CA  . ALA B 137 ? 0.6555 0.8186 0.7433 -0.0073 -0.0019 0.0994  137 ALA B CA  
5243  C C   . ALA B 137 ? 0.6658 0.8147 0.7396 -0.0038 -0.0061 0.0883  137 ALA B C   
5244  O O   . ALA B 137 ? 0.7230 0.8724 0.7949 -0.0059 -0.0102 0.0973  137 ALA B O   
5245  C CB  . ALA B 137 ? 0.6087 0.7536 0.7210 -0.0066 -0.0044 0.1009  137 ALA B CB  
5246  N N   . TRP B 138 ? 0.7117 0.8488 0.7777 0.0014  -0.0054 0.0702  138 TRP B N   
5247  C CA  . TRP B 138 ? 0.6497 0.7733 0.7041 0.0044  -0.0088 0.0593  138 TRP B CA  
5248  C C   . TRP B 138 ? 0.6284 0.7678 0.6649 0.0040  -0.0056 0.0508  138 TRP B C   
5249  O O   . TRP B 138 ? 0.7043 0.8377 0.7351 0.0078  -0.0040 0.0351  138 TRP B O   
5250  C CB  . TRP B 138 ? 0.6164 0.7210 0.6748 0.0095  -0.0102 0.0467  138 TRP B CB  
5251  C CG  . TRP B 138 ? 0.6406 0.7332 0.7153 0.0093  -0.0136 0.0507  138 TRP B CG  
5252  C CD1 . TRP B 138 ? 0.6564 0.7515 0.7457 0.0090  -0.0121 0.0524  138 TRP B CD1 
5253  C CD2 . TRP B 138 ? 0.7340 0.8127 0.8140 0.0090  -0.0187 0.0508  138 TRP B CD2 
5254  N NE1 . TRP B 138 ? 0.7062 0.7905 0.8098 0.0082  -0.0161 0.0524  138 TRP B NE1 
5255  C CE2 . TRP B 138 ? 0.6308 0.7054 0.7291 0.0082  -0.0199 0.0510  138 TRP B CE2 
5256  C CE3 . TRP B 138 ? 0.6662 0.7375 0.7385 0.0089  -0.0222 0.0493  138 TRP B CE3 
5257  C CZ2 . TRP B 138 ? 0.6405 0.7053 0.7499 0.0074  -0.0239 0.0481  138 TRP B CZ2 
5258  C CZ3 . TRP B 138 ? 0.5819 0.6425 0.6648 0.0083  -0.0262 0.0482  138 TRP B CZ3 
5259  C CH2 . TRP B 138 ? 0.6987 0.7568 0.8000 0.0076  -0.0268 0.0468  138 TRP B CH2 
5260  N N   . CYS B 139 ? 0.6969 0.8588 0.7268 -0.0012 -0.0047 0.0616  139 CYS B N   
5261  C CA  . CYS B 139 ? 0.7171 0.9011 0.7300 -0.0031 -0.0014 0.0524  139 CYS B CA  
5262  C C   . CYS B 139 ? 0.7440 0.9298 0.7479 -0.0055 -0.0068 0.0568  139 CYS B C   
5263  O O   . CYS B 139 ? 0.6733 0.8604 0.6835 -0.0085 -0.0114 0.0756  139 CYS B O   
5264  C CB  . CYS B 139 ? 0.6418 0.8599 0.6513 -0.0082 0.0044  0.0604  139 CYS B CB  
5265  S SG  . CYS B 139 ? 0.6502 0.9006 0.6417 -0.0102 0.0113  0.0399  139 CYS B SG  
5266  N N   . GLY B 140 ? 0.7556 0.9413 0.7481 -0.0043 -0.0064 0.0391  140 GLY B N   
5267  C CA  . GLY B 140 ? 0.7168 0.9062 0.7005 -0.0068 -0.0113 0.0406  140 GLY B CA  
5268  C C   . GLY B 140 ? 0.6982 0.9264 0.6685 -0.0132 -0.0101 0.0456  140 GLY B C   
5269  O O   . GLY B 140 ? 0.7095 0.9637 0.6753 -0.0159 -0.0041 0.0438  140 GLY B O   
5270  N N   . ARG B 141 ? 0.6647 0.8991 0.6288 -0.0160 -0.0159 0.0516  141 ARG B N   
5271  C CA  . ARG B 141 ? 0.6125 0.8875 0.5639 -0.0229 -0.0168 0.0609  141 ARG B CA  
5272  C C   . ARG B 141 ? 0.6429 0.9479 0.5797 -0.0258 -0.0098 0.0386  141 ARG B C   
5273  O O   . ARG B 141 ? 0.6525 0.9980 0.5798 -0.0320 -0.0068 0.0456  141 ARG B O   
5274  C CB  . ARG B 141 ? 0.6012 0.8751 0.5501 -0.0244 -0.0249 0.0672  141 ARG B CB  
5275  C CG  . ARG B 141 ? 0.6776 0.9957 0.6103 -0.0315 -0.0267 0.0706  141 ARG B CG  
5276  C CD  . ARG B 141 ? 0.7431 1.0573 0.6765 -0.0322 -0.0355 0.0775  141 ARG B CD  
5277  N NE  . ARG B 141 ? 0.6401 0.9566 0.5625 -0.0327 -0.0349 0.0506  141 ARG B NE  
5278  C CZ  . ARG B 141 ? 0.5469 0.9014 0.4545 -0.0389 -0.0362 0.0439  141 ARG B CZ  
5279  N NH1 . ARG B 141 ? 0.6164 1.0126 0.5162 -0.0452 -0.0393 0.0650  141 ARG B NH1 
5280  N NH2 . ARG B 141 ? 0.5915 0.9443 0.4935 -0.0392 -0.0345 0.0155  141 ARG B NH2 
5281  N N   . THR B 142 ? 0.6454 0.9331 0.5828 -0.0219 -0.0069 0.0115  142 THR B N   
5282  C CA  . THR B 142 ? 0.6719 0.9865 0.6016 -0.0242 0.0003  -0.0142 142 THR B CA  
5283  C C   . THR B 142 ? 0.6686 1.0009 0.6007 -0.0245 0.0084  -0.0154 142 THR B C   
5284  O O   . THR B 142 ? 0.6452 1.0212 0.5663 -0.0307 0.0132  -0.0194 142 THR B O   
5285  C CB  . THR B 142 ? 0.6733 0.9601 0.6116 -0.0190 0.0017  -0.0411 142 THR B CB  
5286  O OG1 . THR B 142 ? 0.8009 1.0778 0.7359 -0.0202 -0.0050 -0.0419 142 THR B OG1 
5287  C CG2 . THR B 142 ? 0.5870 0.8991 0.5250 -0.0206 0.0102  -0.0706 142 THR B CG2 
5288  N N   . LEU B 143 ? 0.6480 0.9497 0.5945 -0.0182 0.0100  -0.0130 143 LEU B N   
5289  C CA  . LEU B 143 ? 0.6257 0.9407 0.5778 -0.0175 0.0180  -0.0174 143 LEU B CA  
5290  C C   . LEU B 143 ? 0.6598 0.9991 0.6088 -0.0230 0.0185  0.0093  143 LEU B C   
5291  O O   . LEU B 143 ? 0.6997 1.0637 0.6492 -0.0250 0.0260  0.0061  143 LEU B O   
5292  C CB  . LEU B 143 ? 0.6648 0.9403 0.6345 -0.0091 0.0186  -0.0234 143 LEU B CB  
5293  C CG  . LEU B 143 ? 0.6580 0.9167 0.6366 -0.0037 0.0210  -0.0513 143 LEU B CG  
5294  C CD1 . LEU B 143 ? 0.6335 0.8715 0.6304 0.0034  0.0243  -0.0571 143 LEU B CD1 
5295  C CD2 . LEU B 143 ? 0.5362 0.8303 0.5080 -0.0080 0.0272  -0.0753 143 LEU B CD2 
5296  N N   . ARG B 144 ? 0.6631 0.9963 0.6123 -0.0253 0.0110  0.0359  144 ARG B N   
5297  C CA  . ARG B 144 ? 0.7260 1.0852 0.6759 -0.0315 0.0110  0.0641  144 ARG B CA  
5298  C C   . ARG B 144 ? 0.7479 1.1625 0.6804 -0.0400 0.0158  0.0629  144 ARG B C   
5299  O O   . ARG B 144 ? 0.7269 1.1706 0.6596 -0.0454 0.0198  0.0796  144 ARG B O   
5300  C CB  . ARG B 144 ? 0.6042 0.9491 0.5614 -0.0326 0.0014  0.0912  144 ARG B CB  
5301  C CG  . ARG B 144 ? 0.6314 0.9293 0.6079 -0.0258 -0.0022 0.0945  144 ARG B CG  
5302  C CD  . ARG B 144 ? 0.5506 0.8401 0.5438 -0.0277 -0.0089 0.1239  144 ARG B CD  
5303  N NE  . ARG B 144 ? 0.6549 0.9014 0.6637 -0.0214 -0.0129 0.1192  144 ARG B NE  
5304  C CZ  . ARG B 144 ? 0.7294 0.9586 0.7607 -0.0210 -0.0171 0.1367  144 ARG B CZ  
5305  N NH1 . ARG B 144 ? 0.7655 1.0126 0.8096 -0.0261 -0.0185 0.1632  144 ARG B NH1 
5306  N NH2 . ARG B 144 ? 0.7495 0.9444 0.7930 -0.0157 -0.0197 0.1272  144 ARG B NH2 
5307  N N   . LYS B 145 ? 0.7287 1.1610 0.6466 -0.0419 0.0156  0.0430  145 LYS B N   
5308  C CA  . LYS B 145 ? 0.7108 1.2005 0.6111 -0.0503 0.0210  0.0346  145 LYS B CA  
5309  C C   . LYS B 145 ? 0.8107 1.3150 0.7128 -0.0491 0.0326  0.0059  145 LYS B C   
5310  O O   . LYS B 145 ? 0.7630 1.3157 0.6558 -0.0563 0.0394  0.0066  145 LYS B O   
5311  C CB  . LYS B 145 ? 0.7423 1.2460 0.6292 -0.0530 0.0166  0.0201  145 LYS B CB  
5312  C CG  . LYS B 145 ? 0.6954 1.1782 0.5842 -0.0524 0.0049  0.0441  145 LYS B CG  
5313  C CD  . LYS B 145 ? 0.6740 1.1545 0.5552 -0.0523 0.0008  0.0229  145 LYS B CD  
5314  C CE  . LYS B 145 ? 0.7483 1.2218 0.6299 -0.0534 -0.0105 0.0483  145 LYS B CE  
5315  N NZ  . LYS B 145 ? 0.9049 1.4275 0.7767 -0.0621 -0.0143 0.0781  145 LYS B NZ  
5316  N N   . ASP B 146 ? 0.8018 1.2667 0.7175 -0.0403 0.0348  -0.0185 146 ASP B N   
5317  C CA  . ASP B 146 ? 0.7682 1.2437 0.6917 -0.0378 0.0453  -0.0466 146 ASP B CA  
5318  C C   . ASP B 146 ? 0.7263 1.2029 0.6594 -0.0370 0.0501  -0.0313 146 ASP B C   
5319  O O   . ASP B 146 ? 0.9056 1.4180 0.8379 -0.0403 0.0596  -0.0434 146 ASP B O   
5320  C CB  . ASP B 146 ? 0.8158 1.2480 0.7555 -0.0283 0.0451  -0.0730 146 ASP B CB  
5321  C CG  . ASP B 146 ? 0.9710 1.4254 0.9172 -0.0278 0.0546  -0.1117 146 ASP B CG  
5322  O OD1 . ASP B 146 ? 1.0377 1.5295 0.9829 -0.0313 0.0635  -0.1193 146 ASP B OD1 
5323  O OD2 . ASP B 146 ? 0.9210 1.3559 0.8762 -0.0240 0.0535  -0.1352 146 ASP B OD2 
5324  N N   . LEU B 147 ? 0.6611 1.1007 0.6049 -0.0331 0.0440  -0.0068 147 LEU B N   
5325  C CA  . LEU B 147 ? 0.6810 1.1157 0.6378 -0.0320 0.0477  0.0068  147 LEU B CA  
5326  C C   . LEU B 147 ? 0.7700 1.2280 0.7231 -0.0401 0.0455  0.0423  147 LEU B C   
5327  O O   . LEU B 147 ? 0.6835 1.1190 0.6515 -0.0386 0.0428  0.0630  147 LEU B O   
5328  C CB  . LEU B 147 ? 0.6661 1.0468 0.6411 -0.0226 0.0429  0.0077  147 LEU B CB  
5329  C CG  . LEU B 147 ? 0.7671 1.1182 0.7481 -0.0146 0.0420  -0.0195 147 LEU B CG  
5330  C CD1 . LEU B 147 ? 0.7015 1.0041 0.6932 -0.0082 0.0337  -0.0094 147 LEU B CD1 
5331  C CD2 . LEU B 147 ? 0.6653 1.0242 0.6584 -0.0103 0.0510  -0.0446 147 LEU B CD2 
5332  N N   . LYS B 148 ? 0.7729 1.2783 0.7084 -0.0493 0.0465  0.0500  148 LYS B N   
5333  C CA  . LYS B 148 ? 0.7622 1.2910 0.6964 -0.0575 0.0429  0.0883  148 LYS B CA  
5334  C C   . LYS B 148 ? 0.7746 1.3190 0.7200 -0.0608 0.0499  0.1023  148 LYS B C   
5335  O O   . LYS B 148 ? 0.8112 1.3360 0.7735 -0.0612 0.0459  0.1300  148 LYS B O   
5336  C CB  . LYS B 148 ? 0.8174 1.4001 0.7291 -0.0672 0.0423  0.0936  148 LYS B CB  
5337  C CG  . LYS B 148 ? 0.8269 1.4268 0.7395 -0.0745 0.0348  0.1371  148 LYS B CG  
5338  C CD  . LYS B 148 ? 0.7599 1.3996 0.6515 -0.0814 0.0299  0.1410  148 LYS B CD  
5339  C CE  . LYS B 148 ? 0.8543 1.5379 0.7244 -0.0852 0.0384  0.1047  148 LYS B CE  
5340  N NZ  . LYS B 148 ? 0.8533 1.5840 0.7186 -0.0919 0.0500  0.1016  148 LYS B NZ  
5341  N N   . ASP B 149 ? 0.7349 1.3155 0.6737 -0.0636 0.0608  0.0821  149 ASP B N   
5342  C CA  . ASP B 149 ? 0.8046 1.4053 0.7537 -0.0678 0.0681  0.0959  149 ASP B CA  
5343  C C   . ASP B 149 ? 0.8256 1.3752 0.7995 -0.0592 0.0667  0.0966  149 ASP B C   
5344  O O   . ASP B 149 ? 0.8783 1.4235 0.8675 -0.0624 0.0658  0.1236  149 ASP B O   
5345  C CB  . ASP B 149 ? 0.8279 1.4766 0.7673 -0.0715 0.0808  0.0691  149 ASP B CB  
5346  C CG  . ASP B 149 ? 1.0946 1.7474 1.0508 -0.0713 0.0892  0.0711  149 ASP B CG  
5347  O OD1 . ASP B 149 ? 1.1097 1.7920 1.0678 -0.0803 0.0914  0.1011  149 ASP B OD1 
5348  O OD2 . ASP B 149 ? 0.9939 1.6213 0.9632 -0.0623 0.0933  0.0439  149 ASP B OD2 
5349  N N   . LEU B 150 ? 0.7580 1.2705 0.7380 -0.0488 0.0663  0.0677  150 LEU B N   
5350  C CA  . LEU B 150 ? 0.6604 1.1271 0.6624 -0.0409 0.0637  0.0685  150 LEU B CA  
5351  C C   . LEU B 150 ? 0.7018 1.1392 0.7146 -0.0417 0.0539  0.0981  150 LEU B C   
5352  O O   . LEU B 150 ? 0.6587 1.0816 0.6908 -0.0418 0.0535  0.1128  150 LEU B O   
5353  C CB  . LEU B 150 ? 0.6148 1.0466 0.6208 -0.0301 0.0624  0.0378  150 LEU B CB  
5354  C CG  . LEU B 150 ? 0.6632 1.1142 0.6708 -0.0268 0.0721  0.0055  150 LEU B CG  
5355  C CD1 . LEU B 150 ? 0.6898 1.1140 0.6980 -0.0187 0.0693  -0.0211 150 LEU B CD1 
5356  C CD2 . LEU B 150 ? 0.6773 1.1216 0.7050 -0.0229 0.0770  0.0031  150 LEU B CD2 
5357  N N   . LEU B 151 ? 0.7839 1.2144 0.7867 -0.0427 0.0462  0.1064  151 LEU B N   
5358  C CA  . LEU B 151 ? 0.7878 1.1927 0.8041 -0.0434 0.0371  0.1331  151 LEU B CA  
5359  C C   . LEU B 151 ? 0.7931 1.2256 0.8194 -0.0528 0.0380  0.1671  151 LEU B C   
5360  O O   . LEU B 151 ? 0.7812 1.1907 0.8312 -0.0529 0.0338  0.1869  151 LEU B O   
5361  C CB  . LEU B 151 ? 0.6551 1.0514 0.6591 -0.0425 0.0292  0.1334  151 LEU B CB  
5362  C CG  . LEU B 151 ? 0.8405 1.1964 0.8433 -0.0332 0.0253  0.1086  151 LEU B CG  
5363  C CD1 . LEU B 151 ? 0.8351 1.1951 0.8216 -0.0339 0.0199  0.1043  151 LEU B CD1 
5364  C CD2 . LEU B 151 ? 0.7998 1.1118 0.8243 -0.0279 0.0196  0.1152  151 LEU B CD2 
5365  N N   . ASN B 152 ? 0.7440 1.2278 0.7544 -0.0612 0.0437  0.1741  152 ASN B N   
5366  C CA  . ASN B 152 ? 0.7868 1.3029 0.8064 -0.0714 0.0448  0.2097  152 ASN B CA  
5367  C C   . ASN B 152 ? 0.7762 1.2991 0.8121 -0.0735 0.0530  0.2123  152 ASN B C   
5368  O O   . ASN B 152 ? 0.7769 1.3097 0.8316 -0.0804 0.0526  0.2440  152 ASN B O   
5369  C CB  . ASN B 152 ? 0.7954 1.3708 0.7897 -0.0809 0.0476  0.2178  152 ASN B CB  
5370  C CG  . ASN B 152 ? 0.8965 1.4711 0.8769 -0.0805 0.0384  0.2213  152 ASN B CG  
5371  O OD1 . ASN B 152 ? 0.9427 1.4814 0.9384 -0.0768 0.0290  0.2362  152 ASN B OD1 
5372  N ND2 . ASN B 152 ? 0.7902 1.4070 0.7431 -0.0848 0.0415  0.2061  152 ASN B ND2 
5373  N N   . LYS B 153 ? 0.7077 1.2263 0.7400 -0.0678 0.0603  0.1807  153 LYS B N   
5374  C CA  . LYS B 153 ? 0.6626 1.1854 0.7125 -0.0690 0.0676  0.1816  153 LYS B CA  
5375  C C   . LYS B 153 ? 0.7596 1.2414 0.8401 -0.0668 0.0615  0.1992  153 LYS B C   
5376  O O   . LYS B 153 ? 0.7709 1.2653 0.8709 -0.0739 0.0637  0.2238  153 LYS B O   
5377  C CB  . LYS B 153 ? 0.7410 1.2580 0.7864 -0.0609 0.0745  0.1432  153 LYS B CB  
5378  C CG  . LYS B 153 ? 0.8471 1.3825 0.9064 -0.0630 0.0841  0.1401  153 LYS B CG  
5379  C CD  . LYS B 153 ? 0.8742 1.4272 0.9243 -0.0580 0.0931  0.1034  153 LYS B CD  
5380  C CE  . LYS B 153 ? 0.7844 1.2962 0.8528 -0.0465 0.0919  0.0819  153 LYS B CE  
5381  N NZ  . LYS B 153 ? 0.5549 1.0881 0.6270 -0.0428 0.1022  0.0534  153 LYS B NZ  
5382  N N   . GLY B 154 ? 0.7382 1.1728 0.8249 -0.0577 0.0540  0.1860  154 GLY B N   
5383  C CA  . GLY B 154 ? 0.6432 1.0400 0.7588 -0.0557 0.0477  0.1978  154 GLY B CA  
5384  C C   . GLY B 154 ? 0.7463 1.1275 0.8813 -0.0522 0.0513  0.1855  154 GLY B C   
5385  O O   . GLY B 154 ? 0.8603 1.2090 1.0186 -0.0497 0.0458  0.1884  154 GLY B O   
5386  N N   . ARG B 155 ? 0.6958 1.1007 0.8234 -0.0520 0.0602  0.1704  155 ARG B N   
5387  C CA  . ARG B 155 ? 0.7485 1.1452 0.8969 -0.0499 0.0639  0.1626  155 ARG B CA  
5388  C C   . ARG B 155 ? 0.7779 1.2013 0.9146 -0.0476 0.0735  0.1404  155 ARG B C   
5389  O O   . ARG B 155 ? 0.7389 1.1906 0.8532 -0.0491 0.0782  0.1319  155 ARG B O   
5390  C CB  . ARG B 155 ? 0.7785 1.1867 0.9531 -0.0594 0.0655  0.1912  155 ARG B CB  
5391  C CG  . ARG B 155 ? 0.6413 1.0957 0.8066 -0.0703 0.0713  0.2151  155 ARG B CG  
5392  C CD  . ARG B 155 ? 0.6633 1.1188 0.8577 -0.0794 0.0687  0.2508  155 ARG B CD  
5393  N NE  . ARG B 155 ? 0.7477 1.1804 0.9750 -0.0786 0.0687  0.2489  155 ARG B NE  
5394  C CZ  . ARG B 155 ? 0.7905 1.1889 1.0471 -0.0780 0.0611  0.2578  155 ARG B CZ  
5395  N NH1 . ARG B 155 ? 0.7219 1.1027 0.9810 -0.0775 0.0530  0.2702  155 ARG B NH1 
5396  N NH2 . ARG B 155 ? 0.8667 1.2500 1.1529 -0.0781 0.0619  0.2529  155 ARG B NH2 
5397  N N   . ASN B 156 ? 0.6214 1.0376 0.7763 -0.0443 0.0764  0.1300  156 ASN B N   
5398  C CA  . ASN B 156 ? 0.6272 1.0684 0.7798 -0.0419 0.0859  0.1098  156 ASN B CA  
5399  C C   . ASN B 156 ? 0.6883 1.1277 0.8215 -0.0337 0.0869  0.0819  156 ASN B C   
5400  O O   . ASN B 156 ? 0.6946 1.1687 0.8153 -0.0356 0.0954  0.0695  156 ASN B O   
5401  C CB  . ASN B 156 ? 0.6471 1.1375 0.7977 -0.0529 0.0960  0.1247  156 ASN B CB  
5402  C CG  . ASN B 156 ? 0.7105 1.2032 0.8796 -0.0629 0.0939  0.1589  156 ASN B CG  
5403  O OD1 . ASN B 156 ? 0.8057 1.3207 0.9668 -0.0716 0.0939  0.1827  156 ASN B OD1 
5404  N ND2 . ASN B 156 ? 0.6824 1.1527 0.8790 -0.0617 0.0916  0.1618  156 ASN B ND2 
5405  N N   . TYR B 157 ? 0.7128 1.1129 0.8457 -0.0249 0.0783  0.0711  157 TYR B N   
5406  C CA  . TYR B 157 ? 0.6846 1.0791 0.8050 -0.0169 0.0787  0.0453  157 TYR B CA  
5407  C C   . TYR B 157 ? 0.6674 1.0618 0.8031 -0.0091 0.0832  0.0235  157 TYR B C   
5408  O O   . TYR B 157 ? 0.7506 1.1394 0.9056 -0.0081 0.0830  0.0279  157 TYR B O   
5409  C CB  . TYR B 157 ? 0.6171 0.9721 0.7317 -0.0114 0.0680  0.0443  157 TYR B CB  
5410  C CG  . TYR B 157 ? 0.6655 1.0222 0.7659 -0.0180 0.0636  0.0629  157 TYR B CG  
5411  C CD1 . TYR B 157 ? 0.6492 1.0320 0.7289 -0.0218 0.0669  0.0593  157 TYR B CD1 
5412  C CD2 . TYR B 157 ? 0.6216 0.9561 0.7319 -0.0205 0.0560  0.0833  157 TYR B CD2 
5413  C CE1 . TYR B 157 ? 0.6826 1.0693 0.7505 -0.0277 0.0621  0.0780  157 TYR B CE1 
5414  C CE2 . TYR B 157 ? 0.7182 1.0543 0.8199 -0.0259 0.0516  0.1014  157 TYR B CE2 
5415  C CZ  . TYR B 157 ? 0.7639 1.1263 0.8437 -0.0294 0.0543  0.1000  157 TYR B CZ  
5416  O OH  . TYR B 157 ? 0.7583 1.1249 0.8304 -0.0347 0.0491  0.1194  157 TYR B OH  
5417  N N   . THR B 158 ? 0.6078 1.0102 0.7378 -0.0037 0.0873  -0.0005 158 THR B N   
5418  C CA  . THR B 158 ? 0.5053 0.9068 0.6533 0.0050  0.0911  -0.0227 158 THR B CA  
5419  C C   . THR B 158 ? 0.6249 0.9898 0.7767 0.0154  0.0832  -0.0357 158 THR B C   
5420  O O   . THR B 158 ? 0.6056 0.9512 0.7429 0.0152  0.0766  -0.0316 158 THR B O   
5421  C CB  . THR B 158 ? 0.5791 1.0221 0.7253 0.0032  0.1035  -0.0427 158 THR B CB  
5422  O OG1 . THR B 158 ? 0.6211 1.0596 0.7592 0.0076  0.1034  -0.0639 158 THR B OG1 
5423  C CG2 . THR B 158 ? 0.5552 1.0381 0.6857 -0.0097 0.1100  -0.0266 158 THR B CG2 
5424  N N   . GLN B 159 ? 0.6114 0.9684 0.7849 0.0244  0.0837  -0.0501 159 GLN B N   
5425  C CA  . GLN B 159 ? 0.5532 0.8782 0.7344 0.0341  0.0762  -0.0601 159 GLN B CA  
5426  C C   . GLN B 159 ? 0.5549 0.8830 0.7270 0.0355  0.0791  -0.0781 159 GLN B C   
5427  O O   . GLN B 159 ? 0.6341 0.9361 0.7987 0.0380  0.0718  -0.0769 159 GLN B O   
5428  C CB  . GLN B 159 ? 0.4871 0.8078 0.6970 0.0433  0.0762  -0.0698 159 GLN B CB  
5429  C CG  . GLN B 159 ? 0.4846 0.7756 0.7063 0.0533  0.0686  -0.0775 159 GLN B CG  
5430  C CD  . GLN B 159 ? 0.5159 0.7775 0.7336 0.0542  0.0564  -0.0591 159 GLN B CD  
5431  O OE1 . GLN B 159 ? 0.5165 0.7782 0.7236 0.0475  0.0538  -0.0431 159 GLN B OE1 
5432  N NE2 . GLN B 159 ? 0.5236 0.7619 0.7521 0.0622  0.0492  -0.0617 159 GLN B NE2 
5433  N N   . GLU B 160 ? 0.5107 0.8734 0.6833 0.0329  0.0901  -0.0955 160 GLU B N   
5434  C CA  . GLU B 160 ? 0.6429 1.0128 0.8091 0.0333  0.0936  -0.1165 160 GLU B CA  
5435  C C   . GLU B 160 ? 0.6635 1.0298 0.8004 0.0259  0.0888  -0.1037 160 GLU B C   
5436  O O   . GLU B 160 ? 0.5695 0.9192 0.7021 0.0284  0.0849  -0.1132 160 GLU B O   
5437  C CB  . GLU B 160 ? 0.5393 0.9544 0.7109 0.0303  0.1072  -0.1390 160 GLU B CB  
5438  C CG  . GLU B 160 ? 0.6847 1.1020 0.8907 0.0396  0.1122  -0.1583 160 GLU B CG  
5439  C CD  . GLU B 160 ? 0.8730 1.3099 1.0876 0.0373  0.1167  -0.1473 160 GLU B CD  
5440  O OE1 . GLU B 160 ? 0.8814 1.3067 1.0856 0.0331  0.1105  -0.1202 160 GLU B OE1 
5441  O OE2 . GLU B 160 ? 0.9895 1.4543 1.2238 0.0394  0.1268  -0.1672 160 GLU B OE2 
5442  N N   . GLU B 161 ? 0.6507 1.0325 0.7702 0.0166  0.0886  -0.0811 161 GLU B N   
5443  C CA  . GLU B 161 ? 0.5800 0.9592 0.6751 0.0098  0.0833  -0.0659 161 GLU B CA  
5444  C C   . GLU B 161 ? 0.5777 0.9112 0.6730 0.0150  0.0715  -0.0566 161 GLU B C   
5445  O O   . GLU B 161 ? 0.5448 0.8679 0.6276 0.0145  0.0673  -0.0595 161 GLU B O   
5446  C CB  . GLU B 161 ? 0.5237 0.9256 0.6080 -0.0003 0.0847  -0.0398 161 GLU B CB  
5447  C CG  . GLU B 161 ? 0.6387 1.0934 0.7166 -0.0081 0.0964  -0.0460 161 GLU B CG  
5448  C CD  . GLU B 161 ? 0.7173 1.1947 0.7913 -0.0180 0.0982  -0.0169 161 GLU B CD  
5449  O OE1 . GLU B 161 ? 0.7122 1.1629 0.7964 -0.0174 0.0917  0.0037  161 GLU B OE1 
5450  O OE2 . GLU B 161 ? 0.7227 1.2469 0.7851 -0.0270 0.1062  -0.0149 161 GLU B OE2 
5451  N N   . LYS B 162 ? 0.5616 0.8706 0.6713 0.0196  0.0663  -0.0462 162 LYS B N   
5452  C CA  . LYS B 162 ? 0.6362 0.9067 0.7465 0.0239  0.0556  -0.0380 162 LYS B CA  
5453  C C   . LYS B 162 ? 0.5775 0.8294 0.6942 0.0316  0.0534  -0.0563 162 LYS B C   
5454  O O   . LYS B 162 ? 0.5409 0.7704 0.6491 0.0323  0.0466  -0.0528 162 LYS B O   
5455  C CB  . LYS B 162 ? 0.6793 0.9347 0.8053 0.0268  0.0513  -0.0268 162 LYS B CB  
5456  C CG  . LYS B 162 ? 0.6502 0.8713 0.7782 0.0313  0.0409  -0.0211 162 LYS B CG  
5457  C CD  . LYS B 162 ? 0.6130 0.8261 0.7572 0.0336  0.0371  -0.0134 162 LYS B CD  
5458  C CE  . LYS B 162 ? 0.6470 0.8748 0.8104 0.0386  0.0426  -0.0243 162 LYS B CE  
5459  N NZ  . LYS B 162 ? 0.5823 0.8009 0.7633 0.0427  0.0371  -0.0195 162 LYS B NZ  
5460  N N   . GLU B 163 ? 0.6030 0.8641 0.7378 0.0373  0.0594  -0.0759 163 GLU B N   
5461  C CA  . GLU B 163 ? 0.6036 0.8475 0.7512 0.0444  0.0579  -0.0933 163 GLU B CA  
5462  C C   . GLU B 163 ? 0.5680 0.8245 0.7017 0.0401  0.0615  -0.1078 163 GLU B C   
5463  O O   . GLU B 163 ? 0.6511 0.8885 0.7908 0.0438  0.0582  -0.1179 163 GLU B O   
5464  C CB  . GLU B 163 ? 0.6044 0.8549 0.7819 0.0522  0.0632  -0.1100 163 GLU B CB  
5465  C CG  . GLU B 163 ? 0.6682 0.9049 0.8621 0.0575  0.0579  -0.0964 163 GLU B CG  
5466  C CD  . GLU B 163 ? 0.7622 1.0130 0.9861 0.0642  0.0641  -0.1110 163 GLU B CD  
5467  O OE1 . GLU B 163 ? 0.7577 1.0330 0.9884 0.0636  0.0741  -0.1321 163 GLU B OE1 
5468  O OE2 . GLU B 163 ? 0.7254 0.9653 0.9671 0.0698  0.0590  -0.1021 163 GLU B OE2 
5469  N N   . TYR B 164 ? 0.5169 0.8077 0.6331 0.0317  0.0680  -0.1084 164 TYR B N   
5470  C CA  . TYR B 164 ? 0.5331 0.8405 0.6322 0.0261  0.0702  -0.1196 164 TYR B CA  
5471  C C   . TYR B 164 ? 0.6211 0.9068 0.7009 0.0228  0.0606  -0.1007 164 TYR B C   
5472  O O   . TYR B 164 ? 0.5529 0.8281 0.6287 0.0231  0.0577  -0.1105 164 TYR B O   
5473  C CB  . TYR B 164 ? 0.5371 0.8931 0.6219 0.0171  0.0794  -0.1224 164 TYR B CB  
5474  C CG  . TYR B 164 ? 0.5715 0.9519 0.6344 0.0094  0.0805  -0.1295 164 TYR B CG  
5475  C CD1 . TYR B 164 ? 0.6229 1.0145 0.6927 0.0106  0.0853  -0.1608 164 TYR B CD1 
5476  C CD2 . TYR B 164 ? 0.5477 0.9410 0.5859 0.0008  0.0766  -0.1051 164 TYR B CD2 
5477  C CE1 . TYR B 164 ? 0.7212 1.1386 0.7709 0.0029  0.0859  -0.1688 164 TYR B CE1 
5478  C CE2 . TYR B 164 ? 0.6561 1.0751 0.6744 -0.0064 0.0767  -0.1101 164 TYR B CE2 
5479  C CZ  . TYR B 164 ? 0.7337 1.1658 0.7563 -0.0056 0.0813  -0.1426 164 TYR B CZ  
5480  O OH  . TYR B 164 ? 0.7369 1.1977 0.7397 -0.0133 0.0811  -0.1492 164 TYR B OH  
5481  N N   . VAL B 165 ? 0.6288 0.9074 0.6999 0.0197  0.0557  -0.0747 165 VAL B N   
5482  C CA  . VAL B 165 ? 0.5344 0.7921 0.5918 0.0172  0.0467  -0.0567 165 VAL B CA  
5483  C C   . VAL B 165 ? 0.5800 0.8002 0.6469 0.0242  0.0398  -0.0611 165 VAL B C   
5484  O O   . VAL B 165 ? 0.6048 0.8123 0.6622 0.0230  0.0348  -0.0606 165 VAL B O   
5485  C CB  . VAL B 165 ? 0.5365 0.7919 0.5921 0.0135  0.0435  -0.0309 165 VAL B CB  
5486  C CG1 . VAL B 165 ? 0.6475 0.8764 0.6965 0.0128  0.0340  -0.0153 165 VAL B CG1 
5487  C CG2 . VAL B 165 ? 0.6302 0.9239 0.6755 0.0050  0.0494  -0.0217 165 VAL B CG2 
5488  N N   . LEU B 166 ? 0.6081 0.8120 0.6947 0.0313  0.0390  -0.0638 166 LEU B N   
5489  C CA  . LEU B 166 ? 0.6871 0.8591 0.7841 0.0375  0.0322  -0.0647 166 LEU B CA  
5490  C C   . LEU B 166 ? 0.7010 0.8697 0.8057 0.0402  0.0344  -0.0853 166 LEU B C   
5491  O O   . LEU B 166 ? 0.7137 0.8600 0.8186 0.0416  0.0286  -0.0839 166 LEU B O   
5492  C CB  . LEU B 166 ? 0.6907 0.8518 0.8084 0.0442  0.0305  -0.0613 166 LEU B CB  
5493  C CG  . LEU B 166 ? 0.6977 0.8499 0.8114 0.0425  0.0246  -0.0411 166 LEU B CG  
5494  C CD1 . LEU B 166 ? 0.6530 0.8080 0.7862 0.0473  0.0252  -0.0399 166 LEU B CD1 
5495  C CD2 . LEU B 166 ? 0.6831 0.8100 0.7907 0.0428  0.0157  -0.0318 166 LEU B CD2 
5496  N N   . ASN B 167 ? 0.6233 0.8155 0.7368 0.0404  0.0430  -0.1056 167 ASN B N   
5497  C CA  . ASN B 167 ? 0.7195 0.9102 0.8450 0.0425  0.0458  -0.1288 167 ASN B CA  
5498  C C   . ASN B 167 ? 0.7528 0.9452 0.8569 0.0360  0.0430  -0.1293 167 ASN B C   
5499  O O   . ASN B 167 ? 0.7789 0.9518 0.8908 0.0378  0.0396  -0.1365 167 ASN B O   
5500  C CB  . ASN B 167 ? 0.7140 0.9358 0.8526 0.0427  0.0566  -0.1536 167 ASN B CB  
5501  C CG  . ASN B 167 ? 0.9940 1.2035 1.1669 0.0502  0.0590  -0.1765 167 ASN B CG  
5502  O OD1 . ASN B 167 ? 0.9964 1.1892 1.1952 0.0582  0.0573  -0.1733 167 ASN B OD1 
5503  N ND2 . ASN B 167 ? 0.9009 1.1190 1.0771 0.0476  0.0626  -0.1995 167 ASN B ND2 
5504  N N   . LYS B 168 ? 0.6702 0.8865 0.7490 0.0282  0.0441  -0.1198 168 LYS B N   
5505  C CA  . LYS B 168 ? 0.6896 0.9117 0.7484 0.0219  0.0409  -0.1189 168 LYS B CA  
5506  C C   . LYS B 168 ? 0.7226 0.9118 0.7756 0.0229  0.0311  -0.0996 168 LYS B C   
5507  O O   . LYS B 168 ? 0.6530 0.8338 0.7003 0.0210  0.0275  -0.1037 168 LYS B O   
5508  C CB  . LYS B 168 ? 0.6475 0.9071 0.6836 0.0133  0.0440  -0.1101 168 LYS B CB  
5509  C CG  . LYS B 168 ? 0.7262 1.0229 0.7663 0.0114  0.0543  -0.1249 168 LYS B CG  
5510  C CD  . LYS B 168 ? 0.7603 1.0786 0.8063 0.0101  0.0607  -0.1579 168 LYS B CD  
5511  C CE  . LYS B 168 ? 0.6475 0.9928 0.6692 0.0011  0.0593  -0.1586 168 LYS B CE  
5512  N NZ  . LYS B 168 ? 0.8803 1.2658 0.9045 -0.0030 0.0684  -0.1917 168 LYS B NZ  
5513  N N   . TYR B 169 ? 0.6582 0.8311 0.7131 0.0253  0.0269  -0.0798 169 TYR B N   
5514  C CA  . TYR B 169 ? 0.5736 0.7186 0.6245 0.0261  0.0183  -0.0639 169 TYR B CA  
5515  C C   . TYR B 169 ? 0.6711 0.7912 0.7361 0.0309  0.0154  -0.0732 169 TYR B C   
5516  O O   . TYR B 169 ? 0.7013 0.8060 0.7600 0.0294  0.0100  -0.0682 169 TYR B O   
5517  C CB  . TYR B 169 ? 0.6248 0.7604 0.6796 0.0278  0.0154  -0.0461 169 TYR B CB  
5518  C CG  . TYR B 169 ? 0.6001 0.7498 0.6421 0.0219  0.0147  -0.0293 169 TYR B CG  
5519  C CD1 . TYR B 169 ? 0.5106 0.6879 0.5395 0.0158  0.0184  -0.0295 169 TYR B CD1 
5520  C CD2 . TYR B 169 ? 0.6324 0.7701 0.6783 0.0220  0.0104  -0.0132 169 TYR B CD2 
5521  C CE1 . TYR B 169 ? 0.5615 0.7519 0.5829 0.0102  0.0172  -0.0103 169 TYR B CE1 
5522  C CE2 . TYR B 169 ? 0.6026 0.7515 0.6435 0.0166  0.0098  0.0026  169 TYR B CE2 
5523  C CZ  . TYR B 169 ? 0.5600 0.7341 0.5895 0.0109  0.0130  0.0057  169 TYR B CZ  
5524  O OH  . TYR B 169 ? 0.5240 0.7093 0.5526 0.0054  0.0119  0.0250  169 TYR B OH  
5525  N N   . PHE B 170 ? 0.6302 0.7468 0.7172 0.0367  0.0190  -0.0859 170 PHE B N   
5526  C CA  . PHE B 170 ? 0.6567 0.7509 0.7624 0.0410  0.0163  -0.0932 170 PHE B CA  
5527  C C   . PHE B 170 ? 0.6900 0.7910 0.7969 0.0380  0.0194  -0.1133 170 PHE B C   
5528  O O   . PHE B 170 ? 0.7769 0.8586 0.8927 0.0387  0.0158  -0.1154 170 PHE B O   
5529  C CB  . PHE B 170 ? 0.7403 0.8282 0.8746 0.0487  0.0184  -0.0983 170 PHE B CB  
5530  C CG  . PHE B 170 ? 0.7660 0.8392 0.9041 0.0523  0.0122  -0.0778 170 PHE B CG  
5531  C CD1 . PHE B 170 ? 0.7531 0.8042 0.8934 0.0532  0.0047  -0.0649 170 PHE B CD1 
5532  C CD2 . PHE B 170 ? 0.8128 0.8976 0.9526 0.0540  0.0140  -0.0719 170 PHE B CD2 
5533  C CE1 . PHE B 170 ? 0.7561 0.7995 0.8989 0.0556  -0.0010 -0.0474 170 PHE B CE1 
5534  C CE2 . PHE B 170 ? 0.7353 0.8101 0.8791 0.0566  0.0081  -0.0550 170 PHE B CE2 
5535  C CZ  . PHE B 170 ? 0.7421 0.7974 0.8866 0.0574  0.0005  -0.0432 170 PHE B CZ  
5536  N N   . GLU B 171 ? 0.6767 0.8077 0.7752 0.0339  0.0261  -0.1283 171 GLU B N   
5537  C CA  . GLU B 171 ? 0.6885 0.8323 0.7843 0.0294  0.0287  -0.1485 171 GLU B CA  
5538  C C   . GLU B 171 ? 0.6667 0.8027 0.7419 0.0242  0.0219  -0.1362 171 GLU B C   
5539  O O   . GLU B 171 ? 0.7583 0.8889 0.8385 0.0222  0.0209  -0.1489 171 GLU B O   
5540  C CB  . GLU B 171 ? 0.6357 0.8208 0.7211 0.0244  0.0367  -0.1642 171 GLU B CB  
5541  C CG  . GLU B 171 ? 0.7224 0.9206 0.8347 0.0278  0.0454  -0.1936 171 GLU B CG  
5542  C CD  . GLU B 171 ? 0.9590 1.1298 1.1037 0.0330  0.0443  -0.2092 171 GLU B CD  
5543  O OE1 . GLU B 171 ? 0.9375 1.0982 1.0796 0.0297  0.0406  -0.2131 171 GLU B OE1 
5544  O OE2 . GLU B 171 ? 1.1688 1.3281 1.3445 0.0404  0.0470  -0.2164 171 GLU B OE2 
5545  N N   . ILE B 172 ? 0.5861 0.7217 0.6411 0.0219  0.0174  -0.1127 172 ILE B N   
5546  C CA  . ILE B 172 ? 0.6100 0.7368 0.6490 0.0179  0.0106  -0.0999 172 ILE B CA  
5547  C C   . ILE B 172 ? 0.6261 0.7193 0.6774 0.0215  0.0053  -0.0943 172 ILE B C   
5548  O O   . ILE B 172 ? 0.5846 0.6698 0.6336 0.0188  0.0020  -0.0971 172 ILE B O   
5549  C CB  . ILE B 172 ? 0.5989 0.7338 0.6203 0.0150  0.0076  -0.0769 172 ILE B CB  
5550  C CG1 . ILE B 172 ? 0.5601 0.7323 0.5687 0.0099  0.0126  -0.0794 172 ILE B CG1 
5551  C CG2 . ILE B 172 ? 0.5880 0.7111 0.5985 0.0121  0.0005  -0.0635 172 ILE B CG2 
5552  C CD1 . ILE B 172 ? 0.5222 0.7182 0.5231 0.0047  0.0148  -0.0975 172 ILE B CD1 
5553  N N   . ILE B 173 ? 0.6458 0.7218 0.7108 0.0271  0.0041  -0.0857 173 ILE B N   
5554  C CA  . ILE B 173 ? 0.6245 0.6733 0.6994 0.0297  -0.0014 -0.0761 173 ILE B CA  
5555  C C   . ILE B 173 ? 0.6184 0.6561 0.7140 0.0310  -0.0003 -0.0913 173 ILE B C   
5556  O O   . ILE B 173 ? 0.5930 0.6145 0.6913 0.0295  -0.0045 -0.0862 173 ILE B O   
5557  C CB  . ILE B 173 ? 0.6343 0.6738 0.7191 0.0350  -0.0031 -0.0633 173 ILE B CB  
5558  C CG1 . ILE B 173 ? 0.5165 0.5624 0.5835 0.0326  -0.0056 -0.0474 173 ILE B CG1 
5559  C CG2 . ILE B 173 ? 0.6390 0.6560 0.7391 0.0378  -0.0079 -0.0554 173 ILE B CG2 
5560  C CD1 . ILE B 173 ? 0.6028 0.6384 0.6768 0.0360  -0.0093 -0.0339 173 ILE B CD1 
5561  N N   . LYS B 174 ? 0.6346 0.6816 0.7481 0.0334  0.0059  -0.1108 174 LYS B N   
5562  C CA  . LYS B 174 ? 0.6597 0.6963 0.7994 0.0345  0.0076  -0.1279 174 LYS B CA  
5563  C C   . LYS B 174 ? 0.6627 0.7084 0.7921 0.0277  0.0080  -0.1418 174 LYS B C   
5564  O O   . LYS B 174 ? 0.7531 0.7870 0.9040 0.0273  0.0081  -0.1539 174 LYS B O   
5565  C CB  . LYS B 174 ? 0.7560 0.8020 0.9222 0.0391  0.0146  -0.1483 174 LYS B CB  
5566  C CG  . LYS B 174 ? 0.7452 0.7837 0.9254 0.0463  0.0140  -0.1355 174 LYS B CG  
5567  C CD  . LYS B 174 ? 0.8111 0.8505 1.0297 0.0523  0.0197  -0.1553 174 LYS B CD  
5568  C CE  . LYS B 174 ? 0.7861 0.8547 0.9998 0.0526  0.0276  -0.1707 174 LYS B CE  
5569  N NZ  . LYS B 174 ? 0.8554 0.9495 1.0599 0.0463  0.0341  -0.1969 174 LYS B NZ  
5570  N N   . LYS B 175 ? 0.6108 0.6781 0.7106 0.0223  0.0078  -0.1395 175 LYS B N   
5571  C CA  . LYS B 175 ? 0.7803 0.8600 0.8683 0.0155  0.0070  -0.1504 175 LYS B CA  
5572  C C   . LYS B 175 ? 0.7571 0.8272 0.8251 0.0122  -0.0003 -0.1297 175 LYS B C   
5573  O O   . LYS B 175 ? 0.6538 0.7350 0.7104 0.0066  -0.0021 -0.1353 175 LYS B O   
5574  C CB  . LYS B 175 ? 0.6875 0.8056 0.7589 0.0109  0.0119  -0.1641 175 LYS B CB  
5575  C CG  . LYS B 175 ? 0.7371 0.8713 0.8291 0.0129  0.0203  -0.1909 175 LYS B CG  
5576  C CD  . LYS B 175 ? 0.8662 1.0444 0.9417 0.0059  0.0254  -0.2096 175 LYS B CD  
5577  C CE  . LYS B 175 ? 0.8359 1.0371 0.8795 0.0024  0.0236  -0.1874 175 LYS B CE  
5578  N NZ  . LYS B 175 ? 0.8212 1.0698 0.8454 -0.0057 0.0270  -0.1999 175 LYS B NZ  
5579  N N   . THR B 176 ? 0.6404 0.6924 0.7053 0.0155  -0.0044 -0.1074 176 THR B N   
5580  C CA  . THR B 176 ? 0.6729 0.7187 0.7207 0.0125  -0.0104 -0.0897 176 THR B CA  
5581  C C   . THR B 176 ? 0.7265 0.7577 0.7818 0.0098  -0.0135 -0.0929 176 THR B C   
5582  O O   . THR B 176 ? 0.6933 0.7332 0.7363 0.0049  -0.0159 -0.0943 176 THR B O   
5583  C CB  . THR B 176 ? 0.6257 0.6584 0.6719 0.0162  -0.0133 -0.0695 176 THR B CB  
5584  O OG1 . THR B 176 ? 0.6860 0.7349 0.7224 0.0169  -0.0111 -0.0646 176 THR B OG1 
5585  C CG2 . THR B 176 ? 0.5659 0.5895 0.6016 0.0136  -0.0190 -0.0548 176 THR B CG2 
5586  N N   . LEU B 177 ? 0.6792 0.6893 0.7564 0.0128  -0.0136 -0.0928 177 LEU B N   
5587  C CA  . LEU B 177 ? 0.6343 0.6301 0.7210 0.0097  -0.0164 -0.0930 177 LEU B CA  
5588  C C   . LEU B 177 ? 0.6443 0.6512 0.7356 0.0049  -0.0141 -0.1153 177 LEU B C   
5589  O O   . LEU B 177 ? 0.7070 0.7108 0.7961 0.0003  -0.0170 -0.1156 177 LEU B O   
5590  C CB  . LEU B 177 ? 0.6050 0.5789 0.7183 0.0134  -0.0168 -0.0867 177 LEU B CB  
5591  C CG  . LEU B 177 ? 0.7003 0.6658 0.8075 0.0163  -0.0205 -0.0632 177 LEU B CG  
5592  C CD1 . LEU B 177 ? 0.6063 0.5541 0.7401 0.0191  -0.0220 -0.0534 177 LEU B CD1 
5593  C CD2 . LEU B 177 ? 0.6390 0.6070 0.7232 0.0122  -0.0247 -0.0504 177 LEU B CD2 
5594  N N   . SER B 178 ? 0.6980 0.7211 0.7960 0.0056  -0.0088 -0.1355 178 SER B N   
5595  C CA  . SER B 178 ? 0.7351 0.7736 0.8386 0.0004  -0.0063 -0.1604 178 SER B CA  
5596  C C   . SER B 178 ? 0.6533 0.7152 0.7275 -0.0056 -0.0095 -0.1583 178 SER B C   
5597  O O   . SER B 178 ? 0.6626 0.7312 0.7381 -0.0111 -0.0108 -0.1702 178 SER B O   
5598  C CB  . SER B 178 ? 0.6993 0.7545 0.8175 0.0021  0.0008  -0.1849 178 SER B CB  
5599  O OG  . SER B 178 ? 0.8452 0.8816 1.0019 0.0048  0.0036  -0.1991 178 SER B OG  
5600  N N   . ILE B 179 ? 0.6094 0.6844 0.6599 -0.0048 -0.0110 -0.1423 179 ILE B N   
5601  C CA  . ILE B 179 ? 0.6161 0.7139 0.6424 -0.0100 -0.0147 -0.1363 179 ILE B CA  
5602  C C   . ILE B 179 ? 0.6759 0.7578 0.6993 -0.0121 -0.0209 -0.1236 179 ILE B C   
5603  O O   . ILE B 179 ? 0.6686 0.7669 0.6812 -0.0172 -0.0243 -0.1252 179 ILE B O   
5604  C CB  . ILE B 179 ? 0.5973 0.7104 0.6052 -0.0085 -0.0149 -0.1195 179 ILE B CB  
5605  C CG1 . ILE B 179 ? 0.6965 0.8473 0.6851 -0.0145 -0.0159 -0.1217 179 ILE B CG1 
5606  C CG2 . ILE B 179 ? 0.6322 0.7260 0.6341 -0.0061 -0.0201 -0.0942 179 ILE B CG2 
5607  C CD1 . ILE B 179 ? 0.8068 0.9867 0.7978 -0.0180 -0.0101 -0.1485 179 ILE B CD1 
5608  N N   . TYR B 180 ? 0.6402 0.6934 0.6742 -0.0086 -0.0223 -0.1110 180 TYR B N   
5609  C CA  . TYR B 180 ? 0.6573 0.6975 0.6899 -0.0110 -0.0272 -0.1004 180 TYR B CA  
5610  C C   . TYR B 180 ? 0.6492 0.6838 0.6978 -0.0152 -0.0268 -0.1163 180 TYR B C   
5611  O O   . TYR B 180 ? 0.5662 0.6048 0.6098 -0.0197 -0.0304 -0.1155 180 TYR B O   
5612  C CB  . TYR B 180 ? 0.6387 0.6562 0.6759 -0.0070 -0.0285 -0.0821 180 TYR B CB  
5613  C CG  . TYR B 180 ? 0.6468 0.6694 0.6693 -0.0043 -0.0301 -0.0659 180 TYR B CG  
5614  C CD1 . TYR B 180 ? 0.5832 0.6122 0.5936 -0.0063 -0.0343 -0.0549 180 TYR B CD1 
5615  C CD2 . TYR B 180 ? 0.6020 0.6231 0.6265 0.0003  -0.0274 -0.0622 180 TYR B CD2 
5616  C CE1 . TYR B 180 ? 0.5274 0.5598 0.5302 -0.0040 -0.0356 -0.0411 180 TYR B CE1 
5617  C CE2 . TYR B 180 ? 0.6009 0.6265 0.6154 0.0022  -0.0287 -0.0484 180 TYR B CE2 
5618  C CZ  . TYR B 180 ? 0.6258 0.6564 0.6305 0.0000  -0.0327 -0.0381 180 TYR B CZ  
5619  O OH  . TYR B 180 ? 0.5834 0.6174 0.5837 0.0016  -0.0339 -0.0254 180 TYR B OH  
5620  N N   . ARG B 181 ? 0.6624 0.6880 0.7338 -0.0138 -0.0225 -0.1312 181 ARG B N   
5621  C CA  . ARG B 181 ? 0.7369 0.7599 0.8281 -0.0185 -0.0215 -0.1502 181 ARG B CA  
5622  C C   . ARG B 181 ? 0.7385 0.7923 0.8176 -0.0242 -0.0216 -0.1691 181 ARG B C   
5623  O O   . ARG B 181 ? 0.7967 0.8545 0.8785 -0.0299 -0.0240 -0.1765 181 ARG B O   
5624  C CB  . ARG B 181 ? 0.6359 0.6453 0.7593 -0.0156 -0.0164 -0.1645 181 ARG B CB  
5625  C CG  . ARG B 181 ? 0.7497 0.7297 0.8923 -0.0115 -0.0173 -0.1461 181 ARG B CG  
5626  C CD  . ARG B 181 ? 0.8182 0.7869 0.9974 -0.0080 -0.0127 -0.1605 181 ARG B CD  
5627  N NE  . ARG B 181 ? 0.8682 0.8193 1.0586 -0.0014 -0.0132 -0.1409 181 ARG B NE  
5628  C CZ  . ARG B 181 ? 0.8708 0.8235 1.0731 0.0047  -0.0097 -0.1466 181 ARG B CZ  
5629  N NH1 . ARG B 181 ? 0.8673 0.8392 1.0713 0.0048  -0.0046 -0.1721 181 ARG B NH1 
5630  N NH2 . ARG B 181 ? 0.8191 0.7569 1.0324 0.0104  -0.0113 -0.1268 181 ARG B NH2 
5631  N N   . GLU B 182 ? 0.6124 0.6913 0.6777 -0.0234 -0.0190 -0.1762 182 GLU B N   
5632  C CA  . GLU B 182 ? 0.7338 0.8485 0.7882 -0.0296 -0.0188 -0.1954 182 GLU B CA  
5633  C C   . GLU B 182 ? 0.7563 0.8852 0.7887 -0.0339 -0.0257 -0.1814 182 GLU B C   
5634  O O   . GLU B 182 ? 0.6903 0.8376 0.7226 -0.0402 -0.0277 -0.1961 182 GLU B O   
5635  C CB  . GLU B 182 ? 0.6322 0.7739 0.6755 -0.0283 -0.0143 -0.2027 182 GLU B CB  
5636  C CG  . GLU B 182 ? 0.7615 0.9486 0.7874 -0.0353 -0.0146 -0.2174 182 GLU B CG  
5637  C CD  . GLU B 182 ? 0.9635 1.1800 0.9783 -0.0347 -0.0094 -0.2227 182 GLU B CD  
5638  O OE1 . GLU B 182 ? 0.7307 0.9297 0.7544 -0.0283 -0.0053 -0.2176 182 GLU B OE1 
5639  O OE2 . GLU B 182 ? 0.8786 1.1383 0.8761 -0.0409 -0.0096 -0.2314 182 GLU B OE2 
5640  N N   . ILE B 183 ? 0.6813 0.8029 0.6980 -0.0306 -0.0297 -0.1542 183 ILE B N   
5641  C CA  . ILE B 183 ? 0.6310 0.7659 0.6322 -0.0340 -0.0364 -0.1409 183 ILE B CA  
5642  C C   . ILE B 183 ? 0.6851 0.8008 0.6981 -0.0364 -0.0394 -0.1412 183 ILE B C   
5643  O O   . ILE B 183 ? 0.6804 0.8114 0.6872 -0.0410 -0.0443 -0.1409 183 ILE B O   
5644  C CB  . ILE B 183 ? 0.6172 0.7499 0.6043 -0.0298 -0.0395 -0.1137 183 ILE B CB  
5645  C CG1 . ILE B 183 ? 0.6872 0.7849 0.6834 -0.0255 -0.0402 -0.0990 183 ILE B CG1 
5646  C CG2 . ILE B 183 ? 0.7018 0.8491 0.6811 -0.0274 -0.0356 -0.1123 183 ILE B CG2 
5647  C CD1 . ILE B 183 ? 0.6662 0.7621 0.6535 -0.0234 -0.0448 -0.0759 183 ILE B CD1 
5648  N N   . LYS B 184 ? 0.6933 0.7776 0.7245 -0.0338 -0.0368 -0.1403 184 LYS B N   
5649  C CA  . LYS B 184 ? 0.6828 0.7509 0.7271 -0.0372 -0.0388 -0.1406 184 LYS B CA  
5650  C C   . LYS B 184 ? 0.6734 0.7541 0.7310 -0.0437 -0.0377 -0.1665 184 LYS B C   
5651  O O   . LYS B 184 ? 0.7858 0.8760 0.8418 -0.0489 -0.0417 -0.1693 184 LYS B O   
5652  C CB  . LYS B 184 ? 0.6186 0.6543 0.6800 -0.0337 -0.0362 -0.1311 184 LYS B CB  
5653  C CG  . LYS B 184 ? 0.7038 0.7247 0.7736 -0.0370 -0.0387 -0.1224 184 LYS B CG  
5654  C CD  . LYS B 184 ? 0.7313 0.7262 0.8140 -0.0340 -0.0369 -0.1077 184 LYS B CD  
5655  C CE  . LYS B 184 ? 0.6408 0.6204 0.7495 -0.0387 -0.0357 -0.1127 184 LYS B CE  
5656  N NZ  . LYS B 184 ? 0.7896 0.7682 0.9209 -0.0396 -0.0320 -0.1350 184 LYS B NZ  
5657  N N   . GLU B 185 ? 0.7225 0.8050 0.7953 -0.0435 -0.0324 -0.1874 185 GLU B N   
5658  C CA  . GLU B 185 ? 0.7238 0.8190 0.8140 -0.0499 -0.0306 -0.2165 185 GLU B CA  
5659  C C   . GLU B 185 ? 0.6878 0.8246 0.7570 -0.0556 -0.0339 -0.2275 185 GLU B C   
5660  O O   . GLU B 185 ? 0.6131 0.7624 0.6881 -0.0623 -0.0364 -0.2412 185 GLU B O   
5661  C CB  . GLU B 185 ? 0.7407 0.8305 0.8552 -0.0478 -0.0235 -0.2381 185 GLU B CB  
5662  C CG  . GLU B 185 ? 0.8687 0.9209 1.0048 -0.0416 -0.0210 -0.2240 185 GLU B CG  
5663  C CD  . GLU B 185 ? 1.0138 1.0499 1.1921 -0.0428 -0.0163 -0.2456 185 GLU B CD  
5664  O OE1 . GLU B 185 ? 0.9368 0.9505 1.1359 -0.0369 -0.0133 -0.2393 185 GLU B OE1 
5665  O OE2 . GLU B 185 ? 1.0715 1.1179 1.2651 -0.0497 -0.0159 -0.2688 185 GLU B OE2 
5666  N N   . GLU B 186 ? 0.7888 0.9499 0.8346 -0.0534 -0.0341 -0.2207 186 GLU B N   
5667  C CA  . GLU B 186 ? 0.7618 0.9673 0.7863 -0.0589 -0.0379 -0.2263 186 GLU B CA  
5668  C C   . GLU B 186 ? 0.7833 0.9938 0.7920 -0.0600 -0.0462 -0.2026 186 GLU B C   
5669  O O   . GLU B 186 ? 0.7672 1.0153 0.7592 -0.0645 -0.0510 -0.2021 186 GLU B O   
5670  C CB  . GLU B 186 ? 0.6373 0.8690 0.6444 -0.0569 -0.0349 -0.2247 186 GLU B CB  
5671  C CG  . GLU B 186 ? 0.8950 1.1361 0.9181 -0.0578 -0.0265 -0.2562 186 GLU B CG  
5672  C CD  . GLU B 186 ? 0.9868 1.2617 0.9918 -0.0574 -0.0230 -0.2574 186 GLU B CD  
5673  O OE1 . GLU B 186 ? 0.9094 1.1973 0.8905 -0.0561 -0.0272 -0.2307 186 GLU B OE1 
5674  O OE2 . GLU B 186 ? 1.0085 1.2984 1.0257 -0.0586 -0.0157 -0.2856 186 GLU B OE2 
5675  N N   . GLY B 187 ? 0.6316 0.8080 0.6467 -0.0562 -0.0482 -0.1833 187 GLY B N   
5676  C CA  . GLY B 187 ? 0.6228 0.8023 0.6297 -0.0573 -0.0553 -0.1652 187 GLY B CA  
5677  C C   . GLY B 187 ? 0.7371 0.9283 0.7250 -0.0534 -0.0596 -0.1395 187 GLY B C   
5678  O O   . GLY B 187 ? 0.7513 0.9477 0.7356 -0.0538 -0.0659 -0.1244 187 GLY B O   
5679  N N   . LYS B 188 ? 0.6098 0.8054 0.5890 -0.0496 -0.0563 -0.1339 188 LYS B N   
5680  C CA  . LYS B 188 ? 0.5363 0.7436 0.5015 -0.0465 -0.0602 -0.1088 188 LYS B CA  
5681  C C   . LYS B 188 ? 0.5649 0.7405 0.5361 -0.0408 -0.0617 -0.0876 188 LYS B C   
5682  O O   . LYS B 188 ? 0.5451 0.7279 0.5114 -0.0387 -0.0663 -0.0668 188 LYS B O   
5683  C CB  . LYS B 188 ? 0.6750 0.8959 0.6311 -0.0446 -0.0555 -0.1090 188 LYS B CB  
5684  C CG  . LYS B 188 ? 0.6530 0.8991 0.6083 -0.0495 -0.0507 -0.1371 188 LYS B CG  
5685  C CD  . LYS B 188 ? 0.6570 0.9396 0.5959 -0.0509 -0.0494 -0.1326 188 LYS B CD  
5686  C CE  . LYS B 188 ? 0.7041 1.0190 0.6421 -0.0568 -0.0445 -0.1639 188 LYS B CE  
5687  N NZ  . LYS B 188 ? 0.7717 1.0845 0.7128 -0.0537 -0.0359 -0.1740 188 LYS B NZ  
5688  N N   . GLY B 189 ? 0.6074 0.7503 0.5910 -0.0387 -0.0579 -0.0923 189 GLY B N   
5689  C CA  . GLY B 189 ? 0.6486 0.7669 0.6373 -0.0344 -0.0590 -0.0749 189 GLY B CA  
5690  C C   . GLY B 189 ? 0.5990 0.6874 0.6008 -0.0337 -0.0550 -0.0799 189 GLY B C   
5691  O O   . GLY B 189 ? 0.6937 0.7729 0.7025 -0.0335 -0.0502 -0.0921 189 GLY B O   
5692  N N   . SER B 190 ? 0.5887 0.6638 0.5958 -0.0334 -0.0570 -0.0701 190 SER B N   
5693  C CA  . SER B 190 ? 0.5908 0.6417 0.6095 -0.0336 -0.0537 -0.0705 190 SER B CA  
5694  C C   . SER B 190 ? 0.5867 0.6226 0.6044 -0.0282 -0.0507 -0.0600 190 SER B C   
5695  O O   . SER B 190 ? 0.5263 0.5672 0.5365 -0.0246 -0.0520 -0.0494 190 SER B O   
5696  C CB  . SER B 190 ? 0.5775 0.6255 0.6014 -0.0362 -0.0564 -0.0646 190 SER B CB  
5697  O OG  . SER B 190 ? 0.7365 0.7885 0.7685 -0.0421 -0.0571 -0.0770 190 SER B OG  
5698  N N   . VAL B 191 ? 0.5930 0.6114 0.6209 -0.0279 -0.0470 -0.0624 191 VAL B N   
5699  C CA  . VAL B 191 ? 0.6396 0.6453 0.6681 -0.0234 -0.0447 -0.0521 191 VAL B CA  
5700  C C   . VAL B 191 ? 0.4957 0.4893 0.5319 -0.0254 -0.0444 -0.0435 191 VAL B C   
5701  O O   . VAL B 191 ? 0.5638 0.5509 0.6114 -0.0296 -0.0437 -0.0477 191 VAL B O   
5702  C CB  . VAL B 191 ? 0.6298 0.6291 0.6654 -0.0208 -0.0409 -0.0596 191 VAL B CB  
5703  C CG1 . VAL B 191 ? 0.5643 0.5546 0.5993 -0.0158 -0.0396 -0.0479 191 VAL B CG1 
5704  C CG2 . VAL B 191 ? 0.5414 0.5582 0.5696 -0.0205 -0.0404 -0.0712 191 VAL B CG2 
5705  N N   . SER B 192 ? 0.5077 0.5005 0.5387 -0.0231 -0.0449 -0.0321 192 SER B N   
5706  C CA  . SER B 192 ? 0.5916 0.5793 0.6274 -0.0254 -0.0442 -0.0235 192 SER B CA  
5707  C C   . SER B 192 ? 0.6128 0.5950 0.6486 -0.0220 -0.0427 -0.0147 192 SER B C   
5708  O O   . SER B 192 ? 0.6878 0.6690 0.7207 -0.0174 -0.0421 -0.0155 192 SER B O   
5709  C CB  . SER B 192 ? 0.5694 0.5671 0.6010 -0.0269 -0.0461 -0.0206 192 SER B CB  
5710  O OG  . SER B 192 ? 0.5828 0.5842 0.6092 -0.0229 -0.0463 -0.0154 192 SER B OG  
5711  N N   . THR B 193 ? 0.5755 0.5573 0.6147 -0.0247 -0.0421 -0.0057 193 THR B N   
5712  C CA  . THR B 193 ? 0.6654 0.6471 0.7040 -0.0223 -0.0416 0.0039  193 THR B CA  
5713  C C   . THR B 193 ? 0.6269 0.6213 0.6606 -0.0253 -0.0417 0.0096  193 THR B C   
5714  O O   . THR B 193 ? 0.5390 0.5405 0.5713 -0.0286 -0.0418 0.0055  193 THR B O   
5715  C CB  . THR B 193 ? 0.6455 0.6171 0.6975 -0.0229 -0.0408 0.0108  193 THR B CB  
5716  O OG1 . THR B 193 ? 0.6069 0.5801 0.6584 -0.0193 -0.0411 0.0201  193 THR B OG1 
5717  C CG2 . THR B 193 ? 0.6558 0.6286 0.7156 -0.0296 -0.0405 0.0183  193 THR B CG2 
5718  N N   . SER B 194 ? 0.5300 0.5297 0.5620 -0.0242 -0.0416 0.0176  194 SER B N   
5719  C CA  . SER B 194 ? 0.5241 0.5406 0.5517 -0.0277 -0.0412 0.0213  194 SER B CA  
5720  C C   . SER B 194 ? 0.5853 0.6068 0.6165 -0.0307 -0.0413 0.0355  194 SER B C   
5721  O O   . SER B 194 ? 0.5996 0.6089 0.6386 -0.0284 -0.0421 0.0425  194 SER B O   
5722  C CB  . SER B 194 ? 0.5676 0.5921 0.5902 -0.0239 -0.0415 0.0163  194 SER B CB  
5723  O OG  . SER B 194 ? 0.6150 0.6349 0.6376 -0.0208 -0.0420 0.0070  194 SER B OG  
5724  N N   . PRO B 195 ? 0.6214 0.6627 0.6488 -0.0364 -0.0406 0.0405  195 PRO B N   
5725  C CA  . PRO B 195 ? 0.6069 0.6597 0.6360 -0.0395 -0.0415 0.0572  195 PRO B CA  
5726  C C   . PRO B 195 ? 0.5891 0.6388 0.6183 -0.0334 -0.0436 0.0615  195 PRO B C   
5727  O O   . PRO B 195 ? 0.6694 0.7212 0.6928 -0.0293 -0.0437 0.0511  195 PRO B O   
5728  C CB  . PRO B 195 ? 0.6082 0.6901 0.6290 -0.0458 -0.0400 0.0556  195 PRO B CB  
5729  C CG  . PRO B 195 ? 0.5908 0.6704 0.6123 -0.0480 -0.0377 0.0427  195 PRO B CG  
5730  C CD  . PRO B 195 ? 0.4924 0.5493 0.5160 -0.0408 -0.0388 0.0316  195 PRO B CD  
5731  N N   . TYR B 196 ? 0.5961 0.6418 0.6350 -0.0332 -0.0455 0.0780  196 TYR B N   
5732  C CA  . TYR B 196 ? 0.6170 0.6523 0.6628 -0.0262 -0.0475 0.0821  196 TYR B CA  
5733  C C   . TYR B 196 ? 0.5589 0.6044 0.5945 -0.0223 -0.0481 0.0741  196 TYR B C   
5734  O O   . TYR B 196 ? 0.4754 0.5075 0.5113 -0.0163 -0.0474 0.0634  196 TYR B O   
5735  C CB  . TYR B 196 ? 0.5128 0.5534 0.5714 -0.0280 -0.0504 0.1050  196 TYR B CB  
5736  C CG  . TYR B 196 ? 0.5013 0.5207 0.5785 -0.0210 -0.0517 0.1091  196 TYR B CG  
5737  C CD1 . TYR B 196 ? 0.6230 0.6423 0.6995 -0.0142 -0.0530 0.1061  196 TYR B CD1 
5738  C CD2 . TYR B 196 ? 0.5558 0.5560 0.6545 -0.0213 -0.0512 0.1143  196 TYR B CD2 
5739  C CE1 . TYR B 196 ? 0.5358 0.5377 0.6316 -0.0076 -0.0536 0.1080  196 TYR B CE1 
5740  C CE2 . TYR B 196 ? 0.6018 0.5837 0.7221 -0.0147 -0.0518 0.1150  196 TYR B CE2 
5741  C CZ  . TYR B 196 ? 0.5862 0.5696 0.7046 -0.0077 -0.0529 0.1117  196 TYR B CZ  
5742  O OH  . TYR B 196 ? 0.7055 0.6725 0.8475 -0.0010 -0.0529 0.1107  196 TYR B OH  
5743  N N   . TYR B 197 ? 0.5984 0.6701 0.6260 -0.0262 -0.0493 0.0786  197 TYR B N   
5744  C CA  . TYR B 197 ? 0.5834 0.6674 0.6055 -0.0232 -0.0503 0.0724  197 TYR B CA  
5745  C C   . TYR B 197 ? 0.5861 0.6810 0.6001 -0.0252 -0.0479 0.0539  197 TYR B C   
5746  O O   . TYR B 197 ? 0.6045 0.7222 0.6144 -0.0274 -0.0483 0.0489  197 TYR B O   
5747  C CB  . TYR B 197 ? 0.5913 0.7004 0.6129 -0.0262 -0.0538 0.0886  197 TYR B CB  
5748  C CG  . TYR B 197 ? 0.6121 0.7085 0.6476 -0.0216 -0.0569 0.1060  197 TYR B CG  
5749  C CD1 . TYR B 197 ? 0.6334 0.7158 0.6752 -0.0137 -0.0577 0.1017  197 TYR B CD1 
5750  C CD2 . TYR B 197 ? 0.5695 0.6673 0.6152 -0.0251 -0.0589 0.1269  197 TYR B CD2 
5751  C CE1 . TYR B 197 ? 0.5711 0.6417 0.6299 -0.0088 -0.0602 0.1155  197 TYR B CE1 
5752  C CE2 . TYR B 197 ? 0.5605 0.6446 0.6257 -0.0201 -0.0620 0.1427  197 TYR B CE2 
5753  C CZ  . TYR B 197 ? 0.6206 0.6911 0.6926 -0.0116 -0.0625 0.1356  197 TYR B CZ  
5754  O OH  . TYR B 197 ? 0.6077 0.6652 0.7025 -0.0060 -0.0651 0.1487  197 TYR B OH  
5755  N N   . HIS B 198 ? 0.5439 0.6242 0.5585 -0.0247 -0.0455 0.0432  198 HIS B N   
5756  C CA  . HIS B 198 ? 0.5765 0.6649 0.5895 -0.0262 -0.0434 0.0270  198 HIS B CA  
5757  C C   . HIS B 198 ? 0.6169 0.7368 0.6263 -0.0330 -0.0424 0.0227  198 HIS B C   
5758  O O   . HIS B 198 ? 0.6762 0.8086 0.6880 -0.0330 -0.0415 0.0092  198 HIS B O   
5759  C CB  . HIS B 198 ? 0.5490 0.6296 0.5654 -0.0205 -0.0436 0.0176  198 HIS B CB  
5760  C CG  . HIS B 198 ? 0.5467 0.6203 0.5682 -0.0193 -0.0421 0.0048  198 HIS B CG  
5761  N ND1 . HIS B 198 ? 0.4901 0.5767 0.5185 -0.0205 -0.0410 -0.0078 198 HIS B ND1 
5762  C CD2 . HIS B 198 ? 0.5530 0.6096 0.5762 -0.0172 -0.0419 0.0032  198 HIS B CD2 
5763  C CE1 . HIS B 198 ? 0.5213 0.5975 0.5574 -0.0186 -0.0405 -0.0144 198 HIS B CE1 
5764  N NE2 . HIS B 198 ? 0.5647 0.6241 0.5960 -0.0167 -0.0412 -0.0073 198 HIS B NE2 
5765  N N   . PRO B 199 ? 0.6535 0.7890 0.6589 -0.0395 -0.0421 0.0328  199 PRO B N   
5766  C CA  . PRO B 199 ? 0.5748 0.7466 0.5754 -0.0470 -0.0405 0.0275  199 PRO B CA  
5767  C C   . PRO B 199 ? 0.5924 0.7714 0.5965 -0.0501 -0.0366 0.0097  199 PRO B C   
5768  O O   . PRO B 199 ? 0.7534 0.9113 0.7623 -0.0479 -0.0356 0.0064  199 PRO B O   
5769  C CB  . PRO B 199 ? 0.6262 0.8116 0.6223 -0.0531 -0.0417 0.0488  199 PRO B CB  
5770  C CG  . PRO B 199 ? 0.5554 0.7092 0.5577 -0.0505 -0.0417 0.0568  199 PRO B CG  
5771  C CD  . PRO B 199 ? 0.6180 0.7412 0.6251 -0.0412 -0.0428 0.0493  199 PRO B CD  
5772  N N   . LEU B 200 ? 0.6399 0.8527 0.6430 -0.0558 -0.0344 -0.0024 200 LEU B N   
5773  C CA  . LEU B 200 ? 0.6595 0.8860 0.6688 -0.0598 -0.0300 -0.0200 200 LEU B CA  
5774  C C   . LEU B 200 ? 0.5413 0.7862 0.5431 -0.0680 -0.0281 -0.0085 200 LEU B C   
5775  O O   . LEU B 200 ? 0.5404 0.8237 0.5353 -0.0760 -0.0264 -0.0082 200 LEU B O   
5776  C CB  . LEU B 200 ? 0.6775 0.9336 0.6933 -0.0623 -0.0277 -0.0422 200 LEU B CB  
5777  C CG  . LEU B 200 ? 0.6477 0.8839 0.6771 -0.0547 -0.0288 -0.0551 200 LEU B CG  
5778  C CD1 . LEU B 200 ? 0.6443 0.9117 0.6811 -0.0580 -0.0272 -0.0747 200 LEU B CD1 
5779  C CD2 . LEU B 200 ? 0.4923 0.7036 0.5376 -0.0498 -0.0277 -0.0650 200 LEU B CD2 
5780  N N   . ILE B 201 ? 0.7003 0.6344 0.7085 -0.0291 -0.0246 0.0538  201 ILE B N   
5781  C CA  . ILE B 201 ? 0.6393 0.5655 0.6284 -0.0367 -0.0202 0.0596  201 ILE B CA  
5782  C C   . ILE B 201 ? 0.7066 0.6449 0.6809 -0.0440 -0.0162 0.0541  201 ILE B C   
5783  O O   . ILE B 201 ? 0.7199 0.6556 0.6735 -0.0496 -0.0171 0.0613  201 ILE B O   
5784  C CB  . ILE B 201 ? 0.5727 0.4903 0.5679 -0.0386 -0.0128 0.0599  201 ILE B CB  
5785  C CG1 . ILE B 201 ? 0.6243 0.5233 0.6206 -0.0344 -0.0173 0.0693  201 ILE B CG1 
5786  C CG2 . ILE B 201 ? 0.6588 0.5773 0.6410 -0.0491 -0.0051 0.0601  201 ILE B CG2 
5787  C CD1 . ILE B 201 ? 0.7157 0.6168 0.7293 -0.0240 -0.0224 0.0677  201 ILE B CD1 
5788  N N   . PRO B 202 ? 0.6689 0.6210 0.6524 -0.0439 -0.0119 0.0417  202 PRO B N   
5789  C CA  . PRO B 202 ? 0.6334 0.5985 0.6034 -0.0497 -0.0073 0.0345  202 PRO B CA  
5790  C C   . PRO B 202 ? 0.6398 0.6084 0.5912 -0.0507 -0.0144 0.0361  202 PRO B C   
5791  O O   . PRO B 202 ? 0.7870 0.7603 0.7167 -0.0579 -0.0106 0.0389  202 PRO B O   
5792  C CB  . PRO B 202 ? 0.6592 0.6355 0.6482 -0.0457 -0.0047 0.0205  202 PRO B CB  
5793  C CG  . PRO B 202 ? 0.6646 0.6341 0.6712 -0.0424 -0.0028 0.0234  202 PRO B CG  
5794  C CD  . PRO B 202 ? 0.6837 0.6399 0.6895 -0.0391 -0.0095 0.0343  202 PRO B CD  
5795  N N   . ILE B 203 ? 0.6540 0.6221 0.6130 -0.0445 -0.0248 0.0351  203 ILE B N   
5796  C CA  . ILE B 203 ? 0.6749 0.6479 0.6160 -0.0455 -0.0334 0.0359  203 ILE B CA  
5797  C C   . ILE B 203 ? 0.6951 0.6575 0.6160 -0.0484 -0.0374 0.0531  203 ILE B C   
5798  O O   . ILE B 203 ? 0.6730 0.6406 0.5689 -0.0534 -0.0398 0.0565  203 ILE B O   
5799  C CB  . ILE B 203 ? 0.6286 0.6042 0.5862 -0.0388 -0.0445 0.0308  203 ILE B CB  
5800  C CG1 . ILE B 203 ? 0.6509 0.6351 0.6259 -0.0373 -0.0413 0.0145  203 ILE B CG1 
5801  C CG2 . ILE B 203 ? 0.6561 0.6371 0.5948 -0.0400 -0.0552 0.0322  203 ILE B CG2 
5802  C CD1 . ILE B 203 ? 0.5885 0.5764 0.5773 -0.0336 -0.0523 0.0080  203 ILE B CD1 
5803  N N   . LEU B 204 ? 0.6765 0.6235 0.6074 -0.0451 -0.0385 0.0641  204 LEU B N   
5804  C CA  . LEU B 204 ? 0.7084 0.6413 0.6230 -0.0471 -0.0432 0.0813  204 LEU B CA  
5805  C C   . LEU B 204 ? 0.7114 0.6432 0.6032 -0.0583 -0.0340 0.0872  204 LEU B C   
5806  O O   . LEU B 204 ? 0.7777 0.7056 0.6459 -0.0631 -0.0384 0.0997  204 LEU B O   
5807  C CB  . LEU B 204 ? 0.7448 0.6606 0.6775 -0.0406 -0.0449 0.0887  204 LEU B CB  
5808  C CG  . LEU B 204 ? 0.7432 0.6616 0.6987 -0.0298 -0.0535 0.0855  204 LEU B CG  
5809  C CD1 . LEU B 204 ? 0.7591 0.6627 0.7315 -0.0234 -0.0524 0.0906  204 LEU B CD1 
5810  C CD2 . LEU B 204 ? 0.6900 0.6127 0.6368 -0.0265 -0.0675 0.0916  204 LEU B CD2 
5811  N N   . LEU B 205 ? 0.7064 0.6425 0.6053 -0.0632 -0.0216 0.0794  205 LEU B N   
5812  C CA  . LEU B 205 ? 0.7523 0.6914 0.6327 -0.0751 -0.0117 0.0842  205 LEU B CA  
5813  C C   . LEU B 205 ? 0.7474 0.7074 0.6075 -0.0801 -0.0089 0.0770  205 LEU B C   
5814  O O   . LEU B 205 ? 0.7642 0.7251 0.5978 -0.0871 -0.0100 0.0880  205 LEU B O   
5815  C CB  . LEU B 205 ? 0.7862 0.7274 0.6830 -0.0785 -0.0001 0.0768  205 LEU B CB  
5816  C CG  . LEU B 205 ? 0.7392 0.6606 0.6534 -0.0745 -0.0020 0.0820  205 LEU B CG  
5817  C CD1 . LEU B 205 ? 0.6906 0.6182 0.6212 -0.0771 0.0078  0.0721  205 LEU B CD1 
5818  C CD2 . LEU B 205 ? 0.6923 0.5925 0.5929 -0.0801 -0.0048 0.1000  205 LEU B CD2 
5819  N N   . ASN B 206 ? 0.7188 0.6957 0.5908 -0.0763 -0.0054 0.0584  206 ASN B N   
5820  C CA  . ASN B 206 ? 0.7962 0.7935 0.6513 -0.0793 -0.0026 0.0472  206 ASN B CA  
5821  C C   . ASN B 206 ? 0.7344 0.7388 0.6040 -0.0701 -0.0101 0.0310  206 ASN B C   
5822  O O   . ASN B 206 ? 0.7022 0.7093 0.5961 -0.0652 -0.0065 0.0188  206 ASN B O   
5823  C CB  . ASN B 206 ? 0.8215 0.8355 0.6756 -0.0867 0.0131  0.0382  206 ASN B CB  
5824  C CG  . ASN B 206 ? 0.8898 0.9251 0.7179 -0.0924 0.0180  0.0310  206 ASN B CG  
5825  O OD1 . ASN B 206 ? 0.9225 0.9568 0.7237 -0.0963 0.0121  0.0416  206 ASN B OD1 
5826  N ND2 . ASN B 206 ? 0.8803 0.9359 0.7162 -0.0925 0.0287  0.0129  206 ASN B ND2 
5827  N N   . PRO B 207 ? 0.8331 0.8403 0.6886 -0.0682 -0.0212 0.0309  207 PRO B N   
5828  C CA  . PRO B 207 ? 0.7728 0.7866 0.6427 -0.0611 -0.0289 0.0145  207 PRO B CA  
5829  C C   . PRO B 207 ? 0.8470 0.8773 0.7206 -0.0613 -0.0204 -0.0070 207 PRO B C   
5830  O O   . PRO B 207 ? 0.7535 0.7848 0.6475 -0.0551 -0.0250 -0.0211 207 PRO B O   
5831  C CB  . PRO B 207 ? 0.6601 0.6762 0.5080 -0.0615 -0.0423 0.0198  207 PRO B CB  
5832  C CG  . PRO B 207 ? 0.6556 0.6589 0.4879 -0.0650 -0.0445 0.0433  207 PRO B CG  
5833  C CD  . PRO B 207 ? 0.6835 0.6873 0.5102 -0.0725 -0.0287 0.0467  207 PRO B CD  
5834  N N   . ASN B 208 ? 0.8201 0.8634 0.6764 -0.0681 -0.0079 -0.0101 208 ASN B N   
5835  C CA  . ASN B 208 ? 0.7422 0.8033 0.6038 -0.0668 0.0009  -0.0323 208 ASN B CA  
5836  C C   . ASN B 208 ? 0.7958 0.8544 0.6903 -0.0617 0.0072  -0.0400 208 ASN B C   
5837  O O   . ASN B 208 ? 0.8237 0.8957 0.7275 -0.0588 0.0139  -0.0585 208 ASN B O   
5838  C CB  . ASN B 208 ? 0.7451 0.8249 0.5802 -0.0757 0.0138  -0.0333 208 ASN B CB  
5839  C CG  . ASN B 208 ? 0.8222 0.9042 0.6210 -0.0825 0.0085  -0.0207 208 ASN B CG  
5840  O OD1 . ASN B 208 ? 0.9431 1.0215 0.7248 -0.0909 0.0130  -0.0015 208 ASN B OD1 
5841  N ND2 . ASN B 208 ? 0.8657 0.9534 0.6522 -0.0794 -0.0019 -0.0310 208 ASN B ND2 
5842  N N   . CYS B 209 ? 0.7950 0.8379 0.7067 -0.0599 0.0053  -0.0270 209 CYS B N   
5843  C CA  . CYS B 209 ? 0.7751 0.8159 0.7169 -0.0546 0.0091  -0.0335 209 CYS B CA  
5844  C C   . CYS B 209 ? 0.8163 0.8545 0.7787 -0.0462 0.0009  -0.0470 209 CYS B C   
5845  O O   . CYS B 209 ? 0.7577 0.7961 0.7440 -0.0413 0.0037  -0.0543 209 CYS B O   
5846  C CB  . CYS B 209 ? 0.7191 0.7443 0.6716 -0.0548 0.0081  -0.0172 209 CYS B CB  
5847  S SG  . CYS B 209 ? 1.2061 1.2132 1.1633 -0.0499 -0.0064 -0.0052 209 CYS B SG  
5848  N N   . VAL B 210 ? 0.8219 0.8576 0.7760 -0.0451 -0.0098 -0.0497 210 VAL B N   
5849  C CA  . VAL B 210 ? 0.7046 0.7369 0.6785 -0.0390 -0.0183 -0.0628 210 VAL B CA  
5850  C C   . VAL B 210 ? 0.6727 0.7171 0.6499 -0.0364 -0.0131 -0.0851 210 VAL B C   
5851  O O   . VAL B 210 ? 0.7646 0.8044 0.7659 -0.0307 -0.0169 -0.0966 210 VAL B O   
5852  C CB  . VAL B 210 ? 0.6993 0.7277 0.6638 -0.0396 -0.0320 -0.0600 210 VAL B CB  
5853  C CG1 . VAL B 210 ? 0.7037 0.7214 0.6666 -0.0405 -0.0369 -0.0386 210 VAL B CG1 
5854  C CG2 . VAL B 210 ? 0.6924 0.7336 0.6260 -0.0439 -0.0325 -0.0677 210 VAL B CG2 
5855  N N   . TYR B 211 ? 0.7409 0.8012 0.6950 -0.0406 -0.0043 -0.0916 211 TYR B N   
5856  C CA  . TYR B 211 ? 0.7724 0.8470 0.7279 -0.0373 0.0010  -0.1154 211 TYR B CA  
5857  C C   . TYR B 211 ? 0.7852 0.8662 0.7634 -0.0330 0.0118  -0.1223 211 TYR B C   
5858  O O   . TYR B 211 ? 0.7881 0.8772 0.7782 -0.0270 0.0144  -0.1433 211 TYR B O   
5859  C CB  . TYR B 211 ? 0.7216 0.8147 0.6417 -0.0437 0.0070  -0.1205 211 TYR B CB  
5860  C CG  . TYR B 211 ? 0.7417 0.8310 0.6375 -0.0475 -0.0052 -0.1146 211 TYR B CG  
5861  C CD1 . TYR B 211 ? 0.7809 0.8671 0.6812 -0.0437 -0.0172 -0.1302 211 TYR B CD1 
5862  C CD2 . TYR B 211 ? 0.7404 0.8287 0.6102 -0.0550 -0.0058 -0.0932 211 TYR B CD2 
5863  C CE1 . TYR B 211 ? 0.8258 0.9108 0.7053 -0.0471 -0.0298 -0.1252 211 TYR B CE1 
5864  C CE2 . TYR B 211 ? 0.7768 0.8626 0.6255 -0.0574 -0.0185 -0.0870 211 TYR B CE2 
5865  C CZ  . TYR B 211 ? 0.8085 0.8941 0.6621 -0.0535 -0.0307 -0.1033 211 TYR B CZ  
5866  O OH  . TYR B 211 ? 0.8716 0.9570 0.7056 -0.0559 -0.0447 -0.0978 211 TYR B OH  
5867  N N   . GLU B 212 ? 0.7582 0.8359 0.7437 -0.0354 0.0172  -0.1061 212 GLU B N   
5868  C CA  . GLU B 212 ? 0.7462 0.8299 0.7560 -0.0308 0.0250  -0.1114 212 GLU B CA  
5869  C C   . GLU B 212 ? 0.7824 0.8541 0.8227 -0.0212 0.0167  -0.1200 212 GLU B C   
5870  O O   . GLU B 212 ? 0.8590 0.9383 0.9178 -0.0142 0.0202  -0.1357 212 GLU B O   
5871  C CB  . GLU B 212 ? 0.7781 0.8579 0.7901 -0.0358 0.0295  -0.0919 212 GLU B CB  
5872  C CG  . GLU B 212 ? 0.8877 0.9708 0.8709 -0.0466 0.0345  -0.0776 212 GLU B CG  
5873  C CD  . GLU B 212 ? 0.8461 0.9272 0.8350 -0.0517 0.0405  -0.0632 212 GLU B CD  
5874  O OE1 . GLU B 212 ? 0.7887 0.8792 0.7980 -0.0489 0.0463  -0.0694 212 GLU B OE1 
5875  O OE2 . GLU B 212 ? 0.9186 0.9886 0.8927 -0.0583 0.0387  -0.0462 212 GLU B OE2 
5876  N N   . THR B 213 ? 0.7688 0.8219 0.8158 -0.0206 0.0055  -0.1095 213 THR B N   
5877  C CA  . THR B 213 ? 0.7525 0.7927 0.8280 -0.0134 -0.0025 -0.1142 213 THR B CA  
5878  C C   . THR B 213 ? 0.7385 0.7727 0.8159 -0.0111 -0.0120 -0.1293 213 THR B C   
5879  O O   . THR B 213 ? 0.6518 0.6809 0.7512 -0.0045 -0.0153 -0.1430 213 THR B O   
5880  C CB  . THR B 213 ? 0.7642 0.7898 0.8500 -0.0145 -0.0080 -0.0942 213 THR B CB  
5881  O OG1 . THR B 213 ? 0.8100 0.8350 0.8733 -0.0213 -0.0076 -0.0800 213 THR B OG1 
5882  C CG2 . THR B 213 ? 0.6618 0.6894 0.7640 -0.0117 -0.0023 -0.0879 213 THR B CG2 
5883  N N   . THR B 214 ? 0.7827 0.8174 0.8380 -0.0165 -0.0171 -0.1278 214 THR B N   
5884  C CA  . THR B 214 ? 0.7752 0.8072 0.8287 -0.0157 -0.0265 -0.1439 214 THR B CA  
5885  C C   . THR B 214 ? 0.7643 0.8128 0.7855 -0.0197 -0.0225 -0.1542 214 THR B C   
5886  O O   . THR B 214 ? 0.7741 0.8247 0.7711 -0.0258 -0.0266 -0.1437 214 THR B O   
5887  C CB  . THR B 214 ? 0.6992 0.7175 0.7587 -0.0186 -0.0394 -0.1327 214 THR B CB  
5888  O OG1 . THR B 214 ? 0.7980 0.8182 0.8378 -0.0241 -0.0393 -0.1127 214 THR B OG1 
5889  C CG2 . THR B 214 ? 0.6860 0.6892 0.7783 -0.0152 -0.0430 -0.1233 214 THR B CG2 
5890  N N   . PRO B 215 ? 0.7387 0.8007 0.7578 -0.0161 -0.0142 -0.1745 215 PRO B N   
5891  C CA  . PRO B 215 ? 0.7243 0.8069 0.7072 -0.0211 -0.0078 -0.1833 215 PRO B CA  
5892  C C   . PRO B 215 ? 0.7918 0.8740 0.7582 -0.0231 -0.0192 -0.1961 215 PRO B C   
5893  O O   . PRO B 215 ? 0.8440 0.9370 0.7775 -0.0297 -0.0192 -0.1907 215 PRO B O   
5894  C CB  . PRO B 215 ? 0.7238 0.8244 0.7135 -0.0152 0.0056  -0.2053 215 PRO B CB  
5895  C CG  . PRO B 215 ? 0.8325 0.9185 0.8622 -0.0064 0.0027  -0.2080 215 PRO B CG  
5896  C CD  . PRO B 215 ? 0.7614 0.8257 0.8074 -0.0076 -0.0072 -0.1874 215 PRO B CD  
5897  N N   . ASN B 216 ? 0.7365 0.8047 0.7263 -0.0182 -0.0305 -0.2100 216 ASN B N   
5898  C CA  . ASN B 216 ? 0.7764 0.8452 0.7521 -0.0206 -0.0425 -0.2254 216 ASN B CA  
5899  C C   . ASN B 216 ? 0.8661 0.9246 0.8376 -0.0265 -0.0569 -0.2070 216 ASN B C   
5900  O O   . ASN B 216 ? 0.8714 0.9298 0.8352 -0.0290 -0.0695 -0.2183 216 ASN B O   
5901  C CB  . ASN B 216 ? 0.8112 0.8693 0.8146 -0.0136 -0.0487 -0.2518 216 ASN B CB  
5902  C CG  . ASN B 216 ? 0.8170 0.8871 0.8255 -0.0059 -0.0355 -0.2735 216 ASN B CG  
5903  O OD1 . ASN B 216 ? 0.8726 0.9658 0.8534 -0.0076 -0.0240 -0.2803 216 ASN B OD1 
5904  N ND2 . ASN B 216 ? 0.8015 0.8573 0.8466 0.0026  -0.0367 -0.2831 216 ASN B ND2 
5905  N N   . VAL B 217 ? 0.7518 0.8031 0.7292 -0.0285 -0.0555 -0.1802 217 VAL B N   
5906  C CA  . VAL B 217 ? 0.7503 0.7936 0.7279 -0.0326 -0.0683 -0.1628 217 VAL B CA  
5907  C C   . VAL B 217 ? 0.8418 0.8984 0.7815 -0.0382 -0.0732 -0.1597 217 VAL B C   
5908  O O   . VAL B 217 ? 0.8263 0.8978 0.7367 -0.0404 -0.0637 -0.1631 217 VAL B O   
5909  C CB  . VAL B 217 ? 0.7379 0.7722 0.7289 -0.0324 -0.0638 -0.1368 217 VAL B CB  
5910  C CG1 . VAL B 217 ? 0.8051 0.8488 0.7686 -0.0357 -0.0535 -0.1222 217 VAL B CG1 
5911  C CG2 . VAL B 217 ? 0.6631 0.6879 0.6679 -0.0342 -0.0768 -0.1223 217 VAL B CG2 
5912  N N   . LYS B 218 ? 0.7811 0.8339 0.7218 -0.0409 -0.0885 -0.1527 218 LYS B N   
5913  C CA  . LYS B 218 ? 0.8573 0.9213 0.7641 -0.0456 -0.0963 -0.1458 218 LYS B CA  
5914  C C   . LYS B 218 ? 0.8739 0.9311 0.7841 -0.0465 -0.1009 -0.1172 218 LYS B C   
5915  O O   . LYS B 218 ? 0.8269 0.8746 0.7652 -0.0449 -0.1096 -0.1105 218 LYS B O   
5916  C CB  . LYS B 218 ? 0.9090 0.9777 0.8127 -0.0476 -0.1125 -0.1645 218 LYS B CB  
5917  C CG  . LYS B 218 ? 0.9484 1.0348 0.8083 -0.0520 -0.1174 -0.1676 218 LYS B CG  
5918  C CD  . LYS B 218 ? 1.0059 1.0934 0.8528 -0.0547 -0.1289 -0.1418 218 LYS B CD  
5919  C CE  . LYS B 218 ? 1.0085 1.0873 0.8877 -0.0540 -0.1455 -0.1373 218 LYS B CE  
5920  N NZ  . LYS B 218 ? 0.8891 0.9691 0.7625 -0.0543 -0.1561 -0.1115 218 LYS B NZ  
5921  N N   . ILE B 219 ? 0.9046 0.9665 0.7876 -0.0489 -0.0943 -0.1005 219 ILE B N   
5922  C CA  . ILE B 219 ? 0.8175 0.8719 0.7008 -0.0488 -0.0985 -0.0740 219 ILE B CA  
5923  C C   . ILE B 219 ? 0.8700 0.9343 0.7162 -0.0528 -0.1068 -0.0649 219 ILE B C   
5924  O O   . ILE B 219 ? 0.8836 0.9613 0.6998 -0.0566 -0.1040 -0.0764 219 ILE B O   
5925  C CB  . ILE B 219 ? 0.8010 0.8471 0.6905 -0.0480 -0.0832 -0.0594 219 ILE B CB  
5926  C CG1 . ILE B 219 ? 0.7588 0.8134 0.6135 -0.0532 -0.0725 -0.0537 219 ILE B CG1 
5927  C CG2 . ILE B 219 ? 0.7562 0.7970 0.6751 -0.0445 -0.0737 -0.0715 219 ILE B CG2 
5928  C CD1 . ILE B 219 ? 0.7502 0.7956 0.6084 -0.0541 -0.0612 -0.0353 219 ILE B CD1 
5929  N N   . PRO B 220 ? 0.9473 1.0062 0.7943 -0.0516 -0.1176 -0.0445 220 PRO B N   
5930  C CA  . PRO B 220 ? 1.0063 1.0732 0.8180 -0.0548 -0.1273 -0.0326 220 PRO B CA  
5931  C C   . PRO B 220 ? 0.9464 1.0136 0.7277 -0.0594 -0.1138 -0.0194 220 PRO B C   
5932  O O   . PRO B 220 ? 0.9725 1.0330 0.7633 -0.0598 -0.0979 -0.0172 220 PRO B O   
5933  C CB  . PRO B 220 ? 0.9169 0.9757 0.7468 -0.0502 -0.1412 -0.0136 220 PRO B CB  
5934  C CG  . PRO B 220 ? 0.8587 0.9037 0.7246 -0.0459 -0.1315 -0.0094 220 PRO B CG  
5935  C CD  . PRO B 220 ? 0.8382 0.8850 0.7194 -0.0467 -0.1222 -0.0319 220 PRO B CD  
5936  N N   . ASP B 221 ? 0.9659 1.0419 0.7097 -0.0638 -0.1207 -0.0100 221 ASP B N   
5937  C CA  . ASP B 221 ? 1.0272 1.1030 0.7407 -0.0699 -0.1095 0.0071  221 ASP B CA  
5938  C C   . ASP B 221 ? 0.9484 1.0046 0.6721 -0.0673 -0.1127 0.0350  221 ASP B C   
5939  O O   . ASP B 221 ? 1.0512 1.1030 0.7760 -0.0634 -0.1296 0.0481  221 ASP B O   
5940  C CB  . ASP B 221 ? 1.0429 1.1357 0.7103 -0.0763 -0.1157 0.0086  221 ASP B CB  
5941  C CG  . ASP B 221 ? 1.1308 1.2260 0.7656 -0.0848 -0.1018 0.0251  221 ASP B CG  
5942  O OD1 . ASP B 221 ? 1.2212 1.3225 0.8570 -0.0885 -0.0827 0.0146  221 ASP B OD1 
5943  O OD2 . ASP B 221 ? 1.2056 1.2966 0.8153 -0.0880 -0.1104 0.0494  221 ASP B OD2 
5944  N N   . PHE B 222 ? 0.8706 0.9156 0.6034 -0.0690 -0.0972 0.0429  222 PHE B N   
5945  C CA  . PHE B 222 ? 0.8654 0.8898 0.6098 -0.0664 -0.0988 0.0665  222 PHE B CA  
5946  C C   . PHE B 222 ? 0.8792 0.9006 0.5869 -0.0741 -0.0979 0.0886  222 PHE B C   
5947  O O   . PHE B 222 ? 0.9462 0.9665 0.6419 -0.0819 -0.0825 0.0935  222 PHE B O   
5948  C CB  . PHE B 222 ? 0.8490 0.8627 0.6220 -0.0650 -0.0838 0.0629  222 PHE B CB  
5949  C CG  . PHE B 222 ? 0.8377 0.8486 0.6493 -0.0567 -0.0869 0.0497  222 PHE B CG  
5950  C CD1 . PHE B 222 ? 0.8407 0.8645 0.6619 -0.0555 -0.0873 0.0268  222 PHE B CD1 
5951  C CD2 . PHE B 222 ? 0.7993 0.7944 0.6378 -0.0504 -0.0888 0.0600  222 PHE B CD2 
5952  C CE1 . PHE B 222 ? 0.8932 0.9135 0.7499 -0.0493 -0.0901 0.0170  222 PHE B CE1 
5953  C CE2 . PHE B 222 ? 0.7668 0.7614 0.6393 -0.0439 -0.0905 0.0494  222 PHE B CE2 
5954  C CZ  . PHE B 222 ? 0.8513 0.8580 0.7329 -0.0439 -0.0913 0.0291  222 PHE B CZ  
5955  N N   . ALA B 223 ? 0.9630 0.9834 0.6531 -0.0724 -0.1153 0.1034  223 ALA B N   
5956  C CA  . ALA B 223 ? 1.0525 1.0687 0.7058 -0.0801 -0.1164 0.1273  223 ALA B CA  
5957  C C   . ALA B 223 ? 1.0333 1.0233 0.6987 -0.0801 -0.1115 0.1493  223 ALA B C   
5958  O O   . ALA B 223 ? 1.2444 1.2296 0.8899 -0.0902 -0.0997 0.1617  223 ALA B O   
5959  C CB  . ALA B 223 ? 1.0801 1.1020 0.7127 -0.0772 -0.1385 0.1383  223 ALA B CB  
5960  N N   . VAL B 224 ? 0.9109 0.8843 0.6097 -0.0693 -0.1200 0.1535  224 VAL B N   
5961  C CA  . VAL B 224 ? 1.0044 0.9512 0.7173 -0.0676 -0.1168 0.1717  224 VAL B CA  
5962  C C   . VAL B 224 ? 1.0043 0.9470 0.7333 -0.0724 -0.0965 0.1611  224 VAL B C   
5963  O O   . VAL B 224 ? 0.9876 0.9480 0.7208 -0.0750 -0.0860 0.1400  224 VAL B O   
5964  C CB  . VAL B 224 ? 1.0465 0.9807 0.7917 -0.0533 -0.1312 0.1757  224 VAL B CB  
5965  C CG1 . VAL B 224 ? 1.0357 0.9817 0.7706 -0.0479 -0.1519 0.1799  224 VAL B CG1 
5966  C CG2 . VAL B 224 ? 0.9625 0.9016 0.7452 -0.0469 -0.1240 0.1538  224 VAL B CG2 
5967  N N   . SER B 225 ? 1.0119 0.9312 0.7510 -0.0732 -0.0918 0.1752  225 SER B N   
5968  C CA  . SER B 225 ? 1.0091 0.9229 0.7686 -0.0762 -0.0753 0.1657  225 SER B CA  
5969  C C   . SER B 225 ? 0.9860 0.8823 0.7811 -0.0644 -0.0796 0.1643  225 SER B C   
5970  O O   . SER B 225 ? 0.8996 0.7779 0.6996 -0.0574 -0.0916 0.1794  225 SER B O   
5971  C CB  . SER B 225 ? 0.9486 0.8512 0.6900 -0.0896 -0.0640 0.1807  225 SER B CB  
5972  O OG  . SER B 225 ? 0.7903 0.6761 0.5566 -0.0895 -0.0553 0.1791  225 SER B OG  
5973  N N   . PHE B 226 ? 0.9415 0.8442 0.7612 -0.0617 -0.0699 0.1460  226 PHE B N   
5974  C CA  . PHE B 226 ? 0.9194 0.8087 0.7711 -0.0522 -0.0704 0.1429  226 PHE B CA  
5975  C C   . PHE B 226 ? 0.8415 0.7192 0.7010 -0.0583 -0.0566 0.1420  226 PHE B C   
5976  O O   . PHE B 226 ? 0.8643 0.7355 0.7491 -0.0518 -0.0538 0.1346  226 PHE B O   
5977  C CB  . PHE B 226 ? 0.9263 0.8320 0.8015 -0.0441 -0.0717 0.1241  226 PHE B CB  
5978  C CG  . PHE B 226 ? 0.9668 0.8842 0.8398 -0.0382 -0.0865 0.1233  226 PHE B CG  
5979  C CD1 . PHE B 226 ? 0.9272 0.8365 0.8129 -0.0281 -0.1001 0.1330  226 PHE B CD1 
5980  C CD2 . PHE B 226 ? 0.9975 0.9353 0.8578 -0.0424 -0.0871 0.1112  226 PHE B CD2 
5981  C CE1 . PHE B 226 ? 0.8994 0.8220 0.7855 -0.0232 -0.1146 0.1317  226 PHE B CE1 
5982  C CE2 . PHE B 226 ? 0.9056 0.8548 0.7646 -0.0379 -0.1018 0.1090  226 PHE B CE2 
5983  C CZ  . PHE B 226 ? 0.8606 0.8029 0.7328 -0.0287 -0.1158 0.1197  226 PHE B CZ  
5984  N N   . ARG B 227 ? 0.8615 0.7380 0.6995 -0.0713 -0.0480 0.1492  227 ARG B N   
5985  C CA  . ARG B 227 ? 0.8585 0.7274 0.7052 -0.0787 -0.0351 0.1469  227 ARG B CA  
5986  C C   . ARG B 227 ? 0.8606 0.7002 0.7204 -0.0747 -0.0394 0.1575  227 ARG B C   
5987  O O   . ARG B 227 ? 0.9379 0.7712 0.8167 -0.0742 -0.0325 0.1492  227 ARG B O   
5988  C CB  . ARG B 227 ? 0.7634 0.6398 0.5854 -0.0947 -0.0250 0.1534  227 ARG B CB  
5989  C CG  . ARG B 227 ? 0.8800 0.7862 0.6880 -0.0981 -0.0199 0.1409  227 ARG B CG  
5990  C CD  . ARG B 227 ? 1.0767 0.9948 0.8668 -0.1138 -0.0057 0.1436  227 ARG B CD  
5991  N NE  . ARG B 227 ? 1.1531 1.0673 0.9631 -0.1188 0.0053  0.1382  227 ARG B NE  
5992  C CZ  . ARG B 227 ? 1.1586 1.0944 0.9733 -0.1255 0.0189  0.1251  227 ARG B CZ  
5993  N NH1 . ARG B 227 ? 1.2322 1.1947 1.0326 -0.1283 0.0248  0.1155  227 ARG B NH1 
5994  N NH2 . ARG B 227 ? 1.0854 1.0169 0.9204 -0.1288 0.0263  0.1204  227 ARG B NH2 
5995  N N   . GLU B 228 ? 0.8740 0.6956 0.7244 -0.0713 -0.0513 0.1752  228 GLU B N   
5996  C CA  . GLU B 228 ? 0.9147 0.7067 0.7799 -0.0658 -0.0560 0.1836  228 GLU B CA  
5997  C C   . GLU B 228 ? 0.9131 0.7056 0.8070 -0.0493 -0.0612 0.1716  228 GLU B C   
5998  O O   . GLU B 228 ? 0.9624 0.7382 0.8748 -0.0447 -0.0591 0.1679  228 GLU B O   
5999  C CB  . GLU B 228 ? 0.7957 0.5664 0.6436 -0.0664 -0.0680 0.2075  228 GLU B CB  
6000  C CG  . GLU B 228 ? 0.9997 0.7453 0.8390 -0.0792 -0.0628 0.2217  228 GLU B CG  
6001  C CD  . GLU B 228 ? 1.1021 0.8221 0.9675 -0.0729 -0.0623 0.2167  228 GLU B CD  
6002  O OE1 . GLU B 228 ? 1.0769 0.7979 0.9514 -0.0808 -0.0504 0.2055  228 GLU B OE1 
6003  O OE2 . GLU B 228 ? 1.2443 0.9446 1.1219 -0.0596 -0.0744 0.2230  228 GLU B OE2 
6004  N N   . ASP B 229 ? 0.8654 0.6780 0.7635 -0.0411 -0.0676 0.1646  229 ASP B N   
6005  C CA  . ASP B 229 ? 0.8759 0.6931 0.8021 -0.0269 -0.0712 0.1535  229 ASP B CA  
6006  C C   . ASP B 229 ? 0.8014 0.6270 0.7443 -0.0281 -0.0584 0.1364  229 ASP B C   
6007  O O   . ASP B 229 ? 0.7688 0.5890 0.7336 -0.0191 -0.0577 0.1299  229 ASP B O   
6008  C CB  . ASP B 229 ? 0.8292 0.6675 0.7565 -0.0205 -0.0808 0.1501  229 ASP B CB  
6009  C CG  . ASP B 229 ? 0.9555 0.7850 0.8757 -0.0138 -0.0970 0.1665  229 ASP B CG  
6010  O OD1 . ASP B 229 ? 0.9646 0.7722 0.8705 -0.0173 -0.1003 0.1830  229 ASP B OD1 
6011  O OD2 . ASP B 229 ? 0.9401 0.7845 0.8695 -0.0056 -0.1073 0.1637  229 ASP B OD2 
6012  N N   . ALA B 230 ? 0.7286 0.5682 0.6614 -0.0389 -0.0483 0.1289  230 ALA B N   
6013  C CA  . ALA B 230 ? 0.7628 0.6101 0.7106 -0.0403 -0.0373 0.1144  230 ALA B CA  
6014  C C   . ALA B 230 ? 0.7633 0.5898 0.7171 -0.0429 -0.0325 0.1164  230 ALA B C   
6015  O O   . ALA B 230 ? 0.7820 0.6083 0.7539 -0.0374 -0.0288 0.1064  230 ALA B O   
6016  C CB  . ALA B 230 ? 0.7758 0.6423 0.7127 -0.0505 -0.0284 0.1066  230 ALA B CB  
6017  N N   . SER B 231 ? 0.7256 0.5345 0.6638 -0.0518 -0.0327 0.1294  231 SER B N   
6018  C CA  . SER B 231 ? 0.8069 0.5922 0.7518 -0.0547 -0.0300 0.1315  231 SER B CA  
6019  C C   . SER B 231 ? 0.8119 0.5796 0.7738 -0.0401 -0.0380 0.1317  231 SER B C   
6020  O O   . SER B 231 ? 0.7756 0.5315 0.7510 -0.0378 -0.0345 0.1239  231 SER B O   
6021  C CB  . SER B 231 ? 0.8745 0.6424 0.7998 -0.0680 -0.0298 0.1481  231 SER B CB  
6022  O OG  . SER B 231 ? 1.0083 0.7964 0.9189 -0.0813 -0.0208 0.1468  231 SER B OG  
6023  N N   . LYS B 232 ? 0.8230 0.5905 0.7852 -0.0299 -0.0489 0.1394  232 LYS B N   
6024  C CA  . LYS B 232 ? 0.8088 0.5630 0.7900 -0.0146 -0.0564 0.1388  232 LYS B CA  
6025  C C   . LYS B 232 ? 0.6998 0.4717 0.7025 -0.0056 -0.0510 0.1211  232 LYS B C   
6026  O O   . LYS B 232 ? 0.6531 0.4140 0.6714 0.0020  -0.0493 0.1139  232 LYS B O   
6027  C CB  . LYS B 232 ? 0.7286 0.4826 0.7067 -0.0058 -0.0702 0.1515  232 LYS B CB  
6028  C CG  . LYS B 232 ? 0.7935 0.5238 0.7521 -0.0120 -0.0777 0.1720  232 LYS B CG  
6029  C CD  . LYS B 232 ? 0.9177 0.6454 0.8759 -0.0009 -0.0937 0.1853  232 LYS B CD  
6030  C CE  . LYS B 232 ? 0.9586 0.6871 0.8861 -0.0119 -0.0992 0.2031  232 LYS B CE  
6031  N NZ  . LYS B 232 ? 1.0154 0.7156 0.9357 -0.0082 -0.1126 0.2252  232 LYS B NZ  
6032  N N   . HIS B 233 ? 0.6617 0.4607 0.6650 -0.0067 -0.0481 0.1139  233 HIS B N   
6033  C CA  . HIS B 233 ? 0.6636 0.4802 0.6860 0.0003  -0.0430 0.0996  233 HIS B CA  
6034  C C   . HIS B 233 ? 0.7584 0.5690 0.7857 -0.0033 -0.0332 0.0897  233 HIS B C   
6035  O O   . HIS B 233 ? 0.7310 0.5426 0.7742 0.0055  -0.0310 0.0810  233 HIS B O   
6036  C CB  . HIS B 233 ? 0.6907 0.5333 0.7111 -0.0036 -0.0409 0.0942  233 HIS B CB  
6037  C CG  . HIS B 233 ? 0.7308 0.5845 0.7532 0.0023  -0.0510 0.0990  233 HIS B CG  
6038  N ND1 . HIS B 233 ? 0.7101 0.5734 0.7535 0.0138  -0.0557 0.0960  233 HIS B ND1 
6039  C CD2 . HIS B 233 ? 0.6384 0.4971 0.6447 -0.0023 -0.0576 0.1059  233 HIS B CD2 
6040  C CE1 . HIS B 233 ? 0.7208 0.5941 0.7625 0.0158  -0.0656 0.1010  233 HIS B CE1 
6041  N NE2 . HIS B 233 ? 0.7351 0.6053 0.7531 0.0063  -0.0673 0.1067  233 HIS B NE2 
6042  N N   . VAL B 234 ? 0.7642 0.5701 0.7780 -0.0164 -0.0274 0.0904  234 VAL B N   
6043  C CA  . VAL B 234 ? 0.6689 0.4718 0.6872 -0.0211 -0.0192 0.0803  234 VAL B CA  
6044  C C   . VAL B 234 ? 0.7049 0.4803 0.7279 -0.0177 -0.0215 0.0809  234 VAL B C   
6045  O O   . VAL B 234 ? 0.8036 0.5778 0.8386 -0.0115 -0.0184 0.0696  234 VAL B O   
6046  C CB  . VAL B 234 ? 0.6981 0.5072 0.7036 -0.0364 -0.0127 0.0805  234 VAL B CB  
6047  C CG1 . VAL B 234 ? 0.6867 0.4978 0.6990 -0.0407 -0.0055 0.0688  234 VAL B CG1 
6048  C CG2 . VAL B 234 ? 0.5859 0.4195 0.5869 -0.0381 -0.0114 0.0792  234 VAL B CG2 
6049  N N   . GLU B 235 ? 0.7563 0.5088 0.7695 -0.0218 -0.0271 0.0942  235 GLU B N   
6050  C CA  . GLU B 235 ? 0.8218 0.5435 0.8404 -0.0192 -0.0302 0.0953  235 GLU B CA  
6051  C C   . GLU B 235 ? 0.7720 0.4899 0.8087 -0.0007 -0.0349 0.0892  235 GLU B C   
6052  O O   . GLU B 235 ? 0.7879 0.4920 0.8352 0.0044  -0.0331 0.0787  235 GLU B O   
6053  C CB  . GLU B 235 ? 0.8540 0.5511 0.8586 -0.0269 -0.0366 0.1141  235 GLU B CB  
6054  C CG  . GLU B 235 ? 0.9515 0.6531 0.9387 -0.0464 -0.0303 0.1204  235 GLU B CG  
6055  C CD  . GLU B 235 ? 1.1549 0.8245 1.1355 -0.0579 -0.0318 0.1316  235 GLU B CD  
6056  O OE1 . GLU B 235 ? 1.0775 0.7337 1.0670 -0.0623 -0.0280 0.1218  235 GLU B OE1 
6057  O OE2 . GLU B 235 ? 1.2338 0.8913 1.1999 -0.0633 -0.0373 0.1505  235 GLU B OE2 
6058  N N   . LEU B 236 ? 0.7756 0.5075 0.8170 0.0094  -0.0409 0.0943  236 LEU B N   
6059  C CA  . LEU B 236 ? 0.7333 0.4668 0.7949 0.0272  -0.0447 0.0882  236 LEU B CA  
6060  C C   . LEU B 236 ? 0.6900 0.4461 0.7637 0.0316  -0.0354 0.0708  236 LEU B C   
6061  O O   . LEU B 236 ? 0.7608 0.5145 0.8502 0.0437  -0.0342 0.0609  236 LEU B O   
6062  C CB  . LEU B 236 ? 0.6801 0.4257 0.7451 0.0356  -0.0541 0.0985  236 LEU B CB  
6063  C CG  . LEU B 236 ? 0.6792 0.4021 0.7328 0.0344  -0.0656 0.1173  236 LEU B CG  
6064  C CD1 . LEU B 236 ? 0.6738 0.4158 0.7245 0.0380  -0.0746 0.1268  236 LEU B CD1 
6065  C CD2 . LEU B 236 ? 0.7088 0.4029 0.7762 0.0467  -0.0723 0.1192  236 LEU B CD2 
6066  N N   . ALA B 237 ? 0.6766 0.4552 0.7434 0.0223  -0.0287 0.0670  237 ALA B N   
6067  C CA  . ALA B 237 ? 0.6584 0.4567 0.7336 0.0245  -0.0201 0.0527  237 ALA B CA  
6068  C C   . ALA B 237 ? 0.6750 0.4584 0.7491 0.0215  -0.0149 0.0418  237 ALA B C   
6069  O O   . ALA B 237 ? 0.7462 0.5375 0.8299 0.0290  -0.0101 0.0292  237 ALA B O   
6070  C CB  . ALA B 237 ? 0.6178 0.4398 0.6861 0.0152  -0.0157 0.0524  237 ALA B CB  
6071  N N   . LYS B 238 ? 0.7240 0.4870 0.7863 0.0098  -0.0156 0.0461  238 LYS B N   
6072  C CA  . LYS B 238 ? 0.7615 0.5094 0.8237 0.0055  -0.0118 0.0349  238 LYS B CA  
6073  C C   . LYS B 238 ? 0.8396 0.5645 0.9132 0.0181  -0.0156 0.0292  238 LYS B C   
6074  O O   . LYS B 238 ? 0.8792 0.5996 0.9576 0.0207  -0.0117 0.0138  238 LYS B O   
6075  C CB  . LYS B 238 ? 0.7958 0.5285 0.8449 -0.0115 -0.0118 0.0418  238 LYS B CB  
6076  C CG  . LYS B 238 ? 0.7849 0.5419 0.8246 -0.0228 -0.0074 0.0457  238 LYS B CG  
6077  C CD  . LYS B 238 ? 0.8048 0.5505 0.8331 -0.0398 -0.0063 0.0532  238 LYS B CD  
6078  C CE  . LYS B 238 ? 0.7890 0.5076 0.8198 -0.0455 -0.0069 0.0479  238 LYS B CE  
6079  N NZ  . LYS B 238 ? 0.8558 0.5626 0.8771 -0.0634 -0.0059 0.0578  238 LYS B NZ  
6080  N N   . GLU B 239 ? 0.8392 0.5501 0.9177 0.0268  -0.0237 0.0405  239 GLU B N   
6081  C CA  . GLU B 239 ? 0.8952 0.5853 0.9883 0.0415  -0.0280 0.0347  239 GLU B CA  
6082  C C   . GLU B 239 ? 0.8643 0.5793 0.9730 0.0568  -0.0232 0.0210  239 GLU B C   
6083  O O   . GLU B 239 ? 0.8170 0.5246 0.9355 0.0657  -0.0202 0.0055  239 GLU B O   
6084  C CB  . GLU B 239 ? 0.8834 0.5528 0.9783 0.0472  -0.0394 0.0524  239 GLU B CB  
6085  C CG  . GLU B 239 ? 1.1173 0.7523 1.1999 0.0344  -0.0443 0.0646  239 GLU B CG  
6086  C CD  . GLU B 239 ? 1.3021 0.9081 1.3901 0.0331  -0.0427 0.0518  239 GLU B CD  
6087  O OE1 . GLU B 239 ? 1.3825 0.9630 1.4841 0.0462  -0.0492 0.0496  239 GLU B OE1 
6088  O OE2 . GLU B 239 ? 1.2262 0.8349 1.3062 0.0191  -0.0358 0.0432  239 GLU B OE2 
6089  N N   . LYS B 240 ? 0.7998 0.5452 0.9114 0.0595  -0.0221 0.0260  240 LYS B N   
6090  C CA  . LYS B 240 ? 0.8129 0.5854 0.9396 0.0718  -0.0164 0.0147  240 LYS B CA  
6091  C C   . LYS B 240 ? 0.8475 0.6325 0.9695 0.0673  -0.0059 -0.0015 240 LYS B C   
6092  O O   . LYS B 240 ? 0.9548 0.7466 1.0871 0.0781  -0.0007 -0.0160 240 LYS B O   
6093  C CB  . LYS B 240 ? 0.6677 0.4694 0.7980 0.0719  -0.0175 0.0241  240 LYS B CB  
6094  C CG  . LYS B 240 ? 0.7110 0.5398 0.8612 0.0853  -0.0134 0.0167  240 LYS B CG  
6095  C CD  . LYS B 240 ? 0.7002 0.5213 0.8691 0.1012  -0.0216 0.0201  240 LYS B CD  
6096  C CE  . LYS B 240 ? 0.8304 0.6640 1.0191 0.1165  -0.0147 0.0043  240 LYS B CE  
6097  N NZ  . LYS B 240 ? 0.8441 0.6695 1.0543 0.1338  -0.0232 0.0065  240 LYS B NZ  
6098  N N   . TYR B 241 ? 0.7275 0.5172 0.8339 0.0519  -0.0027 0.0003  241 TYR B N   
6099  C CA  . TYR B 241 ? 0.7700 0.5714 0.8704 0.0469  0.0053  -0.0138 241 TYR B CA  
6100  C C   . TYR B 241 ? 0.7957 0.5726 0.8968 0.0498  0.0056  -0.0281 241 TYR B C   
6101  O O   . TYR B 241 ? 0.7552 0.5431 0.8588 0.0556  0.0118  -0.0443 241 TYR B O   
6102  C CB  . TYR B 241 ? 0.7168 0.5254 0.8027 0.0304  0.0067  -0.0084 241 TYR B CB  
6103  C CG  . TYR B 241 ? 0.6807 0.5067 0.7605 0.0253  0.0135  -0.0205 241 TYR B CG  
6104  C CD1 . TYR B 241 ? 0.6906 0.5019 0.7642 0.0194  0.0143  -0.0322 241 TYR B CD1 
6105  C CD2 . TYR B 241 ? 0.6797 0.5362 0.7599 0.0257  0.0182  -0.0197 241 TYR B CD2 
6106  C CE1 . TYR B 241 ? 0.7467 0.5754 0.8136 0.0148  0.0190  -0.0432 241 TYR B CE1 
6107  C CE2 . TYR B 241 ? 0.6758 0.5484 0.7491 0.0212  0.0232  -0.0288 241 TYR B CE2 
6108  C CZ  . TYR B 241 ? 0.7518 0.6114 0.8177 0.0160  0.0233  -0.0408 241 TYR B CZ  
6109  O OH  . TYR B 241 ? 0.6876 0.5645 0.7455 0.0116  0.0268  -0.0498 241 TYR B OH  
6110  N N   . PHE B 242 ? 0.8204 0.5637 0.9192 0.0454  -0.0012 -0.0225 242 PHE B N   
6111  C CA  . PHE B 242 ? 0.8355 0.5507 0.9371 0.0478  -0.0023 -0.0362 242 PHE B CA  
6112  C C   . PHE B 242 ? 0.8284 0.5437 0.9464 0.0677  -0.0012 -0.0486 242 PHE B C   
6113  O O   . PHE B 242 ? 0.8565 0.5696 0.9766 0.0725  0.0032  -0.0685 242 PHE B O   
6114  C CB  . PHE B 242 ? 0.8654 0.5428 0.9639 0.0397  -0.0107 -0.0241 242 PHE B CB  
6115  C CG  . PHE B 242 ? 0.9189 0.5617 1.0226 0.0416  -0.0135 -0.0373 242 PHE B CG  
6116  C CD1 . PHE B 242 ? 0.9789 0.6027 1.0984 0.0593  -0.0176 -0.0432 242 PHE B CD1 
6117  C CD2 . PHE B 242 ? 0.9333 0.5623 1.0282 0.0257  -0.0127 -0.0441 242 PHE B CD2 
6118  C CE1 . PHE B 242 ? 1.0728 0.6621 1.1984 0.0616  -0.0207 -0.0568 242 PHE B CE1 
6119  C CE2 . PHE B 242 ? 0.8492 0.4446 0.9499 0.0264  -0.0160 -0.0573 242 PHE B CE2 
6120  C CZ  . PHE B 242 ? 0.9909 0.5649 1.1066 0.0445  -0.0200 -0.0640 242 PHE B CZ  
6121  N N   . GLU B 243 ? 0.8788 0.5984 1.0093 0.0796  -0.0054 -0.0380 243 GLU B N   
6122  C CA  . GLU B 243 ? 0.8753 0.5978 1.0252 0.0999  -0.0044 -0.0493 243 GLU B CA  
6123  C C   . GLU B 243 ? 0.8046 0.5617 0.9562 0.1051  0.0073  -0.0666 243 GLU B C   
6124  O O   . GLU B 243 ? 0.8531 0.6083 1.0139 0.1173  0.0115  -0.0856 243 GLU B O   
6125  C CB  . GLU B 243 ? 0.9258 0.6559 1.0894 0.1103  -0.0111 -0.0336 243 GLU B CB  
6126  C CG  . GLU B 243 ? 1.0285 0.7251 1.1897 0.1072  -0.0236 -0.0150 243 GLU B CG  
6127  C CD  . GLU B 243 ? 1.1679 0.8279 1.3426 0.1198  -0.0304 -0.0209 243 GLU B CD  
6128  O OE1 . GLU B 243 ? 1.2677 0.8988 1.4354 0.1125  -0.0304 -0.0290 243 GLU B OE1 
6129  O OE2 . GLU B 243 ? 1.3202 0.9797 1.5140 0.1370  -0.0365 -0.0176 243 GLU B OE2 
6130  N N   . ILE B 244 ? 0.7971 0.5852 0.9391 0.0957  0.0127  -0.0606 244 ILE B N   
6131  C CA  . ILE B 244 ? 0.8285 0.6513 0.9704 0.0992  0.0237  -0.0731 244 ILE B CA  
6132  C C   . ILE B 244 ? 0.7788 0.5986 0.9051 0.0911  0.0286  -0.0894 244 ILE B C   
6133  O O   . ILE B 244 ? 0.7930 0.6239 0.9209 0.0995  0.0358  -0.1081 244 ILE B O   
6134  C CB  . ILE B 244 ? 0.7922 0.6473 0.9316 0.0925  0.0264  -0.0589 244 ILE B CB  
6135  C CG1 . ILE B 244 ? 0.6954 0.5517 0.8492 0.0985  0.0194  -0.0430 244 ILE B CG1 
6136  C CG2 . ILE B 244 ? 0.8036 0.6947 0.9442 0.0964  0.0377  -0.0690 244 ILE B CG2 
6137  C CD1 . ILE B 244 ? 0.6854 0.5480 0.8620 0.1172  0.0200  -0.0495 244 ILE B CD1 
6138  N N   . PHE B 245 ? 0.8083 0.6154 0.9193 0.0747  0.0249  -0.0833 245 PHE B N   
6139  C CA  . PHE B 245 ? 0.8559 0.6678 0.9518 0.0649  0.0287  -0.0965 245 PHE B CA  
6140  C C   . PHE B 245 ? 0.8412 0.6175 0.9334 0.0595  0.0236  -0.1077 245 PHE B C   
6141  O O   . PHE B 245 ? 0.8519 0.6316 0.9330 0.0522  0.0258  -0.1219 245 PHE B O   
6142  C CB  . PHE B 245 ? 0.8470 0.6767 0.9303 0.0497  0.0288  -0.0837 245 PHE B CB  
6143  C CG  . PHE B 245 ? 0.7675 0.6305 0.8540 0.0528  0.0333  -0.0733 245 PHE B CG  
6144  C CD1 . PHE B 245 ? 0.7310 0.6241 0.8120 0.0542  0.0411  -0.0808 245 PHE B CD1 
6145  C CD2 . PHE B 245 ? 0.7118 0.5759 0.8065 0.0537  0.0295  -0.0560 245 PHE B CD2 
6146  C CE1 . PHE B 245 ? 0.8241 0.7460 0.9094 0.0558  0.0451  -0.0699 245 PHE B CE1 
6147  C CE2 . PHE B 245 ? 0.7028 0.5960 0.8024 0.0556  0.0330  -0.0472 245 PHE B CE2 
6148  C CZ  . PHE B 245 ? 0.7191 0.6403 0.8150 0.0563  0.0410  -0.0536 245 PHE B CZ  
6149  N N   . GLY B 246 ? 0.8592 0.6016 0.9604 0.0621  0.0162  -0.1011 246 GLY B N   
6150  C CA  . GLY B 246 ? 0.8215 0.5265 0.9218 0.0565  0.0107  -0.1103 246 GLY B CA  
6151  C C   . GLY B 246 ? 0.9042 0.5956 0.9934 0.0359  0.0062  -0.0992 246 GLY B C   
6152  O O   . GLY B 246 ? 1.0364 0.6944 1.1264 0.0288  0.0010  -0.1037 246 GLY B O   
6153  N N   . GLU B 247 ? 0.8615 0.5777 0.9420 0.0259  0.0083  -0.0853 247 GLU B N   
6154  C CA  . GLU B 247 ? 0.8219 0.5315 0.8934 0.0067  0.0055  -0.0755 247 GLU B CA  
6155  C C   . GLU B 247 ? 0.8396 0.5622 0.9091 0.0033  0.0047  -0.0533 247 GLU B C   
6156  O O   . GLU B 247 ? 0.8412 0.5832 0.9150 0.0140  0.0067  -0.0475 247 GLU B O   
6157  C CB  . GLU B 247 ? 0.9592 0.6910 1.0208 -0.0038 0.0091  -0.0873 247 GLU B CB  
6158  C CG  . GLU B 247 ? 0.9863 0.7561 1.0445 0.0046  0.0156  -0.0927 247 GLU B CG  
6159  C CD  . GLU B 247 ? 1.0231 0.8114 1.0710 -0.0033 0.0176  -0.1070 247 GLU B CD  
6160  O OE1 . GLU B 247 ? 0.9982 0.7866 1.0414 -0.0183 0.0148  -0.1036 247 GLU B OE1 
6161  O OE2 . GLU B 247 ? 0.9108 0.7153 0.9553 0.0056  0.0220  -0.1215 247 GLU B OE2 
6162  N N   . HIS B 248 ? 0.8708 0.5833 0.9342 -0.0121 0.0020  -0.0416 248 HIS B N   
6163  C CA  . HIS B 248 ? 0.7607 0.4875 0.8202 -0.0161 0.0019  -0.0231 248 HIS B CA  
6164  C C   . HIS B 248 ? 0.6968 0.4591 0.7512 -0.0210 0.0070  -0.0251 248 HIS B C   
6165  O O   . HIS B 248 ? 0.7137 0.4859 0.7654 -0.0262 0.0095  -0.0376 248 HIS B O   
6166  C CB  . HIS B 248 ? 0.7287 0.4338 0.7829 -0.0305 -0.0018 -0.0093 248 HIS B CB  
6167  C CG  . HIS B 248 ? 0.8776 0.5532 0.9352 -0.0244 -0.0082 0.0026  248 HIS B CG  
6168  N ND1 . HIS B 248 ? 0.9516 0.6073 1.0029 -0.0361 -0.0120 0.0193  248 HIS B ND1 
6169  C CD2 . HIS B 248 ? 0.9833 0.6471 1.0504 -0.0074 -0.0120 0.0011  248 HIS B CD2 
6170  C CE1 . HIS B 248 ? 1.0704 0.7013 1.1259 -0.0266 -0.0188 0.0286  248 HIS B CE1 
6171  N NE2 . HIS B 248 ? 1.0708 0.7063 1.1374 -0.0085 -0.0192 0.0173  248 HIS B NE2 
6172  N N   . PRO B 249 ? 0.6747 0.4563 0.7284 -0.0188 0.0079  -0.0135 249 PRO B N   
6173  C CA  . PRO B 249 ? 0.5636 0.3765 0.6146 -0.0219 0.0119  -0.0149 249 PRO B CA  
6174  C C   . PRO B 249 ? 0.6313 0.4492 0.6767 -0.0372 0.0123  -0.0102 249 PRO B C   
6175  O O   . PRO B 249 ? 0.7277 0.5319 0.7699 -0.0449 0.0104  -0.0002 249 PRO B O   
6176  C CB  . PRO B 249 ? 0.5975 0.4248 0.6526 -0.0130 0.0117  -0.0049 249 PRO B CB  
6177  C CG  . PRO B 249 ? 0.6815 0.4868 0.7362 -0.0127 0.0066  0.0066  249 PRO B CG  
6178  C CD  . PRO B 249 ? 0.7561 0.5323 0.8125 -0.0117 0.0043  0.0003  249 PRO B CD  
6179  N N   . VAL B 250 ? 0.6262 0.4656 0.6705 -0.0414 0.0148  -0.0174 250 VAL B N   
6180  C CA  . VAL B 250 ? 0.6602 0.5117 0.7027 -0.0541 0.0156  -0.0141 250 VAL B CA  
6181  C C   . VAL B 250 ? 0.6657 0.5435 0.7099 -0.0511 0.0172  -0.0084 250 VAL B C   
6182  O O   . VAL B 250 ? 0.6383 0.5265 0.6826 -0.0595 0.0181  -0.0045 250 VAL B O   
6183  C CB  . VAL B 250 ? 0.6524 0.5080 0.6947 -0.0626 0.0154  -0.0264 250 VAL B CB  
6184  C CG1 . VAL B 250 ? 0.5720 0.3989 0.6140 -0.0706 0.0132  -0.0299 250 VAL B CG1 
6185  C CG2 . VAL B 250 ? 0.5434 0.4124 0.5846 -0.0536 0.0159  -0.0377 250 VAL B CG2 
6186  N N   . TYR B 251 ? 0.6830 0.5718 0.7297 -0.0398 0.0177  -0.0082 251 TYR B N   
6187  C CA  . TYR B 251 ? 0.5841 0.4945 0.6341 -0.0367 0.0184  -0.0027 251 TYR B CA  
6188  C C   . TYR B 251 ? 0.6401 0.5470 0.6930 -0.0287 0.0174  0.0054  251 TYR B C   
6189  O O   . TYR B 251 ? 0.6702 0.5672 0.7250 -0.0210 0.0169  0.0045  251 TYR B O   
6190  C CB  . TYR B 251 ? 0.5841 0.5139 0.6354 -0.0324 0.0195  -0.0083 251 TYR B CB  
6191  C CG  . TYR B 251 ? 0.6651 0.5975 0.7124 -0.0387 0.0190  -0.0183 251 TYR B CG  
6192  C CD1 . TYR B 251 ? 0.7880 0.7253 0.8364 -0.0491 0.0178  -0.0191 251 TYR B CD1 
6193  C CD2 . TYR B 251 ? 0.6390 0.5707 0.6821 -0.0346 0.0198  -0.0283 251 TYR B CD2 
6194  C CE1 . TYR B 251 ? 0.7939 0.7351 0.8404 -0.0558 0.0162  -0.0287 251 TYR B CE1 
6195  C CE2 . TYR B 251 ? 0.7236 0.6580 0.7622 -0.0411 0.0181  -0.0390 251 TYR B CE2 
6196  C CZ  . TYR B 251 ? 0.8109 0.7499 0.8518 -0.0520 0.0158  -0.0388 251 TYR B CZ  
6197  O OH  . TYR B 251 ? 0.9435 0.8869 0.9818 -0.0593 0.0130  -0.0498 251 TYR B OH  
6198  N N   . MET B 252 ? 0.6415 0.5575 0.6960 -0.0303 0.0167  0.0123  252 MET B N   
6199  C CA  . MET B 252 ? 0.6321 0.5459 0.6891 -0.0246 0.0143  0.0196  252 MET B CA  
6200  C C   . MET B 252 ? 0.6317 0.5637 0.6943 -0.0232 0.0141  0.0221  252 MET B C   
6201  O O   . MET B 252 ? 0.6203 0.5615 0.6827 -0.0287 0.0150  0.0207  252 MET B O   
6202  C CB  . MET B 252 ? 0.6363 0.5350 0.6859 -0.0298 0.0122  0.0259  252 MET B CB  
6203  C CG  . MET B 252 ? 0.6697 0.5586 0.7203 -0.0225 0.0079  0.0324  252 MET B CG  
6204  S SD  . MET B 252 ? 0.8447 0.7095 0.8846 -0.0275 0.0042  0.0410  252 MET B SD  
6205  C CE  . MET B 252 ? 0.5936 0.4374 0.6392 -0.0189 0.0021  0.0382  252 MET B CE  
6206  N N   . TRP B 253 ? 0.6506 0.5883 0.7205 -0.0159 0.0126  0.0253  253 TRP B N   
6207  C CA  . TRP B 253 ? 0.6610 0.6122 0.7381 -0.0150 0.0112  0.0283  253 TRP B CA  
6208  C C   . TRP B 253 ? 0.5868 0.5333 0.6624 -0.0156 0.0073  0.0324  253 TRP B C   
6209  O O   . TRP B 253 ? 0.5825 0.5232 0.6600 -0.0110 0.0044  0.0358  253 TRP B O   
6210  C CB  . TRP B 253 ? 0.5384 0.5004 0.6254 -0.0088 0.0119  0.0301  253 TRP B CB  
6211  C CG  . TRP B 253 ? 0.5836 0.5541 0.6802 -0.0081 0.0088  0.0346  253 TRP B CG  
6212  C CD1 . TRP B 253 ? 0.5427 0.5141 0.6471 -0.0046 0.0056  0.0383  253 TRP B CD1 
6213  C CD2 . TRP B 253 ? 0.5210 0.4993 0.6219 -0.0110 0.0078  0.0349  253 TRP B CD2 
6214  N NE1 . TRP B 253 ? 0.4703 0.4487 0.5831 -0.0063 0.0026  0.0404  253 TRP B NE1 
6215  C CE2 . TRP B 253 ? 0.5062 0.4877 0.6172 -0.0097 0.0039  0.0384  253 TRP B CE2 
6216  C CE3 . TRP B 253 ? 0.5214 0.5045 0.6205 -0.0142 0.0089  0.0323  253 TRP B CE3 
6217  C CZ2 . TRP B 253 ? 0.5650 0.5513 0.6839 -0.0113 0.0014  0.0387  253 TRP B CZ2 
6218  C CZ3 . TRP B 253 ? 0.5746 0.5640 0.6823 -0.0146 0.0063  0.0334  253 TRP B CZ3 
6219  C CH2 . TRP B 253 ? 0.6229 0.6124 0.7402 -0.0131 0.0028  0.0363  253 TRP B CH2 
6220  N N   . PRO B 254 ? 0.6004 0.5506 0.6729 -0.0206 0.0068  0.0315  254 PRO B N   
6221  C CA  . PRO B 254 ? 0.5548 0.5026 0.6235 -0.0213 0.0029  0.0342  254 PRO B CA  
6222  C C   . PRO B 254 ? 0.4939 0.4483 0.5739 -0.0161 -0.0014 0.0360  254 PRO B C   
6223  O O   . PRO B 254 ? 0.5254 0.4892 0.6161 -0.0148 -0.0008 0.0346  254 PRO B O   
6224  C CB  . PRO B 254 ? 0.6049 0.5593 0.6693 -0.0272 0.0051  0.0299  254 PRO B CB  
6225  C CG  . PRO B 254 ? 0.5942 0.5576 0.6668 -0.0273 0.0082  0.0260  254 PRO B CG  
6226  C CD  . PRO B 254 ? 0.5942 0.5522 0.6664 -0.0256 0.0098  0.0271  254 PRO B CD  
6227  N N   . PRO B 255 ? 0.4832 0.4332 0.5623 -0.0133 -0.0064 0.0399  255 PRO B N   
6228  C CA  . PRO B 255 ? 0.4641 0.4220 0.5567 -0.0093 -0.0111 0.0414  255 PRO B CA  
6229  C C   . PRO B 255 ? 0.4472 0.4124 0.5442 -0.0123 -0.0134 0.0375  255 PRO B C   
6230  O O   . PRO B 255 ? 0.5636 0.5273 0.6503 -0.0159 -0.0147 0.0342  255 PRO B O   
6231  C CB  . PRO B 255 ? 0.5670 0.5187 0.6553 -0.0065 -0.0174 0.0460  255 PRO B CB  
6232  C CG  . PRO B 255 ? 0.5591 0.4972 0.6355 -0.0068 -0.0146 0.0482  255 PRO B CG  
6233  C CD  . PRO B 255 ? 0.5316 0.4691 0.5986 -0.0139 -0.0090 0.0441  255 PRO B CD  
6234  N N   . GLN B 256 ? 0.5106 0.4837 0.6232 -0.0109 -0.0137 0.0378  256 GLN B N   
6235  C CA  . GLN B 256 ? 0.5403 0.5177 0.6612 -0.0130 -0.0163 0.0339  256 GLN B CA  
6236  C C   . GLN B 256 ? 0.5375 0.5148 0.6527 -0.0154 -0.0124 0.0285  256 GLN B C   
6237  O O   . GLN B 256 ? 0.5786 0.5573 0.6968 -0.0165 -0.0146 0.0224  256 GLN B O   
6238  C CB  . GLN B 256 ? 0.5129 0.4901 0.6329 -0.0142 -0.0238 0.0306  256 GLN B CB  
6239  C CG  . GLN B 256 ? 0.4859 0.4645 0.6103 -0.0117 -0.0291 0.0357  256 GLN B CG  
6240  C CD  . GLN B 256 ? 0.6397 0.6264 0.7860 -0.0109 -0.0313 0.0389  256 GLN B CD  
6241  O OE1 . GLN B 256 ? 0.6304 0.6192 0.7875 -0.0130 -0.0299 0.0381  256 GLN B OE1 
6242  N NE2 . GLN B 256 ? 0.6324 0.6242 0.7868 -0.0080 -0.0347 0.0435  256 GLN B NE2 
6243  N N   . ALA B 257 ? 0.5467 0.5230 0.6551 -0.0158 -0.0067 0.0294  257 ALA B N   
6244  C CA  . ALA B 257 ? 0.5845 0.5632 0.6881 -0.0184 -0.0028 0.0246  257 ALA B CA  
6245  C C   . ALA B 257 ? 0.6462 0.6242 0.7386 -0.0218 -0.0024 0.0189  257 ALA B C   
6246  O O   . ALA B 257 ? 0.6739 0.6576 0.7659 -0.0238 0.0009  0.0133  257 ALA B O   
6247  C CB  . ALA B 257 ? 0.5626 0.5476 0.6801 -0.0167 -0.0036 0.0231  257 ALA B CB  
6248  N N   . SER B 258 ? 0.5621 0.5354 0.6455 -0.0226 -0.0056 0.0206  258 SER B N   
6249  C CA  . SER B 258 ? 0.6454 0.6204 0.7162 -0.0261 -0.0056 0.0157  258 SER B CA  
6250  C C   . SER B 258 ? 0.6092 0.5834 0.6663 -0.0315 0.0009  0.0164  258 SER B C   
6251  O O   . SER B 258 ? 0.6190 0.5845 0.6692 -0.0331 0.0019  0.0232  258 SER B O   
6252  C CB  . SER B 258 ? 0.6899 0.6608 0.7532 -0.0256 -0.0123 0.0189  258 SER B CB  
6253  O OG  . SER B 258 ? 0.8033 0.7673 0.8685 -0.0228 -0.0145 0.0275  258 SER B OG  
6254  N N   . VAL B 259 ? 0.6694 0.6530 0.7244 -0.0346 0.0054  0.0089  259 VAL B N   
6255  C CA  . VAL B 259 ? 0.6737 0.6604 0.7194 -0.0413 0.0125  0.0091  259 VAL B CA  
6256  C C   . VAL B 259 ? 0.6511 0.6480 0.6858 -0.0454 0.0161  0.0027  259 VAL B C   
6257  O O   . VAL B 259 ? 0.6149 0.6188 0.6536 -0.0418 0.0140  -0.0060 259 VAL B O   
6258  C CB  . VAL B 259 ? 0.5319 0.5259 0.5909 -0.0410 0.0164  0.0057  259 VAL B CB  
6259  C CG1 . VAL B 259 ? 0.6293 0.6139 0.6910 -0.0400 0.0152  0.0124  259 VAL B CG1 
6260  C CG2 . VAL B 259 ? 0.6078 0.6101 0.6835 -0.0346 0.0140  -0.0015 259 VAL B CG2 
6261  N N   . SER B 260 ? 0.6226 0.6205 0.6433 -0.0536 0.0219  0.0066  260 SER B N   
6262  C CA  . SER B 260 ? 0.6228 0.6341 0.6315 -0.0594 0.0281  0.0013  260 SER B CA  
6263  C C   . SER B 260 ? 0.6284 0.6437 0.6340 -0.0688 0.0363  0.0053  260 SER B C   
6264  O O   . SER B 260 ? 0.6312 0.6351 0.6408 -0.0708 0.0354  0.0122  260 SER B O   
6265  C CB  . SER B 260 ? 0.6343 0.6411 0.6215 -0.0616 0.0243  0.0061  260 SER B CB  
6266  O OG  . SER B 260 ? 0.6662 0.6591 0.6388 -0.0676 0.0235  0.0205  260 SER B OG  
6267  N N   . ASN B 261 ? 0.5038 0.5366 0.5032 -0.0750 0.0446  -0.0003 261 ASN B N   
6268  C CA  . ASN B 261 ? 0.6448 0.6827 0.6406 -0.0864 0.0528  0.0048  261 ASN B CA  
6269  C C   . ASN B 261 ? 0.7071 0.7244 0.6850 -0.0941 0.0505  0.0208  261 ASN B C   
6270  O O   . ASN B 261 ? 0.7274 0.7365 0.7083 -0.1012 0.0525  0.0272  261 ASN B O   
6271  C CB  . ASN B 261 ? 0.7313 0.7943 0.7221 -0.0924 0.0632  -0.0032 261 ASN B CB  
6272  C CG  . ASN B 261 ? 0.7585 0.8415 0.7710 -0.0842 0.0657  -0.0196 261 ASN B CG  
6273  O OD1 . ASN B 261 ? 0.6976 0.7830 0.7306 -0.0811 0.0646  -0.0224 261 ASN B OD1 
6274  N ND2 . ASN B 261 ? 0.7027 0.8002 0.7107 -0.0803 0.0685  -0.0310 261 ASN B ND2 
6275  N N   . GLU B 262 ? 0.7407 0.7485 0.7011 -0.0922 0.0450  0.0270  262 GLU B N   
6276  C CA  . GLU B 262 ? 0.7387 0.7259 0.6823 -0.0980 0.0412  0.0433  262 GLU B CA  
6277  C C   . GLU B 262 ? 0.8016 0.7666 0.7563 -0.0911 0.0330  0.0485  262 GLU B C   
6278  O O   . GLU B 262 ? 0.8690 0.8168 0.8213 -0.0965 0.0326  0.0583  262 GLU B O   
6279  C CB  . GLU B 262 ? 0.7707 0.7578 0.6926 -0.0971 0.0365  0.0481  262 GLU B CB  
6280  C CG  . GLU B 262 ? 0.8557 0.8667 0.7615 -0.1039 0.0450  0.0421  262 GLU B CG  
6281  C CD  . GLU B 262 ? 0.9160 0.9498 0.8349 -0.0969 0.0489  0.0218  262 GLU B CD  
6282  O OE1 . GLU B 262 ? 1.0175 1.0683 0.9209 -0.0989 0.0528  0.0151  262 GLU B OE1 
6283  O OE2 . GLU B 262 ? 0.9416 0.9757 0.8850 -0.0894 0.0476  0.0129  262 GLU B OE2 
6284  N N   . ALA B 263 ? 0.7191 0.6839 0.6860 -0.0793 0.0266  0.0420  263 ALA B N   
6285  C CA  . ALA B 263 ? 0.6716 0.6204 0.6506 -0.0722 0.0206  0.0448  263 ALA B CA  
6286  C C   . ALA B 263 ? 0.7160 0.6624 0.7058 -0.0764 0.0254  0.0429  263 ALA B C   
6287  O O   . ALA B 263 ? 0.7183 0.6467 0.7079 -0.0775 0.0232  0.0492  263 ALA B O   
6288  C CB  . ALA B 263 ? 0.6692 0.6243 0.6622 -0.0611 0.0154  0.0371  263 ALA B CB  
6289  N N   . LEU B 264 ? 0.6634 0.6281 0.6633 -0.0787 0.0314  0.0334  264 LEU B N   
6290  C CA  . LEU B 264 ? 0.7006 0.6661 0.7111 -0.0833 0.0349  0.0306  264 LEU B CA  
6291  C C   . LEU B 264 ? 0.7785 0.7331 0.7789 -0.0959 0.0385  0.0389  264 LEU B C   
6292  O O   . LEU B 264 ? 0.7937 0.7370 0.7997 -0.0992 0.0378  0.0396  264 LEU B O   
6293  C CB  . LEU B 264 ? 0.6433 0.6332 0.6671 -0.0834 0.0399  0.0197  264 LEU B CB  
6294  C CG  . LEU B 264 ? 0.5638 0.5600 0.6019 -0.0713 0.0353  0.0128  264 LEU B CG  
6295  C CD1 . LEU B 264 ? 0.4405 0.4593 0.4891 -0.0696 0.0391  0.0028  264 LEU B CD1 
6296  C CD2 . LEU B 264 ? 0.5922 0.5828 0.6405 -0.0684 0.0323  0.0124  264 LEU B CD2 
6297  N N   . GLU B 265 ? 0.7307 0.6880 0.7155 -0.1037 0.0420  0.0453  265 GLU B N   
6298  C CA  . GLU B 265 ? 0.7181 0.6634 0.6926 -0.1172 0.0453  0.0560  265 GLU B CA  
6299  C C   . GLU B 265 ? 0.7629 0.6771 0.7312 -0.1145 0.0374  0.0668  265 GLU B C   
6300  O O   . GLU B 265 ? 0.7683 0.6655 0.7373 -0.1227 0.0376  0.0723  265 GLU B O   
6301  C CB  . GLU B 265 ? 0.6865 0.6445 0.6437 -0.1264 0.0516  0.0616  265 GLU B CB  
6302  C CG  . GLU B 265 ? 0.7394 0.7294 0.7048 -0.1305 0.0614  0.0500  265 GLU B CG  
6303  C CD  . GLU B 265 ? 0.8404 0.8462 0.7869 -0.1387 0.0687  0.0538  265 GLU B CD  
6304  O OE1 . GLU B 265 ? 0.7862 0.8134 0.7333 -0.1325 0.0716  0.0426  265 GLU B OE1 
6305  O OE2 . GLU B 265 ? 0.9510 0.9478 0.8820 -0.1516 0.0717  0.0678  265 GLU B OE2 
6306  N N   . LEU B 266 ? 0.7418 0.6482 0.7061 -0.1028 0.0298  0.0692  266 LEU B N   
6307  C CA  . LEU B 266 ? 0.7665 0.6453 0.7273 -0.0983 0.0218  0.0790  266 LEU B CA  
6308  C C   . LEU B 266 ? 0.7001 0.5678 0.6772 -0.0924 0.0197  0.0720  266 LEU B C   
6309  O O   . LEU B 266 ? 0.7172 0.5615 0.6945 -0.0945 0.0170  0.0773  266 LEU B O   
6310  C CB  . LEU B 266 ? 0.7258 0.6039 0.6804 -0.0874 0.0140  0.0827  266 LEU B CB  
6311  C CG  . LEU B 266 ? 0.7361 0.5897 0.6819 -0.0838 0.0050  0.0968  266 LEU B CG  
6312  C CD1 . LEU B 266 ? 0.7278 0.5632 0.6889 -0.0742 0.0002  0.0944  266 LEU B CD1 
6313  C CD2 . LEU B 266 ? 0.8450 0.6849 0.7741 -0.0973 0.0070  0.1111  266 LEU B CD2 
6314  N N   . TYR B 267 ? 0.7060 0.5900 0.6965 -0.0850 0.0208  0.0600  267 TYR B N   
6315  C CA  . TYR B 267 ? 0.7995 0.6768 0.8027 -0.0801 0.0196  0.0526  267 TYR B CA  
6316  C C   . TYR B 267 ? 0.7399 0.6118 0.7455 -0.0919 0.0236  0.0503  267 TYR B C   
6317  O O   . TYR B 267 ? 0.7335 0.5873 0.7432 -0.0911 0.0211  0.0483  267 TYR B O   
6318  C CB  . TYR B 267 ? 0.7459 0.6438 0.7610 -0.0719 0.0203  0.0424  267 TYR B CB  
6319  C CG  . TYR B 267 ? 0.7506 0.6528 0.7673 -0.0607 0.0157  0.0436  267 TYR B CG  
6320  C CD1 . TYR B 267 ? 0.7176 0.6063 0.7368 -0.0517 0.0104  0.0469  267 TYR B CD1 
6321  C CD2 . TYR B 267 ? 0.6962 0.6165 0.7141 -0.0591 0.0166  0.0404  267 TYR B CD2 
6322  C CE1 . TYR B 267 ? 0.6915 0.5867 0.7149 -0.0425 0.0060  0.0480  267 TYR B CE1 
6323  C CE2 . TYR B 267 ? 0.6558 0.5797 0.6770 -0.0504 0.0117  0.0409  267 TYR B CE2 
6324  C CZ  . TYR B 267 ? 0.7027 0.6148 0.7268 -0.0427 0.0064  0.0451  267 TYR B CZ  
6325  O OH  . TYR B 267 ? 0.6608 0.5790 0.6905 -0.0352 0.0014  0.0455  267 TYR B OH  
6326  N N   . TYR B 268 ? 0.7068 0.5949 0.7110 -0.1032 0.0299  0.0494  268 TYR B N   
6327  C CA  . TYR B 268 ? 0.7969 0.6821 0.8052 -0.1166 0.0335  0.0477  268 TYR B CA  
6328  C C   . TYR B 268 ? 0.7628 0.6186 0.7622 -0.1247 0.0314  0.0591  268 TYR B C   
6329  O O   . TYR B 268 ? 0.7985 0.6373 0.8038 -0.1294 0.0296  0.0562  268 TYR B O   
6330  C CB  . TYR B 268 ? 0.7603 0.6725 0.7707 -0.1269 0.0413  0.0452  268 TYR B CB  
6331  C CG  . TYR B 268 ? 0.7644 0.6751 0.7775 -0.1445 0.0460  0.0473  268 TYR B CG  
6332  C CD1 . TYR B 268 ? 0.7863 0.7006 0.8134 -0.1490 0.0455  0.0376  268 TYR B CD1 
6333  C CD2 . TYR B 268 ? 0.7356 0.6430 0.7370 -0.1577 0.0509  0.0592  268 TYR B CD2 
6334  C CE1 . TYR B 268 ? 0.7187 0.6326 0.7505 -0.1666 0.0492  0.0390  268 TYR B CE1 
6335  C CE2 . TYR B 268 ? 0.7988 0.7058 0.8044 -0.1758 0.0558  0.0623  268 TYR B CE2 
6336  C CZ  . TYR B 268 ? 0.8304 0.7404 0.8524 -0.1804 0.0547  0.0517  268 TYR B CZ  
6337  O OH  . TYR B 268 ? 0.8064 0.7166 0.8345 -0.1996 0.0590  0.0544  268 TYR B OH  
6338  N N   . GLU B 269 ? 0.7214 0.5697 0.7064 -0.1263 0.0306  0.0722  269 GLU B N   
6339  C CA  . GLU B 269 ? 0.7159 0.5351 0.6916 -0.1345 0.0278  0.0863  269 GLU B CA  
6340  C C   . GLU B 269 ? 0.7181 0.5080 0.6980 -0.1230 0.0190  0.0868  269 GLU B C   
6341  O O   . GLU B 269 ? 0.7339 0.4948 0.7114 -0.1287 0.0155  0.0956  269 GLU B O   
6342  C CB  . GLU B 269 ? 0.8414 0.6628 0.7982 -0.1387 0.0284  0.1012  269 GLU B CB  
6343  C CG  . GLU B 269 ? 0.9711 0.8196 0.9221 -0.1526 0.0387  0.1018  269 GLU B CG  
6344  C CD  . GLU B 269 ? 1.1297 0.9904 1.0614 -0.1521 0.0397  0.1105  269 GLU B CD  
6345  O OE1 . GLU B 269 ? 1.1375 1.0280 1.0670 -0.1566 0.0481  0.1043  269 GLU B OE1 
6346  O OE2 . GLU B 269 ? 1.1735 1.0152 1.0925 -0.1465 0.0318  0.1225  269 GLU B OE2 
6347  N N   . LYS B 270 ? 0.7421 0.5388 0.7295 -0.1069 0.0156  0.0776  270 LYS B N   
6348  C CA  . LYS B 270 ? 0.7339 0.5077 0.7277 -0.0946 0.0086  0.0758  270 LYS B CA  
6349  C C   . LYS B 270 ? 0.7116 0.4873 0.7188 -0.0910 0.0099  0.0595  270 LYS B C   
6350  O O   . LYS B 270 ? 0.7304 0.4953 0.7443 -0.0785 0.0059  0.0537  270 LYS B O   
6351  C CB  . LYS B 270 ? 0.6765 0.4565 0.6693 -0.0794 0.0036  0.0787  270 LYS B CB  
6352  C CG  . LYS B 270 ? 0.7401 0.5204 0.7175 -0.0829 0.0012  0.0938  270 LYS B CG  
6353  C CD  . LYS B 270 ? 0.7757 0.5242 0.7469 -0.0823 -0.0064 0.1084  270 LYS B CD  
6354  C CE  . LYS B 270 ? 0.8462 0.5977 0.7994 -0.0852 -0.0099 0.1243  270 LYS B CE  
6355  N NZ  . LYS B 270 ? 0.9287 0.6641 0.8675 -0.1013 -0.0084 0.1398  270 LYS B NZ  
6356  N N   . GLY B 271 ? 0.6395 0.4304 0.6505 -0.1018 0.0153  0.0516  271 GLY B N   
6357  C CA  . GLY B 271 ? 0.6959 0.4858 0.7167 -0.1018 0.0154  0.0372  271 GLY B CA  
6358  C C   . GLY B 271 ? 0.7233 0.5405 0.7506 -0.0931 0.0171  0.0253  271 GLY B C   
6359  O O   . GLY B 271 ? 0.8441 0.6632 0.8773 -0.0928 0.0168  0.0131  271 GLY B O   
6360  N N   . ILE B 272 ? 0.6778 0.5154 0.7037 -0.0866 0.0184  0.0285  272 ILE B N   
6361  C CA  . ILE B 272 ? 0.7341 0.5943 0.7666 -0.0776 0.0191  0.0198  272 ILE B CA  
6362  C C   . ILE B 272 ? 0.7151 0.5982 0.7524 -0.0862 0.0225  0.0139  272 ILE B C   
6363  O O   . ILE B 272 ? 0.7430 0.6378 0.7789 -0.0934 0.0258  0.0184  272 ILE B O   
6364  C CB  . ILE B 272 ? 0.7346 0.6047 0.7662 -0.0673 0.0179  0.0253  272 ILE B CB  
6365  C CG1 . ILE B 272 ? 0.7342 0.5831 0.7623 -0.0598 0.0136  0.0327  272 ILE B CG1 
6366  C CG2 . ILE B 272 ? 0.5658 0.4549 0.6050 -0.0582 0.0181  0.0181  272 ILE B CG2 
6367  C CD1 . ILE B 272 ? 0.6168 0.4558 0.6512 -0.0495 0.0115  0.0258  272 ILE B CD1 
6368  N N   . ASN B 273 ? 0.6619 0.5537 0.7050 -0.0847 0.0217  0.0034  273 ASN B N   
6369  C CA  . ASN B 273 ? 0.6115 0.5268 0.6613 -0.0913 0.0232  -0.0024 273 ASN B CA  
6370  C C   . ASN B 273 ? 0.6492 0.5885 0.7040 -0.0826 0.0232  -0.0028 273 ASN B C   
6371  O O   . ASN B 273 ? 0.7807 0.7404 0.8426 -0.0870 0.0245  -0.0050 273 ASN B O   
6372  C CB  . ASN B 273 ? 0.7171 0.6320 0.7700 -0.0949 0.0207  -0.0136 273 ASN B CB  
6373  C CG  . ASN B 273 ? 0.7964 0.6831 0.8460 -0.1020 0.0194  -0.0156 273 ASN B CG  
6374  O OD1 . ASN B 273 ? 0.8127 0.6905 0.8618 -0.0995 0.0166  -0.0255 273 ASN B OD1 
6375  N ND2 . ASN B 273 ? 0.6894 0.5615 0.7363 -0.1108 0.0213  -0.0063 273 ASN B ND2 
6376  N N   . MET B 274 ? 0.7208 0.6587 0.7743 -0.0707 0.0216  -0.0006 274 MET B N   
6377  C CA  . MET B 274 ? 0.6399 0.5979 0.6995 -0.0633 0.0208  -0.0006 274 MET B CA  
6378  C C   . MET B 274 ? 0.6192 0.5727 0.6777 -0.0538 0.0200  0.0057  274 MET B C   
6379  O O   . MET B 274 ? 0.6351 0.5741 0.6897 -0.0491 0.0192  0.0074  274 MET B O   
6380  C CB  . MET B 274 ? 0.6784 0.6468 0.7403 -0.0599 0.0184  -0.0069 274 MET B CB  
6381  C CG  . MET B 274 ? 0.7052 0.6941 0.7742 -0.0540 0.0166  -0.0050 274 MET B CG  
6382  S SD  . MET B 274 ? 0.7508 0.7385 0.8189 -0.0421 0.0159  0.0005  274 MET B SD  
6383  C CE  . MET B 274 ? 0.6505 0.6481 0.7142 -0.0400 0.0141  -0.0048 274 MET B CE  
6384  N N   . LEU B 275 ? 0.5220 0.4885 0.5858 -0.0510 0.0199  0.0082  275 LEU B N   
6385  C CA  . LEU B 275 ? 0.5329 0.4988 0.5987 -0.0427 0.0182  0.0130  275 LEU B CA  
6386  C C   . LEU B 275 ? 0.6703 0.6532 0.7460 -0.0389 0.0167  0.0124  275 LEU B C   
6387  O O   . LEU B 275 ? 0.5800 0.5749 0.6606 -0.0415 0.0167  0.0087  275 LEU B O   
6388  C CB  . LEU B 275 ? 0.5426 0.5000 0.6029 -0.0442 0.0182  0.0175  275 LEU B CB  
6389  C CG  . LEU B 275 ? 0.7176 0.6829 0.7762 -0.0508 0.0208  0.0164  275 LEU B CG  
6390  C CD1 . LEU B 275 ? 0.7142 0.6938 0.7813 -0.0460 0.0198  0.0141  275 LEU B CD1 
6391  C CD2 . LEU B 275 ? 0.7088 0.6610 0.7555 -0.0548 0.0212  0.0220  275 LEU B CD2 
6392  N N   . ALA B 276 ? 0.6391 0.6225 0.7193 -0.0328 0.0147  0.0163  276 ALA B N   
6393  C CA  . ALA B 276 ? 0.6608 0.6560 0.7517 -0.0285 0.0123  0.0173  276 ALA B CA  
6394  C C   . ALA B 276 ? 0.5253 0.5187 0.6212 -0.0255 0.0103  0.0192  276 ALA B C   
6395  O O   . ALA B 276 ? 0.5993 0.5842 0.6914 -0.0242 0.0095  0.0220  276 ALA B O   
6396  C CB  . ALA B 276 ? 0.5704 0.5690 0.6633 -0.0242 0.0112  0.0209  276 ALA B CB  
6397  N N   . THR B 277 ? 0.4521 0.4537 0.5578 -0.0239 0.0085  0.0170  277 THR B N   
6398  C CA  . THR B 277 ? 0.5723 0.5718 0.6838 -0.0212 0.0058  0.0164  277 THR B CA  
6399  C C   . THR B 277 ? 0.4716 0.4766 0.5984 -0.0168 0.0019  0.0176  277 THR B C   
6400  O O   . THR B 277 ? 0.4528 0.4637 0.5839 -0.0155 0.0011  0.0208  277 THR B O   
6401  C CB  . THR B 277 ? 0.5322 0.5326 0.6375 -0.0247 0.0081  0.0099  277 THR B CB  
6402  O OG1 . THR B 277 ? 0.6133 0.6116 0.7222 -0.0222 0.0048  0.0074  277 THR B OG1 
6403  C CG2 . THR B 277 ? 0.4914 0.5037 0.6023 -0.0261 0.0108  0.0037  277 THR B CG2 
6404  N N   . ASP B 278 ? 0.5408 0.5431 0.6757 -0.0145 -0.0013 0.0152  278 ASP B N   
6405  C CA  . ASP B 278 ? 0.6159 0.6188 0.7672 -0.0103 -0.0062 0.0172  278 ASP B CA  
6406  C C   . ASP B 278 ? 0.6328 0.6430 0.7932 -0.0076 -0.0066 0.0096  278 ASP B C   
6407  O O   . ASP B 278 ? 0.5353 0.5513 0.6902 -0.0094 -0.0025 0.0010  278 ASP B O   
6408  C CB  . ASP B 278 ? 0.5815 0.5766 0.7398 -0.0095 -0.0105 0.0167  278 ASP B CB  
6409  C CG  . ASP B 278 ? 0.6433 0.6352 0.8195 -0.0065 -0.0160 0.0218  278 ASP B CG  
6410  O OD1 . ASP B 278 ? 0.7031 0.6983 0.8821 -0.0058 -0.0162 0.0311  278 ASP B OD1 
6411  O OD2 . ASP B 278 ? 0.6312 0.6170 0.8182 -0.0052 -0.0205 0.0167  278 ASP B OD2 
6412  N N   . GLU B 279 ? 0.5732 0.5840 0.7489 -0.0030 -0.0115 0.0135  279 GLU B N   
6413  C CA  . GLU B 279 ? 0.6605 0.6791 0.8486 0.0015  -0.0129 0.0062  279 GLU B CA  
6414  C C   . GLU B 279 ? 0.6537 0.6687 0.8504 0.0047  -0.0140 -0.0056 279 GLU B C   
6415  O O   . GLU B 279 ? 0.6377 0.6615 0.8436 0.0087  -0.0130 -0.0156 279 GLU B O   
6416  C CB  . GLU B 279 ? 0.6460 0.6659 0.8478 0.0063  -0.0192 0.0153  279 GLU B CB  
6417  C CG  . GLU B 279 ? 0.6617 0.6691 0.8730 0.0077  -0.0251 0.0255  279 GLU B CG  
6418  C CD  . GLU B 279 ? 0.7858 0.7943 1.0107 0.0125  -0.0320 0.0356  279 GLU B CD  
6419  O OE1 . GLU B 279 ? 0.8357 0.8512 1.0717 0.0182  -0.0347 0.0298  279 GLU B OE1 
6420  O OE2 . GLU B 279 ? 0.7641 0.7678 0.9889 0.0107  -0.0349 0.0500  279 GLU B OE2 
6421  N N   . VAL B 280 ? 0.5807 0.5847 0.7750 0.0030  -0.0159 -0.0060 280 VAL B N   
6422  C CA  . VAL B 280 ? 0.6391 0.6405 0.8378 0.0052  -0.0167 -0.0198 280 VAL B CA  
6423  C C   . VAL B 280 ? 0.6522 0.6649 0.8361 0.0023  -0.0091 -0.0304 280 VAL B C   
6424  O O   . VAL B 280 ? 0.6861 0.7048 0.8748 0.0055  -0.0074 -0.0443 280 VAL B O   
6425  C CB  . VAL B 280 ? 0.6607 0.6498 0.8586 0.0025  -0.0213 -0.0181 280 VAL B CB  
6426  C CG1 . VAL B 280 ? 0.5889 0.5792 0.7661 -0.0036 -0.0175 -0.0146 280 VAL B CG1 
6427  C CG2 . VAL B 280 ? 0.6592 0.6441 0.8656 0.0058  -0.0245 -0.0333 280 VAL B CG2 
6428  N N   . ILE B 281 ? 0.6367 0.6528 0.8031 -0.0039 -0.0041 -0.0241 281 ILE B N   
6429  C CA  . ILE B 281 ? 0.5918 0.6181 0.7438 -0.0085 0.0034  -0.0310 281 ILE B CA  
6430  C C   . ILE B 281 ? 0.6899 0.7315 0.8514 -0.0068 0.0075  -0.0362 281 ILE B C   
6431  O O   . ILE B 281 ? 0.7239 0.7781 0.8845 -0.0073 0.0131  -0.0473 281 ILE B O   
6432  C CB  . ILE B 281 ? 0.4808 0.5023 0.6136 -0.0156 0.0062  -0.0215 281 ILE B CB  
6433  C CG1 . ILE B 281 ? 0.6431 0.6523 0.7694 -0.0161 0.0015  -0.0172 281 ILE B CG1 
6434  C CG2 . ILE B 281 ? 0.5359 0.5658 0.6535 -0.0219 0.0137  -0.0257 281 ILE B CG2 
6435  C CD1 . ILE B 281 ? 0.6839 0.6925 0.8117 -0.0141 -0.0014 -0.0279 281 ILE B CD1 
6436  N N   . LEU B 282 ? 0.5605 0.6038 0.7316 -0.0048 0.0046  -0.0285 282 LEU B N   
6437  C CA  . LEU B 282 ? 0.5731 0.6331 0.7555 -0.0030 0.0067  -0.0328 282 LEU B CA  
6438  C C   . LEU B 282 ? 0.6183 0.6852 0.8209 0.0059  0.0048  -0.0443 282 LEU B C   
6439  O O   . LEU B 282 ? 0.6532 0.7378 0.8622 0.0066  0.0103  -0.0548 282 LEU B O   
6440  C CB  . LEU B 282 ? 0.5438 0.6039 0.7308 -0.0023 0.0020  -0.0217 282 LEU B CB  
6441  C CG  . LEU B 282 ? 0.5052 0.5831 0.7069 0.0006  0.0011  -0.0247 282 LEU B CG  
6442  C CD1 . LEU B 282 ? 0.4813 0.5726 0.6736 -0.0083 0.0088  -0.0289 282 LEU B CD1 
6443  C CD2 . LEU B 282 ? 0.4869 0.5628 0.6936 0.0035  -0.0067 -0.0130 282 LEU B CD2 
6444  N N   . LYS B 283 ? 0.5486 0.6021 0.7631 0.0126  -0.0028 -0.0431 283 LYS B N   
6445  C CA  . LYS B 283 ? 0.6234 0.6797 0.8591 0.0223  -0.0056 -0.0552 283 LYS B CA  
6446  C C   . LYS B 283 ? 0.5899 0.6525 0.8191 0.0217  0.0010  -0.0721 283 LYS B C   
6447  O O   . LYS B 283 ? 0.5013 0.5768 0.7451 0.0285  0.0035  -0.0864 283 LYS B O   
6448  C CB  . LYS B 283 ? 0.5816 0.6184 0.8314 0.0281  -0.0158 -0.0492 283 LYS B CB  
6449  C CG  . LYS B 283 ? 0.6018 0.6326 0.8534 0.0272  -0.0217 -0.0305 283 LYS B CG  
6450  C CD  . LYS B 283 ? 0.5529 0.5938 0.8232 0.0348  -0.0263 -0.0282 283 LYS B CD  
6451  C CE  . LYS B 283 ? 0.6125 0.6574 0.8746 0.0308  -0.0285 -0.0118 283 LYS B CE  
6452  N NZ  . LYS B 283 ? 0.6665 0.7179 0.9478 0.0390  -0.0367 -0.0062 283 LYS B NZ  
6453  N N   . ASN B 284 ? 0.6321 0.6876 0.8394 0.0141  0.0038  -0.0709 284 ASN B N   
6454  C CA  . ASN B 284 ? 0.5925 0.6550 0.7884 0.0123  0.0098  -0.0856 284 ASN B CA  
6455  C C   . ASN B 284 ? 0.6469 0.7313 0.8324 0.0066  0.0210  -0.0899 284 ASN B C   
6456  O O   . ASN B 284 ? 0.5973 0.6965 0.7821 0.0081  0.0276  -0.1052 284 ASN B O   
6457  C CB  . ASN B 284 ? 0.5407 0.5891 0.7164 0.0060  0.0074  -0.0807 284 ASN B CB  
6458  C CG  . ASN B 284 ? 0.6893 0.7202 0.8767 0.0108  -0.0023 -0.0826 284 ASN B CG  
6459  O OD1 . ASN B 284 ? 0.8061 0.8319 1.0165 0.0185  -0.0076 -0.0850 284 ASN B OD1 
6460  N ND2 . ASN B 284 ? 0.6307 0.6521 0.8038 0.0060  -0.0054 -0.0810 284 ASN B ND2 
6461  N N   . SER B 285 ? 0.6148 0.7022 0.7921 -0.0006 0.0236  -0.0773 285 SER B N   
6462  C CA  . SER B 285 ? 0.6140 0.7202 0.7811 -0.0088 0.0340  -0.0793 285 SER B CA  
6463  C C   . SER B 285 ? 0.6102 0.7377 0.7987 -0.0054 0.0370  -0.0844 285 SER B C   
6464  O O   . SER B 285 ? 0.6240 0.7734 0.8126 -0.0091 0.0466  -0.0931 285 SER B O   
6465  C CB  . SER B 285 ? 0.6874 0.7841 0.8343 -0.0195 0.0351  -0.0642 285 SER B CB  
6466  O OG  . SER B 285 ? 0.5900 0.6660 0.7236 -0.0201 0.0294  -0.0569 285 SER B OG  
6467  N N   . VAL B 286 ? 0.6377 0.7611 0.8446 0.0013  0.0288  -0.0787 286 VAL B N   
6468  C CA  . VAL B 286 ? 0.6210 0.7650 0.8498 0.0053  0.0290  -0.0819 286 VAL B CA  
6469  C C   . VAL B 286 ? 0.6114 0.7540 0.8665 0.0201  0.0212  -0.0888 286 VAL B C   
6470  O O   . VAL B 286 ? 0.6495 0.7702 0.9064 0.0253  0.0126  -0.0833 286 VAL B O   
6471  C CB  . VAL B 286 ? 0.5922 0.7348 0.8188 -0.0003 0.0250  -0.0680 286 VAL B CB  
6472  C CG1 . VAL B 286 ? 0.5335 0.7027 0.7801 0.0008  0.0263  -0.0726 286 VAL B CG1 
6473  C CG2 . VAL B 286 ? 0.5701 0.7044 0.7706 -0.0136 0.0302  -0.0600 286 VAL B CG2 
6474  N N   . GLU B 287 ? 0.7147 0.8810 0.9922 0.0267  0.0240  -0.1002 287 GLU B N   
6475  C CA  . GLU B 287 ? 0.7590 0.9261 1.0642 0.0423  0.0180  -0.1107 287 GLU B CA  
6476  C C   . GLU B 287 ? 0.7702 0.9157 1.0870 0.0499  0.0036  -0.0977 287 GLU B C   
6477  O O   . GLU B 287 ? 0.9200 1.0411 1.2334 0.0527  -0.0021 -0.0953 287 GLU B O   
6478  C CB  . GLU B 287 ? 0.7271 0.9267 1.0573 0.0482  0.0224  -0.1222 287 GLU B CB  
6479  C CG  . GLU B 287 ? 0.8904 1.1077 1.2216 0.0400  0.0229  -0.1120 287 GLU B CG  
6480  C CD  . GLU B 287 ? 1.1449 1.3905 1.5097 0.0498  0.0204  -0.1194 287 GLU B CD  
6481  O OE1 . GLU B 287 ? 1.0860 1.3256 1.4746 0.0651  0.0102  -0.1213 287 GLU B OE1 
6482  O OE2 . GLU B 287 ? 1.1587 1.4325 1.5275 0.0421  0.0282  -0.1227 287 GLU B OE2 
6483  N N   . ARG B 288 ? 0.6941 0.8496 1.0252 0.0529  -0.0027 -0.0889 288 ARG B N   
6484  C CA  . ARG B 288 ? 0.7420 0.8800 1.0824 0.0593  -0.0163 -0.0741 288 ARG B CA  
6485  C C   . ARG B 288 ? 0.7701 0.9109 1.0954 0.0499  -0.0186 -0.0578 288 ARG B C   
6486  O O   . ARG B 288 ? 0.6796 0.8314 1.0175 0.0538  -0.0260 -0.0508 288 ARG B O   
6487  C CB  . ARG B 288 ? 0.6724 0.8191 1.0470 0.0751  -0.0244 -0.0798 288 ARG B CB  
6488  C CG  . ARG B 288 ? 0.7473 0.8920 1.1388 0.0857  -0.0217 -0.0995 288 ARG B CG  
6489  C CD  . ARG B 288 ? 0.6880 0.8516 1.1158 0.1014  -0.0262 -0.1099 288 ARG B CD  
6490  N NE  . ARG B 288 ? 0.7106 0.8536 1.1596 0.1138  -0.0418 -0.0998 288 ARG B NE  
6491  C CZ  . ARG B 288 ? 0.6583 0.7943 1.1358 0.1295  -0.0473 -0.1121 288 ARG B CZ  
6492  N NH1 . ARG B 288 ? 0.5947 0.7450 1.0828 0.1356  -0.0378 -0.1369 288 ARG B NH1 
6493  N NH2 . ARG B 288 ? 0.6224 0.7360 1.1179 0.1393  -0.0626 -0.0993 288 ARG B NH2 
6494  N N   . ALA B 289 ? 0.7842 0.9156 1.0819 0.0376  -0.0125 -0.0526 289 ALA B N   
6495  C CA  . ALA B 289 ? 0.7326 0.8664 1.0140 0.0280  -0.0129 -0.0407 289 ALA B CA  
6496  C C   . ALA B 289 ? 0.6948 0.8102 0.9707 0.0297  -0.0224 -0.0242 289 ALA B C   
6497  O O   . ALA B 289 ? 0.5957 0.6922 0.8749 0.0346  -0.0268 -0.0202 289 ALA B O   
6498  C CB  . ALA B 289 ? 0.5426 0.6729 0.7986 0.0152  -0.0026 -0.0423 289 ALA B CB  
6499  N N   . SER B 290 ? 0.6335 0.7557 0.9010 0.0249  -0.0254 -0.0150 290 SER B N   
6500  C CA  . SER B 290 ? 0.5899 0.6985 0.8475 0.0245  -0.0323 0.0008  290 SER B CA  
6501  C C   . SER B 290 ? 0.5960 0.6968 0.8274 0.0136  -0.0260 0.0046  290 SER B C   
6502  O O   . SER B 290 ? 0.5933 0.7039 0.8155 0.0060  -0.0201 -0.0014 290 SER B O   
6503  C CB  . SER B 290 ? 0.5838 0.7060 0.8497 0.0284  -0.0420 0.0091  290 SER B CB  
6504  O OG  . SER B 290 ? 0.6740 0.7898 0.9206 0.0232  -0.0446 0.0222  290 SER B OG  
6505  N N   . PRO B 291 ? 0.4965 0.5799 0.7170 0.0126  -0.0271 0.0144  291 PRO B N   
6506  C CA  . PRO B 291 ? 0.5507 0.6274 0.7487 0.0042  -0.0217 0.0178  291 PRO B CA  
6507  C C   . PRO B 291 ? 0.5878 0.6726 0.7752 0.0011  -0.0246 0.0247  291 PRO B C   
6508  O O   . PRO B 291 ? 0.6847 0.7629 0.8548 -0.0040 -0.0211 0.0281  291 PRO B O   
6509  C CB  . PRO B 291 ? 0.5627 0.6215 0.7586 0.0056  -0.0224 0.0252  291 PRO B CB  
6510  C CG  . PRO B 291 ? 0.6331 0.6904 0.8458 0.0132  -0.0313 0.0333  291 PRO B CG  
6511  C CD  . PRO B 291 ? 0.5423 0.6115 0.7729 0.0191  -0.0335 0.0230  291 PRO B CD  
6512  N N   . TYR B 292 ? 0.4899 0.5898 0.6874 0.0045  -0.0314 0.0261  292 TYR B N   
6513  C CA  . TYR B 292 ? 0.5532 0.6628 0.7395 0.0018  -0.0358 0.0320  292 TYR B CA  
6514  C C   . TYR B 292 ? 0.5960 0.7207 0.7795 -0.0048 -0.0337 0.0214  292 TYR B C   
6515  O O   . TYR B 292 ? 0.5958 0.7349 0.7777 -0.0057 -0.0401 0.0230  292 TYR B O   
6516  C CB  . TYR B 292 ? 0.5319 0.6484 0.7295 0.0095  -0.0470 0.0432  292 TYR B CB  
6517  C CG  . TYR B 292 ? 0.5027 0.6028 0.7052 0.0145  -0.0496 0.0550  292 TYR B CG  
6518  C CD1 . TYR B 292 ? 0.5463 0.6331 0.7337 0.0102  -0.0442 0.0612  292 TYR B CD1 
6519  C CD2 . TYR B 292 ? 0.5749 0.6726 0.7993 0.0235  -0.0575 0.0594  292 TYR B CD2 
6520  C CE1 . TYR B 292 ? 0.5943 0.6671 0.7882 0.0130  -0.0465 0.0722  292 TYR B CE1 
6521  C CE2 . TYR B 292 ? 0.6453 0.7256 0.8758 0.0268  -0.0604 0.0703  292 TYR B CE2 
6522  C CZ  . TYR B 292 ? 0.6129 0.6813 0.8279 0.0207  -0.0548 0.0769  292 TYR B CZ  
6523  O OH  . TYR B 292 ? 0.6907 0.7430 0.9137 0.0223  -0.0577 0.0880  292 TYR B OH  
6524  N N   . LEU B 293 ? 0.5820 0.7037 0.7643 -0.0104 -0.0251 0.0111  293 LEU B N   
6525  C CA  . LEU B 293 ? 0.5197 0.6536 0.7011 -0.0188 -0.0218 0.0013  293 LEU B CA  
6526  C C   . LEU B 293 ? 0.5306 0.6493 0.6955 -0.0273 -0.0127 -0.0025 293 LEU B C   
6527  O O   . LEU B 293 ? 0.6408 0.7439 0.8005 -0.0256 -0.0083 -0.0003 293 LEU B O   
6528  C CB  . LEU B 293 ? 0.5306 0.6811 0.7337 -0.0170 -0.0206 -0.0071 293 LEU B CB  
6529  C CG  . LEU B 293 ? 0.5113 0.6778 0.7362 -0.0068 -0.0303 -0.0048 293 LEU B CG  
6530  C CD1 . LEU B 293 ? 0.5831 0.7404 0.8212 0.0034  -0.0305 -0.0037 293 LEU B CD1 
6531  C CD2 . LEU B 293 ? 0.5778 0.7709 0.8205 -0.0095 -0.0308 -0.0144 293 LEU B CD2 
6532  N N   . ARG B 294 ? 0.5594 0.6825 0.7173 -0.0366 -0.0108 -0.0082 294 ARG B N   
6533  C CA  . ARG B 294 ? 0.5901 0.6984 0.7352 -0.0452 -0.0028 -0.0118 294 ARG B CA  
6534  C C   . ARG B 294 ? 0.5745 0.6894 0.7292 -0.0497 0.0037  -0.0175 294 ARG B C   
6535  O O   . ARG B 294 ? 0.5651 0.7005 0.7347 -0.0520 0.0029  -0.0228 294 ARG B O   
6536  C CB  . ARG B 294 ? 0.5965 0.7042 0.7313 -0.0539 -0.0038 -0.0161 294 ARG B CB  
6537  C CG  . ARG B 294 ? 0.6137 0.7047 0.7382 -0.0632 0.0034  -0.0193 294 ARG B CG  
6538  C CD  . ARG B 294 ? 0.7930 0.8854 0.9138 -0.0740 0.0021  -0.0264 294 ARG B CD  
6539  N NE  . ARG B 294 ? 0.7990 0.8920 0.9108 -0.0715 -0.0041 -0.0280 294 ARG B NE  
6540  C CZ  . ARG B 294 ? 0.6927 0.8030 0.8087 -0.0752 -0.0107 -0.0335 294 ARG B CZ  
6541  N NH1 . ARG B 294 ? 0.7673 0.8978 0.9000 -0.0802 -0.0126 -0.0372 294 ARG B NH1 
6542  N NH2 . ARG B 294 ? 0.7377 0.8472 0.8410 -0.0735 -0.0155 -0.0359 294 ARG B NH2 
6543  N N   . TYR B 295 ? 0.5142 0.6140 0.6605 -0.0507 0.0100  -0.0162 295 TYR B N   
6544  C CA  . TYR B 295 ? 0.5066 0.6124 0.6572 -0.0557 0.0173  -0.0208 295 TYR B CA  
6545  C C   . TYR B 295 ? 0.5261 0.6198 0.6626 -0.0679 0.0231  -0.0205 295 TYR B C   
6546  O O   . TYR B 295 ? 0.5402 0.6132 0.6619 -0.0685 0.0225  -0.0161 295 TYR B O   
6547  C CB  . TYR B 295 ? 0.4626 0.5620 0.6137 -0.0479 0.0192  -0.0199 295 TYR B CB  
6548  C CG  . TYR B 295 ? 0.5205 0.6319 0.6899 -0.0367 0.0140  -0.0217 295 TYR B CG  
6549  C CD1 . TYR B 295 ? 0.5335 0.6385 0.7051 -0.0287 0.0061  -0.0151 295 TYR B CD1 
6550  C CD2 . TYR B 295 ? 0.4818 0.6115 0.6674 -0.0342 0.0170  -0.0299 295 TYR B CD2 
6551  C CE1 . TYR B 295 ? 0.5248 0.6378 0.7142 -0.0185 0.0002  -0.0150 295 TYR B CE1 
6552  C CE2 . TYR B 295 ? 0.5780 0.7165 0.7828 -0.0227 0.0113  -0.0321 295 TYR B CE2 
6553  C CZ  . TYR B 295 ? 0.5689 0.6974 0.7756 -0.0149 0.0023  -0.0238 295 TYR B CZ  
6554  O OH  . TYR B 295 ? 0.5453 0.6796 0.7719 -0.0036 -0.0044 -0.0242 295 TYR B OH  
6555  N N   . TYR B 296 ? 0.5483 0.6556 0.6909 -0.0775 0.0287  -0.0249 296 TYR B N   
6556  C CA  . TYR B 296 ? 0.5861 0.6820 0.7169 -0.0907 0.0347  -0.0230 296 TYR B CA  
6557  C C   . TYR B 296 ? 0.6467 0.7467 0.7742 -0.0930 0.0429  -0.0224 296 TYR B C   
6558  O O   . TYR B 296 ? 0.7069 0.8309 0.8476 -0.0948 0.0476  -0.0281 296 TYR B O   
6559  C CB  . TYR B 296 ? 0.5591 0.6680 0.6987 -0.1031 0.0352  -0.0273 296 TYR B CB  
6560  C CG  . TYR B 296 ? 0.6774 0.7749 0.8121 -0.1052 0.0283  -0.0282 296 TYR B CG  
6561  C CD1 . TYR B 296 ? 0.7271 0.7965 0.8447 -0.1043 0.0270  -0.0241 296 TYR B CD1 
6562  C CD2 . TYR B 296 ? 0.8049 0.9215 0.9526 -0.1077 0.0227  -0.0343 296 TYR B CD2 
6563  C CE1 . TYR B 296 ? 0.7620 0.8220 0.8747 -0.1055 0.0215  -0.0273 296 TYR B CE1 
6564  C CE2 . TYR B 296 ? 0.7652 0.8725 0.9062 -0.1098 0.0162  -0.0370 296 TYR B CE2 
6565  C CZ  . TYR B 296 ? 0.8275 0.9063 0.9506 -0.1086 0.0162  -0.0341 296 TYR B CZ  
6566  O OH  . TYR B 296 ? 0.9682 1.0383 1.0841 -0.1099 0.0105  -0.0390 296 TYR B OH  
6567  N N   . PHE B 297 ? 0.5146 0.5930 0.6245 -0.0928 0.0445  -0.0161 297 PHE B N   
6568  C CA  . PHE B 297 ? 0.4995 0.5801 0.6008 -0.0958 0.0515  -0.0147 297 PHE B CA  
6569  C C   . PHE B 297 ? 0.5644 0.6488 0.6612 -0.1121 0.0589  -0.0120 297 PHE B C   
6570  O O   . PHE B 297 ? 0.6217 0.6851 0.7071 -0.1202 0.0579  -0.0049 297 PHE B O   
6571  C CB  . PHE B 297 ? 0.5611 0.6179 0.6454 -0.0903 0.0486  -0.0079 297 PHE B CB  
6572  C CG  . PHE B 297 ? 0.5361 0.5950 0.6086 -0.0920 0.0539  -0.0066 297 PHE B CG  
6573  C CD1 . PHE B 297 ? 0.5635 0.6369 0.6423 -0.0835 0.0549  -0.0142 297 PHE B CD1 
6574  C CD2 . PHE B 297 ? 0.5199 0.5652 0.5741 -0.1016 0.0571  0.0022  297 PHE B CD2 
6575  C CE1 . PHE B 297 ? 0.6413 0.7179 0.7070 -0.0850 0.0594  -0.0148 297 PHE B CE1 
6576  C CE2 . PHE B 297 ? 0.5824 0.6312 0.6226 -0.1033 0.0613  0.0041  297 PHE B CE2 
6577  C CZ  . PHE B 297 ? 0.5684 0.6339 0.6136 -0.0951 0.0627  -0.0053 297 PHE B CZ  
6578  N N   . ARG B 298 ? 0.5831 0.6945 0.6900 -0.1171 0.0666  -0.0175 298 ARG B N   
6579  C CA  . ARG B 298 ? 0.5338 0.6539 0.6372 -0.1341 0.0758  -0.0142 298 ARG B CA  
6580  C C   . ARG B 298 ? 0.5983 0.7075 0.7045 -0.1463 0.0731  -0.0106 298 ARG B C   
6581  O O   . ARG B 298 ? 0.7361 0.8362 0.8331 -0.1612 0.0779  -0.0029 298 ARG B O   
6582  C CB  . ARG B 298 ? 0.4821 0.5885 0.5619 -0.1390 0.0808  -0.0052 298 ARG B CB  
6583  C CG  . ARG B 298 ? 0.5508 0.6668 0.6253 -0.1279 0.0829  -0.0104 298 ARG B CG  
6584  C CD  . ARG B 298 ? 0.4988 0.6096 0.5494 -0.1353 0.0890  -0.0024 298 ARG B CD  
6585  N NE  . ARG B 298 ? 0.6149 0.7337 0.6598 -0.1241 0.0893  -0.0095 298 ARG B NE  
6586  C CZ  . ARG B 298 ? 0.7207 0.8269 0.7425 -0.1236 0.0884  -0.0034 298 ARG B CZ  
6587  N NH1 . ARG B 298 ? 0.5827 0.6688 0.5847 -0.1335 0.0877  0.0115  298 ARG B NH1 
6588  N NH2 . ARG B 298 ? 0.7523 0.8654 0.7716 -0.1126 0.0870  -0.0125 298 ARG B NH2 
6589  N N   . GLU B 299 ? 0.5357 0.6451 0.6541 -0.1403 0.0648  -0.0159 299 GLU B N   
6590  C CA  . GLU B 299 ? 0.6803 0.7803 0.8023 -0.1506 0.0607  -0.0159 299 GLU B CA  
6591  C C   . GLU B 299 ? 0.6911 0.7537 0.7937 -0.1541 0.0579  -0.0072 299 GLU B C   
6592  O O   . GLU B 299 ? 0.7595 0.8085 0.8628 -0.1633 0.0546  -0.0075 299 GLU B O   
6593  C CB  . GLU B 299 ? 0.7945 0.9161 0.9294 -0.1681 0.0676  -0.0176 299 GLU B CB  
6594  C CG  . GLU B 299 ? 0.9056 1.0671 1.0595 -0.1657 0.0740  -0.0252 299 GLU B CG  
6595  C CD  . GLU B 299 ? 0.9257 1.1133 1.1049 -0.1670 0.0691  -0.0345 299 GLU B CD  
6596  O OE1 . GLU B 299 ? 0.9031 1.0782 1.0829 -0.1722 0.0614  -0.0353 299 GLU B OE1 
6597  O OE2 . GLU B 299 ? 0.8530 1.0748 1.0520 -0.1633 0.0730  -0.0418 299 GLU B OE2 
6598  N N   . LEU B 300 ? 0.7009 0.7467 0.7872 -0.1464 0.0583  -0.0004 300 LEU B N   
6599  C CA  . LEU B 300 ? 0.7337 0.7451 0.8034 -0.1482 0.0553  0.0085  300 LEU B CA  
6600  C C   . LEU B 300 ? 0.6491 0.6431 0.7157 -0.1340 0.0469  0.0064  300 LEU B C   
6601  O O   . LEU B 300 ? 0.6578 0.6269 0.7186 -0.1356 0.0429  0.0085  300 LEU B O   
6602  C CB  . LEU B 300 ? 0.6697 0.6738 0.7229 -0.1497 0.0599  0.0186  300 LEU B CB  
6603  C CG  . LEU B 300 ? 0.6548 0.6702 0.7053 -0.1671 0.0693  0.0244  300 LEU B CG  
6604  C CD1 . LEU B 300 ? 0.7028 0.7002 0.7312 -0.1705 0.0712  0.0380  300 LEU B CD1 
6605  C CD2 . LEU B 300 ? 0.6207 0.6311 0.6807 -0.1828 0.0696  0.0244  300 LEU B CD2 
6606  N N   . ILE B 301 ? 0.6365 0.6431 0.7078 -0.1202 0.0444  0.0022  301 ILE B N   
6607  C CA  . ILE B 301 ? 0.6569 0.6502 0.7250 -0.1072 0.0380  0.0018  301 ILE B CA  
6608  C C   . ILE B 301 ? 0.6197 0.6339 0.7006 -0.0980 0.0348  -0.0051 301 ILE B C   
6609  O O   . ILE B 301 ? 0.7217 0.7591 0.8138 -0.0990 0.0372  -0.0092 301 ILE B O   
6610  C CB  . ILE B 301 ? 0.6183 0.5977 0.6747 -0.0992 0.0373  0.0090  301 ILE B CB  
6611  C CG1 . ILE B 301 ? 0.7116 0.6706 0.7634 -0.0904 0.0317  0.0107  301 ILE B CG1 
6612  C CG2 . ILE B 301 ? 0.6005 0.5977 0.6620 -0.0905 0.0378  0.0065  301 ILE B CG2 
6613  C CD1 . ILE B 301 ? 0.7208 0.6663 0.7629 -0.0838 0.0301  0.0183  301 ILE B CD1 
6614  N N   . SER B 302 ? 0.5534 0.5598 0.6329 -0.0889 0.0295  -0.0060 302 SER B N   
6615  C CA  . SER B 302 ? 0.5761 0.5990 0.6653 -0.0800 0.0253  -0.0095 302 SER B CA  
6616  C C   . SER B 302 ? 0.5898 0.6077 0.6767 -0.0683 0.0236  -0.0050 302 SER B C   
6617  O O   . SER B 302 ? 0.5870 0.5874 0.6648 -0.0647 0.0227  -0.0011 302 SER B O   
6618  C CB  . SER B 302 ? 0.5829 0.6045 0.6714 -0.0802 0.0207  -0.0139 302 SER B CB  
6619  O OG  . SER B 302 ? 0.6549 0.6913 0.7499 -0.0713 0.0162  -0.0145 302 SER B OG  
6620  N N   . VAL B 303 ? 0.5335 0.5665 0.6305 -0.0623 0.0227  -0.0058 303 VAL B N   
6621  C CA  . VAL B 303 ? 0.6385 0.6672 0.7361 -0.0525 0.0205  -0.0020 303 VAL B CA  
6622  C C   . VAL B 303 ? 0.5947 0.6345 0.7030 -0.0449 0.0154  -0.0016 303 VAL B C   
6623  O O   . VAL B 303 ? 0.6315 0.6880 0.7519 -0.0444 0.0140  -0.0053 303 VAL B O   
6624  C CB  . VAL B 303 ? 0.6013 0.6339 0.7007 -0.0520 0.0236  -0.0032 303 VAL B CB  
6625  C CG1 . VAL B 303 ? 0.5423 0.5692 0.6439 -0.0429 0.0200  -0.0003 303 VAL B CG1 
6626  C CG2 . VAL B 303 ? 0.5388 0.5617 0.6250 -0.0604 0.0285  -0.0013 303 VAL B CG2 
6627  N N   . PHE B 304 ? 0.6278 0.6596 0.7327 -0.0390 0.0125  0.0035  304 PHE B N   
6628  C CA  . PHE B 304 ? 0.6096 0.6498 0.7229 -0.0321 0.0075  0.0072  304 PHE B CA  
6629  C C   . PHE B 304 ? 0.5507 0.5856 0.6701 -0.0260 0.0062  0.0113  304 PHE B C   
6630  O O   . PHE B 304 ? 0.4901 0.5132 0.6031 -0.0258 0.0079  0.0136  304 PHE B O   
6631  C CB  . PHE B 304 ? 0.5708 0.6088 0.6757 -0.0310 0.0059  0.0105  304 PHE B CB  
6632  C CG  . PHE B 304 ? 0.5479 0.5961 0.6505 -0.0353 0.0040  0.0057  304 PHE B CG  
6633  C CD1 . PHE B 304 ? 0.5754 0.6401 0.6870 -0.0330 -0.0014 0.0066  304 PHE B CD1 
6634  C CD2 . PHE B 304 ? 0.4946 0.5354 0.5869 -0.0416 0.0066  0.0002  304 PHE B CD2 
6635  C CE1 . PHE B 304 ? 0.5140 0.5901 0.6236 -0.0373 -0.0045 0.0017  304 PHE B CE1 
6636  C CE2 . PHE B 304 ? 0.5406 0.5908 0.6313 -0.0465 0.0039  -0.0058 304 PHE B CE2 
6637  C CZ  . PHE B 304 ? 0.4762 0.5454 0.5752 -0.0446 -0.0017 -0.0052 304 PHE B CZ  
6638  N N   . PHE B 305 ? 0.5465 0.5897 0.6796 -0.0211 0.0024  0.0117  305 PHE B N   
6639  C CA  . PHE B 305 ? 0.5594 0.5966 0.7009 -0.0158 0.0000  0.0142  305 PHE B CA  
6640  C C   . PHE B 305 ? 0.5962 0.6321 0.7423 -0.0115 -0.0048 0.0241  305 PHE B C   
6641  O O   . PHE B 305 ? 0.6478 0.6927 0.7993 -0.0093 -0.0089 0.0276  305 PHE B O   
6642  C CB  . PHE B 305 ? 0.5990 0.6439 0.7545 -0.0127 -0.0009 0.0071  305 PHE B CB  
6643  C CG  . PHE B 305 ? 0.4901 0.5397 0.6405 -0.0178 0.0052  -0.0020 305 PHE B CG  
6644  C CD1 . PHE B 305 ? 0.5262 0.5890 0.6776 -0.0223 0.0079  -0.0064 305 PHE B CD1 
6645  C CD2 . PHE B 305 ? 0.5079 0.5501 0.6520 -0.0190 0.0082  -0.0055 305 PHE B CD2 
6646  C CE1 . PHE B 305 ? 0.5777 0.6460 0.7245 -0.0287 0.0145  -0.0131 305 PHE B CE1 
6647  C CE2 . PHE B 305 ? 0.5511 0.5990 0.6881 -0.0247 0.0144  -0.0122 305 PHE B CE2 
6648  C CZ  . PHE B 305 ? 0.5102 0.5710 0.6487 -0.0298 0.0182  -0.0154 305 PHE B CZ  
6649  N N   . ARG B 306 ? 0.5507 0.5767 0.6949 -0.0108 -0.0047 0.0294  306 ARG B N   
6650  C CA  . ARG B 306 ? 0.5329 0.5588 0.6796 -0.0089 -0.0074 0.0403  306 ARG B CA  
6651  C C   . ARG B 306 ? 0.5343 0.5604 0.6975 -0.0045 -0.0139 0.0455  306 ARG B C   
6652  O O   . ARG B 306 ? 0.5760 0.5994 0.7505 -0.0019 -0.0161 0.0391  306 ARG B O   
6653  C CB  . ARG B 306 ? 0.5333 0.5512 0.6770 -0.0099 -0.0052 0.0440  306 ARG B CB  
6654  C CG  . ARG B 306 ? 0.5843 0.5952 0.7416 -0.0083 -0.0090 0.0462  306 ARG B CG  
6655  C CD  . ARG B 306 ? 0.5559 0.5626 0.7129 -0.0099 -0.0076 0.0510  306 ARG B CD  
6656  N NE  . ARG B 306 ? 0.5073 0.5064 0.6761 -0.0098 -0.0117 0.0490  306 ARG B NE  
6657  C CZ  . ARG B 306 ? 0.6341 0.6308 0.8129 -0.0112 -0.0139 0.0560  306 ARG B CZ  
6658  N NH1 . ARG B 306 ? 0.6064 0.6094 0.7846 -0.0126 -0.0111 0.0661  306 ARG B NH1 
6659  N NH2 . ARG B 306 ? 0.7198 0.7091 0.9097 -0.0117 -0.0187 0.0519  306 ARG B NH2 
6660  N N   . ASP B 307 ? 0.5702 0.5995 0.7346 -0.0036 -0.0169 0.0574  307 ASP B N   
6661  C CA  . ASP B 307 ? 0.6206 0.6467 0.8007 0.0001  -0.0239 0.0661  307 ASP B CA  
6662  C C   . ASP B 307 ? 0.7315 0.7464 0.9192 -0.0015 -0.0242 0.0718  307 ASP B C   
6663  O O   . ASP B 307 ? 0.7511 0.7676 0.9345 -0.0046 -0.0224 0.0827  307 ASP B O   
6664  C CB  . ASP B 307 ? 0.5021 0.5376 0.6781 0.0007  -0.0275 0.0784  307 ASP B CB  
6665  C CG  . ASP B 307 ? 0.7399 0.7713 0.9330 0.0054  -0.0365 0.0881  307 ASP B CG  
6666  O OD1 . ASP B 307 ? 0.7384 0.7568 0.9450 0.0058  -0.0389 0.0918  307 ASP B OD1 
6667  O OD2 . ASP B 307 ? 0.7757 0.8164 0.9702 0.0087  -0.0420 0.0916  307 ASP B OD2 
6668  N N   . LYS B 308 ? 0.6418 0.6471 0.8414 0.0001  -0.0264 0.0637  308 LYS B N   
6669  C CA  . LYS B 308 ? 0.6116 0.6064 0.8195 -0.0024 -0.0277 0.0668  308 LYS B CA  
6670  C C   . LYS B 308 ? 0.6257 0.6168 0.8445 -0.0036 -0.0323 0.0834  308 LYS B C   
6671  O O   . LYS B 308 ? 0.6103 0.6005 0.8302 -0.0085 -0.0305 0.0916  308 LYS B O   
6672  C CB  . LYS B 308 ? 0.5909 0.5765 0.8100 0.0000  -0.0309 0.0537  308 LYS B CB  
6673  C CG  . LYS B 308 ? 0.6843 0.6618 0.9065 -0.0038 -0.0314 0.0510  308 LYS B CG  
6674  C CD  . LYS B 308 ? 0.6614 0.6290 0.8963 -0.0011 -0.0363 0.0382  308 LYS B CD  
6675  C CE  . LYS B 308 ? 0.8323 0.7958 1.0647 -0.0052 -0.0367 0.0315  308 LYS B CE  
6676  N NZ  . LYS B 308 ? 0.7799 0.7353 1.0272 -0.0096 -0.0417 0.0405  308 LYS B NZ  
6677  N N   . THR B 309 ? 0.6213 0.6114 0.8490 0.0005  -0.0384 0.0895  309 THR B N   
6678  C CA  . THR B 309 ? 0.5963 0.5795 0.8359 -0.0010 -0.0441 0.1069  309 THR B CA  
6679  C C   . THR B 309 ? 0.6193 0.6140 0.8449 -0.0063 -0.0394 0.1223  309 THR B C   
6680  O O   . THR B 309 ? 0.6566 0.6485 0.8879 -0.0119 -0.0390 0.1351  309 THR B O   
6681  C CB  . THR B 309 ? 0.6460 0.6251 0.8982 0.0059  -0.0529 0.1107  309 THR B CB  
6682  O OG1 . THR B 309 ? 0.7596 0.7326 1.0234 0.0120  -0.0552 0.0927  309 THR B OG1 
6683  C CG2 . THR B 309 ? 0.6096 0.5755 0.8777 0.0041  -0.0603 0.1289  309 THR B CG2 
6684  N N   . LEU B 310 ? 0.5791 0.5884 0.7867 -0.0052 -0.0355 0.1206  310 LEU B N   
6685  C CA  . LEU B 310 ? 0.5990 0.6214 0.7909 -0.0096 -0.0302 0.1324  310 LEU B CA  
6686  C C   . LEU B 310 ? 0.5769 0.6024 0.7635 -0.0140 -0.0215 0.1284  310 LEU B C   
6687  O O   . LEU B 310 ? 0.6159 0.6478 0.8013 -0.0188 -0.0177 0.1406  310 LEU B O   
6688  C CB  . LEU B 310 ? 0.6205 0.6570 0.7947 -0.0072 -0.0292 0.1283  310 LEU B CB  
6689  C CG  . LEU B 310 ? 0.6329 0.6727 0.8104 -0.0030 -0.0383 0.1365  310 LEU B CG  
6690  C CD1 . LEU B 310 ? 0.5753 0.6287 0.7382 -0.0011 -0.0375 0.1259  310 LEU B CD1 
6691  C CD2 . LEU B 310 ? 0.7119 0.7560 0.8857 -0.0061 -0.0411 0.1590  310 LEU B CD2 
6692  N N   . SER B 311 ? 0.5184 0.5407 0.7024 -0.0126 -0.0185 0.1121  311 SER B N   
6693  C CA  . SER B 311 ? 0.5403 0.5649 0.7209 -0.0153 -0.0118 0.1078  311 SER B CA  
6694  C C   . SER B 311 ? 0.6089 0.6275 0.8069 -0.0194 -0.0137 0.1152  311 SER B C   
6695  O O   . SER B 311 ? 0.5712 0.5985 0.7696 -0.0231 -0.0084 0.1217  311 SER B O   
6696  C CB  . SER B 311 ? 0.5714 0.5912 0.7465 -0.0130 -0.0103 0.0910  311 SER B CB  
6697  O OG  . SER B 311 ? 0.6411 0.6674 0.8007 -0.0112 -0.0075 0.0845  311 SER B OG  
6698  N N   . ASP B 312 ? 0.5543 0.5588 0.7682 -0.0189 -0.0211 0.1132  312 ASP B N   
6699  C CA  . ASP B 312 ? 0.6195 0.6164 0.8517 -0.0238 -0.0242 0.1181  312 ASP B CA  
6700  C C   . ASP B 312 ? 0.5816 0.5808 0.8225 -0.0292 -0.0251 0.1383  312 ASP B C   
6701  O O   . ASP B 312 ? 0.6024 0.6016 0.8566 -0.0357 -0.0247 0.1452  312 ASP B O   
6702  C CB  . ASP B 312 ? 0.5519 0.5321 0.7982 -0.0215 -0.0322 0.1076  312 ASP B CB  
6703  C CG  . ASP B 312 ? 0.6624 0.6419 0.9003 -0.0184 -0.0307 0.0890  312 ASP B CG  
6704  O OD1 . ASP B 312 ? 0.5843 0.5734 0.8080 -0.0185 -0.0244 0.0858  312 ASP B OD1 
6705  O OD2 . ASP B 312 ? 0.7620 0.7310 1.0072 -0.0157 -0.0359 0.0777  312 ASP B OD2 
6706  N N   . LEU B 313 ? 0.5751 0.5772 0.8091 -0.0273 -0.0266 0.1486  313 LEU B N   
6707  C CA  . LEU B 313 ? 0.6381 0.6456 0.8750 -0.0333 -0.0261 0.1704  313 LEU B CA  
6708  C C   . LEU B 313 ? 0.6320 0.6595 0.8588 -0.0383 -0.0152 0.1755  313 LEU B C   
6709  O O   . LEU B 313 ? 0.5476 0.5793 0.7856 -0.0461 -0.0128 0.1885  313 LEU B O   
6710  C CB  . LEU B 313 ? 0.5546 0.5644 0.7817 -0.0295 -0.0303 0.1802  313 LEU B CB  
6711  C CG  . LEU B 313 ? 0.5734 0.5638 0.8180 -0.0258 -0.0423 0.1844  313 LEU B CG  
6712  C CD1 . LEU B 313 ? 0.6128 0.6079 0.8470 -0.0181 -0.0469 0.1837  313 LEU B CD1 
6713  C CD2 . LEU B 313 ? 0.5373 0.5188 0.7968 -0.0331 -0.0467 0.2071  313 LEU B CD2 
6714  N N   . ILE B 314 ? 0.6185 0.6591 0.8256 -0.0340 -0.0083 0.1650  314 ILE B N   
6715  C CA  . ILE B 314 ? 0.5846 0.6448 0.7828 -0.0367 0.0025  0.1666  314 ILE B CA  
6716  C C   . ILE B 314 ? 0.5326 0.5922 0.7468 -0.0394 0.0047  0.1609  314 ILE B C   
6717  O O   . ILE B 314 ? 0.6609 0.7334 0.8836 -0.0454 0.0103  0.1705  314 ILE B O   
6718  C CB  . ILE B 314 ? 0.6952 0.7650 0.8708 -0.0306 0.0080  0.1534  314 ILE B CB  
6719  C CG1 . ILE B 314 ? 0.7102 0.7839 0.8701 -0.0286 0.0049  0.1589  314 ILE B CG1 
6720  C CG2 . ILE B 314 ? 0.5348 0.6236 0.7037 -0.0314 0.0193  0.1515  314 ILE B CG2 
6721  C CD1 . ILE B 314 ? 0.5909 0.6710 0.7308 -0.0235 0.0081  0.1438  314 ILE B CD1 
6722  N N   . GLY B 315 ? 0.5506 0.5971 0.7693 -0.0355 0.0000  0.1454  315 GLY B N   
6723  C CA  . GLY B 315 ? 0.5997 0.6474 0.8305 -0.0370 0.0008  0.1383  315 GLY B CA  
6724  C C   . GLY B 315 ? 0.5523 0.5963 0.8070 -0.0451 -0.0034 0.1482  315 GLY B C   
6725  O O   . GLY B 315 ? 0.6576 0.7136 0.9236 -0.0491 0.0003  0.1502  315 GLY B O   
6726  N N   . PHE B 316 ? 0.5447 0.5723 0.8096 -0.0475 -0.0117 0.1540  316 PHE B N   
6727  C CA  . PHE B 316 ? 0.5894 0.6075 0.8791 -0.0555 -0.0181 0.1602  316 PHE B CA  
6728  C C   . PHE B 316 ? 0.6547 0.6682 0.9538 -0.0624 -0.0203 0.1810  316 PHE B C   
6729  O O   . PHE B 316 ? 0.7216 0.7399 1.0378 -0.0723 -0.0193 0.1936  316 PHE B O   
6730  C CB  . PHE B 316 ? 0.5581 0.5553 0.8558 -0.0522 -0.0281 0.1444  316 PHE B CB  
6731  C CG  . PHE B 316 ? 0.5780 0.5776 0.8613 -0.0449 -0.0266 0.1258  316 PHE B CG  
6732  C CD1 . PHE B 316 ? 0.4701 0.4776 0.7579 -0.0464 -0.0257 0.1185  316 PHE B CD1 
6733  C CD2 . PHE B 316 ? 0.5246 0.5195 0.7907 -0.0370 -0.0263 0.1167  316 PHE B CD2 
6734  C CE1 . PHE B 316 ? 0.4563 0.4647 0.7299 -0.0400 -0.0250 0.1038  316 PHE B CE1 
6735  C CE2 . PHE B 316 ? 0.4990 0.4955 0.7517 -0.0319 -0.0246 0.1017  316 PHE B CE2 
6736  C CZ  . PHE B 316 ? 0.4883 0.4904 0.7438 -0.0333 -0.0241 0.0959  316 PHE B CZ  
6737  N N   . SER B 317 ? 0.5924 0.5971 0.8819 -0.0578 -0.0239 0.1861  317 SER B N   
6738  C CA  . SER B 317 ? 0.5569 0.5513 0.8576 -0.0635 -0.0293 0.2064  317 SER B CA  
6739  C C   . SER B 317 ? 0.6127 0.6276 0.9055 -0.0710 -0.0205 0.2279  317 SER B C   
6740  O O   . SER B 317 ? 0.6364 0.6495 0.9453 -0.0816 -0.0214 0.2459  317 SER B O   
6741  C CB  . SER B 317 ? 0.6083 0.5881 0.9029 -0.0549 -0.0372 0.2050  317 SER B CB  
6742  O OG  . SER B 317 ? 0.6130 0.5705 0.9234 -0.0508 -0.0467 0.1906  317 SER B OG  
6743  N N   . TYR B 318 ? 0.6707 0.7057 0.9390 -0.0663 -0.0118 0.2258  318 TYR B N   
6744  C CA  . TYR B 318 ? 0.6523 0.7073 0.9077 -0.0718 -0.0040 0.2456  318 TYR B CA  
6745  C C   . TYR B 318 ? 0.5807 0.6563 0.8453 -0.0817 0.0065  0.2543  318 TYR B C   
6746  O O   . TYR B 318 ? 0.6644 0.7599 0.9177 -0.0872 0.0147  0.2709  318 TYR B O   
6747  C CB  . TYR B 318 ? 0.6548 0.7256 0.8806 -0.0635 0.0020  0.2374  318 TYR B CB  
6748  C CG  . TYR B 318 ? 0.5626 0.6221 0.7770 -0.0566 -0.0071 0.2385  318 TYR B CG  
6749  C CD1 . TYR B 318 ? 0.6280 0.6692 0.8550 -0.0585 -0.0180 0.2539  318 TYR B CD1 
6750  C CD2 . TYR B 318 ? 0.6355 0.7027 0.8284 -0.0482 -0.0053 0.2240  318 TYR B CD2 
6751  C CE1 . TYR B 318 ? 0.6932 0.7263 0.9123 -0.0509 -0.0271 0.2548  318 TYR B CE1 
6752  C CE2 . TYR B 318 ? 0.6266 0.6869 0.8114 -0.0421 -0.0140 0.2246  318 TYR B CE2 
6753  C CZ  . TYR B 318 ? 0.6623 0.7066 0.8605 -0.0429 -0.0249 0.2400  318 TYR B CZ  
6754  O OH  . TYR B 318 ? 0.6742 0.7136 0.8671 -0.0357 -0.0343 0.2404  318 TYR B OH  
6755  N N   . HIS B 319 ? 0.6144 0.6889 0.8987 -0.0844 0.0067  0.2438  319 HIS B N   
6756  C CA  . HIS B 319 ? 0.5317 0.6300 0.8277 -0.0938 0.0169  0.2523  319 HIS B CA  
6757  C C   . HIS B 319 ? 0.6326 0.7284 0.9455 -0.1081 0.0153  0.2781  319 HIS B C   
6758  O O   . HIS B 319 ? 0.6903 0.8115 1.0051 -0.1170 0.0264  0.2924  319 HIS B O   
6759  C CB  . HIS B 319 ? 0.4738 0.5732 0.7881 -0.0929 0.0158  0.2349  319 HIS B CB  
6760  C CG  . HIS B 319 ? 0.5507 0.6269 0.8915 -0.0993 0.0037  0.2345  319 HIS B CG  
6761  N ND1 . HIS B 319 ? 0.5962 0.6476 0.9383 -0.0920 -0.0075 0.2175  319 HIS B ND1 
6762  C CD2 . HIS B 319 ? 0.6766 0.7510 1.0439 -0.1127 0.0010  0.2478  319 HIS B CD2 
6763  C CE1 . HIS B 319 ? 0.6370 0.6718 1.0043 -0.0998 -0.0168 0.2188  319 HIS B CE1 
6764  N NE2 . HIS B 319 ? 0.7001 0.7473 1.0840 -0.1128 -0.0125 0.2373  319 HIS B NE2 
6765  N N   . ALA B 320 ? 0.5603 0.6261 0.8859 -0.1104 0.0021  0.2846  320 ALA B N   
6766  C CA  . ALA B 320 ? 0.6664 0.7245 1.0082 -0.1241 -0.0010 0.3110  320 ALA B CA  
6767  C C   . ALA B 320 ? 0.6250 0.6896 0.9449 -0.1251 0.0016  0.3334  320 ALA B C   
6768  O O   . ALA B 320 ? 0.6016 0.6697 0.9293 -0.1382 0.0035  0.3595  320 ALA B O   
6769  C CB  . ALA B 320 ? 0.7113 0.7321 1.0767 -0.1252 -0.0172 0.3084  320 ALA B CB  
6770  N N   . TRP B 321 ? 0.6303 0.6970 0.9233 -0.1125 0.0012  0.3246  321 TRP B N   
6771  C CA  . TRP B 321 ? 0.7121 0.7832 0.9833 -0.1124 0.0005  0.3447  321 TRP B CA  
6772  C C   . TRP B 321 ? 0.6751 0.7840 0.9245 -0.1174 0.0168  0.3543  321 TRP B C   
6773  O O   . TRP B 321 ? 0.6632 0.7943 0.9077 -0.1146 0.0282  0.3376  321 TRP B O   
6774  C CB  . TRP B 321 ? 0.7255 0.7863 0.9779 -0.0973 -0.0072 0.3303  321 TRP B CB  
6775  C CG  . TRP B 321 ? 0.6699 0.6976 0.9405 -0.0899 -0.0218 0.3177  321 TRP B CG  
6776  C CD1 . TRP B 321 ? 0.6782 0.6902 0.9711 -0.0893 -0.0256 0.3000  321 TRP B CD1 
6777  C CD2 . TRP B 321 ? 0.7530 0.7616 1.0204 -0.0813 -0.0345 0.3207  321 TRP B CD2 
6778  N NE1 . TRP B 321 ? 0.6869 0.6715 0.9898 -0.0809 -0.0388 0.2910  321 TRP B NE1 
6779  C CE2 . TRP B 321 ? 0.6860 0.6683 0.9753 -0.0755 -0.0443 0.3034  321 TRP B CE2 
6780  C CE3 . TRP B 321 ? 0.6927 0.7058 0.9414 -0.0775 -0.0389 0.3360  321 TRP B CE3 
6781  C CZ2 . TRP B 321 ? 0.7653 0.7263 1.0602 -0.0655 -0.0571 0.3002  321 TRP B CZ2 
6782  C CZ3 . TRP B 321 ? 0.6655 0.6572 0.9207 -0.0677 -0.0530 0.3340  321 TRP B CZ3 
6783  C CH2 . TRP B 321 ? 0.8101 0.7764 1.0892 -0.0615 -0.0614 0.3159  321 TRP B CH2 
6784  N N   . ASN B 322 ? 0.7096 0.8259 0.9449 -0.1240 0.0174  0.3810  322 ASN B N   
6785  C CA  . ASN B 322 ? 0.7697 0.9223 0.9753 -0.1257 0.0318  0.3875  322 ASN B CA  
6786  C C   . ASN B 322 ? 0.7658 0.9242 0.9425 -0.1109 0.0309  0.3673  322 ASN B C   
6787  O O   . ASN B 322 ? 0.7451 0.8808 0.9190 -0.1021 0.0173  0.3623  322 ASN B O   
6788  C CB  . ASN B 322 ? 0.8263 0.9853 1.0211 -0.1372 0.0317  0.4229  322 ASN B CB  
6789  C CG  . ASN B 322 ? 1.0133 1.1480 1.2394 -0.1500 0.0234  0.4456  322 ASN B CG  
6790  O OD1 . ASN B 322 ? 1.0215 1.1621 1.2720 -0.1607 0.0302  0.4471  322 ASN B OD1 
6791  N ND2 . ASN B 322 ? 0.9820 1.0893 1.2090 -0.1492 0.0080  0.4636  322 ASN B ND2 
6792  N N   . ALA B 323 ? 0.6449 0.8347 0.8016 -0.1082 0.0454  0.3552  323 ALA B N   
6793  C CA  . ALA B 323 ? 0.7529 0.9472 0.8860 -0.0948 0.0453  0.3312  323 ALA B CA  
6794  C C   . ALA B 323 ? 0.8031 0.9908 0.9135 -0.0905 0.0344  0.3408  323 ALA B C   
6795  O O   . ALA B 323 ? 0.6998 0.8709 0.8077 -0.0802 0.0243  0.3249  323 ALA B O   
6796  C CB  . ALA B 323 ? 0.7479 0.9774 0.8630 -0.0937 0.0630  0.3194  323 ALA B CB  
6797  N N   . GLU B 324 ? 0.7859 0.9875 0.8805 -0.0988 0.0359  0.3678  324 GLU B N   
6798  C CA  . GLU B 324 ? 0.8055 1.0038 0.8777 -0.0946 0.0244  0.3787  324 GLU B CA  
6799  C C   . GLU B 324 ? 0.8514 1.0132 0.9448 -0.0897 0.0053  0.3832  324 GLU B C   
6800  O O   . GLU B 324 ? 0.9175 1.0726 0.9998 -0.0802 -0.0058 0.3765  324 GLU B O   
6801  C CB  . GLU B 324 ? 0.8072 1.0267 0.8590 -0.1057 0.0290  0.4103  324 GLU B CB  
6802  C CG  . GLU B 324 ? 0.9317 1.1881 0.9451 -0.1040 0.0410  0.4025  324 GLU B CG  
6803  C CD  . GLU B 324 ? 1.1308 1.4015 1.1140 -0.1090 0.0361  0.4298  324 GLU B CD  
6804  O OE1 . GLU B 324 ? 1.0765 1.3279 1.0574 -0.1039 0.0183  0.4393  324 GLU B OE1 
6805  O OE2 . GLU B 324 ? 1.2585 1.5613 1.2200 -0.1176 0.0503  0.4420  324 GLU B OE2 
6806  N N   . ASP B 325 ? 0.7634 0.9025 0.8887 -0.0957 0.0010  0.3928  325 ASP B N   
6807  C CA  . ASP B 325 ? 0.7744 0.8782 0.9225 -0.0895 -0.0164 0.3925  325 ASP B CA  
6808  C C   . ASP B 325 ? 0.7657 0.8586 0.9215 -0.0774 -0.0191 0.3587  325 ASP B C   
6809  O O   . ASP B 325 ? 0.7517 0.8271 0.9121 -0.0677 -0.0319 0.3518  325 ASP B O   
6810  C CB  . ASP B 325 ? 0.8261 0.9079 1.0064 -0.0999 -0.0200 0.4095  325 ASP B CB  
6811  C CG  . ASP B 325 ? 0.9122 1.0044 1.0859 -0.1140 -0.0167 0.4453  325 ASP B CG  
6812  O OD1 . ASP B 325 ? 0.8041 0.8962 0.9605 -0.1127 -0.0251 0.4655  325 ASP B OD1 
6813  O OD2 . ASP B 325 ? 0.9818 1.0842 1.1674 -0.1268 -0.0057 0.4538  325 ASP B OD2 
6814  N N   . ALA B 326 ? 0.7659 0.8701 0.9236 -0.0775 -0.0070 0.3381  326 ALA B N   
6815  C CA  . ALA B 326 ? 0.7394 0.8337 0.9024 -0.0671 -0.0091 0.3081  326 ALA B CA  
6816  C C   . ALA B 326 ? 0.7165 0.8226 0.8532 -0.0578 -0.0102 0.2947  326 ALA B C   
6817  O O   . ALA B 326 ? 0.7280 0.8201 0.8694 -0.0490 -0.0189 0.2798  326 ALA B O   
6818  C CB  . ALA B 326 ? 0.6932 0.7965 0.8646 -0.0694 0.0029  0.2918  326 ALA B CB  
6819  N N   . VAL B 327 ? 0.7196 0.8528 0.8290 -0.0602 -0.0012 0.2990  327 VAL B N   
6820  C CA  . VAL B 327 ? 0.7007 0.8456 0.7848 -0.0526 -0.0031 0.2859  327 VAL B CA  
6821  C C   . VAL B 327 ? 0.6719 0.8052 0.7555 -0.0481 -0.0194 0.2971  327 VAL B C   
6822  O O   . VAL B 327 ? 0.6141 0.7430 0.6955 -0.0398 -0.0266 0.2809  327 VAL B O   
6823  C CB  . VAL B 327 ? 0.7143 0.8911 0.7683 -0.0565 0.0090  0.2889  327 VAL B CB  
6824  C CG1 . VAL B 327 ? 0.7015 0.8887 0.7313 -0.0491 0.0066  0.2707  327 VAL B CG1 
6825  C CG2 . VAL B 327 ? 0.7235 0.9126 0.7825 -0.0597 0.0250  0.2779  327 VAL B CG2 
6826  N N   . ARG B 328 ? 0.7028 0.8313 0.7907 -0.0537 -0.0258 0.3257  328 ARG B N   
6827  C CA  . ARG B 328 ? 0.7540 0.8712 0.8437 -0.0483 -0.0426 0.3385  328 ARG B CA  
6828  C C   . ARG B 328 ? 0.6350 0.7240 0.7547 -0.0401 -0.0533 0.3255  328 ARG B C   
6829  O O   . ARG B 328 ? 0.6410 0.7258 0.7619 -0.0311 -0.0649 0.3197  328 ARG B O   
6830  C CB  . ARG B 328 ? 0.7705 0.8858 0.8593 -0.0564 -0.0475 0.3742  328 ARG B CB  
6831  C CG  . ARG B 328 ? 0.8270 0.9708 0.8797 -0.0600 -0.0455 0.3898  328 ARG B CG  
6832  C CD  . ARG B 328 ? 0.8571 1.0093 0.9042 -0.0733 -0.0386 0.4204  328 ARG B CD  
6833  N NE  . ARG B 328 ? 0.9125 1.0349 0.9889 -0.0768 -0.0495 0.4432  328 ARG B NE  
6834  C CZ  . ARG B 328 ? 0.9858 1.1061 1.0699 -0.0900 -0.0443 0.4689  328 ARG B CZ  
6835  N NH1 . ARG B 328 ? 0.9707 1.1199 1.0357 -0.1007 -0.0273 0.4759  328 ARG B NH1 
6836  N NH2 . ARG B 328 ? 0.9726 1.0614 1.0856 -0.0926 -0.0561 0.4875  328 ARG B NH2 
6837  N N   . ASP B 329 ? 0.7267 0.7982 0.8710 -0.0431 -0.0497 0.3198  329 ASP B N   
6838  C CA  . ASP B 329 ? 0.6881 0.7359 0.8579 -0.0351 -0.0577 0.3027  329 ASP B CA  
6839  C C   . ASP B 329 ? 0.6348 0.6914 0.7950 -0.0273 -0.0544 0.2738  329 ASP B C   
6840  O O   . ASP B 329 ? 0.6976 0.7476 0.8647 -0.0184 -0.0638 0.2641  329 ASP B O   
6841  C CB  . ASP B 329 ? 0.7549 0.7857 0.9491 -0.0409 -0.0537 0.3000  329 ASP B CB  
6842  C CG  . ASP B 329 ? 0.7010 0.7067 0.9212 -0.0333 -0.0627 0.2840  329 ASP B CG  
6843  O OD1 . ASP B 329 ? 0.6291 0.6149 0.8673 -0.0303 -0.0751 0.2960  329 ASP B OD1 
6844  O OD2 . ASP B 329 ? 0.6720 0.6779 0.8944 -0.0300 -0.0574 0.2595  329 ASP B OD2 
6845  N N   . PHE B 330 ? 0.6752 0.7476 0.8204 -0.0306 -0.0411 0.2605  330 PHE B N   
6846  C CA  . PHE B 330 ? 0.6471 0.7258 0.7835 -0.0247 -0.0374 0.2342  330 PHE B CA  
6847  C C   . PHE B 330 ? 0.6426 0.7329 0.7629 -0.0192 -0.0447 0.2320  330 PHE B C   
6848  O O   . PHE B 330 ? 0.6849 0.7700 0.8127 -0.0124 -0.0505 0.2167  330 PHE B O   
6849  C CB  . PHE B 330 ? 0.5801 0.6740 0.7019 -0.0289 -0.0227 0.2239  330 PHE B CB  
6850  C CG  . PHE B 330 ? 0.6388 0.7299 0.7605 -0.0243 -0.0186 0.1976  330 PHE B CG  
6851  C CD1 . PHE B 330 ? 0.6654 0.7394 0.8073 -0.0231 -0.0189 0.1869  330 PHE B CD1 
6852  C CD2 . PHE B 330 ? 0.6571 0.7620 0.7579 -0.0218 -0.0149 0.1838  330 PHE B CD2 
6853  C CE1 . PHE B 330 ? 0.7028 0.7742 0.8428 -0.0196 -0.0153 0.1651  330 PHE B CE1 
6854  C CE2 . PHE B 330 ? 0.6577 0.7578 0.7588 -0.0187 -0.0115 0.1617  330 PHE B CE2 
6855  C CZ  . PHE B 330 ? 0.7440 0.8276 0.8641 -0.0176 -0.0115 0.1534  330 PHE B CZ  
6856  N N   . ILE B 331 ? 0.6413 0.7497 0.7396 -0.0225 -0.0447 0.2474  331 ILE B N   
6857  C CA  . ILE B 331 ? 0.6619 0.7837 0.7441 -0.0179 -0.0532 0.2461  331 ILE B CA  
6858  C C   . ILE B 331 ? 0.6768 0.7845 0.7795 -0.0109 -0.0693 0.2540  331 ILE B C   
6859  O O   . ILE B 331 ? 0.6493 0.7608 0.7545 -0.0042 -0.0766 0.2410  331 ILE B O   
6860  C CB  . ILE B 331 ? 0.5863 0.7310 0.6391 -0.0233 -0.0506 0.2627  331 ILE B CB  
6861  C CG1 . ILE B 331 ? 0.5983 0.7583 0.6331 -0.0286 -0.0338 0.2517  331 ILE B CG1 
6862  C CG2 . ILE B 331 ? 0.6491 0.8097 0.6838 -0.0191 -0.0605 0.2599  331 ILE B CG2 
6863  C CD1 . ILE B 331 ? 0.5903 0.7485 0.6258 -0.0249 -0.0278 0.2219  331 ILE B CD1 
6864  N N   . GLY B 332 ? 0.6101 0.7011 0.7304 -0.0123 -0.0749 0.2746  332 GLY B N   
6865  C CA  . GLY B 332 ? 0.5899 0.6649 0.7332 -0.0042 -0.0905 0.2817  332 GLY B CA  
6866  C C   . GLY B 332 ? 0.6017 0.6660 0.7662 0.0039  -0.0922 0.2562  332 GLY B C   
6867  O O   . GLY B 332 ? 0.5780 0.6448 0.7513 0.0125  -0.1026 0.2506  332 GLY B O   
6868  N N   . ARG B 333 ? 0.5441 0.5987 0.7169 0.0010  -0.0819 0.2404  333 ARG B N   
6869  C CA  . ARG B 333 ? 0.6366 0.6832 0.8261 0.0075  -0.0819 0.2161  333 ARG B CA  
6870  C C   . ARG B 333 ? 0.6169 0.6828 0.7913 0.0100  -0.0796 0.1982  333 ARG B C   
6871  O O   . ARG B 333 ? 0.5292 0.5944 0.7171 0.0167  -0.0836 0.1830  333 ARG B O   
6872  C CB  . ARG B 333 ? 0.6050 0.6393 0.8024 0.0030  -0.0718 0.2043  333 ARG B CB  
6873  C CG  . ARG B 333 ? 0.5621 0.5809 0.7716 -0.0029 -0.0720 0.2215  333 ARG B CG  
6874  C CD  . ARG B 333 ? 0.5678 0.5682 0.7978 -0.0029 -0.0699 0.2074  333 ARG B CD  
6875  N NE  . ARG B 333 ? 0.5564 0.5405 0.8020 -0.0091 -0.0722 0.2236  333 ARG B NE  
6876  C CZ  . ARG B 333 ? 0.6473 0.6097 0.9172 -0.0081 -0.0765 0.2170  333 ARG B CZ  
6877  N NH1 . ARG B 333 ? 0.5094 0.4650 0.7894 -0.0004 -0.0782 0.1944  333 ARG B NH1 
6878  N NH2 . ARG B 333 ? 0.6373 0.5853 0.9215 -0.0155 -0.0790 0.2331  333 ARG B NH2 
6879  N N   . LEU B 334 ? 0.5906 0.6743 0.7380 0.0044  -0.0729 0.1990  334 LEU B N   
6880  C CA  . LEU B 334 ? 0.6201 0.7208 0.7533 0.0055  -0.0717 0.1822  334 LEU B CA  
6881  C C   . LEU B 334 ? 0.6362 0.7494 0.7694 0.0109  -0.0853 0.1890  334 LEU B C   
6882  O O   . LEU B 334 ? 0.6476 0.7707 0.7834 0.0140  -0.0882 0.1732  334 LEU B O   
6883  C CB  . LEU B 334 ? 0.6781 0.7925 0.7836 -0.0015 -0.0607 0.1787  334 LEU B CB  
6884  C CG  . LEU B 334 ? 0.6905 0.7952 0.7979 -0.0053 -0.0477 0.1684  334 LEU B CG  
6885  C CD1 . LEU B 334 ? 0.6419 0.7608 0.7245 -0.0105 -0.0368 0.1647  334 LEU B CD1 
6886  C CD2 . LEU B 334 ? 0.6738 0.7694 0.7942 -0.0024 -0.0460 0.1471  334 LEU B CD2 
6887  N N   . LYS B 335 ? 0.5936 0.7075 0.7246 0.0116  -0.0942 0.2131  335 LYS B N   
6888  C CA  . LYS B 335 ? 0.6394 0.7636 0.7744 0.0183  -0.1097 0.2216  335 LYS B CA  
6889  C C   . LYS B 335 ? 0.6183 0.7308 0.7867 0.0281  -0.1180 0.2133  335 LYS B C   
6890  O O   . LYS B 335 ? 0.5506 0.6764 0.7266 0.0343  -0.1267 0.2054  335 LYS B O   
6891  C CB  . LYS B 335 ? 0.6656 0.7899 0.7921 0.0171  -0.1182 0.2521  335 LYS B CB  
6892  C CG  . LYS B 335 ? 0.6739 0.8171 0.7646 0.0083  -0.1116 0.2613  335 LYS B CG  
6893  C CD  . LYS B 335 ? 0.7060 0.8426 0.7908 0.0032  -0.1127 0.2917  335 LYS B CD  
6894  C CE  . LYS B 335 ? 0.7420 0.9036 0.7892 -0.0038 -0.1094 0.3035  335 LYS B CE  
6895  N NZ  . LYS B 335 ? 0.6801 0.8374 0.7209 -0.0101 -0.1098 0.3354  335 LYS B NZ  
6896  N N   . LYS B 336 ? 0.5973 0.6862 0.7869 0.0297  -0.1154 0.2141  336 LYS B N   
6897  C CA  . LYS B 336 ? 0.6303 0.7076 0.8520 0.0398  -0.1222 0.2043  336 LYS B CA  
6898  C C   . LYS B 336 ? 0.6393 0.7265 0.8650 0.0410  -0.1150 0.1762  336 LYS B C   
6899  O O   . LYS B 336 ? 0.6470 0.7414 0.8919 0.0494  -0.1218 0.1662  336 LYS B O   
6900  C CB  . LYS B 336 ? 0.6842 0.7336 0.9251 0.0398  -0.1206 0.2094  336 LYS B CB  
6901  C CG  . LYS B 336 ? 0.6915 0.7257 0.9474 0.0445  -0.1343 0.2345  336 LYS B CG  
6902  C CD  . LYS B 336 ? 0.6560 0.6606 0.9347 0.0443  -0.1335 0.2357  336 LYS B CD  
6903  C CE  . LYS B 336 ? 0.6998 0.6853 1.0028 0.0525  -0.1497 0.2549  336 LYS B CE  
6904  N NZ  . LYS B 336 ? 0.8716 0.8264 1.1998 0.0526  -0.1500 0.2525  336 LYS B NZ  
6905  N N   . ILE B 337 ? 0.6206 0.7091 0.8293 0.0325  -0.1011 0.1639  337 ILE B N   
6906  C CA  . ILE B 337 ? 0.6089 0.7069 0.8174 0.0316  -0.0939 0.1400  337 ILE B CA  
6907  C C   . ILE B 337 ? 0.6097 0.7320 0.8105 0.0324  -0.1001 0.1361  337 ILE B C   
6908  O O   . ILE B 337 ? 0.7290 0.8616 0.9445 0.0362  -0.1020 0.1215  337 ILE B O   
6909  C CB  . ILE B 337 ? 0.6548 0.7483 0.8447 0.0224  -0.0793 0.1310  337 ILE B CB  
6910  C CG1 . ILE B 337 ? 0.6099 0.6824 0.8140 0.0227  -0.0737 0.1265  337 ILE B CG1 
6911  C CG2 . ILE B 337 ? 0.5799 0.6868 0.7610 0.0190  -0.0733 0.1115  337 ILE B CG2 
6912  C CD1 . ILE B 337 ? 0.4727 0.5375 0.6617 0.0148  -0.0638 0.1304  337 ILE B CD1 
6913  N N   . HIS B 338 ? 0.5565 0.6902 0.7349 0.0285  -0.1037 0.1490  338 HIS B N   
6914  C CA  . HIS B 338 ? 0.6322 0.7900 0.8013 0.0284  -0.1112 0.1453  338 HIS B CA  
6915  C C   . HIS B 338 ? 0.6541 0.8200 0.8488 0.0389  -0.1261 0.1491  338 HIS B C   
6916  O O   . HIS B 338 ? 0.6633 0.8483 0.8654 0.0403  -0.1304 0.1363  338 HIS B O   
6917  C CB  . HIS B 338 ? 0.6196 0.7875 0.7588 0.0230  -0.1132 0.1603  338 HIS B CB  
6918  C CG  . HIS B 338 ? 0.5909 0.7837 0.7137 0.0202  -0.1187 0.1527  338 HIS B CG  
6919  N ND1 . HIS B 338 ? 0.6070 0.8167 0.7337 0.0255  -0.1349 0.1623  338 HIS B ND1 
6920  C CD2 . HIS B 338 ? 0.6485 0.8518 0.7511 0.0125  -0.1111 0.1364  338 HIS B CD2 
6921  C CE1 . HIS B 338 ? 0.6739 0.9050 0.7832 0.0205  -0.1372 0.1514  338 HIS B CE1 
6922  N NE2 . HIS B 338 ? 0.7447 0.9712 0.8393 0.0124  -0.1227 0.1352  338 HIS B NE2 
6923  N N   . GLU B 339 ? 0.6873 0.8389 0.8983 0.0463  -0.1345 0.1661  339 GLU B N   
6924  C CA  . GLU B 339 ? 0.7332 0.8910 0.9708 0.0583  -0.1500 0.1713  339 GLU B CA  
6925  C C   . GLU B 339 ? 0.6307 0.7844 0.9004 0.0659  -0.1472 0.1519  339 GLU B C   
6926  O O   . GLU B 339 ? 0.7226 0.8909 1.0150 0.0752  -0.1573 0.1473  339 GLU B O   
6927  C CB  . GLU B 339 ? 0.7590 0.9003 1.0014 0.0633  -0.1608 0.1986  339 GLU B CB  
6928  C CG  . GLU B 339 ? 1.0112 1.1392 1.2912 0.0772  -0.1719 0.2017  339 GLU B CG  
6929  C CD  . GLU B 339 ? 1.2009 1.3031 1.4857 0.0791  -0.1790 0.2278  339 GLU B CD  
6930  O OE1 . GLU B 339 ? 1.2879 1.3653 1.5949 0.0830  -0.1764 0.2241  339 GLU B OE1 
6931  O OE2 . GLU B 339 ? 1.3414 1.4481 1.6075 0.0761  -0.1872 0.2520  339 GLU B OE2 
6932  N N   . SER B 340 ? 0.6096 0.7468 0.8811 0.0620  -0.1335 0.1394  340 SER B N   
6933  C CA  . SER B 340 ? 0.6412 0.7736 0.9412 0.0693  -0.1303 0.1218  340 SER B CA  
6934  C C   . SER B 340 ? 0.7164 0.8723 1.0206 0.0672  -0.1245 0.0999  340 SER B C   
6935  O O   . SER B 340 ? 0.6616 0.8220 0.9919 0.0747  -0.1236 0.0858  340 SER B O   
6936  C CB  . SER B 340 ? 0.5886 0.6962 0.8871 0.0653  -0.1187 0.1166  340 SER B CB  
6937  O OG  . SER B 340 ? 0.7216 0.8346 1.0029 0.0554  -0.1045 0.1007  340 SER B OG  
6938  N N   . VAL B 341 ? 0.6905 0.8616 0.9707 0.0569  -0.1201 0.0962  341 VAL B N   
6939  C CA  . VAL B 341 ? 0.6962 0.8867 0.9790 0.0517  -0.1133 0.0761  341 VAL B CA  
6940  C C   . VAL B 341 ? 0.7120 0.9296 0.9907 0.0502  -0.1236 0.0778  341 VAL B C   
6941  O O   . VAL B 341 ? 0.7558 0.9755 1.0127 0.0469  -0.1300 0.0913  341 VAL B O   
6942  C CB  . VAL B 341 ? 0.5909 0.7718 0.8507 0.0393  -0.0975 0.0660  341 VAL B CB  
6943  C CG1 . VAL B 341 ? 0.6220 0.7799 0.8884 0.0412  -0.0886 0.0622  341 VAL B CG1 
6944  C CG2 . VAL B 341 ? 0.6573 0.8344 0.8854 0.0312  -0.0969 0.0768  341 VAL B CG2 
6945  N N   . ASP B 342 ? 0.6661 0.9063 0.9660 0.0522  -0.1252 0.0637  342 ASP B N   
6946  C CA  . ASP B 342 ? 0.7412 1.0098 1.0394 0.0491  -0.1351 0.0624  342 ASP B CA  
6947  C C   . ASP B 342 ? 0.7227 0.9943 0.9915 0.0336  -0.1268 0.0543  342 ASP B C   
6948  O O   . ASP B 342 ? 0.5975 0.8819 0.8487 0.0291  -0.1351 0.0591  342 ASP B O   
6949  C CB  . ASP B 342 ? 0.7063 1.0001 1.0392 0.0551  -0.1383 0.0489  342 ASP B CB  
6950  C CG  . ASP B 342 ? 0.9343 1.2193 1.2982 0.0701  -0.1400 0.0494  342 ASP B CG  
6951  O OD1 . ASP B 342 ? 1.0463 1.3295 1.4232 0.0825  -0.1547 0.0639  342 ASP B OD1 
6952  O OD2 . ASP B 342 ? 0.9707 1.2499 1.3454 0.0696  -0.1270 0.0351  342 ASP B OD2 
6953  N N   . PHE B 343 ? 0.5338 0.7927 0.7960 0.0256  -0.1111 0.0421  343 PHE B N   
6954  C CA  . PHE B 343 ? 0.5778 0.8359 0.8152 0.0115  -0.1029 0.0333  343 PHE B CA  
6955  C C   . PHE B 343 ? 0.6793 0.9190 0.8855 0.0086  -0.1009 0.0445  343 PHE B C   
6956  O O   . PHE B 343 ? 0.6590 0.8905 0.8620 0.0159  -0.1070 0.0607  343 PHE B O   
6957  C CB  . PHE B 343 ? 0.6184 0.8689 0.8608 0.0047  -0.0878 0.0185  343 PHE B CB  
6958  C CG  . PHE B 343 ? 0.6269 0.8542 0.8731 0.0102  -0.0793 0.0211  343 PHE B CG  
6959  C CD1 . PHE B 343 ? 0.4908 0.7212 0.7645 0.0206  -0.0806 0.0192  343 PHE B CD1 
6960  C CD2 . PHE B 343 ? 0.6161 0.8197 0.8398 0.0052  -0.0702 0.0240  343 PHE B CD2 
6961  C CE1 . PHE B 343 ? 0.4625 0.6715 0.7389 0.0250  -0.0736 0.0197  343 PHE B CE1 
6962  C CE2 . PHE B 343 ? 0.5436 0.7275 0.7711 0.0095  -0.0636 0.0257  343 PHE B CE2 
6963  C CZ  . PHE B 343 ? 0.5008 0.6868 0.7537 0.0189  -0.0655 0.0233  343 PHE B CZ  
6964  N N   . GLN B 344 ? 0.5900 0.8235 0.7738 -0.0023 -0.0921 0.0360  344 GLN B N   
6965  C CA  . GLN B 344 ? 0.6679 0.8855 0.8238 -0.0049 -0.0874 0.0437  344 GLN B CA  
6966  C C   . GLN B 344 ? 0.6526 0.8460 0.8069 -0.0062 -0.0738 0.0412  344 GLN B C   
6967  O O   . GLN B 344 ? 0.5645 0.7528 0.7183 -0.0131 -0.0648 0.0280  344 GLN B O   
6968  C CB  . GLN B 344 ? 0.5924 0.8180 0.7248 -0.0144 -0.0873 0.0350  344 GLN B CB  
6969  C CG  . GLN B 344 ? 0.6253 0.8707 0.7470 -0.0124 -0.1012 0.0433  344 GLN B CG  
6970  C CD  . GLN B 344 ? 0.6918 0.9459 0.7890 -0.0216 -0.1017 0.0324  344 GLN B CD  
6971  O OE1 . GLN B 344 ? 0.7514 1.0076 0.8236 -0.0217 -0.1035 0.0391  344 GLN B OE1 
6972  N NE2 . GLN B 344 ? 0.5808 0.8405 0.6852 -0.0299 -0.0999 0.0149  344 GLN B NE2 
6973  N N   . PRO B 345 ? 0.6652 0.8435 0.8189 -0.0004 -0.0725 0.0539  345 PRO B N   
6974  C CA  . PRO B 345 ? 0.6233 0.7808 0.7791 -0.0010 -0.0614 0.0511  345 PRO B CA  
6975  C C   . PRO B 345 ? 0.6169 0.7634 0.7494 -0.0080 -0.0518 0.0476  345 PRO B C   
6976  O O   . PRO B 345 ? 0.6280 0.7798 0.7413 -0.0105 -0.0531 0.0513  345 PRO B O   
6977  C CB  . PRO B 345 ? 0.5537 0.7009 0.7189 0.0071  -0.0658 0.0667  345 PRO B CB  
6978  C CG  . PRO B 345 ? 0.6354 0.7927 0.7869 0.0079  -0.0745 0.0807  345 PRO B CG  
6979  C CD  . PRO B 345 ? 0.7016 0.8813 0.8527 0.0060  -0.0817 0.0726  345 PRO B CD  
6980  N N   . VAL B 346 ? 0.5379 0.6702 0.6724 -0.0108 -0.0423 0.0398  346 VAL B N   
6981  C CA  . VAL B 346 ? 0.6367 0.7548 0.7544 -0.0147 -0.0333 0.0382  346 VAL B CA  
6982  C C   . VAL B 346 ? 0.5900 0.6933 0.7148 -0.0104 -0.0301 0.0464  346 VAL B C   
6983  O O   . VAL B 346 ? 0.5488 0.6463 0.6888 -0.0080 -0.0293 0.0434  346 VAL B O   
6984  C CB  . VAL B 346 ? 0.5930 0.7057 0.7064 -0.0219 -0.0263 0.0239  346 VAL B CB  
6985  C CG1 . VAL B 346 ? 0.5621 0.6732 0.6927 -0.0221 -0.0239 0.0181  346 VAL B CG1 
6986  C CG2 . VAL B 346 ? 0.4309 0.5278 0.5299 -0.0238 -0.0182 0.0230  346 VAL B CG2 
6987  N N   . VAL B 347 ? 0.5568 0.6558 0.6711 -0.0097 -0.0284 0.0563  347 VAL B N   
6988  C CA  . VAL B 347 ? 0.5466 0.6332 0.6687 -0.0068 -0.0265 0.0654  347 VAL B CA  
6989  C C   . VAL B 347 ? 0.5889 0.6660 0.7004 -0.0100 -0.0173 0.0615  347 VAL B C   
6990  O O   . VAL B 347 ? 0.5845 0.6663 0.6810 -0.0117 -0.0138 0.0632  347 VAL B O   
6991  C CB  . VAL B 347 ? 0.5559 0.6466 0.6782 -0.0041 -0.0322 0.0827  347 VAL B CB  
6992  C CG1 . VAL B 347 ? 0.5355 0.6132 0.6652 -0.0036 -0.0291 0.0917  347 VAL B CG1 
6993  C CG2 . VAL B 347 ? 0.5933 0.6906 0.7302 0.0009  -0.0429 0.0876  347 VAL B CG2 
6994  N N   . PHE B 348 ? 0.5314 0.5964 0.6507 -0.0101 -0.0136 0.0558  348 PHE B N   
6995  C CA  . PHE B 348 ? 0.5117 0.5672 0.6239 -0.0120 -0.0065 0.0524  348 PHE B CA  
6996  C C   . PHE B 348 ? 0.5331 0.5823 0.6536 -0.0102 -0.0061 0.0621  348 PHE B C   
6997  O O   . PHE B 348 ? 0.5335 0.5761 0.6680 -0.0085 -0.0094 0.0635  348 PHE B O   
6998  C CB  . PHE B 348 ? 0.4733 0.5203 0.5867 -0.0143 -0.0034 0.0411  348 PHE B CB  
6999  C CG  . PHE B 348 ? 0.4858 0.5323 0.5864 -0.0184 0.0002  0.0320  348 PHE B CG  
7000  C CD1 . PHE B 348 ? 0.5337 0.5901 0.6311 -0.0211 -0.0024 0.0268  348 PHE B CD1 
7001  C CD2 . PHE B 348 ? 0.4991 0.5347 0.5924 -0.0194 0.0054  0.0285  348 PHE B CD2 
7002  C CE1 . PHE B 348 ? 0.5055 0.5595 0.5926 -0.0260 0.0003  0.0177  348 PHE B CE1 
7003  C CE2 . PHE B 348 ? 0.5249 0.5565 0.6080 -0.0231 0.0080  0.0201  348 PHE B CE2 
7004  C CZ  . PHE B 348 ? 0.5511 0.5911 0.6310 -0.0269 0.0056  0.0143  348 PHE B CZ  
7005  N N   . VAL B 349 ? 0.5537 0.6061 0.6667 -0.0109 -0.0019 0.0678  349 VAL B N   
7006  C CA  . VAL B 349 ? 0.5426 0.5919 0.6642 -0.0108 -0.0006 0.0775  349 VAL B CA  
7007  C C   . VAL B 349 ? 0.5411 0.5858 0.6597 -0.0111 0.0056  0.0711  349 VAL B C   
7008  O O   . VAL B 349 ? 0.5162 0.5675 0.6243 -0.0109 0.0111  0.0695  349 VAL B O   
7009  C CB  . VAL B 349 ? 0.5673 0.6280 0.6849 -0.0117 -0.0003 0.0913  349 VAL B CB  
7010  C CG1 . VAL B 349 ? 0.4907 0.5486 0.6207 -0.0134 0.0010  0.1019  349 VAL B CG1 
7011  C CG2 . VAL B 349 ? 0.4490 0.5148 0.5675 -0.0107 -0.0080 0.0986  349 VAL B CG2 
7012  N N   . VAL B 350 ? 0.5575 0.5914 0.6852 -0.0109 0.0043  0.0671  350 VAL B N   
7013  C CA  . VAL B 350 ? 0.5197 0.5479 0.6454 -0.0105 0.0080  0.0612  350 VAL B CA  
7014  C C   . VAL B 350 ? 0.5222 0.5477 0.6620 -0.0108 0.0063  0.0669  350 VAL B C   
7015  O O   . VAL B 350 ? 0.5550 0.5748 0.7054 -0.0116 0.0012  0.0683  350 VAL B O   
7016  C CB  . VAL B 350 ? 0.5310 0.5497 0.6516 -0.0110 0.0072  0.0507  350 VAL B CB  
7017  C CG1 . VAL B 350 ? 0.5842 0.5960 0.7016 -0.0101 0.0098  0.0468  350 VAL B CG1 
7018  C CG2 . VAL B 350 ? 0.4809 0.5029 0.5911 -0.0123 0.0080  0.0451  350 VAL B CG2 
7019  N N   . LEU B 351 ? 0.5719 0.6021 0.7133 -0.0101 0.0104  0.0689  351 LEU B N   
7020  C CA  . LEU B 351 ? 0.5666 0.5976 0.7231 -0.0113 0.0088  0.0744  351 LEU B CA  
7021  C C   . LEU B 351 ? 0.6058 0.6438 0.7626 -0.0088 0.0140  0.0728  351 LEU B C   
7022  O O   . LEU B 351 ? 0.5559 0.5992 0.7018 -0.0060 0.0196  0.0692  351 LEU B O   
7023  C CB  . LEU B 351 ? 0.4683 0.5057 0.6356 -0.0148 0.0076  0.0868  351 LEU B CB  
7024  C CG  . LEU B 351 ? 0.4003 0.4526 0.5608 -0.0155 0.0138  0.0951  351 LEU B CG  
7025  C CD1 . LEU B 351 ? 0.5119 0.5717 0.6869 -0.0203 0.0140  0.1094  351 LEU B CD1 
7026  C CD2 . LEU B 351 ? 0.5977 0.6505 0.7456 -0.0148 0.0122  0.0955  351 LEU B CD2 
7027  N N   . ASP B 352 ? 0.5223 0.5607 0.6929 -0.0093 0.0115  0.0745  352 ASP B N   
7028  C CA  . ASP B 352 ? 0.4898 0.5376 0.6658 -0.0060 0.0157  0.0738  352 ASP B CA  
7029  C C   . ASP B 352 ? 0.5341 0.5998 0.7112 -0.0063 0.0239  0.0801  352 ASP B C   
7030  O O   . ASP B 352 ? 0.5157 0.5888 0.7001 -0.0115 0.0243  0.0904  352 ASP B O   
7031  C CB  . ASP B 352 ? 0.5494 0.5983 0.7433 -0.0077 0.0102  0.0760  352 ASP B CB  
7032  C CG  . ASP B 352 ? 0.6522 0.6856 0.8435 -0.0088 0.0018  0.0703  352 ASP B CG  
7033  O OD1 . ASP B 352 ? 0.7021 0.7249 0.8779 -0.0065 0.0014  0.0636  352 ASP B OD1 
7034  O OD2 . ASP B 352 ? 0.7393 0.7719 0.9441 -0.0125 -0.0043 0.0721  352 ASP B OD2 
7035  N N   . GLY B 353 ? 0.5337 0.6059 0.7030 -0.0008 0.0304  0.0740  353 GLY B N   
7036  C CA  . GLY B 353 ? 0.5083 0.5993 0.6742 -0.0004 0.0394  0.0773  353 GLY B CA  
7037  C C   . GLY B 353 ? 0.5144 0.6256 0.6974 -0.0001 0.0453  0.0823  353 GLY B C   
7038  O O   . GLY B 353 ? 0.5587 0.6887 0.7379 0.0001  0.0544  0.0847  353 GLY B O   
7039  N N   . GLU B 354 ? 0.5120 0.6228 0.7140 -0.0004 0.0406  0.0839  354 GLU B N   
7040  C CA  . GLU B 354 ? 0.4604 0.5933 0.6825 -0.0001 0.0459  0.0878  354 GLU B CA  
7041  C C   . GLU B 354 ? 0.4936 0.6323 0.7366 -0.0093 0.0416  0.0995  354 GLU B C   
7042  O O   . GLU B 354 ? 0.5362 0.6976 0.7953 -0.0125 0.0480  0.1064  354 GLU B O   
7043  C CB  . GLU B 354 ? 0.4807 0.6128 0.7114 0.0091  0.0441  0.0780  354 GLU B CB  
7044  C CG  . GLU B 354 ? 0.4844 0.5980 0.7200 0.0089  0.0317  0.0760  354 GLU B CG  
7045  C CD  . GLU B 354 ? 0.5592 0.6478 0.7729 0.0113  0.0269  0.0689  354 GLU B CD  
7046  O OE1 . GLU B 354 ? 0.4800 0.5602 0.6882 0.0189  0.0260  0.0612  354 GLU B OE1 
7047  O OE2 . GLU B 354 ? 0.5152 0.5928 0.7188 0.0053  0.0239  0.0714  354 GLU B OE2 
7048  N N   . ASN B 355 ? 0.4459 0.5655 0.6898 -0.0140 0.0312  0.1011  355 ASN B N   
7049  C CA  . ASN B 355 ? 0.4075 0.5294 0.6738 -0.0220 0.0252  0.1087  355 ASN B CA  
7050  C C   . ASN B 355 ? 0.4298 0.5544 0.7011 -0.0319 0.0266  0.1226  355 ASN B C   
7051  O O   . ASN B 355 ? 0.5372 0.6687 0.8302 -0.0399 0.0242  0.1308  355 ASN B O   
7052  C CB  . ASN B 355 ? 0.4530 0.5537 0.7194 -0.0219 0.0128  0.1016  355 ASN B CB  
7053  C CG  . ASN B 355 ? 0.5679 0.6641 0.8281 -0.0130 0.0101  0.0906  355 ASN B CG  
7054  O OD1 . ASN B 355 ? 0.4646 0.5758 0.7359 -0.0084 0.0129  0.0891  355 ASN B OD1 
7055  N ND2 . ASN B 355 ? 0.5535 0.6295 0.7966 -0.0104 0.0046  0.0834  355 ASN B ND2 
7056  N N   . CYS B 356 ? 0.4793 0.5986 0.7322 -0.0320 0.0295  0.1265  356 CYS B N   
7057  C CA  . CYS B 356 ? 0.4797 0.5973 0.7381 -0.0411 0.0281  0.1414  356 CYS B CA  
7058  C C   . CYS B 356 ? 0.4857 0.6283 0.7473 -0.0465 0.0390  0.1549  356 CYS B C   
7059  O O   . CYS B 356 ? 0.5099 0.6535 0.7819 -0.0561 0.0379  0.1706  356 CYS B O   
7060  C CB  . CYS B 356 ? 0.4778 0.5780 0.7175 -0.0391 0.0237  0.1412  356 CYS B CB  
7061  S SG  . CYS B 356 ? 0.6509 0.7608 0.8620 -0.0323 0.0324  0.1367  356 CYS B SG  
7062  N N   . TRP B 357 ? 0.4934 0.6564 0.7472 -0.0407 0.0497  0.1494  357 TRP B N   
7063  C CA  . TRP B 357 ? 0.5153 0.7044 0.7662 -0.0452 0.0619  0.1609  357 TRP B CA  
7064  C C   . TRP B 357 ? 0.4492 0.6593 0.7276 -0.0537 0.0665  0.1713  357 TRP B C   
7065  O O   . TRP B 357 ? 0.4543 0.6820 0.7347 -0.0626 0.0740  0.1873  357 TRP B O   
7066  C CB  . TRP B 357 ? 0.5498 0.7536 0.7820 -0.0353 0.0721  0.1486  357 TRP B CB  
7067  C CG  . TRP B 357 ? 0.5091 0.6921 0.7169 -0.0279 0.0668  0.1369  357 TRP B CG  
7068  C CD1 . TRP B 357 ? 0.4920 0.6668 0.6915 -0.0178 0.0664  0.1193  357 TRP B CD1 
7069  C CD2 . TRP B 357 ? 0.5045 0.6730 0.6953 -0.0306 0.0610  0.1427  357 TRP B CD2 
7070  N NE1 . TRP B 357 ? 0.5434 0.7004 0.7221 -0.0154 0.0612  0.1137  357 TRP B NE1 
7071  C CE2 . TRP B 357 ? 0.5661 0.7203 0.7397 -0.0225 0.0578  0.1273  357 TRP B CE2 
7072  C CE3 . TRP B 357 ? 0.5407 0.7067 0.7307 -0.0388 0.0575  0.1601  357 TRP B CE3 
7073  C CZ2 . TRP B 357 ? 0.4877 0.6286 0.6446 -0.0227 0.0517  0.1277  357 TRP B CZ2 
7074  C CZ3 . TRP B 357 ? 0.5595 0.7107 0.7325 -0.0374 0.0506  0.1608  357 TRP B CZ3 
7075  C CH2 . TRP B 357 ? 0.4514 0.5919 0.6087 -0.0295 0.0480  0.1442  357 TRP B CH2 
7076  N N   . GLU B 358 ? 0.4920 0.7019 0.7921 -0.0522 0.0616  0.1634  358 GLU B N   
7077  C CA  . GLU B 358 ? 0.4768 0.7093 0.8064 -0.0609 0.0653  0.1724  358 GLU B CA  
7078  C C   . GLU B 358 ? 0.4786 0.7039 0.8211 -0.0761 0.0607  0.1912  358 GLU B C   
7079  O O   . GLU B 358 ? 0.4692 0.7169 0.8325 -0.0866 0.0670  0.2037  358 GLU B O   
7080  C CB  . GLU B 358 ? 0.4848 0.7157 0.8352 -0.0566 0.0574  0.1605  358 GLU B CB  
7081  C CG  . GLU B 358 ? 0.5394 0.7374 0.8787 -0.0508 0.0436  0.1490  358 GLU B CG  
7082  C CD  . GLU B 358 ? 0.6355 0.8344 0.9902 -0.0451 0.0361  0.1373  358 GLU B CD  
7083  O OE1 . GLU B 358 ? 0.6349 0.8376 1.0145 -0.0532 0.0291  0.1409  358 GLU B OE1 
7084  O OE2 . GLU B 358 ? 0.5620 0.7572 0.9041 -0.0330 0.0364  0.1249  358 GLU B OE2 
7085  N N   . TYR B 359 ? 0.5156 0.7106 0.8475 -0.0775 0.0501  0.1936  359 TYR B N   
7086  C CA  . TYR B 359 ? 0.5041 0.6866 0.8497 -0.0907 0.0437  0.2106  359 TYR B CA  
7087  C C   . TYR B 359 ? 0.4877 0.6727 0.8160 -0.0956 0.0494  0.2286  359 TYR B C   
7088  O O   . TYR B 359 ? 0.5042 0.6787 0.8435 -0.1068 0.0446  0.2459  359 TYR B O   
7089  C CB  . TYR B 359 ? 0.4368 0.5846 0.7855 -0.0890 0.0278  0.2021  359 TYR B CB  
7090  C CG  . TYR B 359 ? 0.4230 0.5679 0.7856 -0.0849 0.0207  0.1853  359 TYR B CG  
7091  C CD1 . TYR B 359 ? 0.4780 0.6283 0.8707 -0.0946 0.0157  0.1880  359 TYR B CD1 
7092  C CD2 . TYR B 359 ? 0.4096 0.5472 0.7551 -0.0720 0.0186  0.1674  359 TYR B CD2 
7093  C CE1 . TYR B 359 ? 0.5243 0.6736 0.9283 -0.0908 0.0078  0.1729  359 TYR B CE1 
7094  C CE2 . TYR B 359 ? 0.4755 0.6107 0.8313 -0.0683 0.0114  0.1540  359 TYR B CE2 
7095  C CZ  . TYR B 359 ? 0.6392 0.7810 1.0238 -0.0773 0.0056  0.1566  359 TYR B CZ  
7096  O OH  . TYR B 359 ? 0.7517 0.8929 1.1459 -0.0739 -0.0030 0.1437  359 TYR B OH  
7097  N N   . TYR B 360 ? 0.4598 0.6578 0.7613 -0.0876 0.0586  0.2250  360 TYR B N   
7098  C CA  . TYR B 360 ? 0.5014 0.7083 0.7842 -0.0924 0.0648  0.2424  360 TYR B CA  
7099  C C   . TYR B 360 ? 0.5622 0.8061 0.8515 -0.1005 0.0803  0.2546  360 TYR B C   
7100  O O   . TYR B 360 ? 0.5117 0.7779 0.8143 -0.0978 0.0883  0.2443  360 TYR B O   
7101  C CB  . TYR B 360 ? 0.5098 0.7148 0.7594 -0.0807 0.0667  0.2315  360 TYR B CB  
7102  C CG  . TYR B 360 ? 0.5493 0.7221 0.7886 -0.0743 0.0531  0.2241  360 TYR B CG  
7103  C CD1 . TYR B 360 ? 0.5447 0.6951 0.7979 -0.0703 0.0428  0.2104  360 TYR B CD1 
7104  C CD2 . TYR B 360 ? 0.5216 0.6892 0.7370 -0.0719 0.0508  0.2301  360 TYR B CD2 
7105  C CE1 . TYR B 360 ? 0.6076 0.7323 0.8521 -0.0645 0.0320  0.2027  360 TYR B CE1 
7106  C CE2 . TYR B 360 ? 0.6258 0.7676 0.8347 -0.0657 0.0389  0.2226  360 TYR B CE2 
7107  C CZ  . TYR B 360 ? 0.6478 0.7687 0.8716 -0.0620 0.0304  0.2087  360 TYR B CZ  
7108  O OH  . TYR B 360 ? 0.6160 0.7147 0.8342 -0.0559 0.0201  0.2006  360 TYR B OH  
7109  N N   . GLU B 361 ? 0.6550 0.7295 0.7670 -0.1273 0.1270  0.1812  361 GLU B N   
7110  C CA  . GLU B 361 ? 0.7615 0.8924 0.8846 -0.1311 0.1344  0.1954  361 GLU B CA  
7111  C C   . GLU B 361 ? 0.7917 0.9715 0.9046 -0.1123 0.1312  0.1791  361 GLU B C   
7112  O O   . GLU B 361 ? 0.8460 1.0249 0.9411 -0.0947 0.1291  0.1728  361 GLU B O   
7113  C CB  . GLU B 361 ? 0.6881 0.8257 0.8128 -0.1326 0.1472  0.2300  361 GLU B CB  
7114  C CG  . GLU B 361 ? 0.8318 0.9199 0.9699 -0.1522 0.1514  0.2474  361 GLU B CG  
7115  C CD  . GLU B 361 ? 0.9776 1.0925 1.1386 -0.1729 0.1592  0.2684  361 GLU B CD  
7116  O OE1 . GLU B 361 ? 1.1768 1.3536 1.3410 -0.1686 0.1641  0.2758  361 GLU B OE1 
7117  O OE2 . GLU B 361 ? 1.1696 1.2445 1.3458 -0.1938 0.1608  0.2773  361 GLU B OE2 
7118  N N   . GLU B 362 ? 0.7446 0.9669 0.8697 -0.1162 0.1306  0.1712  362 GLU B N   
7119  C CA  . GLU B 362 ? 0.7671 1.0356 0.8851 -0.0986 0.1281  0.1534  362 GLU B CA  
7120  C C   . GLU B 362 ? 0.7134 0.9541 0.8181 -0.0855 0.1164  0.1255  362 GLU B C   
7121  O O   . GLU B 362 ? 0.6884 0.9462 0.7786 -0.0681 0.1148  0.1151  362 GLU B O   
7122  C CB  . GLU B 362 ? 0.8178 1.1300 0.9250 -0.0858 0.1375  0.1691  362 GLU B CB  
7123  C CG  . GLU B 362 ? 0.8811 1.2134 0.9995 -0.0984 0.1502  0.2034  362 GLU B CG  
7124  C CD  . GLU B 362 ? 0.9657 1.3697 1.0828 -0.0891 0.1590  0.2125  362 GLU B CD  
7125  O OE1 . GLU B 362 ? 0.9832 1.4202 1.0925 -0.0737 0.1550  0.1886  362 GLU B OE1 
7126  O OE2 . GLU B 362 ? 0.9772 1.4042 1.1011 -0.0969 0.1703  0.2436  362 GLU B OE2 
7127  N N   . ASN B 363 ? 0.6920 0.8900 0.8016 -0.0950 0.1081  0.1138  363 ASN B N   
7128  C CA  . ASN B 363 ? 0.6743 0.8462 0.7744 -0.0852 0.0967  0.0890  363 ASN B CA  
7129  C C   . ASN B 363 ? 0.6284 0.7824 0.7089 -0.0708 0.0958  0.0878  363 ASN B C   
7130  O O   . ASN B 363 ? 0.6972 0.8540 0.7690 -0.0577 0.0890  0.0691  363 ASN B O   
7131  C CB  . ASN B 363 ? 0.5707 0.7775 0.6761 -0.0755 0.0915  0.0686  363 ASN B CB  
7132  C CG  . ASN B 363 ? 0.6340 0.8114 0.7371 -0.0712 0.0795  0.0465  363 ASN B CG  
7133  O OD1 . ASN B 363 ? 0.6794 0.8236 0.7868 -0.0829 0.0745  0.0451  363 ASN B OD1 
7134  N ND2 . ASN B 363 ? 0.6418 0.8315 0.7380 -0.0547 0.0748  0.0291  363 ASN B ND2 
7135  N N   . GLY B 364 ? 0.6363 0.7723 0.7108 -0.0730 0.1025  0.1083  364 GLY B N   
7136  C CA  . GLY B 364 ? 0.7085 0.8355 0.7656 -0.0588 0.1022  0.1097  364 GLY B CA  
7137  C C   . GLY B 364 ? 0.6278 0.8025 0.6754 -0.0436 0.1039  0.1060  364 GLY B C   
7138  O O   . GLY B 364 ? 0.7148 0.8865 0.7482 -0.0324 0.1028  0.1065  364 GLY B O   
7139  N N   . ILE B 365 ? 0.5996 0.8199 0.6541 -0.0425 0.1065  0.1014  365 ILE B N   
7140  C CA  . ILE B 365 ? 0.6450 0.9127 0.6891 -0.0278 0.1086  0.0961  365 ILE B CA  
7141  C C   . ILE B 365 ? 0.7015 0.9839 0.7348 -0.0233 0.1167  0.1206  365 ILE B C   
7142  O O   . ILE B 365 ? 0.7066 1.0033 0.7249 -0.0105 0.1141  0.1138  365 ILE B O   
7143  C CB  . ILE B 365 ? 0.6639 0.9796 0.7183 -0.0273 0.1121  0.0896  365 ILE B CB  
7144  C CG1 . ILE B 365 ? 0.5737 0.8768 0.6368 -0.0263 0.1025  0.0627  365 ILE B CG1 
7145  C CG2 . ILE B 365 ? 0.6855 1.0537 0.7273 -0.0121 0.1160  0.0855  365 ILE B CG2 
7146  C CD1 . ILE B 365 ? 0.5257 0.8633 0.6054 -0.0305 0.1060  0.0611  365 ILE B CD1 
7147  N N   . PRO B 366 ? 0.7096 0.9890 0.7500 -0.0333 0.1263  0.1499  366 PRO B N   
7148  C CA  . PRO B 366 ? 0.7239 1.0165 0.7538 -0.0267 0.1338  0.1755  366 PRO B CA  
7149  C C   . PRO B 366 ? 0.6728 0.9229 0.6920 -0.0207 0.1293  0.1765  366 PRO B C   
7150  O O   . PRO B 366 ? 0.7229 0.9938 0.7285 -0.0083 0.1304  0.1837  366 PRO B O   
7151  C CB  . PRO B 366 ? 0.6907 0.9817 0.7352 -0.0412 0.1449  0.2071  366 PRO B CB  
7152  C CG  . PRO B 366 ? 0.6736 0.9758 0.7347 -0.0531 0.1439  0.1960  366 PRO B CG  
7153  C CD  . PRO B 366 ? 0.7265 0.9971 0.7858 -0.0510 0.1312  0.1631  366 PRO B CD  
7154  N N   . PHE B 367 ? 0.6197 0.8143 0.6446 -0.0288 0.1242  0.1694  367 PHE B N   
7155  C CA  . PHE B 367 ? 0.6566 0.8125 0.6717 -0.0219 0.1204  0.1694  367 PHE B CA  
7156  C C   . PHE B 367 ? 0.6924 0.8644 0.6944 -0.0087 0.1113  0.1464  367 PHE B C   
7157  O O   . PHE B 367 ? 0.6561 0.8368 0.6466 0.0023  0.1114  0.1537  367 PHE B O   
7158  C CB  . PHE B 367 ? 0.7189 0.8164 0.7418 -0.0328 0.1165  0.1622  367 PHE B CB  
7159  C CG  . PHE B 367 ? 0.6634 0.7240 0.6761 -0.0244 0.1115  0.1565  367 PHE B CG  
7160  C CD1 . PHE B 367 ? 0.6917 0.7337 0.6997 -0.0183 0.1180  0.1790  367 PHE B CD1 
7161  C CD2 . PHE B 367 ? 0.6991 0.7459 0.7078 -0.0218 0.1009  0.1300  367 PHE B CD2 
7162  C CE1 . PHE B 367 ? 0.6761 0.6884 0.6755 -0.0092 0.1141  0.1740  367 PHE B CE1 
7163  C CE2 . PHE B 367 ? 0.8287 0.8462 0.8287 -0.0141 0.0969  0.1260  367 PHE B CE2 
7164  C CZ  . PHE B 367 ? 0.6769 0.6783 0.6721 -0.0076 0.1036  0.1473  367 PHE B CZ  
7165  N N   . LEU B 368 ? 0.5904 0.7671 0.5955 -0.0099 0.1032  0.1190  368 LEU B N   
7166  C CA  . LEU B 368 ? 0.5964 0.7797 0.5918 0.0003  0.0937  0.0957  368 LEU B CA  
7167  C C   . LEU B 368 ? 0.5716 0.8074 0.5560 0.0114  0.0955  0.0955  368 LEU B C   
7168  O O   . LEU B 368 ? 0.5903 0.8323 0.5639 0.0199  0.0901  0.0877  368 LEU B O   
7169  C CB  . LEU B 368 ? 0.5606 0.7359 0.5638 -0.0032 0.0855  0.0689  368 LEU B CB  
7170  C CG  . LEU B 368 ? 0.6306 0.7543 0.6395 -0.0110 0.0801  0.0636  368 LEU B CG  
7171  C CD1 . LEU B 368 ? 0.6790 0.7976 0.6952 -0.0123 0.0713  0.0390  368 LEU B CD1 
7172  C CD2 . LEU B 368 ? 0.6840 0.7817 0.6826 -0.0052 0.0771  0.0665  368 LEU B CD2 
7173  N N   . GLU B 369 ? 0.6227 0.9001 0.6096 0.0110  0.1029  0.1040  369 GLU B N   
7174  C CA  . GLU B 369 ? 0.5932 0.9255 0.5680 0.0219  0.1046  0.1021  369 GLU B CA  
7175  C C   . GLU B 369 ? 0.5864 0.9297 0.5507 0.0280  0.1096  0.1282  369 GLU B C   
7176  O O   . GLU B 369 ? 0.5704 0.9489 0.5214 0.0381  0.1067  0.1224  369 GLU B O   
7177  C CB  . GLU B 369 ? 0.5612 0.9391 0.5412 0.0209  0.1121  0.1047  369 GLU B CB  
7178  C CG  . GLU B 369 ? 0.5884 0.9688 0.5763 0.0206  0.1063  0.0745  369 GLU B CG  
7179  C CD  . GLU B 369 ? 0.7045 1.1387 0.6960 0.0232  0.1137  0.0740  369 GLU B CD  
7180  O OE1 . GLU B 369 ? 0.7801 1.2390 0.7743 0.0190  0.1244  0.1019  369 GLU B OE1 
7181  O OE2 . GLU B 369 ? 0.7500 1.2018 0.7423 0.0300  0.1093  0.0462  369 GLU B OE2 
7182  N N   . LYS B 370 ? 0.5829 0.8962 0.5533 0.0224  0.1166  0.1564  370 LYS B N   
7183  C CA  . LYS B 370 ? 0.6046 0.9234 0.5666 0.0301  0.1213  0.1829  370 LYS B CA  
7184  C C   . LYS B 370 ? 0.6918 0.9809 0.6470 0.0362  0.1129  0.1725  370 LYS B C   
7185  O O   . LYS B 370 ? 0.7495 1.0645 0.6934 0.0469  0.1117  0.1794  370 LYS B O   
7186  C CB  . LYS B 370 ? 0.6192 0.9113 0.5917 0.0227  0.1322  0.2166  370 LYS B CB  
7187  C CG  . LYS B 370 ? 0.6402 0.9750 0.6086 0.0286  0.1429  0.2505  370 LYS B CG  
7188  C CD  . LYS B 370 ? 0.6709 1.0127 0.6272 0.0427  0.1423  0.2650  370 LYS B CD  
7189  C CE  . LYS B 370 ? 0.8038 1.1896 0.7564 0.0495  0.1532  0.3025  370 LYS B CE  
7190  N NZ  . LYS B 370 ? 0.8546 1.2728 0.7923 0.0656  0.1507  0.3113  370 LYS B NZ  
7191  N N   . LEU B 371 ? 0.6438 0.8825 0.6059 0.0295  0.1069  0.1566  371 LEU B N   
7192  C CA  . LEU B 371 ? 0.6623 0.8743 0.6192 0.0347  0.0992  0.1468  371 LEU B CA  
7193  C C   . LEU B 371 ? 0.6797 0.9260 0.6274 0.0413  0.0898  0.1229  371 LEU B C   
7194  O O   . LEU B 371 ? 0.6791 0.9426 0.6178 0.0499  0.0872  0.1275  371 LEU B O   
7195  C CB  . LEU B 371 ? 0.7059 0.8634 0.6716 0.0258  0.0947  0.1330  371 LEU B CB  
7196  C CG  . LEU B 371 ? 0.6204 0.7524 0.5820 0.0298  0.0861  0.1189  371 LEU B CG  
7197  C CD1 . LEU B 371 ? 0.5682 0.6817 0.5259 0.0374  0.0912  0.1415  371 LEU B CD1 
7198  C CD2 . LEU B 371 ? 0.6261 0.7180 0.5956 0.0206  0.0806  0.1005  371 LEU B CD2 
7199  N N   . TYR B 372 ? 0.6141 0.8718 0.5649 0.0373  0.0846  0.0973  372 TYR B N   
7200  C CA  . TYR B 372 ? 0.6599 0.9456 0.6037 0.0422  0.0754  0.0713  372 TYR B CA  
7201  C C   . TYR B 372 ? 0.6251 0.9689 0.5564 0.0509  0.0779  0.0785  372 TYR B C   
7202  O O   . TYR B 372 ? 0.5946 0.9595 0.5177 0.0557  0.0702  0.0645  372 TYR B O   
7203  C CB  . TYR B 372 ? 0.5472 0.8328 0.4983 0.0379  0.0711  0.0447  372 TYR B CB  
7204  C CG  . TYR B 372 ? 0.5913 0.8258 0.5538 0.0302  0.0666  0.0352  372 TYR B CG  
7205  C CD1 . TYR B 372 ? 0.6672 0.8617 0.6301 0.0283  0.0639  0.0421  372 TYR B CD1 
7206  C CD2 . TYR B 372 ? 0.6447 0.8742 0.6172 0.0259  0.0651  0.0194  372 TYR B CD2 
7207  C CE1 . TYR B 372 ? 0.7181 0.8700 0.6898 0.0216  0.0596  0.0331  372 TYR B CE1 
7208  C CE2 . TYR B 372 ? 0.6428 0.8298 0.6251 0.0193  0.0604  0.0117  372 TYR B CE2 
7209  C CZ  . TYR B 372 ? 0.6301 0.7791 0.6113 0.0168  0.0576  0.0185  372 TYR B CZ  
7210  O OH  . TYR B 372 ? 0.6841 0.7953 0.6736 0.0105  0.0529  0.0109  372 TYR B OH  
7211  N N   . SER B 373 ? 0.5774 0.9506 0.5074 0.0524  0.0883  0.1004  373 SER B N   
7212  C CA  . SER B 373 ? 0.6390 1.0724 0.5557 0.0614  0.0911  0.1096  373 SER B CA  
7213  C C   . SER B 373 ? 0.7157 1.1513 0.6257 0.0683  0.0919  0.1335  373 SER B C   
7214  O O   . SER B 373 ? 0.7036 1.1785 0.6022 0.0755  0.0867  0.1278  373 SER B O   
7215  C CB  . SER B 373 ? 0.5835 1.0514 0.5014 0.0611  0.1027  0.1287  373 SER B CB  
7216  O OG  . SER B 373 ? 0.6165 1.0703 0.5388 0.0602  0.1127  0.1671  373 SER B OG  
7217  N N   . THR B 374 ? 0.6593 1.0535 0.5769 0.0666  0.0983  0.1594  374 THR B N   
7218  C CA  . THR B 374 ? 0.6729 1.0672 0.5858 0.0755  0.1002  0.1839  374 THR B CA  
7219  C C   . THR B 374 ? 0.7225 1.1085 0.6316 0.0783  0.0887  0.1640  374 THR B C   
7220  O O   . THR B 374 ? 0.8204 1.2414 0.7208 0.0872  0.0860  0.1717  374 THR B O   
7221  C CB  . THR B 374 ? 0.6985 1.0419 0.6217 0.0731  0.1093  0.2113  374 THR B CB  
7222  O OG1 . THR B 374 ? 0.7088 1.0673 0.6364 0.0699  0.1203  0.2342  374 THR B OG1 
7223  C CG2 . THR B 374 ? 0.7635 1.1016 0.6833 0.0845  0.1113  0.2350  374 THR B CG2 
7224  N N   . LEU B 375 ? 0.7546 1.0982 0.6709 0.0704  0.0816  0.1392  375 LEU B N   
7225  C CA  . LEU B 375 ? 0.7217 1.0581 0.6364 0.0710  0.0705  0.1197  375 LEU B CA  
7226  C C   . LEU B 375 ? 0.6853 1.0745 0.5909 0.0730  0.0621  0.0989  375 LEU B C   
7227  O O   . LEU B 375 ? 0.7661 1.1720 0.6675 0.0764  0.0550  0.0949  375 LEU B O   
7228  C CB  . LEU B 375 ? 0.6157 0.9017 0.5402 0.0615  0.0649  0.0974  375 LEU B CB  
7229  C CG  . LEU B 375 ? 0.6371 0.8694 0.5696 0.0588  0.0713  0.1133  375 LEU B CG  
7230  C CD1 . LEU B 375 ? 0.6417 0.8314 0.5814 0.0511  0.0641  0.0917  375 LEU B CD1 
7231  C CD2 . LEU B 375 ? 0.6905 0.9185 0.6196 0.0685  0.0756  0.1384  375 LEU B CD2 
7232  N N   . GLU B 376 ? 0.6294 1.0469 0.5321 0.0709  0.0628  0.0846  376 GLU B N   
7233  C CA  . GLU B 376 ? 0.7259 1.1925 0.6191 0.0727  0.0550  0.0605  376 GLU B CA  
7234  C C   . GLU B 376 ? 0.7436 1.2651 0.6242 0.0818  0.0558  0.0785  376 GLU B C   
7235  O O   . GLU B 376 ? 0.6546 1.2142 0.5271 0.0826  0.0467  0.0587  376 GLU B O   
7236  C CB  . GLU B 376 ? 0.6856 1.1739 0.5775 0.0714  0.0583  0.0453  376 GLU B CB  
7237  C CG  . GLU B 376 ? 0.6497 1.1403 0.5423 0.0678  0.0483  0.0046  376 GLU B CG  
7238  C CD  . GLU B 376 ? 0.7880 1.3103 0.6776 0.0703  0.0531  -0.0081 376 GLU B CD  
7239  O OE1 . GLU B 376 ? 0.7939 1.3200 0.6862 0.0712  0.0642  0.0143  376 GLU B OE1 
7240  O OE2 . GLU B 376 ? 0.8603 1.4048 0.7453 0.0714  0.0462  -0.0404 376 GLU B OE2 
7241  N N   . LYS B 377 ? 0.7326 1.2597 0.6119 0.0885  0.0663  0.1159  377 LYS B N   
7242  C CA  . LYS B 377 ? 0.7394 1.3224 0.6072 0.0990  0.0685  0.1384  377 LYS B CA  
7243  C C   . LYS B 377 ? 0.7557 1.3214 0.6268 0.1057  0.0694  0.1643  377 LYS B C   
7244  O O   . LYS B 377 ? 0.8988 1.5047 0.7629 0.1164  0.0735  0.1918  377 LYS B O   
7245  C CB  . LYS B 377 ? 0.7457 1.3611 0.6090 0.1038  0.0809  0.1646  377 LYS B CB  
7246  C CG  . LYS B 377 ? 0.7261 1.3723 0.5846 0.1000  0.0811  0.1407  377 LYS B CG  
7247  C CD  . LYS B 377 ? 0.7348 1.4263 0.5814 0.1007  0.0691  0.1054  377 LYS B CD  
7248  C CE  . LYS B 377 ? 0.7789 1.5169 0.6167 0.1020  0.0719  0.0879  377 LYS B CE  
7249  N NZ  . LYS B 377 ? 0.6975 1.4557 0.5284 0.0995  0.0595  0.0421  377 LYS B NZ  
7250  N N   . GLU B 378 ? 0.7953 1.3046 0.6768 0.1010  0.0659  0.1567  378 GLU B N   
7251  C CA  . GLU B 378 ? 0.8730 1.3655 0.7580 0.1084  0.0662  0.1765  378 GLU B CA  
7252  C C   . GLU B 378 ? 0.8436 1.3431 0.7292 0.1041  0.0527  0.1504  378 GLU B C   
7253  O O   . GLU B 378 ? 0.8403 1.3002 0.7333 0.0942  0.0468  0.1260  378 GLU B O   
7254  C CB  . GLU B 378 ? 0.8046 1.2287 0.7007 0.1071  0.0740  0.1901  378 GLU B CB  
7255  C CG  . GLU B 378 ? 0.9508 1.3583 0.8500 0.1077  0.0872  0.2149  378 GLU B CG  
7256  C CD  . GLU B 378 ? 1.0934 1.5438 0.9866 0.1202  0.0959  0.2512  378 GLU B CD  
7257  O OE1 . GLU B 378 ? 1.0512 1.5647 0.9338 0.1237  0.0930  0.2497  378 GLU B OE1 
7258  O OE2 . GLU B 378 ? 1.2003 1.6204 1.0995 0.1267  0.1059  0.2818  378 GLU B OE2 
7259  N N   . GLU B 379 ? 0.7999 1.3511 0.6787 0.1112  0.0478  0.1574  379 GLU B N   
7260  C CA  . GLU B 379 ? 0.8198 1.3856 0.7003 0.1053  0.0344  0.1336  379 GLU B CA  
7261  C C   . GLU B 379 ? 0.8574 1.3824 0.7484 0.1068  0.0338  0.1416  379 GLU B C   
7262  O O   . GLU B 379 ? 0.8622 1.3822 0.7587 0.0983  0.0234  0.1197  379 GLU B O   
7263  C CB  . GLU B 379 ? 0.7647 1.4048 0.6346 0.1118  0.0293  0.1395  379 GLU B CB  
7264  C CG  . GLU B 379 ? 0.9415 1.6197 0.8000 0.1180  0.0370  0.1526  379 GLU B CG  
7265  C CD  . GLU B 379 ? 1.1165 1.8748 0.9616 0.1215  0.0299  0.1479  379 GLU B CD  
7266  O OE1 . GLU B 379 ? 1.0958 1.8840 0.9320 0.1158  0.0260  0.1228  379 GLU B OE1 
7267  O OE2 . GLU B 379 ? 1.1156 1.9102 0.9589 0.1306  0.0282  0.1689  379 GLU B OE2 
7268  N N   . TRP B 380 ? 0.7529 1.2486 0.6473 0.1174  0.0450  0.1722  380 TRP B N   
7269  C CA  . TRP B 380 ? 0.7024 1.1589 0.6058 0.1207  0.0459  0.1791  380 TRP B CA  
7270  C C   . TRP B 380 ? 0.6898 1.0827 0.6010 0.1097  0.0455  0.1599  380 TRP B C   
7271  O O   . TRP B 380 ? 0.7015 1.0608 0.6192 0.1119  0.0464  0.1632  380 TRP B O   
7272  C CB  . TRP B 380 ? 0.6661 1.1139 0.5701 0.1380  0.0582  0.2176  380 TRP B CB  
7273  C CG  . TRP B 380 ? 0.7124 1.1180 0.6177 0.1388  0.0702  0.2318  380 TRP B CG  
7274  C CD1 . TRP B 380 ? 0.7172 1.1433 0.6173 0.1406  0.0770  0.2464  380 TRP B CD1 
7275  C CD2 . TRP B 380 ? 0.7187 1.0565 0.6315 0.1368  0.0767  0.2328  380 TRP B CD2 
7276  N NE1 . TRP B 380 ? 0.8443 1.2179 0.7500 0.1385  0.0873  0.2571  380 TRP B NE1 
7277  C CE2 . TRP B 380 ? 0.7165 1.0349 0.6295 0.1360  0.0868  0.2477  380 TRP B CE2 
7278  C CE3 . TRP B 380 ? 0.7105 1.0045 0.6296 0.1352  0.0748  0.2223  380 TRP B CE3 
7279  C CZ2 . TRP B 380 ? 0.7261 0.9819 0.6459 0.1325  0.0942  0.2507  380 TRP B CZ2 
7280  C CZ3 . TRP B 380 ? 0.7195 0.9530 0.6435 0.1332  0.0824  0.2247  380 TRP B CZ3 
7281  C CH2 . TRP B 380 ? 0.8091 1.0232 0.7335 0.1313  0.0916  0.2379  380 TRP B CH2 
7282  N N   . ILE B 381 ? 0.7802 1.1591 0.6907 0.0989  0.0445  0.1405  381 ILE B N   
7283  C CA  . ILE B 381 ? 0.7856 1.1121 0.7037 0.0879  0.0422  0.1201  381 ILE B CA  
7284  C C   . ILE B 381 ? 0.7597 1.1022 0.6784 0.0758  0.0307  0.0869  381 ILE B C   
7285  O O   . ILE B 381 ? 0.7467 1.1284 0.6587 0.0749  0.0286  0.0781  381 ILE B O   
7286  C CB  . ILE B 381 ? 0.7832 1.0721 0.7029 0.0862  0.0521  0.1279  381 ILE B CB  
7287  C CG1 . ILE B 381 ? 0.8101 1.0809 0.7299 0.0976  0.0641  0.1609  381 ILE B CG1 
7288  C CG2 . ILE B 381 ? 0.6195 0.8579 0.5471 0.0754  0.0490  0.1078  381 ILE B CG2 
7289  C CD1 . ILE B 381 ? 0.7641 1.0263 0.6837 0.0967  0.0740  0.1751  381 ILE B CD1 
7290  N N   . GLU B 382 ? 0.6305 0.9428 0.5574 0.0671  0.0236  0.0685  382 GLU B N   
7291  C CA  . GLU B 382 ? 0.6583 0.9765 0.5888 0.0555  0.0124  0.0371  382 GLU B CA  
7292  C C   . GLU B 382 ? 0.6461 0.9114 0.5852 0.0478  0.0122  0.0244  382 GLU B C   
7293  O O   . GLU B 382 ? 0.6759 0.9125 0.6220 0.0448  0.0097  0.0246  382 GLU B O   
7294  C CB  . GLU B 382 ? 0.6457 0.9880 0.5798 0.0515  0.0020  0.0287  382 GLU B CB  
7295  C CG  . GLU B 382 ? 0.7553 1.1097 0.6930 0.0392  -0.0099 -0.0041 382 GLU B CG  
7296  C CD  . GLU B 382 ? 0.9682 1.3672 0.9064 0.0352  -0.0200 -0.0109 382 GLU B CD  
7297  O OE1 . GLU B 382 ? 0.9375 1.3799 0.8677 0.0440  -0.0177 0.0066  382 GLU B OE1 
7298  O OE2 . GLU B 382 ? 0.9584 1.3501 0.9059 0.0228  -0.0304 -0.0330 382 GLU B OE2 
7299  N N   . THR B 383 ? 0.7047 0.9608 0.6434 0.0451  0.0149  0.0147  383 THR B N   
7300  C CA  . THR B 383 ? 0.6791 0.8917 0.6266 0.0379  0.0133  0.0012  383 THR B CA  
7301  C C   . THR B 383 ? 0.6815 0.8907 0.6368 0.0293  0.0016  -0.0237 383 THR B C   
7302  O O   . THR B 383 ? 0.6032 0.8448 0.5563 0.0271  -0.0051 -0.0392 383 THR B O   
7303  C CB  . THR B 383 ? 0.5945 0.8052 0.5413 0.0376  0.0187  -0.0034 383 THR B CB  
7304  O OG1 . THR B 383 ? 0.6419 0.8871 0.5856 0.0367  0.0139  -0.0237 383 THR B OG1 
7305  C CG2 . THR B 383 ? 0.5650 0.7831 0.5056 0.0445  0.0303  0.0230  383 THR B CG2 
7306  N N   . LEU B 384 ? 0.5991 0.7689 0.5634 0.0240  -0.0011 -0.0274 384 LEU B N   
7307  C CA  . LEU B 384 ? 0.5815 0.7435 0.5554 0.0154  -0.0117 -0.0458 384 LEU B CA  
7308  C C   . LEU B 384 ? 0.5657 0.6885 0.5493 0.0104  -0.0135 -0.0566 384 LEU B C   
7309  O O   . LEU B 384 ? 0.6036 0.7015 0.5869 0.0127  -0.0072 -0.0465 384 LEU B O   
7310  C CB  . LEU B 384 ? 0.5450 0.7071 0.5221 0.0141  -0.0145 -0.0345 384 LEU B CB  
7311  C CG  . LEU B 384 ? 0.5742 0.7793 0.5444 0.0188  -0.0147 -0.0241 384 LEU B CG  
7312  C CD1 . LEU B 384 ? 0.6947 0.8926 0.6670 0.0224  -0.0122 -0.0049 384 LEU B CD1 
7313  C CD2 . LEU B 384 ? 0.6568 0.8927 0.6303 0.0106  -0.0256 -0.0450 384 LEU B CD2 
7314  N N   . THR B 385 ? 0.5667 0.6846 0.5596 0.0032  -0.0226 -0.0773 385 THR B N   
7315  C CA  . THR B 385 ? 0.4989 0.5807 0.5033 -0.0012 -0.0258 -0.0858 385 THR B CA  
7316  C C   . THR B 385 ? 0.5728 0.6325 0.5832 -0.0053 -0.0277 -0.0736 385 THR B C   
7317  O O   . THR B 385 ? 0.6019 0.6762 0.6101 -0.0059 -0.0285 -0.0634 385 THR B O   
7318  C CB  . THR B 385 ? 0.4834 0.5651 0.4973 -0.0065 -0.0345 -0.1114 385 THR B CB  
7319  O OG1 . THR B 385 ? 0.5734 0.6557 0.5951 -0.0152 -0.0428 -0.1150 385 THR B OG1 
7320  C CG2 . THR B 385 ? 0.6224 0.7386 0.6276 -0.0025 -0.0338 -0.1252 385 THR B CG2 
7321  N N   . LEU B 386 ? 0.6080 0.6359 0.6263 -0.0074 -0.0285 -0.0742 386 LEU B N   
7322  C CA  . LEU B 386 ? 0.6121 0.6209 0.6361 -0.0112 -0.0304 -0.0635 386 LEU B CA  
7323  C C   . LEU B 386 ? 0.6961 0.7129 0.7302 -0.0197 -0.0391 -0.0698 386 LEU B C   
7324  O O   . LEU B 386 ? 0.6880 0.7074 0.7238 -0.0222 -0.0397 -0.0573 386 LEU B O   
7325  C CB  . LEU B 386 ? 0.6241 0.6022 0.6550 -0.0120 -0.0308 -0.0643 386 LEU B CB  
7326  C CG  . LEU B 386 ? 0.6291 0.5990 0.6526 -0.0063 -0.0233 -0.0590 386 LEU B CG  
7327  C CD1 . LEU B 386 ? 0.5908 0.5356 0.6226 -0.0079 -0.0254 -0.0604 386 LEU B CD1 
7328  C CD2 . LEU B 386 ? 0.4596 0.4314 0.4712 -0.0019 -0.0155 -0.0415 386 LEU B CD2 
7329  N N   . GLU B 387 ? 0.7080 0.7298 0.7495 -0.0245 -0.0459 -0.0897 387 GLU B N   
7330  C CA  . GLU B 387 ? 0.6501 0.6800 0.7024 -0.0350 -0.0548 -0.0979 387 GLU B CA  
7331  C C   . GLU B 387 ? 0.6608 0.7284 0.7050 -0.0351 -0.0547 -0.0921 387 GLU B C   
7332  O O   . GLU B 387 ? 0.6654 0.7424 0.7158 -0.0417 -0.0584 -0.0837 387 GLU B O   
7333  C CB  . GLU B 387 ? 0.6335 0.6568 0.6952 -0.0395 -0.0618 -0.1236 387 GLU B CB  
7334  C CG  . GLU B 387 ? 0.8490 0.8526 0.9299 -0.0519 -0.0710 -0.1304 387 GLU B CG  
7335  C CD  . GLU B 387 ? 1.1659 1.1683 1.2553 -0.0574 -0.0787 -0.1586 387 GLU B CD  
7336  O OE1 . GLU B 387 ? 1.2341 1.2646 1.3127 -0.0542 -0.0785 -0.1727 387 GLU B OE1 
7337  O OE2 . GLU B 387 ? 1.2134 1.1868 1.3205 -0.0646 -0.0848 -0.1666 387 GLU B OE2 
7338  N N   . GLU B 388 ? 0.5813 0.6741 0.6120 -0.0274 -0.0504 -0.0946 388 GLU B N   
7339  C CA  . GLU B 388 ? 0.6347 0.7678 0.6573 -0.0258 -0.0503 -0.0876 388 GLU B CA  
7340  C C   . GLU B 388 ? 0.6324 0.7675 0.6511 -0.0202 -0.0440 -0.0615 388 GLU B C   
7341  O O   . GLU B 388 ? 0.6088 0.7712 0.6285 -0.0220 -0.0465 -0.0535 388 GLU B O   
7342  C CB  . GLU B 388 ? 0.5540 0.7141 0.5624 -0.0172 -0.0457 -0.0921 388 GLU B CB  
7343  C CG  . GLU B 388 ? 0.5019 0.6807 0.5116 -0.0225 -0.0533 -0.1196 388 GLU B CG  
7344  C CD  . GLU B 388 ? 0.7052 0.9000 0.7024 -0.0130 -0.0472 -0.1260 388 GLU B CD  
7345  O OE1 . GLU B 388 ? 0.6941 0.8940 0.6813 -0.0035 -0.0375 -0.1060 388 GLU B OE1 
7346  O OE2 . GLU B 388 ? 0.7942 0.9968 0.7922 -0.0151 -0.0519 -0.1511 388 GLU B OE2 
7347  N N   . ALA B 389 ? 0.6142 0.7219 0.6287 -0.0131 -0.0360 -0.0490 389 ALA B N   
7348  C CA  . ALA B 389 ? 0.5160 0.6202 0.5271 -0.0072 -0.0300 -0.0273 389 ALA B CA  
7349  C C   . ALA B 389 ? 0.6182 0.7131 0.6416 -0.0155 -0.0353 -0.0245 389 ALA B C   
7350  O O   . ALA B 389 ? 0.7529 0.8585 0.7755 -0.0119 -0.0323 -0.0086 389 ALA B O   
7351  C CB  . ALA B 389 ? 0.5641 0.6399 0.5674 0.0011  -0.0207 -0.0179 389 ALA B CB  
7352  N N   . MET B 390 ? 0.5882 0.6642 0.6239 -0.0261 -0.0427 -0.0384 390 MET B N   
7353  C CA  . MET B 390 ? 0.6176 0.6856 0.6669 -0.0354 -0.0478 -0.0338 390 MET B CA  
7354  C C   . MET B 390 ? 0.7078 0.8061 0.7669 -0.0459 -0.0559 -0.0381 390 MET B C   
7355  O O   . MET B 390 ? 0.6319 0.7360 0.7010 -0.0524 -0.0582 -0.0276 390 MET B O   
7356  C CB  . MET B 390 ? 0.6898 0.7239 0.7504 -0.0422 -0.0523 -0.0441 390 MET B CB  
7357  C CG  . MET B 390 ? 0.7888 0.7958 0.8473 -0.0373 -0.0470 -0.0318 390 MET B CG  
7358  S SD  . MET B 390 ? 1.0162 1.0341 1.0709 -0.0335 -0.0416 -0.0087 390 MET B SD  
7359  C CE  . MET B 390 ? 0.8126 0.8195 0.8875 -0.0473 -0.0494 -0.0054 390 MET B CE  
7360  N N   . ARG B 391 ? 0.7341 0.8550 0.7906 -0.0482 -0.0603 -0.0532 391 ARG B N   
7361  C CA  . ARG B 391 ? 0.6525 0.8060 0.7177 -0.0595 -0.0691 -0.0601 391 ARG B CA  
7362  C C   . ARG B 391 ? 0.6386 0.8371 0.6930 -0.0515 -0.0659 -0.0486 391 ARG B C   
7363  O O   . ARG B 391 ? 0.6815 0.9143 0.7425 -0.0604 -0.0733 -0.0524 391 ARG B O   
7364  C CB  . ARG B 391 ? 0.6085 0.7600 0.6792 -0.0691 -0.0779 -0.0883 391 ARG B CB  
7365  C CG  . ARG B 391 ? 0.6726 0.7793 0.7508 -0.0711 -0.0790 -0.1008 391 ARG B CG  
7366  C CD  . ARG B 391 ? 0.7206 0.8080 0.8207 -0.0877 -0.0883 -0.1079 391 ARG B CD  
7367  N NE  . ARG B 391 ? 0.7424 0.8243 0.8505 -0.0909 -0.0862 -0.0844 391 ARG B NE  
7368  C CZ  . ARG B 391 ? 0.6590 0.7140 0.7656 -0.0838 -0.0798 -0.0695 391 ARG B CZ  
7369  N NH1 . ARG B 391 ? 0.7473 0.7762 0.8471 -0.0745 -0.0756 -0.0750 391 ARG B NH1 
7370  N NH2 . ARG B 391 ? 0.6562 0.7141 0.7683 -0.0862 -0.0777 -0.0488 391 ARG B NH2 
7371  N N   . LYS B 392 ? 0.6593 0.8586 0.6984 -0.0351 -0.0553 -0.0338 392 LYS B N   
7372  C CA  . LYS B 392 ? 0.6999 0.9407 0.7285 -0.0251 -0.0517 -0.0218 392 LYS B CA  
7373  C C   . LYS B 392 ? 0.7939 1.0585 0.8289 -0.0241 -0.0511 -0.0029 392 LYS B C   
7374  O O   . LYS B 392 ? 0.7290 0.9725 0.7665 -0.0199 -0.0455 0.0109  392 LYS B O   
7375  C CB  . LYS B 392 ? 0.6655 0.8952 0.6782 -0.0083 -0.0399 -0.0099 392 LYS B CB  
7376  C CG  . LYS B 392 ? 0.7121 0.9824 0.7129 0.0007  -0.0376 -0.0052 392 LYS B CG  
7377  C CD  . LYS B 392 ? 0.6103 0.8947 0.6087 -0.0064 -0.0443 -0.0289 392 LYS B CD  
7378  C CE  . LYS B 392 ? 0.6237 0.9351 0.6066 0.0060  -0.0378 -0.0214 392 LYS B CE  
7379  N NZ  . LYS B 392 ? 0.7323 1.0692 0.7111 0.0001  -0.0447 -0.0450 392 LYS B NZ  
7380  N N   . GLU B 393 ? 0.8147 1.1273 0.8519 -0.0274 -0.0569 -0.0027 393 GLU B N   
7381  C CA  . GLU B 393 ? 0.8506 1.1963 0.8951 -0.0258 -0.0569 0.0153  393 GLU B CA  
7382  C C   . GLU B 393 ? 0.8960 1.2655 0.9280 -0.0046 -0.0466 0.0383  393 GLU B C   
7383  O O   . GLU B 393 ? 0.9101 1.2975 0.9468 0.0023  -0.0429 0.0569  393 GLU B O   
7384  C CB  . GLU B 393 ? 0.9036 1.2930 0.9601 -0.0425 -0.0699 0.0036  393 GLU B CB  
7385  C CG  . GLU B 393 ? 0.9983 1.3739 1.0755 -0.0634 -0.0788 -0.0049 393 GLU B CG  
7386  C CD  . GLU B 393 ? 1.0715 1.4118 1.1538 -0.0596 -0.0714 0.0109  393 GLU B CD  
7387  O OE1 . GLU B 393 ? 0.9753 1.3343 1.0568 -0.0485 -0.0644 0.0331  393 GLU B OE1 
7388  O OE2 . GLU B 393 ? 1.0199 1.3157 1.1067 -0.0668 -0.0725 0.0008  393 GLU B OE2 
7389  N N   . ASP B 394 ? 0.8432 1.2135 0.8604 0.0066  -0.0414 0.0385  394 ASP B N   
7390  C CA  . ASP B 394 ? 0.8037 1.1933 0.8101 0.0273  -0.0312 0.0620  394 ASP B CA  
7391  C C   . ASP B 394 ? 0.7417 1.0909 0.7442 0.0413  -0.0189 0.0784  394 ASP B C   
7392  O O   . ASP B 394 ? 0.7919 1.1533 0.7890 0.0591  -0.0100 0.0997  394 ASP B O   
7393  C CB  . ASP B 394 ? 0.8332 1.2331 0.8257 0.0341  -0.0287 0.0591  394 ASP B CB  
7394  C CG  . ASP B 394 ? 0.9187 1.3510 0.9122 0.0198  -0.0408 0.0361  394 ASP B CG  
7395  O OD1 . ASP B 394 ? 1.0922 1.5442 1.0979 0.0048  -0.0517 0.0244  394 ASP B OD1 
7396  O OD2 . ASP B 394 ? 1.0365 1.4753 1.0188 0.0232  -0.0394 0.0292  394 ASP B OD2 
7397  N N   . VAL B 395 ? 0.7751 1.0774 0.7801 0.0344  -0.0181 0.0688  395 VAL B N   
7398  C CA  . VAL B 395 ? 0.7854 1.0477 0.7843 0.0466  -0.0069 0.0802  395 VAL B CA  
7399  C C   . VAL B 395 ? 0.6279 0.8933 0.6347 0.0487  -0.0052 0.0907  395 VAL B C   
7400  O O   . VAL B 395 ? 0.6430 0.9235 0.6625 0.0349  -0.0136 0.0848  395 VAL B O   
7401  C CB  . VAL B 395 ? 0.7499 0.9639 0.7460 0.0392  -0.0066 0.0654  395 VAL B CB  
7402  C CG1 . VAL B 395 ? 0.5717 0.7908 0.5633 0.0339  -0.0104 0.0515  395 VAL B CG1 
7403  C CG2 . VAL B 395 ? 0.7364 0.9333 0.7442 0.0246  -0.0136 0.0546  395 VAL B CG2 
7404  N N   . LYS B 396 ? 0.6021 0.8538 0.6019 0.0665  0.0063  0.1067  396 LYS B N   
7405  C CA  . LYS B 396 ? 0.6192 0.8756 0.6243 0.0723  0.0101  0.1174  396 LYS B CA  
7406  C C   . LYS B 396 ? 0.6148 0.8308 0.6210 0.0638  0.0099  0.1079  396 LYS B C   
7407  O O   . LYS B 396 ? 0.6080 0.7848 0.6067 0.0621  0.0119  0.0987  396 LYS B O   
7408  C CB  . LYS B 396 ? 0.6149 0.8716 0.6116 0.0968  0.0229  0.1365  396 LYS B CB  
7409  C CG  . LYS B 396 ? 0.7305 1.0409 0.7312 0.1076  0.0231  0.1526  396 LYS B CG  
7410  C CD  . LYS B 396 ? 0.7788 1.0911 0.7761 0.1326  0.0357  0.1725  396 LYS B CD  
7411  C CE  . LYS B 396 ? 0.8361 1.1388 0.8378 0.1334  0.0388  0.1724  396 LYS B CE  
7412  N NZ  . LYS B 396 ? 0.6423 0.9943 0.6592 0.1230  0.0307  0.1754  396 LYS B NZ  
7413  N N   . THR B 397 ? 0.6595 0.8888 0.6759 0.0577  0.0071  0.1111  397 THR B N   
7414  C CA  . THR B 397 ? 0.6366 0.8354 0.6558 0.0477  0.0053  0.1036  397 THR B CA  
7415  C C   . THR B 397 ? 0.6515 0.8561 0.6707 0.0579  0.0127  0.1164  397 THR B C   
7416  O O   . THR B 397 ? 0.7538 0.9984 0.7817 0.0606  0.0127  0.1280  397 THR B O   
7417  C CB  . THR B 397 ? 0.6762 0.8838 0.7110 0.0247  -0.0075 0.0926  397 THR B CB  
7418  O OG1 . THR B 397 ? 0.6553 0.8515 0.6883 0.0165  -0.0136 0.0772  397 THR B OG1 
7419  C CG2 . THR B 397 ? 0.6546 0.8357 0.6939 0.0164  -0.0086 0.0903  397 THR B CG2 
7420  N N   . GLU B 398 ? 0.6057 0.7737 0.6151 0.0634  0.0188  0.1136  398 GLU B N   
7421  C CA  . GLU B 398 ? 0.6085 0.7792 0.6151 0.0735  0.0263  0.1225  398 GLU B CA  
7422  C C   . GLU B 398 ? 0.5671 0.7168 0.5761 0.0606  0.0222  0.1158  398 GLU B C   
7423  O O   . GLU B 398 ? 0.6532 0.7709 0.6591 0.0518  0.0180  0.1038  398 GLU B O   
7424  C CB  . GLU B 398 ? 0.6548 0.8028 0.6449 0.0959  0.0390  0.1256  398 GLU B CB  
7425  C CG  . GLU B 398 ? 0.7247 0.8700 0.7084 0.1077  0.0474  0.1302  398 GLU B CG  
7426  C CD  . GLU B 398 ? 0.8192 0.9599 0.7918 0.1333  0.0604  0.1372  398 GLU B CD  
7427  O OE1 . GLU B 398 ? 0.8008 0.9438 0.7725 0.1418  0.0628  0.1421  398 GLU B OE1 
7428  O OE2 . GLU B 398 ? 0.9519 1.0876 0.9167 0.1458  0.0686  0.1382  398 GLU B OE2 
7429  N N   . VAL B 399 ? 0.6638 0.8347 0.6790 0.0600  0.0235  0.1253  399 VAL B N   
7430  C CA  . VAL B 399 ? 0.6763 0.8332 0.6939 0.0494  0.0205  0.1233  399 VAL B CA  
7431  C C   . VAL B 399 ? 0.6170 0.7576 0.6176 0.0655  0.0309  0.1239  399 VAL B C   
7432  O O   . VAL B 399 ? 0.6818 0.8420 0.6770 0.0821  0.0400  0.1325  399 VAL B O   
7433  C CB  . VAL B 399 ? 0.6334 0.8260 0.6699 0.0361  0.0150  0.1348  399 VAL B CB  
7434  C CG1 . VAL B 399 ? 0.5112 0.6884 0.5496 0.0266  0.0127  0.1356  399 VAL B CG1 
7435  C CG2 . VAL B 399 ? 0.6633 0.8715 0.7171 0.0187  0.0040  0.1314  399 VAL B CG2 
7436  N N   . ILE B 400 ? 0.5690 0.6758 0.5615 0.0609  0.0293  0.1139  400 ILE B N   
7437  C CA  . ILE B 400 ? 0.5775 0.6683 0.5533 0.0729  0.0373  0.1110  400 ILE B CA  
7438  C C   . ILE B 400 ? 0.5453 0.6361 0.5250 0.0607  0.0320  0.1126  400 ILE B C   
7439  O O   . ILE B 400 ? 0.5549 0.6413 0.5480 0.0436  0.0222  0.1118  400 ILE B O   
7440  C CB  . ILE B 400 ? 0.5873 0.6374 0.5475 0.0800  0.0409  0.0971  400 ILE B CB  
7441  C CG1 . ILE B 400 ? 0.5561 0.5814 0.5208 0.0636  0.0315  0.0867  400 ILE B CG1 
7442  C CG2 . ILE B 400 ? 0.6187 0.6686 0.5761 0.0925  0.0467  0.0989  400 ILE B CG2 
7443  C CD1 . ILE B 400 ? 0.4962 0.4846 0.4466 0.0681  0.0349  0.0739  400 ILE B CD1 
7444  N N   . GLU B 401 ? 0.5616 0.6578 0.5295 0.0706  0.0387  0.1150  401 GLU B N   
7445  C CA  . GLU B 401 ? 0.6195 0.7256 0.5914 0.0609  0.0348  0.1214  401 GLU B CA  
7446  C C   . GLU B 401 ? 0.6612 0.7419 0.6160 0.0637  0.0357  0.1105  401 GLU B C   
7447  O O   . GLU B 401 ? 0.6330 0.7245 0.5890 0.0576  0.0330  0.1171  401 GLU B O   
7448  C CB  . GLU B 401 ? 0.6497 0.7985 0.6253 0.0671  0.0407  0.1377  401 GLU B CB  
7449  C CG  . GLU B 401 ? 0.6597 0.8417 0.6563 0.0603  0.0379  0.1508  401 GLU B CG  
7450  C CD  . GLU B 401 ? 0.6792 0.8775 0.6977 0.0387  0.0284  0.1631  401 GLU B CD  
7451  O OE1 . GLU B 401 ? 0.6497 0.8482 0.6669 0.0339  0.0275  0.1688  401 GLU B OE1 
7452  O OE2 . GLU B 401 ? 0.6802 0.8917 0.7178 0.0262  0.0218  0.1673  401 GLU B OE2 
7453  N N   . SER B 402 ? 0.7218 0.7710 0.6619 0.0715  0.0390  0.0949  402 SER B N   
7454  C CA  . SER B 402 ? 0.7162 0.7436 0.6402 0.0728  0.0392  0.0829  402 SER B CA  
7455  C C   . SER B 402 ? 0.6936 0.6835 0.6090 0.0751  0.0402  0.0667  402 SER B C   
7456  O O   . SER B 402 ? 0.6349 0.6175 0.5511 0.0820  0.0446  0.0657  402 SER B O   
7457  C CB  . SER B 402 ? 0.5428 0.5860 0.4497 0.0876  0.0483  0.0827  402 SER B CB  
7458  O OG  . SER B 402 ? 0.6460 0.6819 0.5423 0.1051  0.0585  0.0766  402 SER B OG  
7459  N N   . VAL B 403 ? 0.6110 0.5800 0.5191 0.0688  0.0360  0.0555  403 VAL B N   
7460  C CA  . VAL B 403 ? 0.7349 0.6697 0.6344 0.0695  0.0372  0.0401  403 VAL B CA  
7461  C C   . VAL B 403 ? 0.7519 0.6762 0.6340 0.0717  0.0383  0.0275  403 VAL B C   
7462  O O   . VAL B 403 ? 0.8157 0.7572 0.6959 0.0675  0.0342  0.0309  403 VAL B O   
7463  C CB  . VAL B 403 ? 0.7449 0.6650 0.6574 0.0554  0.0285  0.0374  403 VAL B CB  
7464  C CG1 . VAL B 403 ? 0.6013 0.5282 0.5272 0.0544  0.0281  0.0448  403 VAL B CG1 
7465  C CG2 . VAL B 403 ? 0.6998 0.6309 0.6214 0.0436  0.0192  0.0420  403 VAL B CG2 
7466  N N   . LYS B 404 ? 0.7479 0.6444 0.6177 0.0777  0.0437  0.0132  404 LYS B N   
7467  C CA  . LYS B 404 ? 0.6975 0.5805 0.5514 0.0768  0.0433  -0.0027 404 LYS B CA  
7468  C C   . LYS B 404 ? 0.8133 0.6791 0.6738 0.0613  0.0345  -0.0097 404 LYS B C   
7469  O O   . LYS B 404 ? 0.7978 0.6444 0.6667 0.0571  0.0343  -0.0110 404 LYS B O   
7470  C CB  . LYS B 404 ? 0.6678 0.5268 0.5060 0.0901  0.0535  -0.0161 404 LYS B CB  
7471  C CG  . LYS B 404 ? 0.8172 0.6931 0.6387 0.1038  0.0602  -0.0205 404 LYS B CG  
7472  C CD  . LYS B 404 ? 0.9436 0.7888 0.7495 0.1168  0.0699  -0.0378 404 LYS B CD  
7473  C CE  . LYS B 404 ? 1.0021 0.8652 0.7986 0.1380  0.0809  -0.0348 404 LYS B CE  
7474  N NZ  . LYS B 404 ? 0.9175 0.7462 0.7019 0.1534  0.0916  -0.0501 404 LYS B NZ  
7475  N N   . ALA B 405 ? 0.8219 0.6986 0.6791 0.0537  0.0274  -0.0130 405 ALA B N   
7476  C CA  . ALA B 405 ? 0.7138 0.5819 0.5795 0.0398  0.0184  -0.0173 405 ALA B CA  
7477  C C   . ALA B 405 ? 0.7340 0.5711 0.5938 0.0363  0.0203  -0.0339 405 ALA B C   
7478  O O   . ALA B 405 ? 0.8322 0.6570 0.6758 0.0408  0.0247  -0.0480 405 ALA B O   
7479  C CB  . ALA B 405 ? 0.7187 0.6079 0.5803 0.0348  0.0111  -0.0166 405 ALA B CB  
7480  N N   . GLY B 406 ? 0.6794 0.5043 0.5529 0.0279  0.0171  -0.0326 406 GLY B N   
7481  C CA  . GLY B 406 ? 0.7561 0.5538 0.6276 0.0223  0.0187  -0.0452 406 GLY B CA  
7482  C C   . GLY B 406 ? 0.7466 0.5427 0.6351 0.0119  0.0133  -0.0412 406 GLY B C   
7483  O O   . GLY B 406 ? 0.7711 0.5852 0.6719 0.0090  0.0075  -0.0316 406 GLY B O   
7484  N N   . THR B 407 ? 0.8115 0.5853 0.7013 0.0063  0.0158  -0.0489 407 THR B N   
7485  C CA  . THR B 407 ? 0.7822 0.5550 0.6870 -0.0031 0.0124  -0.0463 407 THR B CA  
7486  C C   . THR B 407 ? 0.7094 0.4611 0.6157 -0.0008 0.0207  -0.0441 407 THR B C   
7487  O O   . THR B 407 ? 0.7799 0.5153 0.6764 0.0081  0.0287  -0.0450 407 THR B O   
7488  C CB  . THR B 407 ? 0.7190 0.4924 0.6262 -0.0158 0.0055  -0.0566 407 THR B CB  
7489  O OG1 . THR B 407 ? 0.7559 0.5054 0.6537 -0.0199 0.0097  -0.0690 407 THR B OG1 
7490  C CG2 . THR B 407 ? 0.6874 0.4825 0.5911 -0.0168 -0.0024 -0.0577 407 THR B CG2 
7491  N N   . TRP B 408 ? 0.6892 0.4422 0.6080 -0.0078 0.0194  -0.0406 408 TRP B N   
7492  C CA  . TRP B 408 ? 0.7268 0.4617 0.6474 -0.0066 0.0274  -0.0365 408 TRP B CA  
7493  C C   . TRP B 408 ? 0.7703 0.4796 0.6874 -0.0154 0.0301  -0.0465 408 TRP B C   
7494  O O   . TRP B 408 ? 0.7967 0.4875 0.7163 -0.0155 0.0372  -0.0418 408 TRP B O   
7495  C CB  . TRP B 408 ? 0.6145 0.3639 0.5487 -0.0098 0.0262  -0.0279 408 TRP B CB  
7496  C CG  . TRP B 408 ? 0.7032 0.4654 0.6484 -0.0213 0.0189  -0.0324 408 TRP B CG  
7497  C CD1 . TRP B 408 ? 0.7486 0.5125 0.6941 -0.0302 0.0126  -0.0421 408 TRP B CD1 
7498  C CD2 . TRP B 408 ? 0.6698 0.4486 0.6274 -0.0238 0.0174  -0.0275 408 TRP B CD2 
7499  N NE1 . TRP B 408 ? 0.6066 0.3870 0.5654 -0.0375 0.0074  -0.0422 408 TRP B NE1 
7500  C CE2 . TRP B 408 ? 0.6573 0.4462 0.6233 -0.0333 0.0106  -0.0341 408 TRP B CE2 
7501  C CE3 . TRP B 408 ? 0.5489 0.3377 0.5108 -0.0182 0.0210  -0.0188 408 TRP B CE3 
7502  C CZ2 . TRP B 408 ? 0.7363 0.5433 0.7153 -0.0362 0.0082  -0.0326 408 TRP B CZ2 
7503  C CZ3 . TRP B 408 ? 0.6199 0.4268 0.5930 -0.0220 0.0183  -0.0186 408 TRP B CZ3 
7504  C CH2 . TRP B 408 ? 0.6863 0.5013 0.6681 -0.0303 0.0123  -0.0256 408 TRP B CH2 
7505  N N   . PHE B 409 ? 0.7777 0.4861 0.6894 -0.0229 0.0245  -0.0596 409 PHE B N   
7506  C CA  . PHE B 409 ? 0.8602 0.5448 0.7682 -0.0333 0.0256  -0.0724 409 PHE B CA  
7507  C C   . PHE B 409 ? 0.8323 0.4981 0.7228 -0.0249 0.0298  -0.0833 409 PHE B C   
7508  O O   . PHE B 409 ? 0.8982 0.5742 0.7792 -0.0265 0.0242  -0.0946 409 PHE B O   
7509  C CB  . PHE B 409 ? 0.9064 0.6075 0.8206 -0.0483 0.0156  -0.0812 409 PHE B CB  
7510  C CG  . PHE B 409 ? 0.9202 0.6034 0.8401 -0.0639 0.0162  -0.0893 409 PHE B CG  
7511  C CD1 . PHE B 409 ? 1.0306 0.6844 0.9399 -0.0678 0.0194  -0.1033 409 PHE B CD1 
7512  C CD2 . PHE B 409 ? 0.8776 0.5736 0.8140 -0.0750 0.0137  -0.0833 409 PHE B CD2 
7513  C CE1 . PHE B 409 ? 0.9670 0.6025 0.8835 -0.0846 0.0196  -0.1109 409 PHE B CE1 
7514  C CE2 . PHE B 409 ? 0.9393 0.6214 0.8831 -0.0912 0.0143  -0.0892 409 PHE B CE2 
7515  C CZ  . PHE B 409 ? 0.9145 0.5653 0.8490 -0.0970 0.0170  -0.1027 409 PHE B CZ  
7516  N N   . ASP B 410 ? 0.8629 0.5029 0.7492 -0.0148 0.0400  -0.0793 410 ASP B N   
7517  C CA  . ASP B 410 ? 0.9004 0.5177 0.7710 -0.0038 0.0465  -0.0897 410 ASP B CA  
7518  C C   . ASP B 410 ? 0.8796 0.5204 0.7397 0.0110  0.0462  -0.0875 410 ASP B C   
7519  O O   . ASP B 410 ? 0.8754 0.5066 0.7206 0.0200  0.0500  -0.0989 410 ASP B O   
7520  C CB  . ASP B 410 ? 0.8073 0.4046 0.6701 -0.0161 0.0434  -0.1120 410 ASP B CB  
7521  C CG  . ASP B 410 ? 0.9515 0.5217 0.8258 -0.0318 0.0449  -0.1140 410 ASP B CG  
7522  O OD1 . ASP B 410 ? 0.9832 0.5602 0.8724 -0.0361 0.0459  -0.0980 410 ASP B OD1 
7523  O OD2 . ASP B 410 ? 1.0557 0.5988 0.9241 -0.0404 0.0453  -0.1321 410 ASP B OD2 
7524  N N   . GLY B 411 ? 0.9344 0.6064 0.8025 0.0136  0.0421  -0.0732 411 GLY B N   
7525  C CA  . GLY B 411 ? 0.7496 0.4463 0.6108 0.0252  0.0415  -0.0684 411 GLY B CA  
7526  C C   . GLY B 411 ? 0.8570 0.5705 0.7082 0.0212  0.0346  -0.0795 411 GLY B C   
7527  O O   . GLY B 411 ? 0.8464 0.5808 0.6907 0.0311  0.0352  -0.0752 411 GLY B O   
7528  N N   . ASN B 412 ? 0.9182 0.6274 0.7691 0.0069  0.0279  -0.0923 412 ASN B N   
7529  C CA  . ASN B 412 ? 0.8942 0.6224 0.7344 0.0030  0.0209  -0.1032 412 ASN B CA  
7530  C C   . ASN B 412 ? 0.8296 0.5769 0.6817 -0.0120 0.0097  -0.1018 412 ASN B C   
7531  O O   . ASN B 412 ? 0.8501 0.5950 0.7182 -0.0192 0.0080  -0.0941 412 ASN B O   
7532  C CB  . ASN B 412 ? 0.8766 0.5817 0.7000 0.0022  0.0239  -0.1256 412 ASN B CB  
7533  C CG  . ASN B 412 ? 0.9415 0.6165 0.7718 -0.0123 0.0236  -0.1362 412 ASN B CG  
7534  O OD1 . ASN B 412 ? 1.0405 0.7262 0.8808 -0.0280 0.0151  -0.1377 412 ASN B OD1 
7535  N ND2 . ASN B 412 ? 0.8993 0.5371 0.7255 -0.0071 0.0331  -0.1425 412 ASN B ND2 
7536  N N   . PHE B 413 ? 0.7811 0.5504 0.6249 -0.0156 0.0023  -0.1090 413 PHE B N   
7537  C CA  . PHE B 413 ? 0.8189 0.6105 0.6730 -0.0277 -0.0086 -0.1074 413 PHE B CA  
7538  C C   . PHE B 413 ? 0.8879 0.6733 0.7370 -0.0416 -0.0136 -0.1268 413 PHE B C   
7539  O O   . PHE B 413 ? 0.9276 0.7380 0.7817 -0.0505 -0.0234 -0.1275 413 PHE B O   
7540  C CB  . PHE B 413 ? 0.7420 0.5689 0.5934 -0.0224 -0.0146 -0.0974 413 PHE B CB  
7541  C CG  . PHE B 413 ? 0.7119 0.5485 0.5738 -0.0133 -0.0124 -0.0772 413 PHE B CG  
7542  C CD1 . PHE B 413 ? 0.7237 0.5666 0.6056 -0.0176 -0.0169 -0.0650 413 PHE B CD1 
7543  C CD2 . PHE B 413 ? 0.7786 0.6198 0.6308 -0.0008 -0.0059 -0.0712 413 PHE B CD2 
7544  C CE1 . PHE B 413 ? 0.7957 0.6462 0.6876 -0.0110 -0.0156 -0.0489 413 PHE B CE1 
7545  C CE2 . PHE B 413 ? 0.7824 0.6343 0.6458 0.0052  -0.0047 -0.0530 413 PHE B CE2 
7546  C CZ  . PHE B 413 ? 0.8289 0.6841 0.7120 -0.0006 -0.0098 -0.0425 413 PHE B CZ  
7547  N N   . LEU B 414 ? 0.8704 0.6234 0.7110 -0.0440 -0.0073 -0.1422 414 LEU B N   
7548  C CA  . LEU B 414 ? 0.8732 0.6188 0.7088 -0.0590 -0.0124 -0.1631 414 LEU B CA  
7549  C C   . LEU B 414 ? 0.8523 0.5998 0.7079 -0.0760 -0.0180 -0.1604 414 LEU B C   
7550  O O   . LEU B 414 ? 0.8251 0.5785 0.6805 -0.0911 -0.0252 -0.1750 414 LEU B O   
7551  C CB  . LEU B 414 ? 0.8992 0.6043 0.7222 -0.0571 -0.0037 -0.1806 414 LEU B CB  
7552  C CG  . LEU B 414 ? 0.8635 0.5652 0.6672 -0.0379 0.0039  -0.1839 414 LEU B CG  
7553  C CD1 . LEU B 414 ? 0.8344 0.4904 0.6288 -0.0349 0.0134  -0.2010 414 LEU B CD1 
7554  C CD2 . LEU B 414 ? 0.9092 0.6464 0.6965 -0.0360 -0.0033 -0.1927 414 LEU B CD2 
7555  N N   . LYS B 415 ? 0.7975 0.5435 0.6703 -0.0740 -0.0151 -0.1426 415 LYS B N   
7556  C CA  . LYS B 415 ? 0.8688 0.6238 0.7610 -0.0882 -0.0200 -0.1386 415 LYS B CA  
7557  C C   . LYS B 415 ? 0.8904 0.6862 0.7892 -0.0921 -0.0316 -0.1350 415 LYS B C   
7558  O O   . LYS B 415 ? 0.8475 0.6566 0.7601 -0.1053 -0.0374 -0.1365 415 LYS B O   
7559  C CB  . LYS B 415 ? 0.8822 0.6290 0.7891 -0.0829 -0.0134 -0.1212 415 LYS B CB  
7560  C CG  . LYS B 415 ? 0.8887 0.6421 0.8153 -0.0965 -0.0157 -0.1171 415 LYS B CG  
7561  C CD  . LYS B 415 ? 1.0040 0.7320 0.9317 -0.1122 -0.0133 -0.1295 415 LYS B CD  
7562  C CE  . LYS B 415 ? 0.9990 0.7475 0.9450 -0.1295 -0.0196 -0.1294 415 LYS B CE  
7563  N NZ  . LYS B 415 ? 1.0484 0.7803 1.0087 -0.1369 -0.0121 -0.1207 415 LYS B NZ  
7564  N N   . TRP B 416 ? 0.8529 0.6705 0.7435 -0.0806 -0.0347 -0.1286 416 TRP B N   
7565  C CA  . TRP B 416 ? 0.7828 0.6386 0.6807 -0.0820 -0.0452 -0.1218 416 TRP B CA  
7566  C C   . TRP B 416 ? 0.7563 0.6345 0.6369 -0.0810 -0.0515 -0.1304 416 TRP B C   
7567  O O   . TRP B 416 ? 0.8152 0.7265 0.7013 -0.0849 -0.0613 -0.1269 416 TRP B O   
7568  C CB  . TRP B 416 ? 0.7215 0.5892 0.6307 -0.0698 -0.0446 -0.1010 416 TRP B CB  
7569  C CG  . TRP B 416 ? 0.7624 0.6134 0.6866 -0.0692 -0.0387 -0.0930 416 TRP B CG  
7570  C CD1 . TRP B 416 ? 0.7635 0.6254 0.7072 -0.0742 -0.0418 -0.0872 416 TRP B CD1 
7571  C CD2 . TRP B 416 ? 0.8062 0.6308 0.7270 -0.0621 -0.0286 -0.0897 416 TRP B CD2 
7572  N NE1 . TRP B 416 ? 0.7787 0.6229 0.7298 -0.0711 -0.0341 -0.0813 416 TRP B NE1 
7573  C CE2 . TRP B 416 ? 0.7937 0.6154 0.7313 -0.0640 -0.0263 -0.0820 416 TRP B CE2 
7574  C CE3 . TRP B 416 ? 0.7581 0.5640 0.6633 -0.0533 -0.0211 -0.0921 416 TRP B CE3 
7575  C CZ2 . TRP B 416 ? 0.6851 0.4873 0.6236 -0.0581 -0.0174 -0.0761 416 TRP B CZ2 
7576  C CZ3 . TRP B 416 ? 0.7341 0.5199 0.6418 -0.0470 -0.0123 -0.0856 416 TRP B CZ3 
7577  C CH2 . TRP B 416 ? 0.7549 0.5395 0.6787 -0.0498 -0.0108 -0.0773 416 TRP B CH2 
7578  N N   . ILE B 417 ? 0.7742 0.6381 0.6339 -0.0749 -0.0461 -0.1410 417 ILE B N   
7579  C CA  . ILE B 417 ? 0.8292 0.7169 0.6695 -0.0726 -0.0512 -0.1505 417 ILE B CA  
7580  C C   . ILE B 417 ? 0.8232 0.6829 0.6433 -0.0739 -0.0452 -0.1741 417 ILE B C   
7581  O O   . ILE B 417 ? 0.7694 0.5911 0.5907 -0.0718 -0.0357 -0.1776 417 ILE B O   
7582  C CB  . ILE B 417 ? 0.8592 0.7696 0.6945 -0.0568 -0.0502 -0.1322 417 ILE B CB  
7583  C CG1 . ILE B 417 ? 0.8498 0.8019 0.6730 -0.0567 -0.0593 -0.1334 417 ILE B CG1 
7584  C CG2 . ILE B 417 ? 0.8680 0.7550 0.6901 -0.0440 -0.0386 -0.1333 417 ILE B CG2 
7585  C CD1 . ILE B 417 ? 0.7518 0.7315 0.5754 -0.0435 -0.0597 -0.1099 417 ILE B CD1 
7586  N N   . GLY B 418 ? 0.8205 0.6999 0.6222 -0.0769 -0.0508 -0.1909 418 GLY B N   
7587  C CA  . GLY B 418 ? 0.8309 0.6869 0.6104 -0.0750 -0.0452 -0.2154 418 GLY B CA  
7588  C C   . GLY B 418 ? 0.8960 0.7432 0.6704 -0.0937 -0.0514 -0.2431 418 GLY B C   
7589  O O   . GLY B 418 ? 1.0266 0.8611 0.7797 -0.0925 -0.0490 -0.2673 418 GLY B O   
7590  N N   . ASN B 419 ? 0.9608 0.8136 0.7545 -0.1111 -0.0589 -0.2416 419 ASN B N   
7591  C CA  . ASN B 419 ? 1.0360 0.8889 0.8270 -0.1316 -0.0669 -0.2670 419 ASN B CA  
7592  C C   . ASN B 419 ? 0.9827 0.8920 0.7762 -0.1392 -0.0813 -0.2636 419 ASN B C   
7593  O O   . ASN B 419 ? 0.9744 0.9156 0.7778 -0.1300 -0.0844 -0.2389 419 ASN B O   
7594  C CB  . ASN B 419 ? 1.0302 0.8456 0.8414 -0.1479 -0.0637 -0.2698 419 ASN B CB  
7595  C CG  . ASN B 419 ? 1.1067 0.9477 0.9451 -0.1583 -0.0704 -0.2510 419 ASN B CG  
7596  O OD1 . ASN B 419 ? 1.0886 0.9761 0.9315 -0.1607 -0.0810 -0.2442 419 ASN B OD1 
7597  N ND2 . ASN B 419 ? 1.1865 0.9973 1.0432 -0.1631 -0.0634 -0.2416 419 ASN B ND2 
7598  N N   . LYS B 420 ? 1.0083 0.9297 0.7931 -0.1560 -0.0903 -0.2891 420 LYS B N   
7599  C CA  . LYS B 420 ? 0.9740 0.9543 0.7582 -0.1621 -0.1046 -0.2874 420 LYS B CA  
7600  C C   . LYS B 420 ? 0.9734 0.9780 0.7871 -0.1673 -0.1103 -0.2629 420 LYS B C   
7601  O O   . LYS B 420 ? 0.8709 0.9201 0.6888 -0.1587 -0.1169 -0.2436 420 LYS B O   
7602  C CB  . LYS B 420 ? 0.9138 0.9021 0.6856 -0.1822 -0.1138 -0.3212 420 LYS B CB  
7603  C CG  . LYS B 420 ? 1.0009 0.9636 0.7929 -0.2066 -0.1160 -0.3331 420 LYS B CG  
7604  C CD  . LYS B 420 ? 1.0376 1.0181 0.8194 -0.2285 -0.1278 -0.3655 420 LYS B CD  
7605  C CE  . LYS B 420 ? 1.0384 1.0910 0.8239 -0.2332 -0.1433 -0.3574 420 LYS B CE  
7606  N NZ  . LYS B 420 ? 0.9974 1.0763 0.7651 -0.2505 -0.1555 -0.3908 420 LYS B NZ  
7607  N N   . GLU B 421 ? 0.9595 0.9351 0.7945 -0.1798 -0.1069 -0.2619 421 GLU B N   
7608  C CA  . GLU B 421 ? 0.9054 0.9062 0.7685 -0.1849 -0.1119 -0.2416 421 GLU B CA  
7609  C C   . GLU B 421 ? 0.8669 0.8708 0.7397 -0.1640 -0.1061 -0.2117 421 GLU B C   
7610  O O   . GLU B 421 ? 0.8416 0.8844 0.7276 -0.1589 -0.1130 -0.1935 421 GLU B O   
7611  C CB  . GLU B 421 ? 1.0189 0.9893 0.9012 -0.2035 -0.1086 -0.2480 421 GLU B CB  
7612  C CG  . GLU B 421 ? 1.1459 1.1134 1.0226 -0.2276 -0.1156 -0.2775 421 GLU B CG  
7613  C CD  . GLU B 421 ? 1.3515 1.2584 1.2287 -0.2380 -0.1056 -0.2921 421 GLU B CD  
7614  O OE1 . GLU B 421 ? 1.4080 1.2838 1.2627 -0.2341 -0.1009 -0.3119 421 GLU B OE1 
7615  O OE2 . GLU B 421 ? 1.2919 1.1833 1.1922 -0.2496 -0.1020 -0.2834 421 GLU B OE2 
7616  N N   . LYS B 422 ? 0.8724 0.8358 0.7397 -0.1517 -0.0937 -0.2065 422 LYS B N   
7617  C CA  . LYS B 422 ? 0.9365 0.9028 0.8111 -0.1327 -0.0887 -0.1807 422 LYS B CA  
7618  C C   . LYS B 422 ? 0.8552 0.8568 0.7165 -0.1191 -0.0936 -0.1712 422 LYS B C   
7619  O O   . LYS B 422 ? 0.8577 0.8787 0.7313 -0.1083 -0.0952 -0.1482 422 LYS B O   
7620  C CB  . LYS B 422 ? 0.9495 0.8690 0.8198 -0.1232 -0.0750 -0.1784 422 LYS B CB  
7621  C CG  . LYS B 422 ? 0.8844 0.7780 0.7754 -0.1294 -0.0690 -0.1716 422 LYS B CG  
7622  C CD  . LYS B 422 ? 0.8492 0.6954 0.7326 -0.1241 -0.0563 -0.1755 422 LYS B CD  
7623  C CE  . LYS B 422 ? 0.9568 0.7750 0.8524 -0.1402 -0.0527 -0.1832 422 LYS B CE  
7624  N NZ  . LYS B 422 ? 0.9407 0.7676 0.8606 -0.1433 -0.0519 -0.1659 422 LYS B NZ  
7625  N N   . ASN B 423 ? 0.8512 0.8618 0.6879 -0.1194 -0.0958 -0.1884 423 ASN B N   
7626  C CA  . ASN B 423 ? 0.8609 0.9082 0.6840 -0.1061 -0.0996 -0.1774 423 ASN B CA  
7627  C C   . ASN B 423 ? 0.8077 0.9074 0.6403 -0.1103 -0.1130 -0.1674 423 ASN B C   
7628  O O   . ASN B 423 ? 0.7464 0.8773 0.5782 -0.0977 -0.1159 -0.1470 423 ASN B O   
7629  C CB  . ASN B 423 ? 0.8705 0.9156 0.6628 -0.1035 -0.0972 -0.1995 423 ASN B CB  
7630  C CG  . ASN B 423 ? 0.8589 0.8609 0.6410 -0.0916 -0.0830 -0.2019 423 ASN B CG  
7631  O OD1 . ASN B 423 ? 0.9219 0.9021 0.7186 -0.0837 -0.0756 -0.1836 423 ASN B OD1 
7632  N ND2 . ASN B 423 ? 0.8817 0.8723 0.6388 -0.0900 -0.0793 -0.2259 423 ASN B ND2 
7633  N N   . GLU B 424 ? 0.8412 0.9526 0.6843 -0.1276 -0.1211 -0.1796 424 GLU B N   
7634  C CA  . GLU B 424 ? 0.8300 0.9940 0.6855 -0.1305 -0.1338 -0.1681 424 GLU B CA  
7635  C C   . GLU B 424 ? 0.7668 0.9372 0.6477 -0.1184 -0.1326 -0.1375 424 GLU B C   
7636  O O   . GLU B 424 ? 0.6778 0.8876 0.5637 -0.1088 -0.1394 -0.1180 424 GLU B O   
7637  C CB  . GLU B 424 ? 0.9151 1.0907 0.7799 -0.1527 -0.1422 -0.1871 424 GLU B CB  
7638  C CG  . GLU B 424 ? 1.1143 1.2819 0.9563 -0.1680 -0.1448 -0.2211 424 GLU B CG  
7639  C CD  . GLU B 424 ? 1.1560 1.3254 1.0118 -0.1931 -0.1516 -0.2395 424 GLU B CD  
7640  O OE1 . GLU B 424 ? 1.1175 1.2413 0.9834 -0.2025 -0.1437 -0.2470 424 GLU B OE1 
7641  O OE2 . GLU B 424 ? 1.1064 1.3245 0.9635 -0.2041 -0.1648 -0.2458 424 GLU B OE2 
7642  N N   . TYR B 425 ? 0.7973 0.9294 0.6945 -0.1181 -0.1240 -0.1329 425 TYR B N   
7643  C CA  . TYR B 425 ? 0.7781 0.9120 0.6983 -0.1062 -0.1221 -0.1073 425 TYR B CA  
7644  C C   . TYR B 425 ? 0.7139 0.8496 0.6274 -0.0880 -0.1188 -0.0878 425 TYR B C   
7645  O O   . TYR B 425 ? 0.7183 0.8735 0.6476 -0.0776 -0.1222 -0.0655 425 TYR B O   
7646  C CB  . TYR B 425 ? 0.7901 0.8830 0.7246 -0.1091 -0.1126 -0.1087 425 TYR B CB  
7647  C CG  . TYR B 425 ? 0.7597 0.8645 0.7170 -0.1205 -0.1164 -0.1103 425 TYR B CG  
7648  C CD1 . TYR B 425 ? 0.7216 0.8641 0.6820 -0.1332 -0.1273 -0.1188 425 TYR B CD1 
7649  C CD2 . TYR B 425 ? 0.7925 0.8738 0.7675 -0.1191 -0.1090 -0.1038 425 TYR B CD2 
7650  C CE1 . TYR B 425 ? 0.7288 0.8859 0.7115 -0.1441 -0.1304 -0.1193 425 TYR B CE1 
7651  C CE2 . TYR B 425 ? 0.7431 0.8388 0.7390 -0.1290 -0.1115 -0.1045 425 TYR B CE2 
7652  C CZ  . TYR B 425 ? 0.8403 0.9739 0.8407 -0.1415 -0.1220 -0.1117 425 TYR B CZ  
7653  O OH  . TYR B 425 ? 0.9179 1.0700 0.9405 -0.1518 -0.1243 -0.1115 425 TYR B OH  
7654  N N   . TRP B 426 ? 0.8113 0.9261 0.7030 -0.0838 -0.1118 -0.0954 426 TRP B N   
7655  C CA  . TRP B 426 ? 0.8714 0.9911 0.7568 -0.0682 -0.1084 -0.0764 426 TRP B CA  
7656  C C   . TRP B 426 ? 0.7692 0.9381 0.6463 -0.0638 -0.1177 -0.0662 426 TRP B C   
7657  O O   . TRP B 426 ? 0.7519 0.9374 0.6387 -0.0523 -0.1192 -0.0407 426 TRP B O   
7658  C CB  . TRP B 426 ? 0.8106 0.9001 0.6751 -0.0643 -0.0980 -0.0873 426 TRP B CB  
7659  C CG  . TRP B 426 ? 0.8094 0.8543 0.6841 -0.0632 -0.0879 -0.0875 426 TRP B CG  
7660  C CD1 . TRP B 426 ? 0.8113 0.8225 0.6827 -0.0717 -0.0822 -0.1065 426 TRP B CD1 
7661  C CD2 . TRP B 426 ? 0.7663 0.7970 0.6566 -0.0533 -0.0828 -0.0673 426 TRP B CD2 
7662  N NE1 . TRP B 426 ? 0.7784 0.7587 0.6614 -0.0667 -0.0736 -0.0981 426 TRP B NE1 
7663  C CE2 . TRP B 426 ? 0.7342 0.7265 0.6284 -0.0559 -0.0742 -0.0756 426 TRP B CE2 
7664  C CE3 . TRP B 426 ? 0.7436 0.7899 0.6455 -0.0432 -0.0847 -0.0431 426 TRP B CE3 
7665  C CZ2 . TRP B 426 ? 0.7067 0.6798 0.6144 -0.0488 -0.0682 -0.0621 426 TRP B CZ2 
7666  C CZ3 . TRP B 426 ? 0.6592 0.6821 0.5757 -0.0372 -0.0788 -0.0310 426 TRP B CZ3 
7667  C CH2 . TRP B 426 ? 0.7133 0.7018 0.6317 -0.0401 -0.0709 -0.0414 426 TRP B CH2 
7668  N N   . LYS B 427 ? 0.7476 0.9409 0.6074 -0.0732 -0.1244 -0.0855 427 LYS B N   
7669  C CA  . LYS B 427 ? 0.6790 0.9258 0.5302 -0.0693 -0.1342 -0.0756 427 LYS B CA  
7670  C C   . LYS B 427 ? 0.7392 1.0151 0.6168 -0.0660 -0.1426 -0.0527 427 LYS B C   
7671  O O   . LYS B 427 ? 0.8193 1.1265 0.6998 -0.0546 -0.1464 -0.0281 427 LYS B O   
7672  C CB  . LYS B 427 ? 0.7095 0.9785 0.5385 -0.0821 -0.1410 -0.1042 427 LYS B CB  
7673  C CG  . LYS B 427 ? 0.7341 0.9700 0.5378 -0.0849 -0.1324 -0.1306 427 LYS B CG  
7674  C CD  . LYS B 427 ? 0.7680 1.0249 0.5499 -0.0983 -0.1399 -0.1617 427 LYS B CD  
7675  C CE  . LYS B 427 ? 0.8671 1.0735 0.6430 -0.1109 -0.1335 -0.1930 427 LYS B CE  
7676  N NZ  . LYS B 427 ? 0.9131 1.1348 0.6822 -0.1309 -0.1435 -0.2223 427 LYS B NZ  
7677  N N   . ILE B 428 ? 0.6501 0.9158 0.5483 -0.0749 -0.1447 -0.0587 428 ILE B N   
7678  C CA  . ILE B 428 ? 0.6340 0.9263 0.5592 -0.0697 -0.1516 -0.0377 428 ILE B CA  
7679  C C   . ILE B 428 ? 0.6416 0.9162 0.5828 -0.0531 -0.1458 -0.0102 428 ILE B C   
7680  O O   . ILE B 428 ? 0.6424 0.9459 0.5958 -0.0421 -0.1513 0.0144  428 ILE B O   
7681  C CB  . ILE B 428 ? 0.6390 0.9229 0.5833 -0.0821 -0.1531 -0.0504 428 ILE B CB  
7682  C CG1 . ILE B 428 ? 0.6489 0.9608 0.5822 -0.0999 -0.1619 -0.0740 428 ILE B CG1 
7683  C CG2 . ILE B 428 ? 0.6080 0.9114 0.5824 -0.0728 -0.1571 -0.0281 428 ILE B CG2 
7684  C CD1 . ILE B 428 ? 0.6501 0.9344 0.5917 -0.1168 -0.1586 -0.0948 428 ILE B CD1 
7685  N N   . LEU B 429 ? 0.6875 0.9147 0.6299 -0.0515 -0.1350 -0.0136 429 LEU B N   
7686  C CA  . LEU B 429 ? 0.7423 0.9501 0.7004 -0.0381 -0.1298 0.0094  429 LEU B CA  
7687  C C   . LEU B 429 ? 0.7781 1.0034 0.7250 -0.0279 -0.1301 0.0288  429 LEU B C   
7688  O O   . LEU B 429 ? 0.8949 1.1260 0.8587 -0.0170 -0.1313 0.0546  429 LEU B O   
7689  C CB  . LEU B 429 ? 0.6633 0.8213 0.6228 -0.0399 -0.1188 -0.0003 429 LEU B CB  
7690  C CG  . LEU B 429 ? 0.7127 0.8471 0.6900 -0.0288 -0.1136 0.0188  429 LEU B CG  
7691  C CD1 . LEU B 429 ? 0.7679 0.8989 0.7725 -0.0264 -0.1156 0.0234  429 LEU B CD1 
7692  C CD2 . LEU B 429 ? 0.8064 0.9017 0.7744 -0.0299 -0.1031 0.0101  429 LEU B CD2 
7693  N N   . ILE B 430 ? 0.6963 0.9308 0.6155 -0.0311 -0.1286 0.0172  430 ILE B N   
7694  C CA  . ILE B 430 ? 0.6978 0.9554 0.6050 -0.0216 -0.1283 0.0363  430 ILE B CA  
7695  C C   . ILE B 430 ? 0.7871 1.0937 0.7026 -0.0159 -0.1389 0.0579  430 ILE B C   
7696  O O   . ILE B 430 ? 0.8208 1.1375 0.7475 -0.0051 -0.1391 0.0874  430 ILE B O   
7697  C CB  . ILE B 430 ? 0.8535 1.1163 0.7278 -0.0253 -0.1246 0.0163  430 ILE B CB  
7698  C CG1 . ILE B 430 ? 0.8155 1.0294 0.6845 -0.0264 -0.1127 0.0027  430 ILE B CG1 
7699  C CG2 . ILE B 430 ? 0.8813 1.1819 0.7415 -0.0158 -0.1256 0.0363  430 ILE B CG2 
7700  C CD1 . ILE B 430 ? 0.8279 1.0365 0.6678 -0.0314 -0.1086 -0.0253 430 ILE B CD1 
7701  N N   . GLU B 431 ? 0.7684 1.1065 0.6804 -0.0235 -0.1481 0.0447  431 GLU B N   
7702  C CA  . GLU B 431 ? 0.8097 1.1990 0.7307 -0.0174 -0.1589 0.0658  431 GLU B CA  
7703  C C   . GLU B 431 ? 0.8491 1.2288 0.8047 -0.0080 -0.1602 0.0896  431 GLU B C   
7704  O O   . GLU B 431 ? 0.8853 1.2922 0.8527 0.0038  -0.1647 0.1192  431 GLU B O   
7705  C CB  . GLU B 431 ? 0.8060 1.2323 0.7177 -0.0292 -0.1691 0.0444  431 GLU B CB  
7706  C CG  . GLU B 431 ? 0.8982 1.3203 0.7790 -0.0421 -0.1675 0.0103  431 GLU B CG  
7707  C CD  . GLU B 431 ? 1.1326 1.5922 0.9846 -0.0375 -0.1694 0.0129  431 GLU B CD  
7708  O OE1 . GLU B 431 ? 1.1080 1.5906 0.9637 -0.0241 -0.1697 0.0442  431 GLU B OE1 
7709  O OE2 . GLU B 431 ? 1.2793 1.7455 1.1050 -0.0474 -0.1704 -0.0167 431 GLU B OE2 
7710  N N   . ALA B 432 ? 0.7681 1.1101 0.7406 -0.0123 -0.1560 0.0772  432 ALA B N   
7711  C CA  . ALA B 432 ? 0.6967 1.0281 0.7014 -0.0024 -0.1564 0.0958  432 ALA B CA  
7712  C C   . ALA B 432 ? 0.7242 1.0292 0.7393 0.0095  -0.1503 0.1201  432 ALA B C   
7713  O O   . ALA B 432 ? 0.7473 1.0616 0.7841 0.0216  -0.1535 0.1462  432 ALA B O   
7714  C CB  . ALA B 432 ? 0.6645 0.9643 0.6821 -0.0098 -0.1524 0.0753  432 ALA B CB  
7715  N N   . LYS B 433 ? 0.7877 1.0596 0.7888 0.0060  -0.1414 0.1123  433 LYS B N   
7716  C CA  . LYS B 433 ? 0.6770 0.9264 0.6871 0.0144  -0.1358 0.1345  433 LYS B CA  
7717  C C   . LYS B 433 ? 0.7339 1.0204 0.7443 0.0235  -0.1408 0.1652  433 LYS B C   
7718  O O   . LYS B 433 ? 0.6767 0.9515 0.7074 0.0325  -0.1397 0.1915  433 LYS B O   
7719  C CB  . LYS B 433 ? 0.6789 0.9000 0.6697 0.0085  -0.1264 0.1211  433 LYS B CB  
7720  C CG  . LYS B 433 ? 0.7808 0.9734 0.7839 0.0141  -0.1200 0.1401  433 LYS B CG  
7721  C CD  . LYS B 433 ? 0.7753 0.9283 0.8038 0.0154  -0.1172 0.1372  433 LYS B CD  
7722  C CE  . LYS B 433 ? 0.7373 0.8715 0.7858 0.0220  -0.1150 0.1623  433 LYS B CE  
7723  N NZ  . LYS B 433 ? 0.6566 0.7743 0.7352 0.0289  -0.1179 0.1698  433 LYS B NZ  
7724  N N   . LYS B 434 ? 0.7409 1.0724 0.7291 0.0210  -0.1463 0.1623  434 LYS B N   
7725  C CA  . LYS B 434 ? 0.6705 1.0446 0.6563 0.0299  -0.1512 0.1926  434 LYS B CA  
7726  C C   . LYS B 434 ? 0.7344 1.1225 0.7501 0.0411  -0.1580 0.2194  434 LYS B C   
7727  O O   . LYS B 434 ? 0.7856 1.1786 0.8148 0.0512  -0.1578 0.2527  434 LYS B O   
7728  C CB  . LYS B 434 ? 0.6791 1.1032 0.6347 0.0247  -0.1570 0.1797  434 LYS B CB  
7729  C CG  . LYS B 434 ? 0.7672 1.1900 0.6925 0.0205  -0.1499 0.1682  434 LYS B CG  
7730  C CD  . LYS B 434 ? 0.8404 1.2741 0.7378 0.0091  -0.1517 0.1302  434 LYS B CD  
7731  C CE  . LYS B 434 ? 0.7109 1.1544 0.5762 0.0085  -0.1456 0.1205  434 LYS B CE  
7732  N NZ  . LYS B 434 ? 0.7728 1.2030 0.6148 -0.0029 -0.1440 0.0788  434 LYS B NZ  
7733  N N   . LYS B 435 ? 0.9343 1.0461 0.6320 -0.1061 -0.0549 0.1735  435 LYS B N   
7734  C CA  . LYS B 435 ? 1.0333 1.1076 0.7268 -0.0879 -0.0696 0.1993  435 LYS B CA  
7735  C C   . LYS B 435 ? 0.9311 0.9535 0.6560 -0.0777 -0.0767 0.1834  435 LYS B C   
7736  O O   . LYS B 435 ? 1.0303 1.0319 0.7575 -0.0534 -0.0901 0.1915  435 LYS B O   
7737  C CB  . LYS B 435 ? 0.9893 1.1073 0.6628 -0.0661 -0.0843 0.1986  435 LYS B CB  
7738  C CG  . LYS B 435 ? 0.9875 1.1594 0.6214 -0.0720 -0.0799 0.2110  435 LYS B CG  
7739  C CD  . LYS B 435 ? 0.9557 1.1793 0.5886 -0.0765 -0.0773 0.1676  435 LYS B CD  
7740  C CE  . LYS B 435 ? 1.0036 1.2548 0.6430 -0.0597 -0.0976 0.1450  435 LYS B CE  
7741  N NZ  . LYS B 435 ? 1.0255 1.3121 0.6673 -0.0677 -0.0955 0.1010  435 LYS B NZ  
7742  N N   . ALA B 436 ? 0.9099 0.9163 0.6577 -0.0924 -0.0685 0.1599  436 ALA B N   
7743  C CA  . ALA B 436 ? 0.8635 0.8270 0.6346 -0.0810 -0.0749 0.1402  436 ALA B CA  
7744  C C   . ALA B 436 ? 0.9373 0.8313 0.7114 -0.0835 -0.0794 0.1625  436 ALA B C   
7745  O O   . ALA B 436 ? 0.9794 0.8551 0.7539 -0.1102 -0.0719 0.1806  436 ALA B O   
7746  C CB  . ALA B 436 ? 0.7797 0.7549 0.5692 -0.0932 -0.0671 0.1069  436 ALA B CB  
7747  N N   . LYS B 437 ? 0.9940 0.8492 0.7726 -0.0558 -0.0910 0.1609  437 LYS B N   
7748  C CA  . LYS B 437 ? 1.0241 0.8004 0.8042 -0.0523 -0.0976 0.1786  437 LYS B CA  
7749  C C   . LYS B 437 ? 1.0098 0.7408 0.8076 -0.0402 -0.1031 0.1446  437 LYS B C   
7750  O O   . LYS B 437 ? 1.0695 0.7261 0.8691 -0.0345 -0.1106 0.1513  437 LYS B O   
7751  C CB  . LYS B 437 ? 1.0010 0.7600 0.7646 -0.0225 -0.1083 0.2120  437 LYS B CB  
7752  C CG  . LYS B 437 ? 1.0320 0.8540 0.7721 -0.0232 -0.1070 0.2380  437 LYS B CG  
7753  C CD  . LYS B 437 ? 1.1116 0.8961 0.8271 -0.0158 -0.1123 0.2899  437 LYS B CD  
7754  C CE  . LYS B 437 ? 1.2221 0.9797 0.9286 -0.0557 -0.0982 0.3189  437 LYS B CE  
7755  N NZ  . LYS B 437 ? 1.1874 1.0237 0.8821 -0.0810 -0.0839 0.3152  437 LYS B NZ  
7756  N N   . ASN B 438 ? 0.9355 0.7057 0.7435 -0.0349 -0.0997 0.1087  438 ASN B N   
7757  C CA  . ASN B 438 ? 1.0148 0.7509 0.8329 -0.0237 -0.1037 0.0751  438 ASN B CA  
7758  C C   . ASN B 438 ? 0.9760 0.7513 0.8020 -0.0432 -0.0965 0.0473  438 ASN B C   
7759  O O   . ASN B 438 ? 0.9433 0.7669 0.7694 -0.0632 -0.0882 0.0535  438 ASN B O   
7760  C CB  . ASN B 438 ? 0.9334 0.6764 0.7523 0.0190  -0.1078 0.0628  438 ASN B CB  
7761  C CG  . ASN B 438 ? 0.9651 0.7861 0.7888 0.0259  -0.1003 0.0531  438 ASN B CG  
7762  O OD1 . ASN B 438 ? 1.0174 0.8685 0.8445 0.0117  -0.0926 0.0332  438 ASN B OD1 
7763  N ND2 . ASN B 438 ? 1.0280 0.8813 0.8537 0.0477  -0.1036 0.0677  438 ASN B ND2 
7764  N N   . ASP B 439 ? 0.8860 0.6418 0.7156 -0.0329 -0.1003 0.0155  439 ASP B N   
7765  C CA  . ASP B 439 ? 0.8928 0.6794 0.7274 -0.0474 -0.0968 -0.0098 439 ASP B CA  
7766  C C   . ASP B 439 ? 0.9213 0.7620 0.7522 -0.0286 -0.0885 -0.0230 439 ASP B C   
7767  O O   . ASP B 439 ? 0.9783 0.8430 0.8095 -0.0340 -0.0858 -0.0416 439 ASP B O   
7768  C CB  . ASP B 439 ? 0.9186 0.6579 0.7549 -0.0485 -0.1076 -0.0384 439 ASP B CB  
7769  C CG  . ASP B 439 ? 1.1120 0.8305 0.9633 -0.0886 -0.1128 -0.0352 439 ASP B CG  
7770  O OD1 . ASP B 439 ? 1.1037 0.8592 0.9638 -0.1138 -0.1042 -0.0134 439 ASP B OD1 
7771  O OD2 . ASP B 439 ? 1.1347 0.8024 0.9904 -0.0954 -0.1254 -0.0563 439 ASP B OD2 
7772  N N   . TYR B 440 ? 0.8406 0.7023 0.6699 -0.0075 -0.0850 -0.0121 440 TYR B N   
7773  C CA  . TYR B 440 ? 0.7425 0.6571 0.5738 0.0003  -0.0754 -0.0190 440 TYR B CA  
7774  C C   . TYR B 440 ? 0.7479 0.6982 0.5806 -0.0236 -0.0692 -0.0124 440 TYR B C   
7775  O O   . TYR B 440 ? 0.7151 0.6989 0.5495 -0.0220 -0.0615 -0.0197 440 TYR B O   
7776  C CB  . TYR B 440 ? 0.8597 0.7970 0.6970 0.0229  -0.0744 -0.0089 440 TYR B CB  
7777  C CG  . TYR B 440 ? 0.8344 0.7677 0.6735 0.0546  -0.0725 -0.0234 440 TYR B CG  
7778  C CD1 . TYR B 440 ? 0.8269 0.7973 0.6683 0.0630  -0.0610 -0.0360 440 TYR B CD1 
7779  C CD2 . TYR B 440 ? 0.8783 0.7712 0.7159 0.0785  -0.0807 -0.0228 440 TYR B CD2 
7780  C CE1 . TYR B 440 ? 0.8448 0.8215 0.6860 0.0938  -0.0557 -0.0482 440 TYR B CE1 
7781  C CE2 . TYR B 440 ? 0.8978 0.7922 0.7358 0.1126  -0.0773 -0.0392 440 TYR B CE2 
7782  C CZ  . TYR B 440 ? 0.8869 0.8286 0.7266 0.1199  -0.0638 -0.0520 440 TYR B CZ  
7783  O OH  . TYR B 440 ? 0.8725 0.8255 0.7108 0.1552  -0.0568 -0.0674 440 TYR B OH  
7784  N N   . ILE B 441 ? 0.8009 0.7436 0.6324 -0.0447 -0.0712 0.0022  441 ILE B N   
7785  C CA  . ILE B 441 ? 0.8407 0.8186 0.6721 -0.0641 -0.0639 0.0035  441 ILE B CA  
7786  C C   . ILE B 441 ? 0.7162 0.7028 0.5526 -0.0680 -0.0612 -0.0172 441 ILE B C   
7787  O O   . ILE B 441 ? 0.6732 0.6910 0.5097 -0.0698 -0.0542 -0.0235 441 ILE B O   
7788  C CB  . ILE B 441 ? 0.7515 0.7247 0.5799 -0.0849 -0.0637 0.0256  441 ILE B CB  
7789  C CG1 . ILE B 441 ? 0.7451 0.7636 0.5711 -0.0996 -0.0539 0.0257  441 ILE B CG1 
7790  C CG2 . ILE B 441 ? 0.7580 0.6927 0.5955 -0.0997 -0.0684 0.0257  441 ILE B CG2 
7791  C CD1 . ILE B 441 ? 0.6000 0.6502 0.4158 -0.0901 -0.0517 0.0241  441 ILE B CD1 
7792  N N   . LEU B 442 ? 0.6944 0.6525 0.5336 -0.0665 -0.0683 -0.0299 442 LEU B N   
7793  C CA  . LEU B 442 ? 0.7688 0.7408 0.6102 -0.0667 -0.0695 -0.0501 442 LEU B CA  
7794  C C   . LEU B 442 ? 0.7589 0.7461 0.5902 -0.0437 -0.0640 -0.0599 442 LEU B C   
7795  O O   . LEU B 442 ? 0.7741 0.7842 0.6036 -0.0412 -0.0609 -0.0679 442 LEU B O   
7796  C CB  . LEU B 442 ? 0.7748 0.7135 0.6200 -0.0721 -0.0821 -0.0651 442 LEU B CB  
7797  C CG  . LEU B 442 ? 0.8191 0.7251 0.6762 -0.0966 -0.0879 -0.0523 442 LEU B CG  
7798  C CD1 . LEU B 442 ? 0.8424 0.7155 0.7072 -0.1067 -0.1026 -0.0745 442 LEU B CD1 
7799  C CD2 . LEU B 442 ? 0.8101 0.7525 0.6800 -0.1223 -0.0792 -0.0342 442 LEU B CD2 
7800  N N   . VAL B 443 ? 0.7451 0.7224 0.5711 -0.0260 -0.0619 -0.0571 443 VAL B N   
7801  C CA  . VAL B 443 ? 0.6510 0.6482 0.4707 -0.0083 -0.0528 -0.0606 443 VAL B CA  
7802  C C   . VAL B 443 ? 0.6475 0.6714 0.4729 -0.0173 -0.0436 -0.0508 443 VAL B C   
7803  O O   . VAL B 443 ? 0.7123 0.7487 0.5334 -0.0116 -0.0360 -0.0528 443 VAL B O   
7804  C CB  . VAL B 443 ? 0.6554 0.6463 0.4748 0.0121  -0.0509 -0.0592 443 VAL B CB  
7805  C CG1 . VAL B 443 ? 0.7192 0.7304 0.5300 0.0305  -0.0402 -0.0650 443 VAL B CG1 
7806  C CG2 . VAL B 443 ? 0.6406 0.5911 0.4556 0.0194  -0.0625 -0.0686 443 VAL B CG2 
7807  N N   . ALA B 444 ? 0.7577 0.7874 0.5898 -0.0304 -0.0448 -0.0401 444 ALA B N   
7808  C CA  . ALA B 444 ? 0.7841 0.8353 0.6190 -0.0392 -0.0385 -0.0372 444 ALA B CA  
7809  C C   . ALA B 444 ? 0.7663 0.8245 0.5988 -0.0467 -0.0360 -0.0439 444 ALA B C   
7810  O O   . ALA B 444 ? 0.8694 0.9380 0.7018 -0.0495 -0.0304 -0.0464 444 ALA B O   
7811  C CB  . ALA B 444 ? 0.5994 0.6609 0.4365 -0.0479 -0.0425 -0.0268 444 ALA B CB  
7812  N N   . GLU B 445 ? 0.6659 0.7197 0.4989 -0.0496 -0.0409 -0.0487 445 GLU B N   
7813  C CA  . GLU B 445 ? 0.7281 0.7995 0.5643 -0.0526 -0.0392 -0.0558 445 GLU B CA  
7814  C C   . GLU B 445 ? 0.7323 0.8043 0.5622 -0.0355 -0.0379 -0.0634 445 GLU B C   
7815  O O   . GLU B 445 ? 0.6955 0.7841 0.5287 -0.0317 -0.0395 -0.0698 445 GLU B O   
7816  C CB  . GLU B 445 ? 0.7680 0.8449 0.6147 -0.0682 -0.0457 -0.0561 445 GLU B CB  
7817  C CG  . GLU B 445 ? 0.8309 0.9169 0.6801 -0.0851 -0.0416 -0.0425 445 GLU B CG  
7818  C CD  . GLU B 445 ? 0.8058 0.8784 0.6647 -0.1038 -0.0476 -0.0337 445 GLU B CD  
7819  O OE1 . GLU B 445 ? 0.7496 0.8012 0.6146 -0.1043 -0.0572 -0.0432 445 GLU B OE1 
7820  O OE2 . GLU B 445 ? 0.8492 0.9306 0.7082 -0.1189 -0.0427 -0.0172 445 GLU B OE2 
7821  N N   . GLY B 446 ? 0.7949 0.8545 0.6162 -0.0235 -0.0339 -0.0603 446 GLY B N   
7822  C CA  . GLY B 446 ? 0.7487 0.8086 0.5581 -0.0062 -0.0318 -0.0622 446 GLY B CA  
7823  C C   . GLY B 446 ? 0.7566 0.8184 0.5655 -0.0016 -0.0246 -0.0584 446 GLY B C   
7824  O O   . GLY B 446 ? 0.8024 0.8587 0.6178 -0.0105 -0.0183 -0.0555 446 GLY B O   
7825  N N   . SER B 447 ? 0.6282 0.6952 0.4272 0.0151  -0.0265 -0.0593 447 SER B N   
7826  C CA  . SER B 447 ? 0.6946 0.7543 0.4913 0.0254  -0.0200 -0.0540 447 SER B CA  
7827  C C   . SER B 447 ? 0.6898 0.7232 0.4791 0.0271  -0.0076 -0.0394 447 SER B C   
7828  O O   . SER B 447 ? 0.7753 0.7887 0.5673 0.0274  -0.0010 -0.0359 447 SER B O   
7829  C CB  . SER B 447 ? 0.7393 0.8152 0.5273 0.0472  -0.0275 -0.0558 447 SER B CB  
7830  O OG  . SER B 447 ? 0.7359 0.8056 0.5006 0.0643  -0.0267 -0.0458 447 SER B OG  
7831  N N   . ASP B 448 ? 0.5945 0.6281 0.3768 0.0273  -0.0035 -0.0320 448 ASP B N   
7832  C CA  . ASP B 448 ? 0.7360 0.7535 0.5152 0.0271  0.0110  -0.0142 448 ASP B CA  
7833  C C   . ASP B 448 ? 0.7019 0.7101 0.5034 0.0041  0.0162  -0.0146 448 ASP B C   
7834  O O   . ASP B 448 ? 0.6956 0.6828 0.5022 -0.0025 0.0264  -0.0030 448 ASP B O   
7835  C CB  . ASP B 448 ? 0.6834 0.7155 0.4492 0.0369  0.0162  -0.0071 448 ASP B CB  
7836  C CG  . ASP B 448 ? 0.7593 0.8032 0.4980 0.0602  0.0076  -0.0119 448 ASP B CG  
7837  O OD1 . ASP B 448 ? 0.7813 0.8191 0.5009 0.0765  0.0116  0.0022  448 ASP B OD1 
7838  O OD2 . ASP B 448 ? 0.6766 0.7342 0.4125 0.0625  -0.0045 -0.0297 448 ASP B OD2 
7839  N N   . TRP B 449 ? 0.7091 0.7314 0.5236 -0.0090 0.0080  -0.0272 449 TRP B N   
7840  C CA  . TRP B 449 ? 0.7215 0.7433 0.5542 -0.0292 0.0091  -0.0299 449 TRP B CA  
7841  C C   . TRP B 449 ? 0.7470 0.7460 0.5806 -0.0345 0.0095  -0.0381 449 TRP B C   
7842  O O   . TRP B 449 ? 0.8566 0.8407 0.7021 -0.0494 0.0135  -0.0383 449 TRP B O   
7843  C CB  . TRP B 449 ? 0.7182 0.7612 0.5576 -0.0371 -0.0012 -0.0383 449 TRP B CB  
7844  C CG  . TRP B 449 ? 0.6817 0.7361 0.5173 -0.0266 -0.0041 -0.0350 449 TRP B CG  
7845  C CD1 . TRP B 449 ? 0.6432 0.6995 0.4733 -0.0236 -0.0138 -0.0412 449 TRP B CD1 
7846  C CD2 . TRP B 449 ? 0.6600 0.7234 0.4973 -0.0175 0.0034  -0.0264 449 TRP B CD2 
7847  N NE1 . TRP B 449 ? 0.6273 0.6846 0.4537 -0.0119 -0.0150 -0.0404 449 TRP B NE1 
7848  C CE2 . TRP B 449 ? 0.6623 0.7281 0.4915 -0.0054 -0.0038 -0.0323 449 TRP B CE2 
7849  C CE3 . TRP B 449 ? 0.6596 0.7305 0.5056 -0.0192 0.0170  -0.0141 449 TRP B CE3 
7850  C CZ2 . TRP B 449 ? 0.6557 0.7318 0.4815 0.0105  0.0018  -0.0302 449 TRP B CZ2 
7851  C CZ3 . TRP B 449 ? 0.6581 0.7484 0.5031 -0.0054 0.0250  -0.0078 449 TRP B CZ3 
7852  C CH2 . TRP B 449 ? 0.6889 0.7821 0.5219 0.0119  0.0172  -0.0179 449 TRP B CH2 
7853  N N   . PHE B 450 ? 0.6857 0.6828 0.5092 -0.0221 0.0053  -0.0469 450 PHE B N   
7854  C CA  . PHE B 450 ? 0.7376 0.7147 0.5602 -0.0207 0.0060  -0.0590 450 PHE B CA  
7855  C C   . PHE B 450 ? 0.8189 0.7563 0.6355 -0.0081 0.0138  -0.0484 450 PHE B C   
7856  O O   . PHE B 450 ? 0.8286 0.7323 0.6474 -0.0109 0.0161  -0.0571 450 PHE B O   
7857  C CB  . PHE B 450 ? 0.7097 0.7109 0.5281 -0.0102 0.0005  -0.0716 450 PHE B CB  
7858  C CG  . PHE B 450 ? 0.7520 0.7866 0.5744 -0.0238 -0.0055 -0.0755 450 PHE B CG  
7859  C CD1 . PHE B 450 ? 0.6742 0.7247 0.4977 -0.0239 -0.0100 -0.0671 450 PHE B CD1 
7860  C CD2 . PHE B 450 ? 0.7556 0.8019 0.5774 -0.0353 -0.0070 -0.0872 450 PHE B CD2 
7861  C CE1 . PHE B 450 ? 0.6313 0.7010 0.4580 -0.0363 -0.0152 -0.0668 450 PHE B CE1 
7862  C CE2 . PHE B 450 ? 0.7093 0.7831 0.5310 -0.0465 -0.0117 -0.0842 450 PHE B CE2 
7863  C CZ  . PHE B 450 ? 0.6565 0.7382 0.4822 -0.0475 -0.0154 -0.0721 450 PHE B CZ  
7864  N N   . TRP B 451 ? 0.8432 0.7808 0.6492 0.0069  0.0175  -0.0297 451 TRP B N   
7865  C CA  . TRP B 451 ? 0.8164 0.7154 0.6114 0.0220  0.0255  -0.0121 451 TRP B CA  
7866  C C   . TRP B 451 ? 0.8269 0.6908 0.6335 0.0001  0.0365  0.0002  451 TRP B C   
7867  O O   . TRP B 451 ? 0.8635 0.6774 0.6700 0.0010  0.0411  0.0037  451 TRP B O   
7868  C CB  . TRP B 451 ? 0.7400 0.6575 0.5154 0.0435  0.0258  0.0056  451 TRP B CB  
7869  C CG  . TRP B 451 ? 0.8525 0.7368 0.6097 0.0597  0.0361  0.0340  451 TRP B CG  
7870  C CD1 . TRP B 451 ? 0.8944 0.7506 0.6536 0.0453  0.0515  0.0576  451 TRP B CD1 
7871  C CD2 . TRP B 451 ? 0.8529 0.7336 0.5869 0.0935  0.0318  0.0456  451 TRP B CD2 
7872  N NE1 . TRP B 451 ? 0.9257 0.7544 0.6609 0.0676  0.0590  0.0863  451 TRP B NE1 
7873  C CE2 . TRP B 451 ? 0.9305 0.7738 0.6479 0.0999  0.0458  0.0792  451 TRP B CE2 
7874  C CE3 . TRP B 451 ? 0.8639 0.7743 0.5921 0.1185  0.0172  0.0324  451 TRP B CE3 
7875  C CZ2 . TRP B 451 ? 0.9436 0.7743 0.6327 0.1345  0.0445  0.1016  451 TRP B CZ2 
7876  C CZ3 . TRP B 451 ? 0.8777 0.7825 0.5828 0.1526  0.0139  0.0506  451 TRP B CZ3 
7877  C CH2 . TRP B 451 ? 0.9226 0.7858 0.6053 0.1624  0.0270  0.0857  451 TRP B CH2 
7878  N N   . TRP B 452 ? 0.8559 0.7452 0.6757 -0.0203 0.0404  0.0061  452 TRP B N   
7879  C CA  . TRP B 452 ? 0.8378 0.7091 0.6766 -0.0452 0.0518  0.0203  452 TRP B CA  
7880  C C   . TRP B 452 ? 0.8898 0.7512 0.7525 -0.0730 0.0447  -0.0024 452 TRP B C   
7881  O O   . TRP B 452 ? 0.8804 0.7266 0.7657 -0.0992 0.0515  0.0051  452 TRP B O   
7882  C CB  . TRP B 452 ? 0.7851 0.7008 0.6319 -0.0515 0.0599  0.0354  452 TRP B CB  
7883  C CG  . TRP B 452 ? 0.7701 0.6986 0.5895 -0.0252 0.0674  0.0552  452 TRP B CG  
7884  C CD1 . TRP B 452 ? 0.7446 0.7115 0.5497 -0.0079 0.0614  0.0480  452 TRP B CD1 
7885  C CD2 . TRP B 452 ? 0.7598 0.6615 0.5592 -0.0126 0.0816  0.0851  452 TRP B CD2 
7886  N NE1 . TRP B 452 ? 0.7158 0.6863 0.4918 0.0152  0.0693  0.0668  452 TRP B NE1 
7887  C CE2 . TRP B 452 ? 0.7528 0.6865 0.5230 0.0139  0.0823  0.0925  452 TRP B CE2 
7888  C CE3 . TRP B 452 ? 0.8182 0.6679 0.6196 -0.0210 0.0930  0.1070  452 TRP B CE3 
7889  C CZ2 . TRP B 452 ? 0.7997 0.7236 0.5388 0.0346  0.0941  0.1222  452 TRP B CZ2 
7890  C CZ3 . TRP B 452 ? 0.8665 0.6999 0.6391 -0.0013 0.1063  0.1413  452 TRP B CZ3 
7891  C CH2 . TRP B 452 ? 0.8557 0.7304 0.5957 0.0273  0.1068  0.1493  452 TRP B CH2 
7892  N N   . GLN B 453 ? 0.9046 0.7790 0.7633 -0.0694 0.0313  -0.0297 453 GLN B N   
7893  C CA  . GLN B 453 ? 0.9356 0.8125 0.8099 -0.0930 0.0219  -0.0544 453 GLN B CA  
7894  C C   . GLN B 453 ? 1.0103 0.8311 0.8785 -0.0912 0.0202  -0.0725 453 GLN B C   
7895  O O   . GLN B 453 ? 1.0572 0.8635 0.9057 -0.0645 0.0194  -0.0801 453 GLN B O   
7896  C CB  . GLN B 453 ? 0.8801 0.8045 0.7481 -0.0892 0.0098  -0.0713 453 GLN B CB  
7897  C CG  . GLN B 453 ? 0.9234 0.8496 0.7941 -0.1046 -0.0014 -0.1000 453 GLN B CG  
7898  C CD  . GLN B 453 ? 1.0206 0.9816 0.9139 -0.1302 -0.0093 -0.1023 453 GLN B CD  
7899  O OE1 . GLN B 453 ? 1.0785 1.0502 0.9941 -0.1418 -0.0029 -0.0834 453 GLN B OE1 
7900  N NE2 . GLN B 453 ? 0.9947 0.9792 0.8825 -0.1380 -0.0230 -0.1256 453 GLN B NE2 
7901  N N   . GLY B 454 ? 1.0952 0.8853 0.9829 -0.1190 0.0193  -0.0810 454 GLY B N   
7902  C CA  . GLY B 454 ? 1.1979 0.9280 1.0799 -0.1189 0.0152  -0.1059 454 GLY B CA  
7903  C C   . GLY B 454 ? 1.2234 0.8831 1.0946 -0.0995 0.0262  -0.0881 454 GLY B C   
7904  O O   . GLY B 454 ? 1.4364 1.0366 1.3014 -0.0937 0.0228  -0.1101 454 GLY B O   
7905  N N   . GLU B 455 ? 1.1854 0.8482 1.0510 -0.0863 0.0384  -0.0497 455 GLU B N   
7906  C CA  . GLU B 455 ? 1.3519 0.9481 1.2039 -0.0658 0.0486  -0.0257 455 GLU B CA  
7907  C C   . GLU B 455 ? 1.4725 0.9983 1.3452 -0.0982 0.0556  -0.0166 455 GLU B C   
7908  O O   . GLU B 455 ? 1.4746 0.9437 1.3520 -0.1061 0.0480  -0.0458 455 GLU B O   
7909  C CB  . GLU B 455 ? 1.2602 0.8858 1.0965 -0.0449 0.0589  0.0138  455 GLU B CB  
7910  C CG  . GLU B 455 ? 1.2520 0.9042 1.0622 -0.0015 0.0522  0.0097  455 GLU B CG  
7911  C CD  . GLU B 455 ? 1.3803 0.9750 1.1773 0.0289  0.0491  0.0002  455 GLU B CD  
7912  O OE1 . GLU B 455 ? 1.4418 0.9662 1.2337 0.0337  0.0575  0.0234  455 GLU B OE1 
7913  O OE2 . GLU B 455 ? 1.2940 0.9143 1.0864 0.0496  0.0396  -0.0286 455 GLU B OE2 
7914  N N   . GLU B 456 ? 1.4600 0.9892 1.3456 -0.1177 0.0707  0.0230  456 GLU B N   
7915  C CA  . GLU B 456 ? 1.4577 0.9268 1.3698 -0.1559 0.0805  0.0391  456 GLU B CA  
7916  C C   . GLU B 456 ? 1.4229 0.9560 1.3657 -0.1909 0.0918  0.0627  456 GLU B C   
7917  O O   . GLU B 456 ? 1.3938 0.9922 1.3248 -0.1735 0.0992  0.0832  456 GLU B O   
7918  C CB  . GLU B 456 ? 1.5068 0.8919 1.3983 -0.1354 0.0946  0.0779  456 GLU B CB  
7919  C CG  . GLU B 456 ? 1.5160 0.8171 1.3889 -0.1076 0.0842  0.0527  456 GLU B CG  
7920  C CD  . GLU B 456 ? 1.6771 0.8721 1.5700 -0.1387 0.0878  0.0541  456 GLU B CD  
7921  O OE1 . GLU B 456 ? 1.7681 0.9407 1.6801 -0.1716 0.1048  0.0960  456 GLU B OE1 
7922  O OE2 . GLU B 456 ? 1.6274 0.7609 1.5172 -0.1309 0.0746  0.0128  456 GLU B OE2 
7923  N N   . LYS B 457 ? 1.4392 0.9557 1.4237 -0.2400 0.0924  0.0571  457 LYS B N   
7924  C CA  . LYS B 457 ? 1.4482 1.0390 1.4726 -0.2758 0.1014  0.0731  457 LYS B CA  
7925  C C   . LYS B 457 ? 1.4799 1.0786 1.4982 -0.2710 0.1300  0.1311  457 LYS B C   
7926  O O   . LYS B 457 ? 1.5867 1.1167 1.6101 -0.2874 0.1461  0.1636  457 LYS B O   
7927  C CB  . LYS B 457 ? 1.4061 0.9776 1.4814 -0.3321 0.0937  0.0524  457 LYS B CB  
7928  C CG  . LYS B 457 ? 1.3860 1.0569 1.5093 -0.3663 0.0935  0.0521  457 LYS B CG  
7929  C CD  . LYS B 457 ? 1.3963 1.0694 1.5632 -0.4081 0.1186  0.0958  457 LYS B CD  
7930  C CE  . LYS B 457 ? 1.3355 1.0866 1.5681 -0.4577 0.1103  0.0793  457 LYS B CE  
7931  N NZ  . LYS B 457 ? 1.4719 1.2237 1.7567 -0.5073 0.1351  0.1196  457 LYS B NZ  
7932  N N   . ALA B 458 ? 1.4264 1.1056 1.4305 -0.2471 0.1366  0.1442  458 ALA B N   
7933  C CA  . ALA B 458 ? 1.3553 1.0623 1.3465 -0.2363 0.1633  0.1939  458 ALA B CA  
7934  C C   . ALA B 458 ? 1.2881 1.1013 1.3017 -0.2407 0.1676  0.1910  458 ALA B C   
7935  O O   . ALA B 458 ? 1.3088 1.1664 1.3319 -0.2369 0.1470  0.1532  458 ALA B O   
7936  C CB  . ALA B 458 ? 1.4305 1.1149 1.3610 -0.1823 0.1646  0.2093  458 ALA B CB  
7937  N N   . PRO B 459 ? 1.1865 1.0431 1.2070 -0.2457 0.1948  0.2316  459 PRO B N   
7938  C CA  . PRO B 459 ? 1.1595 1.1190 1.2079 -0.2489 0.2005  0.2273  459 PRO B CA  
7939  C C   . PRO B 459 ? 1.1643 1.1661 1.1730 -0.2008 0.1878  0.2059  459 PRO B C   
7940  O O   . PRO B 459 ? 1.2335 1.1972 1.1919 -0.1651 0.1796  0.2021  459 PRO B O   
7941  C CB  . PRO B 459 ? 1.1510 1.1400 1.2079 -0.2604 0.2373  0.2796  459 PRO B CB  
7942  C CG  . PRO B 459 ? 1.2718 1.1838 1.2747 -0.2370 0.2475  0.3112  459 PRO B CG  
7943  C CD  . PRO B 459 ? 1.3338 1.1520 1.3354 -0.2458 0.2235  0.2854  459 PRO B CD  
7944  N N   . PHE B 460 ? 1.0646 1.1470 1.1013 -0.2014 0.1848  0.1907  460 PHE B N   
7945  C CA  . PHE B 460 ? 0.9181 1.0464 0.9288 -0.1619 0.1743  0.1705  460 PHE B CA  
7946  C C   . PHE B 460 ? 0.9020 0.9944 0.8897 -0.1461 0.1439  0.1340  460 PHE B C   
7947  O O   . PHE B 460 ? 0.9646 1.0831 0.9310 -0.1167 0.1331  0.1169  460 PHE B O   
7948  C CB  . PHE B 460 ? 0.9539 1.0938 0.9157 -0.1240 0.1929  0.1940  460 PHE B CB  
7949  C CG  . PHE B 460 ? 0.9447 1.1326 0.9231 -0.1345 0.2270  0.2323  460 PHE B CG  
7950  C CD1 . PHE B 460 ? 1.0108 1.2805 1.0390 -0.1481 0.2364  0.2300  460 PHE B CD1 
7951  C CD2 . PHE B 460 ? 0.9842 1.1403 0.9303 -0.1302 0.2502  0.2729  460 PHE B CD2 
7952  C CE1 . PHE B 460 ? 1.0880 1.4139 1.1368 -0.1586 0.2704  0.2653  460 PHE B CE1 
7953  C CE2 . PHE B 460 ? 1.0284 1.2338 0.9890 -0.1418 0.2853  0.3127  460 PHE B CE2 
7954  C CZ  . PHE B 460 ? 1.0186 1.3119 1.0322 -0.1572 0.2969  0.3086  460 PHE B CZ  
7955  N N   . VAL B 461 ? 0.9219 0.9552 0.9138 -0.1649 0.1308  0.1210  461 VAL B N   
7956  C CA  . VAL B 461 ? 0.9255 0.9337 0.8965 -0.1502 0.1054  0.0875  461 VAL B CA  
7957  C C   . VAL B 461 ? 0.8108 0.8699 0.8081 -0.1589 0.0876  0.0609  461 VAL B C   
7958  O O   . VAL B 461 ? 0.7497 0.8145 0.7260 -0.1385 0.0711  0.0407  461 VAL B O   
7959  C CB  . VAL B 461 ? 1.0609 0.9942 1.0276 -0.1639 0.0988  0.0796  461 VAL B CB  
7960  C CG1 . VAL B 461 ? 1.0520 0.9763 1.0134 -0.1614 0.0740  0.0405  461 VAL B CG1 
7961  C CG2 . VAL B 461 ? 1.0836 0.9651 1.0101 -0.1375 0.1095  0.1027  461 VAL B CG2 
7962  N N   . GLU B 462 ? 0.8724 0.9732 0.9171 -0.1890 0.0905  0.0633  462 GLU B N   
7963  C CA  . GLU B 462 ? 0.7566 0.9092 0.8268 -0.1956 0.0710  0.0400  462 GLU B CA  
7964  C C   . GLU B 462 ? 0.7300 0.9279 0.7850 -0.1607 0.0687  0.0395  462 GLU B C   
7965  O O   . GLU B 462 ? 0.6905 0.9074 0.7436 -0.1522 0.0487  0.0204  462 GLU B O   
7966  C CB  . GLU B 462 ? 0.7479 0.9489 0.8775 -0.2336 0.0745  0.0443  462 GLU B CB  
7967  C CG  . GLU B 462 ? 0.8841 1.1246 1.0379 -0.2385 0.1041  0.0784  462 GLU B CG  
7968  C CD  . GLU B 462 ? 1.0745 1.2558 1.2249 -0.2599 0.1249  0.1041  462 GLU B CD  
7969  O OE1 . GLU B 462 ? 1.0508 1.2370 1.1836 -0.2443 0.1508  0.1359  462 GLU B OE1 
7970  O OE2 . GLU B 462 ? 1.1490 1.2761 1.3113 -0.2906 0.1151  0.0924  462 GLU B OE2 
7971  N N   . VAL B 463 ? 0.6881 0.9003 0.7288 -0.1389 0.0886  0.0602  463 VAL B N   
7972  C CA  . VAL B 463 ? 0.6825 0.9287 0.7071 -0.1041 0.0860  0.0554  463 VAL B CA  
7973  C C   . VAL B 463 ? 0.6514 0.8554 0.6349 -0.0831 0.0677  0.0373  463 VAL B C   
7974  O O   . VAL B 463 ? 0.6609 0.8813 0.6404 -0.0665 0.0539  0.0248  463 VAL B O   
7975  C CB  . VAL B 463 ? 0.6659 0.9339 0.6764 -0.0831 0.1113  0.0768  463 VAL B CB  
7976  C CG1 . VAL B 463 ? 0.5930 0.8879 0.5860 -0.0458 0.1060  0.0646  463 VAL B CG1 
7977  C CG2 . VAL B 463 ? 0.6322 0.9515 0.6886 -0.1070 0.1333  0.0987  463 VAL B CG2 
7978  N N   . PHE B 464 ? 0.6772 0.8275 0.6316 -0.0829 0.0680  0.0378  464 PHE B N   
7979  C CA  . PHE B 464 ? 0.6946 0.8146 0.6166 -0.0659 0.0522  0.0216  464 PHE B CA  
7980  C C   . PHE B 464 ? 0.6600 0.7843 0.5934 -0.0780 0.0326  0.0028  464 PHE B C   
7981  O O   . PHE B 464 ? 0.6758 0.8010 0.5942 -0.0643 0.0203  -0.0071 464 PHE B O   
7982  C CB  . PHE B 464 ? 0.6889 0.7602 0.5851 -0.0627 0.0556  0.0256  464 PHE B CB  
7983  C CG  . PHE B 464 ? 0.6478 0.7152 0.5191 -0.0427 0.0709  0.0445  464 PHE B CG  
7984  C CD1 . PHE B 464 ? 0.6886 0.7582 0.5286 -0.0153 0.0648  0.0374  464 PHE B CD1 
7985  C CD2 . PHE B 464 ? 0.7161 0.7788 0.5942 -0.0525 0.0909  0.0699  464 PHE B CD2 
7986  C CE1 . PHE B 464 ? 0.6573 0.7288 0.4685 0.0055  0.0763  0.0522  464 PHE B CE1 
7987  C CE2 . PHE B 464 ? 0.6867 0.7499 0.5347 -0.0314 0.1057  0.0907  464 PHE B CE2 
7988  C CZ  . PHE B 464 ? 0.6778 0.7476 0.4899 -0.0005 0.0974  0.0803  464 PHE B CZ  
7989  N N   . ASP B 465 ? 0.6752 0.8025 0.6340 -0.1048 0.0292  -0.0020 465 ASP B N   
7990  C CA  . ASP B 465 ? 0.7341 0.8750 0.6995 -0.1148 0.0098  -0.0201 465 ASP B CA  
7991  C C   . ASP B 465 ? 0.7601 0.9508 0.7403 -0.1043 0.0020  -0.0178 465 ASP B C   
7992  O O   . ASP B 465 ? 0.7252 0.9185 0.6901 -0.0934 -0.0121 -0.0247 465 ASP B O   
7993  C CB  . ASP B 465 ? 0.7682 0.9044 0.7577 -0.1462 0.0056  -0.0304 465 ASP B CB  
7994  C CG  . ASP B 465 ? 0.8129 0.9680 0.8022 -0.1544 -0.0158 -0.0516 465 ASP B CG  
7995  O OD1 . ASP B 465 ? 0.7060 0.8309 0.6664 -0.1493 -0.0225 -0.0660 465 ASP B OD1 
7996  O OD2 . ASP B 465 ? 0.8511 1.0566 0.8680 -0.1638 -0.0256 -0.0532 465 ASP B OD2 
7997  N N   . LYS B 466 ? 0.5783 0.8100 0.5888 -0.1053 0.0123  -0.0057 466 LYS B N   
7998  C CA  . LYS B 466 ? 0.6588 0.9402 0.6861 -0.0883 0.0055  -0.0033 466 LYS B CA  
7999  C C   . LYS B 466 ? 0.6089 0.8688 0.6034 -0.0555 0.0037  -0.0029 466 LYS B C   
8000  O O   . LYS B 466 ? 0.5252 0.7965 0.5176 -0.0407 -0.0104 -0.0051 466 LYS B O   
8001  C CB  . LYS B 466 ? 0.5937 0.9294 0.6612 -0.0916 0.0216  0.0098  466 LYS B CB  
8002  C CG  . LYS B 466 ? 0.7558 1.1089 0.8619 -0.1312 0.0254  0.0111  466 LYS B CG  
8003  C CD  . LYS B 466 ? 0.7596 1.1415 0.8885 -0.1507 0.0002  -0.0060 466 LYS B CD  
8004  C CE  . LYS B 466 ? 0.8870 1.3454 1.0781 -0.1730 0.0008  -0.0021 466 LYS B CE  
8005  N NZ  . LYS B 466 ? 0.8621 1.3688 1.0740 -0.1802 -0.0283 -0.0186 466 LYS B NZ  
8006  N N   . LEU B 467 ? 0.6443 0.8705 0.6123 -0.0440 0.0162  0.0002  467 LEU B N   
8007  C CA  . LEU B 467 ? 0.6773 0.8795 0.6158 -0.0176 0.0118  -0.0044 467 LEU B CA  
8008  C C   . LEU B 467 ? 0.7552 0.9235 0.6730 -0.0231 -0.0044 -0.0131 467 LEU B C   
8009  O O   . LEU B 467 ? 0.7327 0.8936 0.6426 -0.0106 -0.0156 -0.0149 467 LEU B O   
8010  C CB  . LEU B 467 ? 0.6413 0.8250 0.5559 -0.0044 0.0266  -0.0015 467 LEU B CB  
8011  C CG  . LEU B 467 ? 0.6480 0.8693 0.5719 0.0135  0.0437  0.0064  467 LEU B CG  
8012  C CD1 . LEU B 467 ? 0.6611 0.8708 0.5606 0.0186  0.0609  0.0153  467 LEU B CD1 
8013  C CD2 . LEU B 467 ? 0.6243 0.8498 0.5396 0.0444  0.0368  -0.0042 467 LEU B CD2 
8014  N N   . PHE B 468 ? 0.6689 0.8158 0.5785 -0.0408 -0.0045 -0.0172 468 PHE B N   
8015  C CA  . PHE B 468 ? 0.6633 0.7891 0.5551 -0.0457 -0.0162 -0.0248 468 PHE B CA  
8016  C C   . PHE B 468 ? 0.6834 0.8308 0.5829 -0.0512 -0.0300 -0.0246 468 PHE B C   
8017  O O   . PHE B 468 ? 0.6617 0.7987 0.5463 -0.0463 -0.0388 -0.0227 468 PHE B O   
8018  C CB  . PHE B 468 ? 0.7079 0.8134 0.5920 -0.0590 -0.0127 -0.0317 468 PHE B CB  
8019  C CG  . PHE B 468 ? 0.6578 0.7554 0.5271 -0.0642 -0.0217 -0.0406 468 PHE B CG  
8020  C CD1 . PHE B 468 ? 0.7080 0.7928 0.5614 -0.0558 -0.0233 -0.0411 468 PHE B CD1 
8021  C CD2 . PHE B 468 ? 0.6751 0.7833 0.5468 -0.0786 -0.0281 -0.0496 468 PHE B CD2 
8022  C CE1 . PHE B 468 ? 0.7462 0.8331 0.5892 -0.0620 -0.0278 -0.0462 468 PHE B CE1 
8023  C CE2 . PHE B 468 ? 0.7662 0.8745 0.6202 -0.0809 -0.0332 -0.0571 468 PHE B CE2 
8024  C CZ  . PHE B 468 ? 0.6635 0.7633 0.5045 -0.0728 -0.0313 -0.0533 468 PHE B CZ  
8025  N N   . ARG B 469 ? 0.6080 0.7881 0.5315 -0.0622 -0.0326 -0.0249 469 ARG B N   
8026  C CA  . ARG B 469 ? 0.6819 0.8907 0.6103 -0.0645 -0.0487 -0.0244 469 ARG B CA  
8027  C C   . ARG B 469 ? 0.6761 0.8994 0.6099 -0.0410 -0.0543 -0.0124 469 ARG B C   
8028  O O   . ARG B 469 ? 0.7014 0.9338 0.6270 -0.0351 -0.0684 -0.0061 469 ARG B O   
8029  C CB  . ARG B 469 ? 0.5438 0.7891 0.4997 -0.0849 -0.0537 -0.0322 469 ARG B CB  
8030  C CG  . ARG B 469 ? 0.7098 0.9292 0.6577 -0.1065 -0.0508 -0.0477 469 ARG B CG  
8031  C CD  . ARG B 469 ? 0.8063 1.0546 0.7710 -0.1293 -0.0644 -0.0633 469 ARG B CD  
8032  N NE  . ARG B 469 ? 0.7140 0.9255 0.6673 -0.1461 -0.0617 -0.0821 469 ARG B NE  
8033  C CZ  . ARG B 469 ? 0.7992 1.0044 0.7268 -0.1499 -0.0723 -0.1010 469 ARG B CZ  
8034  N NH1 . ARG B 469 ? 0.8331 1.0692 0.7417 -0.1412 -0.0863 -0.1001 469 ARG B NH1 
8035  N NH2 . ARG B 469 ? 0.7078 0.8743 0.6266 -0.1603 -0.0682 -0.1203 469 ARG B NH2 
8036  N N   . SER B 470 ? 0.6688 0.8929 0.6129 -0.0245 -0.0432 -0.0086 470 SER B N   
8037  C CA  . SER B 470 ? 0.6646 0.8929 0.6109 0.0035  -0.0481 -0.0012 470 SER B CA  
8038  C C   . SER B 470 ? 0.7067 0.8820 0.6220 0.0127  -0.0534 0.0003  470 SER B C   
8039  O O   . SER B 470 ? 0.7333 0.8993 0.6426 0.0252  -0.0654 0.0100  470 SER B O   
8040  C CB  . SER B 470 ? 0.5942 0.8421 0.5572 0.0211  -0.0328 -0.0016 470 SER B CB  
8041  O OG  . SER B 470 ? 0.6423 0.9198 0.6230 0.0482  -0.0384 0.0037  470 SER B OG  
8042  N N   . PHE B 471 ? 0.6345 0.7756 0.5318 0.0057  -0.0453 -0.0074 471 PHE B N   
8043  C CA  . PHE B 471 ? 0.6913 0.7874 0.5666 0.0085  -0.0508 -0.0077 471 PHE B CA  
8044  C C   . PHE B 471 ? 0.7199 0.8110 0.5849 -0.0064 -0.0607 0.0021  471 PHE B C   
8045  O O   . PHE B 471 ? 0.7551 0.8182 0.6100 -0.0014 -0.0682 0.0122  471 PHE B O   
8046  C CB  . PHE B 471 ? 0.6885 0.7632 0.5509 0.0024  -0.0427 -0.0192 471 PHE B CB  
8047  C CG  . PHE B 471 ? 0.5752 0.6547 0.4379 0.0197  -0.0326 -0.0267 471 PHE B CG  
8048  C CD1 . PHE B 471 ? 0.7299 0.8038 0.5928 0.0448  -0.0336 -0.0301 471 PHE B CD1 
8049  C CD2 . PHE B 471 ? 0.6541 0.7433 0.5139 0.0136  -0.0212 -0.0293 471 PHE B CD2 
8050  C CE1 . PHE B 471 ? 0.7309 0.8162 0.5889 0.0635  -0.0220 -0.0382 471 PHE B CE1 
8051  C CE2 . PHE B 471 ? 0.6660 0.7644 0.5205 0.0304  -0.0097 -0.0320 471 PHE B CE2 
8052  C CZ  . PHE B 471 ? 0.6722 0.7726 0.5248 0.0553  -0.0094 -0.0375 471 PHE B CZ  
8053  N N   . VAL B 472 ? 0.7125 0.8284 0.5778 -0.0245 -0.0602 -0.0004 472 VAL B N   
8054  C CA  . VAL B 472 ? 0.7542 0.8718 0.6033 -0.0362 -0.0672 0.0079  472 VAL B CA  
8055  C C   . VAL B 472 ? 0.7862 0.9191 0.6349 -0.0245 -0.0800 0.0249  472 VAL B C   
8056  O O   . VAL B 472 ? 0.8970 1.0150 0.7275 -0.0253 -0.0855 0.0416  472 VAL B O   
8057  C CB  . VAL B 472 ? 0.6664 0.8059 0.5114 -0.0540 -0.0642 -0.0046 472 VAL B CB  
8058  C CG1 . VAL B 472 ? 0.7629 0.8839 0.6077 -0.0594 -0.0526 -0.0177 472 VAL B CG1 
8059  C CG2 . VAL B 472 ? 0.6946 0.8693 0.5576 -0.0568 -0.0691 -0.0111 472 VAL B CG2 
8060  N N   . ARG B 473 ? 0.7472 0.9132 0.6172 -0.0128 -0.0847 0.0238  473 ARG B N   
8061  C CA  . ARG B 473 ? 0.8220 1.0090 0.6939 0.0043  -0.0994 0.0407  473 ARG B CA  
8062  C C   . ARG B 473 ? 0.8816 1.0243 0.7480 0.0281  -0.1014 0.0552  473 ARG B C   
8063  O O   . ARG B 473 ? 0.9221 1.0509 0.7735 0.0381  -0.1120 0.0770  473 ARG B O   
8064  C CB  . ARG B 473 ? 0.7702 1.0150 0.6746 0.0109  -0.1045 0.0344  473 ARG B CB  
8065  C CG  . ARG B 473 ? 0.7651 1.0401 0.6751 0.0349  -0.1221 0.0523  473 ARG B CG  
8066  C CD  . ARG B 473 ? 0.8849 1.2368 0.8269 0.0319  -0.1333 0.0450  473 ARG B CD  
8067  N NE  . ARG B 473 ? 1.0387 1.4238 1.0227 0.0435  -0.1246 0.0382  473 ARG B NE  
8068  C CZ  . ARG B 473 ? 0.9248 1.3403 0.9316 0.0767  -0.1308 0.0485  473 ARG B CZ  
8069  N NH1 . ARG B 473 ? 1.0358 1.4431 1.0263 0.1038  -0.1474 0.0681  473 ARG B NH1 
8070  N NH2 . ARG B 473 ? 0.6690 1.1253 0.7156 0.0852  -0.1189 0.0410  473 ARG B NH2 
8071  N N   . ARG B 474 ? 0.8147 0.9311 0.6901 0.0381  -0.0917 0.0432  474 ARG B N   
8072  C CA  . ARG B 474 ? 0.8341 0.8993 0.7034 0.0608  -0.0942 0.0488  474 ARG B CA  
8073  C C   . ARG B 474 ? 0.8736 0.8825 0.7197 0.0446  -0.0959 0.0586  474 ARG B C   
8074  O O   . ARG B 474 ? 0.9756 0.9346 0.8146 0.0588  -0.1024 0.0704  474 ARG B O   
8075  C CB  . ARG B 474 ? 0.8085 0.8664 0.6879 0.0744  -0.0831 0.0277  474 ARG B CB  
8076  C CG  . ARG B 474 ? 0.9322 0.9425 0.8074 0.1050  -0.0863 0.0240  474 ARG B CG  
8077  C CD  . ARG B 474 ? 1.0046 1.0181 0.8881 0.1366  -0.0980 0.0414  474 ARG B CD  
8078  N NE  . ARG B 474 ? 1.1945 1.1496 1.0716 0.1673  -0.1002 0.0324  474 ARG B NE  
8079  C CZ  . ARG B 474 ? 1.2337 1.2009 1.1199 0.1966  -0.0920 0.0115  474 ARG B CZ  
8080  N NH1 . ARG B 474 ? 1.1483 1.1903 1.0559 0.2006  -0.0801 0.0042  474 ARG B NH1 
8081  N NH2 . ARG B 474 ? 1.2398 1.1422 1.1132 0.2217  -0.0951 -0.0032 474 ARG B NH2 
8082  N N   . ALA B 475 ? 0.8074 0.8236 0.6441 0.0152  -0.0897 0.0547  475 ALA B N   
8083  C CA  . ALA B 475 ? 0.9255 0.9017 0.7471 -0.0040 -0.0888 0.0652  475 ALA B CA  
8084  C C   . ALA B 475 ? 0.9312 0.9020 0.7368 -0.0051 -0.0963 0.0973  475 ALA B C   
8085  O O   . ALA B 475 ? 0.9002 0.8221 0.6972 -0.0119 -0.0976 0.1153  475 ALA B O   
8086  C CB  . ALA B 475 ? 0.8501 0.8477 0.6695 -0.0301 -0.0788 0.0517  475 ALA B CB  
8087  N N   . GLN B 476 ? 0.8418 0.8622 0.6424 0.0006  -0.1020 0.1058  476 GLN B N   
8088  C CA  . GLN B 476 ? 0.8619 0.8898 0.6394 0.0007  -0.1094 0.1373  476 GLN B CA  
8089  C C   . GLN B 476 ? 0.9160 0.9250 0.6928 0.0325  -0.1234 0.1613  476 GLN B C   
8090  O O   . GLN B 476 ? 1.0417 1.0638 0.7969 0.0390  -0.1322 0.1908  476 GLN B O   
8091  C CB  . GLN B 476 ? 0.8950 0.9899 0.6623 -0.0085 -0.1116 0.1302  476 GLN B CB  
8092  C CG  . GLN B 476 ? 0.8104 0.9286 0.5907 -0.0258 -0.1013 0.0962  476 GLN B CG  
8093  C CD  . GLN B 476 ? 0.8187 0.9867 0.5828 -0.0391 -0.1023 0.0863  476 GLN B CD  
8094  O OE1 . GLN B 476 ? 0.8935 1.0727 0.6286 -0.0458 -0.1019 0.1030  476 GLN B OE1 
8095  N NE2 . GLN B 476 ? 0.8382 1.0350 0.6196 -0.0434 -0.1028 0.0585  476 GLN B NE2 
8096  N N   . GLU B 477 ? 0.9222 0.9026 0.7192 0.0563  -0.1257 0.1498  477 GLU B N   
8097  C CA  . GLU B 477 ? 0.9841 0.9416 0.7823 0.0931  -0.1387 0.1709  477 GLU B CA  
8098  C C   . GLU B 477 ? 1.1877 1.0525 0.9821 0.1004  -0.1378 0.1780  477 GLU B C   
8099  O O   . GLU B 477 ? 1.3211 1.1566 1.1286 0.1330  -0.1421 0.1680  477 GLU B O   
8100  C CB  . GLU B 477 ? 0.9588 0.9662 0.7861 0.1225  -0.1430 0.1512  477 GLU B CB  
8101  C CG  . GLU B 477 ? 0.9152 1.0025 0.7571 0.1036  -0.1395 0.1303  477 GLU B CG  
8102  C CD  . GLU B 477 ? 0.9104 1.0484 0.7882 0.1257  -0.1393 0.1119  477 GLU B CD  
8103  O OE1 . GLU B 477 ? 1.0518 1.1653 0.9412 0.1589  -0.1397 0.1115  477 GLU B OE1 
8104  O OE2 . GLU B 477 ? 0.8526 1.0554 0.7481 0.1097  -0.1383 0.0976  477 GLU B OE2 
8105  N N   . MET C 1   ? 1.1518 1.0732 1.2497 -0.1974 -0.1257 0.4722  1   MET C N   
8106  C CA  . MET C 1   ? 1.0241 0.9200 1.1123 -0.1718 -0.1307 0.4485  1   MET C CA  
8107  C C   . MET C 1   ? 0.9688 0.8607 1.0605 -0.1571 -0.1228 0.4125  1   MET C C   
8108  O O   . MET C 1   ? 0.9122 0.8403 0.9940 -0.1568 -0.1047 0.3964  1   MET C O   
8109  C CB  . MET C 1   ? 1.0919 1.0162 1.1524 -0.1668 -0.1224 0.4502  1   MET C CB  
8110  C CG  . MET C 1   ? 1.2018 1.0982 1.2554 -0.1439 -0.1322 0.4376  1   MET C CG  
8111  S SD  . MET C 1   ? 1.5405 1.4622 1.5698 -0.1471 -0.1334 0.4601  1   MET C SD  
8112  C CE  . MET C 1   ? 1.2323 1.2130 1.2450 -0.1721 -0.1125 0.4705  1   MET C CE  
8113  N N   . LYS C 2   ? 1.0199 0.8670 1.1251 -0.1447 -0.1368 0.3996  2   LYS C N   
8114  C CA  . LYS C 2   ? 0.9657 0.8051 1.0703 -0.1288 -0.1318 0.3661  2   LYS C CA  
8115  C C   . LYS C 2   ? 1.0573 0.9076 1.1390 -0.1113 -0.1240 0.3497  2   LYS C C   
8116  O O   . LYS C 2   ? 1.1059 0.9446 1.1790 -0.1036 -0.1315 0.3589  2   LYS C O   
8117  C CB  . LYS C 2   ? 0.8975 0.6860 1.0175 -0.1199 -0.1493 0.3563  2   LYS C CB  
8118  C CG  . LYS C 2   ? 1.0644 0.8428 1.1802 -0.1033 -0.1459 0.3229  2   LYS C CG  
8119  C CD  . LYS C 2   ? 1.0995 0.8364 1.2321 -0.1023 -0.1612 0.3142  2   LYS C CD  
8120  C CE  . LYS C 2   ? 1.0952 0.7884 1.2237 -0.0849 -0.1748 0.3061  2   LYS C CE  
8121  N NZ  . LYS C 2   ? 1.0154 0.6665 1.1628 -0.0917 -0.1938 0.3159  2   LYS C NZ  
8122  N N   . LYS C 3   ? 1.0389 0.9124 1.1127 -0.1056 -0.1096 0.3265  3   LYS C N   
8123  C CA  . LYS C 3   ? 1.0316 0.9215 1.0840 -0.0925 -0.1004 0.3116  3   LYS C CA  
8124  C C   . LYS C 3   ? 0.9864 0.8532 1.0383 -0.0742 -0.1025 0.2833  3   LYS C C   
8125  O O   . LYS C 3   ? 0.9656 0.8362 1.0246 -0.0742 -0.0972 0.2670  3   LYS C O   
8126  C CB  . LYS C 3   ? 1.0432 0.9806 1.0844 -0.1015 -0.0814 0.3081  3   LYS C CB  
8127  C CG  . LYS C 3   ? 1.1229 1.0870 1.1697 -0.1233 -0.0763 0.3324  3   LYS C CG  
8128  C CD  . LYS C 3   ? 1.1751 1.1877 1.2050 -0.1304 -0.0567 0.3283  3   LYS C CD  
8129  C CE  . LYS C 3   ? 1.1905 1.2319 1.2359 -0.1448 -0.0441 0.3288  3   LYS C CE  
8130  N NZ  . LYS C 3   ? 1.1738 1.2585 1.2056 -0.1459 -0.0232 0.3134  3   LYS C NZ  
8131  N N   . LEU C 4   ? 1.0468 0.8917 1.0910 -0.0590 -0.1102 0.2784  4   LEU C N   
8132  C CA  . LEU C 4   ? 1.0204 0.8521 1.0586 -0.0421 -0.1089 0.2520  4   LEU C CA  
8133  C C   . LEU C 4   ? 0.9108 0.7766 0.9333 -0.0401 -0.0935 0.2387  4   LEU C C   
8134  O O   . LEU C 4   ? 0.8625 0.7535 0.8726 -0.0437 -0.0876 0.2480  4   LEU C O   
8135  C CB  . LEU C 4   ? 0.9687 0.7729 1.0042 -0.0265 -0.1194 0.2507  4   LEU C CB  
8136  C CG  . LEU C 4   ? 0.9708 0.7680 0.9960 -0.0090 -0.1162 0.2259  4   LEU C CG  
8137  C CD1 . LEU C 4   ? 0.9722 0.7299 1.0045 0.0044  -0.1285 0.2194  4   LEU C CD1 
8138  C CD2 . LEU C 4   ? 0.9466 0.7707 0.9563 -0.0036 -0.1081 0.2251  4   LEU C CD2 
8139  N N   . PHE C 5   ? 0.8702 0.7364 0.8934 -0.0353 -0.0881 0.2174  5   PHE C N   
8140  C CA  . PHE C 5   ? 0.9028 0.7971 0.9144 -0.0332 -0.0746 0.2029  5   PHE C CA  
8141  C C   . PHE C 5   ? 0.8490 0.7304 0.8492 -0.0174 -0.0762 0.1862  5   PHE C C   
8142  O O   . PHE C 5   ? 0.9017 0.7603 0.9056 -0.0095 -0.0814 0.1727  5   PHE C O   
8143  C CB  . PHE C 5   ? 0.7678 0.6736 0.7910 -0.0392 -0.0678 0.1924  5   PHE C CB  
8144  C CG  . PHE C 5   ? 0.8616 0.7865 0.8976 -0.0555 -0.0639 0.2085  5   PHE C CG  
8145  C CD1 . PHE C 5   ? 0.8435 0.7985 0.8701 -0.0652 -0.0550 0.2220  5   PHE C CD1 
8146  C CD2 . PHE C 5   ? 0.9216 0.8362 0.9786 -0.0623 -0.0693 0.2107  5   PHE C CD2 
8147  C CE1 . PHE C 5   ? 0.8702 0.8459 0.9076 -0.0813 -0.0501 0.2377  5   PHE C CE1 
8148  C CE2 . PHE C 5   ? 0.9265 0.8616 0.9972 -0.0784 -0.0650 0.2266  5   PHE C CE2 
8149  C CZ  . PHE C 5   ? 1.0009 0.9673 1.0616 -0.0880 -0.0547 0.2403  5   PHE C CZ  
8150  N N   . LEU C 6   ? 0.8546 0.7520 0.8404 -0.0139 -0.0721 0.1879  6   LEU C N   
8151  C CA  . LEU C 6   ? 0.9001 0.7908 0.8759 -0.0003 -0.0727 0.1745  6   LEU C CA  
8152  C C   . LEU C 6   ? 0.8578 0.7712 0.8233 -0.0007 -0.0615 0.1594  6   LEU C C   
8153  O O   . LEU C 6   ? 0.8458 0.7863 0.8038 -0.0087 -0.0536 0.1635  6   LEU C O   
8154  C CB  . LEU C 6   ? 0.9420 0.8344 0.9120 0.0043  -0.0777 0.1874  6   LEU C CB  
8155  C CG  . LEU C 6   ? 0.8506 0.7350 0.8151 0.0190  -0.0798 0.1763  6   LEU C CG  
8156  C CD1 . LEU C 6   ? 0.8592 0.7101 0.8326 0.0294  -0.0875 0.1681  6   LEU C CD1 
8157  C CD2 . LEU C 6   ? 0.8831 0.7790 0.8443 0.0215  -0.0837 0.1909  6   LEU C CD2 
8158  N N   . VAL C 7   ? 0.8683 0.7700 0.8331 0.0073  -0.0613 0.1420  7   VAL C N   
8159  C CA  . VAL C 7   ? 0.8387 0.7558 0.7961 0.0079  -0.0528 0.1269  7   VAL C CA  
8160  C C   . VAL C 7   ? 0.8565 0.7680 0.8035 0.0182  -0.0545 0.1188  7   VAL C C   
8161  O O   . VAL C 7   ? 0.9240 0.8142 0.8722 0.0263  -0.0599 0.1121  7   VAL C O   
8162  C CB  . VAL C 7   ? 0.7581 0.6683 0.7258 0.0067  -0.0517 0.1154  7   VAL C CB  
8163  C CG1 . VAL C 7   ? 0.7807 0.7055 0.7433 0.0075  -0.0438 0.1008  7   VAL C CG1 
8164  C CG2 . VAL C 7   ? 0.7380 0.6554 0.7200 -0.0036 -0.0503 0.1246  7   VAL C CG2 
8165  N N   . PHE C 8   ? 0.7627 0.6947 0.6988 0.0170  -0.0498 0.1192  8   PHE C N   
8166  C CA  . PHE C 8   ? 0.6758 0.6085 0.6035 0.0247  -0.0503 0.1119  8   PHE C CA  
8167  C C   . PHE C 8   ? 0.6236 0.5613 0.5471 0.0236  -0.0447 0.0960  8   PHE C C   
8168  O O   . PHE C 8   ? 0.7356 0.6896 0.6570 0.0164  -0.0383 0.0921  8   PHE C O   
8169  C CB  . PHE C 8   ? 0.7752 0.7281 0.6950 0.0228  -0.0501 0.1218  8   PHE C CB  
8170  C CG  . PHE C 8   ? 0.7892 0.7339 0.7145 0.0284  -0.0581 0.1364  8   PHE C CG  
8171  C CD1 . PHE C 8   ? 0.8109 0.7371 0.7416 0.0404  -0.0630 0.1326  8   PHE C CD1 
8172  C CD2 . PHE C 8   ? 0.6487 0.6045 0.5739 0.0217  -0.0608 0.1538  8   PHE C CD2 
8173  C CE1 . PHE C 8   ? 0.7955 0.7129 0.7344 0.0473  -0.0704 0.1446  8   PHE C CE1 
8174  C CE2 . PHE C 8   ? 0.8680 0.8142 0.8009 0.0275  -0.0697 0.1684  8   PHE C CE2 
8175  C CZ  . PHE C 8   ? 0.7920 0.7182 0.7332 0.0411  -0.0746 0.1631  8   PHE C CZ  
8176  N N   . TRP C 9   ? 0.7096 0.6333 0.6317 0.0306  -0.0471 0.0869  9   TRP C N   
8177  C CA  . TRP C 9   ? 0.7257 0.6498 0.6451 0.0296  -0.0441 0.0736  9   TRP C CA  
8178  C C   . TRP C 9   ? 0.7531 0.6778 0.6644 0.0347  -0.0450 0.0698  9   TRP C C   
8179  O O   . TRP C 9   ? 0.7390 0.6487 0.6494 0.0412  -0.0484 0.0673  9   TRP C O   
8180  C CB  . TRP C 9   ? 0.7255 0.6311 0.6533 0.0304  -0.0472 0.0677  9   TRP C CB  
8181  C CG  . TRP C 9   ? 0.7376 0.6446 0.6680 0.0278  -0.0449 0.0566  9   TRP C CG  
8182  C CD1 . TRP C 9   ? 0.7203 0.6397 0.6456 0.0252  -0.0404 0.0499  9   TRP C CD1 
8183  C CD2 . TRP C 9   ? 0.7424 0.6366 0.6829 0.0275  -0.0484 0.0514  9   TRP C CD2 
8184  N NE1 . TRP C 9   ? 0.6302 0.5436 0.5629 0.0242  -0.0408 0.0407  9   TRP C NE1 
8185  C CE2 . TRP C 9   ? 0.7245 0.6236 0.6670 0.0258  -0.0458 0.0421  9   TRP C CE2 
8186  C CE3 . TRP C 9   ? 0.7211 0.5997 0.6701 0.0283  -0.0547 0.0538  9   TRP C CE3 
8187  C CZ2 . TRP C 9   ? 0.7527 0.6425 0.7071 0.0258  -0.0495 0.0363  9   TRP C CZ2 
8188  C CZ3 . TRP C 9   ? 0.7050 0.5761 0.6644 0.0272  -0.0584 0.0480  9   TRP C CZ3 
8189  C CH2 . TRP C 9   ? 0.7439 0.6210 0.7066 0.0264  -0.0558 0.0399  9   TRP C CH2 
8190  N N   . TRP C 10  ? 0.7330 0.6763 0.6378 0.0312  -0.0417 0.0691  10  TRP C N   
8191  C CA  . TRP C 10  ? 0.6780 0.6263 0.5771 0.0341  -0.0422 0.0667  10  TRP C CA  
8192  C C   . TRP C 10  ? 0.6684 0.6110 0.5651 0.0314  -0.0412 0.0557  10  TRP C C   
8193  O O   . TRP C 10  ? 0.6593 0.6063 0.5565 0.0253  -0.0388 0.0494  10  TRP C O   
8194  C CB  . TRP C 10  ? 0.7328 0.7040 0.6271 0.0301  -0.0411 0.0720  10  TRP C CB  
8195  C CG  . TRP C 10  ? 0.7529 0.7313 0.6495 0.0314  -0.0435 0.0852  10  TRP C CG  
8196  C CD1 . TRP C 10  ? 0.6104 0.6008 0.5043 0.0243  -0.0423 0.0916  10  TRP C CD1 
8197  C CD2 . TRP C 10  ? 0.8262 0.8006 0.7286 0.0404  -0.0479 0.0943  10  TRP C CD2 
8198  N NE1 . TRP C 10  ? 0.6813 0.6743 0.5788 0.0272  -0.0469 0.1064  10  TRP C NE1 
8199  C CE2 . TRP C 10  ? 0.8084 0.7907 0.7127 0.0379  -0.0508 0.1077  10  TRP C CE2 
8200  C CE3 . TRP C 10  ? 0.7307 0.6963 0.6374 0.0504  -0.0494 0.0921  10  TRP C CE3 
8201  C CZ2 . TRP C 10  ? 0.8191 0.7980 0.7318 0.0458  -0.0565 0.1195  10  TRP C CZ2 
8202  C CZ3 . TRP C 10  ? 0.6742 0.6377 0.5891 0.0592  -0.0535 0.1013  10  TRP C CZ3 
8203  C CH2 . TRP C 10  ? 0.7955 0.7644 0.7147 0.0573  -0.0577 0.1151  10  TRP C CH2 
8204  N N   . HIS C 11  ? 0.6684 0.6015 0.5627 0.0359  -0.0432 0.0534  11  HIS C N   
8205  C CA  . HIS C 11  ? 0.6227 0.5476 0.5145 0.0329  -0.0440 0.0458  11  HIS C CA  
8206  C C   . HIS C 11  ? 0.6149 0.5531 0.5014 0.0296  -0.0428 0.0453  11  HIS C C   
8207  O O   . HIS C 11  ? 0.5842 0.5304 0.4684 0.0338  -0.0421 0.0497  11  HIS C O   
8208  C CB  . HIS C 11  ? 0.6461 0.5519 0.5360 0.0378  -0.0475 0.0443  11  HIS C CB  
8209  C CG  . HIS C 11  ? 0.6044 0.5051 0.4884 0.0349  -0.0492 0.0405  11  HIS C CG  
8210  N ND1 . HIS C 11  ? 0.5947 0.4904 0.4818 0.0287  -0.0512 0.0361  11  HIS C ND1 
8211  C CD2 . HIS C 11  ? 0.6437 0.5446 0.5192 0.0368  -0.0489 0.0411  11  HIS C CD2 
8212  C CE1 . HIS C 11  ? 0.6642 0.5554 0.5447 0.0262  -0.0536 0.0359  11  HIS C CE1 
8213  N NE2 . HIS C 11  ? 0.7039 0.5996 0.5762 0.0304  -0.0515 0.0390  11  HIS C NE2 
8214  N N   . MET C 12  ? 0.5759 0.5167 0.4623 0.0221  -0.0427 0.0397  12  MET C N   
8215  C CA  . MET C 12  ? 0.7442 0.6976 0.6270 0.0165  -0.0427 0.0393  12  MET C CA  
8216  C C   . MET C 12  ? 0.6464 0.5871 0.5285 0.0120  -0.0456 0.0351  12  MET C C   
8217  O O   . MET C 12  ? 0.6648 0.5929 0.5514 0.0095  -0.0475 0.0289  12  MET C O   
8218  C CB  . MET C 12  ? 0.7069 0.6750 0.5891 0.0099  -0.0413 0.0364  12  MET C CB  
8219  C CG  . MET C 12  ? 0.7173 0.6948 0.5996 0.0123  -0.0392 0.0410  12  MET C CG  
8220  S SD  . MET C 12  ? 0.9916 0.9850 0.8737 0.0181  -0.0402 0.0537  12  MET C SD  
8221  C CE  . MET C 12  ? 0.9061 0.9206 0.7834 0.0113  -0.0400 0.0572  12  MET C CE  
8222  N N   . HIS C 13  ? 0.6240 0.5691 0.5017 0.0107  -0.0460 0.0391  13  HIS C N   
8223  C CA  . HIS C 13  ? 0.7009 0.6339 0.5765 0.0053  -0.0497 0.0383  13  HIS C CA  
8224  C C   . HIS C 13  ? 0.7548 0.7024 0.6264 0.0003  -0.0486 0.0437  13  HIS C C   
8225  O O   . HIS C 13  ? 0.7507 0.7140 0.6210 0.0053  -0.0444 0.0482  13  HIS C O   
8226  C CB  . HIS C 13  ? 0.6817 0.5963 0.5542 0.0103  -0.0521 0.0388  13  HIS C CB  
8227  C CG  . HIS C 13  ? 0.6594 0.5664 0.5255 0.0049  -0.0557 0.0421  13  HIS C CG  
8228  N ND1 . HIS C 13  ? 0.6535 0.5508 0.5232 -0.0036 -0.0612 0.0414  13  HIS C ND1 
8229  C CD2 . HIS C 13  ? 0.6755 0.5836 0.5312 0.0062  -0.0546 0.0465  13  HIS C CD2 
8230  C CE1 . HIS C 13  ? 0.6633 0.5561 0.5250 -0.0083 -0.0642 0.0474  13  HIS C CE1 
8231  N NE2 . HIS C 13  ? 0.7343 0.6348 0.5861 -0.0027 -0.0596 0.0501  13  HIS C NE2 
8232  N N   . GLN C 14  ? 0.6873 0.6299 0.5592 -0.0096 -0.0525 0.0436  14  GLN C N   
8233  C CA  . GLN C 14  ? 0.7576 0.7131 0.6269 -0.0171 -0.0522 0.0500  14  GLN C CA  
8234  C C   . GLN C 14  ? 0.7350 0.6721 0.6018 -0.0249 -0.0582 0.0523  14  GLN C C   
8235  O O   . GLN C 14  ? 0.7365 0.6551 0.6088 -0.0279 -0.0640 0.0472  14  GLN C O   
8236  C CB  . GLN C 14  ? 0.7514 0.7242 0.6259 -0.0254 -0.0529 0.0496  14  GLN C CB  
8237  C CG  . GLN C 14  ? 0.7029 0.7002 0.5798 -0.0200 -0.0483 0.0520  14  GLN C CG  
8238  C CD  . GLN C 14  ? 0.7190 0.7315 0.5951 -0.0133 -0.0428 0.0590  14  GLN C CD  
8239  O OE1 . GLN C 14  ? 0.7097 0.7255 0.5831 -0.0179 -0.0417 0.0635  14  GLN C OE1 
8240  N NE2 . GLN C 14  ? 0.8086 0.8317 0.6878 -0.0025 -0.0393 0.0600  14  GLN C NE2 
8241  N N   . PRO C 15  ? 0.6985 0.6411 0.5579 -0.0285 -0.0571 0.0602  15  PRO C N   
8242  C CA  . PRO C 15  ? 0.7118 0.6376 0.5676 -0.0379 -0.0641 0.0655  15  PRO C CA  
8243  C C   . PRO C 15  ? 0.6976 0.6221 0.5617 -0.0508 -0.0697 0.0666  15  PRO C C   
8244  O O   . PRO C 15  ? 0.7729 0.7118 0.6433 -0.0533 -0.0678 0.0630  15  PRO C O   
8245  C CB  . PRO C 15  ? 0.6986 0.6376 0.5420 -0.0393 -0.0592 0.0741  15  PRO C CB  
8246  C CG  . PRO C 15  ? 0.8112 0.7677 0.6532 -0.0266 -0.0498 0.0702  15  PRO C CG  
8247  C CD  . PRO C 15  ? 0.7523 0.7173 0.6064 -0.0240 -0.0490 0.0649  15  PRO C CD  
8248  N N   . LEU C 16  ? 0.8136 0.7194 0.6775 -0.0597 -0.0781 0.0720  16  LEU C N   
8249  C CA  . LEU C 16  ? 0.7622 0.6612 0.6351 -0.0728 -0.0854 0.0732  16  LEU C CA  
8250  C C   . LEU C 16  ? 0.7641 0.6853 0.6330 -0.0845 -0.0827 0.0847  16  LEU C C   
8251  O O   . LEU C 16  ? 0.7823 0.7022 0.6435 -0.0920 -0.0846 0.0966  16  LEU C O   
8252  C CB  . LEU C 16  ? 0.7851 0.6530 0.6627 -0.0772 -0.0970 0.0753  16  LEU C CB  
8253  C CG  . LEU C 16  ? 0.7665 0.6208 0.6566 -0.0889 -0.1059 0.0731  16  LEU C CG  
8254  C CD1 . LEU C 16  ? 0.8114 0.6738 0.7089 -0.0854 -0.1019 0.0581  16  LEU C CD1 
8255  C CD2 . LEU C 16  ? 0.7244 0.5453 0.6242 -0.0900 -0.1181 0.0733  16  LEU C CD2 
8256  N N   . TYR C 17  ? 0.8187 0.7632 0.6928 -0.0865 -0.0780 0.0820  17  TYR C N   
8257  C CA  . TYR C 17  ? 0.7726 0.7439 0.6472 -0.0974 -0.0747 0.0926  17  TYR C CA  
8258  C C   . TYR C 17  ? 0.8133 0.7760 0.6953 -0.1160 -0.0844 0.0984  17  TYR C C   
8259  O O   . TYR C 17  ? 0.7894 0.7750 0.6740 -0.1276 -0.0826 0.1086  17  TYR C O   
8260  C CB  . TYR C 17  ? 0.6817 0.6828 0.5617 -0.0919 -0.0675 0.0884  17  TYR C CB  
8261  C CG  . TYR C 17  ? 0.7107 0.7237 0.5856 -0.0747 -0.0579 0.0854  17  TYR C CG  
8262  C CD1 . TYR C 17  ? 0.7580 0.7826 0.6248 -0.0702 -0.0504 0.0920  17  TYR C CD1 
8263  C CD2 . TYR C 17  ? 0.7250 0.7385 0.6028 -0.0636 -0.0563 0.0759  17  TYR C CD2 
8264  C CE1 . TYR C 17  ? 0.7969 0.8297 0.6602 -0.0542 -0.0423 0.0877  17  TYR C CE1 
8265  C CE2 . TYR C 17  ? 0.7386 0.7607 0.6135 -0.0486 -0.0489 0.0742  17  TYR C CE2 
8266  C CZ  . TYR C 17  ? 0.7759 0.8062 0.6444 -0.0435 -0.0423 0.0794  17  TYR C CZ  
8267  O OH  . TYR C 17  ? 0.7784 0.8143 0.6450 -0.0281 -0.0357 0.0762  17  TYR C OH  
8268  N N   . ARG C 18  ? 0.8235 0.7543 0.7110 -0.1192 -0.0948 0.0922  18  ARG C N   
8269  C CA  . ARG C 18  ? 0.8053 0.7226 0.7020 -0.1363 -0.1058 0.0955  18  ARG C CA  
8270  C C   . ARG C 18  ? 0.8979 0.7989 0.7910 -0.1465 -0.1128 0.1113  18  ARG C C   
8271  O O   . ARG C 18  ? 0.8500 0.7245 0.7414 -0.1406 -0.1183 0.1108  18  ARG C O   
8272  C CB  . ARG C 18  ? 0.7865 0.6771 0.6924 -0.1332 -0.1132 0.0788  18  ARG C CB  
8273  C CG  . ARG C 18  ? 0.8993 0.7702 0.8162 -0.1496 -0.1258 0.0783  18  ARG C CG  
8274  C CD  . ARG C 18  ? 0.9156 0.7506 0.8416 -0.1430 -0.1335 0.0630  18  ARG C CD  
8275  N NE  . ARG C 18  ? 0.9036 0.7149 0.8417 -0.1570 -0.1464 0.0596  18  ARG C NE  
8276  C CZ  . ARG C 18  ? 0.9550 0.7430 0.8998 -0.1684 -0.1580 0.0727  18  ARG C CZ  
8277  N NH1 . ARG C 18  ? 0.9953 0.7832 0.9336 -0.1690 -0.1583 0.0910  18  ARG C NH1 
8278  N NH2 . ARG C 18  ? 0.9602 0.7236 0.9179 -0.1801 -0.1704 0.0672  18  ARG C NH2 
8279  N N   . GLU C 19  ? 0.9190 0.8375 0.8118 -0.1627 -0.1131 0.1265  19  GLU C N   
8280  C CA  . GLU C 19  ? 0.9261 0.8315 0.8142 -0.1756 -0.1203 0.1443  19  GLU C CA  
8281  C C   . GLU C 19  ? 0.9618 0.8249 0.8613 -0.1818 -0.1369 0.1423  19  GLU C C   
8282  O O   . GLU C 19  ? 1.0079 0.8599 0.9206 -0.1857 -0.1431 0.1311  19  GLU C O   
8283  C CB  . GLU C 19  ? 0.9243 0.8587 0.8132 -0.1943 -0.1176 0.1608  19  GLU C CB  
8284  C CG  . GLU C 19  ? 0.8665 0.8064 0.7419 -0.2044 -0.1166 0.1816  19  GLU C CG  
8285  C CD  . GLU C 19  ? 1.0134 0.9231 0.8944 -0.2233 -0.1334 0.1959  19  GLU C CD  
8286  O OE1 . GLU C 19  ? 1.0857 0.9700 0.9828 -0.2276 -0.1452 0.1879  19  GLU C OE1 
8287  O OE2 . GLU C 19  ? 1.0328 0.9430 0.9019 -0.2337 -0.1353 0.2149  19  GLU C OE2 
8288  N N   . PRO C 20  ? 0.9553 0.7934 0.8504 -0.1824 -0.1452 0.1520  20  PRO C N   
8289  C CA  . PRO C 20  ? 0.9298 0.7259 0.8397 -0.1855 -0.1618 0.1494  20  PRO C CA  
8290  C C   . PRO C 20  ? 0.9916 0.7751 0.9132 -0.2073 -0.1743 0.1602  20  PRO C C   
8291  O O   . PRO C 20  ? 1.0455 0.8029 0.9838 -0.2087 -0.1842 0.1481  20  PRO C O   
8292  C CB  . PRO C 20  ? 1.0238 0.8028 0.9248 -0.1811 -0.1674 0.1608  20  PRO C CB  
8293  C CG  . PRO C 20  ? 0.9841 0.7953 0.8635 -0.1859 -0.1566 0.1759  20  PRO C CG  
8294  C CD  . PRO C 20  ? 0.8975 0.7440 0.7742 -0.1783 -0.1401 0.1638  20  PRO C CD  
8295  N N   . TYR C 21  ? 1.0519 0.8533 0.9652 -0.2248 -0.1739 0.1824  21  TYR C N   
8296  C CA  . TYR C 21  ? 1.0231 0.8116 0.9482 -0.2480 -0.1870 0.1960  21  TYR C CA  
8297  C C   . TYR C 21  ? 0.9848 0.7911 0.9205 -0.2558 -0.1841 0.1856  21  TYR C C   
8298  O O   . TYR C 21  ? 1.0065 0.7862 0.9582 -0.2611 -0.1958 0.1749  21  TYR C O   
8299  C CB  . TYR C 21  ? 0.9939 0.7992 0.9057 -0.2656 -0.1866 0.2248  21  TYR C CB  
8300  C CG  . TYR C 21  ? 1.0813 0.8648 0.9820 -0.2627 -0.1941 0.2381  21  TYR C CG  
8301  C CD1 . TYR C 21  ? 1.1532 0.8904 1.0678 -0.2637 -0.2134 0.2402  21  TYR C CD1 
8302  C CD2 . TYR C 21  ? 1.1180 0.9271 0.9949 -0.2587 -0.1825 0.2478  21  TYR C CD2 
8303  C CE1 . TYR C 21  ? 1.0619 0.7802 0.9676 -0.2615 -0.2222 0.2539  21  TYR C CE1 
8304  C CE2 . TYR C 21  ? 1.0612 0.8512 0.9258 -0.2572 -0.1908 0.2601  21  TYR C CE2 
8305  C CZ  . TYR C 21  ? 1.0541 0.7994 0.9334 -0.2589 -0.2111 0.2641  21  TYR C CZ  
8306  O OH  . TYR C 21  ? 1.0541 0.7820 0.9221 -0.2579 -0.2208 0.2779  21  TYR C OH  
8307  N N   . THR C 22  ? 1.0251 0.8767 0.9527 -0.2564 -0.1690 0.1880  22  THR C N   
8308  C CA  . THR C 22  ? 1.0123 0.8854 0.9504 -0.2653 -0.1673 0.1809  22  THR C CA  
8309  C C   . THR C 22  ? 0.9612 0.8230 0.9052 -0.2501 -0.1672 0.1534  22  THR C C   
8310  O O   . THR C 22  ? 0.9213 0.7752 0.8768 -0.2596 -0.1753 0.1438  22  THR C O   
8311  C CB  . THR C 22  ? 0.9463 0.8729 0.8774 -0.2667 -0.1510 0.1899  22  THR C CB  
8312  O OG1 . THR C 22  ? 0.9778 0.9228 0.9015 -0.2438 -0.1374 0.1737  22  THR C OG1 
8313  C CG2 . THR C 22  ? 0.9015 0.8426 0.8201 -0.2750 -0.1459 0.2134  22  THR C CG2 
8314  N N   . GLY C 23  ? 0.9801 0.8408 0.9156 -0.2277 -0.1584 0.1404  23  GLY C N   
8315  C CA  . GLY C 23  ? 0.9950 0.8516 0.9334 -0.2135 -0.1557 0.1161  23  GLY C CA  
8316  C C   . GLY C 23  ? 0.9681 0.8661 0.9012 -0.2067 -0.1425 0.1104  23  GLY C C   
8317  O O   . GLY C 23  ? 0.9825 0.8808 0.9147 -0.1940 -0.1389 0.0920  23  GLY C O   
8318  N N   . GLU C 24  ? 0.9471 0.8811 0.8776 -0.2144 -0.1352 0.1261  24  GLU C N   
8319  C CA  . GLU C 24  ? 0.9258 0.9001 0.8552 -0.2074 -0.1239 0.1223  24  GLU C CA  
8320  C C   . GLU C 24  ? 0.9413 0.9235 0.8597 -0.1844 -0.1115 0.1160  24  GLU C C   
8321  O O   . GLU C 24  ? 0.9185 0.8852 0.8284 -0.1768 -0.1095 0.1201  24  GLU C O   
8322  C CB  . GLU C 24  ? 0.9082 0.9207 0.8421 -0.2217 -0.1191 0.1409  24  GLU C CB  
8323  C CG  . GLU C 24  ? 1.0791 1.0835 1.0243 -0.2473 -0.1319 0.1517  24  GLU C CG  
8324  C CD  . GLU C 24  ? 1.1938 1.2349 1.1430 -0.2625 -0.1262 0.1739  24  GLU C CD  
8325  O OE1 . GLU C 24  ? 1.1437 1.2053 1.0831 -0.2537 -0.1133 0.1825  24  GLU C OE1 
8326  O OE2 . GLU C 24  ? 1.2094 1.2591 1.1714 -0.2838 -0.1343 0.1822  24  GLU C OE2 
8327  N N   . TYR C 25  ? 0.9401 0.9459 0.8590 -0.1742 -0.1046 0.1066  25  TYR C N   
8328  C CA  . TYR C 25  ? 0.8395 0.8584 0.7504 -0.1538 -0.0928 0.1026  25  TYR C CA  
8329  C C   . TYR C 25  ? 0.8915 0.9509 0.8039 -0.1539 -0.0824 0.1153  25  TYR C C   
8330  O O   . TYR C 25  ? 0.7691 0.8592 0.6907 -0.1567 -0.0803 0.1164  25  TYR C O   
8331  C CB  . TYR C 25  ? 0.8170 0.8381 0.7284 -0.1433 -0.0920 0.0869  25  TYR C CB  
8332  C CG  . TYR C 25  ? 0.8370 0.8225 0.7449 -0.1360 -0.0966 0.0723  25  TYR C CG  
8333  C CD1 . TYR C 25  ? 0.9184 0.8770 0.8315 -0.1469 -0.1076 0.0649  25  TYR C CD1 
8334  C CD2 . TYR C 25  ? 0.8784 0.8578 0.7797 -0.1181 -0.0900 0.0654  25  TYR C CD2 
8335  C CE1 . TYR C 25  ? 0.9377 0.8662 0.8506 -0.1388 -0.1107 0.0502  25  TYR C CE1 
8336  C CE2 . TYR C 25  ? 0.8394 0.7905 0.7403 -0.1114 -0.0932 0.0523  25  TYR C CE2 
8337  C CZ  . TYR C 25  ? 0.9533 0.8801 0.8604 -0.1211 -0.1029 0.0443  25  TYR C CZ  
8338  O OH  . TYR C 25  ? 1.0678 0.9688 0.9772 -0.1130 -0.1049 0.0300  25  TYR C OH  
8339  N N   . LEU C 26  ? 0.8256 0.8862 0.7293 -0.1506 -0.0759 0.1246  26  LEU C N   
8340  C CA  . LEU C 26  ? 0.8050 0.9042 0.7100 -0.1510 -0.0646 0.1357  26  LEU C CA  
8341  C C   . LEU C 26  ? 0.7598 0.8835 0.6663 -0.1316 -0.0535 0.1289  26  LEU C C   
8342  O O   . LEU C 26  ? 0.7770 0.9365 0.6891 -0.1299 -0.0436 0.1359  26  LEU C O   
8343  C CB  . LEU C 26  ? 0.7467 0.8393 0.6383 -0.1540 -0.0608 0.1464  26  LEU C CB  
8344  C CG  . LEU C 26  ? 0.7363 0.7949 0.6240 -0.1695 -0.0736 0.1536  26  LEU C CG  
8345  C CD1 . LEU C 26  ? 0.7489 0.8050 0.6203 -0.1719 -0.0697 0.1655  26  LEU C CD1 
8346  C CD2 . LEU C 26  ? 0.7430 0.8090 0.6449 -0.1916 -0.0821 0.1624  26  LEU C CD2 
8347  N N   . LEU C 27  ? 0.7242 0.8303 0.6272 -0.1170 -0.0548 0.1161  27  LEU C N   
8348  C CA  . LEU C 27  ? 0.6722 0.7986 0.5785 -0.0996 -0.0466 0.1109  27  LEU C CA  
8349  C C   . LEU C 27  ? 0.7278 0.8460 0.6379 -0.0961 -0.0531 0.1008  27  LEU C C   
8350  O O   . LEU C 27  ? 0.8432 0.9311 0.7481 -0.0996 -0.0608 0.0931  27  LEU C O   
8351  C CB  . LEU C 27  ? 0.6723 0.7860 0.5660 -0.0830 -0.0391 0.1070  27  LEU C CB  
8352  C CG  . LEU C 27  ? 0.7571 0.8907 0.6459 -0.0819 -0.0287 0.1148  27  LEU C CG  
8353  C CD1 . LEU C 27  ? 0.7824 0.9024 0.6584 -0.0645 -0.0225 0.1078  27  LEU C CD1 
8354  C CD2 . LEU C 27  ? 0.6869 0.8652 0.5914 -0.0818 -0.0206 0.1206  27  LEU C CD2 
8355  N N   . PRO C 28  ? 0.7601 0.9057 0.6796 -0.0894 -0.0504 0.1007  28  PRO C N   
8356  C CA  . PRO C 28  ? 0.7483 0.8902 0.6691 -0.0882 -0.0570 0.0926  28  PRO C CA  
8357  C C   . PRO C 28  ? 0.7391 0.8696 0.6534 -0.0705 -0.0536 0.0855  28  PRO C C   
8358  O O   . PRO C 28  ? 0.7356 0.8699 0.6504 -0.0690 -0.0576 0.0810  28  PRO C O   
8359  C CB  . PRO C 28  ? 0.7212 0.9028 0.6571 -0.0929 -0.0577 0.1000  28  PRO C CB  
8360  C CG  . PRO C 28  ? 0.7701 0.9757 0.7131 -0.0824 -0.0465 0.1079  28  PRO C CG  
8361  C CD  . PRO C 28  ? 0.7595 0.9442 0.6908 -0.0842 -0.0419 0.1090  28  PRO C CD  
8362  N N   . TRP C 29  ? 0.7597 0.8761 0.6670 -0.0586 -0.0471 0.0846  29  TRP C N   
8363  C CA  . TRP C 29  ? 0.7825 0.8918 0.6866 -0.0419 -0.0437 0.0800  29  TRP C CA  
8364  C C   . TRP C 29  ? 0.7465 0.8333 0.6441 -0.0424 -0.0492 0.0709  29  TRP C C   
8365  O O   . TRP C 29  ? 0.6683 0.7580 0.5659 -0.0335 -0.0486 0.0690  29  TRP C O   
8366  C CB  . TRP C 29  ? 0.7693 0.8652 0.6660 -0.0314 -0.0371 0.0797  29  TRP C CB  
8367  C CG  . TRP C 29  ? 0.7771 0.8978 0.6786 -0.0279 -0.0290 0.0863  29  TRP C CG  
8368  C CD1 . TRP C 29  ? 0.8750 0.9937 0.7691 -0.0315 -0.0245 0.0894  29  TRP C CD1 
8369  C CD2 . TRP C 29  ? 0.7980 0.9510 0.7135 -0.0197 -0.0240 0.0905  29  TRP C CD2 
8370  N NE1 . TRP C 29  ? 0.7964 0.9455 0.6979 -0.0261 -0.0153 0.0938  29  TRP C NE1 
8371  C CE2 . TRP C 29  ? 0.8700 1.0404 0.7868 -0.0180 -0.0149 0.0943  29  TRP C CE2 
8372  C CE3 . TRP C 29  ? 0.7846 0.9546 0.7121 -0.0137 -0.0266 0.0920  29  TRP C CE3 
8373  C CZ2 . TRP C 29  ? 0.8316 1.0361 0.7642 -0.0090 -0.0075 0.0979  29  TRP C CZ2 
8374  C CZ3 . TRP C 29  ? 0.7684 0.9706 0.7123 -0.0051 -0.0212 0.0974  29  TRP C CZ3 
8375  C CH2 . TRP C 29  ? 0.7633 0.9827 0.7109 -0.0021 -0.0113 0.0995  29  TRP C CH2 
8376  N N   . THR C 30  ? 0.7963 0.8612 0.6894 -0.0527 -0.0544 0.0655  30  THR C N   
8377  C CA  . THR C 30  ? 0.6966 0.7430 0.5854 -0.0532 -0.0583 0.0549  30  THR C CA  
8378  C C   . THR C 30  ? 0.7462 0.8113 0.6363 -0.0586 -0.0618 0.0526  30  THR C C   
8379  O O   . THR C 30  ? 0.8040 0.8682 0.6896 -0.0530 -0.0611 0.0476  30  THR C O   
8380  C CB  . THR C 30  ? 0.7854 0.8055 0.6728 -0.0626 -0.0638 0.0491  30  THR C CB  
8381  O OG1 . THR C 30  ? 0.7832 0.7889 0.6684 -0.0595 -0.0622 0.0541  30  THR C OG1 
8382  C CG2 . THR C 30  ? 0.7885 0.7892 0.6732 -0.0597 -0.0655 0.0361  30  THR C CG2 
8383  N N   . PHE C 31  ? 0.6993 0.7832 0.5951 -0.0705 -0.0660 0.0571  31  PHE C N   
8384  C CA  . PHE C 31  ? 0.6890 0.7920 0.5850 -0.0773 -0.0712 0.0554  31  PHE C CA  
8385  C C   . PHE C 31  ? 0.7205 0.8465 0.6192 -0.0658 -0.0681 0.0626  31  PHE C C   
8386  O O   . PHE C 31  ? 0.7002 0.8287 0.5921 -0.0642 -0.0701 0.0589  31  PHE C O   
8387  C CB  . PHE C 31  ? 0.6813 0.8008 0.5852 -0.0933 -0.0775 0.0601  31  PHE C CB  
8388  C CG  . PHE C 31  ? 0.7676 0.9158 0.6745 -0.0996 -0.0833 0.0626  31  PHE C CG  
8389  C CD1 . PHE C 31  ? 0.7590 0.9389 0.6763 -0.0923 -0.0811 0.0747  31  PHE C CD1 
8390  C CD2 . PHE C 31  ? 0.7728 0.9162 0.6727 -0.1131 -0.0918 0.0525  31  PHE C CD2 
8391  C CE1 . PHE C 31  ? 0.7696 0.9768 0.6910 -0.0986 -0.0884 0.0787  31  PHE C CE1 
8392  C CE2 . PHE C 31  ? 0.7136 0.8835 0.6140 -0.1205 -0.0988 0.0549  31  PHE C CE2 
8393  C CZ  . PHE C 31  ? 0.6948 0.8976 0.6065 -0.1135 -0.0977 0.0693  31  PHE C CZ  
8394  N N   . PHE C 32  ? 0.6924 0.8349 0.6010 -0.0575 -0.0632 0.0730  32  PHE C N   
8395  C CA  . PHE C 32  ? 0.6431 0.8085 0.5591 -0.0464 -0.0618 0.0811  32  PHE C CA  
8396  C C   . PHE C 32  ? 0.7074 0.8561 0.6159 -0.0335 -0.0588 0.0783  32  PHE C C   
8397  O O   . PHE C 32  ? 0.7421 0.9015 0.6500 -0.0304 -0.0620 0.0817  32  PHE C O   
8398  C CB  . PHE C 32  ? 0.7927 0.9780 0.7229 -0.0392 -0.0559 0.0902  32  PHE C CB  
8399  C CG  . PHE C 32  ? 0.7354 0.9492 0.6781 -0.0516 -0.0592 0.0968  32  PHE C CG  
8400  C CD1 . PHE C 32  ? 0.5966 0.8307 0.5439 -0.0611 -0.0682 0.0995  32  PHE C CD1 
8401  C CD2 . PHE C 32  ? 0.7335 0.9538 0.6821 -0.0555 -0.0538 0.1006  32  PHE C CD2 
8402  C CE1 . PHE C 32  ? 0.6743 0.9355 0.6349 -0.0739 -0.0723 0.1060  32  PHE C CE1 
8403  C CE2 . PHE C 32  ? 0.7718 1.0200 0.7337 -0.0685 -0.0567 0.1078  32  PHE C CE2 
8404  C CZ  . PHE C 32  ? 0.7465 1.0150 0.7156 -0.0777 -0.0663 0.1105  32  PHE C CZ  
8405  N N   . HIS C 33  ? 0.7185 0.8415 0.6214 -0.0267 -0.0536 0.0733  33  HIS C N   
8406  C CA  . HIS C 33  ? 0.6640 0.7710 0.5615 -0.0159 -0.0513 0.0711  33  HIS C CA  
8407  C C   . HIS C 33  ? 0.7782 0.8750 0.6653 -0.0227 -0.0544 0.0633  33  HIS C C   
8408  O O   . HIS C 33  ? 0.8131 0.9065 0.6966 -0.0167 -0.0535 0.0642  33  HIS C O   
8409  C CB  . HIS C 33  ? 0.7401 0.8237 0.6349 -0.0081 -0.0461 0.0678  33  HIS C CB  
8410  C CG  . HIS C 33  ? 0.7436 0.8350 0.6455 0.0043  -0.0412 0.0738  33  HIS C CG  
8411  N ND1 . HIS C 33  ? 0.7577 0.8574 0.6663 0.0158  -0.0409 0.0791  33  HIS C ND1 
8412  C CD2 . HIS C 33  ? 0.6918 0.7835 0.5950 0.0073  -0.0364 0.0745  33  HIS C CD2 
8413  C CE1 . HIS C 33  ? 0.7790 0.8827 0.6941 0.0265  -0.0358 0.0811  33  HIS C CE1 
8414  N NE2 . HIS C 33  ? 0.7447 0.8450 0.6553 0.0213  -0.0323 0.0779  33  HIS C NE2 
8415  N N   . ALA C 34  ? 0.7441 0.8364 0.6267 -0.0355 -0.0578 0.0553  34  ALA C N   
8416  C CA  . ALA C 34  ? 0.7673 0.8538 0.6398 -0.0420 -0.0599 0.0456  34  ALA C CA  
8417  C C   . ALA C 34  ? 0.8326 0.9444 0.7014 -0.0462 -0.0642 0.0506  34  ALA C C   
8418  O O   . ALA C 34  ? 0.8647 0.9773 0.7246 -0.0450 -0.0634 0.0488  34  ALA C O   
8419  C CB  . ALA C 34  ? 0.8151 0.8878 0.6852 -0.0538 -0.0631 0.0340  34  ALA C CB  
8420  N N   . VAL C 35  ? 0.7635 0.8979 0.6392 -0.0519 -0.0693 0.0581  35  VAL C N   
8421  C CA  . VAL C 35  ? 0.7279 0.8880 0.6007 -0.0569 -0.0757 0.0644  35  VAL C CA  
8422  C C   . VAL C 35  ? 0.7976 0.9682 0.6759 -0.0439 -0.0745 0.0776  35  VAL C C   
8423  O O   . VAL C 35  ? 0.8776 1.0631 0.7497 -0.0462 -0.0794 0.0834  35  VAL C O   
8424  C CB  . VAL C 35  ? 0.7831 0.9663 0.6651 -0.0674 -0.0828 0.0693  35  VAL C CB  
8425  C CG1 . VAL C 35  ? 0.7072 0.8758 0.5855 -0.0809 -0.0850 0.0571  35  VAL C CG1 
8426  C CG2 . VAL C 35  ? 0.7863 0.9845 0.6874 -0.0580 -0.0801 0.0822  35  VAL C CG2 
8427  N N   . LYS C 36  ? 0.7699 0.9318 0.6589 -0.0306 -0.0688 0.0825  36  LYS C N   
8428  C CA  . LYS C 36  ? 0.7508 0.9200 0.6480 -0.0175 -0.0687 0.0945  36  LYS C CA  
8429  C C   . LYS C 36  ? 0.8397 0.9874 0.7283 -0.0109 -0.0648 0.0925  36  LYS C C   
8430  O O   . LYS C 36  ? 0.8478 1.0022 0.7360 -0.0071 -0.0679 0.1020  36  LYS C O   
8431  C CB  . LYS C 36  ? 0.7191 0.8922 0.6332 -0.0060 -0.0646 0.0997  36  LYS C CB  
8432  C CG  . LYS C 36  ? 0.7485 0.9370 0.6776 0.0068  -0.0668 0.1127  36  LYS C CG  
8433  C CD  . LYS C 36  ? 0.7540 0.9506 0.7005 0.0175  -0.0613 0.1146  36  LYS C CD  
8434  C CE  . LYS C 36  ? 0.8476 1.0165 0.7880 0.0245  -0.0525 0.1054  36  LYS C CE  
8435  N NZ  . LYS C 36  ? 0.6557 0.8053 0.5972 0.0388  -0.0506 0.1065  36  LYS C NZ  
8436  N N   . ASP C 37  ? 0.8480 0.9706 0.7311 -0.0100 -0.0590 0.0817  37  ASP C N   
8437  C CA  . ASP C 37  ? 0.8354 0.9392 0.7156 -0.0024 -0.0552 0.0814  37  ASP C CA  
8438  C C   . ASP C 37  ? 0.8263 0.9133 0.6955 -0.0087 -0.0518 0.0689  37  ASP C C   
8439  O O   . ASP C 37  ? 0.8525 0.9338 0.7172 -0.0072 -0.0498 0.0699  37  ASP C O   
8440  C CB  . ASP C 37  ? 0.8294 0.9181 0.7191 0.0102  -0.0513 0.0827  37  ASP C CB  
8441  C CG  . ASP C 37  ? 0.8375 0.9432 0.7405 0.0177  -0.0525 0.0912  37  ASP C CG  
8442  O OD1 . ASP C 37  ? 0.8234 0.9373 0.7346 0.0259  -0.0552 0.1014  37  ASP C OD1 
8443  O OD2 . ASP C 37  ? 0.7730 0.8840 0.6798 0.0155  -0.0505 0.0880  37  ASP C OD2 
8444  N N   . TYR C 38  ? 0.7761 0.8553 0.6428 -0.0158 -0.0511 0.0576  38  TYR C N   
8445  C CA  . TYR C 38  ? 0.7729 0.8337 0.6343 -0.0187 -0.0475 0.0448  38  TYR C CA  
8446  C C   . TYR C 38  ? 0.7426 0.8131 0.5927 -0.0260 -0.0467 0.0396  38  TYR C C   
8447  O O   . TYR C 38  ? 0.7214 0.7823 0.5691 -0.0246 -0.0418 0.0335  38  TYR C O   
8448  C CB  . TYR C 38  ? 0.7818 0.8304 0.6451 -0.0244 -0.0486 0.0349  38  TYR C CB  
8449  C CG  . TYR C 38  ? 0.7394 0.7751 0.6105 -0.0178 -0.0478 0.0389  38  TYR C CG  
8450  C CD1 . TYR C 38  ? 0.6399 0.6674 0.5144 -0.0067 -0.0450 0.0447  38  TYR C CD1 
8451  C CD2 . TYR C 38  ? 0.7247 0.7564 0.5985 -0.0236 -0.0502 0.0371  38  TYR C CD2 
8452  C CE1 . TYR C 38  ? 0.7568 0.7734 0.6350 -0.0013 -0.0442 0.0469  38  TYR C CE1 
8453  C CE2 . TYR C 38  ? 0.7142 0.7366 0.5919 -0.0188 -0.0491 0.0415  38  TYR C CE2 
8454  C CZ  . TYR C 38  ? 0.8312 0.8464 0.7100 -0.0074 -0.0458 0.0455  38  TYR C CZ  
8455  O OH  . TYR C 38  ? 0.8277 0.8340 0.7070 -0.0031 -0.0445 0.0484  38  TYR C OH  
8456  N N   . TYR C 39  ? 0.7615 0.8529 0.6043 -0.0343 -0.0514 0.0421  39  TYR C N   
8457  C CA  . TYR C 39  ? 0.6787 0.7817 0.5070 -0.0417 -0.0504 0.0379  39  TYR C CA  
8458  C C   . TYR C 39  ? 0.6774 0.7932 0.5033 -0.0377 -0.0511 0.0539  39  TYR C C   
8459  O O   . TYR C 39  ? 0.6855 0.8033 0.5024 -0.0398 -0.0467 0.0527  39  TYR C O   
8460  C CB  . TYR C 39  ? 0.7292 0.8482 0.5476 -0.0543 -0.0564 0.0322  39  TYR C CB  
8461  C CG  . TYR C 39  ? 0.7307 0.8661 0.5300 -0.0633 -0.0563 0.0286  39  TYR C CG  
8462  C CD1 . TYR C 39  ? 0.7400 0.8982 0.5327 -0.0656 -0.0619 0.0447  39  TYR C CD1 
8463  C CD2 . TYR C 39  ? 0.8136 0.9426 0.6012 -0.0697 -0.0511 0.0090  39  TYR C CD2 
8464  C CE1 . TYR C 39  ? 0.7993 0.9741 0.5714 -0.0754 -0.0623 0.0428  39  TYR C CE1 
8465  C CE2 . TYR C 39  ? 0.7986 0.9450 0.5657 -0.0787 -0.0499 0.0044  39  TYR C CE2 
8466  C CZ  . TYR C 39  ? 0.8297 0.9994 0.5875 -0.0823 -0.0556 0.0220  39  TYR C CZ  
8467  O OH  . TYR C 39  ? 0.8439 1.0325 0.5782 -0.0926 -0.0549 0.0191  39  TYR C OH  
8468  N N   . ASP C 40  ? 0.7449 0.8699 0.5803 -0.0320 -0.0566 0.0694  40  ASP C N   
8469  C CA  . ASP C 40  ? 0.7990 0.9377 0.6328 -0.0299 -0.0604 0.0863  40  ASP C CA  
8470  C C   . ASP C 40  ? 0.7786 0.9011 0.6187 -0.0206 -0.0559 0.0924  40  ASP C C   
8471  O O   . ASP C 40  ? 0.7392 0.8684 0.5729 -0.0228 -0.0565 0.1022  40  ASP C O   
8472  C CB  . ASP C 40  ? 0.8475 1.0020 0.6934 -0.0257 -0.0685 0.1003  40  ASP C CB  
8473  C CG  . ASP C 40  ? 0.9189 1.0908 0.7615 -0.0359 -0.0740 0.0956  40  ASP C CG  
8474  O OD1 . ASP C 40  ? 0.9416 1.1038 0.7851 -0.0394 -0.0712 0.0821  40  ASP C OD1 
8475  O OD2 . ASP C 40  ? 0.9682 1.1633 0.8083 -0.0410 -0.0825 0.1065  40  ASP C OD2 
8476  N N   . MET C 41  ? 0.7537 0.8553 0.6055 -0.0114 -0.0522 0.0875  41  MET C N   
8477  C CA  . MET C 41  ? 0.8091 0.8938 0.6676 -0.0033 -0.0493 0.0925  41  MET C CA  
8478  C C   . MET C 41  ? 0.8329 0.9153 0.6825 -0.0095 -0.0437 0.0878  41  MET C C   
8479  O O   . MET C 41  ? 0.8113 0.8939 0.6617 -0.0086 -0.0442 0.0995  41  MET C O   
8480  C CB  . MET C 41  ? 0.6508 0.7141 0.5200 0.0058  -0.0468 0.0856  41  MET C CB  
8481  C CG  . MET C 41  ? 0.6694 0.7338 0.5499 0.0158  -0.0506 0.0944  41  MET C CG  
8482  S SD  . MET C 41  ? 0.9084 0.9714 0.7970 0.0240  -0.0551 0.1117  41  MET C SD  
8483  C CE  . MET C 41  ? 0.8016 0.8352 0.6930 0.0286  -0.0510 0.1064  41  MET C CE  
8484  N N   . PRO C 42  ? 0.8068 0.8875 0.6496 -0.0159 -0.0382 0.0714  42  PRO C N   
8485  C CA  . PRO C 42  ? 0.7593 0.8448 0.5940 -0.0221 -0.0316 0.0668  42  PRO C CA  
8486  C C   . PRO C 42  ? 0.7684 0.8789 0.5858 -0.0325 -0.0328 0.0724  42  PRO C C   
8487  O O   . PRO C 42  ? 0.7872 0.9062 0.5971 -0.0377 -0.0275 0.0746  42  PRO C O   
8488  C CB  . PRO C 42  ? 0.7242 0.7995 0.5601 -0.0237 -0.0260 0.0460  42  PRO C CB  
8489  C CG  . PRO C 42  ? 0.6944 0.7679 0.5306 -0.0244 -0.0314 0.0411  42  PRO C CG  
8490  C CD  . PRO C 42  ? 0.7705 0.8421 0.6153 -0.0168 -0.0373 0.0564  42  PRO C CD  
8491  N N   . ALA C 43  ? 0.7514 0.8758 0.5620 -0.0367 -0.0399 0.0756  43  ALA C N   
8492  C CA  . ALA C 43  ? 0.7984 0.9476 0.5905 -0.0478 -0.0429 0.0816  43  ALA C CA  
8493  C C   . ALA C 43  ? 0.9217 1.0795 0.7135 -0.0471 -0.0473 0.1048  43  ALA C C   
8494  O O   . ALA C 43  ? 0.8708 1.0485 0.6450 -0.0574 -0.0481 0.1116  43  ALA C O   
8495  C CB  . ALA C 43  ? 0.7484 0.9108 0.5358 -0.0528 -0.0515 0.0806  43  ALA C CB  
8496  N N   . TYR C 44  ? 0.9390 1.0819 0.7493 -0.0357 -0.0506 0.1172  44  TYR C N   
8497  C CA  . TYR C 44  ? 0.8905 1.0367 0.7034 -0.0348 -0.0555 0.1394  44  TYR C CA  
8498  C C   . TYR C 44  ? 0.8367 0.9868 0.6390 -0.0430 -0.0477 0.1405  44  TYR C C   
8499  O O   . TYR C 44  ? 0.8552 1.0172 0.6504 -0.0491 -0.0516 0.1591  44  TYR C O   
8500  C CB  . TYR C 44  ? 0.8702 0.9942 0.7055 -0.0204 -0.0589 0.1475  44  TYR C CB  
8501  C CG  . TYR C 44  ? 0.7806 0.9066 0.6288 -0.0115 -0.0677 0.1546  44  TYR C CG  
8502  C CD1 . TYR C 44  ? 0.8109 0.9347 0.6642 -0.0075 -0.0661 0.1409  44  TYR C CD1 
8503  C CD2 . TYR C 44  ? 0.7304 0.8603 0.5882 -0.0065 -0.0774 0.1756  44  TYR C CD2 
8504  C CE1 . TYR C 44  ? 0.8045 0.9336 0.6716 0.0008  -0.0725 0.1472  44  TYR C CE1 
8505  C CE2 . TYR C 44  ? 0.7027 0.8364 0.5761 0.0034  -0.0844 0.1811  44  TYR C CE2 
8506  C CZ  . TYR C 44  ? 0.7702 0.9050 0.6481 0.0070  -0.0811 0.1665  44  TYR C CZ  
8507  O OH  . TYR C 44  ? 0.8349 0.9774 0.7300 0.0167  -0.0866 0.1717  44  TYR C OH  
8508  N N   . LEU C 45  ? 0.8026 0.9443 0.6051 -0.0435 -0.0368 0.1216  45  LEU C N   
8509  C CA  . LEU C 45  ? 0.8451 0.9922 0.6420 -0.0502 -0.0273 0.1211  45  LEU C CA  
8510  C C   . LEU C 45  ? 0.9101 1.0860 0.6815 -0.0646 -0.0244 0.1224  45  LEU C C   
8511  O O   . LEU C 45  ? 0.9201 1.1076 0.6845 -0.0722 -0.0188 0.1311  45  LEU C O   
8512  C CB  . LEU C 45  ? 0.7750 0.9088 0.5809 -0.0462 -0.0170 0.0990  45  LEU C CB  
8513  C CG  . LEU C 45  ? 0.7986 0.9070 0.6272 -0.0357 -0.0177 0.1018  45  LEU C CG  
8514  C CD1 . LEU C 45  ? 0.7299 0.8262 0.5681 -0.0319 -0.0098 0.0807  45  LEU C CD1 
8515  C CD2 . LEU C 45  ? 0.7785 0.8880 0.6119 -0.0386 -0.0178 0.1203  45  LEU C CD2 
8516  N N   . LYS C 46  ? 0.8544 1.0433 0.6110 -0.0697 -0.0281 0.1141  46  LYS C N   
8517  C CA  . LYS C 46  ? 0.8862 1.1030 0.6152 -0.0843 -0.0271 0.1155  46  LYS C CA  
8518  C C   . LYS C 46  ? 0.8990 1.1301 0.6205 -0.0898 -0.0386 0.1448  46  LYS C C   
8519  O O   . LYS C 46  ? 0.8468 1.1011 0.5452 -0.1030 -0.0368 0.1520  46  LYS C O   
8520  C CB  . LYS C 46  ? 1.0306 1.2551 0.7460 -0.0891 -0.0293 0.0966  46  LYS C CB  
8521  C CG  . LYS C 46  ? 1.1708 1.4056 0.8679 -0.0974 -0.0164 0.0718  46  LYS C CG  
8522  C CD  . LYS C 46  ? 1.1680 1.3871 0.8726 -0.0928 -0.0145 0.0456  46  LYS C CD  
8523  C CE  . LYS C 46  ? 1.2140 1.4411 0.9069 -0.0992 -0.0261 0.0427  46  LYS C CE  
8524  N NZ  . LYS C 46  ? 1.0804 1.2894 0.7828 -0.0956 -0.0255 0.0196  46  LYS C NZ  
8525  N N   . ASP C 47  ? 0.9804 1.1987 0.7214 -0.0798 -0.0504 0.1617  47  ASP C N   
8526  C CA  . ASP C 47  ? 0.9667 1.1964 0.7055 -0.0828 -0.0641 0.1899  47  ASP C CA  
8527  C C   . ASP C 47  ? 0.9773 1.1924 0.7328 -0.0775 -0.0669 0.2116  47  ASP C C   
8528  O O   . ASP C 47  ? 1.0463 1.2688 0.8017 -0.0802 -0.0787 0.2373  47  ASP C O   
8529  C CB  . ASP C 47  ? 1.0014 1.2308 0.7522 -0.0752 -0.0771 0.1940  47  ASP C CB  
8530  C CG  . ASP C 47  ? 1.0333 1.2730 0.7721 -0.0803 -0.0757 0.1721  47  ASP C CG  
8531  O OD1 . ASP C 47  ? 1.0433 1.2729 0.7805 -0.0796 -0.0642 0.1480  47  ASP C OD1 
8532  O OD2 . ASP C 47  ? 1.2427 1.5004 0.9752 -0.0853 -0.0872 0.1796  47  ASP C OD2 
8533  N N   . PHE C 48  ? 0.9585 1.1524 0.7293 -0.0703 -0.0578 0.2027  48  PHE C N   
8534  C CA  . PHE C 48  ? 0.9649 1.1429 0.7517 -0.0668 -0.0602 0.2211  48  PHE C CA  
8535  C C   . PHE C 48  ? 0.9816 1.1573 0.7676 -0.0718 -0.0458 0.2103  48  PHE C C   
8536  O O   . PHE C 48  ? 0.9308 1.1063 0.7146 -0.0706 -0.0348 0.1857  48  PHE C O   
8537  C CB  . PHE C 48  ? 0.8994 1.0487 0.7139 -0.0493 -0.0676 0.2227  48  PHE C CB  
8538  C CG  . PHE C 48  ? 0.8532 1.0066 0.6740 -0.0423 -0.0807 0.2323  48  PHE C CG  
8539  C CD1 . PHE C 48  ? 0.8784 1.0406 0.6955 -0.0399 -0.0804 0.2165  48  PHE C CD1 
8540  C CD2 . PHE C 48  ? 0.8716 1.0205 0.7044 -0.0384 -0.0938 0.2578  48  PHE C CD2 
8541  C CE1 . PHE C 48  ? 0.8198 0.9896 0.6457 -0.0338 -0.0921 0.2259  48  PHE C CE1 
8542  C CE2 . PHE C 48  ? 0.8015 0.9568 0.6441 -0.0308 -0.1059 0.2667  48  PHE C CE2 
8543  C CZ  . PHE C 48  ? 0.7444 0.9116 0.5837 -0.0286 -0.1046 0.2507  48  PHE C CZ  
8544  N N   . GLU C 49  ? 0.9611 1.1356 0.7512 -0.0775 -0.0464 0.2298  49  GLU C N   
8545  C CA  . GLU C 49  ? 0.9259 1.1043 0.7168 -0.0843 -0.0326 0.2229  49  GLU C CA  
8546  C C   . GLU C 49  ? 0.8394 0.9873 0.6582 -0.0740 -0.0338 0.2232  49  GLU C C   
8547  O O   . GLU C 49  ? 0.7985 0.9391 0.6273 -0.0780 -0.0373 0.2422  49  GLU C O   
8548  C CB  . GLU C 49  ? 0.8905 1.0936 0.6642 -0.1014 -0.0308 0.2441  49  GLU C CB  
8549  C CG  . GLU C 49  ? 0.9617 1.1980 0.7029 -0.1140 -0.0264 0.2389  49  GLU C CG  
8550  C CD  . GLU C 49  ? 0.9465 1.1968 0.6777 -0.1168 -0.0081 0.2086  49  GLU C CD  
8551  O OE1 . GLU C 49  ? 0.9900 1.2598 0.6974 -0.1227 -0.0049 0.1947  49  GLU C OE1 
8552  O OE2 . GLU C 49  ? 1.1915 1.4327 0.9402 -0.1129 0.0023  0.1981  49  GLU C OE2 
8553  N N   . ILE C 50  ? 0.8447 0.9742 0.6754 -0.0614 -0.0319 0.2020  50  ILE C N   
8554  C CA  . ILE C 50  ? 0.7290 0.8301 0.5831 -0.0516 -0.0326 0.1970  50  ILE C CA  
8555  C C   . ILE C 50  ? 0.7240 0.8226 0.5812 -0.0473 -0.0220 0.1697  50  ILE C C   
8556  O O   . ILE C 50  ? 0.6916 0.8089 0.5345 -0.0517 -0.0140 0.1550  50  ILE C O   
8557  C CB  . ILE C 50  ? 0.7118 0.7871 0.5798 -0.0379 -0.0457 0.2032  50  ILE C CB  
8558  C CG1 . ILE C 50  ? 0.7950 0.8779 0.6540 -0.0323 -0.0493 0.1955  50  ILE C CG1 
8559  C CG2 . ILE C 50  ? 0.7207 0.7885 0.5956 -0.0399 -0.0570 0.2303  50  ILE C CG2 
8560  C CD1 . ILE C 50  ? 0.6868 0.7462 0.5608 -0.0168 -0.0548 0.1875  50  ILE C CD1 
8561  N N   . LYS C 51  ? 0.7815 0.8558 0.6578 -0.0387 -0.0230 0.1628  51  LYS C N   
8562  C CA  . LYS C 51  ? 0.6608 0.7286 0.5436 -0.0334 -0.0159 0.1393  51  LYS C CA  
8563  C C   . LYS C 51  ? 0.6759 0.7201 0.5650 -0.0206 -0.0236 0.1318  51  LYS C C   
8564  O O   . LYS C 51  ? 0.7173 0.7423 0.6155 -0.0141 -0.0325 0.1421  51  LYS C O   
8565  C CB  . LYS C 51  ? 0.6585 0.7211 0.5580 -0.0356 -0.0106 0.1374  51  LYS C CB  
8566  C CG  . LYS C 51  ? 0.7821 0.8714 0.6769 -0.0489 -0.0014 0.1458  51  LYS C CG  
8567  C CD  . LYS C 51  ? 0.7363 0.8527 0.6144 -0.0543 0.0104  0.1304  51  LYS C CD  
8568  C CE  . LYS C 51  ? 0.7071 0.8472 0.5892 -0.0637 0.0242  0.1280  51  LYS C CE  
8569  N NZ  . LYS C 51  ? 0.8426 1.0152 0.7001 -0.0761 0.0320  0.1326  51  LYS C NZ  
8570  N N   . LEU C 52  ? 0.6367 0.6826 0.5208 -0.0175 -0.0200 0.1137  52  LEU C N   
8571  C CA  . LEU C 52  ? 0.6652 0.6917 0.5546 -0.0070 -0.0256 0.1058  52  LEU C CA  
8572  C C   . LEU C 52  ? 0.6510 0.6723 0.5444 -0.0054 -0.0199 0.0859  52  LEU C C   
8573  O O   . LEU C 52  ? 0.6995 0.7365 0.5858 -0.0110 -0.0128 0.0753  52  LEU C O   
8574  C CB  . LEU C 52  ? 0.7221 0.7571 0.6009 -0.0053 -0.0305 0.1087  52  LEU C CB  
8575  C CG  . LEU C 52  ? 0.6763 0.7162 0.5538 -0.0049 -0.0383 0.1290  52  LEU C CG  
8576  C CD1 . LEU C 52  ? 0.6382 0.6944 0.5057 -0.0056 -0.0422 0.1308  52  LEU C CD1 
8577  C CD2 . LEU C 52  ? 0.6342 0.6497 0.5264 0.0055  -0.0452 0.1359  52  LEU C CD2 
8578  N N   . ASN C 53  ? 0.6047 0.6039 0.5091 0.0022  -0.0237 0.0808  53  ASN C N   
8579  C CA  . ASN C 53  ? 0.6149 0.6061 0.5252 0.0043  -0.0210 0.0645  53  ASN C CA  
8580  C C   . ASN C 53  ? 0.6582 0.6381 0.5643 0.0099  -0.0258 0.0585  53  ASN C C   
8581  O O   . ASN C 53  ? 0.5897 0.5631 0.4932 0.0148  -0.0312 0.0663  53  ASN C O   
8582  C CB  . ASN C 53  ? 0.6464 0.6229 0.5727 0.0065  -0.0223 0.0640  53  ASN C CB  
8583  C CG  . ASN C 53  ? 0.6856 0.6748 0.6184 -0.0001 -0.0176 0.0722  53  ASN C CG  
8584  O OD1 . ASN C 53  ? 0.7277 0.7328 0.6640 -0.0048 -0.0091 0.0647  53  ASN C OD1 
8585  N ND2 . ASN C 53  ? 0.6367 0.6198 0.5714 -0.0008 -0.0228 0.0876  53  ASN C ND2 
8586  N N   . PHE C 54  ? 0.6536 0.6317 0.5605 0.0093  -0.0236 0.0448  54  PHE C N   
8587  C CA  . PHE C 54  ? 0.6173 0.5886 0.5191 0.0117  -0.0274 0.0400  54  PHE C CA  
8588  C C   . PHE C 54  ? 0.6554 0.6101 0.5655 0.0139  -0.0292 0.0298  54  PHE C C   
8589  O O   . PHE C 54  ? 0.6978 0.6516 0.6177 0.0127  -0.0262 0.0222  54  PHE C O   
8590  C CB  . PHE C 54  ? 0.5953 0.5839 0.4859 0.0057  -0.0252 0.0358  54  PHE C CB  
8591  C CG  . PHE C 54  ? 0.7375 0.7428 0.6192 0.0034  -0.0261 0.0478  54  PHE C CG  
8592  C CD1 . PHE C 54  ? 0.6007 0.6216 0.4776 -0.0022 -0.0218 0.0521  54  PHE C CD1 
8593  C CD2 . PHE C 54  ? 0.7262 0.7328 0.6052 0.0070  -0.0313 0.0559  54  PHE C CD2 
8594  C CE1 . PHE C 54  ? 0.6624 0.6981 0.5310 -0.0050 -0.0245 0.0656  54  PHE C CE1 
8595  C CE2 . PHE C 54  ? 0.6781 0.7000 0.5521 0.0058  -0.0338 0.0684  54  PHE C CE2 
8596  C CZ  . PHE C 54  ? 0.8058 0.8413 0.6741 -0.0005 -0.0312 0.0739  54  PHE C CZ  
8597  N N   . ASN C 55  ? 0.6813 0.6245 0.5885 0.0170  -0.0343 0.0304  55  ASN C N   
8598  C CA  . ASN C 55  ? 0.6477 0.5750 0.5602 0.0178  -0.0380 0.0233  55  ASN C CA  
8599  C C   . ASN C 55  ? 0.6797 0.6094 0.5849 0.0143  -0.0394 0.0199  55  ASN C C   
8600  O O   . ASN C 55  ? 0.6491 0.5854 0.5460 0.0146  -0.0403 0.0259  55  ASN C O   
8601  C CB  . ASN C 55  ? 0.6185 0.5288 0.5325 0.0230  -0.0436 0.0283  55  ASN C CB  
8602  C CG  . ASN C 55  ? 0.6851 0.5796 0.6035 0.0228  -0.0489 0.0234  55  ASN C CG  
8603  O OD1 . ASN C 55  ? 0.7583 0.6463 0.6893 0.0229  -0.0505 0.0193  55  ASN C OD1 
8604  N ND2 . ASN C 55  ? 0.6189 0.5087 0.5282 0.0221  -0.0520 0.0248  55  ASN C ND2 
8605  N N   . LEU C 56  ? 0.7183 0.6429 0.6289 0.0110  -0.0400 0.0102  56  LEU C N   
8606  C CA  . LEU C 56  ? 0.6590 0.5830 0.5650 0.0058  -0.0426 0.0066  56  LEU C CA  
8607  C C   . LEU C 56  ? 0.7369 0.6407 0.6498 0.0061  -0.0490 0.0048  56  LEU C C   
8608  O O   . LEU C 56  ? 0.7609 0.6545 0.6863 0.0079  -0.0502 -0.0018 56  LEU C O   
8609  C CB  . LEU C 56  ? 0.6298 0.5642 0.5352 0.0004  -0.0388 -0.0041 56  LEU C CB  
8610  C CG  . LEU C 56  ? 0.7813 0.7377 0.6763 -0.0021 -0.0340 -0.0007 56  LEU C CG  
8611  C CD1 . LEU C 56  ? 0.7967 0.7639 0.6880 -0.0083 -0.0299 -0.0133 56  LEU C CD1 
8612  C CD2 . LEU C 56  ? 0.7665 0.7320 0.6526 -0.0035 -0.0371 0.0096  56  LEU C CD2 
8613  N N   . THR C 57  ? 0.7094 0.6087 0.6150 0.0041  -0.0532 0.0114  57  THR C N   
8614  C CA  . THR C 57  ? 0.6941 0.5748 0.6041 0.0025  -0.0605 0.0119  57  THR C CA  
8615  C C   . THR C 57  ? 0.6766 0.5519 0.5928 -0.0039 -0.0633 0.0043  57  THR C C   
8616  O O   . THR C 57  ? 0.7315 0.6186 0.6424 -0.0093 -0.0609 0.0016  57  THR C O   
8617  C CB  . THR C 57  ? 0.6442 0.5236 0.5426 0.0011  -0.0632 0.0218  57  THR C CB  
8618  O OG1 . THR C 57  ? 0.7565 0.6528 0.6472 -0.0033 -0.0598 0.0245  57  THR C OG1 
8619  C CG2 . THR C 57  ? 0.6068 0.4855 0.5005 0.0084  -0.0618 0.0264  57  THR C CG2 
8620  N N   . PRO C 58  ? 0.7613 0.6182 0.6899 -0.0035 -0.0696 0.0008  58  PRO C N   
8621  C CA  . PRO C 58  ? 0.7242 0.5721 0.6612 -0.0088 -0.0733 -0.0077 58  PRO C CA  
8622  C C   . PRO C 58  ? 0.7904 0.6388 0.7178 -0.0185 -0.0773 -0.0018 58  PRO C C   
8623  O O   . PRO C 58  ? 0.8540 0.7039 0.7829 -0.0245 -0.0775 -0.0097 58  PRO C O   
8624  C CB  . PRO C 58  ? 0.7145 0.5408 0.6681 -0.0052 -0.0815 -0.0084 58  PRO C CB  
8625  C CG  . PRO C 58  ? 0.6460 0.4762 0.6030 0.0028  -0.0787 -0.0058 58  PRO C CG  
8626  C CD  . PRO C 58  ? 0.6613 0.5042 0.5989 0.0020  -0.0747 0.0038  58  PRO C CD  
8627  N N   . VAL C 59  ? 0.7359 0.5844 0.6534 -0.0209 -0.0802 0.0114  59  VAL C N   
8628  C CA  . VAL C 59  ? 0.7784 0.6312 0.6881 -0.0312 -0.0830 0.0186  59  VAL C CA  
8629  C C   . VAL C 59  ? 0.7989 0.6749 0.7020 -0.0342 -0.0763 0.0159  59  VAL C C   
8630  O O   . VAL C 59  ? 0.8435 0.7227 0.7466 -0.0439 -0.0790 0.0148  59  VAL C O   
8631  C CB  . VAL C 59  ? 0.8075 0.6606 0.7063 -0.0325 -0.0849 0.0327  59  VAL C CB  
8632  C CG1 . VAL C 59  ? 0.7957 0.6597 0.6866 -0.0228 -0.0780 0.0345  59  VAL C CG1 
8633  C CG2 . VAL C 59  ? 0.7726 0.6386 0.6637 -0.0431 -0.0847 0.0409  59  VAL C CG2 
8634  N N   . LEU C 60  ? 0.7903 0.6822 0.6882 -0.0268 -0.0688 0.0155  60  LEU C N   
8635  C CA  . LEU C 60  ? 0.8200 0.7347 0.7125 -0.0294 -0.0639 0.0144  60  LEU C CA  
8636  C C   . LEU C 60  ? 0.7832 0.6976 0.6794 -0.0335 -0.0640 0.0011  60  LEU C C   
8637  O O   . LEU C 60  ? 0.8302 0.7573 0.7226 -0.0414 -0.0648 -0.0009 60  LEU C O   
8638  C CB  . LEU C 60  ? 0.7301 0.6588 0.6179 -0.0202 -0.0575 0.0184  60  LEU C CB  
8639  C CG  . LEU C 60  ? 0.7056 0.6577 0.5890 -0.0218 -0.0538 0.0183  60  LEU C CG  
8640  C CD1 . LEU C 60  ? 0.7725 0.7403 0.6533 -0.0285 -0.0554 0.0260  60  LEU C CD1 
8641  C CD2 . LEU C 60  ? 0.6705 0.6316 0.5519 -0.0125 -0.0489 0.0227  60  LEU C CD2 
8642  N N   . ILE C 61  ? 0.7484 0.6494 0.6527 -0.0284 -0.0632 -0.0090 61  ILE C N   
8643  C CA  . ILE C 61  ? 0.7481 0.6486 0.6558 -0.0310 -0.0617 -0.0247 61  ILE C CA  
8644  C C   . ILE C 61  ? 0.8240 0.7114 0.7358 -0.0408 -0.0693 -0.0302 61  ILE C C   
8645  O O   . ILE C 61  ? 0.8856 0.7788 0.7937 -0.0473 -0.0693 -0.0409 61  ILE C O   
8646  C CB  . ILE C 61  ? 0.6643 0.5547 0.5837 -0.0222 -0.0584 -0.0340 61  ILE C CB  
8647  C CG1 . ILE C 61  ? 0.6993 0.6081 0.6131 -0.0164 -0.0498 -0.0321 61  ILE C CG1 
8648  C CG2 . ILE C 61  ? 0.7244 0.6053 0.6526 -0.0242 -0.0586 -0.0525 61  ILE C CG2 
8649  C CD1 . ILE C 61  ? 0.7522 0.6545 0.6792 -0.0082 -0.0463 -0.0374 61  ILE C CD1 
8650  N N   . ASP C 62  ? 0.8363 0.7053 0.7548 -0.0429 -0.0769 -0.0224 62  ASP C N   
8651  C CA  . ASP C 62  ? 0.8000 0.6539 0.7236 -0.0535 -0.0857 -0.0246 62  ASP C CA  
8652  C C   . ASP C 62  ? 0.8340 0.7061 0.7475 -0.0649 -0.0867 -0.0190 62  ASP C C   
8653  O O   . ASP C 62  ? 0.8519 0.7209 0.7665 -0.0742 -0.0910 -0.0282 62  ASP C O   
8654  C CB  . ASP C 62  ? 0.7458 0.5787 0.6767 -0.0546 -0.0942 -0.0129 62  ASP C CB  
8655  C CG  . ASP C 62  ? 0.8540 0.6652 0.8004 -0.0457 -0.0972 -0.0202 62  ASP C CG  
8656  O OD1 . ASP C 62  ? 0.9310 0.7402 0.8854 -0.0410 -0.0935 -0.0373 62  ASP C OD1 
8657  O OD2 . ASP C 62  ? 0.9288 0.7266 0.8795 -0.0436 -0.1032 -0.0092 62  ASP C OD2 
8658  N N   . GLN C 63  ? 0.7497 0.6414 0.6547 -0.0643 -0.0831 -0.0045 63  GLN C N   
8659  C CA  . GLN C 63  ? 0.7867 0.6980 0.6863 -0.0749 -0.0845 0.0033  63  GLN C CA  
8660  C C   . GLN C 63  ? 0.8146 0.7453 0.7083 -0.0775 -0.0818 -0.0058 63  GLN C C   
8661  O O   . GLN C 63  ? 0.7544 0.6926 0.6474 -0.0895 -0.0868 -0.0073 63  GLN C O   
8662  C CB  . GLN C 63  ? 0.8465 0.7751 0.7410 -0.0713 -0.0801 0.0196  63  GLN C CB  
8663  C CG  . GLN C 63  ? 0.8269 0.7390 0.7225 -0.0694 -0.0826 0.0291  63  GLN C CG  
8664  C CD  . GLN C 63  ? 0.8472 0.7785 0.7356 -0.0662 -0.0769 0.0423  63  GLN C CD  
8665  O OE1 . GLN C 63  ? 0.8216 0.7620 0.7088 -0.0753 -0.0783 0.0528  63  GLN C OE1 
8666  N NE2 . GLN C 63  ? 0.8047 0.7426 0.6890 -0.0535 -0.0703 0.0416  63  GLN C NE2 
8667  N N   . ILE C 64  ? 0.8147 0.7544 0.7036 -0.0675 -0.0746 -0.0111 64  ILE C N   
8668  C CA  . ILE C 64  ? 0.7976 0.7556 0.6784 -0.0707 -0.0725 -0.0195 64  ILE C CA  
8669  C C   . ILE C 64  ? 0.7965 0.7401 0.6782 -0.0783 -0.0767 -0.0377 64  ILE C C   
8670  O O   . ILE C 64  ? 0.7535 0.7090 0.6282 -0.0883 -0.0800 -0.0437 64  ILE C O   
8671  C CB  . ILE C 64  ? 0.8054 0.7734 0.6810 -0.0594 -0.0641 -0.0203 64  ILE C CB  
8672  C CG1 . ILE C 64  ? 0.7389 0.7189 0.6143 -0.0517 -0.0610 -0.0035 64  ILE C CG1 
8673  C CG2 . ILE C 64  ? 0.6862 0.6731 0.5508 -0.0640 -0.0624 -0.0283 64  ILE C CG2 
8674  C CD1 . ILE C 64  ? 0.6968 0.6804 0.5701 -0.0410 -0.0544 -0.0025 64  ILE C CD1 
8675  N N   . GLN C 65  ? 0.8027 0.7202 0.6940 -0.0736 -0.0773 -0.0476 65  GLN C N   
8676  C CA  . GLN C 65  ? 0.8254 0.7257 0.7205 -0.0788 -0.0811 -0.0672 65  GLN C CA  
8677  C C   . GLN C 65  ? 0.9025 0.7940 0.8005 -0.0934 -0.0920 -0.0652 65  GLN C C   
8678  O O   . GLN C 65  ? 0.9088 0.8003 0.8021 -0.1028 -0.0959 -0.0789 65  GLN C O   
8679  C CB  . GLN C 65  ? 0.7487 0.6230 0.6586 -0.0690 -0.0804 -0.0760 65  GLN C CB  
8680  C CG  . GLN C 65  ? 0.7416 0.6246 0.6506 -0.0575 -0.0696 -0.0862 65  GLN C CG  
8681  C CD  . GLN C 65  ? 0.8957 0.7553 0.8234 -0.0482 -0.0693 -0.0973 65  GLN C CD  
8682  O OE1 . GLN C 65  ? 0.9261 0.7650 0.8672 -0.0463 -0.0766 -0.0889 65  GLN C OE1 
8683  N NE2 . GLN C 65  ? 0.9329 0.7974 0.8623 -0.0425 -0.0609 -0.1159 65  GLN C NE2 
8684  N N   . GLU C 66  ? 0.8887 0.7734 0.7936 -0.0967 -0.0973 -0.0480 66  GLU C N   
8685  C CA  . GLU C 66  ? 0.9234 0.8034 0.8316 -0.1124 -0.1074 -0.0423 66  GLU C CA  
8686  C C   . GLU C 66  ? 0.8590 0.7705 0.7573 -0.1219 -0.1074 -0.0368 66  GLU C C   
8687  O O   . GLU C 66  ? 0.8835 0.7944 0.7817 -0.1358 -0.1153 -0.0429 66  GLU C O   
8688  C CB  . GLU C 66  ? 0.8249 0.6947 0.7407 -0.1144 -0.1116 -0.0231 66  GLU C CB  
8689  C CG  . GLU C 66  ? 0.9144 0.7697 0.8380 -0.1312 -0.1235 -0.0182 66  GLU C CG  
8690  C CD  . GLU C 66  ? 1.0598 0.9067 0.9883 -0.1342 -0.1272 0.0022  66  GLU C CD  
8691  O OE1 . GLU C 66  ? 1.0251 0.8813 0.9487 -0.1235 -0.1199 0.0119  66  GLU C OE1 
8692  O OE2 . GLU C 66  ? 1.0925 0.9229 1.0288 -0.1481 -0.1378 0.0086  66  GLU C OE2 
8693  N N   . TYR C 67  ? 0.7471 0.6858 0.6387 -0.1147 -0.0998 -0.0252 67  TYR C N   
8694  C CA  . TYR C 67  ? 0.7765 0.7472 0.6618 -0.1219 -0.1004 -0.0189 67  TYR C CA  
8695  C C   . TYR C 67  ? 0.8640 0.8405 0.7390 -0.1269 -0.1021 -0.0363 67  TYR C C   
8696  O O   . TYR C 67  ? 0.8569 0.8477 0.7289 -0.1403 -0.1091 -0.0367 67  TYR C O   
8697  C CB  . TYR C 67  ? 0.7931 0.7882 0.6752 -0.1103 -0.0920 -0.0050 67  TYR C CB  
8698  C CG  . TYR C 67  ? 0.7784 0.7864 0.6676 -0.1115 -0.0915 0.0140  67  TYR C CG  
8699  C CD1 . TYR C 67  ? 0.7098 0.7459 0.6024 -0.1208 -0.0945 0.0241  67  TYR C CD1 
8700  C CD2 . TYR C 67  ? 0.8379 0.8321 0.7302 -0.1034 -0.0876 0.0214  67  TYR C CD2 
8701  C CE1 . TYR C 67  ? 0.7331 0.7844 0.6332 -0.1213 -0.0919 0.0403  67  TYR C CE1 
8702  C CE2 . TYR C 67  ? 0.7921 0.7998 0.6882 -0.1046 -0.0856 0.0372  67  TYR C CE2 
8703  C CZ  . TYR C 67  ? 0.7404 0.7771 0.6408 -0.1131 -0.0869 0.0462  67  TYR C CZ  
8704  O OH  . TYR C 67  ? 0.7653 0.8186 0.6706 -0.1137 -0.0829 0.0608  67  TYR C OH  
8705  N N   . ALA C 68  ? 0.8644 0.8314 0.7333 -0.1172 -0.0958 -0.0509 68  ALA C N   
8706  C CA  . ALA C 68  ? 0.8470 0.8212 0.7027 -0.1216 -0.0956 -0.0688 68  ALA C CA  
8707  C C   . ALA C 68  ? 0.9096 0.8596 0.7677 -0.1321 -0.1034 -0.0883 68  ALA C C   
8708  O O   . ALA C 68  ? 0.9542 0.9124 0.8000 -0.1415 -0.1068 -0.1021 68  ALA C O   
8709  C CB  . ALA C 68  ? 0.8211 0.7966 0.6703 -0.1082 -0.0845 -0.0773 68  ALA C CB  
8710  N N   . GLN C 69  ? 0.8812 0.8010 0.7545 -0.1310 -0.1072 -0.0896 69  GLN C N   
8711  C CA  . GLN C 69  ? 0.9055 0.7973 0.7852 -0.1406 -0.1165 -0.1065 69  GLN C CA  
8712  C C   . GLN C 69  ? 0.8859 0.7793 0.7698 -0.1590 -0.1291 -0.0964 69  GLN C C   
8713  O O   . GLN C 69  ? 1.0209 0.8891 0.9113 -0.1692 -0.1389 -0.1087 69  GLN C O   
8714  C CB  . GLN C 69  ? 1.0388 0.8962 0.9360 -0.1313 -0.1170 -0.1101 69  GLN C CB  
8715  C CG  . GLN C 69  ? 1.1211 0.9696 1.0191 -0.1165 -0.1073 -0.1295 69  GLN C CG  
8716  C CD  . GLN C 69  ? 1.0474 0.8653 0.9662 -0.1064 -0.1090 -0.1291 69  GLN C CD  
8717  O OE1 . GLN C 69  ? 1.0679 0.8742 0.9967 -0.1096 -0.1162 -0.1107 69  GLN C OE1 
8718  N NE2 . GLN C 69  ? 1.0175 0.8244 0.9432 -0.0944 -0.1023 -0.1486 69  GLN C NE2 
8719  N N   . GLY C 70  ? 0.8684 0.7905 0.7508 -0.1635 -0.1292 -0.0746 70  GLY C N   
8720  C CA  . GLY C 70  ? 1.0651 0.9950 0.9534 -0.1816 -0.1402 -0.0636 70  GLY C CA  
8721  C C   . GLY C 70  ? 1.0074 0.9158 0.9120 -0.1876 -0.1465 -0.0501 70  GLY C C   
8722  O O   . GLY C 70  ? 0.9484 0.8628 0.8597 -0.2045 -0.1557 -0.0399 70  GLY C O   
8723  N N   . LYS C 71  ? 0.9891 0.8744 0.9005 -0.1754 -0.1423 -0.0482 71  LYS C N   
8724  C CA  . LYS C 71  ? 0.9878 0.8495 0.9129 -0.1811 -0.1493 -0.0352 71  LYS C CA  
8725  C C   . LYS C 71  ? 1.0211 0.9022 0.9471 -0.1770 -0.1431 -0.0101 71  LYS C C   
8726  O O   . LYS C 71  ? 1.1263 0.9884 1.0600 -0.1775 -0.1463 0.0015  71  LYS C O   
8727  C CB  . LYS C 71  ? 1.0218 0.8441 0.9554 -0.1711 -0.1511 -0.0489 71  LYS C CB  
8728  C CG  . LYS C 71  ? 1.0181 0.8314 0.9464 -0.1636 -0.1478 -0.0775 71  LYS C CG  
8729  C CD  . LYS C 71  ? 1.0548 0.8384 0.9940 -0.1483 -0.1453 -0.0890 71  LYS C CD  
8730  C CE  . LYS C 71  ? 1.0437 0.7864 1.0002 -0.1556 -0.1589 -0.0970 71  LYS C CE  
8731  N NZ  . LYS C 71  ? 1.2612 0.9782 1.2296 -0.1395 -0.1560 -0.1161 71  LYS C NZ  
8732  N N   . ALA C 72  ? 0.9859 0.9040 0.9041 -0.1728 -0.1348 -0.0016 72  ALA C N   
8733  C CA  . ALA C 72  ? 1.0044 0.9429 0.9228 -0.1671 -0.1273 0.0190  72  ALA C CA  
8734  C C   . ALA C 72  ? 1.0692 1.0356 0.9929 -0.1828 -0.1306 0.0350  72  ALA C C   
8735  O O   . ALA C 72  ? 1.0793 1.0705 1.0020 -0.1889 -0.1322 0.0323  72  ALA C O   
8736  C CB  . ALA C 72  ? 0.8641 0.8234 0.7734 -0.1495 -0.1154 0.0177  72  ALA C CB  
8737  N N   . LYS C 73  ? 1.0122 0.9767 0.9419 -0.1896 -0.1317 0.0522  73  LYS C N   
8738  C CA  . LYS C 73  ? 0.9933 0.9849 0.9309 -0.2062 -0.1343 0.0686  73  LYS C CA  
8739  C C   . LYS C 73  ? 0.9465 0.9745 0.8826 -0.1967 -0.1215 0.0832  73  LYS C C   
8740  O O   . LYS C 73  ? 0.9542 0.9862 0.8910 -0.1986 -0.1175 0.0981  73  LYS C O   
8741  C CB  . LYS C 73  ? 0.9776 0.9454 0.9230 -0.2229 -0.1441 0.0791  73  LYS C CB  
8742  C CG  . LYS C 73  ? 1.0032 0.9234 0.9504 -0.2238 -0.1545 0.0646  73  LYS C CG  
8743  C CD  . LYS C 73  ? 1.0604 0.9555 1.0152 -0.2368 -0.1636 0.0797  73  LYS C CD  
8744  C CE  . LYS C 73  ? 0.9970 0.8435 0.9588 -0.2384 -0.1762 0.0655  73  LYS C CE  
8745  N NZ  . LYS C 73  ? 1.0138 0.8414 0.9878 -0.2620 -0.1915 0.0748  73  LYS C NZ  
8746  N N   . ASP C 74  ? 0.8862 0.9407 0.8198 -0.1863 -0.1154 0.0784  74  ASP C N   
8747  C CA  . ASP C 74  ? 0.8199 0.9087 0.7548 -0.1752 -0.1036 0.0896  74  ASP C CA  
8748  C C   . ASP C 74  ? 0.8117 0.9362 0.7600 -0.1899 -0.1043 0.1047  74  ASP C C   
8749  O O   . ASP C 74  ? 0.9492 1.0915 0.9053 -0.2007 -0.1114 0.1032  74  ASP C O   
8750  C CB  . ASP C 74  ? 0.7620 0.8648 0.6921 -0.1595 -0.0987 0.0808  74  ASP C CB  
8751  C CG  . ASP C 74  ? 0.8444 0.9713 0.7753 -0.1431 -0.0865 0.0892  74  ASP C CG  
8752  O OD1 . ASP C 74  ? 1.0451 1.2016 0.9860 -0.1469 -0.0821 0.1021  74  ASP C OD1 
8753  O OD2 . ASP C 74  ? 0.7269 0.8435 0.6496 -0.1265 -0.0811 0.0825  74  ASP C OD2 
8754  N N   . VAL C 75  ? 0.7773 0.9141 0.7281 -0.1910 -0.0969 0.1191  75  VAL C N   
8755  C CA  . VAL C 75  ? 0.7372 0.9099 0.7025 -0.2062 -0.0961 0.1347  75  VAL C CA  
8756  C C   . VAL C 75  ? 0.8413 1.0588 0.8180 -0.1980 -0.0900 0.1368  75  VAL C C   
8757  O O   . VAL C 75  ? 0.8348 1.0799 0.8265 -0.2118 -0.0959 0.1424  75  VAL C O   
8758  C CB  . VAL C 75  ? 0.8418 1.0186 0.8041 -0.2085 -0.0877 0.1491  75  VAL C CB  
8759  C CG1 . VAL C 75  ? 0.8910 1.0296 0.8484 -0.2245 -0.0983 0.1529  75  VAL C CG1 
8760  C CG2 . VAL C 75  ? 0.8894 1.0634 0.8390 -0.1854 -0.0750 0.1452  75  VAL C CG2 
8761  N N   . PHE C 76  ? 0.8471 1.0719 0.8185 -0.1757 -0.0794 0.1328  76  PHE C N   
8762  C CA  . PHE C 76  ? 0.8550 1.1207 0.8395 -0.1654 -0.0740 0.1358  76  PHE C CA  
8763  C C   . PHE C 76  ? 0.8826 1.1511 0.8693 -0.1680 -0.0849 0.1279  76  PHE C C   
8764  O O   . PHE C 76  ? 0.8392 1.1450 0.8418 -0.1699 -0.0869 0.1339  76  PHE C O   
8765  C CB  . PHE C 76  ? 0.7578 1.0240 0.7357 -0.1410 -0.0612 0.1330  76  PHE C CB  
8766  C CG  . PHE C 76  ? 0.7774 1.0845 0.7716 -0.1282 -0.0547 0.1374  76  PHE C CG  
8767  C CD1 . PHE C 76  ? 0.6876 1.0310 0.6965 -0.1266 -0.0440 0.1477  76  PHE C CD1 
8768  C CD2 . PHE C 76  ? 0.8461 1.1563 0.8420 -0.1177 -0.0593 0.1317  76  PHE C CD2 
8769  C CE1 . PHE C 76  ? 0.8518 1.2330 0.8799 -0.1132 -0.0383 0.1511  76  PHE C CE1 
8770  C CE2 . PHE C 76  ? 0.7332 1.0796 0.7468 -0.1053 -0.0551 0.1372  76  PHE C CE2 
8771  C CZ  . PHE C 76  ? 0.8293 1.2109 0.8607 -0.1022 -0.0447 0.1464  76  PHE C CZ  
8772  N N   . LEU C 77  ? 0.8402 1.0715 0.8115 -0.1687 -0.0924 0.1144  77  LEU C N   
8773  C CA  . LEU C 77  ? 0.8440 1.0771 0.8127 -0.1726 -0.1024 0.1054  77  LEU C CA  
8774  C C   . LEU C 77  ? 0.8411 1.0883 0.8206 -0.1961 -0.1146 0.1087  77  LEU C C   
8775  O O   . LEU C 77  ? 0.8270 1.0986 0.8123 -0.2007 -0.1219 0.1087  77  LEU C O   
8776  C CB  . LEU C 77  ? 0.9351 1.1262 0.8848 -0.1682 -0.1055 0.0887  77  LEU C CB  
8777  C CG  . LEU C 77  ? 0.8532 1.0456 0.7928 -0.1551 -0.1048 0.0799  77  LEU C CG  
8778  C CD1 . LEU C 77  ? 0.7889 1.0038 0.7339 -0.1357 -0.0946 0.0888  77  LEU C CD1 
8779  C CD2 . LEU C 77  ? 0.7791 0.9303 0.7026 -0.1503 -0.1045 0.0645  77  LEU C CD2 
8780  N N   . GLU C 78  ? 0.8681 1.0988 0.8503 -0.2123 -0.1187 0.1121  78  GLU C N   
8781  C CA  . GLU C 78  ? 0.9403 1.1853 0.9354 -0.2364 -0.1307 0.1173  78  GLU C CA  
8782  C C   . GLU C 78  ? 0.8780 1.1766 0.8952 -0.2393 -0.1270 0.1339  78  GLU C C   
8783  O O   . GLU C 78  ? 0.8684 1.1910 0.8978 -0.2541 -0.1376 0.1368  78  GLU C O   
8784  C CB  . GLU C 78  ? 0.9819 1.1977 0.9773 -0.2531 -0.1357 0.1206  78  GLU C CB  
8785  C CG  . GLU C 78  ? 1.1778 1.4022 1.1864 -0.2800 -0.1501 0.1249  78  GLU C CG  
8786  C CD  . GLU C 78  ? 1.2858 1.4613 1.2862 -0.2936 -0.1630 0.1126  78  GLU C CD  
8787  O OE1 . GLU C 78  ? 1.2532 1.4184 1.2629 -0.3125 -0.1695 0.1227  78  GLU C OE1 
8788  O OE2 . GLU C 78  ? 1.2259 1.3736 1.2114 -0.2853 -0.1665 0.0930  78  GLU C OE2 
8789  N N   . ALA C 79  ? 0.7967 1.1157 0.8201 -0.2250 -0.1121 0.1440  79  ALA C N   
8790  C CA  . ALA C 79  ? 0.8024 1.1750 0.8495 -0.2237 -0.1064 0.1580  79  ALA C CA  
8791  C C   . ALA C 79  ? 0.7802 1.1763 0.8331 -0.2125 -0.1105 0.1547  79  ALA C C   
8792  O O   . ALA C 79  ? 0.8781 1.3162 0.9531 -0.2194 -0.1151 0.1641  79  ALA C O   
8793  C CB  . ALA C 79  ? 0.8089 1.1949 0.8587 -0.2085 -0.0884 0.1658  79  ALA C CB  
8794  N N   . ILE C 80  ? 0.7223 1.0931 0.7566 -0.1959 -0.1095 0.1427  80  ILE C N   
8795  C CA  . ILE C 80  ? 0.7836 1.1713 0.8193 -0.1885 -0.1161 0.1401  80  ILE C CA  
8796  C C   . ILE C 80  ? 0.8414 1.2251 0.8724 -0.2096 -0.1337 0.1340  80  ILE C C   
8797  O O   . ILE C 80  ? 0.7652 1.1822 0.8088 -0.2154 -0.1430 0.1397  80  ILE C O   
8798  C CB  . ILE C 80  ? 0.7741 1.1349 0.7900 -0.1673 -0.1104 0.1300  80  ILE C CB  
8799  C CG1 . ILE C 80  ? 0.7879 1.1651 0.8136 -0.1445 -0.0963 0.1370  80  ILE C CG1 
8800  C CG2 . ILE C 80  ? 0.7552 1.1186 0.7621 -0.1674 -0.1213 0.1241  80  ILE C CG2 
8801  C CD1 . ILE C 80  ? 0.7764 1.1158 0.7819 -0.1287 -0.0877 0.1277  80  ILE C CD1 
8802  N N   . ARG C 81  ? 0.8198 1.1624 0.8330 -0.2212 -0.1392 0.1216  81  ARG C N   
8803  C CA  . ARG C 81  ? 0.8363 1.1679 0.8401 -0.2391 -0.1553 0.1106  81  ARG C CA  
8804  C C   . ARG C 81  ? 0.8538 1.2166 0.8785 -0.2620 -0.1669 0.1210  81  ARG C C   
8805  O O   . ARG C 81  ? 0.7749 1.1584 0.8016 -0.2713 -0.1795 0.1198  81  ARG C O   
8806  C CB  . ARG C 81  ? 0.8898 1.1693 0.8743 -0.2451 -0.1576 0.0944  81  ARG C CB  
8807  C CG  . ARG C 81  ? 1.0600 1.3257 1.0357 -0.2653 -0.1742 0.0807  81  ARG C CG  
8808  C CD  . ARG C 81  ? 1.1201 1.3347 1.0831 -0.2726 -0.1778 0.0648  81  ARG C CD  
8809  N NE  . ARG C 81  ? 1.1764 1.3826 1.1546 -0.2903 -0.1827 0.0739  81  ARG C NE  
8810  C CZ  . ARG C 81  ? 1.0830 1.3004 1.0727 -0.3142 -0.1967 0.0772  81  ARG C CZ  
8811  N NH1 . ARG C 81  ? 0.9699 1.2107 0.9583 -0.3231 -0.2074 0.0726  81  ARG C NH1 
8812  N NH2 . ARG C 81  ? 0.9682 1.1731 0.9708 -0.3307 -0.2010 0.0861  81  ARG C NH2 
8813  N N   . LYS C 82  ? 0.8408 1.2086 0.8811 -0.2725 -0.1633 0.1320  82  LYS C N   
8814  C CA  . LYS C 82  ? 0.8266 1.2183 0.8867 -0.2979 -0.1752 0.1414  82  LYS C CA  
8815  C C   . LYS C 82  ? 0.7924 1.2421 0.8771 -0.2967 -0.1771 0.1554  82  LYS C C   
8816  O O   . LYS C 82  ? 0.7662 1.2418 0.8604 -0.2758 -0.1648 0.1633  82  LYS C O   
8817  C CB  . LYS C 82  ? 0.8687 1.2558 0.9403 -0.3089 -0.1692 0.1532  82  LYS C CB  
8818  C CG  . LYS C 82  ? 0.9379 1.2840 1.0020 -0.3319 -0.1819 0.1460  82  LYS C CG  
8819  C CD  . LYS C 82  ? 0.9615 1.3128 1.0411 -0.3467 -0.1780 0.1634  82  LYS C CD  
8820  C CE  . LYS C 82  ? 0.9953 1.3552 1.0736 -0.3268 -0.1576 0.1729  82  LYS C CE  
8821  N NZ  . LYS C 82  ? 1.0444 1.3903 1.1255 -0.3406 -0.1547 0.1854  82  LYS C NZ  
8822  N N   . ASP C 83  ? 0.7522 1.2214 0.8487 -0.3194 -0.1937 0.1581  83  ASP C N   
8823  C CA  . ASP C 83  ? 0.7892 1.3172 0.9158 -0.3225 -0.1975 0.1743  83  ASP C CA  
8824  C C   . ASP C 83  ? 0.7902 1.3507 0.9445 -0.3203 -0.1826 0.1924  83  ASP C C   
8825  O O   . ASP C 83  ? 0.7954 1.3388 0.9500 -0.3339 -0.1794 0.1958  83  ASP C O   
8826  C CB  . ASP C 83  ? 0.7701 1.3096 0.9043 -0.3515 -0.2195 0.1738  83  ASP C CB  
8827  C CG  . ASP C 83  ? 0.8119 1.4138 0.9785 -0.3551 -0.2262 0.1903  83  ASP C CG  
8828  O OD1 . ASP C 83  ? 0.8930 1.5342 1.0913 -0.3562 -0.2174 0.2078  83  ASP C OD1 
8829  O OD2 . ASP C 83  ? 0.9225 1.5358 1.0829 -0.3567 -0.2403 0.1859  83  ASP C OD2 
8830  N N   . PRO C 84  ? 0.7963 1.4042 0.9746 -0.3037 -0.1733 0.2045  84  PRO C N   
8831  C CA  . PRO C 84  ? 0.7053 1.3438 0.9068 -0.2981 -0.1554 0.2188  84  PRO C CA  
8832  C C   . PRO C 84  ? 0.7148 1.3800 0.9405 -0.3264 -0.1604 0.2326  84  PRO C C   
8833  O O   . PRO C 84  ? 0.7100 1.3921 0.9482 -0.3271 -0.1454 0.2434  84  PRO C O   
8834  C CB  . PRO C 84  ? 0.7059 1.3918 0.9316 -0.2754 -0.1484 0.2266  84  PRO C CB  
8835  C CG  . PRO C 84  ? 0.6844 1.3489 0.8892 -0.2633 -0.1589 0.2151  84  PRO C CG  
8836  C CD  . PRO C 84  ? 0.7593 1.3957 0.9453 -0.2890 -0.1786 0.2059  84  PRO C CD  
8837  N N   . ASP C 85  ? 0.7729 1.4438 1.0052 -0.3507 -0.1813 0.2328  85  ASP C N   
8838  C CA  . ASP C 85  ? 0.8403 1.5327 1.0956 -0.3806 -0.1881 0.2461  85  ASP C CA  
8839  C C   . ASP C 85  ? 0.7662 1.4094 1.0014 -0.3951 -0.1864 0.2429  85  ASP C C   
8840  O O   . ASP C 85  ? 0.7763 1.4363 1.0292 -0.4143 -0.1836 0.2578  85  ASP C O   
8841  C CB  . ASP C 85  ? 0.8044 1.5118 1.0701 -0.4034 -0.2129 0.2456  85  ASP C CB  
8842  C CG  . ASP C 85  ? 0.9503 1.7262 1.2537 -0.3988 -0.2148 0.2600  85  ASP C CG  
8843  O OD1 . ASP C 85  ? 1.0687 1.8808 1.3927 -0.3782 -0.1958 0.2701  85  ASP C OD1 
8844  O OD2 . ASP C 85  ? 1.0706 1.8644 1.3836 -0.4152 -0.2358 0.2607  85  ASP C OD2 
8845  N N   . ASP C 86  ? 0.8104 1.3944 1.0102 -0.3864 -0.1883 0.2247  86  ASP C N   
8846  C CA  . ASP C 86  ? 0.8283 1.3614 1.0090 -0.3959 -0.1871 0.2208  86  ASP C CA  
8847  C C   . ASP C 86  ? 0.8209 1.3425 0.9896 -0.3735 -0.1653 0.2229  86  ASP C C   
8848  O O   . ASP C 86  ? 0.9273 1.4043 1.0777 -0.3773 -0.1639 0.2196  86  ASP C O   
8849  C CB  . ASP C 86  ? 0.8198 1.2950 0.9713 -0.3995 -0.2023 0.1986  86  ASP C CB  
8850  C CG  . ASP C 86  ? 0.9837 1.4648 1.1425 -0.4239 -0.2251 0.1940  86  ASP C CG  
8851  O OD1 . ASP C 86  ? 1.0340 1.5613 1.2222 -0.4415 -0.2309 0.2101  86  ASP C OD1 
8852  O OD2 . ASP C 86  ? 0.9304 1.3707 1.0655 -0.4259 -0.2372 0.1736  86  ASP C OD2 
8853  N N   . LEU C 87  ? 0.7589 1.3188 0.9380 -0.3502 -0.1493 0.2279  87  LEU C N   
8854  C CA  . LEU C 87  ? 0.7732 1.3223 0.9388 -0.3268 -0.1291 0.2269  87  LEU C CA  
8855  C C   . LEU C 87  ? 0.8176 1.3924 0.9969 -0.3364 -0.1156 0.2446  87  LEU C C   
8856  O O   . LEU C 87  ? 0.8309 1.4601 1.0404 -0.3454 -0.1119 0.2592  87  LEU C O   
8857  C CB  . LEU C 87  ? 0.7425 1.3188 0.9136 -0.2973 -0.1184 0.2232  87  LEU C CB  
8858  C CG  . LEU C 87  ? 0.8452 1.3858 0.9917 -0.2780 -0.1228 0.2054  87  LEU C CG  
8859  C CD1 . LEU C 87  ? 0.7591 1.3289 0.9152 -0.2494 -0.1103 0.2063  87  LEU C CD1 
8860  C CD2 . LEU C 87  ? 0.8246 1.3051 0.9388 -0.2736 -0.1204 0.1933  87  LEU C CD2 
8861  N N   . GLU C 88  ? 0.8676 1.4056 1.0249 -0.3346 -0.1079 0.2437  88  GLU C N   
8862  C CA  . GLU C 88  ? 0.8991 1.4614 1.0635 -0.3414 -0.0930 0.2603  88  GLU C CA  
8863  C C   . GLU C 88  ? 0.8727 1.4740 1.0437 -0.3145 -0.0709 0.2608  88  GLU C C   
8864  O O   . GLU C 88  ? 0.8711 1.4619 1.0325 -0.2885 -0.0669 0.2472  88  GLU C O   
8865  C CB  . GLU C 88  ? 0.9566 1.4667 1.0940 -0.3481 -0.0935 0.2603  88  GLU C CB  
8866  C CG  . GLU C 88  ? 1.0327 1.4961 1.1634 -0.3724 -0.1157 0.2576  88  GLU C CG  
8867  C CD  . GLU C 88  ? 1.1645 1.6543 1.3217 -0.4014 -0.1306 0.2678  88  GLU C CD  
8868  O OE1 . GLU C 88  ? 1.1269 1.5804 1.2793 -0.4144 -0.1502 0.2577  88  GLU C OE1 
8869  O OE2 . GLU C 88  ? 1.1251 1.6693 1.3076 -0.4126 -0.1231 0.2855  88  GLU C OE2 
8870  N N   . LYS C 89  ? 0.8096 1.4574 0.9984 -0.3215 -0.0564 0.2767  89  LYS C N   
8871  C CA  . LYS C 89  ? 0.8090 1.4983 1.0076 -0.2965 -0.0343 0.2761  89  LYS C CA  
8872  C C   . LYS C 89  ? 0.8490 1.4991 1.0150 -0.2724 -0.0232 0.2631  89  LYS C C   
8873  O O   . LYS C 89  ? 0.8365 1.4981 1.0043 -0.2446 -0.0125 0.2531  89  LYS C O   
8874  C CB  . LYS C 89  ? 0.8336 1.5776 1.0536 -0.3106 -0.0192 0.2946  89  LYS C CB  
8875  C CG  . LYS C 89  ? 0.8606 1.6353 1.0795 -0.2867 0.0072  0.2923  89  LYS C CG  
8876  C CD  . LYS C 89  ? 0.7802 1.5943 1.0259 -0.2599 0.0141  0.2843  89  LYS C CD  
8877  C CE  . LYS C 89  ? 0.8693 1.6791 1.0997 -0.2279 0.0340  0.2711  89  LYS C CE  
8878  N NZ  . LYS C 89  ? 0.7889 1.6349 1.0477 -0.2005 0.0405  0.2638  89  LYS C NZ  
8879  N N   . GLU C 90  ? 0.8449 1.4474 0.9823 -0.2827 -0.0271 0.2632  90  GLU C N   
8880  C CA  . GLU C 90  ? 0.9231 1.4841 1.0293 -0.2615 -0.0203 0.2505  90  GLU C CA  
8881  C C   . GLU C 90  ? 0.7938 1.3276 0.8934 -0.2404 -0.0282 0.2325  90  GLU C C   
8882  O O   . GLU C 90  ? 0.8550 1.3831 0.9444 -0.2148 -0.0176 0.2221  90  GLU C O   
8883  C CB  . GLU C 90  ? 0.9717 1.4832 1.0519 -0.2781 -0.0284 0.2545  90  GLU C CB  
8884  C CG  . GLU C 90  ? 0.9847 1.4717 1.0707 -0.3046 -0.0500 0.2591  90  GLU C CG  
8885  C CD  . GLU C 90  ? 0.9850 1.5029 1.0880 -0.3342 -0.0506 0.2807  90  GLU C CD  
8886  O OE1 . GLU C 90  ? 0.9541 1.5307 1.0794 -0.3345 -0.0374 0.2903  90  GLU C OE1 
8887  O OE2 . GLU C 90  ? 0.9738 1.4579 1.0697 -0.3570 -0.0643 0.2885  90  GLU C OE2 
8888  N N   . GLU C 91  ? 0.8369 1.3538 0.9413 -0.2516 -0.0470 0.2287  91  GLU C N   
8889  C CA  . GLU C 91  ? 0.7748 1.2695 0.8721 -0.2341 -0.0548 0.2130  91  GLU C CA  
8890  C C   . GLU C 91  ? 0.7697 1.3077 0.8874 -0.2131 -0.0461 0.2119  91  GLU C C   
8891  O O   . GLU C 91  ? 0.7508 1.2732 0.8587 -0.1902 -0.0435 0.2006  91  GLU C O   
8892  C CB  . GLU C 91  ? 0.8471 1.3225 0.9460 -0.2528 -0.0759 0.2093  91  GLU C CB  
8893  C CG  . GLU C 91  ? 0.8682 1.3102 0.9576 -0.2781 -0.0861 0.2139  91  GLU C CG  
8894  C CD  . GLU C 91  ? 0.8943 1.3031 0.9782 -0.2915 -0.1066 0.2035  91  GLU C CD  
8895  O OE1 . GLU C 91  ? 0.9438 1.3082 1.0062 -0.2808 -0.1107 0.1881  91  GLU C OE1 
8896  O OE2 . GLU C 91  ? 0.9091 1.3364 1.0105 -0.3134 -0.1184 0.2100  91  GLU C OE2 
8897  N N   . VAL C 92  ? 0.7505 1.3434 0.8989 -0.2208 -0.0420 0.2244  92  VAL C N   
8898  C CA  . VAL C 92  ? 0.6634 1.3010 0.8366 -0.1999 -0.0333 0.2247  92  VAL C CA  
8899  C C   . VAL C 92  ? 0.7618 1.3963 0.9243 -0.1735 -0.0138 0.2178  92  VAL C C   
8900  O O   . VAL C 92  ? 0.8405 1.4706 1.0034 -0.1493 -0.0116 0.2087  92  VAL C O   
8901  C CB  . VAL C 92  ? 0.7191 1.4193 0.9299 -0.2138 -0.0305 0.2403  92  VAL C CB  
8902  C CG1 . VAL C 92  ? 0.7241 1.4717 0.9646 -0.1897 -0.0208 0.2406  92  VAL C CG1 
8903  C CG2 . VAL C 92  ? 0.7887 1.4908 1.0103 -0.2402 -0.0521 0.2461  92  VAL C CG2 
8904  N N   . GLU C 93  ? 0.7733 1.4085 0.9247 -0.1788 -0.0002 0.2221  93  GLU C N   
8905  C CA  . GLU C 93  ? 0.7347 1.3689 0.8743 -0.1554 0.0187  0.2144  93  GLU C CA  
8906  C C   . GLU C 93  ? 0.8200 1.3982 0.9294 -0.1389 0.0143  0.1995  93  GLU C C   
8907  O O   . GLU C 93  ? 0.8137 1.3906 0.9205 -0.1137 0.0243  0.1899  93  GLU C O   
8908  C CB  . GLU C 93  ? 0.8187 1.4631 0.9472 -0.1684 0.0323  0.2228  93  GLU C CB  
8909  C CG  . GLU C 93  ? 0.9403 1.5844 1.0530 -0.1463 0.0521  0.2137  93  GLU C CG  
8910  C CD  . GLU C 93  ? 0.9295 1.6269 1.0718 -0.1256 0.0684  0.2110  93  GLU C CD  
8911  O OE1 . GLU C 93  ? 0.8167 1.5612 0.9737 -0.1327 0.0835  0.2196  93  GLU C OE1 
8912  O OE2 . GLU C 93  ? 0.9164 1.6092 1.0685 -0.1024 0.0661  0.2007  93  GLU C OE2 
8913  N N   . LYS C 94  ? 0.8503 1.3819 0.9381 -0.1527 -0.0005 0.1970  94  LYS C N   
8914  C CA  . LYS C 94  ? 0.7972 1.2791 0.8604 -0.1379 -0.0057 0.1832  94  LYS C CA  
8915  C C   . LYS C 94  ? 0.7500 1.2389 0.8256 -0.1195 -0.0103 0.1763  94  LYS C C   
8916  O O   . LYS C 94  ? 0.6882 1.1587 0.7536 -0.0979 -0.0053 0.1666  94  LYS C O   
8917  C CB  . LYS C 94  ? 0.6988 1.1353 0.7434 -0.1563 -0.0215 0.1814  94  LYS C CB  
8918  C CG  . LYS C 94  ? 0.7455 1.1735 0.7810 -0.1779 -0.0212 0.1915  94  LYS C CG  
8919  C CD  . LYS C 94  ? 0.7635 1.1342 0.7724 -0.1821 -0.0302 0.1851  94  LYS C CD  
8920  C CE  . LYS C 94  ? 0.7716 1.1345 0.7717 -0.2022 -0.0299 0.1976  94  LYS C CE  
8921  N NZ  . LYS C 94  ? 0.7529 1.0938 0.7288 -0.1917 -0.0208 0.1955  94  LYS C NZ  
8922  N N   . LEU C 95  ? 0.7748 1.2907 0.8728 -0.1290 -0.0207 0.1823  95  LEU C N   
8923  C CA  . LEU C 95  ? 0.7352 1.2591 0.8446 -0.1145 -0.0278 0.1786  95  LEU C CA  
8924  C C   . LEU C 95  ? 0.7958 1.3515 0.9250 -0.0895 -0.0143 0.1787  95  LEU C C   
8925  O O   . LEU C 95  ? 0.7544 1.2963 0.8808 -0.0695 -0.0154 0.1720  95  LEU C O   
8926  C CB  . LEU C 95  ? 0.6360 1.1855 0.7650 -0.1325 -0.0430 0.1864  95  LEU C CB  
8927  C CG  . LEU C 95  ? 0.7225 1.2367 0.8328 -0.1502 -0.0610 0.1809  95  LEU C CG  
8928  C CD1 . LEU C 95  ? 0.7975 1.2641 0.8796 -0.1584 -0.0600 0.1742  95  LEU C CD1 
8929  C CD2 . LEU C 95  ? 0.6318 1.1745 0.7614 -0.1744 -0.0740 0.1899  95  LEU C CD2 
8930  N N   . ILE C 96  ? 0.7472 1.3464 0.8980 -0.0907 -0.0016 0.1863  96  ILE C N   
8931  C CA  . ILE C 96  ? 0.7425 1.3734 0.9142 -0.0660 0.0134  0.1844  96  ILE C CA  
8932  C C   . ILE C 96  ? 0.8205 1.4168 0.9665 -0.0472 0.0252  0.1719  96  ILE C C   
8933  O O   . ILE C 96  ? 0.8345 1.4264 0.9862 -0.0230 0.0287  0.1646  96  ILE C O   
8934  C CB  . ILE C 96  ? 0.6930 1.3802 0.8925 -0.0734 0.0262  0.1945  96  ILE C CB  
8935  C CG1 . ILE C 96  ? 0.6510 1.3640 0.8691 -0.1001 0.0125  0.2077  96  ILE C CG1 
8936  C CG2 . ILE C 96  ? 0.6189 1.3478 0.8509 -0.0476 0.0386  0.1927  96  ILE C CG2 
8937  C CD1 . ILE C 96  ? 0.6024 1.3467 0.8528 -0.0940 0.0008  0.2129  96  ILE C CD1 
8938  N N   . GLU C 97  ? 0.7749 1.3453 0.8930 -0.0586 0.0303  0.1698  97  GLU C N   
8939  C CA  . GLU C 97  ? 0.7675 1.3071 0.8603 -0.0429 0.0409  0.1584  97  GLU C CA  
8940  C C   . GLU C 97  ? 0.7690 1.2623 0.8448 -0.0306 0.0305  0.1486  97  GLU C C   
8941  O O   . GLU C 97  ? 0.7655 1.2443 0.8350 -0.0093 0.0375  0.1388  97  GLU C O   
8942  C CB  . GLU C 97  ? 0.8740 1.3957 0.9402 -0.0605 0.0453  0.1608  97  GLU C CB  
8943  C CG  . GLU C 97  ? 0.9674 1.5288 1.0396 -0.0619 0.0643  0.1650  97  GLU C CG  
8944  C CD  . GLU C 97  ? 0.9890 1.5733 1.0739 -0.0340 0.0803  0.1546  97  GLU C CD  
8945  O OE1 . GLU C 97  ? 1.0558 1.6065 1.1258 -0.0149 0.0801  0.1419  97  GLU C OE1 
8946  O OE2 . GLU C 97  ? 0.9661 1.6024 1.0778 -0.0311 0.0931  0.1589  97  GLU C OE2 
8947  N N   . PHE C 98  ? 0.7210 1.1911 0.7893 -0.0442 0.0140  0.1507  98  PHE C N   
8948  C CA  . PHE C 98  ? 0.7284 1.1591 0.7818 -0.0340 0.0047  0.1424  98  PHE C CA  
8949  C C   . PHE C 98  ? 0.7887 1.2364 0.8629 -0.0136 0.0038  0.1418  98  PHE C C   
8950  O O   . PHE C 98  ? 0.7084 1.1293 0.7731 0.0027  0.0032  0.1344  98  PHE C O   
8951  C CB  . PHE C 98  ? 0.6566 1.0656 0.6998 -0.0532 -0.0116 0.1438  98  PHE C CB  
8952  C CG  . PHE C 98  ? 0.7556 1.1171 0.7746 -0.0481 -0.0179 0.1341  98  PHE C CG  
8953  C CD1 . PHE C 98  ? 0.8284 1.1561 0.8247 -0.0459 -0.0128 0.1276  98  PHE C CD1 
8954  C CD2 . PHE C 98  ? 0.7502 1.1031 0.7695 -0.0460 -0.0291 0.1321  98  PHE C CD2 
8955  C CE1 . PHE C 98  ? 0.8142 1.1014 0.7919 -0.0413 -0.0185 0.1191  98  PHE C CE1 
8956  C CE2 . PHE C 98  ? 0.7214 1.0344 0.7199 -0.0418 -0.0336 0.1234  98  PHE C CE2 
8957  C CZ  . PHE C 98  ? 0.8052 1.0859 0.7846 -0.0391 -0.0281 0.1168  98  PHE C CZ  
8958  N N   . THR C 99  ? 0.8006 1.2933 0.9054 -0.0148 0.0025  0.1508  99  THR C N   
8959  C CA  . THR C 99  ? 0.7753 1.2868 0.9041 0.0046  -0.0001 0.1526  99  THR C CA  
8960  C C   . THR C 99  ? 0.7352 1.2543 0.8735 0.0291  0.0157  0.1457  99  THR C C   
8961  O O   . THR C 99  ? 0.7688 1.2769 0.9136 0.0491  0.0137  0.1422  99  THR C O   
8962  C CB  . THR C 99  ? 0.7371 1.2965 0.8984 -0.0041 -0.0072 0.1649  99  THR C CB  
8963  O OG1 . THR C 99  ? 0.6513 1.2040 0.8014 -0.0303 -0.0202 0.1693  99  THR C OG1 
8964  C CG2 . THR C 99  ? 0.7177 1.2880 0.8996 0.0121  -0.0165 0.1689  99  THR C CG2 
8965  N N   . LYS C 100 ? 0.7371 1.2743 0.8756 0.0275  0.0313  0.1436  100 LYS C N   
8966  C CA  . LYS C 100 ? 0.7557 1.2990 0.8999 0.0507  0.0475  0.1339  100 LYS C CA  
8967  C C   . LYS C 100 ? 0.6362 1.1276 0.7489 0.0610  0.0482  0.1214  100 LYS C C   
8968  O O   . LYS C 100 ? 0.6635 1.1476 0.7824 0.0839  0.0540  0.1126  100 LYS C O   
8969  C CB  . LYS C 100 ? 0.7135 1.2906 0.8614 0.0445  0.0650  0.1342  100 LYS C CB  
8970  C CG  . LYS C 100 ? 0.7282 1.3364 0.8997 0.0690  0.0819  0.1265  100 LYS C CG  
8971  C CD  . LYS C 100 ? 0.7803 1.4344 0.9614 0.0607  0.0996  0.1293  100 LYS C CD  
8972  C CE  . LYS C 100 ? 0.7410 1.4279 0.9385 0.0352  0.0919  0.1464  100 LYS C CE  
8973  N NZ  . LYS C 100 ? 0.8400 1.5607 1.0354 0.0205  0.1081  0.1507  100 LYS C NZ  
8974  N N   . LEU C 101 ? 0.7135 1.1684 0.7945 0.0446  0.0417  0.1204  101 LEU C N   
8975  C CA  . LEU C 101 ? 0.7607 1.1673 0.8134 0.0525  0.0409  0.1097  101 LEU C CA  
8976  C C   . LEU C 101 ? 0.7493 1.1344 0.8075 0.0663  0.0302  0.1081  101 LEU C C   
8977  O O   . LEU C 101 ? 0.6821 1.0460 0.7359 0.0843  0.0337  0.0991  101 LEU C O   
8978  C CB  . LEU C 101 ? 0.6606 1.0359 0.6837 0.0316  0.0344  0.1107  101 LEU C CB  
8979  C CG  . LEU C 101 ? 0.8661 1.1920 0.8631 0.0379  0.0303  0.1012  101 LEU C CG  
8980  C CD1 . LEU C 101 ? 0.9519 1.2695 0.9365 0.0515  0.0431  0.0908  101 LEU C CD1 
8981  C CD2 . LEU C 101 ? 0.9483 1.2454 0.9232 0.0181  0.0212  0.1032  101 LEU C CD2 
8982  N N   . ASN C 102 ? 0.7347 1.1250 0.8017 0.0569  0.0165  0.1171  102 ASN C N   
8983  C CA  . ASN C 102 ? 0.7143 1.0861 0.7840 0.0660  0.0051  0.1184  102 ASN C CA  
8984  C C   . ASN C 102 ? 0.7386 1.1433 0.8427 0.0804  0.0024  0.1257  102 ASN C C   
8985  O O   . ASN C 102 ? 0.7696 1.1667 0.8788 0.0841  -0.0097 0.1314  102 ASN C O   
8986  C CB  . ASN C 102 ? 0.7989 1.1546 0.8534 0.0468  -0.0088 0.1228  102 ASN C CB  
8987  C CG  . ASN C 102 ? 0.7608 1.0904 0.7881 0.0307  -0.0073 0.1174  102 ASN C CG  
8988  O OD1 . ASN C 102 ? 0.7854 1.0823 0.7931 0.0358  -0.0037 0.1092  102 ASN C OD1 
8989  N ND2 . ASN C 102 ? 0.7917 1.1354 0.8193 0.0107  -0.0114 0.1226  102 ASN C ND2 
8990  N N   . TYR C 103 ? 0.7916 1.2336 0.9200 0.0890  0.0136  0.1260  103 TYR C N   
8991  C CA  . TYR C 103 ? 0.7215 1.2011 0.8885 0.1016  0.0104  0.1344  103 TYR C CA  
8992  C C   . TYR C 103 ? 0.7377 1.1975 0.9143 0.1250  0.0064  0.1319  103 TYR C C   
8993  O O   . TYR C 103 ? 0.8136 1.2766 1.0041 0.1275  -0.0078 0.1424  103 TYR C O   
8994  C CB  . TYR C 103 ? 0.7218 1.2460 0.9134 0.1072  0.0261  0.1330  103 TYR C CB  
8995  C CG  . TYR C 103 ? 0.8352 1.4017 1.0721 0.1233  0.0247  0.1405  103 TYR C CG  
8996  C CD1 . TYR C 103 ? 0.7972 1.4022 1.0582 0.1108  0.0144  0.1551  103 TYR C CD1 
8997  C CD2 . TYR C 103 ? 0.8170 1.3850 1.0742 0.1511  0.0329  0.1325  103 TYR C CD2 
8998  C CE1 . TYR C 103 ? 0.8517 1.4972 1.1570 0.1258  0.0118  0.1631  103 TYR C CE1 
8999  C CE2 . TYR C 103 ? 0.8724 1.4790 1.1748 0.1674  0.0309  0.1395  103 TYR C CE2 
9000  C CZ  . TYR C 103 ? 0.9033 1.5497 1.2304 0.1547  0.0202  0.1555  103 TYR C CZ  
9001  O OH  . TYR C 103 ? 0.8545 1.5415 1.2296 0.1710  0.0169  0.1638  103 TYR C OH  
9002  N N   . GLU C 104 ? 0.6636 1.1016 0.8323 0.1413  0.0178  0.1186  104 GLU C N   
9003  C CA  . GLU C 104 ? 0.7532 1.1705 0.9334 0.1644  0.0147  0.1151  104 GLU C CA  
9004  C C   . GLU C 104 ? 0.8588 1.2303 1.0146 0.1599  0.0018  0.1168  104 GLU C C   
9005  O O   . GLU C 104 ? 0.8764 1.2231 1.0368 0.1768  -0.0010 0.1135  104 GLU C O   
9006  C CB  . GLU C 104 ? 0.7245 1.1343 0.9039 0.1826  0.0314  0.0980  104 GLU C CB  
9007  C CG  . GLU C 104 ? 0.8345 1.2895 1.0303 0.1835  0.0477  0.0943  104 GLU C CG  
9008  C CD  . GLU C 104 ? 0.9543 1.4097 1.1579 0.2067  0.0640  0.0772  104 GLU C CD  
9009  O OE1 . GLU C 104 ? 0.9648 1.4619 1.2033 0.2205  0.0734  0.0761  104 GLU C OE1 
9010  O OE2 . GLU C 104 ? 0.8185 1.2336 0.9942 0.2111  0.0673  0.0639  104 GLU C OE2 
9011  N N   . LYS C 105 ? 0.8492 1.2095 0.9809 0.1378  -0.0059 0.1217  105 LYS C N   
9012  C CA  . LYS C 105 ? 0.8027 1.1246 0.9126 0.1327  -0.0168 0.1235  105 LYS C CA  
9013  C C   . LYS C 105 ? 0.7930 1.1272 0.9198 0.1329  -0.0322 0.1389  105 LYS C C   
9014  O O   . LYS C 105 ? 0.8062 1.1763 0.9498 0.1254  -0.0371 0.1486  105 LYS C O   
9015  C CB  . LYS C 105 ? 0.8224 1.1283 0.9013 0.1103  -0.0179 0.1207  105 LYS C CB  
9016  C CG  . LYS C 105 ? 0.8950 1.1881 0.9561 0.1087  -0.0050 0.1082  105 LYS C CG  
9017  C CD  . LYS C 105 ? 0.8431 1.1188 0.8770 0.0874  -0.0076 0.1065  105 LYS C CD  
9018  C CE  . LYS C 105 ? 0.8469 1.1088 0.8624 0.0855  0.0035  0.0961  105 LYS C CE  
9019  N NZ  . LYS C 105 ? 0.9001 1.1465 0.8932 0.0653  0.0003  0.0956  105 LYS C NZ  
9020  N N   . PRO C 106 ? 0.8327 1.1389 0.9553 0.1404  -0.0405 0.1423  106 PRO C N   
9021  C CA  . PRO C 106 ? 0.8007 1.1189 0.9390 0.1412  -0.0559 0.1590  106 PRO C CA  
9022  C C   . PRO C 106 ? 0.8092 1.1426 0.9342 0.1185  -0.0657 0.1679  106 PRO C C   
9023  O O   . PRO C 106 ? 0.7381 1.0981 0.8808 0.1168  -0.0774 0.1822  106 PRO C O   
9024  C CB  . PRO C 106 ? 0.8457 1.1238 0.9734 0.1490  -0.0612 0.1597  106 PRO C CB  
9025  C CG  . PRO C 106 ? 0.8365 1.0919 0.9608 0.1625  -0.0479 0.1429  106 PRO C CG  
9026  C CD  . PRO C 106 ? 0.8530 1.1173 0.9598 0.1496  -0.0367 0.1322  106 PRO C CD  
9027  N N   . ILE C 107 ? 0.8147 1.1319 0.9097 0.1012  -0.0622 0.1595  107 ILE C N   
9028  C CA  . ILE C 107 ? 0.8452 1.1741 0.9261 0.0796  -0.0709 0.1645  107 ILE C CA  
9029  C C   . ILE C 107 ? 0.7911 1.1604 0.8895 0.0711  -0.0714 0.1684  107 ILE C C   
9030  O O   . ILE C 107 ? 0.7419 1.1265 0.8345 0.0543  -0.0815 0.1743  107 ILE C O   
9031  C CB  . ILE C 107 ? 0.8425 1.1408 0.8898 0.0653  -0.0665 0.1526  107 ILE C CB  
9032  C CG1 . ILE C 107 ? 0.8327 1.1318 0.8769 0.0620  -0.0543 0.1416  107 ILE C CG1 
9033  C CG2 . ILE C 107 ? 0.8173 1.0781 0.8502 0.0733  -0.0656 0.1491  107 ILE C CG2 
9034  C CD1 . ILE C 107 ? 0.8327 1.0997 0.8479 0.0508  -0.0503 0.1302  107 ILE C CD1 
9035  N N   . TYR C 108 ? 0.7560 1.1442 0.8754 0.0816  -0.0607 0.1648  108 TYR C N   
9036  C CA  . TYR C 108 ? 0.6869 1.1174 0.8274 0.0741  -0.0598 0.1696  108 TYR C CA  
9037  C C   . TYR C 108 ? 0.7528 1.2191 0.9329 0.0895  -0.0647 0.1813  108 TYR C C   
9038  O O   . TYR C 108 ? 0.8193 1.3228 1.0257 0.0915  -0.0589 0.1833  108 TYR C O   
9039  C CB  . TYR C 108 ? 0.7200 1.1534 0.8580 0.0732  -0.0434 0.1587  108 TYR C CB  
9040  C CG  . TYR C 108 ? 0.7335 1.1556 0.8455 0.0499  -0.0428 0.1536  108 TYR C CG  
9041  C CD1 . TYR C 108 ? 0.7643 1.1439 0.8442 0.0446  -0.0414 0.1441  108 TYR C CD1 
9042  C CD2 . TYR C 108 ? 0.7041 1.1576 0.8260 0.0332  -0.0444 0.1585  108 TYR C CD2 
9043  C CE1 . TYR C 108 ? 0.7256 1.0929 0.7847 0.0248  -0.0419 0.1394  108 TYR C CE1 
9044  C CE2 . TYR C 108 ? 0.6847 1.1242 0.7844 0.0119  -0.0452 0.1539  108 TYR C CE2 
9045  C CZ  . TYR C 108 ? 0.6537 1.0493 0.7224 0.0086  -0.0440 0.1441  108 TYR C CZ  
9046  O OH  . TYR C 108 ? 0.6276 1.0071 0.6770 -0.0109 -0.0457 0.1394  108 TYR C OH  
9047  N N   . ARG C 109 ? 0.7897 1.2464 0.9763 0.1002  -0.0756 0.1902  109 ARG C N   
9048  C CA  . ARG C 109 ? 0.7506 1.2379 0.9772 0.1165  -0.0826 0.2028  109 ARG C CA  
9049  C C   . ARG C 109 ? 0.6917 1.2135 0.9290 0.1012  -0.0994 0.2185  109 ARG C C   
9050  O O   . ARG C 109 ? 0.7162 1.2404 0.9595 0.1030  -0.1153 0.2326  109 ARG C O   
9051  C CB  . ARG C 109 ? 0.7516 1.2107 0.9822 0.1351  -0.0880 0.2068  109 ARG C CB  
9052  C CG  . ARG C 109 ? 0.7744 1.2423 1.0411 0.1627  -0.0797 0.2035  109 ARG C CG  
9053  C CD  . ARG C 109 ? 0.7741 1.2181 1.0526 0.1806  -0.0898 0.2117  109 ARG C CD  
9054  N NE  . ARG C 109 ? 0.7813 1.1766 1.0245 0.1760  -0.0906 0.2066  109 ARG C NE  
9055  C CZ  . ARG C 109 ? 0.8127 1.1743 1.0468 0.1882  -0.0793 0.1917  109 ARG C CZ  
9056  N NH1 . ARG C 109 ? 0.8419 1.2114 1.0947 0.2052  -0.0650 0.1783  109 ARG C NH1 
9057  N NH2 . ARG C 109 ? 0.8537 1.1742 1.0592 0.1828  -0.0824 0.1899  109 ARG C NH2 
9058  N N   . PHE C 110 ? 0.6612 1.2100 0.9002 0.0847  -0.0967 0.2166  110 PHE C N   
9059  C CA  . PHE C 110 ? 0.6982 1.2849 0.9512 0.0694  -0.1120 0.2301  110 PHE C CA  
9060  C C   . PHE C 110 ? 0.6960 1.3317 0.9958 0.0795  -0.1075 0.2359  110 PHE C C   
9061  O O   . PHE C 110 ? 0.6700 1.3152 0.9775 0.0826  -0.0903 0.2260  110 PHE C O   
9062  C CB  . PHE C 110 ? 0.6461 1.2273 0.8682 0.0409  -0.1145 0.2241  110 PHE C CB  
9063  C CG  . PHE C 110 ? 0.7375 1.2771 0.9174 0.0305  -0.1197 0.2185  110 PHE C CG  
9064  C CD1 . PHE C 110 ? 0.8039 1.3350 0.9770 0.0336  -0.1334 0.2288  110 PHE C CD1 
9065  C CD2 . PHE C 110 ? 0.7870 1.2970 0.9349 0.0177  -0.1109 0.2038  110 PHE C CD2 
9066  C CE1 . PHE C 110 ? 0.8337 1.3299 0.9682 0.0237  -0.1364 0.2234  110 PHE C CE1 
9067  C CE2 . PHE C 110 ? 0.6105 1.0847 0.7226 0.0093  -0.1145 0.1977  110 PHE C CE2 
9068  C CZ  . PHE C 110 ? 0.6982 1.1668 0.8033 0.0122  -0.1264 0.2070  110 PHE C CZ  
9069  N N   . GLU C 111 ? 0.7470 1.4155 1.0784 0.0845  -0.1231 0.2527  111 GLU C N   
9070  C CA  . GLU C 111 ? 0.7017 1.4202 1.0838 0.0968  -0.1195 0.2593  111 GLU C CA  
9071  C C   . GLU C 111 ? 0.7169 1.4686 1.1041 0.0763  -0.1139 0.2570  111 GLU C C   
9072  O O   . GLU C 111 ? 0.7112 1.4914 1.1262 0.0851  -0.0983 0.2526  111 GLU C O   
9073  C CB  . GLU C 111 ? 0.6109 1.3582 1.0258 0.1036  -0.1407 0.2799  111 GLU C CB  
9074  C CG  . GLU C 111 ? 0.7124 1.4946 1.1843 0.1316  -0.1357 0.2851  111 GLU C CG  
9075  C CD  . GLU C 111 ? 0.8421 1.6803 1.3505 0.1266  -0.1280 0.2862  111 GLU C CD  
9076  O OE1 . GLU C 111 ? 0.8553 1.7109 1.3506 0.0995  -0.1341 0.2893  111 GLU C OE1 
9077  O OE2 . GLU C 111 ? 0.6825 1.5485 1.2340 0.1497  -0.1159 0.2840  111 GLU C OE2 
9078  N N   . ARG C 112 ? 0.6945 1.4431 1.0552 0.0485  -0.1263 0.2596  112 ARG C N   
9079  C CA  . ARG C 112 ? 0.6724 1.4471 1.0357 0.0263  -0.1228 0.2577  112 ARG C CA  
9080  C C   . ARG C 112 ? 0.6443 1.4028 0.9944 0.0275  -0.0994 0.2424  112 ARG C C   
9081  O O   . ARG C 112 ? 0.6831 1.4762 1.0559 0.0226  -0.0891 0.2429  112 ARG C O   
9082  C CB  . ARG C 112 ? 0.6585 1.4193 0.9879 -0.0030 -0.1395 0.2586  112 ARG C CB  
9083  C CG  . ARG C 112 ? 0.7215 1.5025 1.0511 -0.0285 -0.1385 0.2566  112 ARG C CG  
9084  C CD  . ARG C 112 ? 0.7447 1.5877 1.1231 -0.0315 -0.1455 0.2712  112 ARG C CD  
9085  N NE  . ARG C 112 ? 0.7596 1.6184 1.1318 -0.0628 -0.1594 0.2746  112 ARG C NE  
9086  C CZ  . ARG C 112 ? 0.6620 1.5723 1.0715 -0.0738 -0.1641 0.2852  112 ARG C CZ  
9087  N NH1 . ARG C 112 ? 0.6613 1.6163 1.1192 -0.0555 -0.1553 0.2937  112 ARG C NH1 
9088  N NH2 . ARG C 112 ? 0.6631 1.5806 1.0623 -0.1040 -0.1781 0.2867  112 ARG C NH2 
9089  N N   . ILE C 113 ? 0.6918 1.3995 1.0056 0.0331  -0.0911 0.2297  113 ILE C N   
9090  C CA  . ILE C 113 ? 0.6715 1.3622 0.9707 0.0348  -0.0702 0.2160  113 ILE C CA  
9091  C C   . ILE C 113 ? 0.6867 1.4070 1.0217 0.0580  -0.0535 0.2143  113 ILE C C   
9092  O O   . ILE C 113 ? 0.7793 1.5182 1.1201 0.0539  -0.0378 0.2095  113 ILE C O   
9093  C CB  . ILE C 113 ? 0.6530 1.2849 0.9099 0.0385  -0.0664 0.2037  113 ILE C CB  
9094  C CG1 . ILE C 113 ? 0.7614 1.3662 0.9812 0.0123  -0.0755 0.2000  113 ILE C CG1 
9095  C CG2 . ILE C 113 ? 0.6685 1.2860 0.9191 0.0509  -0.0451 0.1910  113 ILE C CG2 
9096  C CD1 . ILE C 113 ? 0.6861 1.2419 0.8712 0.0150  -0.0799 0.1932  113 ILE C CD1 
9097  N N   . ARG C 114 ? 0.6300 1.3546 0.9892 0.0828  -0.0565 0.2180  114 ARG C N   
9098  C CA  . ARG C 114 ? 0.7390 1.4946 1.1376 0.1074  -0.0416 0.2154  114 ARG C CA  
9099  C C   . ARG C 114 ? 0.7273 1.5451 1.1649 0.0991  -0.0389 0.2244  114 ARG C C   
9100  O O   . ARG C 114 ? 0.5939 1.4356 1.0436 0.1023  -0.0192 0.2175  114 ARG C O   
9101  C CB  . ARG C 114 ? 0.7033 1.4543 1.1265 0.1333  -0.0508 0.2210  114 ARG C CB  
9102  C CG  . ARG C 114 ? 0.7619 1.4847 1.1846 0.1608  -0.0357 0.2066  114 ARG C CG  
9103  C CD  . ARG C 114 ? 0.9337 1.5944 1.3055 0.1559  -0.0348 0.1957  114 ARG C CD  
9104  N NE  . ARG C 114 ? 0.9434 1.5778 1.3132 0.1797  -0.0200 0.1803  114 ARG C NE  
9105  C CZ  . ARG C 114 ? 0.9723 1.5545 1.3121 0.1849  -0.0217 0.1728  114 ARG C CZ  
9106  N NH1 . ARG C 114 ? 0.9738 1.5250 1.2826 0.1688  -0.0359 0.1789  114 ARG C NH1 
9107  N NH2 . ARG C 114 ? 0.9428 1.5046 1.2843 0.2066  -0.0088 0.1581  114 ARG C NH2 
9108  N N   . GLU C 115 ? 0.7469 1.5933 1.2044 0.0874  -0.0588 0.2404  115 GLU C N   
9109  C CA  . GLU C 115 ? 0.6892 1.5979 1.1883 0.0788  -0.0589 0.2509  115 GLU C CA  
9110  C C   . GLU C 115 ? 0.7107 1.6261 1.1905 0.0515  -0.0498 0.2472  115 GLU C C   
9111  O O   . GLU C 115 ? 0.7022 1.6617 1.2103 0.0501  -0.0357 0.2486  115 GLU C O   
9112  C CB  . GLU C 115 ? 0.6762 1.6096 1.1956 0.0694  -0.0854 0.2691  115 GLU C CB  
9113  C CG  . GLU C 115 ? 0.8397 1.8183 1.3759 0.0422  -0.0930 0.2794  115 GLU C CG  
9114  C CD  . GLU C 115 ? 0.8737 1.8633 1.4128 0.0265  -0.1221 0.2948  115 GLU C CD  
9115  O OE1 . GLU C 115 ? 0.8774 1.9037 1.4315 0.0035  -0.1316 0.3037  115 GLU C OE1 
9116  O OE2 . GLU C 115 ? 0.7613 1.7231 1.2865 0.0359  -0.1360 0.2983  115 GLU C OE2 
9117  N N   . LEU C 116 ? 0.6876 1.5595 1.1201 0.0298  -0.0573 0.2428  116 LEU C N   
9118  C CA  . LEU C 116 ? 0.6905 1.5644 1.1052 0.0025  -0.0521 0.2409  116 LEU C CA  
9119  C C   . LEU C 116 ? 0.7250 1.5996 1.1355 0.0100  -0.0261 0.2306  116 LEU C C   
9120  O O   . LEU C 116 ? 0.6324 1.5381 1.0536 -0.0059 -0.0172 0.2344  116 LEU C O   
9121  C CB  . LEU C 116 ? 0.6728 1.4942 1.0381 -0.0178 -0.0646 0.2356  116 LEU C CB  
9122  C CG  . LEU C 116 ? 0.6613 1.4899 1.0258 -0.0373 -0.0897 0.2454  116 LEU C CG  
9123  C CD1 . LEU C 116 ? 0.6385 1.4289 0.9610 -0.0638 -0.0965 0.2383  116 LEU C CD1 
9124  C CD2 . LEU C 116 ? 0.7035 1.5947 1.1137 -0.0460 -0.0968 0.2600  116 LEU C CD2 
9125  N N   . MET C 117 ? 0.7250 1.5666 1.1197 0.0332  -0.0141 0.2182  117 MET C N   
9126  C CA  . MET C 117 ? 0.6750 1.5141 1.0600 0.0403  0.0101  0.2069  117 MET C CA  
9127  C C   . MET C 117 ? 0.7248 1.6253 1.1563 0.0530  0.0262  0.2098  117 MET C C   
9128  O O   . MET C 117 ? 0.7943 1.7124 1.2226 0.0470  0.0450  0.2059  117 MET C O   
9129  C CB  . MET C 117 ? 0.7345 1.5243 1.0935 0.0626  0.0168  0.1925  117 MET C CB  
9130  C CG  . MET C 117 ? 0.7756 1.5047 1.0847 0.0495  0.0079  0.1865  117 MET C CG  
9131  S SD  . MET C 117 ? 0.7927 1.5141 1.0753 0.0117  0.0013  0.1914  117 MET C SD  
9132  C CE  . MET C 117 ? 0.5873 1.2888 0.8418 0.0117  0.0236  0.1798  117 MET C CE  
9133  N N   . ASN C 118 ? 0.7486 1.6835 1.2241 0.0705  0.0192  0.2171  118 ASN C N   
9134  C CA  . ASN C 118 ? 0.7287 1.7254 1.2544 0.0853  0.0347  0.2191  118 ASN C CA  
9135  C C   . ASN C 118 ? 0.6176 1.6690 1.1686 0.0600  0.0334  0.2332  118 ASN C C   
9136  O O   . ASN C 118 ? 0.7183 1.8224 1.3041 0.0663  0.0514  0.2337  118 ASN C O   
9137  C CB  . ASN C 118 ? 0.6826 1.6971 1.2509 0.1134  0.0258  0.2233  118 ASN C CB  
9138  C CG  . ASN C 118 ? 0.7969 1.7591 1.3451 0.1390  0.0269  0.2103  118 ASN C CG  
9139  O OD1 . ASN C 118 ? 0.8102 1.7169 1.3091 0.1315  0.0257  0.2018  118 ASN C OD1 
9140  N ND2 . ASN C 118 ? 0.7281 1.7079 1.3168 0.1695  0.0289  0.2089  118 ASN C ND2 
9141  N N   . LYS C 119 ? 0.6085 1.6492 1.1434 0.0312  0.0131  0.2437  119 LYS C N   
9142  C CA  . LYS C 119 ? 0.7500 1.8388 1.3077 0.0043  0.0097  0.2574  119 LYS C CA  
9143  C C   . LYS C 119 ? 0.7542 1.8408 1.2879 -0.0137 0.0285  0.2532  119 LYS C C   
9144  O O   . LYS C 119 ? 0.7277 1.7601 1.2123 -0.0241 0.0285  0.2452  119 LYS C O   
9145  C CB  . LYS C 119 ? 0.6475 1.7206 1.1921 -0.0214 -0.0189 0.2677  119 LYS C CB  
9146  C CG  . LYS C 119 ? 0.5818 1.7106 1.1758 -0.0262 -0.0359 0.2844  119 LYS C CG  
9147  C CD  . LYS C 119 ? 0.7248 1.9093 1.3482 -0.0489 -0.0293 0.2949  119 LYS C CD  
9148  C CE  . LYS C 119 ? 0.6307 1.8570 1.2884 -0.0670 -0.0535 0.3121  119 LYS C CE  
9149  N NZ  . LYS C 119 ? 0.5841 1.8706 1.2776 -0.0872 -0.0457 0.3233  119 LYS C NZ  
9150  N N   . GLU C 120 ? 0.8124 1.9599 1.3820 -0.0178 0.0443  0.2597  120 GLU C N   
9151  C CA  . GLU C 120 ? 0.8384 1.9903 1.3875 -0.0365 0.0624  0.2587  120 GLU C CA  
9152  C C   . GLU C 120 ? 0.9016 2.0303 1.4241 -0.0746 0.0453  0.2685  120 GLU C C   
9153  O O   . GLU C 120 ? 0.8979 1.9919 1.3807 -0.0897 0.0519  0.2647  120 GLU C O   
9154  C CB  . GLU C 120 ? 0.9444 2.1729 1.5414 -0.0329 0.0832  0.2649  120 GLU C CB  
9155  C CG  . GLU C 120 ? 1.0145 2.2559 1.5925 -0.0511 0.1052  0.2655  120 GLU C CG  
9156  C CD  . GLU C 120 ? 1.0197 2.2742 1.5961 -0.0921 0.0935  0.2831  120 GLU C CD  
9157  O OE1 . GLU C 120 ? 0.8781 2.1324 1.4320 -0.1108 0.1073  0.2858  120 GLU C OE1 
9158  O OE2 . GLU C 120 ? 1.0628 2.3280 1.6606 -0.1060 0.0701  0.2946  120 GLU C OE2 
9159  N N   . LYS C 121 ? 0.8813 2.0274 1.4254 -0.0906 0.0223  0.2808  121 LYS C N   
9160  C CA  . LYS C 121 ? 0.8681 1.9921 1.3906 -0.1265 0.0035  0.2885  121 LYS C CA  
9161  C C   . LYS C 121 ? 0.7741 1.8606 1.2813 -0.1276 -0.0236 0.2866  121 LYS C C   
9162  O O   . LYS C 121 ? 0.7836 1.8858 1.3144 -0.1079 -0.0317 0.2878  121 LYS C O   
9163  C CB  . LYS C 121 ? 0.7163 1.9033 1.2798 -0.1517 0.0009  0.3061  121 LYS C CB  
9164  C CG  . LYS C 121 ? 0.7149 1.8856 1.2543 -0.1878 -0.0012 0.3126  121 LYS C CG  
9165  C CD  . LYS C 121 ? 0.7335 1.9512 1.3091 -0.2177 -0.0164 0.3303  121 LYS C CD  
9166  C CE  . LYS C 121 ? 0.7338 2.0304 1.3588 -0.2173 0.0037  0.3422  121 LYS C CE  
9167  N NZ  . LYS C 121 ? 0.6411 1.9654 1.2789 -0.2564 -0.0008 0.3589  121 LYS C NZ  
9168  N N   . LEU C 122 ? 0.6569 1.6935 1.1239 -0.1508 -0.0374 0.2836  122 LEU C N   
9169  C CA  . LEU C 122 ? 0.7565 1.7516 1.1998 -0.1527 -0.0604 0.2787  122 LEU C CA  
9170  C C   . LEU C 122 ? 0.6978 1.6887 1.1351 -0.1882 -0.0817 0.2853  122 LEU C C   
9171  O O   . LEU C 122 ? 0.7404 1.7130 1.1596 -0.2107 -0.0791 0.2855  122 LEU C O   
9172  C CB  . LEU C 122 ? 0.7358 1.6625 1.1297 -0.1403 -0.0557 0.2627  122 LEU C CB  
9173  C CG  . LEU C 122 ? 0.7502 1.6658 1.1420 -0.1047 -0.0403 0.2532  122 LEU C CG  
9174  C CD1 . LEU C 122 ? 0.6569 1.5994 1.0802 -0.0847 -0.0503 0.2582  122 LEU C CD1 
9175  C CD2 . LEU C 122 ? 0.8213 1.7593 1.2230 -0.0927 -0.0132 0.2506  122 LEU C CD2 
9176  N N   . ASN C 123 ? 0.6163 1.6230 1.0685 -0.1936 -0.1037 0.2908  123 ASN C N   
9177  C CA  . ASN C 123 ? 0.6305 1.6342 1.0776 -0.2271 -0.1258 0.2954  123 ASN C CA  
9178  C C   . ASN C 123 ? 0.6727 1.6072 1.0677 -0.2350 -0.1379 0.2808  123 ASN C C   
9179  O O   . ASN C 123 ? 0.6906 1.5817 1.0550 -0.2159 -0.1283 0.2688  123 ASN C O   
9180  C CB  . ASN C 123 ? 0.7014 1.7552 1.1866 -0.2313 -0.1451 0.3078  123 ASN C CB  
9181  C CG  . ASN C 123 ? 0.6645 1.7018 1.1389 -0.2115 -0.1579 0.3036  123 ASN C CG  
9182  O OD1 . ASN C 123 ? 0.7297 1.7227 1.1727 -0.1918 -0.1501 0.2918  123 ASN C OD1 
9183  N ND2 . ASN C 123 ? 0.7636 1.8381 1.2645 -0.2180 -0.1787 0.3146  123 ASN C ND2 
9184  N N   . ARG C 124 ? 0.7159 1.6408 1.1019 -0.2637 -0.1594 0.2812  124 ARG C N   
9185  C CA  . ARG C 124 ? 0.7704 1.6335 1.1096 -0.2718 -0.1716 0.2658  124 ARG C CA  
9186  C C   . ARG C 124 ? 0.7391 1.5869 1.0624 -0.2502 -0.1782 0.2592  124 ARG C C   
9187  O O   . ARG C 124 ? 0.8633 1.6591 1.1477 -0.2422 -0.1761 0.2450  124 ARG C O   
9188  C CB  . ARG C 124 ? 0.8075 1.6682 1.1438 -0.3065 -0.1943 0.2664  124 ARG C CB  
9189  C CG  . ARG C 124 ? 0.8288 1.6239 1.1180 -0.3180 -0.2036 0.2483  124 ARG C CG  
9190  C CD  . ARG C 124 ? 0.8250 1.6185 1.1123 -0.3510 -0.2278 0.2469  124 ARG C CD  
9191  N NE  . ARG C 124 ? 0.9029 1.6475 1.1488 -0.3546 -0.2411 0.2281  124 ARG C NE  
9192  C CZ  . ARG C 124 ? 0.8699 1.6192 1.1044 -0.3457 -0.2522 0.2241  124 ARG C CZ  
9193  N NH1 . ARG C 124 ? 0.8671 1.6659 1.1303 -0.3326 -0.2541 0.2385  124 ARG C NH1 
9194  N NH2 . ARG C 124 ? 0.9641 1.6680 1.1582 -0.3499 -0.2614 0.2056  124 ARG C NH2 
9195  N N   . GLU C 125 ? 0.7171 1.6107 1.0715 -0.2411 -0.1868 0.2705  125 GLU C N   
9196  C CA  . GLU C 125 ? 0.6519 1.5342 0.9936 -0.2218 -0.1947 0.2679  125 GLU C CA  
9197  C C   . GLU C 125 ? 0.7192 1.5750 1.0485 -0.1909 -0.1743 0.2609  125 GLU C C   
9198  O O   . GLU C 125 ? 0.8118 1.6215 1.1042 -0.1829 -0.1753 0.2495  125 GLU C O   
9199  C CB  . GLU C 125 ? 0.6800 1.6207 1.0640 -0.2171 -0.2077 0.2846  125 GLU C CB  
9200  C CG  . GLU C 125 ? 0.8958 1.8586 1.2855 -0.2469 -0.2341 0.2907  125 GLU C CG  
9201  C CD  . GLU C 125 ? 0.9734 1.9456 1.3725 -0.2763 -0.2347 0.2918  125 GLU C CD  
9202  O OE1 . GLU C 125 ? 0.8811 1.9003 1.3227 -0.2766 -0.2251 0.3044  125 GLU C OE1 
9203  O OE2 . GLU C 125 ? 0.9655 1.8980 1.3303 -0.2990 -0.2446 0.2800  125 GLU C OE2 
9204  N N   . GLU C 126 ? 0.6758 1.5611 1.0359 -0.1738 -0.1553 0.2669  126 GLU C N   
9205  C CA  . GLU C 126 ? 0.6946 1.5572 1.0455 -0.1441 -0.1362 0.2597  126 GLU C CA  
9206  C C   . GLU C 126 ? 0.7494 1.5547 1.0569 -0.1480 -0.1256 0.2447  126 GLU C C   
9207  O O   . GLU C 126 ? 0.6983 1.4647 0.9801 -0.1303 -0.1199 0.2351  126 GLU C O   
9208  C CB  . GLU C 126 ? 0.6836 1.5929 1.0769 -0.1270 -0.1176 0.2673  126 GLU C CB  
9209  C CG  . GLU C 126 ? 0.7718 1.7374 1.2132 -0.1160 -0.1269 0.2817  126 GLU C CG  
9210  C CD  . GLU C 126 ? 0.8195 1.8471 1.3093 -0.1184 -0.1158 0.2923  126 GLU C CD  
9211  O OE1 . GLU C 126 ? 0.9080 1.9367 1.3920 -0.1348 -0.1041 0.2905  126 GLU C OE1 
9212  O OE2 . GLU C 126 ? 0.7871 1.8638 1.3223 -0.1043 -0.1192 0.3032  126 GLU C OE2 
9213  N N   . LEU C 127 ? 0.7418 1.5409 1.0419 -0.1716 -0.1240 0.2436  127 LEU C N   
9214  C CA  . LEU C 127 ? 0.6942 1.4390 0.9554 -0.1765 -0.1163 0.2309  127 LEU C CA  
9215  C C   . LEU C 127 ? 0.7183 1.4147 0.9418 -0.1793 -0.1296 0.2187  127 LEU C C   
9216  O O   . LEU C 127 ? 0.7086 1.3623 0.9040 -0.1661 -0.1213 0.2076  127 LEU C O   
9217  C CB  . LEU C 127 ? 0.6748 1.4234 0.9384 -0.2040 -0.1162 0.2347  127 LEU C CB  
9218  C CG  . LEU C 127 ? 0.6941 1.4688 0.9761 -0.2001 -0.0952 0.2417  127 LEU C CG  
9219  C CD1 . LEU C 127 ? 0.8179 1.5697 1.0839 -0.2253 -0.0944 0.2421  127 LEU C CD1 
9220  C CD2 . LEU C 127 ? 0.7058 1.4663 0.9782 -0.1696 -0.0757 0.2344  127 LEU C CD2 
9221  N N   . LEU C 128 ? 0.6408 1.3449 0.8634 -0.1967 -0.1502 0.2203  128 LEU C N   
9222  C CA  . LEU C 128 ? 0.7022 1.3674 0.8898 -0.1987 -0.1624 0.2085  128 LEU C CA  
9223  C C   . LEU C 128 ? 0.7328 1.3854 0.9113 -0.1709 -0.1560 0.2064  128 LEU C C   
9224  O O   . LEU C 128 ? 0.7266 1.3343 0.8726 -0.1644 -0.1520 0.1939  128 LEU C O   
9225  C CB  . LEU C 128 ? 0.6872 1.3739 0.8791 -0.2187 -0.1855 0.2125  128 LEU C CB  
9226  C CG  . LEU C 128 ? 0.6990 1.3471 0.8552 -0.2400 -0.1996 0.1976  128 LEU C CG  
9227  C CD1 . LEU C 128 ? 0.6953 1.3122 0.8406 -0.2561 -0.1943 0.1890  128 LEU C CD1 
9228  C CD2 . LEU C 128 ? 0.7048 1.3846 0.8715 -0.2606 -0.2221 0.2036  128 LEU C CD2 
9229  N N   . ASP C 129 ? 0.6473 1.3394 0.8567 -0.1543 -0.1552 0.2189  129 ASP C N   
9230  C CA  . ASP C 129 ? 0.6655 1.3469 0.8704 -0.1285 -0.1515 0.2190  129 ASP C CA  
9231  C C   . ASP C 129 ? 0.6681 1.3188 0.8616 -0.1094 -0.1306 0.2103  129 ASP C C   
9232  O O   . ASP C 129 ? 0.6073 1.2223 0.7762 -0.0970 -0.1282 0.2027  129 ASP C O   
9233  C CB  . ASP C 129 ? 0.6166 1.3482 0.8627 -0.1151 -0.1565 0.2352  129 ASP C CB  
9234  C CG  . ASP C 129 ? 0.8868 1.6453 1.1398 -0.1324 -0.1802 0.2444  129 ASP C CG  
9235  O OD1 . ASP C 129 ? 0.9579 1.6981 1.1845 -0.1564 -0.1911 0.2368  129 ASP C OD1 
9236  O OD2 . ASP C 129 ? 0.8874 1.6847 1.1720 -0.1223 -0.1888 0.2588  129 ASP C OD2 
9237  N N   . LEU C 130 ? 0.6703 1.3351 0.8802 -0.1082 -0.1157 0.2114  130 LEU C N   
9238  C CA  . LEU C 130 ? 0.6432 1.2785 0.8387 -0.0926 -0.0968 0.2024  130 LEU C CA  
9239  C C   . LEU C 130 ? 0.7325 1.3138 0.8868 -0.1026 -0.0977 0.1891  130 LEU C C   
9240  O O   . LEU C 130 ? 0.7593 1.3060 0.8934 -0.0875 -0.0902 0.1806  130 LEU C O   
9241  C CB  . LEU C 130 ? 0.6261 1.2892 0.8431 -0.0935 -0.0813 0.2064  130 LEU C CB  
9242  C CG  . LEU C 130 ? 0.7029 1.3505 0.9139 -0.0721 -0.0608 0.1993  130 LEU C CG  
9243  C CD1 . LEU C 130 ? 0.6967 1.3710 0.9362 -0.0446 -0.0544 0.2029  130 LEU C CD1 
9244  C CD2 . LEU C 130 ? 0.6797 1.3394 0.8936 -0.0832 -0.0471 0.2005  130 LEU C CD2 
9245  N N   . GLN C 131 ? 0.6951 1.2684 0.8384 -0.1280 -0.1075 0.1868  131 GLN C N   
9246  C CA  . GLN C 131 ? 0.7847 1.3075 0.8922 -0.1374 -0.1102 0.1733  131 GLN C CA  
9247  C C   . GLN C 131 ? 0.7412 1.2397 0.8271 -0.1277 -0.1168 0.1662  131 GLN C C   
9248  O O   . GLN C 131 ? 0.7381 1.1997 0.8022 -0.1167 -0.1094 0.1568  131 GLN C O   
9249  C CB  . GLN C 131 ? 0.8157 1.3364 0.9191 -0.1661 -0.1228 0.1717  131 GLN C CB  
9250  C CG  . GLN C 131 ? 0.7000 1.2335 0.8177 -0.1803 -0.1168 0.1780  131 GLN C CG  
9251  C CD  . GLN C 131 ? 0.6848 1.2166 0.8015 -0.2094 -0.1324 0.1774  131 GLN C CD  
9252  O OE1 . GLN C 131 ? 0.7255 1.2718 0.8452 -0.2188 -0.1477 0.1778  131 GLN C OE1 
9253  N NE2 . GLN C 131 ? 0.7281 1.2404 0.8395 -0.2245 -0.1298 0.1766  131 GLN C NE2 
9254  N N   . THR C 132 ? 0.7629 1.2839 0.8551 -0.1326 -0.1313 0.1719  132 THR C N   
9255  C CA  . THR C 132 ? 0.7351 1.2357 0.8036 -0.1285 -0.1393 0.1664  132 THR C CA  
9256  C C   . THR C 132 ? 0.6812 1.1769 0.7526 -0.1025 -0.1309 0.1701  132 THR C C   
9257  O O   . THR C 132 ? 0.7019 1.1669 0.7488 -0.0961 -0.1301 0.1628  132 THR C O   
9258  C CB  . THR C 132 ? 0.6533 1.1828 0.7270 -0.1422 -0.1581 0.1733  132 THR C CB  
9259  O OG1 . THR C 132 ? 0.6564 1.1932 0.7324 -0.1669 -0.1664 0.1706  132 THR C OG1 
9260  C CG2 . THR C 132 ? 0.7112 1.2174 0.7534 -0.1433 -0.1662 0.1658  132 THR C CG2 
9261  N N   . LEU C 133 ? 0.6987 1.2253 0.8013 -0.0874 -0.1249 0.1813  133 LEU C N   
9262  C CA  . LEU C 133 ? 0.7025 1.2229 0.8106 -0.0622 -0.1182 0.1844  133 LEU C CA  
9263  C C   . LEU C 133 ? 0.6807 1.1631 0.7716 -0.0512 -0.1024 0.1730  133 LEU C C   
9264  O O   . LEU C 133 ? 0.7204 1.1775 0.7984 -0.0372 -0.0997 0.1699  133 LEU C O   
9265  C CB  . LEU C 133 ? 0.7097 1.2732 0.8586 -0.0479 -0.1158 0.1974  133 LEU C CB  
9266  C CG  . LEU C 133 ? 0.6028 1.2015 0.7722 -0.0490 -0.1329 0.2119  133 LEU C CG  
9267  C CD1 . LEU C 133 ? 0.6185 1.2583 0.8324 -0.0318 -0.1278 0.2228  133 LEU C CD1 
9268  C CD2 . LEU C 133 ? 0.6090 1.1860 0.7593 -0.0413 -0.1418 0.2142  133 LEU C CD2 
9269  N N   . ASN C 134 ? 0.6913 1.1698 0.7819 -0.0582 -0.0926 0.1678  134 ASN C N   
9270  C CA  . ASN C 134 ? 0.7534 1.1937 0.8235 -0.0516 -0.0802 0.1568  134 ASN C CA  
9271  C C   . ASN C 134 ? 0.6982 1.0984 0.7365 -0.0580 -0.0858 0.1466  134 ASN C C   
9272  O O   . ASN C 134 ? 0.7882 1.1576 0.8115 -0.0463 -0.0789 0.1398  134 ASN C O   
9273  C CB  . ASN C 134 ? 0.8240 1.2671 0.8961 -0.0631 -0.0720 0.1550  134 ASN C CB  
9274  C CG  . ASN C 134 ? 0.7359 1.2023 0.8288 -0.0486 -0.0573 0.1591  134 ASN C CG  
9275  O OD1 . ASN C 134 ? 0.6826 1.1269 0.7641 -0.0372 -0.0455 0.1524  134 ASN C OD1 
9276  N ND2 . ASN C 134 ? 0.8227 1.3354 0.9466 -0.0491 -0.0580 0.1694  134 ASN C ND2 
9277  N N   . LEU C 135 ? 0.6026 1.0040 0.6311 -0.0767 -0.0982 0.1448  135 LEU C N   
9278  C CA  . LEU C 135 ? 0.6288 0.9959 0.6281 -0.0825 -0.1025 0.1336  135 LEU C CA  
9279  C C   . LEU C 135 ? 0.6091 0.9731 0.6018 -0.0697 -0.1055 0.1368  135 LEU C C   
9280  O O   . LEU C 135 ? 0.8168 1.1499 0.7899 -0.0640 -0.1014 0.1288  135 LEU C O   
9281  C CB  . LEU C 135 ? 0.6244 0.9947 0.6145 -0.1055 -0.1149 0.1289  135 LEU C CB  
9282  C CG  . LEU C 135 ? 0.6357 0.9786 0.6136 -0.1197 -0.1132 0.1173  135 LEU C CG  
9283  C CD1 . LEU C 135 ? 0.7408 1.0847 0.7084 -0.1403 -0.1270 0.1107  135 LEU C CD1 
9284  C CD2 . LEU C 135 ? 0.6353 0.9366 0.5933 -0.1108 -0.1046 0.1056  135 LEU C CD2 
9285  N N   . LEU C 136 ? 0.6103 1.0068 0.6208 -0.0655 -0.1133 0.1498  136 LEU C N   
9286  C CA  . LEU C 136 ? 0.7347 1.1301 0.7387 -0.0568 -0.1193 0.1560  136 LEU C CA  
9287  C C   . LEU C 136 ? 0.6497 1.0317 0.6615 -0.0338 -0.1097 0.1591  136 LEU C C   
9288  O O   . LEU C 136 ? 0.6633 1.0333 0.6652 -0.0267 -0.1127 0.1625  136 LEU C O   
9289  C CB  . LEU C 136 ? 0.6733 1.1084 0.6949 -0.0612 -0.1336 0.1706  136 LEU C CB  
9290  C CG  . LEU C 136 ? 0.6959 1.1379 0.6978 -0.0823 -0.1483 0.1686  136 LEU C CG  
9291  C CD1 . LEU C 136 ? 0.6589 1.0794 0.6413 -0.0996 -0.1457 0.1516  136 LEU C CD1 
9292  C CD2 . LEU C 136 ? 0.7886 1.2748 0.8138 -0.0898 -0.1627 0.1830  136 LEU C CD2 
9293  N N   . ALA C 137 ? 0.6117 0.9957 0.6403 -0.0228 -0.0984 0.1580  137 ALA C N   
9294  C CA  . ALA C 137 ? 0.7233 1.0927 0.7586 -0.0011 -0.0896 0.1586  137 ALA C CA  
9295  C C   . ALA C 137 ? 0.7522 1.0793 0.7607 0.0004  -0.0837 0.1474  137 ALA C C   
9296  O O   . ALA C 137 ? 0.7533 1.0634 0.7613 0.0151  -0.0809 0.1487  137 ALA C O   
9297  C CB  . ALA C 137 ? 0.7018 1.0860 0.7593 0.0093  -0.0782 0.1582  137 ALA C CB  
9298  N N   . TRP C 138 ? 0.6978 1.0075 0.6859 -0.0149 -0.0828 0.1367  138 TRP C N   
9299  C CA  . TRP C 138 ? 0.6795 0.9519 0.6445 -0.0151 -0.0781 0.1257  138 TRP C CA  
9300  C C   . TRP C 138 ? 0.7536 1.0185 0.6994 -0.0242 -0.0858 0.1238  138 TRP C C   
9301  O O   . TRP C 138 ? 0.8823 1.1213 0.8089 -0.0297 -0.0828 0.1126  138 TRP C O   
9302  C CB  . TRP C 138 ? 0.7544 1.0110 0.7109 -0.0247 -0.0724 0.1149  138 TRP C CB  
9303  C CG  . TRP C 138 ? 0.7757 1.0429 0.7477 -0.0184 -0.0642 0.1172  138 TRP C CG  
9304  C CD1 . TRP C 138 ? 0.7576 1.0546 0.7461 -0.0253 -0.0647 0.1231  138 TRP C CD1 
9305  C CD2 . TRP C 138 ? 0.7455 0.9953 0.7168 -0.0049 -0.0538 0.1135  138 TRP C CD2 
9306  N NE1 . TRP C 138 ? 0.7835 1.0845 0.7812 -0.0166 -0.0539 0.1232  138 TRP C NE1 
9307  C CE2 . TRP C 138 ? 0.7565 1.0279 0.7424 -0.0040 -0.0473 0.1167  138 TRP C CE2 
9308  C CE3 . TRP C 138 ? 0.8010 1.0203 0.7605 0.0057  -0.0495 0.1076  138 TRP C CE3 
9309  C CZ2 . TRP C 138 ? 0.8080 1.0711 0.7941 0.0073  -0.0364 0.1132  138 TRP C CZ2 
9310  C CZ3 . TRP C 138 ? 0.9006 1.1100 0.8614 0.0166  -0.0402 0.1042  138 TRP C CZ3 
9311  C CH2 . TRP C 138 ? 0.7894 1.0204 0.7619 0.0175  -0.0335 0.1065  138 TRP C CH2 
9312  N N   . CYS C 139 ? 0.7697 1.0579 0.7204 -0.0259 -0.0956 0.1349  139 CYS C N   
9313  C CA  . CYS C 139 ? 0.8286 1.1142 0.7583 -0.0365 -0.1029 0.1337  139 CYS C CA  
9314  C C   . CYS C 139 ? 0.7949 1.0576 0.7133 -0.0270 -0.0986 0.1341  139 CYS C C   
9315  O O   . CYS C 139 ? 0.7958 1.0589 0.7273 -0.0125 -0.0984 0.1449  139 CYS C O   
9316  C CB  . CYS C 139 ? 0.7371 1.0562 0.6747 -0.0418 -0.1161 0.1477  139 CYS C CB  
9317  S SG  . CYS C 139 ? 0.8287 1.1505 0.7360 -0.0629 -0.1253 0.1408  139 CYS C SG  
9318  N N   . GLY C 140 ? 0.7576 1.0007 0.6531 -0.0355 -0.0956 0.1221  140 GLY C N   
9319  C CA  . GLY C 140 ? 0.7796 1.0036 0.6645 -0.0292 -0.0913 0.1224  140 GLY C CA  
9320  C C   . GLY C 140 ? 0.7423 0.9815 0.6177 -0.0334 -0.0995 0.1346  140 GLY C C   
9321  O O   . GLY C 140 ? 0.8821 1.1454 0.7540 -0.0436 -0.1091 0.1400  140 GLY C O   
9322  N N   . ARG C 141 ? 0.7603 0.9849 0.6309 -0.0267 -0.0962 0.1396  141 ARG C N   
9323  C CA  . ARG C 141 ? 0.7883 1.0261 0.6525 -0.0290 -0.1042 0.1560  141 ARG C CA  
9324  C C   . ARG C 141 ? 0.8696 1.1256 0.7098 -0.0471 -0.1101 0.1530  141 ARG C C   
9325  O O   . ARG C 141 ? 0.8078 1.0877 0.6468 -0.0524 -0.1218 0.1676  141 ARG C O   
9326  C CB  . ARG C 141 ? 0.7116 0.9281 0.5711 -0.0228 -0.0984 0.1593  141 ARG C CB  
9327  C CG  . ARG C 141 ? 0.8158 1.0430 0.6731 -0.0233 -0.1073 0.1807  141 ARG C CG  
9328  C CD  . ARG C 141 ? 0.7189 0.9225 0.5800 -0.0148 -0.1022 0.1858  141 ARG C CD  
9329  N NE  . ARG C 141 ? 0.7757 0.9689 0.6165 -0.0239 -0.0924 0.1726  141 ARG C NE  
9330  C CZ  . ARG C 141 ? 0.7664 0.9665 0.5888 -0.0342 -0.0923 0.1793  141 ARG C CZ  
9331  N NH1 . ARG C 141 ? 0.8500 1.0643 0.6703 -0.0373 -0.1026 0.2014  141 ARG C NH1 
9332  N NH2 . ARG C 141 ? 0.8177 1.0115 0.6241 -0.0417 -0.0816 0.1639  141 ARG C NH2 
9333  N N   . THR C 142 ? 0.8052 1.0504 0.6266 -0.0566 -0.1025 0.1336  142 THR C N   
9334  C CA  . THR C 142 ? 0.8424 1.1029 0.6383 -0.0737 -0.1067 0.1266  142 THR C CA  
9335  C C   . THR C 142 ? 0.8291 1.1132 0.6290 -0.0823 -0.1186 0.1296  142 THR C C   
9336  O O   . THR C 142 ? 0.9466 1.2539 0.7337 -0.0927 -0.1293 0.1390  142 THR C O   
9337  C CB  . THR C 142 ? 0.9001 1.1425 0.6810 -0.0798 -0.0959 0.1017  142 THR C CB  
9338  O OG1 . THR C 142 ? 1.0028 1.2274 0.7812 -0.0729 -0.0854 0.0999  142 THR C OG1 
9339  C CG2 . THR C 142 ? 0.8056 1.0634 0.5593 -0.0972 -0.0997 0.0911  142 THR C CG2 
9340  N N   . LEU C 143 ? 0.7925 1.0727 0.6101 -0.0794 -0.1176 0.1227  143 LEU C N   
9341  C CA  . LEU C 143 ? 0.8854 1.1879 0.7073 -0.0902 -0.1284 0.1234  143 LEU C CA  
9342  C C   . LEU C 143 ? 0.9044 1.2333 0.7481 -0.0842 -0.1396 0.1462  143 LEU C C   
9343  O O   . LEU C 143 ? 0.8574 1.2114 0.7028 -0.0951 -0.1516 0.1508  143 LEU C O   
9344  C CB  . LEU C 143 ? 0.8018 1.0918 0.6347 -0.0917 -0.1234 0.1087  143 LEU C CB  
9345  C CG  . LEU C 143 ? 0.8492 1.1242 0.6606 -0.1054 -0.1205 0.0856  143 LEU C CG  
9346  C CD1 . LEU C 143 ? 0.7409 1.0133 0.5642 -0.1126 -0.1228 0.0769  143 LEU C CD1 
9347  C CD2 . LEU C 143 ? 0.9184 1.2088 0.7027 -0.1204 -0.1281 0.0818  143 LEU C CD2 
9348  N N   . ARG C 144 ? 0.7765 1.1004 0.6383 -0.0671 -0.1369 0.1603  144 ARG C N   
9349  C CA  . ARG C 144 ? 0.8412 1.1902 0.7250 -0.0602 -0.1485 0.1823  144 ARG C CA  
9350  C C   . ARG C 144 ? 0.7963 1.1656 0.6621 -0.0718 -0.1621 0.1955  144 ARG C C   
9351  O O   . ARG C 144 ? 0.8197 1.2172 0.6990 -0.0740 -0.1762 0.2110  144 ARG C O   
9352  C CB  . ARG C 144 ? 0.8063 1.1419 0.7119 -0.0392 -0.1434 0.1932  144 ARG C CB  
9353  C CG  . ARG C 144 ? 0.7293 1.0421 0.6471 -0.0276 -0.1293 0.1801  144 ARG C CG  
9354  C CD  . ARG C 144 ? 0.7097 1.0162 0.6532 -0.0068 -0.1273 0.1913  144 ARG C CD  
9355  N NE  . ARG C 144 ? 0.7706 1.0849 0.7397 0.0032  -0.1223 0.1881  144 ARG C NE  
9356  C CZ  . ARG C 144 ? 0.8194 1.1301 0.8128 0.0223  -0.1188 0.1937  144 ARG C CZ  
9357  N NH1 . ARG C 144 ? 0.8658 1.1638 0.8641 0.0335  -0.1220 0.2043  144 ARG C NH1 
9358  N NH2 . ARG C 144 ? 0.8506 1.1708 0.8640 0.0297  -0.1121 0.1884  144 ARG C NH2 
9359  N N   . LYS C 145 ? 0.8302 1.1877 0.6659 -0.0797 -0.1583 0.1902  145 LYS C N   
9360  C CA  . LYS C 145 ? 0.9155 1.2933 0.7285 -0.0930 -0.1704 0.2021  145 LYS C CA  
9361  C C   . LYS C 145 ? 0.9511 1.3478 0.7455 -0.1127 -0.1785 0.1909  145 LYS C C   
9362  O O   . LYS C 145 ? 0.9005 1.3245 0.6888 -0.1227 -0.1945 0.2049  145 LYS C O   
9363  C CB  . LYS C 145 ? 0.8493 1.2111 0.6357 -0.0960 -0.1618 0.1996  145 LYS C CB  
9364  C CG  . LYS C 145 ? 0.8364 1.1745 0.6404 -0.0782 -0.1528 0.2070  145 LYS C CG  
9365  C CD  . LYS C 145 ? 0.9171 1.2456 0.6976 -0.0829 -0.1469 0.2101  145 LYS C CD  
9366  C CE  . LYS C 145 ? 1.0026 1.3117 0.7653 -0.0871 -0.1302 0.1841  145 LYS C CE  
9367  N NZ  . LYS C 145 ? 1.1532 1.4731 0.8924 -0.1031 -0.1299 0.1641  145 LYS C NZ  
9368  N N   . ASP C 146 ? 0.9486 1.3304 0.7344 -0.1187 -0.1692 0.1659  146 ASP C N   
9369  C CA  . ASP C 146 ? 0.9346 1.3290 0.7012 -0.1382 -0.1766 0.1518  146 ASP C CA  
9370  C C   . ASP C 146 ? 0.9261 1.3402 0.7182 -0.1411 -0.1877 0.1570  146 ASP C C   
9371  O O   . ASP C 146 ? 1.0152 1.4486 0.7950 -0.1582 -0.2003 0.1537  146 ASP C O   
9372  C CB  . ASP C 146 ? 1.0810 1.4489 0.8297 -0.1435 -0.1631 0.1226  146 ASP C CB  
9373  C CG  . ASP C 146 ? 1.2615 1.6210 0.9772 -0.1485 -0.1550 0.1136  146 ASP C CG  
9374  O OD1 . ASP C 146 ? 1.2896 1.6514 1.0033 -0.1414 -0.1533 0.1303  146 ASP C OD1 
9375  O OD2 . ASP C 146 ? 1.3703 1.7210 1.0631 -0.1596 -0.1501 0.0897  146 ASP C OD2 
9376  N N   . LEU C 147 ? 0.9103 1.3217 0.7371 -0.1255 -0.1833 0.1645  147 LEU C N   
9377  C CA  . LEU C 147 ? 0.8218 1.2551 0.6773 -0.1269 -0.1916 0.1708  147 LEU C CA  
9378  C C   . LEU C 147 ? 0.7877 1.2426 0.6753 -0.1118 -0.1986 0.1961  147 LEU C C   
9379  O O   . LEU C 147 ? 0.8347 1.2978 0.7553 -0.1012 -0.1957 0.2006  147 LEU C O   
9380  C CB  . LEU C 147 ? 0.9131 1.3277 0.7832 -0.1231 -0.1793 0.1556  147 LEU C CB  
9381  C CG  . LEU C 147 ? 1.0284 1.4127 0.8729 -0.1321 -0.1696 0.1304  147 LEU C CG  
9382  C CD1 . LEU C 147 ? 0.9035 1.2686 0.7660 -0.1257 -0.1583 0.1208  147 LEU C CD1 
9383  C CD2 . LEU C 147 ? 0.9845 1.3793 0.8067 -0.1547 -0.1811 0.1190  147 LEU C CD2 
9384  N N   . LYS C 148 ? 0.8233 1.2880 0.7021 -0.1104 -0.2077 0.2130  148 LYS C N   
9385  C CA  . LYS C 148 ? 0.8625 1.3481 0.7736 -0.0962 -0.2173 0.2381  148 LYS C CA  
9386  C C   . LYS C 148 ? 0.9596 1.4832 0.8935 -0.1039 -0.2331 0.2481  148 LYS C C   
9387  O O   . LYS C 148 ? 1.0165 1.5579 0.9898 -0.0894 -0.2362 0.2623  148 LYS C O   
9388  C CB  . LYS C 148 ? 0.8161 1.3027 0.7110 -0.0956 -0.2257 0.2559  148 LYS C CB  
9389  C CG  . LYS C 148 ? 0.7734 1.2708 0.7033 -0.0768 -0.2336 0.2814  148 LYS C CG  
9390  C CD  . LYS C 148 ? 0.9085 1.4129 0.8219 -0.0813 -0.2475 0.3032  148 LYS C CD  
9391  C CE  . LYS C 148 ? 0.8684 1.3562 0.7333 -0.0970 -0.2412 0.2922  148 LYS C CE  
9392  N NZ  . LYS C 148 ? 0.8391 1.2905 0.6982 -0.0860 -0.2217 0.2803  148 LYS C NZ  
9393  N N   . ASP C 149 ? 0.9468 1.4838 0.8577 -0.1266 -0.2432 0.2400  149 ASP C N   
9394  C CA  . ASP C 149 ? 0.9822 1.5563 0.9140 -0.1368 -0.2598 0.2490  149 ASP C CA  
9395  C C   . ASP C 149 ? 0.9860 1.5659 0.9552 -0.1287 -0.2510 0.2441  149 ASP C C   
9396  O O   . ASP C 149 ? 0.9993 1.6054 1.0088 -0.1166 -0.2559 0.2607  149 ASP C O   
9397  C CB  . ASP C 149 ? 1.0507 1.6315 0.9471 -0.1640 -0.2706 0.2361  149 ASP C CB  
9398  C CG  . ASP C 149 ? 1.1409 1.6886 1.0113 -0.1723 -0.2553 0.2065  149 ASP C CG  
9399  O OD1 . ASP C 149 ? 1.1350 1.6532 1.0084 -0.1578 -0.2368 0.1977  149 ASP C OD1 
9400  O OD2 . ASP C 149 ? 1.2389 1.7897 1.0874 -0.1934 -0.2627 0.1920  149 ASP C OD2 
9401  N N   . LEU C 150 ? 0.9622 1.5187 0.9195 -0.1352 -0.2378 0.2217  150 LEU C N   
9402  C CA  . LEU C 150 ? 0.8744 1.4361 0.8631 -0.1303 -0.2289 0.2174  150 LEU C CA  
9403  C C   . LEU C 150 ? 0.8868 1.4448 0.9061 -0.1039 -0.2162 0.2264  150 LEU C C   
9404  O O   . LEU C 150 ? 0.9185 1.4989 0.9741 -0.0964 -0.2137 0.2326  150 LEU C O   
9405  C CB  . LEU C 150 ? 0.8006 1.3314 0.7679 -0.1412 -0.2172 0.1931  150 LEU C CB  
9406  C CG  . LEU C 150 ? 0.8809 1.4121 0.8210 -0.1674 -0.2286 0.1797  150 LEU C CG  
9407  C CD1 . LEU C 150 ? 0.7373 1.2314 0.6591 -0.1735 -0.2156 0.1558  150 LEU C CD1 
9408  C CD2 . LEU C 150 ? 0.9834 1.5534 0.9473 -0.1819 -0.2447 0.1892  150 LEU C CD2 
9409  N N   . LEU C 151 ? 0.9035 1.4346 0.9092 -0.0899 -0.2082 0.2266  151 LEU C N   
9410  C CA  . LEU C 151 ? 0.9444 1.4667 0.9761 -0.0650 -0.1961 0.2321  151 LEU C CA  
9411  C C   . LEU C 151 ? 1.0213 1.5779 1.0918 -0.0518 -0.2069 0.2541  151 LEU C C   
9412  O O   . LEU C 151 ? 0.9897 1.5584 1.0951 -0.0364 -0.1990 0.2566  151 LEU C O   
9413  C CB  . LEU C 151 ? 0.8478 1.3338 0.8556 -0.0557 -0.1879 0.2283  151 LEU C CB  
9414  C CG  . LEU C 151 ? 0.7996 1.2489 0.7907 -0.0539 -0.1696 0.2076  151 LEU C CG  
9415  C CD1 . LEU C 151 ? 0.6675 1.0855 0.6299 -0.0516 -0.1647 0.2034  151 LEU C CD1 
9416  C CD2 . LEU C 151 ? 0.7467 1.1926 0.7667 -0.0358 -0.1565 0.2059  151 LEU C CD2 
9417  N N   . ASN C 152 ? 0.9901 1.5638 1.0555 -0.0574 -0.2250 0.2704  152 ASN C N   
9418  C CA  . ASN C 152 ? 0.9663 1.5715 1.0706 -0.0439 -0.2374 0.2932  152 ASN C CA  
9419  C C   . ASN C 152 ? 0.9107 1.5597 1.0466 -0.0515 -0.2468 0.2992  152 ASN C C   
9420  O O   . ASN C 152 ? 0.8871 1.5643 1.0660 -0.0362 -0.2521 0.3146  152 ASN C O   
9421  C CB  . ASN C 152 ? 1.0346 1.6429 1.1221 -0.0482 -0.2552 0.3112  152 ASN C CB  
9422  C CG  . ASN C 152 ? 1.0425 1.6270 1.1369 -0.0269 -0.2510 0.3211  152 ASN C CG  
9423  O OD1 . ASN C 152 ? 1.0837 1.6820 1.2173 -0.0078 -0.2562 0.3369  152 ASN C OD1 
9424  N ND2 . ASN C 152 ? 1.0640 1.6123 1.1224 -0.0298 -0.2416 0.3114  152 ASN C ND2 
9425  N N   . LYS C 153 ? 0.8865 1.5417 1.0039 -0.0748 -0.2494 0.2873  153 LYS C N   
9426  C CA  . LYS C 153 ? 0.9144 1.6095 1.0627 -0.0840 -0.2565 0.2913  153 LYS C CA  
9427  C C   . LYS C 153 ? 0.9687 1.6753 1.1595 -0.0645 -0.2404 0.2908  153 LYS C C   
9428  O O   . LYS C 153 ? 0.8537 1.5998 1.0885 -0.0554 -0.2468 0.3055  153 LYS C O   
9429  C CB  . LYS C 153 ? 0.8358 1.5235 0.9547 -0.1111 -0.2576 0.2740  153 LYS C CB  
9430  C CG  . LYS C 153 ? 0.8852 1.6126 1.0319 -0.1258 -0.2671 0.2782  153 LYS C CG  
9431  C CD  . LYS C 153 ? 0.8662 1.5764 0.9843 -0.1508 -0.2655 0.2584  153 LYS C CD  
9432  C CE  . LYS C 153 ? 0.9812 1.7300 1.1136 -0.1737 -0.2849 0.2647  153 LYS C CE  
9433  N NZ  . LYS C 153 ? 0.9834 1.7136 1.0908 -0.1985 -0.2848 0.2452  153 LYS C NZ  
9434  N N   . GLY C 154 ? 0.9168 1.5903 1.0949 -0.0578 -0.2193 0.2736  154 GLY C N   
9435  C CA  . GLY C 154 ? 0.7924 1.4717 1.0029 -0.0386 -0.2016 0.2708  154 GLY C CA  
9436  C C   . GLY C 154 ? 0.8665 1.5754 1.1002 -0.0492 -0.1965 0.2676  154 GLY C C   
9437  O O   . GLY C 154 ? 0.8418 1.5466 1.0882 -0.0387 -0.1778 0.2596  154 GLY C O   
9438  N N   . ARG C 155 ? 0.8393 1.5785 1.0783 -0.0707 -0.2127 0.2739  155 ARG C N   
9439  C CA  . ARG C 155 ? 0.8447 1.6174 1.1112 -0.0820 -0.2096 0.2742  155 ARG C CA  
9440  C C   . ARG C 155 ? 0.8585 1.6414 1.1081 -0.1131 -0.2278 0.2734  155 ARG C C   
9441  O O   . ARG C 155 ? 0.7811 1.5490 0.9993 -0.1239 -0.2423 0.2726  155 ARG C O   
9442  C CB  . ARG C 155 ? 0.8192 1.6423 1.1418 -0.0652 -0.2107 0.2906  155 ARG C CB  
9443  C CG  . ARG C 155 ? 0.8383 1.6880 1.1765 -0.0632 -0.2341 0.3094  155 ARG C CG  
9444  C CD  . ARG C 155 ? 0.7134 1.6119 1.1116 -0.0435 -0.2350 0.3253  155 ARG C CD  
9445  N NE  . ARG C 155 ? 0.7719 1.6593 1.1884 -0.0154 -0.2120 0.3185  155 ARG C NE  
9446  C CZ  . ARG C 155 ? 0.8001 1.6572 1.2096 0.0073  -0.2078 0.3180  155 ARG C CZ  
9447  N NH1 . ARG C 155 ? 0.7900 1.6242 1.1737 0.0052  -0.2237 0.3251  155 ARG C NH1 
9448  N NH2 . ARG C 155 ? 0.7623 1.6121 1.1905 0.0319  -0.1872 0.3103  155 ARG C NH2 
9449  N N   . ASN C 156 ? 0.8313 1.6405 1.1018 -0.1281 -0.2265 0.2734  156 ASN C N   
9450  C CA  . ASN C 156 ? 0.8594 1.6840 1.1224 -0.1586 -0.2449 0.2735  156 ASN C CA  
9451  C C   . ASN C 156 ? 0.8522 1.6291 1.0613 -0.1765 -0.2485 0.2555  156 ASN C C   
9452  O O   . ASN C 156 ? 0.9365 1.7151 1.1249 -0.1950 -0.2677 0.2547  156 ASN C O   
9453  C CB  . ASN C 156 ? 0.8519 1.7193 1.1371 -0.1621 -0.2686 0.2919  156 ASN C CB  
9454  C CG  . ASN C 156 ? 0.8057 1.7157 1.1447 -0.1381 -0.2650 0.3094  156 ASN C CG  
9455  O OD1 . ASN C 156 ? 0.8106 1.7282 1.1589 -0.1216 -0.2737 0.3215  156 ASN C OD1 
9456  N ND2 . ASN C 156 ? 0.7611 1.6995 1.1368 -0.1358 -0.2518 0.3109  156 ASN C ND2 
9457  N N   . TYR C 157 ? 0.8734 1.6083 1.0601 -0.1711 -0.2300 0.2401  157 TYR C N   
9458  C CA  . TYR C 157 ? 0.9008 1.5901 1.0410 -0.1860 -0.2311 0.2214  157 TYR C CA  
9459  C C   . TYR C 157 ? 0.9419 1.6342 1.0806 -0.2143 -0.2389 0.2144  157 TYR C C   
9460  O O   . TYR C 157 ? 0.9434 1.6734 1.1167 -0.2230 -0.2426 0.2251  157 TYR C O   
9461  C CB  . TYR C 157 ? 0.8122 1.4574 0.9332 -0.1699 -0.2100 0.2089  157 TYR C CB  
9462  C CG  . TYR C 157 ? 0.8162 1.4509 0.9317 -0.1458 -0.2052 0.2135  157 TYR C CG  
9463  C CD1 . TYR C 157 ? 0.8534 1.4680 0.9358 -0.1482 -0.2138 0.2096  157 TYR C CD1 
9464  C CD2 . TYR C 157 ? 0.7077 1.3533 0.8513 -0.1213 -0.1922 0.2220  157 TYR C CD2 
9465  C CE1 . TYR C 157 ? 0.8652 1.4703 0.9436 -0.1280 -0.2104 0.2160  157 TYR C CE1 
9466  C CE2 . TYR C 157 ? 0.7345 1.3681 0.8748 -0.1000 -0.1893 0.2266  157 TYR C CE2 
9467  C CZ  . TYR C 157 ? 0.8619 1.4749 0.9700 -0.1040 -0.1989 0.2247  157 TYR C CZ  
9468  O OH  . TYR C 157 ? 0.9952 1.5957 1.1005 -0.0846 -0.1969 0.2312  157 TYR C OH  
9469  N N   . THR C 158 ? 0.8760 1.5287 0.9758 -0.2292 -0.2419 0.1961  158 THR C N   
9470  C CA  . THR C 158 ? 0.8766 1.5235 0.9708 -0.2569 -0.2513 0.1869  158 THR C CA  
9471  C C   . THR C 158 ? 0.8004 1.3957 0.8689 -0.2589 -0.2383 0.1678  158 THR C C   
9472  O O   . THR C 158 ? 0.7252 1.2902 0.7764 -0.2406 -0.2241 0.1608  158 THR C O   
9473  C CB  . THR C 158 ? 0.8122 1.4657 0.8850 -0.2776 -0.2743 0.1822  158 THR C CB  
9474  O OG1 . THR C 158 ? 0.9134 1.5201 0.9411 -0.2820 -0.2728 0.1603  158 THR C OG1 
9475  C CG2 . THR C 158 ? 0.7650 1.4541 0.8474 -0.2675 -0.2855 0.1990  158 THR C CG2 
9476  N N   . GLN C 159 ? 0.7598 1.3452 0.8282 -0.2819 -0.2443 0.1604  159 GLN C N   
9477  C CA  . GLN C 159 ? 0.7640 1.2983 0.8081 -0.2864 -0.2361 0.1419  159 GLN C CA  
9478  C C   . GLN C 159 ? 0.8728 1.3717 0.8758 -0.2860 -0.2400 0.1223  159 GLN C C   
9479  O O   . GLN C 159 ? 0.9176 1.3775 0.9007 -0.2744 -0.2272 0.1098  159 GLN C O   
9480  C CB  . GLN C 159 ? 0.7850 1.3162 0.8393 -0.3130 -0.2452 0.1393  159 GLN C CB  
9481  C CG  . GLN C 159 ? 0.8844 1.3616 0.9165 -0.3197 -0.2403 0.1207  159 GLN C CG  
9482  C CD  . GLN C 159 ? 0.8093 1.2700 0.8494 -0.3040 -0.2204 0.1254  159 GLN C CD  
9483  O OE1 . GLN C 159 ? 0.8294 1.3219 0.8950 -0.2928 -0.2104 0.1425  159 GLN C OE1 
9484  N NE2 . GLN C 159 ? 0.8474 1.2587 0.8658 -0.3027 -0.2147 0.1096  159 GLN C NE2 
9485  N N   . GLU C 160 ? 0.9087 1.4235 0.8988 -0.2987 -0.2574 0.1199  160 GLU C N   
9486  C CA  . GLU C 160 ? 0.8798 1.3663 0.8290 -0.3007 -0.2611 0.1007  160 GLU C CA  
9487  C C   . GLU C 160 ? 0.9217 1.4027 0.8579 -0.2759 -0.2488 0.1040  160 GLU C C   
9488  O O   . GLU C 160 ? 0.9240 1.3693 0.8315 -0.2696 -0.2402 0.0872  160 GLU C O   
9489  C CB  . GLU C 160 ? 0.8658 1.3762 0.8040 -0.3217 -0.2836 0.0993  160 GLU C CB  
9490  C CG  . GLU C 160 ? 0.9573 1.4786 0.9118 -0.3488 -0.2993 0.0983  160 GLU C CG  
9491  C CD  . GLU C 160 ? 1.0368 1.6024 1.0380 -0.3493 -0.3010 0.1236  160 GLU C CD  
9492  O OE1 . GLU C 160 ? 1.0698 1.6517 1.0881 -0.3722 -0.3149 0.1265  160 GLU C OE1 
9493  O OE2 . GLU C 160 ? 1.0065 1.5908 1.0285 -0.3269 -0.2881 0.1398  160 GLU C OE2 
9494  N N   . GLU C 161 ? 0.8704 1.3865 0.8293 -0.2616 -0.2482 0.1257  161 GLU C N   
9495  C CA  . GLU C 161 ? 0.8090 1.3187 0.7601 -0.2377 -0.2370 0.1311  161 GLU C CA  
9496  C C   . GLU C 161 ? 0.8407 1.3165 0.7925 -0.2212 -0.2162 0.1241  161 GLU C C   
9497  O O   . GLU C 161 ? 0.8709 1.3176 0.7988 -0.2106 -0.2069 0.1140  161 GLU C O   
9498  C CB  . GLU C 161 ? 0.7703 1.3233 0.7521 -0.2253 -0.2415 0.1560  161 GLU C CB  
9499  C CG  . GLU C 161 ? 0.9704 1.5591 0.9525 -0.2407 -0.2639 0.1656  161 GLU C CG  
9500  C CD  . GLU C 161 ? 0.9835 1.6131 0.9970 -0.2260 -0.2694 0.1909  161 GLU C CD  
9501  O OE1 . GLU C 161 ? 1.0215 1.6668 1.0717 -0.2116 -0.2595 0.2019  161 GLU C OE1 
9502  O OE2 . GLU C 161 ? 0.8872 1.5337 0.8890 -0.2289 -0.2840 0.1997  161 GLU C OE2 
9503  N N   . LYS C 162 ? 0.7793 1.2603 0.7582 -0.2197 -0.2089 0.1301  162 LYS C N   
9504  C CA  . LYS C 162 ? 0.7300 1.1806 0.7091 -0.2058 -0.1906 0.1245  162 LYS C CA  
9505  C C   . LYS C 162 ? 0.7377 1.1422 0.6866 -0.2129 -0.1877 0.1024  162 LYS C C   
9506  O O   . LYS C 162 ? 0.7265 1.1021 0.6622 -0.1982 -0.1752 0.0951  162 LYS C O   
9507  C CB  . LYS C 162 ? 0.7072 1.1739 0.7170 -0.2088 -0.1852 0.1342  162 LYS C CB  
9508  C CG  . LYS C 162 ? 0.7977 1.2379 0.8085 -0.1951 -0.1671 0.1312  162 LYS C CG  
9509  C CD  . LYS C 162 ? 0.7215 1.1768 0.7571 -0.2039 -0.1630 0.1396  162 LYS C CD  
9510  C CE  . LYS C 162 ? 0.7205 1.1934 0.7651 -0.2307 -0.1789 0.1412  162 LYS C CE  
9511  N NZ  . LYS C 162 ? 0.7020 1.1770 0.7634 -0.2436 -0.1750 0.1465  162 LYS C NZ  
9512  N N   . GLU C 163 ? 0.7507 1.1476 0.6899 -0.2352 -0.1996 0.0908  163 GLU C N   
9513  C CA  . GLU C 163 ? 0.8738 1.2265 0.7877 -0.2415 -0.1974 0.0680  163 GLU C CA  
9514  C C   . GLU C 163 ? 0.9466 1.2854 0.8298 -0.2342 -0.1955 0.0556  163 GLU C C   
9515  O O   . GLU C 163 ? 0.8741 1.1772 0.7405 -0.2282 -0.1864 0.0395  163 GLU C O   
9516  C CB  . GLU C 163 ? 0.7954 1.1431 0.7080 -0.2673 -0.2120 0.0579  163 GLU C CB  
9517  C CG  . GLU C 163 ? 0.8956 1.2519 0.8372 -0.2771 -0.2130 0.0694  163 GLU C CG  
9518  C CD  . GLU C 163 ? 1.0711 1.4062 1.0091 -0.3017 -0.2254 0.0561  163 GLU C CD  
9519  O OE1 . GLU C 163 ? 1.1325 1.4411 1.0445 -0.3085 -0.2313 0.0346  163 GLU C OE1 
9520  O OE2 . GLU C 163 ? 1.0501 1.3959 1.0118 -0.3146 -0.2293 0.0670  163 GLU C OE2 
9521  N N   . TYR C 164 ? 0.8837 1.2518 0.7602 -0.2351 -0.2043 0.0639  164 TYR C N   
9522  C CA  . TYR C 164 ? 0.8260 1.1863 0.6737 -0.2279 -0.2014 0.0565  164 TYR C CA  
9523  C C   . TYR C 164 ? 0.8629 1.2090 0.7137 -0.2042 -0.1846 0.0621  164 TYR C C   
9524  O O   . TYR C 164 ? 0.8234 1.1419 0.6536 -0.1980 -0.1753 0.0477  164 TYR C O   
9525  C CB  . TYR C 164 ? 0.8022 1.2002 0.6453 -0.2340 -0.2156 0.0697  164 TYR C CB  
9526  C CG  . TYR C 164 ? 0.8166 1.2136 0.6323 -0.2263 -0.2128 0.0687  164 TYR C CG  
9527  C CD1 . TYR C 164 ? 0.9424 1.3193 0.7226 -0.2353 -0.2120 0.0464  164 TYR C CD1 
9528  C CD2 . TYR C 164 ? 0.7934 1.2103 0.6194 -0.2107 -0.2111 0.0901  164 TYR C CD2 
9529  C CE1 . TYR C 164 ? 0.9256 1.3048 0.6799 -0.2300 -0.2086 0.0466  164 TYR C CE1 
9530  C CE2 . TYR C 164 ? 0.8044 1.2207 0.6055 -0.2057 -0.2094 0.0916  164 TYR C CE2 
9531  C CZ  . TYR C 164 ? 0.8964 1.2951 0.6608 -0.2160 -0.2077 0.0703  164 TYR C CZ  
9532  O OH  . TYR C 164 ? 0.8400 1.2408 0.5783 -0.2128 -0.2049 0.0723  164 TYR C OH  
9533  N N   . VAL C 165 ? 0.8590 1.2248 0.7366 -0.1906 -0.1805 0.0822  165 VAL C N   
9534  C CA  . VAL C 165 ? 0.8634 1.2145 0.7464 -0.1686 -0.1654 0.0872  165 VAL C CA  
9535  C C   . VAL C 165 ? 0.8001 1.1125 0.6778 -0.1659 -0.1538 0.0716  165 VAL C C   
9536  O O   . VAL C 165 ? 0.8719 1.1607 0.7376 -0.1539 -0.1434 0.0649  165 VAL C O   
9537  C CB  . VAL C 165 ? 0.8614 1.2391 0.7769 -0.1559 -0.1630 0.1081  165 VAL C CB  
9538  C CG1 . VAL C 165 ? 0.7387 1.0946 0.6615 -0.1364 -0.1467 0.1085  165 VAL C CG1 
9539  C CG2 . VAL C 165 ? 0.8856 1.2950 0.8066 -0.1508 -0.1722 0.1248  165 VAL C CG2 
9540  N N   . LEU C 166 ? 0.7605 1.0666 0.6488 -0.1776 -0.1563 0.0672  166 LEU C N   
9541  C CA  . LEU C 166 ? 0.7929 1.0621 0.6783 -0.1763 -0.1478 0.0545  166 LEU C CA  
9542  C C   . LEU C 166 ? 0.8010 1.0402 0.6602 -0.1790 -0.1464 0.0330  166 LEU C C   
9543  O O   . LEU C 166 ? 0.8589 1.0716 0.7124 -0.1670 -0.1356 0.0257  166 LEU C O   
9544  C CB  . LEU C 166 ? 0.7873 1.0566 0.6878 -0.1922 -0.1538 0.0552  166 LEU C CB  
9545  C CG  . LEU C 166 ? 0.8217 1.1111 0.7489 -0.1866 -0.1484 0.0736  166 LEU C CG  
9546  C CD1 . LEU C 166 ? 0.7937 1.0979 0.7369 -0.2071 -0.1582 0.0784  166 LEU C CD1 
9547  C CD2 . LEU C 166 ? 0.6886 0.9498 0.6163 -0.1730 -0.1347 0.0719  166 LEU C CD2 
9548  N N   . ASN C 167 ? 0.8374 1.0816 0.6807 -0.1946 -0.1572 0.0218  167 ASN C N   
9549  C CA  . ASN C 167 ? 0.8651 1.0841 0.6829 -0.1969 -0.1548 -0.0010 167 ASN C CA  
9550  C C   . ASN C 167 ? 0.8969 1.1184 0.7000 -0.1822 -0.1454 0.0005  167 ASN C C   
9551  O O   . ASN C 167 ? 0.8856 1.0823 0.6759 -0.1762 -0.1364 -0.0152 167 ASN C O   
9552  C CB  . ASN C 167 ? 0.8972 1.1242 0.6989 -0.2172 -0.1686 -0.0138 167 ASN C CB  
9553  C CG  . ASN C 167 ? 1.0689 1.2796 0.8811 -0.2330 -0.1770 -0.0228 167 ASN C CG  
9554  O OD1 . ASN C 167 ? 1.0184 1.2506 0.8426 -0.2470 -0.1891 -0.0131 167 ASN C OD1 
9555  N ND2 . ASN C 167 ? 1.1379 1.3104 0.9484 -0.2307 -0.1712 -0.0400 167 ASN C ND2 
9556  N N   . LYS C 168 ? 0.8638 1.1153 0.6706 -0.1765 -0.1479 0.0198  168 LYS C N   
9557  C CA  . LYS C 168 ? 0.8279 1.0807 0.6250 -0.1622 -0.1393 0.0256  168 LYS C CA  
9558  C C   . LYS C 168 ? 0.8478 1.0775 0.6576 -0.1449 -0.1257 0.0275  168 LYS C C   
9559  O O   . LYS C 168 ? 0.9499 1.1624 0.7482 -0.1367 -0.1163 0.0193  168 LYS C O   
9560  C CB  . LYS C 168 ? 0.8958 1.1833 0.6995 -0.1591 -0.1466 0.0485  168 LYS C CB  
9561  C CG  . LYS C 168 ? 0.8777 1.1883 0.6605 -0.1741 -0.1594 0.0478  168 LYS C CG  
9562  C CD  . LYS C 168 ? 0.9107 1.2041 0.6612 -0.1805 -0.1545 0.0258  168 LYS C CD  
9563  C CE  . LYS C 168 ? 1.0215 1.3274 0.7515 -0.2015 -0.1678 0.0139  168 LYS C CE  
9564  N NZ  . LYS C 168 ? 0.9612 1.2504 0.7008 -0.2122 -0.1720 -0.0013 168 LYS C NZ  
9565  N N   . TYR C 169 ? 0.7846 1.0154 0.6180 -0.1398 -0.1245 0.0382  169 TYR C N   
9566  C CA  . TYR C 169 ? 0.7382 0.9475 0.5819 -0.1247 -0.1128 0.0398  169 TYR C CA  
9567  C C   . TYR C 169 ? 0.8532 1.0279 0.6882 -0.1265 -0.1074 0.0201  169 TYR C C   
9568  O O   . TYR C 169 ? 0.9034 1.0594 0.7358 -0.1146 -0.0980 0.0163  169 TYR C O   
9569  C CB  . TYR C 169 ? 0.7834 1.0026 0.6510 -0.1219 -0.1127 0.0531  169 TYR C CB  
9570  C CG  . TYR C 169 ? 0.8299 1.0768 0.7120 -0.1106 -0.1126 0.0724  169 TYR C CG  
9571  C CD1 . TYR C 169 ? 0.8238 1.0855 0.6980 -0.1063 -0.1160 0.0794  169 TYR C CD1 
9572  C CD2 . TYR C 169 ? 0.7869 1.0451 0.6912 -0.1041 -0.1091 0.0837  169 TYR C CD2 
9573  C CE1 . TYR C 169 ? 0.7581 1.0427 0.6485 -0.0950 -0.1172 0.0973  169 TYR C CE1 
9574  C CE2 . TYR C 169 ? 0.6937 0.9765 0.6139 -0.0919 -0.1086 0.0994  169 TYR C CE2 
9575  C CZ  . TYR C 169 ? 0.7017 0.9963 0.6162 -0.0869 -0.1134 0.1062  169 TYR C CZ  
9576  O OH  . TYR C 169 ? 0.6832 0.9999 0.6163 -0.0739 -0.1142 0.1222  169 TYR C OH  
9577  N N   . PHE C 170 ? 0.8658 1.0312 0.6980 -0.1413 -0.1141 0.0073  170 PHE C N   
9578  C CA  . PHE C 170 ? 0.9117 1.0426 0.7406 -0.1420 -0.1103 -0.0110 170 PHE C CA  
9579  C C   . PHE C 170 ? 0.9284 1.0494 0.7378 -0.1393 -0.1050 -0.0281 170 PHE C C   
9580  O O   . PHE C 170 ? 0.8608 0.9561 0.6708 -0.1319 -0.0976 -0.0399 170 PHE C O   
9581  C CB  . PHE C 170 ? 0.8538 0.9749 0.6872 -0.1588 -0.1201 -0.0197 170 PHE C CB  
9582  C CG  . PHE C 170 ? 0.9978 1.1139 0.8516 -0.1600 -0.1211 -0.0072 170 PHE C CG  
9583  C CD1 . PHE C 170 ? 0.8775 1.0233 0.7447 -0.1626 -0.1243 0.0121  170 PHE C CD1 
9584  C CD2 . PHE C 170 ? 1.0959 1.1794 0.9562 -0.1584 -0.1187 -0.0139 170 PHE C CD2 
9585  C CE1 . PHE C 170 ? 0.9376 1.0822 0.8221 -0.1645 -0.1235 0.0236  170 PHE C CE1 
9586  C CE2 . PHE C 170 ? 1.0634 1.1437 0.9398 -0.1610 -0.1196 -0.0007 170 PHE C CE2 
9587  C CZ  . PHE C 170 ? 0.9981 1.1099 0.8855 -0.1644 -0.1212 0.0177  170 PHE C CZ  
9588  N N   . GLU C 171 ? 0.9211 1.0644 0.7136 -0.1455 -0.1088 -0.0290 171 GLU C N   
9589  C CA  . GLU C 171 ? 0.9393 1.0793 0.7116 -0.1431 -0.1019 -0.0432 171 GLU C CA  
9590  C C   . GLU C 171 ? 0.9858 1.1219 0.7622 -0.1263 -0.0903 -0.0343 171 GLU C C   
9591  O O   . GLU C 171 ? 0.9770 1.0984 0.7468 -0.1207 -0.0811 -0.0479 171 GLU C O   
9592  C CB  . GLU C 171 ? 0.9155 1.0837 0.6669 -0.1543 -0.1092 -0.0421 171 GLU C CB  
9593  C CG  . GLU C 171 ? 1.1497 1.3130 0.8856 -0.1709 -0.1168 -0.0642 171 GLU C CG  
9594  C CD  . GLU C 171 ? 1.3306 1.4608 1.0649 -0.1684 -0.1090 -0.0905 171 GLU C CD  
9595  O OE1 . GLU C 171 ? 1.2603 1.3887 0.9775 -0.1650 -0.0998 -0.1053 171 GLU C OE1 
9596  O OE2 . GLU C 171 ? 1.3119 1.4188 1.0629 -0.1701 -0.1124 -0.0960 171 GLU C OE2 
9597  N N   . ILE C 172 ? 0.8534 1.0024 0.6423 -0.1179 -0.0906 -0.0121 172 ILE C N   
9598  C CA  . ILE C 172 ? 0.8689 1.0115 0.6636 -0.1025 -0.0812 -0.0032 172 ILE C CA  
9599  C C   . ILE C 172 ? 0.8991 1.0113 0.7050 -0.0948 -0.0742 -0.0128 172 ILE C C   
9600  O O   . ILE C 172 ? 0.8631 0.9636 0.6675 -0.0863 -0.0656 -0.0178 172 ILE C O   
9601  C CB  . ILE C 172 ? 0.7940 0.9540 0.6024 -0.0949 -0.0841 0.0203  172 ILE C CB  
9602  C CG1 . ILE C 172 ? 0.7754 0.9618 0.5726 -0.0972 -0.0887 0.0322  172 ILE C CG1 
9603  C CG2 . ILE C 172 ? 0.8010 0.9447 0.6220 -0.0793 -0.0758 0.0270  172 ILE C CG2 
9604  C CD1 . ILE C 172 ? 0.8530 1.0550 0.6667 -0.0877 -0.0919 0.0545  172 ILE C CD1 
9605  N N   . ILE C 173 ? 0.8508 0.9512 0.6689 -0.0985 -0.0785 -0.0141 173 ILE C N   
9606  C CA  . ILE C 173 ? 0.8208 0.8920 0.6497 -0.0926 -0.0743 -0.0211 173 ILE C CA  
9607  C C   . ILE C 173 ? 0.8825 0.9351 0.7044 -0.0942 -0.0708 -0.0434 173 ILE C C   
9608  O O   . ILE C 173 ? 0.9520 0.9881 0.7791 -0.0844 -0.0636 -0.0487 173 ILE C O   
9609  C CB  . ILE C 173 ? 0.8646 0.9293 0.7060 -0.0993 -0.0810 -0.0162 173 ILE C CB  
9610  C CG1 . ILE C 173 ? 0.8225 0.9065 0.6738 -0.0944 -0.0812 0.0048  173 ILE C CG1 
9611  C CG2 . ILE C 173 ? 0.8011 0.8341 0.6518 -0.0959 -0.0792 -0.0241 173 ILE C CG2 
9612  C CD1 . ILE C 173 ? 0.7309 0.8283 0.5908 -0.1062 -0.0891 0.0121  173 ILE C CD1 
9613  N N   . LYS C 174 ? 0.9294 0.9854 0.7404 -0.1066 -0.0759 -0.0576 174 LYS C N   
9614  C CA  . LYS C 174 ? 0.9058 0.9451 0.7103 -0.1077 -0.0719 -0.0820 174 LYS C CA  
9615  C C   . LYS C 174 ? 0.8973 0.9465 0.6908 -0.1001 -0.0609 -0.0868 174 LYS C C   
9616  O O   . LYS C 174 ? 0.9383 0.9732 0.7327 -0.0959 -0.0539 -0.1052 174 LYS C O   
9617  C CB  . LYS C 174 ? 0.9746 1.0169 0.7669 -0.1233 -0.0802 -0.0973 174 LYS C CB  
9618  C CG  . LYS C 174 ? 1.0276 1.0592 0.8322 -0.1332 -0.0917 -0.0932 174 LYS C CG  
9619  C CD  . LYS C 174 ? 1.1189 1.1559 0.9114 -0.1505 -0.1019 -0.1064 174 LYS C CD  
9620  C CE  . LYS C 174 ? 1.0962 1.1290 0.8698 -0.1527 -0.0975 -0.1331 174 LYS C CE  
9621  N NZ  . LYS C 174 ? 1.1352 1.1383 0.9190 -0.1418 -0.0892 -0.1506 174 LYS C NZ  
9622  N N   . LYS C 175 ? 0.9055 0.9791 0.6905 -0.0983 -0.0594 -0.0702 175 LYS C N   
9623  C CA  . LYS C 175 ? 0.8855 0.9701 0.6607 -0.0925 -0.0494 -0.0704 175 LYS C CA  
9624  C C   . LYS C 175 ? 0.8986 0.9770 0.6885 -0.0790 -0.0438 -0.0551 175 LYS C C   
9625  O O   . LYS C 175 ? 0.8830 0.9683 0.6685 -0.0741 -0.0354 -0.0538 175 LYS C O   
9626  C CB  . LYS C 175 ? 0.9268 1.0418 0.6814 -0.1008 -0.0528 -0.0610 175 LYS C CB  
9627  C CG  . LYS C 175 ? 0.9050 1.0294 0.6368 -0.1135 -0.0537 -0.0810 175 LYS C CG  
9628  C CD  . LYS C 175 ? 1.1614 1.2926 0.8791 -0.1112 -0.0408 -0.0929 175 LYS C CD  
9629  C CE  . LYS C 175 ? 1.1634 1.3231 0.8506 -0.1237 -0.0424 -0.0941 175 LYS C CE  
9630  N NZ  . LYS C 175 ? 1.0507 1.2142 0.7199 -0.1265 -0.0304 -0.1189 175 LYS C NZ  
9631  N N   . THR C 176 ? 0.9080 0.9738 0.7144 -0.0738 -0.0481 -0.0441 176 THR C N   
9632  C CA  . THR C 176 ? 0.7768 0.8383 0.5947 -0.0620 -0.0445 -0.0287 176 THR C CA  
9633  C C   . THR C 176 ? 0.8179 0.8620 0.6441 -0.0537 -0.0364 -0.0382 176 THR C C   
9634  O O   . THR C 176 ? 0.8543 0.9033 0.6813 -0.0473 -0.0306 -0.0309 176 THR C O   
9635  C CB  . THR C 176 ? 0.6948 0.7486 0.5258 -0.0595 -0.0504 -0.0171 176 THR C CB  
9636  O OG1 . THR C 176 ? 0.9532 1.0287 0.7801 -0.0652 -0.0569 -0.0053 176 THR C OG1 
9637  C CG2 . THR C 176 ? 0.6972 0.7422 0.5386 -0.0471 -0.0466 -0.0054 176 THR C CG2 
9638  N N   . LEU C 177 ? 0.8094 0.8330 0.6441 -0.0539 -0.0367 -0.0536 177 LEU C N   
9639  C CA  . LEU C 177 ? 0.8918 0.9001 0.7387 -0.0452 -0.0300 -0.0618 177 LEU C CA  
9640  C C   . LEU C 177 ? 0.8903 0.9123 0.7290 -0.0453 -0.0201 -0.0734 177 LEU C C   
9641  O O   . LEU C 177 ? 0.8779 0.8965 0.7270 -0.0377 -0.0131 -0.0747 177 LEU C O   
9642  C CB  . LEU C 177 ? 0.8357 0.8183 0.6963 -0.0448 -0.0341 -0.0747 177 LEU C CB  
9643  C CG  . LEU C 177 ? 0.8295 0.7973 0.6997 -0.0441 -0.0424 -0.0614 177 LEU C CG  
9644  C CD1 . LEU C 177 ? 0.7580 0.6986 0.6427 -0.0440 -0.0476 -0.0714 177 LEU C CD1 
9645  C CD2 . LEU C 177 ? 0.8007 0.7690 0.6762 -0.0349 -0.0403 -0.0451 177 LEU C CD2 
9646  N N   . SER C 178 ? 0.8752 0.9149 0.6950 -0.0547 -0.0194 -0.0810 178 SER C N   
9647  C CA  . SER C 178 ? 0.9248 0.9806 0.7334 -0.0561 -0.0088 -0.0924 178 SER C CA  
9648  C C   . SER C 178 ? 0.9134 0.9882 0.7164 -0.0542 -0.0042 -0.0734 178 SER C C   
9649  O O   . SER C 178 ? 0.8163 0.9004 0.6193 -0.0520 0.0063  -0.0779 178 SER C O   
9650  C CB  . SER C 178 ? 0.9229 0.9920 0.7094 -0.0681 -0.0103 -0.1065 178 SER C CB  
9651  O OG  . SER C 178 ? 0.9623 1.0140 0.7535 -0.0725 -0.0199 -0.1152 178 SER C OG  
9652  N N   . ILE C 179 ? 0.8296 0.9107 0.6294 -0.0551 -0.0120 -0.0520 179 ILE C N   
9653  C CA  . ILE C 179 ? 0.8623 0.9586 0.6582 -0.0535 -0.0097 -0.0328 179 ILE C CA  
9654  C C   . ILE C 179 ? 0.8457 0.9289 0.6603 -0.0434 -0.0042 -0.0284 179 ILE C C   
9655  O O   . ILE C 179 ? 0.8711 0.9656 0.6841 -0.0430 0.0018  -0.0203 179 ILE C O   
9656  C CB  . ILE C 179 ? 0.8245 0.9282 0.6177 -0.0545 -0.0201 -0.0119 179 ILE C CB  
9657  C CG1 . ILE C 179 ? 0.8081 0.9325 0.5903 -0.0572 -0.0196 0.0058  179 ILE C CG1 
9658  C CG2 . ILE C 179 ? 0.7531 0.8379 0.5655 -0.0446 -0.0243 -0.0017 179 ILE C CG2 
9659  C CD1 . ILE C 179 ? 0.7635 0.9036 0.5371 -0.0622 -0.0301 0.0208  179 ILE C CD1 
9660  N N   . TYR C 180 ? 0.8342 0.8941 0.6664 -0.0362 -0.0069 -0.0331 180 TYR C N   
9661  C CA  . TYR C 180 ? 0.8262 0.8738 0.6760 -0.0274 -0.0036 -0.0285 180 TYR C CA  
9662  C C   . TYR C 180 ? 0.8141 0.8665 0.6700 -0.0266 0.0072  -0.0434 180 TYR C C   
9663  O O   . TYR C 180 ? 0.8184 0.8761 0.6821 -0.0237 0.0126  -0.0363 180 TYR C O   
9664  C CB  . TYR C 180 ? 0.7888 0.8118 0.6535 -0.0212 -0.0105 -0.0283 180 TYR C CB  
9665  C CG  . TYR C 180 ? 0.8208 0.8414 0.6833 -0.0195 -0.0183 -0.0112 180 TYR C CG  
9666  C CD1 . TYR C 180 ? 0.8074 0.8258 0.6751 -0.0136 -0.0191 0.0037  180 TYR C CD1 
9667  C CD2 . TYR C 180 ? 0.8289 0.8504 0.6856 -0.0239 -0.0247 -0.0108 180 TYR C CD2 
9668  C CE1 . TYR C 180 ? 0.7315 0.7480 0.5987 -0.0104 -0.0251 0.0169  180 TYR C CE1 
9669  C CE2 . TYR C 180 ? 0.8133 0.8361 0.6705 -0.0213 -0.0303 0.0040  180 TYR C CE2 
9670  C CZ  . TYR C 180 ? 0.7586 0.7788 0.6211 -0.0138 -0.0301 0.0169  180 TYR C CZ  
9671  O OH  . TYR C 180 ? 0.7384 0.7600 0.6026 -0.0096 -0.0345 0.0293  180 TYR C OH  
9672  N N   . ARG C 181 ? 0.7632 0.8146 0.6171 -0.0291 0.0105  -0.0644 181 ARG C N   
9673  C CA  . ARG C 181 ? 0.8027 0.8630 0.6626 -0.0277 0.0226  -0.0808 181 ARG C CA  
9674  C C   . ARG C 181 ? 0.8347 0.9244 0.6772 -0.0345 0.0315  -0.0748 181 ARG C C   
9675  O O   . ARG C 181 ? 0.8633 0.9632 0.7151 -0.0323 0.0406  -0.0725 181 ARG C O   
9676  C CB  . ARG C 181 ? 0.8138 0.8668 0.6733 -0.0290 0.0241  -0.1064 181 ARG C CB  
9677  C CG  . ARG C 181 ? 0.8180 0.8466 0.6826 -0.0287 0.0116  -0.1075 181 ARG C CG  
9678  C CD  . ARG C 181 ? 0.8723 0.8864 0.7451 -0.0277 0.0123  -0.1331 181 ARG C CD  
9679  N NE  . ARG C 181 ? 0.9901 0.9856 0.8610 -0.0323 -0.0001 -0.1335 181 ARG C NE  
9680  C CZ  . ARG C 181 ? 1.0470 1.0196 0.9310 -0.0307 -0.0047 -0.1494 181 ARG C CZ  
9681  N NH1 . ARG C 181 ? 1.0161 0.9805 0.9182 -0.0228 0.0018  -0.1676 181 ARG C NH1 
9682  N NH2 . ARG C 181 ? 1.0162 0.9742 0.8972 -0.0374 -0.0165 -0.1464 181 ARG C NH2 
9683  N N   . GLU C 182 ? 0.8482 0.9525 0.6657 -0.0439 0.0280  -0.0698 182 GLU C N   
9684  C CA  . GLU C 182 ? 0.8280 0.9614 0.6253 -0.0524 0.0354  -0.0637 182 GLU C CA  
9685  C C   . GLU C 182 ? 0.8592 0.9985 0.6639 -0.0507 0.0362  -0.0397 182 GLU C C   
9686  O O   . GLU C 182 ? 0.8714 1.0298 0.6732 -0.0543 0.0468  -0.0379 182 GLU C O   
9687  C CB  . GLU C 182 ? 0.9384 1.0848 0.7087 -0.0629 0.0279  -0.0597 182 GLU C CB  
9688  C CG  . GLU C 182 ? 1.0383 1.1858 0.8057 -0.0638 0.0162  -0.0322 182 GLU C CG  
9689  C CD  . GLU C 182 ? 1.2075 1.3784 0.9477 -0.0756 0.0110  -0.0239 182 GLU C CD  
9690  O OE1 . GLU C 182 ? 1.2521 1.4360 0.9864 -0.0784 0.0082  -0.0012 182 GLU C OE1 
9691  O OE2 . GLU C 182 ? 1.1993 1.3745 0.9247 -0.0826 0.0083  -0.0391 182 GLU C OE2 
9692  N N   . ILE C 183 ? 0.8214 0.9443 0.6362 -0.0454 0.0254  -0.0216 183 ILE C N   
9693  C CA  . ILE C 183 ? 0.8195 0.9446 0.6417 -0.0440 0.0248  0.0002  183 ILE C CA  
9694  C C   . ILE C 183 ? 0.7838 0.9009 0.6293 -0.0376 0.0320  -0.0050 183 ILE C C   
9695  O O   . ILE C 183 ? 0.7674 0.8939 0.6182 -0.0397 0.0363  0.0075  183 ILE C O   
9696  C CB  . ILE C 183 ? 0.8193 0.9291 0.6459 -0.0392 0.0117  0.0187  183 ILE C CB  
9697  C CG1 . ILE C 183 ? 0.8440 0.9270 0.6886 -0.0296 0.0068  0.0111  183 ILE C CG1 
9698  C CG2 . ILE C 183 ? 0.8732 0.9950 0.6802 -0.0456 0.0041  0.0253  183 ILE C CG2 
9699  C CD1 . ILE C 183 ? 0.7357 0.8025 0.5984 -0.0221 0.0040  0.0226  183 ILE C CD1 
9700  N N   . LYS C 184 ? 0.7798 0.8800 0.6409 -0.0305 0.0325  -0.0225 184 LYS C N   
9701  C CA  . LYS C 184 ? 0.8338 0.9280 0.7197 -0.0242 0.0383  -0.0284 184 LYS C CA  
9702  C C   . LYS C 184 ? 0.8649 0.9842 0.7508 -0.0281 0.0537  -0.0414 184 LYS C C   
9703  O O   . LYS C 184 ? 0.7846 0.9129 0.6865 -0.0273 0.0604  -0.0366 184 LYS C O   
9704  C CB  . LYS C 184 ? 0.7082 0.7769 0.6112 -0.0156 0.0325  -0.0415 184 LYS C CB  
9705  C CG  . LYS C 184 ? 0.8006 0.8597 0.7318 -0.0082 0.0339  -0.0433 184 LYS C CG  
9706  C CD  . LYS C 184 ? 0.8569 0.8925 0.8040 -0.0008 0.0278  -0.0566 184 LYS C CD  
9707  C CE  . LYS C 184 ? 0.8947 0.9371 0.8591 0.0031  0.0375  -0.0780 184 LYS C CE  
9708  N NZ  . LYS C 184 ? 0.9998 1.0558 0.9857 0.0057  0.0454  -0.0752 184 LYS C NZ  
9709  N N   . GLU C 185 ? 0.8952 1.0275 0.7631 -0.0330 0.0597  -0.0583 185 GLU C N   
9710  C CA  . GLU C 185 ? 0.8721 1.0307 0.7377 -0.0365 0.0761  -0.0733 185 GLU C CA  
9711  C C   . GLU C 185 ? 0.8575 1.0457 0.7029 -0.0479 0.0827  -0.0569 185 GLU C C   
9712  O O   . GLU C 185 ? 0.9338 1.1468 0.7812 -0.0512 0.0977  -0.0638 185 GLU C O   
9713  C CB  . GLU C 185 ? 0.8694 1.0305 0.7214 -0.0378 0.0806  -0.1003 185 GLU C CB  
9714  C CG  . GLU C 185 ? 0.9320 1.0619 0.7966 -0.0300 0.0705  -0.1142 185 GLU C CG  
9715  C CD  . GLU C 185 ? 1.1562 1.2672 1.0569 -0.0177 0.0703  -0.1209 185 GLU C CD  
9716  O OE1 . GLU C 185 ? 1.1370 1.2520 1.0561 -0.0143 0.0728  -0.1083 185 GLU C OE1 
9717  O OE2 . GLU C 185 ? 1.2346 1.3254 1.1461 -0.0121 0.0661  -0.1382 185 GLU C OE2 
9718  N N   . GLU C 186 ? 0.8600 1.0441 0.6077 -0.0203 0.0319  -0.0471 186 GLU C N   
9719  C CA  . GLU C 186 ? 0.9192 1.1234 0.6540 -0.0258 0.0361  -0.0289 186 GLU C CA  
9720  C C   . GLU C 186 ? 0.7858 0.9920 0.5419 -0.0320 0.0409  -0.0076 186 GLU C C   
9721  O O   . GLU C 186 ? 0.7387 0.9569 0.4868 -0.0377 0.0437  0.0109  186 GLU C O   
9722  C CB  . GLU C 186 ? 0.8961 1.0971 0.6129 -0.0304 0.0237  -0.0236 186 GLU C CB  
9723  C CG  . GLU C 186 ? 0.8665 1.0735 0.5527 -0.0277 0.0204  -0.0410 186 GLU C CG  
9724  C CD  . GLU C 186 ? 1.2229 1.4236 0.8975 -0.0334 0.0044  -0.0387 186 GLU C CD  
9725  O OE1 . GLU C 186 ? 1.2618 1.4591 0.9508 -0.0377 -0.0019 -0.0202 186 GLU C OE1 
9726  O OE2 . GLU C 186 ? 1.3429 1.5426 0.9940 -0.0334 -0.0018 -0.0555 186 GLU C OE2 
9727  N N   . GLY C 187 ? 0.7045 0.8977 0.4865 -0.0317 0.0413  -0.0095 187 GLY C N   
9728  C CA  . GLY C 187 ? 0.6922 0.8855 0.4931 -0.0386 0.0460  0.0079  187 GLY C CA  
9729  C C   . GLY C 187 ? 0.7255 0.9004 0.5316 -0.0445 0.0376  0.0241  187 GLY C C   
9730  O O   . GLY C 187 ? 0.7352 0.9056 0.5534 -0.0512 0.0409  0.0390  187 GLY C O   
9731  N N   . LYS C 188 ? 0.7326 0.8964 0.5299 -0.0422 0.0266  0.0216  188 LYS C N   
9732  C CA  . LYS C 188 ? 0.7221 0.8704 0.5251 -0.0450 0.0193  0.0374  188 LYS C CA  
9733  C C   . LYS C 188 ? 0.6592 0.7854 0.4855 -0.0447 0.0159  0.0349  188 LYS C C   
9734  O O   . LYS C 188 ? 0.6925 0.8039 0.5257 -0.0461 0.0125  0.0481  188 LYS C O   
9735  C CB  . LYS C 188 ? 0.7537 0.9035 0.5414 -0.0426 0.0086  0.0369  188 LYS C CB  
9736  C CG  . LYS C 188 ? 0.7375 0.9092 0.4996 -0.0439 0.0106  0.0431  188 LYS C CG  
9737  C CD  . LYS C 188 ? 0.9128 1.0852 0.6675 -0.0448 0.0030  0.0625  188 LYS C CD  
9738  C CE  . LYS C 188 ? 0.9351 1.1024 0.6957 -0.0482 0.0094  0.0857  188 LYS C CE  
9739  N NZ  . LYS C 188 ? 0.9371 1.0950 0.6988 -0.0458 0.0014  0.1045  188 LYS C NZ  
9740  N N   . GLY C 189 ? 0.6452 0.7684 0.4826 -0.0420 0.0171  0.0187  189 GLY C N   
9741  C CA  . GLY C 189 ? 0.6696 0.7742 0.5276 -0.0421 0.0141  0.0168  189 GLY C CA  
9742  C C   . GLY C 189 ? 0.6146 0.7206 0.4829 -0.0385 0.0161  0.0000  189 GLY C C   
9743  O O   . GLY C 189 ? 0.7439 0.8612 0.6028 -0.0341 0.0187  -0.0121 189 GLY C O   
9744  N N   . SER C 190 ? 0.5967 0.6902 0.4834 -0.0396 0.0150  -0.0007 190 SER C N   
9745  C CA  . SER C 190 ? 0.6813 0.7749 0.5800 -0.0356 0.0158  -0.0143 190 SER C CA  
9746  C C   . SER C 190 ? 0.7284 0.8041 0.6334 -0.0325 0.0064  -0.0210 190 SER C C   
9747  O O   . SER C 190 ? 0.7449 0.8084 0.6522 -0.0346 0.0012  -0.0130 190 SER C O   
9748  C CB  . SER C 190 ? 0.7035 0.8017 0.6188 -0.0404 0.0217  -0.0098 190 SER C CB  
9749  O OG  . SER C 190 ? 0.6725 0.7894 0.5842 -0.0455 0.0305  -0.0012 190 SER C OG  
9750  N N   . VAL C 191 ? 0.7678 0.8420 0.6750 -0.0270 0.0047  -0.0349 191 VAL C N   
9751  C CA  . VAL C 191 ? 0.7353 0.7938 0.6481 -0.0251 -0.0041 -0.0409 191 VAL C CA  
9752  C C   . VAL C 191 ? 0.6793 0.7335 0.6095 -0.0231 -0.0031 -0.0451 191 VAL C C   
9753  O O   . VAL C 191 ? 0.6720 0.7357 0.6063 -0.0189 0.0025  -0.0513 191 VAL C O   
9754  C CB  . VAL C 191 ? 0.7002 0.7552 0.5996 -0.0218 -0.0091 -0.0530 191 VAL C CB  
9755  C CG1 . VAL C 191 ? 0.7852 0.8262 0.6890 -0.0238 -0.0193 -0.0534 191 VAL C CG1 
9756  C CG2 . VAL C 191 ? 0.7308 0.7966 0.6104 -0.0235 -0.0082 -0.0509 191 VAL C CG2 
9757  N N   . SER C 192 ? 0.6958 0.7380 0.6359 -0.0250 -0.0085 -0.0413 192 SER C N   
9758  C CA  . SER C 192 ? 0.7235 0.7618 0.6786 -0.0237 -0.0091 -0.0443 192 SER C CA  
9759  C C   . SER C 192 ? 0.7662 0.7914 0.7238 -0.0215 -0.0171 -0.0491 192 SER C C   
9760  O O   . SER C 192 ? 0.7988 0.8189 0.7478 -0.0224 -0.0223 -0.0495 192 SER C O   
9761  C CB  . SER C 192 ? 0.6231 0.6593 0.5869 -0.0292 -0.0075 -0.0351 192 SER C CB  
9762  O OG  . SER C 192 ? 0.6082 0.6326 0.5687 -0.0310 -0.0117 -0.0286 192 SER C OG  
9763  N N   . THR C 193 ? 0.6711 0.6929 0.6408 -0.0195 -0.0184 -0.0516 193 THR C N   
9764  C CA  . THR C 193 ? 0.6626 0.6724 0.6360 -0.0185 -0.0256 -0.0540 193 THR C CA  
9765  C C   . THR C 193 ? 0.6755 0.6832 0.6608 -0.0201 -0.0268 -0.0490 193 THR C C   
9766  O O   . THR C 193 ? 0.6531 0.6669 0.6427 -0.0227 -0.0227 -0.0450 193 THR C O   
9767  C CB  . THR C 193 ? 0.7001 0.7046 0.6722 -0.0126 -0.0270 -0.0642 193 THR C CB  
9768  O OG1 . THR C 193 ? 0.7942 0.7851 0.7689 -0.0137 -0.0347 -0.0649 193 THR C OG1 
9769  C CG2 . THR C 193 ? 0.6856 0.6989 0.6681 -0.0068 -0.0218 -0.0667 193 THR C CG2 
9770  N N   . SER C 194 ? 0.7018 0.7011 0.6912 -0.0199 -0.0326 -0.0490 194 SER C N   
9771  C CA  . SER C 194 ? 0.6940 0.6920 0.6926 -0.0206 -0.0342 -0.0453 194 SER C CA  
9772  C C   . SER C 194 ? 0.6687 0.6622 0.6736 -0.0169 -0.0381 -0.0489 194 SER C C   
9773  O O   . SER C 194 ? 0.7328 0.7205 0.7340 -0.0137 -0.0396 -0.0546 194 SER C O   
9774  C CB  . SER C 194 ? 0.6818 0.6755 0.6788 -0.0235 -0.0370 -0.0389 194 SER C CB  
9775  O OG  . SER C 194 ? 0.7069 0.7020 0.6984 -0.0252 -0.0333 -0.0345 194 SER C OG  
9776  N N   . PRO C 195 ? 0.6994 0.6941 0.7124 -0.0168 -0.0398 -0.0457 195 PRO C N   
9777  C CA  . PRO C 195 ? 0.7098 0.6979 0.7279 -0.0137 -0.0448 -0.0461 195 PRO C CA  
9778  C C   . PRO C 195 ? 0.6667 0.6433 0.6795 -0.0165 -0.0498 -0.0454 195 PRO C C   
9779  O O   . PRO C 195 ? 0.6132 0.5913 0.6218 -0.0211 -0.0504 -0.0417 195 PRO C O   
9780  C CB  . PRO C 195 ? 0.7644 0.7575 0.7886 -0.0156 -0.0462 -0.0404 195 PRO C CB  
9781  C CG  . PRO C 195 ? 0.7273 0.7310 0.7526 -0.0177 -0.0414 -0.0409 195 PRO C CG  
9782  C CD  . PRO C 195 ? 0.7155 0.7178 0.7327 -0.0197 -0.0374 -0.0424 195 PRO C CD  
9783  N N   . TYR C 196 ? 0.6368 0.6020 0.6502 -0.0137 -0.0537 -0.0486 196 TYR C N   
9784  C CA  . TYR C 196 ? 0.6622 0.6143 0.6683 -0.0177 -0.0588 -0.0509 196 TYR C CA  
9785  C C   . TYR C 196 ? 0.7118 0.6675 0.7181 -0.0258 -0.0625 -0.0429 196 TYR C C   
9786  O O   . TYR C 196 ? 0.6790 0.6367 0.6789 -0.0305 -0.0640 -0.0433 196 TYR C O   
9787  C CB  . TYR C 196 ? 0.6611 0.5955 0.6685 -0.0143 -0.0633 -0.0536 196 TYR C CB  
9788  C CG  . TYR C 196 ? 0.6915 0.6084 0.6876 -0.0166 -0.0671 -0.0617 196 TYR C CG  
9789  C CD1 . TYR C 196 ? 0.7166 0.6271 0.7084 -0.0274 -0.0739 -0.0586 196 TYR C CD1 
9790  C CD2 . TYR C 196 ? 0.6459 0.5540 0.6352 -0.0081 -0.0639 -0.0727 196 TYR C CD2 
9791  C CE1 . TYR C 196 ? 0.7496 0.6432 0.7294 -0.0317 -0.0786 -0.0670 196 TYR C CE1 
9792  C CE2 . TYR C 196 ? 0.6741 0.5636 0.6497 -0.0103 -0.0675 -0.0822 196 TYR C CE2 
9793  C CZ  . TYR C 196 ? 0.7531 0.6343 0.7234 -0.0230 -0.0755 -0.0796 196 TYR C CZ  
9794  O OH  . TYR C 196 ? 0.7127 0.5745 0.6677 -0.0270 -0.0803 -0.0901 196 TYR C OH  
9795  N N   . TYR C 197 ? 0.6632 0.6222 0.6767 -0.0272 -0.0641 -0.0351 197 TYR C N   
9796  C CA  . TYR C 197 ? 0.6807 0.6455 0.6957 -0.0338 -0.0672 -0.0267 197 TYR C CA  
9797  C C   . TYR C 197 ? 0.6989 0.6780 0.7155 -0.0323 -0.0622 -0.0216 197 TYR C C   
9798  O O   . TYR C 197 ? 0.8012 0.7872 0.8210 -0.0344 -0.0631 -0.0140 197 TYR C O   
9799  C CB  . TYR C 197 ? 0.6921 0.6496 0.7120 -0.0372 -0.0727 -0.0207 197 TYR C CB  
9800  C CG  . TYR C 197 ? 0.7039 0.6417 0.7204 -0.0403 -0.0786 -0.0252 197 TYR C CG  
9801  C CD1 . TYR C 197 ? 0.6438 0.5778 0.6562 -0.0497 -0.0840 -0.0247 197 TYR C CD1 
9802  C CD2 . TYR C 197 ? 0.7013 0.6240 0.7182 -0.0335 -0.0791 -0.0301 197 TYR C CD2 
9803  C CE1 . TYR C 197 ? 0.6616 0.5734 0.6682 -0.0538 -0.0901 -0.0304 197 TYR C CE1 
9804  C CE2 . TYR C 197 ? 0.7275 0.6271 0.7389 -0.0350 -0.0841 -0.0355 197 TYR C CE2 
9805  C CZ  . TYR C 197 ? 0.7909 0.6831 0.7961 -0.0458 -0.0898 -0.0363 197 TYR C CZ  
9806  O OH  . TYR C 197 ? 0.9572 0.8223 0.9545 -0.0485 -0.0956 -0.0432 197 TYR C OH  
9807  N N   . HIS C 198 ? 0.5759 0.5586 0.5894 -0.0286 -0.0568 -0.0256 198 HIS C N   
9808  C CA  . HIS C 198 ? 0.7063 0.6964 0.7186 -0.0271 -0.0521 -0.0222 198 HIS C CA  
9809  C C   . HIS C 198 ? 0.6649 0.6582 0.6802 -0.0262 -0.0518 -0.0184 198 HIS C C   
9810  O O   . HIS C 198 ? 0.5919 0.5910 0.6061 -0.0257 -0.0502 -0.0134 198 HIS C O   
9811  C CB  . HIS C 198 ? 0.5335 0.5297 0.5432 -0.0281 -0.0520 -0.0174 198 HIS C CB  
9812  C CG  . HIS C 198 ? 0.5493 0.5471 0.5542 -0.0247 -0.0464 -0.0168 198 HIS C CG  
9813  N ND1 . HIS C 198 ? 0.5567 0.5572 0.5606 -0.0212 -0.0429 -0.0125 198 HIS C ND1 
9814  C CD2 . HIS C 198 ? 0.5975 0.5925 0.5972 -0.0239 -0.0434 -0.0197 198 HIS C CD2 
9815  C CE1 . HIS C 198 ? 0.5301 0.5263 0.5284 -0.0184 -0.0385 -0.0129 198 HIS C CE1 
9816  N NE2 . HIS C 198 ? 0.6129 0.6067 0.6091 -0.0208 -0.0388 -0.0164 198 HIS C NE2 
9817  N N   . PRO C 199 ? 0.6861 0.6777 0.7047 -0.0252 -0.0529 -0.0205 199 PRO C N   
9818  C CA  . PRO C 199 ? 0.6157 0.6120 0.6352 -0.0249 -0.0532 -0.0170 199 PRO C CA  
9819  C C   . PRO C 199 ? 0.7267 0.7248 0.7414 -0.0244 -0.0489 -0.0205 199 PRO C C   
9820  O O   . PRO C 199 ? 0.7842 0.7797 0.7967 -0.0247 -0.0458 -0.0246 199 PRO C O   
9821  C CB  . PRO C 199 ? 0.6670 0.6612 0.6925 -0.0237 -0.0573 -0.0170 199 PRO C CB  
9822  C CG  . PRO C 199 ? 0.6280 0.6190 0.6547 -0.0213 -0.0556 -0.0240 199 PRO C CG  
9823  C CD  . PRO C 199 ? 0.7149 0.7023 0.7364 -0.0231 -0.0538 -0.0260 199 PRO C CD  
9824  N N   . LEU C 200 ? 0.6607 0.6627 0.6727 -0.0246 -0.0491 -0.0187 200 LEU C N   
9825  C CA  . LEU C 200 ? 0.6233 0.6246 0.6293 -0.0261 -0.0467 -0.0232 200 LEU C CA  
9826  C C   . LEU C 200 ? 0.6211 0.6287 0.6330 -0.0280 -0.0503 -0.0247 200 LEU C C   
9827  O O   . LEU C 200 ? 0.7347 0.7487 0.7467 -0.0283 -0.0537 -0.0220 200 LEU C O   
9828  C CB  . LEU C 200 ? 0.6797 0.6814 0.6764 -0.0250 -0.0447 -0.0221 200 LEU C CB  
9829  C CG  . LEU C 200 ? 0.7539 0.7524 0.7459 -0.0209 -0.0401 -0.0200 200 LEU C CG  
9830  C CD1 . LEU C 200 ? 0.6297 0.6312 0.6126 -0.0175 -0.0373 -0.0190 200 LEU C CD1 
9831  C CD2 . LEU C 200 ? 0.7300 0.7176 0.7175 -0.0204 -0.0362 -0.0240 200 LEU C CD2 
9832  N N   . ILE C 201 ? 0.6122 0.6207 0.6294 -0.0286 -0.0495 -0.0281 201 ILE C N   
9833  C CA  . ILE C 201 ? 0.5622 0.5811 0.5883 -0.0283 -0.0525 -0.0284 201 ILE C CA  
9834  C C   . ILE C 201 ? 0.5497 0.5769 0.5734 -0.0329 -0.0552 -0.0287 201 ILE C C   
9835  O O   . ILE C 201 ? 0.6297 0.6671 0.6592 -0.0312 -0.0599 -0.0253 201 ILE C O   
9836  C CB  . ILE C 201 ? 0.6416 0.6636 0.6733 -0.0277 -0.0495 -0.0319 201 ILE C CB  
9837  C CG1 . ILE C 201 ? 0.7665 0.7815 0.8001 -0.0222 -0.0489 -0.0322 201 ILE C CG1 
9838  C CG2 . ILE C 201 ? 0.5990 0.6366 0.6411 -0.0269 -0.0516 -0.0318 201 ILE C CG2 
9839  C CD1 . ILE C 201 ? 0.7348 0.7485 0.7743 -0.0170 -0.0538 -0.0291 201 ILE C CD1 
9840  N N   . PRO C 202 ? 0.4692 0.4913 0.4832 -0.0388 -0.0530 -0.0326 202 PRO C N   
9841  C CA  . PRO C 202 ? 0.5141 0.5431 0.5233 -0.0447 -0.0569 -0.0342 202 PRO C CA  
9842  C C   . PRO C 202 ? 0.5549 0.5889 0.5601 -0.0420 -0.0607 -0.0302 202 PRO C C   
9843  O O   . PRO C 202 ? 0.6715 0.7192 0.6795 -0.0443 -0.0662 -0.0283 202 PRO C O   
9844  C CB  . PRO C 202 ? 0.5100 0.5240 0.5055 -0.0505 -0.0532 -0.0400 202 PRO C CB  
9845  C CG  . PRO C 202 ? 0.5314 0.5387 0.5310 -0.0498 -0.0484 -0.0402 202 PRO C CG  
9846  C CD  . PRO C 202 ? 0.5511 0.5607 0.5581 -0.0412 -0.0477 -0.0360 202 PRO C CD  
9847  N N   . ILE C 203 ? 0.5833 0.6095 0.5827 -0.0373 -0.0582 -0.0276 203 ILE C N   
9848  C CA  . ILE C 203 ? 0.6609 0.6941 0.6564 -0.0353 -0.0612 -0.0221 203 ILE C CA  
9849  C C   . ILE C 203 ? 0.6648 0.7075 0.6732 -0.0321 -0.0665 -0.0145 203 ILE C C   
9850  O O   . ILE C 203 ? 0.7277 0.7812 0.7353 -0.0324 -0.0714 -0.0096 203 ILE C O   
9851  C CB  . ILE C 203 ? 0.6378 0.6644 0.6265 -0.0313 -0.0566 -0.0195 203 ILE C CB  
9852  C CG1 . ILE C 203 ? 0.6394 0.6558 0.6135 -0.0318 -0.0512 -0.0268 203 ILE C CG1 
9853  C CG2 . ILE C 203 ? 0.6396 0.6764 0.6265 -0.0298 -0.0594 -0.0113 203 ILE C CG2 
9854  C CD1 . ILE C 203 ? 0.5822 0.5997 0.5467 -0.0267 -0.0471 -0.0242 203 ILE C CD1 
9855  N N   . LEU C 204 ? 0.6367 0.6744 0.6557 -0.0285 -0.0656 -0.0133 204 LEU C N   
9856  C CA  . LEU C 204 ? 0.6746 0.7157 0.7046 -0.0237 -0.0702 -0.0069 204 LEU C CA  
9857  C C   . LEU C 204 ? 0.7060 0.7620 0.7436 -0.0232 -0.0742 -0.0067 204 LEU C C   
9858  O O   . LEU C 204 ? 0.7624 0.8267 0.8046 -0.0199 -0.0796 0.0008  204 LEU C O   
9859  C CB  . LEU C 204 ? 0.6847 0.7146 0.7214 -0.0199 -0.0680 -0.0086 204 LEU C CB  
9860  C CG  . LEU C 204 ? 0.5950 0.6136 0.6267 -0.0212 -0.0657 -0.0072 204 LEU C CG  
9861  C CD1 . LEU C 204 ? 0.7460 0.7536 0.7833 -0.0182 -0.0661 -0.0087 204 LEU C CD1 
9862  C CD2 . LEU C 204 ? 0.6737 0.6948 0.7023 -0.0224 -0.0685 0.0017  204 LEU C CD2 
9863  N N   . LEU C 205 ? 0.6445 0.7058 0.6842 -0.0266 -0.0720 -0.0134 205 LEU C N   
9864  C CA  . LEU C 205 ? 0.6427 0.7233 0.6916 -0.0275 -0.0760 -0.0126 205 LEU C CA  
9865  C C   . LEU C 205 ? 0.6446 0.7371 0.6861 -0.0332 -0.0817 -0.0102 205 LEU C C   
9866  O O   . LEU C 205 ? 0.7129 0.8193 0.7605 -0.0295 -0.0877 -0.0027 205 LEU C O   
9867  C CB  . LEU C 205 ? 0.6282 0.7131 0.6805 -0.0326 -0.0720 -0.0193 205 LEU C CB  
9868  C CG  . LEU C 205 ? 0.6204 0.7001 0.6809 -0.0259 -0.0668 -0.0212 205 LEU C CG  
9869  C CD1 . LEU C 205 ? 0.5987 0.6819 0.6594 -0.0326 -0.0620 -0.0266 205 LEU C CD1 
9870  C CD2 . LEU C 205 ? 0.5388 0.6307 0.6140 -0.0154 -0.0692 -0.0167 205 LEU C CD2 
9871  N N   . ASN C 206 ? 0.6172 0.7037 0.6441 -0.0416 -0.0801 -0.0164 206 ASN C N   
9872  C CA  . ASN C 206 ? 0.6734 0.7689 0.6889 -0.0470 -0.0854 -0.0158 206 ASN C CA  
9873  C C   . ASN C 206 ? 0.7070 0.7858 0.7031 -0.0490 -0.0809 -0.0207 206 ASN C C   
9874  O O   . ASN C 206 ? 0.7098 0.7753 0.6970 -0.0539 -0.0765 -0.0293 206 ASN C O   
9875  C CB  . ASN C 206 ? 0.7156 0.8265 0.7323 -0.0570 -0.0900 -0.0201 206 ASN C CB  
9876  C CG  . ASN C 206 ? 0.8101 0.9273 0.8102 -0.0648 -0.0957 -0.0224 206 ASN C CG  
9877  O OD1 . ASN C 206 ? 0.8545 0.9718 0.8458 -0.0764 -0.0979 -0.0303 206 ASN C OD1 
9878  N ND2 . ASN C 206 ? 0.8068 0.9289 0.8011 -0.0595 -0.0986 -0.0154 206 ASN C ND2 
9879  N N   . PRO C 207 ? 0.6853 0.7648 0.6745 -0.0448 -0.0814 -0.0146 207 PRO C N   
9880  C CA  . PRO C 207 ? 0.6688 0.7364 0.6405 -0.0446 -0.0759 -0.0187 207 PRO C CA  
9881  C C   . PRO C 207 ? 0.6237 0.6888 0.5761 -0.0517 -0.0766 -0.0286 207 PRO C C   
9882  O O   . PRO C 207 ? 0.7118 0.7646 0.6485 -0.0498 -0.0707 -0.0339 207 PRO C O   
9883  C CB  . PRO C 207 ? 0.7313 0.8073 0.7023 -0.0396 -0.0774 -0.0075 207 PRO C CB  
9884  C CG  . PRO C 207 ? 0.6515 0.7339 0.6416 -0.0359 -0.0822 0.0019  207 PRO C CG  
9885  C CD  . PRO C 207 ? 0.6393 0.7308 0.6367 -0.0395 -0.0866 -0.0027 207 PRO C CD  
9886  N N   . ASN C 208 ? 0.6147 0.6910 0.5673 -0.0598 -0.0835 -0.0315 208 ASN C N   
9887  C CA  . ASN C 208 ? 0.6981 0.7682 0.6301 -0.0688 -0.0851 -0.0426 208 ASN C CA  
9888  C C   . ASN C 208 ? 0.6710 0.7183 0.5978 -0.0735 -0.0799 -0.0531 208 ASN C C   
9889  O O   . ASN C 208 ? 0.6356 0.6696 0.5428 -0.0808 -0.0802 -0.0637 208 ASN C O   
9890  C CB  . ASN C 208 ? 0.6199 0.7117 0.5540 -0.0783 -0.0956 -0.0418 208 ASN C CB  
9891  C CG  . ASN C 208 ? 0.5973 0.7094 0.5280 -0.0747 -0.1014 -0.0325 208 ASN C CG  
9892  O OD1 . ASN C 208 ? 0.6450 0.7771 0.5933 -0.0716 -0.1071 -0.0214 208 ASN C OD1 
9893  N ND2 . ASN C 208 ? 0.6860 0.7931 0.5936 -0.0742 -0.0995 -0.0364 208 ASN C ND2 
9894  N N   . CYS C 209 ? 0.6698 0.7106 0.6122 -0.0696 -0.0752 -0.0502 209 CYS C N   
9895  C CA  . CYS C 209 ? 0.7003 0.7199 0.6387 -0.0736 -0.0702 -0.0576 209 CYS C CA  
9896  C C   . CYS C 209 ? 0.7081 0.7035 0.6263 -0.0685 -0.0631 -0.0643 209 CYS C C   
9897  O O   . CYS C 209 ? 0.7098 0.6832 0.6182 -0.0728 -0.0601 -0.0718 209 CYS C O   
9898  C CB  . CYS C 209 ? 0.6688 0.6892 0.6265 -0.0687 -0.0664 -0.0520 209 CYS C CB  
9899  S SG  . CYS C 209 ? 0.6928 0.7111 0.6565 -0.0544 -0.0609 -0.0443 209 CYS C SG  
9900  N N   . VAL C 210 ? 0.6651 0.6644 0.5772 -0.0589 -0.0602 -0.0609 210 VAL C N   
9901  C CA  . VAL C 210 ? 0.7122 0.6928 0.6066 -0.0513 -0.0523 -0.0664 210 VAL C CA  
9902  C C   . VAL C 210 ? 0.8359 0.8021 0.7048 -0.0573 -0.0536 -0.0790 210 VAL C C   
9903  O O   . VAL C 210 ? 0.8444 0.7864 0.6967 -0.0525 -0.0470 -0.0872 210 VAL C O   
9904  C CB  . VAL C 210 ? 0.7912 0.7853 0.6879 -0.0403 -0.0486 -0.0578 210 VAL C CB  
9905  C CG1 . VAL C 210 ? 0.6309 0.6373 0.5517 -0.0374 -0.0496 -0.0463 210 VAL C CG1 
9906  C CG2 . VAL C 210 ? 0.7445 0.7550 0.6300 -0.0419 -0.0528 -0.0567 210 VAL C CG2 
9907  N N   . TYR C 211 ? 0.8021 0.7816 0.6666 -0.0676 -0.0622 -0.0812 211 TYR C N   
9908  C CA  . TYR C 211 ? 0.7758 0.7416 0.6136 -0.0752 -0.0649 -0.0945 211 TYR C CA  
9909  C C   . TYR C 211 ? 0.8443 0.7875 0.6773 -0.0884 -0.0676 -0.1038 211 TYR C C   
9910  O O   . TYR C 211 ? 0.9778 0.9020 0.7863 -0.0963 -0.0698 -0.1166 211 TYR C O   
9911  C CB  . TYR C 211 ? 0.7636 0.7552 0.5971 -0.0823 -0.0744 -0.0926 211 TYR C CB  
9912  C CG  . TYR C 211 ? 0.8183 0.8335 0.6568 -0.0716 -0.0731 -0.0810 211 TYR C CG  
9913  C CD1 . TYR C 211 ? 0.7951 0.8055 0.6166 -0.0605 -0.0650 -0.0828 211 TYR C CD1 
9914  C CD2 . TYR C 211 ? 0.7859 0.8284 0.6462 -0.0724 -0.0797 -0.0675 211 TYR C CD2 
9915  C CE1 . TYR C 211 ? 0.7295 0.7629 0.5559 -0.0527 -0.0638 -0.0705 211 TYR C CE1 
9916  C CE2 . TYR C 211 ? 0.6943 0.7552 0.5585 -0.0639 -0.0789 -0.0556 211 TYR C CE2 
9917  C CZ  . TYR C 211 ? 0.7211 0.7781 0.5686 -0.0553 -0.0712 -0.0567 211 TYR C CZ  
9918  O OH  . TYR C 211 ? 0.6865 0.7631 0.5382 -0.0488 -0.0704 -0.0433 211 TYR C OH  
9919  N N   . GLU C 212 ? 0.7504 0.6948 0.6048 -0.0920 -0.0675 -0.0977 212 GLU C N   
9920  C CA  . GLU C 212 ? 0.8371 0.7614 0.6877 -0.1061 -0.0698 -0.1045 212 GLU C CA  
9921  C C   . GLU C 212 ? 0.8204 0.7046 0.6520 -0.1004 -0.0615 -0.1129 212 GLU C C   
9922  O O   . GLU C 212 ? 0.9111 0.7684 0.7258 -0.1121 -0.0637 -0.1230 212 GLU C O   
9923  C CB  . GLU C 212 ? 0.8173 0.7576 0.6958 -0.1106 -0.0710 -0.0946 212 GLU C CB  
9924  C CG  . GLU C 212 ? 0.8183 0.7969 0.7188 -0.1080 -0.0762 -0.0840 212 GLU C CG  
9925  C CD  . GLU C 212 ? 0.8840 0.8806 0.8085 -0.1152 -0.0787 -0.0772 212 GLU C CD  
9926  O OE1 . GLU C 212 ? 0.7905 0.7716 0.7150 -0.1235 -0.0764 -0.0796 212 GLU C OE1 
9927  O OE2 . GLU C 212 ? 0.8974 0.9238 0.8404 -0.1119 -0.0827 -0.0688 212 GLU C OE2 
9928  N N   . THR C 213 ? 0.8611 0.7406 0.6951 -0.0827 -0.0523 -0.1083 213 THR C N   
9929  C CA  . THR C 213 ? 0.9297 0.7746 0.7472 -0.0728 -0.0435 -0.1143 213 THR C CA  
9930  C C   . THR C 213 ? 0.9544 0.7950 0.7525 -0.0579 -0.0374 -0.1198 213 THR C C   
9931  O O   . THR C 213 ? 0.9444 0.7531 0.7222 -0.0502 -0.0309 -0.1286 213 THR C O   
9932  C CB  . THR C 213 ? 0.8172 0.6618 0.6534 -0.0631 -0.0372 -0.1037 213 THR C CB  
9933  O OG1 . THR C 213 ? 0.7697 0.6484 0.6276 -0.0571 -0.0379 -0.0923 213 THR C OG1 
9934  C CG2 . THR C 213 ? 0.7257 0.5597 0.5709 -0.0765 -0.0400 -0.1017 213 THR C CG2 
9935  N N   . THR C 214 ? 0.9261 0.7977 0.7298 -0.0528 -0.0387 -0.1141 214 THR C N   
9936  C CA  . THR C 214 ? 0.9042 0.7786 0.6907 -0.0391 -0.0324 -0.1174 214 THR C CA  
9937  C C   . THR C 214 ? 0.7769 0.6761 0.5568 -0.0467 -0.0399 -0.1182 214 THR C C   
9938  O O   . THR C 214 ? 0.8380 0.7686 0.6342 -0.0441 -0.0420 -0.1060 214 THR C O   
9939  C CB  . THR C 214 ? 0.8160 0.7066 0.6189 -0.0225 -0.0242 -0.1051 214 THR C CB  
9940  O OG1 . THR C 214 ? 0.8004 0.7123 0.6321 -0.0271 -0.0286 -0.0920 214 THR C OG1 
9941  C CG2 . THR C 214 ? 0.7956 0.6589 0.5926 -0.0099 -0.0147 -0.1079 214 THR C CG2 
9942  N N   . PRO C 215 ? 0.8126 0.6972 0.5672 -0.0567 -0.0449 -0.1321 215 PRO C N   
9943  C CA  . PRO C 215 ? 0.8500 0.7603 0.5998 -0.0676 -0.0549 -0.1320 215 PRO C CA  
9944  C C   . PRO C 215 ? 0.8771 0.8112 0.6176 -0.0569 -0.0517 -0.1277 215 PRO C C   
9945  O O   . PRO C 215 ? 0.7746 0.7392 0.5235 -0.0626 -0.0595 -0.1188 215 PRO C O   
9946  C CB  . PRO C 215 ? 0.8120 0.6949 0.5336 -0.0817 -0.0606 -0.1500 215 PRO C CB  
9947  C CG  . PRO C 215 ? 0.8288 0.6766 0.5531 -0.0837 -0.0568 -0.1544 215 PRO C CG  
9948  C CD  . PRO C 215 ? 0.9072 0.7501 0.6390 -0.0622 -0.0438 -0.1478 215 PRO C CD  
9949  N N   . ASN C 216 ? 0.9288 0.8512 0.6517 -0.0413 -0.0404 -0.1328 216 ASN C N   
9950  C CA  . ASN C 216 ? 0.9315 0.8773 0.6417 -0.0320 -0.0364 -0.1296 216 ASN C CA  
9951  C C   . ASN C 216 ? 0.8958 0.8629 0.6272 -0.0172 -0.0276 -0.1132 216 ASN C C   
9952  O O   . ASN C 216 ? 1.0012 0.9802 0.7205 -0.0049 -0.0191 -0.1118 216 ASN C O   
9953  C CB  . ASN C 216 ? 1.0213 0.9437 0.6927 -0.0250 -0.0296 -0.1481 216 ASN C CB  
9954  C CG  . ASN C 216 ? 1.1041 1.0478 0.7521 -0.0291 -0.0341 -0.1516 216 ASN C CG  
9955  O OD1 . ASN C 216 ? 1.0291 1.0089 0.6886 -0.0266 -0.0351 -0.1365 216 ASN C OD1 
9956  N ND2 . ASN C 216 ? 1.0955 1.0156 0.7089 -0.0360 -0.0372 -0.1715 216 ASN C ND2 
9957  N N   . VAL C 217 ? 0.8472 0.8212 0.6096 -0.0190 -0.0297 -0.1008 217 VAL C N   
9958  C CA  . VAL C 217 ? 0.8370 0.8308 0.6202 -0.0081 -0.0233 -0.0852 217 VAL C CA  
9959  C C   . VAL C 217 ? 0.7665 0.7939 0.5580 -0.0116 -0.0286 -0.0713 217 VAL C C   
9960  O O   . VAL C 217 ? 0.7837 0.8204 0.5797 -0.0232 -0.0392 -0.0688 217 VAL C O   
9961  C CB  . VAL C 217 ? 0.7522 0.7383 0.5623 -0.0095 -0.0243 -0.0785 217 VAL C CB  
9962  C CG1 . VAL C 217 ? 0.8402 0.8298 0.6643 -0.0244 -0.0359 -0.0763 217 VAL C CG1 
9963  C CG2 . VAL C 217 ? 0.6659 0.6727 0.4970 -0.0013 -0.0197 -0.0629 217 VAL C CG2 
9964  N N   . LYS C 218 ? 0.8412 0.8883 0.6354 -0.0016 -0.0211 -0.0609 218 LYS C N   
9965  C CA  . LYS C 218 ? 0.8509 0.9283 0.6556 -0.0048 -0.0253 -0.0443 218 LYS C CA  
9966  C C   . LYS C 218 ? 0.8199 0.9035 0.6567 -0.0064 -0.0277 -0.0296 218 LYS C C   
9967  O O   . LYS C 218 ? 0.7736 0.8562 0.6210 0.0012  -0.0204 -0.0256 218 LYS C O   
9968  C CB  . LYS C 218 ? 0.8573 0.9550 0.6476 0.0049  -0.0160 -0.0396 218 LYS C CB  
9969  C CG  . LYS C 218 ? 0.9842 1.0663 0.7511 0.0174  -0.0042 -0.0549 218 LYS C CG  
9970  C CD  . LYS C 218 ? 0.9671 1.0535 0.6995 0.0191  -0.0021 -0.0656 218 LYS C CD  
9971  C CE  . LYS C 218 ? 0.9803 1.0369 0.6859 0.0294  0.0066  -0.0869 218 LYS C CE  
9972  N NZ  . LYS C 218 ? 0.9598 0.9816 0.6581 0.0188  -0.0018 -0.1025 218 LYS C NZ  
9973  N N   . ILE C 219 ? 0.8302 0.9200 0.6816 -0.0156 -0.0382 -0.0220 219 ILE C N   
9974  C CA  . ILE C 219 ? 0.8244 0.9174 0.7033 -0.0173 -0.0412 -0.0093 219 ILE C CA  
9975  C C   . ILE C 219 ? 0.8395 0.9523 0.7263 -0.0215 -0.0481 0.0065  219 ILE C C   
9976  O O   . ILE C 219 ? 0.6720 0.7947 0.5461 -0.0252 -0.0533 0.0066  219 ILE C O   
9977  C CB  . ILE C 219 ? 0.7389 0.8144 0.6305 -0.0222 -0.0463 -0.0159 219 ILE C CB  
9978  C CG1 . ILE C 219 ? 0.6581 0.7369 0.5471 -0.0306 -0.0563 -0.0189 219 ILE C CG1 
9979  C CG2 . ILE C 219 ? 0.7470 0.8014 0.6303 -0.0184 -0.0397 -0.0293 219 ILE C CG2 
9980  C CD1 . ILE C 219 ? 0.6495 0.7168 0.5527 -0.0356 -0.0607 -0.0238 219 ILE C CD1 
9981  N N   . PRO C 220 ? 0.8460 0.9640 0.7527 -0.0218 -0.0489 0.0205  220 PRO C N   
9982  C CA  . PRO C 220 ? 0.8047 0.9372 0.7186 -0.0256 -0.0553 0.0370  220 PRO C CA  
9983  C C   . PRO C 220 ? 0.7667 0.8970 0.6850 -0.0300 -0.0658 0.0368  220 PRO C C   
9984  O O   . PRO C 220 ? 0.8492 0.9669 0.7729 -0.0312 -0.0684 0.0263  220 PRO C O   
9985  C CB  . PRO C 220 ? 0.7861 0.9154 0.7208 -0.0262 -0.0546 0.0482  220 PRO C CB  
9986  C CG  . PRO C 220 ? 0.7249 0.8364 0.6665 -0.0240 -0.0517 0.0357  220 PRO C CG  
9987  C CD  . PRO C 220 ? 0.7111 0.8205 0.6337 -0.0192 -0.0446 0.0221  220 PRO C CD  
9988  N N   . ASP C 221 ? 0.6891 0.8342 0.6057 -0.0321 -0.0718 0.0498  221 ASP C N   
9989  C CA  . ASP C 221 ? 0.7593 0.9067 0.6827 -0.0345 -0.0822 0.0527  221 ASP C CA  
9990  C C   . ASP C 221 ? 0.7478 0.8818 0.6953 -0.0333 -0.0857 0.0580  221 ASP C C   
9991  O O   . ASP C 221 ? 0.8162 0.9470 0.7740 -0.0328 -0.0854 0.0709  221 ASP C O   
9992  C CB  . ASP C 221 ? 0.7867 0.9539 0.7019 -0.0358 -0.0877 0.0676  221 ASP C CB  
9993  C CG  . ASP C 221 ? 0.9055 1.0771 0.8324 -0.0362 -0.0989 0.0756  221 ASP C CG  
9994  O OD1 . ASP C 221 ? 0.8855 1.0523 0.8189 -0.0368 -0.1027 0.0649  221 ASP C OD1 
9995  O OD2 . ASP C 221 ? 0.8981 1.0789 0.8282 -0.0356 -0.1038 0.0936  221 ASP C OD2 
9996  N N   . PHE C 222 ? 0.7464 0.8722 0.7020 -0.0333 -0.0887 0.0478  222 PHE C N   
9997  C CA  . PHE C 222 ? 0.7450 0.8585 0.7213 -0.0306 -0.0912 0.0503  222 PHE C CA  
9998  C C   . PHE C 222 ? 0.7078 0.8302 0.6932 -0.0283 -0.1004 0.0612  222 PHE C C   
9999  O O   . PHE C 222 ? 0.8522 0.9803 0.8441 -0.0274 -0.1050 0.0564  222 PHE C O   
10000 C CB  . PHE C 222 ? 0.7365 0.8396 0.7172 -0.0311 -0.0884 0.0349  222 PHE C CB  
10001 C CG  . PHE C 222 ? 0.7344 0.8245 0.7121 -0.0309 -0.0800 0.0273  222 PHE C CG  
10002 C CD1 . PHE C 222 ? 0.7094 0.8010 0.6702 -0.0319 -0.0741 0.0203  222 PHE C CD1 
10003 C CD2 . PHE C 222 ? 0.7356 0.8122 0.7266 -0.0290 -0.0779 0.0269  222 PHE C CD2 
10004 C CE1 . PHE C 222 ? 0.6889 0.7702 0.6481 -0.0298 -0.0663 0.0147  222 PHE C CE1 
10005 C CE2 . PHE C 222 ? 0.6240 0.6917 0.6127 -0.0287 -0.0710 0.0213  222 PHE C CE2 
10006 C CZ  . PHE C 222 ? 0.6884 0.7592 0.6623 -0.0286 -0.0652 0.0160  222 PHE C CZ  
10007 N N   . ALA C 223 ? 0.6824 0.8072 0.6693 -0.0271 -0.1032 0.0777  223 ALA C N   
10008 C CA  . ALA C 223 ? 0.7216 0.8521 0.7176 -0.0229 -0.1119 0.0912  223 ALA C CA  
10009 C C   . ALA C 223 ? 0.6701 0.7806 0.6850 -0.0168 -0.1134 0.0943  223 ALA C C   
10010 O O   . ALA C 223 ? 0.6809 0.7880 0.7034 -0.0119 -0.1192 0.1086  223 ALA C O   
10011 C CB  . ALA C 223 ? 0.8124 0.9534 0.7993 -0.0247 -0.1145 0.1089  223 ALA C CB  
10012 N N   . VAL C 224 ? 0.7259 0.8218 0.7469 -0.0164 -0.1081 0.0811  224 VAL C N   
10013 C CA  . VAL C 224 ? 0.6642 0.7416 0.7003 -0.0100 -0.1089 0.0799  224 VAL C CA  
10014 C C   . VAL C 224 ? 0.7036 0.7822 0.7445 -0.0086 -0.1054 0.0636  224 VAL C C   
10015 O O   . VAL C 224 ? 0.6881 0.7727 0.7204 -0.0144 -0.1011 0.0529  224 VAL C O   
10016 C CB  . VAL C 224 ? 0.6371 0.6915 0.6753 -0.0124 -0.1059 0.0825  224 VAL C CB  
10017 C CG1 . VAL C 224 ? 0.7910 0.8342 0.8334 -0.0102 -0.1116 0.0997  224 VAL C CG1 
10018 C CG2 . VAL C 224 ? 0.7597 0.8192 0.7868 -0.0206 -0.1000 0.0796  224 VAL C CG2 
10019 N N   . SER C 225 ? 0.7762 0.8476 0.8305 -0.0004 -0.1069 0.0623  225 SER C N   
10020 C CA  . SER C 225 ? 0.6929 0.7670 0.7535 0.0014  -0.1032 0.0490  225 SER C CA  
10021 C C   . SER C 225 ? 0.7126 0.7640 0.7739 0.0014  -0.0975 0.0410  225 SER C C   
10022 O O   . SER C 225 ? 0.7121 0.7443 0.7778 0.0063  -0.0986 0.0452  225 SER C O   
10023 C CB  . SER C 225 ? 0.7447 0.8299 0.8197 0.0118  -0.1072 0.0521  225 SER C CB  
10024 O OG  . SER C 225 ? 0.7616 0.8444 0.8447 0.0156  -0.1022 0.0410  225 SER C OG  
10025 N N   . PHE C 226 ? 0.7039 0.7561 0.7596 -0.0045 -0.0919 0.0298  226 PHE C N   
10026 C CA  . PHE C 226 ? 0.6734 0.7089 0.7295 -0.0047 -0.0868 0.0215  226 PHE C CA  
10027 C C   . PHE C 226 ? 0.6941 0.7344 0.7575 -0.0005 -0.0837 0.0121  226 PHE C C   
10028 O O   . PHE C 226 ? 0.6542 0.6849 0.7159 -0.0016 -0.0788 0.0040  226 PHE C O   
10029 C CB  . PHE C 226 ? 0.7762 0.8095 0.8213 -0.0128 -0.0822 0.0173  226 PHE C CB  
10030 C CG  . PHE C 226 ? 0.7176 0.7466 0.7571 -0.0166 -0.0834 0.0265  226 PHE C CG  
10031 C CD1 . PHE C 226 ? 0.6641 0.6769 0.7070 -0.0167 -0.0850 0.0315  226 PHE C CD1 
10032 C CD2 . PHE C 226 ? 0.7144 0.7560 0.7444 -0.0207 -0.0828 0.0301  226 PHE C CD2 
10033 C CE1 . PHE C 226 ? 0.6618 0.6737 0.7011 -0.0221 -0.0861 0.0415  226 PHE C CE1 
10034 C CE2 . PHE C 226 ? 0.7008 0.7428 0.7263 -0.0240 -0.0828 0.0398  226 PHE C CE2 
10035 C CZ  . PHE C 226 ? 0.6876 0.7161 0.7190 -0.0254 -0.0846 0.0463  226 PHE C CZ  
10036 N N   . ARG C 227 ? 0.7710 0.8291 0.8430 0.0041  -0.0865 0.0140  227 ARG C N   
10037 C CA  . ARG C 227 ? 0.7162 0.7854 0.7961 0.0066  -0.0829 0.0063  227 ARG C CA  
10038 C C   . ARG C 227 ? 0.7066 0.7624 0.7932 0.0171  -0.0799 0.0031  227 ARG C C   
10039 O O   . ARG C 227 ? 0.7859 0.8416 0.8732 0.0173  -0.0741 -0.0055 227 ARG C O   
10040 C CB  . ARG C 227 ? 0.6439 0.7406 0.7330 0.0079  -0.0873 0.0106  227 ARG C CB  
10041 C CG  . ARG C 227 ? 0.7501 0.8599 0.8297 -0.0037 -0.0907 0.0113  227 ARG C CG  
10042 C CD  . ARG C 227 ? 0.7667 0.8886 0.8473 -0.0010 -0.0986 0.0228  227 ARG C CD  
10043 N NE  . ARG C 227 ? 0.8167 0.9534 0.8865 -0.0118 -0.1026 0.0224  227 ARG C NE  
10044 C CZ  . ARG C 227 ? 0.8356 0.9619 0.8884 -0.0191 -0.1012 0.0201  227 ARG C CZ  
10045 N NH1 . ARG C 227 ? 0.8560 0.9605 0.9028 -0.0180 -0.0959 0.0188  227 ARG C NH1 
10046 N NH2 . ARG C 227 ? 0.7677 0.9073 0.8090 -0.0275 -0.1052 0.0190  227 ARG C NH2 
10047 N N   . GLU C 228 ? 0.7134 0.7565 0.8037 0.0262  -0.0835 0.0098  228 GLU C N   
10048 C CA  . GLU C 228 ? 0.8241 0.8495 0.9177 0.0370  -0.0807 0.0049  228 GLU C CA  
10049 C C   . GLU C 228 ? 0.7815 0.7833 0.8639 0.0307  -0.0775 -0.0027 228 GLU C C   
10050 O O   . GLU C 228 ? 0.7986 0.7908 0.8800 0.0361  -0.0732 -0.0115 228 GLU C O   
10051 C CB  . GLU C 228 ? 0.8537 0.8660 0.9524 0.0484  -0.0860 0.0141  228 GLU C CB  
10052 C CG  . GLU C 228 ? 1.0191 1.0127 1.1213 0.0633  -0.0829 0.0080  228 GLU C CG  
10053 C CD  . GLU C 228 ? 1.1461 1.1635 1.2588 0.0736  -0.0770 0.0013  228 GLU C CD  
10054 O OE1 . GLU C 228 ? 1.1098 1.1142 1.2243 0.0878  -0.0732 -0.0046 228 GLU C OE1 
10055 O OE2 . GLU C 228 ? 1.0292 1.0781 1.1482 0.0678  -0.0759 0.0021  228 GLU C OE2 
10056 N N   . ASP C 229 ? 0.8045 0.7994 0.8783 0.0197  -0.0795 0.0010  229 ASP C N   
10057 C CA  . ASP C 229 ? 0.7319 0.7106 0.7966 0.0127  -0.0771 -0.0049 229 ASP C CA  
10058 C C   . ASP C 229 ? 0.7992 0.7888 0.8611 0.0091  -0.0709 -0.0143 229 ASP C C   
10059 O O   . ASP C 229 ? 0.8104 0.7890 0.8672 0.0085  -0.0679 -0.0215 229 ASP C O   
10060 C CB  . ASP C 229 ? 0.6814 0.6565 0.7400 0.0028  -0.0801 0.0029  229 ASP C CB  
10061 C CG  . ASP C 229 ? 0.8728 0.8305 0.9323 0.0038  -0.0861 0.0124  229 ASP C CG  
10062 O OD1 . ASP C 229 ? 0.9259 0.8698 0.9896 0.0131  -0.0880 0.0120  229 ASP C OD1 
10063 O OD2 . ASP C 229 ? 0.7970 0.7544 0.8527 -0.0044 -0.0885 0.0210  229 ASP C OD2 
10064 N N   . ALA C 230 ? 0.7522 0.7623 0.8163 0.0059  -0.0693 -0.0139 230 ALA C N   
10065 C CA  . ALA C 230 ? 0.7205 0.7391 0.7822 0.0018  -0.0636 -0.0213 230 ALA C CA  
10066 C C   . ALA C 230 ? 0.7648 0.7852 0.8312 0.0095  -0.0594 -0.0278 230 ALA C C   
10067 O O   . ALA C 230 ? 0.7963 0.8126 0.8569 0.0074  -0.0548 -0.0340 230 ALA C O   
10068 C CB  . ALA C 230 ? 0.6721 0.7098 0.7352 -0.0039 -0.0639 -0.0197 230 ALA C CB  
10069 N N   . SER C 231 ? 0.6948 0.7231 0.7715 0.0196  -0.0605 -0.0260 231 SER C N   
10070 C CA  . SER C 231 ? 0.7198 0.7511 0.8008 0.0296  -0.0554 -0.0324 231 SER C CA  
10071 C C   . SER C 231 ? 0.7627 0.7671 0.8339 0.0334  -0.0545 -0.0388 231 SER C C   
10072 O O   . SER C 231 ? 0.7055 0.7094 0.7723 0.0364  -0.0488 -0.0470 231 SER C O   
10073 C CB  . SER C 231 ? 0.7470 0.7925 0.8419 0.0423  -0.0568 -0.0281 231 SER C CB  
10074 O OG  . SER C 231 ? 0.8179 0.8951 0.9233 0.0409  -0.0541 -0.0269 231 SER C OG  
10075 N N   . LYS C 232 ? 0.7898 0.7725 0.8566 0.0322  -0.0604 -0.0349 232 LYS C N   
10076 C CA  . LYS C 232 ? 0.7535 0.7087 0.8099 0.0327  -0.0613 -0.0409 232 LYS C CA  
10077 C C   . LYS C 232 ? 0.6827 0.6372 0.7288 0.0227  -0.0585 -0.0466 232 LYS C C   
10078 O O   . LYS C 232 ? 0.7026 0.6470 0.7404 0.0252  -0.0558 -0.0557 232 LYS C O   
10079 C CB  . LYS C 232 ? 0.7535 0.6881 0.8081 0.0292  -0.0689 -0.0331 232 LYS C CB  
10080 C CG  . LYS C 232 ? 0.8171 0.7409 0.8784 0.0417  -0.0721 -0.0288 232 LYS C CG  
10081 C CD  . LYS C 232 ? 0.7850 0.6940 0.8458 0.0358  -0.0797 -0.0171 232 LYS C CD  
10082 C CE  . LYS C 232 ? 0.8714 0.7437 0.9259 0.0396  -0.0837 -0.0192 232 LYS C CE  
10083 N NZ  . LYS C 232 ? 0.9283 0.7922 0.9898 0.0571  -0.0843 -0.0169 232 LYS C NZ  
10084 N N   . HIS C 233 ? 0.6881 0.6530 0.7333 0.0123  -0.0591 -0.0414 233 HIS C N   
10085 C CA  . HIS C 233 ? 0.7014 0.6673 0.7379 0.0042  -0.0566 -0.0447 233 HIS C CA  
10086 C C   . HIS C 233 ? 0.7171 0.6933 0.7516 0.0077  -0.0497 -0.0521 233 HIS C C   
10087 O O   . HIS C 233 ? 0.6427 0.6120 0.6676 0.0064  -0.0480 -0.0580 233 HIS C O   
10088 C CB  . HIS C 233 ? 0.6914 0.6681 0.7284 -0.0041 -0.0569 -0.0380 233 HIS C CB  
10089 C CG  . HIS C 233 ? 0.7770 0.7457 0.8128 -0.0093 -0.0622 -0.0309 233 HIS C CG  
10090 N ND1 . HIS C 233 ? 0.7092 0.6703 0.7389 -0.0155 -0.0641 -0.0302 233 HIS C ND1 
10091 C CD2 . HIS C 233 ? 0.7775 0.7480 0.8176 -0.0097 -0.0660 -0.0230 233 HIS C CD2 
10092 C CE1 . HIS C 233 ? 0.7287 0.6880 0.7602 -0.0198 -0.0682 -0.0220 233 HIS C CE1 
10093 N NE2 . HIS C 233 ? 0.7211 0.6853 0.7580 -0.0163 -0.0692 -0.0175 233 HIS C NE2 
10094 N N   . VAL C 234 ? 0.6986 0.6934 0.7419 0.0115  -0.0460 -0.0511 234 VAL C N   
10095 C CA  . VAL C 234 ? 0.6672 0.6762 0.7100 0.0133  -0.0388 -0.0559 234 VAL C CA  
10096 C C   . VAL C 234 ? 0.6754 0.6785 0.7154 0.0247  -0.0356 -0.0641 234 VAL C C   
10097 O O   . VAL C 234 ? 0.7024 0.7076 0.7339 0.0251  -0.0305 -0.0701 234 VAL C O   
10098 C CB  . VAL C 234 ? 0.6828 0.7160 0.7372 0.0121  -0.0364 -0.0516 234 VAL C CB  
10099 C CG1 . VAL C 234 ? 0.6096 0.6587 0.6633 0.0108  -0.0288 -0.0545 234 VAL C CG1 
10100 C CG2 . VAL C 234 ? 0.6431 0.6778 0.6975 0.0017  -0.0402 -0.0453 234 VAL C CG2 
10101 N N   . GLU C 235 ? 0.6819 0.6770 0.7278 0.0348  -0.0383 -0.0643 235 GLU C N   
10102 C CA  . GLU C 235 ? 0.7256 0.7126 0.7680 0.0483  -0.0345 -0.0732 235 GLU C CA  
10103 C C   . GLU C 235 ? 0.7731 0.7313 0.7984 0.0460  -0.0373 -0.0813 235 GLU C C   
10104 O O   . GLU C 235 ? 0.8193 0.7736 0.8341 0.0518  -0.0324 -0.0914 235 GLU C O   
10105 C CB  . GLU C 235 ? 0.7506 0.7351 0.8044 0.0616  -0.0367 -0.0701 235 GLU C CB  
10106 C CG  . GLU C 235 ? 0.8698 0.8873 0.9413 0.0653  -0.0343 -0.0628 235 GLU C CG  
10107 C CD  . GLU C 235 ? 0.9587 0.9966 1.0368 0.0794  -0.0256 -0.0679 235 GLU C CD  
10108 O OE1 . GLU C 235 ? 0.9965 1.0451 1.0682 0.0765  -0.0185 -0.0735 235 GLU C OE1 
10109 O OE2 . GLU C 235 ? 0.9663 1.0116 1.0563 0.0942  -0.0254 -0.0653 235 GLU C OE2 
10110 N N   . LEU C 236 ? 0.7291 0.6685 0.7508 0.0369  -0.0453 -0.0769 236 LEU C N   
10111 C CA  . LEU C 236 ? 0.7427 0.6571 0.7489 0.0316  -0.0494 -0.0838 236 LEU C CA  
10112 C C   . LEU C 236 ? 0.6812 0.6057 0.6770 0.0230  -0.0466 -0.0872 236 LEU C C   
10113 O O   . LEU C 236 ? 0.7113 0.6221 0.6922 0.0217  -0.0475 -0.0962 236 LEU C O   
10114 C CB  . LEU C 236 ? 0.6718 0.5694 0.6792 0.0221  -0.0585 -0.0759 236 LEU C CB  
10115 C CG  . LEU C 236 ? 0.6619 0.5399 0.6746 0.0303  -0.0628 -0.0731 236 LEU C CG  
10116 C CD1 . LEU C 236 ? 0.7950 0.6606 0.8093 0.0188  -0.0713 -0.0629 236 LEU C CD1 
10117 C CD2 . LEU C 236 ? 0.6893 0.5404 0.6903 0.0399  -0.0622 -0.0858 236 LEU C CD2 
10118 N N   . ALA C 237 ? 0.6880 0.6351 0.6902 0.0171  -0.0435 -0.0799 237 ALA C N   
10119 C CA  . ALA C 237 ? 0.7178 0.6749 0.7108 0.0103  -0.0404 -0.0811 237 ALA C CA  
10120 C C   . ALA C 237 ? 0.7546 0.7207 0.7407 0.0181  -0.0325 -0.0897 237 ALA C C   
10121 O O   . ALA C 237 ? 0.7147 0.6780 0.6861 0.0154  -0.0317 -0.0954 237 ALA C O   
10122 C CB  . ALA C 237 ? 0.6812 0.6561 0.6823 0.0036  -0.0386 -0.0714 237 ALA C CB  
10123 N N   . LYS C 238 ? 0.7955 0.7754 0.7920 0.0277  -0.0266 -0.0899 238 LYS C N   
10124 C CA  . LYS C 238 ? 0.7901 0.7843 0.7822 0.0361  -0.0176 -0.0968 238 LYS C CA  
10125 C C   . LYS C 238 ? 0.7715 0.7452 0.7479 0.0449  -0.0174 -0.1101 238 LYS C C   
10126 O O   . LYS C 238 ? 0.8245 0.8048 0.7878 0.0478  -0.0113 -0.1175 238 LYS C O   
10127 C CB  . LYS C 238 ? 0.7616 0.7784 0.7714 0.0448  -0.0120 -0.0929 238 LYS C CB  
10128 C CG  . LYS C 238 ? 0.7301 0.7672 0.7528 0.0345  -0.0122 -0.0814 238 LYS C CG  
10129 C CD  . LYS C 238 ? 0.7800 0.8449 0.8204 0.0409  -0.0072 -0.0774 238 LYS C CD  
10130 C CE  . LYS C 238 ? 0.7145 0.7946 0.7539 0.0540  0.0023  -0.0843 238 LYS C CE  
10131 N NZ  . LYS C 238 ? 0.6236 0.7233 0.6818 0.0663  0.0045  -0.0816 238 LYS C NZ  
10132 N N   . GLU C 239 ? 0.7520 0.6992 0.7276 0.0485  -0.0241 -0.1133 239 GLU C N   
10133 C CA  . GLU C 239 ? 0.7995 0.7199 0.7572 0.0548  -0.0255 -0.1272 239 GLU C CA  
10134 C C   . GLU C 239 ? 0.8591 0.7678 0.7983 0.0411  -0.0312 -0.1311 239 GLU C C   
10135 O O   . GLU C 239 ? 0.8505 0.7514 0.7705 0.0439  -0.0290 -0.1434 239 GLU C O   
10136 C CB  . GLU C 239 ? 0.9146 0.8064 0.8766 0.0611  -0.0319 -0.1280 239 GLU C CB  
10137 C CG  . GLU C 239 ? 1.1428 0.9970 1.0859 0.0553  -0.0402 -0.1373 239 GLU C CG  
10138 C CD  . GLU C 239 ? 1.2642 1.0870 1.2112 0.0612  -0.0464 -0.1367 239 GLU C CD  
10139 O OE1 . GLU C 239 ? 1.3358 1.1235 1.2659 0.0620  -0.0508 -0.1479 239 GLU C OE1 
10140 O OE2 . GLU C 239 ? 1.3480 1.1801 1.3139 0.0643  -0.0473 -0.1246 239 GLU C OE2 
10141 N N   . LYS C 240 ? 0.8093 0.7192 0.7537 0.0267  -0.0385 -0.1207 240 LYS C N   
10142 C CA  . LYS C 240 ? 0.8253 0.7298 0.7549 0.0139  -0.0443 -0.1224 240 LYS C CA  
10143 C C   . LYS C 240 ? 0.7811 0.7088 0.7021 0.0127  -0.0376 -0.1229 240 LYS C C   
10144 O O   . LYS C 240 ? 0.8642 0.7875 0.7663 0.0087  -0.0395 -0.1305 240 LYS C O   
10145 C CB  . LYS C 240 ? 0.7379 0.6428 0.6773 0.0009  -0.0525 -0.1099 240 LYS C CB  
10146 C CG  . LYS C 240 ? 0.7183 0.6166 0.6445 -0.0120 -0.0606 -0.1112 240 LYS C CG  
10147 C CD  . LYS C 240 ? 0.8069 0.6765 0.7162 -0.0117 -0.0657 -0.1253 240 LYS C CD  
10148 C CE  . LYS C 240 ? 0.8402 0.6995 0.7414 -0.0279 -0.0773 -0.1242 240 LYS C CE  
10149 N NZ  . LYS C 240 ? 0.8158 0.6444 0.7179 -0.0318 -0.0854 -0.1263 240 LYS C NZ  
10150 N N   . TYR C 241 ? 0.6890 0.6412 0.6225 0.0153  -0.0301 -0.1145 241 TYR C N   
10151 C CA  . TYR C 241 ? 0.8051 0.7786 0.7306 0.0148  -0.0226 -0.1139 241 TYR C CA  
10152 C C   . TYR C 241 ? 0.8649 0.8379 0.7752 0.0255  -0.0158 -0.1277 241 TYR C C   
10153 O O   . TYR C 241 ? 0.9289 0.9086 0.8215 0.0230  -0.0136 -0.1319 241 TYR C O   
10154 C CB  . TYR C 241 ? 0.7658 0.7627 0.7083 0.0146  -0.0162 -0.1025 241 TYR C CB  
10155 C CG  . TYR C 241 ? 0.6642 0.6822 0.6006 0.0107  -0.0093 -0.0974 241 TYR C CG  
10156 C CD1 . TYR C 241 ? 0.7963 0.8306 0.7275 0.0182  0.0004  -0.1024 241 TYR C CD1 
10157 C CD2 . TYR C 241 ? 0.6568 0.6791 0.5930 0.0003  -0.0121 -0.0866 241 TYR C CD2 
10158 C CE1 . TYR C 241 ? 0.8656 0.9200 0.7912 0.0137  0.0069  -0.0959 241 TYR C CE1 
10159 C CE2 . TYR C 241 ? 0.7073 0.7463 0.6376 -0.0032 -0.0061 -0.0803 241 TYR C CE2 
10160 C CZ  . TYR C 241 ? 0.7276 0.7828 0.6525 0.0026  0.0032  -0.0845 241 TYR C CZ  
10161 O OH  . TYR C 241 ? 0.7974 0.8700 0.7161 -0.0019 0.0094  -0.0766 241 TYR C OH  
10162 N N   . PHE C 242 ? 0.7405 0.7057 0.6564 0.0386  -0.0124 -0.1349 242 PHE C N   
10163 C CA  . PHE C 242 ? 0.8076 0.7717 0.7087 0.0520  -0.0046 -0.1492 242 PHE C CA  
10164 C C   . PHE C 242 ? 0.8339 0.7700 0.7090 0.0490  -0.0111 -0.1632 242 PHE C C   
10165 O O   . PHE C 242 ? 0.9147 0.8546 0.7693 0.0536  -0.0057 -0.1741 242 PHE C O   
10166 C CB  . PHE C 242 ? 0.8153 0.7765 0.7298 0.0688  0.0003  -0.1527 242 PHE C CB  
10167 C CG  . PHE C 242 ? 0.9163 0.8751 0.8160 0.0860  0.0094  -0.1683 242 PHE C CG  
10168 C CD1 . PHE C 242 ? 0.8664 0.7886 0.7460 0.0920  0.0051  -0.1842 242 PHE C CD1 
10169 C CD2 . PHE C 242 ? 0.9685 0.9615 0.8741 0.0964  0.0226  -0.1670 242 PHE C CD2 
10170 C CE1 . PHE C 242 ? 0.8703 0.7880 0.7339 0.1096  0.0142  -0.2001 242 PHE C CE1 
10171 C CE2 . PHE C 242 ? 0.8504 0.8440 0.7422 0.1142  0.0324  -0.1815 242 PHE C CE2 
10172 C CZ  . PHE C 242 ? 0.8644 0.8193 0.7343 0.1218  0.0285  -0.1988 242 PHE C CZ  
10173 N N   . GLU C 243 ? 0.8238 0.7328 0.6986 0.0403  -0.0230 -0.1630 243 GLU C N   
10174 C CA  . GLU C 243 ? 0.8805 0.7624 0.7309 0.0340  -0.0312 -0.1759 243 GLU C CA  
10175 C C   . GLU C 243 ? 0.8769 0.7757 0.7114 0.0224  -0.0328 -0.1747 243 GLU C C   
10176 O O   . GLU C 243 ? 0.9655 0.8570 0.7746 0.0233  -0.0325 -0.1884 243 GLU C O   
10177 C CB  . GLU C 243 ? 0.9365 0.7912 0.7930 0.0234  -0.0441 -0.1722 243 GLU C CB  
10178 C CG  . GLU C 243 ? 1.1117 0.9564 0.9520 0.0057  -0.0557 -0.1743 243 GLU C CG  
10179 C CD  . GLU C 243 ? 1.2295 1.0420 1.0710 -0.0040 -0.0680 -0.1747 243 GLU C CD  
10180 O OE1 . GLU C 243 ? 1.2059 1.0076 1.0329 -0.0189 -0.0784 -0.1785 243 GLU C OE1 
10181 O OE2 . GLU C 243 ? 1.2929 1.0925 1.1499 0.0024  -0.0678 -0.1702 243 GLU C OE2 
10182 N N   . ILE C 244 ? 0.8919 0.8132 0.7399 0.0124  -0.0343 -0.1582 244 ILE C N   
10183 C CA  . ILE C 244 ? 0.8962 0.8333 0.7308 0.0018  -0.0370 -0.1542 244 ILE C CA  
10184 C C   . ILE C 244 ? 0.8962 0.8580 0.7213 0.0091  -0.0250 -0.1554 244 ILE C C   
10185 O O   . ILE C 244 ? 0.8824 0.8466 0.6832 0.0079  -0.0248 -0.1642 244 ILE C O   
10186 C CB  . ILE C 244 ? 0.8592 0.8091 0.7113 -0.0093 -0.0425 -0.1359 244 ILE C CB  
10187 C CG1 . ILE C 244 ? 0.8125 0.7422 0.6767 -0.0155 -0.0524 -0.1332 244 ILE C CG1 
10188 C CG2 . ILE C 244 ? 0.8559 0.8199 0.6941 -0.0193 -0.0470 -0.1311 244 ILE C CG2 
10189 C CD1 . ILE C 244 ? 0.7810 0.6897 0.6288 -0.0252 -0.0640 -0.1423 244 ILE C CD1 
10190 N N   . PHE C 245 ? 0.9351 0.9168 0.7785 0.0157  -0.0152 -0.1462 245 PHE C N   
10191 C CA  . PHE C 245 ? 0.9287 0.9386 0.7673 0.0193  -0.0039 -0.1422 245 PHE C CA  
10192 C C   . PHE C 245 ? 0.8843 0.9017 0.7207 0.0352  0.0082  -0.1528 245 PHE C C   
10193 O O   . PHE C 245 ? 0.9064 0.9511 0.7414 0.0383  0.0189  -0.1483 245 PHE C O   
10194 C CB  . PHE C 245 ? 0.8729 0.9027 0.7326 0.0133  -0.0011 -0.1233 245 PHE C CB  
10195 C CG  . PHE C 245 ? 0.9410 0.9658 0.8042 0.0009  -0.0111 -0.1120 245 PHE C CG  
10196 C CD1 . PHE C 245 ? 0.9008 0.9352 0.7491 -0.0065 -0.0136 -0.1064 245 PHE C CD1 
10197 C CD2 . PHE C 245 ? 0.8515 0.8645 0.7328 -0.0025 -0.0176 -0.1061 245 PHE C CD2 
10198 C CE1 . PHE C 245 ? 0.7604 0.7929 0.6136 -0.0157 -0.0223 -0.0952 245 PHE C CE1 
10199 C CE2 . PHE C 245 ? 0.7833 0.7945 0.6683 -0.0120 -0.0255 -0.0957 245 PHE C CE2 
10200 C CZ  . PHE C 245 ? 0.8206 0.8418 0.6923 -0.0180 -0.0278 -0.0902 245 PHE C CZ  
10201 N N   . GLY C 246 ? 0.8272 0.8223 0.6639 0.0457  0.0073  -0.1654 246 GLY C N   
10202 C CA  . GLY C 246 ? 0.8250 0.8263 0.6564 0.0635  0.0190  -0.1773 246 GLY C CA  
10203 C C   . GLY C 246 ? 0.9585 0.9883 0.8152 0.0722  0.0297  -0.1674 246 GLY C C   
10204 O O   . GLY C 246 ? 1.0212 1.0612 0.8770 0.0888  0.0404  -0.1758 246 GLY C O   
10205 N N   . GLU C 247 ? 1.0078 1.0515 0.8866 0.0617  0.0271  -0.1502 247 GLU C N   
10206 C CA  . GLU C 247 ? 0.9180 0.9894 0.8218 0.0660  0.0349  -0.1396 247 GLU C CA  
10207 C C   . GLU C 247 ? 0.9048 0.9668 0.8301 0.0578  0.0258  -0.1287 247 GLU C C   
10208 O O   . GLU C 247 ? 0.8589 0.8992 0.7800 0.0475  0.0152  -0.1267 247 GLU C O   
10209 C CB  . GLU C 247 ? 0.7383 0.8440 0.6425 0.0588  0.0436  -0.1285 247 GLU C CB  
10210 C CG  . GLU C 247 ? 0.9939 1.1342 0.9180 0.0662  0.0551  -0.1222 247 GLU C CG  
10211 C CD  . GLU C 247 ? 1.1395 1.2788 1.0697 0.0868  0.0602  -0.1338 247 GLU C CD  
10212 O OE1 . GLU C 247 ? 1.2269 1.3685 1.1397 0.1003  0.0684  -0.1467 247 GLU C OE1 
10213 O OE2 . GLU C 247 ? 1.1302 1.2668 1.0819 0.0904  0.0564  -0.1297 247 GLU C OE2 
10214 N N   . HIS C 248 ? 0.8755 0.9565 0.8239 0.0626  0.0300  -0.1215 248 HIS C N   
10215 C CA  . HIS C 248 ? 0.8043 0.8797 0.7714 0.0543  0.0220  -0.1110 248 HIS C CA  
10216 C C   . HIS C 248 ? 0.7668 0.8565 0.7383 0.0381  0.0215  -0.0976 248 HIS C C   
10217 O O   . HIS C 248 ? 0.8217 0.9334 0.7893 0.0349  0.0294  -0.0936 248 HIS C O   
10218 C CB  . HIS C 248 ? 0.7846 0.8744 0.7737 0.0651  0.0249  -0.1085 248 HIS C CB  
10219 C CG  . HIS C 248 ? 0.8279 0.8916 0.8173 0.0776  0.0199  -0.1169 248 HIS C CG  
10220 N ND1 . HIS C 248 ? 0.8092 0.8804 0.8059 0.0966  0.0261  -0.1225 248 HIS C ND1 
10221 C CD2 . HIS C 248 ? 0.9001 0.9300 0.8833 0.0740  0.0093  -0.1195 248 HIS C CD2 
10222 C CE1 . HIS C 248 ? 0.9787 1.0180 0.9728 0.1044  0.0192  -0.1284 248 HIS C CE1 
10223 N NE2 . HIS C 248 ? 1.0262 1.0405 1.0122 0.0898  0.0089  -0.1264 248 HIS C NE2 
10224 N N   . PRO C 249 ? 0.7645 0.8407 0.7426 0.0279  0.0127  -0.0903 249 PRO C N   
10225 C CA  . PRO C 249 ? 0.7215 0.8044 0.7010 0.0139  0.0119  -0.0787 249 PRO C CA  
10226 C C   . PRO C 249 ? 0.8075 0.9125 0.8053 0.0095  0.0158  -0.0695 249 PRO C C   
10227 O O   . PRO C 249 ? 0.7752 0.8828 0.7884 0.0126  0.0131  -0.0687 249 PRO C O   
10228 C CB  . PRO C 249 ? 0.7737 0.8326 0.7523 0.0076  0.0014  -0.0765 249 PRO C CB  
10229 C CG  . PRO C 249 ? 0.7855 0.8340 0.7734 0.0159  -0.0026 -0.0817 249 PRO C CG  
10230 C CD  . PRO C 249 ? 0.7713 0.8233 0.7537 0.0292  0.0032  -0.0925 249 PRO C CD  
10231 N N   . VAL C 250 ? 0.8262 0.9473 0.8221 0.0009  0.0214  -0.0617 250 VAL C N   
10232 C CA  . VAL C 250 ? 0.7148 0.8553 0.7266 -0.0076 0.0241  -0.0520 250 VAL C CA  
10233 C C   . VAL C 250 ? 0.6628 0.7876 0.6752 -0.0210 0.0178  -0.0438 250 VAL C C   
10234 O O   . VAL C 250 ? 0.6031 0.7371 0.6280 -0.0293 0.0172  -0.0375 250 VAL C O   
10235 C CB  . VAL C 250 ? 0.6019 0.7703 0.6126 -0.0105 0.0345  -0.0469 250 VAL C CB  
10236 C CG1 . VAL C 250 ? 0.5715 0.7637 0.5892 0.0035  0.0420  -0.0536 250 VAL C CG1 
10237 C CG2 . VAL C 250 ? 0.7157 0.8756 0.7049 -0.0132 0.0366  -0.0461 250 VAL C CG2 
10238 N N   . TYR C 251 ? 0.7338 0.8361 0.7327 -0.0231 0.0132  -0.0436 251 TYR C N   
10239 C CA  . TYR C 251 ? 0.6755 0.7614 0.6728 -0.0329 0.0084  -0.0363 251 TYR C CA  
10240 C C   . TYR C 251 ? 0.7377 0.8028 0.7335 -0.0289 0.0003  -0.0404 251 TYR C C   
10241 O O   . TYR C 251 ? 0.7373 0.7955 0.7260 -0.0220 -0.0021 -0.0468 251 TYR C O   
10242 C CB  . TYR C 251 ? 0.6121 0.6943 0.5957 -0.0386 0.0113  -0.0289 251 TYR C CB  
10243 C CG  . TYR C 251 ? 0.6799 0.7848 0.6631 -0.0423 0.0200  -0.0241 251 TYR C CG  
10244 C CD1 . TYR C 251 ? 0.7481 0.8700 0.7452 -0.0492 0.0236  -0.0196 251 TYR C CD1 
10245 C CD2 . TYR C 251 ? 0.7155 0.8278 0.6842 -0.0395 0.0246  -0.0236 251 TYR C CD2 
10246 C CE1 . TYR C 251 ? 0.8137 0.9605 0.8121 -0.0535 0.0321  -0.0138 251 TYR C CE1 
10247 C CE2 . TYR C 251 ? 0.6939 0.8301 0.6618 -0.0428 0.0336  -0.0182 251 TYR C CE2 
10248 C CZ  . TYR C 251 ? 0.7341 0.8880 0.7177 -0.0499 0.0376  -0.0129 251 TYR C CZ  
10249 O OH  . TYR C 251 ? 0.8613 1.0429 0.8459 -0.0542 0.0470  -0.0061 251 TYR C OH  
10250 N N   . MET C 252 ? 0.7523 0.8075 0.7537 -0.0341 -0.0040 -0.0369 252 MET C N   
10251 C CA  . MET C 252 ? 0.7460 0.7850 0.7468 -0.0310 -0.0108 -0.0392 252 MET C CA  
10252 C C   . MET C 252 ? 0.7280 0.7531 0.7251 -0.0370 -0.0129 -0.0332 252 MET C C   
10253 O O   . MET C 252 ? 0.6595 0.6846 0.6579 -0.0443 -0.0106 -0.0289 252 MET C O   
10254 C CB  . MET C 252 ? 0.6777 0.7203 0.6901 -0.0270 -0.0142 -0.0432 252 MET C CB  
10255 C CG  . MET C 252 ? 0.7607 0.8001 0.7721 -0.0177 -0.0162 -0.0500 252 MET C CG  
10256 S SD  . MET C 252 ? 0.8095 0.8508 0.8342 -0.0117 -0.0205 -0.0523 252 MET C SD  
10257 C CE  . MET C 252 ? 0.5706 0.6026 0.5899 -0.0007 -0.0212 -0.0609 252 MET C CE  
10258 N N   . TRP C 253 ? 0.7206 0.7335 0.7129 -0.0339 -0.0172 -0.0329 253 TRP C N   
10259 C CA  . TRP C 253 ? 0.7227 0.7225 0.7121 -0.0361 -0.0188 -0.0284 253 TRP C CA  
10260 C C   . TRP C 253 ? 0.7178 0.7145 0.7133 -0.0343 -0.0232 -0.0312 253 TRP C C   
10261 O O   . TRP C 253 ? 0.6687 0.6652 0.6655 -0.0300 -0.0269 -0.0330 253 TRP C O   
10262 C CB  . TRP C 253 ? 0.5793 0.5726 0.5602 -0.0330 -0.0198 -0.0240 253 TRP C CB  
10263 C CG  . TRP C 253 ? 0.6351 0.6168 0.6144 -0.0313 -0.0213 -0.0204 253 TRP C CG  
10264 C CD1 . TRP C 253 ? 0.6296 0.6107 0.6104 -0.0269 -0.0251 -0.0199 253 TRP C CD1 
10265 C CD2 . TRP C 253 ? 0.6969 0.6658 0.6723 -0.0337 -0.0187 -0.0171 253 TRP C CD2 
10266 N NE1 . TRP C 253 ? 0.7043 0.6757 0.6825 -0.0245 -0.0240 -0.0165 253 TRP C NE1 
10267 C CE2 . TRP C 253 ? 0.7335 0.6946 0.7072 -0.0282 -0.0202 -0.0156 253 TRP C CE2 
10268 C CE3 . TRP C 253 ? 0.7054 0.6679 0.6780 -0.0404 -0.0151 -0.0151 253 TRP C CE3 
10269 C CZ2 . TRP C 253 ? 0.7535 0.6982 0.7211 -0.0273 -0.0179 -0.0139 253 TRP C CZ2 
10270 C CZ3 . TRP C 253 ? 0.7199 0.6634 0.6863 -0.0417 -0.0139 -0.0131 253 TRP C CZ3 
10271 C CH2 . TRP C 253 ? 0.7166 0.6501 0.6797 -0.0342 -0.0151 -0.0133 253 TRP C CH2 
10272 N N   . PRO C 254 ? 0.6332 0.6275 0.6315 -0.0385 -0.0234 -0.0313 254 PRO C N   
10273 C CA  . PRO C 254 ? 0.6782 0.6703 0.6797 -0.0367 -0.0276 -0.0330 254 PRO C CA  
10274 C C   . PRO C 254 ? 0.6529 0.6356 0.6486 -0.0326 -0.0287 -0.0303 254 PRO C C   
10275 O O   . PRO C 254 ? 0.5634 0.5364 0.5517 -0.0323 -0.0261 -0.0272 254 PRO C O   
10276 C CB  . PRO C 254 ? 0.6434 0.6337 0.6449 -0.0438 -0.0274 -0.0338 254 PRO C CB  
10277 C CG  . PRO C 254 ? 0.6857 0.6699 0.6817 -0.0493 -0.0232 -0.0311 254 PRO C CG  
10278 C CD  . PRO C 254 ? 0.6195 0.6126 0.6167 -0.0464 -0.0204 -0.0295 254 PRO C CD  
10279 N N   . PRO C 255 ? 0.6396 0.6255 0.6390 -0.0289 -0.0324 -0.0304 255 PRO C N   
10280 C CA  . PRO C 255 ? 0.6431 0.6257 0.6392 -0.0253 -0.0333 -0.0265 255 PRO C CA  
10281 C C   . PRO C 255 ? 0.6250 0.6002 0.6155 -0.0244 -0.0312 -0.0257 255 PRO C C   
10282 O O   . PRO C 255 ? 0.6137 0.5884 0.6042 -0.0268 -0.0321 -0.0286 255 PRO C O   
10283 C CB  . PRO C 255 ? 0.4960 0.4843 0.4985 -0.0244 -0.0381 -0.0263 255 PRO C CB  
10284 C CG  . PRO C 255 ? 0.5818 0.5730 0.5889 -0.0252 -0.0392 -0.0306 255 PRO C CG  
10285 C CD  . PRO C 255 ? 0.6104 0.6032 0.6176 -0.0278 -0.0360 -0.0328 255 PRO C CD  
10286 N N   . GLN C 256 ? 0.6794 0.6489 0.6641 -0.0202 -0.0283 -0.0219 256 GLN C N   
10287 C CA  . GLN C 256 ? 0.7019 0.6604 0.6786 -0.0167 -0.0250 -0.0220 256 GLN C CA  
10288 C C   . GLN C 256 ? 0.6951 0.6395 0.6651 -0.0225 -0.0230 -0.0263 256 GLN C C   
10289 O O   . GLN C 256 ? 0.6829 0.6153 0.6445 -0.0218 -0.0214 -0.0295 256 GLN C O   
10290 C CB  . GLN C 256 ? 0.7369 0.7009 0.7140 -0.0140 -0.0262 -0.0227 256 GLN C CB  
10291 C CG  . GLN C 256 ? 0.6311 0.6096 0.6152 -0.0103 -0.0281 -0.0167 256 GLN C CG  
10292 C CD  . GLN C 256 ? 0.6287 0.6089 0.6110 -0.0026 -0.0249 -0.0108 256 GLN C CD  
10293 O OE1 . GLN C 256 ? 0.6504 0.6186 0.6245 0.0030  -0.0202 -0.0113 256 GLN C OE1 
10294 N NE2 . GLN C 256 ? 0.5907 0.5854 0.5807 -0.0025 -0.0280 -0.0050 256 GLN C NE2 
10295 N N   . ALA C 257 ? 0.7187 0.6651 0.6918 -0.0287 -0.0231 -0.0265 257 ALA C N   
10296 C CA  . ALA C 257 ? 0.7286 0.6659 0.6981 -0.0373 -0.0220 -0.0291 257 ALA C CA  
10297 C C   . ALA C 257 ? 0.7229 0.6636 0.6938 -0.0430 -0.0252 -0.0348 257 ALA C C   
10298 O O   . ALA C 257 ? 0.7545 0.6864 0.7207 -0.0515 -0.0254 -0.0376 257 ALA C O   
10299 C CB  . ALA C 257 ? 0.6959 0.6102 0.6533 -0.0362 -0.0182 -0.0272 257 ALA C CB  
10300 N N   . SER C 258 ? 0.6956 0.6496 0.6728 -0.0395 -0.0285 -0.0357 258 SER C N   
10301 C CA  . SER C 258 ? 0.7127 0.6722 0.6905 -0.0437 -0.0323 -0.0395 258 SER C CA  
10302 C C   . SER C 258 ? 0.7638 0.7349 0.7500 -0.0522 -0.0346 -0.0408 258 SER C C   
10303 O O   . SER C 258 ? 0.7377 0.7223 0.7346 -0.0505 -0.0347 -0.0388 258 SER C O   
10304 C CB  . SER C 258 ? 0.6850 0.6564 0.6683 -0.0378 -0.0353 -0.0376 258 SER C CB  
10305 O OG  . SER C 258 ? 0.9027 0.8676 0.8778 -0.0317 -0.0333 -0.0366 258 SER C OG  
10306 N N   . VAL C 259 ? 0.7169 0.6839 0.6981 -0.0612 -0.0364 -0.0443 259 VAL C N   
10307 C CA  . VAL C 259 ? 0.7013 0.6837 0.6919 -0.0707 -0.0389 -0.0444 259 VAL C CA  
10308 C C   . VAL C 259 ? 0.7302 0.7177 0.7178 -0.0776 -0.0447 -0.0482 259 VAL C C   
10309 O O   . VAL C 259 ? 0.7503 0.7223 0.7236 -0.0779 -0.0455 -0.0525 259 VAL C O   
10310 C CB  . VAL C 259 ? 0.7686 0.7426 0.7569 -0.0800 -0.0355 -0.0431 259 VAL C CB  
10311 C CG1 . VAL C 259 ? 0.7153 0.6952 0.7099 -0.0743 -0.0307 -0.0384 259 VAL C CG1 
10312 C CG2 . VAL C 259 ? 0.7058 0.6496 0.6764 -0.0828 -0.0338 -0.0459 259 VAL C CG2 
10313 N N   . SER C 260 ? 0.7023 0.7136 0.7031 -0.0825 -0.0487 -0.0467 260 SER C N   
10314 C CA  . SER C 260 ? 0.6694 0.6915 0.6693 -0.0908 -0.0556 -0.0491 260 SER C CA  
10315 C C   . SER C 260 ? 0.7368 0.7865 0.7540 -0.0981 -0.0580 -0.0455 260 SER C C   
10316 O O   . SER C 260 ? 0.6860 0.7469 0.7155 -0.0933 -0.0537 -0.0416 260 SER C O   
10317 C CB  . SER C 260 ? 0.6368 0.6667 0.6362 -0.0820 -0.0594 -0.0481 260 SER C CB  
10318 O OG  . SER C 260 ? 0.7468 0.7992 0.7637 -0.0747 -0.0611 -0.0425 260 SER C OG  
10319 N N   . ASN C 261 ? 0.7650 0.8274 0.7825 -0.1098 -0.0649 -0.0470 261 ASN C N   
10320 C CA  . ASN C 261 ? 0.6701 0.7661 0.7069 -0.1159 -0.0681 -0.0422 261 ASN C CA  
10321 C C   . ASN C 261 ? 0.7273 0.8453 0.7814 -0.0997 -0.0669 -0.0367 261 ASN C C   
10322 O O   . ASN C 261 ? 0.7835 0.9200 0.8530 -0.0964 -0.0628 -0.0328 261 ASN C O   
10323 C CB  . ASN C 261 ? 0.6864 0.7967 0.7212 -0.1296 -0.0777 -0.0440 261 ASN C CB  
10324 C CG  . ASN C 261 ? 0.7404 0.8237 0.7550 -0.1463 -0.0797 -0.0514 261 ASN C CG  
10325 O OD1 . ASN C 261 ? 0.7291 0.7918 0.7382 -0.1518 -0.0742 -0.0524 261 ASN C OD1 
10326 N ND2 . ASN C 261 ? 0.5751 0.6578 0.5775 -0.1547 -0.0879 -0.0566 261 ASN C ND2 
10327 N N   . GLU C 262 ? 0.6139 0.7285 0.6645 -0.0891 -0.0698 -0.0362 262 GLU C N   
10328 C CA  . GLU C 262 ? 0.6575 0.7879 0.7228 -0.0741 -0.0697 -0.0309 262 GLU C CA  
10329 C C   . GLU C 262 ? 0.6513 0.7685 0.7181 -0.0634 -0.0617 -0.0313 262 GLU C C   
10330 O O   . GLU C 262 ? 0.5749 0.7066 0.6555 -0.0539 -0.0593 -0.0285 262 GLU C O   
10331 C CB  . GLU C 262 ? 0.7202 0.8477 0.7797 -0.0675 -0.0753 -0.0288 262 GLU C CB  
10332 C CG  . GLU C 262 ? 0.7449 0.8865 0.7998 -0.0779 -0.0840 -0.0288 262 GLU C CG  
10333 C CD  . GLU C 262 ? 1.0187 1.1366 1.0500 -0.0842 -0.0850 -0.0350 262 GLU C CD  
10334 O OE1 . GLU C 262 ? 1.0186 1.1427 1.0411 -0.0959 -0.0914 -0.0382 262 GLU C OE1 
10335 O OE2 . GLU C 262 ? 1.0378 1.1322 1.0590 -0.0774 -0.0794 -0.0370 262 GLU C OE2 
10336 N N   . ALA C 263 ? 0.6891 0.7794 0.7412 -0.0641 -0.0577 -0.0348 263 ALA C N   
10337 C CA  . ALA C 263 ? 0.6336 0.7124 0.6854 -0.0552 -0.0515 -0.0351 263 ALA C CA  
10338 C C   . ALA C 263 ? 0.6812 0.7715 0.7410 -0.0577 -0.0461 -0.0348 263 ALA C C   
10339 O O   . ALA C 263 ? 0.6707 0.7688 0.7384 -0.0481 -0.0426 -0.0342 263 ALA C O   
10340 C CB  . ALA C 263 ? 0.5668 0.6191 0.6025 -0.0559 -0.0489 -0.0376 263 ALA C CB  
10341 N N   . LEU C 264 ? 0.6767 0.7677 0.7334 -0.0710 -0.0453 -0.0351 264 LEU C N   
10342 C CA  . LEU C 264 ? 0.7421 0.8474 0.8066 -0.0754 -0.0399 -0.0329 264 LEU C CA  
10343 C C   . LEU C 264 ? 0.7788 0.9181 0.8627 -0.0700 -0.0401 -0.0298 264 LEU C C   
10344 O O   . LEU C 264 ? 0.8221 0.9751 0.9135 -0.0653 -0.0337 -0.0285 264 LEU C O   
10345 C CB  . LEU C 264 ? 0.7907 0.8904 0.8491 -0.0933 -0.0405 -0.0324 264 LEU C CB  
10346 C CG  . LEU C 264 ? 0.6473 0.7141 0.6879 -0.0969 -0.0371 -0.0340 264 LEU C CG  
10347 C CD1 . LEU C 264 ? 0.6514 0.7020 0.6809 -0.1114 -0.0416 -0.0366 264 LEU C CD1 
10348 C CD2 . LEU C 264 ? 0.6521 0.7221 0.6944 -0.0993 -0.0300 -0.0298 264 LEU C CD2 
10349 N N   . GLU C 265 ? 0.5965 0.7510 0.6885 -0.0691 -0.0471 -0.0283 265 GLU C N   
10350 C CA  . GLU C 265 ? 0.6402 0.8277 0.7519 -0.0604 -0.0474 -0.0243 265 GLU C CA  
10351 C C   . GLU C 265 ? 0.6841 0.8653 0.7981 -0.0408 -0.0433 -0.0257 265 GLU C C   
10352 O O   . GLU C 265 ? 0.7053 0.9073 0.8321 -0.0310 -0.0386 -0.0244 265 GLU C O   
10353 C CB  . GLU C 265 ? 0.6575 0.8619 0.7759 -0.0632 -0.0568 -0.0212 265 GLU C CB  
10354 C CG  . GLU C 265 ? 0.7087 0.9257 0.8271 -0.0836 -0.0619 -0.0203 265 GLU C CG  
10355 C CD  . GLU C 265 ? 0.6941 0.9304 0.8177 -0.0866 -0.0723 -0.0173 265 GLU C CD  
10356 O OE1 . GLU C 265 ? 0.7520 1.0085 0.8895 -0.0723 -0.0743 -0.0123 265 GLU C OE1 
10357 O OE2 . GLU C 265 ? 0.7025 0.9329 0.8153 -0.1030 -0.0787 -0.0199 265 GLU C OE2 
10358 N N   . LEU C 266 ? 0.6273 0.7800 0.7288 -0.0351 -0.0451 -0.0285 266 LEU C N   
10359 C CA  . LEU C 266 ? 0.6612 0.8032 0.7629 -0.0190 -0.0427 -0.0302 266 LEU C CA  
10360 C C   . LEU C 266 ? 0.7383 0.8729 0.8344 -0.0160 -0.0345 -0.0345 266 LEU C C   
10361 O O   . LEU C 266 ? 0.6760 0.8129 0.7759 -0.0030 -0.0307 -0.0369 266 LEU C O   
10362 C CB  . LEU C 266 ? 0.6683 0.7846 0.7589 -0.0168 -0.0476 -0.0305 266 LEU C CB  
10363 C CG  . LEU C 266 ? 0.7083 0.8041 0.7940 -0.0054 -0.0462 -0.0330 266 LEU C CG  
10364 C CD1 . LEU C 266 ? 0.7137 0.8142 0.8094 0.0076  -0.0496 -0.0299 266 LEU C CD1 
10365 C CD2 . LEU C 266 ? 0.7562 0.8282 0.8283 -0.0101 -0.0487 -0.0331 266 LEU C CD2 
10366 N N   . TYR C 267 ? 0.6486 0.7731 0.7343 -0.0273 -0.0317 -0.0354 267 TYR C N   
10367 C CA  . TYR C 267 ? 0.6743 0.7948 0.7537 -0.0254 -0.0242 -0.0380 267 TYR C CA  
10368 C C   . TYR C 267 ? 0.6984 0.8487 0.7898 -0.0241 -0.0180 -0.0363 267 TYR C C   
10369 O O   . TYR C 267 ? 0.7702 0.9242 0.8598 -0.0152 -0.0115 -0.0395 267 TYR C O   
10370 C CB  . TYR C 267 ? 0.7871 0.8897 0.8528 -0.0370 -0.0231 -0.0373 267 TYR C CB  
10371 C CG  . TYR C 267 ? 0.7723 0.8480 0.8258 -0.0353 -0.0268 -0.0389 267 TYR C CG  
10372 C CD1 . TYR C 267 ? 0.6979 0.7618 0.7463 -0.0257 -0.0266 -0.0420 267 TYR C CD1 
10373 C CD2 . TYR C 267 ? 0.7444 0.8072 0.7908 -0.0434 -0.0303 -0.0376 267 TYR C CD2 
10374 C CE1 . TYR C 267 ? 0.6609 0.7051 0.7003 -0.0254 -0.0300 -0.0420 267 TYR C CE1 
10375 C CE2 . TYR C 267 ? 0.7022 0.7451 0.7388 -0.0407 -0.0325 -0.0382 267 TYR C CE2 
10376 C CZ  . TYR C 267 ? 0.7035 0.7393 0.7380 -0.0322 -0.0325 -0.0395 267 TYR C CZ  
10377 O OH  . TYR C 267 ? 0.6689 0.6896 0.6957 -0.0308 -0.0349 -0.0387 267 TYR C OH  
10378 N N   . TYR C 268 ? 0.7328 0.9066 0.8362 -0.0333 -0.0199 -0.0315 268 TYR C N   
10379 C CA  . TYR C 268 ? 0.6658 0.8746 0.7837 -0.0331 -0.0140 -0.0281 268 TYR C CA  
10380 C C   . TYR C 268 ? 0.6296 0.8561 0.7600 -0.0137 -0.0118 -0.0296 268 TYR C C   
10381 O O   . TYR C 268 ? 0.6945 0.9386 0.8294 -0.0048 -0.0033 -0.0307 268 TYR C O   
10382 C CB  . TYR C 268 ? 0.6379 0.8688 0.7666 -0.0495 -0.0184 -0.0220 268 TYR C CB  
10383 C CG  . TYR C 268 ? 0.7492 1.0254 0.8999 -0.0471 -0.0153 -0.0166 268 TYR C CG  
10384 C CD1 . TYR C 268 ? 0.7542 1.0529 0.9101 -0.0483 -0.0056 -0.0138 268 TYR C CD1 
10385 C CD2 . TYR C 268 ? 0.8102 1.1098 0.9768 -0.0430 -0.0219 -0.0132 268 TYR C CD2 
10386 C CE1 . TYR C 268 ? 0.6860 1.0314 0.8640 -0.0453 -0.0019 -0.0080 268 TYR C CE1 
10387 C CE2 . TYR C 268 ? 0.6785 1.0243 0.8677 -0.0395 -0.0191 -0.0071 268 TYR C CE2 
10388 C CZ  . TYR C 268 ? 0.6440 1.0133 0.8394 -0.0405 -0.0087 -0.0046 268 TYR C CZ  
10389 O OH  . TYR C 268 ? 0.7738 1.1933 0.9931 -0.0362 -0.0052 0.0023  268 TYR C OH  
10390 N N   . GLU C 269 ? 0.6436 0.8654 0.7789 -0.0060 -0.0191 -0.0292 269 GLU C N   
10391 C CA  . GLU C 269 ? 0.7131 0.9483 0.8603 0.0138  -0.0175 -0.0296 269 GLU C CA  
10392 C C   . GLU C 269 ? 0.7218 0.9302 0.8564 0.0287  -0.0129 -0.0378 269 GLU C C   
10393 O O   . GLU C 269 ? 0.7081 0.9254 0.8496 0.0465  -0.0086 -0.0402 269 GLU C O   
10394 C CB  . GLU C 269 ? 0.7404 0.9773 0.8957 0.0171  -0.0273 -0.0250 269 GLU C CB  
10395 C CG  . GLU C 269 ? 0.9178 1.1937 1.0910 0.0081  -0.0315 -0.0170 269 GLU C CG  
10396 C CD  . GLU C 269 ? 1.0534 1.3690 1.2484 0.0230  -0.0265 -0.0129 269 GLU C CD  
10397 O OE1 . GLU C 269 ? 0.9863 1.3358 1.1928 0.0148  -0.0219 -0.0092 269 GLU C OE1 
10398 O OE2 . GLU C 269 ? 1.0886 1.4020 1.2895 0.0431  -0.0272 -0.0126 269 GLU C OE2 
10399 N N   . LYS C 270 ? 0.7147 0.8912 0.8307 0.0218  -0.0140 -0.0421 270 LYS C N   
10400 C CA  . LYS C 270 ? 0.7077 0.8588 0.8095 0.0318  -0.0108 -0.0502 270 LYS C CA  
10401 C C   . LYS C 270 ? 0.6720 0.8297 0.7652 0.0296  -0.0017 -0.0539 270 LYS C C   
10402 O O   . LYS C 270 ? 0.7314 0.8687 0.8097 0.0350  0.0005  -0.0612 270 LYS C O   
10403 C CB  . LYS C 270 ? 0.6689 0.7859 0.7567 0.0254  -0.0178 -0.0514 270 LYS C CB  
10404 C CG  . LYS C 270 ? 0.6686 0.7749 0.7615 0.0302  -0.0260 -0.0483 270 LYS C CG  
10405 C CD  . LYS C 270 ? 0.6819 0.7829 0.7790 0.0486  -0.0251 -0.0516 270 LYS C CD  
10406 C CE  . LYS C 270 ? 0.7602 0.8663 0.8697 0.0545  -0.0319 -0.0444 270 LYS C CE  
10407 N NZ  . LYS C 270 ? 0.8540 0.9987 0.9820 0.0569  -0.0303 -0.0385 270 LYS C NZ  
10408 N N   . GLY C 271 ? 0.5394 0.7253 0.6407 0.0205  0.0030  -0.0485 271 GLY C N   
10409 C CA  . GLY C 271 ? 0.6636 0.8625 0.7589 0.0200  0.0127  -0.0500 271 GLY C CA  
10410 C C   . GLY C 271 ? 0.6941 0.8792 0.7750 0.0044  0.0130  -0.0476 271 GLY C C   
10411 O O   . GLY C 271 ? 0.7315 0.9263 0.8051 0.0032  0.0209  -0.0476 271 GLY C O   
10412 N N   . ILE C 272 ? 0.6361 0.7999 0.7121 -0.0067 0.0053  -0.0448 272 ILE C N   
10413 C CA  . ILE C 272 ? 0.7075 0.8555 0.7698 -0.0192 0.0054  -0.0419 272 ILE C CA  
10414 C C   . ILE C 272 ? 0.6929 0.8607 0.7622 -0.0338 0.0085  -0.0337 272 ILE C C   
10415 O O   . ILE C 272 ? 0.6848 0.8622 0.7656 -0.0418 0.0042  -0.0298 272 ILE C O   
10416 C CB  . ILE C 272 ? 0.6575 0.7764 0.7121 -0.0236 -0.0030 -0.0422 272 ILE C CB  
10417 C CG1 . ILE C 272 ? 0.6608 0.7623 0.7108 -0.0114 -0.0068 -0.0488 272 ILE C CG1 
10418 C CG2 . ILE C 272 ? 0.6345 0.7368 0.6751 -0.0331 -0.0022 -0.0389 272 ILE C CG2 
10419 C CD1 . ILE C 272 ? 0.6179 0.7142 0.6565 -0.0032 -0.0023 -0.0551 272 ILE C CD1 
10420 N N   . ASN C 273 ? 0.6596 0.8335 0.7211 -0.0384 0.0156  -0.0304 273 ASN C N   
10421 C CA  . ASN C 273 ? 0.6817 0.8729 0.7489 -0.0540 0.0190  -0.0211 273 ASN C CA  
10422 C C   . ASN C 273 ? 0.7114 0.8757 0.7678 -0.0689 0.0147  -0.0160 273 ASN C C   
10423 O O   . ASN C 273 ? 0.7301 0.9017 0.7917 -0.0843 0.0146  -0.0088 273 ASN C O   
10424 C CB  . ASN C 273 ? 0.6248 0.8384 0.6889 -0.0522 0.0296  -0.0181 273 ASN C CB  
10425 C CG  . ASN C 273 ? 0.6876 0.9299 0.7618 -0.0360 0.0358  -0.0234 273 ASN C CG  
10426 O OD1 . ASN C 273 ? 0.7545 1.0038 0.8417 -0.0274 0.0322  -0.0272 273 ASN C OD1 
10427 N ND2 . ASN C 273 ? 0.8101 1.0689 0.8774 -0.0306 0.0456  -0.0236 273 ASN C ND2 
10428 N N   . MET C 274 ? 0.6626 0.7963 0.7045 -0.0646 0.0110  -0.0194 274 MET C N   
10429 C CA  . MET C 274 ? 0.7215 0.8292 0.7527 -0.0755 0.0080  -0.0145 274 MET C CA  
10430 C C   . MET C 274 ? 0.6666 0.7468 0.6890 -0.0682 0.0019  -0.0195 274 MET C C   
10431 O O   . MET C 274 ? 0.6725 0.7514 0.6931 -0.0563 0.0009  -0.0254 274 MET C O   
10432 C CB  . MET C 274 ? 0.7583 0.8640 0.7782 -0.0801 0.0141  -0.0071 274 MET C CB  
10433 C CG  . MET C 274 ? 0.7129 0.7917 0.7229 -0.0913 0.0119  -0.0001 274 MET C CG  
10434 S SD  . MET C 274 ? 0.9412 0.9916 0.9339 -0.0809 0.0096  -0.0008 274 MET C SD  
10435 C CE  . MET C 274 ? 0.8498 0.9207 0.8357 -0.0735 0.0162  0.0004  274 MET C CE  
10436 N N   . LEU C 275 ? 0.6719 0.7300 0.6886 -0.0757 -0.0020 -0.0173 275 LEU C N   
10437 C CA  . LEU C 275 ? 0.7068 0.7406 0.7145 -0.0694 -0.0064 -0.0201 275 LEU C CA  
10438 C C   . LEU C 275 ? 0.7331 0.7427 0.7305 -0.0775 -0.0067 -0.0152 275 LEU C C   
10439 O O   . LEU C 275 ? 0.6847 0.6940 0.6814 -0.0889 -0.0042 -0.0097 275 LEU C O   
10440 C CB  . LEU C 275 ? 0.5980 0.6329 0.6127 -0.0644 -0.0120 -0.0263 275 LEU C CB  
10441 C CG  . LEU C 275 ? 0.6758 0.7112 0.6956 -0.0733 -0.0161 -0.0272 275 LEU C CG  
10442 C CD1 . LEU C 275 ? 0.7567 0.7660 0.7654 -0.0749 -0.0195 -0.0285 275 LEU C CD1 
10443 C CD2 . LEU C 275 ? 0.7738 0.8275 0.8060 -0.0675 -0.0197 -0.0309 275 LEU C CD2 
10444 N N   . ALA C 276 ? 0.7614 0.7503 0.7508 -0.0713 -0.0096 -0.0167 276 ALA C N   
10445 C CA  . ALA C 276 ? 0.7615 0.7239 0.7397 -0.0752 -0.0094 -0.0131 276 ALA C CA  
10446 C C   . ALA C 276 ? 0.7119 0.6594 0.6863 -0.0694 -0.0133 -0.0184 276 ALA C C   
10447 O O   . ALA C 276 ? 0.6819 0.6389 0.6612 -0.0614 -0.0158 -0.0223 276 ALA C O   
10448 C CB  . ALA C 276 ? 0.7638 0.7172 0.7327 -0.0705 -0.0061 -0.0055 276 ALA C CB  
10449 N N   . THR C 277 ? 0.6642 0.5872 0.6289 -0.0736 -0.0134 -0.0182 277 THR C N   
10450 C CA  . THR C 277 ? 0.6955 0.6031 0.6535 -0.0673 -0.0156 -0.0234 277 THR C CA  
10451 C C   . THR C 277 ? 0.7587 0.6341 0.7022 -0.0671 -0.0132 -0.0210 277 THR C C   
10452 O O   . THR C 277 ? 0.8407 0.7055 0.7801 -0.0732 -0.0106 -0.0146 277 THR C O   
10453 C CB  . THR C 277 ? 0.7293 0.6448 0.6915 -0.0736 -0.0201 -0.0308 277 THR C CB  
10454 O OG1 . THR C 277 ? 0.7862 0.6829 0.7374 -0.0694 -0.0212 -0.0359 277 THR C OG1 
10455 C CG2 . THR C 277 ? 0.6555 0.5735 0.6202 -0.0898 -0.0212 -0.0306 277 THR C CG2 
10456 N N   . ASP C 278 ? 0.7714 0.6306 0.7062 -0.0593 -0.0135 -0.0257 278 ASP C N   
10457 C CA  . ASP C 278 ? 0.8354 0.6612 0.7552 -0.0549 -0.0105 -0.0245 278 ASP C CA  
10458 C C   . ASP C 278 ? 0.8426 0.6439 0.7523 -0.0695 -0.0119 -0.0292 278 ASP C C   
10459 O O   . ASP C 278 ? 0.8563 0.6673 0.7692 -0.0807 -0.0161 -0.0359 278 ASP C O   
10460 C CB  . ASP C 278 ? 0.8313 0.6510 0.7450 -0.0400 -0.0093 -0.0288 278 ASP C CB  
10461 C CG  . ASP C 278 ? 0.9323 0.7260 0.8346 -0.0274 -0.0046 -0.0239 278 ASP C CG  
10462 O OD1 . ASP C 278 ? 1.0641 0.8532 0.9670 -0.0267 -0.0027 -0.0144 278 ASP C OD1 
10463 O OD2 . ASP C 278 ? 0.9478 0.7268 0.8403 -0.0170 -0.0023 -0.0291 278 ASP C OD2 
10464 N N   . GLU C 279 ? 0.8753 0.6437 0.7723 -0.0697 -0.0090 -0.0250 279 GLU C N   
10465 C CA  . GLU C 279 ? 0.9079 0.6467 0.7930 -0.0853 -0.0109 -0.0294 279 GLU C CA  
10466 C C   . GLU C 279 ? 0.9393 0.6595 0.8110 -0.0837 -0.0130 -0.0429 279 GLU C C   
10467 O O   . GLU C 279 ? 0.9687 0.6706 0.8312 -0.0997 -0.0167 -0.0495 279 GLU C O   
10468 C CB  . GLU C 279 ? 0.8866 0.5894 0.7598 -0.0852 -0.0072 -0.0209 279 GLU C CB  
10469 C CG  . GLU C 279 ? 0.9975 0.6842 0.8633 -0.0627 -0.0023 -0.0164 279 GLU C CG  
10470 C CD  . GLU C 279 ? 1.0334 0.6792 0.8857 -0.0621 0.0008  -0.0077 279 GLU C CD  
10471 O OE1 . GLU C 279 ? 0.9373 0.5598 0.7826 -0.0806 -0.0012 -0.0074 279 GLU C OE1 
10472 O OE2 . GLU C 279 ? 1.1189 0.7564 0.9682 -0.0434 0.0048  -0.0001 279 GLU C OE2 
10473 N N   . VAL C 280 ? 0.9453 0.6710 0.8150 -0.0656 -0.0108 -0.0468 280 VAL C N   
10474 C CA  . VAL C 280 ? 0.9694 0.6826 0.8254 -0.0631 -0.0121 -0.0597 280 VAL C CA  
10475 C C   . VAL C 280 ? 0.9059 0.6424 0.7685 -0.0791 -0.0191 -0.0663 280 VAL C C   
10476 O O   . VAL C 280 ? 0.9449 0.6642 0.7934 -0.0891 -0.0228 -0.0768 280 VAL C O   
10477 C CB  . VAL C 280 ? 0.9541 0.6787 0.8105 -0.0410 -0.0078 -0.0600 280 VAL C CB  
10478 C CG1 . VAL C 280 ? 0.9249 0.6462 0.7687 -0.0389 -0.0090 -0.0727 280 VAL C CG1 
10479 C CG2 . VAL C 280 ? 0.9879 0.6873 0.8357 -0.0241 -0.0012 -0.0544 280 VAL C CG2 
10480 N N   . ILE C 281 ? 0.8500 0.6255 0.7332 -0.0816 -0.0212 -0.0603 281 ILE C N   
10481 C CA  . ILE C 281 ? 0.9220 0.7229 0.8145 -0.0956 -0.0279 -0.0640 281 ILE C CA  
10482 C C   . ILE C 281 ? 0.9072 0.6976 0.7978 -0.1170 -0.0315 -0.0642 281 ILE C C   
10483 O O   . ILE C 281 ? 0.8755 0.6690 0.7626 -0.1310 -0.0378 -0.0712 281 ILE C O   
10484 C CB  . ILE C 281 ? 0.8558 0.6969 0.7705 -0.0910 -0.0284 -0.0570 281 ILE C CB  
10485 C CG1 . ILE C 281 ? 0.7795 0.6282 0.6959 -0.0721 -0.0251 -0.0553 281 ILE C CG1 
10486 C CG2 . ILE C 281 ? 0.7194 0.5882 0.6444 -0.1014 -0.0350 -0.0601 281 ILE C CG2 
10487 C CD1 . ILE C 281 ? 0.8845 0.7276 0.7891 -0.0659 -0.0260 -0.0632 281 ILE C CD1 
10488 N N   . LEU C 282 ? 0.9243 0.7037 0.8171 -0.1210 -0.0280 -0.0555 282 LEU C N   
10489 C CA  . LEU C 282 ? 0.9026 0.6715 0.7940 -0.1430 -0.0310 -0.0536 282 LEU C CA  
10490 C C   . LEU C 282 ? 0.9135 0.6404 0.7816 -0.1524 -0.0342 -0.0641 282 LEU C C   
10491 O O   . LEU C 282 ? 0.9937 0.7212 0.8600 -0.1732 -0.0408 -0.0686 282 LEU C O   
10492 C CB  . LEU C 282 ? 0.8736 0.6355 0.7688 -0.1437 -0.0257 -0.0409 282 LEU C CB  
10493 C CG  . LEU C 282 ? 0.9039 0.6463 0.7945 -0.1660 -0.0273 -0.0363 282 LEU C CG  
10494 C CD1 . LEU C 282 ? 0.8728 0.6569 0.7836 -0.1835 -0.0304 -0.0311 282 LEU C CD1 
10495 C CD2 . LEU C 282 ? 0.9006 0.6176 0.7846 -0.1603 -0.0212 -0.0250 282 LEU C CD2 
10496 N N   . LYS C 283 ? 0.8894 0.5806 0.7390 -0.1369 -0.0297 -0.0686 283 LYS C N   
10497 C CA  . LYS C 283 ? 1.0017 0.6473 0.8255 -0.1431 -0.0318 -0.0804 283 LYS C CA  
10498 C C   . LYS C 283 ? 1.0851 0.7427 0.9025 -0.1509 -0.0388 -0.0938 283 LYS C C   
10499 O O   . LYS C 283 ? 1.0752 0.7086 0.8768 -0.1690 -0.0448 -0.1031 283 LYS C O   
10500 C CB  . LYS C 283 ? 0.9978 0.6087 0.8048 -0.1197 -0.0243 -0.0825 283 LYS C CB  
10501 C CG  . LYS C 283 ? 1.1400 0.7291 0.9477 -0.1141 -0.0187 -0.0696 283 LYS C CG  
10502 C CD  . LYS C 283 ? 1.1420 0.7180 0.9512 -0.1395 -0.0224 -0.0628 283 LYS C CD  
10503 C CE  . LYS C 283 ? 1.1452 0.7241 0.9647 -0.1349 -0.0173 -0.0452 283 LYS C CE  
10504 N NZ  . LYS C 283 ? 1.2814 0.8048 1.0815 -0.1319 -0.0139 -0.0410 283 LYS C NZ  
10505 N N   . ASN C 284 ? 1.0181 0.7125 0.8467 -0.1385 -0.0388 -0.0945 284 ASN C N   
10506 C CA  . ASN C 284 ? 0.9527 0.6629 0.7759 -0.1449 -0.0456 -0.1050 284 ASN C CA  
10507 C C   . ASN C 284 ? 0.9332 0.6763 0.7730 -0.1671 -0.0543 -0.1018 284 ASN C C   
10508 O O   . ASN C 284 ? 0.9730 0.7212 0.8046 -0.1801 -0.0623 -0.1107 284 ASN C O   
10509 C CB  . ASN C 284 ? 0.9229 0.6611 0.7529 -0.1245 -0.0426 -0.1044 284 ASN C CB  
10510 C CG  . ASN C 284 ? 0.8815 0.5969 0.7004 -0.1017 -0.0335 -0.1048 284 ASN C CG  
10511 O OD1 . ASN C 284 ? 0.8947 0.5702 0.6986 -0.0990 -0.0293 -0.1067 284 ASN C OD1 
10512 N ND2 . ASN C 284 ? 0.8700 0.6111 0.6969 -0.0850 -0.0304 -0.1020 284 ASN C ND2 
10513 N N   . SER C 285 ? 0.9482 0.7158 0.8109 -0.1713 -0.0528 -0.0892 285 SER C N   
10514 C CA  . SER C 285 ? 0.9501 0.7573 0.8328 -0.1883 -0.0596 -0.0845 285 SER C CA  
10515 C C   . SER C 285 ? 0.9701 0.7643 0.8511 -0.2142 -0.0638 -0.0825 285 SER C C   
10516 O O   . SER C 285 ? 1.0295 0.8451 0.9162 -0.2332 -0.0724 -0.0845 285 SER C O   
10517 C CB  . SER C 285 ? 0.9249 0.7715 0.8339 -0.1772 -0.0552 -0.0726 285 SER C CB  
10518 O OG  . SER C 285 ? 0.9364 0.7933 0.8470 -0.1558 -0.0522 -0.0737 285 SER C OG  
10519 N N   . VAL C 286 ? 0.9818 0.7428 0.8554 -0.2165 -0.0584 -0.0775 286 VAL C N   
10520 C CA  . VAL C 286 ? 1.0290 0.7770 0.9018 -0.2425 -0.0620 -0.0731 286 VAL C CA  
10521 C C   . VAL C 286 ? 1.0969 0.7814 0.9394 -0.2479 -0.0622 -0.0817 286 VAL C C   
10522 O O   . VAL C 286 ? 1.1291 0.7810 0.9577 -0.2276 -0.0550 -0.0833 286 VAL C O   
10523 C CB  . VAL C 286 ? 0.9836 0.7496 0.8753 -0.2435 -0.0556 -0.0567 286 VAL C CB  
10524 C CG1 . VAL C 286 ? 1.0196 0.7654 0.9075 -0.2708 -0.0585 -0.0509 286 VAL C CG1 
10525 C CG2 . VAL C 286 ? 0.9407 0.7673 0.8609 -0.2401 -0.0556 -0.0497 286 VAL C CG2 
10526 N N   . GLU C 287 ? 1.1098 0.7771 0.9426 -0.2755 -0.0706 -0.0865 287 GLU C N   
10527 C CA  . GLU C 287 ? 1.2735 0.8767 1.0746 -0.2848 -0.0729 -0.0973 287 GLU C CA  
10528 C C   . GLU C 287 ? 1.4103 0.9672 1.2002 -0.2715 -0.0635 -0.0905 287 GLU C C   
10529 O O   . GLU C 287 ? 1.4752 1.0086 1.2518 -0.2453 -0.0567 -0.0958 287 GLU C O   
10530 C CB  . GLU C 287 ? 1.3269 0.9247 1.1260 -0.3217 -0.0834 -0.0981 287 GLU C CB  
10531 C CG  . GLU C 287 ? 1.4427 0.9943 1.2091 -0.3354 -0.0919 -0.1175 287 GLU C CG  
10532 C CD  . GLU C 287 ? 1.6450 1.1686 1.4035 -0.3718 -0.1004 -0.1161 287 GLU C CD  
10533 O OE1 . GLU C 287 ? 1.5541 1.1207 1.3387 -0.3930 -0.1043 -0.1025 287 GLU C OE1 
10534 O OE2 . GLU C 287 ? 1.7336 1.1924 1.4597 -0.3794 -0.1029 -0.1285 287 GLU C OE2 
10535 N N   . ARG C 288 ? 1.2756 0.8204 1.0707 -0.2892 -0.0630 -0.0777 288 ARG C N   
10536 C CA  . ARG C 288 ? 1.3356 0.8418 1.1229 -0.2769 -0.0544 -0.0674 288 ARG C CA  
10537 C C   . ARG C 288 ? 1.3027 0.8555 1.1184 -0.2750 -0.0490 -0.0476 288 ARG C C   
10538 O O   . ARG C 288 ? 1.4603 1.0288 1.2882 -0.2992 -0.0516 -0.0365 288 ARG C O   
10539 C CB  . ARG C 288 ? 1.4498 0.8936 1.2143 -0.2985 -0.0579 -0.0684 288 ARG C CB  
10540 C CG  . ARG C 288 ? 1.5679 0.9531 1.3117 -0.2770 -0.0498 -0.0661 288 ARG C CG  
10541 C CD  . ARG C 288 ? 1.6672 1.0026 1.3994 -0.2979 -0.0509 -0.0556 288 ARG C CD  
10542 N NE  . ARG C 288 ? 1.8347 1.1181 1.5499 -0.2741 -0.0426 -0.0507 288 ARG C NE  
10543 C CZ  . ARG C 288 ? 1.8135 1.1086 1.5411 -0.2593 -0.0348 -0.0314 288 ARG C CZ  
10544 N NH1 . ARG C 288 ? 1.7292 1.0831 1.4846 -0.2663 -0.0335 -0.0160 288 ARG C NH1 
10545 N NH2 . ARG C 288 ? 1.8118 1.0594 1.5230 -0.2361 -0.0282 -0.0276 288 ARG C NH2 
10546 N N   . ALA C 289 ? 1.1881 0.7644 1.0138 -0.2471 -0.0416 -0.0433 289 ALA C N   
10547 C CA  . ALA C 289 ? 1.1010 0.7252 0.9519 -0.2427 -0.0366 -0.0278 289 ALA C CA  
10548 C C   . ALA C 289 ? 1.0252 0.6316 0.8721 -0.2216 -0.0279 -0.0168 289 ALA C C   
10549 O O   . ALA C 289 ? 0.9995 0.5841 0.8346 -0.1983 -0.0245 -0.0228 289 ALA C O   
10550 C CB  . ALA C 289 ? 1.0408 0.7205 0.9111 -0.2307 -0.0373 -0.0323 289 ALA C CB  
10551 N N   . SER C 290 ? 1.0444 0.6642 0.9016 -0.2296 -0.0243 0.0000  290 SER C N   
10552 C CA  . SER C 290 ? 1.1106 0.7266 0.9673 -0.2090 -0.0168 0.0119  290 SER C CA  
10553 C C   . SER C 290 ? 0.9599 0.6305 0.8360 -0.1923 -0.0136 0.0131  290 SER C C   
10554 O O   . SER C 290 ? 0.9016 0.6164 0.7952 -0.2017 -0.0156 0.0121  290 SER C O   
10555 C CB  . SER C 290 ? 1.0852 0.6910 0.9419 -0.2239 -0.0140 0.0303  290 SER C CB  
10556 O OG  . SER C 290 ? 0.9828 0.6169 0.8490 -0.2083 -0.0076 0.0431  290 SER C OG  
10557 N N   . PRO C 291 ? 0.9389 0.6071 0.8121 -0.1678 -0.0091 0.0155  291 PRO C N   
10558 C CA  . PRO C 291 ? 0.9618 0.6776 0.8513 -0.1534 -0.0069 0.0162  291 PRO C CA  
10559 C C   . PRO C 291 ? 0.8884 0.6306 0.7874 -0.1564 -0.0025 0.0315  291 PRO C C   
10560 O O   . PRO C 291 ? 0.8810 0.6525 0.7880 -0.1419 0.0001  0.0337  291 PRO C O   
10561 C CB  . PRO C 291 ? 0.8243 0.5240 0.7053 -0.1280 -0.0048 0.0123  291 PRO C CB  
10562 C CG  . PRO C 291 ? 0.8711 0.5204 0.7339 -0.1261 -0.0027 0.0186  291 PRO C CG  
10563 C CD  . PRO C 291 ? 0.9147 0.5368 0.7694 -0.1506 -0.0065 0.0151  291 PRO C CD  
10564 N N   . TYR C 292 ? 0.8532 0.5860 0.7504 -0.1761 -0.0019 0.0420  292 TYR C N   
10565 C CA  . TYR C 292 ? 0.9578 0.7109 0.8598 -0.1790 0.0032  0.0584  292 TYR C CA  
10566 C C   . TYR C 292 ? 0.9635 0.7582 0.8817 -0.1982 0.0039  0.0623  292 TYR C C   
10567 O O   . TYR C 292 ? 0.9850 0.7916 0.9050 -0.2078 0.0082  0.0771  292 TYR C O   
10568 C CB  . TYR C 292 ? 0.9843 0.6928 0.8702 -0.1835 0.0050  0.0721  292 TYR C CB  
10569 C CG  . TYR C 292 ? 1.0074 0.6742 0.8778 -0.1627 0.0050  0.0688  292 TYR C CG  
10570 C CD1 . TYR C 292 ? 0.9398 0.6235 0.8126 -0.1383 0.0070  0.0676  292 TYR C CD1 
10571 C CD2 . TYR C 292 ? 0.9810 0.5920 0.8343 -0.1673 0.0030  0.0669  292 TYR C CD2 
10572 C CE1 . TYR C 292 ? 0.9683 0.6199 0.8293 -0.1183 0.0074  0.0658  292 TYR C CE1 
10573 C CE2 . TYR C 292 ? 0.9379 0.5127 0.7775 -0.1455 0.0042  0.0638  292 TYR C CE2 
10574 C CZ  . TYR C 292 ? 0.9876 0.5855 0.8324 -0.1207 0.0066  0.0640  292 TYR C CZ  
10575 O OH  . TYR C 292 ? 1.0258 0.5935 0.8593 -0.0982 0.0083  0.0622  292 TYR C OH  
10576 N N   . LEU C 293 ? 0.9104 0.7304 0.8407 -0.2030 0.0000  0.0504  293 LEU C N   
10577 C CA  . LEU C 293 ? 0.8932 0.7563 0.8412 -0.2197 0.0005  0.0537  293 LEU C CA  
10578 C C   . LEU C 293 ? 0.8531 0.7599 0.8165 -0.2056 0.0008  0.0443  293 LEU C C   
10579 O O   . LEU C 293 ? 0.9281 0.8278 0.8898 -0.1928 -0.0031 0.0318  293 LEU C O   
10580 C CB  . LEU C 293 ? 0.8767 0.7290 0.8260 -0.2441 -0.0061 0.0499  293 LEU C CB  
10581 C CG  . LEU C 293 ? 0.9352 0.7357 0.8676 -0.2623 -0.0091 0.0548  293 LEU C CG  
10582 C CD1 . LEU C 293 ? 0.9537 0.7012 0.8654 -0.2487 -0.0120 0.0440  293 LEU C CD1 
10583 C CD2 . LEU C 293 ? 0.9083 0.7196 0.8489 -0.2905 -0.0155 0.0529  293 LEU C CD2 
10584 N N   . ARG C 294 ? 0.7785 0.7296 0.7562 -0.2074 0.0057  0.0506  294 ARG C N   
10585 C CA  . ARG C 294 ? 0.7547 0.7455 0.7477 -0.1958 0.0057  0.0416  294 ARG C CA  
10586 C C   . ARG C 294 ? 0.8574 0.8583 0.8609 -0.2081 -0.0013 0.0340  294 ARG C C   
10587 O O   . ARG C 294 ? 0.8379 0.8472 0.8477 -0.2300 -0.0030 0.0401  294 ARG C O   
10588 C CB  . ARG C 294 ? 0.7340 0.7694 0.7387 -0.1942 0.0135  0.0494  294 ARG C CB  
10589 C CG  . ARG C 294 ? 0.8191 0.8851 0.8338 -0.1751 0.0149  0.0398  294 ARG C CG  
10590 C CD  . ARG C 294 ? 0.8750 0.9900 0.9050 -0.1763 0.0218  0.0447  294 ARG C CD  
10591 N NE  . ARG C 294 ? 0.8855 1.0107 0.9082 -0.1735 0.0304  0.0544  294 ARG C NE  
10592 C CZ  . ARG C 294 ? 0.9729 1.1125 0.9975 -0.1897 0.0357  0.0683  294 ARG C CZ  
10593 N NH1 . ARG C 294 ? 0.8889 1.0308 0.9223 -0.2118 0.0327  0.0746  294 ARG C NH1 
10594 N NH2 . ARG C 294 ? 0.9209 1.0736 0.9376 -0.1848 0.0440  0.0766  294 ARG C NH2 
10595 N N   . TYR C 295 ? 0.7528 0.7525 0.7575 -0.1956 -0.0060 0.0216  295 TYR C N   
10596 C CA  . TYR C 295 ? 0.7347 0.7477 0.7488 -0.2053 -0.0134 0.0145  295 TYR C CA  
10597 C C   . TYR C 295 ? 0.7226 0.7840 0.7570 -0.1950 -0.0121 0.0123  295 TYR C C   
10598 O O   . TYR C 295 ? 0.7458 0.8150 0.7811 -0.1749 -0.0083 0.0093  295 TYR C O   
10599 C CB  . TYR C 295 ? 0.7591 0.7366 0.7589 -0.1996 -0.0199 0.0029  295 TYR C CB  
10600 C CG  . TYR C 295 ? 0.7578 0.6855 0.7373 -0.2105 -0.0218 0.0033  295 TYR C CG  
10601 C CD1 . TYR C 295 ? 0.7859 0.7010 0.7619 -0.2339 -0.0280 0.0021  295 TYR C CD1 
10602 C CD2 . TYR C 295 ? 0.7729 0.6656 0.7364 -0.1972 -0.0178 0.0048  295 TYR C CD2 
10603 C CE1 . TYR C 295 ? 0.8696 0.7335 0.8247 -0.2433 -0.0297 0.0013  295 TYR C CE1 
10604 C CE2 . TYR C 295 ? 0.8451 0.6895 0.7895 -0.2044 -0.0190 0.0053  295 TYR C CE2 
10605 C CZ  . TYR C 295 ? 0.9426 0.7702 0.8819 -0.2273 -0.0248 0.0029  295 TYR C CZ  
10606 O OH  . TYR C 295 ? 0.9632 0.7373 0.8814 -0.2343 -0.0260 0.0023  295 TYR C OH  
10607 N N   . TYR C 296 ? 0.6871 0.7811 0.7379 -0.2091 -0.0155 0.0144  296 TYR C N   
10608 C CA  . TYR C 296 ? 0.6247 0.7645 0.6959 -0.1989 -0.0152 0.0124  296 TYR C CA  
10609 C C   . TYR C 296 ? 0.7538 0.8904 0.8260 -0.1990 -0.0252 0.0034  296 TYR C C   
10610 O O   . TYR C 296 ? 0.7950 0.9256 0.8654 -0.2187 -0.0326 0.0028  296 TYR C O   
10611 C CB  . TYR C 296 ? 0.7120 0.8981 0.8034 -0.2126 -0.0119 0.0226  296 TYR C CB  
10612 C CG  . TYR C 296 ? 0.8418 1.0413 0.9339 -0.2106 -0.0007 0.0323  296 TYR C CG  
10613 C CD1 . TYR C 296 ? 0.9343 1.1058 1.0094 -0.1968 0.0048  0.0314  296 TYR C CD1 
10614 C CD2 . TYR C 296 ? 0.8883 1.1308 0.9976 -0.2235 0.0042  0.0433  296 TYR C CD2 
10615 C CE1 . TYR C 296 ? 0.8900 1.0744 0.9633 -0.1953 0.0144  0.0404  296 TYR C CE1 
10616 C CE2 . TYR C 296 ? 0.9522 1.2083 1.0601 -0.2217 0.0151  0.0528  296 TYR C CE2 
10617 C CZ  . TYR C 296 ? 0.9567 1.1824 1.0453 -0.2074 0.0200  0.0509  296 TYR C CZ  
10618 O OH  . TYR C 296 ? 0.9662 1.2052 1.0507 -0.2053 0.0303  0.0600  296 TYR C OH  
10619 N N   . PHE C 297 ? 0.7376 0.8774 0.8113 -0.1782 -0.0259 -0.0034 297 PHE C N   
10620 C CA  . PHE C 297 ? 0.6923 0.8320 0.7666 -0.1765 -0.0350 -0.0107 297 PHE C CA  
10621 C C   . PHE C 297 ? 0.7200 0.9096 0.8183 -0.1779 -0.0378 -0.0070 297 PHE C C   
10622 O O   . PHE C 297 ? 0.7461 0.9616 0.8575 -0.1604 -0.0332 -0.0057 297 PHE C O   
10623 C CB  . PHE C 297 ? 0.6098 0.7298 0.6748 -0.1548 -0.0346 -0.0176 297 PHE C CB  
10624 C CG  . PHE C 297 ? 0.6755 0.7939 0.7387 -0.1526 -0.0433 -0.0238 297 PHE C CG  
10625 C CD1 . PHE C 297 ? 0.7400 0.8250 0.7844 -0.1603 -0.0484 -0.0299 297 PHE C CD1 
10626 C CD2 . PHE C 297 ? 0.6420 0.7920 0.7212 -0.1421 -0.0461 -0.0232 297 PHE C CD2 
10627 C CE1 . PHE C 297 ? 0.7019 0.7872 0.7424 -0.1585 -0.0560 -0.0354 297 PHE C CE1 
10628 C CE2 . PHE C 297 ? 0.5973 0.7470 0.6738 -0.1405 -0.0544 -0.0273 297 PHE C CE2 
10629 C CZ  . PHE C 297 ? 0.6820 0.8005 0.7388 -0.1492 -0.0593 -0.0335 297 PHE C CZ  
10630 N N   . ARG C 298 ? 0.7017 0.9048 0.8055 -0.1987 -0.0454 -0.0052 298 ARG C N   
10631 C CA  . ARG C 298 ? 0.6192 0.8741 0.7475 -0.2026 -0.0494 0.0001  298 ARG C CA  
10632 C C   . ARG C 298 ? 0.7077 1.0029 0.8561 -0.1967 -0.0395 0.0091  298 ARG C C   
10633 O O   . ARG C 298 ? 0.8133 1.1530 0.9834 -0.1875 -0.0394 0.0128  298 ARG C O   
10634 C CB  . ARG C 298 ? 0.5314 0.7978 0.6650 -0.1854 -0.0551 -0.0045 298 ARG C CB  
10635 C CG  . ARG C 298 ? 0.5947 0.8257 0.7077 -0.1895 -0.0639 -0.0133 298 ARG C CG  
10636 C CD  . ARG C 298 ? 0.5327 0.7860 0.6537 -0.1815 -0.0725 -0.0145 298 ARG C CD  
10637 N NE  . ARG C 298 ? 0.5417 0.7575 0.6395 -0.1806 -0.0780 -0.0234 298 ARG C NE  
10638 C CZ  . ARG C 298 ? 0.5761 0.7839 0.6693 -0.1621 -0.0788 -0.0262 298 ARG C CZ  
10639 N NH1 . ARG C 298 ? 0.5100 0.7423 0.6200 -0.1432 -0.0761 -0.0213 298 ARG C NH1 
10640 N NH2 . ARG C 298 ? 0.6037 0.7774 0.6744 -0.1624 -0.0821 -0.0338 298 ARG C NH2 
10641 N N   . GLU C 299 ? 0.7337 1.0140 0.8741 -0.2002 -0.0307 0.0129  299 GLU C N   
10642 C CA  . GLU C 299 ? 0.7549 1.0675 0.9084 -0.1927 -0.0192 0.0205  299 GLU C CA  
10643 C C   . GLU C 299 ? 0.7817 1.1003 0.9374 -0.1627 -0.0130 0.0153  299 GLU C C   
10644 O O   . GLU C 299 ? 0.8089 1.1507 0.9717 -0.1524 -0.0027 0.0190  299 GLU C O   
10645 C CB  . GLU C 299 ? 0.6920 1.0614 0.8718 -0.2061 -0.0194 0.0306  299 GLU C CB  
10646 C CG  . GLU C 299 ? 0.9562 1.3422 1.1406 -0.2258 -0.0121 0.0425  299 GLU C CG  
10647 C CD  . GLU C 299 ? 1.0475 1.4435 1.2305 -0.2108 0.0025  0.0466  299 GLU C CD  
10648 O OE1 . GLU C 299 ? 0.9025 1.3199 1.0915 -0.2264 0.0089  0.0581  299 GLU C OE1 
10649 O OE2 . GLU C 299 ? 0.9588 1.3423 1.1341 -0.1852 0.0073  0.0388  299 GLU C OE2 
10650 N N   . LEU C 300 ? 0.6893 0.9863 0.8377 -0.1488 -0.0187 0.0068  300 LEU C N   
10651 C CA  . LEU C 300 ? 0.7029 1.0051 0.8544 -0.1222 -0.0138 0.0023  300 LEU C CA  
10652 C C   . LEU C 300 ? 0.6772 0.9475 0.8100 -0.1127 -0.0065 -0.0014 300 LEU C C   
10653 O O   . LEU C 300 ? 0.5989 0.8846 0.7346 -0.1006 0.0027  -0.0008 300 LEU C O   
10654 C CB  . LEU C 300 ? 0.6900 0.9837 0.8419 -0.1121 -0.0228 -0.0033 300 LEU C CB  
10655 C CG  . LEU C 300 ? 0.7789 1.1141 0.9522 -0.1184 -0.0296 0.0019  300 LEU C CG  
10656 C CD1 . LEU C 300 ? 0.8267 1.1650 1.0052 -0.1007 -0.0354 -0.0010 300 LEU C CD1 
10657 C CD2 . LEU C 300 ? 0.5439 0.9301 0.7401 -0.1185 -0.0223 0.0103  300 LEU C CD2 
10658 N N   . ILE C 301 ? 0.6006 0.8283 0.7137 -0.1183 -0.0102 -0.0050 301 ILE C N   
10659 C CA  . ILE C 301 ? 0.5687 0.7669 0.6643 -0.1091 -0.0051 -0.0078 301 ILE C CA  
10660 C C   . ILE C 301 ? 0.6811 0.8503 0.7615 -0.1252 -0.0052 -0.0041 301 ILE C C   
10661 O O   . ILE C 301 ? 0.6474 0.8040 0.7249 -0.1406 -0.0115 -0.0035 301 ILE C O   
10662 C CB  . ILE C 301 ? 0.6192 0.7932 0.7065 -0.0934 -0.0094 -0.0159 301 ILE C CB  
10663 C CG1 . ILE C 301 ? 0.6447 0.7934 0.7157 -0.0845 -0.0050 -0.0183 301 ILE C CG1 
10664 C CG2 . ILE C 301 ? 0.6635 0.8161 0.7443 -0.1019 -0.0185 -0.0185 301 ILE C CG2 
10665 C CD1 . ILE C 301 ? 0.6682 0.7943 0.7316 -0.0722 -0.0095 -0.0248 301 ILE C CD1 
10666 N N   . SER C 302 ? 0.6397 0.7972 0.7090 -0.1213 0.0015  -0.0015 302 SER C N   
10667 C CA  . SER C 302 ? 0.6458 0.7739 0.6999 -0.1334 0.0022  0.0037  302 SER C CA  
10668 C C   . SER C 302 ? 0.7094 0.7984 0.7468 -0.1245 -0.0014 -0.0019 302 SER C C   
10669 O O   . SER C 302 ? 0.6623 0.7485 0.6961 -0.1084 -0.0001 -0.0064 302 SER C O   
10670 C CB  . SER C 302 ? 0.6922 0.8312 0.7427 -0.1341 0.0113  0.0117  302 SER C CB  
10671 O OG  . SER C 302 ? 0.8469 1.0289 0.9141 -0.1375 0.0165  0.0163  302 SER C OG  
10672 N N   . VAL C 303 ? 0.6708 0.7301 0.6981 -0.1351 -0.0059 -0.0018 303 VAL C N   
10673 C CA  . VAL C 303 ? 0.6617 0.6857 0.6737 -0.1266 -0.0085 -0.0062 303 VAL C CA  
10674 C C   . VAL C 303 ? 0.6882 0.6835 0.6858 -0.1332 -0.0057 0.0008  303 VAL C C   
10675 O O   . VAL C 303 ? 0.7178 0.7090 0.7147 -0.1499 -0.0052 0.0069  303 VAL C O   
10676 C CB  . VAL C 303 ? 0.6875 0.6980 0.6972 -0.1294 -0.0160 -0.0138 303 VAL C CB  
10677 C CG1 . VAL C 303 ? 0.6764 0.6626 0.6746 -0.1152 -0.0172 -0.0188 303 VAL C CG1 
10678 C CG2 . VAL C 303 ? 0.7297 0.7726 0.7559 -0.1286 -0.0196 -0.0173 303 VAL C CG2 
10679 N N   . PHE C 304 ? 0.7388 0.7146 0.7252 -0.1204 -0.0042 0.0010  304 PHE C N   
10680 C CA  . PHE C 304 ? 0.7833 0.7271 0.7548 -0.1226 -0.0025 0.0076  304 PHE C CA  
10681 C C   . PHE C 304 ? 0.7825 0.6964 0.7434 -0.1133 -0.0059 0.0014  304 PHE C C   
10682 O O   . PHE C 304 ? 0.7664 0.6881 0.7306 -0.1015 -0.0081 -0.0055 304 PHE C O   
10683 C CB  . PHE C 304 ? 0.6548 0.6052 0.6221 -0.1145 0.0027  0.0156  304 PHE C CB  
10684 C CG  . PHE C 304 ? 0.6271 0.5994 0.5991 -0.1250 0.0078  0.0246  304 PHE C CG  
10685 C CD1 . PHE C 304 ? 0.6805 0.6361 0.6457 -0.1389 0.0098  0.0354  304 PHE C CD1 
10686 C CD2 . PHE C 304 ? 0.6373 0.6460 0.6196 -0.1205 0.0112  0.0228  304 PHE C CD2 
10687 C CE1 . PHE C 304 ? 0.7022 0.6808 0.6719 -0.1494 0.0151  0.0454  304 PHE C CE1 
10688 C CE2 . PHE C 304 ? 0.6450 0.6773 0.6312 -0.1290 0.0172  0.0314  304 PHE C CE2 
10689 C CZ  . PHE C 304 ? 0.7075 0.7265 0.6878 -0.1441 0.0193  0.0434  304 PHE C CZ  
10690 N N   . PHE C 305 ? 0.7338 0.6132 0.6817 -0.1183 -0.0059 0.0043  305 PHE C N   
10691 C CA  . PHE C 305 ? 0.7900 0.6399 0.7260 -0.1077 -0.0075 -0.0011 305 PHE C CA  
10692 C C   . PHE C 305 ? 0.8737 0.7041 0.7997 -0.0969 -0.0038 0.0079  305 PHE C C   
10693 O O   . PHE C 305 ? 0.9256 0.7435 0.8463 -0.1046 -0.0012 0.0179  305 PHE C O   
10694 C CB  . PHE C 305 ? 0.7851 0.6070 0.7117 -0.1198 -0.0109 -0.0073 305 PHE C CB  
10695 C CG  . PHE C 305 ? 0.8165 0.6599 0.7525 -0.1297 -0.0160 -0.0158 305 PHE C CG  
10696 C CD1 . PHE C 305 ? 0.7777 0.6273 0.7143 -0.1202 -0.0191 -0.0253 305 PHE C CD1 
10697 C CD2 . PHE C 305 ? 0.8197 0.6806 0.7650 -0.1484 -0.0176 -0.0127 305 PHE C CD2 
10698 C CE1 . PHE C 305 ? 0.7917 0.6626 0.7368 -0.1286 -0.0244 -0.0316 305 PHE C CE1 
10699 C CE2 . PHE C 305 ? 0.7671 0.6518 0.7226 -0.1566 -0.0229 -0.0192 305 PHE C CE2 
10700 C CZ  . PHE C 305 ? 0.8346 0.7234 0.7895 -0.1464 -0.0265 -0.0285 305 PHE C CZ  
10701 N N   . ARG C 306 ? 0.7673 0.5979 0.6917 -0.0796 -0.0036 0.0059  306 ARG C N   
10702 C CA  . ARG C 306 ? 0.8226 0.6418 0.7399 -0.0674 -0.0009 0.0153  306 ARG C CA  
10703 C C   . ARG C 306 ? 0.9221 0.6990 0.8245 -0.0641 0.0005  0.0169  306 ARG C C   
10704 O O   . ARG C 306 ? 0.9522 0.7077 0.8482 -0.0703 -0.0010 0.0083  306 ARG C O   
10705 C CB  . ARG C 306 ? 0.8939 0.7321 0.8165 -0.0513 -0.0019 0.0131  306 ARG C CB  
10706 C CG  . ARG C 306 ? 0.9263 0.7465 0.8429 -0.0391 -0.0020 0.0080  306 ARG C CG  
10707 C CD  . ARG C 306 ? 0.9318 0.7748 0.8558 -0.0260 -0.0034 0.0071  306 ARG C CD  
10708 N NE  . ARG C 306 ? 0.8356 0.6682 0.7559 -0.0167 -0.0031 0.0006  306 ARG C NE  
10709 C CZ  . ARG C 306 ? 0.8408 0.6735 0.7599 -0.0013 -0.0014 0.0045  306 ARG C CZ  
10710 N NH1 . ARG C 306 ? 0.9206 0.7650 0.8429 0.0063  -0.0012 0.0149  306 ARG C NH1 
10711 N NH2 . ARG C 306 ? 0.8690 0.6926 0.7835 0.0069  0.0002  -0.0019 306 ARG C NH2 
10712 N N   . ASP C 307 ? 0.9265 0.6910 0.8225 -0.0535 0.0032  0.0280  307 ASP C N   
10713 C CA  . ASP C 307 ? 0.9611 0.6836 0.8426 -0.0457 0.0053  0.0311  307 ASP C CA  
10714 C C   . ASP C 307 ? 0.9811 0.7059 0.8624 -0.0243 0.0061  0.0276  307 ASP C C   
10715 O O   . ASP C 307 ? 0.9225 0.6655 0.8087 -0.0115 0.0067  0.0362  307 ASP C O   
10716 C CB  . ASP C 307 ? 0.9757 0.6835 0.8507 -0.0463 0.0077  0.0477  307 ASP C CB  
10717 C CG  . ASP C 307 ? 1.0886 0.7454 0.9473 -0.0414 0.0098  0.0511  307 ASP C CG  
10718 O OD1 . ASP C 307 ? 1.0499 0.6915 0.9032 -0.0229 0.0113  0.0471  307 ASP C OD1 
10719 O OD2 . ASP C 307 ? 1.0791 0.7105 0.9301 -0.0559 0.0102  0.0579  307 ASP C OD2 
10720 N N   . LYS C 308 ? 1.0299 0.7384 0.9053 -0.0211 0.0061  0.0153  308 LYS C N   
10721 C CA  . LYS C 308 ? 0.9667 0.6817 0.8427 -0.0015 0.0077  0.0115  308 LYS C CA  
10722 C C   . LYS C 308 ? 0.9361 0.6320 0.8052 0.0171  0.0118  0.0224  308 LYS C C   
10723 O O   . LYS C 308 ? 0.9023 0.6227 0.7797 0.0318  0.0124  0.0291  308 LYS C O   
10724 C CB  . LYS C 308 ? 0.9239 0.6224 0.7913 -0.0024 0.0077  -0.0037 308 LYS C CB  
10725 C CG  . LYS C 308 ? 1.0443 0.7583 0.9143 0.0155  0.0097  -0.0081 308 LYS C CG  
10726 C CD  . LYS C 308 ? 1.0700 0.7772 0.9322 0.0119  0.0089  -0.0234 308 LYS C CD  
10727 C CE  . LYS C 308 ? 1.0315 0.7230 0.8823 0.0325  0.0146  -0.0278 308 LYS C CE  
10728 N NZ  . LYS C 308 ? 1.0367 0.7665 0.8999 0.0446  0.0157  -0.0264 308 LYS C NZ  
10729 N N   . THR C 309 ? 0.9767 0.6285 0.8306 0.0165  0.0142  0.0249  309 THR C N   
10730 C CA  . THR C 309 ? 1.0158 0.6449 0.8622 0.0361  0.0182  0.0361  309 THR C CA  
10731 C C   . THR C 309 ? 1.0020 0.6606 0.8593 0.0410  0.0171  0.0533  309 THR C C   
10732 O O   . THR C 309 ? 0.9522 0.6259 0.8144 0.0607  0.0186  0.0611  309 THR C O   
10733 C CB  . THR C 309 ? 1.0418 0.6156 0.8699 0.0302  0.0199  0.0375  309 THR C CB  
10734 O OG1 . THR C 309 ? 1.0010 0.5436 0.8153 0.0301  0.0212  0.0206  309 THR C OG1 
10735 C CG2 . THR C 309 ? 0.9559 0.5067 0.7775 0.0499  0.0237  0.0531  309 THR C CG2 
10736 N N   . LEU C 310 ? 0.9667 0.6367 0.8275 0.0230  0.0144  0.0594  310 LEU C N   
10737 C CA  . LEU C 310 ? 0.9925 0.6899 0.8602 0.0260  0.0131  0.0750  310 LEU C CA  
10738 C C   . LEU C 310 ? 0.9839 0.7285 0.8660 0.0325  0.0103  0.0722  310 LEU C C   
10739 O O   . LEU C 310 ? 0.9840 0.7473 0.8704 0.0464  0.0095  0.0829  310 LEU C O   
10740 C CB  . LEU C 310 ? 1.0263 0.7275 0.8934 0.0046  0.0119  0.0805  310 LEU C CB  
10741 C CG  . LEU C 310 ? 0.9984 0.6686 0.8539 0.0019  0.0139  0.0969  310 LEU C CG  
10742 C CD1 . LEU C 310 ? 1.0037 0.6192 0.8448 0.0099  0.0167  0.0961  310 LEU C CD1 
10743 C CD2 . LEU C 310 ? 1.1348 0.8111 0.9907 -0.0224 0.0134  0.0999  310 LEU C CD2 
10744 N N   . SER C 311 ? 0.9171 0.6811 0.8067 0.0222  0.0082  0.0586  311 SER C N   
10745 C CA  . SER C 311 ? 0.8490 0.6543 0.7516 0.0254  0.0048  0.0558  311 SER C CA  
10746 C C   . SER C 311 ? 0.7952 0.6077 0.7016 0.0442  0.0058  0.0559  311 SER C C   
10747 O O   . SER C 311 ? 0.8046 0.6480 0.7200 0.0511  0.0030  0.0619  311 SER C O   
10748 C CB  . SER C 311 ? 0.9215 0.7413 0.8306 0.0111  0.0025  0.0422  311 SER C CB  
10749 O OG  . SER C 311 ? 0.8822 0.7010 0.7899 -0.0054 0.0023  0.0428  311 SER C OG  
10750 N N   . ASP C 312 ? 0.8883 0.6740 0.7875 0.0522  0.0097  0.0491  312 ASP C N   
10751 C CA  . ASP C 312 ? 0.8792 0.6743 0.7821 0.0716  0.0121  0.0495  312 ASP C CA  
10752 C C   . ASP C 312 ? 0.9027 0.6974 0.8054 0.0895  0.0139  0.0655  312 ASP C C   
10753 O O   . ASP C 312 ? 0.8711 0.6919 0.7831 0.1042  0.0142  0.0707  312 ASP C O   
10754 C CB  . ASP C 312 ? 0.8224 0.5882 0.7146 0.0770  0.0167  0.0371  312 ASP C CB  
10755 C CG  . ASP C 312 ? 0.9145 0.6877 0.8083 0.0618  0.0143  0.0221  312 ASP C CG  
10756 O OD1 . ASP C 312 ? 0.8253 0.6313 0.7316 0.0522  0.0097  0.0212  312 ASP C OD1 
10757 O OD2 . ASP C 312 ? 0.9060 0.6507 0.7874 0.0602  0.0166  0.0111  312 ASP C OD2 
10758 N N   . LEU C 313 ? 0.8843 0.6510 0.7769 0.0884  0.0150  0.0747  313 LEU C N   
10759 C CA  . LEU C 313 ? 0.8357 0.6014 0.7278 0.1061  0.0163  0.0919  313 LEU C CA  
10760 C C   . LEU C 313 ? 0.8797 0.6930 0.7850 0.1059  0.0105  0.1026  313 LEU C C   
10761 O O   . LEU C 313 ? 0.8779 0.7131 0.7910 0.1231  0.0102  0.1126  313 LEU C O   
10762 C CB  . LEU C 313 ? 0.9159 0.6414 0.7940 0.1020  0.0178  0.1009  313 LEU C CB  
10763 C CG  . LEU C 313 ? 0.9454 0.6160 0.8074 0.1082  0.0234  0.0948  313 LEU C CG  
10764 C CD1 . LEU C 313 ? 0.9608 0.5951 0.8104 0.0915  0.0230  0.0998  313 LEU C CD1 
10765 C CD2 . LEU C 313 ? 0.8884 0.5460 0.7478 0.1370  0.0281  0.1041  313 LEU C CD2 
10766 N N   . ILE C 314 ? 0.9079 0.7388 0.8155 0.0865  0.0059  0.1003  314 ILE C N   
10767 C CA  . ILE C 314 ? 0.8540 0.7283 0.7714 0.0841  -0.0003 0.1070  314 ILE C CA  
10768 C C   . ILE C 314 ? 0.8516 0.7568 0.7822 0.0873  -0.0026 0.0992  314 ILE C C   
10769 O O   . ILE C 314 ? 0.8332 0.7718 0.7732 0.0939  -0.0069 0.1075  314 ILE C O   
10770 C CB  . ILE C 314 ? 0.8882 0.7713 0.8025 0.0638  -0.0036 0.1044  314 ILE C CB  
10771 C CG1 . ILE C 314 ? 0.9127 0.7605 0.8142 0.0561  0.0002  0.1085  314 ILE C CG1 
10772 C CG2 . ILE C 314 ? 0.8854 0.8041 0.8030 0.0635  -0.0097 0.1147  314 ILE C CG2 
10773 C CD1 . ILE C 314 ? 0.8107 0.6712 0.7090 0.0385  -0.0016 0.1094  314 ILE C CD1 
10774 N N   . GLY C 315 ? 0.8435 0.7393 0.7749 0.0816  -0.0004 0.0841  315 GLY C N   
10775 C CA  . GLY C 315 ? 0.7575 0.6791 0.7003 0.0843  -0.0018 0.0776  315 GLY C CA  
10776 C C   . GLY C 315 ? 0.8481 0.7788 0.7964 0.1056  0.0016  0.0855  315 GLY C C   
10777 O O   . GLY C 315 ? 0.9733 0.9401 0.9336 0.1106  -0.0023 0.0940  315 GLY C O   
10778 N N   . PHE C 316 ? 0.8687 0.7670 0.8077 0.1185  0.0089  0.0832  316 PHE C N   
10779 C CA  . PHE C 316 ? 0.8810 0.7870 0.8245 0.1403  0.0143  0.0867  316 PHE C CA  
10780 C C   . PHE C 316 ? 0.8629 0.7577 0.8034 0.1612  0.0177  0.1020  316 PHE C C   
10781 O O   . PHE C 316 ? 0.9408 0.8684 0.8937 0.1761  0.0172  0.1140  316 PHE C O   
10782 C CB  . PHE C 316 ? 0.8506 0.7296 0.7844 0.1423  0.0208  0.0712  316 PHE C CB  
10783 C CG  . PHE C 316 ? 0.7517 0.6410 0.6884 0.1225  0.0170  0.0578  316 PHE C CG  
10784 C CD1 . PHE C 316 ? 0.7640 0.6938 0.7154 0.1190  0.0136  0.0582  316 PHE C CD1 
10785 C CD2 . PHE C 316 ? 0.8075 0.6669 0.7328 0.1069  0.0165  0.0463  316 PHE C CD2 
10786 C CE1 . PHE C 316 ? 0.7718 0.7091 0.7257 0.1021  0.0100  0.0474  316 PHE C CE1 
10787 C CE2 . PHE C 316 ? 0.8667 0.7378 0.7958 0.0905  0.0128  0.0355  316 PHE C CE2 
10788 C CZ  . PHE C 316 ? 0.8212 0.7297 0.7641 0.0890  0.0097  0.0362  316 PHE C CZ  
10789 N N   . SER C 317 ? 0.8145 0.6642 0.7392 0.1625  0.0208  0.1028  317 SER C N   
10790 C CA  . SER C 317 ? 0.8808 0.7113 0.8006 0.1864  0.0258  0.1159  317 SER C CA  
10791 C C   . SER C 317 ? 0.9390 0.7935 0.8659 0.1900  0.0202  0.1362  317 SER C C   
10792 O O   . SER C 317 ? 0.9755 0.8452 0.9093 0.2125  0.0220  0.1503  317 SER C O   
10793 C CB  . SER C 317 ? 0.9119 0.6803 0.8107 0.1865  0.0309  0.1100  317 SER C CB  
10794 O OG  . SER C 317 ? 1.0574 0.8056 0.9479 0.1746  0.0332  0.0900  317 SER C OG  
10795 N N   . TYR C 318 ? 0.9532 0.8134 0.8780 0.1691  0.0136  0.1385  318 TYR C N   
10796 C CA  . TYR C 318 ? 0.9780 0.8487 0.9025 0.1724  0.0092  0.1580  318 TYR C CA  
10797 C C   . TYR C 318 ? 0.9024 0.8283 0.8438 0.1808  0.0032  0.1704  318 TYR C C   
10798 O O   . TYR C 318 ? 0.9365 0.8746 0.8779 0.1872  -0.0007 0.1884  318 TYR C O   
10799 C CB  . TYR C 318 ? 0.9232 0.7882 0.8396 0.1479  0.0046  0.1567  318 TYR C CB  
10800 C CG  . TYR C 318 ? 0.9698 0.7818 0.8692 0.1420  0.0091  0.1560  318 TYR C CG  
10801 C CD1 . TYR C 318 ? 0.9589 0.7291 0.8489 0.1602  0.0153  0.1618  318 TYR C CD1 
10802 C CD2 . TYR C 318 ? 1.0117 0.8154 0.9044 0.1179  0.0073  0.1498  318 TYR C CD2 
10803 C CE1 . TYR C 318 ? 1.0686 0.7875 0.9423 0.1521  0.0186  0.1613  318 TYR C CE1 
10804 C CE2 . TYR C 318 ? 0.9867 0.7448 0.8652 0.1098  0.0109  0.1504  318 TYR C CE2 
10805 C CZ  . TYR C 318 ? 1.0465 0.7610 0.9152 0.1257  0.0160  0.1562  318 TYR C CZ  
10806 O OH  . TYR C 318 ? 1.0601 0.7262 0.9138 0.1153  0.0188  0.1570  318 TYR C OH  
10807 N N   . HIS C 319 ? 0.8999 0.8601 0.8553 0.1799  0.0018  0.1624  319 HIS C N   
10808 C CA  . HIS C 319 ? 0.8634 0.8769 0.8358 0.1872  -0.0042 0.1752  319 HIS C CA  
10809 C C   . HIS C 319 ? 0.9074 0.9240 0.8850 0.2172  0.0005  0.1917  319 HIS C C   
10810 O O   . HIS C 319 ? 0.8209 0.8750 0.8090 0.2252  -0.0054 0.2092  319 HIS C O   
10811 C CB  . HIS C 319 ? 0.7677 0.8150 0.7540 0.1786  -0.0063 0.1642  319 HIS C CB  
10812 C CG  . HIS C 319 ? 0.8185 0.8631 0.8105 0.1966  0.0026  0.1595  319 HIS C CG  
10813 N ND1 . HIS C 319 ? 0.8836 0.8829 0.8622 0.2008  0.0116  0.1461  319 HIS C ND1 
10814 C CD2 . HIS C 319 ? 0.8694 0.9528 0.8782 0.2116  0.0042  0.1667  319 HIS C CD2 
10815 C CE1 . HIS C 319 ? 0.8464 0.8553 0.8316 0.2184  0.0188  0.1441  319 HIS C CE1 
10816 N NE2 . HIS C 319 ? 0.9520 1.0129 0.9563 0.2257  0.0150  0.1571  319 HIS C NE2 
10817 N N   . ALA C 320 ? 0.8648 0.8423 0.8345 0.2345  0.0110  0.1863  320 ALA C N   
10818 C CA  . ALA C 320 ? 0.9191 0.8909 0.8910 0.2660  0.0170  0.2013  320 ALA C CA  
10819 C C   . ALA C 320 ? 1.0112 0.9555 0.9715 0.2717  0.0152  0.2178  320 ALA C C   
10820 O O   . ALA C 320 ? 1.0216 0.9818 0.9888 0.2943  0.0150  0.2375  320 ALA C O   
10821 C CB  . ALA C 320 ? 0.8346 0.7670 0.7974 0.2826  0.0292  0.1881  320 ALA C CB  
10822 N N   . TRP C 321 ? 1.1207 1.0265 1.0642 0.2518  0.0139  0.2116  321 TRP C N   
10823 C CA  . TRP C 321 ? 1.0543 0.9292 0.9847 0.2555  0.0130  0.2276  321 TRP C CA  
10824 C C   . TRP C 321 ? 1.1020 1.0222 1.0397 0.2493  0.0027  0.2459  321 TRP C C   
10825 O O   . TRP C 321 ? 1.1300 1.0907 1.0754 0.2298  -0.0048 0.2401  321 TRP C O   
10826 C CB  . TRP C 321 ? 1.0661 0.8915 0.9777 0.2332  0.0145  0.2163  321 TRP C CB  
10827 C CG  . TRP C 321 ? 1.1568 0.9333 1.0573 0.2340  0.0229  0.1973  321 TRP C CG  
10828 C CD1 . TRP C 321 ? 1.0448 0.8285 0.9510 0.2391  0.0274  0.1804  321 TRP C CD1 
10829 C CD2 . TRP C 321 ? 1.2414 0.9550 1.1219 0.2272  0.0271  0.1930  321 TRP C CD2 
10830 N NE1 . TRP C 321 ? 1.1657 0.8948 1.0552 0.2368  0.0339  0.1651  321 TRP C NE1 
10831 C CE2 . TRP C 321 ? 1.3024 0.9870 1.1763 0.2288  0.0335  0.1722  321 TRP C CE2 
10832 C CE3 . TRP C 321 ? 1.1505 0.8299 1.0174 0.2188  0.0258  0.2056  321 TRP C CE3 
10833 C CZ2 . TRP C 321 ? 1.3783 1.0005 1.2323 0.2214  0.0376  0.1625  321 TRP C CZ2 
10834 C CZ3 . TRP C 321 ? 1.1902 0.8078 1.0390 0.2111  0.0303  0.1972  321 TRP C CZ3 
10835 C CH2 . TRP C 321 ? 1.3405 0.9296 1.1829 0.2120  0.0357  0.1752  321 TRP C CH2 
10836 N N   . ASN C 322 ? 1.1339 1.0443 1.0671 0.2656  0.0021  0.2681  322 ASN C N   
10837 C CA  . ASN C 322 ? 1.0844 1.0278 1.0177 0.2569  -0.0078 0.2859  322 ASN C CA  
10838 C C   . ASN C 322 ? 1.1566 1.0792 1.0740 0.2276  -0.0101 0.2783  322 ASN C C   
10839 O O   . ASN C 322 ? 1.1961 1.0682 1.1004 0.2195  -0.0036 0.2676  322 ASN C O   
10840 C CB  . ASN C 322 ? 1.0956 1.0294 1.0263 0.2822  -0.0074 0.3128  322 ASN C CB  
10841 C CG  . ASN C 322 ? 1.1926 1.1684 1.1433 0.3101  -0.0079 0.3251  322 ASN C CG  
10842 O OD1 . ASN C 322 ? 1.2738 1.2442 1.2256 0.3360  -0.0066 0.3466  322 ASN C OD1 
10843 N ND2 . ASN C 322 ? 1.1582 1.1774 1.1256 0.3051  -0.0098 0.3125  322 ASN C ND2 
10844 N N   . ALA C 323 ? 1.1386 1.1023 1.0568 0.2114  -0.0195 0.2837  323 ALA C N   
10845 C CA  . ALA C 323 ? 1.0944 1.0502 1.0003 0.1829  -0.0213 0.2729  323 ALA C CA  
10846 C C   . ALA C 323 ? 1.1449 1.0519 1.0325 0.1792  -0.0165 0.2823  323 ALA C C   
10847 O O   . ALA C 323 ? 1.1846 1.0609 1.0633 0.1615  -0.0121 0.2684  323 ALA C O   
10848 C CB  . ALA C 323 ? 1.0789 1.0875 0.9866 0.1694  -0.0320 0.2776  323 ALA C CB  
10849 N N   . GLU C 324 ? 1.0931 0.9939 0.9756 0.1950  -0.0177 0.3072  324 GLU C N   
10850 C CA  . GLU C 324 ? 1.1142 0.9670 0.9789 0.1907  -0.0134 0.3190  324 GLU C CA  
10851 C C   . GLU C 324 ? 1.1769 0.9683 1.0359 0.1946  -0.0040 0.3071  324 GLU C C   
10852 O O   . GLU C 324 ? 1.2450 0.9975 1.0906 0.1776  -0.0004 0.3038  324 GLU C O   
10853 C CB  . GLU C 324 ? 1.1653 1.0209 1.0261 0.2101  -0.0165 0.3496  324 GLU C CB  
10854 C CG  . GLU C 324 ? 1.1973 1.0928 1.0513 0.1970  -0.0248 0.3644  324 GLU C CG  
10855 C CD  . GLU C 324 ? 1.2963 1.2500 1.1628 0.2112  -0.0340 0.3773  324 GLU C CD  
10856 O OE1 . GLU C 324 ? 1.3455 1.3270 1.2290 0.2178  -0.0356 0.3646  324 GLU C OE1 
10857 O OE2 . GLU C 324 ? 1.3833 1.3564 1.2427 0.2149  -0.0401 0.4011  324 GLU C OE2 
10858 N N   . ASP C 325 ? 1.0876 0.8709 0.9558 0.2163  0.0001  0.3005  325 ASP C N   
10859 C CA  . ASP C 325 ? 1.1318 0.8573 0.9924 0.2203  0.0088  0.2861  325 ASP C CA  
10860 C C   . ASP C 325 ? 1.1553 0.8775 1.0153 0.1946  0.0100  0.2595  325 ASP C C   
10861 O O   . ASP C 325 ? 1.1771 0.8509 1.0246 0.1824  0.0144  0.2503  325 ASP C O   
10862 C CB  . ASP C 325 ? 1.2579 0.9823 1.1281 0.2512  0.0134  0.2846  325 ASP C CB  
10863 C CG  . ASP C 325 ? 1.3377 1.0788 1.2134 0.2789  0.0113  0.3116  325 ASP C CG  
10864 O OD1 . ASP C 325 ? 1.2913 1.0895 1.1780 0.2773  0.0032  0.3239  325 ASP C OD1 
10865 O OD2 . ASP C 325 ? 1.4068 1.1028 1.2749 0.3025  0.0175  0.3208  325 ASP C OD2 
10866 N N   . ALA C 326 ? 1.1356 0.9085 1.0090 0.1856  0.0056  0.2476  326 ALA C N   
10867 C CA  . ALA C 326 ? 1.1141 0.8872 0.9885 0.1636  0.0064  0.2233  326 ALA C CA  
10868 C C   . ALA C 326 ? 1.0631 0.8259 0.9270 0.1371  0.0052  0.2227  326 ALA C C   
10869 O O   . ALA C 326 ? 1.0366 0.7670 0.8936 0.1223  0.0089  0.2092  326 ALA C O   
10870 C CB  . ALA C 326 ? 1.0733 0.9021 0.9641 0.1607  0.0014  0.2135  326 ALA C CB  
10871 N N   . VAL C 327 ? 1.0267 0.8196 0.8889 0.1304  -0.0001 0.2373  327 VAL C N   
10872 C CA  . VAL C 327 ? 1.0361 0.8249 0.8883 0.1065  -0.0003 0.2381  327 VAL C CA  
10873 C C   . VAL C 327 ? 0.9874 0.7205 0.8255 0.1037  0.0050  0.2477  327 VAL C C   
10874 O O   . VAL C 327 ? 1.0311 0.7449 0.8630 0.0827  0.0076  0.2400  327 VAL C O   
10875 C CB  . VAL C 327 ? 1.0163 0.8494 0.8668 0.1024  -0.0067 0.2525  327 VAL C CB  
10876 C CG1 . VAL C 327 ? 1.0198 0.8525 0.8595 0.0788  -0.0054 0.2530  327 VAL C CG1 
10877 C CG2 . VAL C 327 ? 0.8515 0.7355 0.7149 0.1033  -0.0128 0.2415  327 VAL C CG2 
10878 N N   . ARG C 328 ? 1.0313 0.7370 0.8647 0.1247  0.0065  0.2649  328 ARG C N   
10879 C CA  . ARG C 328 ? 1.1273 0.7734 0.9459 0.1222  0.0110  0.2743  328 ARG C CA  
10880 C C   . ARG C 328 ? 1.1378 0.7414 0.9531 0.1138  0.0159  0.2524  328 ARG C C   
10881 O O   . ARG C 328 ? 1.2632 0.8313 1.0681 0.0945  0.0180  0.2516  328 ARG C O   
10882 C CB  . ARG C 328 ? 1.1512 0.7733 0.9657 0.1503  0.0119  0.2957  328 ARG C CB  
10883 C CG  . ARG C 328 ? 1.2066 0.7852 1.0050 0.1467  0.0134  0.3183  328 ARG C CG  
10884 C CD  . ARG C 328 ? 1.3152 0.8265 1.1024 0.1397  0.0190  0.3067  328 ARG C CD  
10885 N NE  . ARG C 328 ? 1.4193 0.8720 1.1913 0.1488  0.0214  0.3271  328 ARG C NE  
10886 C CZ  . ARG C 328 ? 1.5220 0.9202 1.2795 0.1299  0.0238  0.3281  328 ARG C CZ  
10887 N NH1 . ARG C 328 ? 1.5415 0.9415 1.2987 0.0993  0.0239  0.3119  328 ARG C NH1 
10888 N NH2 . ARG C 328 ? 1.4043 0.7454 1.1477 0.1414  0.0257  0.3471  328 ARG C NH2 
10889 N N   . ASP C 329 ? 1.0864 0.6931 0.9098 0.1278  0.0175  0.2356  329 ASP C N   
10890 C CA  . ASP C 329 ? 1.1190 0.6888 0.9377 0.1203  0.0214  0.2136  329 ASP C CA  
10891 C C   . ASP C 329 ? 1.1007 0.6873 0.9221 0.0900  0.0196  0.1987  329 ASP C C   
10892 O O   . ASP C 329 ? 1.0931 0.6430 0.9050 0.0719  0.0213  0.1930  329 ASP C O   
10893 C CB  . ASP C 329 ? 1.1369 0.7183 0.9645 0.1411  0.0235  0.1993  329 ASP C CB  
10894 C CG  . ASP C 329 ? 1.1913 0.7272 1.0095 0.1390  0.0281  0.1789  329 ASP C CG  
10895 O OD1 . ASP C 329 ? 1.2576 0.7361 1.0604 0.1465  0.0318  0.1828  329 ASP C OD1 
10896 O OD2 . ASP C 329 ? 1.0763 0.6327 0.9015 0.1305  0.0277  0.1590  329 ASP C OD2 
10897 N N   . PHE C 330 ? 1.0542 0.6964 0.8887 0.0844  0.0160  0.1925  330 PHE C N   
10898 C CA  . PHE C 330 ? 1.0709 0.7340 0.9093 0.0589  0.0146  0.1794  330 PHE C CA  
10899 C C   . PHE C 330 ? 1.0794 0.7270 0.9083 0.0386  0.0154  0.1910  330 PHE C C   
10900 O O   . PHE C 330 ? 1.1474 0.7738 0.9729 0.0195  0.0170  0.1817  330 PHE C O   
10901 C CB  . PHE C 330 ? 0.9673 0.6896 0.8184 0.0586  0.0102  0.1760  330 PHE C CB  
10902 C CG  . PHE C 330 ? 0.9656 0.7092 0.8239 0.0405  0.0093  0.1567  330 PHE C CG  
10903 C CD1 . PHE C 330 ? 0.9727 0.7088 0.8362 0.0416  0.0102  0.1379  330 PHE C CD1 
10904 C CD2 . PHE C 330 ? 1.0740 0.8456 0.9330 0.0234  0.0078  0.1578  330 PHE C CD2 
10905 C CE1 . PHE C 330 ? 1.0444 0.8004 0.9150 0.0260  0.0090  0.1218  330 PHE C CE1 
10906 C CE2 . PHE C 330 ? 1.0816 0.8725 0.9478 0.0091  0.0074  0.1407  330 PHE C CE2 
10907 C CZ  . PHE C 330 ? 1.0535 0.8364 0.9261 0.0105  0.0076  0.1232  330 PHE C CZ  
10908 N N   . ILE C 331 ? 1.0222 0.6822 0.8469 0.0421  0.0141  0.2125  331 ILE C N   
10909 C CA  . ILE C 331 ? 1.1048 0.7542 0.9201 0.0231  0.0154  0.2266  331 ILE C CA  
10910 C C   . ILE C 331 ? 1.1435 0.7306 0.9474 0.0165  0.0187  0.2292  331 ILE C C   
10911 O O   . ILE C 331 ? 1.1964 0.7712 0.9971 -0.0074 0.0201  0.2266  331 ILE C O   
10912 C CB  . ILE C 331 ? 1.1044 0.7742 0.9146 0.0317  0.0134  0.2514  331 ILE C CB  
10913 C CG1 . ILE C 331 ? 1.0500 0.7820 0.8680 0.0298  0.0095  0.2471  331 ILE C CG1 
10914 C CG2 . ILE C 331 ? 1.0826 0.7275 0.8801 0.0160  0.0158  0.2707  331 ILE C CG2 
10915 C CD1 . ILE C 331 ? 1.0676 0.8252 0.8820 0.0071  0.0108  0.2484  331 ILE C CD1 
10916 N N   . GLY C 332 ? 1.1043 0.6514 0.9019 0.0374  0.0198  0.2339  332 GLY C N   
10917 C CA  . GLY C 332 ? 1.1591 0.6404 0.9433 0.0323  0.0225  0.2337  332 GLY C CA  
10918 C C   . GLY C 332 ? 1.1694 0.6345 0.9547 0.0182  0.0231  0.2080  332 GLY C C   
10919 O O   . GLY C 332 ? 1.2431 0.6664 1.0185 -0.0005 0.0237  0.2060  332 GLY C O   
10920 N N   . ARG C 333 ? 1.0967 0.5951 0.8937 0.0257  0.0223  0.1888  333 ARG C N   
10921 C CA  . ARG C 333 ? 1.1226 0.6120 0.9210 0.0123  0.0222  0.1649  333 ARG C CA  
10922 C C   . ARG C 333 ? 1.1883 0.6980 0.9915 -0.0186 0.0206  0.1617  333 ARG C C   
10923 O O   . ARG C 333 ? 1.2285 0.7124 1.0271 -0.0366 0.0201  0.1501  333 ARG C O   
10924 C CB  . ARG C 333 ? 1.0537 0.5782 0.8639 0.0274  0.0216  0.1482  333 ARG C CB  
10925 C CG  . ARG C 333 ? 1.1077 0.6053 0.9125 0.0551  0.0245  0.1448  333 ARG C CG  
10926 C CD  . ARG C 333 ? 1.1340 0.6388 0.9428 0.0584  0.0251  0.1212  333 ARG C CD  
10927 N NE  . ARG C 333 ? 1.1132 0.6199 0.9237 0.0884  0.0282  0.1205  333 ARG C NE  
10928 C CZ  . ARG C 333 ? 1.2126 0.6915 1.0149 0.1006  0.0319  0.1056  333 ARG C CZ  
10929 N NH1 . ARG C 333 ? 1.1925 0.6375 0.9829 0.0847  0.0319  0.0888  333 ARG C NH1 
10930 N NH2 . ARG C 333 ? 1.1687 0.6561 0.9743 0.1294  0.0357  0.1076  333 ARG C NH2 
10931 N N   . LEU C 334 ? 1.0737 0.6312 0.8856 -0.0249 0.0198  0.1714  334 LEU C N   
10932 C CA  . LEU C 334 ? 1.1270 0.7063 0.9437 -0.0521 0.0197  0.1702  334 LEU C CA  
10933 C C   . LEU C 334 ? 1.1269 0.6694 0.9323 -0.0699 0.0211  0.1865  334 LEU C C   
10934 O O   . LEU C 334 ? 1.1268 0.6697 0.9344 -0.0948 0.0211  0.1826  334 LEU C O   
10935 C CB  . LEU C 334 ? 1.1014 0.7400 0.9278 -0.0521 0.0193  0.1753  334 LEU C CB  
10936 C CG  . LEU C 334 ? 1.0366 0.7131 0.8736 -0.0352 0.0171  0.1629  334 LEU C CG  
10937 C CD1 . LEU C 334 ? 1.0477 0.7628 0.8857 -0.0268 0.0159  0.1761  334 LEU C CD1 
10938 C CD2 . LEU C 334 ? 0.9779 0.6815 0.8264 -0.0465 0.0161  0.1426  334 LEU C CD2 
10939 N N   . LYS C 335 ? 1.1383 0.6501 0.9323 -0.0578 0.0221  0.2060  335 LYS C N   
10940 C CA  . LYS C 335 ? 1.2779 0.7462 1.0593 -0.0741 0.0231  0.2230  335 LYS C CA  
10941 C C   . LYS C 335 ? 1.3578 0.7744 1.1316 -0.0879 0.0221  0.2088  335 LYS C C   
10942 O O   . LYS C 335 ? 1.3665 0.7687 1.1376 -0.1155 0.0216  0.2128  335 LYS C O   
10943 C CB  . LYS C 335 ? 1.3814 0.8198 1.1511 -0.0540 0.0239  0.2456  335 LYS C CB  
10944 C CG  . LYS C 335 ? 1.3347 0.8089 1.1046 -0.0561 0.0246  0.2698  335 LYS C CG  
10945 C CD  . LYS C 335 ? 1.4412 0.8845 1.1995 -0.0358 0.0246  0.2939  335 LYS C CD  
10946 C CE  . LYS C 335 ? 1.4888 0.9387 1.2395 -0.0503 0.0257  0.3222  335 LYS C CE  
10947 N NZ  . LYS C 335 ? 1.2130 0.7096 0.9652 -0.0337 0.0244  0.3384  335 LYS C NZ  
10948 N N   . LYS C 336 ? 1.3194 0.7085 1.0889 -0.0695 0.0217  0.1923  336 LYS C N   
10949 C CA  . LYS C 336 ? 1.4076 0.7477 1.1671 -0.0818 0.0202  0.1757  336 LYS C CA  
10950 C C   . LYS C 336 ? 1.4321 0.8046 1.2029 -0.1087 0.0176  0.1605  336 LYS C C   
10951 O O   . LYS C 336 ? 1.5584 0.9004 1.3225 -0.1336 0.0152  0.1569  336 LYS C O   
10952 C CB  . LYS C 336 ? 1.3217 0.6371 1.0751 -0.0547 0.0211  0.1591  336 LYS C CB  
10953 C CG  . LYS C 336 ? 1.3911 0.6776 1.1353 -0.0247 0.0241  0.1743  336 LYS C CG  
10954 C CD  . LYS C 336 ? 1.4589 0.6813 1.1849 -0.0326 0.0246  0.1918  336 LYS C CD  
10955 C CE  . LYS C 336 ? 1.4781 0.6276 1.1841 -0.0225 0.0257  0.1783  336 LYS C CE  
10956 N NZ  . LYS C 336 ? 1.4312 0.5174 1.1197 -0.0482 0.0236  0.1838  336 LYS C NZ  
10957 N N   . ILE C 337 ? 1.1980 0.6324 0.9860 -0.1046 0.0175  0.1523  337 ILE C N   
10958 C CA  . ILE C 337 ? 1.2429 0.7125 1.0433 -0.1276 0.0153  0.1398  337 ILE C CA  
10959 C C   . ILE C 337 ? 1.3027 0.7861 1.1066 -0.1545 0.0161  0.1562  337 ILE C C   
10960 O O   . ILE C 337 ? 1.2828 0.7682 1.0908 -0.1801 0.0138  0.1503  337 ILE C O   
10961 C CB  . ILE C 337 ? 1.1974 0.7267 1.0144 -0.1150 0.0154  0.1287  337 ILE C CB  
10962 C CG1 . ILE C 337 ? 1.1824 0.7006 0.9965 -0.0885 0.0152  0.1157  337 ILE C CG1 
10963 C CG2 . ILE C 337 ? 1.1456 0.7083 0.9755 -0.1358 0.0131  0.1154  337 ILE C CG2 
10964 C CD1 . ILE C 337 ? 1.0393 0.6115 0.8679 -0.0729 0.0152  0.1103  337 ILE C CD1 
10965 N N   . HIS C 338 ? 1.3245 0.8203 1.1270 -0.1494 0.0191  0.1779  338 HIS C N   
10966 C CA  . HIS C 338 ? 1.3380 0.8516 1.1434 -0.1739 0.0210  0.1954  338 HIS C CA  
10967 C C   . HIS C 338 ? 1.3753 0.8355 1.1697 -0.1985 0.0191  0.2016  338 HIS C C   
10968 O O   . HIS C 338 ? 1.3071 0.7827 1.1091 -0.2265 0.0181  0.2011  338 HIS C O   
10969 C CB  . HIS C 338 ? 1.2372 0.7670 1.0386 -0.1621 0.0244  0.2185  338 HIS C CB  
10970 C CG  . HIS C 338 ? 1.2976 0.8637 1.1040 -0.1836 0.0278  0.2350  338 HIS C CG  
10971 N ND1 . HIS C 338 ? 1.3130 0.8542 1.1089 -0.1966 0.0296  0.2600  338 HIS C ND1 
10972 C CD2 . HIS C 338 ? 1.2452 0.8713 1.0658 -0.1934 0.0303  0.2306  338 HIS C CD2 
10973 C CE1 . HIS C 338 ? 1.2481 0.8353 1.0515 -0.2143 0.0335  0.2706  338 HIS C CE1 
10974 N NE2 . HIS C 338 ? 1.2958 0.9350 1.1142 -0.2118 0.0342  0.2525  338 HIS C NE2 
10975 N N   . GLU C 339 ? 1.4199 0.8164 1.1964 -0.1884 0.0183  0.2077  339 GLU C N   
10976 C CA  . GLU C 339 ? 1.4798 0.8156 1.2426 -0.2111 0.0157  0.2119  339 GLU C CA  
10977 C C   . GLU C 339 ? 1.4288 0.7443 1.1903 -0.2240 0.0107  0.1863  339 GLU C C   
10978 O O   . GLU C 339 ? 1.4401 0.7164 1.1931 -0.2507 0.0072  0.1874  339 GLU C O   
10979 C CB  . GLU C 339 ? 1.5540 0.8236 1.2964 -0.1927 0.0165  0.2247  339 GLU C CB  
10980 C CG  . GLU C 339 ? 1.5375 0.8300 1.2808 -0.1694 0.0204  0.2462  339 GLU C CG  
10981 C CD  . GLU C 339 ? 1.5937 0.8395 1.3233 -0.1363 0.0212  0.2481  339 GLU C CD  
10982 O OE1 . GLU C 339 ? 1.6060 0.7988 1.3241 -0.1307 0.0197  0.2320  339 GLU C OE1 
10983 O OE2 . GLU C 339 ? 1.5407 0.8049 1.2711 -0.1151 0.0233  0.2653  339 GLU C OE2 
10984 N N   . SER C 340 ? 1.3500 0.6918 1.1192 -0.2073 0.0099  0.1640  340 SER C N   
10985 C CA  . SER C 340 ? 1.3985 0.7210 1.1640 -0.2169 0.0050  0.1396  340 SER C CA  
10986 C C   . SER C 340 ? 1.4240 0.7905 1.2058 -0.2469 0.0015  0.1333  340 SER C C   
10987 O O   . SER C 340 ? 1.4036 0.7540 1.1816 -0.2603 -0.0040 0.1152  340 SER C O   
10988 C CB  . SER C 340 ? 1.3026 0.6368 1.0695 -0.1869 0.0057  0.1199  340 SER C CB  
10989 O OG  . SER C 340 ? 1.2823 0.6849 1.0701 -0.1862 0.0057  0.1115  340 SER C OG  
10990 N N   . VAL C 341 ? 1.3712 0.7938 1.1703 -0.2569 0.0045  0.1474  341 VAL C N   
10991 C CA  . VAL C 341 ? 1.3291 0.8023 1.1468 -0.2812 0.0023  0.1423  341 VAL C CA  
10992 C C   . VAL C 341 ? 1.3539 0.8463 1.1782 -0.3059 0.0050  0.1659  341 VAL C C   
10993 O O   . VAL C 341 ? 1.3932 0.8875 1.2138 -0.2975 0.0103  0.1855  341 VAL C O   
10994 C CB  . VAL C 341 ? 1.2945 0.8333 1.1310 -0.2638 0.0043  0.1310  341 VAL C CB  
10995 C CG1 . VAL C 341 ? 1.3387 0.8634 1.1706 -0.2450 0.0010  0.1076  341 VAL C CG1 
10996 C CG2 . VAL C 341 ? 1.2740 0.8431 1.1143 -0.2432 0.0109  0.1451  341 VAL C CG2 
10997 N N   . ASP C 342 ? 1.3466 0.8564 1.1810 -0.3372 0.0013  0.1645  342 ASP C N   
10998 C CA  . ASP C 342 ? 1.3774 0.9161 1.2217 -0.3632 0.0044  0.1867  342 ASP C CA  
10999 C C   . ASP C 342 ? 1.3073 0.9261 1.1730 -0.3550 0.0112  0.1910  342 ASP C C   
11000 O O   . ASP C 342 ? 1.2531 0.8973 1.1224 -0.3616 0.0174  0.2122  342 ASP C O   
11001 C CB  . ASP C 342 ? 1.4463 0.9780 1.2953 -0.4008 -0.0025 0.1841  342 ASP C CB  
11002 C CG  . ASP C 342 ? 1.5559 1.1084 1.4144 -0.4011 -0.0089 0.1584  342 ASP C CG  
11003 O OD1 . ASP C 342 ? 1.5105 1.0423 1.3598 -0.3757 -0.0105 0.1400  342 ASP C OD1 
11004 O OD2 . ASP C 342 ? 1.5477 1.1397 1.4231 -0.4266 -0.0123 0.1578  342 ASP C OD2 
11005 N N   . PHE C 343 ? 1.2678 0.9251 1.1463 -0.3404 0.0102  0.1715  343 PHE C N   
11006 C CA  . PHE C 343 ? 1.1404 0.8690 1.0376 -0.3301 0.0163  0.1720  343 PHE C CA  
11007 C C   . PHE C 343 ? 1.1201 0.8528 1.0096 -0.2992 0.0216  0.1753  343 PHE C C   
11008 O O   . PHE C 343 ? 1.1695 0.8545 1.0421 -0.2835 0.0202  0.1757  343 PHE C O   
11009 C CB  . PHE C 343 ? 1.1449 0.9084 1.0579 -0.3267 0.0123  0.1504  343 PHE C CB  
11010 C CG  . PHE C 343 ? 1.1284 0.8578 1.0312 -0.3058 0.0072  0.1300  343 PHE C CG  
11011 C CD1 . PHE C 343 ? 1.1549 0.8351 1.0460 -0.3169 -0.0004 0.1194  343 PHE C CD1 
11012 C CD2 . PHE C 343 ? 1.1574 0.9050 1.0616 -0.2759 0.0100  0.1214  343 PHE C CD2 
11013 C CE1 . PHE C 343 ? 1.1359 0.7879 1.0167 -0.2969 -0.0040 0.1009  343 PHE C CE1 
11014 C CE2 . PHE C 343 ? 1.1456 0.8660 1.0416 -0.2575 0.0060  0.1043  343 PHE C CE2 
11015 C CZ  . PHE C 343 ? 1.0490 0.7228 0.9333 -0.2672 -0.0005 0.0942  343 PHE C CZ  
11016 N N   . GLN C 344 ? 1.1141 0.9056 1.0160 -0.2900 0.0276  0.1774  344 GLN C N   
11017 C CA  . GLN C 344 ? 1.0674 0.8707 0.9633 -0.2618 0.0314  0.1774  344 GLN C CA  
11018 C C   . GLN C 344 ? 1.0270 0.8278 0.9252 -0.2398 0.0271  0.1547  344 GLN C C   
11019 O O   . GLN C 344 ? 1.0294 0.8688 0.9426 -0.2379 0.0268  0.1411  344 GLN C O   
11020 C CB  . GLN C 344 ? 1.0348 0.8994 0.9404 -0.2606 0.0391  0.1854  344 GLN C CB  
11021 C CG  . GLN C 344 ? 1.0900 0.9526 0.9831 -0.2620 0.0447  0.2090  344 GLN C CG  
11022 C CD  . GLN C 344 ? 1.0282 0.9502 0.9306 -0.2703 0.0531  0.2190  344 GLN C CD  
11023 O OE1 . GLN C 344 ? 1.0311 0.9858 0.9499 -0.2864 0.0548  0.2160  344 GLN C OE1 
11024 N NE2 . GLN C 344 ? 1.0129 0.9516 0.9045 -0.2590 0.0585  0.2313  344 GLN C NE2 
11025 N N   . PRO C 345 ? 1.0492 0.8071 0.9335 -0.2224 0.0242  0.1512  345 PRO C N   
11026 C CA  . PRO C 345 ? 1.0145 0.7674 0.9008 -0.2045 0.0201  0.1305  345 PRO C CA  
11027 C C   . PRO C 345 ? 0.9262 0.7224 0.8202 -0.1842 0.0224  0.1242  345 PRO C C   
11028 O O   . PRO C 345 ? 0.9323 0.7464 0.8226 -0.1760 0.0264  0.1355  345 PRO C O   
11029 C CB  . PRO C 345 ? 1.0107 0.7062 0.8792 -0.1918 0.0179  0.1326  345 PRO C CB  
11030 C CG  . PRO C 345 ? 1.0581 0.7471 0.9176 -0.1907 0.0220  0.1549  345 PRO C CG  
11031 C CD  . PRO C 345 ? 1.1092 0.8232 0.9758 -0.2168 0.0250  0.1673  345 PRO C CD  
11032 N N   . VAL C 346 ? 0.9195 0.7315 0.8231 -0.1771 0.0193  0.1058  346 VAL C N   
11033 C CA  . VAL C 346 ? 0.8758 0.7209 0.7857 -0.1580 0.0200  0.0970  346 VAL C CA  
11034 C C   . VAL C 346 ? 0.9111 0.7302 0.8157 -0.1406 0.0158  0.0855  346 VAL C C   
11035 O O   . VAL C 346 ? 0.8915 0.6977 0.7987 -0.1435 0.0119  0.0729  346 VAL C O   
11036 C CB  . VAL C 346 ? 0.7885 0.6781 0.7153 -0.1633 0.0207  0.0870  346 VAL C CB  
11037 C CG1 . VAL C 346 ? 0.8330 0.7413 0.7644 -0.1436 0.0191  0.0738  346 VAL C CG1 
11038 C CG2 . VAL C 346 ? 0.8509 0.7760 0.7825 -0.1726 0.0271  0.0988  346 VAL C CG2 
11039 N N   . VAL C 347 ? 0.8783 0.6928 0.7756 -0.1226 0.0164  0.0905  347 VAL C N   
11040 C CA  . VAL C 347 ? 0.8507 0.6453 0.7438 -0.1045 0.0134  0.0824  347 VAL C CA  
11041 C C   . VAL C 347 ? 0.8685 0.6988 0.7698 -0.0908 0.0123  0.0745  347 VAL C C   
11042 O O   . VAL C 347 ? 0.8365 0.6902 0.7370 -0.0859 0.0139  0.0818  347 VAL C O   
11043 C CB  . VAL C 347 ? 0.8480 0.6089 0.7274 -0.0940 0.0142  0.0956  347 VAL C CB  
11044 C CG1 . VAL C 347 ? 0.9479 0.6953 0.8252 -0.0736 0.0121  0.0876  347 VAL C CG1 
11045 C CG2 . VAL C 347 ? 0.8736 0.5928 0.7431 -0.1083 0.0149  0.1032  347 VAL C CG2 
11046 N N   . PHE C 348 ? 0.8901 0.7235 0.7979 -0.0855 0.0092  0.0597  348 PHE C N   
11047 C CA  . PHE C 348 ? 0.8243 0.6854 0.7396 -0.0733 0.0073  0.0516  348 PHE C CA  
11048 C C   . PHE C 348 ? 0.8775 0.7229 0.7882 -0.0565 0.0054  0.0509  348 PHE C C   
11049 O O   . PHE C 348 ? 0.8812 0.7010 0.7883 -0.0537 0.0046  0.0456  348 PHE C O   
11050 C CB  . PHE C 348 ? 0.7950 0.6730 0.7216 -0.0785 0.0052  0.0375  348 PHE C CB  
11051 C CG  . PHE C 348 ? 0.7612 0.6734 0.6969 -0.0856 0.0071  0.0362  348 PHE C CG  
11052 C CD1 . PHE C 348 ? 0.7320 0.6508 0.6683 -0.0996 0.0107  0.0440  348 PHE C CD1 
11053 C CD2 . PHE C 348 ? 0.7285 0.6659 0.6723 -0.0780 0.0055  0.0272  348 PHE C CD2 
11054 C CE1 . PHE C 348 ? 0.6352 0.5887 0.5804 -0.1041 0.0138  0.0427  348 PHE C CE1 
11055 C CE2 . PHE C 348 ? 0.6267 0.5935 0.5779 -0.0819 0.0081  0.0249  348 PHE C CE2 
11056 C CZ  . PHE C 348 ? 0.6006 0.5771 0.5527 -0.0941 0.0126  0.0325  348 PHE C CZ  
11057 N N   . VAL C 349 ? 0.8930 0.7554 0.8033 -0.0456 0.0045  0.0561  349 VAL C N   
11058 C CA  . VAL C 349 ? 0.7937 0.6515 0.7032 -0.0294 0.0025  0.0567  349 VAL C CA  
11059 C C   . VAL C 349 ? 0.7810 0.6683 0.7001 -0.0255 -0.0010 0.0471  349 VAL C C   
11060 O O   . VAL C 349 ? 0.7812 0.6922 0.7012 -0.0250 -0.0025 0.0495  349 VAL C O   
11061 C CB  . VAL C 349 ? 0.8118 0.6663 0.7137 -0.0205 0.0030  0.0724  349 VAL C CB  
11062 C CG1 . VAL C 349 ? 0.8591 0.7151 0.7630 -0.0031 0.0009  0.0737  349 VAL C CG1 
11063 C CG2 . VAL C 349 ? 0.8723 0.6933 0.7640 -0.0254 0.0064  0.0828  349 VAL C CG2 
11064 N N   . VAL C 350 ? 0.7982 0.6829 0.7230 -0.0237 -0.0024 0.0362  350 VAL C N   
11065 C CA  . VAL C 350 ? 0.8666 0.7750 0.8006 -0.0218 -0.0059 0.0273  350 VAL C CA  
11066 C C   . VAL C 350 ? 0.8438 0.7508 0.7800 -0.0096 -0.0076 0.0267  350 VAL C C   
11067 O O   . VAL C 350 ? 0.8464 0.7353 0.7804 -0.0062 -0.0060 0.0230  350 VAL C O   
11068 C CB  . VAL C 350 ? 0.7649 0.6775 0.7053 -0.0314 -0.0063 0.0163  350 VAL C CB  
11069 C CG1 . VAL C 350 ? 0.7903 0.7236 0.7394 -0.0285 -0.0101 0.0087  350 VAL C CG1 
11070 C CG2 . VAL C 350 ? 0.6480 0.5669 0.5882 -0.0431 -0.0038 0.0182  350 VAL C CG2 
11071 N N   . LEU C 351 ? 0.7230 0.6505 0.6629 -0.0035 -0.0109 0.0301  351 LEU C N   
11072 C CA  . LEU C 351 ? 0.7684 0.7024 0.7133 0.0071  -0.0127 0.0309  351 LEU C CA  
11073 C C   . LEU C 351 ? 0.7490 0.7103 0.7008 0.0058  -0.0182 0.0299  351 LEU C C   
11074 O O   . LEU C 351 ? 0.7015 0.6734 0.6517 -0.0013 -0.0204 0.0284  351 LEU C O   
11075 C CB  . LEU C 351 ? 0.7111 0.6349 0.6512 0.0196  -0.0103 0.0422  351 LEU C CB  
11076 C CG  . LEU C 351 ? 0.8441 0.7803 0.7813 0.0218  -0.0124 0.0542  351 LEU C CG  
11077 C CD1 . LEU C 351 ? 0.6512 0.5957 0.5913 0.0371  -0.0131 0.0648  351 LEU C CD1 
11078 C CD2 . LEU C 351 ? 0.8146 0.7311 0.7416 0.0166  -0.0089 0.0601  351 LEU C CD2 
11079 N N   . ASP C 352 ? 0.7257 0.6980 0.6844 0.0124  -0.0204 0.0307  352 ASP C N   
11080 C CA  . ASP C 352 ? 0.7105 0.7069 0.6758 0.0095  -0.0267 0.0306  352 ASP C CA  
11081 C C   . ASP C 352 ? 0.7321 0.7419 0.6938 0.0114  -0.0299 0.0402  352 ASP C C   
11082 O O   . ASP C 352 ? 0.8551 0.8629 0.8148 0.0210  -0.0278 0.0508  352 ASP C O   
11083 C CB  . ASP C 352 ? 0.7305 0.7380 0.7050 0.0151  -0.0279 0.0316  352 ASP C CB  
11084 C CG  . ASP C 352 ? 0.8887 0.8861 0.8654 0.0126  -0.0257 0.0225  352 ASP C CG  
11085 O OD1 . ASP C 352 ? 0.8445 0.8300 0.8179 0.0053  -0.0248 0.0148  352 ASP C OD1 
11086 O OD2 . ASP C 352 ? 0.9279 0.9319 0.9100 0.0181  -0.0247 0.0238  352 ASP C OD2 
11087 N N   . GLY C 353 ? 0.7217 0.7445 0.6815 0.0030  -0.0351 0.0366  353 GLY C N   
11088 C CA  . GLY C 353 ? 0.6829 0.7186 0.6358 0.0024  -0.0386 0.0440  353 GLY C CA  
11089 C C   . GLY C 353 ? 0.7540 0.8137 0.7121 0.0044  -0.0459 0.0512  353 GLY C C   
11090 O O   . GLY C 353 ? 0.7808 0.8537 0.7327 0.0044  -0.0497 0.0588  353 GLY C O   
11091 N N   . GLU C 354 ? 0.8308 0.8995 0.8004 0.0055  -0.0482 0.0504  354 GLU C N   
11092 C CA  . GLU C 354 ? 0.7667 0.8626 0.7434 0.0047  -0.0560 0.0577  354 GLU C CA  
11093 C C   . GLU C 354 ? 0.7383 0.8464 0.7271 0.0166  -0.0537 0.0682  354 GLU C C   
11094 O O   . GLU C 354 ? 0.8247 0.9598 0.8204 0.0185  -0.0593 0.0785  354 GLU C O   
11095 C CB  . GLU C 354 ? 0.7004 0.8033 0.6807 -0.0082 -0.0630 0.0480  354 GLU C CB  
11096 C CG  . GLU C 354 ? 0.7858 0.8822 0.7763 -0.0083 -0.0602 0.0432  354 GLU C CG  
11097 C CD  . GLU C 354 ? 0.7752 0.8471 0.7606 -0.0121 -0.0559 0.0305  354 GLU C CD  
11098 O OE1 . GLU C 354 ? 0.7804 0.8490 0.7649 -0.0215 -0.0604 0.0216  354 GLU C OE1 
11099 O OE2 . GLU C 354 ? 0.7537 0.8096 0.7362 -0.0055 -0.0483 0.0296  354 GLU C OE2 
11100 N N   . ASN C 355 ? 0.7304 0.8215 0.7216 0.0248  -0.0456 0.0660  355 ASN C N   
11101 C CA  . ASN C 355 ? 0.7950 0.9003 0.7977 0.0358  -0.0429 0.0735  355 ASN C CA  
11102 C C   . ASN C 355 ? 0.7386 0.8443 0.7405 0.0532  -0.0382 0.0861  355 ASN C C   
11103 O O   . ASN C 355 ? 0.8156 0.9465 0.8285 0.0630  -0.0386 0.0968  355 ASN C O   
11104 C CB  . ASN C 355 ? 0.7900 0.8793 0.7944 0.0371  -0.0367 0.0645  355 ASN C CB  
11105 C CG  . ASN C 355 ? 0.6915 0.7807 0.6981 0.0219  -0.0414 0.0541  355 ASN C CG  
11106 O OD1 . ASN C 355 ? 0.6408 0.7513 0.6553 0.0136  -0.0486 0.0563  355 ASN C OD1 
11107 N ND2 . ASN C 355 ? 0.7838 0.8486 0.7836 0.0181  -0.0379 0.0433  355 ASN C ND2 
11108 N N   . CYS C 356 ? 0.7690 0.8481 0.7588 0.0575  -0.0335 0.0862  356 CYS C N   
11109 C CA  . CYS C 356 ? 0.7114 0.7830 0.6993 0.0756  -0.0280 0.0978  356 CYS C CA  
11110 C C   . CYS C 356 ? 0.7018 0.8014 0.6938 0.0810  -0.0340 0.1135  356 CYS C C   
11111 O O   . CYS C 356 ? 0.7697 0.8742 0.7655 0.0989  -0.0306 0.1258  356 CYS C O   
11112 C CB  . CYS C 356 ? 0.7288 0.7615 0.7020 0.0764  -0.0222 0.0948  356 CYS C CB  
11113 S SG  . CYS C 356 ? 0.7229 0.7518 0.6856 0.0579  -0.0271 0.0906  356 CYS C SG  
11114 N N   . TRP C 357 ? 0.7718 0.8900 0.7622 0.0667  -0.0430 0.1131  357 TRP C N   
11115 C CA  . TRP C 357 ? 0.7739 0.9139 0.7627 0.0699  -0.0492 0.1275  357 TRP C CA  
11116 C C   . TRP C 357 ? 0.7431 0.9237 0.7483 0.0776  -0.0543 0.1401  357 TRP C C   
11117 O O   . TRP C 357 ? 0.8292 1.0270 0.8362 0.0887  -0.0568 0.1560  357 TRP C O   
11118 C CB  . TRP C 357 ? 0.6811 0.8273 0.6597 0.0518  -0.0571 0.1214  357 TRP C CB  
11119 C CG  . TRP C 357 ? 0.6728 0.7862 0.6372 0.0445  -0.0517 0.1108  357 TRP C CG  
11120 C CD1 . TRP C 357 ? 0.7339 0.8412 0.6920 0.0290  -0.0538 0.0962  357 TRP C CD1 
11121 C CD2 . TRP C 357 ? 0.7282 0.8112 0.6832 0.0521  -0.0435 0.1148  357 TRP C CD2 
11122 N NE1 . TRP C 357 ? 0.7973 0.8773 0.7446 0.0268  -0.0471 0.0913  357 TRP C NE1 
11123 C CE2 . TRP C 357 ? 0.8012 0.8655 0.7463 0.0393  -0.0411 0.1027  357 TRP C CE2 
11124 C CE3 . TRP C 357 ? 0.6981 0.7670 0.6522 0.0686  -0.0379 0.1277  357 TRP C CE3 
11125 C CZ2 . TRP C 357 ? 0.7810 0.8159 0.7164 0.0400  -0.0339 0.1038  357 TRP C CZ2 
11126 C CZ3 . TRP C 357 ? 0.7304 0.7647 0.6729 0.0692  -0.0311 0.1280  357 TRP C CZ3 
11127 C CH2 . TRP C 357 ? 0.7113 0.7303 0.6451 0.0538  -0.0293 0.1165  357 TRP C CH2 
11128 N N   . GLU C 358 ? 0.7838 0.9823 0.8017 0.0719  -0.0562 0.1346  358 GLU C N   
11129 C CA  . GLU C 358 ? 0.7942 1.0364 0.8299 0.0769  -0.0613 0.1474  358 GLU C CA  
11130 C C   . GLU C 358 ? 0.8367 1.0843 0.8811 0.1028  -0.0527 0.1606  358 GLU C C   
11131 O O   . GLU C 358 ? 0.8741 1.1610 0.9325 0.1115  -0.0568 0.1761  358 GLU C O   
11132 C CB  . GLU C 358 ? 0.8280 1.0840 0.8742 0.0630  -0.0644 0.1385  358 GLU C CB  
11133 C CG  . GLU C 358 ? 0.8892 1.1307 0.9406 0.0732  -0.0534 0.1333  358 GLU C CG  
11134 C CD  . GLU C 358 ? 0.9877 1.2539 1.0532 0.0622  -0.0567 0.1313  358 GLU C CD  
11135 O OE1 . GLU C 358 ? 1.0611 1.3586 1.1348 0.0485  -0.0678 0.1364  358 GLU C OE1 
11136 O OE2 . GLU C 358 ? 1.0472 1.2998 1.1138 0.0653  -0.0490 0.1241  358 GLU C OE2 
11137 N N   . TYR C 359 ? 0.8341 1.0436 0.8703 0.1153  -0.0412 0.1547  359 TYR C N   
11138 C CA  . TYR C 359 ? 0.7847 0.9896 0.8245 0.1418  -0.0319 0.1651  359 TYR C CA  
11139 C C   . TYR C 359 ? 0.8613 1.0463 0.8898 0.1535  -0.0309 0.1759  359 TYR C C   
11140 O O   . TYR C 359 ? 0.8589 1.0339 0.8881 0.1771  -0.0233 0.1853  359 TYR C O   
11141 C CB  . TYR C 359 ? 0.7910 0.9616 0.8249 0.1490  -0.0204 0.1520  359 TYR C CB  
11142 C CG  . TYR C 359 ? 0.8026 0.9903 0.8458 0.1373  -0.0210 0.1422  359 TYR C CG  
11143 C CD1 . TYR C 359 ? 0.8682 1.0955 0.9292 0.1461  -0.0195 0.1504  359 TYR C CD1 
11144 C CD2 . TYR C 359 ? 0.8126 0.9788 0.8475 0.1174  -0.0230 0.1261  359 TYR C CD2 
11145 C CE1 . TYR C 359 ? 0.9611 1.2042 1.0304 0.1343  -0.0201 0.1433  359 TYR C CE1 
11146 C CE2 . TYR C 359 ? 1.0012 1.1814 1.0441 0.1070  -0.0239 0.1188  359 TYR C CE2 
11147 C CZ  . TYR C 359 ? 1.0260 1.2437 1.0855 0.1147  -0.0225 0.1276  359 TYR C CZ  
11148 O OH  . TYR C 359 ? 1.0231 1.2549 1.0902 0.1033  -0.0233 0.1222  359 TYR C OH  
11149 N N   . TYR C 360 ? 0.8623 1.0399 0.8793 0.1381  -0.0378 0.1749  360 TYR C N   
11150 C CA  . TYR C 360 ? 0.8011 0.9668 0.8076 0.1464  -0.0385 0.1882  360 TYR C CA  
11151 C C   . TYR C 360 ? 0.8345 1.0485 0.8517 0.1510  -0.0482 0.2067  360 TYR C C   
11152 O O   . TYR C 360 ? 0.8221 1.0775 0.8529 0.1414  -0.0562 0.2069  360 TYR C O   
11153 C CB  . TYR C 360 ? 0.7635 0.9038 0.7521 0.1276  -0.0410 0.1796  360 TYR C CB  
11154 C CG  . TYR C 360 ? 0.7607 0.8492 0.7354 0.1272  -0.0315 0.1694  360 TYR C CG  
11155 C CD1 . TYR C 360 ? 0.7560 0.8257 0.7312 0.1203  -0.0265 0.1516  360 TYR C CD1 
11156 C CD2 . TYR C 360 ? 0.7178 0.7773 0.6784 0.1317  -0.0285 0.1782  360 TYR C CD2 
11157 C CE1 . TYR C 360 ? 0.7761 0.8011 0.7387 0.1177  -0.0192 0.1422  360 TYR C CE1 
11158 C CE2 . TYR C 360 ? 0.8826 0.8957 0.8310 0.1283  -0.0208 0.1692  360 TYR C CE2 
11159 C CZ  . TYR C 360 ? 0.8350 0.8318 0.7845 0.1210  -0.0165 0.1508  360 TYR C CZ  
11160 O OH  . TYR C 360 ? 0.8361 0.7895 0.7737 0.1159  -0.0101 0.1422  360 TYR C OH  
11161 N N   . GLU C 361 ? 0.8962 1.1045 0.9069 0.1643  -0.0483 0.2231  361 GLU C N   
11162 C CA  . GLU C 361 ? 0.8405 1.0936 0.8579 0.1669  -0.0589 0.2419  361 GLU C CA  
11163 C C   . GLU C 361 ? 0.8285 1.0944 0.8346 0.1409  -0.0700 0.2358  361 GLU C C   
11164 O O   . GLU C 361 ? 0.8926 1.1264 0.8799 0.1313  -0.0681 0.2293  361 GLU C O   
11165 C CB  . GLU C 361 ? 0.9092 1.1487 0.9210 0.1895  -0.0555 0.2621  361 GLU C CB  
11166 C CG  . GLU C 361 ? 1.1004 1.3599 1.1301 0.2184  -0.0508 0.2772  361 GLU C CG  
11167 C CD  . GLU C 361 ? 1.1676 1.4920 1.2147 0.2214  -0.0624 0.2956  361 GLU C CD  
11168 O OE1 . GLU C 361 ? 1.1863 1.5276 1.2255 0.2127  -0.0728 0.3063  361 GLU C OE1 
11169 O OE2 . GLU C 361 ? 1.1525 1.5131 1.2211 0.2321  -0.0614 0.2998  361 GLU C OE2 
11170 N N   . GLU C 362 ? 0.8718 1.1850 0.8889 0.1293  -0.0816 0.2377  362 GLU C N   
11171 C CA  . GLU C 362 ? 0.8591 1.1876 0.8642 0.1054  -0.0934 0.2314  362 GLU C CA  
11172 C C   . GLU C 362 ? 0.8155 1.1084 0.8070 0.0867  -0.0897 0.2076  362 GLU C C   
11173 O O   . GLU C 362 ? 0.7864 1.0670 0.7592 0.0741  -0.0924 0.2017  362 GLU C O   
11174 C CB  . GLU C 362 ? 0.7064 1.0400 0.6970 0.1092  -0.0983 0.2472  362 GLU C CB  
11175 C CG  . GLU C 362 ? 0.7951 1.1545 0.7980 0.1333  -0.0994 0.2730  362 GLU C CG  
11176 C CD  . GLU C 362 ? 0.9852 1.4011 0.9933 0.1265  -0.1153 0.2867  362 GLU C CD  
11177 O OE1 . GLU C 362 ? 1.0744 1.5001 1.0686 0.1034  -0.1251 0.2770  362 GLU C OE1 
11178 O OE2 . GLU C 362 ? 0.9591 1.4104 0.9848 0.1443  -0.1181 0.3068  362 GLU C OE2 
11179 N N   . ASN C 363 ? 0.7942 1.0724 0.7951 0.0860  -0.0831 0.1946  363 ASN C N   
11180 C CA  . ASN C 363 ? 0.7555 1.0015 0.7468 0.0707  -0.0790 0.1729  363 ASN C CA  
11181 C C   . ASN C 363 ? 0.7936 0.9979 0.7671 0.0725  -0.0707 0.1692  363 ASN C C   
11182 O O   . ASN C 363 ? 0.7582 0.9444 0.7195 0.0576  -0.0703 0.1548  363 ASN C O   
11183 C CB  . ASN C 363 ? 0.6490 0.9123 0.6354 0.0474  -0.0901 0.1613  363 ASN C CB  
11184 C CG  . ASN C 363 ? 0.7542 1.0036 0.7455 0.0361  -0.0879 0.1432  363 ASN C CG  
11185 O OD1 . ASN C 363 ? 0.8256 1.0916 0.8337 0.0379  -0.0883 0.1446  363 ASN C OD1 
11186 N ND2 . ASN C 363 ? 0.7798 1.0007 0.7570 0.0249  -0.0853 0.1272  363 ASN C ND2 
11187 N N   . GLY C 364 ? 0.8173 1.0055 0.7895 0.0911  -0.0638 0.1825  364 GLY C N   
11188 C CA  . GLY C 364 ? 0.8163 0.9650 0.7723 0.0921  -0.0564 0.1820  364 GLY C CA  
11189 C C   . GLY C 364 ? 0.7710 0.9250 0.7105 0.0815  -0.0616 0.1869  364 GLY C C   
11190 O O   . GLY C 364 ? 0.8839 1.0076 0.8100 0.0785  -0.0554 0.1858  364 GLY C O   
11191 N N   . ILE C 365 ? 0.6601 0.8528 0.5994 0.0747  -0.0728 0.1922  365 ILE C N   
11192 C CA  . ILE C 365 ? 0.6744 0.8744 0.5953 0.0649  -0.0777 0.1963  365 ILE C CA  
11193 C C   . ILE C 365 ? 0.7438 0.9262 0.6554 0.0777  -0.0726 0.2154  365 ILE C C   
11194 O O   . ILE C 365 ? 0.8113 0.9753 0.7060 0.0696  -0.0689 0.2140  365 ILE C O   
11195 C CB  . ILE C 365 ? 0.7208 0.9662 0.6425 0.0564  -0.0918 0.1997  365 ILE C CB  
11196 C CG1 . ILE C 365 ? 0.6683 0.9171 0.5875 0.0364  -0.0963 0.1767  365 ILE C CG1 
11197 C CG2 . ILE C 365 ? 0.6951 0.9540 0.5989 0.0549  -0.0970 0.2134  365 ILE C CG2 
11198 C CD1 . ILE C 365 ? 0.6452 0.9326 0.5748 0.0287  -0.1089 0.1765  365 ILE C CD1 
11199 N N   . PRO C 366 ? 0.7208 0.9057 0.6423 0.0980  -0.0712 0.2337  366 PRO C N   
11200 C CA  . PRO C 366 ? 0.7445 0.9045 0.6554 0.1101  -0.0658 0.2518  366 PRO C CA  
11201 C C   . PRO C 366 ? 0.7532 0.8619 0.6562 0.1077  -0.0540 0.2429  366 PRO C C   
11202 O O   . PRO C 366 ? 0.8535 0.9424 0.7408 0.1028  -0.0508 0.2501  366 PRO C O   
11203 C CB  . PRO C 366 ? 0.7567 0.9278 0.6830 0.1349  -0.0659 0.2700  366 PRO C CB  
11204 C CG  . PRO C 366 ? 0.7528 0.9733 0.6947 0.1316  -0.0759 0.2675  366 PRO C CG  
11205 C CD  . PRO C 366 ? 0.8312 1.0458 0.7731 0.1114  -0.0753 0.2415  366 PRO C CD  
11206 N N   . PHE C 367 ? 0.8078 0.8963 0.7209 0.1099  -0.0477 0.2278  367 PHE C N   
11207 C CA  . PHE C 367 ? 0.7779 0.8186 0.6840 0.1071  -0.0375 0.2191  367 PHE C CA  
11208 C C   . PHE C 367 ? 0.7808 0.8154 0.6745 0.0851  -0.0368 0.2072  367 PHE C C   
11209 O O   . PHE C 367 ? 0.8035 0.8100 0.6852 0.0803  -0.0314 0.2119  367 PHE C O   
11210 C CB  . PHE C 367 ? 0.7835 0.8104 0.7019 0.1124  -0.0324 0.2038  367 PHE C CB  
11211 C CG  . PHE C 367 ? 0.8515 0.8340 0.7627 0.1051  -0.0239 0.1909  367 PHE C CG  
11212 C CD1 . PHE C 367 ? 0.9218 0.8623 0.8257 0.1158  -0.0168 0.1988  367 PHE C CD1 
11213 C CD2 . PHE C 367 ? 0.7757 0.7578 0.6872 0.0873  -0.0234 0.1711  367 PHE C CD2 
11214 C CE1 . PHE C 367 ? 0.8551 0.7555 0.7519 0.1066  -0.0102 0.1866  367 PHE C CE1 
11215 C CE2 . PHE C 367 ? 0.9260 0.8716 0.8320 0.0799  -0.0166 0.1601  367 PHE C CE2 
11216 C CZ  . PHE C 367 ? 0.8771 0.7826 0.7756 0.0884  -0.0104 0.1676  367 PHE C CZ  
11217 N N   . LEU C 368 ? 0.8161 0.8768 0.7126 0.0716  -0.0420 0.1920  368 LEU C N   
11218 C CA  . LEU C 368 ? 0.7979 0.8548 0.6836 0.0531  -0.0404 0.1791  368 LEU C CA  
11219 C C   . LEU C 368 ? 0.8053 0.8733 0.6744 0.0480  -0.0425 0.1922  368 LEU C C   
11220 O O   . LEU C 368 ? 0.8078 0.8594 0.6659 0.0384  -0.0367 0.1908  368 LEU C O   
11221 C CB  . LEU C 368 ? 0.7573 0.8372 0.6488 0.0422  -0.0459 0.1604  368 LEU C CB  
11222 C CG  . LEU C 368 ? 0.8142 0.8748 0.7131 0.0359  -0.0406 0.1408  368 LEU C CG  
11223 C CD1 . LEU C 368 ? 0.7811 0.8035 0.6796 0.0402  -0.0312 0.1422  368 LEU C CD1 
11224 C CD2 . LEU C 368 ? 0.7880 0.8638 0.7022 0.0397  -0.0451 0.1337  368 LEU C CD2 
11225 N N   . GLU C 369 ? 0.7505 0.8489 0.6176 0.0536  -0.0509 0.2058  369 GLU C N   
11226 C CA  . GLU C 369 ? 0.7522 0.8632 0.6015 0.0493  -0.0533 0.2198  369 GLU C CA  
11227 C C   . GLU C 369 ? 0.7941 0.8742 0.6369 0.0570  -0.0461 0.2386  369 GLU C C   
11228 O O   . GLU C 369 ? 0.7979 0.8732 0.6251 0.0482  -0.0428 0.2453  369 GLU C O   
11229 C CB  . GLU C 369 ? 0.8486 1.0003 0.6976 0.0542  -0.0651 0.2315  369 GLU C CB  
11230 C CG  . GLU C 369 ? 0.9005 1.0833 0.7458 0.0399  -0.0737 0.2142  369 GLU C CG  
11231 C CD  . GLU C 369 ? 0.9503 1.1748 0.7968 0.0428  -0.0870 0.2255  369 GLU C CD  
11232 O OE1 . GLU C 369 ? 0.9627 1.1952 0.8186 0.0585  -0.0893 0.2459  369 GLU C OE1 
11233 O OE2 . GLU C 369 ? 1.0477 1.2969 0.8853 0.0295  -0.0954 0.2138  369 GLU C OE2 
11234 N N   . LYS C 370 ? 0.8268 0.8844 0.6803 0.0732  -0.0430 0.2473  370 LYS C N   
11235 C CA  . LYS C 370 ? 0.8238 0.8435 0.6703 0.0803  -0.0361 0.2637  370 LYS C CA  
11236 C C   . LYS C 370 ? 0.8606 0.8458 0.7022 0.0660  -0.0272 0.2512  370 LYS C C   
11237 O O   . LYS C 370 ? 0.9795 0.9495 0.8080 0.0579  -0.0231 0.2617  370 LYS C O   
11238 C CB  . LYS C 370 ? 0.8371 0.8378 0.6952 0.1026  -0.0344 0.2729  370 LYS C CB  
11239 C CG  . LYS C 370 ? 0.9286 0.8874 0.7777 0.1124  -0.0285 0.2923  370 LYS C CG  
11240 C CD  . LYS C 370 ? 0.9966 0.9746 0.8374 0.1215  -0.0342 0.3199  370 LYS C CD  
11241 C CE  . LYS C 370 ? 1.0979 1.0389 0.9223 0.1176  -0.0289 0.3376  370 LYS C CE  
11242 N NZ  . LYS C 370 ? 1.1443 1.0816 0.9651 0.1380  -0.0317 0.3675  370 LYS C NZ  
11243 N N   . LEU C 371 ? 0.8359 0.8104 0.6880 0.0623  -0.0243 0.2298  371 LEU C N   
11244 C CA  . LEU C 371 ? 0.8628 0.8071 0.7123 0.0489  -0.0167 0.2179  371 LEU C CA  
11245 C C   . LEU C 371 ? 0.7937 0.7558 0.6330 0.0305  -0.0157 0.2140  371 LEU C C   
11246 O O   . LEU C 371 ? 0.8145 0.7588 0.6444 0.0216  -0.0104 0.2226  371 LEU C O   
11247 C CB  . LEU C 371 ? 0.8327 0.7703 0.6953 0.0485  -0.0153 0.1959  371 LEU C CB  
11248 C CG  . LEU C 371 ? 0.7957 0.7138 0.6577 0.0324  -0.0095 0.1805  371 LEU C CG  
11249 C CD1 . LEU C 371 ? 0.8307 0.7030 0.6871 0.0321  -0.0033 0.1877  371 LEU C CD1 
11250 C CD2 . LEU C 371 ? 0.8236 0.7483 0.6980 0.0315  -0.0105 0.1592  371 LEU C CD2 
11251 N N   . TYR C 372 ? 0.7838 0.7815 0.6241 0.0249  -0.0207 0.2016  372 TYR C N   
11252 C CA  . TYR C 372 ? 0.7787 0.7952 0.6084 0.0098  -0.0191 0.1952  372 TYR C CA  
11253 C C   . TYR C 372 ? 0.8773 0.9019 0.6902 0.0076  -0.0185 0.2163  372 TYR C C   
11254 O O   . TYR C 372 ? 0.9017 0.9278 0.7052 -0.0047 -0.0127 0.2165  372 TYR C O   
11255 C CB  . TYR C 372 ? 0.7393 0.7888 0.5706 0.0069  -0.0257 0.1789  372 TYR C CB  
11256 C CG  . TYR C 372 ? 0.7548 0.7979 0.6010 0.0057  -0.0256 0.1578  372 TYR C CG  
11257 C CD1 . TYR C 372 ? 0.7901 0.8033 0.6450 0.0045  -0.0190 0.1517  372 TYR C CD1 
11258 C CD2 . TYR C 372 ? 0.7480 0.8143 0.5984 0.0045  -0.0327 0.1443  372 TYR C CD2 
11259 C CE1 . TYR C 372 ? 0.6838 0.6928 0.5512 0.0035  -0.0192 0.1336  372 TYR C CE1 
11260 C CE2 . TYR C 372 ? 0.7075 0.7675 0.5710 0.0031  -0.0326 0.1269  372 TYR C CE2 
11261 C CZ  . TYR C 372 ? 0.6639 0.6965 0.5358 0.0032  -0.0257 0.1220  372 TYR C CZ  
11262 O OH  . TYR C 372 ? 0.7182 0.7462 0.6021 0.0019  -0.0259 0.1059  372 TYR C OH  
11263 N N   . SER C 373 ? 0.8103 0.8426 0.6197 0.0196  -0.0241 0.2353  373 SER C N   
11264 C CA  . SER C 373 ? 0.9002 0.9383 0.6930 0.0183  -0.0237 0.2581  373 SER C CA  
11265 C C   . SER C 373 ? 0.9374 0.9349 0.7276 0.0166  -0.0156 0.2726  373 SER C C   
11266 O O   . SER C 373 ? 1.0145 1.0124 0.7916 0.0063  -0.0112 0.2845  373 SER C O   
11267 C CB  . SER C 373 ? 0.8696 0.9282 0.6603 0.0326  -0.0328 0.2761  373 SER C CB  
11268 O OG  . SER C 373 ? 0.9266 0.9556 0.7265 0.0484  -0.0317 0.2899  373 SER C OG  
11269 N N   . THR C 374 ? 0.8732 0.8352 0.6749 0.0261  -0.0137 0.2719  374 THR C N   
11270 C CA  . THR C 374 ? 0.9049 0.8220 0.7028 0.0237  -0.0069 0.2843  374 THR C CA  
11271 C C   . THR C 374 ? 1.0180 0.9248 0.8151 0.0031  0.0002  0.2721  374 THR C C   
11272 O O   . THR C 374 ? 1.1409 1.0336 0.9282 -0.0079 0.0051  0.2865  374 THR C O   
11273 C CB  . THR C 374 ? 0.9288 0.8093 0.7370 0.0396  -0.0065 0.2827  374 THR C CB  
11274 O OG1 . THR C 374 ? 1.0091 0.9049 0.8205 0.0601  -0.0127 0.2952  374 THR C OG1 
11275 C CG2 . THR C 374 ? 0.9542 0.7829 0.7553 0.0372  -0.0006 0.2960  374 THR C CG2 
11276 N N   . LEU C 375 ? 0.9309 0.8463 0.7388 -0.0027 0.0010  0.2469  375 LEU C N   
11277 C CA  . LEU C 375 ? 0.9241 0.8364 0.7333 -0.0213 0.0073  0.2355  375 LEU C CA  
11278 C C   . LEU C 375 ? 0.9625 0.9063 0.7600 -0.0333 0.0101  0.2426  375 LEU C C   
11279 O O   . LEU C 375 ? 0.9243 0.8639 0.7200 -0.0487 0.0167  0.2443  375 LEU C O   
11280 C CB  . LEU C 375 ? 0.8184 0.7414 0.6410 -0.0234 0.0066  0.2085  375 LEU C CB  
11281 C CG  . LEU C 375 ? 0.8459 0.7493 0.6803 -0.0113 0.0037  0.1973  375 LEU C CG  
11282 C CD1 . LEU C 375 ? 0.8196 0.7520 0.6633 -0.0100 -0.0001 0.1765  375 LEU C CD1 
11283 C CD2 . LEU C 375 ? 0.8946 0.7583 0.7331 -0.0179 0.0083  0.1921  375 LEU C CD2 
11284 N N   . GLU C 376 ? 0.9701 0.9481 0.7593 -0.0271 0.0051  0.2461  376 GLU C N   
11285 C CA  . GLU C 376 ? 0.9737 0.9824 0.7477 -0.0365 0.0079  0.2538  376 GLU C CA  
11286 C C   . GLU C 376 ? 1.0465 1.0377 0.8099 -0.0427 0.0126  0.2805  376 GLU C C   
11287 O O   . GLU C 376 ? 1.0276 1.0269 0.7854 -0.0576 0.0200  0.2843  376 GLU C O   
11288 C CB  . GLU C 376 ? 0.9811 1.0249 0.7457 -0.0277 -0.0001 0.2544  376 GLU C CB  
11289 C CG  . GLU C 376 ? 1.0398 1.1212 0.7944 -0.0358 0.0012  0.2396  376 GLU C CG  
11290 C CD  . GLU C 376 ? 1.0806 1.1941 0.8194 -0.0301 -0.0070 0.2458  376 GLU C CD  
11291 O OE1 . GLU C 376 ? 1.0536 1.1744 0.7985 -0.0212 -0.0162 0.2382  376 GLU C OE1 
11292 O OE2 . GLU C 376 ? 1.1877 1.3209 0.9077 -0.0354 -0.0045 0.2588  376 GLU C OE2 
11293 N N   . LYS C 377 ? 1.0568 1.0235 0.8176 -0.0312 0.0088  0.3003  377 LYS C N   
11294 C CA  . LYS C 377 ? 1.1388 1.0825 0.8890 -0.0356 0.0123  0.3281  377 LYS C CA  
11295 C C   . LYS C 377 ? 1.1586 1.0559 0.9158 -0.0457 0.0181  0.3287  377 LYS C C   
11296 O O   . LYS C 377 ? 1.2598 1.1336 1.0081 -0.0532 0.0215  0.3512  377 LYS C O   
11297 C CB  . LYS C 377 ? 1.2139 1.1478 0.9586 -0.0170 0.0055  0.3497  377 LYS C CB  
11298 C CG  . LYS C 377 ? 1.3232 1.2908 1.0499 -0.0165 0.0028  0.3712  377 LYS C CG  
11299 C CD  . LYS C 377 ? 1.3355 1.3555 1.0566 -0.0209 0.0002  0.3537  377 LYS C CD  
11300 C CE  . LYS C 377 ? 1.2565 1.3020 0.9783 -0.0047 -0.0110 0.3521  377 LYS C CE  
11301 N NZ  . LYS C 377 ? 1.0760 1.1669 0.7909 -0.0100 -0.0146 0.3326  377 LYS C NZ  
11302 N N   . GLU C 378 ? 1.0793 0.9623 0.8510 -0.0473 0.0188  0.3053  378 GLU C N   
11303 C CA  . GLU C 378 ? 1.1169 0.9573 0.8944 -0.0587 0.0232  0.3029  378 GLU C CA  
11304 C C   . GLU C 378 ? 1.1107 0.9719 0.8904 -0.0813 0.0297  0.2964  378 GLU C C   
11305 O O   . GLU C 378 ? 1.1334 1.0151 0.9240 -0.0854 0.0307  0.2735  378 GLU C O   
11306 C CB  . GLU C 378 ? 1.1155 0.9329 0.9062 -0.0493 0.0205  0.2815  378 GLU C CB  
11307 C CG  . GLU C 378 ? 1.2081 0.9789 0.9966 -0.0330 0.0180  0.2916  378 GLU C CG  
11308 C CD  . GLU C 378 ? 1.2768 1.0130 1.0521 -0.0373 0.0202  0.3193  378 GLU C CD  
11309 O OE1 . GLU C 378 ? 1.3556 1.0901 1.1235 -0.0213 0.0172  0.3388  378 GLU C OE1 
11310 O OE2 . GLU C 378 ? 1.2490 0.9600 1.0219 -0.0569 0.0245  0.3226  378 GLU C OE2 
11311 N N   . GLU C 379 ? 1.1104 0.9669 0.8807 -0.0956 0.0344  0.3178  379 GLU C N   
11312 C CA  . GLU C 379 ? 1.1701 1.0546 0.9424 -0.1165 0.0416  0.3160  379 GLU C CA  
11313 C C   . GLU C 379 ? 1.1054 0.9669 0.8911 -0.1328 0.0442  0.3038  379 GLU C C   
11314 O O   . GLU C 379 ? 1.0660 0.9581 0.8591 -0.1473 0.0495  0.2953  379 GLU C O   
11315 C CB  . GLU C 379 ? 1.2837 1.1734 1.0406 -0.1259 0.0455  0.3461  379 GLU C CB  
11316 C CG  . GLU C 379 ? 1.3389 1.1760 1.0878 -0.1210 0.0422  0.3689  379 GLU C CG  
11317 C CD  . GLU C 379 ? 1.4252 1.2246 1.1757 -0.1427 0.0462  0.3799  379 GLU C CD  
11318 O OE1 . GLU C 379 ? 1.4484 1.2734 1.1984 -0.1633 0.0527  0.3879  379 GLU C OE1 
11319 O OE2 . GLU C 379 ? 1.4412 1.1859 1.1931 -0.1397 0.0430  0.3799  379 GLU C OE2 
11320 N N   . TRP C 380 ? 1.1212 0.9315 0.9098 -0.1301 0.0406  0.3019  380 TRP C N   
11321 C CA  . TRP C 380 ? 1.1029 0.8913 0.9029 -0.1450 0.0414  0.2876  380 TRP C CA  
11322 C C   . TRP C 380 ? 1.0977 0.8984 0.9109 -0.1355 0.0384  0.2583  380 TRP C C   
11323 O O   . TRP C 380 ? 1.0977 0.8894 0.9212 -0.1478 0.0386  0.2445  380 TRP C O   
11324 C CB  . TRP C 380 ? 1.1672 0.8904 0.9608 -0.1482 0.0390  0.2977  380 TRP C CB  
11325 C CG  . TRP C 380 ? 1.1663 0.8568 0.9560 -0.1230 0.0339  0.2935  380 TRP C CG  
11326 C CD1 . TRP C 380 ? 1.1292 0.8097 0.9082 -0.1045 0.0319  0.3113  380 TRP C CD1 
11327 C CD2 . TRP C 380 ? 1.2135 0.8811 1.0103 -0.1125 0.0306  0.2709  380 TRP C CD2 
11328 N NE1 . TRP C 380 ? 1.2807 0.9348 1.0612 -0.0827 0.0280  0.3013  380 TRP C NE1 
11329 C CE2 . TRP C 380 ? 1.1812 0.8267 0.9718 -0.0873 0.0275  0.2763  380 TRP C CE2 
11330 C CE3 . TRP C 380 ? 1.2133 0.8791 1.0208 -0.1217 0.0299  0.2475  380 TRP C CE3 
11331 C CZ2 . TRP C 380 ? 1.0478 0.6706 0.8424 -0.0709 0.0248  0.2589  380 TRP C CZ2 
11332 C CZ3 . TRP C 380 ? 1.1825 0.8239 0.9924 -0.1061 0.0266  0.2302  380 TRP C CZ3 
11333 C CH2 . TRP C 380 ? 1.1217 0.7421 0.9251 -0.0810 0.0246  0.2359  380 TRP C CH2 
11334 N N   . ILE C 381 ? 1.0409 0.8624 0.8542 -0.1151 0.0350  0.2495  381 ILE C N   
11335 C CA  . ILE C 381 ? 0.9985 0.8369 0.8239 -0.1065 0.0323  0.2236  381 ILE C CA  
11336 C C   . ILE C 381 ? 0.9497 0.8420 0.7775 -0.1078 0.0349  0.2159  381 ILE C C   
11337 O O   . ILE C 381 ? 0.9265 0.8424 0.7442 -0.1006 0.0347  0.2255  381 ILE C O   
11338 C CB  . ILE C 381 ? 0.9689 0.7917 0.7936 -0.0837 0.0265  0.2184  381 ILE C CB  
11339 C CG1 . ILE C 381 ? 1.0111 0.7784 0.8328 -0.0802 0.0251  0.2225  381 ILE C CG1 
11340 C CG2 . ILE C 381 ? 0.8452 0.6905 0.6819 -0.0761 0.0237  0.1936  381 ILE C CG2 
11341 C CD1 . ILE C 381 ? 0.9857 0.7381 0.8057 -0.0560 0.0210  0.2229  381 ILE C CD1 
11342 N N   . GLU C 382 ? 0.8388 0.7504 0.6790 -0.1165 0.0371  0.1986  382 GLU C N   
11343 C CA  . GLU C 382 ? 0.8121 0.7713 0.6549 -0.1161 0.0402  0.1882  382 GLU C CA  
11344 C C   . GLU C 382 ? 0.7930 0.7594 0.6464 -0.1050 0.0358  0.1643  382 GLU C C   
11345 O O   . GLU C 382 ? 0.8762 0.8336 0.7422 -0.1104 0.0353  0.1517  382 GLU C O   
11346 C CB  . GLU C 382 ? 0.9159 0.8966 0.7652 -0.1349 0.0476  0.1906  382 GLU C CB  
11347 C CG  . GLU C 382 ? 1.0835 1.1126 0.9355 -0.1324 0.0523  0.1787  382 GLU C CG  
11348 C CD  . GLU C 382 ? 1.0561 1.1119 0.9159 -0.1493 0.0608  0.1832  382 GLU C CD  
11349 O OE1 . GLU C 382 ? 1.1887 1.2267 1.0510 -0.1657 0.0624  0.1978  382 GLU C OE1 
11350 O OE2 . GLU C 382 ? 1.0923 1.1871 0.9558 -0.1462 0.0658  0.1724  382 GLU C OE2 
11351 N N   . THR C 383 ? 0.9040 0.8864 0.7519 -0.0907 0.0320  0.1588  383 THR C N   
11352 C CA  . THR C 383 ? 0.8729 0.8657 0.7299 -0.0818 0.0280  0.1373  383 THR C CA  
11353 C C   . THR C 383 ? 0.8508 0.8754 0.7138 -0.0877 0.0330  0.1245  383 THR C C   
11354 O O   . THR C 383 ? 0.8515 0.9014 0.7067 -0.0926 0.0387  0.1308  383 THR C O   
11355 C CB  . THR C 383 ? 0.8601 0.8625 0.7094 -0.0673 0.0218  0.1359  383 THR C CB  
11356 O OG1 . THR C 383 ? 0.8851 0.9128 0.7196 -0.0680 0.0238  0.1456  383 THR C OG1 
11357 C CG2 . THR C 383 ? 0.7443 0.7171 0.5924 -0.0577 0.0167  0.1458  383 THR C CG2 
11358 N N   . LEU C 384 ? 0.8883 0.9124 0.7648 -0.0863 0.0312  0.1071  384 LEU C N   
11359 C CA  . LEU C 384 ? 0.8277 0.8782 0.7134 -0.0908 0.0361  0.0954  384 LEU C CA  
11360 C C   . LEU C 384 ? 0.8512 0.9091 0.7428 -0.0800 0.0317  0.0758  384 LEU C C   
11361 O O   . LEU C 384 ? 0.8282 0.8661 0.7245 -0.0741 0.0253  0.0699  384 LEU C O   
11362 C CB  . LEU C 384 ? 0.7302 0.7719 0.6293 -0.1041 0.0386  0.0967  384 LEU C CB  
11363 C CG  . LEU C 384 ? 0.8224 0.8644 0.7187 -0.1198 0.0444  0.1149  384 LEU C CG  
11364 C CD1 . LEU C 384 ? 0.8871 0.9380 0.7995 -0.1337 0.0472  0.1115  384 LEU C CD1 
11365 C CD2 . LEU C 384 ? 0.9048 0.9772 0.7893 -0.1198 0.0511  0.1245  384 LEU C CD2 
11366 N N   . THR C 385 ? 0.7830 0.8689 0.6735 -0.0770 0.0356  0.0662  385 THR C N   
11367 C CA  . THR C 385 ? 0.7035 0.7936 0.6015 -0.0686 0.0322  0.0476  385 THR C CA  
11368 C C   . THR C 385 ? 0.6734 0.7589 0.5899 -0.0733 0.0325  0.0417  385 THR C C   
11369 O O   . THR C 385 ? 0.7875 0.8719 0.7105 -0.0844 0.0361  0.0505  385 THR C O   
11370 C CB  . THR C 385 ? 0.7045 0.8219 0.5950 -0.0630 0.0368  0.0379  385 THR C CB  
11371 O OG1 . THR C 385 ? 0.8265 0.9640 0.7285 -0.0670 0.0447  0.0352  385 THR C OG1 
11372 C CG2 . THR C 385 ? 0.6829 0.8123 0.5536 -0.0635 0.0396  0.0482  385 THR C CG2 
11373 N N   . LEU C 386 ? 0.7406 0.8235 0.6652 -0.0659 0.0281  0.0273  386 LEU C N   
11374 C CA  . LEU C 386 ? 0.7556 0.8377 0.6971 -0.0694 0.0276  0.0214  386 LEU C CA  
11375 C C   . LEU C 386 ? 0.7503 0.8608 0.7001 -0.0746 0.0356  0.0222  386 LEU C C   
11376 O O   . LEU C 386 ? 0.7498 0.8626 0.7110 -0.0852 0.0370  0.0274  386 LEU C O   
11377 C CB  . LEU C 386 ? 0.6842 0.7611 0.6315 -0.0596 0.0218  0.0071  386 LEU C CB  
11378 C CG  . LEU C 386 ? 0.6329 0.6864 0.5757 -0.0548 0.0139  0.0063  386 LEU C CG  
11379 C CD1 . LEU C 386 ? 0.6278 0.6767 0.5804 -0.0491 0.0088  -0.0053 386 LEU C CD1 
11380 C CD2 . LEU C 386 ? 0.6318 0.6645 0.5740 -0.0611 0.0126  0.0168  386 LEU C CD2 
11381 N N   . GLU C 387 ? 0.7288 0.8621 0.6724 -0.0674 0.0410  0.0171  387 GLU C N   
11382 C CA  . GLU C 387 ? 0.7449 0.9103 0.6966 -0.0697 0.0501  0.0180  387 GLU C CA  
11383 C C   . GLU C 387 ? 0.7613 0.9354 0.7121 -0.0845 0.0557  0.0353  387 GLU C C   
11384 O O   . GLU C 387 ? 0.8544 1.0471 0.8198 -0.0937 0.0600  0.0402  387 GLU C O   
11385 C CB  . GLU C 387 ? 0.8139 0.9987 0.7545 -0.0573 0.0555  0.0083  387 GLU C CB  
11386 C CG  . GLU C 387 ? 0.9510 1.1722 0.9001 -0.0558 0.0662  0.0080  387 GLU C CG  
11387 C CD  . GLU C 387 ? 1.1564 1.3993 1.0892 -0.0567 0.0754  0.0150  387 GLU C CD  
11388 O OE1 . GLU C 387 ? 1.1275 1.3572 1.0399 -0.0546 0.0724  0.0157  387 GLU C OE1 
11389 O OE2 . GLU C 387 ? 1.2084 1.4842 1.1491 -0.0597 0.0854  0.0205  387 GLU C OE2 
11390 N N   . GLU C 388 ? 0.7423 0.9038 0.6766 -0.0875 0.0552  0.0458  388 GLU C N   
11391 C CA  . GLU C 388 ? 0.7796 0.9448 0.7112 -0.1020 0.0601  0.0642  388 GLU C CA  
11392 C C   . GLU C 388 ? 0.7332 0.8769 0.6769 -0.1157 0.0558  0.0708  388 GLU C C   
11393 O O   . GLU C 388 ? 0.8604 1.0165 0.8120 -0.1306 0.0604  0.0815  388 GLU C O   
11394 C CB  . GLU C 388 ? 0.8121 0.9643 0.7229 -0.1004 0.0589  0.0746  388 GLU C CB  
11395 C CG  . GLU C 388 ? 0.7853 0.9632 0.6807 -0.0911 0.0642  0.0707  388 GLU C CG  
11396 C CD  . GLU C 388 ? 0.8264 0.9939 0.7008 -0.0895 0.0614  0.0816  388 GLU C CD  
11397 O OE1 . GLU C 388 ? 0.8432 0.9824 0.7164 -0.0936 0.0556  0.0924  388 GLU C OE1 
11398 O OE2 . GLU C 388 ? 0.8533 1.0415 0.7118 -0.0835 0.0651  0.0792  388 GLU C OE2 
11399 N N   . ALA C 389 ? 0.7175 0.8294 0.6621 -0.1118 0.0471  0.0643  389 ALA C N   
11400 C CA  . ALA C 389 ? 0.8204 0.9106 0.7746 -0.1235 0.0427  0.0666  389 ALA C CA  
11401 C C   . ALA C 389 ? 0.8496 0.9645 0.8230 -0.1296 0.0441  0.0603  389 ALA C C   
11402 O O   . ALA C 389 ? 0.8615 0.9728 0.8432 -0.1457 0.0431  0.0664  389 ALA C O   
11403 C CB  . ALA C 389 ? 0.7059 0.7624 0.6569 -0.1151 0.0341  0.0586  389 ALA C CB  
11404 N N   . MET C 390 ? 0.8053 0.9448 0.7856 -0.1170 0.0458  0.0482  390 MET C N   
11405 C CA  . MET C 390 ? 0.8505 1.0170 0.8503 -0.1199 0.0472  0.0431  390 MET C CA  
11406 C C   . MET C 390 ? 0.8693 1.0725 0.8770 -0.1309 0.0562  0.0541  390 MET C C   
11407 O O   . MET C 390 ? 0.7680 0.9932 0.7938 -0.1402 0.0566  0.0556  390 MET C O   
11408 C CB  . MET C 390 ? 0.7821 0.9614 0.7862 -0.1013 0.0468  0.0280  390 MET C CB  
11409 C CG  . MET C 390 ? 0.8168 0.9725 0.8247 -0.0949 0.0374  0.0173  390 MET C CG  
11410 S SD  . MET C 390 ? 0.9394 1.1039 0.9681 -0.1061 0.0326  0.0167  390 MET C SD  
11411 C CE  . MET C 390 ? 0.7793 0.9087 0.7996 -0.1249 0.0276  0.0261  390 MET C CE  
11412 N N   . ARG C 391 ? 0.8104 1.0239 0.8052 -0.1301 0.0635  0.0624  391 ARG C N   
11413 C CA  . ARG C 391 ? 0.7829 1.0363 0.7840 -0.1386 0.0738  0.0732  391 ARG C CA  
11414 C C   . ARG C 391 ? 0.8767 1.1201 0.8747 -0.1608 0.0746  0.0925  391 ARG C C   
11415 O O   . ARG C 391 ? 0.7933 1.0704 0.8003 -0.1732 0.0823  0.1041  391 ARG C O   
11416 C CB  . ARG C 391 ? 0.8646 1.1391 0.8514 -0.1237 0.0823  0.0702  391 ARG C CB  
11417 C CG  . ARG C 391 ? 0.9240 1.2094 0.9127 -0.1021 0.0829  0.0510  391 ARG C CG  
11418 C CD  . ARG C 391 ? 0.9964 1.2919 1.0087 -0.1014 0.0794  0.0437  391 ARG C CD  
11419 N NE  . ARG C 391 ? 1.0284 1.3554 1.0488 -0.0843 0.0859  0.0325  391 ARG C NE  
11420 C CZ  . ARG C 391 ? 1.1117 1.4277 1.1232 -0.0649 0.0843  0.0167  391 ARG C CZ  
11421 N NH1 . ARG C 391 ? 0.9789 1.2565 0.9748 -0.0608 0.0760  0.0104  391 ARG C NH1 
11422 N NH2 . ARG C 391 ? 1.0900 1.4342 1.1082 -0.0491 0.0916  0.0075  391 ARG C NH2 
11423 N N   . LYS C 392 ? 0.8924 1.0905 0.8785 -0.1660 0.0671  0.0965  392 LYS C N   
11424 C CA  . LYS C 392 ? 0.9826 1.1624 0.9628 -0.1860 0.0673  0.1149  392 LYS C CA  
11425 C C   . LYS C 392 ? 1.0289 1.2135 1.0267 -0.2072 0.0646  0.1192  392 LYS C C   
11426 O O   . LYS C 392 ? 1.0342 1.1967 1.0382 -0.2089 0.0560  0.1092  392 LYS C O   
11427 C CB  . LYS C 392 ? 0.9306 1.0584 0.8936 -0.1820 0.0599  0.1164  392 LYS C CB  
11428 C CG  . LYS C 392 ? 1.0096 1.1177 0.9592 -0.1950 0.0620  0.1370  392 LYS C CG  
11429 C CD  . LYS C 392 ? 0.9496 1.0857 0.8875 -0.1886 0.0705  0.1466  392 LYS C CD  
11430 C CE  . LYS C 392 ? 0.9636 1.0727 0.8814 -0.1737 0.0668  0.1479  392 LYS C CE  
11431 N NZ  . LYS C 392 ? 1.0047 1.1457 0.9120 -0.1593 0.0722  0.1445  392 LYS C NZ  
11432 N N   . GLU C 393 ? 1.0604 1.2764 1.0661 -0.2243 0.0717  0.1342  393 GLU C N   
11433 C CA  . GLU C 393 ? 1.0320 1.2557 1.0545 -0.2486 0.0686  0.1408  393 GLU C CA  
11434 C C   . GLU C 393 ? 1.0040 1.1793 1.0153 -0.2696 0.0626  0.1532  393 GLU C C   
11435 O O   . GLU C 393 ? 1.0422 1.2116 1.0640 -0.2910 0.0571  0.1556  393 GLU C O   
11436 C CB  . GLU C 393 ? 1.0194 1.3029 1.0578 -0.2589 0.0791  0.1526  393 GLU C CB  
11437 C CG  . GLU C 393 ? 1.0446 1.3755 1.1062 -0.2495 0.0810  0.1407  393 GLU C CG  
11438 C CD  . GLU C 393 ? 1.1685 1.5525 1.2339 -0.2345 0.0945  0.1418  393 GLU C CD  
11439 O OE1 . GLU C 393 ? 1.2296 1.6217 1.2820 -0.2377 0.1029  0.1550  393 GLU C OE1 
11440 O OE2 . GLU C 393 ? 1.2276 1.6442 1.3074 -0.2184 0.0969  0.1294  393 GLU C OE2 
11441 N N   . ASP C 394 ? 1.0491 1.1886 1.0389 -0.2640 0.0631  0.1608  394 ASP C N   
11442 C CA  . ASP C 394 ? 0.9865 1.0737 0.9633 -0.2804 0.0577  0.1725  394 ASP C CA  
11443 C C   . ASP C 394 ? 0.9808 1.0204 0.9543 -0.2787 0.0468  0.1580  394 ASP C C   
11444 O O   . ASP C 394 ? 0.9892 0.9825 0.9527 -0.2933 0.0417  0.1648  394 ASP C O   
11445 C CB  . ASP C 394 ? 1.0092 1.0722 0.9642 -0.2702 0.0608  0.1845  394 ASP C CB  
11446 C CG  . ASP C 394 ? 1.0584 1.1685 1.0113 -0.2587 0.0710  0.1899  394 ASP C CG  
11447 O OD1 . ASP C 394 ? 1.1561 1.3174 1.1247 -0.2606 0.0772  0.1868  394 ASP C OD1 
11448 O OD2 . ASP C 394 ? 1.0285 1.1251 0.9632 -0.2472 0.0727  0.1973  394 ASP C OD2 
11449 N N   . VAL C 395 ? 0.9792 1.0276 0.9592 -0.2609 0.0433  0.1384  395 VAL C N   
11450 C CA  . VAL C 395 ? 0.9647 0.9710 0.9393 -0.2555 0.0340  0.1240  395 VAL C CA  
11451 C C   . VAL C 395 ? 0.9294 0.9339 0.9153 -0.2774 0.0275  0.1199  395 VAL C C   
11452 O O   . VAL C 395 ? 0.8571 0.9079 0.8624 -0.2866 0.0289  0.1196  395 VAL C O   
11453 C CB  . VAL C 395 ? 0.9471 0.9657 0.9243 -0.2293 0.0328  0.1064  395 VAL C CB  
11454 C CG1 . VAL C 395 ? 0.9598 0.9310 0.9260 -0.2203 0.0250  0.0950  395 VAL C CG1 
11455 C CG2 . VAL C 395 ? 0.9857 1.0225 0.9556 -0.2113 0.0397  0.1102  395 VAL C CG2 
11456 N N   . LYS C 396 ? 0.9679 0.9195 0.9412 -0.2850 0.0199  0.1160  396 LYS C N   
11457 C CA  . LYS C 396 ? 0.8872 0.8318 0.8673 -0.3035 0.0116  0.1076  396 LYS C CA  
11458 C C   . LYS C 396 ? 0.9059 0.8724 0.8962 -0.2872 0.0078  0.0889  396 LYS C C   
11459 O O   . LYS C 396 ? 0.8063 0.7585 0.7885 -0.2632 0.0078  0.0791  396 LYS C O   
11460 C CB  . LYS C 396 ? 0.8602 0.7373 0.8197 -0.3132 0.0050  0.1061  396 LYS C CB  
11461 C CG  . LYS C 396 ? 1.1144 0.9806 1.0770 -0.3455 -0.0023 0.1071  396 LYS C CG  
11462 C CD  . LYS C 396 ? 1.0952 0.8928 1.0356 -0.3494 -0.0102 0.0968  396 LYS C CD  
11463 C CE  . LYS C 396 ? 1.0802 0.8797 1.0252 -0.3678 -0.0204 0.0832  396 LYS C CE  
11464 N NZ  . LYS C 396 ? 1.0835 0.8199 1.0046 -0.3633 -0.0270 0.0680  396 LYS C NZ  
11465 N N   . THR C 397 ? 0.8735 0.8765 0.8823 -0.3006 0.0041  0.0853  397 THR C N   
11466 C CA  . THR C 397 ? 0.7711 0.8034 0.7927 -0.2858 0.0010  0.0709  397 THR C CA  
11467 C C   . THR C 397 ? 0.7436 0.7705 0.7693 -0.3033 -0.0096 0.0624  397 THR C C   
11468 O O   . THR C 397 ? 0.7672 0.8005 0.7988 -0.3306 -0.0130 0.0701  397 THR C O   
11469 C CB  . THR C 397 ? 0.8037 0.8999 0.8470 -0.2787 0.0083  0.0754  397 THR C CB  
11470 O OG1 . THR C 397 ? 0.7906 0.8945 0.8288 -0.2734 0.0183  0.0875  397 THR C OG1 
11471 C CG2 . THR C 397 ? 0.8329 0.9470 0.8827 -0.2530 0.0077  0.0613  397 THR C CG2 
11472 N N   . GLU C 398 ? 0.7572 0.7739 0.7793 -0.2885 -0.0152 0.0471  398 GLU C N   
11473 C CA  . GLU C 398 ? 0.7432 0.7538 0.7657 -0.3017 -0.0259 0.0370  398 GLU C CA  
11474 C C   . GLU C 398 ? 0.7682 0.8145 0.8045 -0.2841 -0.0282 0.0271  398 GLU C C   
11475 O O   . GLU C 398 ? 0.7033 0.7521 0.7385 -0.2587 -0.0235 0.0228  398 GLU C O   
11476 C CB  . GLU C 398 ? 0.8674 0.8127 0.8629 -0.3029 -0.0313 0.0276  398 GLU C CB  
11477 C CG  . GLU C 398 ? 0.9913 0.9280 0.9823 -0.3115 -0.0424 0.0137  398 GLU C CG  
11478 C CD  . GLU C 398 ? 1.1864 1.0701 1.1559 -0.3340 -0.0491 0.0102  398 GLU C CD  
11479 O OE1 . GLU C 398 ? 1.1626 0.9926 1.1093 -0.3247 -0.0466 0.0070  398 GLU C OE1 
11480 O OE2 . GLU C 398 ? 1.2147 1.1106 1.1901 -0.3611 -0.0570 0.0109  398 GLU C OE2 
11481 N N   . VAL C 399 ? 0.7884 0.8625 0.8378 -0.2984 -0.0362 0.0243  399 VAL C N   
11482 C CA  . VAL C 399 ? 0.8167 0.9235 0.8792 -0.2834 -0.0399 0.0163  399 VAL C CA  
11483 C C   . VAL C 399 ? 0.8085 0.8795 0.8532 -0.2824 -0.0492 0.0025  399 VAL C C   
11484 O O   . VAL C 399 ? 0.8759 0.9154 0.9061 -0.3029 -0.0561 -0.0009 399 VAL C O   
11485 C CB  . VAL C 399 ? 0.7500 0.9163 0.8396 -0.2971 -0.0430 0.0233  399 VAL C CB  
11486 C CG1 . VAL C 399 ? 0.7554 0.9442 0.8537 -0.2892 -0.0515 0.0146  399 VAL C CG1 
11487 C CG2 . VAL C 399 ? 0.8044 1.0147 0.9130 -0.2857 -0.0315 0.0337  399 VAL C CG2 
11488 N N   . ILE C 400 ? 0.7667 0.8408 0.8108 -0.2586 -0.0492 -0.0055 400 ILE C N   
11489 C CA  . ILE C 400 ? 0.8687 0.9174 0.8974 -0.2549 -0.0571 -0.0180 400 ILE C CA  
11490 C C   . ILE C 400 ? 0.8000 0.8904 0.8454 -0.2440 -0.0615 -0.0204 400 ILE C C   
11491 O O   . ILE C 400 ? 0.8083 0.9334 0.8721 -0.2290 -0.0560 -0.0151 400 ILE C O   
11492 C CB  . ILE C 400 ? 0.9218 0.9249 0.9290 -0.2357 -0.0524 -0.0244 400 ILE C CB  
11493 C CG1 . ILE C 400 ? 0.8279 0.8493 0.8447 -0.2102 -0.0449 -0.0218 400 ILE C CG1 
11494 C CG2 . ILE C 400 ? 0.8877 0.8467 0.8774 -0.2445 -0.0484 -0.0211 400 ILE C CG2 
11495 C CD1 . ILE C 400 ? 0.7948 0.7917 0.7979 -0.1911 -0.0451 -0.0304 400 ILE C CD1 
11496 N N   . GLU C 401 ? 0.7893 0.8746 0.8268 -0.2508 -0.0715 -0.0287 401 GLU C N   
11497 C CA  . GLU C 401 ? 0.7517 0.8764 0.8042 -0.2426 -0.0773 -0.0294 401 GLU C CA  
11498 C C   . GLU C 401 ? 0.7161 0.8210 0.7542 -0.2243 -0.0794 -0.0384 401 GLU C C   
11499 O O   . GLU C 401 ? 0.6110 0.7452 0.6598 -0.2159 -0.0843 -0.0380 401 GLU C O   
11500 C CB  . GLU C 401 ? 0.6399 0.7898 0.6994 -0.2675 -0.0889 -0.0288 401 GLU C CB  
11501 C CG  . GLU C 401 ? 0.7406 0.9055 0.8113 -0.2919 -0.0882 -0.0198 401 GLU C CG  
11502 C CD  . GLU C 401 ? 0.7211 0.9483 0.8251 -0.2886 -0.0845 -0.0074 401 GLU C CD  
11503 O OE1 . GLU C 401 ? 0.6672 0.9267 0.7860 -0.2691 -0.0846 -0.0064 401 GLU C OE1 
11504 O OE2 . GLU C 401 ? 0.6403 0.8843 0.7555 -0.3056 -0.0814 0.0020  401 GLU C OE2 
11505 N N   . SER C 402 ? 0.7897 0.8482 0.8050 -0.2169 -0.0754 -0.0450 402 SER C N   
11506 C CA  . SER C 402 ? 0.7715 0.8127 0.7720 -0.2023 -0.0774 -0.0531 402 SER C CA  
11507 C C   . SER C 402 ? 0.7013 0.7008 0.6844 -0.1891 -0.0692 -0.0563 402 SER C C   
11508 O O   . SER C 402 ? 0.8285 0.8036 0.8046 -0.1954 -0.0645 -0.0543 402 SER C O   
11509 C CB  . SER C 402 ? 0.6520 0.6840 0.6366 -0.2177 -0.0880 -0.0620 402 SER C CB  
11510 O OG  . SER C 402 ? 0.8336 0.8324 0.7944 -0.2070 -0.0874 -0.0715 402 SER C OG  
11511 N N   . VAL C 403 ? 0.6160 0.6093 0.5927 -0.1707 -0.0678 -0.0598 403 VAL C N   
11512 C CA  . VAL C 403 ? 0.7189 0.6771 0.6797 -0.1570 -0.0609 -0.0627 403 VAL C CA  
11513 C C   . VAL C 403 ? 0.7151 0.6652 0.6624 -0.1469 -0.0634 -0.0698 403 VAL C C   
11514 O O   . VAL C 403 ? 0.7134 0.6903 0.6705 -0.1404 -0.0670 -0.0679 403 VAL C O   
11515 C CB  . VAL C 403 ? 0.7145 0.6814 0.6877 -0.1413 -0.0530 -0.0552 403 VAL C CB  
11516 C CG1 . VAL C 403 ? 0.7155 0.6771 0.6926 -0.1494 -0.0481 -0.0491 403 VAL C CG1 
11517 C CG2 . VAL C 403 ? 0.7031 0.7081 0.6965 -0.1328 -0.0548 -0.0509 403 VAL C CG2 
11518 N N   . LYS C 404 ? 0.7384 0.6515 0.6629 -0.1444 -0.0609 -0.0770 404 LYS C N   
11519 C CA  . LYS C 404 ? 0.7866 0.6920 0.6969 -0.1323 -0.0608 -0.0831 404 LYS C CA  
11520 C C   . LYS C 404 ? 0.7747 0.6860 0.6932 -0.1121 -0.0540 -0.0770 404 LYS C C   
11521 O O   . LYS C 404 ? 0.8271 0.7223 0.7453 -0.1054 -0.0473 -0.0736 404 LYS C O   
11522 C CB  . LYS C 404 ? 0.7845 0.6486 0.6668 -0.1350 -0.0595 -0.0939 404 LYS C CB  
11523 C CG  . LYS C 404 ? 0.8274 0.6900 0.6918 -0.1327 -0.0633 -0.1033 404 LYS C CG  
11524 C CD  . LYS C 404 ? 0.8188 0.6447 0.6555 -0.1448 -0.0660 -0.1164 404 LYS C CD  
11525 C CE  . LYS C 404 ? 0.9572 0.7912 0.7973 -0.1703 -0.0759 -0.1182 404 LYS C CE  
11526 N NZ  . LYS C 404 ? 1.0796 0.9396 0.9162 -0.1788 -0.0859 -0.1228 404 LYS C NZ  
11527 N N   . ALA C 405 ? 0.7372 0.6716 0.6626 -0.1036 -0.0562 -0.0747 405 ALA C N   
11528 C CA  . ALA C 405 ? 0.6623 0.6055 0.5979 -0.0877 -0.0514 -0.0679 405 ALA C CA  
11529 C C   . ALA C 405 ? 0.8119 0.7307 0.7331 -0.0761 -0.0445 -0.0701 405 ALA C C   
11530 O O   . ALA C 405 ? 0.9011 0.8020 0.8031 -0.0754 -0.0438 -0.0776 405 ALA C O   
11531 C CB  . ALA C 405 ? 0.6820 0.6507 0.6256 -0.0823 -0.0558 -0.0645 405 ALA C CB  
11532 N N   . GLY C 406 ? 0.7653 0.6848 0.6955 -0.0665 -0.0394 -0.0636 406 GLY C N   
11533 C CA  . GLY C 406 ? 0.7315 0.6346 0.6520 -0.0541 -0.0331 -0.0633 406 GLY C CA  
11534 C C   . GLY C 406 ? 0.7666 0.6760 0.6995 -0.0464 -0.0295 -0.0551 406 GLY C C   
11535 O O   . GLY C 406 ? 0.7316 0.6579 0.6794 -0.0495 -0.0317 -0.0507 406 GLY C O   
11536 N N   . THR C 407 ? 0.7569 0.6531 0.6828 -0.0357 -0.0240 -0.0534 407 THR C N   
11537 C CA  . THR C 407 ? 0.7513 0.6523 0.6858 -0.0279 -0.0209 -0.0455 407 THR C CA  
11538 C C   . THR C 407 ? 0.8412 0.7171 0.7656 -0.0247 -0.0162 -0.0446 407 THR C C   
11539 O O   . THR C 407 ? 0.8471 0.6992 0.7575 -0.0285 -0.0152 -0.0507 407 THR C O   
11540 C CB  . THR C 407 ? 0.8146 0.7297 0.7528 -0.0165 -0.0194 -0.0413 407 THR C CB  
11541 O OG1 . THR C 407 ? 0.8161 0.7171 0.7404 -0.0072 -0.0144 -0.0442 407 THR C OG1 
11542 C CG2 . THR C 407 ? 0.6982 0.6333 0.6434 -0.0196 -0.0241 -0.0414 407 THR C CG2 
11543 N N   . TRP C 408 ? 0.8159 0.6958 0.7464 -0.0178 -0.0137 -0.0368 408 TRP C N   
11544 C CA  . TRP C 408 ? 0.7872 0.6442 0.7082 -0.0113 -0.0090 -0.0335 408 TRP C CA  
11545 C C   . TRP C 408 ? 0.8512 0.7002 0.7636 0.0038  -0.0044 -0.0341 408 TRP C C   
11546 O O   . TRP C 408 ? 0.8621 0.6953 0.7686 0.0136  0.0000  -0.0296 408 TRP C O   
11547 C CB  . TRP C 408 ? 0.7702 0.6364 0.6998 -0.0096 -0.0086 -0.0239 408 TRP C CB  
11548 C CG  . TRP C 408 ? 0.8456 0.7379 0.7867 -0.0024 -0.0100 -0.0184 408 TRP C CG  
11549 C CD1 . TRP C 408 ? 0.8734 0.7810 0.8188 0.0035  -0.0107 -0.0190 408 TRP C CD1 
11550 C CD2 . TRP C 408 ? 0.7993 0.7054 0.7479 -0.0021 -0.0113 -0.0109 408 TRP C CD2 
11551 N NE1 . TRP C 408 ? 0.7912 0.7201 0.7474 0.0062  -0.0129 -0.0124 408 TRP C NE1 
11552 C CE2 . TRP C 408 ? 0.7548 0.6827 0.7122 0.0030  -0.0135 -0.0082 408 TRP C CE2 
11553 C CE3 . TRP C 408 ? 0.6995 0.6021 0.6472 -0.0066 -0.0108 -0.0061 408 TRP C CE3 
11554 C CZ2 . TRP C 408 ? 0.8496 0.7939 0.8138 0.0031  -0.0163 -0.0023 408 TRP C CZ2 
11555 C CZ3 . TRP C 408 ? 0.6866 0.6071 0.6402 -0.0050 -0.0128 -0.0002 408 TRP C CZ3 
11556 C CH2 . TRP C 408 ? 0.8111 0.7513 0.7725 -0.0004 -0.0159 0.0009  408 TRP C CH2 
11557 N N   . PHE C 409 ? 0.7906 0.6513 0.7021 0.0068  -0.0048 -0.0388 409 PHE C N   
11558 C CA  . PHE C 409 ? 0.8760 0.7365 0.7806 0.0220  0.0005  -0.0392 409 PHE C CA  
11559 C C   . PHE C 409 ? 0.9116 0.7523 0.7978 0.0203  0.0017  -0.0512 409 PHE C C   
11560 O O   . PHE C 409 ? 0.9125 0.7680 0.7984 0.0161  -0.0009 -0.0554 409 PHE C O   
11561 C CB  . PHE C 409 ? 0.8863 0.7810 0.8048 0.0260  -0.0007 -0.0331 409 PHE C CB  
11562 C CG  . PHE C 409 ? 0.9062 0.8106 0.8259 0.0427  0.0051  -0.0268 409 PHE C CG  
11563 C CD1 . PHE C 409 ? 0.9649 0.8785 0.8945 0.0492  0.0058  -0.0165 409 PHE C CD1 
11564 C CD2 . PHE C 409 ? 0.9777 0.8847 0.8883 0.0524  0.0102  -0.0307 409 PHE C CD2 
11565 C CE1 . PHE C 409 ? 1.0303 0.9576 0.9632 0.0650  0.0110  -0.0094 409 PHE C CE1 
11566 C CE2 . PHE C 409 ? 0.9192 0.8397 0.8326 0.0691  0.0166  -0.0240 409 PHE C CE2 
11567 C CZ  . PHE C 409 ? 0.9110 0.8426 0.8367 0.0754  0.0168  -0.0129 409 PHE C CZ  
11568 N N   . ASP C 410 ? 0.8847 0.6906 0.7545 0.0230  0.0051  -0.0565 410 ASP C N   
11569 C CA  . ASP C 410 ? 0.8959 0.6754 0.7439 0.0206  0.0060  -0.0697 410 ASP C CA  
11570 C C   . ASP C 410 ? 0.8597 0.6404 0.7066 -0.0002 -0.0020 -0.0766 410 ASP C C   
11571 O O   . ASP C 410 ? 0.9832 0.7473 0.8121 -0.0053 -0.0033 -0.0883 410 ASP C O   
11572 C CB  . ASP C 410 ? 0.8850 0.6748 0.7242 0.0346  0.0110  -0.0743 410 ASP C CB  
11573 C CG  . ASP C 410 ? 1.0912 0.8777 0.9290 0.0568  0.0200  -0.0688 410 ASP C CG  
11574 O OD1 . ASP C 410 ? 1.3853 1.1381 1.2118 0.0637  0.0238  -0.0704 410 ASP C OD1 
11575 O OD2 . ASP C 410 ? 1.1259 0.9442 0.9746 0.0672  0.0229  -0.0618 410 ASP C OD2 
11576 N N   . GLY C 411 ? 0.8548 0.6560 0.7200 -0.0120 -0.0073 -0.0699 411 GLY C N   
11577 C CA  . GLY C 411 ? 0.7771 0.5859 0.6448 -0.0300 -0.0147 -0.0745 411 GLY C CA  
11578 C C   . GLY C 411 ? 0.8681 0.7037 0.7395 -0.0315 -0.0187 -0.0768 411 GLY C C   
11579 O O   . GLY C 411 ? 0.8697 0.7131 0.7422 -0.0453 -0.0253 -0.0807 411 GLY C O   
11580 N N   . ASN C 412 ? 0.8374 0.6893 0.7116 -0.0181 -0.0152 -0.0732 412 ASN C N   
11581 C CA  . ASN C 412 ? 0.7016 0.5778 0.5779 -0.0189 -0.0185 -0.0736 412 ASN C CA  
11582 C C   . ASN C 412 ? 0.7667 0.6707 0.6623 -0.0122 -0.0180 -0.0621 412 ASN C C   
11583 O O   . ASN C 412 ? 0.8472 0.7520 0.7524 -0.0062 -0.0150 -0.0553 412 ASN C O   
11584 C CB  . ASN C 412 ? 0.7763 0.6427 0.6308 -0.0109 -0.0143 -0.0820 412 ASN C CB  
11585 C CG  . ASN C 412 ? 0.7772 0.6373 0.6274 0.0075  -0.0049 -0.0793 412 ASN C CG  
11586 O OD1 . ASN C 412 ? 0.9172 0.8000 0.7830 0.0156  -0.0026 -0.0688 412 ASN C OD1 
11587 N ND2 . ASN C 412 ? 0.8794 0.7085 0.7083 0.0144  0.0004  -0.0888 412 ASN C ND2 
11588 N N   . PHE C 413 ? 0.7953 0.7217 0.6956 -0.0140 -0.0217 -0.0596 413 PHE C N   
11589 C CA  . PHE C 413 ? 0.7265 0.6769 0.6434 -0.0098 -0.0224 -0.0490 413 PHE C CA  
11590 C C   . PHE C 413 ? 0.7256 0.6869 0.6374 0.0014  -0.0168 -0.0454 413 PHE C C   
11591 O O   . PHE C 413 ? 0.7451 0.7281 0.6675 0.0018  -0.0186 -0.0368 413 PHE C O   
11592 C CB  . PHE C 413 ? 0.7683 0.7362 0.6954 -0.0187 -0.0301 -0.0459 413 PHE C CB  
11593 C CG  . PHE C 413 ? 0.6922 0.6558 0.6256 -0.0289 -0.0351 -0.0490 413 PHE C CG  
11594 C CD1 . PHE C 413 ? 0.6875 0.6441 0.6104 -0.0376 -0.0385 -0.0569 413 PHE C CD1 
11595 C CD2 . PHE C 413 ? 0.6702 0.6385 0.6194 -0.0303 -0.0363 -0.0440 413 PHE C CD2 
11596 C CE1 . PHE C 413 ? 0.6791 0.6365 0.6097 -0.0477 -0.0428 -0.0582 413 PHE C CE1 
11597 C CE2 . PHE C 413 ? 0.6428 0.6111 0.5983 -0.0387 -0.0396 -0.0462 413 PHE C CE2 
11598 C CZ  . PHE C 413 ? 0.7207 0.6851 0.6683 -0.0476 -0.0428 -0.0525 413 PHE C CZ  
11599 N N   . LEU C 414 ? 0.7571 0.7035 0.6530 0.0108  -0.0097 -0.0512 414 LEU C N   
11600 C CA  . LEU C 414 ? 0.7354 0.6953 0.6247 0.0224  -0.0033 -0.0487 414 LEU C CA  
11601 C C   . LEU C 414 ? 0.7228 0.7006 0.6278 0.0314  0.0007  -0.0369 414 LEU C C   
11602 O O   . LEU C 414 ? 0.7137 0.7106 0.6182 0.0399  0.0058  -0.0317 414 LEU C O   
11603 C CB  . LEU C 414 ? 0.6602 0.5970 0.5252 0.0314  0.0036  -0.0605 414 LEU C CB  
11604 C CG  . LEU C 414 ? 0.7542 0.6844 0.5981 0.0257  0.0014  -0.0717 414 LEU C CG  
11605 C CD1 . LEU C 414 ? 0.6680 0.6231 0.5055 0.0328  0.0054  -0.0684 414 LEU C CD1 
11606 C CD2 . LEU C 414 ? 0.8507 0.7842 0.7016 0.0081  -0.0095 -0.0722 414 LEU C CD2 
11607 N N   . LYS C 415 ? 0.7354 0.7101 0.6540 0.0290  -0.0017 -0.0321 415 LYS C N   
11608 C CA  . LYS C 415 ? 0.7520 0.7470 0.6868 0.0341  -0.0004 -0.0204 415 LYS C CA  
11609 C C   . LYS C 415 ? 0.8235 0.8422 0.7732 0.0251  -0.0066 -0.0116 415 LYS C C   
11610 O O   . LYS C 415 ? 0.8896 0.9288 0.8515 0.0275  -0.0060 -0.0014 415 LYS C O   
11611 C CB  . LYS C 415 ? 0.8288 0.8114 0.7700 0.0341  -0.0015 -0.0188 415 LYS C CB  
11612 C CG  . LYS C 415 ? 0.8699 0.8725 0.8262 0.0387  -0.0013 -0.0074 415 LYS C CG  
11613 C CD  . LYS C 415 ? 0.9683 0.9684 0.9200 0.0549  0.0067  -0.0049 415 LYS C CD  
11614 C CE  . LYS C 415 ? 1.0246 1.0575 0.9914 0.0609  0.0079  0.0078  415 LYS C CE  
11615 N NZ  . LYS C 415 ? 0.9414 0.9988 0.9138 0.0559  0.0069  0.0121  415 LYS C NZ  
11616 N N   . TRP C 416 ? 0.7972 0.8138 0.7462 0.0148  -0.0128 -0.0146 416 TRP C N   
11617 C CA  . TRP C 416 ? 0.7315 0.7646 0.6937 0.0067  -0.0191 -0.0063 416 TRP C CA  
11618 C C   . TRP C 416 ? 0.7315 0.7734 0.6875 0.0033  -0.0211 -0.0054 416 TRP C C   
11619 O O   . TRP C 416 ? 0.7585 0.8129 0.7244 -0.0025 -0.0261 0.0032  416 TRP C O   
11620 C CB  . TRP C 416 ? 0.7472 0.7710 0.7188 -0.0018 -0.0260 -0.0079 416 TRP C CB  
11621 C CG  . TRP C 416 ? 0.8078 0.8230 0.7835 0.0003  -0.0246 -0.0087 416 TRP C CG  
11622 C CD1 . TRP C 416 ? 0.7709 0.7942 0.7580 -0.0010 -0.0268 -0.0022 416 TRP C CD1 
11623 C CD2 . TRP C 416 ? 0.8037 0.8003 0.7707 0.0031  -0.0213 -0.0159 416 TRP C CD2 
11624 N NE1 . TRP C 416 ? 0.7343 0.7475 0.7202 0.0018  -0.0250 -0.0045 416 TRP C NE1 
11625 C CE2 . TRP C 416 ? 0.7246 0.7207 0.6986 0.0044  -0.0213 -0.0122 416 TRP C CE2 
11626 C CE3 . TRP C 416 ? 0.7820 0.7613 0.7349 0.0034  -0.0188 -0.0249 416 TRP C CE3 
11627 C CZ2 . TRP C 416 ? 0.6951 0.6747 0.6632 0.0068  -0.0184 -0.0156 416 TRP C CZ2 
11628 C CZ3 . TRP C 416 ? 0.7859 0.7462 0.7332 0.0048  -0.0162 -0.0289 416 TRP C CZ3 
11629 C CH2 . TRP C 416 ? 0.7678 0.7286 0.7230 0.0069  -0.0157 -0.0234 416 TRP C CH2 
11630 N N   . ILE C 417 ? 0.6787 0.7133 0.6173 0.0064  -0.0180 -0.0139 417 ILE C N   
11631 C CA  . ILE C 417 ? 0.7058 0.7499 0.6359 0.0028  -0.0205 -0.0135 417 ILE C CA  
11632 C C   . ILE C 417 ? 0.7729 0.8116 0.6808 0.0104  -0.0136 -0.0226 417 ILE C C   
11633 O O   . ILE C 417 ? 0.8026 0.8241 0.7019 0.0173  -0.0081 -0.0309 417 ILE C O   
11634 C CB  . ILE C 417 ? 0.6867 0.7239 0.6192 -0.0072 -0.0294 -0.0170 417 ILE C CB  
11635 C CG1 . ILE C 417 ? 0.7116 0.7654 0.6436 -0.0114 -0.0343 -0.0097 417 ILE C CG1 
11636 C CG2 . ILE C 417 ? 0.6745 0.6928 0.5922 -0.0092 -0.0293 -0.0306 417 ILE C CG2 
11637 C CD1 . ILE C 417 ? 0.6266 0.6814 0.5731 -0.0185 -0.0430 -0.0047 417 ILE C CD1 
11638 N N   . GLY C 418 ? 0.6765 0.7291 0.5739 0.0098  -0.0137 -0.0209 418 GLY C N   
11639 C CA  . GLY C 418 ? 0.6486 0.6942 0.5208 0.0155  -0.0084 -0.0321 418 GLY C CA  
11640 C C   . GLY C 418 ? 0.7771 0.8379 0.6402 0.0284  0.0024  -0.0293 418 GLY C C   
11641 O O   . GLY C 418 ? 0.8901 0.9443 0.7292 0.0344  0.0075  -0.0401 418 GLY C O   
11642 N N   . ASN C 419 ? 0.8742 0.9558 0.7548 0.0328  0.0061  -0.0158 419 ASN C N   
11643 C CA  . ASN C 419 ? 0.8707 0.9767 0.7467 0.0440  0.0162  -0.0094 419 ASN C CA  
11644 C C   . ASN C 419 ? 0.8249 0.9619 0.7155 0.0361  0.0128  0.0086  419 ASN C C   
11645 O O   . ASN C 419 ? 0.8785 1.0147 0.7848 0.0239  0.0031  0.0161  419 ASN C O   
11646 C CB  . ASN C 419 ? 0.7997 0.9065 0.6829 0.0578  0.0252  -0.0083 419 ASN C CB  
11647 C CG  . ASN C 419 ? 0.8517 0.9674 0.7625 0.0522  0.0204  0.0041  419 ASN C CG  
11648 O OD1 . ASN C 419 ? 0.9283 1.0553 0.8540 0.0395  0.0124  0.0144  419 ASN C OD1 
11649 N ND2 . ASN C 419 ? 0.8339 0.9433 0.7503 0.0623  0.0252  0.0030  419 ASN C ND2 
11650 N N   . LYS C 420 ? 0.8153 0.9793 0.6999 0.0434  0.0214  0.0157  420 LYS C N   
11651 C CA  . LYS C 420 ? 0.8026 0.9960 0.6983 0.0346  0.0185  0.0339  420 LYS C CA  
11652 C C   . LYS C 420 ? 0.9088 1.1093 0.8331 0.0258  0.0126  0.0480  420 LYS C C   
11653 O O   . LYS C 420 ? 0.8674 1.0705 0.8024 0.0128  0.0036  0.0585  420 LYS C O   
11654 C CB  . LYS C 420 ? 0.8193 1.0441 0.7053 0.0449  0.0306  0.0403  420 LYS C CB  
11655 C CG  . LYS C 420 ? 0.9951 1.2544 0.8979 0.0359  0.0294  0.0629  420 LYS C CG  
11656 C CD  . LYS C 420 ? 0.9930 1.2874 0.9001 0.0473  0.0426  0.0721  420 LYS C CD  
11657 C CE  . LYS C 420 ? 0.9938 1.3178 0.9274 0.0351  0.0392  0.0955  420 LYS C CE  
11658 N NZ  . LYS C 420 ? 1.0348 1.3527 0.9726 0.0169  0.0270  0.1058  420 LYS C NZ  
11659 N N   . GLU C 421 ? 0.8734 1.0751 0.8092 0.0328  0.0171  0.0479  421 GLU C N   
11660 C CA  . GLU C 421 ? 0.7590 0.9700 0.7200 0.0239  0.0114  0.0608  421 GLU C CA  
11661 C C   . GLU C 421 ? 0.8399 1.0227 0.8084 0.0129  -0.0003 0.0559  421 GLU C C   
11662 O O   . GLU C 421 ? 0.8696 1.0553 0.8525 0.0004  -0.0085 0.0664  421 GLU C O   
11663 C CB  . GLU C 421 ? 0.8158 1.0391 0.7865 0.0351  0.0188  0.0625  421 GLU C CB  
11664 C CG  . GLU C 421 ? 0.9406 1.1872 0.9010 0.0525  0.0330  0.0625  421 GLU C CG  
11665 C CD  . GLU C 421 ? 1.0083 1.2282 0.9437 0.0670  0.0397  0.0431  421 GLU C CD  
11666 O OE1 . GLU C 421 ? 0.9280 1.1596 0.8536 0.0845  0.0520  0.0400  421 GLU C OE1 
11667 O OE2 . GLU C 421 ? 1.0353 1.2225 0.9606 0.0605  0.0326  0.0310  421 GLU C OE2 
11668 N N   . LYS C 422 ? 0.8087 0.9637 0.7673 0.0173  -0.0010 0.0402  422 LYS C N   
11669 C CA  . LYS C 422 ? 0.7378 0.8696 0.7037 0.0081  -0.0107 0.0357  422 LYS C CA  
11670 C C   . LYS C 422 ? 0.6893 0.8161 0.6523 -0.0014 -0.0186 0.0372  422 LYS C C   
11671 O O   . LYS C 422 ? 0.6589 0.7769 0.6336 -0.0100 -0.0269 0.0406  422 LYS C O   
11672 C CB  . LYS C 422 ? 0.8024 0.9087 0.7589 0.0143  -0.0088 0.0204  422 LYS C CB  
11673 C CG  . LYS C 422 ? 0.7847 0.8901 0.7497 0.0210  -0.0050 0.0209  422 LYS C CG  
11674 C CD  . LYS C 422 ? 0.7750 0.8545 0.7273 0.0284  -0.0015 0.0071  422 LYS C CD  
11675 C CE  . LYS C 422 ? 0.7944 0.8781 0.7460 0.0428  0.0072  0.0079  422 LYS C CE  
11676 N NZ  . LYS C 422 ? 0.8170 0.9070 0.7862 0.0410  0.0041  0.0158  422 LYS C NZ  
11677 N N   . ASN C 423 ? 0.7441 0.8767 0.6908 0.0010  -0.0161 0.0348  423 ASN C N   
11678 C CA  . ASN C 423 ? 0.6451 0.7766 0.5892 -0.0071 -0.0241 0.0382  423 ASN C CA  
11679 C C   . ASN C 423 ? 0.6700 0.8164 0.6283 -0.0151 -0.0286 0.0563  423 ASN C C   
11680 O O   . ASN C 423 ? 0.7022 0.8417 0.6655 -0.0222 -0.0372 0.0612  423 ASN C O   
11681 C CB  . ASN C 423 ? 0.6639 0.8016 0.5855 -0.0032 -0.0208 0.0324  423 ASN C CB  
11682 C CG  . ASN C 423 ? 0.6815 0.7984 0.5868 0.0017  -0.0184 0.0134  423 ASN C CG  
11683 O OD1 . ASN C 423 ? 0.7355 0.8328 0.6475 0.0000  -0.0215 0.0057  423 ASN C OD1 
11684 N ND2 . ASN C 423 ? 0.6550 0.7755 0.5377 0.0074  -0.0129 0.0057  423 ASN C ND2 
11685 N N   . GLU C 424 ? 0.7523 0.9191 0.7179 -0.0143 -0.0232 0.0672  424 GLU C N   
11686 C CA  . GLU C 424 ? 0.7314 0.9112 0.7102 -0.0245 -0.0279 0.0855  424 GLU C CA  
11687 C C   . GLU C 424 ? 0.7069 0.8673 0.7020 -0.0329 -0.0370 0.0871  424 GLU C C   
11688 O O   . GLU C 424 ? 0.7658 0.9202 0.7672 -0.0416 -0.0448 0.0968  424 GLU C O   
11689 C CB  . GLU C 424 ? 0.6657 0.8752 0.6500 -0.0230 -0.0199 0.0971  424 GLU C CB  
11690 C CG  . GLU C 424 ? 0.8477 1.0804 0.8321 -0.0302 -0.0200 0.1155  424 GLU C CG  
11691 C CD  . GLU C 424 ? 0.9753 1.2077 0.9788 -0.0450 -0.0282 0.1317  424 GLU C CD  
11692 O OE1 . GLU C 424 ? 0.9730 1.2032 0.9906 -0.0483 -0.0297 0.1315  424 GLU C OE1 
11693 O OE2 . GLU C 424 ? 0.9627 1.1958 0.9662 -0.0538 -0.0337 0.1448  424 GLU C OE2 
11694 N N   . TYR C 425 ? 0.5925 0.7415 0.5931 -0.0299 -0.0362 0.0774  425 TYR C N   
11695 C CA  . TYR C 425 ? 0.6156 0.7445 0.6279 -0.0367 -0.0444 0.0757  425 TYR C CA  
11696 C C   . TYR C 425 ? 0.6592 0.7677 0.6675 -0.0373 -0.0507 0.0693  425 TYR C C   
11697 O O   . TYR C 425 ? 0.7186 0.8139 0.7350 -0.0435 -0.0583 0.0738  425 TYR C O   
11698 C CB  . TYR C 425 ? 0.6753 0.7974 0.6909 -0.0321 -0.0418 0.0658  425 TYR C CB  
11699 C CG  . TYR C 425 ? 0.7332 0.8692 0.7615 -0.0369 -0.0419 0.0746  425 TYR C CG  
11700 C CD1 . TYR C 425 ? 0.6964 0.8587 0.7305 -0.0412 -0.0396 0.0894  425 TYR C CD1 
11701 C CD2 . TYR C 425 ? 0.6557 0.7814 0.6902 -0.0380 -0.0447 0.0687  425 TYR C CD2 
11702 C CE1 . TYR C 425 ? 0.6947 0.8735 0.7419 -0.0472 -0.0406 0.0982  425 TYR C CE1 
11703 C CE2 . TYR C 425 ? 0.6463 0.7871 0.6921 -0.0434 -0.0461 0.0768  425 TYR C CE2 
11704 C CZ  . TYR C 425 ? 0.7472 0.9151 0.8002 -0.0485 -0.0444 0.0916  425 TYR C CZ  
11705 O OH  . TYR C 425 ? 0.7814 0.9685 0.8473 -0.0556 -0.0466 0.1008  425 TYR C OH  
11706 N N   . TRP C 426 ? 0.6501 0.7559 0.6458 -0.0307 -0.0479 0.0589  426 TRP C N   
11707 C CA  . TRP C 426 ? 0.7574 0.8499 0.7509 -0.0313 -0.0541 0.0538  426 TRP C CA  
11708 C C   . TRP C 426 ? 0.7478 0.8469 0.7415 -0.0354 -0.0595 0.0669  426 TRP C C   
11709 O O   . TRP C 426 ? 0.8415 0.9290 0.8412 -0.0371 -0.0667 0.0689  426 TRP C O   
11710 C CB  . TRP C 426 ? 0.7370 0.8270 0.7166 -0.0258 -0.0505 0.0402  426 TRP C CB  
11711 C CG  . TRP C 426 ? 0.7474 0.8235 0.7285 -0.0229 -0.0477 0.0281  426 TRP C CG  
11712 C CD1 . TRP C 426 ? 0.7097 0.7862 0.6854 -0.0174 -0.0403 0.0224  426 TRP C CD1 
11713 C CD2 . TRP C 426 ? 0.6225 0.6834 0.6111 -0.0245 -0.0520 0.0215  426 TRP C CD2 
11714 N NE1 . TRP C 426 ? 0.6067 0.6677 0.5855 -0.0166 -0.0403 0.0135  426 TRP C NE1 
11715 C CE2 . TRP C 426 ? 0.6310 0.6837 0.6176 -0.0213 -0.0471 0.0126  426 TRP C CE2 
11716 C CE3 . TRP C 426 ? 0.5374 0.5919 0.5341 -0.0271 -0.0589 0.0227  426 TRP C CE3 
11717 C CZ2 . TRP C 426 ? 0.5726 0.6123 0.5643 -0.0223 -0.0488 0.0054  426 TRP C CZ2 
11718 C CZ3 . TRP C 426 ? 0.5782 0.6209 0.5804 -0.0267 -0.0600 0.0146  426 TRP C CZ3 
11719 C CH2 . TRP C 426 ? 0.6057 0.6419 0.6052 -0.0251 -0.0549 0.0062  426 TRP C CH2 
11720 N N   . LYS C 427 ? 0.7098 0.8285 0.6969 -0.0362 -0.0558 0.0769  427 LYS C N   
11721 C CA  . LYS C 427 ? 0.7048 0.8306 0.6921 -0.0410 -0.0609 0.0923  427 LYS C CA  
11722 C C   . LYS C 427 ? 0.6923 0.8080 0.6950 -0.0489 -0.0668 0.1048  427 LYS C C   
11723 O O   . LYS C 427 ? 0.6979 0.8056 0.7037 -0.0520 -0.0739 0.1148  427 LYS C O   
11724 C CB  . LYS C 427 ? 0.7182 0.8699 0.6938 -0.0403 -0.0545 0.1008  427 LYS C CB  
11725 C CG  . LYS C 427 ? 0.7494 0.9095 0.7068 -0.0362 -0.0545 0.0963  427 LYS C CG  
11726 C CD  . LYS C 427 ? 0.8062 0.9596 0.7661 -0.0393 -0.0648 0.1039  427 LYS C CD  
11727 C CE  . LYS C 427 ? 0.8210 0.9782 0.7653 -0.0357 -0.0672 0.0934  427 LYS C CE  
11728 N NZ  . LYS C 427 ? 0.6962 0.8421 0.6484 -0.0359 -0.0771 0.0930  427 LYS C NZ  
11729 N N   . ILE C 428 ? 0.6203 0.7352 0.6318 -0.0523 -0.0644 0.1046  428 ILE C N   
11730 C CA  . ILE C 428 ? 0.6011 0.7026 0.6254 -0.0617 -0.0709 0.1139  428 ILE C CA  
11731 C C   . ILE C 428 ? 0.6545 0.7272 0.6832 -0.0597 -0.0775 0.1044  428 ILE C C   
11732 O O   . ILE C 428 ? 0.6624 0.7178 0.6962 -0.0640 -0.0847 0.1122  428 ILE C O   
11733 C CB  . ILE C 428 ? 0.6781 0.7898 0.7102 -0.0666 -0.0674 0.1151  428 ILE C CB  
11734 C CG1 . ILE C 428 ? 0.6395 0.7832 0.6704 -0.0691 -0.0609 0.1283  428 ILE C CG1 
11735 C CG2 . ILE C 428 ? 0.6390 0.7317 0.6822 -0.0776 -0.0755 0.1202  428 ILE C CG2 
11736 C CD1 . ILE C 428 ? 0.5838 0.7465 0.6185 -0.0660 -0.0536 0.1247  428 ILE C CD1 
11737 N N   . LEU C 429 ? 0.6857 0.7523 0.7120 -0.0526 -0.0747 0.0879  429 LEU C N   
11738 C CA  . LEU C 429 ? 0.6490 0.6926 0.6794 -0.0495 -0.0794 0.0783  429 LEU C CA  
11739 C C   . LEU C 429 ? 0.6890 0.7281 0.7177 -0.0448 -0.0838 0.0807  429 LEU C C   
11740 O O   . LEU C 429 ? 0.7395 0.7601 0.7742 -0.0437 -0.0896 0.0825  429 LEU C O   
11741 C CB  . LEU C 429 ? 0.6088 0.6510 0.6368 -0.0441 -0.0745 0.0622  429 LEU C CB  
11742 C CG  . LEU C 429 ? 0.6501 0.6753 0.6808 -0.0393 -0.0771 0.0510  429 LEU C CG  
11743 C CD1 . LEU C 429 ? 0.6789 0.6872 0.7156 -0.0428 -0.0798 0.0481  429 LEU C CD1 
11744 C CD2 . LEU C 429 ? 0.6302 0.6608 0.6552 -0.0341 -0.0717 0.0384  429 LEU C CD2 
11745 N N   . ILE C 430 ? 0.6605 0.7167 0.6803 -0.0413 -0.0814 0.0808  430 ILE C N   
11746 C CA  . ILE C 430 ? 0.7318 0.7893 0.7500 -0.0374 -0.0865 0.0846  430 ILE C CA  
11747 C C   . ILE C 430 ? 0.7828 0.8335 0.8059 -0.0407 -0.0928 0.1022  430 ILE C C   
11748 O O   . ILE C 430 ? 0.7919 0.8300 0.8205 -0.0362 -0.0988 0.1054  430 ILE C O   
11749 C CB  . ILE C 430 ? 0.7779 0.8566 0.7829 -0.0356 -0.0835 0.0823  430 ILE C CB  
11750 C CG1 . ILE C 430 ? 0.7361 0.8140 0.7373 -0.0318 -0.0809 0.0649  430 ILE C CG1 
11751 C CG2 . ILE C 430 ? 0.6801 0.7681 0.6818 -0.0348 -0.0896 0.0945  430 ILE C CG2 
11752 C CD1 . ILE C 430 ? 0.7296 0.8215 0.7151 -0.0316 -0.0752 0.0584  430 ILE C CD1 
11753 N N   . GLU C 431 ? 0.7486 0.8074 0.7702 -0.0482 -0.0912 0.1146  431 GLU C N   
11754 C CA  . GLU C 431 ? 0.8007 0.8527 0.8256 -0.0534 -0.0971 0.1336  431 GLU C CA  
11755 C C   . GLU C 431 ? 0.8265 0.8475 0.8616 -0.0561 -0.1026 0.1342  431 GLU C C   
11756 O O   . GLU C 431 ? 0.9468 0.9503 0.9851 -0.0546 -0.1092 0.1442  431 GLU C O   
11757 C CB  . GLU C 431 ? 0.8020 0.8744 0.8233 -0.0622 -0.0932 0.1475  431 GLU C CB  
11758 C CG  . GLU C 431 ? 0.9378 1.0366 0.9468 -0.0599 -0.0907 0.1554  431 GLU C CG  
11759 C CD  . GLU C 431 ? 1.0141 1.1076 1.0219 -0.0577 -0.0987 0.1685  431 GLU C CD  
11760 O OE1 . GLU C 431 ? 0.9684 1.0536 0.9772 -0.0495 -0.1028 0.1602  431 GLU C OE1 
11761 O OE2 . GLU C 431 ? 1.0200 1.1192 1.0267 -0.0642 -0.1009 0.1886  431 GLU C OE2 
11762 N N   . ALA C 432 ? 0.7594 0.7721 0.7983 -0.0596 -0.1001 0.1236  432 ALA C N   
11763 C CA  . ALA C 432 ? 0.8094 0.7910 0.8547 -0.0626 -0.1055 0.1213  432 ALA C CA  
11764 C C   . ALA C 432 ? 0.7032 0.6661 0.7503 -0.0504 -0.1081 0.1109  432 ALA C C   
11765 O O   . ALA C 432 ? 0.6826 0.6188 0.7329 -0.0485 -0.1140 0.1153  432 ALA C O   
11766 C CB  . ALA C 432 ? 0.7353 0.7163 0.7827 -0.0693 -0.1026 0.1118  432 ALA C CB  
11767 N N   . LYS C 433 ? 0.6664 0.6433 0.7116 -0.0417 -0.1037 0.0980  433 LYS C N   
11768 C CA  . LYS C 433 ? 0.7473 0.7136 0.7962 -0.0301 -0.1054 0.0889  433 LYS C CA  
11769 C C   . LYS C 433 ? 0.8409 0.8019 0.8924 -0.0237 -0.1114 0.1019  433 LYS C C   
11770 O O   . LYS C 433 ? 0.8003 0.7435 0.8572 -0.0141 -0.1143 0.0989  433 LYS C O   
11771 C CB  . LYS C 433 ? 0.6544 0.6414 0.7008 -0.0250 -0.1001 0.0760  433 LYS C CB  
11772 C CG  . LYS C 433 ? 0.7280 0.7140 0.7798 -0.0139 -0.1013 0.0689  433 LYS C CG  
11773 C CD  . LYS C 433 ? 0.7804 0.7490 0.8358 -0.0101 -0.0991 0.0555  433 LYS C CD  
11774 C CE  . LYS C 433 ? 0.8145 0.7866 0.8767 0.0019  -0.0991 0.0494  433 LYS C CE  
11775 N NZ  . LYS C 433 ? 0.9393 0.8900 1.0072 0.0111  -0.1036 0.0548  433 LYS C NZ  
11776 N N   . LYS C 434 ? 0.8154 0.7922 0.8630 -0.0278 -0.1131 0.1170  434 LYS C N   
11777 C CA  . LYS C 434 ? 0.7952 0.7670 0.8450 -0.0222 -0.1196 0.1325  434 LYS C CA  
11778 C C   . LYS C 434 ? 0.7705 0.7066 0.8244 -0.0238 -0.1248 0.1410  434 LYS C C   
11779 O O   . LYS C 434 ? 0.8649 0.7832 0.9233 -0.0132 -0.1296 0.1456  434 LYS C O   
11780 C CB  . LYS C 434 ? 0.7936 0.7905 0.8359 -0.0280 -0.1201 0.1477  434 LYS C CB  
11781 C CG  . LYS C 434 ? 0.8328 0.8604 0.8671 -0.0286 -0.1144 0.1375  434 LYS C CG  
11782 C CD  . LYS C 434 ? 0.7838 0.8363 0.8091 -0.0292 -0.1164 0.1506  434 LYS C CD  
11783 C CE  . LYS C 434 ? 0.8167 0.8944 0.8331 -0.0270 -0.1131 0.1375  434 LYS C CE  
11784 N NZ  . LYS C 434 ? 1.0712 1.1738 1.0757 -0.0281 -0.1156 0.1489  434 LYS C NZ  
11785 N N   . LYS C 435 ? 0.8499 0.7745 0.9021 -0.0369 -0.1243 0.1434  435 LYS C N   
11786 C CA  . LYS C 435 ? 0.8185 0.7060 0.8726 -0.0422 -0.1300 0.1505  435 LYS C CA  
11787 C C   . LYS C 435 ? 0.8248 0.6882 0.8795 -0.0429 -0.1290 0.1324  435 LYS C C   
11788 O O   . LYS C 435 ? 0.9187 0.7514 0.9724 -0.0517 -0.1335 0.1351  435 LYS C O   
11789 C CB  . LYS C 435 ? 0.8936 0.7859 0.9455 -0.0594 -0.1317 0.1687  435 LYS C CB  
11790 C CG  . LYS C 435 ? 1.0002 0.9242 1.0486 -0.0598 -0.1308 0.1854  435 LYS C CG  
11791 C CD  . LYS C 435 ? 1.0251 0.9708 1.0710 -0.0762 -0.1278 0.1974  435 LYS C CD  
11792 C CE  . LYS C 435 ? 0.9104 0.8961 0.9493 -0.0738 -0.1234 0.2051  435 LYS C CE  
11793 N NZ  . LYS C 435 ? 0.8865 0.8973 0.9229 -0.0875 -0.1190 0.2176  435 LYS C NZ  
11794 N N   . ALA C 436 ? 0.7833 0.6595 0.8384 -0.0351 -0.1235 0.1141  436 ALA C N   
11795 C CA  . ALA C 436 ? 0.7870 0.6449 0.8408 -0.0361 -0.1220 0.0970  436 ALA C CA  
11796 C C   . ALA C 436 ? 0.8169 0.6395 0.8712 -0.0243 -0.1253 0.0908  436 ALA C C   
11797 O O   . ALA C 436 ? 0.8876 0.7138 0.9459 -0.0087 -0.1247 0.0905  436 ALA C O   
11798 C CB  . ALA C 436 ? 0.7836 0.6669 0.8371 -0.0319 -0.1147 0.0812  436 ALA C CB  
11799 N N   . LYS C 437 ? 0.8799 0.6691 0.9297 -0.0315 -0.1288 0.0857  437 LYS C N   
11800 C CA  . LYS C 437 ? 0.8328 0.5825 0.8799 -0.0203 -0.1316 0.0782  437 LYS C CA  
11801 C C   . LYS C 437 ? 0.8459 0.5785 0.8859 -0.0212 -0.1296 0.0574  437 LYS C C   
11802 O O   . LYS C 437 ? 0.8649 0.5612 0.8995 -0.0124 -0.1315 0.0488  437 LYS C O   
11803 C CB  . LYS C 437 ? 0.7770 0.4903 0.8215 -0.0275 -0.1398 0.0937  437 LYS C CB  
11804 C CG  . LYS C 437 ? 0.8093 0.5412 0.8593 -0.0288 -0.1421 0.1167  437 LYS C CG  
11805 C CD  . LYS C 437 ? 0.9708 0.6663 1.0179 -0.0386 -0.1503 0.1339  437 LYS C CD  
11806 C CE  . LYS C 437 ? 0.9518 0.6685 0.9998 -0.0604 -0.1521 0.1512  437 LYS C CE  
11807 N NZ  . LYS C 437 ? 1.0032 0.7318 1.0540 -0.0587 -0.1545 0.1750  437 LYS C NZ  
11808 N N   . ASN C 438 ? 0.8310 0.5882 0.8697 -0.0307 -0.1258 0.0493  438 ASN C N   
11809 C CA  . ASN C 438 ? 0.8503 0.5975 0.8816 -0.0308 -0.1235 0.0300  438 ASN C CA  
11810 C C   . ASN C 438 ? 0.8036 0.5898 0.8373 -0.0309 -0.1163 0.0230  438 ASN C C   
11811 O O   . ASN C 438 ? 0.8780 0.6952 0.9178 -0.0325 -0.1136 0.0320  438 ASN C O   
11812 C CB  . ASN C 438 ? 0.9190 0.6397 0.9420 -0.0490 -0.1303 0.0284  438 ASN C CB  
11813 C CG  . ASN C 438 ? 0.9848 0.7299 1.0122 -0.0685 -0.1326 0.0417  438 ASN C CG  
11814 O OD1 . ASN C 438 ? 0.9558 0.7264 0.9834 -0.0753 -0.1296 0.0365  438 ASN C OD1 
11815 N ND2 . ASN C 438 ? 1.0271 0.7650 1.0582 -0.0772 -0.1377 0.0599  438 ASN C ND2 
11816 N N   . ASP C 439 ? 0.8047 0.5873 0.8318 -0.0289 -0.1133 0.0065  439 ASP C N   
11817 C CA  . ASP C 439 ? 0.8582 0.6729 0.8871 -0.0253 -0.1059 -0.0010 439 ASP C CA  
11818 C C   . ASP C 439 ? 0.8214 0.6583 0.8504 -0.0398 -0.1057 0.0032  439 ASP C C   
11819 O O   . ASP C 439 ? 0.8182 0.6784 0.8475 -0.0378 -0.0999 -0.0023 439 ASP C O   
11820 C CB  . ASP C 439 ? 0.8392 0.6438 0.8606 -0.0163 -0.1019 -0.0189 439 ASP C CB  
11821 C CG  . ASP C 439 ? 0.9925 0.7986 1.0187 0.0031  -0.0971 -0.0232 439 ASP C CG  
11822 O OD1 . ASP C 439 ? 0.9141 0.7377 0.9504 0.0087  -0.0962 -0.0131 439 ASP C OD1 
11823 O OD2 . ASP C 439 ? 0.9867 0.7786 1.0065 0.0129  -0.0941 -0.0366 439 ASP C OD2 
11824 N N   . TYR C 440 ? 0.8808 0.7123 0.9104 -0.0541 -0.1116 0.0140  440 TYR C N   
11825 C CA  . TYR C 440 ? 0.8423 0.7003 0.8744 -0.0659 -0.1107 0.0200  440 TYR C CA  
11826 C C   . TYR C 440 ? 0.8159 0.7053 0.8541 -0.0608 -0.1046 0.0276  440 TYR C C   
11827 O O   . TYR C 440 ? 0.7394 0.6529 0.7791 -0.0655 -0.1014 0.0300  440 TYR C O   
11828 C CB  . TYR C 440 ? 0.7752 0.6242 0.8085 -0.0829 -0.1183 0.0317  440 TYR C CB  
11829 C CG  . TYR C 440 ? 0.8723 0.7073 0.8988 -0.0946 -0.1237 0.0233  440 TYR C CG  
11830 C CD1 . TYR C 440 ? 0.8452 0.7060 0.8727 -0.1018 -0.1224 0.0221  440 TYR C CD1 
11831 C CD2 . TYR C 440 ? 0.8482 0.6436 0.8662 -0.0979 -0.1305 0.0164  440 TYR C CD2 
11832 C CE1 . TYR C 440 ? 0.8099 0.6613 0.8308 -0.1134 -0.1284 0.0150  440 TYR C CE1 
11833 C CE2 . TYR C 440 ? 0.8609 0.6430 0.8703 -0.1101 -0.1365 0.0076  440 TYR C CE2 
11834 C CZ  . TYR C 440 ? 0.8654 0.6775 0.8766 -0.1185 -0.1358 0.0073  440 TYR C CZ  
11835 O OH  . TYR C 440 ? 0.9714 0.7736 0.9735 -0.1315 -0.1428 -0.0009 440 TYR C OH  
11836 N N   . ILE C 441 ? 0.8434 0.7327 0.8844 -0.0507 -0.1033 0.0311  441 ILE C N   
11837 C CA  . ILE C 441 ? 0.8002 0.7173 0.8440 -0.0456 -0.0979 0.0351  441 ILE C CA  
11838 C C   . ILE C 441 ? 0.7362 0.6662 0.7780 -0.0394 -0.0915 0.0223  441 ILE C C   
11839 O O   . ILE C 441 ? 0.7588 0.7105 0.8002 -0.0391 -0.0868 0.0232  441 ILE C O   
11840 C CB  . ILE C 441 ? 0.7905 0.7053 0.8376 -0.0371 -0.0997 0.0421  441 ILE C CB  
11841 C CG1 . ILE C 441 ? 0.7146 0.6577 0.7621 -0.0356 -0.0961 0.0484  441 ILE C CG1 
11842 C CG2 . ILE C 441 ? 0.8046 0.7067 0.8527 -0.0242 -0.0989 0.0317  441 ILE C CG2 
11843 C CD1 . ILE C 441 ? 0.7760 0.7320 0.8226 -0.0458 -0.0966 0.0616  441 ILE C CD1 
11844 N N   . LEU C 442 ? 0.7167 0.6326 0.7559 -0.0344 -0.0909 0.0102  442 LEU C N   
11845 C CA  . LEU C 442 ? 0.7313 0.6592 0.7681 -0.0301 -0.0849 -0.0003 442 LEU C CA  
11846 C C   . LEU C 442 ? 0.7021 0.6394 0.7355 -0.0384 -0.0837 -0.0008 442 LEU C C   
11847 O O   . LEU C 442 ? 0.7043 0.6574 0.7366 -0.0365 -0.0783 -0.0035 442 LEU C O   
11848 C CB  . LEU C 442 ? 0.7782 0.6911 0.8124 -0.0222 -0.0839 -0.0122 442 LEU C CB  
11849 C CG  . LEU C 442 ? 0.7097 0.6144 0.7487 -0.0111 -0.0846 -0.0118 442 LEU C CG  
11850 C CD1 . LEU C 442 ? 0.7000 0.5874 0.7348 -0.0029 -0.0833 -0.0238 442 LEU C CD1 
11851 C CD2 . LEU C 442 ? 0.7296 0.6580 0.7745 -0.0055 -0.0805 -0.0102 442 LEU C CD2 
11852 N N   . VAL C 443 ? 0.7056 0.6333 0.7378 -0.0479 -0.0890 0.0025  443 VAL C N   
11853 C CA  . VAL C 443 ? 0.7462 0.6882 0.7777 -0.0559 -0.0888 0.0050  443 VAL C CA  
11854 C C   . VAL C 443 ? 0.6758 0.6411 0.7118 -0.0565 -0.0852 0.0153  443 VAL C C   
11855 O O   . VAL C 443 ? 0.6016 0.5836 0.6367 -0.0545 -0.0803 0.0144  443 VAL C O   
11856 C CB  . VAL C 443 ? 0.6889 0.6181 0.7190 -0.0683 -0.0967 0.0075  443 VAL C CB  
11857 C CG1 . VAL C 443 ? 0.6072 0.5528 0.6364 -0.0749 -0.0969 0.0075  443 VAL C CG1 
11858 C CG2 . VAL C 443 ? 0.7596 0.6587 0.7827 -0.0665 -0.1007 -0.0031 443 VAL C CG2 
11859 N N   . ALA C 444 ? 0.7255 0.6916 0.7651 -0.0584 -0.0871 0.0253  444 ALA C N   
11860 C CA  . ALA C 444 ? 0.7488 0.7374 0.7904 -0.0584 -0.0832 0.0348  444 ALA C CA  
11861 C C   . ALA C 444 ? 0.7158 0.7142 0.7538 -0.0485 -0.0765 0.0288  444 ALA C C   
11862 O O   . ALA C 444 ? 0.7924 0.8083 0.8288 -0.0468 -0.0717 0.0327  444 ALA C O   
11863 C CB  . ALA C 444 ? 0.6912 0.6781 0.7358 -0.0628 -0.0870 0.0474  444 ALA C CB  
11864 N N   . GLU C 445 ? 0.6026 0.6857 0.5066 -0.1293 0.0242  0.0304  445 GLU C N   
11865 C CA  . GLU C 445 ? 0.6445 0.7090 0.5458 -0.1423 0.0086  0.0374  445 GLU C CA  
11866 C C   . GLU C 445 ? 0.6702 0.6914 0.5248 -0.1509 -0.0020 0.0376  445 GLU C C   
11867 O O   . GLU C 445 ? 0.7833 0.7834 0.6319 -0.1655 -0.0168 0.0455  445 GLU C O   
11868 C CB  . GLU C 445 ? 0.6991 0.7878 0.6501 -0.1601 0.0255  0.0508  445 GLU C CB  
11869 C CG  . GLU C 445 ? 0.6686 0.7902 0.6684 -0.1569 0.0182  0.0568  445 GLU C CG  
11870 C CD  . GLU C 445 ? 0.6946 0.8538 0.7580 -0.1634 0.0456  0.0672  445 GLU C CD  
11871 O OE1 . GLU C 445 ? 0.7742 0.9335 0.8495 -0.1765 0.0677  0.0746  445 GLU C OE1 
11872 O OE2 . GLU C 445 ? 0.6877 0.8761 0.7899 -0.1550 0.0462  0.0686  445 GLU C OE2 
11873 N N   . GLY C 446 ? 0.6791 0.6850 0.5016 -0.1448 0.0011  0.0321  446 GLY C N   
11874 C CA  . GLY C 446 ? 0.7224 0.6856 0.5022 -0.1549 -0.0129 0.0352  446 GLY C CA  
11875 C C   . GLY C 446 ? 0.7448 0.6788 0.5041 -0.1414 -0.0450 0.0307  446 GLY C C   
11876 O O   . GLY C 446 ? 0.7950 0.7402 0.5601 -0.1182 -0.0529 0.0215  446 GLY C O   
11877 N N   . SER C 447 ? 0.7890 0.6823 0.5212 -0.1565 -0.0629 0.0372  447 SER C N   
11878 C CA  . SER C 447 ? 0.8685 0.7235 0.5785 -0.1440 -0.0946 0.0317  447 SER C CA  
11879 C C   . SER C 447 ? 0.8759 0.7166 0.5679 -0.1177 -0.1052 0.0231  447 SER C C   
11880 O O   . SER C 447 ? 0.8873 0.7077 0.5688 -0.0947 -0.1225 0.0126  447 SER C O   
11881 C CB  . SER C 447 ? 0.8726 0.6844 0.5601 -0.1699 -0.1148 0.0437  447 SER C CB  
11882 O OG  . SER C 447 ? 0.8953 0.6886 0.5596 -0.1861 -0.1132 0.0529  447 SER C OG  
11883 N N   . ASP C 448 ? 0.8250 0.6754 0.5141 -0.1202 -0.0949 0.0280  448 ASP C N   
11884 C CA  . ASP C 448 ? 0.8325 0.6701 0.5123 -0.0991 -0.1093 0.0267  448 ASP C CA  
11885 C C   . ASP C 448 ? 0.8024 0.6729 0.5047 -0.0652 -0.1035 0.0156  448 ASP C C   
11886 O O   . ASP C 448 ? 0.8242 0.6788 0.5230 -0.0392 -0.1179 0.0096  448 ASP C O   
11887 C CB  . ASP C 448 ? 0.8489 0.6876 0.5176 -0.1159 -0.1029 0.0382  448 ASP C CB  
11888 C CG  . ASP C 448 ? 0.8896 0.7029 0.5320 -0.1531 -0.0988 0.0485  448 ASP C CG  
11889 O OD1 . ASP C 448 ? 0.8550 0.6918 0.5065 -0.1687 -0.0720 0.0483  448 ASP C OD1 
11890 O OD2 . ASP C 448 ? 0.9107 0.6813 0.5255 -0.1665 -0.1218 0.0578  448 ASP C OD2 
11891 N N   . TRP C 449 ? 0.7573 0.6731 0.4836 -0.0644 -0.0820 0.0129  449 TRP C N   
11892 C CA  . TRP C 449 ? 0.7303 0.6816 0.4762 -0.0363 -0.0756 0.0053  449 TRP C CA  
11893 C C   . TRP C 449 ? 0.8044 0.7346 0.5368 -0.0156 -0.0872 -0.0077 449 TRP C C   
11894 O O   . TRP C 449 ? 0.9294 0.8685 0.6643 0.0138  -0.0872 -0.0143 449 TRP C O   
11895 C CB  . TRP C 449 ? 0.7028 0.6994 0.4750 -0.0441 -0.0552 0.0062  449 TRP C CB  
11896 C CG  . TRP C 449 ? 0.6704 0.6736 0.4466 -0.0668 -0.0418 0.0149  449 TRP C CG  
11897 C CD1 . TRP C 449 ? 0.7183 0.7295 0.5063 -0.0871 -0.0259 0.0169  449 TRP C CD1 
11898 C CD2 . TRP C 449 ? 0.7571 0.7556 0.5228 -0.0714 -0.0424 0.0230  449 TRP C CD2 
11899 N NE1 . TRP C 449 ? 0.7922 0.8004 0.5717 -0.1020 -0.0125 0.0219  449 TRP C NE1 
11900 C CE2 . TRP C 449 ? 0.7813 0.7785 0.5424 -0.0951 -0.0247 0.0260  449 TRP C CE2 
11901 C CE3 . TRP C 449 ? 0.6865 0.6806 0.4473 -0.0585 -0.0569 0.0296  449 TRP C CE3 
11902 C CZ2 . TRP C 449 ? 0.7464 0.7299 0.4857 -0.1083 -0.0225 0.0328  449 TRP C CZ2 
11903 C CZ3 . TRP C 449 ? 0.7568 0.7421 0.5040 -0.0739 -0.0590 0.0408  449 TRP C CZ3 
11904 C CH2 . TRP C 449 ? 0.7864 0.7624 0.5167 -0.0997 -0.0425 0.0411  449 TRP C CH2 
11905 N N   . PHE C 450 ? 0.7852 0.6845 0.5011 -0.0310 -0.0971 -0.0108 450 PHE C N   
11906 C CA  . PHE C 450 ? 0.8460 0.7127 0.5370 -0.0153 -0.1111 -0.0245 450 PHE C CA  
11907 C C   . PHE C 450 ? 0.9071 0.7193 0.5708 0.0008  -0.1316 -0.0304 450 PHE C C   
11908 O O   . PHE C 450 ? 0.9231 0.7091 0.5648 0.0270  -0.1377 -0.0460 450 PHE C O   
11909 C CB  . PHE C 450 ? 0.9789 0.8296 0.6634 -0.0420 -0.1201 -0.0215 450 PHE C CB  
11910 C CG  . PHE C 450 ? 0.8467 0.7499 0.5663 -0.0561 -0.1022 -0.0142 450 PHE C CG  
11911 C CD1 . PHE C 450 ? 0.8160 0.7437 0.5391 -0.0436 -0.0971 -0.0214 450 PHE C CD1 
11912 C CD2 . PHE C 450 ? 0.7668 0.6935 0.5152 -0.0809 -0.0893 0.0000  450 PHE C CD2 
11913 C CE1 . PHE C 450 ? 0.7590 0.7331 0.5189 -0.0570 -0.0846 -0.0125 450 PHE C CE1 
11914 C CE2 . PHE C 450 ? 0.7472 0.7198 0.5339 -0.0902 -0.0726 0.0063  450 PHE C CE2 
11915 C CZ  . PHE C 450 ? 0.7659 0.7620 0.5609 -0.0786 -0.0727 0.0011  450 PHE C CZ  
11916 N N   . TRP C 451 ? 0.9778 0.7701 0.6406 -0.0137 -0.1417 -0.0182 451 TRP C N   
11917 C CA  . TRP C 451 ? 0.9986 0.7341 0.6390 -0.0024 -0.1666 -0.0203 451 TRP C CA  
11918 C C   . TRP C 451 ? 0.9956 0.7399 0.6486 0.0393  -0.1627 -0.0283 451 TRP C C   
11919 O O   . TRP C 451 ? 1.0815 0.7817 0.7160 0.0650  -0.1758 -0.0415 451 TRP C O   
11920 C CB  . TRP C 451 ? 0.9609 0.6776 0.5974 -0.0327 -0.1789 -0.0015 451 TRP C CB  
11921 C CG  . TRP C 451 ? 1.1260 0.7966 0.7519 -0.0222 -0.2047 0.0033  451 TRP C CG  
11922 C CD1 . TRP C 451 ? 1.1724 0.8553 0.8191 0.0014  -0.2061 0.0079  451 TRP C CD1 
11923 C CD2 . TRP C 451 ? 1.2089 0.8143 0.8063 -0.0379 -0.2362 0.0084  451 TRP C CD2 
11924 N NE1 . TRP C 451 ? 1.2534 0.8825 0.8892 0.0037  -0.2364 0.0147  451 TRP C NE1 
11925 C CE2 . TRP C 451 ? 1.2358 0.8146 0.8385 -0.0206 -0.2559 0.0144  451 TRP C CE2 
11926 C CE3 . TRP C 451 ? 1.1726 0.7406 0.7443 -0.0664 -0.2524 0.0116  451 TRP C CE3 
11927 C CZ2 . TRP C 451 ? 1.2689 0.7813 0.8493 -0.0300 -0.2916 0.0215  451 TRP C CZ2 
11928 C CZ3 . TRP C 451 ? 1.2175 0.7203 0.7643 -0.0773 -0.2879 0.0192  451 TRP C CZ3 
11929 C CH2 . TRP C 451 ? 1.3203 0.7941 0.8702 -0.0589 -0.3074 0.0232  451 TRP C CH2 
11930 N N   . TRP C 452 ? 0.9130 0.7132 0.5992 0.0472  -0.1444 -0.0199 452 TRP C N   
11931 C CA  . TRP C 452 ? 0.9688 0.7871 0.6789 0.0847  -0.1402 -0.0206 452 TRP C CA  
11932 C C   . TRP C 452 ? 1.0760 0.9191 0.7872 0.1173  -0.1200 -0.0385 452 TRP C C   
11933 O O   . TRP C 452 ? 1.1824 1.0282 0.9072 0.1547  -0.1151 -0.0441 452 TRP C O   
11934 C CB  . TRP C 452 ? 0.9943 0.8615 0.7391 0.0763  -0.1333 0.0000  452 TRP C CB  
11935 C CG  . TRP C 452 ? 0.9256 0.7672 0.6587 0.0407  -0.1501 0.0172  452 TRP C CG  
11936 C CD1 . TRP C 452 ? 0.8490 0.7067 0.5752 0.0063  -0.1411 0.0262  452 TRP C CD1 
11937 C CD2 . TRP C 452 ? 0.9231 0.7153 0.6460 0.0355  -0.1782 0.0276  452 TRP C CD2 
11938 N NE1 . TRP C 452 ? 0.8796 0.7007 0.5855 -0.0214 -0.1591 0.0405  452 TRP C NE1 
11939 C CE2 . TRP C 452 ? 0.9573 0.7385 0.6614 -0.0060 -0.1845 0.0434  452 TRP C CE2 
11940 C CE3 . TRP C 452 ? 1.0165 0.7700 0.7436 0.0624  -0.1986 0.0251  452 TRP C CE3 
11941 C CZ2 . TRP C 452 ? 1.0728 0.8071 0.7589 -0.0256 -0.2127 0.0588  452 TRP C CZ2 
11942 C CZ3 . TRP C 452 ? 1.1429 0.8498 0.8596 0.0447  -0.2293 0.0412  452 TRP C CZ3 
11943 C CH2 . TRP C 452 ? 1.1193 0.8176 0.8140 -0.0009 -0.2372 0.0589  452 TRP C CH2 
11944 N N   . GLN C 453 ? 1.0526 0.9143 0.7513 0.1039  -0.1076 -0.0461 453 GLN C N   
11945 C CA  . GLN C 453 ? 1.0156 0.8994 0.7067 0.1290  -0.0890 -0.0616 453 GLN C CA  
11946 C C   . GLN C 453 ? 1.0459 0.8683 0.6960 0.1563  -0.0968 -0.0839 453 GLN C C   
11947 O O   . GLN C 453 ? 1.1652 0.9243 0.7784 0.1412  -0.1191 -0.0908 453 GLN C O   
11948 C CB  . GLN C 453 ? 0.9972 0.9029 0.6801 0.1030  -0.0822 -0.0623 453 GLN C CB  
11949 C CG  . GLN C 453 ? 1.0142 0.9929 0.7358 0.0985  -0.0626 -0.0496 453 GLN C CG  
11950 C CD  . GLN C 453 ? 1.0102 1.0299 0.7523 0.1333  -0.0453 -0.0497 453 GLN C CD  
11951 O OE1 . GLN C 453 ? 0.8021 0.8475 0.5787 0.1418  -0.0443 -0.0351 453 GLN C OE1 
11952 N NE2 . GLN C 453 ? 1.0754 1.1023 0.7959 0.1517  -0.0317 -0.0640 453 GLN C NE2 
11953 N N   . GLY C 454 ? 1.0655 0.9052 0.7209 0.1965  -0.0776 -0.0947 454 GLY C N   
11954 C CA  . GLY C 454 ? 1.2347 1.0132 0.8463 0.2282  -0.0788 -0.1201 454 GLY C CA  
11955 C C   . GLY C 454 ? 1.4318 1.1510 1.0437 0.2440  -0.1008 -0.1216 454 GLY C C   
11956 O O   . GLY C 454 ? 1.5429 1.2019 1.1173 0.2737  -0.1031 -0.1446 454 GLY C O   
11957 N N   . GLU C 455 ? 1.4521 1.1811 1.1007 0.2242  -0.1184 -0.0981 455 GLU C N   
11958 C CA  . GLU C 455 ? 1.6287 1.3041 1.2829 0.2371  -0.1429 -0.0949 455 GLU C CA  
11959 C C   . GLU C 455 ? 1.6559 1.3535 1.3510 0.2886  -0.1260 -0.0969 455 GLU C C   
11960 O O   . GLU C 455 ? 1.6018 1.3696 1.3304 0.3076  -0.0957 -0.0932 455 GLU C O   
11961 C CB  . GLU C 455 ? 1.5332 1.2159 1.2120 0.1989  -0.1655 -0.0665 455 GLU C CB  
11962 C CG  . GLU C 455 ? 1.6383 1.2408 1.2872 0.1816  -0.2026 -0.0648 455 GLU C CG  
11963 C CD  . GLU C 455 ? 1.6422 1.1861 1.2321 0.1701  -0.2129 -0.0852 455 GLU C CD  
11964 O OE1 . GLU C 455 ? 1.5595 1.1204 1.1352 0.1332  -0.2108 -0.0800 455 GLU C OE1 
11965 O OE2 . GLU C 455 ? 1.7106 1.1891 1.2696 0.1978  -0.2245 -0.1052 455 GLU C OE2 
11966 N N   . GLU C 456 ? 1.6589 1.2971 1.3558 0.3112  -0.1468 -0.1005 456 GLU C N   
11967 C CA  . GLU C 456 ? 1.7183 1.3771 1.4699 0.3596  -0.1355 -0.0959 456 GLU C CA  
11968 C C   . GLU C 456 ? 1.6964 1.4418 1.5192 0.3492  -0.1294 -0.0613 456 GLU C C   
11969 O O   . GLU C 456 ? 1.6878 1.4592 1.5079 0.3034  -0.1388 -0.0436 456 GLU C O   
11970 C CB  . GLU C 456 ? 1.8098 1.3895 1.5615 0.3736  -0.1699 -0.0962 456 GLU C CB  
11971 C CG  . GLU C 456 ? 1.7430 1.3346 1.5423 0.3459  -0.2023 -0.0589 456 GLU C CG  
11972 C CD  . GLU C 456 ? 1.7845 1.2880 1.5712 0.3456  -0.2449 -0.0569 456 GLU C CD  
11973 O OE1 . GLU C 456 ? 1.8818 1.3204 1.6078 0.3143  -0.2687 -0.0665 456 GLU C OE1 
11974 O OE2 . GLU C 456 ? 1.7459 1.2465 1.5876 0.3748  -0.2570 -0.0425 456 GLU C OE2 
11975 N N   . LYS C 457 ? 1.7035 1.4922 1.5903 0.3910  -0.1138 -0.0506 457 LYS C N   
11976 C CA  . LYS C 457 ? 1.6617 1.5249 1.6204 0.3807  -0.1166 -0.0125 457 LYS C CA  
11977 C C   . LYS C 457 ? 1.6356 1.4712 1.5826 0.3272  -0.1567 0.0107  457 LYS C C   
11978 O O   . LYS C 457 ? 1.6574 1.4309 1.5988 0.3228  -0.1898 0.0158  457 LYS C O   
11979 C CB  . LYS C 457 ? 1.6104 1.4968 1.6453 0.4303  -0.1120 0.0018  457 LYS C CB  
11980 C CG  . LYS C 457 ? 1.4756 1.4082 1.5853 0.4133  -0.1373 0.0486  457 LYS C CG  
11981 C CD  . LYS C 457 ? 1.4798 1.4789 1.5967 0.3697  -0.1348 0.0726  457 LYS C CD  
11982 C CE  . LYS C 457 ? 1.3645 1.3901 1.5405 0.3477  -0.1678 0.1185  457 LYS C CE  
11983 N NZ  . LYS C 457 ? 1.2824 1.3397 1.4381 0.2953  -0.1746 0.1364  457 LYS C NZ  
11984 N N   . ALA C 458 ? 1.5737 1.4504 1.5116 0.2860  -0.1533 0.0236  458 ALA C N   
11985 C CA  . ALA C 458 ? 1.5385 1.3884 1.4518 0.2334  -0.1827 0.0411  458 ALA C CA  
11986 C C   . ALA C 458 ? 1.4569 1.3679 1.4066 0.2095  -0.1837 0.0721  458 ALA C C   
11987 O O   . ALA C 458 ? 1.3673 1.3452 1.3499 0.2246  -0.1585 0.0763  458 ALA C O   
11988 C CB  . ALA C 458 ? 1.5133 1.3329 1.3614 0.2007  -0.1783 0.0206  458 ALA C CB  
11989 N N   . PRO C 459 ? 1.4200 1.3054 1.3597 0.1700  -0.2142 0.0952  459 PRO C N   
11990 C CA  . PRO C 459 ? 1.2221 1.1514 1.1925 0.1473  -0.2232 0.1275  459 PRO C CA  
11991 C C   . PRO C 459 ? 1.1575 1.1210 1.1013 0.1185  -0.2021 0.1229  459 PRO C C   
11992 O O   . PRO C 459 ? 1.2634 1.1966 1.1545 0.0911  -0.1967 0.1065  459 PRO C O   
11993 C CB  . PRO C 459 ? 1.1769 1.0496 1.1261 0.1115  -0.2642 0.1492  459 PRO C CB  
11994 C CG  . PRO C 459 ? 1.2395 1.0525 1.1782 0.1330  -0.2783 0.1338  459 PRO C CG  
11995 C CD  . PRO C 459 ? 1.3796 1.1899 1.2834 0.1475  -0.2471 0.0971  459 PRO C CD  
11996 N N   . PHE C 460 ? 0.9820 1.0098 0.9678 0.1249  -0.1914 0.1397  460 PHE C N   
11997 C CA  . PHE C 460 ? 0.8572 0.9189 0.8265 0.0988  -0.1758 0.1402  460 PHE C CA  
11998 C C   . PHE C 460 ? 0.9469 1.0031 0.8767 0.0977  -0.1489 0.1078  460 PHE C C   
11999 O O   . PHE C 460 ? 1.0220 1.0752 0.9207 0.0665  -0.1424 0.1037  460 PHE C O   
12000 C CB  . PHE C 460 ? 0.9086 0.9399 0.8442 0.0502  -0.1990 0.1589  460 PHE C CB  
12001 C CG  . PHE C 460 ? 1.0745 1.0833 1.0294 0.0408  -0.2363 0.1901  460 PHE C CG  
12002 C CD1 . PHE C 460 ? 0.9667 1.0226 0.9887 0.0603  -0.2476 0.2191  460 PHE C CD1 
12003 C CD2 . PHE C 460 ? 1.1108 1.0531 1.0185 0.0090  -0.2616 0.1942  460 PHE C CD2 
12004 C CE1 . PHE C 460 ? 0.9227 0.9580 0.9682 0.0491  -0.2867 0.2522  460 PHE C CE1 
12005 C CE2 . PHE C 460 ? 1.1286 1.0465 1.0515 -0.0040 -0.3005 0.2258  460 PHE C CE2 
12006 C CZ  . PHE C 460 ? 1.0736 1.0371 1.0672 0.0161  -0.3147 0.2554  460 PHE C CZ  
12007 N N   . VAL C 461 ? 0.9675 1.0188 0.8975 0.1313  -0.1339 0.0850  461 VAL C N   
12008 C CA  . VAL C 461 ? 0.9392 0.9879 0.8347 0.1286  -0.1123 0.0584  461 VAL C CA  
12009 C C   . VAL C 461 ? 0.8960 1.0069 0.8089 0.1236  -0.0917 0.0628  461 VAL C C   
12010 O O   . VAL C 461 ? 0.9455 1.0571 0.8334 0.1044  -0.0807 0.0509  461 VAL C O   
12011 C CB  . VAL C 461 ? 1.0153 1.0420 0.9010 0.1656  -0.1025 0.0341  461 VAL C CB  
12012 C CG1 . VAL C 461 ? 1.0150 1.0592 0.8771 0.1685  -0.0784 0.0127  461 VAL C CG1 
12013 C CG2 . VAL C 461 ? 1.0711 1.0227 0.9212 0.1571  -0.1251 0.0249  461 VAL C CG2 
12014 N N   . GLU C 462 ? 0.7422 0.9069 0.7028 0.1392  -0.0888 0.0833  462 GLU C N   
12015 C CA  . GLU C 462 ? 0.7783 1.0014 0.7576 0.1306  -0.0749 0.0928  462 GLU C CA  
12016 C C   . GLU C 462 ? 0.8232 1.0314 0.7796 0.0881  -0.0859 0.1013  462 GLU C C   
12017 O O   . GLU C 462 ? 0.8329 1.0606 0.7803 0.0744  -0.0732 0.0950  462 GLU C O   
12018 C CB  . GLU C 462 ? 0.8739 1.1573 0.9133 0.1517  -0.0745 0.1197  462 GLU C CB  
12019 C CG  . GLU C 462 ? 0.9754 1.2615 1.0461 0.1949  -0.0692 0.1181  462 GLU C CG  
12020 C CD  . GLU C 462 ? 1.0088 1.2486 1.0876 0.1920  -0.0990 0.1311  462 GLU C CD  
12021 O OE1 . GLU C 462 ? 1.0318 1.2305 1.1010 0.2170  -0.0993 0.1139  462 GLU C OE1 
12022 O OE2 . GLU C 462 ? 0.8995 1.1390 0.9905 0.1634  -0.1246 0.1590  462 GLU C OE2 
12023 N N   . VAL C 463 ? 0.7721 0.9414 0.7157 0.0665  -0.1094 0.1150  463 VAL C N   
12024 C CA  . VAL C 463 ? 0.7263 0.8727 0.6381 0.0267  -0.1169 0.1208  463 VAL C CA  
12025 C C   . VAL C 463 ? 0.7625 0.8781 0.6335 0.0116  -0.1014 0.0955  463 VAL C C   
12026 O O   . VAL C 463 ? 0.7786 0.9018 0.6382 -0.0074 -0.0904 0.0919  463 VAL C O   
12027 C CB  . VAL C 463 ? 0.6948 0.7994 0.5917 0.0051  -0.1463 0.1410  463 VAL C CB  
12028 C CG1 . VAL C 463 ? 0.7027 0.7785 0.5565 -0.0358 -0.1509 0.1454  463 VAL C CG1 
12029 C CG2 . VAL C 463 ? 0.7268 0.8671 0.6767 0.0212  -0.1644 0.1706  463 VAL C CG2 
12030 N N   . PHE C 464 ? 0.7680 0.8481 0.6201 0.0199  -0.1015 0.0796  464 PHE C N   
12031 C CA  . PHE C 464 ? 0.8307 0.8892 0.6542 0.0064  -0.0881 0.0598  464 PHE C CA  
12032 C C   . PHE C 464 ? 0.8152 0.9157 0.6557 0.0189  -0.0680 0.0484  464 PHE C C   
12033 O O   . PHE C 464 ? 0.8023 0.9027 0.6337 0.0017  -0.0564 0.0405  464 PHE C O   
12034 C CB  . PHE C 464 ? 0.7588 0.7705 0.5602 0.0122  -0.0976 0.0483  464 PHE C CB  
12035 C CG  . PHE C 464 ? 0.8296 0.7930 0.6063 -0.0092 -0.1186 0.0596  464 PHE C CG  
12036 C CD1 . PHE C 464 ? 0.9364 0.8904 0.7281 0.0023  -0.1403 0.0752  464 PHE C CD1 
12037 C CD2 . PHE C 464 ? 0.8410 0.7702 0.5820 -0.0418 -0.1167 0.0572  464 PHE C CD2 
12038 C CE1 . PHE C 464 ? 0.9083 0.8149 0.6747 -0.0212 -0.1641 0.0885  464 PHE C CE1 
12039 C CE2 . PHE C 464 ? 0.8283 0.7121 0.5400 -0.0651 -0.1361 0.0693  464 PHE C CE2 
12040 C CZ  . PHE C 464 ? 0.8866 0.7566 0.6084 -0.0562 -0.1620 0.0851  464 PHE C CZ  
12041 N N   . ASP C 465 ? 0.7433 0.8811 0.6103 0.0483  -0.0630 0.0490  465 ASP C N   
12042 C CA  . ASP C 465 ? 0.8506 1.0258 0.7270 0.0571  -0.0459 0.0398  465 ASP C CA  
12043 C C   . ASP C 465 ? 0.7355 0.9494 0.6310 0.0402  -0.0409 0.0525  465 ASP C C   
12044 O O   . ASP C 465 ? 0.6523 0.8796 0.5480 0.0307  -0.0311 0.0457  465 ASP C O   
12045 C CB  . ASP C 465 ? 0.8294 1.0321 0.7218 0.0928  -0.0381 0.0366  465 ASP C CB  
12046 C CG  . ASP C 465 ? 0.7749 1.0160 0.6702 0.0987  -0.0215 0.0296  465 ASP C CG  
12047 O OD1 . ASP C 465 ? 0.8076 1.0242 0.6748 0.0946  -0.0184 0.0122  465 ASP C OD1 
12048 O OD2 . ASP C 465 ? 0.7674 1.0627 0.6928 0.1042  -0.0144 0.0444  465 ASP C OD2 
12049 N N   . LYS C 466 ? 0.6742 0.9029 0.5866 0.0350  -0.0510 0.0728  466 LYS C N   
12050 C CA  . LYS C 466 ? 0.6815 0.9338 0.6047 0.0156  -0.0515 0.0854  466 LYS C CA  
12051 C C   . LYS C 466 ? 0.7429 0.9597 0.6390 -0.0105 -0.0457 0.0740  466 LYS C C   
12052 O O   . LYS C 466 ? 0.7343 0.9694 0.6398 -0.0180 -0.0362 0.0706  466 LYS C O   
12053 C CB  . LYS C 466 ? 0.5969 0.8540 0.5325 0.0085  -0.0703 0.1106  466 LYS C CB  
12054 C CG  . LYS C 466 ? 0.5996 0.8945 0.5568 -0.0031 -0.0752 0.1296  466 LYS C CG  
12055 C CD  . LYS C 466 ? 0.7997 1.0628 0.7281 -0.0317 -0.0741 0.1230  466 LYS C CD  
12056 C CE  . LYS C 466 ? 0.8501 1.1523 0.8017 -0.0378 -0.0741 0.1334  466 LYS C CE  
12057 N NZ  . LYS C 466 ? 0.7983 1.1414 0.7726 -0.0221 -0.0574 0.1232  466 LYS C NZ  
12058 N N   . LEU C 467 ? 0.7677 0.9346 0.6327 -0.0241 -0.0506 0.0693  467 LEU C N   
12059 C CA  . LEU C 467 ? 0.7363 0.8713 0.5765 -0.0479 -0.0401 0.0598  467 LEU C CA  
12060 C C   . LEU C 467 ? 0.7365 0.8816 0.5875 -0.0443 -0.0247 0.0447  467 LEU C C   
12061 O O   . LEU C 467 ? 0.7503 0.9045 0.6116 -0.0546 -0.0124 0.0415  467 LEU C O   
12062 C CB  . LEU C 467 ? 0.7533 0.8357 0.5557 -0.0636 -0.0476 0.0596  467 LEU C CB  
12063 C CG  . LEU C 467 ? 0.7522 0.8112 0.5335 -0.0782 -0.0662 0.0766  467 LEU C CG  
12064 C CD1 . LEU C 467 ? 0.7113 0.7298 0.4684 -0.0829 -0.0817 0.0800  467 LEU C CD1 
12065 C CD2 . LEU C 467 ? 0.7607 0.7932 0.5096 -0.1052 -0.0577 0.0757  467 LEU C CD2 
12066 N N   . PHE C 468 ? 0.6599 0.7998 0.5091 -0.0302 -0.0274 0.0365  468 PHE C N   
12067 C CA  . PHE C 468 ? 0.6188 0.7630 0.4749 -0.0310 -0.0189 0.0255  468 PHE C CA  
12068 C C   . PHE C 468 ? 0.7317 0.9203 0.6172 -0.0273 -0.0119 0.0280  468 PHE C C   
12069 O O   . PHE C 468 ? 0.7713 0.9658 0.6718 -0.0394 -0.0037 0.0259  468 PHE C O   
12070 C CB  . PHE C 468 ? 0.6372 0.7644 0.4795 -0.0149 -0.0275 0.0166  468 PHE C CB  
12071 C CG  . PHE C 468 ? 0.6950 0.8230 0.5396 -0.0183 -0.0251 0.0082  468 PHE C CG  
12072 C CD1 . PHE C 468 ? 0.7270 0.8313 0.5684 -0.0389 -0.0241 0.0072  468 PHE C CD1 
12073 C CD2 . PHE C 468 ? 0.6345 0.7877 0.4841 -0.0033 -0.0247 0.0040  468 PHE C CD2 
12074 C CE1 . PHE C 468 ? 0.7116 0.8171 0.5600 -0.0452 -0.0270 0.0044  468 PHE C CE1 
12075 C CE2 . PHE C 468 ? 0.7470 0.8954 0.5936 -0.0109 -0.0278 -0.0011 468 PHE C CE2 
12076 C CZ  . PHE C 468 ? 0.6908 0.8153 0.5395 -0.0323 -0.0311 0.0003  468 PHE C CZ  
12077 N N   . ARG C 469 ? 0.7141 0.9367 0.6125 -0.0116 -0.0157 0.0352  469 ARG C N   
12078 C CA  . ARG C 469 ? 0.6373 0.9034 0.5615 -0.0107 -0.0119 0.0407  469 ARG C CA  
12079 C C   . ARG C 469 ? 0.6896 0.9615 0.6285 -0.0276 -0.0101 0.0492  469 ARG C C   
12080 O O   . ARG C 469 ? 0.6765 0.9676 0.6372 -0.0346 -0.0067 0.0506  469 ARG C O   
12081 C CB  . ARG C 469 ? 0.4713 0.7754 0.4051 0.0098  -0.0140 0.0486  469 ARG C CB  
12082 C CG  . ARG C 469 ? 0.5996 0.8943 0.5145 0.0299  -0.0115 0.0359  469 ARG C CG  
12083 C CD  . ARG C 469 ? 0.6926 1.0245 0.6178 0.0547  -0.0069 0.0428  469 ARG C CD  
12084 N NE  . ARG C 469 ? 0.7516 1.0609 0.6511 0.0775  -0.0021 0.0266  469 ARG C NE  
12085 C CZ  . ARG C 469 ? 0.7584 1.0638 0.6341 0.0828  0.0039  0.0133  469 ARG C CZ  
12086 N NH1 . ARG C 469 ? 0.7580 1.0874 0.6383 0.0666  0.0047  0.0172  469 ARG C NH1 
12087 N NH2 . ARG C 469 ? 0.7471 1.0190 0.5908 0.1039  0.0069  -0.0037 469 ARG C NH2 
12088 N N   . SER C 470 ? 0.6293 0.8791 0.5536 -0.0354 -0.0143 0.0550  470 SER C N   
12089 C CA  . SER C 470 ? 0.6279 0.8692 0.5534 -0.0520 -0.0129 0.0600  470 SER C CA  
12090 C C   . SER C 470 ? 0.6461 0.8609 0.5687 -0.0644 0.0032  0.0475  470 SER C C   
12091 O O   . SER C 470 ? 0.6433 0.8637 0.5837 -0.0711 0.0094  0.0477  470 SER C O   
12092 C CB  . SER C 470 ? 0.6960 0.9107 0.5954 -0.0606 -0.0242 0.0695  470 SER C CB  
12093 O OG  . SER C 470 ? 0.9052 1.1240 0.8084 -0.0718 -0.0312 0.0802  470 SER C OG  
12094 N N   . PHE C 471 ? 0.6529 0.8391 0.5569 -0.0675 0.0100  0.0382  471 PHE C N   
12095 C CA  . PHE C 471 ? 0.6268 0.7963 0.5367 -0.0787 0.0282  0.0297  471 PHE C CA  
12096 C C   . PHE C 471 ? 0.6573 0.8588 0.6091 -0.0741 0.0306  0.0295  471 PHE C C   
12097 O O   . PHE C 471 ? 0.7084 0.9137 0.6874 -0.0805 0.0439  0.0284  471 PHE C O   
12098 C CB  . PHE C 471 ? 0.5922 0.7277 0.4740 -0.0861 0.0319  0.0246  471 PHE C CB  
12099 C CG  . PHE C 471 ? 0.6873 0.7852 0.5244 -0.0963 0.0282  0.0267  471 PHE C CG  
12100 C CD1 . PHE C 471 ? 0.8027 0.8811 0.6198 -0.1079 0.0360  0.0270  471 PHE C CD1 
12101 C CD2 . PHE C 471 ? 0.7956 0.8718 0.6072 -0.0956 0.0139  0.0290  471 PHE C CD2 
12102 C CE1 . PHE C 471 ? 0.8414 0.8793 0.6094 -0.1219 0.0287  0.0308  471 PHE C CE1 
12103 C CE2 . PHE C 471 ? 0.8174 0.8574 0.5883 -0.1085 0.0057  0.0345  471 PHE C CE2 
12104 C CZ  . PHE C 471 ? 0.8546 0.8753 0.6014 -0.1232 0.0125  0.0361  471 PHE C CZ  
12105 N N   . VAL C 472 ? 0.6114 0.8329 0.5675 -0.0632 0.0177  0.0309  472 VAL C N   
12106 C CA  . VAL C 472 ? 0.6915 0.9394 0.6794 -0.0629 0.0147  0.0331  472 VAL C CA  
12107 C C   . VAL C 472 ? 0.6915 0.9688 0.7113 -0.0644 0.0141  0.0412  472 VAL C C   
12108 O O   . VAL C 472 ? 0.7200 1.0097 0.7762 -0.0710 0.0166  0.0447  472 VAL C O   
12109 C CB  . VAL C 472 ? 0.6435 0.8993 0.6148 -0.0514 0.0016  0.0311  472 VAL C CB  
12110 C CG1 . VAL C 472 ? 0.6337 0.9249 0.6279 -0.0508 -0.0055 0.0378  472 VAL C CG1 
12111 C CG2 . VAL C 472 ? 0.6239 0.8499 0.5794 -0.0561 -0.0017 0.0246  472 VAL C CG2 
12112 N N   . ARG C 473 ? 0.6269 0.9155 0.6374 -0.0596 0.0079  0.0471  473 ARG C N   
12113 C CA  . ARG C 473 ? 0.6935 1.0066 0.7317 -0.0632 0.0028  0.0571  473 ARG C CA  
12114 C C   . ARG C 473 ? 0.6679 0.9561 0.7176 -0.0723 0.0151  0.0530  473 ARG C C   
12115 O O   . ARG C 473 ? 0.6653 0.9658 0.7528 -0.0757 0.0158  0.0566  473 ARG C O   
12116 C CB  . ARG C 473 ? 0.7181 1.0495 0.7447 -0.0584 -0.0089 0.0683  473 ARG C CB  
12117 C CG  . ARG C 473 ? 0.7144 1.0734 0.7676 -0.0644 -0.0198 0.0826  473 ARG C CG  
12118 C CD  . ARG C 473 ? 0.7317 1.1096 0.7761 -0.0626 -0.0327 0.0982  473 ARG C CD  
12119 N NE  . ARG C 473 ? 0.9473 1.3190 0.9673 -0.0520 -0.0309 0.0959  473 ARG C NE  
12120 C CZ  . ARG C 473 ? 0.9918 1.3923 1.0122 -0.0368 -0.0295 0.0974  473 ARG C CZ  
12121 N NH1 . ARG C 473 ? 0.8805 1.3174 0.9158 -0.0329 -0.0290 0.1009  473 ARG C NH1 
12122 N NH2 . ARG C 473 ? 0.9269 1.3157 0.9296 -0.0255 -0.0286 0.0953  473 ARG C NH2 
12123 N N   . ARG C 474 ? 0.7220 0.9720 0.7376 -0.0763 0.0250  0.0455  474 ARG C N   
12124 C CA  . ARG C 474 ? 0.8017 1.0202 0.8162 -0.0836 0.0421  0.0380  474 ARG C CA  
12125 C C   . ARG C 474 ? 0.6824 0.9047 0.7352 -0.0837 0.0609  0.0325  474 ARG C C   
12126 O O   . ARG C 474 ? 0.7083 0.9252 0.7896 -0.0838 0.0733  0.0301  474 ARG C O   
12127 C CB  . ARG C 474 ? 0.7737 0.9460 0.7330 -0.0911 0.0500  0.0308  474 ARG C CB  
12128 C CG  . ARG C 474 ? 0.8224 0.9551 0.7683 -0.0981 0.0744  0.0191  474 ARG C CG  
12129 C CD  . ARG C 474 ? 0.9792 1.0841 0.8988 -0.1039 0.0657  0.0202  474 ARG C CD  
12130 N NE  . ARG C 474 ? 1.0209 1.0766 0.9143 -0.1090 0.0929  0.0047  474 ARG C NE  
12131 C CZ  . ARG C 474 ? 1.2062 1.2167 1.0584 -0.1168 0.0893  0.0007  474 ARG C CZ  
12132 N NH1 . ARG C 474 ? 1.0783 1.0895 0.9150 -0.1233 0.0562  0.0148  474 ARG C NH1 
12133 N NH2 . ARG C 474 ? 1.2579 1.2200 1.0823 -0.1188 0.1199  -0.0172 474 ARG C NH2 
12134 N N   . ALA C 475 ? 0.6876 0.9187 0.7453 -0.0835 0.0614  0.0323  475 ALA C N   
12135 C CA  . ALA C 475 ? 0.6643 0.9044 0.7652 -0.0865 0.0746  0.0331  475 ALA C CA  
12136 C C   . ALA C 475 ? 0.5763 0.8508 0.7356 -0.0849 0.0638  0.0437  475 ALA C C   
12137 O O   . ALA C 475 ? 0.6086 0.8917 0.8177 -0.0869 0.0757  0.0474  475 ALA C O   
12138 C CB  . ALA C 475 ? 0.6527 0.8908 0.7407 -0.0901 0.0690  0.0337  475 ALA C CB  
12139 N N   . GLN C 476 ? 0.6067 0.9032 0.7645 -0.0823 0.0412  0.0512  476 GLN C N   
12140 C CA  . GLN C 476 ? 0.6141 0.9414 0.8216 -0.0844 0.0264  0.0640  476 GLN C CA  
12141 C C   . GLN C 476 ? 0.6405 0.9639 0.8666 -0.0828 0.0271  0.0660  476 GLN C C   
12142 O O   . GLN C 476 ? 0.6848 1.0322 0.9324 -0.0855 0.0067  0.0785  476 GLN C O   
12143 C CB  . GLN C 476 ? 0.6097 0.9633 0.8006 -0.0852 0.0023  0.0725  476 GLN C CB  
12144 C CG  . GLN C 476 ? 0.6372 0.9811 0.7909 -0.0834 0.0009  0.0659  476 GLN C CG  
12145 C CD  . GLN C 476 ? 0.6832 1.0479 0.8281 -0.0856 -0.0189 0.0729  476 GLN C CD  
12146 O OE1 . GLN C 476 ? 0.8053 1.1673 0.9067 -0.0775 -0.0223 0.0671  476 GLN C OE1 
12147 N NE2 . GLN C 476 ? 0.7239 1.1068 0.9084 -0.0964 -0.0320 0.0856  476 GLN C NE2 
12148 N N   . GLU C 477 ? 0.7143 1.0031 0.9268 -0.0800 0.0495  0.0538  477 GLU C N   
12149 C CA  . GLU C 477 ? 0.6785 0.9487 0.9001 -0.0781 0.0516  0.0520  477 GLU C CA  
12150 C C   . GLU C 477 ? 0.7430 0.9908 0.9965 -0.0722 0.0827  0.0415  477 GLU C C   
12151 O O   . GLU C 477 ? 0.7960 1.0350 1.0441 -0.0717 0.1071  0.0337  477 GLU C O   
12152 C CB  . GLU C 477 ? 0.6389 0.8761 0.7962 -0.0807 0.0485  0.0456  477 GLU C CB  
12153 C CG  . GLU C 477 ? 0.8021 1.0657 0.9365 -0.0841 0.0206  0.0587  477 GLU C CG  
12154 C CD  . GLU C 477 ? 0.8548 1.0887 0.9381 -0.0894 0.0121  0.0590  477 GLU C CD  
12155 O OE1 . GLU C 477 ? 0.9182 1.1161 0.9558 -0.0917 0.0253  0.0480  477 GLU C OE1 
12156 O OE2 . GLU C 477 ? 0.8163 1.0627 0.9046 -0.0942 -0.0109 0.0731  477 GLU C OE2 
12157 N N   . LEU C 478 ? 0.7634 1.0017 1.0515 -0.0673 0.0826  0.0422  478 LEU C N   
12158 C CA  . LEU C 478 ? 0.7516 0.9606 1.0628 -0.0571 0.1181  0.0285  478 LEU C CA  
12159 C C   . LEU C 478 ? 0.8447 0.9964 1.0763 -0.0578 0.1405  0.0078  478 LEU C C   
12160 O O   . LEU C 478 ? 0.9926 1.1213 1.1652 -0.0656 0.1204  0.0071  478 LEU C O   
12161 C CB  . LEU C 478 ? 0.7303 0.9375 1.0994 -0.0492 0.1104  0.0336  478 LEU C CB  
12162 C CG  . LEU C 478 ? 0.7065 0.9625 1.1483 -0.0532 0.0777  0.0579  478 LEU C CG  
12163 C CD1 . LEU C 478 ? 0.6462 0.8846 1.1210 -0.0480 0.0636  0.0614  478 LEU C CD1 
12164 C CD2 . LEU C 478 ? 0.7065 0.9971 1.2222 -0.0505 0.0903  0.0679  478 LEU C CD2 
12165 N N   . GLU C 479 ? 0.7703 0.8992 1.0001 -0.0515 0.1821  -0.0069 479 GLU C N   
12166 C CA  . GLU C 479 ? 1.0232 1.0935 1.1679 -0.0559 0.2054  -0.0265 479 GLU C CA  
12167 C C   . GLU C 479 ? 1.0474 1.0618 1.1742 -0.0464 0.2274  -0.0447 479 GLU C C   
12168 O O   . GLU C 479 ? 1.1649 1.1206 1.2110 -0.0521 0.2473  -0.0625 479 GLU C O   
12169 C CB  . GLU C 479 ? 1.1239 1.1962 1.2567 -0.0589 0.2398  -0.0323 479 GLU C CB  
12170 C CG  . GLU C 479 ? 1.2785 1.3514 1.3517 -0.0745 0.2211  -0.0274 479 GLU C CG  
12171 C CD  . GLU C 479 ? 1.3477 1.3815 1.3427 -0.0847 0.1949  -0.0302 479 GLU C CD  
12172 O OE1 . GLU C 479 ? 1.3667 1.3420 1.2935 -0.0910 0.2120  -0.0449 479 GLU C OE1 
12173 O OE2 . GLU C 479 ? 1.0551 1.1166 1.0556 -0.0876 0.1572  -0.0159 479 GLU C OE2 
12174 N N   . HIS C 480 ? 0.9465 0.9713 1.1410 -0.0332 0.2226  -0.0408 480 HIS C N   
12175 C CA  . HIS C 480 ? 1.0028 0.9699 1.1872 -0.0193 0.2499  -0.0612 480 HIS C CA  
12176 C C   . HIS C 480 ? 1.0437 0.9682 1.1921 -0.0240 0.2140  -0.0616 480 HIS C C   
12177 O O   . HIS C 480 ? 1.1552 1.0225 1.2910 -0.0121 0.2316  -0.0795 480 HIS C O   
12178 C CB  . HIS C 480 ? 0.8484 0.8472 1.1402 0.0025  0.2757  -0.0582 480 HIS C CB  
12179 C CG  . HIS C 480 ? 0.7791 0.7868 1.0901 0.0119  0.3308  -0.0677 480 HIS C CG  
12180 N ND1 . HIS C 480 ? 0.8969 0.8623 1.1194 0.0046  0.3646  -0.0868 480 HIS C ND1 
12181 C CD2 . HIS C 480 ? 0.8082 0.8640 1.2203 0.0263  0.3575  -0.0577 480 HIS C CD2 
12182 C CE1 . HIS C 480 ? 0.9732 0.9630 1.2399 0.0140  0.4120  -0.0884 480 HIS C CE1 
12183 N NE2 . HIS C 480 ? 0.9585 1.0048 1.3437 0.0280  0.4087  -0.0703 480 HIS C NE2 
12184 N N   . HIS C 481 ? 0.8094 0.7595 0.9419 -0.0407 0.1654  -0.0418 481 HIS C N   
12185 C CA  . HIS C 481 ? 0.8343 0.7519 0.9335 -0.0506 0.1255  -0.0353 481 HIS C CA  
12186 C C   . HIS C 481 ? 0.7636 0.6939 0.9410 -0.0397 0.1082  -0.0258 481 HIS C C   
12187 O O   . HIS C 481 ? 0.8637 0.7676 1.0783 -0.0204 0.1381  -0.0409 481 HIS C O   
12188 C CB  . HIS C 481 ? 0.8738 0.6990 0.8734 -0.0564 0.1381  -0.0582 481 HIS C CB  
12189 C CG  . HIS C 481 ? 1.0429 0.8516 0.9573 -0.0793 0.1175  -0.0525 481 HIS C CG  
12190 N ND1 . HIS C 481 ? 1.0287 0.7533 0.8428 -0.0928 0.1169  -0.0668 481 HIS C ND1 
12191 C CD2 . HIS C 481 ? 1.0368 0.8994 0.9523 -0.0909 0.0958  -0.0331 481 HIS C CD2 
12192 C CE1 . HIS C 481 ? 1.0950 0.8270 0.8590 -0.1132 0.0928  -0.0532 481 HIS C CE1 
12193 N NE2 . HIS C 481 ? 0.9704 0.7864 0.7970 -0.1102 0.0816  -0.0336 481 HIS C NE2 
12194 N N   . HIS C 482 ? 0.7086 0.6786 0.9128 -0.0518 0.0606  0.0003  482 HIS C N   
12195 C CA  . HIS C 482 ? 0.6823 0.6804 0.9734 -0.0447 0.0411  0.0156  482 HIS C CA  
12196 C C   . HIS C 482 ? 0.6905 0.7033 0.9770 -0.0633 -0.0135 0.0410  482 HIS C C   
12197 O O   . HIS C 482 ? 0.7328 0.7533 0.9638 -0.0805 -0.0350 0.0511  482 HIS C O   
12198 C CB  . HIS C 482 ? 0.6197 0.6912 0.9909 -0.0394 0.0488  0.0294  482 HIS C CB  
12199 C CG  . HIS C 482 ? 0.6791 0.8051 1.0303 -0.0553 0.0290  0.0460  482 HIS C CG  
12200 N ND1 . HIS C 482 ? 0.6313 0.8112 1.0175 -0.0674 -0.0099 0.0731  482 HIS C ND1 
12201 C CD2 . HIS C 482 ? 0.7091 0.8396 1.0052 -0.0604 0.0430  0.0388  482 HIS C CD2 
12202 C CE1 . HIS C 482 ? 0.7023 0.9168 1.0554 -0.0764 -0.0151 0.0794  482 HIS C CE1 
12203 N NE2 . HIS C 482 ? 0.7582 0.9435 1.0600 -0.0718 0.0149  0.0594  482 HIS C NE2 
12204 N N   . HIS C 483 ? 0.7021 0.7223 1.0540 -0.0602 -0.0363 0.0544  483 HIS C N   
12205 C CA  . HIS C 483 ? 0.6511 0.7004 1.0178 -0.0796 -0.0890 0.0849  483 HIS C CA  
12206 C C   . HIS C 483 ? 0.6835 0.7809 1.1477 -0.0763 -0.1046 0.1049  483 HIS C C   
12207 O O   . HIS C 483 ? 0.5898 0.6904 1.1126 -0.0578 -0.0765 0.0951  483 HIS C O   
12208 C CB  . HIS C 483 ? 0.6990 0.6781 1.0203 -0.0876 -0.1148 0.0829  483 HIS C CB  
12209 C CG  . HIS C 483 ? 0.8352 0.7495 1.1846 -0.0676 -0.1002 0.0633  483 HIS C CG  
12210 N ND1 . HIS C 483 ? 0.8127 0.7447 1.2499 -0.0607 -0.1187 0.0780  483 HIS C ND1 
12211 C CD2 . HIS C 483 ? 0.9922 0.8213 1.2925 -0.0519 -0.0675 0.0296  483 HIS C CD2 
12212 C CE1 . HIS C 483 ? 0.8451 0.7071 1.2929 -0.0385 -0.0972 0.0539  483 HIS C CE1 
12213 N NE2 . HIS C 483 ? 0.9352 0.7327 1.2972 -0.0322 -0.0637 0.0228  483 HIS C NE2 
12214 N N   . HIS C 484 ? 0.6904 0.8273 1.1738 -0.0964 -0.1507 0.1361  484 HIS C N   
12215 C CA  . HIS C 484 ? 0.5837 0.7642 1.1527 -0.0999 -0.1738 0.1600  484 HIS C CA  
12216 C C   . HIS C 484 ? 0.5802 0.7178 1.1884 -0.0987 -0.2019 0.1676  484 HIS C C   
12217 O O   . HIS C 484 ? 0.5736 0.7101 1.2604 -0.0857 -0.1997 0.1701  484 HIS C O   
12218 C CB  . HIS C 484 ? 0.5375 0.7886 1.1028 -0.1244 -0.2060 0.1909  484 HIS C CB  
12219 C CG  . HIS C 484 ? 0.4740 0.7792 1.1032 -0.1276 -0.2106 0.2071  484 HIS C CG  
12220 N ND1 . HIS C 484 ? 0.4845 0.8080 1.1796 -0.1390 -0.2466 0.2340  484 HIS C ND1 
12221 C CD2 . HIS C 484 ? 0.4833 0.8237 1.1172 -0.1241 -0.1884 0.2024  484 HIS C CD2 
12222 C CE1 . HIS C 484 ? 0.4994 0.8437 1.2006 -0.1367 -0.2356 0.2380  484 HIS C CE1 
12223 N NE2 . HIS C 484 ? 0.5130 0.8805 1.1977 -0.1317 -0.2076 0.2232  484 HIS C NE2 
12224 N N   . MET D 1   ? 1.6428 1.1757 1.2232 -0.4582 0.2837  -0.3623 1   MET D N   
12225 C CA  . MET D 1   ? 1.5448 1.0244 1.1389 -0.4330 0.3081  -0.3507 1   MET D CA  
12226 C C   . MET D 1   ? 1.6072 1.0859 1.2190 -0.4005 0.2954  -0.3122 1   MET D C   
12227 O O   . MET D 1   ? 1.6696 1.1841 1.2860 -0.3995 0.2721  -0.2979 1   MET D O   
12228 C CB  . MET D 1   ? 1.5676 1.0401 1.1464 -0.4244 0.3151  -0.3574 1   MET D CB  
12229 C CG  . MET D 1   ? 1.7125 1.2352 1.2721 -0.4164 0.2837  -0.3436 1   MET D CG  
12230 S SD  . MET D 1   ? 1.9195 1.4359 1.4589 -0.4102 0.2936  -0.3537 1   MET D SD  
12231 C CE  . MET D 1   ? 1.6425 1.0883 1.2079 -0.3947 0.3351  -0.3593 1   MET D CE  
12232 N N   . LYS D 2   ? 1.5641 1.0035 1.1874 -0.3745 0.3111  -0.2961 2   LYS D N   
12233 C CA  . LYS D 2   ? 1.4269 0.8649 1.0640 -0.3432 0.3004  -0.2598 2   LYS D CA  
12234 C C   . LYS D 2   ? 1.4694 0.9203 1.0989 -0.3196 0.2893  -0.2462 2   LYS D C   
12235 O O   . LYS D 2   ? 1.4531 0.8736 1.0852 -0.3097 0.3079  -0.2508 2   LYS D O   
12236 C CB  . LYS D 2   ? 1.4293 0.8140 1.0874 -0.3318 0.3252  -0.2479 2   LYS D CB  
12237 C CG  . LYS D 2   ? 1.4540 0.8404 1.1236 -0.3321 0.3202  -0.2302 2   LYS D CG  
12238 C CD  . LYS D 2   ? 1.4753 0.8248 1.1608 -0.3056 0.3310  -0.2002 2   LYS D CD  
12239 C CE  . LYS D 2   ? 1.5817 0.9240 1.2768 -0.3112 0.3331  -0.1860 2   LYS D CE  
12240 N NZ  . LYS D 2   ? 1.5559 0.8754 1.2613 -0.2848 0.3357  -0.1507 2   LYS D NZ  
12241 N N   . LYS D 3   ? 1.4633 0.9587 1.0865 -0.3108 0.2604  -0.2300 3   LYS D N   
12242 C CA  . LYS D 3   ? 1.4450 0.9569 1.0613 -0.2895 0.2476  -0.2157 3   LYS D CA  
12243 C C   . LYS D 3   ? 1.4470 0.9657 1.0776 -0.2621 0.2346  -0.1829 3   LYS D C   
12244 O O   . LYS D 3   ? 1.3815 0.9164 1.0201 -0.2645 0.2234  -0.1729 3   LYS D O   
12245 C CB  . LYS D 3   ? 1.3193 0.8786 0.9152 -0.3034 0.2245  -0.2248 3   LYS D CB  
12246 C CG  . LYS D 3   ? 1.4090 0.9643 0.9840 -0.3202 0.2360  -0.2509 3   LYS D CG  
12247 C CD  . LYS D 3   ? 1.4609 1.0602 1.0145 -0.3474 0.2164  -0.2660 3   LYS D CD  
12248 C CE  . LYS D 3   ? 1.4747 1.0791 1.0016 -0.3615 0.2228  -0.2864 3   LYS D CE  
12249 N NZ  . LYS D 3   ? 1.3891 1.0395 0.8981 -0.3600 0.1938  -0.2736 3   LYS D NZ  
12250 N N   . LEU D 4   ? 1.3681 0.8754 1.0026 -0.2374 0.2373  -0.1675 4   LEU D N   
12251 C CA  . LEU D 4   ? 1.2759 0.7952 0.9209 -0.2122 0.2233  -0.1377 4   LEU D CA  
12252 C C   . LEU D 4   ? 1.3219 0.8871 0.9569 -0.2091 0.1973  -0.1326 4   LEU D C   
12253 O O   . LEU D 4   ? 1.3803 0.9523 1.0064 -0.2021 0.1948  -0.1343 4   LEU D O   
12254 C CB  . LEU D 4   ? 1.3140 0.8020 0.9707 -0.1880 0.2375  -0.1230 4   LEU D CB  
12255 C CG  . LEU D 4   ? 1.3431 0.8437 1.0095 -0.1628 0.2241  -0.0924 4   LEU D CG  
12256 C CD1 . LEU D 4   ? 1.3257 0.7879 1.0088 -0.1453 0.2413  -0.0761 4   LEU D CD1 
12257 C CD2 . LEU D 4   ? 1.2334 0.7643 0.8936 -0.1492 0.2076  -0.0861 4   LEU D CD2 
12258 N N   . PHE D 5   ? 1.2998 0.8962 0.9380 -0.2153 0.1788  -0.1272 5   PHE D N   
12259 C CA  . PHE D 5   ? 1.2733 0.9118 0.9081 -0.2104 0.1537  -0.1190 5   PHE D CA  
12260 C C   . PHE D 5   ? 1.1879 0.8291 0.8314 -0.1831 0.1478  -0.0955 5   PHE D C   
12261 O O   . PHE D 5   ? 1.1673 0.8022 0.8235 -0.1726 0.1495  -0.0808 5   PHE D O   
12262 C CB  . PHE D 5   ? 1.2029 0.8730 0.8457 -0.2237 0.1373  -0.1203 5   PHE D CB  
12263 C CG  . PHE D 5   ? 1.2146 0.8901 0.8492 -0.2521 0.1394  -0.1436 5   PHE D CG  
12264 C CD1 . PHE D 5   ? 1.2730 0.9380 0.8883 -0.2654 0.1486  -0.1623 5   PHE D CD1 
12265 C CD2 . PHE D 5   ? 1.2550 0.9487 0.9017 -0.2668 0.1327  -0.1483 5   PHE D CD2 
12266 C CE1 . PHE D 5   ? 1.3459 1.0187 0.9519 -0.2940 0.1503  -0.1854 5   PHE D CE1 
12267 C CE2 . PHE D 5   ? 1.3223 1.0243 0.9624 -0.2942 0.1337  -0.1705 5   PHE D CE2 
12268 C CZ  . PHE D 5   ? 1.3234 1.0153 0.9421 -0.3082 0.1421  -0.1891 5   PHE D CZ  
12269 N N   . LEU D 6   ? 1.2332 0.8848 0.8689 -0.1733 0.1414  -0.0924 6   LEU D N   
12270 C CA  . LEU D 6   ? 1.2241 0.8791 0.8676 -0.1488 0.1369  -0.0728 6   LEU D CA  
12271 C C   . LEU D 6   ? 1.1973 0.8909 0.8402 -0.1453 0.1139  -0.0652 6   LEU D C   
12272 O O   . LEU D 6   ? 1.1484 0.8583 0.7785 -0.1569 0.1055  -0.0745 6   LEU D O   
12273 C CB  . LEU D 6   ? 1.1868 0.8172 0.8261 -0.1385 0.1527  -0.0754 6   LEU D CB  
12274 C CG  . LEU D 6   ? 1.1499 0.7885 0.7955 -0.1154 0.1473  -0.0587 6   LEU D CG  
12275 C CD1 . LEU D 6   ? 1.2046 0.8457 0.8656 -0.0994 0.1425  -0.0378 6   LEU D CD1 
12276 C CD2 . LEU D 6   ? 1.1120 0.7242 0.7581 -0.1077 0.1663  -0.0647 6   LEU D CD2 
12277 N N   . VAL D 7   ? 1.1143 0.8224 0.7712 -0.1303 0.1041  -0.0482 7   VAL D N   
12278 C CA  . VAL D 7   ? 1.0879 0.8296 0.7502 -0.1246 0.0841  -0.0397 7   VAL D CA  
12279 C C   . VAL D 7   ? 1.0848 0.8253 0.7512 -0.1035 0.0848  -0.0260 7   VAL D C   
12280 O O   . VAL D 7   ? 1.0894 0.8198 0.7647 -0.0915 0.0912  -0.0157 7   VAL D O   
12281 C CB  . VAL D 7   ? 0.9684 0.7327 0.6477 -0.1280 0.0724  -0.0353 7   VAL D CB  
12282 C CG1 . VAL D 7   ? 0.9193 0.7162 0.6090 -0.1217 0.0529  -0.0271 7   VAL D CG1 
12283 C CG2 . VAL D 7   ? 0.9309 0.6972 0.6092 -0.1492 0.0727  -0.0493 7   VAL D CG2 
12284 N N   . PHE D 8   ? 1.0217 0.7736 0.6807 -0.1003 0.0781  -0.0254 8   PHE D N   
12285 C CA  . PHE D 8   ? 0.9939 0.7508 0.6584 -0.0821 0.0765  -0.0136 8   PHE D CA  
12286 C C   . PHE D 8   ? 0.9874 0.7751 0.6639 -0.0784 0.0580  -0.0046 8   PHE D C   
12287 O O   . PHE D 8   ? 1.0532 0.8582 0.7261 -0.0880 0.0457  -0.0071 8   PHE D O   
12288 C CB  . PHE D 8   ? 1.0721 0.8211 0.7224 -0.0819 0.0834  -0.0196 8   PHE D CB  
12289 C CG  . PHE D 8   ? 1.0551 0.7747 0.7053 -0.0743 0.1036  -0.0231 8   PHE D CG  
12290 C CD1 . PHE D 8   ? 1.1510 0.8657 0.8152 -0.0550 0.1078  -0.0101 8   PHE D CD1 
12291 C CD2 . PHE D 8   ? 0.9946 0.6924 0.6327 -0.0869 0.1185  -0.0396 8   PHE D CD2 
12292 C CE1 . PHE D 8   ? 1.1743 0.8629 0.8438 -0.0463 0.1254  -0.0111 8   PHE D CE1 
12293 C CE2 . PHE D 8   ? 1.1086 0.7777 0.7524 -0.0788 0.1384  -0.0430 8   PHE D CE2 
12294 C CZ  . PHE D 8   ? 1.1593 0.8237 0.8204 -0.0575 0.1414  -0.0275 8   PHE D CZ  
12295 N N   . TRP D 9   ? 1.0153 0.8102 0.7066 -0.0652 0.0561  0.0061  9   TRP D N   
12296 C CA  . TRP D 9   ? 0.9775 0.7995 0.6846 -0.0611 0.0415  0.0129  9   TRP D CA  
12297 C C   . TRP D 9   ? 0.9121 0.7385 0.6247 -0.0452 0.0426  0.0221  9   TRP D C   
12298 O O   . TRP D 9   ? 0.9578 0.7776 0.6742 -0.0363 0.0499  0.0274  9   TRP D O   
12299 C CB  . TRP D 9   ? 0.9982 0.8299 0.7206 -0.0651 0.0388  0.0128  9   TRP D CB  
12300 C CG  . TRP D 9   ? 0.9094 0.7687 0.6520 -0.0658 0.0245  0.0147  9   TRP D CG  
12301 C CD1 . TRP D 9   ? 0.9106 0.7852 0.6606 -0.0607 0.0139  0.0197  9   TRP D CD1 
12302 C CD2 . TRP D 9   ? 0.9296 0.8036 0.6914 -0.0718 0.0206  0.0116  9   TRP D CD2 
12303 N NE1 . TRP D 9   ? 0.9129 0.8095 0.6878 -0.0621 0.0035  0.0204  9   TRP D NE1 
12304 C CE2 . TRP D 9   ? 0.9294 0.8272 0.7128 -0.0688 0.0077  0.0145  9   TRP D CE2 
12305 C CE3 . TRP D 9   ? 0.9268 0.7958 0.6914 -0.0799 0.0279  0.0063  9   TRP D CE3 
12306 C CZ2 . TRP D 9   ? 0.9014 0.8188 0.7117 -0.0728 0.0023  0.0111  9   TRP D CZ2 
12307 C CZ3 . TRP D 9   ? 0.9126 0.8024 0.7009 -0.0851 0.0227  0.0025  9   TRP D CZ3 
12308 C CH2 . TRP D 9   ? 0.8960 0.8102 0.7084 -0.0810 0.0102  0.0043  9   TRP D CH2 
12309 N N   . TRP D 10  ? 0.9047 0.7430 0.6174 -0.0425 0.0351  0.0246  10  TRP D N   
12310 C CA  . TRP D 10  ? 0.9340 0.7788 0.6528 -0.0293 0.0358  0.0316  10  TRP D CA  
12311 C C   . TRP D 10  ? 0.9059 0.7742 0.6448 -0.0263 0.0245  0.0363  10  TRP D C   
12312 O O   . TRP D 10  ? 0.9147 0.7947 0.6599 -0.0327 0.0138  0.0363  10  TRP D O   
12313 C CB  . TRP D 10  ? 0.9279 0.7681 0.6335 -0.0293 0.0382  0.0303  10  TRP D CB  
12314 C CG  . TRP D 10  ? 1.0210 0.8383 0.7091 -0.0334 0.0517  0.0223  10  TRP D CG  
12315 C CD1 . TRP D 10  ? 1.0692 0.8787 0.7399 -0.0479 0.0531  0.0128  10  TRP D CD1 
12316 C CD2 . TRP D 10  ? 1.0075 0.8072 0.6962 -0.0234 0.0661  0.0223  10  TRP D CD2 
12317 N NE1 . TRP D 10  ? 1.0694 0.8560 0.7301 -0.0483 0.0697  0.0045  10  TRP D NE1 
12318 C CE2 . TRP D 10  ? 1.0646 0.8439 0.7383 -0.0322 0.0778  0.0111  10  TRP D CE2 
12319 C CE3 . TRP D 10  ? 1.0097 0.8104 0.7117 -0.0083 0.0700  0.0311  10  TRP D CE3 
12320 C CZ2 . TRP D 10  ? 1.0897 0.8472 0.7654 -0.0248 0.0944  0.0083  10  TRP D CZ2 
12321 C CZ3 . TRP D 10  ? 1.0156 0.7967 0.7186 -0.0005 0.0840  0.0310  10  TRP D CZ3 
12322 C CH2 . TRP D 10  ? 1.1122 0.8708 0.8042 -0.0079 0.0966  0.0196  10  TRP D CH2 
12323 N N   . HIS D 11  ? 0.8721 0.7478 0.6222 -0.0170 0.0270  0.0403  11  HIS D N   
12324 C CA  . HIS D 11  ? 0.8026 0.6996 0.5738 -0.0150 0.0197  0.0416  11  HIS D CA  
12325 C C   . HIS D 11  ? 0.8914 0.7973 0.6681 -0.0073 0.0178  0.0456  11  HIS D C   
12326 O O   . HIS D 11  ? 0.9575 0.8598 0.7282 0.0006  0.0243  0.0483  11  HIS D O   
12327 C CB  . HIS D 11  ? 0.7455 0.6481 0.5235 -0.0133 0.0243  0.0414  11  HIS D CB  
12328 C CG  . HIS D 11  ? 0.7356 0.6599 0.5334 -0.0103 0.0210  0.0406  11  HIS D CG  
12329 N ND1 . HIS D 11  ? 0.7903 0.7290 0.6095 -0.0156 0.0155  0.0353  11  HIS D ND1 
12330 C CD2 . HIS D 11  ? 0.8059 0.7409 0.6075 -0.0032 0.0233  0.0430  11  HIS D CD2 
12331 C CE1 . HIS D 11  ? 0.7703 0.7256 0.6054 -0.0124 0.0160  0.0331  11  HIS D CE1 
12332 N NE2 . HIS D 11  ? 0.8221 0.7763 0.6451 -0.0057 0.0203  0.0375  11  HIS D NE2 
12333 N N   . MET D 12  ? 0.7693 0.6869 0.5598 -0.0095 0.0090  0.0466  12  MET D N   
12334 C CA  . MET D 12  ? 0.7831 0.7079 0.5800 -0.0042 0.0075  0.0503  12  MET D CA  
12335 C C   . MET D 12  ? 0.7654 0.7078 0.5902 -0.0026 0.0034  0.0490  12  MET D C   
12336 O O   . MET D 12  ? 0.8268 0.7756 0.6688 -0.0071 -0.0041 0.0489  12  MET D O   
12337 C CB  . MET D 12  ? 0.7839 0.7035 0.5702 -0.0093 0.0021  0.0545  12  MET D CB  
12338 C CG  . MET D 12  ? 0.7921 0.6993 0.5556 -0.0077 0.0104  0.0545  12  MET D CG  
12339 S SD  . MET D 12  ? 0.9236 0.8109 0.6641 -0.0120 0.0191  0.0482  12  MET D SD  
12340 C CE  . MET D 12  ? 0.9843 0.8601 0.7053 -0.0108 0.0297  0.0462  12  MET D CE  
12341 N N   . HIS D 13  ? 0.7234 0.6750 0.5551 0.0033  0.0086  0.0474  13  HIS D N   
12342 C CA  . HIS D 13  ? 0.7374 0.7059 0.5956 0.0032  0.0077  0.0425  13  HIS D CA  
12343 C C   . HIS D 13  ? 0.7498 0.7277 0.6123 0.0083  0.0118  0.0421  13  HIS D C   
12344 O O   . HIS D 13  ? 0.7571 0.7333 0.6039 0.0130  0.0164  0.0443  13  HIS D O   
12345 C CB  . HIS D 13  ? 0.7006 0.6768 0.5641 -0.0002 0.0111  0.0357  13  HIS D CB  
12346 C CG  . HIS D 13  ? 0.7049 0.7002 0.5906 -0.0012 0.0144  0.0274  13  HIS D CG  
12347 N ND1 . HIS D 13  ? 0.6882 0.6919 0.6042 -0.0034 0.0120  0.0223  13  HIS D ND1 
12348 C CD2 . HIS D 13  ? 0.6964 0.7048 0.5791 -0.0014 0.0201  0.0229  13  HIS D CD2 
12349 C CE1 . HIS D 13  ? 0.6882 0.7083 0.6192 -0.0055 0.0181  0.0122  13  HIS D CE1 
12350 N NE2 . HIS D 13  ? 0.6862 0.7109 0.5953 -0.0052 0.0224  0.0124  13  HIS D NE2 
12351 N N   . GLN D 14  ? 0.7073 0.6951 0.5939 0.0075  0.0102  0.0393  14  GLN D N   
12352 C CA  . GLN D 14  ? 0.6746 0.6754 0.5713 0.0098  0.0148  0.0354  14  GLN D CA  
12353 C C   . GLN D 14  ? 0.6835 0.6991 0.6096 0.0056  0.0168  0.0247  14  GLN D C   
12354 O O   . GLN D 14  ? 0.7450 0.7576 0.6924 0.0032  0.0132  0.0242  14  GLN D O   
12355 C CB  . GLN D 14  ? 0.7356 0.7307 0.6330 0.0116  0.0138  0.0417  14  GLN D CB  
12356 C CG  . GLN D 14  ? 0.8009 0.7857 0.6715 0.0152  0.0160  0.0482  14  GLN D CG  
12357 C CD  . GLN D 14  ? 0.7593 0.7528 0.6209 0.0203  0.0215  0.0456  14  GLN D CD  
12358 O OE1 . GLN D 14  ? 0.7111 0.7223 0.5856 0.0206  0.0237  0.0399  14  GLN D OE1 
12359 N NE2 . GLN D 14  ? 0.7690 0.7507 0.6098 0.0239  0.0237  0.0498  14  GLN D NE2 
12360 N N   . PRO D 15  ? 0.6735 0.7064 0.6034 0.0039  0.0225  0.0157  15  PRO D N   
12361 C CA  . PRO D 15  ? 0.6473 0.6951 0.6064 -0.0021 0.0271  0.0019  15  PRO D CA  
12362 C C   . PRO D 15  ? 0.6583 0.7042 0.6432 -0.0017 0.0277  0.0010  15  PRO D C   
12363 O O   . PRO D 15  ? 0.6354 0.6716 0.6122 0.0023  0.0249  0.0111  15  PRO D O   
12364 C CB  . PRO D 15  ? 0.6165 0.6848 0.5656 -0.0054 0.0325  -0.0061 15  PRO D CB  
12365 C CG  . PRO D 15  ? 0.7199 0.7846 0.6448 0.0016  0.0299  0.0054  15  PRO D CG  
12366 C CD  . PRO D 15  ? 0.6996 0.7408 0.6084 0.0067  0.0251  0.0175  15  PRO D CD  
12367 N N   . LEU D 16  ? 0.7395 0.7942 0.7572 -0.0067 0.0328  -0.0117 16  LEU D N   
12368 C CA  . LEU D 16  ? 0.7435 0.7935 0.7921 -0.0067 0.0345  -0.0123 16  LEU D CA  
12369 C C   . LEU D 16  ? 0.5747 0.6367 0.6239 -0.0093 0.0412  -0.0197 16  LEU D C   
12370 O O   . LEU D 16  ? 0.6288 0.7089 0.6915 -0.0162 0.0495  -0.0371 16  LEU D O   
12371 C CB  . LEU D 16  ? 0.6389 0.6923 0.7285 -0.0105 0.0391  -0.0243 16  LEU D CB  
12372 C CG  . LEU D 16  ? 0.5754 0.6195 0.7020 -0.0092 0.0403  -0.0216 16  LEU D CG  
12373 C CD1 . LEU D 16  ? 0.6099 0.6347 0.7267 -0.0027 0.0282  0.0021  16  LEU D CD1 
12374 C CD2 . LEU D 16  ? 0.5656 0.6133 0.7395 -0.0120 0.0468  -0.0352 16  LEU D CD2 
12375 N N   . TYR D 17  ? 0.5912 0.6450 0.6266 -0.0052 0.0382  -0.0079 17  TYR D N   
12376 C CA  . TYR D 17  ? 0.6433 0.7092 0.6802 -0.0077 0.0442  -0.0140 17  TYR D CA  
12377 C C   . TYR D 17  ? 0.6998 0.7619 0.7720 -0.0118 0.0502  -0.0195 17  TYR D C   
12378 O O   . TYR D 17  ? 0.6154 0.6860 0.6916 -0.0149 0.0557  -0.0245 17  TYR D O   
12379 C CB  . TYR D 17  ? 0.5695 0.6293 0.5781 -0.0020 0.0405  -0.0003 17  TYR D CB  
12380 C CG  . TYR D 17  ? 0.5702 0.6317 0.5471 0.0028  0.0363  0.0054  17  TYR D CG  
12381 C CD1 . TYR D 17  ? 0.5668 0.6478 0.5363 0.0008  0.0379  -0.0031 17  TYR D CD1 
12382 C CD2 . TYR D 17  ? 0.5897 0.6331 0.5441 0.0083  0.0313  0.0194  17  TYR D CD2 
12383 C CE1 . TYR D 17  ? 0.5706 0.6507 0.5136 0.0057  0.0343  0.0046  17  TYR D CE1 
12384 C CE2 . TYR D 17  ? 0.6224 0.6645 0.5515 0.0127  0.0293  0.0238  17  TYR D CE2 
12385 C CZ  . TYR D 17  ? 0.5771 0.6364 0.5018 0.0122  0.0306  0.0175  17  TYR D CZ  
12386 O OH  . TYR D 17  ? 0.5955 0.6509 0.4974 0.0170  0.0288  0.0244  17  TYR D OH  
12387 N N   . ARG D 18  ? 0.6357 0.6853 0.7362 -0.0116 0.0495  -0.0181 18  ARG D N   
12388 C CA  . ARG D 18  ? 0.6092 0.6502 0.7469 -0.0142 0.0550  -0.0198 18  ARG D CA  
12389 C C   . ARG D 18  ? 0.6113 0.6676 0.7821 -0.0223 0.0674  -0.0449 18  ARG D C   
12390 O O   . ARG D 18  ? 0.6687 0.7285 0.8559 -0.0235 0.0692  -0.0542 18  ARG D O   
12391 C CB  . ARG D 18  ? 0.6679 0.6877 0.8232 -0.0090 0.0468  -0.0025 18  ARG D CB  
12392 C CG  . ARG D 18  ? 0.7245 0.7320 0.9207 -0.0105 0.0518  0.0002  18  ARG D CG  
12393 C CD  . ARG D 18  ? 0.6874 0.6786 0.9096 -0.0051 0.0427  0.0165  18  ARG D CD  
12394 N NE  . ARG D 18  ? 0.7974 0.7714 1.0484 -0.0048 0.0434  0.0301  18  ARG D NE  
12395 C CZ  . ARG D 18  ? 0.7756 0.7451 1.0771 -0.0067 0.0538  0.0201  18  ARG D CZ  
12396 N NH1 . ARG D 18  ? 0.7585 0.7411 1.0877 -0.0102 0.0654  -0.0062 18  ARG D NH1 
12397 N NH2 . ARG D 18  ? 0.6813 0.6321 1.0067 -0.0059 0.0533  0.0369  18  ARG D NH2 
12398 N N   . GLU D 19  ? 0.7443 0.8108 0.9254 -0.0292 0.0769  -0.0574 19  GLU D N   
12399 C CA  . GLU D 19  ? 0.6909 0.7728 0.9032 -0.0395 0.0905  -0.0841 19  GLU D CA  
12400 C C   . GLU D 19  ? 0.7463 0.8102 1.0080 -0.0385 0.0958  -0.0863 19  GLU D C   
12401 O O   . GLU D 19  ? 0.7381 0.7798 1.0157 -0.0329 0.0921  -0.0685 19  GLU D O   
12402 C CB  . GLU D 19  ? 0.7035 0.7997 0.9183 -0.0483 0.0993  -0.0968 19  GLU D CB  
12403 C CG  . GLU D 19  ? 0.7916 0.9186 1.0096 -0.0616 0.1097  -0.1256 19  GLU D CG  
12404 C CD  . GLU D 19  ? 0.8357 0.9621 1.1020 -0.0724 0.1263  -0.1493 19  GLU D CD  
12405 O OE1 . GLU D 19  ? 0.8653 0.9654 1.1667 -0.0672 0.1289  -0.1417 19  GLU D OE1 
12406 O OE2 . GLU D 19  ? 0.8604 1.0131 1.1304 -0.0865 0.1367  -0.1753 19  GLU D OE2 
12407 N N   . PRO D 20  ? 0.8493 0.9223 1.1376 -0.0438 0.1047  -0.1067 20  PRO D N   
12408 C CA  . PRO D 20  ? 0.7311 0.7867 1.0726 -0.0406 0.1095  -0.1075 20  PRO D CA  
12409 C C   . PRO D 20  ? 0.7665 0.8093 1.1494 -0.0440 0.1205  -0.1123 20  PRO D C   
12410 O O   . PRO D 20  ? 0.8513 0.8700 1.2633 -0.0360 0.1160  -0.0933 20  PRO D O   
12411 C CB  . PRO D 20  ? 0.6889 0.7626 1.0476 -0.0484 0.1206  -0.1346 20  PRO D CB  
12412 C CG  . PRO D 20  ? 0.7637 0.8651 1.0846 -0.0599 0.1254  -0.1520 20  PRO D CG  
12413 C CD  . PRO D 20  ? 0.8068 0.9063 1.0780 -0.0527 0.1102  -0.1280 20  PRO D CD  
12414 N N   . TYR D 21  ? 0.7324 0.7912 1.1188 -0.0566 0.1345  -0.1364 21  TYR D N   
12415 C CA  . TYR D 21  ? 0.7337 0.7803 1.1637 -0.0623 0.1482  -0.1455 21  TYR D CA  
12416 C C   . TYR D 21  ? 0.7869 0.8166 1.2019 -0.0577 0.1407  -0.1205 21  TYR D C   
12417 O O   . TYR D 21  ? 0.8407 0.8438 1.2873 -0.0521 0.1402  -0.1035 21  TYR D O   
12418 C CB  . TYR D 21  ? 0.7281 0.8005 1.1657 -0.0800 0.1663  -0.1825 21  TYR D CB  
12419 C CG  . TYR D 21  ? 0.7475 0.8397 1.1948 -0.0879 0.1757  -0.2096 21  TYR D CG  
12420 C CD1 . TYR D 21  ? 0.7569 0.8740 1.1570 -0.0905 0.1680  -0.2122 21  TYR D CD1 
12421 C CD2 . TYR D 21  ? 0.6455 0.7310 1.1506 -0.0933 0.1935  -0.2324 21  TYR D CD2 
12422 C CE1 . TYR D 21  ? 0.7020 0.8375 1.1080 -0.0996 0.1774  -0.2363 21  TYR D CE1 
12423 C CE2 . TYR D 21  ? 0.6268 0.7316 1.1407 -0.1022 0.2042  -0.2591 21  TYR D CE2 
12424 C CZ  . TYR D 21  ? 0.6814 0.8117 1.1434 -0.1060 0.1959  -0.2607 21  TYR D CZ  
12425 O OH  . TYR D 21  ? 0.7271 0.8772 1.1945 -0.1168 0.2073  -0.2867 21  TYR D OH  
12426 N N   . THR D 22  ? 0.7774 0.8230 1.1455 -0.0603 0.1351  -0.1173 22  THR D N   
12427 C CA  . THR D 22  ? 0.8234 0.8562 1.1767 -0.0581 0.1306  -0.0971 22  THR D CA  
12428 C C   . THR D 22  ? 0.7549 0.7665 1.0859 -0.0450 0.1135  -0.0624 22  THR D C   
12429 O O   . THR D 22  ? 0.6991 0.6942 1.0251 -0.0435 0.1108  -0.0429 22  THR D O   
12430 C CB  . THR D 22  ? 0.7059 0.7652 1.0214 -0.0648 0.1308  -0.1060 22  THR D CB  
12431 O OG1 . THR D 22  ? 0.7554 0.8223 1.0235 -0.0562 0.1159  -0.0905 22  THR D OG1 
12432 C CG2 . THR D 22  ? 0.6823 0.7715 1.0083 -0.0788 0.1435  -0.1406 22  THR D CG2 
12433 N N   . GLY D 23  ? 0.7010 0.7135 1.0179 -0.0373 0.1027  -0.0550 23  GLY D N   
12434 C CA  . GLY D 23  ? 0.7815 0.7771 1.0750 -0.0271 0.0863  -0.0245 23  GLY D CA  
12435 C C   . GLY D 23  ? 0.7978 0.7972 1.0409 -0.0259 0.0791  -0.0113 23  GLY D C   
12436 O O   . GLY D 23  ? 0.8339 0.8168 1.0594 -0.0211 0.0691  0.0137  23  GLY D O   
12437 N N   . GLU D 24  ? 0.8066 0.8288 1.0269 -0.0307 0.0840  -0.0274 24  GLU D N   
12438 C CA  . GLU D 24  ? 0.7918 0.8197 0.9714 -0.0292 0.0796  -0.0178 24  GLU D CA  
12439 C C   . GLU D 24  ? 0.7706 0.8104 0.9135 -0.0237 0.0708  -0.0164 24  GLU D C   
12440 O O   . GLU D 24  ? 0.6837 0.7369 0.8296 -0.0247 0.0716  -0.0301 24  GLU D O   
12441 C CB  . GLU D 24  ? 0.7282 0.7747 0.9122 -0.0379 0.0906  -0.0345 24  GLU D CB  
12442 C CG  . GLU D 24  ? 0.7803 0.8126 0.9976 -0.0445 0.1005  -0.0345 24  GLU D CG  
12443 C CD  . GLU D 24  ? 0.8126 0.8668 1.0418 -0.0557 0.1131  -0.0571 24  GLU D CD  
12444 O OE1 . GLU D 24  ? 0.7349 0.8179 0.9465 -0.0581 0.1125  -0.0718 24  GLU D OE1 
12445 O OE2 . GLU D 24  ? 0.8786 0.9220 1.1356 -0.0627 0.1233  -0.0596 24  GLU D OE2 
12446 N N   . TYR D 25  ? 0.7536 0.7874 0.8620 -0.0187 0.0638  0.0000  25  TYR D N   
12447 C CA  . TYR D 25  ? 0.6791 0.7211 0.7529 -0.0132 0.0568  0.0026  25  TYR D CA  
12448 C C   . TYR D 25  ? 0.6860 0.7522 0.7476 -0.0151 0.0616  -0.0087 25  TYR D C   
12449 O O   . TYR D 25  ? 0.7678 0.8356 0.8193 -0.0150 0.0640  -0.0038 25  TYR D O   
12450 C CB  . TYR D 25  ? 0.7564 0.7799 0.8022 -0.0079 0.0485  0.0235  25  TYR D CB  
12451 C CG  . TYR D 25  ? 0.8333 0.8411 0.8837 -0.0051 0.0397  0.0341  25  TYR D CG  
12452 C CD1 . TYR D 25  ? 0.8343 0.8285 0.9147 -0.0068 0.0384  0.0416  25  TYR D CD1 
12453 C CD2 . TYR D 25  ? 0.8055 0.8127 0.8334 -0.0010 0.0325  0.0371  25  TYR D CD2 
12454 C CE1 . TYR D 25  ? 0.8459 0.8294 0.9346 -0.0038 0.0289  0.0523  25  TYR D CE1 
12455 C CE2 . TYR D 25  ? 0.7470 0.7432 0.7813 0.0005  0.0239  0.0459  25  TYR D CE2 
12456 C CZ  . TYR D 25  ? 0.8531 0.8389 0.9185 -0.0006 0.0215  0.0538  25  TYR D CZ  
12457 O OH  . TYR D 25  ? 0.7889 0.7669 0.8653 0.0014  0.0115  0.0638  25  TYR D OH  
12458 N N   . LEU D 26  ? 0.6300 0.7171 0.6934 -0.0177 0.0630  -0.0236 26  LEU D N   
12459 C CA  . LEU D 26  ? 0.6026 0.7176 0.6582 -0.0206 0.0657  -0.0339 26  LEU D CA  
12460 C C   . LEU D 26  ? 0.6004 0.7193 0.6239 -0.0119 0.0591  -0.0220 26  LEU D C   
12461 O O   . LEU D 26  ? 0.5643 0.7053 0.5832 -0.0121 0.0601  -0.0257 26  LEU D O   
12462 C CB  . LEU D 26  ? 0.6130 0.7510 0.6787 -0.0284 0.0689  -0.0529 26  LEU D CB  
12463 C CG  . LEU D 26  ? 0.6206 0.7559 0.7229 -0.0379 0.0784  -0.0692 26  LEU D CG  
12464 C CD1 . LEU D 26  ? 0.6373 0.8012 0.7452 -0.0487 0.0837  -0.0916 26  LEU D CD1 
12465 C CD2 . LEU D 26  ? 0.6363 0.7661 0.7610 -0.0426 0.0860  -0.0717 26  LEU D CD2 
12466 N N   . LEU D 27  ? 0.5694 0.6685 0.5737 -0.0046 0.0528  -0.0085 27  LEU D N   
12467 C CA  . LEU D 27  ? 0.5709 0.6691 0.5478 0.0038  0.0486  0.0020  27  LEU D CA  
12468 C C   . LEU D 27  ? 0.6576 0.7284 0.6202 0.0080  0.0464  0.0162  27  LEU D C   
12469 O O   . LEU D 27  ? 0.6705 0.7237 0.6361 0.0065  0.0431  0.0209  27  LEU D O   
12470 C CB  . LEU D 27  ? 0.5686 0.6741 0.5311 0.0066  0.0437  0.0017  27  LEU D CB  
12471 C CG  . LEU D 27  ? 0.6544 0.7917 0.6181 0.0037  0.0437  -0.0073 27  LEU D CG  
12472 C CD1 . LEU D 27  ? 0.6097 0.7513 0.5538 0.0070  0.0385  -0.0023 27  LEU D CD1 
12473 C CD2 . LEU D 27  ? 0.6413 0.7954 0.6064 0.0065  0.0451  -0.0060 27  LEU D CD2 
12474 N N   . PRO D 28  ? 0.7037 0.7722 0.6514 0.0123  0.0484  0.0227  28  PRO D N   
12475 C CA  . PRO D 28  ? 0.6863 0.7311 0.6174 0.0132  0.0479  0.0342  28  PRO D CA  
12476 C C   . PRO D 28  ? 0.7442 0.7754 0.6520 0.0183  0.0433  0.0407  28  PRO D C   
12477 O O   . PRO D 28  ? 0.7728 0.7872 0.6630 0.0178  0.0438  0.0483  28  PRO D O   
12478 C CB  . PRO D 28  ? 0.7579 0.8101 0.6863 0.0142  0.0552  0.0341  28  PRO D CB  
12479 C CG  . PRO D 28  ? 0.7151 0.7913 0.6475 0.0198  0.0553  0.0276  28  PRO D CG  
12480 C CD  . PRO D 28  ? 0.6840 0.7742 0.6320 0.0156  0.0517  0.0190  28  PRO D CD  
12481 N N   . TRP D 29  ? 0.7482 0.7863 0.6547 0.0212  0.0397  0.0373  29  TRP D N   
12482 C CA  . TRP D 29  ? 0.6985 0.7250 0.5838 0.0261  0.0373  0.0425  29  TRP D CA  
12483 C C   . TRP D 29  ? 0.7799 0.7842 0.6536 0.0225  0.0333  0.0488  29  TRP D C   
12484 O O   . TRP D 29  ? 0.8570 0.8474 0.7102 0.0241  0.0341  0.0532  29  TRP D O   
12485 C CB  . TRP D 29  ? 0.7593 0.7973 0.6458 0.0279  0.0343  0.0388  29  TRP D CB  
12486 C CG  . TRP D 29  ? 0.7449 0.8059 0.6356 0.0320  0.0360  0.0363  29  TRP D CG  
12487 C CD1 . TRP D 29  ? 0.6949 0.7794 0.5964 0.0285  0.0346  0.0293  29  TRP D CD1 
12488 C CD2 . TRP D 29  ? 0.8469 0.9121 0.7326 0.0398  0.0391  0.0409  29  TRP D CD2 
12489 N NE1 . TRP D 29  ? 0.7762 0.8810 0.6782 0.0335  0.0345  0.0311  29  TRP D NE1 
12490 C CE2 . TRP D 29  ? 0.8583 0.9513 0.7533 0.0416  0.0373  0.0386  29  TRP D CE2 
12491 C CE3 . TRP D 29  ? 0.7386 0.7880 0.6141 0.0448  0.0439  0.0458  29  TRP D CE3 
12492 C CZ2 . TRP D 29  ? 0.8549 0.9610 0.7530 0.0499  0.0385  0.0432  29  TRP D CZ2 
12493 C CZ3 . TRP D 29  ? 0.8614 0.9219 0.7412 0.0530  0.0476  0.0480  29  TRP D CZ3 
12494 C CH2 . TRP D 29  ? 0.8341 0.9229 0.7267 0.0564  0.0441  0.0477  29  TRP D CH2 
12495 N N   . THR D 30  ? 0.7978 0.7995 0.6864 0.0172  0.0290  0.0492  30  THR D N   
12496 C CA  . THR D 30  ? 0.8264 0.8114 0.7068 0.0137  0.0225  0.0569  30  THR D CA  
12497 C C   . THR D 30  ? 0.7944 0.7675 0.6575 0.0104  0.0238  0.0652  30  THR D C   
12498 O O   . THR D 30  ? 0.7928 0.7534 0.6346 0.0077  0.0207  0.0703  30  THR D O   
12499 C CB  . THR D 30  ? 0.8363 0.8230 0.7432 0.0101  0.0174  0.0567  30  THR D CB  
12500 O OG1 . THR D 30  ? 0.7276 0.7265 0.6488 0.0111  0.0184  0.0463  30  THR D OG1 
12501 C CG2 . THR D 30  ? 0.7539 0.7272 0.6548 0.0069  0.0084  0.0665  30  THR D CG2 
12502 N N   . PHE D 31  ? 0.8400 0.8178 0.7105 0.0090  0.0293  0.0655  31  PHE D N   
12503 C CA  . PHE D 31  ? 0.9232 0.8909 0.7759 0.0038  0.0320  0.0732  31  PHE D CA  
12504 C C   . PHE D 31  ? 0.8649 0.8285 0.6924 0.0061  0.0388  0.0699  31  PHE D C   
12505 O O   . PHE D 31  ? 0.7682 0.7194 0.5719 0.0006  0.0384  0.0743  31  PHE D O   
12506 C CB  . PHE D 31  ? 0.8267 0.8009 0.6952 0.0009  0.0381  0.0733  31  PHE D CB  
12507 C CG  . PHE D 31  ? 0.8844 0.8522 0.7330 -0.0047 0.0449  0.0783  31  PHE D CG  
12508 C CD1 . PHE D 31  ? 0.9206 0.8756 0.7559 -0.0137 0.0404  0.0913  31  PHE D CD1 
12509 C CD2 . PHE D 31  ? 0.9311 0.9076 0.7753 -0.0018 0.0558  0.0703  31  PHE D CD2 
12510 C CE1 . PHE D 31  ? 0.9084 0.8586 0.7221 -0.0214 0.0479  0.0952  31  PHE D CE1 
12511 C CE2 . PHE D 31  ? 0.8972 0.8688 0.7242 -0.0082 0.0643  0.0727  31  PHE D CE2 
12512 C CZ  . PHE D 31  ? 0.8616 0.8198 0.6714 -0.0189 0.0610  0.0846  31  PHE D CZ  
12513 N N   . PHE D 32  ? 0.8193 0.7941 0.6532 0.0138  0.0452  0.0619  32  PHE D N   
12514 C CA  . PHE D 32  ? 0.8090 0.7799 0.6268 0.0178  0.0534  0.0586  32  PHE D CA  
12515 C C   . PHE D 32  ? 0.8652 0.8215 0.6645 0.0182  0.0508  0.0590  32  PHE D C   
12516 O O   . PHE D 32  ? 0.8709 0.8161 0.6517 0.0164  0.0579  0.0569  32  PHE D O   
12517 C CB  . PHE D 32  ? 0.8356 0.8242 0.6698 0.0273  0.0584  0.0528  32  PHE D CB  
12518 C CG  . PHE D 32  ? 0.8600 0.8639 0.7102 0.0257  0.0638  0.0500  32  PHE D CG  
12519 C CD1 . PHE D 32  ? 0.8215 0.8194 0.6630 0.0196  0.0718  0.0509  32  PHE D CD1 
12520 C CD2 . PHE D 32  ? 0.8675 0.8928 0.7405 0.0284  0.0618  0.0457  32  PHE D CD2 
12521 C CE1 . PHE D 32  ? 0.8362 0.8478 0.6931 0.0170  0.0779  0.0480  32  PHE D CE1 
12522 C CE2 . PHE D 32  ? 0.8736 0.9137 0.7624 0.0254  0.0674  0.0417  32  PHE D CE2 
12523 C CZ  . PHE D 32  ? 0.8041 0.8367 0.6858 0.0201  0.0757  0.0432  32  PHE D CZ  
12524 N N   . HIS D 33  ? 0.8921 0.8483 0.6970 0.0192  0.0424  0.0599  33  HIS D N   
12525 C CA  . HIS D 33  ? 0.8218 0.7645 0.6106 0.0183  0.0405  0.0596  33  HIS D CA  
12526 C C   . HIS D 33  ? 0.8198 0.7508 0.5923 0.0076  0.0346  0.0640  33  HIS D C   
12527 O O   . HIS D 33  ? 0.8054 0.7243 0.5593 0.0038  0.0356  0.0620  33  HIS D O   
12528 C CB  . HIS D 33  ? 0.7675 0.7161 0.5680 0.0222  0.0349  0.0584  33  HIS D CB  
12529 C CG  . HIS D 33  ? 0.9006 0.8566 0.7062 0.0316  0.0400  0.0562  33  HIS D CG  
12530 N ND1 . HIS D 33  ? 0.8628 0.8390 0.6863 0.0360  0.0397  0.0548  33  HIS D ND1 
12531 C CD2 . HIS D 33  ? 0.8805 0.8271 0.6768 0.0370  0.0452  0.0563  33  HIS D CD2 
12532 C CE1 . HIS D 33  ? 0.8171 0.7981 0.6408 0.0439  0.0426  0.0560  33  HIS D CE1 
12533 N NE2 . HIS D 33  ? 0.8512 0.8129 0.6600 0.0454  0.0463  0.0577  33  HIS D NE2 
12534 N N   . ALA D 34  ? 0.8383 0.7731 0.6180 0.0020  0.0284  0.0706  34  ALA D N   
12535 C CA  . ALA D 34  ? 0.8431 0.7698 0.6064 -0.0087 0.0210  0.0782  34  ALA D CA  
12536 C C   . ALA D 34  ? 0.8627 0.7820 0.5989 -0.0160 0.0295  0.0774  34  ALA D C   
12537 O O   . ALA D 34  ? 0.9524 0.8636 0.6645 -0.0252 0.0276  0.0776  34  ALA D O   
12538 C CB  . ALA D 34  ? 0.8662 0.7984 0.6487 -0.0116 0.0115  0.0884  34  ALA D CB  
12539 N N   . VAL D 35  ? 0.8692 0.7929 0.6091 -0.0135 0.0397  0.0749  35  VAL D N   
12540 C CA  . VAL D 35  ? 0.9490 0.8669 0.6647 -0.0212 0.0508  0.0716  35  VAL D CA  
12541 C C   . VAL D 35  ? 0.9763 0.8858 0.6798 -0.0180 0.0612  0.0597  35  VAL D C   
12542 O O   . VAL D 35  ? 0.9958 0.8966 0.6738 -0.0280 0.0683  0.0548  35  VAL D O   
12543 C CB  . VAL D 35  ? 0.8827 0.8093 0.6098 -0.0196 0.0601  0.0711  35  VAL D CB  
12544 C CG1 . VAL D 35  ? 0.9054 0.8382 0.6511 -0.0212 0.0509  0.0819  35  VAL D CG1 
12545 C CG2 . VAL D 35  ? 0.8519 0.7871 0.5988 -0.0062 0.0695  0.0612  35  VAL D CG2 
12546 N N   . LYS D 36  ? 0.9774 0.8892 0.6988 -0.0053 0.0627  0.0551  36  LYS D N   
12547 C CA  . LYS D 36  ? 0.9403 0.8423 0.6557 -0.0004 0.0738  0.0456  36  LYS D CA  
12548 C C   . LYS D 36  ? 0.9723 0.8612 0.6723 -0.0062 0.0690  0.0438  36  LYS D C   
12549 O O   . LYS D 36  ? 1.0675 0.9442 0.7463 -0.0148 0.0771  0.0362  36  LYS D O   
12550 C CB  . LYS D 36  ? 0.9134 0.8241 0.6542 0.0155  0.0765  0.0446  36  LYS D CB  
12551 C CG  . LYS D 36  ? 0.9478 0.8528 0.6918 0.0231  0.0917  0.0369  36  LYS D CG  
12552 C CD  . LYS D 36  ? 0.9013 0.8201 0.6722 0.0386  0.0915  0.0397  36  LYS D CD  
12553 C CE  . LYS D 36  ? 1.0032 0.9258 0.7809 0.0428  0.0791  0.0462  36  LYS D CE  
12554 N NZ  . LYS D 36  ? 0.9965 0.9014 0.7660 0.0446  0.0805  0.0459  36  LYS D NZ  
12555 N N   . ASP D 37  ? 0.9419 0.8341 0.6528 -0.0031 0.0570  0.0489  37  ASP D N   
12556 C CA  . ASP D 37  ? 0.8660 0.7473 0.5681 -0.0065 0.0540  0.0459  37  ASP D CA  
12557 C C   . ASP D 37  ? 0.8744 0.7590 0.5721 -0.0164 0.0391  0.0517  37  ASP D C   
12558 O O   . ASP D 37  ? 0.9535 0.8295 0.6366 -0.0248 0.0376  0.0477  37  ASP D O   
12559 C CB  . ASP D 37  ? 0.9514 0.8331 0.6710 0.0056  0.0549  0.0458  37  ASP D CB  
12560 C CG  . ASP D 37  ? 0.9506 0.8403 0.6866 0.0185  0.0627  0.0461  37  ASP D CG  
12561 O OD1 . ASP D 37  ? 1.0467 0.9272 0.7799 0.0227  0.0752  0.0410  37  ASP D OD1 
12562 O OD2 . ASP D 37  ? 0.7915 0.6976 0.5452 0.0241  0.0566  0.0507  37  ASP D OD2 
12563 N N   . TYR D 38  ? 0.8219 0.7191 0.5347 -0.0159 0.0284  0.0605  38  TYR D N   
12564 C CA  . TYR D 38  ? 0.8913 0.7930 0.6099 -0.0218 0.0138  0.0664  38  TYR D CA  
12565 C C   . TYR D 38  ? 1.0547 0.9537 0.7495 -0.0365 0.0073  0.0702  38  TYR D C   
12566 O O   . TYR D 38  ? 1.0346 0.9352 0.7278 -0.0431 -0.0027 0.0716  38  TYR D O   
12567 C CB  . TYR D 38  ? 0.7853 0.6999 0.5319 -0.0167 0.0054  0.0742  38  TYR D CB  
12568 C CG  . TYR D 38  ? 0.7982 0.7196 0.5673 -0.0057 0.0093  0.0691  38  TYR D CG  
12569 C CD1 . TYR D 38  ? 0.8447 0.7607 0.6085 -0.0011 0.0162  0.0622  38  TYR D CD1 
12570 C CD2 . TYR D 38  ? 0.7584 0.6915 0.5532 -0.0012 0.0067  0.0714  38  TYR D CD2 
12571 C CE1 . TYR D 38  ? 0.8260 0.7504 0.6064 0.0071  0.0188  0.0595  38  TYR D CE1 
12572 C CE2 . TYR D 38  ? 0.7524 0.6947 0.5643 0.0061  0.0105  0.0654  38  TYR D CE2 
12573 C CZ  . TYR D 38  ? 0.8039 0.7429 0.6068 0.0100  0.0157  0.0603  38  TYR D CZ  
12574 O OH  . TYR D 38  ? 0.7865 0.7367 0.6025 0.0156  0.0184  0.0563  38  TYR D OH  
12575 N N   . TYR D 39  ? 0.9568 0.8537 0.6324 -0.0431 0.0128  0.0715  39  TYR D N   
12576 C CA  . TYR D 39  ? 0.9914 0.8868 0.6377 -0.0597 0.0082  0.0734  39  TYR D CA  
12577 C C   . TYR D 39  ? 1.0977 0.9807 0.7187 -0.0664 0.0226  0.0577  39  TYR D C   
12578 O O   . TYR D 39  ? 1.1051 0.9866 0.7052 -0.0802 0.0184  0.0541  39  TYR D O   
12579 C CB  . TYR D 39  ? 1.0165 0.9170 0.6519 -0.0671 0.0061  0.0844  39  TYR D CB  
12580 C CG  . TYR D 39  ? 1.0575 0.9574 0.6545 -0.0866 0.0059  0.0847  39  TYR D CG  
12581 C CD1 . TYR D 39  ? 1.1179 1.0090 0.6891 -0.0938 0.0239  0.0690  39  TYR D CD1 
12582 C CD2 . TYR D 39  ? 1.1685 1.0780 0.7562 -0.0985 -0.0122 0.1008  39  TYR D CD2 
12583 C CE1 . TYR D 39  ? 1.1799 1.0723 0.7137 -0.1143 0.0250  0.0669  39  TYR D CE1 
12584 C CE2 . TYR D 39  ? 1.2574 1.1698 0.8064 -0.1187 -0.0137 0.1019  39  TYR D CE2 
12585 C CZ  . TYR D 39  ? 1.2248 1.1287 0.7451 -0.1276 0.0056  0.0837  39  TYR D CZ  
12586 O OH  . TYR D 39  ? 1.2194 1.1277 0.6989 -0.1503 0.0056  0.0823  39  TYR D OH  
12587 N N   . ASP D 40  ? 1.0877 0.9627 0.7129 -0.0572 0.0397  0.0479  40  ASP D N   
12588 C CA  . ASP D 40  ? 1.0390 0.9004 0.6439 -0.0634 0.0563  0.0323  40  ASP D CA  
12589 C C   . ASP D 40  ? 1.0175 0.8685 0.6225 -0.0641 0.0571  0.0239  40  ASP D C   
12590 O O   . ASP D 40  ? 1.0802 0.9218 0.6630 -0.0772 0.0646  0.0120  40  ASP D O   
12591 C CB  . ASP D 40  ? 1.0222 0.8792 0.6392 -0.0511 0.0738  0.0255  40  ASP D CB  
12592 C CG  . ASP D 40  ? 1.2225 1.0849 0.8263 -0.0585 0.0812  0.0256  40  ASP D CG  
12593 O OD1 . ASP D 40  ? 1.1791 1.0356 0.7562 -0.0732 0.0915  0.0153  40  ASP D OD1 
12594 O OD2 . ASP D 40  ? 1.2810 1.1539 0.9007 -0.0513 0.0775  0.0349  40  ASP D OD2 
12595 N N   . MET D 41  ? 1.0150 0.8675 0.6440 -0.0519 0.0505  0.0288  41  MET D N   
12596 C CA  . MET D 41  ? 1.0487 0.8902 0.6788 -0.0528 0.0528  0.0215  41  MET D CA  
12597 C C   . MET D 41  ? 1.0319 0.8766 0.6449 -0.0703 0.0422  0.0196  41  MET D C   
12598 O O   . MET D 41  ? 1.0268 0.8587 0.6243 -0.0802 0.0513  0.0067  41  MET D O   
12599 C CB  . MET D 41  ? 1.0018 0.8470 0.6590 -0.0381 0.0479  0.0281  41  MET D CB  
12600 C CG  . MET D 41  ? 0.9767 0.8189 0.6490 -0.0220 0.0589  0.0287  41  MET D CG  
12601 S SD  . MET D 41  ? 1.2235 1.0419 0.8939 -0.0173 0.0777  0.0184  41  MET D SD  
12602 C CE  . MET D 41  ? 1.0726 0.8837 0.7441 -0.0224 0.0716  0.0181  41  MET D CE  
12603 N N   . PRO D 42  ? 1.0186 0.8801 0.6354 -0.0753 0.0236  0.0314  42  PRO D N   
12604 C CA  . PRO D 42  ? 0.9678 0.8361 0.5667 -0.0934 0.0125  0.0304  42  PRO D CA  
12605 C C   . PRO D 42  ? 1.0313 0.8991 0.5960 -0.1104 0.0174  0.0251  42  PRO D C   
12606 O O   . PRO D 42  ? 1.0641 0.9365 0.6082 -0.1283 0.0117  0.0200  42  PRO D O   
12607 C CB  . PRO D 42  ? 0.9152 0.8028 0.5344 -0.0909 -0.0087 0.0473  42  PRO D CB  
12608 C CG  . PRO D 42  ? 0.9664 0.8562 0.6027 -0.0766 -0.0065 0.0562  42  PRO D CG  
12609 C CD  . PRO D 42  ? 0.9872 0.8628 0.6286 -0.0646 0.0117  0.0457  42  PRO D CD  
12610 N N   . ALA D 43  ? 1.0468 0.9110 0.6044 -0.1068 0.0285  0.0248  43  ALA D N   
12611 C CA  . ALA D 43  ? 1.0747 0.9388 0.5980 -0.1245 0.0362  0.0179  43  ALA D CA  
12612 C C   . ALA D 43  ? 1.0597 0.9068 0.5659 -0.1333 0.0567  -0.0052 43  ALA D C   
12613 O O   . ALA D 43  ? 1.1151 0.9639 0.5892 -0.1537 0.0620  -0.0151 43  ALA D O   
12614 C CB  . ALA D 43  ? 1.0893 0.9554 0.6131 -0.1184 0.0436  0.0238  43  ALA D CB  
12615 N N   . TYR D 44  ? 1.1176 0.9482 0.6444 -0.1192 0.0690  -0.0141 44  TYR D N   
12616 C CA  . TYR D 44  ? 1.1169 0.9282 0.6328 -0.1270 0.0891  -0.0357 44  TYR D CA  
12617 C C   . TYR D 44  ? 1.1023 0.9170 0.5955 -0.1494 0.0824  -0.0447 44  TYR D C   
12618 O O   . TYR D 44  ? 1.1240 0.9266 0.5980 -0.1642 0.0991  -0.0652 44  TYR D O   
12619 C CB  . TYR D 44  ? 1.0960 0.8895 0.6411 -0.1076 0.0993  -0.0382 44  TYR D CB  
12620 C CG  . TYR D 44  ? 1.0643 0.8512 0.6292 -0.0884 0.1130  -0.0366 44  TYR D CG  
12621 C CD1 . TYR D 44  ? 0.9992 0.7996 0.5838 -0.0726 0.1023  -0.0198 44  TYR D CD1 
12622 C CD2 . TYR D 44  ? 1.1096 0.8777 0.6763 -0.0866 0.1370  -0.0527 44  TYR D CD2 
12623 C CE1 . TYR D 44  ? 1.1061 0.9042 0.7099 -0.0560 0.1135  -0.0185 44  TYR D CE1 
12624 C CE2 . TYR D 44  ? 1.0680 0.8330 0.6570 -0.0684 0.1483  -0.0503 44  TYR D CE2 
12625 C CZ  . TYR D 44  ? 1.0607 0.8421 0.6672 -0.0535 0.1356  -0.0329 44  TYR D CZ  
12626 O OH  . TYR D 44  ? 1.0175 0.7997 0.6472 -0.0364 0.1456  -0.0307 44  TYR D OH  
12627 N N   . LEU D 45  ? 1.0032 0.8353 0.5003 -0.1530 0.0589  -0.0310 45  LEU D N   
12628 C CA  . LEU D 45  ? 1.1349 0.9745 0.6150 -0.1738 0.0501  -0.0385 45  LEU D CA  
12629 C C   . LEU D 45  ? 1.1658 1.0179 0.6064 -0.1996 0.0484  -0.0447 45  LEU D C   
12630 O O   . LEU D 45  ? 1.0762 0.9316 0.4965 -0.2207 0.0481  -0.0584 45  LEU D O   
12631 C CB  . LEU D 45  ? 1.0417 0.9001 0.5422 -0.1692 0.0248  -0.0207 45  LEU D CB  
12632 C CG  . LEU D 45  ? 1.0856 0.9333 0.6184 -0.1523 0.0273  -0.0203 45  LEU D CG  
12633 C CD1 . LEU D 45  ? 1.0977 0.9663 0.6524 -0.1492 0.0040  -0.0050 45  LEU D CD1 
12634 C CD2 . LEU D 45  ? 1.1638 0.9919 0.6901 -0.1614 0.0436  -0.0409 45  LEU D CD2 
12635 N N   . LYS D 46  ? 1.1610 1.0212 0.5890 -0.1999 0.0477  -0.0352 46  LYS D N   
12636 C CA  . LYS D 46  ? 1.1287 1.0012 0.5151 -0.2260 0.0477  -0.0406 46  LYS D CA  
12637 C C   . LYS D 46  ? 1.1295 0.9837 0.4949 -0.2391 0.0771  -0.0707 46  LYS D C   
12638 O O   . LYS D 46  ? 1.1672 1.0289 0.4982 -0.2663 0.0796  -0.0853 46  LYS D O   
12639 C CB  . LYS D 46  ? 1.1129 0.9972 0.4924 -0.2230 0.0408  -0.0215 46  LYS D CB  
12640 C CG  . LYS D 46  ? 1.3029 1.2131 0.6778 -0.2300 0.0101  0.0051  46  LYS D CG  
12641 C CD  . LYS D 46  ? 1.3088 1.2372 0.6375 -0.2622 0.0023  0.0022  46  LYS D CD  
12642 C CE  . LYS D 46  ? 1.2455 1.1994 0.5784 -0.2694 -0.0301 0.0229  46  LYS D CE  
12643 N NZ  . LYS D 46  ? 1.1750 1.1268 0.5291 -0.2664 -0.0338 0.0117  46  LYS D NZ  
12644 N N   . ASP D 47  ? 1.2069 1.0384 0.5939 -0.2207 0.0997  -0.0806 47  ASP D N   
12645 C CA  . ASP D 47  ? 1.2737 1.0865 0.6480 -0.2304 0.1302  -0.1090 47  ASP D CA  
12646 C C   . ASP D 47  ? 1.2407 1.0326 0.6249 -0.2330 0.1434  -0.1295 47  ASP D C   
12647 O O   . ASP D 47  ? 1.1971 0.9763 0.5647 -0.2498 0.1664  -0.1564 47  ASP D O   
12648 C CB  . ASP D 47  ? 1.1693 0.9691 0.5659 -0.2092 0.1488  -0.1093 47  ASP D CB  
12649 C CG  . ASP D 47  ? 1.2922 1.1107 0.6842 -0.2048 0.1363  -0.0881 47  ASP D CG  
12650 O OD1 . ASP D 47  ? 1.2338 1.0690 0.6294 -0.2013 0.1100  -0.0645 47  ASP D OD1 
12651 O OD2 . ASP D 47  ? 1.4649 1.2812 0.8521 -0.2051 0.1540  -0.0955 47  ASP D OD2 
12652 N N   . PHE D 48  ? 1.2051 0.9931 0.6162 -0.2184 0.1310  -0.1185 48  PHE D N   
12653 C CA  . PHE D 48  ? 1.2657 1.0320 0.6890 -0.2198 0.1437  -0.1352 48  PHE D CA  
12654 C C   . PHE D 48  ? 1.3253 1.1066 0.7469 -0.2297 0.1210  -0.1279 48  PHE D C   
12655 O O   . PHE D 48  ? 1.2825 1.0817 0.7177 -0.2186 0.0972  -0.1045 48  PHE D O   
12656 C CB  . PHE D 48  ? 1.2408 0.9830 0.7037 -0.1904 0.1558  -0.1300 48  PHE D CB  
12657 C CG  . PHE D 48  ? 1.2376 0.9712 0.7116 -0.1751 0.1728  -0.1308 48  PHE D CG  
12658 C CD1 . PHE D 48  ? 1.2387 0.9885 0.7220 -0.1595 0.1599  -0.1097 48  PHE D CD1 
12659 C CD2 . PHE D 48  ? 1.3012 1.0108 0.7797 -0.1766 0.2027  -0.1537 48  PHE D CD2 
12660 C CE1 . PHE D 48  ? 1.2684 1.0131 0.7639 -0.1464 0.1754  -0.1111 48  PHE D CE1 
12661 C CE2 . PHE D 48  ? 1.2357 0.9401 0.7291 -0.1620 0.2184  -0.1547 48  PHE D CE2 
12662 C CZ  . PHE D 48  ? 1.2136 0.9368 0.7147 -0.1473 0.2042  -0.1333 48  PHE D CZ  
12663 N N   . GLU D 49  ? 1.4087 1.1831 0.8165 -0.2508 0.1295  -0.1495 49  GLU D N   
12664 C CA  . GLU D 49  ? 1.4486 1.2360 0.8596 -0.2604 0.1109  -0.1458 49  GLU D CA  
12665 C C   . GLU D 49  ? 1.4284 1.1917 0.8749 -0.2403 0.1191  -0.1438 49  GLU D C   
12666 O O   . GLU D 49  ? 1.5112 1.2474 0.9630 -0.2441 0.1413  -0.1631 49  GLU D O   
12667 C CB  . GLU D 49  ? 1.3265 1.1206 0.7062 -0.2944 0.1155  -0.1703 49  GLU D CB  
12668 C CG  . GLU D 49  ? 1.5435 1.3646 0.9203 -0.3104 0.0899  -0.1648 49  GLU D CG  
12669 C CD  . GLU D 49  ? 1.5937 1.4074 1.0052 -0.2969 0.0838  -0.1579 49  GLU D CD  
12670 O OE1 . GLU D 49  ? 1.6014 1.3823 1.0324 -0.2857 0.1056  -0.1682 49  GLU D OE1 
12671 O OE2 . GLU D 49  ? 1.6559 1.4985 1.0750 -0.2990 0.0567  -0.1417 49  GLU D OE2 
12672 N N   . ILE D 50  ? 1.3412 1.1135 0.8123 -0.2189 0.1022  -0.1196 50  ILE D N   
12673 C CA  . ILE D 50  ? 1.2843 1.0445 0.7839 -0.2061 0.1020  -0.1144 50  ILE D CA  
12674 C C   . ILE D 50  ? 1.3201 1.1100 0.8317 -0.2015 0.0734  -0.0934 50  ILE D C   
12675 O O   . ILE D 50  ? 1.3540 1.1703 0.8520 -0.2097 0.0552  -0.0844 50  ILE D O   
12676 C CB  . ILE D 50  ? 1.2632 0.9977 0.7875 -0.1798 0.1181  -0.1082 50  ILE D CB  
12677 C CG1 . ILE D 50  ? 1.2922 1.0371 0.8191 -0.1636 0.1133  -0.0934 50  ILE D CG1 
12678 C CG2 . ILE D 50  ? 1.3232 1.0238 0.8465 -0.1839 0.1474  -0.1297 50  ILE D CG2 
12679 C CD1 . ILE D 50  ? 1.2153 0.9475 0.7709 -0.1364 0.1188  -0.0800 50  ILE D CD1 
12680 N N   . LYS D 51  ? 1.2114 0.9972 0.7493 -0.1891 0.0698  -0.0853 51  LYS D N   
12681 C CA  . LYS D 51  ? 1.1224 0.9339 0.6793 -0.1811 0.0463  -0.0664 51  LYS D CA  
12682 C C   . LYS D 51  ? 1.1317 0.9345 0.7128 -0.1549 0.0496  -0.0520 51  LYS D C   
12683 O O   . LYS D 51  ? 1.2462 1.0258 0.8380 -0.1457 0.0652  -0.0554 51  LYS D O   
12684 C CB  . LYS D 51  ? 1.1808 1.0016 0.7481 -0.1930 0.0382  -0.0712 51  LYS D CB  
12685 C CG  . LYS D 51  ? 1.2200 1.0540 0.7640 -0.2209 0.0332  -0.0860 51  LYS D CG  
12686 C CD  . LYS D 51  ? 1.2198 1.0925 0.7652 -0.2281 0.0045  -0.0722 51  LYS D CD  
12687 C CE  . LYS D 51  ? 1.2660 1.1549 0.7784 -0.2553 -0.0016 -0.0831 51  LYS D CE  
12688 N NZ  . LYS D 51  ? 1.4118 1.2790 0.8943 -0.2617 0.0197  -0.0978 51  LYS D NZ  
12689 N N   . LEU D 52  ? 1.0704 0.8920 0.6597 -0.1440 0.0352  -0.0356 52  LEU D N   
12690 C CA  . LEU D 52  ? 1.1005 0.9192 0.7116 -0.1213 0.0366  -0.0227 52  LEU D CA  
12691 C C   . LEU D 52  ? 1.0620 0.9056 0.6956 -0.1160 0.0166  -0.0088 52  LEU D C   
12692 O O   . LEU D 52  ? 1.0077 0.8725 0.6388 -0.1242 -0.0001 -0.0028 52  LEU D O   
12693 C CB  . LEU D 52  ? 1.1035 0.9184 0.7064 -0.1121 0.0430  -0.0188 52  LEU D CB  
12694 C CG  . LEU D 52  ? 1.0830 0.8713 0.6759 -0.1097 0.0664  -0.0311 52  LEU D CG  
12695 C CD1 . LEU D 52  ? 0.9965 0.7862 0.5841 -0.1017 0.0718  -0.0277 52  LEU D CD1 
12696 C CD2 . LEU D 52  ? 1.1209 0.8903 0.7330 -0.0960 0.0777  -0.0300 52  LEU D CD2 
12697 N N   . ASN D 53  ? 1.0710 0.9126 0.7274 -0.1027 0.0186  -0.0035 53  ASN D N   
12698 C CA  . ASN D 53  ? 1.0091 0.8726 0.6914 -0.0976 0.0036  0.0061  53  ASN D CA  
12699 C C   . ASN D 53  ? 0.9493 0.8153 0.6470 -0.0795 0.0048  0.0161  53  ASN D C   
12700 O O   . ASN D 53  ? 1.0052 0.8556 0.6993 -0.0698 0.0180  0.0155  53  ASN D O   
12701 C CB  . ASN D 53  ? 0.9400 0.8028 0.6358 -0.1024 0.0057  0.0003  53  ASN D CB  
12702 C CG  . ASN D 53  ? 1.0153 0.8828 0.7013 -0.1219 0.0010  -0.0096 53  ASN D CG  
12703 O OD1 . ASN D 53  ? 1.1020 0.9700 0.7978 -0.1289 0.0029  -0.0160 53  ASN D OD1 
12704 N ND2 . ASN D 53  ? 1.0441 0.9171 0.7098 -0.1323 -0.0052 -0.0112 53  ASN D ND2 
12705 N N   . PHE D 54  ? 0.9101 0.7969 0.6272 -0.0754 -0.0093 0.0255  54  PHE D N   
12706 C CA  . PHE D 54  ? 0.8868 0.7784 0.6178 -0.0610 -0.0090 0.0335  54  PHE D CA  
12707 C C   . PHE D 54  ? 0.8989 0.8088 0.6623 -0.0563 -0.0177 0.0374  54  PHE D C   
12708 O O   . PHE D 54  ? 0.8721 0.7960 0.6499 -0.0633 -0.0294 0.0385  54  PHE D O   
12709 C CB  . PHE D 54  ? 0.9188 0.8148 0.6399 -0.0608 -0.0146 0.0408  54  PHE D CB  
12710 C CG  . PHE D 54  ? 0.9576 0.8381 0.6478 -0.0670 -0.0047 0.0349  54  PHE D CG  
12711 C CD1 . PHE D 54  ? 0.9280 0.7920 0.6109 -0.0585 0.0115  0.0302  54  PHE D CD1 
12712 C CD2 . PHE D 54  ? 0.9135 0.7975 0.5831 -0.0822 -0.0112 0.0334  54  PHE D CD2 
12713 C CE1 . PHE D 54  ? 1.0399 0.8894 0.6989 -0.0642 0.0229  0.0226  54  PHE D CE1 
12714 C CE2 . PHE D 54  ? 0.9678 0.8382 0.6087 -0.0901 0.0003  0.0247  54  PHE D CE2 
12715 C CZ  . PHE D 54  ? 1.0602 0.9124 0.6973 -0.0807 0.0184  0.0183  54  PHE D CZ  
12716 N N   . ASN D 55  ? 0.9080 0.8191 0.6842 -0.0450 -0.0116 0.0389  55  ASN D N   
12717 C CA  . ASN D 55  ? 0.8461 0.7742 0.6539 -0.0404 -0.0164 0.0400  55  ASN D CA  
12718 C C   . ASN D 55  ? 0.8313 0.7665 0.6505 -0.0319 -0.0193 0.0468  55  ASN D C   
12719 O O   . ASN D 55  ? 0.7685 0.6959 0.5739 -0.0258 -0.0121 0.0483  55  ASN D O   
12720 C CB  . ASN D 55  ? 0.8189 0.7453 0.6318 -0.0377 -0.0058 0.0341  55  ASN D CB  
12721 C CG  . ASN D 55  ? 0.8320 0.7772 0.6773 -0.0359 -0.0084 0.0314  55  ASN D CG  
12722 O OD1 . ASN D 55  ? 0.8950 0.8496 0.7579 -0.0424 -0.0122 0.0269  55  ASN D OD1 
12723 N ND2 . ASN D 55  ? 0.8015 0.7533 0.6567 -0.0280 -0.0052 0.0323  55  ASN D ND2 
12724 N N   . LEU D 56  ? 0.7765 0.7268 0.6244 -0.0314 -0.0293 0.0506  56  LEU D N   
12725 C CA  . LEU D 56  ? 0.8010 0.7574 0.6648 -0.0247 -0.0323 0.0572  56  LEU D CA  
12726 C C   . LEU D 56  ? 0.7656 0.7359 0.6671 -0.0207 -0.0311 0.0521  56  LEU D C   
12727 O O   . LEU D 56  ? 0.8424 0.8231 0.7704 -0.0235 -0.0385 0.0518  56  LEU D O   
12728 C CB  . LEU D 56  ? 0.7683 0.7274 0.6322 -0.0288 -0.0457 0.0691  56  LEU D CB  
12729 C CG  . LEU D 56  ? 0.8779 0.8270 0.7132 -0.0292 -0.0438 0.0757  56  LEU D CG  
12730 C CD1 . LEU D 56  ? 0.8812 0.8160 0.6808 -0.0330 -0.0339 0.0683  56  LEU D CD1 
12731 C CD2 . LEU D 56  ? 0.8471 0.8011 0.6808 -0.0356 -0.0583 0.0893  56  LEU D CD2 
12732 N N   . THR D 57  ? 0.6302 0.6024 0.5360 -0.0150 -0.0215 0.0469  57  THR D N   
12733 C CA  . THR D 57  ? 0.6382 0.6245 0.5794 -0.0134 -0.0183 0.0391  57  THR D CA  
12734 C C   . THR D 57  ? 0.6306 0.6224 0.6029 -0.0102 -0.0255 0.0455  57  THR D C   
12735 O O   . THR D 57  ? 0.6671 0.6522 0.6289 -0.0077 -0.0286 0.0550  57  THR D O   
12736 C CB  . THR D 57  ? 0.6391 0.6293 0.5748 -0.0105 -0.0065 0.0310  57  THR D CB  
12737 O OG1 . THR D 57  ? 0.7911 0.7758 0.7118 -0.0056 -0.0052 0.0368  57  THR D OG1 
12738 C CG2 . THR D 57  ? 0.6940 0.6799 0.6057 -0.0137 0.0001  0.0267  57  THR D CG2 
12739 N N   . PRO D 58  ? 0.6540 0.6575 0.6670 -0.0103 -0.0270 0.0405  58  PRO D N   
12740 C CA  . PRO D 58  ? 0.6845 0.6912 0.7333 -0.0063 -0.0335 0.0482  58  PRO D CA  
12741 C C   . PRO D 58  ? 0.6684 0.6724 0.7214 -0.0023 -0.0262 0.0473  58  PRO D C   
12742 O O   . PRO D 58  ? 0.7341 0.7328 0.7968 0.0003  -0.0326 0.0599  58  PRO D O   
12743 C CB  . PRO D 58  ? 0.6405 0.6609 0.7352 -0.0069 -0.0314 0.0376  58  PRO D CB  
12744 C CG  . PRO D 58  ? 0.6268 0.6503 0.7042 -0.0130 -0.0309 0.0312  58  PRO D CG  
12745 C CD  . PRO D 58  ? 0.6005 0.6142 0.6310 -0.0145 -0.0227 0.0283  58  PRO D CD  
12746 N N   . VAL D 59  ? 0.6092 0.6180 0.6560 -0.0027 -0.0134 0.0332  59  VAL D N   
12747 C CA  . VAL D 59  ? 0.6846 0.6935 0.7353 -0.0004 -0.0065 0.0308  59  VAL D CA  
12748 C C   . VAL D 59  ? 0.6809 0.6782 0.6976 0.0015  -0.0104 0.0441  59  VAL D C   
12749 O O   . VAL D 59  ? 0.5962 0.5901 0.6209 0.0032  -0.0098 0.0495  59  VAL D O   
12750 C CB  . VAL D 59  ? 0.6219 0.6426 0.6686 -0.0032 0.0065  0.0133  59  VAL D CB  
12751 C CG1 . VAL D 59  ? 0.5796 0.5994 0.5910 -0.0054 0.0075  0.0123  59  VAL D CG1 
12752 C CG2 . VAL D 59  ? 0.7069 0.7297 0.7473 -0.0019 0.0126  0.0113  59  VAL D CG2 
12753 N N   . LEU D 60  ? 0.6230 0.6133 0.6029 0.0003  -0.0131 0.0485  60  LEU D N   
12754 C CA  . LEU D 60  ? 0.6605 0.6400 0.6091 0.0010  -0.0149 0.0587  60  LEU D CA  
12755 C C   . LEU D 60  ? 0.6762 0.6493 0.6292 -0.0008 -0.0259 0.0740  60  LEU D C   
12756 O O   . LEU D 60  ? 0.8062 0.7740 0.7512 -0.0007 -0.0254 0.0820  60  LEU D O   
12757 C CB  . LEU D 60  ? 0.7381 0.7104 0.6505 -0.0004 -0.0132 0.0578  60  LEU D CB  
12758 C CG  . LEU D 60  ? 0.7168 0.6774 0.5977 -0.0011 -0.0135 0.0660  60  LEU D CG  
12759 C CD1 . LEU D 60  ? 0.6297 0.5924 0.5096 0.0029  -0.0061 0.0654  60  LEU D CD1 
12760 C CD2 . LEU D 60  ? 0.6495 0.6013 0.5009 -0.0025 -0.0097 0.0628  60  LEU D CD2 
12761 N N   . ILE D 61  ? 0.6290 0.6042 0.5948 -0.0033 -0.0362 0.0793  61  ILE D N   
12762 C CA  . ILE D 61  ? 0.7621 0.7342 0.7319 -0.0058 -0.0493 0.0969  61  ILE D CA  
12763 C C   . ILE D 61  ? 0.8176 0.7897 0.8206 -0.0021 -0.0493 0.1039  61  ILE D C   
12764 O O   . ILE D 61  ? 0.7783 0.7435 0.7710 -0.0039 -0.0538 0.1184  61  ILE D O   
12765 C CB  . ILE D 61  ? 0.7068 0.6859 0.6907 -0.0088 -0.0615 0.1008  61  ILE D CB  
12766 C CG1 . ILE D 61  ? 0.7325 0.7098 0.6831 -0.0141 -0.0597 0.0926  61  ILE D CG1 
12767 C CG2 . ILE D 61  ? 0.7151 0.6945 0.7024 -0.0120 -0.0777 0.1219  61  ILE D CG2 
12768 C CD1 . ILE D 61  ? 0.6994 0.6869 0.6715 -0.0164 -0.0647 0.0869  61  ILE D CD1 
12769 N N   . ASP D 62  ? 0.8214 0.8005 0.8645 0.0020  -0.0429 0.0927  62  ASP D N   
12770 C CA  . ASP D 62  ? 0.7975 0.7746 0.8767 0.0051  -0.0404 0.0968  62  ASP D CA  
12771 C C   . ASP D 62  ? 0.7526 0.7230 0.8101 0.0042  -0.0320 0.0974  62  ASP D C   
12772 O O   . ASP D 62  ? 0.7948 0.7575 0.8606 0.0038  -0.0347 0.1111  62  ASP D O   
12773 C CB  . ASP D 62  ? 0.7681 0.7545 0.8907 0.0076  -0.0304 0.0785  62  ASP D CB  
12774 C CG  . ASP D 62  ? 0.8954 0.8875 1.0612 0.0099  -0.0387 0.0823  62  ASP D CG  
12775 O OD1 . ASP D 62  ? 0.9187 0.9065 1.1206 0.0133  -0.0448 0.0956  62  ASP D OD1 
12776 O OD2 . ASP D 62  ? 0.8668 0.8680 1.0330 0.0084  -0.0388 0.0722  62  ASP D OD2 
12777 N N   . GLN D 63  ? 0.7312 0.7050 0.7618 0.0038  -0.0219 0.0835  63  GLN D N   
12778 C CA  . GLN D 63  ? 0.7846 0.7561 0.7983 0.0033  -0.0132 0.0818  63  GLN D CA  
12779 C C   . GLN D 63  ? 0.8607 0.8216 0.8422 0.0002  -0.0187 0.0982  63  GLN D C   
12780 O O   . GLN D 63  ? 0.7550 0.7116 0.7354 -0.0014 -0.0145 0.1037  63  GLN D O   
12781 C CB  . GLN D 63  ? 0.6998 0.6797 0.6933 0.0043  -0.0037 0.0660  63  GLN D CB  
12782 C CG  . GLN D 63  ? 0.6683 0.6615 0.6895 0.0045  0.0045  0.0486  63  GLN D CG  
12783 C CD  . GLN D 63  ? 0.6749 0.6787 0.6740 0.0047  0.0121  0.0370  63  GLN D CD  
12784 O OE1 . GLN D 63  ? 0.8408 0.8512 0.8378 0.0045  0.0186  0.0324  63  GLN D OE1 
12785 N NE2 . GLN D 63  ? 0.6331 0.6392 0.6164 0.0048  0.0109  0.0335  63  GLN D NE2 
12786 N N   . ILE D 64  ? 0.8789 0.8363 0.8333 -0.0025 -0.0269 0.1048  64  ILE D N   
12787 C CA  . ILE D 64  ? 0.7934 0.7425 0.7151 -0.0081 -0.0313 0.1185  64  ILE D CA  
12788 C C   . ILE D 64  ? 0.8420 0.7869 0.7810 -0.0110 -0.0416 0.1382  64  ILE D C   
12789 O O   . ILE D 64  ? 0.9662 0.9048 0.8908 -0.0155 -0.0402 0.1490  64  ILE D O   
12790 C CB  . ILE D 64  ? 0.8624 0.8096 0.7515 -0.0124 -0.0367 0.1185  64  ILE D CB  
12791 C CG1 . ILE D 64  ? 0.8610 0.8067 0.7245 -0.0104 -0.0246 0.1041  64  ILE D CG1 
12792 C CG2 . ILE D 64  ? 0.9899 0.9312 0.8513 -0.0214 -0.0446 0.1346  64  ILE D CG2 
12793 C CD1 . ILE D 64  ? 0.8699 0.8134 0.7137 -0.0128 -0.0269 0.0986  64  ILE D CD1 
12794 N N   . GLN D 65  ? 0.8540 0.8027 0.8255 -0.0087 -0.0521 0.1443  65  GLN D N   
12795 C CA  . GLN D 65  ? 0.8831 0.8281 0.8763 -0.0101 -0.0638 0.1664  65  GLN D CA  
12796 C C   . GLN D 65  ? 0.9901 0.9278 1.0028 -0.0088 -0.0547 0.1696  65  GLN D C   
12797 O O   . GLN D 65  ? 1.0205 0.9504 1.0219 -0.0140 -0.0589 0.1885  65  GLN D O   
12798 C CB  . GLN D 65  ? 0.8447 0.7969 0.8818 -0.0051 -0.0741 0.1694  65  GLN D CB  
12799 C CG  . GLN D 65  ? 0.9665 0.9255 0.9879 -0.0098 -0.0912 0.1810  65  GLN D CG  
12800 C CD  . GLN D 65  ? 1.0037 0.9733 1.0716 -0.0044 -0.1000 0.1805  65  GLN D CD  
12801 O OE1 . GLN D 65  ? 0.9369 0.9152 1.0019 -0.0079 -0.1157 0.1915  65  GLN D OE1 
12802 N NE2 . GLN D 65  ? 0.9503 0.9211 1.0623 0.0031  -0.0892 0.1663  65  GLN D NE2 
12803 N N   . GLU D 66  ? 0.9872 0.9280 1.0273 -0.0036 -0.0415 0.1506  66  GLU D N   
12804 C CA  . GLU D 66  ? 0.9317 0.8667 0.9922 -0.0037 -0.0309 0.1498  66  GLU D CA  
12805 C C   . GLU D 66  ? 0.9287 0.8586 0.9492 -0.0099 -0.0251 0.1545  66  GLU D C   
12806 O O   . GLU D 66  ? 0.9901 0.9107 1.0146 -0.0140 -0.0246 0.1694  66  GLU D O   
12807 C CB  . GLU D 66  ? 0.8833 0.8269 0.9704 -0.0001 -0.0167 0.1242  66  GLU D CB  
12808 C CG  . GLU D 66  ? 1.0209 0.9596 1.1583 0.0011  -0.0098 0.1225  66  GLU D CG  
12809 C CD  . GLU D 66  ? 1.0804 1.0307 1.2424 0.0019  0.0046  0.0944  66  GLU D CD  
12810 O OE1 . GLU D 66  ? 1.0330 0.9928 1.2070 0.0045  0.0039  0.0822  66  GLU D OE1 
12811 O OE2 . GLU D 66  ? 0.9972 0.9486 1.1660 -0.0014 0.0169  0.0840  66  GLU D OE2 
12812 N N   . TYR D 67  ? 0.8699 0.8053 0.8533 -0.0108 -0.0199 0.1423  67  TYR D N   
12813 C CA  . TYR D 67  ? 0.9260 0.8583 0.8746 -0.0163 -0.0125 0.1442  67  TYR D CA  
12814 C C   . TYR D 67  ? 0.9799 0.9033 0.9030 -0.0247 -0.0222 0.1672  67  TYR D C   
12815 O O   . TYR D 67  ? 1.0008 0.9185 0.9104 -0.0312 -0.0166 0.1753  67  TYR D O   
12816 C CB  . TYR D 67  ? 0.8075 0.7465 0.7258 -0.0145 -0.0059 0.1282  67  TYR D CB  
12817 C CG  . TYR D 67  ? 0.8789 0.8283 0.8104 -0.0096 0.0068  0.1090  67  TYR D CG  
12818 C CD1 . TYR D 67  ? 0.8512 0.8027 0.7860 -0.0119 0.0174  0.1058  67  TYR D CD1 
12819 C CD2 . TYR D 67  ? 0.9321 0.8909 0.8716 -0.0040 0.0078  0.0945  67  TYR D CD2 
12820 C CE1 . TYR D 67  ? 0.8116 0.7769 0.7587 -0.0084 0.0272  0.0884  67  TYR D CE1 
12821 C CE2 . TYR D 67  ? 0.7968 0.7683 0.7457 -0.0010 0.0175  0.0787  67  TYR D CE2 
12822 C CZ  . TYR D 67  ? 0.8028 0.7787 0.7559 -0.0030 0.0264  0.0756  67  TYR D CZ  
12823 O OH  . TYR D 67  ? 0.8494 0.8421 0.8121 -0.0008 0.0341  0.0599  67  TYR D OH  
12824 N N   . ALA D 68  ? 0.9590 0.8829 0.8750 -0.0261 -0.0370 0.1781  68  ALA D N   
12825 C CA  . ALA D 68  ? 0.9900 0.9093 0.8772 -0.0363 -0.0481 0.2003  68  ALA D CA  
12826 C C   . ALA D 68  ? 1.0279 0.9397 0.9410 -0.0382 -0.0546 0.2236  68  ALA D C   
12827 O O   . ALA D 68  ? 1.0685 0.9747 0.9562 -0.0483 -0.0567 0.2412  68  ALA D O   
12828 C CB  . ALA D 68  ? 0.8168 0.7421 0.6914 -0.0384 -0.0632 0.2049  68  ALA D CB  
12829 N N   . GLN D 69  ? 1.0389 0.9499 1.0032 -0.0293 -0.0570 0.2240  69  GLN D N   
12830 C CA  . GLN D 69  ? 0.9974 0.8984 0.9948 -0.0294 -0.0614 0.2457  69  GLN D CA  
12831 C C   . GLN D 69  ? 1.0106 0.9031 1.0159 -0.0315 -0.0441 0.2398  69  GLN D C   
12832 O O   . GLN D 69  ? 1.0675 0.9488 1.1017 -0.0323 -0.0449 0.2569  69  GLN D O   
12833 C CB  . GLN D 69  ? 1.0767 0.9793 1.1324 -0.0189 -0.0680 0.2460  69  GLN D CB  
12834 C CG  . GLN D 69  ? 1.0119 0.9269 1.0682 -0.0152 -0.0809 0.2425  69  GLN D CG  
12835 C CD  . GLN D 69  ? 1.0799 0.9986 1.1975 -0.0046 -0.0819 0.2352  69  GLN D CD  
12836 O OE1 . GLN D 69  ? 1.0965 1.0067 1.2591 0.0000  -0.0754 0.2372  69  GLN D OE1 
12837 N NE2 . GLN D 69  ? 1.0469 0.9779 1.1677 -0.0014 -0.0883 0.2249  69  GLN D NE2 
12838 N N   . GLY D 70  ? 1.0201 0.9179 1.0031 -0.0326 -0.0287 0.2169  70  GLY D N   
12839 C CA  . GLY D 70  ? 0.9907 0.8846 0.9829 -0.0352 -0.0120 0.2084  70  GLY D CA  
12840 C C   . GLY D 70  ? 1.0561 0.9496 1.1014 -0.0285 -0.0034 0.1945  70  GLY D C   
12841 O O   . GLY D 70  ? 0.9966 0.8860 1.0561 -0.0321 0.0096  0.1896  70  GLY D O   
12842 N N   . LYS D 71  ? 1.0116 0.9105 1.0868 -0.0203 -0.0089 0.1861  71  LYS D N   
12843 C CA  . LYS D 71  ? 0.9622 0.8613 1.0904 -0.0153 -0.0001 0.1713  71  LYS D CA  
12844 C C   . LYS D 71  ? 0.9693 0.8842 1.0971 -0.0137 0.0132  0.1393  71  LYS D C   
12845 O O   . LYS D 71  ? 1.0493 0.9676 1.2171 -0.0120 0.0225  0.1226  71  LYS D O   
12846 C CB  . LYS D 71  ? 1.0070 0.9051 1.1726 -0.0081 -0.0119 0.1785  71  LYS D CB  
12847 C CG  . LYS D 71  ? 1.0760 0.9578 1.2837 -0.0069 -0.0174 0.2025  71  LYS D CG  
12848 C CD  . LYS D 71  ? 1.0333 0.9154 1.3044 0.0011  -0.0144 0.1915  71  LYS D CD  
12849 C CE  . LYS D 71  ? 0.9894 0.8524 1.3107 0.0018  -0.0099 0.2063  71  LYS D CE  
12850 N NZ  . LYS D 71  ? 0.9481 0.8103 1.3366 0.0092  -0.0032 0.1920  71  LYS D NZ  
12851 N N   . ALA D 72  ? 0.8506 0.7758 0.9355 -0.0146 0.0146  0.1306  72  ALA D N   
12852 C CA  . ALA D 72  ? 0.8720 0.8139 0.9568 -0.0128 0.0248  0.1041  72  ALA D CA  
12853 C C   . ALA D 72  ? 0.9534 0.8999 1.0440 -0.0180 0.0391  0.0933  72  ALA D C   
12854 O O   . ALA D 72  ? 1.0011 0.9378 1.0837 -0.0233 0.0419  0.1060  72  ALA D O   
12855 C CB  . ALA D 72  ? 0.8918 0.8423 0.9341 -0.0105 0.0208  0.1000  72  ALA D CB  
12856 N N   . LYS D 73  ? 0.8965 0.8598 1.0008 -0.0177 0.0481  0.0695  73  LYS D N   
12857 C CA  . LYS D 73  ? 0.7777 0.7513 0.8917 -0.0235 0.0613  0.0552  73  LYS D CA  
12858 C C   . LYS D 73  ? 0.8198 0.8163 0.9088 -0.0217 0.0637  0.0397  73  LYS D C   
12859 O O   . LYS D 73  ? 0.8425 0.8573 0.9455 -0.0229 0.0687  0.0200  73  LYS D O   
12860 C CB  . LYS D 73  ? 0.7972 0.7719 0.9590 -0.0272 0.0704  0.0405  73  LYS D CB  
12861 C CG  . LYS D 73  ? 0.7961 0.7511 0.9855 -0.0323 0.0759  0.0522  73  LYS D CG  
12862 C CD  . LYS D 73  ? 1.0100 0.9647 1.1770 -0.0385 0.0818  0.0582  73  LYS D CD  
12863 C CE  . LYS D 73  ? 1.1309 1.0652 1.3257 -0.0453 0.0890  0.0700  73  LYS D CE  
12864 N NZ  . LYS D 73  ? 0.9982 0.9262 1.1643 -0.0515 0.0916  0.0849  73  LYS D NZ  
12865 N N   . ASP D 74  ? 0.8570 0.8528 0.9092 -0.0193 0.0600  0.0492  74  ASP D N   
12866 C CA  . ASP D 74  ? 0.7956 0.8108 0.8260 -0.0160 0.0618  0.0384  74  ASP D CA  
12867 C C   . ASP D 74  ? 0.7980 0.8286 0.8370 -0.0211 0.0724  0.0283  74  ASP D C   
12868 O O   . ASP D 74  ? 0.8248 0.8488 0.8537 -0.0244 0.0768  0.0366  74  ASP D O   
12869 C CB  . ASP D 74  ? 0.8831 0.8897 0.8763 -0.0117 0.0560  0.0510  74  ASP D CB  
12870 C CG  . ASP D 74  ? 0.8670 0.8895 0.8423 -0.0054 0.0558  0.0423  74  ASP D CG  
12871 O OD1 . ASP D 74  ? 0.8937 0.9338 0.8709 -0.0053 0.0623  0.0335  74  ASP D OD1 
12872 O OD2 . ASP D 74  ? 0.8272 0.8447 0.7879 -0.0007 0.0488  0.0452  74  ASP D OD2 
12873 N N   . VAL D 75  ? 0.7402 0.7932 0.7974 -0.0233 0.0769  0.0097  75  VAL D N   
12874 C CA  . VAL D 75  ? 0.6618 0.7337 0.7308 -0.0296 0.0863  -0.0019 75  VAL D CA  
12875 C C   . VAL D 75  ? 0.6462 0.7286 0.6908 -0.0253 0.0868  0.0023  75  VAL D C   
12876 O O   . VAL D 75  ? 0.7207 0.8086 0.7701 -0.0303 0.0947  0.0010  75  VAL D O   
12877 C CB  . VAL D 75  ? 0.5936 0.6919 0.6829 -0.0343 0.0894  -0.0235 75  VAL D CB  
12878 C CG1 . VAL D 75  ? 0.6558 0.7428 0.7666 -0.0365 0.0891  -0.0287 75  VAL D CG1 
12879 C CG2 . VAL D 75  ? 0.6604 0.7833 0.7296 -0.0283 0.0832  -0.0281 75  VAL D CG2 
12880 N N   . PHE D 76  ? 0.6714 0.7555 0.6920 -0.0162 0.0795  0.0073  76  PHE D N   
12881 C CA  . PHE D 76  ? 0.7155 0.8089 0.7181 -0.0109 0.0812  0.0102  76  PHE D CA  
12882 C C   . PHE D 76  ? 0.8275 0.8988 0.8135 -0.0128 0.0851  0.0231  76  PHE D C   
12883 O O   . PHE D 76  ? 0.8168 0.8959 0.7995 -0.0139 0.0927  0.0220  76  PHE D O   
12884 C CB  . PHE D 76  ? 0.7012 0.8002 0.6859 -0.0009 0.0736  0.0121  76  PHE D CB  
12885 C CG  . PHE D 76  ? 0.7972 0.9080 0.7714 0.0062  0.0762  0.0136  76  PHE D CG  
12886 C CD1 . PHE D 76  ? 0.8120 0.9538 0.8017 0.0068  0.0787  0.0047  76  PHE D CD1 
12887 C CD2 . PHE D 76  ? 0.8761 0.9682 0.8275 0.0117  0.0767  0.0230  76  PHE D CD2 
12888 C CE1 . PHE D 76  ? 0.8265 0.9801 0.8128 0.0148  0.0811  0.0067  76  PHE D CE1 
12889 C CE2 . PHE D 76  ? 0.7939 0.8956 0.7408 0.0187  0.0812  0.0229  76  PHE D CE2 
12890 C CZ  . PHE D 76  ? 0.8298 0.9621 0.7961 0.0212  0.0833  0.0155  76  PHE D CZ  
12891 N N   . LEU D 77  ? 0.8343 0.8800 0.8099 -0.0141 0.0799  0.0353  77  LEU D N   
12892 C CA  . LEU D 77  ? 0.8030 0.8291 0.7582 -0.0184 0.0824  0.0488  77  LEU D CA  
12893 C C   . LEU D 77  ? 0.8277 0.8518 0.7963 -0.0285 0.0919  0.0503  77  LEU D C   
12894 O O   . LEU D 77  ? 0.8068 0.8249 0.7584 -0.0334 0.0986  0.0566  77  LEU D O   
12895 C CB  . LEU D 77  ? 0.8362 0.8397 0.7797 -0.0187 0.0723  0.0626  77  LEU D CB  
12896 C CG  . LEU D 77  ? 1.0036 1.0013 0.9190 -0.0126 0.0659  0.0660  77  LEU D CG  
12897 C CD1 . LEU D 77  ? 0.9753 0.9518 0.8732 -0.0172 0.0577  0.0820  77  LEU D CD1 
12898 C CD2 . LEU D 77  ? 0.8155 0.8207 0.7125 -0.0100 0.0742  0.0609  77  LEU D CD2 
12899 N N   . GLU D 78  ? 0.8545 0.8828 0.8536 -0.0329 0.0942  0.0438  78  GLU D N   
12900 C CA  . GLU D 78  ? 0.9346 0.9613 0.9496 -0.0433 0.1050  0.0436  78  GLU D CA  
12901 C C   . GLU D 78  ? 0.9512 1.0031 0.9695 -0.0448 0.1149  0.0304  78  GLU D C   
12902 O O   . GLU D 78  ? 1.0063 1.0562 1.0251 -0.0533 0.1252  0.0327  78  GLU D O   
12903 C CB  . GLU D 78  ? 0.9054 0.9292 0.9560 -0.0481 0.1066  0.0376  78  GLU D CB  
12904 C CG  . GLU D 78  ? 1.0395 1.0374 1.0998 -0.0565 0.1098  0.0534  78  GLU D CG  
12905 C CD  . GLU D 78  ? 1.1532 1.1274 1.1987 -0.0527 0.0976  0.0745  78  GLU D CD  
12906 O OE1 . GLU D 78  ? 1.1889 1.1488 1.2087 -0.0569 0.0963  0.0925  78  GLU D OE1 
12907 O OE2 . GLU D 78  ? 1.1653 1.1371 1.2248 -0.0466 0.0894  0.0724  78  GLU D OE2 
12908 N N   . ALA D 79  ? 0.7705 0.8473 0.7920 -0.0371 0.1119  0.0176  79  ALA D N   
12909 C CA  . ALA D 79  ? 0.9270 1.0310 0.9538 -0.0365 0.1192  0.0070  79  ALA D CA  
12910 C C   . ALA D 79  ? 0.9162 1.0125 0.9189 -0.0346 0.1246  0.0150  79  ALA D C   
12911 O O   . ALA D 79  ? 0.9294 1.0364 0.9382 -0.0402 0.1358  0.0107  79  ALA D O   
12912 C CB  . ALA D 79  ? 0.8994 1.0311 0.9324 -0.0277 0.1120  -0.0037 79  ALA D CB  
12913 N N   . ILE D 80  ? 0.8500 0.9286 0.8262 -0.0281 0.1181  0.0251  80  ILE D N   
12914 C CA  . ILE D 80  ? 0.8957 0.9665 0.8479 -0.0278 0.1248  0.0299  80  ILE D CA  
12915 C C   . ILE D 80  ? 0.8733 0.9244 0.8133 -0.0414 0.1324  0.0402  80  ILE D C   
12916 O O   . ILE D 80  ? 0.8630 0.9170 0.7945 -0.0471 0.1446  0.0385  80  ILE D O   
12917 C CB  . ILE D 80  ? 0.9050 0.9625 0.8324 -0.0189 0.1165  0.0357  80  ILE D CB  
12918 C CG1 . ILE D 80  ? 0.8667 0.9447 0.8039 -0.0057 0.1123  0.0272  80  ILE D CG1 
12919 C CG2 . ILE D 80  ? 0.9828 1.0260 0.8820 -0.0230 0.1245  0.0407  80  ILE D CG2 
12920 C CD1 . ILE D 80  ? 0.8709 0.9345 0.7873 0.0024  0.1045  0.0324  80  ILE D CD1 
12921 N N   . ARG D 81  ? 0.8685 0.8999 0.8087 -0.0470 0.1256  0.0515  81  ARG D N   
12922 C CA  . ARG D 81  ? 0.9518 0.9623 0.8768 -0.0598 0.1300  0.0665  81  ARG D CA  
12923 C C   . ARG D 81  ? 1.0079 1.0262 0.9521 -0.0706 0.1439  0.0619  81  ARG D C   
12924 O O   . ARG D 81  ? 0.9896 1.0025 0.9170 -0.0809 0.1546  0.0672  81  ARG D O   
12925 C CB  . ARG D 81  ? 0.9278 0.9165 0.8536 -0.0608 0.1172  0.0821  81  ARG D CB  
12926 C CG  . ARG D 81  ? 1.0191 0.9846 0.9295 -0.0734 0.1169  0.1037  81  ARG D CG  
12927 C CD  . ARG D 81  ? 1.2202 1.1823 1.1544 -0.0840 0.1272  0.1063  81  ARG D CD  
12928 N NE  . ARG D 81  ? 1.0981 1.0516 1.0664 -0.0818 0.1210  0.1094  81  ARG D NE  
12929 C CZ  . ARG D 81  ? 1.0479 1.0040 1.0500 -0.0871 0.1304  0.1018  81  ARG D CZ  
12930 N NH1 . ARG D 81  ? 0.9405 0.9082 0.9465 -0.0957 0.1454  0.0923  81  ARG D NH1 
12931 N NH2 . ARG D 81  ? 1.1533 1.1007 1.1882 -0.0846 0.1257  0.1022  81  ARG D NH2 
12932 N N   . LYS D 82  ? 0.9403 0.9721 0.9189 -0.0700 0.1450  0.0507  82  LYS D N   
12933 C CA  . LYS D 82  ? 0.9376 0.9767 0.9379 -0.0816 0.1585  0.0449  82  LYS D CA  
12934 C C   . LYS D 82  ? 0.9214 0.9808 0.9163 -0.0840 0.1716  0.0348  82  LYS D C   
12935 O O   . LYS D 82  ? 0.9022 0.9796 0.8922 -0.0734 0.1698  0.0257  82  LYS D O   
12936 C CB  . LYS D 82  ? 0.9895 1.0452 1.0275 -0.0806 0.1577  0.0293  82  LYS D CB  
12937 C CG  . LYS D 82  ? 1.0383 1.0724 1.0973 -0.0889 0.1583  0.0365  82  LYS D CG  
12938 C CD  . LYS D 82  ? 0.9717 1.0155 1.0595 -0.0843 0.1525  0.0227  82  LYS D CD  
12939 C CE  . LYS D 82  ? 0.9566 1.0377 1.0523 -0.0789 0.1520  0.0014  82  LYS D CE  
12940 N NZ  . LYS D 82  ? 1.0491 1.1448 1.1781 -0.0836 0.1537  -0.0167 82  LYS D NZ  
12941 N N   . ASP D 83  ? 0.8928 0.9484 0.8904 -0.0983 0.1855  0.0372  83  ASP D N   
12942 C CA  . ASP D 83  ? 0.8186 0.8975 0.8206 -0.1021 0.2003  0.0244  83  ASP D CA  
12943 C C   . ASP D 83  ? 0.9060 1.0204 0.9429 -0.0949 0.1996  0.0039  83  ASP D C   
12944 O O   . ASP D 83  ? 0.9896 1.1081 1.0505 -0.0962 0.1947  -0.0016 83  ASP D O   
12945 C CB  . ASP D 83  ? 0.8558 0.9249 0.8587 -0.1208 0.2162  0.0299  83  ASP D CB  
12946 C CG  . ASP D 83  ? 0.8858 0.9780 0.8911 -0.1263 0.2335  0.0170  83  ASP D CG  
12947 O OD1 . ASP D 83  ? 0.8549 0.9762 0.8933 -0.1265 0.2399  -0.0003 83  ASP D OD1 
12948 O OD2 . ASP D 83  ? 0.8907 0.9734 0.8656 -0.1313 0.2411  0.0234  83  ASP D OD2 
12949 N N   . PRO D 84  ? 0.8449 0.9868 0.8868 -0.0877 0.2042  -0.0079 84  PRO D N   
12950 C CA  . PRO D 84  ? 0.8515 1.0315 0.9258 -0.0805 0.2006  -0.0248 84  PRO D CA  
12951 C C   . PRO D 84  ? 0.9114 1.1083 1.0176 -0.0940 0.2087  -0.0364 84  PRO D C   
12952 O O   . PRO D 84  ? 0.9182 1.1444 1.0500 -0.0913 0.2028  -0.0497 84  PRO D O   
12953 C CB  . PRO D 84  ? 0.8796 1.0818 0.9547 -0.0724 0.2074  -0.0315 84  PRO D CB  
12954 C CG  . PRO D 84  ? 0.8327 1.0051 0.8708 -0.0683 0.2070  -0.0190 84  PRO D CG  
12955 C CD  . PRO D 84  ? 0.8877 1.0272 0.9058 -0.0838 0.2109  -0.0058 84  PRO D CD  
12956 N N   . ASP D 85  ? 0.8933 1.0720 0.9972 -0.1099 0.2224  -0.0313 85  ASP D N   
12957 C CA  . ASP D 85  ? 0.9111 1.1027 1.0461 -0.1247 0.2327  -0.0428 85  ASP D CA  
12958 C C   . ASP D 85  ? 0.9635 1.1401 1.1128 -0.1289 0.2259  -0.0428 85  ASP D C   
12959 O O   . ASP D 85  ? 0.8868 1.0856 1.0675 -0.1364 0.2294  -0.0596 85  ASP D O   
12960 C CB  . ASP D 85  ? 0.8755 1.0509 1.0030 -0.1413 0.2511  -0.0362 85  ASP D CB  
12961 C CG  . ASP D 85  ? 0.9869 1.1825 1.1080 -0.1399 0.2622  -0.0420 85  ASP D CG  
12962 O OD1 . ASP D 85  ? 1.0341 1.2389 1.1433 -0.1242 0.2543  -0.0423 85  ASP D OD1 
12963 O OD2 . ASP D 85  ? 0.8411 1.0441 0.9722 -0.1547 0.2799  -0.0474 85  ASP D OD2 
12964 N N   . ASP D 86  ? 1.0686 1.2095 1.1977 -0.1249 0.2170  -0.0255 86  ASP D N   
12965 C CA  . ASP D 86  ? 1.0289 1.1538 1.1745 -0.1268 0.2109  -0.0254 86  ASP D CA  
12966 C C   . ASP D 86  ? 0.8741 1.0162 1.0233 -0.1134 0.1957  -0.0346 86  ASP D C   
12967 O O   . ASP D 86  ? 0.9344 1.0632 1.0950 -0.1134 0.1902  -0.0353 86  ASP D O   
12968 C CB  . ASP D 86  ? 1.0106 1.0907 1.1376 -0.1288 0.2078  -0.0008 86  ASP D CB  
12969 C CG  . ASP D 86  ? 1.1369 1.1988 1.2452 -0.1405 0.2199  0.0143  86  ASP D CG  
12970 O OD1 . ASP D 86  ? 1.2594 1.3246 1.3871 -0.1550 0.2349  0.0083  86  ASP D OD1 
12971 O OD2 . ASP D 86  ? 1.0962 1.1409 1.1695 -0.1368 0.2149  0.0318  86  ASP D OD2 
12972 N N   . LEU D 87  ? 0.9438 1.1146 1.0850 -0.1025 0.1897  -0.0413 87  LEU D N   
12973 C CA  . LEU D 87  ? 0.9974 1.1846 1.1377 -0.0902 0.1751  -0.0472 87  LEU D CA  
12974 C C   . LEU D 87  ? 0.9460 1.1691 1.1170 -0.0967 0.1754  -0.0691 87  LEU D C   
12975 O O   . LEU D 87  ? 0.9706 1.2207 1.1609 -0.1053 0.1844  -0.0814 87  LEU D O   
12976 C CB  . LEU D 87  ? 0.9866 1.1881 1.1073 -0.0758 0.1688  -0.0430 87  LEU D CB  
12977 C CG  . LEU D 87  ? 0.9374 1.1080 1.0244 -0.0659 0.1622  -0.0251 87  LEU D CG  
12978 C CD1 . LEU D 87  ? 0.8503 1.0372 0.9255 -0.0535 0.1605  -0.0250 87  LEU D CD1 
12979 C CD2 . LEU D 87  ? 0.9750 1.1311 1.0564 -0.0600 0.1490  -0.0209 87  LEU D CD2 
12980 N N   . GLU D 88  ? 0.9563 1.1817 1.1315 -0.0941 0.1660  -0.0749 88  GLU D N   
12981 C CA  . GLU D 88  ? 1.0075 1.2703 1.2061 -0.1012 0.1647  -0.0966 88  GLU D CA  
12982 C C   . GLU D 88  ? 0.9729 1.2754 1.1644 -0.0903 0.1533  -0.0995 88  GLU D C   
12983 O O   . GLU D 88  ? 0.9814 1.2767 1.1507 -0.0755 0.1458  -0.0851 88  GLU D O   
12984 C CB  . GLU D 88  ? 1.0221 1.2724 1.2279 -0.1044 0.1610  -0.1034 88  GLU D CB  
12985 C CG  . GLU D 88  ? 1.1015 1.3059 1.3133 -0.1093 0.1685  -0.0936 88  GLU D CG  
12986 C CD  . GLU D 88  ? 1.0708 1.2653 1.2972 -0.1122 0.1668  -0.1030 88  GLU D CD  
12987 O OE1 . GLU D 88  ? 0.9973 1.1606 1.2129 -0.1038 0.1609  -0.0878 88  GLU D OE1 
12988 O OE2 . GLU D 88  ? 1.0195 1.2384 1.2689 -0.1237 0.1719  -0.1264 88  GLU D OE2 
12989 N N   . LYS D 89  ? 0.8822 1.2277 1.0943 -0.0986 0.1520  -0.1182 89  LYS D N   
12990 C CA  . LYS D 89  ? 0.8643 1.2524 1.0744 -0.0891 0.1402  -0.1191 89  LYS D CA  
12991 C C   . LYS D 89  ? 0.8760 1.2584 1.0626 -0.0753 0.1252  -0.1084 89  LYS D C   
12992 O O   . LYS D 89  ? 0.8753 1.2681 1.0503 -0.0604 0.1164  -0.0967 89  LYS D O   
12993 C CB  . LYS D 89  ? 0.7976 1.2354 1.0332 -0.1033 0.1399  -0.1408 89  LYS D CB  
12994 C CG  . LYS D 89  ? 0.7562 1.2260 1.0133 -0.1075 0.1465  -0.1468 89  LYS D CG  
12995 C CD  . LYS D 89  ? 0.7567 1.2850 1.0355 -0.1187 0.1403  -0.1659 89  LYS D CD  
12996 C CE  . LYS D 89  ? 0.7754 1.3035 1.0644 -0.1390 0.1463  -0.1868 89  LYS D CE  
12997 N NZ  . LYS D 89  ? 0.5916 1.1744 0.9067 -0.1570 0.1471  -0.2101 89  LYS D NZ  
12998 N N   . GLU D 90  ? 0.9826 1.3472 1.1641 -0.0801 0.1234  -0.1126 90  GLU D N   
12999 C CA  . GLU D 90  ? 0.9794 1.3390 1.1391 -0.0691 0.1104  -0.1038 90  GLU D CA  
13000 C C   . GLU D 90  ? 0.9474 1.2698 1.0832 -0.0533 0.1077  -0.0823 90  GLU D C   
13001 O O   . GLU D 90  ? 0.9464 1.2735 1.0650 -0.0401 0.0972  -0.0716 90  GLU D O   
13002 C CB  . GLU D 90  ? 0.8593 1.2079 1.0229 -0.0793 0.1119  -0.1156 90  GLU D CB  
13003 C CG  . GLU D 90  ? 0.8745 1.2146 1.0647 -0.0965 0.1268  -0.1319 90  GLU D CG  
13004 C CD  . GLU D 90  ? 1.0258 1.3581 1.2255 -0.1066 0.1300  -0.1466 90  GLU D CD  
13005 O OE1 . GLU D 90  ? 0.9541 1.3042 1.1416 -0.1051 0.1209  -0.1507 90  GLU D OE1 
13006 O OE2 . GLU D 90  ? 1.0075 1.3159 1.2286 -0.1165 0.1427  -0.1543 90  GLU D OE2 
13007 N N   . GLU D 91  ? 0.9860 1.2718 1.1200 -0.0555 0.1172  -0.0753 91  GLU D N   
13008 C CA  . GLU D 91  ? 0.9457 1.1974 1.0550 -0.0437 0.1152  -0.0564 91  GLU D CA  
13009 C C   . GLU D 91  ? 0.8673 1.1331 0.9678 -0.0319 0.1132  -0.0489 91  GLU D C   
13010 O O   . GLU D 91  ? 0.7815 1.0296 0.8604 -0.0200 0.1079  -0.0363 91  GLU D O   
13011 C CB  . GLU D 91  ? 1.0118 1.2282 1.1212 -0.0510 0.1256  -0.0496 91  GLU D CB  
13012 C CG  . GLU D 91  ? 1.1015 1.3131 1.2356 -0.0658 0.1335  -0.0611 91  GLU D CG  
13013 C CD  . GLU D 91  ? 1.1422 1.3138 1.2748 -0.0710 0.1409  -0.0486 91  GLU D CD  
13014 O OE1 . GLU D 91  ? 1.1059 1.2756 1.2483 -0.0803 0.1524  -0.0493 91  GLU D OE1 
13015 O OE2 . GLU D 91  ? 1.0613 1.2045 1.1834 -0.0664 0.1350  -0.0370 91  GLU D OE2 
13016 N N   . VAL D 92  ? 0.7590 1.0571 0.8788 -0.0351 0.1181  -0.0574 92  VAL D N   
13017 C CA  . VAL D 92  ? 0.7341 1.0484 0.8531 -0.0229 0.1171  -0.0515 92  VAL D CA  
13018 C C   . VAL D 92  ? 0.7303 1.0669 0.8452 -0.0106 0.1024  -0.0472 92  VAL D C   
13019 O O   . VAL D 92  ? 0.6756 1.0043 0.7791 0.0038  0.0990  -0.0358 92  VAL D O   
13020 C CB  . VAL D 92  ? 0.7607 1.1065 0.9065 -0.0299 0.1264  -0.0622 92  VAL D CB  
13021 C CG1 . VAL D 92  ? 0.7375 1.0968 0.8871 -0.0164 0.1279  -0.0562 92  VAL D CG1 
13022 C CG2 . VAL D 92  ? 0.7888 1.1115 0.9382 -0.0446 0.1416  -0.0658 92  VAL D CG2 
13023 N N   . GLU D 93  ? 0.7868 1.1513 0.9107 -0.0171 0.0942  -0.0562 93  GLU D N   
13024 C CA  . GLU D 93  ? 0.8143 1.1995 0.9307 -0.0075 0.0794  -0.0499 93  GLU D CA  
13025 C C   . GLU D 93  ? 0.8068 1.1558 0.8959 -0.0001 0.0744  -0.0386 93  GLU D C   
13026 O O   . GLU D 93  ? 0.8362 1.1890 0.9145 0.0122  0.0649  -0.0273 93  GLU D O   
13027 C CB  . GLU D 93  ? 0.8100 1.2345 0.9381 -0.0200 0.0726  -0.0636 93  GLU D CB  
13028 C CG  . GLU D 93  ? 0.8493 1.3003 1.0040 -0.0349 0.0813  -0.0806 93  GLU D CG  
13029 C CD  . GLU D 93  ? 1.0440 1.5146 1.2060 -0.0534 0.0809  -0.0993 93  GLU D CD  
13030 O OE1 . GLU D 93  ? 1.2312 1.7453 1.4134 -0.0642 0.0800  -0.1128 93  GLU D OE1 
13031 O OE2 . GLU D 93  ? 0.8712 1.3154 1.0203 -0.0577 0.0819  -0.1016 93  GLU D OE2 
13032 N N   . LYS D 94  ? 0.7710 1.0854 0.8510 -0.0074 0.0803  -0.0407 94  LYS D N   
13033 C CA  . LYS D 94  ? 0.7933 1.0746 0.8498 -0.0009 0.0756  -0.0304 94  LYS D CA  
13034 C C   . LYS D 94  ? 0.7897 1.0475 0.8310 0.0120  0.0774  -0.0165 94  LYS D C   
13035 O O   . LYS D 94  ? 0.8129 1.0596 0.8377 0.0220  0.0707  -0.0067 94  LYS D O   
13036 C CB  . LYS D 94  ? 0.8572 1.1091 0.9128 -0.0110 0.0809  -0.0346 94  LYS D CB  
13037 C CG  . LYS D 94  ? 0.9109 1.1803 0.9859 -0.0257 0.0835  -0.0518 94  LYS D CG  
13038 C CD  . LYS D 94  ? 0.9682 1.2830 1.0505 -0.0292 0.0765  -0.0618 94  LYS D CD  
13039 C CE  . LYS D 94  ? 0.9990 1.3254 1.0913 -0.0439 0.0781  -0.0793 94  LYS D CE  
13040 N NZ  . LYS D 94  ? 0.8924 1.2654 0.9848 -0.0486 0.0696  -0.0872 94  LYS D NZ  
13041 N N   . LEU D 95  ? 0.8257 1.0759 0.8723 0.0106  0.0880  -0.0166 95  LEU D N   
13042 C CA  . LEU D 95  ? 0.7994 1.0314 0.8333 0.0210  0.0923  -0.0071 95  LEU D CA  
13043 C C   . LEU D 95  ? 0.7761 1.0345 0.8209 0.0341  0.0883  -0.0039 95  LEU D C   
13044 O O   . LEU D 95  ? 0.7729 1.0156 0.8063 0.0456  0.0882  0.0047  95  LEU D O   
13045 C CB  . LEU D 95  ? 0.7836 1.0031 0.8196 0.0135  0.1062  -0.0094 95  LEU D CB  
13046 C CG  . LEU D 95  ? 0.9050 1.0833 0.9165 0.0084  0.1096  -0.0017 95  LEU D CG  
13047 C CD1 . LEU D 95  ? 0.9470 1.1166 0.9621 -0.0042 0.1219  -0.0037 95  LEU D CD1 
13048 C CD2 . LEU D 95  ? 0.8473 1.0056 0.8367 0.0183  0.1102  0.0066  95  LEU D CD2 
13049 N N   . ILE D 96  ? 0.7691 1.0682 0.8376 0.0325  0.0846  -0.0106 96  ILE D N   
13050 C CA  . ILE D 96  ? 0.7642 1.0922 0.8467 0.0459  0.0775  -0.0045 96  ILE D CA  
13051 C C   . ILE D 96  ? 0.8168 1.1395 0.8829 0.0543  0.0645  0.0066  96  ILE D C   
13052 O O   . ILE D 96  ? 0.8767 1.1929 0.9410 0.0688  0.0622  0.0179  96  ILE D O   
13053 C CB  . ILE D 96  ? 0.7726 1.1499 0.8837 0.0402  0.0740  -0.0135 96  ILE D CB  
13054 C CG1 . ILE D 96  ? 0.7255 1.1123 0.8582 0.0379  0.0876  -0.0210 96  ILE D CG1 
13055 C CG2 . ILE D 96  ? 0.7839 1.1956 0.9061 0.0521  0.0597  -0.0040 96  ILE D CG2 
13056 C CD1 . ILE D 96  ? 0.5824 1.0177 0.7444 0.0295  0.0851  -0.0320 96  ILE D CD1 
13057 N N   . GLU D 97  ? 0.8048 1.1286 0.8598 0.0446  0.0575  0.0028  97  GLU D N   
13058 C CA  . GLU D 97  ? 0.8325 1.1529 0.8708 0.0499  0.0462  0.0124  97  GLU D CA  
13059 C C   . GLU D 97  ? 0.8171 1.0938 0.8335 0.0583  0.0493  0.0222  97  GLU D C   
13060 O O   . GLU D 97  ? 0.8627 1.1351 0.8715 0.0694  0.0432  0.0343  97  GLU D O   
13061 C CB  . GLU D 97  ? 0.8643 1.1932 0.8959 0.0354  0.0415  0.0027  97  GLU D CB  
13062 C CG  . GLU D 97  ? 1.0555 1.4087 1.0791 0.0364  0.0283  0.0090  97  GLU D CG  
13063 C CD  . GLU D 97  ? 1.1500 1.5550 1.1925 0.0344  0.0202  0.0073  97  GLU D CD  
13064 O OE1 . GLU D 97  ? 1.2995 1.7247 1.3400 0.0432  0.0086  0.0215  97  GLU D OE1 
13065 O OE2 . GLU D 97  ? 1.1864 1.6124 1.2467 0.0235  0.0252  -0.0075 97  GLU D OE2 
13066 N N   . PHE D 98  ? 0.7793 1.0240 0.7857 0.0524  0.0586  0.0179  98  PHE D N   
13067 C CA  . PHE D 98  ? 0.8099 1.0156 0.7942 0.0575  0.0612  0.0255  98  PHE D CA  
13068 C C   . PHE D 98  ? 0.8693 1.0681 0.8558 0.0711  0.0659  0.0328  98  PHE D C   
13069 O O   . PHE D 98  ? 0.8452 1.0278 0.8200 0.0797  0.0629  0.0416  98  PHE D O   
13070 C CB  . PHE D 98  ? 0.7342 0.9124 0.7089 0.0475  0.0690  0.0209  98  PHE D CB  
13071 C CG  . PHE D 98  ? 0.8385 0.9832 0.7898 0.0471  0.0667  0.0266  98  PHE D CG  
13072 C CD1 . PHE D 98  ? 0.7794 0.9220 0.7255 0.0425  0.0590  0.0259  98  PHE D CD1 
13073 C CD2 . PHE D 98  ? 0.8867 1.0042 0.8220 0.0501  0.0729  0.0312  98  PHE D CD2 
13074 C CE1 . PHE D 98  ? 0.8015 0.9162 0.7294 0.0420  0.0565  0.0307  98  PHE D CE1 
13075 C CE2 . PHE D 98  ? 0.9241 1.0141 0.8386 0.0484  0.0698  0.0358  98  PHE D CE2 
13076 C CZ  . PHE D 98  ? 0.7933 0.8822 0.7052 0.0449  0.0611  0.0362  98  PHE D CZ  
13077 N N   . THR D 99  ? 0.8456 1.0555 0.8490 0.0727  0.0751  0.0282  99  THR D N   
13078 C CA  . THR D 99  ? 0.8121 1.0180 0.8242 0.0859  0.0818  0.0328  99  THR D CA  
13079 C C   . THR D 99  ? 0.8478 1.0754 0.8741 0.0994  0.0712  0.0434  99  THR D C   
13080 O O   . THR D 99  ? 0.8093 1.0197 0.8332 0.1112  0.0726  0.0519  99  THR D O   
13081 C CB  . THR D 99  ? 0.8268 1.0475 0.8597 0.0843  0.0940  0.0243  99  THR D CB  
13082 O OG1 . THR D 99  ? 0.9212 1.1854 0.9836 0.0878  0.0874  0.0235  99  THR D OG1 
13083 C CG2 . THR D 99  ? 0.7794 0.9876 0.8011 0.0682  0.1016  0.0158  99  THR D CG2 
13084 N N   . LYS D 100 ? 0.8530 1.1189 0.8944 0.0970  0.0605  0.0434  100 LYS D N   
13085 C CA  . LYS D 100 ? 0.8198 1.1109 0.8732 0.1084  0.0478  0.0565  100 LYS D CA  
13086 C C   . LYS D 100 ? 0.8326 1.0998 0.8613 0.1113  0.0406  0.0676  100 LYS D C   
13087 O O   . LYS D 100 ? 0.8745 1.1393 0.9085 0.1249  0.0364  0.0819  100 LYS D O   
13088 C CB  . LYS D 100 ? 0.8034 1.1414 0.8708 0.1003  0.0368  0.0527  100 LYS D CB  
13089 C CG  . LYS D 100 ? 0.7707 1.1497 0.8666 0.1124  0.0270  0.0637  100 LYS D CG  
13090 C CD  . LYS D 100 ? 0.8388 1.2576 0.9322 0.1041  0.0101  0.0668  100 LYS D CD  
13091 C CE  . LYS D 100 ? 0.8493 1.2551 0.9192 0.1082  -0.0005 0.0829  100 LYS D CE  
13092 N NZ  . LYS D 100 ? 0.8842 1.2760 0.9643 0.1286  -0.0018 0.1026  100 LYS D NZ  
13093 N N   . LEU D 101 ? 0.8234 1.0720 0.8276 0.0988  0.0399  0.0615  101 LEU D N   
13094 C CA  . LEU D 101 ? 0.8548 1.0821 0.8361 0.0995  0.0340  0.0702  101 LEU D CA  
13095 C C   . LEU D 101 ? 0.7979 0.9857 0.7695 0.1086  0.0425  0.0758  101 LEU D C   
13096 O O   . LEU D 101 ? 0.8461 1.0231 0.8118 0.1169  0.0384  0.0882  101 LEU D O   
13097 C CB  . LEU D 101 ? 0.8570 1.0755 0.8203 0.0840  0.0327  0.0604  101 LEU D CB  
13098 C CG  . LEU D 101 ? 0.9092 1.1001 0.8489 0.0831  0.0300  0.0663  101 LEU D CG  
13099 C CD1 . LEU D 101 ? 0.8745 1.0863 0.8101 0.0849  0.0187  0.0771  101 LEU D CD1 
13100 C CD2 . LEU D 101 ? 0.9481 1.1239 0.8762 0.0695  0.0323  0.0550  101 LEU D CD2 
13101 N N   . ASN D 102 ? 0.8600 1.0259 0.8288 0.1058  0.0548  0.0665  102 ASN D N   
13102 C CA  . ASN D 102 ? 0.8950 1.0247 0.8529 0.1112  0.0646  0.0681  102 ASN D CA  
13103 C C   . ASN D 102 ? 0.8808 1.0136 0.8619 0.1236  0.0747  0.0687  102 ASN D C   
13104 O O   . ASN D 102 ? 0.9224 1.0271 0.8970 0.1252  0.0872  0.0643  102 ASN D O   
13105 C CB  . ASN D 102 ? 0.8088 0.9125 0.7457 0.0985  0.0718  0.0581  102 ASN D CB  
13106 C CG  . ASN D 102 ? 0.8711 0.9791 0.7967 0.0861  0.0633  0.0550  102 ASN D CG  
13107 O OD1 . ASN D 102 ? 0.9352 1.0364 0.8487 0.0846  0.0558  0.0595  102 ASN D OD1 
13108 N ND2 . ASN D 102 ? 0.8308 0.9497 0.7628 0.0769  0.0657  0.0468  102 ASN D ND2 
13109 N N   . TYR D 103 ? 0.8336 1.0018 0.8431 0.1319  0.0696  0.0733  103 TYR D N   
13110 C CA  . TYR D 103 ? 0.8299 1.0060 0.8690 0.1441  0.0798  0.0725  103 TYR D CA  
13111 C C   . TYR D 103 ? 0.8656 1.0134 0.9082 0.1574  0.0866  0.0802  103 TYR D C   
13112 O O   . TYR D 103 ? 0.9382 1.0677 0.9886 0.1607  0.1033  0.0716  103 TYR D O   
13113 C CB  . TYR D 103 ? 0.7631 0.9863 0.8343 0.1514  0.0693  0.0791  103 TYR D CB  
13114 C CG  . TYR D 103 ? 0.7801 1.0193 0.8879 0.1616  0.0803  0.0748  103 TYR D CG  
13115 C CD1 . TYR D 103 ? 0.9126 1.1401 1.0202 0.1541  0.0979  0.0583  103 TYR D CD1 
13116 C CD2 . TYR D 103 ? 0.8622 1.1298 1.0059 0.1782  0.0731  0.0879  103 TYR D CD2 
13117 C CE1 . TYR D 103 ? 0.9907 1.2340 1.1333 0.1624  0.1101  0.0523  103 TYR D CE1 
13118 C CE2 . TYR D 103 ? 0.8653 1.1496 1.0482 0.1883  0.0838  0.0830  103 TYR D CE2 
13119 C CZ  . TYR D 103 ? 0.9376 1.2095 1.1199 0.1800  0.1033  0.0639  103 TYR D CZ  
13120 O OH  . TYR D 103 ? 1.0072 1.2967 1.2296 0.1890  0.1160  0.0572  103 TYR D OH  
13121 N N   . GLU D 104 ? 0.8419 0.9853 0.8788 0.1638  0.0754  0.0956  104 GLU D N   
13122 C CA  . GLU D 104 ? 0.7531 0.8717 0.7992 0.1777  0.0810  0.1056  104 GLU D CA  
13123 C C   . GLU D 104 ? 0.7364 0.8097 0.7518 0.1702  0.0903  0.0992  104 GLU D C   
13124 O O   . GLU D 104 ? 0.8358 0.8833 0.8576 0.1795  0.0980  0.1044  104 GLU D O   
13125 C CB  . GLU D 104 ? 0.8255 0.9623 0.8812 0.1877  0.0640  0.1281  104 GLU D CB  
13126 C CG  . GLU D 104 ? 0.9356 1.1231 1.0072 0.1869  0.0491  0.1330  104 GLU D CG  
13127 C CD  . GLU D 104 ? 1.2412 1.4544 1.3434 0.2039  0.0374  0.1556  104 GLU D CD  
13128 O OE1 . GLU D 104 ? 1.3356 1.5911 1.4655 0.2079  0.0302  0.1575  104 GLU D OE1 
13129 O OE2 . GLU D 104 ? 1.3273 1.5191 1.4269 0.2128  0.0349  0.1723  104 GLU D OE2 
13130 N N   . LYS D 105 ? 0.7685 0.8320 0.7535 0.1534  0.0900  0.0882  105 LYS D N   
13131 C CA  . LYS D 105 ? 0.8971 0.9215 0.8544 0.1451  0.0983  0.0813  105 LYS D CA  
13132 C C   . LYS D 105 ? 0.9117 0.9169 0.8743 0.1453  0.1182  0.0676  105 LYS D C   
13133 O O   . LYS D 105 ? 0.8648 0.8856 0.8382 0.1427  0.1252  0.0581  105 LYS D O   
13134 C CB  . LYS D 105 ? 0.8522 0.8743 0.7799 0.1278  0.0915  0.0747  105 LYS D CB  
13135 C CG  . LYS D 105 ? 0.8912 0.9388 0.8172 0.1249  0.0747  0.0827  105 LYS D CG  
13136 C CD  . LYS D 105 ? 0.8978 0.9337 0.7972 0.1103  0.0692  0.0779  105 LYS D CD  
13137 C CE  . LYS D 105 ? 0.8518 0.9128 0.7510 0.1064  0.0554  0.0830  105 LYS D CE  
13138 N NZ  . LYS D 105 ? 0.9889 1.0346 0.8663 0.0956  0.0509  0.0810  105 LYS D NZ  
13139 N N   . PRO D 106 ? 0.9249 0.8968 0.8806 0.1470  0.1289  0.0651  106 PRO D N   
13140 C CA  . PRO D 106 ? 0.9837 0.9378 0.9446 0.1457  0.1502  0.0494  106 PRO D CA  
13141 C C   . PRO D 106 ? 0.9982 0.9524 0.9353 0.1280  0.1565  0.0341  106 PRO D C   
13142 O O   . PRO D 106 ? 0.9356 0.8894 0.8818 0.1263  0.1732  0.0211  106 PRO D O   
13143 C CB  . PRO D 106 ? 1.0415 0.9583 0.9901 0.1453  0.1579  0.0484  106 PRO D CB  
13144 C CG  . PRO D 106 ? 1.0025 0.9232 0.9594 0.1562  0.1426  0.0689  106 PRO D CG  
13145 C CD  . PRO D 106 ? 0.9715 0.9215 0.9164 0.1497  0.1237  0.0755  106 PRO D CD  
13146 N N   . ILE D 107 ? 0.9905 0.9455 0.8989 0.1147  0.1441  0.0357  107 ILE D N   
13147 C CA  . ILE D 107 ? 0.9858 0.9409 0.8726 0.0981  0.1484  0.0252  107 ILE D CA  
13148 C C   . ILE D 107 ? 0.9326 0.9168 0.8393 0.0993  0.1500  0.0230  107 ILE D C   
13149 O O   . ILE D 107 ? 0.7586 0.7428 0.6544 0.0875  0.1594  0.0133  107 ILE D O   
13150 C CB  . ILE D 107 ? 0.9384 0.8879 0.7964 0.0856  0.1337  0.0298  107 ILE D CB  
13151 C CG1 . ILE D 107 ? 0.9837 0.9515 0.8527 0.0927  0.1164  0.0424  107 ILE D CG1 
13152 C CG2 . ILE D 107 ? 0.8741 0.7936 0.7075 0.0784  0.1367  0.0263  107 ILE D CG2 
13153 C CD1 . ILE D 107 ? 0.9521 0.9270 0.8060 0.0810  0.1038  0.0442  107 ILE D CD1 
13154 N N   . TYR D 108 ? 0.9880 0.9985 0.9232 0.1121  0.1410  0.0320  108 TYR D N   
13155 C CA  . TYR D 108 ? 0.9644 1.0066 0.9233 0.1136  0.1419  0.0295  108 TYR D CA  
13156 C C   . TYR D 108 ? 0.9576 1.0096 0.9516 0.1271  0.1556  0.0254  108 TYR D C   
13157 O O   . TYR D 108 ? 0.9379 1.0215 0.9638 0.1368  0.1507  0.0300  108 TYR D O   
13158 C CB  . TYR D 108 ? 0.8077 0.8780 0.7771 0.1170  0.1231  0.0401  108 TYR D CB  
13159 C CG  . TYR D 108 ? 0.9082 0.9817 0.8568 0.1018  0.1142  0.0386  108 TYR D CG  
13160 C CD1 . TYR D 108 ? 0.8801 0.9311 0.8002 0.0936  0.1074  0.0411  108 TYR D CD1 
13161 C CD2 . TYR D 108 ? 0.9083 1.0078 0.8697 0.0959  0.1130  0.0343  108 TYR D CD2 
13162 C CE1 . TYR D 108 ? 0.8584 0.9121 0.7657 0.0812  0.0997  0.0402  108 TYR D CE1 
13163 C CE2 . TYR D 108 ? 0.9108 1.0108 0.8579 0.0826  0.1062  0.0329  108 TYR D CE2 
13164 C CZ  . TYR D 108 ? 0.8951 0.9719 0.8165 0.0760  0.0995  0.0364  108 TYR D CZ  
13165 O OH  . TYR D 108 ? 0.8318 0.9087 0.7448 0.0643  0.0933  0.0355  108 TYR D OH  
13166 N N   . ARG D 109 ? 0.9629 0.9900 0.9546 0.1276  0.1733  0.0159  109 ARG D N   
13167 C CA  . ARG D 109 ? 0.9822 1.0160 1.0124 0.1415  0.1887  0.0106  109 ARG D CA  
13168 C C   . ARG D 109 ? 0.9520 0.9889 0.9813 0.1299  0.2086  -0.0077 109 ARG D C   
13169 O O   . ARG D 109 ? 0.8577 0.8710 0.8751 0.1229  0.2277  -0.0218 109 ARG D O   
13170 C CB  . ARG D 109 ? 0.9768 0.9806 1.0117 0.1510  0.1971  0.0114  109 ARG D CB  
13171 C CG  . ARG D 109 ? 1.0123 1.0255 1.0763 0.1711  0.1837  0.0308  109 ARG D CG  
13172 C CD  . ARG D 109 ? 1.0902 1.0843 1.1854 0.1862  0.1999  0.0289  109 ARG D CD  
13173 N NE  . ARG D 109 ? 1.1035 1.0584 1.1745 0.1826  0.2032  0.0293  109 ARG D NE  
13174 C CZ  . ARG D 109 ? 1.1214 1.0683 1.1834 0.1876  0.1871  0.0473  109 ARG D CZ  
13175 N NH1 . ARG D 109 ? 1.1212 1.0966 1.1935 0.1958  0.1659  0.0668  109 ARG D NH1 
13176 N NH2 . ARG D 109 ? 1.2163 1.1266 1.2578 0.1827  0.1931  0.0448  109 ARG D NH2 
13177 N N   . PHE D 110 ? 0.8900 0.9573 0.9309 0.1262  0.2047  -0.0082 110 PHE D N   
13178 C CA  . PHE D 110 ? 0.8495 0.9266 0.8962 0.1162  0.2234  -0.0238 110 PHE D CA  
13179 C C   . PHE D 110 ? 0.9126 1.0275 1.0100 0.1301  0.2242  -0.0231 110 PHE D C   
13180 O O   . PHE D 110 ? 0.9963 1.1369 1.1099 0.1381  0.2050  -0.0101 110 PHE D O   
13181 C CB  . PHE D 110 ? 0.9251 1.0026 0.9367 0.0950  0.2190  -0.0254 110 PHE D CB  
13182 C CG  . PHE D 110 ? 0.9637 1.0104 0.9282 0.0820  0.2122  -0.0221 110 PHE D CG  
13183 C CD1 . PHE D 110 ? 0.9938 1.0369 0.9464 0.0850  0.1909  -0.0083 110 PHE D CD1 
13184 C CD2 . PHE D 110 ? 0.7945 0.8186 0.7271 0.0656  0.2272  -0.0332 110 PHE D CD2 
13185 C CE1 . PHE D 110 ? 0.9600 0.9776 0.8738 0.0734  0.1843  -0.0054 110 PHE D CE1 
13186 C CE2 . PHE D 110 ? 0.8381 0.8379 0.7293 0.0533  0.2190  -0.0291 110 PHE D CE2 
13187 C CZ  . PHE D 110 ? 0.8731 0.8698 0.7571 0.0580  0.1975  -0.0151 110 PHE D CZ  
13188 N N   . GLU D 111 ? 1.0283 1.1488 1.1516 0.1319  0.2468  -0.0379 111 GLU D N   
13189 C CA  . GLU D 111 ? 0.9990 1.1583 1.1762 0.1458  0.2482  -0.0378 111 GLU D CA  
13190 C C   . GLU D 111 ? 0.9488 1.1396 1.1259 0.1345  0.2403  -0.0380 111 GLU D C   
13191 O O   . GLU D 111 ? 0.9096 1.1371 1.1219 0.1449  0.2274  -0.0301 111 GLU D O   
13192 C CB  . GLU D 111 ? 0.9238 1.0815 1.1320 0.1500  0.2768  -0.0559 111 GLU D CB  
13193 C CG  . GLU D 111 ? 1.0622 1.2636 1.3267 0.1604  0.2812  -0.0593 111 GLU D CG  
13194 C CD  . GLU D 111 ? 1.1575 1.3856 1.4662 0.1848  0.2604  -0.0396 111 GLU D CD  
13195 O OE1 . GLU D 111 ? 1.1783 1.3854 1.4869 0.1981  0.2525  -0.0271 111 GLU D OE1 
13196 O OE2 . GLU D 111 ? 1.1051 1.3763 1.4484 0.1896  0.2518  -0.0361 111 GLU D OE2 
13197 N N   . ARG D 112 ? 0.9110 1.0887 1.0494 0.1122  0.2472  -0.0462 112 ARG D N   
13198 C CA  . ARG D 112 ? 0.9506 1.1528 1.0871 0.0999  0.2400  -0.0457 112 ARG D CA  
13199 C C   . ARG D 112 ? 1.0022 1.2192 1.1383 0.1051  0.2129  -0.0300 112 ARG D C   
13200 O O   . ARG D 112 ? 0.9678 1.2202 1.1290 0.1055  0.2047  -0.0289 112 ARG D O   
13201 C CB  . ARG D 112 ? 0.9179 1.0965 1.0083 0.0757  0.2493  -0.0521 112 ARG D CB  
13202 C CG  . ARG D 112 ? 0.9283 1.1266 1.0171 0.0611  0.2455  -0.0521 112 ARG D CG  
13203 C CD  . ARG D 112 ? 0.9067 1.1334 1.0294 0.0579  0.2640  -0.0656 112 ARG D CD  
13204 N NE  . ARG D 112 ? 0.8940 1.1277 1.0040 0.0381  0.2667  -0.0677 112 ARG D NE  
13205 C CZ  . ARG D 112 ? 0.8543 1.1228 0.9979 0.0356  0.2699  -0.0736 112 ARG D CZ  
13206 N NH1 . ARG D 112 ? 0.7498 1.0531 0.9427 0.0519  0.2691  -0.0773 112 ARG D NH1 
13207 N NH2 . ARG D 112 ? 0.8746 1.1434 1.0038 0.0159  0.2738  -0.0750 112 ARG D NH2 
13208 N N   . ILE D 113 ? 0.9624 1.1544 1.0709 0.1078  0.1996  -0.0193 113 ILE D N   
13209 C CA  . ILE D 113 ? 0.9535 1.1590 1.0600 0.1116  0.1756  -0.0059 113 ILE D CA  
13210 C C   . ILE D 113 ? 1.0018 1.2453 1.1530 0.1292  0.1656  0.0014  113 ILE D C   
13211 O O   . ILE D 113 ? 1.0525 1.3268 1.2142 0.1273  0.1507  0.0059  113 ILE D O   
13212 C CB  . ILE D 113 ? 0.9019 1.0742 0.9754 0.1130  0.1659  0.0034  113 ILE D CB  
13213 C CG1 . ILE D 113 ? 0.9162 1.0587 0.9465 0.0940  0.1701  -0.0010 113 ILE D CG1 
13214 C CG2 . ILE D 113 ? 0.9733 1.1625 1.0502 0.1193  0.1432  0.0168  113 ILE D CG2 
13215 C CD1 . ILE D 113 ? 0.9762 1.0929 0.9759 0.0928  0.1575  0.0080  113 ILE D CD1 
13216 N N   . ARG D 114 ? 0.9451 1.1876 1.1242 0.1460  0.1736  0.0027  114 ARG D N   
13217 C CA  . ARG D 114 ? 0.9411 1.2199 1.1661 0.1647  0.1629  0.0132  114 ARG D CA  
13218 C C   . ARG D 114 ? 0.9057 1.2301 1.1644 0.1613  0.1638  0.0058  114 ARG D C   
13219 O O   . ARG D 114 ? 0.9384 1.2999 1.2140 0.1642  0.1452  0.0145  114 ARG D O   
13220 C CB  . ARG D 114 ? 1.0177 1.2822 1.2708 0.1830  0.1754  0.0145  114 ARG D CB  
13221 C CG  . ARG D 114 ? 1.0614 1.2750 1.2777 0.1799  0.1838  0.0132  114 ARG D CG  
13222 C CD  . ARG D 114 ? 1.0817 1.2795 1.3260 0.2001  0.1902  0.0198  114 ARG D CD  
13223 N NE  . ARG D 114 ? 1.1631 1.3236 1.3725 0.1994  0.1835  0.0288  114 ARG D NE  
13224 C CZ  . ARG D 114 ? 1.1691 1.2985 1.3856 0.2097  0.1941  0.0298  114 ARG D CZ  
13225 N NH1 . ARG D 114 ? 1.0674 1.1966 1.3266 0.2227  0.2127  0.0224  114 ARG D NH1 
13226 N NH2 . ARG D 114 ? 1.1063 1.2038 1.2886 0.2063  0.1872  0.0374  114 ARG D NH2 
13227 N N   . GLU D 115 ? 0.9397 1.2637 1.2082 0.1536  0.1858  -0.0112 115 GLU D N   
13228 C CA  . GLU D 115 ? 0.9570 1.3243 1.2606 0.1495  0.1895  -0.0200 115 GLU D CA  
13229 C C   . GLU D 115 ? 0.9977 1.3810 1.2811 0.1319  0.1768  -0.0207 115 GLU D C   
13230 O O   . GLU D 115 ? 0.9831 1.4106 1.2963 0.1318  0.1673  -0.0210 115 GLU D O   
13231 C CB  . GLU D 115 ? 0.9049 1.2640 1.2165 0.1414  0.2183  -0.0392 115 GLU D CB  
13232 C CG  . GLU D 115 ? 1.0143 1.3358 1.3194 0.1481  0.2370  -0.0447 115 GLU D CG  
13233 C CD  . GLU D 115 ? 0.9940 1.3050 1.2941 0.1334  0.2665  -0.0658 115 GLU D CD  
13234 O OE1 . GLU D 115 ? 0.8464 1.1809 1.1531 0.1199  0.2725  -0.0747 115 GLU D OE1 
13235 O OE2 . GLU D 115 ? 0.9555 1.2349 1.2441 0.1337  0.2847  -0.0743 115 GLU D OE2 
13236 N N   . LEU D 116 ? 1.0045 1.3528 1.2397 0.1164  0.1770  -0.0218 116 LEU D N   
13237 C CA  . LEU D 116 ? 0.9598 1.3176 1.1777 0.0994  0.1676  -0.0236 116 LEU D CA  
13238 C C   . LEU D 116 ? 0.9147 1.3049 1.1454 0.1054  0.1437  -0.0135 116 LEU D C   
13239 O O   . LEU D 116 ? 0.9282 1.3522 1.1740 0.0961  0.1378  -0.0189 116 LEU D O   
13240 C CB  . LEU D 116 ? 0.9019 1.2143 1.0694 0.0859  0.1694  -0.0225 116 LEU D CB  
13241 C CG  . LEU D 116 ? 0.9409 1.2289 1.0861 0.0686  0.1891  -0.0326 116 LEU D CG  
13242 C CD1 . LEU D 116 ? 0.9399 1.2415 1.0845 0.0510  0.1882  -0.0376 116 LEU D CD1 
13243 C CD2 . LEU D 116 ? 0.7819 1.0749 0.9481 0.0714  0.2112  -0.0436 116 LEU D CD2 
13244 N N   . MET D 117 ? 0.8926 1.2738 1.1172 0.1196  0.1305  0.0008  117 MET D N   
13245 C CA  . MET D 117 ? 0.8780 1.2908 1.1112 0.1244  0.1078  0.0119  117 MET D CA  
13246 C C   . MET D 117 ? 0.9269 1.3915 1.2095 0.1358  0.1017  0.0148  117 MET D C   
13247 O O   . MET D 117 ? 0.9241 1.4288 1.2177 0.1320  0.0851  0.0178  117 MET D O   
13248 C CB  . MET D 117 ? 0.9035 1.2903 1.1153 0.1354  0.0970  0.0277  117 MET D CB  
13249 C CG  . MET D 117 ? 0.8088 1.1445 0.9757 0.1259  0.1039  0.0250  117 MET D CG  
13250 S SD  . MET D 117 ? 0.9000 1.2288 1.0318 0.1066  0.0927  0.0223  117 MET D SD  
13251 C CE  . MET D 117 ? 0.6077 0.9476 0.7453 0.0873  0.1045  0.0049  117 MET D CE  
13252 N N   . ASN D 118 ? 0.9926 1.4589 1.3069 0.1491  0.1151  0.0130  118 ASN D N   
13253 C CA  . ASN D 118 ? 0.9134 1.4310 1.2811 0.1610  0.1099  0.0158  118 ASN D CA  
13254 C C   . ASN D 118 ? 0.9058 1.4592 1.2910 0.1447  0.1153  -0.0009 118 ASN D C   
13255 O O   . ASN D 118 ? 1.0043 1.6100 1.4220 0.1463  0.1017  0.0015  118 ASN D O   
13256 C CB  . ASN D 118 ? 0.8863 1.3936 1.2875 0.1797  0.1257  0.0163  118 ASN D CB  
13257 C CG  . ASN D 118 ? 1.0432 1.5135 1.4312 0.1957  0.1221  0.0321  118 ASN D CG  
13258 O OD1 . ASN D 118 ? 1.0119 1.4656 1.4237 0.2101  0.1369  0.0314  118 ASN D OD1 
13259 N ND2 . ASN D 118 ? 1.0292 1.4866 1.3815 0.1925  0.1043  0.0451  118 ASN D ND2 
13260 N N   . LYS D 119 ? 0.8818 1.4088 1.2452 0.1279  0.1345  -0.0170 119 LYS D N   
13261 C CA  . LYS D 119 ? 0.9087 1.4643 1.2857 0.1101  0.1413  -0.0328 119 LYS D CA  
13262 C C   . LYS D 119 ? 0.9541 1.5257 1.3124 0.0954  0.1239  -0.0326 119 LYS D C   
13263 O O   . LYS D 119 ? 0.9883 1.5259 1.3054 0.0882  0.1190  -0.0289 119 LYS D O   
13264 C CB  . LYS D 119 ? 0.9029 1.4226 1.2587 0.0953  0.1667  -0.0471 119 LYS D CB  
13265 C CG  . LYS D 119 ? 0.8933 1.4246 1.2850 0.1005  0.1884  -0.0580 119 LYS D CG  
13266 C CD  . LYS D 119 ? 0.9809 1.5564 1.4063 0.0879  0.1949  -0.0721 119 LYS D CD  
13267 C CE  . LYS D 119 ? 0.8582 1.4331 1.3056 0.0850  0.2230  -0.0871 119 LYS D CE  
13268 N NZ  . LYS D 119 ? 0.7925 1.3888 1.2497 0.0632  0.2352  -0.1026 119 LYS D NZ  
13269 N N   . GLU D 120 ? 0.8992 1.5249 1.2907 0.0905  0.1154  -0.0380 120 GLU D N   
13270 C CA  . GLU D 120 ? 0.8633 1.5131 1.2438 0.0752  0.0999  -0.0413 120 GLU D CA  
13271 C C   . GLU D 120 ? 0.9562 1.5780 1.3098 0.0518  0.1132  -0.0563 120 GLU D C   
13272 O O   . GLU D 120 ? 0.9306 1.5302 1.2513 0.0427  0.1063  -0.0551 120 GLU D O   
13273 C CB  . GLU D 120 ? 0.8905 1.6085 1.3164 0.0744  0.0891  -0.0453 120 GLU D CB  
13274 C CG  . GLU D 120 ? 1.0216 1.7645 1.4875 0.0696  0.1073  -0.0609 120 GLU D CG  
13275 C CD  . GLU D 120 ? 0.9949 1.7173 1.4790 0.0865  0.1248  -0.0585 120 GLU D CD  
13276 O OE1 . GLU D 120 ? 1.0325 1.7527 1.5311 0.0777  0.1469  -0.0736 120 GLU D OE1 
13277 O OE2 . GLU D 120 ? 0.9924 1.7005 1.4768 0.1073  0.1179  -0.0423 120 GLU D OE2 
13278 N N   . LYS D 121 ? 0.9405 1.5623 1.3092 0.0420  0.1331  -0.0700 121 LYS D N   
13279 C CA  . LYS D 121 ? 0.9634 1.5589 1.3115 0.0199  0.1473  -0.0822 121 LYS D CA  
13280 C C   . LYS D 121 ? 0.9427 1.4876 1.2671 0.0201  0.1670  -0.0807 121 LYS D C   
13281 O O   . LYS D 121 ? 0.9070 1.4521 1.2466 0.0318  0.1774  -0.0798 121 LYS D O   
13282 C CB  . LYS D 121 ? 0.9726 1.6100 1.3550 0.0040  0.1551  -0.0992 121 LYS D CB  
13283 C CG  . LYS D 121 ? 1.0122 1.6235 1.3785 -0.0199 0.1709  -0.1111 121 LYS D CG  
13284 C CD  . LYS D 121 ? 1.0348 1.6205 1.3696 -0.0290 0.1608  -0.1089 121 LYS D CD  
13285 C CE  . LYS D 121 ? 1.0056 1.6001 1.3494 -0.0533 0.1682  -0.1251 121 LYS D CE  
13286 N NZ  . LYS D 121 ? 0.8058 1.3471 1.1243 -0.0659 0.1845  -0.1244 121 LYS D NZ  
13287 N N   . LEU D 122 ? 0.8599 1.3626 1.1483 0.0065  0.1723  -0.0806 122 LEU D N   
13288 C CA  . LEU D 122 ? 0.8053 1.2585 1.0626 0.0053  0.1867  -0.0760 122 LEU D CA  
13289 C C   . LEU D 122 ? 0.7976 1.2297 1.0417 -0.0169 0.2017  -0.0829 122 LEU D C   
13290 O O   . LEU D 122 ? 0.8127 1.2483 1.0569 -0.0297 0.1966  -0.0869 122 LEU D O   
13291 C CB  . LEU D 122 ? 0.8328 1.2492 1.0540 0.0143  0.1745  -0.0624 122 LEU D CB  
13292 C CG  . LEU D 122 ? 0.8942 1.3266 1.1263 0.0359  0.1600  -0.0530 122 LEU D CG  
13293 C CD1 . LEU D 122 ? 0.7489 1.1616 0.9529 0.0397  0.1427  -0.0422 122 LEU D CD1 
13294 C CD2 . LEU D 122 ? 0.9008 1.3183 1.1359 0.0494  0.1719  -0.0503 122 LEU D CD2 
13295 N N   . ASN D 123 ? 0.8357 1.2456 1.0687 -0.0224 0.2210  -0.0843 123 ASN D N   
13296 C CA  . ASN D 123 ? 0.8241 1.2120 1.0427 -0.0439 0.2362  -0.0875 123 ASN D CA  
13297 C C   . ASN D 123 ? 0.8058 1.1415 0.9780 -0.0479 0.2351  -0.0743 123 ASN D C   
13298 O O   . ASN D 123 ? 0.7224 1.0406 0.8749 -0.0353 0.2222  -0.0648 123 ASN D O   
13299 C CB  . ASN D 123 ? 0.6970 1.0964 0.9311 -0.0512 0.2593  -0.0974 123 ASN D CB  
13300 C CG  . ASN D 123 ? 0.7080 1.1008 0.9378 -0.0370 0.2669  -0.0963 123 ASN D CG  
13301 O OD1 . ASN D 123 ? 0.7694 1.1959 1.0344 -0.0228 0.2666  -0.1022 123 ASN D OD1 
13302 N ND2 . ASN D 123 ? 0.8459 1.1960 1.0345 -0.0411 0.2738  -0.0887 123 ASN D ND2 
13303 N N   . ARG D 124 ? 0.8273 1.1390 0.9828 -0.0666 0.2486  -0.0727 124 ARG D N   
13304 C CA  . ARG D 124 ? 0.8555 1.1208 0.9692 -0.0725 0.2463  -0.0582 124 ARG D CA  
13305 C C   . ARG D 124 ? 0.8147 1.0597 0.9003 -0.0634 0.2489  -0.0523 124 ARG D C   
13306 O O   . ARG D 124 ? 0.8555 1.0736 0.9134 -0.0577 0.2371  -0.0411 124 ARG D O   
13307 C CB  . ARG D 124 ? 0.7513 0.9976 0.8547 -0.0947 0.2611  -0.0554 124 ARG D CB  
13308 C CG  . ARG D 124 ? 0.8164 1.0176 0.8759 -0.1018 0.2602  -0.0380 124 ARG D CG  
13309 C CD  . ARG D 124 ? 0.8267 1.0103 0.8759 -0.1241 0.2754  -0.0323 124 ARG D CD  
13310 N NE  . ARG D 124 ? 0.8248 0.9688 0.8305 -0.1314 0.2733  -0.0132 124 ARG D NE  
13311 C CZ  . ARG D 124 ? 0.8853 1.0176 0.8587 -0.1326 0.2800  -0.0097 124 ARG D CZ  
13312 N NH1 . ARG D 124 ? 0.9448 1.0987 0.9264 -0.1261 0.2911  -0.0245 124 ARG D NH1 
13313 N NH2 . ARG D 124 ? 1.0690 1.1684 1.0026 -0.1411 0.2755  0.0088  124 ARG D NH2 
13314 N N   . GLU D 125 ? 0.8304 1.0889 0.9251 -0.0626 0.2655  -0.0615 125 GLU D N   
13315 C CA  . GLU D 125 ? 0.8729 1.1116 0.9421 -0.0567 0.2720  -0.0596 125 GLU D CA  
13316 C C   . GLU D 125 ? 0.8864 1.1287 0.9616 -0.0344 0.2564  -0.0569 125 GLU D C   
13317 O O   . GLU D 125 ? 0.9977 1.2118 1.0420 -0.0302 0.2520  -0.0495 125 GLU D O   
13318 C CB  . GLU D 125 ? 0.8813 1.1364 0.9652 -0.0615 0.2961  -0.0734 125 GLU D CB  
13319 C CG  . GLU D 125 ? 0.9612 1.2070 1.0298 -0.0864 0.3152  -0.0748 125 GLU D CG  
13320 C CD  . GLU D 125 ? 1.0262 1.2858 1.1160 -0.0975 0.3124  -0.0747 125 GLU D CD  
13321 O OE1 . GLU D 125 ? 1.1104 1.3467 1.1766 -0.1164 0.3176  -0.0658 125 GLU D OE1 
13322 O OE2 . GLU D 125 ? 1.0267 1.3207 1.1572 -0.0880 0.3051  -0.0832 125 GLU D OE2 
13323 N N   . GLU D 126 ? 0.7978 1.0753 0.9118 -0.0209 0.2473  -0.0621 126 GLU D N   
13324 C CA  . GLU D 126 ? 0.8344 1.1164 0.9548 -0.0003 0.2312  -0.0568 126 GLU D CA  
13325 C C   . GLU D 126 ? 0.8565 1.1171 0.9518 -0.0001 0.2119  -0.0450 126 GLU D C   
13326 O O   . GLU D 126 ? 0.8641 1.1024 0.9380 0.0091  0.2041  -0.0372 126 GLU D O   
13327 C CB  . GLU D 126 ? 0.7550 1.0839 0.9231 0.0121  0.2250  -0.0628 126 GLU D CB  
13328 C CG  . GLU D 126 ? 0.8636 1.2197 1.0643 0.0093  0.2444  -0.0760 126 GLU D CG  
13329 C CD  . GLU D 126 ? 0.9500 1.3567 1.2014 0.0224  0.2362  -0.0804 126 GLU D CD  
13330 O OE1 . GLU D 126 ? 0.8129 1.2470 1.0811 0.0147  0.2277  -0.0836 126 GLU D OE1 
13331 O OE2 . GLU D 126 ? 1.0064 1.4261 1.2824 0.0398  0.2384  -0.0808 126 GLU D OE2 
13332 N N   . LEU D 127 ? 0.8310 1.0980 0.9309 -0.0108 0.2053  -0.0448 127 LEU D N   
13333 C CA  . LEU D 127 ? 0.8598 1.1069 0.9400 -0.0118 0.1892  -0.0356 127 LEU D CA  
13334 C C   . LEU D 127 ? 0.8303 1.0342 0.8700 -0.0175 0.1911  -0.0254 127 LEU D C   
13335 O O   . LEU D 127 ? 0.8273 1.0129 0.8484 -0.0103 0.1786  -0.0172 127 LEU D O   
13336 C CB  . LEU D 127 ? 0.8670 1.1254 0.9619 -0.0250 0.1870  -0.0400 127 LEU D CB  
13337 C CG  . LEU D 127 ? 0.8404 1.1438 0.9716 -0.0213 0.1799  -0.0500 127 LEU D CG  
13338 C CD1 . LEU D 127 ? 0.6870 0.9950 0.8287 -0.0369 0.1792  -0.0561 127 LEU D CD1 
13339 C CD2 . LEU D 127 ? 0.7978 1.1128 0.9296 -0.0047 0.1622  -0.0449 127 LEU D CD2 
13340 N N   . LEU D 128 ? 0.8390 1.0278 0.8642 -0.0316 0.2065  -0.0254 128 LEU D N   
13341 C CA  . LEU D 128 ? 0.8670 1.0190 0.8518 -0.0386 0.2083  -0.0152 128 LEU D CA  
13342 C C   . LEU D 128 ? 0.8959 1.0387 0.8660 -0.0260 0.2072  -0.0153 128 LEU D C   
13343 O O   . LEU D 128 ? 0.9095 1.0268 0.8512 -0.0252 0.1983  -0.0061 128 LEU D O   
13344 C CB  . LEU D 128 ? 0.8682 1.0119 0.8400 -0.0568 0.2269  -0.0160 128 LEU D CB  
13345 C CG  . LEU D 128 ? 0.8543 0.9726 0.8051 -0.0731 0.2240  -0.0024 128 LEU D CG  
13346 C CD1 . LEU D 128 ? 0.9104 1.0240 0.8498 -0.0920 0.2431  -0.0023 128 LEU D CD1 
13347 C CD2 . LEU D 128 ? 1.0697 1.1585 0.9852 -0.0716 0.2123  0.0112  128 LEU D CD2 
13348 N N   . ASP D 129 ? 0.8746 1.0385 0.8670 -0.0158 0.2165  -0.0258 129 ASP D N   
13349 C CA  . ASP D 129 ? 0.9067 1.0603 0.8904 -0.0034 0.2177  -0.0270 129 ASP D CA  
13350 C C   . ASP D 129 ? 0.8528 1.0046 0.8387 0.0116  0.1976  -0.0192 129 ASP D C   
13351 O O   . ASP D 129 ? 0.8931 1.0208 0.8547 0.0152  0.1932  -0.0142 129 ASP D O   
13352 C CB  . ASP D 129 ? 0.8958 1.0730 0.9107 0.0053  0.2331  -0.0397 129 ASP D CB  
13353 C CG  . ASP D 129 ? 1.0140 1.1809 1.0132 -0.0086 0.2566  -0.0488 129 ASP D CG  
13354 O OD1 . ASP D 129 ? 1.0847 1.2347 1.0541 -0.0275 0.2605  -0.0442 129 ASP D OD1 
13355 O OD2 . ASP D 129 ? 1.0212 1.1973 1.0389 -0.0013 0.2717  -0.0602 129 ASP D OD2 
13356 N N   . LEU D 130 ? 0.7860 0.9639 0.7994 0.0183  0.1858  -0.0188 130 LEU D N   
13357 C CA  . LEU D 130 ? 0.8779 1.0556 0.8906 0.0295  0.1670  -0.0111 130 LEU D CA  
13358 C C   . LEU D 130 ? 0.8368 0.9835 0.8167 0.0215  0.1580  -0.0024 130 LEU D C   
13359 O O   . LEU D 130 ? 0.7931 0.9223 0.7562 0.0285  0.1502  0.0035  130 LEU D O   
13360 C CB  . LEU D 130 ? 0.7860 0.9990 0.8291 0.0326  0.1567  -0.0134 130 LEU D CB  
13361 C CG  . LEU D 130 ? 0.7982 1.0189 0.8443 0.0455  0.1392  -0.0065 130 LEU D CG  
13362 C CD1 . LEU D 130 ? 0.9166 1.1476 0.9788 0.0629  0.1403  -0.0042 130 LEU D CD1 
13363 C CD2 . LEU D 130 ? 0.7886 1.0402 0.8539 0.0420  0.1280  -0.0093 130 LEU D CD2 
13364 N N   . GLN D 131 ? 0.8284 0.9684 0.8018 0.0068  0.1593  -0.0010 131 GLN D N   
13365 C CA  . GLN D 131 ? 0.8680 0.9796 0.8150 -0.0011 0.1511  0.0087  131 GLN D CA  
13366 C C   . GLN D 131 ? 0.9169 1.0012 0.8313 -0.0017 0.1538  0.0136  131 GLN D C   
13367 O O   . GLN D 131 ? 0.9418 1.0112 0.8415 0.0033  0.1428  0.0195  131 GLN D O   
13368 C CB  . GLN D 131 ? 0.9160 1.0219 0.8626 -0.0173 0.1566  0.0109  131 GLN D CB  
13369 C CG  . GLN D 131 ? 0.8695 0.9975 0.8465 -0.0203 0.1539  0.0050  131 GLN D CG  
13370 C CD  . GLN D 131 ? 0.9256 1.0444 0.9038 -0.0369 0.1626  0.0075  131 GLN D CD  
13371 O OE1 . GLN D 131 ? 0.8657 0.9738 0.8286 -0.0459 0.1747  0.0102  131 GLN D OE1 
13372 N NE2 . GLN D 131 ? 0.8454 0.9676 0.8420 -0.0421 0.1576  0.0062  131 GLN D NE2 
13373 N N   . THR D 132 ? 0.9029 0.9816 0.8054 -0.0096 0.1695  0.0097  132 THR D N   
13374 C CA  . THR D 132 ? 0.9453 0.9991 0.8133 -0.0148 0.1736  0.0124  132 THR D CA  
13375 C C   . THR D 132 ? 0.9774 1.0273 0.8453 -0.0004 0.1711  0.0088  132 THR D C   
13376 O O   . THR D 132 ? 0.9575 0.9865 0.8002 -0.0017 0.1647  0.0138  132 THR D O   
13377 C CB  . THR D 132 ? 0.9414 0.9942 0.7980 -0.0274 0.1936  0.0058  132 THR D CB  
13378 O OG1 . THR D 132 ? 0.9614 1.0167 0.8186 -0.0416 0.1965  0.0108  132 THR D OG1 
13379 C CG2 . THR D 132 ? 0.8695 0.8980 0.6860 -0.0369 0.1976  0.0077  132 THR D CG2 
13380 N N   . LEU D 133 ? 0.9565 1.0269 0.8543 0.0133  0.1758  0.0011  133 LEU D N   
13381 C CA  . LEU D 133 ? 0.9145 0.9793 0.8157 0.0276  0.1752  -0.0008 133 LEU D CA  
13382 C C   . LEU D 133 ? 0.8960 0.9541 0.7925 0.0350  0.1562  0.0087  133 LEU D C   
13383 O O   . LEU D 133 ? 0.9446 0.9845 0.8267 0.0397  0.1542  0.0102  133 LEU D O   
13384 C CB  . LEU D 133 ? 0.9059 0.9961 0.8452 0.0416  0.1830  -0.0081 133 LEU D CB  
13385 C CG  . LEU D 133 ? 0.9071 1.0041 0.8553 0.0360  0.2051  -0.0204 133 LEU D CG  
13386 C CD1 . LEU D 133 ? 0.8952 1.0248 0.8897 0.0504  0.2088  -0.0255 133 LEU D CD1 
13387 C CD2 . LEU D 133 ? 0.9384 1.0106 0.8650 0.0331  0.2195  -0.0277 133 LEU D CD2 
13388 N N   . ASN D 134 ? 0.8774 0.9501 0.7863 0.0349  0.1436  0.0135  134 ASN D N   
13389 C CA  . ASN D 134 ? 0.8519 0.9183 0.7545 0.0388  0.1272  0.0211  134 ASN D CA  
13390 C C   . ASN D 134 ? 0.9076 0.9451 0.7779 0.0291  0.1235  0.0264  134 ASN D C   
13391 O O   . ASN D 134 ? 0.9262 0.9506 0.7851 0.0336  0.1159  0.0301  134 ASN D O   
13392 C CB  . ASN D 134 ? 0.8267 0.9134 0.7475 0.0365  0.1177  0.0220  134 ASN D CB  
13393 C CG  . ASN D 134 ? 0.8232 0.9406 0.7724 0.0479  0.1136  0.0196  134 ASN D CG  
13394 O OD1 . ASN D 134 ? 0.8757 0.9979 0.8268 0.0557  0.1027  0.0240  134 ASN D OD1 
13395 N ND2 . ASN D 134 ? 0.8358 0.9762 0.8073 0.0480  0.1219  0.0132  134 ASN D ND2 
13396 N N   . LEU D 135 ? 0.9082 0.9366 0.7637 0.0151  0.1285  0.0278  135 LEU D N   
13397 C CA  . LEU D 135 ? 0.9348 0.9392 0.7596 0.0048  0.1237  0.0348  135 LEU D CA  
13398 C C   . LEU D 135 ? 0.9625 0.9511 0.7651 0.0046  0.1315  0.0301  135 LEU D C   
13399 O O   . LEU D 135 ? 0.9600 0.9327 0.7437 0.0028  0.1237  0.0340  135 LEU D O   
13400 C CB  . LEU D 135 ? 0.9179 0.9181 0.7322 -0.0106 0.1275  0.0398  135 LEU D CB  
13401 C CG  . LEU D 135 ? 1.0420 1.0422 0.8666 -0.0144 0.1152  0.0491  135 LEU D CG  
13402 C CD1 . LEU D 135 ? 1.0293 1.0183 0.8373 -0.0302 0.1183  0.0584  135 LEU D CD1 
13403 C CD2 . LEU D 135 ? 0.9677 0.9584 0.7884 -0.0094 0.0999  0.0548  135 LEU D CD2 
13404 N N   . LEU D 136 ? 0.9291 0.9227 0.7364 0.0059  0.1480  0.0202  136 LEU D N   
13405 C CA  . LEU D 136 ? 0.8866 0.8649 0.6762 0.0045  0.1593  0.0122  136 LEU D CA  
13406 C C   . LEU D 136 ? 0.9374 0.9108 0.7382 0.0198  0.1553  0.0109  136 LEU D C   
13407 O O   . LEU D 136 ? 0.9292 0.8848 0.7133 0.0177  0.1616  0.0054  136 LEU D O   
13408 C CB  . LEU D 136 ? 0.9625 0.9491 0.7606 0.0021  0.1804  0.0000  136 LEU D CB  
13409 C CG  . LEU D 136 ? 0.9693 0.9573 0.7497 -0.0164 0.1889  0.0000  136 LEU D CG  
13410 C CD1 . LEU D 136 ? 0.9571 0.9602 0.7574 -0.0157 0.2098  -0.0132 136 LEU D CD1 
13411 C CD2 . LEU D 136 ? 0.9401 0.9078 0.6766 -0.0345 0.1904  0.0016  136 LEU D CD2 
13412 N N   . ALA D 137 ? 1.0026 0.9915 0.8304 0.0337  0.1455  0.0158  137 ALA D N   
13413 C CA  . ALA D 137 ? 0.9519 0.9367 0.7906 0.0480  0.1417  0.0173  137 ALA D CA  
13414 C C   . ALA D 137 ? 1.0102 0.9763 0.8266 0.0442  0.1299  0.0231  137 ALA D C   
13415 O O   . ALA D 137 ? 1.0479 1.0014 0.8635 0.0513  0.1309  0.0227  137 ALA D O   
13416 C CB  . ALA D 137 ? 0.9071 0.9174 0.7776 0.0615  0.1333  0.0223  137 ALA D CB  
13417 N N   . TRP D 138 ? 0.9790 0.9430 0.7804 0.0333  0.1192  0.0289  138 TRP D N   
13418 C CA  . TRP D 138 ? 0.9613 0.9102 0.7443 0.0285  0.1079  0.0340  138 TRP D CA  
13419 C C   . TRP D 138 ? 0.9603 0.8919 0.7120 0.0132  0.1114  0.0319  138 TRP D C   
13420 O O   . TRP D 138 ? 1.0076 0.9315 0.7444 0.0055  0.0999  0.0380  138 TRP D O   
13421 C CB  . TRP D 138 ? 0.9462 0.9056 0.7384 0.0275  0.0928  0.0420  138 TRP D CB  
13422 C CG  . TRP D 138 ? 0.9221 0.9033 0.7423 0.0386  0.0899  0.0423  138 TRP D CG  
13423 C CD1 . TRP D 138 ? 0.8973 0.8979 0.7361 0.0398  0.0942  0.0399  138 TRP D CD1 
13424 C CD2 . TRP D 138 ? 0.9256 0.9137 0.7568 0.0480  0.0820  0.0452  138 TRP D CD2 
13425 N NE1 . TRP D 138 ? 0.8544 0.8753 0.7149 0.0491  0.0885  0.0406  138 TRP D NE1 
13426 C CE2 . TRP D 138 ? 0.8987 0.9123 0.7536 0.0542  0.0809  0.0446  138 TRP D CE2 
13427 C CE3 . TRP D 138 ? 0.9719 0.9480 0.7942 0.0505  0.0760  0.0483  138 TRP D CE3 
13428 C CZ2 . TRP D 138 ? 0.8959 0.9245 0.7632 0.0620  0.0731  0.0478  138 TRP D CZ2 
13429 C CZ3 . TRP D 138 ? 1.0068 0.9958 0.8420 0.0586  0.0695  0.0518  138 TRP D CZ3 
13430 C CH2 . TRP D 138 ? 0.9727 0.9882 0.8289 0.0640  0.0677  0.0520  138 TRP D CH2 
13431 N N   . CYS D 139 ? 0.9442 0.8717 0.6865 0.0077  0.1273  0.0230  139 CYS D N   
13432 C CA  . CYS D 139 ? 1.0645 0.9789 0.7733 -0.0098 0.1317  0.0200  139 CYS D CA  
13433 C C   . CYS D 139 ? 1.0937 0.9908 0.7860 -0.0121 0.1304  0.0157  139 CYS D C   
13434 O O   . CYS D 139 ? 1.0972 0.9868 0.8005 -0.0024 0.1397  0.0075  139 CYS D O   
13435 C CB  . CYS D 139 ? 1.0892 1.0050 0.7924 -0.0164 0.1519  0.0086  139 CYS D CB  
13436 S SG  . CYS D 139 ? 1.1839 1.0886 0.8405 -0.0423 0.1573  0.0053  139 CYS D SG  
13437 N N   . GLY D 140 ? 1.1330 1.0240 0.8008 -0.0253 0.1186  0.0218  140 GLY D N   
13438 C CA  . GLY D 140 ? 1.1234 1.0003 0.7751 -0.0302 0.1158  0.0175  140 GLY D CA  
13439 C C   . GLY D 140 ? 1.1332 0.9989 0.7571 -0.0451 0.1311  0.0034  140 GLY D C   
13440 O O   . GLY D 140 ? 1.1962 1.0655 0.8089 -0.0541 0.1432  -0.0022 140 GLY D O   
13441 N N   . ARG D 141 ? 1.1619 1.0142 0.7745 -0.0493 0.1313  -0.0036 141 ARG D N   
13442 C CA  . ARG D 141 ? 1.1925 1.0330 0.7793 -0.0648 0.1473  -0.0207 141 ARG D CA  
13443 C C   . ARG D 141 ? 1.1980 1.0462 0.7496 -0.0875 0.1449  -0.0190 141 ARG D C   
13444 O O   . ARG D 141 ? 1.2622 1.1082 0.7958 -0.1000 0.1631  -0.0332 141 ARG D O   
13445 C CB  . ARG D 141 ? 1.1638 0.9903 0.7435 -0.0682 0.1441  -0.0265 141 ARG D CB  
13446 C CG  . ARG D 141 ? 1.2543 1.0631 0.8287 -0.0731 0.1672  -0.0483 141 ARG D CG  
13447 C CD  . ARG D 141 ? 1.1730 0.9681 0.7381 -0.0799 0.1634  -0.0541 141 ARG D CD  
13448 N NE  . ARG D 141 ? 1.2105 1.0160 0.7492 -0.0968 0.1435  -0.0457 141 ARG D NE  
13449 C CZ  . ARG D 141 ? 1.2420 1.0432 0.7522 -0.1178 0.1446  -0.0572 141 ARG D CZ  
13450 N NH1 . ARG D 141 ? 1.2018 0.9862 0.7045 -0.1259 0.1666  -0.0797 141 ARG D NH1 
13451 N NH2 . ARG D 141 ? 1.3202 1.1351 0.8108 -0.1313 0.1234  -0.0462 141 ARG D NH2 
13452 N N   . THR D 142 ? 1.2535 1.1114 0.7959 -0.0935 0.1229  -0.0013 142 THR D N   
13453 C CA  . THR D 142 ? 1.2637 1.1287 0.7697 -0.1166 0.1171  0.0039  142 THR D CA  
13454 C C   . THR D 142 ? 1.2177 1.0904 0.7178 -0.1218 0.1276  0.0060  142 THR D C   
13455 O O   . THR D 142 ? 1.2371 1.1110 0.7045 -0.1419 0.1385  -0.0021 142 THR D O   
13456 C CB  . THR D 142 ? 1.1888 1.0625 0.6940 -0.1189 0.0899  0.0249  142 THR D CB  
13457 O OG1 . THR D 142 ? 1.2273 1.0949 0.7347 -0.1177 0.0823  0.0202  142 THR D OG1 
13458 C CG2 . THR D 142 ? 1.3152 1.1983 0.7845 -0.1419 0.0808  0.0355  142 THR D CG2 
13459 N N   . LEU D 143 ? 1.2260 1.1049 0.7567 -0.1054 0.1259  0.0151  143 LEU D N   
13460 C CA  . LEU D 143 ? 1.2902 1.1773 0.8192 -0.1102 0.1353  0.0180  143 LEU D CA  
13461 C C   . LEU D 143 ? 1.2457 1.1308 0.7858 -0.1052 0.1617  -0.0022 143 LEU D C   
13462 O O   . LEU D 143 ? 1.1930 1.0863 0.7383 -0.1071 0.1720  -0.0022 143 LEU D O   
13463 C CB  . LEU D 143 ? 1.2091 1.1049 0.7677 -0.0968 0.1219  0.0357  143 LEU D CB  
13464 C CG  . LEU D 143 ? 1.1732 1.0731 0.7208 -0.1060 0.1002  0.0582  143 LEU D CG  
13465 C CD1 . LEU D 143 ? 1.2179 1.1247 0.7980 -0.0940 0.0932  0.0712  143 LEU D CD1 
13466 C CD2 . LEU D 143 ? 1.1964 1.0982 0.7028 -0.1305 0.1032  0.0628  143 LEU D CD2 
13467 N N   . ARG D 144 ? 1.2432 1.1174 0.7900 -0.0991 0.1735  -0.0194 144 ARG D N   
13468 C CA  . ARG D 144 ? 1.2298 1.1019 0.7943 -0.0923 0.1991  -0.0385 144 ARG D CA  
13469 C C   . ARG D 144 ? 1.2869 1.1618 0.8215 -0.1145 0.2183  -0.0512 144 ARG D C   
13470 O O   . ARG D 144 ? 1.3606 1.2431 0.9108 -0.1116 0.2351  -0.0585 144 ARG D O   
13471 C CB  . ARG D 144 ? 1.2278 1.0842 0.8049 -0.0830 0.2085  -0.0533 144 ARG D CB  
13472 C CG  . ARG D 144 ? 1.0809 0.9352 0.6943 -0.0582 0.1967  -0.0438 144 ARG D CG  
13473 C CD  . ARG D 144 ? 1.1878 1.0552 0.8408 -0.0383 0.2006  -0.0396 144 ARG D CD  
13474 N NE  . ARG D 144 ? 1.3163 1.1812 1.0006 -0.0167 0.1926  -0.0332 144 ARG D NE  
13475 C CZ  . ARG D 144 ? 1.3596 1.2364 1.0805 0.0024  0.1934  -0.0288 144 ARG D CZ  
13476 N NH1 . ARG D 144 ? 1.2430 1.1362 0.9783 0.0041  0.2015  -0.0307 144 ARG D NH1 
13477 N NH2 . ARG D 144 ? 1.2189 1.0927 0.9621 0.0192  0.1854  -0.0217 144 ARG D NH2 
13478 N N   . LYS D 145 ? 1.3066 1.1776 0.7979 -0.1383 0.2163  -0.0544 145 LYS D N   
13479 C CA  . LYS D 145 ? 1.2732 1.1474 0.7310 -0.1627 0.2365  -0.0690 145 LYS D CA  
13480 C C   . LYS D 145 ? 1.3149 1.2031 0.7625 -0.1716 0.2331  -0.0535 145 LYS D C   
13481 O O   . LYS D 145 ? 1.3810 1.2749 0.8293 -0.1780 0.2552  -0.0657 145 LYS D O   
13482 C CB  . LYS D 145 ? 1.2583 1.1282 0.6693 -0.1883 0.2328  -0.0753 145 LYS D CB  
13483 C CG  . LYS D 145 ? 1.2992 1.1766 0.6663 -0.2187 0.2495  -0.0862 145 LYS D CG  
13484 C CD  . LYS D 145 ? 1.2707 1.1434 0.5970 -0.2438 0.2558  -0.1045 145 LYS D CD  
13485 C CE  . LYS D 145 ? 1.2698 1.1561 0.5398 -0.2786 0.2575  -0.1023 145 LYS D CE  
13486 N NZ  . LYS D 145 ? 1.3050 1.1999 0.5408 -0.2936 0.2264  -0.0794 145 LYS D NZ  
13487 N N   . ASP D 146 ? 1.3477 1.2413 0.7879 -0.1725 0.2067  -0.0268 146 ASP D N   
13488 C CA  . ASP D 146 ? 1.3896 1.2936 0.8204 -0.1819 0.2030  -0.0098 146 ASP D CA  
13489 C C   . ASP D 146 ? 1.4219 1.3320 0.8955 -0.1632 0.2134  -0.0115 146 ASP D C   
13490 O O   . ASP D 146 ? 1.5434 1.4612 1.0116 -0.1733 0.2273  -0.0129 146 ASP D O   
13491 C CB  . ASP D 146 ? 1.4294 1.3358 0.8513 -0.1841 0.1723  0.0199  146 ASP D CB  
13492 C CG  . ASP D 146 ? 1.5958 1.5098 0.9970 -0.2005 0.1684  0.0395  146 ASP D CG  
13493 O OD1 . ASP D 146 ? 1.6341 1.5518 1.0628 -0.1905 0.1724  0.0458  146 ASP D OD1 
13494 O OD2 . ASP D 146 ? 1.6300 1.5468 0.9873 -0.2244 0.1612  0.0492  146 ASP D OD2 
13495 N N   . LEU D 147 ? 1.2638 1.1723 0.7796 -0.1372 0.2072  -0.0119 147 LEU D N   
13496 C CA  . LEU D 147 ? 1.3036 1.2215 0.8620 -0.1190 0.2149  -0.0141 147 LEU D CA  
13497 C C   . LEU D 147 ? 1.2796 1.1975 0.8612 -0.1091 0.2394  -0.0384 147 LEU D C   
13498 O O   . LEU D 147 ? 1.3237 1.2497 0.9476 -0.0885 0.2419  -0.0404 147 LEU D O   
13499 C CB  . LEU D 147 ? 1.2324 1.1523 0.8235 -0.0978 0.1934  0.0007  147 LEU D CB  
13500 C CG  . LEU D 147 ? 1.2283 1.1477 0.8057 -0.1051 0.1700  0.0243  147 LEU D CG  
13501 C CD1 . LEU D 147 ? 1.2179 1.1418 0.8326 -0.0849 0.1538  0.0346  147 LEU D CD1 
13502 C CD2 . LEU D 147 ? 1.3455 1.2706 0.9052 -0.1225 0.1744  0.0341  147 LEU D CD2 
13503 N N   . LYS D 148 ? 1.2456 1.1556 0.8019 -0.1239 0.2576  -0.0571 148 LYS D N   
13504 C CA  . LYS D 148 ? 1.3093 1.2165 0.8923 -0.1135 0.2820  -0.0811 148 LYS D CA  
13505 C C   . LYS D 148 ? 1.2005 1.1228 0.8078 -0.1115 0.3022  -0.0903 148 LYS D C   
13506 O O   . LYS D 148 ? 1.1399 1.0684 0.7933 -0.0903 0.3108  -0.0978 148 LYS D O   
13507 C CB  . LYS D 148 ? 1.3452 1.2396 0.8958 -0.1322 0.2989  -0.1019 148 LYS D CB  
13508 C CG  . LYS D 148 ? 1.4245 1.3127 1.0116 -0.1174 0.3225  -0.1248 148 LYS D CG  
13509 C CD  . LYS D 148 ? 1.4082 1.2769 0.9938 -0.1126 0.3199  -0.1321 148 LYS D CD  
13510 C CE  . LYS D 148 ? 1.4044 1.2660 1.0427 -0.0868 0.3342  -0.1437 148 LYS D CE  
13511 N NZ  . LYS D 148 ? 1.4303 1.2945 1.1018 -0.0602 0.3102  -0.1217 148 LYS D NZ  
13512 N N   . ASP D 149 ? 1.2021 1.1315 0.7791 -0.1344 0.3107  -0.0898 149 ASP D N   
13513 C CA  . ASP D 149 ? 1.2016 1.1461 0.7998 -0.1357 0.3324  -0.1005 149 ASP D CA  
13514 C C   . ASP D 149 ? 1.2144 1.1734 0.8580 -0.1139 0.3202  -0.0869 149 ASP D C   
13515 O O   . ASP D 149 ? 1.1899 1.1615 0.8768 -0.0989 0.3343  -0.0986 149 ASP D O   
13516 C CB  . ASP D 149 ? 1.2377 1.1864 0.7900 -0.1666 0.3411  -0.0985 149 ASP D CB  
13517 C CG  . ASP D 149 ? 1.4210 1.3615 0.9329 -0.1904 0.3615  -0.1199 149 ASP D CG  
13518 O OD1 . ASP D 149 ? 1.4072 1.3433 0.9411 -0.1828 0.3828  -0.1451 149 ASP D OD1 
13519 O OD2 . ASP D 149 ? 1.4778 1.4167 0.9369 -0.2173 0.3564  -0.1114 149 ASP D OD2 
13520 N N   . LEU D 150 ? 1.1278 1.0864 0.7645 -0.1117 0.2938  -0.0629 150 LEU D N   
13521 C CA  . LEU D 150 ? 1.0602 1.0331 0.7386 -0.0929 0.2821  -0.0519 150 LEU D CA  
13522 C C   . LEU D 150 ? 1.0856 1.0620 0.8073 -0.0661 0.2803  -0.0587 150 LEU D C   
13523 O O   . LEU D 150 ? 1.0766 1.0712 0.8402 -0.0515 0.2847  -0.0620 150 LEU D O   
13524 C CB  . LEU D 150 ? 0.9971 0.9657 0.6622 -0.0950 0.2551  -0.0274 150 LEU D CB  
13525 C CG  . LEU D 150 ? 0.9819 0.9468 0.6072 -0.1203 0.2540  -0.0153 150 LEU D CG  
13526 C CD1 . LEU D 150 ? 1.1807 1.1335 0.7824 -0.1243 0.2281  0.0060  150 LEU D CD1 
13527 C CD2 . LEU D 150 ? 1.0437 1.0226 0.6895 -0.1225 0.2592  -0.0100 150 LEU D CD2 
13528 N N   . LEU D 151 ? 1.1436 1.1036 0.8557 -0.0604 0.2743  -0.0607 151 LEU D N   
13529 C CA  . LEU D 151 ? 1.0502 1.0105 0.8006 -0.0358 0.2719  -0.0641 151 LEU D CA  
13530 C C   . LEU D 151 ? 1.0590 1.0272 0.8424 -0.0274 0.2975  -0.0837 151 LEU D C   
13531 O O   . LEU D 151 ? 1.0420 1.0238 0.8708 -0.0059 0.2961  -0.0827 151 LEU D O   
13532 C CB  . LEU D 151 ? 1.0854 1.0238 0.8151 -0.0351 0.2629  -0.0629 151 LEU D CB  
13533 C CG  . LEU D 151 ? 1.1552 1.0909 0.8854 -0.0256 0.2351  -0.0437 151 LEU D CG  
13534 C CD1 . LEU D 151 ? 1.2411 1.1552 0.9459 -0.0302 0.2295  -0.0450 151 LEU D CD1 
13535 C CD2 . LEU D 151 ? 0.9981 0.9476 0.7739 -0.0011 0.2277  -0.0381 151 LEU D CD2 
13536 N N   . ASN D 152 ? 1.0489 1.0107 0.8116 -0.0449 0.3213  -0.1019 152 ASN D N   
13537 C CA  . ASN D 152 ? 1.0820 1.0492 0.8794 -0.0369 0.3482  -0.1233 152 ASN D CA  
13538 C C   . ASN D 152 ? 1.0811 1.0759 0.9155 -0.0309 0.3566  -0.1251 152 ASN D C   
13539 O O   . ASN D 152 ? 1.0836 1.0900 0.9662 -0.0136 0.3699  -0.1357 152 ASN D O   
13540 C CB  . ASN D 152 ? 1.1857 1.1392 0.9493 -0.0600 0.3737  -0.1454 152 ASN D CB  
13541 C CG  . ASN D 152 ? 1.2354 1.1688 1.0098 -0.0518 0.3856  -0.1608 152 ASN D CG  
13542 O OD1 . ASN D 152 ? 1.2306 1.1668 1.0554 -0.0296 0.3952  -0.1678 152 ASN D OD1 
13543 N ND2 . ASN D 152 ? 1.3682 1.2815 1.0969 -0.0697 0.3844  -0.1654 152 ASN D ND2 
13544 N N   . LYS D 153 ? 1.0836 1.0897 0.8992 -0.0448 0.3493  -0.1147 153 LYS D N   
13545 C CA  . LYS D 153 ? 1.0536 1.0871 0.9047 -0.0406 0.3561  -0.1162 153 LYS D CA  
13546 C C   . LYS D 153 ? 0.9978 1.0490 0.9013 -0.0124 0.3411  -0.1075 153 LYS D C   
13547 O O   . LYS D 153 ? 0.9407 1.0108 0.8915 0.0017  0.3539  -0.1179 153 LYS D O   
13548 C CB  . LYS D 153 ? 1.0815 1.1197 0.9032 -0.0596 0.3469  -0.1025 153 LYS D CB  
13549 C CG  . LYS D 153 ? 1.1217 1.1436 0.8858 -0.0889 0.3560  -0.1045 153 LYS D CG  
13550 C CD  . LYS D 153 ? 1.1146 1.1401 0.8555 -0.1050 0.3447  -0.0864 153 LYS D CD  
13551 C CE  . LYS D 153 ? 1.0834 1.1337 0.8671 -0.0971 0.3476  -0.0858 153 LYS D CE  
13552 N NZ  . LYS D 153 ? 1.0346 1.0961 0.8149 -0.1155 0.3754  -0.1005 153 LYS D NZ  
13553 N N   . GLY D 154 ? 1.0684 1.1153 0.9648 -0.0046 0.3138  -0.0883 154 GLY D N   
13554 C CA  . GLY D 154 ? 1.1094 1.1746 1.0483 0.0188  0.2976  -0.0786 154 GLY D CA  
13555 C C   . GLY D 154 ? 1.0575 1.1530 1.0225 0.0194  0.2923  -0.0742 154 GLY D C   
13556 O O   . GLY D 154 ? 1.1110 1.2242 1.1047 0.0351  0.2752  -0.0645 154 GLY D O   
13557 N N   . ARG D 155 ? 0.9810 1.0837 0.9358 0.0011  0.3067  -0.0811 155 ARG D N   
13558 C CA  . ARG D 155 ? 1.0057 1.1368 0.9863 -0.0008 0.3043  -0.0790 155 ARG D CA  
13559 C C   . ARG D 155 ? 1.0592 1.1835 1.0066 -0.0271 0.3158  -0.0803 155 ARG D C   
13560 O O   . ARG D 155 ? 1.0057 1.1054 0.9090 -0.0431 0.3224  -0.0806 155 ARG D O   
13561 C CB  . ARG D 155 ? 1.0296 1.1917 1.0655 0.0137  0.3175  -0.0915 155 ARG D CB  
13562 C CG  . ARG D 155 ? 1.0236 1.1778 1.0684 0.0162  0.3426  -0.1091 155 ARG D CG  
13563 C CD  . ARG D 155 ? 0.9869 1.1727 1.0951 0.0350  0.3529  -0.1190 155 ARG D CD  
13564 N NE  . ARG D 155 ? 0.9720 1.1790 1.1153 0.0567  0.3285  -0.1045 155 ARG D NE  
13565 C CZ  . ARG D 155 ? 1.0302 1.2352 1.1986 0.0791  0.3205  -0.0988 155 ARG D CZ  
13566 N NH1 . ARG D 155 ? 1.0860 1.2667 1.2523 0.0842  0.3355  -0.1075 155 ARG D NH1 
13567 N NH2 . ARG D 155 ? 1.0623 1.2902 1.2583 0.0956  0.2974  -0.0841 155 ARG D NH2 
13568 N N   . ASN D 156 ? 1.0305 1.1778 0.9992 -0.0328 0.3182  -0.0806 156 ASN D N   
13569 C CA  . ASN D 156 ? 1.1145 1.2589 1.0594 -0.0576 0.3325  -0.0821 156 ASN D CA  
13570 C C   . ASN D 156 ? 1.0792 1.1952 0.9738 -0.0736 0.3192  -0.0647 156 ASN D C   
13571 O O   . ASN D 156 ? 1.1542 1.2582 1.0144 -0.0959 0.3309  -0.0632 156 ASN D O   
13572 C CB  . ASN D 156 ? 1.1516 1.2955 1.0898 -0.0687 0.3623  -0.1007 156 ASN D CB  
13573 C CG  . ASN D 156 ? 1.1116 1.2746 1.0979 -0.0483 0.3741  -0.1172 156 ASN D CG  
13574 O OD1 . ASN D 156 ? 1.1603 1.3085 1.1393 -0.0436 0.3839  -0.1265 156 ASN D OD1 
13575 N ND2 . ASN D 156 ? 1.0203 1.2165 1.0580 -0.0362 0.3732  -0.1207 156 ASN D ND2 
13576 N N   . TYR D 157 ? 1.0405 1.1468 0.9314 -0.0626 0.2946  -0.0508 157 TYR D N   
13577 C CA  . TYR D 157 ? 1.0639 1.1455 0.9149 -0.0750 0.2800  -0.0333 157 TYR D CA  
13578 C C   . TYR D 157 ? 1.0972 1.1833 0.9515 -0.0884 0.2784  -0.0240 157 TYR D C   
13579 O O   . TYR D 157 ? 1.2048 1.3136 1.0968 -0.0828 0.2788  -0.0287 157 TYR D O   
13580 C CB  . TYR D 157 ? 0.9284 1.0009 0.7808 -0.0592 0.2558  -0.0230 157 TYR D CB  
13581 C CG  . TYR D 157 ? 0.9708 1.0338 0.8171 -0.0474 0.2567  -0.0298 157 TYR D CG  
13582 C CD1 . TYR D 157 ? 0.9793 1.0179 0.7833 -0.0582 0.2581  -0.0279 157 TYR D CD1 
13583 C CD2 . TYR D 157 ? 0.9632 1.0421 0.8468 -0.0264 0.2560  -0.0376 157 TYR D CD2 
13584 C CE1 . TYR D 157 ? 0.9709 0.9994 0.7711 -0.0488 0.2606  -0.0360 157 TYR D CE1 
13585 C CE2 . TYR D 157 ? 1.0290 1.0964 0.9100 -0.0155 0.2579  -0.0430 157 TYR D CE2 
13586 C CZ  . TYR D 157 ? 0.9831 1.0244 0.8229 -0.0270 0.2612  -0.0434 157 TYR D CZ  
13587 O OH  . TYR D 157 ? 0.9797 1.0083 0.8189 -0.0172 0.2648  -0.0504 157 TYR D OH  
13588 N N   . THR D 158 ? 1.0904 1.1548 0.9053 -0.1071 0.2765  -0.0102 158 THR D N   
13589 C CA  . THR D 158 ? 1.1176 1.1788 0.9324 -0.1205 0.2734  0.0030  158 THR D CA  
13590 C C   . THR D 158 ? 1.0454 1.0890 0.8525 -0.1161 0.2489  0.0219  158 THR D C   
13591 O O   . THR D 158 ? 1.0750 1.1079 0.8691 -0.1062 0.2353  0.0255  158 THR D O   
13592 C CB  . THR D 158 ? 1.0192 1.0695 0.7978 -0.1461 0.2899  0.0079  158 THR D CB  
13593 O OG1 . THR D 158 ? 1.0304 1.0562 0.7626 -0.1557 0.2792  0.0238  158 THR D OG1 
13594 C CG2 . THR D 158 ? 1.0070 1.0722 0.7877 -0.1507 0.3156  -0.0135 158 THR D CG2 
13595 N N   . GLN D 159 ? 0.9325 1.1806 0.9340 -0.1054 0.2198  0.3629  159 GLN D N   
13596 C CA  . GLN D 159 ? 0.9270 1.1481 0.9157 -0.1058 0.1986  0.3636  159 GLN D CA  
13597 C C   . GLN D 159 ? 0.9535 1.1721 0.9017 -0.1040 0.1994  0.3586  159 GLN D C   
13598 O O   . GLN D 159 ? 0.9771 1.1782 0.9114 -0.0976 0.1884  0.3450  159 GLN D O   
13599 C CB  . GLN D 159 ? 0.9842 1.1972 0.9883 -0.1171 0.1864  0.3861  159 GLN D CB  
13600 C CG  . GLN D 159 ? 1.0631 1.2482 1.0555 -0.1171 0.1654  0.3882  159 GLN D CG  
13601 C CD  . GLN D 159 ? 0.9835 1.1491 1.0036 -0.1165 0.1489  0.3847  159 GLN D CD  
13602 O OE1 . GLN D 159 ? 0.9015 1.0674 0.9367 -0.1095 0.1490  0.3693  159 GLN D OE1 
13603 N NE2 . GLN D 159 ? 0.9646 1.1131 0.9913 -0.1239 0.1349  0.3992  159 GLN D NE2 
13604 N N   . GLU D 160 ? 0.9098 1.1484 0.8386 -0.1097 0.2129  0.3687  160 GLU D N   
13605 C CA  . GLU D 160 ? 0.9564 1.1967 0.8452 -0.1094 0.2131  0.3658  160 GLU D CA  
13606 C C   . GLU D 160 ? 0.9928 1.2289 0.8654 -0.0992 0.2165  0.3381  160 GLU D C   
13607 O O   . GLU D 160 ? 0.9782 1.2001 0.8303 -0.0964 0.2040  0.3304  160 GLU D O   
13608 C CB  . GLU D 160 ? 0.9142 1.1817 0.7859 -0.1167 0.2308  0.3787  160 GLU D CB  
13609 C CG  . GLU D 160 ? 0.9304 1.1992 0.8070 -0.1280 0.2250  0.4087  160 GLU D CG  
13610 C CD  . GLU D 160 ? 1.0639 1.3353 0.9812 -0.1334 0.2273  0.4207  160 GLU D CD  
13611 O OE1 . GLU D 160 ? 1.0567 1.3486 0.9895 -0.1324 0.2447  0.4153  160 GLU D OE1 
13612 O OE2 . GLU D 160 ? 1.0447 1.2980 0.9797 -0.1387 0.2115  0.4351  160 GLU D OE2 
13613 N N   . GLU D 161 ? 1.0017 1.2502 0.8847 -0.0937 0.2338  0.3230  161 GLU D N   
13614 C CA  . GLU D 161 ? 0.9744 1.2165 0.8459 -0.0842 0.2381  0.2965  161 GLU D CA  
13615 C C   . GLU D 161 ? 0.8986 1.1143 0.7827 -0.0781 0.2198  0.2872  161 GLU D C   
13616 O O   . GLU D 161 ? 1.0036 1.2086 0.8704 -0.0728 0.2161  0.2693  161 GLU D O   
13617 C CB  . GLU D 161 ? 0.9646 1.2225 0.8511 -0.0784 0.2602  0.2837  161 GLU D CB  
13618 C CG  . GLU D 161 ? 1.0193 1.3055 0.9027 -0.0843 0.2796  0.2948  161 GLU D CG  
13619 C CD  . GLU D 161 ? 1.0797 1.3808 0.9921 -0.0784 0.2984  0.2882  161 GLU D CD  
13620 O OE1 . GLU D 161 ? 1.1173 1.4286 1.0188 -0.0726 0.3169  0.2702  161 GLU D OE1 
13621 O OE2 . GLU D 161 ? 1.0125 1.3157 0.9594 -0.0794 0.2947  0.3006  161 GLU D OE2 
13622 N N   . LYS D 162 ? 0.8248 1.0308 0.7388 -0.0792 0.2085  0.2983  162 LYS D N   
13623 C CA  . LYS D 162 ? 0.8586 1.0405 0.7827 -0.0741 0.1905  0.2907  162 LYS D CA  
13624 C C   . LYS D 162 ? 0.9384 1.1055 0.8390 -0.0766 0.1737  0.2942  162 LYS D C   
13625 O O   . LYS D 162 ? 0.9213 1.0747 0.8107 -0.0709 0.1659  0.2791  162 LYS D O   
13626 C CB  . LYS D 162 ? 0.8849 1.0618 0.8445 -0.0761 0.1819  0.3016  162 LYS D CB  
13627 C CG  . LYS D 162 ? 1.0259 1.1839 1.0001 -0.0685 0.1695  0.2890  162 LYS D CG  
13628 C CD  . LYS D 162 ? 0.9708 1.1140 0.9621 -0.0734 0.1503  0.3009  162 LYS D CD  
13629 C CE  . LYS D 162 ? 0.8310 0.9875 0.8472 -0.0818 0.1537  0.3185  162 LYS D CE  
13630 N NZ  . LYS D 162 ? 0.7449 0.8868 0.7732 -0.0896 0.1365  0.3321  162 LYS D NZ  
13631 N N   . GLU D 163 ? 0.9401 1.1100 0.8344 -0.0850 0.1681  0.3151  163 GLU D N   
13632 C CA  . GLU D 163 ? 0.8449 1.0024 0.7181 -0.0866 0.1524  0.3209  163 GLU D CA  
13633 C C   . GLU D 163 ? 0.8880 1.0542 0.7263 -0.0843 0.1578  0.3082  163 GLU D C   
13634 O O   . GLU D 163 ? 0.9528 1.1075 0.7759 -0.0817 0.1445  0.3027  163 GLU D O   
13635 C CB  . GLU D 163 ? 0.8878 1.0475 0.7621 -0.0958 0.1474  0.3478  163 GLU D CB  
13636 C CG  . GLU D 163 ? 1.0250 1.1862 0.9328 -0.1012 0.1500  0.3606  163 GLU D CG  
13637 C CD  . GLU D 163 ? 1.1106 1.2673 1.0240 -0.1107 0.1423  0.3869  163 GLU D CD  
13638 O OE1 . GLU D 163 ? 1.2232 1.3973 1.1232 -0.1173 0.1528  0.4020  163 GLU D OE1 
13639 O OE2 . GLU D 163 ? 1.2162 1.3520 1.1478 -0.1118 0.1267  0.3924  163 GLU D OE2 
13640 N N   . TYR D 164 ? 0.8861 1.0736 0.7117 -0.0855 0.1771  0.3025  164 TYR D N   
13641 C CA  . TYR D 164 ? 1.0019 1.1980 0.7950 -0.0837 0.1832  0.2860  164 TYR D CA  
13642 C C   . TYR D 164 ? 0.9960 1.1761 0.7914 -0.0755 0.1785  0.2616  164 TYR D C   
13643 O O   . TYR D 164 ? 1.0813 1.2575 0.8541 -0.0746 0.1707  0.2515  164 TYR D O   
13644 C CB  . TYR D 164 ? 0.9582 1.1787 0.7410 -0.0856 0.2068  0.2807  164 TYR D CB  
13645 C CG  . TYR D 164 ? 1.0373 1.2676 0.7866 -0.0846 0.2148  0.2608  164 TYR D CG  
13646 C CD1 . TYR D 164 ? 1.1547 1.3906 0.8719 -0.0891 0.2052  0.2657  164 TYR D CD1 
13647 C CD2 . TYR D 164 ? 1.0572 1.2914 0.8075 -0.0794 0.2317  0.2369  164 TYR D CD2 
13648 C CE1 . TYR D 164 ? 1.1972 1.4440 0.8832 -0.0895 0.2118  0.2463  164 TYR D CE1 
13649 C CE2 . TYR D 164 ? 1.1737 1.4159 0.8935 -0.0796 0.2393  0.2167  164 TYR D CE2 
13650 C CZ  . TYR D 164 ? 1.2348 1.4841 0.9220 -0.0853 0.2289  0.2210  164 TYR D CZ  
13651 O OH  . TYR D 164 ? 1.2904 1.5497 0.9466 -0.0868 0.2355  0.2001  164 TYR D OH  
13652 N N   . VAL D 165 ? 0.8876 1.0596 0.7107 -0.0699 0.1829  0.2527  165 VAL D N   
13653 C CA  . VAL D 165 ? 0.9167 1.0731 0.7443 -0.0622 0.1795  0.2312  165 VAL D CA  
13654 C C   . VAL D 165 ? 0.8834 1.0208 0.7100 -0.0612 0.1574  0.2336  165 VAL D C   
13655 O O   . VAL D 165 ? 0.9332 1.0632 0.7450 -0.0584 0.1520  0.2185  165 VAL D O   
13656 C CB  . VAL D 165 ? 0.9437 1.0965 0.8036 -0.0561 0.1875  0.2260  165 VAL D CB  
13657 C CG1 . VAL D 165 ? 0.8366 0.9691 0.7062 -0.0486 0.1786  0.2105  165 VAL D CG1 
13658 C CG2 . VAL D 165 ? 0.8062 0.9765 0.6656 -0.0542 0.2113  0.2169  165 VAL D CG2 
13659 N N   . LEU D 166 ? 0.8634 0.9928 0.7067 -0.0638 0.1447  0.2520  166 LEU D N   
13660 C CA  . LEU D 166 ? 0.9058 1.0163 0.7514 -0.0620 0.1245  0.2538  166 LEU D CA  
13661 C C   . LEU D 166 ? 0.9749 1.0883 0.7913 -0.0642 0.1163  0.2559  166 LEU D C   
13662 O O   . LEU D 166 ? 0.9751 1.0777 0.7851 -0.0605 0.1049  0.2459  166 LEU D O   
13663 C CB  . LEU D 166 ? 0.8714 0.9729 0.7406 -0.0652 0.1140  0.2727  166 LEU D CB  
13664 C CG  . LEU D 166 ? 0.8293 0.9195 0.7284 -0.0610 0.1109  0.2669  166 LEU D CG  
13665 C CD1 . LEU D 166 ? 0.7457 0.8340 0.6691 -0.0666 0.1060  0.2850  166 LEU D CD1 
13666 C CD2 . LEU D 166 ? 0.8555 0.9273 0.7548 -0.0550 0.0969  0.2545  166 LEU D CD2 
13667 N N   . ASN D 167 ? 0.9185 1.0485 0.7172 -0.0704 0.1220  0.2693  167 ASN D N   
13668 C CA  . ASN D 167 ? 0.9752 1.1121 0.7445 -0.0725 0.1146  0.2722  167 ASN D CA  
13669 C C   . ASN D 167 ? 0.9797 1.1235 0.7278 -0.0702 0.1207  0.2477  167 ASN D C   
13670 O O   . ASN D 167 ? 1.0740 1.2163 0.8060 -0.0692 0.1093  0.2423  167 ASN D O   
13671 C CB  . ASN D 167 ? 0.9766 1.1319 0.7308 -0.0799 0.1207  0.2929  167 ASN D CB  
13672 C CG  . ASN D 167 ? 1.0747 1.2204 0.8386 -0.0827 0.1065  0.3185  167 ASN D CG  
13673 O OD1 . ASN D 167 ? 1.1227 1.2606 0.9118 -0.0848 0.1069  0.3308  167 ASN D OD1 
13674 N ND2 . ASN D 167 ? 1.1105 1.2565 0.8560 -0.0826 0.0934  0.3267  167 ASN D ND2 
13675 N N   . LYS D 168 ? 0.8964 1.0478 0.6458 -0.0692 0.1388  0.2324  168 LYS D N   
13676 C CA  . LYS D 168 ? 0.9827 1.1365 0.7158 -0.0671 0.1456  0.2069  168 LYS D CA  
13677 C C   . LYS D 168 ? 1.0094 1.1424 0.7567 -0.0610 0.1349  0.1930  168 LYS D C   
13678 O O   . LYS D 168 ? 1.0520 1.1839 0.7836 -0.0608 0.1289  0.1792  168 LYS D O   
13679 C CB  . LYS D 168 ? 0.9380 1.1018 0.6731 -0.0665 0.1684  0.1939  168 LYS D CB  
13680 C CG  . LYS D 168 ? 1.0362 1.2246 0.7473 -0.0729 0.1816  0.1994  168 LYS D CG  
13681 C CD  . LYS D 168 ? 1.1277 1.3273 0.8048 -0.0760 0.1837  0.1817  168 LYS D CD  
13682 C CE  . LYS D 168 ? 1.1454 1.3685 0.7932 -0.0836 0.1840  0.1968  168 LYS D CE  
13683 N NZ  . LYS D 168 ? 1.1845 1.4038 0.8391 -0.0853 0.1671  0.2259  168 LYS D NZ  
13684 N N   . TYR D 169 ? 0.9855 1.1037 0.7625 -0.0566 0.1323  0.1967  169 TYR D N   
13685 C CA  . TYR D 169 ? 0.9149 1.0143 0.7056 -0.0508 0.1225  0.1853  169 TYR D CA  
13686 C C   . TYR D 169 ? 0.9011 0.9937 0.6840 -0.0512 0.1027  0.1913  169 TYR D C   
13687 O O   . TYR D 169 ? 0.9313 1.0180 0.7079 -0.0489 0.0966  0.1769  169 TYR D O   
13688 C CB  . TYR D 169 ? 0.8774 0.9654 0.6999 -0.0467 0.1223  0.1910  169 TYR D CB  
13689 C CG  . TYR D 169 ? 0.9223 1.0141 0.7575 -0.0434 0.1405  0.1808  169 TYR D CG  
13690 C CD1 . TYR D 169 ? 0.9498 1.0534 0.7684 -0.0443 0.1573  0.1676  169 TYR D CD1 
13691 C CD2 . TYR D 169 ? 0.8701 0.9543 0.7340 -0.0389 0.1410  0.1838  169 TYR D CD2 
13692 C CE1 . TYR D 169 ? 0.9668 1.0729 0.7991 -0.0400 0.1747  0.1583  169 TYR D CE1 
13693 C CE2 . TYR D 169 ? 0.8754 0.9639 0.7529 -0.0345 0.1572  0.1759  169 TYR D CE2 
13694 C CZ  . TYR D 169 ? 0.9993 1.0980 0.8619 -0.0346 0.1745  0.1633  169 TYR D CZ  
13695 O OH  . TYR D 169 ? 1.0585 1.1606 0.9367 -0.0291 0.1916  0.1555  169 TYR D OH  
13696 N N   . PHE D 170 ? 0.9152 1.0088 0.6997 -0.0540 0.0930  0.2130  170 PHE D N   
13697 C CA  . PHE D 170 ? 0.9923 1.0784 0.7730 -0.0529 0.0742  0.2205  170 PHE D CA  
13698 C C   . PHE D 170 ? 0.9525 1.0521 0.7044 -0.0551 0.0711  0.2140  170 PHE D C   
13699 O O   . PHE D 170 ? 0.9891 1.0836 0.7381 -0.0525 0.0573  0.2108  170 PHE D O   
13700 C CB  . PHE D 170 ? 0.9750 1.0580 0.7648 -0.0555 0.0659  0.2459  170 PHE D CB  
13701 C CG  . PHE D 170 ? 1.0256 1.0887 0.8442 -0.0522 0.0571  0.2504  170 PHE D CG  
13702 C CD1 . PHE D 170 ? 1.0698 1.1180 0.8955 -0.0470 0.0430  0.2439  170 PHE D CD1 
13703 C CD2 . PHE D 170 ? 0.9793 1.0402 0.8180 -0.0548 0.0629  0.2603  170 PHE D CD2 
13704 C CE1 . PHE D 170 ? 1.0756 1.1065 0.9260 -0.0444 0.0352  0.2464  170 PHE D CE1 
13705 C CE2 . PHE D 170 ? 0.9967 1.0407 0.8608 -0.0527 0.0543  0.2629  170 PHE D CE2 
13706 C CZ  . PHE D 170 ? 1.0460 1.0747 0.9150 -0.0475 0.0406  0.2555  170 PHE D CZ  
13707 N N   . GLU D 171 ? 0.9170 1.0355 0.6476 -0.0600 0.0839  0.2111  171 GLU D N   
13708 C CA  . GLU D 171 ? 0.9369 1.0709 0.6388 -0.0630 0.0822  0.2011  171 GLU D CA  
13709 C C   . GLU D 171 ? 0.9429 1.0694 0.6457 -0.0602 0.0820  0.1755  171 GLU D C   
13710 O O   . GLU D 171 ? 1.0520 1.1825 0.7430 -0.0605 0.0706  0.1696  171 GLU D O   
13711 C CB  . GLU D 171 ? 0.9967 1.1521 0.6763 -0.0689 0.0986  0.1993  171 GLU D CB  
13712 C CG  . GLU D 171 ? 1.1271 1.3014 0.7836 -0.0741 0.0929  0.2190  171 GLU D CG  
13713 C CD  . GLU D 171 ? 1.2111 1.4087 0.8429 -0.0802 0.1101  0.2146  171 GLU D CD  
13714 O OE1 . GLU D 171 ? 1.1020 1.3027 0.7273 -0.0807 0.1234  0.1901  171 GLU D OE1 
13715 O OE2 . GLU D 171 ? 1.2234 1.4359 0.8424 -0.0846 0.1108  0.2355  171 GLU D OE2 
13716 N N   . ILE D 172 ? 0.8678 0.9842 0.5857 -0.0575 0.0945  0.1608  172 ILE D N   
13717 C CA  . ILE D 172 ? 0.8808 0.9871 0.6029 -0.0549 0.0952  0.1380  172 ILE D CA  
13718 C C   . ILE D 172 ? 0.8957 0.9881 0.6318 -0.0505 0.0775  0.1413  172 ILE D C   
13719 O O   . ILE D 172 ? 1.0368 1.1279 0.7676 -0.0503 0.0715  0.1273  172 ILE D O   
13720 C CB  . ILE D 172 ? 0.9984 1.0945 0.7384 -0.0514 0.1115  0.1265  172 ILE D CB  
13721 C CG1 . ILE D 172 ? 0.9613 1.0722 0.6892 -0.0550 0.1303  0.1235  172 ILE D CG1 
13722 C CG2 . ILE D 172 ? 0.8693 0.9532 0.6149 -0.0488 0.1127  0.1045  172 ILE D CG2 
13723 C CD1 . ILE D 172 ? 1.0543 1.1709 0.7651 -0.0578 0.1428  0.0986  172 ILE D CD1 
13724 N N   . ILE D 173 ? 0.8247 0.9066 0.5793 -0.0472 0.0693  0.1590  173 ILE D N   
13725 C CA  . ILE D 173 ? 0.8745 0.9432 0.6426 -0.0426 0.0530  0.1621  173 ILE D CA  
13726 C C   . ILE D 173 ? 0.8970 0.9759 0.6485 -0.0440 0.0391  0.1675  173 ILE D C   
13727 O O   . ILE D 173 ? 0.8410 0.9161 0.5947 -0.0413 0.0292  0.1589  173 ILE D O   
13728 C CB  . ILE D 173 ? 0.8899 0.9459 0.6804 -0.0398 0.0478  0.1793  173 ILE D CB  
13729 C CG1 . ILE D 173 ? 0.8668 0.9145 0.6758 -0.0377 0.0597  0.1727  173 ILE D CG1 
13730 C CG2 . ILE D 173 ? 0.9250 0.9684 0.7270 -0.0352 0.0308  0.1831  173 ILE D CG2 
13731 C CD1 . ILE D 173 ? 0.8822 0.9209 0.7127 -0.0366 0.0557  0.1883  173 ILE D CD1 
13732 N N   . LYS D 174 ? 0.8956 0.9894 0.6304 -0.0481 0.0385  0.1823  174 LYS D N   
13733 C CA  . LYS D 174 ? 0.9063 1.0122 0.6255 -0.0489 0.0247  0.1907  174 LYS D CA  
13734 C C   . LYS D 174 ? 0.8961 1.0169 0.5954 -0.0521 0.0251  0.1711  174 LYS D C   
13735 O O   . LYS D 174 ? 0.8340 0.9632 0.5263 -0.0512 0.0113  0.1734  174 LYS D O   
13736 C CB  . LYS D 174 ? 0.8826 1.0019 0.5881 -0.0528 0.0250  0.2130  174 LYS D CB  
13737 C CG  . LYS D 174 ? 0.8179 0.9228 0.5429 -0.0500 0.0178  0.2365  174 LYS D CG  
13738 C CD  . LYS D 174 ? 0.8966 1.0148 0.6081 -0.0550 0.0207  0.2589  174 LYS D CD  
13739 C CE  . LYS D 174 ? 0.9916 1.1052 0.7149 -0.0581 0.0349  0.2647  174 LYS D CE  
13740 N NZ  . LYS D 174 ? 1.0175 1.1322 0.7430 -0.0612 0.0323  0.2929  174 LYS D NZ  
13741 N N   . LYS D 175 ? 0.8661 0.9904 0.5577 -0.0558 0.0405  0.1516  175 LYS D N   
13742 C CA  . LYS D 175 ? 0.9509 1.0876 0.6251 -0.0602 0.0424  0.1300  175 LYS D CA  
13743 C C   . LYS D 175 ? 0.9439 1.0651 0.6342 -0.0575 0.0432  0.1098  175 LYS D C   
13744 O O   . LYS D 175 ? 0.9251 1.0542 0.6040 -0.0619 0.0449  0.0905  175 LYS D O   
13745 C CB  . LYS D 175 ? 0.8713 1.0215 0.5252 -0.0668 0.0599  0.1189  175 LYS D CB  
13746 C CG  . LYS D 175 ? 1.0527 1.2189 0.6905 -0.0700 0.0621  0.1389  175 LYS D CG  
13747 C CD  . LYS D 175 ? 1.1402 1.3249 0.7526 -0.0772 0.0780  0.1251  175 LYS D CD  
13748 C CE  . LYS D 175 ? 1.1201 1.2922 0.7421 -0.0768 0.0952  0.1002  175 LYS D CE  
13749 N NZ  . LYS D 175 ? 1.2074 1.3966 0.8046 -0.0836 0.1115  0.0840  175 LYS D NZ  
13750 N N   . THR D 176 ? 0.9093 1.0096 0.6252 -0.0511 0.0420  0.1140  176 THR D N   
13751 C CA  . THR D 176 ? 0.9155 1.0009 0.6465 -0.0486 0.0460  0.0960  176 THR D CA  
13752 C C   . THR D 176 ? 0.8825 0.9724 0.6114 -0.0492 0.0339  0.0864  176 THR D C   
13753 O O   . THR D 176 ? 0.8608 0.9530 0.5843 -0.0533 0.0396  0.0661  176 THR D O   
13754 C CB  . THR D 176 ? 0.8467 0.9121 0.6040 -0.0417 0.0454  0.1049  176 THR D CB  
13755 O OG1 . THR D 176 ? 0.9052 0.9693 0.6655 -0.0420 0.0571  0.1132  176 THR D OG1 
13756 C CG2 . THR D 176 ? 0.7450 0.7958 0.5172 -0.0389 0.0502  0.0884  176 THR D CG2 
13757 N N   . LEU D 177 ? 0.8119 0.9030 0.5465 -0.0451 0.0174  0.1004  177 LEU D N   
13758 C CA  . LEU D 177 ? 0.8633 0.9592 0.6001 -0.0446 0.0061  0.0914  177 LEU D CA  
13759 C C   . LEU D 177 ? 0.9129 1.0325 0.6263 -0.0522 0.0042  0.0815  177 LEU D C   
13760 O O   . LEU D 177 ? 0.9489 1.0739 0.6624 -0.0550 0.0010  0.0657  177 LEU D O   
13761 C CB  . LEU D 177 ? 0.7918 0.8844 0.5414 -0.0375 -0.0105 0.1086  177 LEU D CB  
13762 C CG  . LEU D 177 ? 0.8568 0.9271 0.6316 -0.0302 -0.0123 0.1108  177 LEU D CG  
13763 C CD1 . LEU D 177 ? 1.0222 1.0872 0.8059 -0.0302 -0.0097 0.0915  177 LEU D CD1 
13764 C CD2 . LEU D 177 ? 0.8893 0.9452 0.6725 -0.0293 -0.0014 0.1164  177 LEU D CD2 
13765 N N   . SER D 178 ? 0.8156 0.9508 0.5085 -0.0564 0.0064  0.0901  178 SER D N   
13766 C CA  . SER D 178 ? 0.9228 1.0835 0.5909 -0.0643 0.0038  0.0809  178 SER D CA  
13767 C C   . SER D 178 ? 0.9776 1.1381 0.6386 -0.0717 0.0178  0.0531  178 SER D C   
13768 O O   . SER D 178 ? 1.0540 1.2305 0.7033 -0.0782 0.0136  0.0381  178 SER D O   
13769 C CB  . SER D 178 ? 0.8985 1.0759 0.5451 -0.0671 0.0045  0.0971  178 SER D CB  
13770 O OG  . SER D 178 ? 1.0199 1.1866 0.6796 -0.0600 -0.0017 0.1222  178 SER D OG  
13771 N N   . ILE D 179 ? 0.8504 0.9932 0.5194 -0.0709 0.0346  0.0457  179 ILE D N   
13772 C CA  . ILE D 179 ? 0.9019 1.0423 0.5652 -0.0775 0.0491  0.0194  179 ILE D CA  
13773 C C   . ILE D 179 ? 0.8747 1.0040 0.5549 -0.0772 0.0455  0.0049  179 ILE D C   
13774 O O   . ILE D 179 ? 0.9299 1.0635 0.6031 -0.0848 0.0508  -0.0172 179 ILE D O   
13775 C CB  . ILE D 179 ? 1.0066 1.1321 0.6752 -0.0758 0.0688  0.0159  179 ILE D CB  
13776 C CG1 . ILE D 179 ? 1.0133 1.1381 0.6728 -0.0831 0.0846  -0.0117 179 ILE D CG1 
13777 C CG2 . ILE D 179 ? 0.9977 1.0983 0.6951 -0.0670 0.0706  0.0229  179 ILE D CG2 
13778 C CD1 . ILE D 179 ? 0.8868 1.0100 0.5390 -0.0837 0.1039  -0.0155 179 ILE D CD1 
13779 N N   . TYR D 180 ? 0.8859 1.0014 0.5882 -0.0690 0.0368  0.0164  180 TYR D N   
13780 C CA  . TYR D 180 ? 0.8567 0.9654 0.5737 -0.0690 0.0322  0.0045  180 TYR D CA  
13781 C C   . TYR D 180 ? 0.8916 1.0236 0.5983 -0.0738 0.0174  0.0012  180 TYR D C   
13782 O O   . TYR D 180 ? 0.9795 1.1151 0.6881 -0.0797 0.0176  -0.0169 180 TYR D O   
13783 C CB  . TYR D 180 ? 0.7492 0.8393 0.4908 -0.0590 0.0269  0.0173  180 TYR D CB  
13784 C CG  . TYR D 180 ? 0.8146 0.8828 0.5694 -0.0548 0.0412  0.0174  180 TYR D CG  
13785 C CD1 . TYR D 180 ? 0.8396 0.8929 0.6062 -0.0556 0.0520  0.0019  180 TYR D CD1 
13786 C CD2 . TYR D 180 ? 0.7836 0.8470 0.5403 -0.0502 0.0439  0.0339  180 TYR D CD2 
13787 C CE1 . TYR D 180 ? 0.7847 0.8198 0.5644 -0.0508 0.0645  0.0036  180 TYR D CE1 
13788 C CE2 . TYR D 180 ? 0.8481 0.8945 0.6184 -0.0462 0.0562  0.0345  180 TYR D CE2 
13789 C CZ  . TYR D 180 ? 0.8366 0.8693 0.6182 -0.0460 0.0662  0.0197  180 TYR D CZ  
13790 O OH  . TYR D 180 ? 0.8189 0.8363 0.6150 -0.0411 0.0779  0.0219  180 TYR D OH  
13791 N N   . ARG D 181 ? 0.8354 0.9842 0.5319 -0.0716 0.0044  0.0191  181 ARG D N   
13792 C CA  . ARG D 181 ? 0.9045 1.0790 0.5910 -0.0756 -0.0104 0.0177  181 ARG D CA  
13793 C C   . ARG D 181 ? 0.8418 1.0347 0.5057 -0.0880 -0.0041 -0.0030 181 ARG D C   
13794 O O   . ARG D 181 ? 0.9322 1.1412 0.5937 -0.0943 -0.0115 -0.0161 181 ARG D O   
13795 C CB  . ARG D 181 ? 0.8861 1.0745 0.5657 -0.0702 -0.0245 0.0430  181 ARG D CB  
13796 C CG  . ARG D 181 ? 0.9797 1.1676 0.6787 -0.0616 -0.0407 0.0552  181 ARG D CG  
13797 C CD  . ARG D 181 ? 0.9783 1.1762 0.6725 -0.0554 -0.0535 0.0815  181 ARG D CD  
13798 N NE  . ARG D 181 ? 1.0808 1.2586 0.7803 -0.0501 -0.0469 0.0975  181 ARG D NE  
13799 C CZ  . ARG D 181 ? 1.0537 1.2219 0.7662 -0.0412 -0.0560 0.1191  181 ARG D CZ  
13800 N NH1 . ARG D 181 ? 1.1015 1.2773 0.8240 -0.0349 -0.0717 0.1282  181 ARG D NH1 
13801 N NH2 . ARG D 181 ? 0.9392 1.0902 0.6561 -0.0386 -0.0489 0.1316  181 ARG D NH2 
13802 N N   . GLU D 182 ? 0.9893 1.1805 0.6372 -0.0921 0.0100  -0.0073 182 GLU D N   
13803 C CA  . GLU D 182 ? 1.0393 1.2473 0.6639 -0.1042 0.0176  -0.0287 182 GLU D CA  
13804 C C   . GLU D 182 ? 1.0342 1.2304 0.6692 -0.1106 0.0266  -0.0558 182 GLU D C   
13805 O O   . GLU D 182 ? 1.1197 1.3332 0.7483 -0.1194 0.0199  -0.0710 182 GLU D O   
13806 C CB  . GLU D 182 ? 1.0713 1.2774 0.6791 -0.1058 0.0332  -0.0278 182 GLU D CB  
13807 C CG  . GLU D 182 ? 1.2194 1.4301 0.8101 -0.1171 0.0487  -0.0565 182 GLU D CG  
13808 C CD  . GLU D 182 ? 1.3062 1.5037 0.8925 -0.1157 0.0692  -0.0591 182 GLU D CD  
13809 O OE1 . GLU D 182 ? 1.3483 1.5402 0.9393 -0.1077 0.0698  -0.0367 182 GLU D OE1 
13810 O OE2 . GLU D 182 ? 1.1511 1.3446 0.7297 -0.1228 0.0849  -0.0837 182 GLU D OE2 
13811 N N   . ILE D 183 ? 0.9492 1.1163 0.6016 -0.1065 0.0415  -0.0613 183 ILE D N   
13812 C CA  . ILE D 183 ? 0.8640 1.0168 0.5263 -0.1127 0.0528  -0.0862 183 ILE D CA  
13813 C C   . ILE D 183 ? 0.9757 1.1350 0.6509 -0.1152 0.0398  -0.0914 183 ILE D C   
13814 O O   . ILE D 183 ? 1.0019 1.1631 0.6771 -0.1253 0.0440  -0.1139 183 ILE D O   
13815 C CB  . ILE D 183 ? 0.8964 1.0170 0.5791 -0.1052 0.0685  -0.0853 183 ILE D CB  
13816 C CG1 . ILE D 183 ? 0.8748 0.9825 0.5812 -0.0942 0.0588  -0.0665 183 ILE D CG1 
13817 C CG2 . ILE D 183 ? 0.9684 1.0850 0.6409 -0.1020 0.0813  -0.0788 183 ILE D CG2 
13818 C CD1 . ILE D 183 ? 0.8800 0.9615 0.6097 -0.0912 0.0688  -0.0742 183 ILE D CD1 
13819 N N   . LYS D 184 ? 0.9727 1.1362 0.6596 -0.1066 0.0241  -0.0712 184 LYS D N   
13820 C CA  . LYS D 184 ? 0.8974 1.0696 0.5979 -0.1077 0.0115  -0.0745 184 LYS D CA  
13821 C C   . LYS D 184 ? 0.9310 1.1369 0.6138 -0.1179 -0.0002 -0.0832 184 LYS D C   
13822 O O   . LYS D 184 ? 0.9287 1.1425 0.6159 -0.1271 -0.0012 -0.1019 184 LYS D O   
13823 C CB  . LYS D 184 ? 0.8475 1.0155 0.5648 -0.0948 -0.0013 -0.0508 184 LYS D CB  
13824 C CG  . LYS D 184 ? 0.9019 1.0674 0.6417 -0.0930 -0.0080 -0.0548 184 LYS D CG  
13825 C CD  . LYS D 184 ? 0.8763 1.0481 0.6274 -0.0817 -0.0243 -0.0333 184 LYS D CD  
13826 C CE  . LYS D 184 ? 0.9317 1.1244 0.6921 -0.0841 -0.0373 -0.0385 184 LYS D CE  
13827 N NZ  . LYS D 184 ? 0.9346 1.1598 0.6786 -0.0871 -0.0518 -0.0327 184 LYS D NZ  
13828 N N   . GLU D 185 ? 0.9225 1.1500 0.5854 -0.1168 -0.0093 -0.0693 185 GLU D N   
13829 C CA  . GLU D 185 ? 1.0728 1.3358 0.7168 -0.1262 -0.0215 -0.0758 185 GLU D CA  
13830 C C   . GLU D 185 ? 0.9803 1.2498 0.6047 -0.1410 -0.0091 -0.1034 185 GLU D C   
13831 O O   . GLU D 185 ? 0.9227 1.2133 0.5416 -0.1523 -0.0151 -0.1208 185 GLU D O   
13832 C CB  . GLU D 185 ? 1.1167 1.4004 0.7439 -0.1205 -0.0339 -0.0513 185 GLU D CB  
13833 C CG  . GLU D 185 ? 1.1619 1.4680 0.7978 -0.1148 -0.0559 -0.0349 185 GLU D CG  
13834 C CD  . GLU D 185 ? 1.2425 1.5759 0.8776 -0.1252 -0.0655 -0.0528 185 GLU D CD  
13835 O OE1 . GLU D 185 ? 1.3386 1.6866 0.9887 -0.1198 -0.0814 -0.0428 185 GLU D OE1 
13836 O OE2 . GLU D 185 ? 1.3876 1.7291 1.0074 -0.1390 -0.0572 -0.0770 185 GLU D OE2 
13837 N N   . GLU D 186 ? 0.9716 1.2234 0.5864 -0.1415 0.0087  -0.1087 186 GLU D N   
13838 C CA  . GLU D 186 ? 0.9676 1.2248 0.5619 -0.1547 0.0219  -0.1349 186 GLU D CA  
13839 C C   . GLU D 186 ? 1.0090 1.2475 0.6187 -0.1629 0.0336  -0.1621 186 GLU D C   
13840 O O   . GLU D 186 ? 1.0488 1.2867 0.6447 -0.1741 0.0465  -0.1867 186 GLU D O   
13841 C CB  . GLU D 186 ? 0.9660 1.2109 0.5469 -0.1512 0.0381  -0.1309 186 GLU D CB  
13842 C CG  . GLU D 186 ? 1.0926 1.3538 0.6591 -0.1437 0.0285  -0.1026 186 GLU D CG  
13843 C CD  . GLU D 186 ? 1.1930 1.4695 0.7282 -0.1500 0.0383  -0.1078 186 GLU D CD  
13844 O OE1 . GLU D 186 ? 1.2354 1.5004 0.7649 -0.1564 0.0569  -0.1310 186 GLU D OE1 
13845 O OE2 . GLU D 186 ? 1.1519 1.4520 0.6686 -0.1483 0.0278  -0.0884 186 GLU D OE2 
13846 N N   . GLY D 187 ? 0.9348 1.1580 0.5725 -0.1580 0.0299  -0.1587 187 GLY D N   
13847 C CA  . GLY D 187 ? 0.9118 1.1147 0.5655 -0.1654 0.0421  -0.1817 187 GLY D CA  
13848 C C   . GLY D 187 ? 1.0404 1.2093 0.7003 -0.1625 0.0647  -0.1895 187 GLY D C   
13849 O O   . GLY D 187 ? 1.0810 1.2325 0.7512 -0.1699 0.0773  -0.2108 187 GLY D O   
13850 N N   . LYS D 188 ? 0.9984 1.1576 0.6537 -0.1518 0.0706  -0.1726 188 LYS D N   
13851 C CA  . LYS D 188 ? 1.0195 1.1477 0.6838 -0.1474 0.0918  -0.1782 188 LYS D CA  
13852 C C   . LYS D 188 ? 0.9420 1.0424 0.6370 -0.1383 0.0950  -0.1693 188 LYS D C   
13853 O O   . LYS D 188 ? 0.9348 1.0089 0.6426 -0.1376 0.1121  -0.1799 188 LYS D O   
13854 C CB  . LYS D 188 ? 1.0475 1.1771 0.6985 -0.1395 0.0972  -0.1627 188 LYS D CB  
13855 C CG  . LYS D 188 ? 1.0710 1.2086 0.6973 -0.1480 0.1112  -0.1812 188 LYS D CG  
13856 C CD  . LYS D 188 ? 1.0207 1.1941 0.6171 -0.1532 0.0984  -0.1751 188 LYS D CD  
13857 C CE  . LYS D 188 ? 1.1887 1.3692 0.7604 -0.1578 0.1137  -0.1865 188 LYS D CE  
13858 N NZ  . LYS D 188 ? 1.3121 1.4980 0.8700 -0.1728 0.1226  -0.2206 188 LYS D NZ  
13859 N N   . GLY D 189 ? 0.8432 0.9492 0.5504 -0.1309 0.0791  -0.1502 189 GLY D N   
13860 C CA  . GLY D 189 ? 0.9519 1.0339 0.6860 -0.1222 0.0816  -0.1413 189 GLY D CA  
13861 C C   . GLY D 189 ? 0.9040 0.9976 0.6484 -0.1164 0.0627  -0.1246 189 GLY D C   
13862 O O   . GLY D 189 ? 0.9351 1.0543 0.6674 -0.1174 0.0473  -0.1172 189 GLY D O   
13863 N N   . SER D 190 ? 0.8878 0.9625 0.6552 -0.1097 0.0644  -0.1185 190 SER D N   
13864 C CA  . SER D 190 ? 1.0038 1.0860 0.7845 -0.1033 0.0490  -0.1045 190 SER D CA  
13865 C C   . SER D 190 ? 0.7607 0.8285 0.5506 -0.0893 0.0478  -0.0826 190 SER D C   
13866 O O   . SER D 190 ? 0.7648 0.8114 0.5604 -0.0850 0.0611  -0.0809 190 SER D O   
13867 C CB  . SER D 190 ? 0.9691 1.0439 0.7686 -0.1077 0.0514  -0.1155 190 SER D CB  
13868 O OG  . SER D 190 ? 0.9961 1.0940 0.7907 -0.1191 0.0432  -0.1294 190 SER D OG  
13869 N N   . VAL D 191 ? 0.7177 0.7976 0.5098 -0.0823 0.0319  -0.0661 191 VAL D N   
13870 C CA  . VAL D 191 ? 0.8984 0.9659 0.7001 -0.0700 0.0289  -0.0462 191 VAL D CA  
13871 C C   . VAL D 191 ? 0.8779 0.9438 0.6983 -0.0644 0.0200  -0.0410 191 VAL D C   
13872 O O   . VAL D 191 ? 0.7996 0.8830 0.6217 -0.0674 0.0094  -0.0449 191 VAL D O   
13873 C CB  . VAL D 191 ? 0.8534 0.9331 0.6416 -0.0658 0.0195  -0.0298 191 VAL D CB  
13874 C CG1 . VAL D 191 ? 0.8922 0.9956 0.6765 -0.0660 0.0018  -0.0244 191 VAL D CG1 
13875 C CG2 . VAL D 191 ? 0.8477 0.9112 0.6466 -0.0548 0.0193  -0.0116 191 VAL D CG2 
13876 N N   . SER D 192 ? 0.7744 0.8207 0.6088 -0.0563 0.0246  -0.0328 192 SER D N   
13877 C CA  . SER D 192 ? 0.7369 0.7796 0.5886 -0.0507 0.0189  -0.0288 192 SER D CA  
13878 C C   . SER D 192 ? 0.7513 0.7856 0.6089 -0.0396 0.0130  -0.0108 192 SER D C   
13879 O O   . SER D 192 ? 0.8292 0.8598 0.6790 -0.0370 0.0140  -0.0016 192 SER D O   
13880 C CB  . SER D 192 ? 0.7935 0.8201 0.6573 -0.0532 0.0318  -0.0388 192 SER D CB  
13881 O OG  . SER D 192 ? 0.7934 0.8006 0.6586 -0.0494 0.0436  -0.0344 192 SER D OG  
13882 N N   . THR D 193 ? 0.7448 0.7761 0.6167 -0.0335 0.0074  -0.0066 193 THR D N   
13883 C CA  . THR D 193 ? 0.8015 0.8235 0.6803 -0.0237 0.0021  0.0080  193 THR D CA  
13884 C C   . THR D 193 ? 0.7954 0.8059 0.6890 -0.0196 0.0061  0.0066  193 THR D C   
13885 O O   . THR D 193 ? 0.8164 0.8258 0.7149 -0.0243 0.0134  -0.0040 193 THR D O   
13886 C CB  . THR D 193 ? 0.7000 0.7349 0.5778 -0.0189 -0.0136 0.0177  193 THR D CB  
13887 O OG1 . THR D 193 ? 0.8287 0.8529 0.7096 -0.0114 -0.0173 0.0319  193 THR D OG1 
13888 C CG2 . THR D 193 ? 0.6300 0.6742 0.5199 -0.0162 -0.0212 0.0136  193 THR D CG2 
13889 N N   . SER D 194 ? 0.7011 0.7030 0.6014 -0.0115 0.0020  0.0175  194 SER D N   
13890 C CA  . SER D 194 ? 0.7039 0.6974 0.6164 -0.0067 0.0038  0.0179  194 SER D CA  
13891 C C   . SER D 194 ? 0.7619 0.7597 0.6806 0.0007  -0.0090 0.0247  194 SER D C   
13892 O O   . SER D 194 ? 0.6964 0.7006 0.6108 0.0025  -0.0183 0.0309  194 SER D O   
13893 C CB  . SER D 194 ? 0.7734 0.7511 0.6882 -0.0041 0.0125  0.0237  194 SER D CB  
13894 O OG  . SER D 194 ? 0.7605 0.7329 0.6709 -0.0098 0.0252  0.0178  194 SER D OG  
13895 N N   . PRO D 195 ? 0.8588 0.8531 0.7877 0.0053  -0.0094 0.0237  195 PRO D N   
13896 C CA  . PRO D 195 ? 0.7592 0.7535 0.6946 0.0133  -0.0200 0.0298  195 PRO D CA  
13897 C C   . PRO D 195 ? 0.8042 0.7883 0.7366 0.0163  -0.0233 0.0408  195 PRO D C   
13898 O O   . PRO D 195 ? 0.7789 0.7540 0.7083 0.0142  -0.0158 0.0438  195 PRO D O   
13899 C CB  . PRO D 195 ? 0.7973 0.7876 0.7413 0.0164  -0.0159 0.0261  195 PRO D CB  
13900 C CG  . PRO D 195 ? 0.7668 0.7621 0.7109 0.0098  -0.0068 0.0169  195 PRO D CG  
13901 C CD  . PRO D 195 ? 0.7628 0.7542 0.6977 0.0033  -0.0002 0.0166  195 PRO D CD  
13902 N N   . TYR D 196 ? 0.8330 0.8185 0.7683 0.0215  -0.0343 0.0471  196 TYR D N   
13903 C CA  . TYR D 196 ? 0.8160 0.7955 0.7474 0.0223  -0.0388 0.0583  196 TYR D CA  
13904 C C   . TYR D 196 ? 0.7315 0.6987 0.6624 0.0210  -0.0322 0.0630  196 TYR D C   
13905 O O   . TYR D 196 ? 0.7270 0.6933 0.6505 0.0167  -0.0272 0.0673  196 TYR D O   
13906 C CB  . TYR D 196 ? 0.7048 0.6824 0.6440 0.0294  -0.0506 0.0643  196 TYR D CB  
13907 C CG  . TYR D 196 ? 0.7306 0.7093 0.6648 0.0293  -0.0573 0.0759  196 TYR D CG  
13908 C CD1 . TYR D 196 ? 0.7271 0.6950 0.6594 0.0280  -0.0566 0.0859  196 TYR D CD1 
13909 C CD2 . TYR D 196 ? 0.7210 0.7133 0.6525 0.0301  -0.0643 0.0777  196 TYR D CD2 
13910 C CE1 . TYR D 196 ? 0.7738 0.7429 0.7013 0.0274  -0.0620 0.0980  196 TYR D CE1 
13911 C CE2 . TYR D 196 ? 0.7344 0.7288 0.6603 0.0301  -0.0705 0.0902  196 TYR D CE2 
13912 C CZ  . TYR D 196 ? 0.7967 0.7789 0.7203 0.0287  -0.0689 0.1006  196 TYR D CZ  
13913 O OH  . TYR D 196 ? 0.8315 0.8164 0.7494 0.0283  -0.0745 0.1144  196 TYR D OH  
13914 N N   . TYR D 197 ? 0.7070 0.6664 0.6457 0.0245  -0.0318 0.0620  197 TYR D N   
13915 C CA  . TYR D 197 ? 0.7366 0.6866 0.6771 0.0240  -0.0283 0.0679  197 TYR D CA  
13916 C C   . TYR D 197 ? 0.7608 0.7094 0.7017 0.0223  -0.0175 0.0635  197 TYR D C   
13917 O O   . TYR D 197 ? 0.7723 0.7159 0.7183 0.0242  -0.0165 0.0657  197 TYR D O   
13918 C CB  . TYR D 197 ? 0.7076 0.6503 0.6563 0.0287  -0.0366 0.0710  197 TYR D CB  
13919 C CG  . TYR D 197 ? 0.7423 0.6829 0.6926 0.0307  -0.0464 0.0777  197 TYR D CG  
13920 C CD1 . TYR D 197 ? 0.7916 0.7283 0.7394 0.0277  -0.0474 0.0883  197 TYR D CD1 
13921 C CD2 . TYR D 197 ? 0.7426 0.6855 0.6979 0.0358  -0.0541 0.0743  197 TYR D CD2 
13922 C CE1 . TYR D 197 ? 0.7312 0.6652 0.6807 0.0294  -0.0559 0.0964  197 TYR D CE1 
13923 C CE2 . TYR D 197 ? 0.7259 0.6659 0.6840 0.0386  -0.0630 0.0820  197 TYR D CE2 
13924 C CZ  . TYR D 197 ? 0.7057 0.6406 0.6606 0.0352  -0.0639 0.0936  197 TYR D CZ  
13925 O OH  . TYR D 197 ? 0.7948 0.7259 0.7528 0.0378  -0.0723 0.1033  197 TYR D OH  
13926 N N   . HIS D 198 ? 0.8010 0.7541 0.7370 0.0185  -0.0095 0.0576  198 HIS D N   
13927 C CA  . HIS D 198 ? 0.7715 0.7219 0.7090 0.0169  0.0018  0.0539  198 HIS D CA  
13928 C C   . HIS D 198 ? 0.8105 0.7592 0.7547 0.0208  0.0013  0.0524  198 HIS D C   
13929 O O   . HIS D 198 ? 0.8322 0.7764 0.7795 0.0220  0.0063  0.0566  198 HIS D O   
13930 C CB  . HIS D 198 ? 0.7338 0.6788 0.6707 0.0156  0.0090  0.0604  198 HIS D CB  
13931 C CG  . HIS D 198 ? 0.7446 0.6870 0.6809 0.0129  0.0223  0.0560  198 HIS D CG  
13932 N ND1 . HIS D 198 ? 0.7377 0.6747 0.6804 0.0151  0.0299  0.0600  198 HIS D ND1 
13933 C CD2 . HIS D 198 ? 0.6684 0.6125 0.5994 0.0080  0.0294  0.0480  198 HIS D CD2 
13934 C CE1 . HIS D 198 ? 0.7464 0.6799 0.6887 0.0125  0.0417  0.0551  198 HIS D CE1 
13935 N NE2 . HIS D 198 ? 0.7545 0.6918 0.6894 0.0076  0.0418  0.0467  198 HIS D NE2 
13936 N N   . PRO D 199 ? 0.7469 0.7007 0.6936 0.0231  -0.0044 0.0470  199 PRO D N   
13937 C CA  . PRO D 199 ? 0.7226 0.6764 0.6740 0.0266  -0.0045 0.0452  199 PRO D CA  
13938 C C   . PRO D 199 ? 0.8579 0.8138 0.8101 0.0242  0.0058  0.0407  199 PRO D C   
13939 O O   . PRO D 199 ? 0.8911 0.8480 0.8413 0.0195  0.0123  0.0368  199 PRO D O   
13940 C CB  . PRO D 199 ? 0.7919 0.7509 0.7462 0.0303  -0.0142 0.0408  199 PRO D CB  
13941 C CG  . PRO D 199 ? 0.8093 0.7751 0.7612 0.0273  -0.0150 0.0374  199 PRO D CG  
13942 C CD  . PRO D 199 ? 0.7504 0.7121 0.6960 0.0228  -0.0109 0.0424  199 PRO D CD  
13943 N N   . LEU D 200 ? 0.8748 0.8314 0.8297 0.0271  0.0074  0.0412  200 LEU D N   
13944 C CA  . LEU D 200 ? 0.8695 0.8281 0.8260 0.0252  0.0170  0.0386  200 LEU D CA  
13945 C C   . LEU D 200 ? 0.7841 0.7524 0.7430 0.0260  0.0141  0.0307  200 LEU D C   
13946 O O   . LEU D 200 ? 0.7844 0.7568 0.7443 0.0298  0.0119  0.0300  200 LEU D O   
13947 C CB  . LEU D 200 ? 0.8200 0.7758 0.7773 0.0279  0.0210  0.0457  200 LEU D CB  
13948 C CG  . LEU D 200 ? 0.7661 0.7144 0.7240 0.0276  0.0259  0.0541  200 LEU D CG  
13949 C CD1 . LEU D 200 ? 0.7602 0.7099 0.7192 0.0317  0.0231  0.0617  200 LEU D CD1 
13950 C CD2 . LEU D 200 ? 0.7461 0.6890 0.7061 0.0243  0.0390  0.0543  200 LEU D CD2 
13951 N N   . ILE D 201 ? 0.8074 0.7809 0.7673 0.0222  0.0143  0.0244  201 ILE D N   
13952 C CA  . ILE D 201 ? 0.7824 0.7678 0.7468 0.0233  0.0107  0.0170  201 ILE D CA  
13953 C C   . ILE D 201 ? 0.7513 0.7415 0.7189 0.0231  0.0181  0.0151  201 ILE D C   
13954 O O   . ILE D 201 ? 0.7569 0.7554 0.7273 0.0274  0.0142  0.0116  201 ILE D O   
13955 C CB  . ILE D 201 ? 0.6509 0.6437 0.6164 0.0184  0.0094  0.0112  201 ILE D CB  
13956 C CG1 . ILE D 201 ? 0.7583 0.7486 0.7193 0.0196  0.0009  0.0146  201 ILE D CG1 
13957 C CG2 . ILE D 201 ? 0.6213 0.6289 0.5939 0.0198  0.0058  0.0041  201 ILE D CG2 
13958 C CD1 . ILE D 201 ? 0.7417 0.7341 0.7056 0.0270  -0.0107 0.0165  201 ILE D CD1 
13959 N N   . PRO D 202 ? 0.6697 0.6553 0.6374 0.0183  0.0294  0.0173  202 PRO D N   
13960 C CA  . PRO D 202 ? 0.6808 0.6714 0.6512 0.0182  0.0366  0.0177  202 PRO D CA  
13961 C C   . PRO D 202 ? 0.7283 0.7223 0.6958 0.0250  0.0322  0.0207  202 PRO D C   
13962 O O   . PRO D 202 ? 0.7536 0.7584 0.7231 0.0266  0.0331  0.0166  202 PRO D O   
13963 C CB  . PRO D 202 ? 0.6315 0.6110 0.6019 0.0139  0.0483  0.0238  202 PRO D CB  
13964 C CG  . PRO D 202 ? 0.7624 0.7366 0.7330 0.0086  0.0493  0.0195  202 PRO D CG  
13965 C CD  . PRO D 202 ? 0.7627 0.7390 0.7292 0.0124  0.0370  0.0186  202 PRO D CD  
13966 N N   . ILE D 203 ? 0.7537 0.7400 0.7166 0.0287  0.0276  0.0270  203 ILE D N   
13967 C CA  . ILE D 203 ? 0.7401 0.7301 0.6994 0.0341  0.0227  0.0286  203 ILE D CA  
13968 C C   . ILE D 203 ? 0.7513 0.7474 0.7123 0.0384  0.0129  0.0201  203 ILE D C   
13969 O O   . ILE D 203 ? 0.7815 0.7856 0.7415 0.0419  0.0117  0.0158  203 ILE D O   
13970 C CB  . ILE D 203 ? 0.7517 0.7333 0.7074 0.0358  0.0200  0.0374  203 ILE D CB  
13971 C CG1 . ILE D 203 ? 0.7304 0.7045 0.6874 0.0324  0.0300  0.0455  203 ILE D CG1 
13972 C CG2 . ILE D 203 ? 0.7515 0.7388 0.7026 0.0397  0.0165  0.0393  203 ILE D CG2 
13973 C CD1 . ILE D 203 ? 0.7137 0.6833 0.6692 0.0348  0.0293  0.0556  203 ILE D CD1 
13974 N N   . LEU D 204 ? 0.6742 0.6666 0.6378 0.0385  0.0062  0.0179  204 LEU D N   
13975 C CA  . LEU D 204 ? 0.6902 0.6863 0.6575 0.0436  -0.0033 0.0115  204 LEU D CA  
13976 C C   . LEU D 204 ? 0.8016 0.8113 0.7747 0.0451  -0.0011 0.0031  204 LEU D C   
13977 O O   . LEU D 204 ? 0.7792 0.7936 0.7553 0.0510  -0.0061 -0.0030 204 LEU D O   
13978 C CB  . LEU D 204 ? 0.7419 0.7322 0.7109 0.0432  -0.0103 0.0132  204 LEU D CB  
13979 C CG  . LEU D 204 ? 0.8231 0.8013 0.7882 0.0428  -0.0141 0.0209  204 LEU D CG  
13980 C CD1 . LEU D 204 ? 0.7806 0.7552 0.7470 0.0426  -0.0210 0.0230  204 LEU D CD1 
13981 C CD2 . LEU D 204 ? 0.7380 0.7126 0.7020 0.0469  -0.0193 0.0207  204 LEU D CD2 
13982 N N   . LEU D 205 ? 0.7452 0.7616 0.7211 0.0397  0.0066  0.0019  205 LEU D N   
13983 C CA  . LEU D 205 ? 0.7379 0.7697 0.7210 0.0402  0.0097  -0.0055 205 LEU D CA  
13984 C C   . LEU D 205 ? 0.7956 0.8335 0.7758 0.0415  0.0167  -0.0060 205 LEU D C   
13985 O O   . LEU D 205 ? 0.9762 1.0221 0.9580 0.0473  0.0140  -0.0121 205 LEU D O   
13986 C CB  . LEU D 205 ? 0.7135 0.7513 0.7016 0.0325  0.0156  -0.0072 205 LEU D CB  
13987 C CG  . LEU D 205 ? 0.7149 0.7488 0.7033 0.0296  0.0098  -0.0067 205 LEU D CG  
13988 C CD1 . LEU D 205 ? 0.6346 0.6682 0.6235 0.0199  0.0183  -0.0073 205 LEU D CD1 
13989 C CD2 . LEU D 205 ? 0.7171 0.7630 0.7134 0.0341  0.0003  -0.0119 205 LEU D CD2 
13990 N N   . ASN D 206 ? 0.6911 0.7256 0.6670 0.0363  0.0260  0.0005  206 ASN D N   
13991 C CA  . ASN D 206 ? 0.7232 0.7634 0.6940 0.0373  0.0326  0.0029  206 ASN D CA  
13992 C C   . ASN D 206 ? 0.7528 0.7819 0.7150 0.0369  0.0341  0.0134  206 ASN D C   
13993 O O   . ASN D 206 ? 0.7017 0.7232 0.6645 0.0320  0.0412  0.0207  206 ASN D O   
13994 C CB  . ASN D 206 ? 0.6564 0.7070 0.6324 0.0317  0.0439  0.0026  206 ASN D CB  
13995 C CG  . ASN D 206 ? 0.8211 0.8782 0.7906 0.0323  0.0516  0.0075  206 ASN D CG  
13996 O OD1 . ASN D 206 ? 0.8226 0.8821 0.7842 0.0379  0.0472  0.0071  206 ASN D OD1 
13997 N ND2 . ASN D 206 ? 0.8279 0.8885 0.8006 0.0261  0.0631  0.0121  206 ASN D ND2 
13998 N N   . PRO D 207 ? 0.7771 0.8052 0.7324 0.0419  0.0279  0.0141  207 PRO D N   
13999 C CA  . PRO D 207 ? 0.7424 0.7633 0.6908 0.0416  0.0285  0.0247  207 PRO D CA  
14000 C C   . PRO D 207 ? 0.7172 0.7423 0.6626 0.0390  0.0394  0.0338  207 PRO D C   
14001 O O   . PRO D 207 ? 0.7543 0.7724 0.6972 0.0384  0.0418  0.0447  207 PRO D O   
14002 C CB  . PRO D 207 ? 0.7193 0.7431 0.6616 0.0467  0.0193  0.0206  207 PRO D CB  
14003 C CG  . PRO D 207 ? 0.7095 0.7340 0.6577 0.0498  0.0124  0.0089  207 PRO D CG  
14004 C CD  . PRO D 207 ? 0.7645 0.7979 0.7192 0.0479  0.0195  0.0046  207 PRO D CD  
14005 N N   . ASN D 208 ? 0.6965 0.7329 0.6430 0.0376  0.0467  0.0307  208 ASN D N   
14006 C CA  . ASN D 208 ? 0.7042 0.7442 0.6483 0.0347  0.0578  0.0409  208 ASN D CA  
14007 C C   . ASN D 208 ? 0.7255 0.7541 0.6776 0.0287  0.0668  0.0473  208 ASN D C   
14008 O O   . ASN D 208 ? 0.7347 0.7637 0.6873 0.0258  0.0772  0.0566  208 ASN D O   
14009 C CB  . ASN D 208 ? 0.8029 0.8599 0.7463 0.0344  0.0635  0.0355  208 ASN D CB  
14010 C CG  . ASN D 208 ? 0.7877 0.8559 0.7218 0.0402  0.0567  0.0289  208 ASN D CG  
14011 O OD1 . ASN D 208 ? 0.8425 0.9115 0.7665 0.0426  0.0536  0.0351  208 ASN D OD1 
14012 N ND2 . ASN D 208 ? 0.7266 0.8042 0.6648 0.0426  0.0541  0.0155  208 ASN D ND2 
14013 N N   . CYS D 209 ? 0.8008 0.8191 0.7590 0.0266  0.0635  0.0425  209 CYS D N   
14014 C CA  . CYS D 209 ? 0.7883 0.7942 0.7531 0.0208  0.0720  0.0470  209 CYS D CA  
14015 C C   . CYS D 209 ? 0.7454 0.7403 0.7078 0.0226  0.0761  0.0608  209 CYS D C   
14016 O O   . CYS D 209 ? 0.7696 0.7541 0.7379 0.0185  0.0863  0.0666  209 CYS D O   
14017 C CB  . CYS D 209 ? 0.6936 0.6930 0.6626 0.0186  0.0663  0.0385  209 CYS D CB  
14018 S SG  . CYS D 209 ? 0.8008 0.7941 0.7639 0.0249  0.0533  0.0394  209 CYS D SG  
14019 N N   . VAL D 210 ? 0.7592 0.7563 0.7146 0.0285  0.0685  0.0660  210 VAL D N   
14020 C CA  . VAL D 210 ? 0.8022 0.7916 0.7570 0.0310  0.0713  0.0798  210 VAL D CA  
14021 C C   . VAL D 210 ? 0.7956 0.7882 0.7501 0.0307  0.0817  0.0921  210 VAL D C   
14022 O O   . VAL D 210 ? 0.8523 0.8353 0.8112 0.0316  0.0886  0.1045  210 VAL D O   
14023 C CB  . VAL D 210 ? 0.7748 0.7691 0.7231 0.0365  0.0595  0.0816  210 VAL D CB  
14024 C CG1 . VAL D 210 ? 0.7981 0.7866 0.7482 0.0364  0.0504  0.0721  210 VAL D CG1 
14025 C CG2 . VAL D 210 ? 0.8048 0.8152 0.7439 0.0391  0.0546  0.0786  210 VAL D CG2 
14026 N N   . TYR D 211 ? 0.6778 0.6838 0.6279 0.0298  0.0838  0.0895  211 TYR D N   
14027 C CA  . TYR D 211 ? 0.7504 0.7618 0.6982 0.0296  0.0932  0.1028  211 TYR D CA  
14028 C C   . TYR D 211 ? 0.7132 0.7139 0.6716 0.0233  0.1072  0.1068  211 TYR D C   
14029 O O   . TYR D 211 ? 0.7197 0.7207 0.6786 0.0229  0.1166  0.1208  211 TYR D O   
14030 C CB  . TYR D 211 ? 0.6967 0.7282 0.6348 0.0307  0.0910  0.0982  211 TYR D CB  
14031 C CG  . TYR D 211 ? 0.6894 0.7309 0.6167 0.0363  0.0781  0.0940  211 TYR D CG  
14032 C CD1 . TYR D 211 ? 0.6736 0.7194 0.5935 0.0404  0.0746  0.1065  211 TYR D CD1 
14033 C CD2 . TYR D 211 ? 0.7218 0.7682 0.6475 0.0374  0.0692  0.0774  211 TYR D CD2 
14034 C CE1 . TYR D 211 ? 0.6877 0.7430 0.5982 0.0441  0.0625  0.1012  211 TYR D CE1 
14035 C CE2 . TYR D 211 ? 0.7308 0.7840 0.6479 0.0417  0.0579  0.0723  211 TYR D CE2 
14036 C CZ  . TYR D 211 ? 0.7341 0.7918 0.6433 0.0444  0.0545  0.0835  211 TYR D CZ  
14037 O OH  . TYR D 211 ? 0.7326 0.7975 0.6338 0.0473  0.0430  0.0768  211 TYR D OH  
14038 N N   . GLU D 212 ? 0.6895 0.6811 0.6565 0.0179  0.1088  0.0952  212 GLU D N   
14039 C CA  . GLU D 212 ? 0.7958 0.7756 0.7739 0.0106  0.1220  0.0972  212 GLU D CA  
14040 C C   . GLU D 212 ? 0.7234 0.6855 0.7067 0.0127  0.1294  0.1115  212 GLU D C   
14041 O O   . GLU D 212 ? 0.8617 0.8175 0.8505 0.0105  0.1412  0.1233  212 GLU D O   
14042 C CB  . GLU D 212 ? 0.7203 0.6957 0.7053 0.0043  0.1203  0.0806  212 GLU D CB  
14043 C CG  . GLU D 212 ? 0.7755 0.7674 0.7559 0.0057  0.1091  0.0670  212 GLU D CG  
14044 C CD  . GLU D 212 ? 0.9053 0.8991 0.8940 -0.0017 0.1094  0.0527  212 GLU D CD  
14045 O OE1 . GLU D 212 ? 0.9613 0.9420 0.9576 -0.0083 0.1166  0.0512  212 GLU D OE1 
14046 O OE2 . GLU D 212 ? 0.7449 0.7540 0.7330 -0.0007 0.1023  0.0427  212 GLU D OE2 
14047 N N   . THR D 213 ? 0.7261 0.6804 0.7086 0.0175  0.1229  0.1117  213 THR D N   
14048 C CA  . THR D 213 ? 0.7936 0.7324 0.7827 0.0209  0.1295  0.1246  213 THR D CA  
14049 C C   . THR D 213 ? 0.8226 0.7699 0.8059 0.0295  0.1254  0.1414  213 THR D C   
14050 O O   . THR D 213 ? 0.7389 0.6771 0.7287 0.0329  0.1335  0.1570  213 THR D O   
14051 C CB  . THR D 213 ? 0.7982 0.7255 0.7908 0.0213  0.1260  0.1161  213 THR D CB  
14052 O OG1 . THR D 213 ? 0.8920 0.8311 0.8760 0.0229  0.1118  0.1055  213 THR D OG1 
14053 C CG2 . THR D 213 ? 0.8042 0.7178 0.8053 0.0126  0.1350  0.1046  213 THR D CG2 
14054 N N   . THR D 214 ? 0.8659 0.8306 0.8377 0.0331  0.1130  0.1384  214 THR D N   
14055 C CA  . THR D 214 ? 0.7990 0.7749 0.7642 0.0404  0.1067  0.1520  214 THR D CA  
14056 C C   . THR D 214 ? 0.7377 0.7342 0.6900 0.0405  0.1020  0.1507  214 THR D C   
14057 O O   . THR D 214 ? 0.7350 0.7426 0.6788 0.0413  0.0907  0.1389  214 THR D O   
14058 C CB  . THR D 214 ? 0.8368 0.8127 0.8013 0.0444  0.0953  0.1481  214 THR D CB  
14059 O OG1 . THR D 214 ? 0.8534 0.8335 0.8126 0.0416  0.0860  0.1301  214 THR D OG1 
14060 C CG2 . THR D 214 ? 0.8292 0.7866 0.8061 0.0453  0.1018  0.1516  214 THR D CG2 
14061 N N   . PRO D 215 ? 0.7668 0.7688 0.7173 0.0397  0.1110  0.1627  215 PRO D N   
14062 C CA  . PRO D 215 ? 0.7640 0.7861 0.7022 0.0385  0.1090  0.1589  215 PRO D CA  
14063 C C   . PRO D 215 ? 0.8458 0.8870 0.7696 0.0441  0.0979  0.1632  215 PRO D C   
14064 O O   . PRO D 215 ? 0.8158 0.8733 0.7282 0.0434  0.0930  0.1531  215 PRO D O   
14065 C CB  . PRO D 215 ? 0.6710 0.6913 0.6130 0.0352  0.1238  0.1727  215 PRO D CB  
14066 C CG  . PRO D 215 ? 0.7488 0.7443 0.7074 0.0327  0.1335  0.1766  215 PRO D CG  
14067 C CD  . PRO D 215 ? 0.7704 0.7588 0.7314 0.0387  0.1252  0.1783  215 PRO D CD  
14068 N N   . ASN D 216 ? 0.8281 0.8693 0.7524 0.0494  0.0939  0.1773  216 ASN D N   
14069 C CA  . ASN D 216 ? 0.7482 0.8102 0.6587 0.0537  0.0833  0.1820  216 ASN D CA  
14070 C C   . ASN D 216 ? 0.7810 0.8437 0.6913 0.0559  0.0693  0.1726  216 ASN D C   
14071 O O   . ASN D 216 ? 0.7677 0.8460 0.6695 0.0590  0.0599  0.1779  216 ASN D O   
14072 C CB  . ASN D 216 ? 0.7357 0.8041 0.6457 0.0581  0.0878  0.2072  216 ASN D CB  
14073 C CG  . ASN D 216 ? 0.9508 1.0454 0.8423 0.0591  0.0846  0.2133  216 ASN D CG  
14074 O OD1 . ASN D 216 ? 1.1278 1.2318 1.0096 0.0553  0.0872  0.2030  216 ASN D OD1 
14075 N ND2 . ASN D 216 ? 0.9311 1.0394 0.8176 0.0642  0.0787  0.2299  216 ASN D ND2 
14076 N N   . VAL D 217 ? 0.6912 0.7386 0.6102 0.0537  0.0674  0.1588  217 VAL D N   
14077 C CA  . VAL D 217 ? 0.6428 0.6907 0.5618 0.0549  0.0545  0.1500  217 VAL D CA  
14078 C C   . VAL D 217 ? 0.7071 0.7691 0.6133 0.0538  0.0444  0.1346  217 VAL D C   
14079 O O   . VAL D 217 ? 0.7720 0.8399 0.6718 0.0518  0.0480  0.1260  217 VAL D O   
14080 C CB  . VAL D 217 ? 0.7769 0.8052 0.7077 0.0529  0.0558  0.1409  217 VAL D CB  
14081 C CG1 . VAL D 217 ? 0.8972 0.9113 0.8404 0.0542  0.0663  0.1542  217 VAL D CG1 
14082 C CG2 . VAL D 217 ? 0.7436 0.7673 0.6740 0.0484  0.0587  0.1248  217 VAL D CG2 
14083 N N   . LYS D 218 ? 0.7045 0.7718 0.6083 0.0550  0.0322  0.1306  218 LYS D N   
14084 C CA  . LYS D 218 ? 0.7293 0.8068 0.6229 0.0539  0.0219  0.1145  218 LYS D CA  
14085 C C   . LYS D 218 ? 0.7011 0.7644 0.6027 0.0524  0.0155  0.1009  218 LYS D C   
14086 O O   . LYS D 218 ? 0.6544 0.7098 0.5645 0.0526  0.0116  0.1057  218 LYS D O   
14087 C CB  . LYS D 218 ? 0.6603 0.7564 0.5441 0.0552  0.0123  0.1199  218 LYS D CB  
14088 C CG  . LYS D 218 ? 0.8129 0.9273 0.6846 0.0565  0.0174  0.1316  218 LYS D CG  
14089 C CD  . LYS D 218 ? 0.8803 1.0171 0.7392 0.0569  0.0062  0.1331  218 LYS D CD  
14090 C CE  . LYS D 218 ? 0.8250 0.9678 0.6902 0.0598  0.0034  0.1538  218 LYS D CE  
14091 N NZ  . LYS D 218 ? 0.8100 0.9702 0.6690 0.0586  -0.0114 0.1503  218 LYS D NZ  
14092 N N   . ILE D 219 ? 0.7232 0.7841 0.6227 0.0511  0.0147  0.0849  219 ILE D N   
14093 C CA  . ILE D 219 ? 0.7743 0.8228 0.6807 0.0502  0.0082  0.0723  219 ILE D CA  
14094 C C   . ILE D 219 ? 0.7719 0.8283 0.6706 0.0506  -0.0006 0.0570  219 ILE D C   
14095 O O   . ILE D 219 ? 0.6810 0.7519 0.5688 0.0513  0.0008  0.0537  219 ILE D O   
14096 C CB  . ILE D 219 ? 0.7499 0.7867 0.6644 0.0489  0.0158  0.0676  219 ILE D CB  
14097 C CG1 . ILE D 219 ? 0.7313 0.7772 0.6409 0.0490  0.0205  0.0582  219 ILE D CG1 
14098 C CG2 . ILE D 219 ? 0.7607 0.7892 0.6824 0.0479  0.0256  0.0811  219 ILE D CG2 
14099 C CD1 . ILE D 219 ? 0.6321 0.6702 0.5503 0.0476  0.0247  0.0501  219 ILE D CD1 
14100 N N   . PRO D 220 ? 0.7921 0.8389 0.6960 0.0501  -0.0093 0.0475  220 PRO D N   
14101 C CA  . PRO D 220 ? 0.7258 0.7766 0.6243 0.0506  -0.0171 0.0315  220 PRO D CA  
14102 C C   . PRO D 220 ? 0.7410 0.7938 0.6386 0.0528  -0.0116 0.0199  220 PRO D C   
14103 O O   . PRO D 220 ? 0.7572 0.8069 0.6600 0.0529  -0.0033 0.0234  220 PRO D O   
14104 C CB  . PRO D 220 ? 0.7474 0.7836 0.6553 0.0494  -0.0259 0.0272  220 PRO D CB  
14105 C CG  . PRO D 220 ? 0.7373 0.7617 0.6548 0.0491  -0.0201 0.0360  220 PRO D CG  
14106 C CD  . PRO D 220 ? 0.7128 0.7441 0.6280 0.0489  -0.0117 0.0506  220 PRO D CD  
14107 N N   . ASP D 221 ? 0.7597 0.8188 0.6512 0.0543  -0.0161 0.0053  221 ASP D N   
14108 C CA  . ASP D 221 ? 0.7125 0.7747 0.6052 0.0574  -0.0115 -0.0075 221 ASP D CA  
14109 C C   . ASP D 221 ? 0.8390 0.8851 0.7448 0.0592  -0.0161 -0.0152 221 ASP D C   
14110 O O   . ASP D 221 ? 0.8585 0.8951 0.7675 0.0593  -0.0253 -0.0213 221 ASP D O   
14111 C CB  . ASP D 221 ? 0.7773 0.8528 0.6585 0.0589  -0.0135 -0.0212 221 ASP D CB  
14112 C CG  . ASP D 221 ? 0.9781 1.0562 0.8630 0.0633  -0.0092 -0.0364 221 ASP D CG  
14113 O OD1 . ASP D 221 ? 1.0692 1.1503 0.9597 0.0642  -0.0006 -0.0328 221 ASP D OD1 
14114 O OD2 . ASP D 221 ? 1.0093 1.0870 0.8926 0.0658  -0.0142 -0.0526 221 ASP D OD2 
14115 N N   . PHE D 222 ? 0.7251 0.7690 0.6392 0.0603  -0.0099 -0.0141 222 PHE D N   
14116 C CA  . PHE D 222 ? 0.7422 0.7738 0.6686 0.0625  -0.0140 -0.0196 222 PHE D CA  
14117 C C   . PHE D 222 ? 0.7894 0.8263 0.7187 0.0679  -0.0143 -0.0355 222 PHE D C   
14118 O O   . PHE D 222 ? 0.7588 0.8048 0.6922 0.0699  -0.0073 -0.0387 222 PHE D O   
14119 C CB  . PHE D 222 ? 0.8018 0.8303 0.7356 0.0605  -0.0081 -0.0111 222 PHE D CB  
14120 C CG  . PHE D 222 ? 0.7351 0.7548 0.6689 0.0562  -0.0081 0.0026  222 PHE D CG  
14121 C CD1 . PHE D 222 ? 0.6185 0.6433 0.5447 0.0538  -0.0042 0.0126  222 PHE D CD1 
14122 C CD2 . PHE D 222 ? 0.5879 0.5953 0.5294 0.0552  -0.0117 0.0058  222 PHE D CD2 
14123 C CE1 . PHE D 222 ? 0.7452 0.7624 0.6735 0.0511  -0.0034 0.0249  222 PHE D CE1 
14124 C CE2 . PHE D 222 ? 0.6162 0.6165 0.5580 0.0517  -0.0106 0.0173  222 PHE D CE2 
14125 C CZ  . PHE D 222 ? 0.7022 0.7070 0.6383 0.0499  -0.0063 0.0265  222 PHE D CZ  
14126 N N   . ALA D 223 ? 0.7839 0.8152 0.7125 0.0702  -0.0220 -0.0460 223 ALA D N   
14127 C CA  . ALA D 223 ? 0.7916 0.8251 0.7246 0.0763  -0.0225 -0.0624 223 ALA D CA  
14128 C C   . ALA D 223 ? 0.7349 0.7555 0.6839 0.0808  -0.0270 -0.0650 223 ALA D C   
14129 O O   . ALA D 223 ? 0.7945 0.8105 0.7500 0.0866  -0.0303 -0.0779 223 ALA D O   
14130 C CB  . ALA D 223 ? 0.7949 0.8271 0.7199 0.0764  -0.0282 -0.0740 223 ALA D CB  
14131 N N   . VAL D 224 ? 0.7444 0.7591 0.6996 0.0784  -0.0273 -0.0531 224 VAL D N   
14132 C CA  . VAL D 224 ? 0.8452 0.8513 0.8144 0.0824  -0.0315 -0.0531 224 VAL D CA  
14133 C C   . VAL D 224 ? 0.7978 0.8113 0.7703 0.0796  -0.0259 -0.0440 224 VAL D C   
14134 O O   . VAL D 224 ? 0.7801 0.7991 0.7450 0.0740  -0.0199 -0.0360 224 VAL D O   
14135 C CB  . VAL D 224 ? 0.9042 0.8911 0.8775 0.0810  -0.0411 -0.0481 224 VAL D CB  
14136 C CG1 . VAL D 224 ? 0.8120 0.7950 0.7827 0.0746  -0.0407 -0.0328 224 VAL D CG1 
14137 C CG2 . VAL D 224 ? 0.7398 0.7176 0.7273 0.0880  -0.0467 -0.0528 224 VAL D CG2 
14138 N N   . SER D 225 ? 0.8066 0.8203 0.7912 0.0837  -0.0281 -0.0454 225 SER D N   
14139 C CA  . SER D 225 ? 0.8009 0.8214 0.7896 0.0803  -0.0245 -0.0382 225 SER D CA  
14140 C C   . SER D 225 ? 0.8207 0.8276 0.8104 0.0772  -0.0309 -0.0282 225 SER D C   
14141 O O   . SER D 225 ? 0.8187 0.8137 0.8132 0.0808  -0.0391 -0.0282 225 SER D O   
14142 C CB  . SER D 225 ? 0.7444 0.7777 0.7460 0.0860  -0.0234 -0.0452 225 SER D CB  
14143 O OG  . SER D 225 ? 0.8513 0.8903 0.8581 0.0822  -0.0226 -0.0389 225 SER D OG  
14144 N N   . PHE D 226 ? 0.7690 0.7770 0.7541 0.0702  -0.0264 -0.0196 226 PHE D N   
14145 C CA  . PHE D 226 ? 0.7688 0.7677 0.7543 0.0669  -0.0307 -0.0108 226 PHE D CA  
14146 C C   . PHE D 226 ? 0.8797 0.8886 0.8704 0.0646  -0.0284 -0.0100 226 PHE D C   
14147 O O   . PHE D 226 ? 0.9004 0.9047 0.8895 0.0606  -0.0302 -0.0033 226 PHE D O   
14148 C CB  . PHE D 226 ? 0.7911 0.7820 0.7673 0.0606  -0.0275 -0.0021 226 PHE D CB  
14149 C CG  . PHE D 226 ? 0.7308 0.7109 0.7036 0.0615  -0.0331 -0.0005 226 PHE D CG  
14150 C CD1 . PHE D 226 ? 0.6995 0.6677 0.6760 0.0625  -0.0414 0.0028  226 PHE D CD1 
14151 C CD2 . PHE D 226 ? 0.7573 0.7400 0.7233 0.0605  -0.0300 -0.0016 226 PHE D CD2 
14152 C CE1 . PHE D 226 ? 0.8319 0.7905 0.8068 0.0619  -0.0463 0.0038  226 PHE D CE1 
14153 C CE2 . PHE D 226 ? 0.7298 0.7047 0.6931 0.0602  -0.0357 -0.0009 226 PHE D CE2 
14154 C CZ  . PHE D 226 ? 0.8073 0.7698 0.7757 0.0605  -0.0438 0.0013  226 PHE D CZ  
14155 N N   . ARG D 227 ? 0.8867 0.9106 0.8838 0.0666  -0.0243 -0.0171 227 ARG D N   
14156 C CA  . ARG D 227 ? 0.8204 0.8568 0.8233 0.0630  -0.0217 -0.0175 227 ARG D CA  
14157 C C   . ARG D 227 ? 0.8540 0.8908 0.8637 0.0661  -0.0312 -0.0152 227 ARG D C   
14158 O O   . ARG D 227 ? 0.8114 0.8526 0.8205 0.0605  -0.0315 -0.0118 227 ARG D O   
14159 C CB  . ARG D 227 ? 0.7732 0.8273 0.7834 0.0648  -0.0155 -0.0257 227 ARG D CB  
14160 C CG  . ARG D 227 ? 0.9301 0.9952 0.9410 0.0562  -0.0064 -0.0255 227 ARG D CG  
14161 C CD  . ARG D 227 ? 0.9383 1.0156 0.9509 0.0564  0.0028  -0.0306 227 ARG D CD  
14162 N NE  . ARG D 227 ? 1.0561 1.1397 1.0744 0.0661  -0.0006 -0.0381 227 ARG D NE  
14163 C CZ  . ARG D 227 ? 1.0627 1.1471 1.0753 0.0694  0.0035  -0.0418 227 ARG D CZ  
14164 N NH1 . ARG D 227 ? 1.0722 1.1533 1.0734 0.0640  0.0109  -0.0371 227 ARG D NH1 
14165 N NH2 . ARG D 227 ? 0.8919 0.9808 0.9104 0.0786  0.0003  -0.0504 227 ARG D NH2 
14166 N N   . GLU D 228 ? 0.8389 0.8712 0.8552 0.0748  -0.0390 -0.0169 228 GLU D N   
14167 C CA  . GLU D 228 ? 0.7590 0.7906 0.7818 0.0785  -0.0485 -0.0121 228 GLU D CA  
14168 C C   . GLU D 228 ? 0.8299 0.8475 0.8431 0.0733  -0.0520 -0.0019 228 GLU D C   
14169 O O   . GLU D 228 ? 0.8349 0.8568 0.8486 0.0717  -0.0567 0.0037  228 GLU D O   
14170 C CB  . GLU D 228 ? 0.8060 0.8326 0.8395 0.0897  -0.0552 -0.0154 228 GLU D CB  
14171 C CG  . GLU D 228 ? 1.0709 1.0794 1.0992 0.0916  -0.0558 -0.0172 228 GLU D CG  
14172 C CD  . GLU D 228 ? 1.1021 1.1150 1.1251 0.0904  -0.0474 -0.0261 228 GLU D CD  
14173 O OE1 . GLU D 228 ? 0.9059 0.9357 0.9313 0.0895  -0.0405 -0.0314 228 GLU D OE1 
14174 O OE2 . GLU D 228 ? 1.0926 1.0929 1.1091 0.0901  -0.0479 -0.0275 228 GLU D OE2 
14175 N N   . ASP D 229 ? 0.8130 0.8160 0.8175 0.0705  -0.0496 0.0006  229 ASP D N   
14176 C CA  . ASP D 229 ? 0.7302 0.7212 0.7268 0.0657  -0.0518 0.0103  229 ASP D CA  
14177 C C   . ASP D 229 ? 0.7969 0.7939 0.7862 0.0571  -0.0458 0.0131  229 ASP D C   
14178 O O   . ASP D 229 ? 0.8089 0.8016 0.7930 0.0536  -0.0482 0.0203  229 ASP D O   
14179 C CB  . ASP D 229 ? 0.7912 0.7683 0.7823 0.0646  -0.0505 0.0118  229 ASP D CB  
14180 C CG  . ASP D 229 ? 0.8963 0.8628 0.8939 0.0712  -0.0581 0.0102  229 ASP D CG  
14181 O OD1 . ASP D 229 ? 0.9171 0.8844 0.9236 0.0772  -0.0644 0.0101  229 ASP D OD1 
14182 O OD2 . ASP D 229 ? 0.7536 0.7109 0.7480 0.0703  -0.0580 0.0090  229 ASP D OD2 
14183 N N   . ALA D 230 ? 0.7450 0.7515 0.7337 0.0534  -0.0373 0.0073  230 ALA D N   
14184 C CA  . ALA D 230 ? 0.7205 0.7321 0.7044 0.0451  -0.0311 0.0079  230 ALA D CA  
14185 C C   . ALA D 230 ? 0.8316 0.8559 0.8192 0.0442  -0.0366 0.0070  230 ALA D C   
14186 O O   . ALA D 230 ? 0.8012 0.8260 0.7823 0.0381  -0.0360 0.0099  230 ALA D O   
14187 C CB  . ALA D 230 ? 0.7061 0.7240 0.6907 0.0412  -0.0206 0.0023  230 ALA D CB  
14188 N N   . SER D 231 ? 0.8451 0.8813 0.8434 0.0505  -0.0420 0.0029  231 SER D N   
14189 C CA  . SER D 231 ? 0.7855 0.8363 0.7887 0.0508  -0.0491 0.0036  231 SER D CA  
14190 C C   . SER D 231 ? 0.7598 0.8023 0.7575 0.0525  -0.0576 0.0135  231 SER D C   
14191 O O   . SER D 231 ? 0.8227 0.8736 0.8155 0.0478  -0.0605 0.0164  231 SER D O   
14192 C CB  . SER D 231 ? 0.7676 0.8324 0.7857 0.0593  -0.0537 -0.0013 231 SER D CB  
14193 O OG  . SER D 231 ? 0.9557 1.0318 0.9789 0.0564  -0.0452 -0.0100 231 SER D OG  
14194 N N   . LYS D 232 ? 0.7113 0.7380 0.7096 0.0586  -0.0614 0.0186  232 LYS D N   
14195 C CA  . LYS D 232 ? 0.7970 0.8151 0.7917 0.0603  -0.0692 0.0294  232 LYS D CA  
14196 C C   . LYS D 232 ? 0.7897 0.8019 0.7704 0.0512  -0.0646 0.0345  232 LYS D C   
14197 O O   . LYS D 232 ? 0.7476 0.7626 0.7228 0.0493  -0.0694 0.0421  232 LYS D O   
14198 C CB  . LYS D 232 ? 0.7328 0.7337 0.7329 0.0675  -0.0734 0.0326  232 LYS D CB  
14199 C CG  . LYS D 232 ? 0.7501 0.7547 0.7639 0.0768  -0.0757 0.0251  232 LYS D CG  
14200 C CD  . LYS D 232 ? 0.8249 0.8176 0.8481 0.0859  -0.0847 0.0307  232 LYS D CD  
14201 C CE  . LYS D 232 ? 0.9069 0.8808 0.9308 0.0878  -0.0832 0.0272  232 LYS D CE  
14202 N NZ  . LYS D 232 ? 0.8577 0.8196 0.8940 0.0971  -0.0910 0.0298  232 LYS D NZ  
14203 N N   . HIS D 233 ? 0.7738 0.7788 0.7489 0.0461  -0.0551 0.0309  233 HIS D N   
14204 C CA  . HIS D 233 ? 0.8196 0.8187 0.7832 0.0385  -0.0495 0.0351  233 HIS D CA  
14205 C C   . HIS D 233 ? 0.8346 0.8474 0.7923 0.0317  -0.0476 0.0320  233 HIS D C   
14206 O O   . HIS D 233 ? 0.8298 0.8417 0.7778 0.0272  -0.0472 0.0369  233 HIS D O   
14207 C CB  . HIS D 233 ? 0.7994 0.7895 0.7606 0.0355  -0.0395 0.0322  233 HIS D CB  
14208 C CG  . HIS D 233 ? 0.7541 0.7300 0.7160 0.0387  -0.0411 0.0379  233 HIS D CG  
14209 N ND1 . HIS D 233 ? 0.7682 0.7403 0.7355 0.0431  -0.0413 0.0342  233 HIS D ND1 
14210 C CD2 . HIS D 233 ? 0.7704 0.7365 0.7282 0.0372  -0.0425 0.0465  233 HIS D CD2 
14211 C CE1 . HIS D 233 ? 0.6745 0.6351 0.6413 0.0439  -0.0434 0.0397  233 HIS D CE1 
14212 N NE2 . HIS D 233 ? 0.7594 0.7161 0.7214 0.0404  -0.0440 0.0476  233 HIS D NE2 
14213 N N   . VAL D 234 ? 0.7947 0.8214 0.7580 0.0304  -0.0461 0.0232  234 VAL D N   
14214 C CA  . VAL D 234 ? 0.8438 0.8848 0.8022 0.0225  -0.0444 0.0181  234 VAL D CA  
14215 C C   . VAL D 234 ? 0.8339 0.8898 0.7931 0.0252  -0.0562 0.0225  234 VAL D C   
14216 O O   . VAL D 234 ? 0.7791 0.8444 0.7289 0.0188  -0.0574 0.0227  234 VAL D O   
14217 C CB  . VAL D 234 ? 0.7299 0.7800 0.6951 0.0182  -0.0372 0.0069  234 VAL D CB  
14218 C CG1 . VAL D 234 ? 0.7412 0.8049 0.7017 0.0082  -0.0348 -0.0001 234 VAL D CG1 
14219 C CG2 . VAL D 234 ? 0.6411 0.6763 0.6054 0.0164  -0.0259 0.0052  234 VAL D CG2 
14220 N N   . GLU D 235 ? 0.8568 0.9157 0.8272 0.0349  -0.0649 0.0263  235 GLU D N   
14221 C CA  . GLU D 235 ? 0.7660 0.8395 0.7394 0.0392  -0.0766 0.0325  235 GLU D CA  
14222 C C   . GLU D 235 ? 0.7710 0.8356 0.7341 0.0397  -0.0817 0.0455  235 GLU D C   
14223 O O   . GLU D 235 ? 0.8627 0.9406 0.8181 0.0365  -0.0871 0.0502  235 GLU D O   
14224 C CB  . GLU D 235 ? 0.8575 0.9347 0.8480 0.0507  -0.0834 0.0329  235 GLU D CB  
14225 C CG  . GLU D 235 ? 0.9142 1.0068 0.9162 0.0503  -0.0795 0.0210  235 GLU D CG  
14226 C CD  . GLU D 235 ? 1.1368 1.2537 1.1514 0.0555  -0.0889 0.0213  235 GLU D CD  
14227 O OE1 . GLU D 235 ? 1.0204 1.1556 1.0300 0.0486  -0.0923 0.0208  235 GLU D OE1 
14228 O OE2 . GLU D 235 ? 1.2388 1.3578 1.2687 0.0663  -0.0929 0.0215  235 GLU D OE2 
14229 N N   . LEU D 236 ? 0.8067 0.8502 0.7695 0.0432  -0.0800 0.0517  236 LEU D N   
14230 C CA  . LEU D 236 ? 0.7693 0.8036 0.7235 0.0428  -0.0836 0.0647  236 LEU D CA  
14231 C C   . LEU D 236 ? 0.7443 0.7810 0.6818 0.0325  -0.0766 0.0641  236 LEU D C   
14232 O O   . LEU D 236 ? 0.7485 0.7878 0.6762 0.0305  -0.0802 0.0741  236 LEU D O   
14233 C CB  . LEU D 236 ? 0.7193 0.7311 0.6784 0.0473  -0.0827 0.0698  236 LEU D CB  
14234 C CG  . LEU D 236 ? 0.7386 0.7440 0.7135 0.0579  -0.0897 0.0707  236 LEU D CG  
14235 C CD1 . LEU D 236 ? 0.5778 0.5643 0.5571 0.0595  -0.0853 0.0672  236 LEU D CD1 
14236 C CD2 . LEU D 236 ? 0.7004 0.7045 0.6789 0.0637  -0.1003 0.0848  236 LEU D CD2 
14237 N N   . ALA D 237 ? 0.7380 0.7735 0.6722 0.0260  -0.0659 0.0529  237 ALA D N   
14238 C CA  . ALA D 237 ? 0.7145 0.7530 0.6344 0.0164  -0.0582 0.0497  237 ALA D CA  
14239 C C   . ALA D 237 ? 0.7806 0.8412 0.6935 0.0116  -0.0632 0.0466  237 ALA D C   
14240 O O   . ALA D 237 ? 0.8071 0.8731 0.7057 0.0059  -0.0623 0.0495  237 ALA D O   
14241 C CB  . ALA D 237 ? 0.6819 0.7133 0.6028 0.0114  -0.0456 0.0384  237 ALA D CB  
14242 N N   . LYS D 238 ? 0.7774 0.8528 0.7003 0.0136  -0.0684 0.0403  238 LYS D N   
14243 C CA  . LYS D 238 ? 0.8063 0.9062 0.7243 0.0088  -0.0747 0.0370  238 LYS D CA  
14244 C C   . LYS D 238 ? 0.8027 0.9109 0.7145 0.0131  -0.0862 0.0519  238 LYS D C   
14245 O O   . LYS D 238 ? 0.7609 0.8860 0.6597 0.0069  -0.0894 0.0523  238 LYS D O   
14246 C CB  . LYS D 238 ? 0.8585 0.9742 0.7920 0.0111  -0.0786 0.0288  238 LYS D CB  
14247 C CG  . LYS D 238 ? 0.9037 1.0213 0.8392 0.0020  -0.0677 0.0128  238 LYS D CG  
14248 C CD  . LYS D 238 ? 0.8706 1.0118 0.8192 0.0011  -0.0725 0.0046  238 LYS D CD  
14249 C CE  . LYS D 238 ? 0.8644 1.0117 0.8290 0.0140  -0.0826 0.0122  238 LYS D CE  
14250 N NZ  . LYS D 238 ? 0.8128 0.9791 0.7936 0.0135  -0.0829 0.0024  238 LYS D NZ  
14251 N N   . GLU D 239 ? 0.8851 0.9813 0.8057 0.0234  -0.0923 0.0643  239 GLU D N   
14252 C CA  . GLU D 239 ? 0.8987 1.0003 0.8153 0.0282  -0.1031 0.0808  239 GLU D CA  
14253 C C   . GLU D 239 ? 0.8576 0.9499 0.7570 0.0227  -0.0985 0.0894  239 GLU D C   
14254 O O   . GLU D 239 ? 0.9360 1.0410 0.8239 0.0212  -0.1046 0.0997  239 GLU D O   
14255 C CB  . GLU D 239 ? 0.8875 0.9772 0.8215 0.0408  -0.1103 0.0904  239 GLU D CB  
14256 C CG  . GLU D 239 ? 0.8763 0.9778 0.8285 0.0478  -0.1152 0.0830  239 GLU D CG  
14257 C CD  . GLU D 239 ? 1.1419 1.2745 1.0924 0.0435  -0.1205 0.0775  239 GLU D CD  
14258 O OE1 . GLU D 239 ? 1.2107 1.3589 1.1505 0.0413  -0.1279 0.0867  239 GLU D OE1 
14259 O OE2 . GLU D 239 ? 1.0988 1.2416 1.0590 0.0420  -0.1175 0.0641  239 GLU D OE2 
14260 N N   . LYS D 240 ? 0.7316 0.8037 0.6291 0.0199  -0.0876 0.0859  240 LYS D N   
14261 C CA  . LYS D 240 ? 0.8067 0.8721 0.6891 0.0143  -0.0817 0.0928  240 LYS D CA  
14262 C C   . LYS D 240 ? 0.8455 0.9272 0.7104 0.0039  -0.0762 0.0837  240 LYS D C   
14263 O O   . LYS D 240 ? 0.8656 0.9538 0.7148 -0.0002 -0.0761 0.0914  240 LYS D O   
14264 C CB  . LYS D 240 ? 0.7162 0.7588 0.6032 0.0142  -0.0717 0.0910  240 LYS D CB  
14265 C CG  . LYS D 240 ? 0.8102 0.8449 0.6865 0.0106  -0.0667 0.1014  240 LYS D CG  
14266 C CD  . LYS D 240 ? 0.8526 0.8830 0.7321 0.0161  -0.0764 0.1200  240 LYS D CD  
14267 C CE  . LYS D 240 ? 0.8886 0.9149 0.7566 0.0111  -0.0709 0.1309  240 LYS D CE  
14268 N NZ  . LYS D 240 ? 0.9747 0.9897 0.8501 0.0160  -0.0780 0.1491  240 LYS D NZ  
14269 N N   . TYR D 241 ? 0.7588 0.8471 0.6258 -0.0010 -0.0710 0.0668  241 TYR D N   
14270 C CA  . TYR D 241 ? 0.8014 0.9051 0.6530 -0.0117 -0.0660 0.0553  241 TYR D CA  
14271 C C   . TYR D 241 ? 0.8346 0.9646 0.6773 -0.0129 -0.0783 0.0606  241 TYR D C   
14272 O O   . TYR D 241 ? 0.8016 0.9449 0.6257 -0.0210 -0.0764 0.0579  241 TYR D O   
14273 C CB  . TYR D 241 ? 0.7838 0.8873 0.6430 -0.0166 -0.0583 0.0368  241 TYR D CB  
14274 C CG  . TYR D 241 ? 0.8060 0.9181 0.6515 -0.0288 -0.0495 0.0216  241 TYR D CG  
14275 C CD1 . TYR D 241 ? 0.8321 0.9693 0.6713 -0.0354 -0.0561 0.0137  241 TYR D CD1 
14276 C CD2 . TYR D 241 ? 0.8176 0.9131 0.6579 -0.0336 -0.0346 0.0143  241 TYR D CD2 
14277 C CE1 . TYR D 241 ? 0.8469 0.9914 0.6737 -0.0475 -0.0479 -0.0023 241 TYR D CE1 
14278 C CE2 . TYR D 241 ? 0.8721 0.9733 0.7010 -0.0446 -0.0255 -0.0012 241 TYR D CE2 
14279 C CZ  . TYR D 241 ? 0.8057 0.9309 0.6274 -0.0520 -0.0322 -0.0102 241 TYR D CZ  
14280 O OH  . TYR D 241 ? 0.8750 1.0056 0.6852 -0.0639 -0.0233 -0.0275 241 TYR D OH  
14281 N N   . PHE D 242 ? 0.8830 1.0219 0.7390 -0.0045 -0.0909 0.0682  242 PHE D N   
14282 C CA  . PHE D 242 ? 0.8855 1.0505 0.7351 -0.0038 -0.1041 0.0768  242 PHE D CA  
14283 C C   . PHE D 242 ? 0.8894 1.0527 0.7250 -0.0022 -0.1075 0.0955  242 PHE D C   
14284 O O   . PHE D 242 ? 0.9433 1.1288 0.7629 -0.0064 -0.1136 0.1007  242 PHE D O   
14285 C CB  . PHE D 242 ? 0.8074 0.9802 0.6778 0.0068  -0.1161 0.0822  242 PHE D CB  
14286 C CG  . PHE D 242 ? 0.9251 1.1313 0.7936 0.0057  -0.1285 0.0832  242 PHE D CG  
14287 C CD1 . PHE D 242 ? 0.9991 1.2252 0.8682 -0.0029 -0.1273 0.0654  242 PHE D CD1 
14288 C CD2 . PHE D 242 ? 0.8514 1.0698 0.7186 0.0132  -0.1416 0.1029  242 PHE D CD2 
14289 C CE1 . PHE D 242 ? 0.8801 1.1401 0.7484 -0.0045 -0.1398 0.0662  242 PHE D CE1 
14290 C CE2 . PHE D 242 ? 0.8092 1.0610 0.6752 0.0127  -0.1541 0.1052  242 PHE D CE2 
14291 C CZ  . PHE D 242 ? 0.8029 1.0766 0.6694 0.0037  -0.1535 0.0865  242 PHE D CZ  
14292 N N   . GLU D 243 ? 0.8574 0.9957 0.6985 0.0034  -0.1036 0.1062  243 GLU D N   
14293 C CA  . GLU D 243 ? 0.9276 1.0625 0.7576 0.0044  -0.1057 0.1251  243 GLU D CA  
14294 C C   . GLU D 243 ? 0.9707 1.1149 0.7764 -0.0068 -0.0969 0.1203  243 GLU D C   
14295 O O   . GLU D 243 ? 0.9912 1.1542 0.7802 -0.0096 -0.1025 0.1302  243 GLU D O   
14296 C CB  . GLU D 243 ? 0.9113 1.0170 0.7536 0.0103  -0.1015 0.1340  243 GLU D CB  
14297 C CG  . GLU D 243 ? 0.9637 1.0645 0.8046 0.0151  -0.1084 0.1576  243 GLU D CG  
14298 C CD  . GLU D 243 ? 1.0405 1.1139 0.8896 0.0168  -0.1017 0.1642  243 GLU D CD  
14299 O OE1 . GLU D 243 ? 1.0438 1.1000 0.9112 0.0224  -0.1014 0.1590  243 GLU D OE1 
14300 O OE2 . GLU D 243 ? 1.0389 1.1095 0.8763 0.0120  -0.0965 0.1742  243 GLU D OE2 
14301 N N   . ILE D 244 ? 0.8929 1.0249 0.6961 -0.0130 -0.0827 0.1050  244 ILE D N   
14302 C CA  . ILE D 244 ? 0.8822 1.0195 0.6641 -0.0227 -0.0720 0.0993  244 ILE D CA  
14303 C C   . ILE D 244 ? 0.9363 1.1001 0.7029 -0.0314 -0.0742 0.0857  244 ILE D C   
14304 O O   . ILE D 244 ? 0.9745 1.1575 0.7209 -0.0361 -0.0773 0.0913  244 ILE D O   
14305 C CB  . ILE D 244 ? 0.8409 0.9563 0.6276 -0.0253 -0.0560 0.0875  244 ILE D CB  
14306 C CG1 . ILE D 244 ? 0.9273 1.0189 0.7334 -0.0166 -0.0564 0.0977  244 ILE D CG1 
14307 C CG2 . ILE D 244 ? 0.9858 1.1032 0.7534 -0.0325 -0.0446 0.0865  244 ILE D CG2 
14308 C CD1 . ILE D 244 ? 0.8542 0.9410 0.6590 -0.0123 -0.0617 0.1198  244 ILE D CD1 
14309 N N   . PHE D 245 ? 0.9082 1.0744 0.6839 -0.0342 -0.0726 0.0675  245 PHE D N   
14310 C CA  . PHE D 245 ? 0.9696 1.1573 0.7320 -0.0452 -0.0712 0.0497  245 PHE D CA  
14311 C C   . PHE D 245 ? 0.9431 1.1585 0.7085 -0.0445 -0.0871 0.0508  245 PHE D C   
14312 O O   . PHE D 245 ? 0.8320 1.0687 0.5867 -0.0545 -0.0880 0.0360  245 PHE D O   
14313 C CB  . PHE D 245 ? 0.8954 1.0685 0.6658 -0.0509 -0.0575 0.0279  245 PHE D CB  
14314 C CG  . PHE D 245 ? 0.9469 1.0929 0.7190 -0.0495 -0.0427 0.0282  245 PHE D CG  
14315 C CD1 . PHE D 245 ? 0.9598 1.1047 0.7141 -0.0565 -0.0308 0.0222  245 PHE D CD1 
14316 C CD2 . PHE D 245 ? 0.8995 1.0230 0.6911 -0.0408 -0.0408 0.0348  245 PHE D CD2 
14317 C CE1 . PHE D 245 ? 0.8999 1.0221 0.6580 -0.0544 -0.0172 0.0234  245 PHE D CE1 
14318 C CE2 . PHE D 245 ? 0.8294 0.9311 0.6234 -0.0394 -0.0283 0.0360  245 PHE D CE2 
14319 C CZ  . PHE D 245 ? 0.8434 0.9446 0.6216 -0.0459 -0.0165 0.0308  245 PHE D CZ  
14320 N N   . GLY D 246 ? 0.8756 1.0919 0.6558 -0.0333 -0.0997 0.0676  246 GLY D N   
14321 C CA  . GLY D 246 ? 0.7916 1.0365 0.5755 -0.0310 -0.1156 0.0720  246 GLY D CA  
14322 C C   . GLY D 246 ? 0.8500 1.1041 0.6511 -0.0327 -0.1178 0.0556  246 GLY D C   
14323 O O   . GLY D 246 ? 0.9062 1.1876 0.7119 -0.0314 -0.1310 0.0579  246 GLY D O   
14324 N N   . GLU D 247 ? 0.8623 1.0960 0.6740 -0.0353 -0.1054 0.0404  247 GLU D N   
14325 C CA  . GLU D 247 ? 0.8614 1.1039 0.6898 -0.0380 -0.1060 0.0251  247 GLU D CA  
14326 C C   . GLU D 247 ? 0.8547 1.0684 0.7016 -0.0323 -0.0963 0.0215  247 GLU D C   
14327 O O   . GLU D 247 ? 0.8416 1.0297 0.6870 -0.0279 -0.0888 0.0285  247 GLU D O   
14328 C CB  . GLU D 247 ? 0.8955 1.1531 0.7115 -0.0539 -0.1000 0.0035  247 GLU D CB  
14329 C CG  . GLU D 247 ? 0.9525 1.1870 0.7567 -0.0620 -0.0820 -0.0087 247 GLU D CG  
14330 C CD  . GLU D 247 ? 1.1070 1.3484 0.9093 -0.0764 -0.0739 -0.0333 247 GLU D CD  
14331 O OE1 . GLU D 247 ? 1.2072 1.4566 1.0269 -0.0779 -0.0767 -0.0418 247 GLU D OE1 
14332 O OE2 . GLU D 247 ? 0.9928 1.2317 0.7768 -0.0863 -0.0642 -0.0446 247 GLU D OE2 
14333 N N   . HIS D 248 ? 0.8179 1.0381 0.6822 -0.0324 -0.0971 0.0115  248 HIS D N   
14334 C CA  . HIS D 248 ? 0.8544 1.0487 0.7341 -0.0270 -0.0879 0.0092  248 HIS D CA  
14335 C C   . HIS D 248 ? 0.8282 1.0077 0.7031 -0.0377 -0.0717 -0.0074 248 HIS D C   
14336 O O   . HIS D 248 ? 0.8075 1.0002 0.6737 -0.0498 -0.0685 -0.0213 248 HIS D O   
14337 C CB  . HIS D 248 ? 0.7714 0.9764 0.6740 -0.0205 -0.0944 0.0076  248 HIS D CB  
14338 C CG  . HIS D 248 ? 0.8411 1.0488 0.7542 -0.0060 -0.1069 0.0249  248 HIS D CG  
14339 N ND1 . HIS D 248 ? 0.9452 1.1285 0.8592 0.0035  -0.1059 0.0379  248 HIS D ND1 
14340 C CD2 . HIS D 248 ? 0.8918 1.1234 0.8163 0.0007  -0.1205 0.0312  248 HIS D CD2 
14341 C CE1 . HIS D 248 ? 0.9603 1.1501 0.8858 0.0152  -0.1177 0.0509  248 HIS D CE1 
14342 N NE2 . HIS D 248 ? 0.9327 1.1518 0.8650 0.0145  -0.1267 0.0477  248 HIS D NE2 
14343 N N   . PRO D 249 ? 0.8145 0.9665 0.6949 -0.0337 -0.0611 -0.0062 249 PRO D N   
14344 C CA  . PRO D 249 ? 0.8130 0.9493 0.6898 -0.0426 -0.0453 -0.0196 249 PRO D CA  
14345 C C   . PRO D 249 ? 0.8754 1.0167 0.7665 -0.0480 -0.0410 -0.0335 249 PRO D C   
14346 O O   . PRO D 249 ? 0.8852 1.0292 0.7927 -0.0412 -0.0454 -0.0305 249 PRO D O   
14347 C CB  . PRO D 249 ? 0.7355 0.8441 0.6155 -0.0346 -0.0380 -0.0103 249 PRO D CB  
14348 C CG  . PRO D 249 ? 0.7345 0.8440 0.6280 -0.0228 -0.0485 0.0012  249 PRO D CG  
14349 C CD  . PRO D 249 ? 0.7828 0.9168 0.6730 -0.0212 -0.0632 0.0075  249 PRO D CD  
14350 N N   . VAL D 250 ? 0.9027 1.0456 0.7881 -0.0608 -0.0319 -0.0493 250 VAL D N   
14351 C CA  . VAL D 250 ? 0.8492 0.9944 0.7482 -0.0682 -0.0256 -0.0631 250 VAL D CA  
14352 C C   . VAL D 250 ? 0.8793 0.9969 0.7810 -0.0714 -0.0083 -0.0692 250 VAL D C   
14353 O O   . VAL D 250 ? 0.8617 0.9766 0.7766 -0.0763 -0.0015 -0.0777 250 VAL D O   
14354 C CB  . VAL D 250 ? 0.9705 1.1407 0.8647 -0.0818 -0.0292 -0.0780 250 VAL D CB  
14355 C CG1 . VAL D 250 ? 0.8606 1.0621 0.7563 -0.0779 -0.0475 -0.0709 250 VAL D CG1 
14356 C CG2 . VAL D 250 ? 0.9094 1.0745 0.7829 -0.0911 -0.0221 -0.0864 250 VAL D CG2 
14357 N N   . TYR D 251 ? 0.8624 0.9606 0.7532 -0.0690 -0.0007 -0.0646 251 TYR D N   
14358 C CA  . TYR D 251 ? 0.8030 0.8748 0.6979 -0.0694 0.0152  -0.0671 251 TYR D CA  
14359 C C   . TYR D 251 ? 0.8030 0.8587 0.6988 -0.0568 0.0148  -0.0508 251 TYR D C   
14360 O O   . TYR D 251 ? 0.8446 0.9039 0.7307 -0.0516 0.0075  -0.0409 251 TYR D O   
14361 C CB  . TYR D 251 ? 0.8910 0.9546 0.7734 -0.0793 0.0269  -0.0793 251 TYR D CB  
14362 C CG  . TYR D 251 ? 0.9656 1.0497 0.8408 -0.0925 0.0240  -0.0954 251 TYR D CG  
14363 C CD1 . TYR D 251 ? 0.9885 1.0766 0.8753 -0.1023 0.0281  -0.1092 251 TYR D CD1 
14364 C CD2 . TYR D 251 ? 0.9181 1.0181 0.7745 -0.0961 0.0174  -0.0970 251 TYR D CD2 
14365 C CE1 . TYR D 251 ? 0.9878 1.0959 0.8689 -0.1156 0.0249  -0.1251 251 TYR D CE1 
14366 C CE2 . TYR D 251 ? 0.9402 1.0613 0.7889 -0.1090 0.0140  -0.1126 251 TYR D CE2 
14367 C CZ  . TYR D 251 ? 0.9305 1.0556 0.7920 -0.1190 0.0175  -0.1273 251 TYR D CZ  
14368 O OH  . TYR D 251 ? 1.0379 1.1853 0.8929 -0.1330 0.0136  -0.1440 251 TYR D OH  
14369 N N   . MET D 252 ? 0.7894 0.8285 0.6971 -0.0522 0.0223  -0.0476 252 MET D N   
14370 C CA  . MET D 252 ? 0.7911 0.8162 0.7008 -0.0412 0.0218  -0.0333 252 MET D CA  
14371 C C   . MET D 252 ? 0.7991 0.8026 0.7139 -0.0409 0.0365  -0.0335 252 MET D C   
14372 O O   . MET D 252 ? 0.7869 0.7854 0.7095 -0.0462 0.0453  -0.0416 252 MET D O   
14373 C CB  . MET D 252 ? 0.7092 0.7401 0.6296 -0.0324 0.0118  -0.0253 252 MET D CB  
14374 C CG  . MET D 252 ? 0.7369 0.7757 0.6529 -0.0249 -0.0019 -0.0143 252 MET D CG  
14375 S SD  . MET D 252 ? 0.8982 0.9450 0.8285 -0.0152 -0.0128 -0.0090 252 MET D SD  
14376 C CE  . MET D 252 ? 0.6450 0.6985 0.5698 -0.0076 -0.0276 0.0036  252 MET D CE  
14377 N N   . TRP D 253 ? 0.8081 0.7992 0.7195 -0.0345 0.0389  -0.0235 253 TRP D N   
14378 C CA  . TRP D 253 ? 0.7922 0.7646 0.7101 -0.0317 0.0511  -0.0202 253 TRP D CA  
14379 C C   . TRP D 253 ? 0.7493 0.7181 0.6757 -0.0225 0.0460  -0.0089 253 TRP D C   
14380 O O   . TRP D 253 ? 0.6646 0.6356 0.5884 -0.0162 0.0370  0.0006  253 TRP D O   
14381 C CB  . TRP D 253 ? 0.7089 0.6718 0.6195 -0.0307 0.0581  -0.0169 253 TRP D CB  
14382 C CG  . TRP D 253 ? 0.6941 0.6407 0.6130 -0.0247 0.0672  -0.0088 253 TRP D CG  
14383 C CD1 . TRP D 253 ? 0.7384 0.6811 0.6589 -0.0167 0.0639  0.0042  253 TRP D CD1 
14384 C CD2 . TRP D 253 ? 0.7216 0.6544 0.6494 -0.0262 0.0809  -0.0125 253 TRP D CD2 
14385 N NE1 . TRP D 253 ? 0.7511 0.6809 0.6806 -0.0129 0.0739  0.0089  253 TRP D NE1 
14386 C CE2 . TRP D 253 ? 0.8106 0.7333 0.7447 -0.0180 0.0847  -0.0004 253 TRP D CE2 
14387 C CE3 . TRP D 253 ? 0.7693 0.6973 0.7013 -0.0339 0.0904  -0.0245 253 TRP D CE3 
14388 C CZ2 . TRP D 253 ? 0.8008 0.7094 0.7450 -0.0162 0.0972  0.0016  253 TRP D CZ2 
14389 C CZ3 . TRP D 253 ? 0.8566 0.7679 0.7990 -0.0326 0.1037  -0.0228 253 TRP D CZ3 
14390 C CH2 . TRP D 253 ? 0.7334 0.6354 0.6817 -0.0232 0.1068  -0.0091 253 TRP D CH2 
14391 N N   . PRO D 254 ? 0.7884 0.7521 0.7247 -0.0219 0.0515  -0.0096 254 PRO D N   
14392 C CA  . PRO D 254 ? 0.7335 0.6948 0.6760 -0.0135 0.0473  0.0003  254 PRO D CA  
14393 C C   . PRO D 254 ? 0.7269 0.6761 0.6686 -0.0079 0.0511  0.0104  254 PRO D C   
14394 O O   . PRO D 254 ? 0.6768 0.6153 0.6195 -0.0099 0.0627  0.0099  254 PRO D O   
14395 C CB  . PRO D 254 ? 0.7069 0.6661 0.6584 -0.0159 0.0550  -0.0032 254 PRO D CB  
14396 C CG  . PRO D 254 ? 0.7106 0.6617 0.6623 -0.0241 0.0673  -0.0114 254 PRO D CG  
14397 C CD  . PRO D 254 ? 0.7160 0.6756 0.6582 -0.0295 0.0624  -0.0192 254 PRO D CD  
14398 N N   . PRO D 255 ? 0.7498 0.7006 0.6911 -0.0011 0.0419  0.0193  255 PRO D N   
14399 C CA  . PRO D 255 ? 0.7246 0.6667 0.6670 0.0036  0.0445  0.0292  255 PRO D CA  
14400 C C   . PRO D 255 ? 0.7959 0.7296 0.7456 0.0057  0.0543  0.0327  255 PRO D C   
14401 O O   . PRO D 255 ? 0.7706 0.7066 0.7246 0.0066  0.0543  0.0320  255 PRO D O   
14402 C CB  . PRO D 255 ? 0.6901 0.6367 0.6326 0.0093  0.0316  0.0359  255 PRO D CB  
14403 C CG  . PRO D 255 ? 0.7204 0.6770 0.6593 0.0074  0.0227  0.0303  255 PRO D CG  
14404 C CD  . PRO D 255 ? 0.8391 0.7999 0.7803 0.0025  0.0285  0.0206  255 PRO D CD  
14405 N N   . GLN D 256 ? 0.7230 0.6480 0.6746 0.0067  0.0632  0.0372  256 GLN D N   
14406 C CA  . GLN D 256 ? 0.7010 0.6174 0.6605 0.0095  0.0734  0.0428  256 GLN D CA  
14407 C C   . GLN D 256 ? 0.7389 0.6507 0.7023 0.0047  0.0829  0.0356  256 GLN D C   
14408 O O   . GLN D 256 ? 0.7885 0.6948 0.7588 0.0071  0.0895  0.0414  256 GLN D O   
14409 C CB  . GLN D 256 ? 0.7459 0.6660 0.7091 0.0160  0.0668  0.0530  256 GLN D CB  
14410 C CG  . GLN D 256 ? 0.6644 0.5901 0.6247 0.0193  0.0553  0.0584  256 GLN D CG  
14411 C CD  . GLN D 256 ? 0.7467 0.6687 0.7105 0.0219  0.0595  0.0664  256 GLN D CD  
14412 O OE1 . GLN D 256 ? 0.6769 0.5919 0.6451 0.0220  0.0714  0.0672  256 GLN D OE1 
14413 N NE2 . GLN D 256 ? 0.7550 0.6815 0.7182 0.0240  0.0504  0.0721  256 GLN D NE2 
14414 N N   . ALA D 257 ? 0.7553 0.6700 0.7145 -0.0027 0.0834  0.0236  257 ALA D N   
14415 C CA  . ALA D 257 ? 0.7477 0.6598 0.7112 -0.0093 0.0910  0.0150  257 ALA D CA  
14416 C C   . ALA D 257 ? 0.7969 0.7161 0.7647 -0.0077 0.0869  0.0179  257 ALA D C   
14417 O O   . ALA D 257 ? 0.7793 0.6957 0.7531 -0.0124 0.0946  0.0143  257 ALA D O   
14418 C CB  . ALA D 257 ? 0.6922 0.5879 0.6628 -0.0106 0.1071  0.0153  257 ALA D CB  
14419 N N   . SER D 258 ? 0.7274 0.6557 0.6926 -0.0017 0.0753  0.0239  258 SER D N   
14420 C CA  . SER D 258 ? 0.7199 0.6555 0.6882 0.0008  0.0721  0.0264  258 SER D CA  
14421 C C   . SER D 258 ? 0.7306 0.6767 0.7005 -0.0053 0.0700  0.0158  258 SER D C   
14422 O O   . SER D 258 ? 0.7952 0.7502 0.7614 -0.0069 0.0614  0.0093  258 SER D O   
14423 C CB  . SER D 258 ? 0.7788 0.7210 0.7437 0.0083  0.0602  0.0328  258 SER D CB  
14424 O OG  . SER D 258 ? 0.8971 0.8486 0.8584 0.0079  0.0492  0.0267  258 SER D OG  
14425 N N   . VAL D 259 ? 0.8793 0.8253 0.8555 -0.0087 0.0781  0.0148  259 VAL D N   
14426 C CA  . VAL D 259 ? 0.7046 0.6625 0.6851 -0.0150 0.0775  0.0053  259 VAL D CA  
14427 C C   . VAL D 259 ? 0.7416 0.7064 0.7264 -0.0122 0.0791  0.0100  259 VAL D C   
14428 O O   . VAL D 259 ? 0.7033 0.6607 0.6886 -0.0085 0.0851  0.0199  259 VAL D O   
14429 C CB  . VAL D 259 ? 0.6865 0.6379 0.6718 -0.0257 0.0882  -0.0035 259 VAL D CB  
14430 C CG1 . VAL D 259 ? 0.7331 0.6855 0.7124 -0.0300 0.0842  -0.0124 259 VAL D CG1 
14431 C CG2 . VAL D 259 ? 0.7203 0.6531 0.7102 -0.0261 0.1023  0.0035  259 VAL D CG2 
14432 N N   . SER D 260 ? 0.8065 0.7875 0.7945 -0.0138 0.0736  0.0031  260 SER D N   
14433 C CA  . SER D 260 ? 0.7410 0.7320 0.7337 -0.0127 0.0764  0.0048  260 SER D CA  
14434 C C   . SER D 260 ? 0.6838 0.6903 0.6845 -0.0197 0.0757  -0.0060 260 SER D C   
14435 O O   . SER D 260 ? 0.6805 0.6928 0.6813 -0.0229 0.0692  -0.0140 260 SER D O   
14436 C CB  . SER D 260 ? 0.6875 0.6858 0.6752 -0.0026 0.0672  0.0093  260 SER D CB  
14437 O OG  . SER D 260 ? 0.7349 0.7475 0.7244 -0.0004 0.0568  0.0014  260 SER D OG  
14438 N N   . ASN D 261 ? 0.7052 0.7204 0.7128 -0.0224 0.0824  -0.0057 261 ASN D N   
14439 C CA  . ASN D 261 ? 0.6957 0.7293 0.7132 -0.0287 0.0816  -0.0156 261 ASN D CA  
14440 C C   . ASN D 261 ? 0.7441 0.7942 0.7612 -0.0219 0.0675  -0.0208 261 ASN D C   
14441 O O   . ASN D 261 ? 0.7402 0.8027 0.7628 -0.0263 0.0620  -0.0294 261 ASN D O   
14442 C CB  . ASN D 261 ? 0.6821 0.7239 0.7071 -0.0316 0.0914  -0.0127 261 ASN D CB  
14443 C CG  . ASN D 261 ? 0.7912 0.8168 0.8196 -0.0397 0.1061  -0.0073 261 ASN D CG  
14444 O OD1 . ASN D 261 ? 0.8136 0.8318 0.8474 -0.0496 0.1110  -0.0136 261 ASN D OD1 
14445 N ND2 . ASN D 261 ? 0.8545 0.8747 0.8800 -0.0358 0.1133  0.0044  261 ASN D ND2 
14446 N N   . GLU D 262 ? 0.7179 0.7682 0.7291 -0.0110 0.0612  -0.0157 262 GLU D N   
14447 C CA  . GLU D 262 ? 0.7818 0.8442 0.7939 -0.0035 0.0483  -0.0200 262 GLU D CA  
14448 C C   . GLU D 262 ? 0.7377 0.7933 0.7444 -0.0032 0.0394  -0.0207 262 GLU D C   
14449 O O   . GLU D 262 ? 0.7231 0.7914 0.7339 -0.0021 0.0303  -0.0259 262 GLU D O   
14450 C CB  . GLU D 262 ? 0.7759 0.8377 0.7829 0.0072  0.0447  -0.0156 262 GLU D CB  
14451 C CG  . GLU D 262 ? 0.8395 0.9062 0.8475 0.0069  0.0547  -0.0128 262 GLU D CG  
14452 C CD  . GLU D 262 ? 1.0079 1.0582 1.0064 0.0072  0.0610  -0.0024 262 GLU D CD  
14453 O OE1 . GLU D 262 ? 0.9669 1.0091 0.9671 -0.0003 0.0711  0.0017  262 GLU D OE1 
14454 O OE2 . GLU D 262 ? 1.0086 1.0541 0.9990 0.0147  0.0557  0.0017  262 GLU D OE2 
14455 N N   . ALA D 263 ? 0.7111 0.7481 0.7089 -0.0038 0.0420  -0.0149 263 ALA D N   
14456 C CA  . ALA D 263 ? 0.7280 0.7591 0.7195 -0.0039 0.0348  -0.0149 263 ALA D CA  
14457 C C   . ALA D 263 ? 0.7347 0.7739 0.7293 -0.0136 0.0355  -0.0233 263 ALA D C   
14458 O O   . ALA D 263 ? 0.7199 0.7680 0.7130 -0.0129 0.0257  -0.0262 263 ALA D O   
14459 C CB  . ALA D 263 ? 0.6787 0.6901 0.6618 -0.0030 0.0394  -0.0073 263 ALA D CB  
14460 N N   . LEU D 264 ? 0.6619 0.6987 0.6613 -0.0229 0.0468  -0.0273 264 LEU D N   
14461 C CA  . LEU D 264 ? 0.7184 0.7642 0.7217 -0.0338 0.0478  -0.0374 264 LEU D CA  
14462 C C   . LEU D 264 ? 0.7108 0.7818 0.7221 -0.0330 0.0377  -0.0432 264 LEU D C   
14463 O O   . LEU D 264 ? 0.7465 0.8286 0.7566 -0.0370 0.0304  -0.0489 264 LEU D O   
14464 C CB  . LEU D 264 ? 0.7207 0.7593 0.7307 -0.0441 0.0624  -0.0408 264 LEU D CB  
14465 C CG  . LEU D 264 ? 0.6844 0.6978 0.6891 -0.0455 0.0735  -0.0355 264 LEU D CG  
14466 C CD1 . LEU D 264 ? 0.6933 0.6994 0.7046 -0.0585 0.0858  -0.0431 264 LEU D CD1 
14467 C CD2 . LEU D 264 ? 0.6882 0.6916 0.6812 -0.0413 0.0683  -0.0332 264 LEU D CD2 
14468 N N   . GLU D 265 ? 0.7769 0.8587 0.7966 -0.0273 0.0372  -0.0416 265 GLU D N   
14469 C CA  . GLU D 265 ? 0.7168 0.8235 0.7467 -0.0247 0.0281  -0.0466 265 GLU D CA  
14470 C C   . GLU D 265 ? 0.7526 0.8626 0.7776 -0.0149 0.0139  -0.0431 265 GLU D C   
14471 O O   . GLU D 265 ? 0.8247 0.9542 0.8563 -0.0144 0.0046  -0.0468 265 GLU D O   
14472 C CB  . GLU D 265 ? 0.7702 0.8870 0.8100 -0.0200 0.0324  -0.0459 265 GLU D CB  
14473 C CG  . GLU D 265 ? 0.7751 0.8887 0.8201 -0.0295 0.0472  -0.0469 265 GLU D CG  
14474 C CD  . GLU D 265 ? 0.7495 0.8687 0.7989 -0.0236 0.0528  -0.0433 265 GLU D CD  
14475 O OE1 . GLU D 265 ? 0.7049 0.8298 0.7533 -0.0120 0.0455  -0.0417 265 GLU D OE1 
14476 O OE2 . GLU D 265 ? 0.6571 0.7747 0.7109 -0.0307 0.0652  -0.0421 265 GLU D OE2 
14477 N N   . LEU D 266 ? 0.7089 0.8006 0.7233 -0.0073 0.0119  -0.0353 266 LEU D N   
14478 C CA  . LEU D 266 ? 0.7513 0.8435 0.7616 0.0013  -0.0009 -0.0308 266 LEU D CA  
14479 C C   . LEU D 266 ? 0.7498 0.8438 0.7527 -0.0048 -0.0059 -0.0317 266 LEU D C   
14480 O O   . LEU D 266 ? 0.7237 0.8307 0.7282 -0.0012 -0.0172 -0.0308 266 LEU D O   
14481 C CB  . LEU D 266 ? 0.7202 0.7929 0.7225 0.0095  -0.0013 -0.0226 266 LEU D CB  
14482 C CG  . LEU D 266 ? 0.7501 0.8191 0.7482 0.0173  -0.0133 -0.0168 266 LEU D CG  
14483 C CD1 . LEU D 266 ? 0.7463 0.8305 0.7554 0.0260  -0.0230 -0.0181 266 LEU D CD1 
14484 C CD2 . LEU D 266 ? 0.6578 0.7067 0.6478 0.0221  -0.0123 -0.0095 266 LEU D CD2 
14485 N N   . TYR D 267 ? 0.7170 0.7985 0.7117 -0.0138 0.0028  -0.0336 267 TYR D N   
14486 C CA  . TYR D 267 ? 0.7141 0.7974 0.6996 -0.0205 -0.0003 -0.0361 267 TYR D CA  
14487 C C   . TYR D 267 ? 0.7438 0.8512 0.7360 -0.0283 -0.0048 -0.0454 267 TYR D C   
14488 O O   . TYR D 267 ? 0.7667 0.8864 0.7537 -0.0289 -0.0146 -0.0453 267 TYR D O   
14489 C CB  . TYR D 267 ? 0.7103 0.7743 0.6873 -0.0279 0.0118  -0.0377 267 TYR D CB  
14490 C CG  . TYR D 267 ? 0.7804 0.8237 0.7494 -0.0208 0.0140  -0.0278 267 TYR D CG  
14491 C CD1 . TYR D 267 ? 0.8153 0.8554 0.7745 -0.0169 0.0066  -0.0217 267 TYR D CD1 
14492 C CD2 . TYR D 267 ? 0.7412 0.7699 0.7129 -0.0185 0.0234  -0.0238 267 TYR D CD2 
14493 C CE1 . TYR D 267 ? 0.7716 0.7945 0.7253 -0.0113 0.0086  -0.0128 267 TYR D CE1 
14494 C CE2 . TYR D 267 ? 0.7137 0.7264 0.6793 -0.0124 0.0246  -0.0148 267 TYR D CE2 
14495 C CZ  . TYR D 267 ? 0.7395 0.7495 0.6969 -0.0090 0.0173  -0.0097 267 TYR D CZ  
14496 O OH  . TYR D 267 ? 0.8143 0.8100 0.7675 -0.0038 0.0186  -0.0008 267 TYR D OH  
14497 N N   . TYR D 268 ? 0.7797 0.8957 0.7834 -0.0348 0.0022  -0.0528 268 TYR D N   
14498 C CA  . TYR D 268 ? 0.7549 0.8971 0.7679 -0.0424 -0.0027 -0.0618 268 TYR D CA  
14499 C C   . TYR D 268 ? 0.7329 0.8965 0.7536 -0.0321 -0.0170 -0.0575 268 TYR D C   
14500 O O   . TYR D 268 ? 0.8315 1.0159 0.8530 -0.0351 -0.0268 -0.0602 268 TYR D O   
14501 C CB  . TYR D 268 ? 0.7467 0.8935 0.7730 -0.0509 0.0083  -0.0691 268 TYR D CB  
14502 C CG  . TYR D 268 ? 0.8386 1.0166 0.8810 -0.0550 0.0027  -0.0762 268 TYR D CG  
14503 C CD1 . TYR D 268 ? 0.8424 1.0364 0.8870 -0.0687 0.0012  -0.0869 268 TYR D CD1 
14504 C CD2 . TYR D 268 ? 0.7540 0.9464 0.8101 -0.0456 -0.0005 -0.0730 268 TYR D CD2 
14505 C CE1 . TYR D 268 ? 0.7405 0.9655 0.8014 -0.0729 -0.0043 -0.0932 268 TYR D CE1 
14506 C CE2 . TYR D 268 ? 0.7864 1.0090 0.8592 -0.0488 -0.0051 -0.0790 268 TYR D CE2 
14507 C CZ  . TYR D 268 ? 0.6886 0.9282 0.7644 -0.0626 -0.0074 -0.0886 268 TYR D CZ  
14508 O OH  . TYR D 268 ? 0.7171 0.9897 0.8113 -0.0663 -0.0126 -0.0945 268 TYR D OH  
14509 N N   . GLU D 269 ? 0.7676 0.9264 0.7939 -0.0197 -0.0185 -0.0506 269 GLU D N   
14510 C CA  . GLU D 269 ? 0.8324 1.0089 0.8685 -0.0084 -0.0309 -0.0466 269 GLU D CA  
14511 C C   . GLU D 269 ? 0.7438 0.9183 0.7695 -0.0030 -0.0427 -0.0387 269 GLU D C   
14512 O O   . GLU D 269 ? 0.6580 0.8520 0.6909 0.0028  -0.0545 -0.0359 269 GLU D O   
14513 C CB  . GLU D 269 ? 0.7664 0.9349 0.8094 0.0033  -0.0283 -0.0427 269 GLU D CB  
14514 C CG  . GLU D 269 ? 0.8222 1.0041 0.8801 0.0009  -0.0201 -0.0494 269 GLU D CG  
14515 C CD  . GLU D 269 ? 0.9046 1.0800 0.9670 0.0126  -0.0174 -0.0466 269 GLU D CD  
14516 O OE1 . GLU D 269 ? 0.6901 0.8427 0.7411 0.0176  -0.0159 -0.0409 269 GLU D OE1 
14517 O OE2 . GLU D 269 ? 1.0281 1.2224 1.1058 0.0165  -0.0166 -0.0507 269 GLU D OE2 
14518 N N   . LYS D 270 ? 0.6701 0.8222 0.6796 -0.0045 -0.0395 -0.0341 270 LYS D N   
14519 C CA  . LYS D 270 ? 0.6778 0.8263 0.6764 -0.0001 -0.0492 -0.0253 270 LYS D CA  
14520 C C   . LYS D 270 ? 0.7528 0.9109 0.7396 -0.0113 -0.0509 -0.0294 270 LYS D C   
14521 O O   . LYS D 270 ? 0.8673 1.0203 0.8411 -0.0100 -0.0560 -0.0222 270 LYS D O   
14522 C CB  . LYS D 270 ? 0.6968 0.8174 0.6856 0.0053  -0.0451 -0.0173 270 LYS D CB  
14523 C CG  . LYS D 270 ? 0.7870 0.8990 0.7855 0.0163  -0.0448 -0.0140 270 LYS D CG  
14524 C CD  . LYS D 270 ? 0.7904 0.9047 0.7934 0.0280  -0.0572 -0.0054 270 LYS D CD  
14525 C CE  . LYS D 270 ? 0.7872 0.9032 0.8048 0.0384  -0.0582 -0.0069 270 LYS D CE  
14526 N NZ  . LYS D 270 ? 0.7216 0.8600 0.7527 0.0362  -0.0558 -0.0159 270 LYS D NZ  
14527 N N   . GLY D 271 ? 0.6720 0.8443 0.6631 -0.0228 -0.0463 -0.0411 271 GLY D N   
14528 C CA  . GLY D 271 ? 0.7088 0.8954 0.6901 -0.0342 -0.0493 -0.0477 271 GLY D CA  
14529 C C   . GLY D 271 ? 0.7862 0.9549 0.7537 -0.0456 -0.0372 -0.0550 271 GLY D C   
14530 O O   . GLY D 271 ? 0.8596 1.0393 0.8173 -0.0559 -0.0386 -0.0626 271 GLY D O   
14531 N N   . ILE D 272 ? 0.7545 0.8971 0.7211 -0.0438 -0.0253 -0.0534 272 ILE D N   
14532 C CA  . ILE D 272 ? 0.8313 0.9552 0.7866 -0.0528 -0.0130 -0.0594 272 ILE D CA  
14533 C C   . ILE D 272 ? 0.8246 0.9536 0.7874 -0.0665 -0.0039 -0.0742 272 ILE D C   
14534 O O   . ILE D 272 ? 0.8889 1.0217 0.8667 -0.0668 -0.0003 -0.0765 272 ILE D O   
14535 C CB  . ILE D 272 ? 0.8193 0.9152 0.7730 -0.0455 -0.0040 -0.0511 272 ILE D CB  
14536 C CG1 . ILE D 272 ? 0.7689 0.8606 0.7183 -0.0327 -0.0137 -0.0370 272 ILE D CG1 
14537 C CG2 . ILE D 272 ? 0.7826 0.8597 0.7257 -0.0529 0.0083  -0.0558 272 ILE D CG2 
14538 C CD1 . ILE D 272 ? 0.7229 0.8241 0.6593 -0.0329 -0.0231 -0.0330 272 ILE D CD1 
14539 N N   . ASN D 273 ? 0.8427 0.9723 0.7950 -0.0782 0.0001  -0.0847 273 ASN D N   
14540 C CA  . ASN D 273 ? 0.9014 1.0324 0.8604 -0.0929 0.0098  -0.1002 273 ASN D CA  
14541 C C   . ASN D 273 ? 0.8345 0.9350 0.7914 -0.0970 0.0272  -0.1037 273 ASN D C   
14542 O O   . ASN D 273 ? 0.8002 0.8953 0.7675 -0.1066 0.0375  -0.1130 273 ASN D O   
14543 C CB  . ASN D 273 ? 0.9518 1.1042 0.9019 -0.1053 0.0037  -0.1129 273 ASN D CB  
14544 C CG  . ASN D 273 ? 0.9328 1.1146 0.8804 -0.0995 -0.0147 -0.1063 273 ASN D CG  
14545 O OD1 . ASN D 273 ? 1.1074 1.3014 1.0682 -0.0903 -0.0228 -0.0979 273 ASN D OD1 
14546 N ND2 . ASN D 273 ? 0.8296 1.0236 0.7604 -0.1045 -0.0212 -0.1097 273 ASN D ND2 
14547 N N   . MET D 274 ? 0.8798 0.9606 0.8248 -0.0899 0.0309  -0.0958 274 MET D N   
14548 C CA  . MET D 274 ? 0.9295 0.9826 0.8731 -0.0928 0.0473  -0.0986 274 MET D CA  
14549 C C   . MET D 274 ? 0.8329 0.8673 0.7732 -0.0794 0.0493  -0.0830 274 MET D C   
14550 O O   . MET D 274 ? 0.7824 0.8227 0.7148 -0.0707 0.0389  -0.0731 274 MET D O   
14551 C CB  . MET D 274 ? 0.8654 0.9151 0.7958 -0.1033 0.0530  -0.1118 274 MET D CB  
14552 C CG  . MET D 274 ? 0.9049 0.9263 0.8389 -0.1076 0.0716  -0.1174 274 MET D CG  
14553 S SD  . MET D 274 ? 0.9095 0.9068 0.8336 -0.0964 0.0793  -0.1061 274 MET D SD  
14554 C CE  . MET D 274 ? 0.9346 0.9526 0.8385 -0.0948 0.0654  -0.1045 274 MET D CE  
14555 N N   . LEU D 275 ? 0.7810 0.7931 0.7283 -0.0781 0.0626  -0.0804 275 LEU D N   
14556 C CA  . LEU D 275 ? 0.8137 0.8078 0.7589 -0.0669 0.0662  -0.0668 275 LEU D CA  
14557 C C   . LEU D 275 ? 0.8032 0.7737 0.7536 -0.0701 0.0834  -0.0693 275 LEU D C   
14558 O O   . LEU D 275 ? 0.8076 0.7743 0.7649 -0.0803 0.0922  -0.0804 275 LEU D O   
14559 C CB  . LEU D 275 ? 0.7639 0.7619 0.7166 -0.0563 0.0591  -0.0543 275 LEU D CB  
14560 C CG  . LEU D 275 ? 0.8373 0.8336 0.8039 -0.0585 0.0658  -0.0551 275 LEU D CG  
14561 C CD1 . LEU D 275 ? 0.8541 0.8307 0.8243 -0.0514 0.0749  -0.0441 275 LEU D CD1 
14562 C CD2 . LEU D 275 ? 0.8203 0.8374 0.7939 -0.0552 0.0548  -0.0537 275 LEU D CD2 
14563 N N   . ALA D 276 ? 0.7831 0.7376 0.7317 -0.0612 0.0882  -0.0584 276 ALA D N   
14564 C CA  . ALA D 276 ? 0.8756 0.8073 0.8300 -0.0619 0.1044  -0.0584 276 ALA D CA  
14565 C C   . ALA D 276 ? 0.8372 0.7585 0.7975 -0.0503 0.1061  -0.0416 276 ALA D C   
14566 O O   . ALA D 276 ? 0.8195 0.7485 0.7757 -0.0418 0.0955  -0.0314 276 ALA D O   
14567 C CB  . ALA D 276 ? 0.8127 0.7359 0.7577 -0.0645 0.1113  -0.0653 276 ALA D CB  
14568 N N   . THR D 277 ? 0.8181 0.7220 0.7884 -0.0502 0.1195  -0.0387 277 THR D N   
14569 C CA  . THR D 277 ? 0.8228 0.7183 0.7988 -0.0397 0.1216  -0.0224 277 THR D CA  
14570 C C   . THR D 277 ? 0.8810 0.7543 0.8654 -0.0391 0.1381  -0.0200 277 THR D C   
14571 O O   . THR D 277 ? 0.8343 0.6973 0.8204 -0.0470 0.1483  -0.0322 277 THR D O   
14572 C CB  . THR D 277 ? 0.8616 0.7662 0.8436 -0.0382 0.1168  -0.0165 277 THR D CB  
14573 O OG1 . THR D 277 ? 0.9226 0.8180 0.9099 -0.0296 0.1214  -0.0016 277 THR D OG1 
14574 C CG2 . THR D 277 ? 0.8169 0.7219 0.8067 -0.0493 0.1237  -0.0270 277 THR D CG2 
14575 N N   . ASP D 278 ? 0.8522 0.7185 0.8423 -0.0295 0.1407  -0.0043 278 ASP D N   
14576 C CA  . ASP D 278 ? 0.8914 0.7373 0.8912 -0.0263 0.1556  0.0015  278 ASP D CA  
14577 C C   . ASP D 278 ? 0.9015 0.7360 0.9128 -0.0330 0.1671  -0.0008 278 ASP D C   
14578 O O   . ASP D 278 ? 0.9315 0.7755 0.9444 -0.0365 0.1629  0.0001  278 ASP D O   
14579 C CB  . ASP D 278 ? 0.8978 0.7434 0.9005 -0.0138 0.1532  0.0204  278 ASP D CB  
14580 C CG  . ASP D 278 ? 0.9622 0.7900 0.9741 -0.0080 0.1665  0.0267  278 ASP D CG  
14581 O OD1 . ASP D 278 ? 0.9610 0.7787 0.9731 -0.0120 0.1753  0.0153  278 ASP D OD1 
14582 O OD2 . ASP D 278 ? 1.0333 0.8584 1.0524 0.0008  0.1682  0.0430  278 ASP D OD2 
14583 N N   . GLU D 279 ? 0.9568 0.8270 0.8345 -0.0425 0.0591  0.0667  279 GLU D N   
14584 C CA  . GLU D 279 ? 0.9420 0.8003 0.8143 -0.0503 0.0622  0.0700  279 GLU D CA  
14585 C C   . GLU D 279 ? 1.0121 0.8693 0.8820 -0.0470 0.0606  0.0807  279 GLU D C   
14586 O O   . GLU D 279 ? 1.0772 0.9270 0.9413 -0.0544 0.0640  0.0854  279 GLU D O   
14587 C CB  . GLU D 279 ? 0.9230 0.7568 0.7940 -0.0518 0.0682  0.0671  279 GLU D CB  
14588 C CG  . GLU D 279 ? 0.9202 0.7416 0.7967 -0.0395 0.0692  0.0716  279 GLU D CG  
14589 C CD  . GLU D 279 ? 0.9362 0.7296 0.8110 -0.0399 0.0769  0.0690  279 GLU D CD  
14590 O OE1 . GLU D 279 ? 0.9382 0.7156 0.8064 -0.0499 0.0814  0.0687  279 GLU D OE1 
14591 O OE2 . GLU D 279 ? 0.9595 0.7467 0.8403 -0.0306 0.0795  0.0666  279 GLU D OE2 
14592 N N   . VAL D 280 ? 0.9706 0.8359 0.8443 -0.0371 0.0558  0.0845  280 VAL D N   
14593 C CA  . VAL D 280 ? 0.9375 0.8070 0.8058 -0.0342 0.0529  0.0940  280 VAL D CA  
14594 C C   . VAL D 280 ? 1.0014 0.8865 0.8634 -0.0414 0.0528  0.0932  280 VAL D C   
14595 O O   . VAL D 280 ? 1.0902 0.9745 0.9434 -0.0441 0.0542  0.1011  280 VAL D O   
14596 C CB  . VAL D 280 ? 0.8896 0.7701 0.7639 -0.0236 0.0463  0.0955  280 VAL D CB  
14597 C CG1 . VAL D 280 ? 0.9114 0.8000 0.7772 -0.0208 0.0419  0.1045  280 VAL D CG1 
14598 C CG2 . VAL D 280 ? 1.0065 0.8746 0.8896 -0.0157 0.0475  0.0970  280 VAL D CG2 
14599 N N   . ILE D 281 ? 0.9374 0.8368 0.8034 -0.0436 0.0520  0.0844  281 ILE D N   
14600 C CA  . ILE D 281 ? 0.9461 0.8622 0.8088 -0.0488 0.0530  0.0827  281 ILE D CA  
14601 C C   . ILE D 281 ? 1.0331 0.9450 0.8928 -0.0601 0.0587  0.0846  281 ILE D C   
14602 O O   . ILE D 281 ? 1.0259 0.9450 0.8802 -0.0652 0.0617  0.0892  281 ILE D O   
14603 C CB  . ILE D 281 ? 0.9290 0.8595 0.7979 -0.0463 0.0514  0.0740  281 ILE D CB  
14604 C CG1 . ILE D 281 ? 0.9433 0.8783 0.8147 -0.0378 0.0474  0.0714  281 ILE D CG1 
14605 C CG2 . ILE D 281 ? 0.9063 0.8547 0.7748 -0.0508 0.0536  0.0718  281 ILE D CG2 
14606 C CD1 . ILE D 281 ? 0.9580 0.8826 0.8343 -0.0326 0.0449  0.0722  281 ILE D CD1 
14607 N N   . LEU D 282 ? 1.0161 0.9164 0.8791 -0.0654 0.0610  0.0804  282 LEU D N   
14608 C CA  . LEU D 282 ? 0.9753 0.8702 0.8369 -0.0789 0.0667  0.0800  282 LEU D CA  
14609 C C   . LEU D 282 ? 1.0410 0.9169 0.8948 -0.0820 0.0716  0.0912  282 LEU D C   
14610 O O   . LEU D 282 ? 0.9989 0.8790 0.8497 -0.0924 0.0768  0.0948  282 LEU D O   
14611 C CB  . LEU D 282 ? 0.9523 0.8353 0.8166 -0.0837 0.0679  0.0716  282 LEU D CB  
14612 C CG  . LEU D 282 ? 0.9392 0.8153 0.8031 -0.1002 0.0736  0.0677  282 LEU D CG  
14613 C CD1 . LEU D 282 ? 0.8328 0.7389 0.7018 -0.1095 0.0732  0.0645  282 LEU D CD1 
14614 C CD2 . LEU D 282 ? 0.8468 0.7112 0.7108 -0.1032 0.0739  0.0572  282 LEU D CD2 
14615 N N   . LYS D 283 ? 1.0649 0.9209 0.9157 -0.0724 0.0705  0.0978  283 LYS D N   
14616 C CA  . LYS D 283 ? 1.1076 0.9444 0.9494 -0.0720 0.0747  0.1113  283 LYS D CA  
14617 C C   . LYS D 283 ? 1.0626 0.9168 0.8958 -0.0701 0.0731  0.1197  283 LYS D C   
14618 O O   . LYS D 283 ? 1.0065 0.8500 0.8296 -0.0746 0.0786  0.1311  283 LYS D O   
14619 C CB  . LYS D 283 ? 1.1132 0.9291 0.9558 -0.0589 0.0729  0.1169  283 LYS D CB  
14620 C CG  . LYS D 283 ? 1.1002 0.9263 0.9407 -0.0440 0.0652  0.1256  283 LYS D CG  
14621 C CD  . LYS D 283 ? 1.2251 1.0403 1.0523 -0.0415 0.0673  0.1427  283 LYS D CD  
14622 C CE  . LYS D 283 ? 1.1868 1.0192 1.0100 -0.0280 0.0577  0.1501  283 LYS D CE  
14623 N NZ  . LYS D 283 ? 1.1328 0.9598 0.9386 -0.0260 0.0591  0.1674  283 LYS D NZ  
14624 N N   . ASN D 284 ? 1.0832 0.9622 0.9189 -0.0637 0.0665  0.1141  284 ASN D N   
14625 C CA  . ASN D 284 ? 0.9960 0.8939 0.8227 -0.0629 0.0658  0.1179  284 ASN D CA  
14626 C C   . ASN D 284 ? 0.9871 0.9028 0.8158 -0.0741 0.0716  0.1128  284 ASN D C   
14627 O O   . ASN D 284 ? 0.9386 0.8660 0.7581 -0.0763 0.0751  0.1178  284 ASN D O   
14628 C CB  . ASN D 284 ? 0.9819 0.8965 0.8108 -0.0522 0.0574  0.1119  284 ASN D CB  
14629 C CG  . ASN D 284 ? 1.0714 0.9764 0.9006 -0.0414 0.0510  0.1170  284 ASN D CG  
14630 O OD1 . ASN D 284 ? 1.1586 1.0441 0.9849 -0.0394 0.0528  0.1268  284 ASN D OD1 
14631 N ND2 . ASN D 284 ? 1.0266 0.9456 0.8604 -0.0342 0.0438  0.1103  284 ASN D ND2 
14632 N N   . SER D 285 ? 0.9727 0.8932 0.8133 -0.0807 0.0729  0.1030  285 SER D N   
14633 C CA  . SER D 285 ? 0.9305 0.8745 0.7773 -0.0895 0.0769  0.0971  285 SER D CA  
14634 C C   . SER D 285 ? 0.9596 0.8977 0.8089 -0.1061 0.0850  0.0987  285 SER D C   
14635 O O   . SER D 285 ? 1.0429 1.0026 0.8967 -0.1150 0.0902  0.0970  285 SER D O   
14636 C CB  . SER D 285 ? 0.8818 0.8416 0.7406 -0.0849 0.0717  0.0853  285 SER D CB  
14637 O OG  . SER D 285 ? 0.8806 0.8430 0.7379 -0.0716 0.0659  0.0833  285 SER D OG  
14638 N N   . VAL D 286 ? 1.0245 0.9345 0.8726 -0.1110 0.0869  0.1006  286 VAL D N   
14639 C CA  . VAL D 286 ? 0.9989 0.8961 0.8482 -0.1287 0.0957  0.1016  286 VAL D CA  
14640 C C   . VAL D 286 ? 1.0902 0.9480 0.9285 -0.1268 0.1000  0.1131  286 VAL D C   
14641 O O   . VAL D 286 ? 1.1134 0.9572 0.9478 -0.1121 0.0945  0.1166  286 VAL D O   
14642 C CB  . VAL D 286 ? 0.8433 0.7465 0.7047 -0.1391 0.0944  0.0872  286 VAL D CB  
14643 C CG1 . VAL D 286 ? 0.9054 0.8097 0.7715 -0.1608 0.1034  0.0854  286 VAL D CG1 
14644 C CG2 . VAL D 286 ? 0.7763 0.7146 0.6476 -0.1325 0.0866  0.0774  286 VAL D CG2 
14645 N N   . GLU D 287 ? 1.1739 1.0138 1.0083 -0.1417 0.1106  0.1196  287 GLU D N   
14646 C CA  . GLU D 287 ? 1.1544 0.9541 0.9767 -0.1391 0.1166  0.1340  287 GLU D CA  
14647 C C   . GLU D 287 ? 1.2754 1.0464 1.0997 -0.1299 0.1135  0.1300  287 GLU D C   
14648 O O   . GLU D 287 ? 1.4192 1.1887 1.2411 -0.1113 0.1060  0.1344  287 GLU D O   
14649 C CB  . GLU D 287 ? 1.0988 0.8799 0.9185 -0.1598 0.1305  0.1394  287 GLU D CB  
14650 C CG  . GLU D 287 ? 1.2733 1.0138 1.0768 -0.1555 0.1385  0.1598  287 GLU D CG  
14651 C CD  . GLU D 287 ? 1.3669 1.0995 1.1635 -0.1741 0.1529  0.1709  287 GLU D CD  
14652 O OE1 . GLU D 287 ? 1.2990 1.0501 1.1074 -0.1946 0.1585  0.1596  287 GLU D OE1 
14653 O OE2 . GLU D 287 ? 1.2312 0.9411 1.0106 -0.1680 0.1587  0.1914  287 GLU D OE2 
14654 N N   . ARG D 288 ? 1.1706 0.9196 0.9998 -0.1430 0.1198  0.1210  288 ARG D N   
14655 C CA  . ARG D 288 ? 1.1468 0.8682 0.9776 -0.1350 0.1190  0.1149  288 ARG D CA  
14656 C C   . ARG D 288 ? 1.0492 0.7841 0.8897 -0.1447 0.1160  0.0938  288 ARG D C   
14657 O O   . ARG D 288 ? 1.0977 0.8062 0.9384 -0.1513 0.1211  0.0844  288 ARG D O   
14658 C CB  . ARG D 288 ? 1.1974 0.8698 1.0207 -0.1389 0.1307  0.1240  288 ARG D CB  
14659 C CG  . ARG D 288 ? 1.2358 0.8966 1.0566 -0.1624 0.1428  0.1268  288 ARG D CG  
14660 C CD  . ARG D 288 ? 1.2560 0.8637 1.0666 -0.1626 0.1554  0.1413  288 ARG D CD  
14661 N NE  . ARG D 288 ? 1.1297 0.7321 0.9327 -0.1769 0.1656  0.1554  288 ARG D NE  
14662 C CZ  . ARG D 288 ? 1.1744 0.7833 0.9654 -0.1660 0.1650  0.1761  288 ARG D CZ  
14663 N NH1 . ARG D 288 ? 1.1866 0.8082 0.9728 -0.1413 0.1536  0.1845  288 ARG D NH1 
14664 N NH2 . ARG D 288 ? 1.2794 0.8841 1.0628 -0.1813 0.1763  0.1881  288 ARG D NH2 
14665 N N   . ALA D 289 ? 1.0170 0.7931 0.8642 -0.1447 0.1078  0.0861  289 ALA D N   
14666 C CA  . ALA D 289 ? 0.9307 0.7249 0.7854 -0.1524 0.1036  0.0681  289 ALA D CA  
14667 C C   . ALA D 289 ? 0.9822 0.7643 0.8357 -0.1385 0.0993  0.0618  289 ALA D C   
14668 O O   . ALA D 289 ? 0.9941 0.7768 0.8465 -0.1204 0.0948  0.0694  289 ALA D O   
14669 C CB  . ALA D 289 ? 0.9144 0.7549 0.7766 -0.1521 0.0962  0.0646  289 ALA D CB  
14670 N N   . SER D 290 ? 0.9530 0.7252 0.8064 -0.1480 0.1013  0.0471  290 SER D N   
14671 C CA  . SER D 290 ? 1.0243 0.7851 0.8754 -0.1360 0.0994  0.0401  290 SER D CA  
14672 C C   . SER D 290 ? 0.9662 0.7626 0.8205 -0.1269 0.0894  0.0357  290 SER D C   
14673 O O   . SER D 290 ? 0.9450 0.7738 0.8036 -0.1326 0.0841  0.0338  290 SER D O   
14674 C CB  . SER D 290 ? 0.9783 0.7164 0.8254 -0.1496 0.1057  0.0242  290 SER D CB  
14675 O OG  . SER D 290 ? 1.0493 0.7530 0.8923 -0.1379 0.1115  0.0240  290 SER D OG  
14676 N N   . PRO D 291 ? 0.9031 0.6940 0.7563 -0.1120 0.0875  0.0348  291 PRO D N   
14677 C CA  . PRO D 291 ? 0.9023 0.7219 0.7570 -0.1043 0.0799  0.0310  291 PRO D CA  
14678 C C   . PRO D 291 ? 0.9028 0.7313 0.7523 -0.1130 0.0786  0.0159  291 PRO D C   
14679 O O   . PRO D 291 ? 1.0183 0.8729 0.8676 -0.1083 0.0721  0.0139  291 PRO D O   
14680 C CB  . PRO D 291 ? 0.9284 0.7366 0.7846 -0.0867 0.0803  0.0367  291 PRO D CB  
14681 C CG  . PRO D 291 ? 0.9684 0.7411 0.8222 -0.0868 0.0888  0.0359  291 PRO D CG  
14682 C CD  . PRO D 291 ? 0.8731 0.6337 0.7254 -0.0994 0.0926  0.0404  291 PRO D CD  
14683 N N   . TYR D 292 ? 0.9377 0.7450 0.7820 -0.1257 0.0847  0.0054  292 TYR D N   
14684 C CA  . TYR D 292 ? 0.9920 0.8054 0.8283 -0.1344 0.0838  -0.0111 292 TYR D CA  
14685 C C   . TYR D 292 ? 0.9852 0.8271 0.8235 -0.1519 0.0783  -0.0192 292 TYR D C   
14686 O O   . TYR D 292 ? 0.9833 0.8210 0.8161 -0.1679 0.0801  -0.0344 292 TYR D O   
14687 C CB  . TYR D 292 ? 0.9549 0.7291 0.7842 -0.1389 0.0939  -0.0208 292 TYR D CB  
14688 C CG  . TYR D 292 ? 0.9154 0.6623 0.7476 -0.1214 0.1000  -0.0102 292 TYR D CG  
14689 C CD1 . TYR D 292 ? 0.9427 0.6984 0.7758 -0.1042 0.0980  -0.0064 292 TYR D CD1 
14690 C CD2 . TYR D 292 ? 0.9908 0.7053 0.8259 -0.1217 0.1077  -0.0027 292 TYR D CD2 
14691 C CE1 . TYR D 292 ? 0.9503 0.6872 0.7894 -0.0884 0.1026  0.0029  292 TYR D CE1 
14692 C CE2 . TYR D 292 ? 0.9582 0.6524 0.7973 -0.1037 0.1118  0.0081  292 TYR D CE2 
14693 C CZ  . TYR D 292 ? 0.9097 0.6174 0.7520 -0.0874 0.1087  0.0102  292 TYR D CZ  
14694 O OH  . TYR D 292 ? 1.0241 0.7169 0.8735 -0.0700 0.1121  0.0203  292 TYR D OH  
14695 N N   . LEU D 293 ? 0.9927 0.8657 0.8397 -0.1492 0.0717  -0.0104 293 LEU D N   
14696 C CA  . LEU D 293 ? 0.9938 0.9014 0.8469 -0.1632 0.0660  -0.0164 293 LEU D CA  
14697 C C   . LEU D 293 ? 0.9623 0.9070 0.8195 -0.1496 0.0566  -0.0098 293 LEU D C   
14698 O O   . LEU D 293 ? 1.0049 0.9453 0.8621 -0.1324 0.0561  0.0009  293 LEU D O   
14699 C CB  . LEU D 293 ? 0.9621 0.8686 0.8252 -0.1764 0.0709  -0.0115 293 LEU D CB  
14700 C CG  . LEU D 293 ? 1.0041 0.8692 0.8645 -0.1889 0.0823  -0.0125 293 LEU D CG  
14701 C CD1 . LEU D 293 ? 1.0420 0.8743 0.8984 -0.1721 0.0876  0.0014  293 LEU D CD1 
14702 C CD2 . LEU D 293 ? 1.0520 0.9283 0.9224 -0.2064 0.0862  -0.0099 293 LEU D CD2 
14703 N N   . ARG D 294 ? 0.8863 0.8680 0.7482 -0.1576 0.0493  -0.0163 294 ARG D N   
14704 C CA  . ARG D 294 ? 0.9451 0.9624 0.8133 -0.1443 0.0413  -0.0086 294 ARG D CA  
14705 C C   . ARG D 294 ? 0.9494 0.9847 0.8330 -0.1480 0.0428  -0.0018 294 ARG D C   
14706 O O   . ARG D 294 ? 0.9214 0.9670 0.8130 -0.1663 0.0450  -0.0080 294 ARG D O   
14707 C CB  . ARG D 294 ? 1.0198 1.0723 0.8850 -0.1468 0.0316  -0.0173 294 ARG D CB  
14708 C CG  . ARG D 294 ? 0.9514 1.0361 0.8225 -0.1292 0.0242  -0.0073 294 ARG D CG  
14709 C CD  . ARG D 294 ? 1.0438 1.1756 0.9208 -0.1341 0.0139  -0.0134 294 ARG D CD  
14710 N NE  . ARG D 294 ? 1.1026 1.2387 0.9682 -0.1486 0.0099  -0.0284 294 ARG D NE  
14711 C CZ  . ARG D 294 ? 1.1037 1.2560 0.9554 -0.1410 0.0018  -0.0307 294 ARG D CZ  
14712 N NH1 . ARG D 294 ? 1.1073 1.2695 0.9553 -0.1190 -0.0023 -0.0175 294 ARG D NH1 
14713 N NH2 . ARG D 294 ? 1.0700 1.2278 0.9099 -0.1561 -0.0018 -0.0466 294 ARG D NH2 
14714 N N   . TYR D 295 ? 0.8844 0.9227 0.7716 -0.1316 0.0428  0.0100  295 TYR D N   
14715 C CA  . TYR D 295 ? 0.8534 0.9078 0.7528 -0.1325 0.0455  0.0167  295 TYR D CA  
14716 C C   . TYR D 295 ? 0.9052 0.9994 0.8138 -0.1208 0.0387  0.0192  295 TYR D C   
14717 O O   . TYR D 295 ? 0.8776 0.9725 0.7809 -0.1043 0.0342  0.0228  295 TYR D O   
14718 C CB  . TYR D 295 ? 0.9203 0.9459 0.8153 -0.1235 0.0517  0.0271  295 TYR D CB  
14719 C CG  . TYR D 295 ? 1.0041 0.9928 0.8922 -0.1340 0.0590  0.0270  295 TYR D CG  
14720 C CD1 . TYR D 295 ? 0.8825 0.8409 0.7606 -0.1295 0.0600  0.0250  295 TYR D CD1 
14721 C CD2 . TYR D 295 ? 0.9790 0.9627 0.8709 -0.1480 0.0660  0.0296  295 TYR D CD2 
14722 C CE1 . TYR D 295 ? 0.9155 0.8390 0.7884 -0.1365 0.0673  0.0255  295 TYR D CE1 
14723 C CE2 . TYR D 295 ? 0.9401 0.8867 0.8251 -0.1560 0.0735  0.0314  295 TYR D CE2 
14724 C CZ  . TYR D 295 ? 1.0155 0.9316 0.8914 -0.1494 0.0739  0.0292  295 TYR D CZ  
14725 O OH  . TYR D 295 ? 0.9802 0.8577 0.8500 -0.1551 0.0820  0.0316  295 TYR D OH  
14726 N N   . TYR D 296 ? 0.8252 0.9524 0.7486 -0.1293 0.0388  0.0175  296 TYR D N   
14727 C CA  . TYR D 296 ? 0.8090 0.9769 0.7450 -0.1171 0.0338  0.0204  296 TYR D CA  
14728 C C   . TYR D 296 ? 0.8294 0.9985 0.7724 -0.1112 0.0412  0.0279  296 TYR D C   
14729 O O   . TYR D 296 ? 0.9688 1.1439 0.9192 -0.1256 0.0479  0.0272  296 TYR D O   
14730 C CB  . TYR D 296 ? 0.9531 1.1653 0.9037 -0.1303 0.0283  0.0118  296 TYR D CB  
14731 C CG  . TYR D 296 ? 1.0085 1.2262 0.9509 -0.1372 0.0198  0.0023  296 TYR D CG  
14732 C CD1 . TYR D 296 ? 1.0263 1.2223 0.9614 -0.1584 0.0227  -0.0079 296 TYR D CD1 
14733 C CD2 . TYR D 296 ? 1.0111 1.2558 0.9518 -0.1225 0.0092  0.0035  296 TYR D CD2 
14734 C CE1 . TYR D 296 ? 1.0902 1.2918 1.0155 -0.1656 0.0153  -0.0189 296 TYR D CE1 
14735 C CE2 . TYR D 296 ? 1.0827 1.3350 1.0126 -0.1289 0.0010  -0.0054 296 TYR D CE2 
14736 C CZ  . TYR D 296 ? 1.0965 1.3282 1.0186 -0.1510 0.0040  -0.0177 296 TYR D CZ  
14737 O OH  . TYR D 296 ? 1.0985 1.3379 1.0078 -0.1579 -0.0037 -0.0286 296 TYR D OH  
14738 N N   . PHE D 297 ? 0.7814 0.9448 0.7212 -0.0910 0.0409  0.0346  297 PHE D N   
14739 C CA  . PHE D 297 ? 0.8039 0.9663 0.7468 -0.0842 0.0479  0.0400  297 PHE D CA  
14740 C C   . PHE D 297 ? 0.6871 0.8946 0.6485 -0.0805 0.0482  0.0390  297 PHE D C   
14741 O O   . PHE D 297 ? 0.7297 0.9563 0.6970 -0.0640 0.0434  0.0403  297 PHE D O   
14742 C CB  . PHE D 297 ? 0.7526 0.8898 0.6850 -0.0661 0.0478  0.0450  297 PHE D CB  
14743 C CG  . PHE D 297 ? 0.7138 0.8471 0.6458 -0.0597 0.0546  0.0484  297 PHE D CG  
14744 C CD1 . PHE D 297 ? 0.7867 0.8957 0.7088 -0.0673 0.0598  0.0511  297 PHE D CD1 
14745 C CD2 . PHE D 297 ? 0.7849 0.9384 0.7250 -0.0450 0.0560  0.0488  297 PHE D CD2 
14746 C CE1 . PHE D 297 ? 0.7591 0.8667 0.6777 -0.0618 0.0654  0.0535  297 PHE D CE1 
14747 C CE2 . PHE D 297 ? 0.8210 0.9705 0.7585 -0.0397 0.0629  0.0497  297 PHE D CE2 
14748 C CZ  . PHE D 297 ? 0.7953 0.9231 0.7211 -0.0488 0.0673  0.0516  297 PHE D CZ  
14749 N N   . ARG D 298 ? 0.6564 0.8813 0.6279 -0.0956 0.0548  0.0373  298 ARG D N   
14750 C CA  . ARG D 298 ? 0.7121 0.9839 0.7044 -0.0942 0.0571  0.0358  298 ARG D CA  
14751 C C   . ARG D 298 ? 0.7993 1.1106 0.8060 -0.0907 0.0467  0.0314  298 ARG D C   
14752 O O   . ARG D 298 ? 0.7612 1.1119 0.7854 -0.0790 0.0460  0.0319  298 ARG D O   
14753 C CB  . ARG D 298 ? 0.6479 0.9225 0.6410 -0.0743 0.0626  0.0401  298 ARG D CB  
14754 C CG  . ARG D 298 ? 0.7059 0.9434 0.6817 -0.0747 0.0704  0.0441  298 ARG D CG  
14755 C CD  . ARG D 298 ? 0.6492 0.8915 0.6251 -0.0568 0.0761  0.0453  298 ARG D CD  
14756 N NE  . ARG D 298 ? 0.7147 0.9243 0.6719 -0.0579 0.0818  0.0481  298 ARG D NE  
14757 C CZ  . ARG D 298 ? 0.7419 0.9414 0.6914 -0.0434 0.0853  0.0475  298 ARG D CZ  
14758 N NH1 . ARG D 298 ? 0.7477 0.9621 0.7065 -0.0257 0.0852  0.0447  298 ARG D NH1 
14759 N NH2 . ARG D 298 ? 0.7608 0.9346 0.6927 -0.0466 0.0889  0.0496  298 ARG D NH2 
14760 N N   . GLU D 299 ? 0.8215 1.1238 0.8206 -0.0995 0.0386  0.0270  299 GLU D N   
14761 C CA  . GLU D 299 ? 0.7450 1.0817 0.7517 -0.0971 0.0267  0.0226  299 GLU D CA  
14762 C C   . GLU D 299 ? 0.8157 1.1613 0.8211 -0.0690 0.0202  0.0296  299 GLU D C   
14763 O O   . GLU D 299 ? 0.8552 1.2392 0.8700 -0.0625 0.0103  0.0287  299 GLU D O   
14764 C CB  . GLU D 299 ? 0.7933 1.1841 0.8254 -0.1112 0.0256  0.0160  299 GLU D CB  
14765 C CG  . GLU D 299 ? 1.0316 1.4274 1.0643 -0.1389 0.0221  0.0049  299 GLU D CG  
14766 C CD  . GLU D 299 ? 1.1982 1.6332 1.2554 -0.1603 0.0276  -0.0014 299 GLU D CD  
14767 O OE1 . GLU D 299 ? 1.1520 1.6286 1.2303 -0.1504 0.0297  0.0017  299 GLU D OE1 
14768 O OE2 . GLU D 299 ? 1.3170 1.7402 1.3730 -0.1873 0.0312  -0.0097 299 GLU D OE2 
14769 N N   . LEU D 300 ? 0.7532 1.0641 0.7466 -0.0526 0.0253  0.0367  300 LEU D N   
14770 C CA  . LEU D 300 ? 0.7497 1.0606 0.7406 -0.0264 0.0217  0.0440  300 LEU D CA  
14771 C C   . LEU D 300 ? 0.7813 1.0544 0.7502 -0.0206 0.0178  0.0474  300 LEU D C   
14772 O O   . LEU D 300 ? 0.7062 0.9871 0.6714 -0.0048 0.0112  0.0528  300 LEU D O   
14773 C CB  . LEU D 300 ? 0.7611 1.0614 0.7557 -0.0121 0.0315  0.0480  300 LEU D CB  
14774 C CG  . LEU D 300 ? 0.7883 1.1231 0.8028 -0.0174 0.0386  0.0448  300 LEU D CG  
14775 C CD1 . LEU D 300 ? 0.7269 1.0364 0.7352 -0.0153 0.0507  0.0454  300 LEU D CD1 
14776 C CD2 . LEU D 300 ? 0.7238 1.1064 0.7598 0.0000  0.0351  0.0467  300 LEU D CD2 
14777 N N   . ILE D 301 ? 0.8434 1.0767 0.7980 -0.0322 0.0223  0.0454  301 ILE D N   
14778 C CA  . ILE D 301 ? 0.7938 0.9921 0.7295 -0.0279 0.0206  0.0479  301 ILE D CA  
14779 C C   . ILE D 301 ? 0.8493 1.0253 0.7755 -0.0481 0.0220  0.0413  301 ILE D C   
14780 O O   . ILE D 301 ? 0.8129 0.9845 0.7437 -0.0624 0.0273  0.0378  301 ILE D O   
14781 C CB  . ILE D 301 ? 0.7871 0.9529 0.7162 -0.0135 0.0270  0.0540  301 ILE D CB  
14782 C CG1 . ILE D 301 ? 0.8558 0.9937 0.7690 -0.0062 0.0253  0.0580  301 ILE D CG1 
14783 C CG2 . ILE D 301 ? 0.7909 0.9347 0.7186 -0.0238 0.0346  0.0516  301 ILE D CG2 
14784 C CD1 . ILE D 301 ? 0.8117 0.9324 0.7228 0.0125  0.0293  0.0651  301 ILE D CD1 
14785 N N   . SER D 302 ? 0.8459 1.0071 0.7578 -0.0486 0.0181  0.0400  302 SER D N   
14786 C CA  . SER D 302 ? 0.8285 0.9656 0.7303 -0.0650 0.0201  0.0330  302 SER D CA  
14787 C C   . SER D 302 ? 0.8360 0.9314 0.7277 -0.0597 0.0265  0.0373  302 SER D C   
14788 O O   . SER D 302 ? 0.7925 0.8773 0.6791 -0.0447 0.0268  0.0437  302 SER D O   
14789 C CB  . SER D 302 ? 0.7989 0.9461 0.6901 -0.0693 0.0130  0.0272  302 SER D CB  
14790 O OG  . SER D 302 ? 0.9633 1.1551 0.8648 -0.0727 0.0049  0.0234  302 SER D OG  
14791 N N   . VAL D 303 ? 0.7916 0.8640 0.6813 -0.0720 0.0319  0.0340  303 VAL D N   
14792 C CA  . VAL D 303 ? 0.8686 0.9062 0.7516 -0.0673 0.0372  0.0379  303 VAL D CA  
14793 C C   . VAL D 303 ? 0.8675 0.8814 0.7422 -0.0784 0.0400  0.0320  303 VAL D C   
14794 O O   . VAL D 303 ? 0.8775 0.8941 0.7536 -0.0934 0.0408  0.0255  303 VAL D O   
14795 C CB  . VAL D 303 ? 0.8204 0.8520 0.7095 -0.0664 0.0419  0.0427  303 VAL D CB  
14796 C CG1 . VAL D 303 ? 0.7606 0.7623 0.6439 -0.0600 0.0451  0.0467  303 VAL D CG1 
14797 C CG2 . VAL D 303 ? 0.6527 0.7089 0.5506 -0.0563 0.0406  0.0461  303 VAL D CG2 
14798 N N   . PHE D 304 ? 0.8542 0.8446 0.7210 -0.0711 0.0423  0.0336  304 PHE D N   
14799 C CA  . PHE D 304 ? 0.8786 0.8426 0.7385 -0.0775 0.0468  0.0288  304 PHE D CA  
14800 C C   . PHE D 304 ? 0.8529 0.7938 0.7151 -0.0702 0.0512  0.0353  304 PHE D C   
14801 O O   . PHE D 304 ? 0.8661 0.8090 0.7309 -0.0591 0.0504  0.0411  304 PHE D O   
14802 C CB  . PHE D 304 ? 0.8101 0.7718 0.6587 -0.0749 0.0460  0.0237  304 PHE D CB  
14803 C CG  . PHE D 304 ? 0.8885 0.8691 0.7315 -0.0854 0.0415  0.0143  304 PHE D CG  
14804 C CD1 . PHE D 304 ? 0.9389 0.9101 0.7803 -0.1014 0.0441  0.0040  304 PHE D CD1 
14805 C CD2 . PHE D 304 ? 0.8798 0.8876 0.7190 -0.0794 0.0345  0.0155  304 PHE D CD2 
14806 C CE1 . PHE D 304 ? 0.9301 0.9211 0.7667 -0.1133 0.0392  -0.0071 304 PHE D CE1 
14807 C CE2 . PHE D 304 ? 0.8958 0.9263 0.7298 -0.0892 0.0285  0.0062  304 PHE D CE2 
14808 C CZ  . PHE D 304 ? 0.9492 0.9724 0.7823 -0.1072 0.0306  -0.0062 304 PHE D CZ  
14809 N N   . PHE D 305 ? 0.8515 0.7707 0.7131 -0.0763 0.0559  0.0343  305 PHE D N   
14810 C CA  . PHE D 305 ? 0.8886 0.7896 0.7532 -0.0689 0.0589  0.0412  305 PHE D CA  
14811 C C   . PHE D 305 ? 0.9502 0.8304 0.8115 -0.0650 0.0632  0.0380  305 PHE D C   
14812 O O   . PHE D 305 ? 1.0356 0.9019 0.8919 -0.0724 0.0671  0.0311  305 PHE D O   
14813 C CB  . PHE D 305 ? 0.8954 0.7878 0.7620 -0.0755 0.0614  0.0458  305 PHE D CB  
14814 C CG  . PHE D 305 ? 0.8312 0.7454 0.7016 -0.0784 0.0589  0.0492  305 PHE D CG  
14815 C CD1 . PHE D 305 ? 0.8594 0.7802 0.7321 -0.0696 0.0572  0.0559  305 PHE D CD1 
14816 C CD2 . PHE D 305 ? 0.9310 0.8611 0.8032 -0.0904 0.0588  0.0444  305 PHE D CD2 
14817 C CE1 . PHE D 305 ? 0.9667 0.9075 0.8422 -0.0714 0.0565  0.0579  305 PHE D CE1 
14818 C CE2 . PHE D 305 ? 0.8737 0.8268 0.7514 -0.0922 0.0578  0.0474  305 PHE D CE2 
14819 C CZ  . PHE D 305 ? 0.9025 0.8598 0.7812 -0.0820 0.0573  0.0542  305 PHE D CZ  
14820 N N   . ARG D 306 ? 0.9594 0.8379 0.8244 -0.0540 0.0634  0.0420  306 ARG D N   
14821 C CA  . ARG D 306 ? 1.0452 0.9084 0.9096 -0.0490 0.0685  0.0391  306 ARG D CA  
14822 C C   . ARG D 306 ? 1.0741 0.9158 0.9418 -0.0484 0.0728  0.0410  306 ARG D C   
14823 O O   . ARG D 306 ? 1.0275 0.8657 0.8972 -0.0505 0.0714  0.0470  306 ARG D O   
14824 C CB  . ARG D 306 ? 0.9370 0.8063 0.8078 -0.0389 0.0684  0.0432  306 ARG D CB  
14825 C CG  . ARG D 306 ? 0.9706 0.8372 0.8522 -0.0327 0.0672  0.0499  306 ARG D CG  
14826 C CD  . ARG D 306 ? 0.8792 0.7489 0.7698 -0.0250 0.0693  0.0510  306 ARG D CD  
14827 N NE  . ARG D 306 ? 0.9028 0.7760 0.8042 -0.0201 0.0658  0.0565  306 ARG D NE  
14828 C CZ  . ARG D 306 ? 0.8467 0.7273 0.7597 -0.0150 0.0658  0.0574  306 ARG D CZ  
14829 N NH1 . ARG D 306 ? 0.8758 0.7585 0.7916 -0.0141 0.0709  0.0543  306 ARG D NH1 
14830 N NH2 . ARG D 306 ? 0.8721 0.7595 0.7935 -0.0114 0.0607  0.0617  306 ARG D NH2 
14831 N N   . ASP D 307 ? 1.0164 0.8431 0.8839 -0.0442 0.0790  0.0366  307 ASP D N   
14832 C CA  . ASP D 307 ? 0.9746 0.7795 0.8469 -0.0392 0.0841  0.0395  307 ASP D CA  
14833 C C   . ASP D 307 ? 0.9599 0.7717 0.8449 -0.0261 0.0832  0.0462  307 ASP D C   
14834 O O   . ASP D 307 ? 1.0075 0.8245 0.8960 -0.0211 0.0866  0.0424  307 ASP D O   
14835 C CB  . ASP D 307 ? 1.0163 0.8001 0.8817 -0.0422 0.0927  0.0288  307 ASP D CB  
14836 C CG  . ASP D 307 ? 1.1155 0.8722 0.9856 -0.0360 0.0992  0.0322  307 ASP D CG  
14837 O OD1 . ASP D 307 ? 1.1622 0.9203 1.0440 -0.0228 0.0988  0.0408  307 ASP D OD1 
14838 O OD2 . ASP D 307 ? 1.1688 0.9026 1.0314 -0.0443 0.1048  0.0259  307 ASP D OD2 
14839 N N   . LYS D 308 ? 1.0293 0.8434 0.9209 -0.0214 0.0787  0.0561  308 LYS D N   
14840 C CA  . LYS D 308 ? 0.9740 0.8001 0.8790 -0.0104 0.0758  0.0618  308 LYS D CA  
14841 C C   . LYS D 308 ? 0.8967 0.7127 0.8111 -0.0005 0.0827  0.0601  308 LYS D C   
14842 O O   . LYS D 308 ? 0.9440 0.7731 0.8690 0.0047  0.0843  0.0579  308 LYS D O   
14843 C CB  . LYS D 308 ? 0.8983 0.7291 0.8052 -0.0073 0.0690  0.0724  308 LYS D CB  
14844 C CG  . LYS D 308 ? 0.9437 0.7982 0.8598 -0.0030 0.0617  0.0751  308 LYS D CG  
14845 C CD  . LYS D 308 ? 0.8372 0.6964 0.7568 0.0044  0.0556  0.0854  308 LYS D CD  
14846 C CE  . LYS D 308 ? 0.9032 0.7877 0.8336 0.0077  0.0482  0.0850  308 LYS D CE  
14847 N NZ  . LYS D 308 ? 0.9369 0.8323 0.8638 -0.0009 0.0469  0.0779  308 LYS D NZ  
14848 N N   . THR D 309 ? 0.8782 0.6700 0.7894 0.0019  0.0883  0.0608  309 THR D N   
14849 C CA  . THR D 309 ? 0.8437 0.6241 0.7649 0.0138  0.0961  0.0594  309 THR D CA  
14850 C C   . THR D 309 ? 0.9375 0.7208 0.8579 0.0123  0.1039  0.0475  309 THR D C   
14851 O O   . THR D 309 ? 0.8807 0.6757 0.8152 0.0216  0.1074  0.0469  309 THR D O   
14852 C CB  . THR D 309 ? 0.8161 0.5633 0.7307 0.0153  0.1027  0.0609  309 THR D CB  
14853 O OG1 . THR D 309 ? 0.9837 0.7162 0.8818 -0.0003 0.1060  0.0516  309 THR D OG1 
14854 C CG2 . THR D 309 ? 0.8548 0.5987 0.7704 0.0199  0.0963  0.0760  309 THR D CG2 
14855 N N   . LEU D 310 ? 0.9421 0.7177 0.8460 0.0003  0.1066  0.0379  310 LEU D N   
14856 C CA  . LEU D 310 ? 0.9186 0.6971 0.8170 -0.0013 0.1140  0.0271  310 LEU D CA  
14857 C C   . LEU D 310 ? 0.9353 0.7403 0.8404 0.0000  0.1108  0.0299  310 LEU D C   
14858 O O   . LEU D 310 ? 0.8890 0.7005 0.8012 0.0057  0.1181  0.0269  310 LEU D O   
14859 C CB  . LEU D 310 ? 1.0165 0.7858 0.8944 -0.0150 0.1150  0.0167  310 LEU D CB  
14860 C CG  . LEU D 310 ? 1.0487 0.7887 0.9173 -0.0179 0.1245  0.0058  310 LEU D CG  
14861 C CD1 . LEU D 310 ? 1.0775 0.7933 0.9549 -0.0110 0.1272  0.0127  310 LEU D CD1 
14862 C CD2 . LEU D 310 ? 1.0009 0.7394 0.8513 -0.0346 0.1217  -0.0039 310 LEU D CD2 
14863 N N   . SER D 311 ? 0.9716 0.7910 0.8750 -0.0056 0.1012  0.0355  311 SER D N   
14864 C CA  . SER D 311 ? 0.9795 0.8191 0.8882 -0.0055 0.0992  0.0379  311 SER D CA  
14865 C C   . SER D 311 ? 0.9273 0.7791 0.8576 0.0031  0.0987  0.0432  311 SER D C   
14866 O O   . SER D 311 ? 0.9737 0.8375 0.9122 0.0043  0.1031  0.0423  311 SER D O   
14867 C CB  . SER D 311 ? 0.9168 0.7659 0.8182 -0.0125 0.0901  0.0415  311 SER D CB  
14868 O OG  . SER D 311 ? 0.8992 0.7439 0.7832 -0.0203 0.0901  0.0361  311 SER D OG  
14869 N N   . ASP D 312 ? 0.8380 0.6887 0.7779 0.0087  0.0935  0.0492  312 ASP D N   
14870 C CA  . ASP D 312 ? 0.8838 0.7515 0.8452 0.0170  0.0911  0.0539  312 ASP D CA  
14871 C C   . ASP D 312 ? 0.9610 0.8270 0.9362 0.0272  0.1007  0.0512  312 ASP D C   
14872 O O   . ASP D 312 ? 0.9255 0.8116 0.9206 0.0320  0.1019  0.0519  312 ASP D O   
14873 C CB  . ASP D 312 ? 0.9342 0.8047 0.8991 0.0208  0.0810  0.0625  312 ASP D CB  
14874 C CG  . ASP D 312 ? 1.1385 1.0275 1.1044 0.0151  0.0714  0.0648  312 ASP D CG  
14875 O OD1 . ASP D 312 ? 1.1777 1.0675 1.1339 0.0063  0.0717  0.0609  312 ASP D OD1 
14876 O OD2 . ASP D 312 ? 1.2680 1.1708 1.2438 0.0200  0.0636  0.0703  312 ASP D OD2 
14877 N N   . LEU D 313 ? 0.9329 0.7759 0.8986 0.0301  0.1086  0.0470  313 LEU D N   
14878 C CA  . LEU D 313 ? 0.8586 0.6983 0.8362 0.0406  0.1201  0.0427  313 LEU D CA  
14879 C C   . LEU D 313 ? 0.8718 0.7272 0.8536 0.0375  0.1283  0.0366  313 LEU D C   
14880 O O   . LEU D 313 ? 0.9217 0.7953 0.9257 0.0451  0.1330  0.0372  313 LEU D O   
14881 C CB  . LEU D 313 ? 0.9184 0.7263 0.8805 0.0414  0.1286  0.0360  313 LEU D CB  
14882 C CG  . LEU D 313 ? 0.8990 0.6867 0.8657 0.0518  0.1281  0.0424  313 LEU D CG  
14883 C CD1 . LEU D 313 ? 0.8693 0.6227 0.8145 0.0442  0.1337  0.0353  313 LEU D CD1 
14884 C CD2 . LEU D 313 ? 0.9658 0.7568 0.9542 0.0697  0.1361  0.0435  313 LEU D CD2 
14885 N N   . ILE D 314 ? 0.8472 0.6976 0.8085 0.0262  0.1303  0.0315  314 ILE D N   
14886 C CA  . ILE D 314 ? 0.8683 0.7312 0.8295 0.0227  0.1387  0.0280  314 ILE D CA  
14887 C C   . ILE D 314 ? 0.8612 0.7484 0.8421 0.0212  0.1340  0.0342  314 ILE D C   
14888 O O   . ILE D 314 ? 0.7735 0.6753 0.7684 0.0222  0.1429  0.0330  314 ILE D O   
14889 C CB  . ILE D 314 ? 0.8313 0.6853 0.7643 0.0122  0.1392  0.0240  314 ILE D CB  
14890 C CG1 . ILE D 314 ? 0.9517 0.7843 0.8663 0.0094  0.1373  0.0184  314 ILE D CG1 
14891 C CG2 . ILE D 314 ? 0.8044 0.6622 0.7301 0.0113  0.1524  0.0190  314 ILE D CG2 
14892 C CD1 . ILE D 314 ? 1.0536 0.8836 0.9427 -0.0009 0.1349  0.0145  314 ILE D CD1 
14893 N N   . GLY D 315 ? 0.8316 0.7236 0.8138 0.0175  0.1210  0.0400  315 GLY D N   
14894 C CA  . GLY D 315 ? 0.8630 0.7755 0.8605 0.0133  0.1165  0.0433  315 GLY D CA  
14895 C C   . GLY D 315 ? 0.8596 0.7932 0.8866 0.0208  0.1146  0.0451  315 GLY D C   
14896 O O   . GLY D 315 ? 0.7762 0.7297 0.8214 0.0172  0.1172  0.0443  315 GLY D O   
14897 N N   . PHE D 316 ? 0.8513 0.7820 0.8844 0.0312  0.1100  0.0480  316 PHE D N   
14898 C CA  . PHE D 316 ? 0.7975 0.7523 0.8582 0.0400  0.1046  0.0517  316 PHE D CA  
14899 C C   . PHE D 316 ? 0.7776 0.7306 0.8518 0.0560  0.1110  0.0526  316 PHE D C   
14900 O O   . PHE D 316 ? 0.9350 0.9142 1.0366 0.0648  0.1086  0.0551  316 PHE D O   
14901 C CB  . PHE D 316 ? 0.7653 0.7256 0.8235 0.0397  0.0885  0.0581  316 PHE D CB  
14902 C CG  . PHE D 316 ? 0.7858 0.7474 0.8319 0.0259  0.0824  0.0564  316 PHE D CG  
14903 C CD1 . PHE D 316 ? 0.7992 0.7835 0.8611 0.0185  0.0800  0.0533  316 PHE D CD1 
14904 C CD2 . PHE D 316 ? 0.8758 0.8161 0.8962 0.0203  0.0797  0.0574  316 PHE D CD2 
14905 C CE1 . PHE D 316 ? 0.8126 0.7940 0.8630 0.0069  0.0757  0.0512  316 PHE D CE1 
14906 C CE2 . PHE D 316 ? 0.8792 0.8208 0.8898 0.0100  0.0749  0.0559  316 PHE D CE2 
14907 C CZ  . PHE D 316 ? 0.7406 0.7006 0.7654 0.0040  0.0733  0.0529  316 PHE D CZ  
14908 N N   . SER D 317 ? 0.7526 0.6768 0.8097 0.0602  0.1192  0.0500  317 SER D N   
14909 C CA  . SER D 317 ? 0.7780 0.6949 0.8469 0.0769  0.1260  0.0509  317 SER D CA  
14910 C C   . SER D 317 ? 0.9328 0.8478 1.0066 0.0806  0.1439  0.0416  317 SER D C   
14911 O O   . SER D 317 ? 1.0094 0.9408 1.1089 0.0941  0.1502  0.0417  317 SER D O   
14912 C CB  . SER D 317 ? 0.7855 0.6676 0.8334 0.0801  0.1242  0.0538  317 SER D CB  
14913 O OG  . SER D 317 ? 0.9258 0.8127 0.9747 0.0826  0.1097  0.0648  317 SER D OG  
14914 N N   . TYR D 318 ? 0.8390 0.7364 0.8886 0.0696  0.1522  0.0336  318 TYR D N   
14915 C CA  . TYR D 318 ? 0.8908 0.7813 0.9384 0.0738  0.1701  0.0240  318 TYR D CA  
14916 C C   . TYR D 318 ? 0.9169 0.8390 0.9879 0.0742  0.1792  0.0224  318 TYR D C   
14917 O O   . TYR D 318 ? 1.0344 0.9558 1.1088 0.0804  0.1955  0.0150  318 TYR D O   
14918 C CB  . TYR D 318 ? 0.9269 0.7935 0.9396 0.0615  0.1753  0.0158  318 TYR D CB  
14919 C CG  . TYR D 318 ? 0.9693 0.8029 0.9599 0.0603  0.1719  0.0130  318 TYR D CG  
14920 C CD1 . TYR D 318 ? 0.9797 0.7955 0.9787 0.0734  0.1737  0.0143  318 TYR D CD1 
14921 C CD2 . TYR D 318 ? 0.9762 0.7967 0.9383 0.0459  0.1671  0.0096  318 TYR D CD2 
14922 C CE1 . TYR D 318 ? 1.0115 0.7942 0.9903 0.0699  0.1721  0.0116  318 TYR D CE1 
14923 C CE2 . TYR D 318 ? 1.0587 0.8517 1.0027 0.0421  0.1644  0.0059  318 TYR D CE2 
14924 C CZ  . TYR D 318 ? 1.1162 0.8889 1.0683 0.0530  0.1675  0.0067  318 TYR D CZ  
14925 O OH  . TYR D 318 ? 1.1313 0.8739 1.0657 0.0471  0.1663  0.0030  318 TYR D OH  
14926 N N   . HIS D 319 ? 0.8270 0.7762 0.9142 0.0670  0.1705  0.0281  319 HIS D N   
14927 C CA  . HIS D 319 ? 0.8061 0.7856 0.9174 0.0646  0.1804  0.0262  319 HIS D CA  
14928 C C   . HIS D 319 ? 0.8517 0.8519 0.9961 0.0817  0.1882  0.0251  319 HIS D C   
14929 O O   . HIS D 319 ? 0.8643 0.8847 1.0257 0.0817  0.2027  0.0208  319 HIS D O   
14930 C CB  . HIS D 319 ? 0.7234 0.7268 0.8487 0.0531  0.1687  0.0313  319 HIS D CB  
14931 C CG  . HIS D 319 ? 0.8299 0.8562 0.9816 0.0615  0.1542  0.0367  319 HIS D CG  
14932 N ND1 . HIS D 319 ? 0.8238 0.8367 0.9633 0.0651  0.1387  0.0424  319 HIS D ND1 
14933 C CD2 . HIS D 319 ? 0.7801 0.8442 0.9692 0.0671  0.1526  0.0376  319 HIS D CD2 
14934 C CE1 . HIS D 319 ? 0.8244 0.8648 0.9900 0.0734  0.1278  0.0473  319 HIS D CE1 
14935 N NE2 . HIS D 319 ? 0.7197 0.7929 0.9166 0.0748  0.1351  0.0441  319 HIS D NE2 
14936 N N   . ALA D 320 ? 0.8454 0.8420 0.9998 0.0970  0.1798  0.0297  320 ALA D N   
14937 C CA  . ALA D 320 ? 0.8585 0.8752 1.0457 0.1169  0.1857  0.0305  320 ALA D CA  
14938 C C   . ALA D 320 ? 0.8704 0.8544 1.0453 0.1317  0.1992  0.0251  320 ALA D C   
14939 O O   . ALA D 320 ? 0.8135 0.7989 1.0074 0.1520  0.1996  0.0289  320 ALA D O   
14940 C CB  . ALA D 320 ? 0.8522 0.8904 1.0615 0.1267  0.1671  0.0411  320 ALA D CB  
14941 N N   . TRP D 321 ? 0.8677 0.8217 1.0102 0.1220  0.2102  0.0159  321 TRP D N   
14942 C CA  . TRP D 321 ? 0.9469 0.8655 1.0723 0.1320  0.2234  0.0074  321 TRP D CA  
14943 C C   . TRP D 321 ? 0.9813 0.9012 1.0981 0.1280  0.2443  -0.0052 321 TRP D C   
14944 O O   . TRP D 321 ? 1.0670 1.0065 1.1812 0.1140  0.2472  -0.0057 321 TRP D O   
14945 C CB  . TRP D 321 ? 1.0407 0.9179 1.1284 0.1222  0.2154  0.0062  321 TRP D CB  
14946 C CG  . TRP D 321 ? 1.0455 0.9122 1.1356 0.1274  0.1985  0.0181  321 TRP D CG  
14947 C CD1 . TRP D 321 ? 1.0607 0.9557 1.1747 0.1326  0.1837  0.0307  321 TRP D CD1 
14948 C CD2 . TRP D 321 ? 1.0023 0.8280 1.0683 0.1267  0.1952  0.0182  321 TRP D CD2 
14949 N NE1 . TRP D 321 ? 0.9989 0.8727 1.1032 0.1365  0.1718  0.0399  321 TRP D NE1 
14950 C CE2 . TRP D 321 ? 1.1164 0.9468 1.1923 0.1325  0.1792  0.0329  321 TRP D CE2 
14951 C CE3 . TRP D 321 ? 1.1013 0.8875 1.1380 0.1204  0.2045  0.0066  321 TRP D CE3 
14952 C CZ2 . TRP D 321 ? 1.2269 1.0224 1.2846 0.1324  0.1738  0.0380  321 TRP D CZ2 
14953 C CZ3 . TRP D 321 ? 1.1183 0.8703 1.1394 0.1190  0.1985  0.0102  321 TRP D CZ3 
14954 C CH2 . TRP D 321 ? 1.1556 0.9117 1.1873 0.1250  0.1841  0.0265  321 TRP D CH2 
14955 N N   . ASN D 322 ? 0.8899 0.7864 1.0001 0.1404  0.2600  -0.0154 322 ASN D N   
14956 C CA  . ASN D 322 ? 0.9931 0.8821 1.0823 0.1341  0.2793  -0.0292 322 ASN D CA  
14957 C C   . ASN D 322 ? 1.0397 0.8998 1.0838 0.1151  0.2736  -0.0343 322 ASN D C   
14958 O O   . ASN D 322 ? 1.0712 0.9068 1.1005 0.1113  0.2600  -0.0313 322 ASN D O   
14959 C CB  . ASN D 322 ? 1.0395 0.9109 1.1337 0.1531  0.2986  -0.0409 322 ASN D CB  
14960 C CG  . ASN D 322 ? 1.0696 0.9211 1.1295 0.1451  0.3167  -0.0580 322 ASN D CG  
14961 O OD1 . ASN D 322 ? 1.1423 0.9587 1.1658 0.1353  0.3140  -0.0661 322 ASN D OD1 
14962 N ND2 . ASN D 322 ? 1.0840 0.9606 1.1546 0.1480  0.3351  -0.0637 322 ASN D ND2 
14963 N N   . ALA D 323 ? 1.0926 0.9582 1.1154 0.1032  0.2841  -0.0412 323 ALA D N   
14964 C CA  . ALA D 323 ? 1.1149 0.9611 1.0962 0.0856  0.2777  -0.0448 323 ALA D CA  
14965 C C   . ALA D 323 ? 1.0862 0.8930 1.0411 0.0861  0.2785  -0.0570 323 ALA D C   
14966 O O   . ALA D 323 ? 1.1935 0.9834 1.1304 0.0760  0.2636  -0.0548 323 ALA D O   
14967 C CB  . ALA D 323 ? 1.0981 0.9571 1.0602 0.0763  0.2914  -0.0496 323 ALA D CB  
14968 N N   . GLU D 324 ? 1.0120 0.8034 0.9646 0.0971  0.2967  -0.0712 324 GLU D N   
14969 C CA  . GLU D 324 ? 1.1465 0.8971 1.0731 0.0956  0.2995  -0.0855 324 GLU D CA  
14970 C C   . GLU D 324 ? 1.1476 0.8768 1.0871 0.1012  0.2862  -0.0773 324 GLU D C   
14971 O O   . GLU D 324 ? 1.2034 0.9050 1.1195 0.0900  0.2781  -0.0819 324 GLU D O   
14972 C CB  . GLU D 324 ? 1.3123 1.0489 1.2371 0.1084  0.3235  -0.1030 324 GLU D CB  
14973 C CG  . GLU D 324 ? 1.3901 1.1564 1.3169 0.1100  0.3406  -0.1069 324 GLU D CG  
14974 C CD  . GLU D 324 ? 1.5169 1.2717 1.4485 0.1264  0.3654  -0.1236 324 GLU D CD  
14975 O OE1 . GLU D 324 ? 1.3733 1.1013 1.3176 0.1408  0.3686  -0.1281 324 GLU D OE1 
14976 O OE2 . GLU D 324 ? 1.6113 1.3827 1.5333 0.1254  0.3828  -0.1318 324 GLU D OE2 
14977 N N   . ASP D 325 ? 1.0876 0.8310 1.0642 0.1180  0.2839  -0.0647 325 ASP D N   
14978 C CA  . ASP D 325 ? 1.1272 0.8517 1.1151 0.1251  0.2715  -0.0540 325 ASP D CA  
14979 C C   . ASP D 325 ? 1.1256 0.8553 1.1025 0.1083  0.2501  -0.0426 325 ASP D C   
14980 O O   . ASP D 325 ? 1.1364 0.8396 1.1043 0.1053  0.2414  -0.0391 325 ASP D O   
14981 C CB  . ASP D 325 ? 1.0916 0.8385 1.1214 0.1475  0.2718  -0.0415 325 ASP D CB  
14982 C CG  . ASP D 325 ? 1.1771 0.9125 1.2205 0.1683  0.2931  -0.0519 325 ASP D CG  
14983 O OD1 . ASP D 325 ? 1.2624 0.9842 1.2848 0.1637  0.3097  -0.0699 325 ASP D OD1 
14984 O OD2 . ASP D 325 ? 1.2406 0.9813 1.3149 0.1901  0.2932  -0.0422 325 ASP D OD2 
14985 N N   . ALA D 326 ? 1.0414 0.8037 1.0188 0.0974  0.2428  -0.0367 326 ALA D N   
14986 C CA  . ALA D 326 ? 1.0145 0.7820 0.9805 0.0821  0.2241  -0.0274 326 ALA D CA  
14987 C C   . ALA D 326 ? 1.1365 0.8798 1.0657 0.0656  0.2225  -0.0383 326 ALA D C   
14988 O O   . ALA D 326 ? 1.1458 0.8739 1.0653 0.0577  0.2107  -0.0345 326 ALA D O   
14989 C CB  . ALA D 326 ? 0.9138 0.7186 0.8899 0.0756  0.2190  -0.0194 326 ALA D CB  
14990 N N   . VAL D 327 ? 1.0642 0.8062 0.9724 0.0598  0.2343  -0.0519 327 VAL D N   
14991 C CA  . VAL D 327 ? 1.1028 0.8261 0.9758 0.0440  0.2322  -0.0640 327 VAL D CA  
14992 C C   . VAL D 327 ? 1.1566 0.8415 1.0231 0.0447  0.2348  -0.0733 327 VAL D C   
14993 O O   . VAL D 327 ? 1.1325 0.8031 0.9810 0.0306  0.2255  -0.0766 327 VAL D O   
14994 C CB  . VAL D 327 ? 1.1261 0.8565 0.9761 0.0394  0.2452  -0.0772 327 VAL D CB  
14995 C CG1 . VAL D 327 ? 1.0842 0.8042 0.8977 0.0219  0.2391  -0.0883 327 VAL D CG1 
14996 C CG2 . VAL D 327 ? 1.0934 0.8582 0.9529 0.0398  0.2456  -0.0659 327 VAL D CG2 
14997 N N   . ARG D 328 ? 1.1618 0.8293 1.0442 0.0613  0.2481  -0.0773 328 ARG D N   
14998 C CA  . ARG D 328 ? 1.1611 0.7866 1.0394 0.0637  0.2524  -0.0843 328 ARG D CA  
14999 C C   . ARG D 328 ? 1.1242 0.7424 1.0091 0.0591  0.2361  -0.0689 328 ARG D C   
15000 O O   . ARG D 328 ? 1.1883 0.7794 1.0557 0.0460  0.2330  -0.0752 328 ARG D O   
15001 C CB  . ARG D 328 ? 1.2204 0.8316 1.1205 0.0870  0.2686  -0.0862 328 ARG D CB  
15002 C CG  . ARG D 328 ? 1.2557 0.8182 1.1406 0.0880  0.2827  -0.1041 328 ARG D CG  
15003 C CD  . ARG D 328 ? 1.2475 0.8006 1.1509 0.1120  0.3023  -0.1098 328 ARG D CD  
15004 N NE  . ARG D 328 ? 1.3924 0.9675 1.2868 0.1112  0.3152  -0.1238 328 ARG D NE  
15005 C CZ  . ARG D 328 ? 1.4247 1.0382 1.3426 0.1238  0.3197  -0.1158 328 ARG D CZ  
15006 N NH1 . ARG D 328 ? 1.4053 1.0402 1.3590 0.1395  0.3125  -0.0961 328 ARG D NH1 
15007 N NH2 . ARG D 328 ? 1.4013 1.0332 1.3062 0.1200  0.3322  -0.1282 328 ARG D NH2 
15008 N N   . ASP D 329 ? 1.0958 0.7392 1.0057 0.0689  0.2260  -0.0495 329 ASP D N   
15009 C CA  . ASP D 329 ? 1.1058 0.7458 1.0200 0.0648  0.2107  -0.0342 329 ASP D CA  
15010 C C   . ASP D 329 ? 1.1288 0.7749 1.0205 0.0421  0.1990  -0.0368 329 ASP D C   
15011 O O   . ASP D 329 ? 1.1678 0.7915 1.0485 0.0317  0.1944  -0.0370 329 ASP D O   
15012 C CB  . ASP D 329 ? 1.0980 0.7706 1.0402 0.0775  0.2011  -0.0153 329 ASP D CB  
15013 C CG  . ASP D 329 ? 1.0937 0.7532 1.0459 0.0849  0.1923  0.0004  329 ASP D CG  
15014 O OD1 . ASP D 329 ? 1.1604 0.7870 1.1152 0.0963  0.2011  0.0001  329 ASP D OD1 
15015 O OD2 . ASP D 329 ? 1.0770 0.7577 1.0330 0.0796  0.1773  0.0132  329 ASP D OD2 
15016 N N   . PHE D 330 ? 1.0265 0.7030 0.9117 0.0345  0.1952  -0.0385 330 PHE D N   
15017 C CA  . PHE D 330 ? 1.0918 0.7792 0.9583 0.0161  0.1833  -0.0389 330 PHE D CA  
15018 C C   . PHE D 330 ? 1.1065 0.7686 0.9479 0.0014  0.1867  -0.0557 330 PHE D C   
15019 O O   . PHE D 330 ? 1.1289 0.7837 0.9633 -0.0110 0.1778  -0.0540 330 PHE D O   
15020 C CB  . PHE D 330 ? 1.0504 0.7700 0.9126 0.0132  0.1816  -0.0379 330 PHE D CB  
15021 C CG  . PHE D 330 ? 1.0458 0.7816 0.8948 -0.0009 0.1679  -0.0336 330 PHE D CG  
15022 C CD1 . PHE D 330 ? 1.0837 0.8340 0.9460 -0.0010 0.1552  -0.0187 330 PHE D CD1 
15023 C CD2 . PHE D 330 ? 1.0642 0.8024 0.8873 -0.0133 0.1676  -0.0449 330 PHE D CD2 
15024 C CE1 . PHE D 330 ? 1.1232 0.8882 0.9748 -0.0121 0.1438  -0.0151 330 PHE D CE1 
15025 C CE2 . PHE D 330 ? 1.0697 0.8254 0.8830 -0.0239 0.1548  -0.0400 330 PHE D CE2 
15026 C CZ  . PHE D 330 ? 1.1160 0.8842 0.9443 -0.0227 0.1435  -0.0251 330 PHE D CZ  
15027 N N   . ILE D 331 ? 1.0845 0.7342 0.9123 0.0017  0.2002  -0.0730 331 ILE D N   
15028 C CA  . ILE D 331 ? 1.1113 0.7383 0.9140 -0.0140 0.2036  -0.0923 331 ILE D CA  
15029 C C   . ILE D 331 ? 1.1022 0.6910 0.9096 -0.0161 0.2061  -0.0934 331 ILE D C   
15030 O O   . ILE D 331 ? 1.1296 0.7073 0.9239 -0.0340 0.2006  -0.1002 331 ILE D O   
15031 C CB  . ILE D 331 ? 1.1070 0.7274 0.8934 -0.0116 0.2192  -0.1117 331 ILE D CB  
15032 C CG1 . ILE D 331 ? 1.1215 0.7789 0.9027 -0.0094 0.2179  -0.1074 331 ILE D CG1 
15033 C CG2 . ILE D 331 ? 1.1829 0.7834 0.9413 -0.0301 0.2214  -0.1342 331 ILE D CG2 
15034 C CD1 . ILE D 331 ? 1.0540 0.7343 0.8143 -0.0258 0.2043  -0.1075 331 ILE D CD1 
15035 N N   . GLY D 332 ? 1.0600 0.6288 0.8867 0.0022  0.2148  -0.0860 332 GLY D N   
15036 C CA  . GLY D 332 ? 1.1443 0.6733 0.9750 0.0023  0.2182  -0.0836 332 GLY D CA  
15037 C C   . GLY D 332 ? 1.2252 0.7624 1.0616 -0.0058 0.2031  -0.0661 332 GLY D C   
15038 O O   . GLY D 332 ? 1.1913 0.7017 1.0200 -0.0189 0.2031  -0.0686 332 GLY D O   
15039 N N   . ARG D 333 ? 1.1580 0.7320 1.0080 0.0009  0.1911  -0.0488 333 ARG D N   
15040 C CA  . ARG D 333 ? 1.1370 0.7230 0.9906 -0.0068 0.1770  -0.0333 333 ARG D CA  
15041 C C   . ARG D 333 ? 1.2052 0.7994 1.0405 -0.0306 0.1699  -0.0431 333 ARG D C   
15042 O O   . ARG D 333 ? 1.2265 0.8108 1.0595 -0.0421 0.1651  -0.0384 333 ARG D O   
15043 C CB  . ARG D 333 ? 1.0660 0.6906 0.9357 0.0040  0.1666  -0.0171 333 ARG D CB  
15044 C CG  . ARG D 333 ? 1.0337 0.6550 0.9251 0.0254  0.1685  -0.0025 333 ARG D CG  
15045 C CD  . ARG D 333 ? 0.9433 0.5996 0.8487 0.0304  0.1548  0.0143  333 ARG D CD  
15046 N NE  . ARG D 333 ? 1.0444 0.7094 0.9723 0.0517  0.1567  0.0243  333 ARG D NE  
15047 C CZ  . ARG D 333 ? 1.0574 0.7173 0.9966 0.0636  0.1519  0.0401  333 ARG D CZ  
15048 N NH1 . ARG D 333 ? 1.0573 0.7017 0.9862 0.0559  0.1461  0.0488  333 ARG D NH1 
15049 N NH2 . ARG D 333 ? 1.1608 0.8338 1.1220 0.0839  0.1531  0.0479  333 ARG D NH2 
15050 N N   . LEU D 334 ? 1.1620 0.7765 0.9843 -0.0378 0.1692  -0.0561 334 LEU D N   
15051 C CA  . LEU D 334 ? 1.1318 0.7565 0.9365 -0.0592 0.1624  -0.0673 334 LEU D CA  
15052 C C   . LEU D 334 ? 1.2374 0.8256 1.0305 -0.0736 0.1707  -0.0840 334 LEU D C   
15053 O O   . LEU D 334 ? 1.3249 0.9155 1.1117 -0.0925 0.1644  -0.0881 334 LEU D O   
15054 C CB  . LEU D 334 ? 1.0990 0.7512 0.8901 -0.0608 0.1610  -0.0768 334 LEU D CB  
15055 C CG  . LEU D 334 ? 1.1438 0.8364 0.9385 -0.0586 0.1487  -0.0635 334 LEU D CG  
15056 C CD1 . LEU D 334 ? 1.0482 0.7496 0.8646 -0.0413 0.1477  -0.0453 334 LEU D CD1 
15057 C CD2 . LEU D 334 ? 1.0969 0.8095 0.8733 -0.0608 0.1496  -0.0732 334 LEU D CD2 
15058 N N   . LYS D 335 ? 1.2466 0.8008 1.0382 -0.0652 0.1858  -0.0943 335 LYS D N   
15059 C CA  . LYS D 335 ? 1.2792 0.7916 1.0601 -0.0787 0.1960  -0.1112 335 LYS D CA  
15060 C C   . LYS D 335 ? 1.3547 0.8438 1.1454 -0.0840 0.1944  -0.0978 335 LYS D C   
15061 O O   . LYS D 335 ? 1.3584 0.8352 1.1408 -0.1061 0.1937  -0.1072 335 LYS D O   
15062 C CB  . LYS D 335 ? 1.3704 0.8484 1.1501 -0.0643 0.2140  -0.1229 335 LYS D CB  
15063 C CG  . LYS D 335 ? 1.3821 0.8518 1.1384 -0.0764 0.2226  -0.1521 335 LYS D CG  
15064 C CD  . LYS D 335 ? 1.4837 0.9404 1.2243 -0.1052 0.2196  -0.1692 335 LYS D CD  
15065 C CE  . LYS D 335 ? 1.4070 0.8471 1.1235 -0.1169 0.2303  -0.2010 335 LYS D CE  
15066 N NZ  . LYS D 335 ? 1.3016 0.7548 1.0008 -0.1470 0.2211  -0.2192 335 LYS D NZ  
15067 N N   . LYS D 336 ? 1.2859 0.7706 1.0942 -0.0646 0.1940  -0.0755 336 LYS D N   
15068 C CA  . LYS D 336 ? 1.3192 0.7831 1.1344 -0.0679 0.1927  -0.0596 336 LYS D CA  
15069 C C   . LYS D 336 ? 1.3033 0.7966 1.1153 -0.0881 0.1794  -0.0557 336 LYS D C   
15070 O O   . LYS D 336 ? 1.3350 0.8080 1.1440 -0.1047 0.1816  -0.0558 336 LYS D O   
15071 C CB  . LYS D 336 ? 1.1990 0.6648 1.0319 -0.0423 0.1911  -0.0352 336 LYS D CB  
15072 C CG  . LYS D 336 ? 1.2995 0.7223 1.1386 -0.0231 0.2062  -0.0339 336 LYS D CG  
15073 C CD  . LYS D 336 ? 1.4544 0.8611 1.3048 -0.0089 0.2048  -0.0081 336 LYS D CD  
15074 C CE  . LYS D 336 ? 1.5324 0.9381 1.3997 0.0221  0.2090  0.0032  336 LYS D CE  
15075 N NZ  . LYS D 336 ? 1.4893 0.9257 1.3702 0.0361  0.1956  0.0287  336 LYS D NZ  
15076 N N   . ILE D 337 ? 1.1825 0.7232 0.9960 -0.0870 0.1667  -0.0523 337 ILE D N   
15077 C CA  . ILE D 337 ? 1.2524 0.8244 1.0639 -0.1042 0.1545  -0.0500 337 ILE D CA  
15078 C C   . ILE D 337 ? 1.3088 0.8737 1.1073 -0.1296 0.1567  -0.0714 337 ILE D C   
15079 O O   . ILE D 337 ? 1.2772 0.8455 1.0769 -0.1473 0.1533  -0.0702 337 ILE D O   
15080 C CB  . ILE D 337 ? 1.2025 0.8222 1.0162 -0.0969 0.1425  -0.0450 337 ILE D CB  
15081 C CG1 . ILE D 337 ? 1.1424 0.7701 0.9703 -0.0743 0.1404  -0.0261 337 ILE D CG1 
15082 C CG2 . ILE D 337 ? 1.0096 0.6623 0.8229 -0.1118 0.1304  -0.0422 337 ILE D CG2 
15083 C CD1 . ILE D 337 ? 1.0167 0.6845 0.8470 -0.0675 0.1314  -0.0223 337 ILE D CD1 
15084 N N   . HIS D 338 ? 1.2654 0.8220 1.0514 -0.1325 0.1628  -0.0922 338 HIS D N   
15085 C CA  . HIS D 338 ? 1.3118 0.8655 1.0840 -0.1576 0.1637  -0.1156 338 HIS D CA  
15086 C C   . HIS D 338 ? 1.3322 0.8419 1.1057 -0.1734 0.1739  -0.1201 338 HIS D C   
15087 O O   . HIS D 338 ? 1.3189 0.8379 1.0919 -0.1969 0.1697  -0.1265 338 HIS D O   
15088 C CB  . HIS D 338 ? 1.3951 0.9432 1.1510 -0.1556 0.1704  -0.1372 338 HIS D CB  
15089 C CG  . HIS D 338 ? 1.4067 0.9772 1.1460 -0.1785 0.1641  -0.1597 338 HIS D CG  
15090 N ND1 . HIS D 338 ? 1.3872 1.0089 1.1253 -0.1848 0.1479  -0.1557 338 HIS D ND1 
15091 C CD2 . HIS D 338 ? 1.3112 0.8612 1.0343 -0.1964 0.1713  -0.1868 338 HIS D CD2 
15092 C CE1 . HIS D 338 ? 1.3722 1.0075 1.0947 -0.2049 0.1442  -0.1784 338 HIS D CE1 
15093 N NE2 . HIS D 338 ? 1.3815 0.9743 1.0940 -0.2134 0.1580  -0.1985 338 HIS D NE2 
15094 N N   . GLU D 339 ? 1.3691 0.8306 1.1454 -0.1604 0.1882  -0.1164 339 GLU D N   
15095 C CA  . GLU D 339 ? 1.3839 0.7961 1.1609 -0.1732 0.2002  -0.1180 339 GLU D CA  
15096 C C   . GLU D 339 ? 1.3347 0.7496 1.1238 -0.1738 0.1958  -0.0926 339 GLU D C   
15097 O O   . GLU D 339 ? 1.3998 0.7808 1.1889 -0.1897 0.2043  -0.0922 339 GLU D O   
15098 C CB  . GLU D 339 ? 1.3774 0.7355 1.1534 -0.1555 0.2175  -0.1202 339 GLU D CB  
15099 C CG  . GLU D 339 ? 1.4488 0.8039 1.2125 -0.1508 0.2240  -0.1443 339 GLU D CG  
15100 C CD  . GLU D 339 ? 1.4905 0.8313 1.2619 -0.1185 0.2325  -0.1346 339 GLU D CD  
15101 O OE1 . GLU D 339 ? 1.4354 0.7730 1.1977 -0.1121 0.2401  -0.1530 339 GLU D OE1 
15102 O OE2 . GLU D 339 ? 1.4524 0.7883 1.2391 -0.0993 0.2314  -0.1090 339 GLU D OE2 
15103 N N   . SER D 340 ? 1.3477 0.8011 1.1460 -0.1579 0.1837  -0.0721 340 SER D N   
15104 C CA  . SER D 340 ? 1.3176 0.7754 1.1249 -0.1571 0.1798  -0.0483 340 SER D CA  
15105 C C   . SER D 340 ? 1.2892 0.7776 1.0973 -0.1827 0.1720  -0.0519 340 SER D C   
15106 O O   . SER D 340 ? 1.3136 0.7937 1.1262 -0.1904 0.1742  -0.0377 340 SER D O   
15107 C CB  . SER D 340 ? 1.2328 0.7208 1.0492 -0.1315 0.1700  -0.0273 340 SER D CB  
15108 O OG  . SER D 340 ? 1.1535 0.6890 0.9736 -0.1382 0.1564  -0.0207 340 SER D OG  
15109 N N   . VAL D 341 ? 1.3026 0.8283 1.1067 -0.1954 0.1632  -0.0697 341 VAL D N   
15110 C CA  . VAL D 341 ? 1.2453 0.8104 1.0537 -0.2162 0.1537  -0.0722 341 VAL D CA  
15111 C C   . VAL D 341 ? 1.3468 0.9116 1.1480 -0.2435 0.1556  -0.0998 341 VAL D C   
15112 O O   . VAL D 341 ? 1.3828 0.9354 1.1726 -0.2433 0.1589  -0.1187 341 VAL D O   
15113 C CB  . VAL D 341 ? 1.2409 0.8623 1.0535 -0.2040 0.1379  -0.0643 341 VAL D CB  
15114 C CG1 . VAL D 341 ? 1.3154 0.9395 1.1359 -0.1814 0.1355  -0.0389 341 VAL D CG1 
15115 C CG2 . VAL D 341 ? 1.2080 0.8435 1.0111 -0.1951 0.1339  -0.0782 341 VAL D CG2 
15116 N N   . ASP D 342 ? 1.3847 0.9660 1.1928 -0.2680 0.1537  -0.1027 342 ASP D N   
15117 C CA  . ASP D 342 ? 1.3469 0.9352 1.1511 -0.2977 0.1538  -0.1294 342 ASP D CA  
15118 C C   . ASP D 342 ? 1.3779 1.0291 1.1812 -0.3015 0.1367  -0.1404 342 ASP D C   
15119 O O   . ASP D 342 ? 1.4923 1.1538 1.2877 -0.3204 0.1342  -0.1653 342 ASP D O   
15120 C CB  . ASP D 342 ? 1.3210 0.9000 1.1357 -0.3243 0.1606  -0.1280 342 ASP D CB  
15121 C CG  . ASP D 342 ? 1.4233 1.0629 1.2523 -0.3315 0.1479  -0.1191 342 ASP D CG  
15122 O OD1 . ASP D 342 ? 1.4443 1.1293 1.2763 -0.3474 0.1372  -0.1361 342 ASP D OD1 
15123 O OD2 . ASP D 342 ? 1.5477 1.1911 1.3848 -0.3201 0.1485  -0.0950 342 ASP D OD2 
15124 N N   . PHE D 343 ? 1.3363 1.0295 1.1470 -0.2842 0.1249  -0.1225 343 PHE D N   
15125 C CA  . PHE D 343 ? 1.3002 1.0514 1.1101 -0.2829 0.1089  -0.1285 343 PHE D CA  
15126 C C   . PHE D 343 ? 1.2017 0.9523 0.9964 -0.2621 0.1060  -0.1318 343 PHE D C   
15127 O O   . PHE D 343 ? 1.1938 0.9032 0.9819 -0.2480 0.1162  -0.1289 343 PHE D O   
15128 C CB  . PHE D 343 ? 1.2151 1.0084 1.0402 -0.2740 0.0994  -0.1081 343 PHE D CB  
15129 C CG  . PHE D 343 ? 1.2386 1.0091 1.0686 -0.2529 0.1048  -0.0837 343 PHE D CG  
15130 C CD1 . PHE D 343 ? 1.2117 0.9460 1.0469 -0.2592 0.1165  -0.0738 343 PHE D CD1 
15131 C CD2 . PHE D 343 ? 1.2267 1.0138 1.0556 -0.2273 0.0979  -0.0703 343 PHE D CD2 
15132 C CE1 . PHE D 343 ? 1.2439 0.9616 1.0816 -0.2391 0.1197  -0.0512 343 PHE D CE1 
15133 C CE2 . PHE D 343 ? 1.1269 0.8973 0.9603 -0.2091 0.1014  -0.0498 343 PHE D CE2 
15134 C CZ  . PHE D 343 ? 1.1266 0.8643 0.9639 -0.2145 0.1114  -0.0403 343 PHE D CZ  
15135 N N   . GLN D 344 ? 1.2085 1.0060 0.9977 -0.2600 0.0927  -0.1376 344 GLN D N   
15136 C CA  . GLN D 344 ? 1.2205 1.0217 0.9952 -0.2394 0.0902  -0.1368 344 GLN D CA  
15137 C C   . GLN D 344 ? 1.1438 0.9551 0.9281 -0.2143 0.0870  -0.1113 344 GLN D C   
15138 O O   . GLN D 344 ? 1.1111 0.9625 0.9041 -0.2105 0.0761  -0.1008 344 GLN D O   
15139 C CB  . GLN D 344 ? 1.2129 1.0581 0.9747 -0.2456 0.0777  -0.1511 344 GLN D CB  
15140 C CG  . GLN D 344 ? 1.2660 1.0908 1.0058 -0.2551 0.0835  -0.1759 344 GLN D CG  
15141 C CD  . GLN D 344 ? 1.2038 1.0753 0.9291 -0.2645 0.0698  -0.1910 344 GLN D CD  
15142 O OE1 . GLN D 344 ? 1.1551 1.0751 0.8890 -0.2641 0.0557  -0.1827 344 GLN D OE1 
15143 N NE2 . GLN D 344 ? 1.2487 1.1065 0.9513 -0.2726 0.0741  -0.2138 344 GLN D NE2 
15144 N N   . PRO D 345 ? 1.1931 0.9697 0.9770 -0.1970 0.0963  -0.1016 345 PRO D N   
15145 C CA  . PRO D 345 ? 1.1730 0.9573 0.9679 -0.1763 0.0936  -0.0786 345 PRO D CA  
15146 C C   . PRO D 345 ? 1.0963 0.9118 0.8856 -0.1610 0.0854  -0.0736 345 PRO D C   
15147 O O   . PRO D 345 ? 1.1339 0.9496 0.9081 -0.1585 0.0866  -0.0843 345 PRO D O   
15148 C CB  . PRO D 345 ? 1.1657 0.9043 0.9620 -0.1644 0.1062  -0.0731 345 PRO D CB  
15149 C CG  . PRO D 345 ? 1.1870 0.9030 0.9681 -0.1697 0.1141  -0.0934 345 PRO D CG  
15150 C CD  . PRO D 345 ? 1.2006 0.9304 0.9753 -0.1952 0.1100  -0.1121 345 PRO D CD  
15151 N N   . VAL D 346 ? 1.0033 0.8436 0.8034 -0.1510 0.0780  -0.0571 346 VAL D N   
15152 C CA  . VAL D 346 ? 1.0094 0.8718 0.8064 -0.1342 0.0723  -0.0481 346 VAL D CA  
15153 C C   . VAL D 346 ? 0.9945 0.8387 0.8008 -0.1172 0.0774  -0.0330 346 VAL D C   
15154 O O   . VAL D 346 ? 1.0105 0.8528 0.8294 -0.1153 0.0767  -0.0217 346 VAL D O   
15155 C CB  . VAL D 346 ? 0.9672 0.8721 0.7691 -0.1348 0.0603  -0.0424 346 VAL D CB  
15156 C CG1 . VAL D 346 ? 1.0059 0.9173 0.8253 -0.1344 0.0587  -0.0299 346 VAL D CG1 
15157 C CG2 . VAL D 346 ? 0.9523 0.8745 0.7470 -0.1185 0.0560  -0.0346 346 VAL D CG2 
15158 N N   . VAL D 347 ? 1.0657 0.8977 0.8657 -0.1057 0.0829  -0.0336 347 VAL D N   
15159 C CA  . VAL D 347 ? 1.0114 0.8292 0.8217 -0.0903 0.0877  -0.0215 347 VAL D CA  
15160 C C   . VAL D 347 ? 1.0069 0.8468 0.8174 -0.0784 0.0833  -0.0126 347 VAL D C   
15161 O O   . VAL D 347 ? 1.0649 0.9121 0.8631 -0.0760 0.0846  -0.0176 347 VAL D O   
15162 C CB  . VAL D 347 ? 0.9747 0.7616 0.7820 -0.0856 0.0993  -0.0285 347 VAL D CB  
15163 C CG1 . VAL D 347 ? 1.0286 0.8052 0.8509 -0.0705 0.1027  -0.0153 347 VAL D CG1 
15164 C CG2 . VAL D 347 ? 0.9713 0.7324 0.7747 -0.0989 0.1050  -0.0400 347 VAL D CG2 
15165 N N   . PHE D 348 ? 0.9554 0.8044 0.7787 -0.0715 0.0791  0.0005  348 PHE D N   
15166 C CA  . PHE D 348 ? 0.9147 0.7801 0.7405 -0.0611 0.0759  0.0096  348 PHE D CA  
15167 C C   . PHE D 348 ? 0.8926 0.7452 0.7289 -0.0503 0.0816  0.0159  348 PHE D C   
15168 O O   . PHE D 348 ? 0.8976 0.7431 0.7456 -0.0479 0.0811  0.0218  348 PHE D O   
15169 C CB  . PHE D 348 ? 0.9713 0.8561 0.8044 -0.0612 0.0677  0.0176  348 PHE D CB  
15170 C CG  . PHE D 348 ? 0.8567 0.7659 0.6817 -0.0639 0.0610  0.0159  348 PHE D CG  
15171 C CD1 . PHE D 348 ? 0.8765 0.7943 0.6940 -0.0759 0.0580  0.0058  348 PHE D CD1 
15172 C CD2 . PHE D 348 ? 0.8348 0.7588 0.6604 -0.0543 0.0577  0.0245  348 PHE D CD2 
15173 C CE1 . PHE D 348 ? 0.8877 0.8331 0.6991 -0.0771 0.0503  0.0048  348 PHE D CE1 
15174 C CE2 . PHE D 348 ? 0.7856 0.7328 0.6042 -0.0539 0.0511  0.0249  348 PHE D CE2 
15175 C CZ  . PHE D 348 ? 0.8854 0.8459 0.6972 -0.0648 0.0467  0.0153  348 PHE D CZ  
15176 N N   . VAL D 349 ? 0.8925 0.7446 0.7247 -0.0442 0.0871  0.0148  349 VAL D N   
15177 C CA  . VAL D 349 ? 0.9248 0.7704 0.7696 -0.0347 0.0930  0.0197  349 VAL D CA  
15178 C C   . VAL D 349 ? 0.9471 0.8075 0.7953 -0.0298 0.0909  0.0278  349 VAL D C   
15179 O O   . VAL D 349 ? 0.8865 0.7520 0.7241 -0.0286 0.0943  0.0275  349 VAL D O   
15180 C CB  . VAL D 349 ? 0.9199 0.7528 0.7599 -0.0320 0.1037  0.0115  349 VAL D CB  
15181 C CG1 . VAL D 349 ? 0.9463 0.7809 0.8017 -0.0222 0.1097  0.0170  349 VAL D CG1 
15182 C CG2 . VAL D 349 ? 1.0066 0.8187 0.8459 -0.0355 0.1073  0.0038  349 VAL D CG2 
15183 N N   . VAL D 350 ? 0.9813 0.8470 0.8427 -0.0272 0.0858  0.0353  350 VAL D N   
15184 C CA  . VAL D 350 ? 0.9640 0.8402 0.8292 -0.0239 0.0838  0.0420  350 VAL D CA  
15185 C C   . VAL D 350 ? 0.9393 0.8149 0.8220 -0.0194 0.0863  0.0453  350 VAL D C   
15186 O O   . VAL D 350 ? 0.9431 0.8178 0.8363 -0.0183 0.0827  0.0466  350 VAL D O   
15187 C CB  . VAL D 350 ? 0.9062 0.7918 0.7704 -0.0260 0.0753  0.0454  350 VAL D CB  
15188 C CG1 . VAL D 350 ? 0.8724 0.7641 0.7403 -0.0217 0.0747  0.0514  350 VAL D CG1 
15189 C CG2 . VAL D 350 ? 0.9036 0.7955 0.7539 -0.0312 0.0718  0.0414  350 VAL D CG2 
15190 N N   . LEU D 351 ? 0.8895 0.7673 0.7754 -0.0171 0.0925  0.0472  351 LEU D N   
15191 C CA  . LEU D 351 ? 0.8700 0.7520 0.7750 -0.0148 0.0948  0.0492  351 LEU D CA  
15192 C C   . LEU D 351 ? 0.9144 0.7982 0.8192 -0.0156 0.1009  0.0525  351 LEU D C   
15193 O O   . LEU D 351 ? 0.9065 0.7871 0.7950 -0.0159 0.1039  0.0545  351 LEU D O   
15194 C CB  . LEU D 351 ? 0.8291 0.7091 0.7449 -0.0111 0.1005  0.0458  351 LEU D CB  
15195 C CG  . LEU D 351 ? 0.9589 0.8337 0.8662 -0.0100 0.1116  0.0416  351 LEU D CG  
15196 C CD1 . LEU D 351 ? 0.9028 0.7814 0.8290 -0.0046 0.1194  0.0395  351 LEU D CD1 
15197 C CD2 . LEU D 351 ? 1.0036 0.8677 0.8920 -0.0121 0.1110  0.0359  351 LEU D CD2 
15198 N N   . ASP D 352 ? 0.9284 0.8179 0.8515 -0.0163 0.1026  0.0534  352 ASP D N   
15199 C CA  . ASP D 352 ? 0.8752 0.7635 0.8007 -0.0189 0.1105  0.0565  352 ASP D CA  
15200 C C   . ASP D 352 ? 0.9275 0.8148 0.8499 -0.0183 0.1228  0.0561  352 ASP D C   
15201 O O   . ASP D 352 ? 0.9517 0.8445 0.8856 -0.0160 0.1264  0.0519  352 ASP D O   
15202 C CB  . ASP D 352 ? 0.8481 0.7444 0.7959 -0.0225 0.1092  0.0552  352 ASP D CB  
15203 C CG  . ASP D 352 ? 0.9023 0.8008 0.8515 -0.0231 0.0977  0.0540  352 ASP D CG  
15204 O OD1 . ASP D 352 ? 0.8835 0.7764 0.8171 -0.0211 0.0926  0.0558  352 ASP D OD1 
15205 O OD2 . ASP D 352 ? 0.9481 0.8563 0.9142 -0.0259 0.0939  0.0509  352 ASP D OD2 
15206 N N   . GLY D 353 ? 0.9535 0.8339 0.8599 -0.0191 0.1298  0.0610  353 GLY D N   
15207 C CA  . GLY D 353 ? 0.9440 0.8230 0.8410 -0.0185 0.1423  0.0612  353 GLY D CA  
15208 C C   . GLY D 353 ? 0.9464 0.8290 0.8588 -0.0223 0.1553  0.0634  353 GLY D C   
15209 O O   . GLY D 353 ? 0.9964 0.8780 0.8988 -0.0222 0.1676  0.0647  353 GLY D O   
15210 N N   . GLU D 354 ? 0.9414 0.8297 0.8777 -0.0268 0.1537  0.0630  354 GLU D N   
15211 C CA  . GLU D 354 ? 0.8655 0.7588 0.8189 -0.0332 0.1666  0.0644  354 GLU D CA  
15212 C C   . GLU D 354 ? 0.9038 0.8166 0.8908 -0.0359 0.1648  0.0577  354 GLU D C   
15213 O O   . GLU D 354 ? 0.9429 0.8661 0.9476 -0.0409 0.1769  0.0570  354 GLU D O   
15214 C CB  . GLU D 354 ? 0.8614 0.7413 0.8108 -0.0394 0.1695  0.0713  354 GLU D CB  
15215 C CG  . GLU D 354 ? 0.9132 0.7936 0.8764 -0.0427 0.1578  0.0676  354 GLU D CG  
15216 C CD  . GLU D 354 ? 0.9679 0.8397 0.9123 -0.0362 0.1451  0.0691  354 GLU D CD  
15217 O OE1 . GLU D 354 ? 1.0165 0.8960 0.9576 -0.0309 0.1360  0.0652  354 GLU D OE1 
15218 O OE2 . GLU D 354 ? 0.9014 0.7584 0.8353 -0.0362 0.1452  0.0743  354 GLU D OE2 
15219 N N   . ASN D 355 ? 0.8780 0.7983 0.8745 -0.0326 0.1506  0.0533  355 ASN D N   
15220 C CA  . ASN D 355 ? 0.8503 0.7921 0.8780 -0.0347 0.1464  0.0482  355 ASN D CA  
15221 C C   . ASN D 355 ? 0.7436 0.7004 0.7852 -0.0260 0.1481  0.0449  355 ASN D C   
15222 O O   . ASN D 355 ? 0.8523 0.8317 0.9227 -0.0270 0.1499  0.0418  355 ASN D O   
15223 C CB  . ASN D 355 ? 0.9238 0.8673 0.9534 -0.0353 0.1301  0.0462  355 ASN D CB  
15224 C CG  . ASN D 355 ? 0.8892 0.8156 0.9046 -0.0416 0.1289  0.0485  355 ASN D CG  
15225 O OD1 . ASN D 355 ? 0.8320 0.7535 0.8531 -0.0501 0.1379  0.0493  355 ASN D OD1 
15226 N ND2 . ASN D 355 ? 0.8676 0.7843 0.8656 -0.0373 0.1186  0.0497  355 ASN D ND2 
15227 N N   . CYS D 356 ? 0.7925 0.7379 0.8157 -0.0175 0.1478  0.0449  356 CYS D N   
15228 C CA  . CYS D 356 ? 0.7919 0.7470 0.8284 -0.0077 0.1498  0.0414  356 CYS D CA  
15229 C C   . CYS D 356 ? 0.8473 0.8095 0.8914 -0.0063 0.1674  0.0392  356 CYS D C   
15230 O O   . CYS D 356 ? 0.8539 0.8305 0.9185 0.0020  0.1713  0.0360  356 CYS D O   
15231 C CB  . CYS D 356 ? 0.7896 0.7267 0.8044 -0.0003 0.1445  0.0406  356 CYS D CB  
15232 S SG  . CYS D 356 ? 0.8802 0.7947 0.8574 -0.0035 0.1514  0.0403  356 CYS D SG  
15233 N N   . TRP D 357 ? 0.8515 0.8046 0.8795 -0.0133 0.1788  0.0416  357 TRP D N   
15234 C CA  . TRP D 357 ? 0.9270 0.8831 0.9533 -0.0115 0.1970  0.0396  357 TRP D CA  
15235 C C   . TRP D 357 ? 0.8573 0.8393 0.9182 -0.0153 0.2077  0.0385  357 TRP D C   
15236 O O   . TRP D 357 ? 0.7882 0.7818 0.8603 -0.0093 0.2207  0.0346  357 TRP D O   
15237 C CB  . TRP D 357 ? 0.9278 0.8656 0.9207 -0.0169 0.2051  0.0443  357 TRP D CB  
15238 C CG  . TRP D 357 ? 0.9467 0.8652 0.9088 -0.0140 0.1934  0.0448  357 TRP D CG  
15239 C CD1 . TRP D 357 ? 0.9572 0.8629 0.8984 -0.0184 0.1866  0.0512  357 TRP D CD1 
15240 C CD2 . TRP D 357 ? 0.9497 0.8604 0.9004 -0.0066 0.1879  0.0382  357 TRP D CD2 
15241 N NE1 . TRP D 357 ? 0.9812 0.8764 0.9005 -0.0146 0.1765  0.0488  357 TRP D NE1 
15242 C CE2 . TRP D 357 ? 0.9831 0.8797 0.9072 -0.0086 0.1774  0.0405  357 TRP D CE2 
15243 C CE3 . TRP D 357 ? 1.0224 0.9357 0.9837 0.0019  0.1916  0.0307  357 TRP D CE3 
15244 C CZ2 . TRP D 357 ? 1.0087 0.8950 0.9173 -0.0052 0.1706  0.0345  357 TRP D CZ2 
15245 C CZ3 . TRP D 357 ? 1.0539 0.9517 0.9978 0.0061  0.1855  0.0252  357 TRP D CZ3 
15246 C CH2 . TRP D 357 ? 0.9735 0.8586 0.8916 0.0012  0.1751  0.0267  357 TRP D CH2 
15247 N N   . GLU D 358 ? 0.8722 0.8645 0.9515 -0.0255 0.2030  0.0407  358 GLU D N   
15248 C CA  . GLU D 358 ? 0.7397 0.7605 0.8554 -0.0315 0.2124  0.0384  358 GLU D CA  
15249 C C   . GLU D 358 ? 0.7654 0.8127 0.9109 -0.0195 0.2083  0.0331  358 GLU D C   
15250 O O   . GLU D 358 ? 0.8011 0.8738 0.9740 -0.0186 0.2208  0.0302  358 GLU D O   
15251 C CB  . GLU D 358 ? 0.7795 0.8064 0.9105 -0.0457 0.2055  0.0390  358 GLU D CB  
15252 C CG  . GLU D 358 ? 0.8448 0.8604 0.9646 -0.0443 0.1851  0.0390  358 GLU D CG  
15253 C CD  . GLU D 358 ? 0.9004 0.9085 1.0213 -0.0589 0.1821  0.0396  358 GLU D CD  
15254 O OE1 . GLU D 358 ? 0.9108 0.8940 1.0091 -0.0646 0.1910  0.0453  358 GLU D OE1 
15255 O OE2 . GLU D 358 ? 0.9416 0.9678 1.0848 -0.0641 0.1710  0.0342  358 GLU D OE2 
15256 N N   . TYR D 359 ? 0.7099 0.7522 0.8508 -0.0095 0.1917  0.0327  359 TYR D N   
15257 C CA  . TYR D 359 ? 0.6987 0.7629 0.8657 0.0046  0.1867  0.0302  359 TYR D CA  
15258 C C   . TYR D 359 ? 0.7439 0.7956 0.8997 0.0189  0.1976  0.0277  359 TYR D C   
15259 O O   . TYR D 359 ? 0.7155 0.7854 0.8957 0.0325  0.1991  0.0257  359 TYR D O   
15260 C CB  . TYR D 359 ? 0.7506 0.8138 0.9168 0.0090  0.1650  0.0324  359 TYR D CB  
15261 C CG  . TYR D 359 ? 0.7667 0.8438 0.9444 -0.0046 0.1542  0.0322  359 TYR D CG  
15262 C CD1 . TYR D 359 ? 0.7273 0.8426 0.9422 -0.0064 0.1487  0.0294  359 TYR D CD1 
15263 C CD2 . TYR D 359 ? 0.7609 0.8141 0.9128 -0.0156 0.1496  0.0338  359 TYR D CD2 
15264 C CE1 . TYR D 359 ? 0.7809 0.9083 1.0052 -0.0206 0.1389  0.0266  359 TYR D CE1 
15265 C CE2 . TYR D 359 ? 0.8062 0.8686 0.9674 -0.0280 0.1410  0.0318  359 TYR D CE2 
15266 C CZ  . TYR D 359 ? 0.9046 1.0032 1.1012 -0.0315 0.1358  0.0273  359 TYR D CZ  
15267 O OH  . TYR D 359 ? 0.9573 1.0645 1.1620 -0.0455 0.1274  0.0227  359 TYR D OH  
15268 N N   . TYR D 360 ? 0.7672 0.7893 0.8871 0.0167  0.2049  0.0273  360 TYR D N   
15269 C CA  . TYR D 360 ? 0.7447 0.7553 0.8524 0.0272  0.2185  0.0222  360 TYR D CA  
15270 C C   . TYR D 360 ? 0.9595 0.9906 1.0844 0.0257  0.2396  0.0193  360 TYR D C   
15271 O O   . TYR D 360 ? 0.9317 0.9750 1.0644 0.0126  0.2458  0.0224  360 TYR D O   
15272 C CB  . TYR D 360 ? 0.8230 0.8006 0.8863 0.0231  0.2196  0.0213  360 TYR D CB  
15273 C CG  . TYR D 360 ? 0.9437 0.8982 0.9876 0.0284  0.2054  0.0205  360 TYR D CG  
15274 C CD1 . TYR D 360 ? 0.9196 0.8725 0.9646 0.0247  0.1872  0.0260  360 TYR D CD1 
15275 C CD2 . TYR D 360 ? 0.9084 0.8416 0.9310 0.0352  0.2114  0.0134  360 TYR D CD2 
15276 C CE1 . TYR D 360 ? 0.9931 0.9257 1.0206 0.0279  0.1758  0.0260  360 TYR D CE1 
15277 C CE2 . TYR D 360 ? 0.9788 0.8899 0.9845 0.0373  0.1997  0.0124  360 TYR D CE2 
15278 C CZ  . TYR D 360 ? 0.9619 0.8734 0.9706 0.0336  0.1821  0.0195  360 TYR D CZ  
15279 O OH  . TYR D 360 ? 0.8956 0.7865 0.8884 0.0344  0.1719  0.0193  360 TYR D OH  
15280 N N   . GLU D 361 ? 1.0738 1.1065 1.2039 0.0391  0.2522  0.0129  361 GLU D N   
15281 C CA  . GLU D 361 ? 0.9426 0.9938 1.0857 0.0392  0.2749  0.0091  361 GLU D CA  
15282 C C   . GLU D 361 ? 0.9307 0.9601 1.0337 0.0298  0.2884  0.0085  361 GLU D C   
15283 O O   . GLU D 361 ? 0.9587 0.9591 1.0252 0.0324  0.2858  0.0052  361 GLU D O   
15284 C CB  . GLU D 361 ? 0.9829 1.0412 1.1432 0.0586  0.2848  0.0016  361 GLU D CB  
15285 C CG  . GLU D 361 ? 1.0780 1.1547 1.2734 0.0719  0.2702  0.0040  361 GLU D CG  
15286 C CD  . GLU D 361 ? 1.1719 1.2965 1.4163 0.0718  0.2741  0.0055  361 GLU D CD  
15287 O OE1 . GLU D 361 ? 1.2530 1.3950 1.5059 0.0625  0.2919  0.0034  361 GLU D OE1 
15288 O OE2 . GLU D 361 ? 1.1536 1.3004 1.4281 0.0806  0.2591  0.0090  361 GLU D OE2 
15289 N N   . GLU D 362 ? 0.9239 0.9689 1.0340 0.0186  0.3034  0.0119  362 GLU D N   
15290 C CA  . GLU D 362 ? 1.0017 1.0290 1.0738 0.0088  0.3161  0.0151  362 GLU D CA  
15291 C C   . GLU D 362 ? 1.0274 1.0259 1.0637 0.0021  0.2990  0.0212  362 GLU D C   
15292 O O   . GLU D 362 ? 1.0585 1.0338 1.0560 0.0046  0.2979  0.0188  362 GLU D O   
15293 C CB  . GLU D 362 ? 1.0740 1.0937 1.1245 0.0182  0.3342  0.0060  362 GLU D CB  
15294 C CG  . GLU D 362 ? 1.1371 1.1414 1.1448 0.0092  0.3476  0.0097  362 GLU D CG  
15295 C CD  . GLU D 362 ? 1.0768 1.0928 1.0819 0.0129  0.3744  0.0032  362 GLU D CD  
15296 O OE1 . GLU D 362 ? 1.2678 1.3081 1.3110 0.0213  0.3844  -0.0031 362 GLU D OE1 
15297 O OE2 . GLU D 362 ? 1.0277 1.0299 0.9918 0.0086  0.3855  0.0044  362 GLU D OE2 
15298 N N   . ASN D 363 ? 1.0724 1.0756 1.1247 -0.0063 0.2853  0.0280  363 ASN D N   
15299 C CA  . ASN D 363 ? 0.9117 0.8930 0.9397 -0.0120 0.2683  0.0342  363 ASN D CA  
15300 C C   . ASN D 363 ? 0.9399 0.8989 0.9373 -0.0039 0.2569  0.0300  363 ASN D C   
15301 O O   . ASN D 363 ? 1.0573 0.9978 1.0248 -0.0082 0.2486  0.0347  363 ASN D O   
15302 C CB  . ASN D 363 ? 0.8147 0.7843 0.8193 -0.0236 0.2777  0.0438  363 ASN D CB  
15303 C CG  . ASN D 363 ? 0.8181 0.7790 0.8243 -0.0323 0.2640  0.0512  363 ASN D CG  
15304 O OD1 . ASN D 363 ? 0.7824 0.7577 0.8206 -0.0361 0.2557  0.0496  363 ASN D OD1 
15305 N ND2 . ASN D 363 ? 0.9354 0.8737 0.9068 -0.0349 0.2613  0.0589  363 ASN D ND2 
15306 N N   . GLY D 364 ? 0.8633 0.8241 0.8697 0.0078  0.2565  0.0213  364 GLY D N   
15307 C CA  . GLY D 364 ? 0.9785 0.9172 0.9579 0.0139  0.2490  0.0152  364 GLY D CA  
15308 C C   . GLY D 364 ? 0.9748 0.8983 0.9148 0.0124  0.2598  0.0107  364 GLY D C   
15309 O O   . GLY D 364 ? 1.0302 0.9353 0.9449 0.0140  0.2520  0.0049  364 GLY D O   
15310 N N   . ILE D 365 ? 0.9349 0.8663 0.8676 0.0082  0.2774  0.0130  365 ILE D N   
15311 C CA  . ILE D 365 ? 1.0053 0.9248 0.8973 0.0075  0.2881  0.0083  365 ILE D CA  
15312 C C   . ILE D 365 ? 1.0794 0.9900 0.9642 0.0170  0.2936  -0.0075 365 ILE D C   
15313 O O   . ILE D 365 ? 1.0766 0.9707 0.9253 0.0156  0.2906  -0.0146 365 ILE D O   
15314 C CB  . ILE D 365 ? 1.0189 0.9495 0.9057 0.0020  0.3083  0.0148  365 ILE D CB  
15315 C CG1 . ILE D 365 ? 1.0275 0.9585 0.9160 -0.0082 0.3027  0.0307  365 ILE D CG1 
15316 C CG2 . ILE D 365 ? 0.9708 0.8921 0.8139 0.0024  0.3206  0.0092  365 ILE D CG2 
15317 C CD1 . ILE D 365 ? 1.0719 1.0225 0.9989 -0.0131 0.3131  0.0355  365 ILE D CD1 
15318 N N   . PRO D 366 ? 1.0886 1.0091 1.0054 0.0268  0.3022  -0.0143 366 PRO D N   
15319 C CA  . PRO D 366 ? 1.0289 0.9341 0.9376 0.0369  0.3071  -0.0297 366 PRO D CA  
15320 C C   . PRO D 366 ? 1.0325 0.9152 0.9289 0.0367  0.2879  -0.0328 366 PRO D C   
15321 O O   . PRO D 366 ? 1.0874 0.9500 0.9553 0.0367  0.2897  -0.0452 366 PRO D O   
15322 C CB  . PRO D 366 ? 0.9560 0.8793 0.9092 0.0492  0.3167  -0.0318 366 PRO D CB  
15323 C CG  . PRO D 366 ? 0.9686 0.9197 0.9423 0.0428  0.3259  -0.0218 366 PRO D CG  
15324 C CD  . PRO D 366 ? 0.9947 0.9419 0.9546 0.0293  0.3109  -0.0095 366 PRO D CD  
15325 N N   . PHE D 367 ? 0.9952 0.8813 0.9119 0.0353  0.2701  -0.0228 367 PHE D N   
15326 C CA  . PHE D 367 ? 1.0103 0.8764 0.9182 0.0349  0.2532  -0.0248 367 PHE D CA  
15327 C C   . PHE D 367 ? 1.0104 0.8644 0.8792 0.0234  0.2447  -0.0257 367 PHE D C   
15328 O O   . PHE D 367 ? 1.0723 0.9073 0.9184 0.0218  0.2429  -0.0369 367 PHE D O   
15329 C CB  . PHE D 367 ? 0.9877 0.8637 0.9251 0.0361  0.2373  -0.0133 367 PHE D CB  
15330 C CG  . PHE D 367 ? 0.9418 0.7994 0.8692 0.0338  0.2203  -0.0126 367 PHE D CG  
15331 C CD1 . PHE D 367 ? 1.0527 0.8898 0.9798 0.0413  0.2210  -0.0206 367 PHE D CD1 
15332 C CD2 . PHE D 367 ? 0.9315 0.7913 0.8506 0.0243  0.2050  -0.0040 367 PHE D CD2 
15333 C CE1 . PHE D 367 ? 1.0195 0.8394 0.9378 0.0375  0.2069  -0.0192 367 PHE D CE1 
15334 C CE2 . PHE D 367 ? 0.9551 0.8007 0.8663 0.0216  0.1909  -0.0033 367 PHE D CE2 
15335 C CZ  . PHE D 367 ? 0.9199 0.7460 0.8306 0.0273  0.1919  -0.0106 367 PHE D CZ  
15336 N N   . LEU D 368 ? 0.9879 0.8530 0.8495 0.0154  0.2395  -0.0143 368 LEU D N   
15337 C CA  . LEU D 368 ? 1.0544 0.9125 0.8822 0.0067  0.2294  -0.0127 368 LEU D CA  
15338 C C   . LEU D 368 ? 1.0148 0.8654 0.8073 0.0049  0.2396  -0.0249 368 LEU D C   
15339 O O   . LEU D 368 ? 1.1171 0.9577 0.8844 -0.0002 0.2305  -0.0322 368 LEU D O   
15340 C CB  . LEU D 368 ? 1.0477 0.9174 0.8744 0.0012  0.2258  0.0026  368 LEU D CB  
15341 C CG  . LEU D 368 ? 0.9505 0.8232 0.7981 -0.0007 0.2095  0.0126  368 LEU D CG  
15342 C CD1 . LEU D 368 ? 0.8966 0.7754 0.7397 -0.0059 0.2083  0.0261  368 LEU D CD1 
15343 C CD2 . LEU D 368 ? 0.9432 0.8050 0.7799 -0.0026 0.1934  0.0087  368 LEU D CD2 
15344 N N   . GLU D 369 ? 1.0540 0.9110 0.8442 0.0085  0.2588  -0.0286 369 GLU D N   
15345 C CA  . GLU D 369 ? 1.1607 1.0113 0.9146 0.0069  0.2695  -0.0417 369 GLU D CA  
15346 C C   . GLU D 369 ? 1.1531 0.9848 0.9041 0.0101  0.2710  -0.0609 369 GLU D C   
15347 O O   . GLU D 369 ? 1.2695 1.0908 0.9881 0.0039  0.2674  -0.0730 369 GLU D O   
15348 C CB  . GLU D 369 ? 1.0679 0.9308 0.8207 0.0099  0.2917  -0.0405 369 GLU D CB  
15349 C CG  . GLU D 369 ? 1.0870 0.9631 0.8340 0.0044  0.2920  -0.0218 369 GLU D CG  
15350 C CD  . GLU D 369 ? 1.1807 1.0686 0.9258 0.0056  0.3156  -0.0194 369 GLU D CD  
15351 O OE1 . GLU D 369 ? 1.3120 1.2061 1.0837 0.0122  0.3300  -0.0270 369 GLU D OE1 
15352 O OE2 . GLU D 369 ? 1.3083 1.2000 1.0257 0.0006  0.3205  -0.0090 369 GLU D OE2 
15353 N N   . LYS D 370 ? 1.1022 0.9290 0.8868 0.0196  0.2760  -0.0638 370 LYS D N   
15354 C CA  . LYS D 370 ? 1.1113 0.9143 0.8952 0.0239  0.2780  -0.0801 370 LYS D CA  
15355 C C   . LYS D 370 ? 1.1995 0.9880 0.9724 0.0150  0.2584  -0.0811 370 LYS D C   
15356 O O   . LYS D 370 ? 1.2253 0.9948 0.9749 0.0095  0.2586  -0.0972 370 LYS D O   
15357 C CB  . LYS D 370 ? 1.1052 0.9078 0.9303 0.0383  0.2849  -0.0781 370 LYS D CB  
15358 C CG  . LYS D 370 ? 1.2534 1.0292 1.0792 0.0470  0.2946  -0.0952 370 LYS D CG  
15359 C CD  . LYS D 370 ? 1.2393 1.0002 1.0263 0.0416  0.3071  -0.1157 370 LYS D CD  
15360 C CE  . LYS D 370 ? 1.2008 0.9347 0.9944 0.0532  0.3221  -0.1330 370 LYS D CE  
15361 N NZ  . LYS D 370 ? 1.2158 0.9287 0.9689 0.0450  0.3309  -0.1566 370 LYS D NZ  
15362 N N   . LEU D 371 ? 1.1759 0.9736 0.9656 0.0125  0.2422  -0.0650 371 LEU D N   
15363 C CA  . LEU D 371 ? 1.1111 0.8999 0.8917 0.0034  0.2241  -0.0642 371 LEU D CA  
15364 C C   . LEU D 371 ? 1.1107 0.9032 0.8530 -0.0083 0.2192  -0.0709 371 LEU D C   
15365 O O   . LEU D 371 ? 1.1642 0.9422 0.8874 -0.0157 0.2164  -0.0857 371 LEU D O   
15366 C CB  . LEU D 371 ? 1.0959 0.8982 0.8994 0.0034  0.2097  -0.0456 371 LEU D CB  
15367 C CG  . LEU D 371 ? 1.0671 0.8661 0.8676 -0.0047 0.1911  -0.0407 371 LEU D CG  
15368 C CD1 . LEU D 371 ? 1.0439 0.8189 0.8376 -0.0086 0.1894  -0.0537 371 LEU D CD1 
15369 C CD2 . LEU D 371 ? 1.0346 0.8434 0.8638 -0.0007 0.1815  -0.0251 371 LEU D CD2 
15370 N N   . TYR D 372 ? 1.1292 0.9414 0.8597 -0.0101 0.2184  -0.0601 372 TYR D N   
15371 C CA  . TYR D 372 ? 1.1711 0.9918 0.8663 -0.0192 0.2106  -0.0621 372 TYR D CA  
15372 C C   . TYR D 372 ? 1.1796 0.9929 0.8429 -0.0228 0.2209  -0.0824 372 TYR D C   
15373 O O   . TYR D 372 ? 1.1368 0.9521 0.7735 -0.0324 0.2113  -0.0917 372 TYR D O   
15374 C CB  . TYR D 372 ? 1.0655 0.9052 0.7544 -0.0177 0.2103  -0.0443 372 TYR D CB  
15375 C CG  . TYR D 372 ? 1.1169 0.9633 0.8307 -0.0166 0.1980  -0.0265 372 TYR D CG  
15376 C CD1 . TYR D 372 ? 1.0463 0.8859 0.7806 -0.0179 0.1857  -0.0269 372 TYR D CD1 
15377 C CD2 . TYR D 372 ? 1.0446 0.9023 0.7604 -0.0145 0.2000  -0.0097 372 TYR D CD2 
15378 C CE1 . TYR D 372 ? 0.9710 0.8171 0.7257 -0.0170 0.1752  -0.0123 372 TYR D CE1 
15379 C CE2 . TYR D 372 ? 1.0391 0.9007 0.7768 -0.0139 0.1897  0.0042  372 TYR D CE2 
15380 C CZ  . TYR D 372 ? 1.0202 0.8771 0.7767 -0.0150 0.1772  0.0021  372 TYR D CZ  
15381 O OH  . TYR D 372 ? 1.0423 0.9036 0.8183 -0.0145 0.1677  0.0144  372 TYR D OH  
15382 N N   . SER D 373 ? 1.0967 0.9035 0.7625 -0.0156 0.2404  -0.0907 373 SER D N   
15383 C CA  . SER D 373 ? 1.2136 1.0110 0.8482 -0.0189 0.2519  -0.1127 373 SER D CA  
15384 C C   . SER D 373 ? 1.3121 1.0848 0.9471 -0.0243 0.2482  -0.1317 373 SER D C   
15385 O O   . SER D 373 ? 1.3822 1.1501 0.9860 -0.0348 0.2456  -0.1494 373 SER D O   
15386 C CB  . SER D 373 ? 1.1865 0.9832 0.8263 -0.0086 0.2757  -0.1173 373 SER D CB  
15387 O OG  . SER D 373 ? 1.2355 1.0197 0.9140 0.0016  0.2824  -0.1174 373 SER D OG  
15388 N N   . THR D 374 ? 1.1958 0.9524 0.8650 -0.0179 0.2479  -0.1284 374 THR D N   
15389 C CA  . THR D 374 ? 1.2488 0.9771 0.9196 -0.0230 0.2458  -0.1440 374 THR D CA  
15390 C C   . THR D 374 ? 1.2762 1.0086 0.9324 -0.0390 0.2263  -0.1454 374 THR D C   
15391 O O   . THR D 374 ? 1.3610 1.0758 1.0011 -0.0501 0.2256  -0.1649 374 THR D O   
15392 C CB  . THR D 374 ? 1.2638 0.9768 0.9740 -0.0113 0.2478  -0.1347 374 THR D CB  
15393 O OG1 . THR D 374 ? 1.2401 0.9636 0.9706 0.0040  0.2616  -0.1268 374 THR D OG1 
15394 C CG2 . THR D 374 ? 1.3382 1.0141 1.0490 -0.0118 0.2549  -0.1524 374 THR D CG2 
15395 N N   . LEU D 375 ? 1.2018 0.9581 0.8644 -0.0408 0.2110  -0.1260 375 LEU D N   
15396 C CA  . LEU D 375 ? 1.2296 0.9941 0.8842 -0.0542 0.1923  -0.1255 375 LEU D CA  
15397 C C   . LEU D 375 ? 1.2558 1.0334 0.8721 -0.0660 0.1883  -0.1404 375 LEU D C   
15398 O O   . LEU D 375 ? 1.2915 1.0687 0.8981 -0.0801 0.1777  -0.1519 375 LEU D O   
15399 C CB  . LEU D 375 ? 1.0990 0.8855 0.7706 -0.0506 0.1789  -0.1012 375 LEU D CB  
15400 C CG  . LEU D 375 ? 1.0696 0.8475 0.7758 -0.0457 0.1736  -0.0883 375 LEU D CG  
15401 C CD1 . LEU D 375 ? 1.1420 0.9160 0.8495 -0.0579 0.1601  -0.0916 375 LEU D CD1 
15402 C CD2 . LEU D 375 ? 1.1717 0.9249 0.8964 -0.0360 0.1878  -0.0934 375 LEU D CD2 
15403 N N   . GLU D 376 ? 1.2614 1.0529 0.8557 -0.0611 0.1966  -0.1399 376 GLU D N   
15404 C CA  . GLU D 376 ? 1.3219 1.1269 0.8757 -0.0708 0.1940  -0.1549 376 GLU D CA  
15405 C C   . GLU D 376 ? 1.3942 1.1754 0.9332 -0.0813 0.2014  -0.1849 376 GLU D C   
15406 O O   . GLU D 376 ? 1.3656 1.1543 0.8835 -0.0965 0.1904  -0.1999 376 GLU D O   
15407 C CB  . GLU D 376 ? 1.3053 1.1244 0.8381 -0.0619 0.2059  -0.1483 376 GLU D CB  
15408 C CG  . GLU D 376 ? 1.2902 1.1383 0.8130 -0.0593 0.1942  -0.1260 376 GLU D CG  
15409 C CD  . GLU D 376 ? 1.3588 1.2157 0.8657 -0.0499 0.2090  -0.1156 376 GLU D CD  
15410 O OE1 . GLU D 376 ? 1.3614 1.2043 0.8828 -0.0424 0.2278  -0.1180 376 GLU D OE1 
15411 O OE2 . GLU D 376 ? 1.4213 1.2999 0.9019 -0.0496 0.2023  -0.1042 376 GLU D OE2 
15412 N N   . LYS D 377 ? 1.3935 1.1461 0.9438 -0.0731 0.2207  -0.1947 377 LYS D N   
15413 C CA  . LYS D 377 ? 1.4213 1.1450 0.9576 -0.0814 0.2311  -0.2242 377 LYS D CA  
15414 C C   . LYS D 377 ? 1.4250 1.1276 0.9794 -0.0927 0.2214  -0.2299 377 LYS D C   
15415 O O   . LYS D 377 ? 1.5093 1.2006 1.0447 -0.1093 0.2193  -0.2535 377 LYS D O   
15416 C CB  . LYS D 377 ? 1.4351 1.1351 0.9790 -0.0664 0.2561  -0.2321 377 LYS D CB  
15417 C CG  . LYS D 377 ? 1.5124 1.1706 1.0538 -0.0701 0.2701  -0.2598 377 LYS D CG  
15418 C CD  . LYS D 377 ? 1.6269 1.2559 1.2046 -0.0672 0.2676  -0.2527 377 LYS D CD  
15419 C CE  . LYS D 377 ? 1.6239 1.2114 1.1927 -0.0785 0.2752  -0.2801 377 LYS D CE  
15420 N NZ  . LYS D 377 ? 1.4887 1.0408 1.0916 -0.0707 0.2791  -0.2720 377 LYS D NZ  
15421 N N   . GLU D 378 ? 1.3952 1.0935 0.9847 -0.0857 0.2154  -0.2091 378 GLU D N   
15422 C CA  . GLU D 378 ? 1.4519 1.1274 1.0590 -0.0954 0.2089  -0.2122 378 GLU D CA  
15423 C C   . GLU D 378 ? 1.3729 1.0734 0.9688 -0.1141 0.1887  -0.2135 378 GLU D C   
15424 O O   . GLU D 378 ? 1.3403 1.0695 0.9469 -0.1118 0.1744  -0.1926 378 GLU D O   
15425 C CB  . GLU D 378 ? 1.4419 1.1084 1.0868 -0.0813 0.2085  -0.1887 378 GLU D CB  
15426 C CG  . GLU D 378 ? 1.4692 1.1097 1.1304 -0.0630 0.2279  -0.1892 378 GLU D CG  
15427 C CD  . GLU D 378 ? 1.5438 1.1396 1.2155 -0.0642 0.2368  -0.2005 378 GLU D CD  
15428 O OE1 . GLU D 378 ? 1.6092 1.1900 1.2675 -0.0829 0.2322  -0.2158 378 GLU D OE1 
15429 O OE2 . GLU D 378 ? 1.5470 1.1229 1.2409 -0.0466 0.2486  -0.1938 378 GLU D OE2 
15430 N N   . GLU D 379 ? 1.3919 1.0822 0.9675 -0.1328 0.1882  -0.2392 379 GLU D N   
15431 C CA  . GLU D 379 ? 1.3638 1.0837 0.9259 -0.1520 0.1697  -0.2454 379 GLU D CA  
15432 C C   . GLU D 379 ? 1.3969 1.1135 0.9848 -0.1623 0.1587  -0.2369 379 GLU D C   
15433 O O   . GLU D 379 ? 1.4064 1.1561 0.9918 -0.1747 0.1416  -0.2349 379 GLU D O   
15434 C CB  . GLU D 379 ? 1.4378 1.1504 0.9679 -0.1705 0.1734  -0.2792 379 GLU D CB  
15435 C CG  . GLU D 379 ? 1.4984 1.1599 1.0337 -0.1807 0.1879  -0.3021 379 GLU D CG  
15436 C CD  . GLU D 379 ? 1.6414 1.2622 1.1920 -0.1601 0.2091  -0.2973 379 GLU D CD  
15437 O OE1 . GLU D 379 ? 1.6346 1.2653 1.1784 -0.1424 0.2177  -0.2904 379 GLU D OE1 
15438 O OE2 . GLU D 379 ? 1.6709 1.2512 1.2412 -0.1612 0.2173  -0.2992 379 GLU D OE2 
15439 N N   . TRP D 380 ? 1.4091 1.0885 1.0215 -0.1569 0.1684  -0.2312 380 TRP D N   
15440 C CA  . TRP D 380 ? 1.3070 0.9826 0.9423 -0.1664 0.1596  -0.2213 380 TRP D CA  
15441 C C   . TRP D 380 ? 1.3370 1.0415 0.9928 -0.1537 0.1479  -0.1912 380 TRP D C   
15442 O O   . TRP D 380 ? 1.3741 1.0844 1.0468 -0.1615 0.1389  -0.1818 380 TRP D O   
15443 C CB  . TRP D 380 ? 1.2792 0.9021 0.9299 -0.1651 0.1745  -0.2251 380 TRP D CB  
15444 C CG  . TRP D 380 ? 1.3502 0.9554 1.0189 -0.1395 0.1851  -0.2069 380 TRP D CG  
15445 C CD1 . TRP D 380 ? 1.3806 0.9693 1.0435 -0.1239 0.2005  -0.2131 380 TRP D CD1 
15446 C CD2 . TRP D 380 ? 1.3837 0.9896 1.0800 -0.1268 0.1809  -0.1801 380 TRP D CD2 
15447 N NE1 . TRP D 380 ? 1.4152 0.9966 1.1029 -0.1023 0.2053  -0.1916 380 TRP D NE1 
15448 C CE2 . TRP D 380 ? 1.3726 0.9641 1.0797 -0.1039 0.1929  -0.1714 380 TRP D CE2 
15449 C CE3 . TRP D 380 ? 1.3949 1.0143 1.1074 -0.1327 0.1684  -0.1634 380 TRP D CE3 
15450 C CZ2 . TRP D 380 ? 1.3726 0.9642 1.1057 -0.0876 0.1911  -0.1472 380 TRP D CZ2 
15451 C CZ3 . TRP D 380 ? 1.3914 1.0080 1.1269 -0.1161 0.1677  -0.1395 380 TRP D CZ3 
15452 C CH2 . TRP D 380 ? 1.3712 0.9747 1.1164 -0.0942 0.1782  -0.1318 380 TRP D CH2 
15453 N N   . ILE D 381 ? 1.2897 1.0119 0.9443 -0.1354 0.1488  -0.1770 381 ILE D N   
15454 C CA  . ILE D 381 ? 1.2684 1.0183 0.9393 -0.1242 0.1381  -0.1509 381 ILE D CA  
15455 C C   . ILE D 381 ? 1.2762 1.0670 0.9274 -0.1256 0.1267  -0.1487 381 ILE D C   
15456 O O   . ILE D 381 ? 1.2564 1.0524 0.8840 -0.1229 0.1324  -0.1580 381 ILE D O   
15457 C CB  . ILE D 381 ? 1.1833 0.9216 0.8709 -0.1028 0.1479  -0.1345 381 ILE D CB  
15458 C CG1 . ILE D 381 ? 1.2309 0.9284 0.9347 -0.0985 0.1602  -0.1376 381 ILE D CG1 
15459 C CG2 . ILE D 381 ? 1.1454 0.9076 0.8515 -0.0940 0.1371  -0.1098 381 ILE D CG2 
15460 C CD1 . ILE D 381 ? 1.2221 0.9085 0.9364 -0.0784 0.1735  -0.1308 381 ILE D CD1 
15461 N N   . GLU D 382 ? 1.2498 1.0696 0.9099 -0.1286 0.1114  -0.1358 382 GLU D N   
15462 C CA  . GLU D 382 ? 1.2126 1.0721 0.8575 -0.1262 0.0994  -0.1287 382 GLU D CA  
15463 C C   . GLU D 382 ? 1.1755 1.0479 0.8386 -0.1106 0.0949  -0.1023 382 GLU D C   
15464 O O   . GLU D 382 ? 1.1065 0.9826 0.7914 -0.1117 0.0882  -0.0923 382 GLU D O   
15465 C CB  . GLU D 382 ? 1.2744 1.1614 0.9132 -0.1437 0.0845  -0.1391 382 GLU D CB  
15466 C CG  . GLU D 382 ? 1.3055 1.2296 0.9172 -0.1439 0.0744  -0.1417 382 GLU D CG  
15467 C CD  . GLU D 382 ? 1.2759 1.2373 0.8893 -0.1576 0.0566  -0.1464 382 GLU D CD  
15468 O OE1 . GLU D 382 ? 1.3047 1.3003 0.9200 -0.1483 0.0445  -0.1295 382 GLU D OE1 
15469 O OE2 . GLU D 382 ? 1.2944 1.2512 0.9084 -0.1778 0.0553  -0.1671 382 GLU D OE2 
15470 N N   . THR D 383 ? 1.2102 1.0882 0.8640 -0.0969 0.1000  -0.0919 383 THR D N   
15471 C CA  . THR D 383 ? 1.0777 0.9692 0.7452 -0.0839 0.0955  -0.0686 383 THR D CA  
15472 C C   . THR D 383 ? 1.1666 1.0929 0.8261 -0.0855 0.0796  -0.0615 383 THR D C   
15473 O O   . THR D 383 ? 1.1892 1.1346 0.8240 -0.0905 0.0742  -0.0700 383 THR D O   
15474 C CB  . THR D 383 ? 1.0477 0.9334 0.7079 -0.0708 0.1072  -0.0601 383 THR D CB  
15475 O OG1 . THR D 383 ? 1.0917 0.9895 0.7194 -0.0727 0.1087  -0.0683 383 THR D OG1 
15476 C CG2 . THR D 383 ? 1.1246 0.9805 0.7982 -0.0672 0.1224  -0.0661 383 THR D CG2 
15477 N N   . LEU D 384 ? 1.1446 1.0805 0.8252 -0.0806 0.0721  -0.0463 384 LEU D N   
15478 C CA  . LEU D 384 ? 1.1037 1.0727 0.7832 -0.0808 0.0571  -0.0394 384 LEU D CA  
15479 C C   . LEU D 384 ? 1.1123 1.0876 0.8017 -0.0650 0.0557  -0.0171 384 LEU D C   
15480 O O   . LEU D 384 ? 1.0736 1.0284 0.7779 -0.0579 0.0641  -0.0085 384 LEU D O   
15481 C CB  . LEU D 384 ? 1.1012 1.0776 0.7987 -0.0938 0.0492  -0.0467 384 LEU D CB  
15482 C CG  . LEU D 384 ? 1.1162 1.1068 0.8020 -0.1119 0.0428  -0.0672 384 LEU D CG  
15483 C CD1 . LEU D 384 ? 1.1220 1.0786 0.8035 -0.1232 0.0546  -0.0856 384 LEU D CD1 
15484 C CD2 . LEU D 384 ? 0.9817 0.9953 0.6868 -0.1215 0.0320  -0.0673 384 LEU D CD2 
15485 N N   . THR D 385 ? 1.1082 1.1124 0.7892 -0.0594 0.0448  -0.0082 385 THR D N   
15486 C CA  . THR D 385 ? 1.0566 1.0662 0.7484 -0.0450 0.0426  0.0120  385 THR D CA  
15487 C C   . THR D 385 ? 0.9814 1.0011 0.6987 -0.0473 0.0350  0.0142  385 THR D C   
15488 O O   . THR D 385 ? 0.9861 1.0136 0.7111 -0.0605 0.0303  0.0016  385 THR D O   
15489 C CB  . THR D 385 ? 1.1061 1.1404 0.7772 -0.0347 0.0352  0.0230  385 THR D CB  
15490 O OG1 . THR D 385 ? 1.0736 1.1419 0.7407 -0.0415 0.0208  0.0150  385 THR D OG1 
15491 C CG2 . THR D 385 ? 1.0510 1.0760 0.6936 -0.0324 0.0439  0.0222  385 THR D CG2 
15492 N N   . LEU D 386 ? 0.9865 1.0052 0.7165 -0.0348 0.0351  0.0301  386 LEU D N   
15493 C CA  . LEU D 386 ? 0.8973 0.9278 0.6498 -0.0347 0.0289  0.0332  386 LEU D CA  
15494 C C   . LEU D 386 ? 0.9367 1.0055 0.6878 -0.0370 0.0157  0.0306  386 LEU D C   
15495 O O   . LEU D 386 ? 0.9192 1.0019 0.6864 -0.0464 0.0108  0.0238  386 LEU D O   
15496 C CB  . LEU D 386 ? 0.9772 0.9979 0.7404 -0.0202 0.0325  0.0492  386 LEU D CB  
15497 C CG  . LEU D 386 ? 0.8257 0.8145 0.5979 -0.0190 0.0439  0.0516  386 LEU D CG  
15498 C CD1 . LEU D 386 ? 0.8361 0.8192 0.6211 -0.0079 0.0456  0.0640  386 LEU D CD1 
15499 C CD2 . LEU D 386 ? 0.8017 0.7782 0.5859 -0.0310 0.0466  0.0403  386 LEU D CD2 
15500 N N   . GLU D 387 ? 1.0444 1.1329 0.7767 -0.0286 0.0097  0.0365  387 GLU D N   
15501 C CA  . GLU D 387 ? 1.0490 1.1798 0.7799 -0.0304 -0.0045 0.0335  387 GLU D CA  
15502 C C   . GLU D 387 ? 1.0442 1.1859 0.7695 -0.0514 -0.0085 0.0122  387 GLU D C   
15503 O O   . GLU D 387 ? 1.0869 1.2610 0.8236 -0.0603 -0.0187 0.0046  387 GLU D O   
15504 C CB  . GLU D 387 ? 1.0143 1.1634 0.7236 -0.0146 -0.0104 0.0467  387 GLU D CB  
15505 C CG  . GLU D 387 ? 1.2346 1.3794 0.9125 -0.0197 -0.0085 0.0396  387 GLU D CG  
15506 C CD  . GLU D 387 ? 1.3802 1.5337 1.0340 -0.0018 -0.0106 0.0573  387 GLU D CD  
15507 O OE1 . GLU D 387 ? 1.4885 1.6588 1.1502 0.0143  -0.0170 0.0737  387 GLU D OE1 
15508 O OE2 . GLU D 387 ? 1.3701 1.5128 0.9965 -0.0032 -0.0049 0.0553  387 GLU D OE2 
15509 N N   . GLU D 388 ? 0.9998 1.1150 0.7091 -0.0601 0.0001  0.0014  388 GLU D N   
15510 C CA  . GLU D 388 ? 1.0442 1.1619 0.7484 -0.0810 -0.0013 -0.0208 388 GLU D CA  
15511 C C   . GLU D 388 ? 1.0390 1.1444 0.7690 -0.0940 0.0021  -0.0281 388 GLU D C   
15512 O O   . GLU D 388 ? 1.0447 1.1707 0.7824 -0.1101 -0.0045 -0.0411 388 GLU D O   
15513 C CB  . GLU D 388 ? 1.0773 1.1660 0.7584 -0.0849 0.0094  -0.0307 388 GLU D CB  
15514 C CG  . GLU D 388 ? 1.1139 1.2222 0.7626 -0.0808 0.0044  -0.0321 388 GLU D CG  
15515 C CD  . GLU D 388 ? 1.1587 1.2357 0.7857 -0.0791 0.0186  -0.0365 388 GLU D CD  
15516 O OE1 . GLU D 388 ? 1.1547 1.2094 0.7802 -0.0926 0.0267  -0.0550 388 GLU D OE1 
15517 O OE2 . GLU D 388 ? 1.1452 1.2190 0.7572 -0.0642 0.0229  -0.0213 388 GLU D OE2 
15518 N N   . ALA D 389 ? 1.0312 1.1048 0.7746 -0.0877 0.0124  -0.0195 389 ALA D N   
15519 C CA  . ALA D 389 ? 0.9696 1.0294 0.7343 -0.0985 0.0164  -0.0239 389 ALA D CA  
15520 C C   . ALA D 389 ? 1.0131 1.1072 0.7966 -0.1016 0.0071  -0.0209 389 ALA D C   
15521 O O   . ALA D 389 ? 1.1015 1.1970 0.8983 -0.1173 0.0078  -0.0297 389 ALA D O   
15522 C CB  . ALA D 389 ? 0.8890 0.9156 0.6637 -0.0883 0.0268  -0.0128 389 ALA D CB  
15523 N N   . MET D 390 ? 1.0158 1.1376 0.8013 -0.0863 -0.0006 -0.0081 390 MET D N   
15524 C CA  . MET D 390 ? 0.9491 1.1082 0.7539 -0.0869 -0.0091 -0.0054 390 MET D CA  
15525 C C   . MET D 390 ? 0.8637 1.0608 0.6663 -0.1023 -0.0199 -0.0198 390 MET D C   
15526 O O   . MET D 390 ? 0.9036 1.1170 0.7235 -0.1183 -0.0216 -0.0287 390 MET D O   
15527 C CB  . MET D 390 ? 0.9849 1.1600 0.7927 -0.0638 -0.0132 0.0126  390 MET D CB  
15528 C CG  . MET D 390 ? 1.0101 1.1564 0.8289 -0.0524 -0.0037 0.0243  390 MET D CG  
15529 S SD  . MET D 390 ? 1.0600 1.2155 0.9063 -0.0608 -0.0017 0.0223  390 MET D SD  
15530 C CE  . MET D 390 ? 1.0353 1.2385 0.8950 -0.0449 -0.0114 0.0319  390 MET D CE  
15531 N N   . ARG D 391 ? 0.9435 1.1556 0.7239 -0.0991 -0.0269 -0.0228 391 ARG D N   
15532 C CA  . ARG D 391 ? 0.9628 1.2180 0.7395 -0.1125 -0.0397 -0.0365 391 ARG D CA  
15533 C C   . ARG D 391 ? 0.9468 1.1882 0.7207 -0.1401 -0.0358 -0.0599 391 ARG D C   
15534 O O   . ARG D 391 ? 0.9406 1.2183 0.7184 -0.1567 -0.0456 -0.0744 391 ARG D O   
15535 C CB  . ARG D 391 ? 1.0008 1.2746 0.7502 -0.1002 -0.0482 -0.0323 391 ARG D CB  
15536 C CG  . ARG D 391 ? 1.0638 1.3567 0.8153 -0.0732 -0.0537 -0.0091 391 ARG D CG  
15537 C CD  . ARG D 391 ? 1.0349 1.3298 0.7538 -0.0600 -0.0572 -0.0017 391 ARG D CD  
15538 N NE  . ARG D 391 ? 1.0504 1.3741 0.7698 -0.0358 -0.0660 0.0192  391 ARG D NE  
15539 C CZ  . ARG D 391 ? 1.1645 1.4885 0.8570 -0.0189 -0.0681 0.0328  391 ARG D CZ  
15540 N NH1 . ARG D 391 ? 1.1963 1.4963 0.8588 -0.0239 -0.0617 0.0273  391 ARG D NH1 
15541 N NH2 . ARG D 391 ? 1.2022 1.5507 0.8975 0.0043  -0.0757 0.0531  391 ARG D NH2 
15542 N N   . LYS D 392 ? 1.0180 1.2084 0.7860 -0.1454 -0.0217 -0.0644 392 LYS D N   
15543 C CA  . LYS D 392 ? 1.0920 1.2622 0.8549 -0.1698 -0.0161 -0.0864 392 LYS D CA  
15544 C C   . LYS D 392 ? 1.0381 1.2155 0.8271 -0.1884 -0.0150 -0.0927 392 LYS D C   
15545 O O   . LYS D 392 ? 0.9400 1.1004 0.7468 -0.1831 -0.0077 -0.0806 392 LYS D O   
15546 C CB  . LYS D 392 ? 1.0077 1.1215 0.7586 -0.1666 -0.0007 -0.0875 392 LYS D CB  
15547 C CG  . LYS D 392 ? 0.9179 1.0235 0.6394 -0.1578 0.0006  -0.0904 392 LYS D CG  
15548 C CD  . LYS D 392 ? 1.0010 1.0803 0.7057 -0.1753 0.0082  -0.1137 392 LYS D CD  
15549 C CE  . LYS D 392 ? 1.0584 1.1369 0.7315 -0.1668 0.0091  -0.1173 392 LYS D CE  
15550 N NZ  . LYS D 392 ? 1.1128 1.1528 0.7705 -0.1778 0.0220  -0.1372 392 LYS D NZ  
15551 N N   . GLU D 393 ? 1.1249 1.3280 0.9154 -0.2115 -0.0215 -0.1122 393 GLU D N   
15552 C CA  . GLU D 393 ? 1.1519 1.3683 0.9676 -0.2325 -0.0205 -0.1194 393 GLU D CA  
15553 C C   . GLU D 393 ? 1.1823 1.3478 0.9975 -0.2531 -0.0056 -0.1324 393 GLU D C   
15554 O O   . GLU D 393 ? 1.2911 1.4510 1.1271 -0.2660 0.0006  -0.1313 393 GLU D O   
15555 C CB  . GLU D 393 ? 1.1468 1.4235 0.9682 -0.2483 -0.0361 -0.1340 393 GLU D CB  
15556 C CG  . GLU D 393 ? 1.2521 1.5515 1.1023 -0.2732 -0.0355 -0.1431 393 GLU D CG  
15557 C CD  . GLU D 393 ? 1.3217 1.6568 1.1999 -0.2601 -0.0388 -0.1246 393 GLU D CD  
15558 O OE1 . GLU D 393 ? 1.2715 1.6660 1.1594 -0.2529 -0.0536 -0.1219 393 GLU D OE1 
15559 O OE2 . GLU D 393 ? 1.3701 1.6746 1.2604 -0.2564 -0.0264 -0.1128 393 GLU D OE2 
15560 N N   . ASP D 394 ? 1.1235 1.2499 0.9153 -0.2551 0.0015  -0.1436 394 ASP D N   
15561 C CA  . ASP D 394 ? 1.0644 1.1402 0.8549 -0.2734 0.0162  -0.1567 394 ASP D CA  
15562 C C   . ASP D 394 ? 1.1091 1.1393 0.9092 -0.2612 0.0299  -0.1389 394 ASP D C   
15563 O O   . ASP D 394 ? 1.1436 1.1270 0.9421 -0.2720 0.0431  -0.1461 394 ASP D O   
15564 C CB  . ASP D 394 ? 1.2235 1.2722 0.9858 -0.2776 0.0206  -0.1754 394 ASP D CB  
15565 C CG  . ASP D 394 ? 1.2903 1.3511 1.0317 -0.2534 0.0148  -0.1666 394 ASP D CG  
15566 O OD1 . ASP D 394 ? 1.2922 1.3600 1.0409 -0.2306 0.0130  -0.1435 394 ASP D OD1 
15567 O OD2 . ASP D 394 ? 1.2351 1.2968 0.9516 -0.2580 0.0131  -0.1831 394 ASP D OD2 
15568 N N   . VAL D 395 ? 1.1156 1.1577 0.9253 -0.2391 0.0272  -0.1164 395 VAL D N   
15569 C CA  . VAL D 395 ? 1.1166 1.1209 0.9346 -0.2276 0.0382  -0.1000 395 VAL D CA  
15570 C C   . VAL D 395 ? 1.0664 1.0795 0.9064 -0.2399 0.0408  -0.0944 395 VAL D C   
15571 O O   . VAL D 395 ? 1.0007 1.0589 0.8539 -0.2497 0.0323  -0.0974 395 VAL D O   
15572 C CB  . VAL D 395 ? 1.0229 1.0326 0.8389 -0.1992 0.0352  -0.0805 395 VAL D CB  
15573 C CG1 . VAL D 395 ? 1.0814 1.0734 0.8757 -0.1879 0.0371  -0.0844 395 VAL D CG1 
15574 C CG2 . VAL D 395 ? 1.0355 1.0976 0.8613 -0.1917 0.0224  -0.0724 395 VAL D CG2 
15575 N N   . LYS D 396 ? 1.0632 1.0350 0.9074 -0.2387 0.0529  -0.0853 396 LYS D N   
15576 C CA  . LYS D 396 ? 1.0496 1.0262 0.9118 -0.2479 0.0573  -0.0766 396 LYS D CA  
15577 C C   . LYS D 396 ? 1.0560 1.0626 0.9287 -0.2285 0.0514  -0.0583 396 LYS D C   
15578 O O   . LYS D 396 ? 1.0047 1.0112 0.8705 -0.2062 0.0475  -0.0491 396 LYS D O   
15579 C CB  . LYS D 396 ? 0.9716 0.8931 0.8317 -0.2513 0.0721  -0.0710 396 LYS D CB  
15580 C CG  . LYS D 396 ? 1.0200 0.9377 0.8930 -0.2739 0.0799  -0.0714 396 LYS D CG  
15581 C CD  . LYS D 396 ? 1.0900 0.9573 0.9605 -0.2697 0.0934  -0.0573 396 LYS D CD  
15582 C CE  . LYS D 396 ? 1.1502 1.0287 1.0345 -0.2807 0.0988  -0.0460 396 LYS D CE  
15583 N NZ  . LYS D 396 ? 1.1686 0.9961 1.0497 -0.2937 0.1144  -0.0419 396 LYS D NZ  
15584 N N   . THR D 397 ? 1.2148 0.9156 0.9484 -0.2156 -0.2405 0.0605  397 THR D N   
15585 C CA  . THR D 397 ? 1.1806 0.9406 0.9539 -0.2093 -0.2183 0.0789  397 THR D CA  
15586 C C   . THR D 397 ? 1.1729 0.9450 0.9786 -0.2184 -0.2054 0.0991  397 THR D C   
15587 O O   . THR D 397 ? 1.2041 0.9475 1.0124 -0.2380 -0.2193 0.1055  397 THR D O   
15588 C CB  . THR D 397 ? 1.0654 0.8669 0.8690 -0.2222 -0.2306 0.0904  397 THR D CB  
15589 O OG1 . THR D 397 ? 1.1490 1.0028 1.0070 -0.2265 -0.2143 0.1132  397 THR D OG1 
15590 C CG2 . THR D 397 ? 1.1381 0.9151 0.9402 -0.2493 -0.2648 0.0903  397 THR D CG2 
15591 N N   . GLU D 398 ? 1.1274 0.9401 0.9545 -0.2050 -0.1786 0.1090  398 GLU D N   
15592 C CA  . GLU D 398 ? 1.0907 0.9222 0.9458 -0.2134 -0.1619 0.1288  398 GLU D CA  
15593 C C   . GLU D 398 ? 1.0356 0.9256 0.9241 -0.2032 -0.1376 0.1389  398 GLU D C   
15594 O O   . GLU D 398 ? 0.9972 0.9009 0.8758 -0.1824 -0.1290 0.1286  398 GLU D O   
15595 C CB  . GLU D 398 ? 1.0780 0.8706 0.9023 -0.2021 -0.1529 0.1241  398 GLU D CB  
15596 C CG  . GLU D 398 ? 1.1263 0.9120 0.9643 -0.2219 -0.1492 0.1447  398 GLU D CG  
15597 C CD  . GLU D 398 ? 1.3377 1.0875 1.1759 -0.2490 -0.1761 0.1493  398 GLU D CD  
15598 O OE1 . GLU D 398 ? 1.3910 1.1686 1.2662 -0.2746 -0.1788 0.1678  398 GLU D OE1 
15599 O OE2 . GLU D 398 ? 1.4351 1.1291 1.2385 -0.2446 -0.1944 0.1337  398 GLU D OE2 
15600 N N   . VAL D 399 ? 0.9994 0.9228 0.9274 -0.2183 -0.1258 0.1589  399 VAL D N   
15601 C CA  . VAL D 399 ? 0.9052 0.8827 0.8674 -0.2087 -0.1001 0.1678  399 VAL D CA  
15602 C C   . VAL D 399 ? 0.9413 0.9142 0.8886 -0.2011 -0.0745 0.1724  399 VAL D C   
15603 O O   . VAL D 399 ? 0.9894 0.9434 0.9313 -0.2178 -0.0737 0.1835  399 VAL D O   
15604 C CB  . VAL D 399 ? 0.8586 0.8838 0.8800 -0.2293 -0.1013 0.1854  399 VAL D CB  
15605 C CG1 . VAL D 399 ? 0.8838 0.9609 0.9402 -0.2185 -0.0698 0.1936  399 VAL D CG1 
15606 C CG2 . VAL D 399 ? 0.9468 0.9818 0.9846 -0.2339 -0.1285 0.1814  399 VAL D CG2 
15607 N N   . ILE D 400 ? 0.8703 0.8576 0.8082 -0.1773 -0.0554 0.1646  400 ILE D N   
15608 C CA  . ILE D 400 ? 0.9391 0.9252 0.8612 -0.1688 -0.0317 0.1679  400 ILE D CA  
15609 C C   . ILE D 400 ? 0.9120 0.9490 0.8662 -0.1600 -0.0065 0.1723  400 ILE D C   
15610 O O   . ILE D 400 ? 0.9133 0.9772 0.8908 -0.1503 -0.0083 0.1675  400 ILE D O   
15611 C CB  . ILE D 400 ? 0.9386 0.8877 0.8154 -0.1475 -0.0335 0.1519  400 ILE D CB  
15612 C CG1 . ILE D 400 ? 0.8109 0.7807 0.6881 -0.1249 -0.0250 0.1392  400 ILE D CG1 
15613 C CG2 . ILE D 400 ? 1.0732 0.9755 0.9238 -0.1507 -0.0591 0.1419  400 ILE D CG2 
15614 C CD1 . ILE D 400 ? 0.8690 0.8208 0.7148 -0.1057 -0.0152 0.1291  400 ILE D CD1 
15615 N N   . GLU D 401 ? 0.7853 0.8331 0.7385 -0.1635 0.0167  0.1815  401 GLU D N   
15616 C CA  . GLU D 401 ? 0.7830 0.8785 0.7685 -0.1571 0.0431  0.1850  401 GLU D CA  
15617 C C   . GLU D 401 ? 0.8250 0.9161 0.7814 -0.1381 0.0642  0.1770  401 GLU D C   
15618 O O   . GLU D 401 ? 0.8297 0.9561 0.8088 -0.1299 0.0868  0.1765  401 GLU D O   
15619 C CB  . GLU D 401 ? 0.9288 1.0532 0.9471 -0.1807 0.0577  0.2029  401 GLU D CB  
15620 C CG  . GLU D 401 ? 0.9180 1.0626 0.9819 -0.2000 0.0392  0.2117  401 GLU D CG  
15621 C CD  . GLU D 401 ? 0.9049 1.1115 1.0327 -0.1982 0.0541  0.2163  401 GLU D CD  
15622 O OE1 . GLU D 401 ? 0.8763 1.1027 1.0446 -0.2071 0.0341  0.2202  401 GLU D OE1 
15623 O OE2 . GLU D 401 ? 0.8745 1.1095 1.0125 -0.1875 0.0847  0.2154  401 GLU D OE2 
15624 N N   . SER D 402 ? 0.8942 0.9434 0.8033 -0.1306 0.0567  0.1702  402 SER D N   
15625 C CA  . SER D 402 ? 0.8480 0.8916 0.7293 -0.1132 0.0723  0.1620  402 SER D CA  
15626 C C   . SER D 402 ? 0.8739 0.8764 0.7171 -0.1010 0.0548  0.1507  402 SER D C   
15627 O O   . SER D 402 ? 0.8905 0.8609 0.7190 -0.1088 0.0353  0.1521  402 SER D O   
15628 C CB  . SER D 402 ? 0.8260 0.8702 0.6902 -0.1237 0.0930  0.1728  402 SER D CB  
15629 O OG  . SER D 402 ? 0.9356 0.9352 0.7551 -0.1271 0.0813  0.1755  402 SER D OG  
15630 N N   . VAL D 403 ? 0.7622 0.7661 0.5919 -0.0818 0.0622  0.1388  403 VAL D N   
15631 C CA  . VAL D 403 ? 0.8280 0.8002 0.6269 -0.0688 0.0496  0.1277  403 VAL D CA  
15632 C C   . VAL D 403 ? 0.8550 0.8205 0.6280 -0.0619 0.0617  0.1269  403 VAL D C   
15633 O O   . VAL D 403 ? 0.8758 0.8633 0.6533 -0.0625 0.0818  0.1298  403 VAL D O   
15634 C CB  . VAL D 403 ? 0.8181 0.7969 0.6248 -0.0534 0.0433  0.1132  403 VAL D CB  
15635 C CG1 . VAL D 403 ? 0.7692 0.7424 0.5872 -0.0606 0.0258  0.1122  403 VAL D CG1 
15636 C CG2 . VAL D 403 ? 0.7763 0.7885 0.6037 -0.0449 0.0601  0.1109  403 VAL D CG2 
15637 N N   . LYS D 404 ? 0.8851 0.8192 0.6309 -0.0549 0.0484  0.1220  404 LYS D N   
15638 C CA  . LYS D 404 ? 0.8965 0.8218 0.6165 -0.0464 0.0536  0.1190  404 LYS D CA  
15639 C C   . LYS D 404 ? 0.9260 0.8620 0.6527 -0.0281 0.0540  0.1029  404 LYS D C   
15640 O O   . LYS D 404 ? 0.9322 0.8597 0.6642 -0.0199 0.0410  0.0936  404 LYS D O   
15641 C CB  . LYS D 404 ? 0.9326 0.8192 0.6241 -0.0483 0.0359  0.1240  404 LYS D CB  
15642 C CG  . LYS D 404 ? 1.0742 0.9458 0.7478 -0.0681 0.0379  0.1429  404 LYS D CG  
15643 C CD  . LYS D 404 ? 1.0957 0.9818 0.7512 -0.0734 0.0595  0.1489  404 LYS D CD  
15644 C CE  . LYS D 404 ? 1.1147 1.0038 0.7659 -0.0968 0.0715  0.1676  404 LYS D CE  
15645 N NZ  . LYS D 404 ? 1.0873 1.0197 0.7751 -0.1018 0.0940  0.1672  404 LYS D NZ  
15646 N N   . ALA D 405 ? 0.8111 0.7646 0.5366 -0.0226 0.0699  0.0991  405 ALA D N   
15647 C CA  . ALA D 405 ? 0.8592 0.8239 0.5937 -0.0082 0.0714  0.0856  405 ALA D CA  
15648 C C   . ALA D 405 ? 0.9197 0.8649 0.6396 0.0013  0.0566  0.0774  405 ALA D C   
15649 O O   . ALA D 405 ? 1.0561 0.9840 0.7529 0.0009  0.0514  0.0801  405 ALA D O   
15650 C CB  . ALA D 405 ? 0.7939 0.7745 0.5270 -0.0049 0.0900  0.0828  405 ALA D CB  
15651 N N   . GLY D 406 ? 0.7827 0.7312 0.5163 0.0095  0.0495  0.0677  406 GLY D N   
15652 C CA  . GLY D 406 ? 0.8490 0.7857 0.5773 0.0198  0.0378  0.0584  406 GLY D CA  
15653 C C   . GLY D 406 ? 0.7645 0.7142 0.5089 0.0279  0.0385  0.0466  406 GLY D C   
15654 O O   . GLY D 406 ? 0.7917 0.7570 0.5473 0.0257  0.0465  0.0466  406 GLY D O   
15655 N N   . THR D 407 ? 0.7950 0.7384 0.5409 0.0373  0.0298  0.0372  407 THR D N   
15656 C CA  . THR D 407 ? 0.8070 0.7629 0.5659 0.0446  0.0322  0.0251  407 THR D CA  
15657 C C   . THR D 407 ? 0.8322 0.7735 0.5933 0.0520  0.0210  0.0165  407 THR D C   
15658 O O   . THR D 407 ? 0.8767 0.7959 0.6304 0.0521  0.0091  0.0208  407 THR D O   
15659 C CB  . THR D 407 ? 0.7392 0.7101 0.5050 0.0500  0.0374  0.0192  407 THR D CB  
15660 O OG1 . THR D 407 ? 0.8114 0.7733 0.5768 0.0565  0.0261  0.0164  407 THR D OG1 
15661 C CG2 . THR D 407 ? 0.8096 0.7881 0.5706 0.0444  0.0471  0.0257  407 THR D CG2 
15662 N N   . TRP D 408 ? 0.7961 0.7482 0.5667 0.0584  0.0254  0.0040  408 TRP D N   
15663 C CA  . TRP D 408 ? 0.7984 0.7387 0.5742 0.0686  0.0176  -0.0081 408 TRP D CA  
15664 C C   . TRP D 408 ? 0.7700 0.7133 0.5604 0.0804  0.0110  -0.0137 408 TRP D C   
15665 O O   . TRP D 408 ? 0.8910 0.8276 0.6927 0.0921  0.0050  -0.0253 408 TRP D O   
15666 C CB  . TRP D 408 ? 0.8169 0.7677 0.5943 0.0707  0.0272  -0.0211 408 TRP D CB  
15667 C CG  . TRP D 408 ? 0.7154 0.6942 0.5018 0.0707  0.0413  -0.0251 408 TRP D CG  
15668 C CD1 . TRP D 408 ? 0.7970 0.7917 0.5939 0.0703  0.0450  -0.0206 408 TRP D CD1 
15669 C CD2 . TRP D 408 ? 0.7038 0.6948 0.4860 0.0689  0.0530  -0.0337 408 TRP D CD2 
15670 N NE1 . TRP D 408 ? 0.7570 0.7730 0.5598 0.0680  0.0579  -0.0251 408 TRP D NE1 
15671 C CE2 . TRP D 408 ? 0.7471 0.7617 0.5399 0.0668  0.0637  -0.0323 408 TRP D CE2 
15672 C CE3 . TRP D 408 ? 0.7303 0.7119 0.4970 0.0675  0.0549  -0.0424 408 TRP D CE3 
15673 C CZ2 . TRP D 408 ? 0.7810 0.8107 0.5694 0.0625  0.0771  -0.0372 408 TRP D CZ2 
15674 C CZ3 . TRP D 408 ? 0.6988 0.6957 0.4579 0.0639  0.0684  -0.0484 408 TRP D CZ3 
15675 C CH2 . TRP D 408 ? 0.7039 0.7248 0.4739 0.0610  0.0798  -0.0448 408 TRP D CH2 
15676 N N   . PHE D 409 ? 0.7212 0.6735 0.5126 0.0781  0.0107  -0.0066 409 PHE D N   
15677 C CA  . PHE D 409 ? 0.8627 0.8166 0.6675 0.0874  -0.0006 -0.0096 409 PHE D CA  
15678 C C   . PHE D 409 ? 0.8438 0.7706 0.6297 0.0841  -0.0165 0.0036  409 PHE D C   
15679 O O   . PHE D 409 ? 0.8500 0.7762 0.6211 0.0767  -0.0169 0.0130  409 PHE D O   
15680 C CB  . PHE D 409 ? 0.8899 0.8692 0.7054 0.0854  0.0072  -0.0114 409 PHE D CB  
15681 C CG  . PHE D 409 ? 0.9079 0.8986 0.7481 0.0955  -0.0032 -0.0186 409 PHE D CG  
15682 C CD1 . PHE D 409 ? 1.0699 1.0447 0.9052 0.0984  -0.0230 -0.0120 409 PHE D CD1 
15683 C CD2 . PHE D 409 ? 0.9730 0.9919 0.8422 0.1010  0.0063  -0.0311 409 PHE D CD2 
15684 C CE1 . PHE D 409 ? 1.1057 1.0930 0.9683 0.1080  -0.0361 -0.0179 409 PHE D CE1 
15685 C CE2 . PHE D 409 ? 0.9677 1.0027 0.8676 0.1100  -0.0033 -0.0377 409 PHE D CE2 
15686 C CZ  . PHE D 409 ? 1.0617 1.0813 0.9603 0.1142  -0.0260 -0.0312 409 PHE D CZ  
15687 N N   . ASP D 410 ? 0.8182 0.7196 0.6018 0.0892  -0.0297 0.0040  410 ASP D N   
15688 C CA  . ASP D 410 ? 0.9086 0.7786 0.6723 0.0853  -0.0471 0.0181  410 ASP D CA  
15689 C C   . ASP D 410 ? 0.9824 0.8437 0.7182 0.0674  -0.0394 0.0337  410 ASP D C   
15690 O O   . ASP D 410 ? 1.0201 0.8612 0.7336 0.0602  -0.0489 0.0477  410 ASP D O   
15691 C CB  . ASP D 410 ? 0.9805 0.8490 0.7462 0.0911  -0.0626 0.0215  410 ASP D CB  
15692 C CG  . ASP D 410 ? 1.1602 1.0406 0.9617 0.1096  -0.0720 0.0069  410 ASP D CG  
15693 O OD1 . ASP D 410 ? 1.1145 0.9775 0.9281 0.1208  -0.0822 0.0010  410 ASP D OD1 
15694 O OD2 . ASP D 410 ? 1.1514 1.0590 0.9712 0.1130  -0.0692 0.0008  410 ASP D OD2 
15695 N N   . GLY D 411 ? 0.7973 0.6744 0.5344 0.0598  -0.0224 0.0323  411 GLY D N   
15696 C CA  . GLY D 411 ? 0.8469 0.7221 0.5664 0.0443  -0.0135 0.0460  411 GLY D CA  
15697 C C   . GLY D 411 ? 0.8193 0.7072 0.5271 0.0390  -0.0038 0.0517  411 GLY D C   
15698 O O   . GLY D 411 ? 0.7415 0.6297 0.4359 0.0271  0.0058  0.0623  411 GLY D O   
15699 N N   . ASN D 412 ? 0.8182 0.7173 0.5317 0.0471  -0.0054 0.0440  412 ASN D N   
15700 C CA  . ASN D 412 ? 0.7695 0.6755 0.4683 0.0425  0.0016  0.0467  412 ASN D CA  
15701 C C   . ASN D 412 ? 0.6948 0.6268 0.4116 0.0463  0.0142  0.0360  412 ASN D C   
15702 O O   . ASN D 412 ? 0.7507 0.6960 0.4899 0.0523  0.0164  0.0272  412 ASN D O   
15703 C CB  . ASN D 412 ? 0.7229 0.6122 0.4063 0.0454  -0.0168 0.0495  412 ASN D CB  
15704 C CG  . ASN D 412 ? 0.7923 0.6897 0.5027 0.0590  -0.0304 0.0383  412 ASN D CG  
15705 O OD1 . ASN D 412 ? 0.8310 0.7522 0.5621 0.0633  -0.0228 0.0276  412 ASN D OD1 
15706 N ND2 . ASN D 412 ? 0.9028 0.7807 0.6160 0.0658  -0.0504 0.0410  412 ASN D ND2 
15707 N N   . PHE D 413 ? 0.7426 0.6792 0.4465 0.0417  0.0233  0.0367  413 PHE D N   
15708 C CA  . PHE D 413 ? 0.7452 0.6999 0.4626 0.0440  0.0323  0.0278  413 PHE D CA  
15709 C C   . PHE D 413 ? 0.7545 0.7082 0.4706 0.0470  0.0205  0.0217  413 PHE D C   
15710 O O   . PHE D 413 ? 0.7967 0.7602 0.5183 0.0461  0.0263  0.0154  413 PHE D O   
15711 C CB  . PHE D 413 ? 0.7563 0.7153 0.4643 0.0384  0.0497  0.0301  413 PHE D CB  
15712 C CG  . PHE D 413 ? 0.8288 0.7923 0.5425 0.0343  0.0599  0.0374  413 PHE D CG  
15713 C CD1 . PHE D 413 ? 0.8480 0.8005 0.5448 0.0272  0.0612  0.0474  413 PHE D CD1 
15714 C CD2 . PHE D 413 ? 0.6784 0.6570 0.4141 0.0359  0.0669  0.0355  413 PHE D CD2 
15715 C CE1 . PHE D 413 ? 0.9129 0.8728 0.6203 0.0217  0.0693  0.0545  413 PHE D CE1 
15716 C CE2 . PHE D 413 ? 0.7586 0.7425 0.5023 0.0314  0.0726  0.0426  413 PHE D CE2 
15717 C CZ  . PHE D 413 ? 0.9123 0.8885 0.6447 0.0243  0.0739  0.0517  413 PHE D CZ  
15718 N N   . LEU D 414 ? 0.7068 0.6478 0.4176 0.0503  0.0018  0.0241  414 LEU D N   
15719 C CA  . LEU D 414 ? 0.7687 0.7072 0.4760 0.0516  -0.0135 0.0205  414 LEU D CA  
15720 C C   . LEU D 414 ? 0.7053 0.6680 0.4486 0.0568  -0.0142 0.0094  414 LEU D C   
15721 O O   . LEU D 414 ? 0.8078 0.7744 0.5527 0.0547  -0.0223 0.0050  414 LEU D O   
15722 C CB  . LEU D 414 ? 0.7123 0.6312 0.4096 0.0549  -0.0367 0.0273  414 LEU D CB  
15723 C CG  . LEU D 414 ? 0.7540 0.6453 0.4058 0.0455  -0.0397 0.0401  414 LEU D CG  
15724 C CD1 . LEU D 414 ? 0.7867 0.6549 0.4307 0.0489  -0.0645 0.0494  414 LEU D CD1 
15725 C CD2 . LEU D 414 ? 0.7707 0.6561 0.3920 0.0379  -0.0385 0.0382  414 LEU D CD2 
15726 N N   . LYS D 415 ? 0.7322 0.7110 0.5029 0.0621  -0.0057 0.0049  415 LYS D N   
15727 C CA  . LYS D 415 ? 0.7942 0.7985 0.5983 0.0651  -0.0025 -0.0048 415 LYS D CA  
15728 C C   . LYS D 415 ? 0.7472 0.7597 0.5489 0.0566  0.0097  -0.0070 415 LYS D C   
15729 O O   . LYS D 415 ? 0.7247 0.7546 0.5491 0.0550  0.0088  -0.0131 415 LYS D O   
15730 C CB  . LYS D 415 ? 0.8063 0.8229 0.6312 0.0712  0.0069  -0.0096 415 LYS D CB  
15731 C CG  . LYS D 415 ? 0.8534 0.8984 0.7105 0.0726  0.0152  -0.0191 415 LYS D CG  
15732 C CD  . LYS D 415 ? 0.8869 0.9454 0.7752 0.0822  0.0011  -0.0262 415 LYS D CD  
15733 C CE  . LYS D 415 ? 0.8534 0.9448 0.7772 0.0835  0.0140  -0.0362 415 LYS D CE  
15734 N NZ  . LYS D 415 ? 0.9168 1.0305 0.8754 0.0852  0.0026  -0.0412 415 LYS D NZ  
15735 N N   . TRP D 416 ? 0.7290 0.7286 0.5055 0.0511  0.0204  -0.0020 416 TRP D N   
15736 C CA  . TRP D 416 ? 0.7128 0.7149 0.4868 0.0450  0.0315  -0.0043 416 TRP D CA  
15737 C C   . TRP D 416 ? 0.7244 0.7072 0.4682 0.0405  0.0297  -0.0041 416 TRP D C   
15738 O O   . TRP D 416 ? 0.7441 0.7241 0.4843 0.0366  0.0380  -0.0077 416 TRP D O   
15739 C CB  . TRP D 416 ? 0.6969 0.7033 0.4738 0.0443  0.0481  -0.0006 416 TRP D CB  
15740 C CG  . TRP D 416 ? 0.7677 0.7883 0.5640 0.0476  0.0507  -0.0014 416 TRP D CG  
15741 C CD1 . TRP D 416 ? 0.6819 0.7189 0.4968 0.0456  0.0576  -0.0048 416 TRP D CD1 
15742 C CD2 . TRP D 416 ? 0.8441 0.8609 0.6391 0.0524  0.0470  0.0005  416 TRP D CD2 
15743 N NE1 . TRP D 416 ? 0.6654 0.7098 0.4881 0.0497  0.0599  -0.0066 416 TRP D NE1 
15744 C CE2 . TRP D 416 ? 0.7037 0.7348 0.5155 0.0544  0.0525  -0.0041 416 TRP D CE2 
15745 C CE3 . TRP D 416 ? 0.7623 0.7627 0.5414 0.0540  0.0395  0.0059  416 TRP D CE3 
15746 C CZ2 . TRP D 416 ? 0.7242 0.7519 0.5370 0.0594  0.0503  -0.0060 416 TRP D CZ2 
15747 C CZ3 . TRP D 416 ? 0.7646 0.7611 0.5476 0.0581  0.0358  0.0060  416 TRP D CZ3 
15748 C CH2 . TRP D 416 ? 0.8218 0.8311 0.6215 0.0615  0.0409  -0.0011 416 TRP D CH2 
15749 N N   . ILE D 417 ? 0.7593 0.7263 0.4787 0.0406  0.0188  -0.0004 417 ILE D N   
15750 C CA  . ILE D 417 ? 0.8146 0.7614 0.4969 0.0354  0.0196  -0.0007 417 ILE D CA  
15751 C C   . ILE D 417 ? 0.7654 0.6956 0.4224 0.0343  0.0011  0.0049  417 ILE D C   
15752 O O   . ILE D 417 ? 0.7486 0.6806 0.4174 0.0388  -0.0092 0.0106  417 ILE D O   
15753 C CB  . ILE D 417 ? 0.7377 0.6805 0.4064 0.0344  0.0411  0.0025  417 ILE D CB  
15754 C CG1 . ILE D 417 ? 0.7265 0.6548 0.3678 0.0308  0.0494  -0.0045 417 ILE D CG1 
15755 C CG2 . ILE D 417 ? 0.7574 0.6930 0.4105 0.0334  0.0420  0.0129  417 ILE D CG2 
15756 C CD1 . ILE D 417 ? 0.7823 0.7139 0.4255 0.0327  0.0723  -0.0043 417 ILE D CD1 
15757 N N   . GLY D 418 ? 0.7679 0.6786 0.3874 0.0283  -0.0043 0.0029  418 GLY D N   
15758 C CA  . GLY D 418 ? 0.8921 0.7813 0.4757 0.0248  -0.0211 0.0107  418 GLY D CA  
15759 C C   . GLY D 418 ? 1.0360 0.9167 0.6109 0.0223  -0.0481 0.0069  418 GLY D C   
15760 O O   . GLY D 418 ? 0.9434 0.7997 0.4743 0.0163  -0.0617 0.0121  418 GLY D O   
15761 N N   . ASN D 419 ? 1.0856 0.9862 0.7012 0.0253  -0.0570 -0.0009 419 ASN D N   
15762 C CA  . ASN D 419 ? 1.0237 0.9220 0.6412 0.0220  -0.0840 -0.0051 419 ASN D CA  
15763 C C   . ASN D 419 ? 1.1031 0.9980 0.7117 0.0140  -0.0785 -0.0172 419 ASN D C   
15764 O O   . ASN D 419 ? 1.1291 1.0247 0.7360 0.0133  -0.0539 -0.0223 419 ASN D O   
15765 C CB  . ASN D 419 ? 1.0195 0.9454 0.6944 0.0303  -0.0996 -0.0053 419 ASN D CB  
15766 C CG  . ASN D 419 ? 1.0733 1.0298 0.7959 0.0330  -0.0801 -0.0125 419 ASN D CG  
15767 O OD1 . ASN D 419 ? 1.0039 0.9605 0.7215 0.0269  -0.0637 -0.0184 419 ASN D OD1 
15768 N ND2 . ASN D 419 ? 1.0688 1.0497 0.8368 0.0421  -0.0829 -0.0123 419 ASN D ND2 
15769 N N   . LYS D 420 ? 1.0339 0.9415 0.9059 0.0584  -0.2197 0.0680  420 LYS D N   
15770 C CA  . LYS D 420 ? 1.0090 0.9090 0.8525 0.0463  -0.2353 0.0587  420 LYS D CA  
15771 C C   . LYS D 420 ? 1.0386 0.9734 0.9339 0.0399  -0.2202 0.0460  420 LYS D C   
15772 O O   . LYS D 420 ? 1.1059 1.0309 0.9693 0.0315  -0.2091 0.0340  420 LYS D O   
15773 C CB  . LYS D 420 ? 0.9732 0.8627 0.8114 0.0433  -0.2836 0.0684  420 LYS D CB  
15774 C CG  . LYS D 420 ? 1.0497 0.9550 0.9138 0.0302  -0.3063 0.0601  420 LYS D CG  
15775 C CD  . LYS D 420 ? 1.0644 0.9732 0.9529 0.0278  -0.3576 0.0727  420 LYS D CD  
15776 C CE  . LYS D 420 ? 0.9746 0.9192 0.9430 0.0419  -0.3609 0.0879  420 LYS D CE  
15777 N NZ  . LYS D 420 ? 1.1599 1.1026 1.1440 0.0428  -0.4138 0.1043  420 LYS D NZ  
15778 N N   . GLU D 421 ? 1.0084 0.9816 0.9820 0.0448  -0.2169 0.0492  421 GLU D N   
15779 C CA  . GLU D 421 ? 0.9798 0.9842 1.0012 0.0386  -0.2005 0.0393  421 GLU D CA  
15780 C C   . GLU D 421 ? 0.8775 0.8773 0.8743 0.0383  -0.1616 0.0277  421 GLU D C   
15781 O O   . GLU D 421 ? 0.9045 0.9057 0.8918 0.0294  -0.1525 0.0175  421 GLU D O   
15782 C CB  . GLU D 421 ? 0.9178 0.9621 1.0259 0.0466  -0.1986 0.0464  421 GLU D CB  
15783 C CG  . GLU D 421 ? 1.1271 1.1794 1.2706 0.0536  -0.2342 0.0626  421 GLU D CG  
15784 C CD  . GLU D 421 ? 1.2302 1.2604 1.3502 0.0682  -0.2335 0.0725  421 GLU D CD  
15785 O OE1 . GLU D 421 ? 1.1794 1.1778 1.2345 0.0679  -0.2165 0.0681  421 GLU D OE1 
15786 O OE2 . GLU D 421 ? 1.3600 1.4051 1.5303 0.0801  -0.2489 0.0859  421 GLU D OE2 
15787 N N   . LYS D 422 ? 0.8089 0.8017 0.7960 0.0474  -0.1404 0.0297  422 LYS D N   
15788 C CA  . LYS D 422 ? 0.8825 0.8745 0.8546 0.0464  -0.1075 0.0199  422 LYS D CA  
15789 C C   . LYS D 422 ? 0.8647 0.8315 0.7739 0.0403  -0.1027 0.0149  422 LYS D C   
15790 O O   . LYS D 422 ? 0.7154 0.6858 0.6166 0.0364  -0.0839 0.0057  422 LYS D O   
15791 C CB  . LYS D 422 ? 0.8291 0.8179 0.8095 0.0554  -0.0898 0.0234  422 LYS D CB  
15792 C CG  . LYS D 422 ? 0.7599 0.7717 0.7987 0.0631  -0.0787 0.0227  422 LYS D CG  
15793 C CD  . LYS D 422 ? 0.6768 0.6753 0.7205 0.0740  -0.0730 0.0292  422 LYS D CD  
15794 C CE  . LYS D 422 ? 0.7054 0.7231 0.8096 0.0860  -0.0706 0.0326  422 LYS D CE  
15795 N NZ  . LYS D 422 ? 0.7227 0.7220 0.8285 0.0970  -0.0568 0.0344  422 LYS D NZ  
15796 N N   . ASN D 423 ? 0.9450 0.8841 0.8077 0.0409  -0.1184 0.0217  423 ASN D N   
15797 C CA  . ASN D 423 ? 0.8200 0.7322 0.6206 0.0375  -0.1104 0.0174  423 ASN D CA  
15798 C C   . ASN D 423 ? 0.7912 0.6995 0.5795 0.0298  -0.1191 0.0072  423 ASN D C   
15799 O O   . ASN D 423 ? 0.7834 0.6773 0.5355 0.0286  -0.1029 -0.0001 423 ASN D O   
15800 C CB  . ASN D 423 ? 0.8751 0.7533 0.6224 0.0403  -0.1242 0.0278  423 ASN D CB  
15801 C CG  . ASN D 423 ? 0.8251 0.6994 0.5746 0.0465  -0.1107 0.0385  423 ASN D CG  
15802 O OD1 . ASN D 423 ? 0.8572 0.7449 0.6264 0.0470  -0.0851 0.0356  423 ASN D OD1 
15803 N ND2 . ASN D 423 ? 0.9599 0.8125 0.6873 0.0505  -0.1300 0.0514  423 ASN D ND2 
15804 N N   . GLU D 424 ? 0.8677 0.7882 0.6886 0.0246  -0.1444 0.0073  424 GLU D N   
15805 C CA  . GLU D 424 ? 0.9503 0.8656 0.7645 0.0147  -0.1538 -0.0023 424 GLU D CA  
15806 C C   . GLU D 424 ? 0.8661 0.8021 0.7085 0.0130  -0.1266 -0.0108 424 GLU D C   
15807 O O   . GLU D 424 ? 0.9192 0.8400 0.7357 0.0079  -0.1222 -0.0196 424 GLU D O   
15808 C CB  . GLU D 424 ? 0.8996 0.8276 0.7529 0.0071  -0.1888 0.0020  424 GLU D CB  
15809 C CG  . GLU D 424 ? 1.0220 0.9336 0.8579 -0.0064 -0.2075 -0.0069 424 GLU D CG  
15810 C CD  . GLU D 424 ? 1.2049 1.0645 0.9512 -0.0074 -0.2123 -0.0141 424 GLU D CD  
15811 O OE1 . GLU D 424 ? 1.2656 1.0994 0.9647 -0.0017 -0.2224 -0.0079 424 GLU D OE1 
15812 O OE2 . GLU D 424 ? 1.2669 1.1083 0.9876 -0.0130 -0.2043 -0.0255 424 GLU D OE2 
15813 N N   . TYR D 425 ? 0.6967 0.6620 0.5868 0.0178  -0.1086 -0.0082 425 TYR D N   
15814 C CA  . TYR D 425 ? 0.6998 0.6785 0.6049 0.0168  -0.0833 -0.0153 425 TYR D CA  
15815 C C   . TYR D 425 ? 0.7668 0.7281 0.6271 0.0206  -0.0637 -0.0194 425 TYR D C   
15816 O O   . TYR D 425 ? 0.7637 0.7221 0.6146 0.0185  -0.0518 -0.0260 425 TYR D O   
15817 C CB  . TYR D 425 ? 0.7889 0.7949 0.7432 0.0218  -0.0678 -0.0126 425 TYR D CB  
15818 C CG  . TYR D 425 ? 0.8058 0.8362 0.8123 0.0171  -0.0682 -0.0126 425 TYR D CG  
15819 C CD1 . TYR D 425 ? 0.7721 0.8066 0.7977 0.0085  -0.0922 -0.0103 425 TYR D CD1 
15820 C CD2 . TYR D 425 ? 0.7415 0.7892 0.7779 0.0206  -0.0445 -0.0141 425 TYR D CD2 
15821 C CE1 . TYR D 425 ? 0.7204 0.7807 0.8016 0.0029  -0.0904 -0.0080 425 TYR D CE1 
15822 C CE2 . TYR D 425 ? 0.7917 0.8614 0.8760 0.0169  -0.0397 -0.0124 425 TYR D CE2 
15823 C CZ  . TYR D 425 ? 0.8098 0.8885 0.9207 0.0078  -0.0618 -0.0086 425 TYR D CZ  
15824 O OH  . TYR D 425 ? 0.8065 0.9104 0.9726 0.0025  -0.0556 -0.0048 425 TYR D OH  
15825 N N   . TRP D 426 ? 0.7607 0.7112 0.5971 0.0264  -0.0593 -0.0139 426 TRP D N   
15826 C CA  . TRP D 426 ? 0.7168 0.6563 0.5206 0.0299  -0.0389 -0.0153 426 TRP D CA  
15827 C C   . TRP D 426 ? 0.7795 0.6921 0.5362 0.0294  -0.0409 -0.0206 426 TRP D C   
15828 O O   . TRP D 426 ? 0.7946 0.7048 0.5398 0.0320  -0.0232 -0.0251 426 TRP D O   
15829 C CB  . TRP D 426 ? 0.6847 0.6178 0.4763 0.0343  -0.0333 -0.0063 426 TRP D CB  
15830 C CG  . TRP D 426 ? 0.7470 0.7001 0.5777 0.0354  -0.0240 -0.0040 426 TRP D CG  
15831 C CD1 . TRP D 426 ? 0.7620 0.7202 0.6180 0.0379  -0.0331 0.0014  426 TRP D CD1 
15832 C CD2 . TRP D 426 ? 0.7139 0.6803 0.5597 0.0346  -0.0052 -0.0074 426 TRP D CD2 
15833 N NE1 . TRP D 426 ? 0.6675 0.6371 0.5487 0.0387  -0.0189 -0.0002 426 TRP D NE1 
15834 C CE2 . TRP D 426 ? 0.6369 0.6115 0.5108 0.0355  -0.0036 -0.0056 426 TRP D CE2 
15835 C CE3 . TRP D 426 ? 0.7182 0.6888 0.5564 0.0338  0.0088  -0.0115 426 TRP D CE3 
15836 C CZ2 . TRP D 426 ? 0.6895 0.6722 0.5771 0.0336  0.0095  -0.0090 426 TRP D CZ2 
15837 C CZ3 . TRP D 426 ? 0.7705 0.7545 0.6287 0.0321  0.0198  -0.0129 426 TRP D CZ3 
15838 C CH2 . TRP D 426 ? 0.7835 0.7717 0.6630 0.0310  0.0192  -0.0123 426 TRP D CH2 
15839 N N   . LYS D 427 ? 0.8361 0.7256 0.5638 0.0266  -0.0635 -0.0202 427 LYS D N   
15840 C CA  . LYS D 427 ? 0.8662 0.7215 0.5413 0.0258  -0.0667 -0.0276 427 LYS D CA  
15841 C C   . LYS D 427 ? 0.8363 0.6966 0.5283 0.0213  -0.0634 -0.0371 427 LYS D C   
15842 O O   . LYS D 427 ? 0.8395 0.6789 0.4986 0.0252  -0.0497 -0.0436 427 LYS D O   
15843 C CB  . LYS D 427 ? 0.7877 0.6143 0.4276 0.0210  -0.0983 -0.0264 427 LYS D CB  
15844 C CG  . LYS D 427 ? 0.8703 0.6778 0.4721 0.0266  -0.1004 -0.0163 427 LYS D CG  
15845 C CD  . LYS D 427 ? 0.9546 0.7447 0.5410 0.0212  -0.1393 -0.0116 427 LYS D CD  
15846 C CE  . LYS D 427 ? 0.9467 0.7439 0.5436 0.0264  -0.1448 0.0032  427 LYS D CE  
15847 N NZ  . LYS D 427 ? 1.0169 0.8376 0.6673 0.0227  -0.1767 0.0097  427 LYS D NZ  
15848 N N   . ILE D 428 ? 0.8147 0.7013 0.5585 0.0140  -0.0735 -0.0369 428 ILE D N   
15849 C CA  . ILE D 428 ? 0.7916 0.6815 0.5523 0.0083  -0.0696 -0.0436 428 ILE D CA  
15850 C C   . ILE D 428 ? 0.7848 0.6847 0.5495 0.0158  -0.0412 -0.0449 428 ILE D C   
15851 O O   . ILE D 428 ? 0.8862 0.7686 0.6298 0.0177  -0.0325 -0.0507 428 ILE D O   
15852 C CB  . ILE D 428 ? 0.7773 0.6962 0.5968 -0.0008 -0.0815 -0.0404 428 ILE D CB  
15853 C CG1 . ILE D 428 ? 0.6929 0.6045 0.5152 -0.0091 -0.1145 -0.0379 428 ILE D CG1 
15854 C CG2 . ILE D 428 ? 0.7634 0.6849 0.5998 -0.0073 -0.0731 -0.0451 428 ILE D CG2 
15855 C CD1 . ILE D 428 ? 0.6736 0.6189 0.5634 -0.0171 -0.1244 -0.0325 428 ILE D CD1 
15856 N N   . LEU D 429 ? 0.7392 0.6650 0.5310 0.0203  -0.0282 -0.0393 429 LEU D N   
15857 C CA  . LEU D 429 ? 0.7442 0.6808 0.5418 0.0262  -0.0064 -0.0392 429 LEU D CA  
15858 C C   . LEU D 429 ? 0.8131 0.7308 0.5727 0.0347  0.0062  -0.0398 429 LEU D C   
15859 O O   . LEU D 429 ? 0.8339 0.7502 0.5906 0.0397  0.0194  -0.0418 429 LEU D O   
15860 C CB  . LEU D 429 ? 0.7213 0.6829 0.5493 0.0274  0.0009  -0.0339 429 LEU D CB  
15861 C CG  . LEU D 429 ? 0.7663 0.7421 0.6078 0.0300  0.0167  -0.0337 429 LEU D CG  
15862 C CD1 . LEU D 429 ? 0.7366 0.7148 0.5897 0.0265  0.0181  -0.0373 429 LEU D CD1 
15863 C CD2 . LEU D 429 ? 0.7178 0.7092 0.5810 0.0296  0.0203  -0.0302 429 LEU D CD2 
15864 N N   . ILE D 430 ? 0.7598 0.6615 0.4894 0.0374  0.0035  -0.0369 430 ILE D N   
15865 C CA  . ILE D 430 ? 0.8329 0.7156 0.5252 0.0467  0.0207  -0.0362 430 ILE D CA  
15866 C C   . ILE D 430 ? 0.9045 0.7561 0.5620 0.0499  0.0215  -0.0453 430 ILE D C   
15867 O O   . ILE D 430 ? 0.9692 0.8142 0.6154 0.0600  0.0417  -0.0464 430 ILE D O   
15868 C CB  . ILE D 430 ? 0.7676 0.6338 0.4276 0.0482  0.0185  -0.0300 430 ILE D CB  
15869 C CG1 . ILE D 430 ? 0.6742 0.5668 0.3659 0.0477  0.0264  -0.0199 430 ILE D CG1 
15870 C CG2 . ILE D 430 ? 0.9204 0.7549 0.5278 0.0578  0.0361  -0.0312 430 ILE D CG2 
15871 C CD1 . ILE D 430 ? 0.7024 0.5804 0.3717 0.0465  0.0172  -0.0120 430 ILE D CD1 
15872 N N   . GLU D 431 ? 0.9674 0.7990 0.6106 0.0413  -0.0010 -0.0517 431 GLU D N   
15873 C CA  . GLU D 431 ? 1.0125 0.8070 0.6186 0.0421  -0.0034 -0.0618 431 GLU D CA  
15874 C C   . GLU D 431 ? 0.9803 0.7870 0.6165 0.0429  0.0058  -0.0643 431 GLU D C   
15875 O O   . GLU D 431 ? 1.0543 0.8380 0.6666 0.0523  0.0199  -0.0690 431 GLU D O   
15876 C CB  . GLU D 431 ? 0.8809 0.6515 0.4681 0.0292  -0.0350 -0.0670 431 GLU D CB  
15877 C CG  . GLU D 431 ? 1.0595 0.7919 0.5848 0.0309  -0.0454 -0.0683 431 GLU D CG  
15878 C CD  . GLU D 431 ? 1.3846 1.0845 0.8543 0.0462  -0.0179 -0.0713 431 GLU D CD  
15879 O OE1 . GLU D 431 ? 1.4308 1.1408 0.8945 0.0546  0.0003  -0.0626 431 GLU D OE1 
15880 O OE2 . GLU D 431 ? 1.5653 1.2280 0.9980 0.0498  -0.0130 -0.0820 431 GLU D OE2 
15881 N N   . ALA D 432 ? 0.8215 0.6614 0.5076 0.0347  -0.0002 -0.0603 432 ALA D N   
15882 C CA  . ALA D 432 ? 0.8985 0.7469 0.6080 0.0350  0.0081  -0.0607 432 ALA D CA  
15883 C C   . ALA D 432 ? 0.8779 0.7388 0.5929 0.0488  0.0305  -0.0563 432 ALA D C   
15884 O O   . ALA D 432 ? 0.8795 0.7298 0.5916 0.0550  0.0389  -0.0577 432 ALA D O   
15885 C CB  . ALA D 432 ? 0.9492 0.8287 0.7054 0.0244  0.0011  -0.0563 432 ALA D CB  
15886 N N   . LYS D 433 ? 0.8528 0.7363 0.5793 0.0533  0.0389  -0.0499 433 LYS D N   
15887 C CA  . LYS D 433 ? 0.8557 0.7570 0.5976 0.0641  0.0571  -0.0440 433 LYS D CA  
15888 C C   . LYS D 433 ? 0.9163 0.7925 0.6284 0.0783  0.0730  -0.0463 433 LYS D C   
15889 O O   . LYS D 433 ? 0.9412 0.8261 0.6694 0.0886  0.0853  -0.0427 433 LYS D O   
15890 C CB  . LYS D 433 ? 0.8317 0.7588 0.5922 0.0630  0.0614  -0.0364 433 LYS D CB  
15891 C CG  . LYS D 433 ? 0.8293 0.7799 0.6146 0.0710  0.0768  -0.0286 433 LYS D CG  
15892 C CD  . LYS D 433 ? 0.7911 0.7632 0.6085 0.0675  0.0710  -0.0264 433 LYS D CD  
15893 C CE  . LYS D 433 ? 0.8496 0.8395 0.6896 0.0773  0.0819  -0.0188 433 LYS D CE  
15894 N NZ  . LYS D 433 ? 0.7830 0.7827 0.6410 0.0761  0.0734  -0.0170 433 LYS D NZ  
15895 N N   . LYS D 434 ? 0.8650 0.7073 0.5319 0.0801  0.0728  -0.0521 434 LYS D N   
15896 C CA  . LYS D 434 ? 0.8666 0.6776 0.4974 0.0956  0.0917  -0.0559 434 LYS D CA  
15897 C C   . LYS D 434 ? 0.9343 0.7215 0.5580 0.0997  0.0904  -0.0627 434 LYS D C   
15898 O O   . LYS D 434 ? 1.0730 0.8460 0.6872 0.1165  0.1102  -0.0630 434 LYS D O   
15899 C CB  . LYS D 434 ? 1.0542 0.8242 0.6251 0.0955  0.0896  -0.0622 434 LYS D CB  
15900 C CG  . LYS D 434 ? 1.0952 0.8803 0.6644 0.0923  0.0913  -0.0540 434 LYS D CG  
15901 C CD  . LYS D 434 ? 1.0704 0.8203 0.5905 0.0828  0.0693  -0.0599 434 LYS D CD  
15902 C CE  . LYS D 434 ? 1.1786 0.9195 0.6670 0.0867  0.0801  -0.0524 434 LYS D CE  
15903 N NZ  . LYS D 434 ? 1.3175 1.0081 0.7368 0.0821  0.0613  -0.0591 434 LYS D NZ  
15904 N N   . LYS D 435 ? 0.9451 0.7273 0.5760 0.0852  0.0691  -0.0671 435 LYS D N   
15905 C CA  . LYS D 435 ? 1.0103 0.7668 0.6348 0.0860  0.0664  -0.0722 435 LYS D CA  
15906 C C   . LYS D 435 ? 0.9447 0.7329 0.6156 0.0787  0.0602  -0.0649 435 LYS D C   
15907 O O   . LYS D 435 ? 0.9587 0.7292 0.6289 0.0703  0.0507  -0.0677 435 LYS D O   
15908 C CB  . LYS D 435 ? 1.0290 0.7405 0.6134 0.0736  0.0472  -0.0838 435 LYS D CB  
15909 C CG  . LYS D 435 ? 1.1040 0.7660 0.6246 0.0828  0.0535  -0.0937 435 LYS D CG  
15910 C CD  . LYS D 435 ? 1.2558 0.8825 0.7515 0.1020  0.0749  -0.0985 435 LYS D CD  
15911 C CE  . LYS D 435 ? 1.3619 0.9175 0.7845 0.1026  0.0697  -0.1142 435 LYS D CE  
15912 N NZ  . LYS D 435 ? 1.3622 0.8787 0.7746 0.1012  0.0645  -0.1216 435 LYS D NZ  
15913 N N   . ALA D 436 ? 0.8974 0.7284 0.6050 0.0808  0.0658  -0.0554 436 ALA D N   
15914 C CA  . ALA D 436 ? 0.8748 0.7313 0.6166 0.0732  0.0595  -0.0491 436 ALA D CA  
15915 C C   . ALA D 436 ? 0.8341 0.6865 0.5833 0.0850  0.0674  -0.0439 436 ALA D C   
15916 O O   . ALA D 436 ? 0.9752 0.8284 0.7251 0.1016  0.0804  -0.0408 436 ALA D O   
15917 C CB  . ALA D 436 ? 0.8318 0.7284 0.6028 0.0694  0.0592  -0.0425 436 ALA D CB  
15918 N N   . LYS D 437 ? 0.7621 0.6105 0.5188 0.0772  0.0602  -0.0413 437 LYS D N   
15919 C CA  . LYS D 437 ? 0.8196 0.6578 0.5788 0.0879  0.0644  -0.0350 437 LYS D CA  
15920 C C   . LYS D 437 ? 0.7293 0.5916 0.5101 0.0834  0.0592  -0.0252 437 LYS D C   
15921 O O   . LYS D 437 ? 0.6623 0.5213 0.4472 0.0940  0.0601  -0.0172 437 LYS D O   
15922 C CB  . LYS D 437 ? 0.7359 0.5294 0.4700 0.0845  0.0616  -0.0402 437 LYS D CB  
15923 C CG  . LYS D 437 ? 0.8489 0.6090 0.5513 0.0835  0.0613  -0.0526 437 LYS D CG  
15924 C CD  . LYS D 437 ? 0.9801 0.7184 0.6630 0.1062  0.0767  -0.0551 437 LYS D CD  
15925 C CE  . LYS D 437 ? 1.0932 0.7981 0.7350 0.1065  0.0783  -0.0680 437 LYS D CE  
15926 N NZ  . LYS D 437 ? 1.0894 0.8061 0.7264 0.1239  0.0966  -0.0671 437 LYS D NZ  
15927 N N   . ASN D 438 ? 0.7854 0.6684 0.5769 0.0694  0.0537  -0.0254 438 ASN D N   
15928 C CA  . ASN D 438 ? 0.7448 0.6426 0.5457 0.0645  0.0500  -0.0179 438 ASN D CA  
15929 C C   . ASN D 438 ? 0.8394 0.7657 0.6544 0.0570  0.0479  -0.0196 438 ASN D C   
15930 O O   . ASN D 438 ? 0.8064 0.7408 0.6258 0.0551  0.0488  -0.0251 438 ASN D O   
15931 C CB  . ASN D 438 ? 0.6542 0.5312 0.4443 0.0536  0.0495  -0.0160 438 ASN D CB  
15932 C CG  . ASN D 438 ? 0.8417 0.7068 0.6308 0.0407  0.0489  -0.0237 438 ASN D CG  
15933 O OD1 . ASN D 438 ? 0.8165 0.6595 0.5942 0.0425  0.0473  -0.0296 438 ASN D OD1 
15934 N ND2 . ASN D 438 ? 0.8716 0.7499 0.6729 0.0277  0.0496  -0.0234 438 ASN D ND2 
15935 N N   . ASP D 439 ? 0.7949 0.7313 0.6121 0.0530  0.0446  -0.0149 439 ASP D N   
15936 C CA  . ASP D 439 ? 0.6954 0.6532 0.5228 0.0474  0.0424  -0.0168 439 ASP D CA  
15937 C C   . ASP D 439 ? 0.7791 0.7363 0.6072 0.0362  0.0462  -0.0221 439 ASP D C   
15938 O O   . ASP D 439 ? 0.7742 0.7427 0.6069 0.0321  0.0461  -0.0239 439 ASP D O   
15939 C CB  . ASP D 439 ? 0.8015 0.7651 0.6254 0.0482  0.0350  -0.0106 439 ASP D CB  
15940 C CG  . ASP D 439 ? 1.0507 1.0256 0.8884 0.0594  0.0287  -0.0036 439 ASP D CG  
15941 O OD1 . ASP D 439 ? 1.0774 1.0585 0.9284 0.0674  0.0347  -0.0044 439 ASP D OD1 
15942 O OD2 . ASP D 439 ? 1.0649 1.0420 0.9002 0.0608  0.0179  0.0034  439 ASP D OD2 
15943 N N   . TYR D 440 ? 0.8296 0.7734 0.6562 0.0313  0.0493  -0.0242 440 TYR D N   
15944 C CA  . TYR D 440 ? 0.7528 0.7029 0.5925 0.0219  0.0517  -0.0280 440 TYR D CA  
15945 C C   . TYR D 440 ? 0.7430 0.7056 0.5935 0.0229  0.0467  -0.0326 440 TYR D C   
15946 O O   . TYR D 440 ? 0.7717 0.7430 0.6377 0.0172  0.0462  -0.0345 440 TYR D O   
15947 C CB  . TYR D 440 ? 0.7136 0.6482 0.5554 0.0141  0.0529  -0.0276 440 TYR D CB  
15948 C CG  . TYR D 440 ? 0.7633 0.6919 0.6044 0.0073  0.0629  -0.0221 440 TYR D CG  
15949 C CD1 . TYR D 440 ? 0.7744 0.7167 0.6287 0.0027  0.0722  -0.0217 440 TYR D CD1 
15950 C CD2 . TYR D 440 ? 0.8172 0.7230 0.6423 0.0064  0.0655  -0.0165 440 TYR D CD2 
15951 C CE1 . TYR D 440 ? 0.7380 0.6719 0.5876 -0.0027 0.0865  -0.0159 440 TYR D CE1 
15952 C CE2 . TYR D 440 ? 0.8925 0.7891 0.7123 -0.0004 0.0773  -0.0096 440 TYR D CE2 
15953 C CZ  . TYR D 440 ? 0.7857 0.6967 0.6168 -0.0050 0.0890  -0.0093 440 TYR D CZ  
15954 O OH  . TYR D 440 ? 0.8833 0.7825 0.7051 -0.0108 0.1053  -0.0018 440 TYR D OH  
15955 N N   . ILE D 441 ? 0.7171 0.6802 0.5608 0.0310  0.0442  -0.0329 441 ILE D N   
15956 C CA  . ILE D 441 ? 0.7475 0.7201 0.5957 0.0323  0.0416  -0.0351 441 ILE D CA  
15957 C C   . ILE D 441 ? 0.7467 0.7364 0.6065 0.0309  0.0425  -0.0336 441 ILE D C   
15958 O O   . ILE D 441 ? 0.7475 0.7439 0.6144 0.0294  0.0405  -0.0346 441 ILE D O   
15959 C CB  . ILE D 441 ? 0.8386 0.8047 0.6744 0.0419  0.0440  -0.0346 441 ILE D CB  
15960 C CG1 . ILE D 441 ? 0.8947 0.8578 0.7228 0.0419  0.0418  -0.0371 441 ILE D CG1 
15961 C CG2 . ILE D 441 ? 0.7203 0.7015 0.5655 0.0486  0.0480  -0.0289 441 ILE D CG2 
15962 C CD1 . ILE D 441 ? 0.7740 0.7226 0.5949 0.0343  0.0319  -0.0419 441 ILE D CD1 
15963 N N   . LEU D 442 ? 0.7212 0.7136 0.5794 0.0312  0.0439  -0.0311 442 LEU D N   
15964 C CA  . LEU D 442 ? 0.7400 0.7412 0.6029 0.0285  0.0428  -0.0314 442 LEU D CA  
15965 C C   . LEU D 442 ? 0.7265 0.7247 0.5921 0.0235  0.0475  -0.0350 442 LEU D C   
15966 O O   . LEU D 442 ? 0.7154 0.7165 0.5854 0.0222  0.0478  -0.0373 442 LEU D O   
15967 C CB  . LEU D 442 ? 0.7573 0.7585 0.6127 0.0295  0.0385  -0.0278 442 LEU D CB  
15968 C CG  . LEU D 442 ? 0.7691 0.7777 0.6314 0.0367  0.0351  -0.0220 442 LEU D CG  
15969 C CD1 . LEU D 442 ? 0.7209 0.7288 0.5779 0.0377  0.0266  -0.0167 442 LEU D CD1 
15970 C CD2 . LEU D 442 ? 0.7423 0.7664 0.6215 0.0375  0.0354  -0.0202 442 LEU D CD2 
15971 N N   . VAL D 443 ? 0.7450 0.7366 0.6102 0.0211  0.0527  -0.0350 443 VAL D N   
15972 C CA  . VAL D 443 ? 0.6901 0.6835 0.5672 0.0179  0.0609  -0.0369 443 VAL D CA  
15973 C C   . VAL D 443 ? 0.6288 0.6328 0.5279 0.0181  0.0561  -0.0381 443 VAL D C   
15974 O O   . VAL D 443 ? 0.5583 0.5668 0.4689 0.0196  0.0595  -0.0396 443 VAL D O   
15975 C CB  . VAL D 443 ? 0.6212 0.6079 0.4998 0.0136  0.0690  -0.0342 443 VAL D CB  
15976 C CG1 . VAL D 443 ? 0.6604 0.6497 0.5506 0.0120  0.0836  -0.0347 443 VAL D CG1 
15977 C CG2 . VAL D 443 ? 0.6557 0.6278 0.5081 0.0145  0.0693  -0.0308 443 VAL D CG2 
15978 N N   . ALA D 444 ? 0.5909 0.5946 0.4920 0.0175  0.0471  -0.0373 444 ALA D N   
15979 C CA  . ALA D 444 ? 0.6206 0.6301 0.5363 0.0172  0.0383  -0.0373 444 ALA D CA  
15980 C C   . ALA D 444 ? 0.6251 0.6369 0.5363 0.0215  0.0353  -0.0368 444 ALA D C   
15981 O O   . ALA D 444 ? 0.6883 0.7032 0.6103 0.0223  0.0283  -0.0353 444 ALA D O   
15982 C CB  . ALA D 444 ? 0.6313 0.6308 0.5376 0.0147  0.0280  -0.0378 444 ALA D CB  
15983 N N   . GLU D 445 ? 0.6556 0.6747 0.5810 -0.0843 0.0963  0.0754  445 GLU D N   
15984 C CA  . GLU D 445 ? 0.6565 0.6537 0.5430 -0.0928 0.0982  0.0745  445 GLU D CA  
15985 C C   . GLU D 445 ? 0.7520 0.7154 0.6089 -0.0891 0.1080  0.0804  445 GLU D C   
15986 O O   . GLU D 445 ? 0.7416 0.6795 0.5617 -0.0983 0.1128  0.0795  445 GLU D O   
15987 C CB  . GLU D 445 ? 0.6736 0.6808 0.5542 -0.1093 0.0973  0.0670  445 GLU D CB  
15988 C CG  . GLU D 445 ? 0.8003 0.8327 0.7005 -0.1156 0.0917  0.0573  445 GLU D CG  
15989 C CD  . GLU D 445 ? 0.7385 0.7968 0.6635 -0.1234 0.0879  0.0488  445 GLU D CD  
15990 O OE1 . GLU D 445 ? 0.7259 0.7800 0.6388 -0.1302 0.0882  0.0480  445 GLU D OE1 
15991 O OE2 . GLU D 445 ? 0.7529 0.8362 0.7106 -0.1221 0.0837  0.0417  445 GLU D OE2 
15992 N N   . GLY D 446 ? 0.7481 0.7089 0.6206 -0.0778 0.1139  0.0843  446 GLY D N   
15993 C CA  . GLY D 446 ? 0.7178 0.6466 0.5660 -0.0745 0.1264  0.0872  446 GLY D CA  
15994 C C   . GLY D 446 ? 0.7800 0.6892 0.6204 -0.0601 0.1251  0.0899  446 GLY D C   
15995 O O   . GLY D 446 ? 0.8186 0.7448 0.6814 -0.0486 0.1133  0.0903  446 GLY D O   
15996 N N   . SER D 447 ? 0.7713 0.6420 0.5775 -0.0605 0.1360  0.0915  447 SER D N   
15997 C CA  . SER D 447 ? 0.7833 0.6251 0.5722 -0.0465 0.1327  0.0961  447 SER D CA  
15998 C C   . SER D 447 ? 0.8306 0.6827 0.6590 -0.0212 0.1304  0.0966  447 SER D C   
15999 O O   . SER D 447 ? 0.7992 0.6427 0.6288 -0.0036 0.1176  0.1010  447 SER D O   
16000 C CB  . SER D 447 ? 0.7915 0.5835 0.5312 -0.0550 0.1472  0.0966  447 SER D CB  
16001 O OG  . SER D 447 ? 0.8521 0.6374 0.5912 -0.0610 0.1639  0.0919  447 SER D OG  
16002 N N   . ASP D 448 ? 0.8214 0.6924 0.6824 -0.0199 0.1421  0.0914  448 ASP D N   
16003 C CA  . ASP D 448 ? 0.7326 0.6123 0.6345 0.0014  0.1471  0.0872  448 ASP D CA  
16004 C C   . ASP D 448 ? 0.7140 0.6297 0.6581 0.0176  0.1261  0.0863  448 ASP D C   
16005 O O   . ASP D 448 ? 0.8182 0.7324 0.7828 0.0406  0.1180  0.0857  448 ASP D O   
16006 C CB  . ASP D 448 ? 0.7813 0.6731 0.7047 -0.0068 0.1677  0.0800  448 ASP D CB  
16007 C CG  . ASP D 448 ? 0.9302 0.7853 0.8073 -0.0234 0.1870  0.0798  448 ASP D CG  
16008 O OD1 . ASP D 448 ? 0.8716 0.7185 0.7119 -0.0417 0.1820  0.0836  448 ASP D OD1 
16009 O OD2 . ASP D 448 ? 0.9555 0.7916 0.8350 -0.0188 0.2075  0.0737  448 ASP D OD2 
16010 N N   . TRP D 449 ? 0.7024 0.6502 0.6597 0.0065  0.1156  0.0852  449 TRP D N   
16011 C CA  . TRP D 449 ? 0.6906 0.6756 0.6882 0.0182  0.0967  0.0813  449 TRP D CA  
16012 C C   . TRP D 449 ? 0.7346 0.7025 0.7082 0.0327  0.0748  0.0882  449 TRP D C   
16013 O O   . TRP D 449 ? 0.8196 0.8071 0.8259 0.0530  0.0585  0.0854  449 TRP D O   
16014 C CB  . TRP D 449 ? 0.7029 0.7170 0.7110 0.0011  0.0921  0.0782  449 TRP D CB  
16015 C CG  . TRP D 449 ? 0.6945 0.7064 0.6987 -0.0160 0.1101  0.0775  449 TRP D CG  
16016 C CD1 . TRP D 449 ? 0.7127 0.7151 0.6861 -0.0331 0.1108  0.0809  449 TRP D CD1 
16017 C CD2 . TRP D 449 ? 0.6459 0.6640 0.6760 -0.0176 0.1288  0.0727  449 TRP D CD2 
16018 N NE1 . TRP D 449 ? 0.6015 0.6025 0.5776 -0.0427 0.1245  0.0808  449 TRP D NE1 
16019 C CE2 . TRP D 449 ? 0.5931 0.5998 0.5987 -0.0350 0.1373  0.0766  449 TRP D CE2 
16020 C CE3 . TRP D 449 ? 0.6128 0.6451 0.6849 -0.0069 0.1400  0.0644  449 TRP D CE3 
16021 C CZ2 . TRP D 449 ? 0.7126 0.7138 0.7233 -0.0425 0.1557  0.0752  449 TRP D CZ2 
16022 C CZ3 . TRP D 449 ? 0.5684 0.5976 0.6495 -0.0171 0.1631  0.0603  449 TRP D CZ3 
16023 C CH2 . TRP D 449 ? 0.6104 0.6205 0.6558 -0.0351 0.1705  0.0672  449 TRP D CH2 
16024 N N   . PHE D 450 ? 0.7649 0.6948 0.6799 0.0219  0.0740  0.0966  450 PHE D N   
16025 C CA  . PHE D 450 ? 0.7829 0.6835 0.6600 0.0327  0.0556  0.1054  450 PHE D CA  
16026 C C   . PHE D 450 ? 0.8476 0.7098 0.7148 0.0561  0.0568  0.1114  450 PHE D C   
16027 O O   . PHE D 450 ? 0.8838 0.7251 0.7325 0.0748  0.0363  0.1195  450 PHE D O   
16028 C CB  . PHE D 450 ? 0.7781 0.6479 0.5944 0.0091  0.0596  0.1100  450 PHE D CB  
16029 C CG  . PHE D 450 ? 0.7999 0.7055 0.6287 -0.0127 0.0603  0.1023  450 PHE D CG  
16030 C CD1 . PHE D 450 ? 0.6731 0.5943 0.5171 -0.0285 0.0765  0.0964  450 PHE D CD1 
16031 C CD2 . PHE D 450 ? 0.8127 0.7342 0.6365 -0.0167 0.0440  0.1005  450 PHE D CD2 
16032 C CE1 . PHE D 450 ? 0.6324 0.5847 0.4920 -0.0447 0.0756  0.0893  450 PHE D CE1 
16033 C CE2 . PHE D 450 ? 0.7837 0.7367 0.6229 -0.0357 0.0470  0.0912  450 PHE D CE2 
16034 C CZ  . PHE D 450 ? 0.6906 0.6592 0.5506 -0.0481 0.0624  0.0859  450 PHE D CZ  
16035 N N   . TRP D 451 ? 0.8898 0.7386 0.7657 0.0557  0.0801  0.1075  451 TRP D N   
16036 C CA  . TRP D 451 ? 0.8604 0.6718 0.7324 0.0785  0.0851  0.1104  451 TRP D CA  
16037 C C   . TRP D 451 ? 0.9608 0.8053 0.8941 0.1102  0.0677  0.1056  451 TRP D C   
16038 O O   . TRP D 451 ? 0.9904 0.8097 0.9147 0.1362  0.0491  0.1133  451 TRP D O   
16039 C CB  . TRP D 451 ? 0.8237 0.6183 0.6942 0.0675  0.1168  0.1034  451 TRP D CB  
16040 C CG  . TRP D 451 ? 0.9260 0.6876 0.8050 0.0900  0.1290  0.1011  451 TRP D CG  
16041 C CD1 . TRP D 451 ? 0.9385 0.7254 0.8800 0.1169  0.1278  0.0924  451 TRP D CD1 
16042 C CD2 . TRP D 451 ? 0.9791 0.6775 0.8069 0.0864  0.1469  0.1045  451 TRP D CD2 
16043 N NE1 . TRP D 451 ? 0.9699 0.7126 0.9038 0.1326  0.1436  0.0905  451 TRP D NE1 
16044 C CE2 . TRP D 451 ? 1.0224 0.7078 0.8843 0.1138  0.1560  0.0984  451 TRP D CE2 
16045 C CE3 . TRP D 451 ? 0.9732 0.6260 0.7330 0.0617  0.1575  0.1097  451 TRP D CE3 
16046 C CZ2 . TRP D 451 ? 1.0734 0.6967 0.8995 0.1180  0.1755  0.0986  451 TRP D CZ2 
16047 C CZ3 . TRP D 451 ? 0.9928 0.5853 0.7159 0.0634  0.1768  0.1096  451 TRP D CZ3 
16048 C CH2 . TRP D 451 ? 1.0887 0.6644 0.8430 0.0918  0.1859  0.1047  451 TRP D CH2 
16049 N N   . TRP D 452 ? 0.9244 0.8252 0.9208 0.1081  0.0725  0.0924  452 TRP D N   
16050 C CA  . TRP D 452 ? 0.8800 0.8232 0.9470 0.1344  0.0593  0.0823  452 TRP D CA  
16051 C C   . TRP D 452 ? 0.9065 0.8784 0.9829 0.1448  0.0227  0.0853  452 TRP D C   
16052 O O   . TRP D 452 ? 1.0155 1.0205 1.1464 0.1706  0.0037  0.0777  452 TRP D O   
16053 C CB  . TRP D 452 ? 0.7333 0.7230 0.8598 0.1226  0.0822  0.0652  452 TRP D CB  
16054 C CG  . TRP D 452 ? 0.7845 0.7444 0.8937 0.1096  0.1173  0.0620  452 TRP D CG  
16055 C CD1 . TRP D 452 ? 0.7571 0.7097 0.8377 0.0800  0.1381  0.0625  452 TRP D CD1 
16056 C CD2 . TRP D 452 ? 0.7955 0.7260 0.9115 0.1258  0.1351  0.0573  452 TRP D CD2 
16057 N NE1 . TRP D 452 ? 0.7965 0.7173 0.8612 0.0749  0.1670  0.0584  452 TRP D NE1 
16058 C CE2 . TRP D 452 ? 0.8138 0.7201 0.9006 0.1017  0.1681  0.0541  452 TRP D CE2 
16059 C CE3 . TRP D 452 ? 0.8462 0.7676 0.9911 0.1597  0.1256  0.0547  452 TRP D CE3 
16060 C CZ2 . TRP D 452 ? 0.8637 0.7367 0.9467 0.1071  0.1948  0.0469  452 TRP D CZ2 
16061 C CZ3 . TRP D 452 ? 0.8588 0.7474 1.0058 0.1677  0.1527  0.0475  452 TRP D CZ3 
16062 C CH2 . TRP D 452 ? 0.9046 0.7690 1.0197 0.1399  0.1886  0.0429  452 TRP D CH2 
16063 N N   . GLN D 453 ? 0.8783 0.8404 0.9050 0.1248  0.0125  0.0939  453 GLN D N   
16064 C CA  . GLN D 453 ? 0.9467 0.9348 0.9758 0.1298  -0.0200 0.0949  453 GLN D CA  
16065 C C   . GLN D 453 ? 0.9869 0.9437 0.9910 0.1599  -0.0501 0.1067  453 GLN D C   
16066 O O   . GLN D 453 ? 1.0302 0.9232 0.9698 0.1626  -0.0475 0.1218  453 GLN D O   
16067 C CB  . GLN D 453 ? 0.8803 0.8582 0.8570 0.1001  -0.0193 0.0998  453 GLN D CB  
16068 C CG  . GLN D 453 ? 0.8852 0.9190 0.9066 0.0826  -0.0162 0.0859  453 GLN D CG  
16069 C CD  . GLN D 453 ? 0.9232 1.0097 1.0070 0.0998  -0.0386 0.0741  453 GLN D CD  
16070 O OE1 . GLN D 453 ? 0.8095 0.9317 0.9589 0.1073  -0.0278 0.0611  453 GLN D OE1 
16071 N NE2 . GLN D 453 ? 0.8611 0.9530 0.9235 0.1038  -0.0690 0.0766  453 GLN D NE2 
16072 N N   . GLY D 454 ? 1.0676 1.0681 1.1214 0.1821  -0.0796 0.0996  454 GLY D N   
16073 C CA  . GLY D 454 ? 1.0880 1.0619 1.1155 0.2124  -0.1167 0.1122  454 GLY D CA  
16074 C C   . GLY D 454 ? 1.1714 1.0934 1.1871 0.2407  -0.1128 0.1221  454 GLY D C   
16075 O O   . GLY D 454 ? 1.1630 1.0326 1.1233 0.2606  -0.1379 0.1400  454 GLY D O   
16076 N N   . GLU D 455 ? 1.2206 1.1500 1.2821 0.2424  -0.0804 0.1109  455 GLU D N   
16077 C CA  . GLU D 455 ? 1.3229 1.2119 1.3910 0.2739  -0.0769 0.1151  455 GLU D CA  
16078 C C   . GLU D 455 ? 1.3682 1.3031 1.5130 0.3152  -0.1103 0.1057  455 GLU D C   
16079 O O   . GLU D 455 ? 1.3424 1.2995 1.4842 0.3261  -0.1510 0.1102  455 GLU D O   
16080 C CB  . GLU D 455 ? 1.2109 1.0934 1.3016 0.2604  -0.0301 0.1033  455 GLU D CB  
16081 C CG  . GLU D 455 ? 1.1837 1.0142 1.1953 0.2245  -0.0016 0.1132  455 GLU D CG  
16082 C CD  . GLU D 455 ? 1.3158 1.0672 1.2361 0.2276  -0.0135 0.1355  455 GLU D CD  
16083 O OE1 . GLU D 455 ? 1.3770 1.0856 1.2885 0.2601  -0.0257 0.1440  455 GLU D OE1 
16084 O OE2 . GLU D 455 ? 1.2358 0.9654 1.0932 0.1969  -0.0087 0.1436  455 GLU D OE2 
16085 N N   . GLU D 456 ? 1.4213 1.3729 1.6364 0.3379  -0.0942 0.0908  456 GLU D N   
16086 C CA  . GLU D 456 ? 1.4416 1.4321 1.7319 0.3826  -0.1278 0.0815  456 GLU D CA  
16087 C C   . GLU D 456 ? 1.4223 1.5059 1.8278 0.3811  -0.1156 0.0493  456 GLU D C   
16088 O O   . GLU D 456 ? 1.3827 1.4878 1.8637 0.4080  -0.1061 0.0322  456 GLU D O   
16089 C CB  . GLU D 456 ? 1.4149 1.3499 1.7061 0.4196  -0.1235 0.0873  456 GLU D CB  
16090 C CG  . GLU D 456 ? 1.4860 1.3157 1.6645 0.4209  -0.1248 0.1170  456 GLU D CG  
16091 C CD  . GLU D 456 ? 1.5522 1.3515 1.6425 0.4090  -0.1589 0.1406  456 GLU D CD  
16092 O OE1 . GLU D 456 ? 1.4896 1.2926 1.5804 0.4411  -0.2076 0.1500  456 GLU D OE1 
16093 O OE2 . GLU D 456 ? 1.5747 1.3437 1.5931 0.3680  -0.1369 0.1490  456 GLU D OE2 
16094 N N   . LYS D 457 ? 1.3790 1.5173 1.8018 0.3504  -0.1144 0.0388  457 LYS D N   
16095 C CA  . LYS D 457 ? 1.2701 1.4853 1.7897 0.3377  -0.0899 0.0078  457 LYS D CA  
16096 C C   . LYS D 457 ? 1.3349 1.5250 1.8673 0.3288  -0.0374 -0.0014 457 LYS D C   
16097 O O   . LYS D 457 ? 1.3401 1.5545 1.9477 0.3510  -0.0240 -0.0210 457 LYS D O   
16098 C CB  . LYS D 457 ? 1.2310 1.5196 1.8510 0.3721  -0.1249 -0.0130 457 LYS D CB  
16099 C CG  . LYS D 457 ? 1.2643 1.6371 2.0062 0.3677  -0.0991 -0.0515 457 LYS D CG  
16100 C CD  . LYS D 457 ? 1.3235 1.7080 2.0669 0.3205  -0.0472 -0.0640 457 LYS D CD  
16101 C CE  . LYS D 457 ? 1.2036 1.6578 2.0605 0.3172  -0.0164 -0.1019 457 LYS D CE  
16102 N NZ  . LYS D 457 ? 1.1615 1.6056 1.9995 0.2714  0.0375  -0.1087 457 LYS D NZ  
16103 N N   . ALA D 458 ? 1.3327 1.4698 1.7858 0.2969  -0.0091 0.0132  458 ALA D N   
16104 C CA  . ALA D 458 ? 1.3467 1.4492 1.7912 0.2848  0.0385  0.0075  458 ALA D CA  
16105 C C   . ALA D 458 ? 1.2908 1.4504 1.8036 0.2617  0.0727  -0.0190 458 ALA D C   
16106 O O   . ALA D 458 ? 1.1833 1.4032 1.7429 0.2540  0.0589  -0.0306 458 ALA D O   
16107 C CB  . ALA D 458 ? 1.2613 1.2933 1.6001 0.2577  0.0531  0.0301  458 ALA D CB  
16108 N N   . PRO D 459 ? 1.2515 1.3923 1.7707 0.2493  0.1182  -0.0304 459 PRO D N   
16109 C CA  . PRO D 459 ? 1.1392 1.3297 1.7227 0.2282  0.1528  -0.0568 459 PRO D CA  
16110 C C   . PRO D 459 ? 0.9932 1.1827 1.5316 0.1859  0.1675  -0.0502 459 PRO D C   
16111 O O   . PRO D 459 ? 0.9652 1.1029 1.4200 0.1666  0.1736  -0.0302 459 PRO D O   
16112 C CB  . PRO D 459 ? 0.9801 1.1381 1.5708 0.2300  0.1963  -0.0694 459 PRO D CB  
16113 C CG  . PRO D 459 ? 1.0352 1.1158 1.5322 0.2307  0.1931  -0.0440 459 PRO D CG  
16114 C CD  . PRO D 459 ? 1.1503 1.2230 1.6216 0.2547  0.1418  -0.0229 459 PRO D CD  
16115 N N   . PHE D 460 ? 0.8569 1.1053 1.4551 0.1723  0.1723  -0.0685 460 PHE D N   
16116 C CA  . PHE D 460 ? 0.7844 1.0348 1.3527 0.1344  0.1881  -0.0654 460 PHE D CA  
16117 C C   . PHE D 460 ? 0.7403 0.9647 1.2348 0.1255  0.1587  -0.0394 460 PHE D C   
16118 O O   . PHE D 460 ? 0.6661 0.8713 1.1147 0.0967  0.1725  -0.0306 460 PHE D O   
16119 C CB  . PHE D 460 ? 0.7424 0.9539 1.2752 0.1073  0.2365  -0.0678 460 PHE D CB  
16120 C CG  . PHE D 460 ? 0.8029 1.0447 1.4070 0.1024  0.2751  -0.0977 460 PHE D CG  
16121 C CD1 . PHE D 460 ? 0.7591 1.0667 1.4468 0.1008  0.2745  -0.1213 460 PHE D CD1 
16122 C CD2 . PHE D 460 ? 0.8568 1.0613 1.4439 0.0966  0.3147  -0.1049 460 PHE D CD2 
16123 C CE1 . PHE D 460 ? 0.9023 1.2395 1.6590 0.0931  0.3145  -0.1523 460 PHE D CE1 
16124 C CE2 . PHE D 460 ? 0.7633 0.9944 1.4153 0.0893  0.3552  -0.1352 460 PHE D CE2 
16125 C CZ  . PHE D 460 ? 0.8046 1.1028 1.5430 0.0873  0.3558  -0.1592 460 PHE D CZ  
16126 N N   . VAL D 461 ? 0.7324 0.9539 1.2134 0.1499  0.1184  -0.0273 461 VAL D N   
16127 C CA  . VAL D 461 ? 0.7292 0.9268 1.1415 0.1393  0.0939  -0.0058 461 VAL D CA  
16128 C C   . VAL D 461 ? 0.7085 0.9466 1.1395 0.1176  0.0883  -0.0125 461 VAL D C   
16129 O O   . VAL D 461 ? 0.7403 0.9585 1.1171 0.0994  0.0818  0.0012  461 VAL D O   
16130 C CB  . VAL D 461 ? 0.8934 1.0776 1.2852 0.1685  0.0527  0.0072  461 VAL D CB  
16131 C CG1 . VAL D 461 ? 0.9254 1.0593 1.2919 0.1884  0.0611  0.0152  461 VAL D CG1 
16132 C CG2 . VAL D 461 ? 0.8969 1.1430 1.3648 0.1914  0.0226  -0.0086 461 VAL D CG2 
16133 N N   . GLU D 462 ? 0.5954 0.8906 1.1054 0.1182  0.0925  -0.0357 462 GLU D N   
16134 C CA  . GLU D 462 ? 0.5448 0.8749 1.0738 0.0953  0.0914  -0.0445 462 GLU D CA  
16135 C C   . GLU D 462 ? 0.5505 0.8484 1.0373 0.0638  0.1244  -0.0376 462 GLU D C   
16136 O O   . GLU D 462 ? 0.6371 0.9306 1.0939 0.0462  0.1176  -0.0302 462 GLU D O   
16137 C CB  . GLU D 462 ? 0.5612 0.9577 1.1861 0.0987  0.0952  -0.0741 462 GLU D CB  
16138 C CG  . GLU D 462 ? 0.7262 1.1542 1.3737 0.0700  0.1040  -0.0869 462 GLU D CG  
16139 C CD  . GLU D 462 ? 0.9562 1.3870 1.5673 0.0640  0.0709  -0.0764 462 GLU D CD  
16140 O OE1 . GLU D 462 ? 0.9459 1.3614 1.5180 0.0824  0.0368  -0.0610 462 GLU D OE1 
16141 O OE2 . GLU D 462 ? 0.9236 1.3680 1.5428 0.0390  0.0821  -0.0847 462 GLU D OE2 
16142 N N   . VAL D 463 ? 0.5339 0.8067 1.0158 0.0570  0.1596  -0.0402 463 VAL D N   
16143 C CA  . VAL D 463 ? 0.5536 0.7914 0.9899 0.0286  0.1885  -0.0323 463 VAL D CA  
16144 C C   . VAL D 463 ? 0.6286 0.8240 0.9865 0.0233  0.1727  -0.0078 463 VAL D C   
16145 O O   . VAL D 463 ? 0.6163 0.8007 0.9454 0.0037  0.1758  -0.0004 463 VAL D O   
16146 C CB  . VAL D 463 ? 0.5567 0.7702 0.9924 0.0232  0.2273  -0.0393 463 VAL D CB  
16147 C CG1 . VAL D 463 ? 0.5611 0.7503 0.9666 -0.0076 0.2576  -0.0373 463 VAL D CG1 
16148 C CG2 . VAL D 463 ? 0.5610 0.8191 1.0808 0.0374  0.2379  -0.0656 463 VAL D CG2 
16149 N N   . PHE D 464 ? 0.5589 0.7294 0.8834 0.0406  0.1565  0.0039  464 PHE D N   
16150 C CA  . PHE D 464 ? 0.6110 0.7436 0.8648 0.0333  0.1445  0.0236  464 PHE D CA  
16151 C C   . PHE D 464 ? 0.6495 0.8030 0.8999 0.0289  0.1182  0.0269  464 PHE D C   
16152 O O   . PHE D 464 ? 0.6950 0.8308 0.9041 0.0133  0.1165  0.0367  464 PHE D O   
16153 C CB  . PHE D 464 ? 0.5848 0.6829 0.8040 0.0510  0.1357  0.0334  464 PHE D CB  
16154 C CG  . PHE D 464 ? 0.6096 0.6741 0.8121 0.0490  0.1648  0.0320  464 PHE D CG  
16155 C CD1 . PHE D 464 ? 0.7038 0.7293 0.8471 0.0292  0.1795  0.0419  464 PHE D CD1 
16156 C CD2 . PHE D 464 ? 0.6270 0.7007 0.8751 0.0665  0.1775  0.0187  464 PHE D CD2 
16157 C CE1 . PHE D 464 ? 0.6828 0.6758 0.8053 0.0248  0.2064  0.0392  464 PHE D CE1 
16158 C CE2 . PHE D 464 ? 0.6540 0.6945 0.8850 0.0627  0.2077  0.0149  464 PHE D CE2 
16159 C CZ  . PHE D 464 ? 0.6653 0.6637 0.8298 0.0407  0.2223  0.0255  464 PHE D CZ  
16160 N N   . ASP D 465 ? 0.5718 0.7648 0.8671 0.0423  0.0971  0.0169  465 ASP D N   
16161 C CA  . ASP D 465 ? 0.6292 0.8432 0.9216 0.0353  0.0745  0.0166  465 ASP D CA  
16162 C C   . ASP D 465 ? 0.6083 0.8384 0.9200 0.0124  0.0914  0.0085  465 ASP D C   
16163 O O   . ASP D 465 ? 0.5862 0.8053 0.8667 -0.0016 0.0877  0.0151  465 ASP D O   
16164 C CB  . ASP D 465 ? 0.6058 0.8592 0.9403 0.0545  0.0461  0.0063  465 ASP D CB  
16165 C CG  . ASP D 465 ? 0.7055 0.9865 1.0442 0.0434  0.0267  0.0004  465 ASP D CG  
16166 O OD1 . ASP D 465 ? 0.7145 0.9737 1.0006 0.0406  0.0092  0.0120  465 ASP D OD1 
16167 O OD2 . ASP D 465 ? 0.6344 0.9572 1.0280 0.0350  0.0318  -0.0177 465 ASP D OD2 
16168 N N   . LYS D 466 ? 0.4954 0.7487 0.8586 0.0080  0.1124  -0.0065 466 LYS D N   
16169 C CA  . LYS D 466 ? 0.5399 0.7990 0.9177 -0.0144 0.1325  -0.0135 466 LYS D CA  
16170 C C   . LYS D 466 ? 0.6146 0.8280 0.9339 -0.0287 0.1450  0.0036  466 LYS D C   
16171 O O   . LYS D 466 ? 0.5843 0.7946 0.8942 -0.0420 0.1443  0.0055  466 LYS D O   
16172 C CB  . LYS D 466 ? 0.5145 0.7925 0.9451 -0.0192 0.1606  -0.0311 466 LYS D CB  
16173 C CG  . LYS D 466 ? 0.5492 0.8257 0.9918 -0.0438 0.1852  -0.0386 466 LYS D CG  
16174 C CD  . LYS D 466 ? 0.4765 0.8047 0.9954 -0.0485 0.1923  -0.0657 466 LYS D CD  
16175 C CE  . LYS D 466 ? 0.6206 0.9353 1.1529 -0.0726 0.2335  -0.0757 466 LYS D CE  
16176 N NZ  . LYS D 466 ? 0.7898 1.0519 1.2604 -0.0892 0.2445  -0.0564 466 LYS D NZ  
16177 N N   . LEU D 467 ? 0.6075 0.7855 0.8885 -0.0252 0.1554  0.0150  467 LEU D N   
16178 C CA  . LEU D 467 ? 0.6149 0.7529 0.8413 -0.0377 0.1637  0.0300  467 LEU D CA  
16179 C C   . LEU D 467 ? 0.6352 0.7668 0.8274 -0.0374 0.1402  0.0402  467 LEU D C   
16180 O O   . LEU D 467 ? 0.6385 0.7600 0.8130 -0.0487 0.1400  0.0456  467 LEU D O   
16181 C CB  . LEU D 467 ? 0.6179 0.7220 0.8114 -0.0360 0.1801  0.0365  467 LEU D CB  
16182 C CG  . LEU D 467 ? 0.7064 0.8002 0.9120 -0.0462 0.2125  0.0290  467 LEU D CG  
16183 C CD1 . LEU D 467 ? 0.5673 0.6367 0.7533 -0.0403 0.2278  0.0290  467 LEU D CD1 
16184 C CD2 . LEU D 467 ? 0.6713 0.7371 0.8430 -0.0656 0.2247  0.0380  467 LEU D CD2 
16185 N N   . PHE D 468 ? 0.5537 0.6883 0.7354 -0.0245 0.1215  0.0424  468 PHE D N   
16186 C CA  . PHE D 468 ? 0.5407 0.6661 0.6862 -0.0276 0.1039  0.0499  468 PHE D CA  
16187 C C   . PHE D 468 ? 0.6139 0.7643 0.7801 -0.0364 0.0952  0.0427  468 PHE D C   
16188 O O   . PHE D 468 ? 0.5593 0.7009 0.7049 -0.0466 0.0936  0.0463  468 PHE D O   
16189 C CB  . PHE D 468 ? 0.6187 0.7381 0.7464 -0.0134 0.0865  0.0533  468 PHE D CB  
16190 C CG  . PHE D 468 ? 0.6551 0.7648 0.7444 -0.0198 0.0711  0.0582  468 PHE D CG  
16191 C CD1 . PHE D 468 ? 0.6251 0.7077 0.6722 -0.0310 0.0772  0.0657  468 PHE D CD1 
16192 C CD2 . PHE D 468 ? 0.6789 0.8078 0.7745 -0.0165 0.0515  0.0532  468 PHE D CD2 
16193 C CE1 . PHE D 468 ? 0.6990 0.7748 0.7148 -0.0397 0.0675  0.0666  468 PHE D CE1 
16194 C CE2 . PHE D 468 ? 0.6660 0.7829 0.7222 -0.0256 0.0417  0.0559  468 PHE D CE2 
16195 C CZ  . PHE D 468 ? 0.6193 0.7100 0.6377 -0.0377 0.0515  0.0618  468 PHE D CZ  
16196 N N   . ARG D 469 ? 0.5815 0.7650 0.7926 -0.0330 0.0904  0.0300  469 ARG D N   
16197 C CA  . ARG D 469 ? 0.5443 0.7505 0.7744 -0.0428 0.0831  0.0203  469 ARG D CA  
16198 C C   . ARG D 469 ? 0.5700 0.7691 0.8120 -0.0564 0.1019  0.0189  469 ARG D C   
16199 O O   . ARG D 469 ? 0.6815 0.8856 0.9270 -0.0656 0.0992  0.0143  469 ARG D O   
16200 C CB  . ARG D 469 ? 0.5568 0.8024 0.8312 -0.0367 0.0708  0.0050  469 ARG D CB  
16201 C CG  . ARG D 469 ? 0.5614 0.8110 0.8207 -0.0202 0.0465  0.0082  469 ARG D CG  
16202 C CD  . ARG D 469 ? 0.5978 0.8915 0.9070 -0.0122 0.0308  -0.0081 469 ARG D CD  
16203 N NE  . ARG D 469 ? 0.6961 0.9903 0.9822 0.0037  0.0005  -0.0035 469 ARG D NE  
16204 C CZ  . ARG D 469 ? 0.7299 1.0221 0.9823 -0.0023 -0.0189 -0.0030 469 ARG D CZ  
16205 N NH1 . ARG D 469 ? 0.5919 0.8867 0.8377 -0.0230 -0.0108 -0.0094 469 ARG D NH1 
16206 N NH2 . ARG D 469 ? 0.6124 0.8960 0.8345 0.0128  -0.0464 0.0040  469 ARG D NH2 
16207 N N   . SER D 470 ? 0.5433 0.7262 0.7883 -0.0582 0.1220  0.0226  470 SER D N   
16208 C CA  . SER D 470 ? 0.6079 0.7715 0.8504 -0.0704 0.1389  0.0256  470 SER D CA  
16209 C C   . SER D 470 ? 0.6126 0.7469 0.8113 -0.0722 0.1339  0.0401  470 SER D C   
16210 O O   . SER D 470 ? 0.6334 0.7602 0.8328 -0.0784 0.1342  0.0411  470 SER D O   
16211 C CB  . SER D 470 ? 0.5845 0.7348 0.8355 -0.0746 0.1636  0.0248  470 SER D CB  
16212 O OG  . SER D 470 ? 0.7137 0.8987 1.0170 -0.0750 0.1694  0.0067  470 SER D OG  
16213 N N   . PHE D 471 ? 0.6282 0.7465 0.7917 -0.0666 0.1290  0.0499  471 PHE D N   
16214 C CA  . PHE D 471 ? 0.6464 0.7450 0.7740 -0.0692 0.1219  0.0600  471 PHE D CA  
16215 C C   . PHE D 471 ? 0.6140 0.7303 0.7475 -0.0708 0.1068  0.0540  471 PHE D C   
16216 O O   . PHE D 471 ? 0.5971 0.7075 0.7233 -0.0744 0.1029  0.0564  471 PHE D O   
16217 C CB  . PHE D 471 ? 0.5787 0.6582 0.6687 -0.0660 0.1212  0.0681  471 PHE D CB  
16218 C CG  . PHE D 471 ? 0.5464 0.6044 0.6247 -0.0666 0.1388  0.0724  471 PHE D CG  
16219 C CD1 . PHE D 471 ? 0.7026 0.7408 0.7723 -0.0741 0.1510  0.0777  471 PHE D CD1 
16220 C CD2 . PHE D 471 ? 0.6101 0.6631 0.6822 -0.0598 0.1443  0.0711  471 PHE D CD2 
16221 C CE1 . PHE D 471 ? 0.6815 0.6960 0.7337 -0.0781 0.1705  0.0803  471 PHE D CE1 
16222 C CE2 . PHE D 471 ? 0.6843 0.7172 0.7467 -0.0620 0.1643  0.0720  471 PHE D CE2 
16223 C CZ  . PHE D 471 ? 0.6709 0.6848 0.7215 -0.0729 0.1785  0.0761  471 PHE D CZ  
16224 N N   . VAL D 472 ? 0.5998 0.7377 0.7458 -0.0679 0.0979  0.0454  472 VAL D N   
16225 C CA  . VAL D 472 ? 0.5915 0.7436 0.7374 -0.0725 0.0866  0.0377  472 VAL D CA  
16226 C C   . VAL D 472 ? 0.5836 0.7483 0.7618 -0.0789 0.0906  0.0279  472 VAL D C   
16227 O O   . VAL D 472 ? 0.5587 0.7246 0.7367 -0.0839 0.0883  0.0237  472 VAL D O   
16228 C CB  . VAL D 472 ? 0.6256 0.7909 0.7664 -0.0680 0.0742  0.0327  472 VAL D CB  
16229 C CG1 . VAL D 472 ? 0.6980 0.8779 0.8383 -0.0764 0.0655  0.0216  472 VAL D CG1 
16230 C CG2 . VAL D 472 ? 0.5521 0.6949 0.6526 -0.0624 0.0706  0.0432  472 VAL D CG2 
16231 N N   . ARG D 473 ? 0.5768 0.7504 0.7859 -0.0796 0.0988  0.0222  473 ARG D N   
16232 C CA  . ARG D 473 ? 0.6695 0.8488 0.9071 -0.0872 0.1054  0.0123  473 ARG D CA  
16233 C C   . ARG D 473 ? 0.6293 0.7798 0.8583 -0.0874 0.1138  0.0227  473 ARG D C   
16234 O O   . ARG D 473 ? 0.6617 0.8097 0.9027 -0.0901 0.1139  0.0177  473 ARG D O   
16235 C CB  . ARG D 473 ? 0.5890 0.7852 0.8628 -0.0913 0.1141  0.0009  473 ARG D CB  
16236 C CG  . ARG D 473 ? 0.6693 0.8661 0.9709 -0.1016 0.1241  -0.0107 473 ARG D CG  
16237 C CD  . ARG D 473 ? 0.7877 1.0048 1.1282 -0.1095 0.1344  -0.0259 473 ARG D CD  
16238 N NE  . ARG D 473 ? 0.8870 1.0982 1.2315 -0.1071 0.1468  -0.0203 473 ARG D NE  
16239 C CZ  . ARG D 473 ? 0.9225 1.1179 1.2820 -0.1168 0.1700  -0.0228 473 ARG D CZ  
16240 N NH1 . ARG D 473 ? 0.8462 1.0243 1.2151 -0.1279 0.1824  -0.0277 473 ARG D NH1 
16241 N NH2 . ARG D 473 ? 0.8376 1.0310 1.2015 -0.1163 0.1834  -0.0212 473 ARG D NH2 
16242 N N   . ARG D 474 ? 0.6080 0.7348 0.8146 -0.0839 0.1200  0.0370  474 ARG D N   
16243 C CA  . ARG D 474 ? 0.6271 0.7223 0.8182 -0.0832 0.1243  0.0491  474 ARG D CA  
16244 C C   . ARG D 474 ? 0.5848 0.6794 0.7627 -0.0787 0.1097  0.0526  474 ARG D C   
16245 O O   . ARG D 474 ? 0.6194 0.6993 0.8018 -0.0757 0.1074  0.0562  474 ARG D O   
16246 C CB  . ARG D 474 ? 0.6491 0.7178 0.8114 -0.0831 0.1344  0.0622  474 ARG D CB  
16247 C CG  . ARG D 474 ? 0.6696 0.6986 0.8062 -0.0832 0.1382  0.0768  474 ARG D CG  
16248 C CD  . ARG D 474 ? 0.7365 0.7527 0.8942 -0.0853 0.1437  0.0741  474 ARG D CD  
16249 N NE  . ARG D 474 ? 0.7908 0.7586 0.9157 -0.0859 0.1504  0.0907  474 ARG D NE  
16250 C CZ  . ARG D 474 ? 0.8908 0.8355 0.9961 -0.0769 0.1352  0.1032  474 ARG D CZ  
16251 N NH1 . ARG D 474 ? 0.8323 0.8023 0.9546 -0.0677 0.1153  0.0982  474 ARG D NH1 
16252 N NH2 . ARG D 474 ? 0.8572 0.7518 0.9245 -0.0773 0.1398  0.1202  474 ARG D NH2 
16253 N N   . ALA D 475 ? 0.5511 0.6609 0.7148 -0.0782 0.1002  0.0503  475 ALA D N   
16254 C CA  . ALA D 475 ? 0.6292 0.7444 0.7858 -0.0773 0.0892  0.0490  475 ALA D CA  
16255 C C   . ALA D 475 ? 0.5155 0.6487 0.7037 -0.0793 0.0874  0.0341  475 ALA D C   
16256 O O   . ALA D 475 ? 0.5723 0.7117 0.7665 -0.0777 0.0807  0.0302  475 ALA D O   
16257 C CB  . ALA D 475 ? 0.6042 0.7270 0.7352 -0.0802 0.0842  0.0480  475 ALA D CB  
16258 N N   . GLN D 476 ? 0.5133 0.6571 0.7246 -0.0835 0.0940  0.0234  476 GLN D N   
16259 C CA  . GLN D 476 ? 0.6033 0.7624 0.8430 -0.0879 0.0955  0.0064  476 GLN D CA  
16260 C C   . GLN D 476 ? 0.6312 0.7746 0.8974 -0.0853 0.1036  0.0054  476 GLN D C   
16261 O O   . GLN D 476 ? 0.7308 0.8832 1.0237 -0.0890 0.1078  -0.0103 476 GLN D O   
16262 C CB  . GLN D 476 ? 0.6095 0.7906 0.8520 -0.0969 0.0958  -0.0077 476 GLN D CB  
16263 C CG  . GLN D 476 ? 0.5953 0.7829 0.8047 -0.0989 0.0877  -0.0050 476 GLN D CG  
16264 C CD  . GLN D 476 ? 0.6464 0.8496 0.8519 -0.1041 0.0833  -0.0141 476 GLN D CD  
16265 O OE1 . GLN D 476 ? 0.6402 0.8556 0.8443 -0.1134 0.0818  -0.0287 476 GLN D OE1 
16266 N NE2 . GLN D 476 ? 0.5878 0.7911 0.7917 -0.0982 0.0806  -0.0067 476 GLN D NE2 
16267 N N   . GLU D 477 ? 0.6056 0.7208 0.8611 -0.0803 0.1077  0.0213  477 GLU D N   
16268 C CA  . GLU D 477 ? 0.6158 0.7053 0.8878 -0.0789 0.1173  0.0228  477 GLU D CA  
16269 C C   . GLU D 477 ? 0.6339 0.7072 0.9119 -0.0667 0.1082  0.0280  477 GLU D C   
16270 O O   . GLU D 477 ? 0.6434 0.7191 0.9059 -0.0588 0.0942  0.0364  477 GLU D O   
16271 C CB  . GLU D 477 ? 0.5660 0.6256 0.8175 -0.0809 0.1282  0.0375  477 GLU D CB  
16272 C CG  . GLU D 477 ? 0.7551 0.8355 1.0140 -0.0912 0.1381  0.0286  477 GLU D CG  
16273 C CD  . GLU D 477 ? 0.8478 0.9263 1.1363 -0.1021 0.1551  0.0154  477 GLU D CD  
16274 O OE1 . GLU D 477 ? 0.9346 1.0107 1.2445 -0.1038 0.1571  0.0050  477 GLU D OE1 
16275 O OE2 . GLU D 477 ? 0.8486 0.9298 1.1420 -0.1101 0.1679  0.0127  477 GLU D OE2 
16276 N N   . LEU D 478 ? 0.5858 0.6429 0.8892 -0.0649 0.1159  0.0214  478 LEU D N   
16277 C CA  . LEU D 478 ? 0.5681 0.6097 0.8867 -0.0499 0.1066  0.0240  478 LEU D CA  
16278 C C   . LEU D 478 ? 0.5932 0.5878 0.8808 -0.0380 0.0997  0.0499  478 LEU D C   
16279 O O   . LEU D 478 ? 0.6593 0.6237 0.9190 -0.0451 0.1111  0.0623  478 LEU D O   
16280 C CB  . LEU D 478 ? 0.5803 0.6170 0.9372 -0.0517 0.1191  0.0061  478 LEU D CB  
16281 C CG  . LEU D 478 ? 0.6918 0.7704 1.0814 -0.0564 0.1192  -0.0200 478 LEU D CG  
16282 C CD1 . LEU D 478 ? 0.6519 0.7685 1.0246 -0.0702 0.1172  -0.0276 478 LEU D CD1 
16283 C CD2 . LEU D 478 ? 0.7302 0.8032 1.1520 -0.0640 0.1364  -0.0406 478 LEU D CD2 
16284 N N   . GLU D 479 ? 0.6663 0.6549 0.9587 -0.0203 0.0806  0.0569  479 GLU D N   
16285 C CA  . GLU D 479 ? 0.6980 0.6433 0.9511 -0.0081 0.0671  0.0833  479 GLU D CA  
16286 C C   . GLU D 479 ? 0.7834 0.6691 1.0230 -0.0055 0.0791  0.0959  479 GLU D C   
16287 O O   . GLU D 479 ? 0.8104 0.6498 1.0007 -0.0049 0.0782  0.1189  479 GLU D O   
16288 C CB  . GLU D 479 ? 0.6406 0.5993 0.9081 0.0119  0.0394  0.0854  479 GLU D CB  
16289 C CG  . GLU D 479 ? 0.7882 0.7245 1.0065 0.0192  0.0190  0.1091  479 GLU D CG  
16290 C CD  . GLU D 479 ? 0.8424 0.7723 1.0754 0.0444  -0.0108 0.1159  479 GLU D CD  
16291 O OE1 . GLU D 479 ? 0.9151 0.8036 1.1027 0.0549  -0.0288 0.1402  479 GLU D OE1 
16292 O OE2 . GLU D 479 ? 0.7619 0.7285 1.0526 0.0538  -0.0163 0.0957  479 GLU D OE2 
16293 N N   . HIS D 480 ? 0.7742 0.6557 1.0521 -0.0062 0.0927  0.0806  480 HIS D N   
16294 C CA  . HIS D 480 ? 0.7576 0.5767 1.0253 -0.0025 0.1045  0.0913  480 HIS D CA  
16295 C C   . HIS D 480 ? 0.7668 0.5869 1.0544 -0.0244 0.1353  0.0726  480 HIS D C   
16296 O O   . HIS D 480 ? 0.6937 0.5654 1.0166 -0.0358 0.1421  0.0479  480 HIS D O   
16297 C CB  . HIS D 480 ? 0.7789 0.5801 1.0768 0.0229  0.0886  0.0913  480 HIS D CB  
16298 C CG  . HIS D 480 ? 0.7948 0.5990 1.0805 0.0463  0.0543  0.1074  480 HIS D CG  
16299 N ND1 . HIS D 480 ? 0.8627 0.6080 1.0965 0.0599  0.0381  0.1380  480 HIS D ND1 
16300 C CD2 . HIS D 480 ? 0.7568 0.6158 1.0752 0.0572  0.0328  0.0957  480 HIS D CD2 
16301 C CE1 . HIS D 480 ? 0.8637 0.6312 1.1006 0.0794  0.0049  0.1443  480 HIS D CE1 
16302 N NE2 . HIS D 480 ? 0.8292 0.6674 1.1205 0.0776  0.0023  0.1178  480 HIS D NE2 
16303 N N   . HIS D 481 ? 0.8120 0.5726 1.0733 -0.0319 0.1540  0.0842  481 HIS D N   
16304 C CA  . HIS D 481 ? 0.7920 0.5487 1.0760 -0.0533 0.1840  0.0646  481 HIS D CA  
16305 C C   . HIS D 481 ? 0.7855 0.5527 1.1201 -0.0465 0.1860  0.0429  481 HIS D C   
16306 O O   . HIS D 481 ? 0.8129 0.5575 1.1570 -0.0228 0.1705  0.0503  481 HIS D O   
16307 C CB  . HIS D 481 ? 0.8641 0.5462 1.1078 -0.0632 0.2059  0.0812  481 HIS D CB  
16308 C CG  . HIS D 481 ? 0.9702 0.6322 1.1586 -0.0698 0.2066  0.1028  481 HIS D CG  
16309 N ND1 . HIS D 481 ? 0.9653 0.6433 1.1482 -0.0951 0.2304  0.0938  481 HIS D ND1 
16310 C CD2 . HIS D 481 ? 1.0634 0.6915 1.2005 -0.0550 0.1869  0.1310  481 HIS D CD2 
16311 C CE1 . HIS D 481 ? 0.9727 0.6255 1.1033 -0.0962 0.2286  0.1148  481 HIS D CE1 
16312 N NE2 . HIS D 481 ? 1.1190 0.7399 1.2171 -0.0732 0.2020  0.1381  481 HIS D NE2 
16313 N N   . HIS D 482 ? 0.7522 0.5552 1.1207 -0.0670 0.2042  0.0146  482 HIS D N   
16314 C CA  . HIS D 482 ? 0.7430 0.5621 1.1581 -0.0640 0.2079  -0.0103 482 HIS D CA  
16315 C C   . HIS D 482 ? 0.7747 0.6091 1.2128 -0.0919 0.2340  -0.0380 482 HIS D C   
16316 O O   . HIS D 482 ? 0.8392 0.6926 1.2665 -0.1121 0.2436  -0.0415 482 HIS D O   
16317 C CB  . HIS D 482 ? 0.6891 0.5696 1.1276 -0.0547 0.1877  -0.0222 482 HIS D CB  
16318 C CG  . HIS D 482 ? 0.6600 0.5969 1.0918 -0.0723 0.1857  -0.0318 482 HIS D CG  
16319 N ND1 . HIS D 482 ? 0.6415 0.5925 1.0413 -0.0686 0.1708  -0.0132 482 HIS D ND1 
16320 C CD2 . HIS D 482 ? 0.6031 0.5816 1.0531 -0.0929 0.1955  -0.0575 482 HIS D CD2 
16321 C CE1 . HIS D 482 ? 0.5745 0.5715 0.9752 -0.0841 0.1718  -0.0261 482 HIS D CE1 
16322 N NE2 . HIS D 482 ? 0.6182 0.6334 1.0478 -0.0984 0.1848  -0.0522 482 HIS D NE2 
16323 N N   . HIS D 483 ? 0.8290 0.6574 1.3023 -0.0926 0.2449  -0.0600 483 HIS D N   
16324 C CA  . HIS D 483 ? 0.7991 0.6471 1.2983 -0.1197 0.2674  -0.0919 483 HIS D CA  
16325 C C   . HIS D 483 ? 0.7880 0.6628 1.3253 -0.1160 0.2668  -0.1189 483 HIS D C   
16326 O O   . HIS D 483 ? 0.7388 0.6029 1.2889 -0.0915 0.2551  -0.1129 483 HIS D O   
16327 C CB  . HIS D 483 ? 0.7999 0.5853 1.2939 -0.1335 0.2957  -0.0925 483 HIS D CB  
16328 C CG  . HIS D 483 ? 0.8998 0.6081 1.3823 -0.1103 0.2970  -0.0717 483 HIS D CG  
16329 N ND1 . HIS D 483 ? 1.0196 0.6915 1.5295 -0.1066 0.3122  -0.0878 483 HIS D ND1 
16330 C CD2 . HIS D 483 ? 0.9704 0.6275 1.4139 -0.0888 0.2839  -0.0359 483 HIS D CD2 
16331 C CE1 . HIS D 483 ? 1.1422 0.7428 1.6325 -0.0813 0.3068  -0.0613 483 HIS D CE1 
16332 N NE2 . HIS D 483 ? 1.1283 0.7189 1.5758 -0.0704 0.2884  -0.0291 483 HIS D NE2 
16333 N N   . HIS D 484 ? 0.7891 0.7012 1.3454 -0.1412 0.2794  -0.1504 484 HIS D N   
16334 C CA  . HIS D 484 ? 0.6963 0.6317 1.2838 -0.1434 0.2839  -0.1800 484 HIS D CA  
16335 C C   . HIS D 484 ? 0.7506 0.6329 1.3629 -0.1431 0.3078  -0.1940 484 HIS D C   
16336 O O   . HIS D 484 ? 0.8562 0.6957 1.4616 -0.1556 0.3265  -0.1921 484 HIS D O   
16337 C CB  . HIS D 484 ? 0.6621 0.6553 1.2512 -0.1714 0.2855  -0.2079 484 HIS D CB  
16338 C CG  . HIS D 484 ? 0.7632 0.7971 1.3621 -0.1709 0.2782  -0.2273 484 HIS D CG  
16339 N ND1 . HIS D 484 ? 0.7768 0.8077 1.4033 -0.1786 0.2957  -0.2585 484 HIS D ND1 
16340 C CD2 . HIS D 484 ? 0.6306 0.7054 1.2132 -0.1657 0.2587  -0.2213 484 HIS D CD2 
16341 C CE1 . HIS D 484 ? 0.6741 0.7438 1.3001 -0.1794 0.2881  -0.2715 484 HIS D CE1 
16342 N NE2 . HIS D 484 ? 0.7018 0.7973 1.3004 -0.1720 0.2656  -0.2488 484 HIS D NE2 
16343 N N   . HIS D 485 ? 0.7574 0.6401 1.3998 -0.1292 0.3090  -0.2093 485 HIS D N   
16344 C CA  . HIS D 485 ? 0.8579 0.6915 1.5290 -0.1276 0.3329  -0.2270 485 HIS D CA  
16345 C C   . HIS D 485 ? 0.9419 0.7987 1.6262 -0.1634 0.3565  -0.2675 485 HIS D C   
16346 O O   . HIS D 485 ? 0.9949 0.9117 1.6711 -0.1829 0.3493  -0.2835 485 HIS D O   
16347 C CB  . HIS D 485 ? 0.8201 0.6488 1.5267 -0.0975 0.3263  -0.2318 485 HIS D CB  
16348 C CG  . HIS D 485 ? 0.8864 0.6479 1.6199 -0.0838 0.3457  -0.2383 485 HIS D CG  
16349 N ND1 . HIS D 485 ? 0.9345 0.6343 1.6638 -0.0500 0.3345  -0.2069 485 HIS D ND1 
16350 C CD2 . HIS D 485 ? 0.9188 0.6613 1.6812 -0.0987 0.3751  -0.2727 485 HIS D CD2 
16351 C CE1 . HIS D 485 ? 0.9949 0.6378 1.7500 -0.0427 0.3558  -0.2201 485 HIS D CE1 
16352 N NE2 . HIS D 485 ? 0.9851 0.6531 1.7624 -0.0725 0.3823  -0.2612 485 HIS D NE2 
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